data_3AL4
# 
_entry.id   3AL4 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3AL4         
RCSB  RCSB029384   
WWPDB D_1000029384 
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             2010-08-04 
_pdbx_database_PDB_obs_spr.pdb_id           3AL4 
_pdbx_database_PDB_obs_spr.replace_pdb_id   3LYJ 
_pdbx_database_PDB_obs_spr.details          ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1RU7 '1934 Human H1 Hemagglutinin'                     unspecified 
PDB 1RV0 '1930 Swine H1 Hemagglutinin complexed with LSTA' unspecified 
PDB 1RUZ '1918 H1 Hemagglutinin'                           unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3AL4 
_pdbx_database_status.recvd_initial_deposition_date   2010-07-22 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Zhang, W.' 1 
'Qi, J.X.'  2 
'Shi, Y.'   3 
'Li, Q.'    4 
'Yan, J.H.' 5 
'Gao, G.F.' 6 
# 
_citation.id                        primary 
_citation.title                     
;Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus
;
_citation.journal_abbrev            'Protein Cell' 
_citation.journal_volume            1 
_citation.page_first                459 
_citation.page_last                 467 
_citation.year                      2010 
_citation.journal_id_ASTM           ? 
_citation.country                   CN 
_citation.journal_id_ISSN           1674-800X 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   21203961 
_citation.pdbx_database_id_DOI      10.1007/s13238-010-0059-1 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Zhang, W.'      1  
primary 'Qi, J.'         2  
primary 'Shi, Y.'        3  
primary 'Li, Q.'         4  
primary 'Gao, F.'        5  
primary 'Sun, Y.'        6  
primary 'Lu, X.'         7  
primary 'Lu, Q.'         8  
primary 'Vavricka, C.J.' 9  
primary 'Liu, D.'        10 
primary 'Yan, J.'        11 
primary 'Gao, G.F.'      12 
# 
_cell.entry_id           3AL4 
_cell.length_a           66.020 
_cell.length_b           115.190 
_cell.length_c           114.985 
_cell.angle_alpha        62.31 
_cell.angle_beta         77.94 
_cell.angle_gamma        81.05 
_cell.Z_PDB              6 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3AL4 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Hemagglutinin          36989.715 6   ? ? 'UNP residues 18-344'  'HEMAGGLUTININ HA1' 
2 polymer     man Hemagglutinin          20757.035 6   ? ? 'UNP residues 345-520' 'HEMAGGLUTININ HA2' 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   30  ? ? ?                      ?                   
4 non-polymer man BETA-D-MANNOSE         180.156   2   ? ? ?                      ?                   
5 water       nat water                  18.015    317 ? ? ?                      ?                   
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;ADLGSRDTLCIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDKHNGKLCKLRGVAPLHLGKCNIAGWILGNPECESLSTAS
SWSYIVETPSSDNGTCYPGDFIDYEELREQLSSVSSFERFEIFPKTSSWPNHDSNKGVTAACPHAGAKSFYKNLIWLVKK
GNSYPKLSKSYINDKGKEVLVLWGIHHPSTSADQQSLYQNADTYVFVGSSRYSKKFKPEIAIRPKVRDQEGRMNYYWTLV
EPGDKITFEATGNLVVPRYAFAMERNAGSGIIISDTPVHDCNTTCQTPKGAINTSLPFQNIHPITIGKCPKYVKSTKLRL
ATGLRNIPSIQSR
;
;ADLGSRDTLCIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDKHNGKLCKLRGVAPLHLGKCNIAGWILGNPECESLSTAS
SWSYIVETPSSDNGTCYPGDFIDYEELREQLSSVSSFERFEIFPKTSSWPNHDSNKGVTAACPHAGAKSFYKNLIWLVKK
GNSYPKLSKSYINDKGKEVLVLWGIHHPSTSADQQSLYQNADTYVFVGSSRYSKKFKPEIAIRPKVRDQEGRMNYYWTLV
EPGDKITFEATGNLVVPRYAFAMERNAGSGIIISDTPVHDCNTTCQTPKGAINTSLPFQNIHPITIGKCPKYVKSTKLRL
ATGLRNIPSIQSR
;
A,C,E,G,I,K ? 
2 'polypeptide(L)' no no 
;GLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADLKSTQNAIDEITNKVNSVIEKMNTQFTAVGKEFNHLEKRIENL
NKKVDDGFLDIWTYNAELLVLLENERTLDYHDSNVKNLYEKVRSQLKNNAKEIGNGCFEFYHKCDNTCMESVKNGTYDYP
KYSEEAKLNREEIDGVRLVPR
;
;GLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADLKSTQNAIDEITNKVNSVIEKMNTQFTAVGKEFNHLEKRIENL
NKKVDDGFLDIWTYNAELLVLLENERTLDYHDSNVKNLYEKVRSQLKNNAKEIGNGCFEFYHKCDNTCMESVKNGTYDYP
KYSEEAKLNREEIDGVRLVPR
;
B,D,F,H,J,L ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   ASP n 
1 3   LEU n 
1 4   GLY n 
1 5   SER n 
1 6   ARG n 
1 7   ASP n 
1 8   THR n 
1 9   LEU n 
1 10  CYS n 
1 11  ILE n 
1 12  GLY n 
1 13  TYR n 
1 14  HIS n 
1 15  ALA n 
1 16  ASN n 
1 17  ASN n 
1 18  SER n 
1 19  THR n 
1 20  ASP n 
1 21  THR n 
1 22  VAL n 
1 23  ASP n 
1 24  THR n 
1 25  VAL n 
1 26  LEU n 
1 27  GLU n 
1 28  LYS n 
1 29  ASN n 
1 30  VAL n 
1 31  THR n 
1 32  VAL n 
1 33  THR n 
1 34  HIS n 
1 35  SER n 
1 36  VAL n 
1 37  ASN n 
1 38  LEU n 
1 39  LEU n 
1 40  GLU n 
1 41  ASP n 
1 42  LYS n 
1 43  HIS n 
1 44  ASN n 
1 45  GLY n 
1 46  LYS n 
1 47  LEU n 
1 48  CYS n 
1 49  LYS n 
1 50  LEU n 
1 51  ARG n 
1 52  GLY n 
1 53  VAL n 
1 54  ALA n 
1 55  PRO n 
1 56  LEU n 
1 57  HIS n 
1 58  LEU n 
1 59  GLY n 
1 60  LYS n 
1 61  CYS n 
1 62  ASN n 
1 63  ILE n 
1 64  ALA n 
1 65  GLY n 
1 66  TRP n 
1 67  ILE n 
1 68  LEU n 
1 69  GLY n 
1 70  ASN n 
1 71  PRO n 
1 72  GLU n 
1 73  CYS n 
1 74  GLU n 
1 75  SER n 
1 76  LEU n 
1 77  SER n 
1 78  THR n 
1 79  ALA n 
1 80  SER n 
1 81  SER n 
1 82  TRP n 
1 83  SER n 
1 84  TYR n 
1 85  ILE n 
1 86  VAL n 
1 87  GLU n 
1 88  THR n 
1 89  PRO n 
1 90  SER n 
1 91  SER n 
1 92  ASP n 
1 93  ASN n 
1 94  GLY n 
1 95  THR n 
1 96  CYS n 
1 97  TYR n 
1 98  PRO n 
1 99  GLY n 
1 100 ASP n 
1 101 PHE n 
1 102 ILE n 
1 103 ASP n 
1 104 TYR n 
1 105 GLU n 
1 106 GLU n 
1 107 LEU n 
1 108 ARG n 
1 109 GLU n 
1 110 GLN n 
1 111 LEU n 
1 112 SER n 
1 113 SER n 
1 114 VAL n 
1 115 SER n 
1 116 SER n 
1 117 PHE n 
1 118 GLU n 
1 119 ARG n 
1 120 PHE n 
1 121 GLU n 
1 122 ILE n 
1 123 PHE n 
1 124 PRO n 
1 125 LYS n 
1 126 THR n 
1 127 SER n 
1 128 SER n 
1 129 TRP n 
1 130 PRO n 
1 131 ASN n 
1 132 HIS n 
1 133 ASP n 
1 134 SER n 
1 135 ASN n 
1 136 LYS n 
1 137 GLY n 
1 138 VAL n 
1 139 THR n 
1 140 ALA n 
1 141 ALA n 
1 142 CYS n 
1 143 PRO n 
1 144 HIS n 
1 145 ALA n 
1 146 GLY n 
1 147 ALA n 
1 148 LYS n 
1 149 SER n 
1 150 PHE n 
1 151 TYR n 
1 152 LYS n 
1 153 ASN n 
1 154 LEU n 
1 155 ILE n 
1 156 TRP n 
1 157 LEU n 
1 158 VAL n 
1 159 LYS n 
1 160 LYS n 
1 161 GLY n 
1 162 ASN n 
1 163 SER n 
1 164 TYR n 
1 165 PRO n 
1 166 LYS n 
1 167 LEU n 
1 168 SER n 
1 169 LYS n 
1 170 SER n 
1 171 TYR n 
1 172 ILE n 
1 173 ASN n 
1 174 ASP n 
1 175 LYS n 
1 176 GLY n 
1 177 LYS n 
1 178 GLU n 
1 179 VAL n 
1 180 LEU n 
1 181 VAL n 
1 182 LEU n 
1 183 TRP n 
1 184 GLY n 
1 185 ILE n 
1 186 HIS n 
1 187 HIS n 
1 188 PRO n 
1 189 SER n 
1 190 THR n 
1 191 SER n 
1 192 ALA n 
1 193 ASP n 
1 194 GLN n 
1 195 GLN n 
1 196 SER n 
1 197 LEU n 
1 198 TYR n 
1 199 GLN n 
1 200 ASN n 
1 201 ALA n 
1 202 ASP n 
1 203 THR n 
1 204 TYR n 
1 205 VAL n 
1 206 PHE n 
1 207 VAL n 
1 208 GLY n 
1 209 SER n 
1 210 SER n 
1 211 ARG n 
1 212 TYR n 
1 213 SER n 
1 214 LYS n 
1 215 LYS n 
1 216 PHE n 
1 217 LYS n 
1 218 PRO n 
1 219 GLU n 
1 220 ILE n 
1 221 ALA n 
1 222 ILE n 
1 223 ARG n 
1 224 PRO n 
1 225 LYS n 
1 226 VAL n 
1 227 ARG n 
1 228 ASP n 
1 229 GLN n 
1 230 GLU n 
1 231 GLY n 
1 232 ARG n 
1 233 MET n 
1 234 ASN n 
1 235 TYR n 
1 236 TYR n 
1 237 TRP n 
1 238 THR n 
1 239 LEU n 
1 240 VAL n 
1 241 GLU n 
1 242 PRO n 
1 243 GLY n 
1 244 ASP n 
1 245 LYS n 
1 246 ILE n 
1 247 THR n 
1 248 PHE n 
1 249 GLU n 
1 250 ALA n 
1 251 THR n 
1 252 GLY n 
1 253 ASN n 
1 254 LEU n 
1 255 VAL n 
1 256 VAL n 
1 257 PRO n 
1 258 ARG n 
1 259 TYR n 
1 260 ALA n 
1 261 PHE n 
1 262 ALA n 
1 263 MET n 
1 264 GLU n 
1 265 ARG n 
1 266 ASN n 
1 267 ALA n 
1 268 GLY n 
1 269 SER n 
1 270 GLY n 
1 271 ILE n 
1 272 ILE n 
1 273 ILE n 
1 274 SER n 
1 275 ASP n 
1 276 THR n 
1 277 PRO n 
1 278 VAL n 
1 279 HIS n 
1 280 ASP n 
1 281 CYS n 
1 282 ASN n 
1 283 THR n 
1 284 THR n 
1 285 CYS n 
1 286 GLN n 
1 287 THR n 
1 288 PRO n 
1 289 LYS n 
1 290 GLY n 
1 291 ALA n 
1 292 ILE n 
1 293 ASN n 
1 294 THR n 
1 295 SER n 
1 296 LEU n 
1 297 PRO n 
1 298 PHE n 
1 299 GLN n 
1 300 ASN n 
1 301 ILE n 
1 302 HIS n 
1 303 PRO n 
1 304 ILE n 
1 305 THR n 
1 306 ILE n 
1 307 GLY n 
1 308 LYS n 
1 309 CYS n 
1 310 PRO n 
1 311 LYS n 
1 312 TYR n 
1 313 VAL n 
1 314 LYS n 
1 315 SER n 
1 316 THR n 
1 317 LYS n 
1 318 LEU n 
1 319 ARG n 
1 320 LEU n 
1 321 ALA n 
1 322 THR n 
1 323 GLY n 
1 324 LEU n 
1 325 ARG n 
1 326 ASN n 
1 327 ILE n 
1 328 PRO n 
1 329 SER n 
1 330 ILE n 
1 331 GLN n 
1 332 SER n 
1 333 ARG n 
2 1   GLY n 
2 2   LEU n 
2 3   PHE n 
2 4   GLY n 
2 5   ALA n 
2 6   ILE n 
2 7   ALA n 
2 8   GLY n 
2 9   PHE n 
2 10  ILE n 
2 11  GLU n 
2 12  GLY n 
2 13  GLY n 
2 14  TRP n 
2 15  THR n 
2 16  GLY n 
2 17  MET n 
2 18  VAL n 
2 19  ASP n 
2 20  GLY n 
2 21  TRP n 
2 22  TYR n 
2 23  GLY n 
2 24  TYR n 
2 25  HIS n 
2 26  HIS n 
2 27  GLN n 
2 28  ASN n 
2 29  GLU n 
2 30  GLN n 
2 31  GLY n 
2 32  SER n 
2 33  GLY n 
2 34  TYR n 
2 35  ALA n 
2 36  ALA n 
2 37  ASP n 
2 38  LEU n 
2 39  LYS n 
2 40  SER n 
2 41  THR n 
2 42  GLN n 
2 43  ASN n 
2 44  ALA n 
2 45  ILE n 
2 46  ASP n 
2 47  GLU n 
2 48  ILE n 
2 49  THR n 
2 50  ASN n 
2 51  LYS n 
2 52  VAL n 
2 53  ASN n 
2 54  SER n 
2 55  VAL n 
2 56  ILE n 
2 57  GLU n 
2 58  LYS n 
2 59  MET n 
2 60  ASN n 
2 61  THR n 
2 62  GLN n 
2 63  PHE n 
2 64  THR n 
2 65  ALA n 
2 66  VAL n 
2 67  GLY n 
2 68  LYS n 
2 69  GLU n 
2 70  PHE n 
2 71  ASN n 
2 72  HIS n 
2 73  LEU n 
2 74  GLU n 
2 75  LYS n 
2 76  ARG n 
2 77  ILE n 
2 78  GLU n 
2 79  ASN n 
2 80  LEU n 
2 81  ASN n 
2 82  LYS n 
2 83  LYS n 
2 84  VAL n 
2 85  ASP n 
2 86  ASP n 
2 87  GLY n 
2 88  PHE n 
2 89  LEU n 
2 90  ASP n 
2 91  ILE n 
2 92  TRP n 
2 93  THR n 
2 94  TYR n 
2 95  ASN n 
2 96  ALA n 
2 97  GLU n 
2 98  LEU n 
2 99  LEU n 
2 100 VAL n 
2 101 LEU n 
2 102 LEU n 
2 103 GLU n 
2 104 ASN n 
2 105 GLU n 
2 106 ARG n 
2 107 THR n 
2 108 LEU n 
2 109 ASP n 
2 110 TYR n 
2 111 HIS n 
2 112 ASP n 
2 113 SER n 
2 114 ASN n 
2 115 VAL n 
2 116 LYS n 
2 117 ASN n 
2 118 LEU n 
2 119 TYR n 
2 120 GLU n 
2 121 LYS n 
2 122 VAL n 
2 123 ARG n 
2 124 SER n 
2 125 GLN n 
2 126 LEU n 
2 127 LYS n 
2 128 ASN n 
2 129 ASN n 
2 130 ALA n 
2 131 LYS n 
2 132 GLU n 
2 133 ILE n 
2 134 GLY n 
2 135 ASN n 
2 136 GLY n 
2 137 CYS n 
2 138 PHE n 
2 139 GLU n 
2 140 PHE n 
2 141 TYR n 
2 142 HIS n 
2 143 LYS n 
2 144 CYS n 
2 145 ASP n 
2 146 ASN n 
2 147 THR n 
2 148 CYS n 
2 149 MET n 
2 150 GLU n 
2 151 SER n 
2 152 VAL n 
2 153 LYS n 
2 154 ASN n 
2 155 GLY n 
2 156 THR n 
2 157 TYR n 
2 158 ASP n 
2 159 TYR n 
2 160 PRO n 
2 161 LYS n 
2 162 TYR n 
2 163 SER n 
2 164 GLU n 
2 165 GLU n 
2 166 ALA n 
2 167 LYS n 
2 168 LEU n 
2 169 ASN n 
2 170 ARG n 
2 171 GLU n 
2 172 GLU n 
2 173 ILE n 
2 174 ASP n 
2 175 GLY n 
2 176 VAL n 
2 177 ARG n 
2 178 LEU n 
2 179 VAL n 
2 180 PRO n 
2 181 ARG n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample ? ? ? ? ? HEMAGGLUTININ ? 'A/CALIFORNIA/04/2009(H1N1)' ? ? ? ? 'Influenza A virus' 641501 ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? SF9 ? ? ? ? ? ? ? BACULOVIRUS PACGP67-B ? ? ? ? ? 
2 1 sample ? ? ? ? ? HEMAGGLUTININ ? 'A/CALIFORNIA/04/2009(H1N1)' ? ? ? ? 'Influenza A virus' 641501 ? ? ? ? ? ? ? 'fall armyworm' 
'Spodoptera frugiperda' 7108 ? ? ? ? ? ? SF9 ? ? ? ? ? ? ? BACULOVIRUS PACGP67-B ? ? ? ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_isoform 
1 UNP C3W5S1_I09A0 C3W5S1 1 
;DTLCIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDKHNGKLCKLRGVAPLHLGKCNIAGWILGNPECESLSTASSWSYIV
ETPSSDNGTCYPGDFIDYEELREQLSSVSSFERFEIFPKTSSWPNHDSNKGVTAACPHAGAKSFYKNLIWLVKKGNSYPK
LSKSYINDKGKEVLVLWGIHHPSTSADQQSLYQNADTYVFVGSSRYSKKFKPEIAIRPKVRDQEGRMNYYWTLVEPGDKI
TFEATGNLVVPRYAFAMERNAGSGIIISDTPVHDCNTTCQTPKGAINTSLPFQNIHPITIGKCPKYVKSTKLRLATGLRN
IPSIQSR
;
18  ? 
2 UNP C3W5S1_I09A0 C3W5S1 2 
;GLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADLKSTQNAIDEITNKVNSVIEKMNTQFTAVGKEFNHLEKRIENL
NKKVDDGFLDIWTYNAELLVLLENERTLDYHDSNVKNLYEKVRSQLKNNAKEIGNGCFEFYHKCDNTCMESVKNGTYDYP
KYSEEAKLNREEIDGV
;
345 ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1  1 3AL4 A 7 ? 333 ? C3W5S1 18  ? 344 ? 7 333 
2  2 3AL4 B 1 ? 176 ? C3W5S1 345 ? 520 ? 1 176 
3  1 3AL4 C 7 ? 333 ? C3W5S1 18  ? 344 ? 7 333 
4  2 3AL4 D 1 ? 176 ? C3W5S1 345 ? 520 ? 1 176 
5  1 3AL4 E 7 ? 333 ? C3W5S1 18  ? 344 ? 7 333 
6  2 3AL4 F 1 ? 176 ? C3W5S1 345 ? 520 ? 1 176 
7  1 3AL4 G 7 ? 333 ? C3W5S1 18  ? 344 ? 7 333 
8  2 3AL4 H 1 ? 176 ? C3W5S1 345 ? 520 ? 1 176 
9  1 3AL4 I 7 ? 333 ? C3W5S1 18  ? 344 ? 7 333 
10 2 3AL4 J 1 ? 176 ? C3W5S1 345 ? 520 ? 1 176 
11 1 3AL4 K 7 ? 333 ? C3W5S1 18  ? 344 ? 7 333 
12 2 3AL4 L 1 ? 176 ? C3W5S1 345 ? 520 ? 1 176 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1  3AL4 ALA A 1   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 1   1  
1  3AL4 ASP A 2   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 2   2  
1  3AL4 LEU A 3   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 3   3  
1  3AL4 GLY A 4   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 4   4  
1  3AL4 SER A 5   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 5   5  
1  3AL4 ARG A 6   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 6   6  
2  3AL4 ARG B 177 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 177 7  
2  3AL4 LEU B 178 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 178 8  
2  3AL4 VAL B 179 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 179 9  
2  3AL4 PRO B 180 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 180 10 
2  3AL4 ARG B 181 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 181 11 
3  3AL4 ALA C 1   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 1   12 
3  3AL4 ASP C 2   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 2   13 
3  3AL4 LEU C 3   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 3   14 
3  3AL4 GLY C 4   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 4   15 
3  3AL4 SER C 5   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 5   16 
3  3AL4 ARG C 6   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 6   17 
4  3AL4 ARG D 177 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 177 18 
4  3AL4 LEU D 178 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 178 19 
4  3AL4 VAL D 179 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 179 20 
4  3AL4 PRO D 180 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 180 21 
4  3AL4 ARG D 181 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 181 22 
5  3AL4 ALA E 1   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 1   23 
5  3AL4 ASP E 2   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 2   24 
5  3AL4 LEU E 3   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 3   25 
5  3AL4 GLY E 4   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 4   26 
5  3AL4 SER E 5   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 5   27 
5  3AL4 ARG E 6   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 6   28 
6  3AL4 ARG F 177 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 177 29 
6  3AL4 LEU F 178 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 178 30 
6  3AL4 VAL F 179 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 179 31 
6  3AL4 PRO F 180 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 180 32 
6  3AL4 ARG F 181 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 181 33 
7  3AL4 ALA G 1   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 1   34 
7  3AL4 ASP G 2   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 2   35 
7  3AL4 LEU G 3   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 3   36 
7  3AL4 GLY G 4   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 4   37 
7  3AL4 SER G 5   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 5   38 
7  3AL4 ARG G 6   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 6   39 
8  3AL4 ARG H 177 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 177 40 
8  3AL4 LEU H 178 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 178 41 
8  3AL4 VAL H 179 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 179 42 
8  3AL4 PRO H 180 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 180 43 
8  3AL4 ARG H 181 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 181 44 
9  3AL4 ALA I 1   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 1   45 
9  3AL4 ASP I 2   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 2   46 
9  3AL4 LEU I 3   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 3   47 
9  3AL4 GLY I 4   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 4   48 
9  3AL4 SER I 5   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 5   49 
9  3AL4 ARG I 6   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 6   50 
10 3AL4 ARG J 177 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 177 51 
10 3AL4 LEU J 178 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 178 52 
10 3AL4 VAL J 179 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 179 53 
10 3AL4 PRO J 180 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 180 54 
10 3AL4 ARG J 181 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 181 55 
11 3AL4 ALA K 1   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 1   56 
11 3AL4 ASP K 2   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 2   57 
11 3AL4 LEU K 3   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 3   58 
11 3AL4 GLY K 4   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 4   59 
11 3AL4 SER K 5   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 5   60 
11 3AL4 ARG K 6   ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 6   61 
12 3AL4 ARG L 177 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 177 62 
12 3AL4 LEU L 178 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 178 63 
12 3AL4 VAL L 179 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 179 64 
12 3AL4 PRO L 180 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 180 65 
12 3AL4 ARG L 181 ? UNP C3W5S1 ? ? 'EXPRESSION TAG' 181 66 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
BMA D-saccharide        . BETA-D-MANNOSE         ? 'C6 H12 O6'      180.156 
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                  ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE             ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE              ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE               ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          3AL4 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.18 
_exptl_crystal.density_percent_sol   43.59 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pdbx_details    '10% PEG 6000, 5% MPD, 0.1M MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MARMOSAIC 225 mm CCD' 
_diffrn_detector.pdbx_collection_date   2010-01-23 
_diffrn_detector.details                MIRRORS 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    GRAPHITE 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9795 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRF BEAMLINE BL17U' 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_synchrotron_beamline   BL17U 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
# 
_reflns.entry_id                     3AL4 
_reflns.observed_criterion_sigma_I   1.500 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.000 
_reflns.d_resolution_high            2.872 
_reflns.number_obs                   64796 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.0 
_reflns.pdbx_Rmerge_I_obs            0.10500 
_reflns.pdbx_Rsym_value              0.10500 
_reflns.B_iso_Wilson_estimate        56.27 
_reflns.pdbx_redundancy              3.700 
_reflns.pdbx_netI_over_sigmaI        12.900 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.87 
_reflns_shell.d_res_low              3.00 
_reflns_shell.percent_possible_all   90.7 
_reflns_shell.Rmerge_I_obs           0.50100 
_reflns_shell.pdbx_Rsym_value        0.50100 
_reflns_shell.meanI_over_sigI_obs    1.900 
_reflns_shell.pdbx_redundancy        2.70 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 3AL4 
_refine.ls_number_reflns_obs                     61067 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.070 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             24.19 
_refine.ls_d_res_high                            2.872 
_refine.ls_percent_reflns_obs                    91.6 
_refine.ls_R_factor_obs                          0.247 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.246 
_refine.ls_R_factor_R_free                       0.270 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.050 
_refine.ls_number_reflns_R_free                  3085 
_refine.ls_number_reflns_R_work                  57982 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               81.17 
_refine.aniso_B[1][1]                            -5.51000 
_refine.aniso_B[2][2]                            0.61800 
_refine.aniso_B[3][3]                            4.89300 
_refine.aniso_B[1][2]                            2.92400 
_refine.aniso_B[1][3]                            -2.52100 
_refine.aniso_B[2][3]                            17.08300 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 0.29 
_refine.solvent_model_param_bsol                 39.94 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 1RU7' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.370 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                330.340 
_refine.B_iso_min                                16.640 
_refine.pdbx_overall_phase_error                 29.5100 
_refine.occupancy_max                            1.000 
_refine.occupancy_min                            1.000 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        22867 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         442 
_refine_hist.number_atoms_solvent             317 
_refine_hist.number_atoms_total               23626 
_refine_hist.d_res_high                       2.872 
_refine_hist.d_res_low                        24.19 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.004  ? ? 23966 'X-RAY DIFFRACTION' ? 
f_angle_d          0.971  ? ? 32453 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 19.606 ? ? 8661  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.066  ? ? 3553  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.004  ? ? 4140  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
. 2.8716 2.9164  1567 0.3254 57.00  0.3783 . . 85  . . . . 'X-RAY DIFFRACTION' 
. 2.9164 2.9641  2233 0.3179 77.00  0.3668 . . 116 . . . . 'X-RAY DIFFRACTION' 
. 2.9641 3.0151  2338 0.3152 80.00  0.3527 . . 127 . . . . 'X-RAY DIFFRACTION' 
. 3.0151 3.0699  2389 0.3170 84.00  0.3285 . . 105 . . . . 'X-RAY DIFFRACTION' 
. 3.0699 3.1288  2541 0.2933 86.00  0.3302 . . 123 . . . . 'X-RAY DIFFRACTION' 
. 3.1288 3.1925  2503 0.2953 88.00  0.3273 . . 147 . . . . 'X-RAY DIFFRACTION' 
. 3.1925 3.2618  2574 0.2911 90.00  0.3123 . . 137 . . . . 'X-RAY DIFFRACTION' 
. 3.2618 3.3375  2652 0.2840 91.00  0.3183 . . 132 . . . . 'X-RAY DIFFRACTION' 
. 3.3375 3.4207  2670 0.2804 92.00  0.3081 . . 123 . . . . 'X-RAY DIFFRACTION' 
. 3.4207 3.5129  2697 0.2782 93.00  0.3091 . . 134 . . . . 'X-RAY DIFFRACTION' 
. 3.5129 3.6160  2745 0.2576 96.00  0.3033 . . 139 . . . . 'X-RAY DIFFRACTION' 
. 3.6160 3.7323  2787 0.2568 97.00  0.2877 . . 162 . . . . 'X-RAY DIFFRACTION' 
. 3.7323 3.8652  2823 0.2484 97.00  0.2488 . . 150 . . . . 'X-RAY DIFFRACTION' 
. 3.8652 4.0192  2787 0.2452 97.00  0.2772 . . 137 . . . . 'X-RAY DIFFRACTION' 
. 4.0192 4.2013  2737 0.2340 97.00  0.2546 . . 173 . . . . 'X-RAY DIFFRACTION' 
. 4.2013 4.4215  2915 0.2247 99.00  0.2494 . . 154 . . . . 'X-RAY DIFFRACTION' 
. 4.4215 4.6966  2788 0.2050 98.00  0.2543 . . 151 . . . . 'X-RAY DIFFRACTION' 
. 4.6966 5.0562  2862 0.2196 99.00  0.2618 . . 148 . . . . 'X-RAY DIFFRACTION' 
. 5.0562 5.5594  2826 0.2089 99.00  0.2304 . . 180 . . . . 'X-RAY DIFFRACTION' 
. 5.5594 6.3512  2821 0.2390 99.00  0.2647 . . 172 . . . . 'X-RAY DIFFRACTION' 
. 6.3512 7.9542  2883 0.2298 100.00 0.2602 . . 140 . . . . 'X-RAY DIFFRACTION' 
. 7.9542 24.1880 2844 0.1996 98.00  0.1940 . . 150 . . . . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3AL4 
_struct.title                     
;Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus
;
_struct.pdbx_descriptor           Hemagglutinin 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3AL4 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN/VIRAL PROTEIN' 
_struct_keywords.text            'TRIMER, ENVELOPE PROTEIN, HEMAGGLUTININ, VIRAL PROTEIN-VIRAL PROTEIN complex' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 2 ? 
C  N N 1 ? 
D  N N 2 ? 
E  N N 1 ? 
F  N N 2 ? 
G  N N 1 ? 
H  N N 2 ? 
I  N N 1 ? 
J  N N 2 ? 
K  N N 1 ? 
L  N N 2 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 3 ? 
R  N N 3 ? 
S  N N 3 ? 
T  N N 3 ? 
U  N N 3 ? 
V  N N 4 ? 
W  N N 3 ? 
X  N N 3 ? 
Y  N N 3 ? 
Z  N N 3 ? 
AA N N 3 ? 
BA N N 3 ? 
CA N N 3 ? 
DA N N 3 ? 
EA N N 3 ? 
FA N N 3 ? 
GA N N 3 ? 
HA N N 3 ? 
IA N N 3 ? 
JA N N 3 ? 
KA N N 4 ? 
LA N N 3 ? 
MA N N 3 ? 
NA N N 3 ? 
OA N N 3 ? 
PA N N 3 ? 
QA N N 3 ? 
RA N N 3 ? 
SA N N 5 ? 
TA N N 5 ? 
UA N N 5 ? 
VA N N 5 ? 
WA N N 5 ? 
XA N N 5 ? 
YA N N 5 ? 
ZA N N 5 ? 
AB N N 5 ? 
BB N N 5 ? 
CB N N 5 ? 
DB N N 5 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  ASN A 62  ? GLY A 69  ? ASN A 62  GLY A 69  1 ? 8  
HELX_P HELX_P2  2  ASP A 103 ? SER A 112 ? ASP A 103 SER A 112 1 ? 10 
HELX_P HELX_P3  3  PRO A 124 ? TRP A 129 ? PRO A 124 TRP A 129 1 ? 6  
HELX_P HELX_P4  4  THR A 190 ? TYR A 198 ? THR A 190 TYR A 198 1 ? 9  
HELX_P HELX_P5  5  ASP B 37  ? LYS B 58  ? ASP B 37  LYS B 58  1 ? 22 
HELX_P HELX_P6  6  GLU B 74  ? SER B 124 ? GLU B 74  SER B 124 1 ? 51 
HELX_P HELX_P7  7  ASP B 145 ? ASN B 154 ? ASP B 145 ASN B 154 1 ? 10 
HELX_P HELX_P8  8  ASN C 62  ? GLY C 69  ? ASN C 62  GLY C 69  1 ? 8  
HELX_P HELX_P9  9  ASP C 103 ? SER C 112 ? ASP C 103 SER C 112 1 ? 10 
HELX_P HELX_P10 10 THR C 190 ? TYR C 198 ? THR C 190 TYR C 198 1 ? 9  
HELX_P HELX_P11 11 ASP D 37  ? LYS D 58  ? ASP D 37  LYS D 58  1 ? 22 
HELX_P HELX_P12 12 GLU D 74  ? SER D 124 ? GLU D 74  SER D 124 1 ? 51 
HELX_P HELX_P13 13 ASP D 145 ? ASN D 154 ? ASP D 145 ASN D 154 1 ? 10 
HELX_P HELX_P14 14 ASN E 62  ? GLY E 69  ? ASN E 62  GLY E 69  1 ? 8  
HELX_P HELX_P15 15 ASP E 103 ? SER E 112 ? ASP E 103 SER E 112 1 ? 10 
HELX_P HELX_P16 16 PRO E 124 ? TRP E 129 ? PRO E 124 TRP E 129 1 ? 6  
HELX_P HELX_P17 17 THR E 190 ? TYR E 198 ? THR E 190 TYR E 198 1 ? 9  
HELX_P HELX_P18 18 ASP F 37  ? LYS F 58  ? ASP F 37  LYS F 58  1 ? 22 
HELX_P HELX_P19 19 GLU F 74  ? LEU F 126 ? GLU F 74  LEU F 126 1 ? 53 
HELX_P HELX_P20 20 ASP F 145 ? ASN F 154 ? ASP F 145 ASN F 154 1 ? 10 
HELX_P HELX_P21 21 ASN G 62  ? GLY G 69  ? ASN G 62  GLY G 69  1 ? 8  
HELX_P HELX_P22 22 ASN G 70  ? GLU G 74  ? ASN G 70  GLU G 74  5 ? 5  
HELX_P HELX_P23 23 ASP G 103 ? SER G 112 ? ASP G 103 SER G 112 1 ? 10 
HELX_P HELX_P24 24 PRO G 124 ? TRP G 129 ? PRO G 124 TRP G 129 1 ? 6  
HELX_P HELX_P25 25 THR G 190 ? TYR G 198 ? THR G 190 TYR G 198 1 ? 9  
HELX_P HELX_P26 26 ASP H 37  ? LYS H 58  ? ASP H 37  LYS H 58  1 ? 22 
HELX_P HELX_P27 27 GLU H 74  ? SER H 124 ? GLU H 74  SER H 124 1 ? 51 
HELX_P HELX_P28 28 ASP H 145 ? ASN H 154 ? ASP H 145 ASN H 154 1 ? 10 
HELX_P HELX_P29 29 ASN I 62  ? GLY I 69  ? ASN I 62  GLY I 69  1 ? 8  
HELX_P HELX_P30 30 ASP I 103 ? SER I 112 ? ASP I 103 SER I 112 1 ? 10 
HELX_P HELX_P31 31 THR I 190 ? GLN I 199 ? THR I 190 GLN I 199 1 ? 10 
HELX_P HELX_P32 32 ASP J 37  ? LYS J 58  ? ASP J 37  LYS J 58  1 ? 22 
HELX_P HELX_P33 33 GLU J 74  ? SER J 124 ? GLU J 74  SER J 124 1 ? 51 
HELX_P HELX_P34 34 ASP J 145 ? ASN J 154 ? ASP J 145 ASN J 154 1 ? 10 
HELX_P HELX_P35 35 ASN K 62  ? GLY K 69  ? ASN K 62  GLY K 69  1 ? 8  
HELX_P HELX_P36 36 ASP K 103 ? SER K 112 ? ASP K 103 SER K 112 1 ? 10 
HELX_P HELX_P37 37 PRO K 124 ? TRP K 129 ? PRO K 124 TRP K 129 1 ? 6  
HELX_P HELX_P38 38 THR K 190 ? GLN K 199 ? THR K 190 GLN K 199 1 ? 10 
HELX_P HELX_P39 39 ASP L 37  ? LYS L 58  ? ASP L 37  LYS L 58  1 ? 22 
HELX_P HELX_P40 40 GLU L 74  ? SER L 124 ? GLU L 74  SER L 124 1 ? 51 
HELX_P HELX_P41 41 ASP L 145 ? ASN L 154 ? ASP L 145 ASN L 154 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A  CYS 10  SG  ? ? ? 1_555 B  CYS 137 SG ? ? A CYS 10  B CYS 137 1_555 ? ? ? ? ? ? ? 1.986 ? 
disulf2  disulf ? ? A  CYS 48  SG  ? ? ? 1_555 A  CYS 281 SG ? ? A CYS 48  A CYS 281 1_555 ? ? ? ? ? ? ? 2.058 ? 
disulf3  disulf ? ? A  CYS 61  SG  ? ? ? 1_555 A  CYS 73  SG ? ? A CYS 61  A CYS 73  1_555 ? ? ? ? ? ? ? 2.052 ? 
disulf4  disulf ? ? A  CYS 96  SG  ? ? ? 1_555 A  CYS 142 SG ? ? A CYS 96  A CYS 142 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf5  disulf ? ? A  CYS 285 SG  ? ? ? 1_555 A  CYS 309 SG ? ? A CYS 285 A CYS 309 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf6  disulf ? ? B  CYS 144 SG  ? ? ? 1_555 B  CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.020 ? 
disulf7  disulf ? ? C  CYS 10  SG  ? ? ? 1_555 D  CYS 137 SG ? ? C CYS 10  D CYS 137 1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf8  disulf ? ? C  CYS 48  SG  ? ? ? 1_555 C  CYS 281 SG ? ? C CYS 48  C CYS 281 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf9  disulf ? ? C  CYS 61  SG  ? ? ? 1_555 C  CYS 73  SG ? ? C CYS 61  C CYS 73  1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf10 disulf ? ? C  CYS 96  SG  ? ? ? 1_555 C  CYS 142 SG ? ? C CYS 96  C CYS 142 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf11 disulf ? ? C  CYS 285 SG  ? ? ? 1_555 C  CYS 309 SG ? ? C CYS 285 C CYS 309 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf12 disulf ? ? D  CYS 144 SG  ? ? ? 1_555 D  CYS 148 SG ? ? D CYS 144 D CYS 148 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf13 disulf ? ? E  CYS 10  SG  ? ? ? 1_555 F  CYS 137 SG ? ? E CYS 10  F CYS 137 1_555 ? ? ? ? ? ? ? 1.986 ? 
disulf14 disulf ? ? E  CYS 48  SG  ? ? ? 1_555 E  CYS 281 SG ? ? E CYS 48  E CYS 281 1_555 ? ? ? ? ? ? ? 2.377 ? 
disulf15 disulf ? ? E  CYS 61  SG  ? ? ? 1_555 E  CYS 73  SG ? ? E CYS 61  E CYS 73  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf16 disulf ? ? E  CYS 96  SG  ? ? ? 1_555 E  CYS 142 SG ? ? E CYS 96  E CYS 142 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf17 disulf ? ? E  CYS 285 SG  ? ? ? 1_555 E  CYS 309 SG ? ? E CYS 285 E CYS 309 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf18 disulf ? ? F  CYS 144 SG  ? ? ? 1_555 F  CYS 148 SG ? ? F CYS 144 F CYS 148 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf19 disulf ? ? G  CYS 10  SG  ? ? ? 1_555 H  CYS 137 SG ? ? G CYS 10  H CYS 137 1_555 ? ? ? ? ? ? ? 1.991 ? 
disulf20 disulf ? ? G  CYS 48  SG  ? ? ? 1_555 G  CYS 281 SG ? ? G CYS 48  G CYS 281 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf21 disulf ? ? G  CYS 61  SG  ? ? ? 1_555 G  CYS 73  SG ? ? G CYS 61  G CYS 73  1_555 ? ? ? ? ? ? ? 2.009 ? 
disulf22 disulf ? ? G  CYS 96  SG  ? ? ? 1_555 G  CYS 142 SG ? ? G CYS 96  G CYS 142 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf23 disulf ? ? G  CYS 285 SG  ? ? ? 1_555 G  CYS 309 SG ? ? G CYS 285 G CYS 309 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf24 disulf ? ? H  CYS 144 SG  ? ? ? 1_555 H  CYS 148 SG ? ? H CYS 144 H CYS 148 1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf25 disulf ? ? I  CYS 10  SG  ? ? ? 1_555 J  CYS 137 SG ? ? I CYS 10  J CYS 137 1_555 ? ? ? ? ? ? ? 1.985 ? 
disulf26 disulf ? ? I  CYS 48  SG  ? ? ? 1_555 I  CYS 281 SG ? ? I CYS 48  I CYS 281 1_555 ? ? ? ? ? ? ? 2.011 ? 
disulf27 disulf ? ? I  CYS 61  SG  ? ? ? 1_555 I  CYS 73  SG ? ? I CYS 61  I CYS 73  1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf28 disulf ? ? I  CYS 96  SG  ? ? ? 1_555 I  CYS 142 SG ? ? I CYS 96  I CYS 142 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf29 disulf ? ? I  CYS 285 SG  ? ? ? 1_555 I  CYS 309 SG ? ? I CYS 285 I CYS 309 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf30 disulf ? ? J  CYS 144 SG  ? ? ? 1_555 J  CYS 148 SG ? ? J CYS 144 J CYS 148 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf31 disulf ? ? K  CYS 10  SG  ? ? ? 1_555 L  CYS 137 SG ? ? K CYS 10  L CYS 137 1_555 ? ? ? ? ? ? ? 1.979 ? 
disulf32 disulf ? ? K  CYS 48  SG  ? ? ? 1_555 K  CYS 281 SG ? ? K CYS 48  K CYS 281 1_555 ? ? ? ? ? ? ? 2.023 ? 
disulf33 disulf ? ? K  CYS 61  SG  ? ? ? 1_555 K  CYS 73  SG ? ? K CYS 61  K CYS 73  1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf34 disulf ? ? K  CYS 96  SG  ? ? ? 1_555 K  CYS 142 SG ? ? K CYS 96  K CYS 142 1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf35 disulf ? ? K  CYS 285 SG  ? ? ? 1_555 K  CYS 309 SG ? ? K CYS 285 K CYS 309 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf36 disulf ? ? L  CYS 144 SG  ? ? ? 1_555 L  CYS 148 SG ? ? L CYS 144 L CYS 148 1_555 ? ? ? ? ? ? ? 2.032 ? 
covale1  covale ? ? AA NAG .   O4  ? ? ? 1_555 BA NAG .   C1 ? ? E NAG 602 E NAG 603 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale2  covale ? ? G  ASN 282 ND2 ? ? ? 1_555 HA NAG .   C1 ? ? G ASN 282 G NAG 603 1_555 ? ? ? ? ? ? ? 1.435 ? 
covale3  covale ? ? U  NAG .   O4  ? ? ? 1_555 V  BMA .   C1 ? ? C NAG 603 C BMA 604 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale4  covale ? ? C  ASN 17  ND2 ? ? ? 1_555 S  NAG .   C1 ? ? C ASN 17  C NAG 601 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale5  covale ? ? E  ASN 282 ND2 ? ? ? 1_555 CA NAG .   C1 ? ? E ASN 282 E NAG 604 1_555 ? ? ? ? ? ? ? 1.436 ? 
covale6  covale ? ? A  ASN 29  ND2 ? ? ? 1_555 M  NAG .   C1 ? ? A ASN 29  A NAG 601 1_555 ? ? ? ? ? ? ? 1.437 ? 
covale7  covale ? ? K  ASN 29  ND2 ? ? ? 1_555 OA NAG .   C1 ? ? K ASN 29  K NAG 602 1_555 ? ? ? ? ? ? ? 1.437 ? 
covale8  covale ? ? G  ASN 17  ND2 ? ? ? 1_555 FA NAG .   C1 ? ? G ASN 17  G NAG 601 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale9  covale ? ? F  ASN 154 ND2 ? ? ? 1_555 EA NAG .   C1 ? ? F ASN 154 F NAG 601 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale10 covale ? ? JA NAG .   O4  ? ? ? 1_555 KA BMA .   C1 ? ? I NAG 602 I BMA 603 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale11 covale ? ? A  ASN 282 ND2 ? ? ? 1_555 P  NAG .   C1 ? ? A ASN 282 A NAG 604 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale12 covale ? ? A  ASN 293 ND2 ? ? ? 1_555 R  NAG .   C1 ? ? A ASN 293 A NAG 606 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale13 covale ? ? E  ASN 93  ND2 ? ? ? 1_555 AA NAG .   C1 ? ? E ASN 93  E NAG 602 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale14 covale ? ? G  ASN 29  ND2 ? ? ? 1_555 GA NAG .   C1 ? ? G ASN 29  G NAG 602 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale15 covale ? ? N  NAG .   O4  ? ? ? 1_555 O  NAG .   C1 ? ? A NAG 602 A NAG 603 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale16 covale ? ? P  NAG .   O4  ? ? ? 1_555 Q  NAG .   C1 ? ? A NAG 604 A NAG 605 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale17 covale ? ? I  ASN 93  ND2 ? ? ? 1_555 LA NAG .   C1 ? ? I ASN 93  I NAG 604 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale18 covale ? ? IA NAG .   O4  ? ? ? 1_555 JA NAG .   C1 ? ? I NAG 601 I NAG 602 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale19 covale ? ? K  ASN 282 ND2 ? ? ? 1_555 PA NAG .   C1 ? ? K ASN 282 K NAG 603 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale20 covale ? ? L  ASN 154 ND2 ? ? ? 1_555 RA NAG .   C1 ? ? L ASN 154 L NAG 601 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale21 covale ? ? K  ASN 17  ND2 ? ? ? 1_555 NA NAG .   C1 ? ? K ASN 17  K NAG 601 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale22 covale ? ? A  ASN 93  ND2 ? ? ? 1_555 N  NAG .   C1 ? ? A ASN 93  A NAG 602 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale23 covale ? ? C  ASN 93  ND2 ? ? ? 1_555 W  NAG .   C1 ? ? C ASN 93  C NAG 605 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale24 covale ? ? K  ASN 293 ND2 ? ? ? 1_555 QA NAG .   C1 ? ? K ASN 293 K NAG 604 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale25 covale ? ? C  ASN 282 ND2 ? ? ? 1_555 Y  NAG .   C1 ? ? C ASN 282 C NAG 607 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale26 covale ? ? T  NAG .   O4  ? ? ? 1_555 U  NAG .   C1 ? ? C NAG 602 C NAG 603 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale27 covale ? ? C  ASN 29  ND2 ? ? ? 1_555 T  NAG .   C1 ? ? C ASN 29  C NAG 602 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale28 covale ? ? LA NAG .   O4  ? ? ? 1_555 MA NAG .   C1 ? ? I NAG 604 I NAG 605 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale29 covale ? ? W  NAG .   O4  ? ? ? 1_555 X  NAG .   C1 ? ? C NAG 605 C NAG 606 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale30 covale ? ? I  ASN 29  ND2 ? ? ? 1_555 IA NAG .   C1 ? ? I ASN 29  I NAG 601 1_555 ? ? ? ? ? ? ? 1.450 ? 
covale31 covale ? ? E  ASN 293 ND2 ? ? ? 1_555 DA NAG .   C1 ? ? E ASN 293 E NAG 605 1_555 ? ? ? ? ? ? ? 1.560 ? 
covale32 covale ? ? E  ASN 17  ND2 ? ? ? 1_555 Z  NAG .   C1 ? ? E ASN 17  E NAG 601 1_555 ? ? ? ? ? ? ? 1.938 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A  ? 4 ? 
B  ? 4 ? 
C  ? 2 ? 
D  ? 2 ? 
E  ? 3 ? 
F  ? 2 ? 
G  ? 3 ? 
H  ? 5 ? 
I  ? 4 ? 
J  ? 2 ? 
K  ? 4 ? 
L  ? 3 ? 
M  ? 5 ? 
N  ? 2 ? 
O  ? 2 ? 
P  ? 3 ? 
Q  ? 2 ? 
R  ? 3 ? 
S  ? 5 ? 
T  ? 4 ? 
U  ? 2 ? 
V  ? 4 ? 
W  ? 3 ? 
X  ? 5 ? 
Y  ? 2 ? 
Z  ? 2 ? 
AA ? 3 ? 
AB ? 2 ? 
AC ? 3 ? 
AD ? 5 ? 
AE ? 4 ? 
AF ? 2 ? 
AG ? 4 ? 
AH ? 3 ? 
AI ? 3 ? 
AJ ? 2 ? 
AK ? 2 ? 
AL ? 3 ? 
AM ? 2 ? 
AN ? 3 ? 
AO ? 5 ? 
AP ? 4 ? 
AQ ? 2 ? 
AR ? 4 ? 
AS ? 3 ? 
AT ? 2 ? 
AU ? 5 ? 
AV ? 2 ? 
AW ? 2 ? 
AX ? 3 ? 
AY ? 2 ? 
AZ ? 3 ? 
BA ? 5 ? 
BB ? 4 ? 
BC ? 2 ? 
BD ? 4 ? 
BE ? 3 ? 
BF ? 3 ? 
BG ? 2 ? 
BH ? 2 ? 
BI ? 3 ? 
BJ ? 2 ? 
BK ? 3 ? 
BL ? 5 ? 
BM ? 4 ? 
BN ? 2 ? 
BO ? 4 ? 
BP ? 3 ? 
BQ ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A  1 2 ? parallel      
A  2 3 ? anti-parallel 
A  3 4 ? anti-parallel 
B  1 2 ? parallel      
B  2 3 ? anti-parallel 
B  3 4 ? anti-parallel 
C  1 2 ? anti-parallel 
D  1 2 ? anti-parallel 
E  1 2 ? parallel      
E  2 3 ? parallel      
F  1 2 ? parallel      
G  1 2 ? parallel      
G  2 3 ? parallel      
H  1 2 ? anti-parallel 
H  2 3 ? anti-parallel 
H  3 4 ? anti-parallel 
H  4 5 ? anti-parallel 
I  1 2 ? anti-parallel 
I  2 3 ? anti-parallel 
I  3 4 ? anti-parallel 
J  1 2 ? anti-parallel 
K  1 2 ? anti-parallel 
K  2 3 ? anti-parallel 
K  3 4 ? anti-parallel 
L  1 2 ? anti-parallel 
L  2 3 ? anti-parallel 
M  1 2 ? anti-parallel 
M  2 3 ? anti-parallel 
M  3 4 ? anti-parallel 
M  4 5 ? anti-parallel 
N  1 2 ? anti-parallel 
O  1 2 ? anti-parallel 
P  1 2 ? parallel      
P  2 3 ? parallel      
Q  1 2 ? parallel      
R  1 2 ? parallel      
R  2 3 ? parallel      
S  1 2 ? anti-parallel 
S  2 3 ? anti-parallel 
S  3 4 ? anti-parallel 
S  4 5 ? anti-parallel 
T  1 2 ? anti-parallel 
T  2 3 ? anti-parallel 
T  3 4 ? anti-parallel 
U  1 2 ? anti-parallel 
V  1 2 ? anti-parallel 
V  2 3 ? anti-parallel 
V  3 4 ? anti-parallel 
W  1 2 ? anti-parallel 
W  2 3 ? anti-parallel 
X  1 2 ? anti-parallel 
X  2 3 ? anti-parallel 
X  3 4 ? anti-parallel 
X  4 5 ? anti-parallel 
Y  1 2 ? anti-parallel 
Z  1 2 ? anti-parallel 
AA 1 2 ? parallel      
AA 2 3 ? parallel      
AB 1 2 ? parallel      
AC 1 2 ? parallel      
AC 2 3 ? parallel      
AD 1 2 ? anti-parallel 
AD 2 3 ? anti-parallel 
AD 3 4 ? anti-parallel 
AD 4 5 ? anti-parallel 
AE 1 2 ? anti-parallel 
AE 2 3 ? anti-parallel 
AE 3 4 ? anti-parallel 
AF 1 2 ? anti-parallel 
AG 1 2 ? anti-parallel 
AG 2 3 ? anti-parallel 
AG 3 4 ? anti-parallel 
AH 1 2 ? anti-parallel 
AH 2 3 ? anti-parallel 
AI 1 2 ? anti-parallel 
AI 2 3 ? anti-parallel 
AJ 1 2 ? anti-parallel 
AK 1 2 ? anti-parallel 
AL 1 2 ? parallel      
AL 2 3 ? parallel      
AM 1 2 ? parallel      
AN 1 2 ? parallel      
AN 2 3 ? parallel      
AO 1 2 ? anti-parallel 
AO 2 3 ? anti-parallel 
AO 3 4 ? anti-parallel 
AO 4 5 ? anti-parallel 
AP 1 2 ? anti-parallel 
AP 2 3 ? anti-parallel 
AP 3 4 ? anti-parallel 
AQ 1 2 ? anti-parallel 
AR 1 2 ? anti-parallel 
AR 2 3 ? anti-parallel 
AR 3 4 ? anti-parallel 
AS 1 2 ? anti-parallel 
AS 2 3 ? anti-parallel 
AT 1 2 ? anti-parallel 
AU 1 2 ? anti-parallel 
AU 2 3 ? anti-parallel 
AU 3 4 ? anti-parallel 
AU 4 5 ? anti-parallel 
AV 1 2 ? anti-parallel 
AW 1 2 ? anti-parallel 
AX 1 2 ? parallel      
AX 2 3 ? parallel      
AY 1 2 ? parallel      
AZ 1 2 ? parallel      
AZ 2 3 ? parallel      
BA 1 2 ? anti-parallel 
BA 2 3 ? anti-parallel 
BA 3 4 ? anti-parallel 
BA 4 5 ? anti-parallel 
BB 1 2 ? anti-parallel 
BB 2 3 ? anti-parallel 
BB 3 4 ? anti-parallel 
BC 1 2 ? anti-parallel 
BD 1 2 ? anti-parallel 
BD 2 3 ? anti-parallel 
BD 3 4 ? anti-parallel 
BE 1 2 ? anti-parallel 
BE 2 3 ? anti-parallel 
BF 1 2 ? anti-parallel 
BF 2 3 ? anti-parallel 
BG 1 2 ? anti-parallel 
BH 1 2 ? anti-parallel 
BI 1 2 ? parallel      
BI 2 3 ? parallel      
BJ 1 2 ? parallel      
BK 1 2 ? parallel      
BK 2 3 ? parallel      
BL 1 2 ? anti-parallel 
BL 2 3 ? anti-parallel 
BL 3 4 ? anti-parallel 
BL 4 5 ? anti-parallel 
BM 1 2 ? anti-parallel 
BM 2 3 ? anti-parallel 
BM 3 4 ? anti-parallel 
BN 1 2 ? anti-parallel 
BO 1 2 ? anti-parallel 
BO 2 3 ? anti-parallel 
BO 3 4 ? anti-parallel 
BP 1 2 ? anti-parallel 
BP 2 3 ? anti-parallel 
BQ 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A  1 GLY B 13  ? TRP B 14  ? GLY B 13  TRP B 14  
A  2 THR A 8   ? HIS A 14  ? THR A 8   HIS A 14  
A  3 GLY B 23  ? ASN B 28  ? GLY B 23  ASN B 28  
A  4 GLY B 31  ? ALA B 36  ? GLY B 31  ALA B 36  
B  1 GLY B 13  ? TRP B 14  ? GLY B 13  TRP B 14  
B  2 THR A 8   ? HIS A 14  ? THR A 8   HIS A 14  
B  3 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 
B  4 ALA B 130 ? GLU B 132 ? ALA B 130 GLU B 132 
C  1 THR A 21  ? VAL A 22  ? THR A 21  VAL A 22  
C  2 VAL A 30  ? THR A 31  ? VAL A 30  THR A 31  
D  1 SER A 35  ? ASN A 37  ? SER A 35  ASN A 37  
D  2 ARG A 319 ? ALA A 321 ? ARG A 319 ALA A 321 
E  1 LEU A 39  ? GLU A 40  ? LEU A 39  GLU A 40  
E  2 PHE A 298 ? GLN A 299 ? PHE A 298 GLN A 299 
E  3 LYS A 311 ? TYR A 312 ? LYS A 311 TYR A 312 
F  1 LEU A 47  ? LYS A 49  ? LEU A 47  LYS A 49  
F  2 VAL A 278 ? ASN A 282 ? VAL A 278 ASN A 282 
G  1 LEU A 56  ? HIS A 57  ? LEU A 56  HIS A 57  
G  2 ILE A 85  ? GLU A 87  ? ILE A 85  GLU A 87  
G  3 ILE A 271 ? ILE A 273 ? ILE A 271 ILE A 273 
H  1 VAL A 114 ? GLU A 121 ? VAL A 114 GLU A 121 
H  2 TYR A 259 ? ARG A 265 ? TYR A 259 ARG A 265 
H  3 GLU A 178 ? HIS A 187 ? GLU A 178 HIS A 187 
H  4 LEU A 254 ? PRO A 257 ? LEU A 254 PRO A 257 
H  5 LEU A 154 ? TRP A 156 ? LEU A 154 TRP A 156 
I  1 VAL A 114 ? GLU A 121 ? VAL A 114 GLU A 121 
I  2 TYR A 259 ? ARG A 265 ? TYR A 259 ARG A 265 
I  3 GLU A 178 ? HIS A 187 ? GLU A 178 HIS A 187 
I  4 ARG A 232 ? VAL A 240 ? ARG A 232 VAL A 240 
J  1 THR A 139 ? HIS A 144 ? THR A 139 HIS A 144 
J  2 ALA A 147 ? SER A 149 ? ALA A 147 SER A 149 
K  1 SER A 170 ? ILE A 172 ? SER A 170 ILE A 172 
K  2 LYS A 245 ? ALA A 250 ? LYS A 245 ALA A 250 
K  3 VAL A 205 ? GLY A 208 ? VAL A 205 GLY A 208 
K  4 SER A 213 ? PHE A 216 ? SER A 213 PHE A 216 
L  1 CYS A 285 ? GLN A 286 ? CYS A 285 GLN A 286 
L  2 ILE A 306 ? GLY A 307 ? ILE A 306 GLY A 307 
L  3 THR B 64  ? ALA B 65  ? THR B 64  ALA B 65  
M  1 GLY D 31  ? ALA D 36  ? GLY D 31  ALA D 36  
M  2 TYR D 22  ? ASN D 28  ? TYR D 22  ASN D 28  
M  3 THR C 8   ? TYR C 13  ? THR C 8   TYR C 13  
M  4 CYS D 137 ? PHE D 140 ? CYS D 137 PHE D 140 
M  5 ALA D 130 ? GLU D 132 ? ALA D 130 GLU D 132 
N  1 THR C 21  ? VAL C 22  ? THR C 21  VAL C 22  
N  2 VAL C 30  ? THR C 31  ? VAL C 30  THR C 31  
O  1 SER C 35  ? ASN C 37  ? SER C 35  ASN C 37  
O  2 ARG C 319 ? ALA C 321 ? ARG C 319 ALA C 321 
P  1 LEU C 39  ? GLU C 40  ? LEU C 39  GLU C 40  
P  2 PHE C 298 ? GLN C 299 ? PHE C 298 GLN C 299 
P  3 LYS C 311 ? TYR C 312 ? LYS C 311 TYR C 312 
Q  1 LEU C 47  ? LYS C 49  ? LEU C 47  LYS C 49  
Q  2 VAL C 278 ? ASN C 282 ? VAL C 278 ASN C 282 
R  1 LEU C 56  ? HIS C 57  ? LEU C 56  HIS C 57  
R  2 ILE C 85  ? GLU C 87  ? ILE C 85  GLU C 87  
R  3 ILE C 271 ? ILE C 273 ? ILE C 271 ILE C 273 
S  1 VAL C 114 ? GLU C 121 ? VAL C 114 GLU C 121 
S  2 TYR C 259 ? ARG C 265 ? TYR C 259 ARG C 265 
S  3 GLU C 178 ? HIS C 187 ? GLU C 178 HIS C 187 
S  4 LEU C 254 ? PRO C 257 ? LEU C 254 PRO C 257 
S  5 LEU C 154 ? TRP C 156 ? LEU C 154 TRP C 156 
T  1 VAL C 114 ? GLU C 121 ? VAL C 114 GLU C 121 
T  2 TYR C 259 ? ARG C 265 ? TYR C 259 ARG C 265 
T  3 GLU C 178 ? HIS C 187 ? GLU C 178 HIS C 187 
T  4 ARG C 232 ? VAL C 240 ? ARG C 232 VAL C 240 
U  1 THR C 139 ? HIS C 144 ? THR C 139 HIS C 144 
U  2 ALA C 147 ? SER C 149 ? ALA C 147 SER C 149 
V  1 LEU C 167 ? ILE C 172 ? LEU C 167 ILE C 172 
V  2 LYS C 245 ? ALA C 250 ? LYS C 245 ALA C 250 
V  3 VAL C 205 ? GLY C 208 ? VAL C 205 GLY C 208 
V  4 SER C 213 ? PHE C 216 ? SER C 213 PHE C 216 
W  1 CYS C 285 ? GLN C 286 ? CYS C 285 GLN C 286 
W  2 ILE C 306 ? GLY C 307 ? ILE C 306 GLY C 307 
W  3 THR D 64  ? ALA D 65  ? THR D 64  ALA D 65  
X  1 SER F 32  ? ALA F 36  ? SER F 32  ALA F 36  
X  2 TYR F 22  ? GLN F 27  ? TYR F 22  GLN F 27  
X  3 LEU E 9   ? TYR E 13  ? LEU E 9   TYR E 13  
X  4 CYS F 137 ? PHE F 140 ? CYS F 137 PHE F 140 
X  5 ALA F 130 ? GLU F 132 ? ALA F 130 GLU F 132 
Y  1 THR E 21  ? VAL E 22  ? THR E 21  VAL E 22  
Y  2 VAL E 30  ? THR E 31  ? VAL E 30  THR E 31  
Z  1 SER E 35  ? ASN E 37  ? SER E 35  ASN E 37  
Z  2 ARG E 319 ? ALA E 321 ? ARG E 319 ALA E 321 
AA 1 LEU E 39  ? GLU E 40  ? LEU E 39  GLU E 40  
AA 2 PHE E 298 ? GLN E 299 ? PHE E 298 GLN E 299 
AA 3 LYS E 311 ? TYR E 312 ? LYS E 311 TYR E 312 
AB 1 LEU E 47  ? LYS E 49  ? LEU E 47  LYS E 49  
AB 2 VAL E 278 ? ASN E 282 ? VAL E 278 ASN E 282 
AC 1 LEU E 56  ? HIS E 57  ? LEU E 56  HIS E 57  
AC 2 ILE E 85  ? GLU E 87  ? ILE E 85  GLU E 87  
AC 3 ILE E 271 ? ILE E 273 ? ILE E 271 ILE E 273 
AD 1 VAL E 114 ? PHE E 120 ? VAL E 114 PHE E 120 
AD 2 ALA E 260 ? ARG E 265 ? ALA E 260 ARG E 265 
AD 3 GLU E 178 ? HIS E 187 ? GLU E 178 HIS E 187 
AD 4 LEU E 254 ? PRO E 257 ? LEU E 254 PRO E 257 
AD 5 LEU E 154 ? TRP E 156 ? LEU E 154 TRP E 156 
AE 1 VAL E 114 ? PHE E 120 ? VAL E 114 PHE E 120 
AE 2 ALA E 260 ? ARG E 265 ? ALA E 260 ARG E 265 
AE 3 GLU E 178 ? HIS E 187 ? GLU E 178 HIS E 187 
AE 4 ARG E 232 ? VAL E 240 ? ARG E 232 VAL E 240 
AF 1 THR E 139 ? HIS E 144 ? THR E 139 HIS E 144 
AF 2 ALA E 147 ? SER E 149 ? ALA E 147 SER E 149 
AG 1 LEU E 167 ? ILE E 172 ? LEU E 167 ILE E 172 
AG 2 LYS E 245 ? ALA E 250 ? LYS E 245 ALA E 250 
AG 3 VAL E 205 ? GLY E 208 ? VAL E 205 GLY E 208 
AG 4 SER E 213 ? PHE E 216 ? SER E 213 PHE E 216 
AH 1 GLY E 290 ? ALA E 291 ? GLY E 290 ALA E 291 
AH 2 CYS E 285 ? THR E 287 ? CYS E 285 THR E 287 
AH 3 ILE E 306 ? GLY E 307 ? ILE E 306 GLY E 307 
AI 1 GLY G 12  ? TYR G 13  ? GLY G 12  TYR G 13  
AI 2 TYR H 22  ? HIS H 25  ? TYR H 22  HIS H 25  
AI 3 TYR H 34  ? ALA H 36  ? TYR H 34  ALA H 36  
AJ 1 THR G 21  ? VAL G 22  ? THR G 21  VAL G 22  
AJ 2 VAL G 30  ? THR G 31  ? VAL G 30  THR G 31  
AK 1 SER G 35  ? ASN G 37  ? SER G 35  ASN G 37  
AK 2 ARG G 319 ? ALA G 321 ? ARG G 319 ALA G 321 
AL 1 LEU G 39  ? GLU G 40  ? LEU G 39  GLU G 40  
AL 2 PHE G 298 ? GLN G 299 ? PHE G 298 GLN G 299 
AL 3 LYS G 311 ? TYR G 312 ? LYS G 311 TYR G 312 
AM 1 LEU G 47  ? LYS G 49  ? LEU G 47  LYS G 49  
AM 2 VAL G 278 ? ASN G 282 ? VAL G 278 ASN G 282 
AN 1 LEU G 56  ? HIS G 57  ? LEU G 56  HIS G 57  
AN 2 ILE G 85  ? GLU G 87  ? ILE G 85  GLU G 87  
AN 3 ILE G 271 ? ILE G 273 ? ILE G 271 ILE G 273 
AO 1 VAL G 114 ? GLU G 121 ? VAL G 114 GLU G 121 
AO 2 TYR G 259 ? ARG G 265 ? TYR G 259 ARG G 265 
AO 3 GLU G 178 ? HIS G 187 ? GLU G 178 HIS G 187 
AO 4 LEU G 254 ? PRO G 257 ? LEU G 254 PRO G 257 
AO 5 LEU G 154 ? TRP G 156 ? LEU G 154 TRP G 156 
AP 1 VAL G 114 ? GLU G 121 ? VAL G 114 GLU G 121 
AP 2 TYR G 259 ? ARG G 265 ? TYR G 259 ARG G 265 
AP 3 GLU G 178 ? HIS G 187 ? GLU G 178 HIS G 187 
AP 4 ARG G 232 ? VAL G 240 ? ARG G 232 VAL G 240 
AQ 1 PRO G 143 ? HIS G 144 ? PRO G 143 HIS G 144 
AQ 2 ALA G 147 ? LYS G 148 ? ALA G 147 LYS G 148 
AR 1 LEU G 167 ? ILE G 172 ? LEU G 167 ILE G 172 
AR 2 LYS G 245 ? ALA G 250 ? LYS G 245 ALA G 250 
AR 3 VAL G 205 ? GLY G 208 ? VAL G 205 GLY G 208 
AR 4 SER G 213 ? PHE G 216 ? SER G 213 PHE G 216 
AS 1 CYS G 285 ? GLN G 286 ? CYS G 285 GLN G 286 
AS 2 ILE G 306 ? GLY G 307 ? ILE G 306 GLY G 307 
AS 3 THR H 64  ? ALA H 65  ? THR H 64  ALA H 65  
AT 1 ALA H 130 ? GLU H 132 ? ALA H 130 GLU H 132 
AT 2 PHE H 138 ? PHE H 140 ? PHE H 138 PHE H 140 
AU 1 SER J 32  ? ALA J 36  ? SER J 32  ALA J 36  
AU 2 TYR J 22  ? GLN J 27  ? TYR J 22  GLN J 27  
AU 3 THR I 8   ? TYR I 13  ? THR I 8   TYR I 13  
AU 4 CYS J 137 ? PHE J 140 ? CYS J 137 PHE J 140 
AU 5 ALA J 130 ? GLU J 132 ? ALA J 130 GLU J 132 
AV 1 THR I 21  ? VAL I 22  ? THR I 21  VAL I 22  
AV 2 VAL I 30  ? THR I 31  ? VAL I 30  THR I 31  
AW 1 SER I 35  ? ASN I 37  ? SER I 35  ASN I 37  
AW 2 ARG I 319 ? ALA I 321 ? ARG I 319 ALA I 321 
AX 1 LEU I 39  ? GLU I 40  ? LEU I 39  GLU I 40  
AX 2 PHE I 298 ? GLN I 299 ? PHE I 298 GLN I 299 
AX 3 LYS I 311 ? TYR I 312 ? LYS I 311 TYR I 312 
AY 1 LEU I 47  ? LYS I 49  ? LEU I 47  LYS I 49  
AY 2 VAL I 278 ? ASN I 282 ? VAL I 278 ASN I 282 
AZ 1 LEU I 56  ? HIS I 57  ? LEU I 56  HIS I 57  
AZ 2 ILE I 85  ? GLU I 87  ? ILE I 85  GLU I 87  
AZ 3 ILE I 271 ? ILE I 273 ? ILE I 271 ILE I 273 
BA 1 VAL I 114 ? GLU I 121 ? VAL I 114 GLU I 121 
BA 2 TYR I 259 ? ARG I 265 ? TYR I 259 ARG I 265 
BA 3 GLU I 178 ? HIS I 187 ? GLU I 178 HIS I 187 
BA 4 LEU I 254 ? PRO I 257 ? LEU I 254 PRO I 257 
BA 5 LEU I 154 ? TRP I 156 ? LEU I 154 TRP I 156 
BB 1 VAL I 114 ? GLU I 121 ? VAL I 114 GLU I 121 
BB 2 TYR I 259 ? ARG I 265 ? TYR I 259 ARG I 265 
BB 3 GLU I 178 ? HIS I 187 ? GLU I 178 HIS I 187 
BB 4 ARG I 232 ? VAL I 240 ? ARG I 232 VAL I 240 
BC 1 THR I 139 ? HIS I 144 ? THR I 139 HIS I 144 
BC 2 ALA I 147 ? SER I 149 ? ALA I 147 SER I 149 
BD 1 LEU I 167 ? ILE I 172 ? LEU I 167 ILE I 172 
BD 2 LYS I 245 ? ALA I 250 ? LYS I 245 ALA I 250 
BD 3 VAL I 205 ? GLY I 208 ? VAL I 205 GLY I 208 
BD 4 SER I 213 ? PHE I 216 ? SER I 213 PHE I 216 
BE 1 CYS I 285 ? GLN I 286 ? CYS I 285 GLN I 286 
BE 2 ILE I 306 ? GLY I 307 ? ILE I 306 GLY I 307 
BE 3 THR J 64  ? ALA J 65  ? THR J 64  ALA J 65  
BF 1 THR K 8   ? CYS K 10  ? THR K 8   CYS K 10  
BF 2 CYS L 137 ? PHE L 140 ? CYS L 137 PHE L 140 
BF 3 ALA L 130 ? GLU L 132 ? ALA L 130 GLU L 132 
BG 1 THR K 21  ? VAL K 22  ? THR K 21  VAL K 22  
BG 2 VAL K 30  ? THR K 31  ? VAL K 30  THR K 31  
BH 1 SER K 35  ? ASN K 37  ? SER K 35  ASN K 37  
BH 2 ARG K 319 ? ALA K 321 ? ARG K 319 ALA K 321 
BI 1 LEU K 39  ? GLU K 40  ? LEU K 39  GLU K 40  
BI 2 PHE K 298 ? GLN K 299 ? PHE K 298 GLN K 299 
BI 3 LYS K 311 ? TYR K 312 ? LYS K 311 TYR K 312 
BJ 1 LEU K 47  ? LYS K 49  ? LEU K 47  LYS K 49  
BJ 2 VAL K 278 ? ASN K 282 ? VAL K 278 ASN K 282 
BK 1 LEU K 56  ? HIS K 57  ? LEU K 56  HIS K 57  
BK 2 ILE K 85  ? GLU K 87  ? ILE K 85  GLU K 87  
BK 3 ILE K 271 ? ILE K 273 ? ILE K 271 ILE K 273 
BL 1 VAL K 114 ? GLU K 121 ? VAL K 114 GLU K 121 
BL 2 TYR K 259 ? ARG K 265 ? TYR K 259 ARG K 265 
BL 3 VAL K 179 ? HIS K 187 ? VAL K 179 HIS K 187 
BL 4 LEU K 254 ? PRO K 257 ? LEU K 254 PRO K 257 
BL 5 LEU K 154 ? TRP K 156 ? LEU K 154 TRP K 156 
BM 1 VAL K 114 ? GLU K 121 ? VAL K 114 GLU K 121 
BM 2 TYR K 259 ? ARG K 265 ? TYR K 259 ARG K 265 
BM 3 VAL K 179 ? HIS K 187 ? VAL K 179 HIS K 187 
BM 4 ARG K 232 ? VAL K 240 ? ARG K 232 VAL K 240 
BN 1 THR K 139 ? HIS K 144 ? THR K 139 HIS K 144 
BN 2 ALA K 147 ? SER K 149 ? ALA K 147 SER K 149 
BO 1 LEU K 167 ? ILE K 172 ? LEU K 167 ILE K 172 
BO 2 LYS K 245 ? ALA K 250 ? LYS K 245 ALA K 250 
BO 3 VAL K 205 ? GLY K 208 ? VAL K 205 GLY K 208 
BO 4 SER K 213 ? PHE K 216 ? SER K 213 PHE K 216 
BP 1 CYS K 285 ? GLN K 286 ? CYS K 285 GLN K 286 
BP 2 ILE K 306 ? GLY K 307 ? ILE K 306 GLY K 307 
BP 3 THR L 64  ? ALA L 65  ? THR L 64  ALA L 65  
BQ 1 GLY L 23  ? ASN L 28  ? GLY L 23  ASN L 28  
BQ 2 GLY L 31  ? ALA L 36  ? GLY L 31  ALA L 36  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A  1 2 O TRP B 14  ? O TRP B 14  N TYR A 13  ? N TYR A 13  
A  2 3 N THR A 8   ? N THR A 8   O GLN B 27  ? O GLN B 27  
A  3 4 N TYR B 24  ? N TYR B 24  O ALA B 35  ? O ALA B 35  
B  1 2 O TRP B 14  ? O TRP B 14  N TYR A 13  ? N TYR A 13  
B  2 3 N LEU A 9   ? N LEU A 9   O PHE B 138 ? O PHE B 138 
B  3 4 O GLU B 139 ? O GLU B 139 N LYS B 131 ? N LYS B 131 
C  1 2 N VAL A 22  ? N VAL A 22  O VAL A 30  ? O VAL A 30  
D  1 2 N VAL A 36  ? N VAL A 36  O LEU A 320 ? O LEU A 320 
E  1 2 N GLU A 40  ? N GLU A 40  O PHE A 298 ? O PHE A 298 
E  2 3 N GLN A 299 ? N GLN A 299 O LYS A 311 ? O LYS A 311 
F  1 2 N LYS A 49  ? N LYS A 49  O CYS A 281 ? O CYS A 281 
G  1 2 N LEU A 56  ? N LEU A 56  O VAL A 86  ? O VAL A 86  
G  2 3 N GLU A 87  ? N GLU A 87  O ILE A 272 ? O ILE A 272 
H  1 2 N SER A 115 ? N SER A 115 O GLU A 264 ? O GLU A 264 
H  2 3 O MET A 263 ? O MET A 263 N GLU A 178 ? N GLU A 178 
H  3 4 N GLY A 184 ? N GLY A 184 O VAL A 255 ? O VAL A 255 
H  4 5 O VAL A 256 ? O VAL A 256 N ILE A 155 ? N ILE A 155 
I  1 2 N SER A 115 ? N SER A 115 O GLU A 264 ? O GLU A 264 
I  2 3 O MET A 263 ? O MET A 263 N GLU A 178 ? N GLU A 178 
I  3 4 N HIS A 187 ? N HIS A 187 O ARG A 232 ? O ARG A 232 
J  1 2 N HIS A 144 ? N HIS A 144 O ALA A 147 ? O ALA A 147 
K  1 2 N TYR A 171 ? N TYR A 171 O ILE A 246 ? O ILE A 246 
K  2 3 O THR A 247 ? O THR A 247 N GLY A 208 ? N GLY A 208 
K  3 4 N VAL A 205 ? N VAL A 205 O PHE A 216 ? O PHE A 216 
L  1 2 N GLN A 286 ? N GLN A 286 O ILE A 306 ? O ILE A 306 
L  2 3 N GLY A 307 ? N GLY A 307 O THR B 64  ? O THR B 64  
M  1 2 O ALA D 35  ? O ALA D 35  N TYR D 24  ? N TYR D 24  
M  2 3 O GLY D 23  ? O GLY D 23  N GLY C 12  ? N GLY C 12  
M  3 4 N LEU C 9   ? N LEU C 9   O PHE D 138 ? O PHE D 138 
M  4 5 O GLU D 139 ? O GLU D 139 N LYS D 131 ? N LYS D 131 
N  1 2 N VAL C 22  ? N VAL C 22  O VAL C 30  ? O VAL C 30  
O  1 2 N VAL C 36  ? N VAL C 36  O LEU C 320 ? O LEU C 320 
P  1 2 N GLU C 40  ? N GLU C 40  O PHE C 298 ? O PHE C 298 
P  2 3 N GLN C 299 ? N GLN C 299 O LYS C 311 ? O LYS C 311 
Q  1 2 N LYS C 49  ? N LYS C 49  O CYS C 281 ? O CYS C 281 
R  1 2 N LEU C 56  ? N LEU C 56  O VAL C 86  ? O VAL C 86  
R  2 3 N GLU C 87  ? N GLU C 87  O ILE C 272 ? O ILE C 272 
S  1 2 N SER C 115 ? N SER C 115 O GLU C 264 ? O GLU C 264 
S  2 3 O MET C 263 ? O MET C 263 N GLU C 178 ? N GLU C 178 
S  3 4 N GLY C 184 ? N GLY C 184 O VAL C 255 ? O VAL C 255 
S  4 5 O VAL C 256 ? O VAL C 256 N ILE C 155 ? N ILE C 155 
T  1 2 N SER C 115 ? N SER C 115 O GLU C 264 ? O GLU C 264 
T  2 3 O MET C 263 ? O MET C 263 N GLU C 178 ? N GLU C 178 
T  3 4 N HIS C 187 ? N HIS C 187 O ARG C 232 ? O ARG C 232 
U  1 2 N HIS C 144 ? N HIS C 144 O ALA C 147 ? O ALA C 147 
V  1 2 N LYS C 169 ? N LYS C 169 O PHE C 248 ? O PHE C 248 
V  2 3 O THR C 247 ? O THR C 247 N GLY C 208 ? N GLY C 208 
V  3 4 N VAL C 205 ? N VAL C 205 O PHE C 216 ? O PHE C 216 
W  1 2 N GLN C 286 ? N GLN C 286 O ILE C 306 ? O ILE C 306 
W  2 3 N GLY C 307 ? N GLY C 307 O THR D 64  ? O THR D 64  
X  1 2 O ALA F 35  ? O ALA F 35  N TYR F 24  ? N TYR F 24  
X  2 3 O HIS F 25  ? O HIS F 25  N CYS E 10  ? N CYS E 10  
X  3 4 N LEU E 9   ? N LEU E 9   O PHE F 138 ? O PHE F 138 
X  4 5 O GLU F 139 ? O GLU F 139 N LYS F 131 ? N LYS F 131 
Y  1 2 N VAL E 22  ? N VAL E 22  O VAL E 30  ? O VAL E 30  
Z  1 2 N VAL E 36  ? N VAL E 36  O LEU E 320 ? O LEU E 320 
AA 1 2 N GLU E 40  ? N GLU E 40  O PHE E 298 ? O PHE E 298 
AA 2 3 N GLN E 299 ? N GLN E 299 O LYS E 311 ? O LYS E 311 
AB 1 2 N LYS E 49  ? N LYS E 49  O CYS E 281 ? O CYS E 281 
AC 1 2 N LEU E 56  ? N LEU E 56  O VAL E 86  ? O VAL E 86  
AC 2 3 N ILE E 85  ? N ILE E 85  O ILE E 272 ? O ILE E 272 
AD 1 2 N PHE E 120 ? N PHE E 120 O ALA E 260 ? O ALA E 260 
AD 2 3 O MET E 263 ? O MET E 263 N GLU E 178 ? N GLU E 178 
AD 3 4 N GLY E 184 ? N GLY E 184 O VAL E 255 ? O VAL E 255 
AD 4 5 O VAL E 256 ? O VAL E 256 N ILE E 155 ? N ILE E 155 
AE 1 2 N PHE E 120 ? N PHE E 120 O ALA E 260 ? O ALA E 260 
AE 2 3 O MET E 263 ? O MET E 263 N GLU E 178 ? N GLU E 178 
AE 3 4 N TRP E 183 ? N TRP E 183 O TYR E 236 ? O TYR E 236 
AF 1 2 N HIS E 144 ? N HIS E 144 O ALA E 147 ? O ALA E 147 
AG 1 2 N LYS E 169 ? N LYS E 169 O PHE E 248 ? O PHE E 248 
AG 2 3 O THR E 247 ? O THR E 247 N GLY E 208 ? N GLY E 208 
AG 3 4 N VAL E 205 ? N VAL E 205 O PHE E 216 ? O PHE E 216 
AH 1 2 O GLY E 290 ? O GLY E 290 N THR E 287 ? N THR E 287 
AH 2 3 N GLN E 286 ? N GLN E 286 O ILE E 306 ? O ILE E 306 
AI 1 2 N GLY G 12  ? N GLY G 12  O GLY H 23  ? O GLY H 23  
AI 2 3 N TYR H 24  ? N TYR H 24  O ALA H 35  ? O ALA H 35  
AJ 1 2 N VAL G 22  ? N VAL G 22  O VAL G 30  ? O VAL G 30  
AK 1 2 N VAL G 36  ? N VAL G 36  O LEU G 320 ? O LEU G 320 
AL 1 2 N GLU G 40  ? N GLU G 40  O PHE G 298 ? O PHE G 298 
AL 2 3 N GLN G 299 ? N GLN G 299 O LYS G 311 ? O LYS G 311 
AM 1 2 N LEU G 47  ? N LEU G 47  O HIS G 279 ? O HIS G 279 
AN 1 2 N LEU G 56  ? N LEU G 56  O VAL G 86  ? O VAL G 86  
AN 2 3 N GLU G 87  ? N GLU G 87  O ILE G 272 ? O ILE G 272 
AO 1 2 N SER G 115 ? N SER G 115 O GLU G 264 ? O GLU G 264 
AO 2 3 O MET G 263 ? O MET G 263 N GLU G 178 ? N GLU G 178 
AO 3 4 N GLY G 184 ? N GLY G 184 O VAL G 255 ? O VAL G 255 
AO 4 5 O VAL G 256 ? O VAL G 256 N ILE G 155 ? N ILE G 155 
AP 1 2 N SER G 115 ? N SER G 115 O GLU G 264 ? O GLU G 264 
AP 2 3 O MET G 263 ? O MET G 263 N GLU G 178 ? N GLU G 178 
AP 3 4 N HIS G 187 ? N HIS G 187 O ARG G 232 ? O ARG G 232 
AQ 1 2 N HIS G 144 ? N HIS G 144 O ALA G 147 ? O ALA G 147 
AR 1 2 N LYS G 169 ? N LYS G 169 O PHE G 248 ? O PHE G 248 
AR 2 3 O THR G 247 ? O THR G 247 N GLY G 208 ? N GLY G 208 
AR 3 4 N VAL G 205 ? N VAL G 205 O PHE G 216 ? O PHE G 216 
AS 1 2 N GLN G 286 ? N GLN G 286 O ILE G 306 ? O ILE G 306 
AS 2 3 N GLY G 307 ? N GLY G 307 O THR H 64  ? O THR H 64  
AT 1 2 N LYS H 131 ? N LYS H 131 O GLU H 139 ? O GLU H 139 
AU 1 2 O ALA J 35  ? O ALA J 35  N TYR J 24  ? N TYR J 24  
AU 2 3 O GLY J 23  ? O GLY J 23  N GLY I 12  ? N GLY I 12  
AU 3 4 N LEU I 9   ? N LEU I 9   O PHE J 138 ? O PHE J 138 
AU 4 5 O GLU J 139 ? O GLU J 139 N LYS J 131 ? N LYS J 131 
AV 1 2 N VAL I 22  ? N VAL I 22  O VAL I 30  ? O VAL I 30  
AW 1 2 N VAL I 36  ? N VAL I 36  O LEU I 320 ? O LEU I 320 
AX 1 2 N GLU I 40  ? N GLU I 40  O PHE I 298 ? O PHE I 298 
AX 2 3 N GLN I 299 ? N GLN I 299 O LYS I 311 ? O LYS I 311 
AY 1 2 N LEU I 47  ? N LEU I 47  O HIS I 279 ? O HIS I 279 
AZ 1 2 N LEU I 56  ? N LEU I 56  O VAL I 86  ? O VAL I 86  
AZ 2 3 N GLU I 87  ? N GLU I 87  O ILE I 272 ? O ILE I 272 
BA 1 2 N SER I 115 ? N SER I 115 O GLU I 264 ? O GLU I 264 
BA 2 3 O MET I 263 ? O MET I 263 N GLU I 178 ? N GLU I 178 
BA 3 4 N GLY I 184 ? N GLY I 184 O VAL I 255 ? O VAL I 255 
BA 4 5 O VAL I 256 ? O VAL I 256 N ILE I 155 ? N ILE I 155 
BB 1 2 N SER I 115 ? N SER I 115 O GLU I 264 ? O GLU I 264 
BB 2 3 O MET I 263 ? O MET I 263 N GLU I 178 ? N GLU I 178 
BB 3 4 N HIS I 187 ? N HIS I 187 O ARG I 232 ? O ARG I 232 
BC 1 2 N THR I 139 ? N THR I 139 O SER I 149 ? O SER I 149 
BD 1 2 N LYS I 169 ? N LYS I 169 O PHE I 248 ? O PHE I 248 
BD 2 3 O THR I 247 ? O THR I 247 N GLY I 208 ? N GLY I 208 
BD 3 4 N VAL I 205 ? N VAL I 205 O PHE I 216 ? O PHE I 216 
BE 1 2 N GLN I 286 ? N GLN I 286 O ILE I 306 ? O ILE I 306 
BE 2 3 N GLY I 307 ? N GLY I 307 O THR J 64  ? O THR J 64  
BF 1 2 N LEU K 9   ? N LEU K 9   O PHE L 138 ? O PHE L 138 
BF 2 3 O GLU L 139 ? O GLU L 139 N LYS L 131 ? N LYS L 131 
BG 1 2 N VAL K 22  ? N VAL K 22  O VAL K 30  ? O VAL K 30  
BH 1 2 N VAL K 36  ? N VAL K 36  O LEU K 320 ? O LEU K 320 
BI 1 2 N GLU K 40  ? N GLU K 40  O PHE K 298 ? O PHE K 298 
BI 2 3 N GLN K 299 ? N GLN K 299 O LYS K 311 ? O LYS K 311 
BJ 1 2 N LEU K 47  ? N LEU K 47  O HIS K 279 ? O HIS K 279 
BK 1 2 N LEU K 56  ? N LEU K 56  O VAL K 86  ? O VAL K 86  
BK 2 3 N GLU K 87  ? N GLU K 87  O ILE K 272 ? O ILE K 272 
BL 1 2 N SER K 115 ? N SER K 115 O GLU K 264 ? O GLU K 264 
BL 2 3 O PHE K 261 ? O PHE K 261 N LEU K 180 ? N LEU K 180 
BL 3 4 N GLY K 184 ? N GLY K 184 O VAL K 255 ? O VAL K 255 
BL 4 5 O VAL K 256 ? O VAL K 256 N ILE K 155 ? N ILE K 155 
BM 1 2 N SER K 115 ? N SER K 115 O GLU K 264 ? O GLU K 264 
BM 2 3 O PHE K 261 ? O PHE K 261 N LEU K 180 ? N LEU K 180 
BM 3 4 N HIS K 187 ? N HIS K 187 O ARG K 232 ? O ARG K 232 
BN 1 2 N HIS K 144 ? N HIS K 144 O ALA K 147 ? O ALA K 147 
BO 1 2 N LYS K 169 ? N LYS K 169 O PHE K 248 ? O PHE K 248 
BO 2 3 O THR K 247 ? O THR K 247 N GLY K 208 ? N GLY K 208 
BO 3 4 N VAL K 205 ? N VAL K 205 O PHE K 216 ? O PHE K 216 
BP 1 2 N GLN K 286 ? N GLN K 286 O ILE K 306 ? O ILE K 306 
BP 2 3 N GLY K 307 ? N GLY K 307 O THR L 64  ? O THR L 64  
BQ 1 2 N TYR L 24  ? N TYR L 24  O ALA L 35  ? O ALA L 35  
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 601' 
AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 602' 
AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 603' 
AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 604' 
AC5 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 605' 
AC6 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 606' 
AC7 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG C 601' 
AC8 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG C 602' 
AC9 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG C 603' 
BC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE BMA C 604' 
BC2 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG C 605' 
BC3 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG C 606' 
BC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG C 607' 
BC5 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG E 601' 
BC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG E 602' 
BC7 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG E 603' 
BC8 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG E 604' 
BC9 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG E 605' 
CC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG F 601' 
CC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG G 601' 
CC3 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG G 602' 
CC4 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG G 603' 
CC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG I 601' 
CC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG I 602' 
CC7 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE BMA I 603' 
CC8 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE NAG I 604' 
CC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG I 605' 
DC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG K 601' 
DC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG K 602' 
DC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG K 603' 
DC4 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG K 604' 
DC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG L 601' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 2 ASP A  23  ? ASP A 23  . ? 1_555 ? 
2   AC1 2 ASN A  29  ? ASN A 29  . ? 1_555 ? 
3   AC2 5 GLU A  72  ? GLU A 72  . ? 1_555 ? 
4   AC2 5 ASN A  93  ? ASN A 93  . ? 1_555 ? 
5   AC2 5 PRO A  143 ? PRO A 143 . ? 1_555 ? 
6   AC2 5 ARG A  227 ? ARG A 227 . ? 1_555 ? 
7   AC2 5 NAG O  .   ? NAG A 603 . ? 1_555 ? 
8   AC3 4 NAG N  .   ? NAG A 602 . ? 1_555 ? 
9   AC3 4 LYS K  49  ? LYS K 49  . ? 1_555 ? 
10  AC3 4 ASP K  280 ? ASP K 280 . ? 1_555 ? 
11  AC3 4 NAG PA .   ? NAG K 603 . ? 1_555 ? 
12  AC4 6 ARG A  51  ? ARG A 51  . ? 1_555 ? 
13  AC4 6 GLY A  52  ? GLY A 52  . ? 1_555 ? 
14  AC4 6 ASP A  280 ? ASP A 280 . ? 1_555 ? 
15  AC4 6 ASN A  282 ? ASN A 282 . ? 1_555 ? 
16  AC4 6 HOH SA .   ? HOH A 355 . ? 1_555 ? 
17  AC4 6 NAG Q  .   ? NAG A 605 . ? 1_555 ? 
18  AC5 1 NAG P  .   ? NAG A 604 . ? 1_555 ? 
19  AC6 1 ASN A  293 ? ASN A 293 . ? 1_555 ? 
20  AC7 1 ASN C  17  ? ASN C 17  . ? 1_555 ? 
21  AC8 9 HIS A  279 ? HIS A 279 . ? 1_455 ? 
22  AC8 9 ASP A  280 ? ASP A 280 . ? 1_455 ? 
23  AC8 9 THR C  21  ? THR C 21  . ? 1_555 ? 
24  AC8 9 ASP C  23  ? ASP C 23  . ? 1_555 ? 
25  AC8 9 ASN C  29  ? ASN C 29  . ? 1_555 ? 
26  AC8 9 LYS C  317 ? LYS C 317 . ? 1_555 ? 
27  AC8 9 HOH UA .   ? HOH C 356 . ? 1_555 ? 
28  AC8 9 HOH UA .   ? HOH C 363 . ? 1_555 ? 
29  AC8 9 NAG U  .   ? NAG C 603 . ? 1_555 ? 
30  AC9 5 HIS A  57  ? HIS A 57  . ? 1_455 ? 
31  AC9 5 VAL A  278 ? VAL A 278 . ? 1_455 ? 
32  AC9 5 NAG T  .   ? NAG C 602 . ? 1_555 ? 
33  AC9 5 BMA V  .   ? BMA C 604 . ? 1_555 ? 
34  AC9 5 GLU F  57  ? GLU F 57  . ? 1_555 ? 
35  BC1 4 LEU A  76  ? LEU A 76  . ? 1_455 ? 
36  BC1 4 SER A  77  ? SER A 77  . ? 1_455 ? 
37  BC1 4 THR A  78  ? THR A 78  . ? 1_455 ? 
38  BC1 4 NAG U  .   ? NAG C 603 . ? 1_555 ? 
39  BC2 8 ASN C  70  ? ASN C 70  . ? 1_555 ? 
40  BC2 8 GLU C  72  ? GLU C 72  . ? 1_555 ? 
41  BC2 8 ASP C  92  ? ASP C 92  . ? 1_555 ? 
42  BC2 8 ASN C  93  ? ASN C 93  . ? 1_555 ? 
43  BC2 8 CYS C  96  ? CYS C 96  . ? 1_555 ? 
44  BC2 8 PRO C  143 ? PRO C 143 . ? 1_555 ? 
45  BC2 8 ARG C  227 ? ARG C 227 . ? 1_555 ? 
46  BC2 8 NAG X  .   ? NAG C 606 . ? 1_555 ? 
47  BC3 1 NAG W  .   ? NAG C 605 . ? 1_555 ? 
48  BC4 3 ASN C  282 ? ASN C 282 . ? 1_555 ? 
49  BC4 3 ASP I  20  ? ASP I 20  . ? 1_555 ? 
50  BC4 3 ARG I  319 ? ARG I 319 . ? 1_555 ? 
51  BC5 1 ASN E  17  ? ASN E 17  . ? 1_555 ? 
52  BC6 6 ASN E  70  ? ASN E 70  . ? 1_555 ? 
53  BC6 6 GLU E  72  ? GLU E 72  . ? 1_555 ? 
54  BC6 6 ASN E  93  ? ASN E 93  . ? 1_555 ? 
55  BC6 6 PRO E  143 ? PRO E 143 . ? 1_555 ? 
56  BC6 6 ARG E  227 ? ARG E 227 . ? 1_555 ? 
57  BC6 6 NAG BA .   ? NAG E 603 . ? 1_555 ? 
58  BC7 1 NAG AA .   ? NAG E 602 . ? 1_555 ? 
59  BC8 3 ARG E  51  ? ARG E 51  . ? 1_555 ? 
60  BC8 3 GLY E  52  ? GLY E 52  . ? 1_555 ? 
61  BC8 3 ASN E  282 ? ASN E 282 . ? 1_555 ? 
62  BC9 1 ASN E  293 ? ASN E 293 . ? 1_555 ? 
63  CC1 3 ASN F  154 ? ASN F 154 . ? 1_555 ? 
64  CC1 3 THR F  156 ? THR F 156 . ? 1_555 ? 
65  CC1 3 THR G  78  ? THR G 78  . ? 1_445 ? 
66  CC2 2 ASN G  17  ? ASN G 17  . ? 1_555 ? 
67  CC2 2 HOH YA .   ? HOH G 352 . ? 1_555 ? 
68  CC3 1 ASN G  29  ? ASN G 29  . ? 1_555 ? 
69  CC4 1 ASN G  282 ? ASN G 282 . ? 1_555 ? 
70  CC5 6 ASP I  23  ? ASP I 23  . ? 1_555 ? 
71  CC5 6 ASN I  29  ? ASN I 29  . ? 1_555 ? 
72  CC5 6 LYS I  317 ? LYS I 317 . ? 1_555 ? 
73  CC5 6 HOH AB .   ? HOH I 346 . ? 1_555 ? 
74  CC5 6 HOH AB .   ? HOH I 360 . ? 1_555 ? 
75  CC5 6 NAG JA .   ? NAG I 602 . ? 1_555 ? 
76  CC6 3 HOH AB .   ? HOH I 360 . ? 1_555 ? 
77  CC6 3 NAG IA .   ? NAG I 601 . ? 1_555 ? 
78  CC6 3 BMA KA .   ? BMA I 603 . ? 1_555 ? 
79  CC7 1 NAG JA .   ? NAG I 602 . ? 1_555 ? 
80  CC8 8 ASN C  135 ? ASN C 135 . ? 1_555 ? 
81  CC8 8 ASN I  70  ? ASN I 70  . ? 1_555 ? 
82  CC8 8 GLU I  72  ? GLU I 72  . ? 1_555 ? 
83  CC8 8 ASN I  93  ? ASN I 93  . ? 1_555 ? 
84  CC8 8 PRO I  143 ? PRO I 143 . ? 1_555 ? 
85  CC8 8 ARG I  227 ? ARG I 227 . ? 1_555 ? 
86  CC8 8 HOH AB .   ? HOH I 345 . ? 1_555 ? 
87  CC8 8 NAG MA .   ? NAG I 605 . ? 1_555 ? 
88  CC9 4 ASN C  135 ? ASN C 135 . ? 1_555 ? 
89  CC9 4 LYS C  136 ? LYS C 136 . ? 1_555 ? 
90  CC9 4 HOH AB .   ? HOH I 356 . ? 1_555 ? 
91  CC9 4 NAG LA .   ? NAG I 604 . ? 1_555 ? 
92  DC1 5 GLN J  30  ? GLN J 30  . ? 1_655 ? 
93  DC1 5 GLY J  31  ? GLY J 31  . ? 1_655 ? 
94  DC1 5 SER J  32  ? SER J 32  . ? 1_655 ? 
95  DC1 5 HOH BB .   ? HOH J 234 . ? 1_655 ? 
96  DC1 5 ASN K  17  ? ASN K 17  . ? 1_555 ? 
97  DC2 3 ASP K  23  ? ASP K 23  . ? 1_555 ? 
98  DC2 3 ASN K  29  ? ASN K 29  . ? 1_555 ? 
99  DC2 3 HOH CB .   ? HOH K 344 . ? 1_555 ? 
100 DC3 4 NAG O  .   ? NAG A 603 . ? 1_555 ? 
101 DC3 4 ARG K  51  ? ARG K 51  . ? 1_555 ? 
102 DC3 4 GLY K  52  ? GLY K 52  . ? 1_555 ? 
103 DC3 4 ASN K  282 ? ASN K 282 . ? 1_555 ? 
104 DC4 2 ASN K  282 ? ASN K 282 . ? 1_555 ? 
105 DC4 2 ASN K  293 ? ASN K 293 . ? 1_555 ? 
106 DC5 3 THR A  19  ? THR A 19  . ? 1_555 ? 
107 DC5 3 GLU L  150 ? GLU L 150 . ? 1_555 ? 
108 DC5 3 ASN L  154 ? ASN L 154 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3AL4 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3AL4 
_atom_sites.fract_transf_matrix[1][1]   0.015147 
_atom_sites.fract_transf_matrix[1][2]   -0.002385 
_atom_sites.fract_transf_matrix[1][3]   -0.002425 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008788 
_atom_sites.fract_transf_matrix[2][3]   -0.004396 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.009944 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . ASP A  1 7   ? -38.624 -78.825  22.734  1.00 119.35 ? 7   ASP A N   1 
ATOM   2     C CA  . ASP A  1 7   ? -38.002 -79.316  21.508  1.00 131.27 ? 7   ASP A CA  1 
ATOM   3     C C   . ASP A  1 7   ? -38.585 -78.638  20.273  1.00 118.78 ? 7   ASP A C   1 
ATOM   4     O O   . ASP A  1 7   ? -39.781 -78.755  20.000  1.00 132.48 ? 7   ASP A O   1 
ATOM   5     C CB  . ASP A  1 7   ? -38.130 -80.843  21.395  1.00 134.32 ? 7   ASP A CB  1 
ATOM   6     C CG  . ASP A  1 7   ? -37.040 -81.577  22.163  1.00 137.22 ? 7   ASP A CG  1 
ATOM   7     O OD1 . ASP A  1 7   ? -36.559 -80.991  23.159  1.00 135.04 ? 7   ASP A OD1 1 
ATOM   8     O OD2 . ASP A  1 7   ? -36.667 -82.712  21.774  1.00 145.72 ? 7   ASP A OD2 1 
ATOM   9     N N   . THR A  1 8   ? -37.736 -77.939  19.523  1.00 129.69 ? 8   THR A N   1 
ATOM   10    C CA  . THR A  1 8   ? -38.196 -77.191  18.354  1.00 132.01 ? 8   THR A CA  1 
ATOM   11    C C   . THR A  1 8   ? -37.441 -77.527  17.058  1.00 117.54 ? 8   THR A C   1 
ATOM   12    O O   . THR A  1 8   ? -36.246 -77.807  17.077  1.00 111.22 ? 8   THR A O   1 
ATOM   13    C CB  . THR A  1 8   ? -38.130 -75.673  18.600  1.00 118.86 ? 8   THR A CB  1 
ATOM   14    O OG1 . THR A  1 8   ? -36.846 -75.175  18.207  1.00 111.64 ? 8   THR A OG1 1 
ATOM   15    C CG2 . THR A  1 8   ? -38.368 -75.366  20.064  1.00 122.93 ? 8   THR A CG2 1 
ATOM   16    N N   . LEU A  1 9   ? -38.157 -77.505  15.937  1.00 113.77 ? 9   LEU A N   1 
ATOM   17    C CA  . LEU A  1 9   ? -37.559 -77.762  14.628  1.00 120.57 ? 9   LEU A CA  1 
ATOM   18    C C   . LEU A  1 9   ? -38.065 -76.745  13.618  1.00 83.68  ? 9   LEU A C   1 
ATOM   19    O O   . LEU A  1 9   ? -39.161 -76.891  13.076  1.00 98.82  ? 9   LEU A O   1 
ATOM   20    C CB  . LEU A  1 9   ? -37.834 -79.193  14.148  1.00 136.14 ? 9   LEU A CB  1 
ATOM   21    C CG  . LEU A  1 9   ? -37.281 -79.535  12.762  1.00 102.97 ? 9   LEU A CG  1 
ATOM   22    C CD1 . LEU A  1 9   ? -35.757 -79.420  12.714  1.00 93.75  ? 9   LEU A CD1 1 
ATOM   23    C CD2 . LEU A  1 9   ? -37.717 -80.924  12.364  1.00 126.82 ? 9   LEU A CD2 1 
ATOM   24    N N   . CYS A  1 10  ? -37.277 -75.708  13.360  1.00 105.98 ? 10  CYS A N   1 
ATOM   25    C CA  . CYS A  1 10  ? -37.736 -74.649  12.461  1.00 110.95 ? 10  CYS A CA  1 
ATOM   26    C C   . CYS A  1 10  ? -36.942 -74.687  11.141  1.00 101.79 ? 10  CYS A C   1 
ATOM   27    O O   . CYS A  1 10  ? -36.213 -75.654  10.847  1.00 95.91  ? 10  CYS A O   1 
ATOM   28    C CB  . CYS A  1 10  ? -37.527 -73.276  13.110  1.00 110.02 ? 10  CYS A CB  1 
ATOM   29    S SG  . CYS A  1 10  ? -37.920 -73.196  14.878  1.00 136.75 ? 10  CYS A SG  1 
ATOM   30    N N   . ILE A  1 11  ? -37.097 -73.641  10.330  1.00 110.57 ? 11  ILE A N   1 
ATOM   31    C CA  . ILE A  1 11  ? -36.461 -73.599  9.013   1.00 108.72 ? 11  ILE A CA  1 
ATOM   32    C C   . ILE A  1 11  ? -36.272 -72.148  8.592   1.00 96.12  ? 11  ILE A C   1 
ATOM   33    O O   . ILE A  1 11  ? -37.072 -71.277  8.937   1.00 100.32 ? 11  ILE A O   1 
ATOM   34    C CB  . ILE A  1 11  ? -37.329 -74.326  7.951   1.00 94.36  ? 11  ILE A CB  1 
ATOM   35    C CG1 . ILE A  1 11  ? -36.503 -74.751  6.721   1.00 100.78 ? 11  ILE A CG1 1 
ATOM   36    C CG2 . ILE A  1 11  ? -38.515 -73.449  7.549   1.00 89.75  ? 11  ILE A CG2 1 
ATOM   37    C CD1 . ILE A  1 11  ? -35.965 -76.238  6.687   1.00 93.59  ? 11  ILE A CD1 1 
ATOM   38    N N   . GLY A  1 12  ? -35.223 -71.897  7.821   1.00 119.67 ? 12  GLY A N   1 
ATOM   39    C CA  . GLY A  1 12  ? -34.935 -70.556  7.354   1.00 115.14 ? 12  GLY A CA  1 
ATOM   40    C C   . GLY A  1 12  ? -33.897 -70.557  6.253   1.00 113.16 ? 12  GLY A C   1 
ATOM   41    O O   . GLY A  1 12  ? -33.666 -71.586  5.620   1.00 107.25 ? 12  GLY A O   1 
ATOM   42    N N   . TYR A  1 13  ? -33.255 -69.414  6.030   1.00 86.32  ? 13  TYR A N   1 
ATOM   43    C CA  . TYR A  1 13  ? -32.337 -69.277  4.905   1.00 79.15  ? 13  TYR A CA  1 
ATOM   44    C C   . TYR A  1 13  ? -30.937 -68.817  5.283   1.00 74.63  ? 13  TYR A C   1 
ATOM   45    O O   . TYR A  1 13  ? -30.457 -69.079  6.382   1.00 88.48  ? 13  TYR A O   1 
ATOM   46    C CB  . TYR A  1 13  ? -32.921 -68.354  3.837   1.00 68.00  ? 13  TYR A CB  1 
ATOM   47    C CG  . TYR A  1 13  ? -33.995 -67.423  4.336   1.00 70.40  ? 13  TYR A CG  1 
ATOM   48    C CD1 . TYR A  1 13  ? -33.731 -66.078  4.543   1.00 65.87  ? 13  TYR A CD1 1 
ATOM   49    C CD2 . TYR A  1 13  ? -35.278 -67.887  4.584   1.00 54.82  ? 13  TYR A CD2 1 
ATOM   50    C CE1 . TYR A  1 13  ? -34.708 -65.227  4.986   1.00 56.82  ? 13  TYR A CE1 1 
ATOM   51    C CE2 . TYR A  1 13  ? -36.258 -67.043  5.030   1.00 59.31  ? 13  TYR A CE2 1 
ATOM   52    C CZ  . TYR A  1 13  ? -35.966 -65.715  5.230   1.00 63.70  ? 13  TYR A CZ  1 
ATOM   53    O OH  . TYR A  1 13  ? -36.938 -64.863  5.674   1.00 69.36  ? 13  TYR A OH  1 
ATOM   54    N N   . HIS A  1 14  ? -30.298 -68.118  4.354   1.00 84.76  ? 14  HIS A N   1 
ATOM   55    C CA  . HIS A  1 14  ? -28.873 -67.845  4.427   1.00 68.52  ? 14  HIS A CA  1 
ATOM   56    C C   . HIS A  1 14  ? -28.623 -66.347  4.389   1.00 87.88  ? 14  HIS A C   1 
ATOM   57    O O   . HIS A  1 14  ? -29.393 -65.607  3.777   1.00 105.60 ? 14  HIS A O   1 
ATOM   58    C CB  . HIS A  1 14  ? -28.206 -68.511  3.227   1.00 86.01  ? 14  HIS A CB  1 
ATOM   59    C CG  . HIS A  1 14  ? -26.715 -68.532  3.283   1.00 93.46  ? 14  HIS A CG  1 
ATOM   60    N ND1 . HIS A  1 14  ? -26.016 -69.319  4.175   1.00 105.44 ? 14  HIS A ND1 1 
ATOM   61    C CD2 . HIS A  1 14  ? -25.784 -67.900  2.531   1.00 103.11 ? 14  HIS A CD2 1 
ATOM   62    C CE1 . HIS A  1 14  ? -24.721 -69.152  3.983   1.00 113.57 ? 14  HIS A CE1 1 
ATOM   63    N NE2 . HIS A  1 14  ? -24.552 -68.297  2.991   1.00 101.75 ? 14  HIS A NE2 1 
ATOM   64    N N   . ALA A  1 15  ? -27.555 -65.897  5.042   1.00 67.29  ? 15  ALA A N   1 
ATOM   65    C CA  . ALA A  1 15  ? -27.177 -64.486  5.013   1.00 83.67  ? 15  ALA A CA  1 
ATOM   66    C C   . ALA A  1 15  ? -25.705 -64.357  5.327   1.00 82.01  ? 15  ALA A C   1 
ATOM   67    O O   . ALA A  1 15  ? -25.082 -65.302  5.808   1.00 84.08  ? 15  ALA A O   1 
ATOM   68    C CB  . ALA A  1 15  ? -27.983 -63.700  6.022   1.00 76.56  ? 15  ALA A CB  1 
ATOM   69    N N   . ASN A  1 16  ? -25.158 -63.176  5.073   1.00 86.46  ? 16  ASN A N   1 
ATOM   70    C CA  . ASN A  1 16  ? -23.720 -62.979  5.166   1.00 95.05  ? 16  ASN A CA  1 
ATOM   71    C C   . ASN A  1 16  ? -23.285 -61.511  5.190   1.00 99.87  ? 16  ASN A C   1 
ATOM   72    O O   . ASN A  1 16  ? -24.107 -60.611  5.357   1.00 103.00 ? 16  ASN A O   1 
ATOM   73    C CB  . ASN A  1 16  ? -23.016 -63.732  4.035   1.00 97.70  ? 16  ASN A CB  1 
ATOM   74    C CG  . ASN A  1 16  ? -23.548 -63.359  2.660   1.00 100.66 ? 16  ASN A CG  1 
ATOM   75    O OD1 . ASN A  1 16  ? -24.238 -62.352  2.499   1.00 94.11  ? 16  ASN A OD1 1 
ATOM   76    N ND2 . ASN A  1 16  ? -23.221 -64.169  1.659   1.00 96.06  ? 16  ASN A ND2 1 
ATOM   77    N N   . ASN A  1 17  ? -21.984 -61.283  5.040   1.00 97.33  ? 17  ASN A N   1 
ATOM   78    C CA  . ASN A  1 17  ? -21.432 -59.935  5.021   1.00 106.12 ? 17  ASN A CA  1 
ATOM   79    C C   . ASN A  1 17  ? -21.470 -59.349  3.616   1.00 116.64 ? 17  ASN A C   1 
ATOM   80    O O   . ASN A  1 17  ? -20.728 -58.417  3.300   1.00 128.78 ? 17  ASN A O   1 
ATOM   81    C CB  . ASN A  1 17  ? -19.993 -59.946  5.540   1.00 125.68 ? 17  ASN A CB  1 
ATOM   82    C CG  . ASN A  1 17  ? -19.088 -60.844  4.720   1.00 128.68 ? 17  ASN A CG  1 
ATOM   83    O OD1 . ASN A  1 17  ? -19.350 -61.099  3.544   1.00 131.16 ? 17  ASN A OD1 1 
ATOM   84    N ND2 . ASN A  1 17  ? -18.017 -61.330  5.335   1.00 138.90 ? 17  ASN A ND2 1 
ATOM   85    N N   . SER A  1 18  ? -22.333 -59.909  2.773   1.00 104.75 ? 18  SER A N   1 
ATOM   86    C CA  . SER A  1 18  ? -22.410 -59.489  1.380   1.00 99.88  ? 18  SER A CA  1 
ATOM   87    C C   . SER A  1 18  ? -23.067 -58.132  1.253   1.00 96.50  ? 18  SER A C   1 
ATOM   88    O O   . SER A  1 18  ? -23.984 -57.790  1.999   1.00 84.69  ? 18  SER A O   1 
ATOM   89    C CB  . SER A  1 18  ? -23.159 -60.505  0.521   1.00 93.68  ? 18  SER A CB  1 
ATOM   90    O OG  . SER A  1 18  ? -23.138 -60.103  -0.838  1.00 86.13  ? 18  SER A OG  1 
ATOM   91    N N   . THR A  1 19  ? -22.597 -57.366  0.285   1.00 97.77  ? 19  THR A N   1 
ATOM   92    C CA  . THR A  1 19  ? -22.983 -55.980  0.171   1.00 99.55  ? 19  THR A CA  1 
ATOM   93    C C   . THR A  1 19  ? -23.409 -55.775  -1.271  1.00 90.88  ? 19  THR A C   1 
ATOM   94    O O   . THR A  1 19  ? -23.841 -54.692  -1.670  1.00 93.51  ? 19  THR A O   1 
ATOM   95    C CB  . THR A  1 19  ? -21.799 -55.083  0.537   1.00 99.39  ? 19  THR A CB  1 
ATOM   96    O OG1 . THR A  1 19  ? -20.805 -55.169  -0.489  1.00 106.19 ? 19  THR A OG1 1 
ATOM   97    C CG2 . THR A  1 19  ? -21.182 -55.531  1.876   1.00 107.11 ? 19  THR A CG2 1 
ATOM   98    N N   . ASP A  1 20  ? -23.281 -56.850  -2.043  1.00 83.01  ? 20  ASP A N   1 
ATOM   99    C CA  . ASP A  1 20  ? -23.788 -56.905  -3.404  1.00 82.58  ? 20  ASP A CA  1 
ATOM   100   C C   . ASP A  1 20  ? -25.235 -56.443  -3.448  1.00 78.95  ? 20  ASP A C   1 
ATOM   101   O O   . ASP A  1 20  ? -26.060 -56.871  -2.641  1.00 77.82  ? 20  ASP A O   1 
ATOM   102   C CB  . ASP A  1 20  ? -23.687 -58.333  -3.949  1.00 82.13  ? 20  ASP A CB  1 
ATOM   103   C CG  . ASP A  1 20  ? -22.254 -58.785  -4.132  1.00 81.36  ? 20  ASP A CG  1 
ATOM   104   O OD1 . ASP A  1 20  ? -22.032 -59.982  -4.414  1.00 81.15  ? 20  ASP A OD1 1 
ATOM   105   O OD2 . ASP A  1 20  ? -21.349 -57.937  -3.993  1.00 85.35  ? 20  ASP A OD2 1 
ATOM   106   N N   . THR A  1 21  ? -25.533 -55.560  -4.392  1.00 74.46  ? 21  THR A N   1 
ATOM   107   C CA  . THR A  1 21  ? -26.895 -55.096  -4.601  1.00 69.53  ? 21  THR A CA  1 
ATOM   108   C C   . THR A  1 21  ? -27.297 -55.288  -6.056  1.00 64.89  ? 21  THR A C   1 
ATOM   109   O O   . THR A  1 21  ? -26.514 -55.023  -6.970  1.00 75.31  ? 21  THR A O   1 
ATOM   110   C CB  . THR A  1 21  ? -27.062 -53.614  -4.212  1.00 72.83  ? 21  THR A CB  1 
ATOM   111   O OG1 . THR A  1 21  ? -26.013 -52.840  -4.807  1.00 97.75  ? 21  THR A OG1 1 
ATOM   112   C CG2 . THR A  1 21  ? -27.008 -53.452  -2.702  1.00 70.45  ? 21  THR A CG2 1 
ATOM   113   N N   . VAL A  1 22  ? -28.518 -55.769  -6.260  1.00 65.14  ? 22  VAL A N   1 
ATOM   114   C CA  . VAL A  1 22  ? -29.066 -55.940  -7.596  1.00 58.90  ? 22  VAL A CA  1 
ATOM   115   C C   . VAL A  1 22  ? -30.394 -55.202  -7.689  1.00 55.75  ? 22  VAL A C   1 
ATOM   116   O O   . VAL A  1 22  ? -30.947 -54.778  -6.675  1.00 56.24  ? 22  VAL A O   1 
ATOM   117   C CB  . VAL A  1 22  ? -29.300 -57.424  -7.926  1.00 53.18  ? 22  VAL A CB  1 
ATOM   118   C CG1 . VAL A  1 22  ? -28.071 -58.247  -7.574  1.00 48.66  ? 22  VAL A CG1 1 
ATOM   119   C CG2 . VAL A  1 22  ? -30.523 -57.944  -7.186  1.00 42.00  ? 22  VAL A CG2 1 
ATOM   120   N N   . ASP A  1 23  ? -30.898 -55.046  -8.908  1.00 55.59  ? 23  ASP A N   1 
ATOM   121   C CA  . ASP A  1 23  ? -32.201 -54.433  -9.124  1.00 53.43  ? 23  ASP A CA  1 
ATOM   122   C C   . ASP A  1 23  ? -33.177 -55.463  -9.679  1.00 47.44  ? 23  ASP A C   1 
ATOM   123   O O   . ASP A  1 23  ? -32.776 -56.408  -10.359 1.00 46.95  ? 23  ASP A O   1 
ATOM   124   C CB  . ASP A  1 23  ? -32.095 -53.253  -10.095 1.00 61.77  ? 23  ASP A CB  1 
ATOM   125   C CG  . ASP A  1 23  ? -31.399 -52.049  -9.486  1.00 72.34  ? 23  ASP A CG  1 
ATOM   126   O OD1 . ASP A  1 23  ? -30.945 -52.139  -8.324  1.00 84.12  ? 23  ASP A OD1 1 
ATOM   127   O OD2 . ASP A  1 23  ? -31.308 -51.007  -10.171 1.00 81.36  ? 23  ASP A OD2 1 
ATOM   128   N N   . THR A  1 24  ? -34.458 -55.278  -9.374  1.00 43.41  ? 24  THR A N   1 
ATOM   129   C CA  . THR A  1 24  ? -35.522 -56.077  -9.968  1.00 52.24  ? 24  THR A CA  1 
ATOM   130   C C   . THR A  1 24  ? -36.525 -55.139  -10.632 1.00 47.63  ? 24  THR A C   1 
ATOM   131   O O   . THR A  1 24  ? -36.345 -53.922  -10.616 1.00 41.62  ? 24  THR A O   1 
ATOM   132   C CB  . THR A  1 24  ? -36.260 -56.930  -8.916  1.00 58.79  ? 24  THR A CB  1 
ATOM   133   O OG1 . THR A  1 24  ? -37.223 -56.124  -8.226  1.00 67.69  ? 24  THR A OG1 1 
ATOM   134   C CG2 . THR A  1 24  ? -35.279 -57.516  -7.913  1.00 55.12  ? 24  THR A CG2 1 
ATOM   135   N N   . VAL A  1 25  ? -37.577 -55.708  -11.217 1.00 55.62  ? 25  VAL A N   1 
ATOM   136   C CA  . VAL A  1 25  ? -38.662 -54.915  -11.788 1.00 59.98  ? 25  VAL A CA  1 
ATOM   137   C C   . VAL A  1 25  ? -39.372 -54.128  -10.689 1.00 57.87  ? 25  VAL A C   1 
ATOM   138   O O   . VAL A  1 25  ? -39.755 -52.976  -10.889 1.00 52.58  ? 25  VAL A O   1 
ATOM   139   C CB  . VAL A  1 25  ? -39.714 -55.808  -12.485 1.00 53.40  ? 25  VAL A CB  1 
ATOM   140   C CG1 . VAL A  1 25  ? -40.375 -55.072  -13.634 1.00 47.80  ? 25  VAL A CG1 1 
ATOM   141   C CG2 . VAL A  1 25  ? -39.084 -57.074  -13.000 1.00 60.07  ? 25  VAL A CG2 1 
ATOM   142   N N   . LEU A  1 26  ? -39.524 -54.757  -9.526  1.00 56.38  ? 26  LEU A N   1 
ATOM   143   C CA  . LEU A  1 26  ? -40.353 -54.225  -8.448  1.00 52.74  ? 26  LEU A CA  1 
ATOM   144   C C   . LEU A  1 26  ? -39.573 -53.402  -7.416  1.00 61.12  ? 26  LEU A C   1 
ATOM   145   O O   . LEU A  1 26  ? -40.144 -52.541  -6.742  1.00 61.21  ? 26  LEU A O   1 
ATOM   146   C CB  . LEU A  1 26  ? -41.092 -55.371  -7.744  1.00 52.88  ? 26  LEU A CB  1 
ATOM   147   C CG  . LEU A  1 26  ? -41.709 -56.455  -8.633  1.00 52.96  ? 26  LEU A CG  1 
ATOM   148   C CD1 . LEU A  1 26  ? -42.505 -57.463  -7.826  1.00 46.30  ? 26  LEU A CD1 1 
ATOM   149   C CD2 . LEU A  1 26  ? -42.593 -55.818  -9.662  1.00 60.63  ? 26  LEU A CD2 1 
ATOM   150   N N   . GLU A  1 27  ? -38.273 -53.659  -7.299  1.00 61.05  ? 27  GLU A N   1 
ATOM   151   C CA  . GLU A  1 27  ? -37.480 -53.033  -6.247  1.00 49.68  ? 27  GLU A CA  1 
ATOM   152   C C   . GLU A  1 27  ? -36.064 -52.687  -6.707  1.00 59.51  ? 27  GLU A C   1 
ATOM   153   O O   . GLU A  1 27  ? -35.460 -53.410  -7.501  1.00 63.45  ? 27  GLU A O   1 
ATOM   154   C CB  . GLU A  1 27  ? -37.440 -53.941  -5.014  1.00 72.59  ? 27  GLU A CB  1 
ATOM   155   C CG  . GLU A  1 27  ? -37.160 -53.212  -3.711  1.00 93.33  ? 27  GLU A CG  1 
ATOM   156   C CD  . GLU A  1 27  ? -37.433 -54.068  -2.485  1.00 102.49 ? 27  GLU A CD  1 
ATOM   157   O OE1 . GLU A  1 27  ? -36.930 -53.721  -1.396  1.00 95.57  ? 27  GLU A OE1 1 
ATOM   158   O OE2 . GLU A  1 27  ? -38.146 -55.086  -2.608  1.00 97.89  ? 27  GLU A OE2 1 
ATOM   159   N N   . LYS A  1 28  ? -35.548 -51.571  -6.202  1.00 69.56  ? 28  LYS A N   1 
ATOM   160   C CA  . LYS A  1 28  ? -34.199 -51.124  -6.531  1.00 70.93  ? 28  LYS A CA  1 
ATOM   161   C C   . LYS A  1 28  ? -33.234 -51.384  -5.379  1.00 73.08  ? 28  LYS A C   1 
ATOM   162   O O   . LYS A  1 28  ? -33.652 -51.536  -4.231  1.00 67.68  ? 28  LYS A O   1 
ATOM   163   C CB  . LYS A  1 28  ? -34.196 -49.636  -6.889  1.00 63.05  ? 28  LYS A CB  1 
ATOM   164   C CG  . LYS A  1 28  ? -34.455 -49.347  -8.356  1.00 67.43  ? 28  LYS A CG  1 
ATOM   165   C CD  . LYS A  1 28  ? -34.405 -47.855  -8.637  1.00 82.62  ? 28  LYS A CD  1 
ATOM   166   C CE  . LYS A  1 28  ? -34.230 -47.578  -10.121 1.00 96.20  ? 28  LYS A CE  1 
ATOM   167   N NZ  . LYS A  1 28  ? -35.274 -48.249  -10.944 1.00 91.99  ? 28  LYS A NZ  1 
ATOM   168   N N   . ASN A  1 29  ? -31.944 -51.430  -5.699  1.00 82.47  ? 29  ASN A N   1 
ATOM   169   C CA  . ASN A  1 29  ? -30.895 -51.663  -4.707  1.00 68.01  ? 29  ASN A CA  1 
ATOM   170   C C   . ASN A  1 29  ? -31.271 -52.662  -3.624  1.00 69.29  ? 29  ASN A C   1 
ATOM   171   O O   . ASN A  1 29  ? -31.363 -52.314  -2.447  1.00 73.43  ? 29  ASN A O   1 
ATOM   172   C CB  . ASN A  1 29  ? -30.449 -50.348  -4.069  1.00 69.92  ? 29  ASN A CB  1 
ATOM   173   C CG  . ASN A  1 29  ? -29.471 -49.591  -4.935  1.00 97.98  ? 29  ASN A CG  1 
ATOM   174   O OD1 . ASN A  1 29  ? -28.340 -50.029  -5.143  1.00 104.94 ? 29  ASN A OD1 1 
ATOM   175   N ND2 . ASN A  1 29  ? -29.901 -48.454  -5.455  1.00 91.54  ? 29  ASN A ND2 1 
ATOM   176   N N   . VAL A  1 30  ? -31.485 -53.905  -4.035  1.00 65.76  ? 30  VAL A N   1 
ATOM   177   C CA  . VAL A  1 30  ? -31.755 -54.984  -3.099  1.00 55.03  ? 30  VAL A CA  1 
ATOM   178   C C   . VAL A  1 30  ? -30.469 -55.752  -2.826  1.00 66.01  ? 30  VAL A C   1 
ATOM   179   O O   . VAL A  1 30  ? -29.865 -56.313  -3.740  1.00 63.18  ? 30  VAL A O   1 
ATOM   180   C CB  . VAL A  1 30  ? -32.820 -55.947  -3.648  1.00 57.08  ? 30  VAL A CB  1 
ATOM   181   C CG1 . VAL A  1 30  ? -32.983 -57.143  -2.722  1.00 46.33  ? 30  VAL A CG1 1 
ATOM   182   C CG2 . VAL A  1 30  ? -34.142 -55.219  -3.833  1.00 62.39  ? 30  VAL A CG2 1 
ATOM   183   N N   . THR A  1 31  ? -30.049 -55.762  -1.566  1.00 70.37  ? 31  THR A N   1 
ATOM   184   C CA  . THR A  1 31  ? -28.826 -56.449  -1.167  1.00 68.87  ? 31  THR A CA  1 
ATOM   185   C C   . THR A  1 31  ? -29.008 -57.957  -1.216  1.00 61.64  ? 31  THR A C   1 
ATOM   186   O O   . THR A  1 31  ? -29.899 -58.485  -0.558  1.00 65.89  ? 31  THR A O   1 
ATOM   187   C CB  . THR A  1 31  ? -28.418 -56.074  0.265   1.00 72.60  ? 31  THR A CB  1 
ATOM   188   O OG1 . THR A  1 31  ? -28.174 -54.665  0.343   1.00 64.72  ? 31  THR A OG1 1 
ATOM   189   C CG2 . THR A  1 31  ? -27.163 -56.832  0.672   1.00 69.86  ? 31  THR A CG2 1 
ATOM   190   N N   . VAL A  1 32  ? -28.155 -58.640  -1.981  1.00 66.64  ? 32  VAL A N   1 
ATOM   191   C CA  . VAL A  1 32  ? -28.215 -60.100  -2.110  1.00 66.11  ? 32  VAL A CA  1 
ATOM   192   C C   . VAL A  1 32  ? -27.001 -60.831  -1.528  1.00 71.15  ? 32  VAL A C   1 
ATOM   193   O O   . VAL A  1 32  ? -25.921 -60.255  -1.400  1.00 79.27  ? 32  VAL A O   1 
ATOM   194   C CB  . VAL A  1 32  ? -28.453 -60.557  -3.571  1.00 57.78  ? 32  VAL A CB  1 
ATOM   195   C CG1 . VAL A  1 32  ? -29.855 -60.177  -4.036  1.00 47.70  ? 32  VAL A CG1 1 
ATOM   196   C CG2 . VAL A  1 32  ? -27.396 -59.977  -4.492  1.00 59.08  ? 32  VAL A CG2 1 
ATOM   197   N N   . THR A  1 33  ? -27.192 -62.101  -1.172  1.00 66.73  ? 33  THR A N   1 
ATOM   198   C CA  . THR A  1 33  ? -26.116 -62.911  -0.605  1.00 71.79  ? 33  THR A CA  1 
ATOM   199   C C   . THR A  1 33  ? -25.043 -63.209  -1.642  1.00 76.76  ? 33  THR A C   1 
ATOM   200   O O   . THR A  1 33  ? -23.850 -63.175  -1.341  1.00 93.13  ? 33  THR A O   1 
ATOM   201   C CB  . THR A  1 33  ? -26.627 -64.256  -0.038  1.00 72.63  ? 33  THR A CB  1 
ATOM   202   O OG1 . THR A  1 33  ? -27.241 -65.021  -1.083  1.00 72.32  ? 33  THR A OG1 1 
ATOM   203   C CG2 . THR A  1 33  ? -27.627 -64.032  1.083   1.00 79.09  ? 33  THR A CG2 1 
ATOM   204   N N   . HIS A  1 34  ? -25.474 -63.509  -2.864  1.00 77.00  ? 34  HIS A N   1 
ATOM   205   C CA  . HIS A  1 34  ? -24.549 -63.832  -3.944  1.00 76.04  ? 34  HIS A CA  1 
ATOM   206   C C   . HIS A  1 34  ? -25.055 -63.318  -5.288  1.00 74.26  ? 34  HIS A C   1 
ATOM   207   O O   . HIS A  1 34  ? -26.253 -63.104  -5.470  1.00 63.40  ? 34  HIS A O   1 
ATOM   208   C CB  . HIS A  1 34  ? -24.345 -65.345  -4.032  1.00 68.78  ? 34  HIS A CB  1 
ATOM   209   C CG  . HIS A  1 34  ? -23.896 -65.972  -2.750  1.00 80.54  ? 34  HIS A CG  1 
ATOM   210   N ND1 . HIS A  1 34  ? -24.746 -66.173  -1.684  1.00 79.82  ? 34  HIS A ND1 1 
ATOM   211   C CD2 . HIS A  1 34  ? -22.691 -66.454  -2.366  1.00 87.43  ? 34  HIS A CD2 1 
ATOM   212   C CE1 . HIS A  1 34  ? -24.081 -66.744  -0.695  1.00 92.99  ? 34  HIS A CE1 1 
ATOM   213   N NE2 . HIS A  1 34  ? -22.832 -66.927  -1.085  1.00 105.08 ? 34  HIS A NE2 1 
ATOM   214   N N   . SER A  1 35  ? -24.133 -63.134  -6.229  1.00 70.43  ? 35  SER A N   1 
ATOM   215   C CA  . SER A  1 35  ? -24.489 -62.734  -7.586  1.00 60.04  ? 35  SER A CA  1 
ATOM   216   C C   . SER A  1 35  ? -23.292 -62.822  -8.535  1.00 57.99  ? 35  SER A C   1 
ATOM   217   O O   . SER A  1 35  ? -22.204 -63.241  -8.138  1.00 74.70  ? 35  SER A O   1 
ATOM   218   C CB  . SER A  1 35  ? -25.102 -61.328  -7.602  1.00 60.79  ? 35  SER A CB  1 
ATOM   219   O OG  . SER A  1 35  ? -24.262 -60.379  -6.971  1.00 68.90  ? 35  SER A OG  1 
ATOM   220   N N   . VAL A  1 36  ? -23.509 -62.450  -9.794  1.00 62.00  ? 36  VAL A N   1 
ATOM   221   C CA  . VAL A  1 36  ? -22.442 -62.418  -10.790 1.00 69.96  ? 36  VAL A CA  1 
ATOM   222   C C   . VAL A  1 36  ? -22.668 -61.248  -11.737 1.00 63.63  ? 36  VAL A C   1 
ATOM   223   O O   . VAL A  1 36  ? -23.792 -60.768  -11.887 1.00 58.70  ? 36  VAL A O   1 
ATOM   224   C CB  . VAL A  1 36  ? -22.373 -63.719  -11.626 1.00 61.19  ? 36  VAL A CB  1 
ATOM   225   C CG1 . VAL A  1 36  ? -22.412 -64.949  -10.728 1.00 70.97  ? 36  VAL A CG1 1 
ATOM   226   C CG2 . VAL A  1 36  ? -23.500 -63.759  -12.649 1.00 54.76  ? 36  VAL A CG2 1 
ATOM   227   N N   . ASN A  1 37  ? -21.602 -60.788  -12.379 1.00 68.29  ? 37  ASN A N   1 
ATOM   228   C CA  . ASN A  1 37  ? -21.718 -59.692  -13.327 1.00 63.92  ? 37  ASN A CA  1 
ATOM   229   C C   . ASN A  1 37  ? -21.777 -60.222  -14.753 1.00 59.22  ? 37  ASN A C   1 
ATOM   230   O O   . ASN A  1 37  ? -20.896 -60.964  -15.184 1.00 63.14  ? 37  ASN A O   1 
ATOM   231   C CB  . ASN A  1 37  ? -20.553 -58.715  -13.168 1.00 54.00  ? 37  ASN A CB  1 
ATOM   232   C CG  . ASN A  1 37  ? -20.841 -57.358  -13.778 1.00 71.75  ? 37  ASN A CG  1 
ATOM   233   O OD1 . ASN A  1 37  ? -19.961 -56.500  -13.852 1.00 96.78  ? 37  ASN A OD1 1 
ATOM   234   N ND2 . ASN A  1 37  ? -22.078 -57.154  -14.216 1.00 57.19  ? 37  ASN A ND2 1 
ATOM   235   N N   . LEU A  1 38  ? -22.829 -59.851  -15.474 1.00 57.42  ? 38  LEU A N   1 
ATOM   236   C CA  . LEU A  1 38  ? -22.994 -60.275  -16.857 1.00 49.97  ? 38  LEU A CA  1 
ATOM   237   C C   . LEU A  1 38  ? -22.327 -59.283  -17.798 1.00 43.77  ? 38  LEU A C   1 
ATOM   238   O O   . LEU A  1 38  ? -22.205 -59.533  -18.995 1.00 49.59  ? 38  LEU A O   1 
ATOM   239   C CB  . LEU A  1 38  ? -24.478 -60.412  -17.203 1.00 45.17  ? 38  LEU A CB  1 
ATOM   240   C CG  . LEU A  1 38  ? -25.237 -61.559  -16.533 1.00 39.61  ? 38  LEU A CG  1 
ATOM   241   C CD1 . LEU A  1 38  ? -26.737 -61.388  -16.717 1.00 53.53  ? 38  LEU A CD1 1 
ATOM   242   C CD2 . LEU A  1 38  ? -24.772 -62.901  -17.077 1.00 43.21  ? 38  LEU A CD2 1 
ATOM   243   N N   . LEU A  1 39  ? -21.892 -58.155  -17.247 1.00 47.53  ? 39  LEU A N   1 
ATOM   244   C CA  . LEU A  1 39  ? -21.277 -57.109  -18.054 1.00 44.61  ? 39  LEU A CA  1 
ATOM   245   C C   . LEU A  1 39  ? -19.752 -57.093  -17.958 1.00 54.79  ? 39  LEU A C   1 
ATOM   246   O O   . LEU A  1 39  ? -19.186 -56.973  -16.871 1.00 63.31  ? 39  LEU A O   1 
ATOM   247   C CB  . LEU A  1 39  ? -21.835 -55.738  -17.667 1.00 39.78  ? 39  LEU A CB  1 
ATOM   248   C CG  . LEU A  1 39  ? -21.165 -54.557  -18.368 1.00 49.81  ? 39  LEU A CG  1 
ATOM   249   C CD1 . LEU A  1 39  ? -21.282 -54.683  -19.885 1.00 46.24  ? 39  LEU A CD1 1 
ATOM   250   C CD2 . LEU A  1 39  ? -21.742 -53.241  -17.877 1.00 51.76  ? 39  LEU A CD2 1 
ATOM   251   N N   . GLU A  1 40  ? -19.095 -57.205  -19.108 1.00 58.77  ? 40  GLU A N   1 
ATOM   252   C CA  . GLU A  1 40  ? -17.642 -57.100  -19.178 1.00 54.68  ? 40  GLU A CA  1 
ATOM   253   C C   . GLU A  1 40  ? -17.250 -55.629  -19.276 1.00 52.13  ? 40  GLU A C   1 
ATOM   254   O O   . GLU A  1 40  ? -17.787 -54.887  -20.101 1.00 55.75  ? 40  GLU A O   1 
ATOM   255   C CB  . GLU A  1 40  ? -17.114 -57.877  -20.388 1.00 51.84  ? 40  GLU A CB  1 
ATOM   256   C CG  . GLU A  1 40  ? -15.596 -58.008  -20.475 1.00 57.60  ? 40  GLU A CG  1 
ATOM   257   C CD  . GLU A  1 40  ? -15.016 -58.861  -19.363 1.00 71.05  ? 40  GLU A CD  1 
ATOM   258   O OE1 . GLU A  1 40  ? -14.791 -60.069  -19.581 1.00 81.69  ? 40  GLU A OE1 1 
ATOM   259   O OE2 . GLU A  1 40  ? -14.785 -58.320  -18.264 1.00 69.25  ? 40  GLU A OE2 1 
ATOM   260   N N   . ASP A  1 41  ? -16.327 -55.208  -18.419 1.00 67.86  ? 41  ASP A N   1 
ATOM   261   C CA  . ASP A  1 41  ? -15.862 -53.828  -18.410 1.00 60.46  ? 41  ASP A CA  1 
ATOM   262   C C   . ASP A  1 41  ? -14.356 -53.768  -18.174 1.00 68.25  ? 41  ASP A C   1 
ATOM   263   O O   . ASP A  1 41  ? -13.855 -52.840  -17.539 1.00 78.17  ? 41  ASP A O   1 
ATOM   264   C CB  . ASP A  1 41  ? -16.606 -53.016  -17.343 1.00 64.85  ? 41  ASP A CB  1 
ATOM   265   C CG  . ASP A  1 41  ? -16.485 -53.620  -15.952 1.00 99.86  ? 41  ASP A CG  1 
ATOM   266   O OD1 . ASP A  1 41  ? -15.791 -54.647  -15.795 1.00 94.59  ? 41  ASP A OD1 1 
ATOM   267   O OD2 . ASP A  1 41  ? -17.090 -53.062  -15.012 1.00 97.54  ? 41  ASP A OD2 1 
ATOM   268   N N   . LYS A  1 42  ? -13.638 -54.761  -18.690 1.00 71.88  ? 42  LYS A N   1 
ATOM   269   C CA  . LYS A  1 42  ? -12.202 -54.859  -18.456 1.00 65.48  ? 42  LYS A CA  1 
ATOM   270   C C   . LYS A  1 42  ? -11.442 -55.434  -19.652 1.00 58.60  ? 42  LYS A C   1 
ATOM   271   O O   . LYS A  1 42  ? -11.601 -56.605  -20.001 1.00 67.01  ? 42  LYS A O   1 
ATOM   272   C CB  . LYS A  1 42  ? -11.932 -55.698  -17.205 1.00 89.85  ? 42  LYS A CB  1 
ATOM   273   C CG  . LYS A  1 42  ? -10.938 -55.076  -16.242 1.00 111.94 ? 42  LYS A CG  1 
ATOM   274   C CD  . LYS A  1 42  ? -11.111 -55.646  -14.846 1.00 126.00 ? 42  LYS A CD  1 
ATOM   275   C CE  . LYS A  1 42  ? -12.521 -55.396  -14.331 1.00 112.88 ? 42  LYS A CE  1 
ATOM   276   N NZ  . LYS A  1 42  ? -12.768 -56.048  -13.016 1.00 110.13 ? 42  LYS A NZ  1 
ATOM   277   N N   . HIS A  1 43  ? -10.617 -54.594  -20.273 1.00 45.98  ? 43  HIS A N   1 
ATOM   278   C CA  . HIS A  1 43  ? -9.755  -55.002  -21.376 1.00 60.62  ? 43  HIS A CA  1 
ATOM   279   C C   . HIS A  1 43  ? -8.305  -55.045  -20.905 1.00 62.32  ? 43  HIS A C   1 
ATOM   280   O O   . HIS A  1 43  ? -7.948  -54.381  -19.933 1.00 61.76  ? 43  HIS A O   1 
ATOM   281   C CB  . HIS A  1 43  ? -9.887  -54.020  -22.540 1.00 56.09  ? 43  HIS A CB  1 
ATOM   282   C CG  . HIS A  1 43  ? -9.518  -52.612  -22.185 1.00 58.96  ? 43  HIS A CG  1 
ATOM   283   N ND1 . HIS A  1 43  ? -8.300  -52.056  -22.514 1.00 66.35  ? 43  HIS A ND1 1 
ATOM   284   C CD2 . HIS A  1 43  ? -10.203 -51.651  -21.523 1.00 56.57  ? 43  HIS A CD2 1 
ATOM   285   C CE1 . HIS A  1 43  ? -8.254  -50.810  -22.075 1.00 59.53  ? 43  HIS A CE1 1 
ATOM   286   N NE2 . HIS A  1 43  ? -9.396  -50.540  -21.470 1.00 56.11  ? 43  HIS A NE2 1 
ATOM   287   N N   . ASN A  1 44  ? -7.469  -55.817  -21.592 1.00 64.10  ? 44  ASN A N   1 
ATOM   288   C CA  . ASN A  1 44  ? -6.064  -55.934  -21.205 1.00 59.95  ? 44  ASN A CA  1 
ATOM   289   C C   . ASN A  1 44  ? -5.200  -54.783  -21.712 1.00 64.58  ? 44  ASN A C   1 
ATOM   290   O O   . ASN A  1 44  ? -3.997  -54.740  -21.460 1.00 68.50  ? 44  ASN A O   1 
ATOM   291   C CB  . ASN A  1 44  ? -5.478  -57.281  -21.639 1.00 51.56  ? 44  ASN A CB  1 
ATOM   292   C CG  . ASN A  1 44  ? -5.516  -57.485  -23.142 1.00 69.62  ? 44  ASN A CG  1 
ATOM   293   O OD1 . ASN A  1 44  ? -5.182  -58.561  -23.636 1.00 81.73  ? 44  ASN A OD1 1 
ATOM   294   N ND2 . ASN A  1 44  ? -5.925  -56.457  -23.875 1.00 64.20  ? 44  ASN A ND2 1 
ATOM   295   N N   . GLY A  1 45  ? -5.820  -53.851  -22.427 1.00 61.38  ? 45  GLY A N   1 
ATOM   296   C CA  . GLY A  1 45  ? -5.119  -52.684  -22.927 1.00 59.59  ? 45  GLY A CA  1 
ATOM   297   C C   . GLY A  1 45  ? -3.997  -53.015  -23.892 1.00 61.59  ? 45  GLY A C   1 
ATOM   298   O O   . GLY A  1 45  ? -3.034  -52.260  -24.011 1.00 61.12  ? 45  GLY A O   1 
ATOM   299   N N   . LYS A  1 46  ? -4.124  -54.145  -24.580 1.00 54.56  ? 46  LYS A N   1 
ATOM   300   C CA  . LYS A  1 46  ? -3.131  -54.568  -25.560 1.00 64.76  ? 46  LYS A CA  1 
ATOM   301   C C   . LYS A  1 46  ? -3.793  -54.967  -26.877 1.00 56.18  ? 46  LYS A C   1 
ATOM   302   O O   . LYS A  1 46  ? -4.821  -55.644  -26.887 1.00 63.79  ? 46  LYS A O   1 
ATOM   303   C CB  . LYS A  1 46  ? -2.309  -55.743  -25.017 1.00 77.49  ? 46  LYS A CB  1 
ATOM   304   C CG  . LYS A  1 46  ? -1.514  -55.426  -23.765 1.00 79.70  ? 46  LYS A CG  1 
ATOM   305   C CD  . LYS A  1 46  ? -1.182  -56.693  -23.003 1.00 98.33  ? 46  LYS A CD  1 
ATOM   306   C CE  . LYS A  1 46  ? -1.466  -56.505  -21.525 1.00 111.58 ? 46  LYS A CE  1 
ATOM   307   N NZ  . LYS A  1 46  ? -1.376  -57.774  -20.759 1.00 100.92 ? 46  LYS A NZ  1 
ATOM   308   N N   . LEU A  1 47  ? -3.201  -54.540  -27.987 1.00 50.80  ? 47  LEU A N   1 
ATOM   309   C CA  . LEU A  1 47  ? -3.672  -54.943  -29.301 1.00 57.74  ? 47  LEU A CA  1 
ATOM   310   C C   . LEU A  1 47  ? -3.279  -56.385  -29.555 1.00 57.22  ? 47  LEU A C   1 
ATOM   311   O O   . LEU A  1 47  ? -2.500  -56.678  -30.461 1.00 62.44  ? 47  LEU A O   1 
ATOM   312   C CB  . LEU A  1 47  ? -3.081  -54.032  -30.370 1.00 56.74  ? 47  LEU A CB  1 
ATOM   313   C CG  . LEU A  1 47  ? -3.344  -52.556  -30.063 1.00 56.72  ? 47  LEU A CG  1 
ATOM   314   C CD1 . LEU A  1 47  ? -3.264  -51.746  -31.353 1.00 46.31  ? 47  LEU A CD1 1 
ATOM   315   C CD2 . LEU A  1 47  ? -4.696  -52.334  -29.328 1.00 43.75  ? 47  LEU A CD2 1 
ATOM   316   N N   . CYS A  1 48  ? -3.811  -57.283  -28.736 1.00 59.56  ? 48  CYS A N   1 
ATOM   317   C CA  . CYS A  1 48  ? -3.499  -58.692  -28.873 1.00 62.43  ? 48  CYS A CA  1 
ATOM   318   C C   . CYS A  1 48  ? -3.920  -59.172  -30.252 1.00 57.83  ? 48  CYS A C   1 
ATOM   319   O O   . CYS A  1 48  ? -4.706  -58.513  -30.937 1.00 60.49  ? 48  CYS A O   1 
ATOM   320   C CB  . CYS A  1 48  ? -4.201  -59.501  -27.786 1.00 52.22  ? 48  CYS A CB  1 
ATOM   321   S SG  . CYS A  1 48  ? -3.862  -58.891  -26.129 1.00 77.15  ? 48  CYS A SG  1 
ATOM   322   N N   . LYS A  1 49  ? -3.397  -60.322  -30.659 1.00 63.29  ? 49  LYS A N   1 
ATOM   323   C CA  . LYS A  1 49  ? -3.679  -60.840  -31.990 1.00 65.27  ? 49  LYS A CA  1 
ATOM   324   C C   . LYS A  1 49  ? -5.003  -61.591  -32.050 1.00 61.61  ? 49  LYS A C   1 
ATOM   325   O O   . LYS A  1 49  ? -5.492  -62.084  -31.037 1.00 63.12  ? 49  LYS A O   1 
ATOM   326   C CB  . LYS A  1 49  ? -2.572  -61.775  -32.459 1.00 73.39  ? 49  LYS A CB  1 
ATOM   327   C CG  . LYS A  1 49  ? -1.355  -61.816  -31.574 1.00 66.45  ? 49  LYS A CG  1 
ATOM   328   C CD  . LYS A  1 49  ? -0.798  -63.221  -31.555 1.00 78.48  ? 49  LYS A CD  1 
ATOM   329   C CE  . LYS A  1 49  ? 0.702   -63.219  -31.370 1.00 91.11  ? 49  LYS A CE  1 
ATOM   330   N NZ  . LYS A  1 49  ? 1.310   -64.329  -32.153 1.00 87.56  ? 49  LYS A NZ  1 
ATOM   331   N N   . LEU A  1 50  ? -5.502  -61.894  -33.228 1.00 68.26  ? 50  LEU A N   1 
ATOM   332   C CA  . LEU A  1 50  ? -6.822  -62.490  -33.290 1.00 67.71  ? 50  LEU A CA  1 
ATOM   333   C C   . LEU A  1 50  ? -7.009  -64.004  -33.237 1.00 85.81  ? 50  LEU A C   1 
ATOM   334   O O   . LEU A  1 50  ? -7.539  -64.491  -32.253 1.00 107.69 ? 50  LEU A O   1 
ATOM   335   C CB  . LEU A  1 50  ? -7.646  -61.879  -34.410 1.00 66.86  ? 50  LEU A CB  1 
ATOM   336   C CG  . LEU A  1 50  ? -8.444  -60.648  -33.976 1.00 61.18  ? 50  LEU A CG  1 
ATOM   337   C CD1 . LEU A  1 50  ? -9.169  -60.073  -35.130 1.00 55.97  ? 50  LEU A CD1 1 
ATOM   338   C CD2 . LEU A  1 50  ? -9.380  -60.939  -32.872 1.00 61.03  ? 50  LEU A CD2 1 
ATOM   339   N N   . ARG A  1 51  ? -6.635  -64.747  -34.269 1.00 82.89  ? 51  ARG A N   1 
ATOM   340   C CA  . ARG A  1 51  ? -7.064  -66.139  -34.406 1.00 95.60  ? 51  ARG A CA  1 
ATOM   341   C C   . ARG A  1 51  ? -5.814  -66.625  -33.696 1.00 94.64  ? 51  ARG A C   1 
ATOM   342   O O   . ARG A  1 51  ? -5.836  -66.959  -32.510 1.00 109.91 ? 51  ARG A O   1 
ATOM   343   C CB  . ARG A  1 51  ? -6.781  -66.290  -35.909 1.00 105.62 ? 51  ARG A CB  1 
ATOM   344   C CG  . ARG A  1 51  ? -7.742  -65.576  -36.827 1.00 117.31 ? 51  ARG A CG  1 
ATOM   345   C CD  . ARG A  1 51  ? -8.164  -66.520  -37.947 1.00 145.99 ? 51  ARG A CD  1 
ATOM   346   N NE  . ARG A  1 51  ? -9.030  -67.569  -37.420 1.00 161.47 ? 51  ARG A NE  1 
ATOM   347   C CZ  . ARG A  1 51  ? -8.743  -68.865  -37.388 1.00 148.23 ? 51  ARG A CZ  1 
ATOM   348   N NH1 . ARG A  1 51  ? -7.603  -69.308  -37.897 1.00 135.56 ? 51  ARG A NH1 1 
ATOM   349   N NH2 . ARG A  1 51  ? -9.610  -69.719  -36.859 1.00 136.24 ? 51  ARG A NH2 1 
ATOM   350   N N   . GLY A  1 52  ? -4.716  -66.646  -34.448 1.00 83.11  ? 52  GLY A N   1 
ATOM   351   C CA  . GLY A  1 52  ? -3.387  -66.799  -33.885 1.00 100.77 ? 52  GLY A CA  1 
ATOM   352   C C   . GLY A  1 52  ? -2.451  -65.969  -34.742 1.00 92.36  ? 52  GLY A C   1 
ATOM   353   O O   . GLY A  1 52  ? -1.226  -66.026  -34.610 1.00 93.52  ? 52  GLY A O   1 
ATOM   354   N N   . VAL A  1 53  ? -3.050  -65.196  -35.641 1.00 87.25  ? 53  VAL A N   1 
ATOM   355   C CA  . VAL A  1 53  ? -2.298  -64.342  -36.549 1.00 65.83  ? 53  VAL A CA  1 
ATOM   356   C C   . VAL A  1 53  ? -2.155  -62.941  -35.959 1.00 55.44  ? 53  VAL A C   1 
ATOM   357   O O   . VAL A  1 53  ? -3.076  -62.433  -35.321 1.00 60.37  ? 53  VAL A O   1 
ATOM   358   C CB  . VAL A  1 53  ? -2.985  -64.251  -37.927 1.00 58.13  ? 53  VAL A CB  1 
ATOM   359   C CG1 . VAL A  1 53  ? -2.130  -63.444  -38.907 1.00 56.19  ? 53  VAL A CG1 1 
ATOM   360   C CG2 . VAL A  1 53  ? -3.281  -65.645  -38.467 1.00 50.24  ? 53  VAL A CG2 1 
ATOM   361   N N   . ALA A  1 54  ? -0.996  -62.324  -36.163 1.00 58.44  ? 54  ALA A N   1 
ATOM   362   C CA  . ALA A  1 54  ? -0.736  -60.995  -35.619 1.00 58.72  ? 54  ALA A CA  1 
ATOM   363   C C   . ALA A  1 54  ? -1.281  -59.906  -36.534 1.00 57.19  ? 54  ALA A C   1 
ATOM   364   O O   . ALA A  1 54  ? -1.427  -60.118  -37.737 1.00 54.10  ? 54  ALA A O   1 
ATOM   365   C CB  . ALA A  1 54  ? 0.756   -60.797  -35.390 1.00 62.38  ? 54  ALA A CB  1 
ATOM   366   N N   . PRO A  1 55  ? -1.596  -58.737  -35.959 1.00 49.00  ? 55  PRO A N   1 
ATOM   367   C CA  . PRO A  1 55  ? -2.035  -57.580  -36.743 1.00 44.81  ? 55  PRO A CA  1 
ATOM   368   C C   . PRO A  1 55  ? -0.869  -56.955  -37.494 1.00 50.60  ? 55  PRO A C   1 
ATOM   369   O O   . PRO A  1 55  ? 0.282   -57.100  -37.079 1.00 57.53  ? 55  PRO A O   1 
ATOM   370   C CB  . PRO A  1 55  ? -2.541  -56.610  -35.674 1.00 46.20  ? 55  PRO A CB  1 
ATOM   371   C CG  . PRO A  1 55  ? -1.786  -56.985  -34.446 1.00 31.62  ? 55  PRO A CG  1 
ATOM   372   C CD  . PRO A  1 55  ? -1.660  -58.476  -34.511 1.00 46.68  ? 55  PRO A CD  1 
ATOM   373   N N   . LEU A  1 56  ? -1.169  -56.278  -38.595 1.00 52.14  ? 56  LEU A N   1 
ATOM   374   C CA  . LEU A  1 56  ? -0.161  -55.535  -39.334 1.00 44.28  ? 56  LEU A CA  1 
ATOM   375   C C   . LEU A  1 56  ? -0.115  -54.111  -38.805 1.00 40.89  ? 56  LEU A C   1 
ATOM   376   O O   . LEU A  1 56  ? -0.996  -53.303  -39.096 1.00 57.23  ? 56  LEU A O   1 
ATOM   377   C CB  . LEU A  1 56  ? -0.484  -55.530  -40.829 1.00 52.92  ? 56  LEU A CB  1 
ATOM   378   C CG  . LEU A  1 56  ? 0.476   -54.776  -41.752 1.00 43.83  ? 56  LEU A CG  1 
ATOM   379   C CD1 . LEU A  1 56  ? 1.854   -55.413  -41.728 1.00 57.40  ? 56  LEU A CD1 1 
ATOM   380   C CD2 . LEU A  1 56  ? -0.068  -54.742  -43.169 1.00 49.37  ? 56  LEU A CD2 1 
ATOM   381   N N   . HIS A  1 57  ? 0.908   -53.811  -38.016 1.00 49.04  ? 57  HIS A N   1 
ATOM   382   C CA  . HIS A  1 57  ? 1.065   -52.478  -37.453 1.00 51.95  ? 57  HIS A CA  1 
ATOM   383   C C   . HIS A  1 57  ? 1.897   -51.598  -38.387 1.00 66.54  ? 57  HIS A C   1 
ATOM   384   O O   . HIS A  1 57  ? 3.010   -51.962  -38.765 1.00 66.74  ? 57  HIS A O   1 
ATOM   385   C CB  . HIS A  1 57  ? 1.710   -52.565  -36.069 1.00 56.40  ? 57  HIS A CB  1 
ATOM   386   C CG  . HIS A  1 57  ? 1.569   -51.319  -35.255 1.00 58.88  ? 57  HIS A CG  1 
ATOM   387   N ND1 . HIS A  1 57  ? 2.408   -50.234  -35.400 1.00 58.24  ? 57  HIS A ND1 1 
ATOM   388   C CD2 . HIS A  1 57  ? 0.688   -50.985  -34.280 1.00 66.91  ? 57  HIS A CD2 1 
ATOM   389   C CE1 . HIS A  1 57  ? 2.047   -49.287  -34.553 1.00 70.16  ? 57  HIS A CE1 1 
ATOM   390   N NE2 . HIS A  1 57  ? 1.010   -49.715  -33.863 1.00 74.89  ? 57  HIS A NE2 1 
ATOM   391   N N   . LEU A  1 58  ? 1.351   -50.443  -38.762 1.00 69.65  ? 58  LEU A N   1 
ATOM   392   C CA  . LEU A  1 58  ? 2.017   -49.558  -39.718 1.00 61.67  ? 58  LEU A CA  1 
ATOM   393   C C   . LEU A  1 58  ? 2.876   -48.470  -39.079 1.00 71.77  ? 58  LEU A C   1 
ATOM   394   O O   . LEU A  1 58  ? 3.659   -47.814  -39.765 1.00 74.20  ? 58  LEU A O   1 
ATOM   395   C CB  . LEU A  1 58  ? 1.004   -48.909  -40.652 1.00 64.92  ? 58  LEU A CB  1 
ATOM   396   C CG  . LEU A  1 58  ? 0.747   -49.613  -41.984 1.00 57.31  ? 58  LEU A CG  1 
ATOM   397   C CD1 . LEU A  1 58  ? 1.027   -51.106  -41.897 1.00 59.20  ? 58  LEU A CD1 1 
ATOM   398   C CD2 . LEU A  1 58  ? -0.670  -49.332  -42.446 1.00 62.57  ? 58  LEU A CD2 1 
ATOM   399   N N   . GLY A  1 59  ? 2.726   -48.271  -37.775 1.00 71.75  ? 59  GLY A N   1 
ATOM   400   C CA  . GLY A  1 59  ? 3.563   -47.326  -37.057 1.00 66.86  ? 59  GLY A CA  1 
ATOM   401   C C   . GLY A  1 59  ? 3.365   -45.871  -37.446 1.00 74.10  ? 59  GLY A C   1 
ATOM   402   O O   . GLY A  1 59  ? 2.330   -45.278  -37.147 1.00 88.06  ? 59  GLY A O   1 
ATOM   403   N N   . LYS A  1 60  ? 4.361   -45.290  -38.108 1.00 82.19  ? 60  LYS A N   1 
ATOM   404   C CA  . LYS A  1 60  ? 4.299   -43.883  -38.501 1.00 93.45  ? 60  LYS A CA  1 
ATOM   405   C C   . LYS A  1 60  ? 3.655   -43.700  -39.880 1.00 88.25  ? 60  LYS A C   1 
ATOM   406   O O   . LYS A  1 60  ? 3.438   -42.575  -40.328 1.00 96.03  ? 60  LYS A O   1 
ATOM   407   C CB  . LYS A  1 60  ? 5.699   -43.258  -38.473 1.00 99.19  ? 60  LYS A CB  1 
ATOM   408   C CG  . LYS A  1 60  ? 5.722   -41.737  -38.591 1.00 134.62 ? 60  LYS A CG  1 
ATOM   409   C CD  . LYS A  1 60  ? 5.083   -41.069  -37.381 1.00 145.22 ? 60  LYS A CD  1 
ATOM   410   C CE  . LYS A  1 60  ? 5.852   -41.375  -36.105 1.00 155.75 ? 60  LYS A CE  1 
ATOM   411   N NZ  . LYS A  1 60  ? 5.240   -40.717  -34.918 1.00 148.56 ? 60  LYS A NZ  1 
ATOM   412   N N   . CYS A  1 61  ? 3.339   -44.811  -40.541 1.00 73.14  ? 61  CYS A N   1 
ATOM   413   C CA  . CYS A  1 61  ? 2.806   -44.776  -41.905 1.00 71.59  ? 61  CYS A CA  1 
ATOM   414   C C   . CYS A  1 61  ? 1.346   -45.220  -41.983 1.00 69.33  ? 61  CYS A C   1 
ATOM   415   O O   . CYS A  1 61  ? 0.874   -45.969  -41.136 1.00 71.71  ? 61  CYS A O   1 
ATOM   416   C CB  . CYS A  1 61  ? 3.643   -45.670  -42.822 1.00 67.47  ? 61  CYS A CB  1 
ATOM   417   S SG  . CYS A  1 61  ? 5.333   -45.099  -43.120 1.00 85.35  ? 61  CYS A SG  1 
ATOM   418   N N   . ASN A  1 62  ? 0.630   -44.759  -43.005 1.00 52.50  ? 62  ASN A N   1 
ATOM   419   C CA  . ASN A  1 62  ? -0.706  -45.284  -43.287 1.00 63.22  ? 62  ASN A CA  1 
ATOM   420   C C   . ASN A  1 62  ? -0.694  -46.262  -44.448 1.00 57.99  ? 62  ASN A C   1 
ATOM   421   O O   . ASN A  1 62  ? 0.325   -46.437  -45.114 1.00 50.53  ? 62  ASN A O   1 
ATOM   422   C CB  . ASN A  1 62  ? -1.708  -44.164  -43.575 1.00 68.26  ? 62  ASN A CB  1 
ATOM   423   C CG  . ASN A  1 62  ? -1.229  -43.213  -44.649 1.00 65.39  ? 62  ASN A CG  1 
ATOM   424   O OD1 . ASN A  1 62  ? -0.492  -43.600  -45.556 1.00 63.03  ? 62  ASN A OD1 1 
ATOM   425   N ND2 . ASN A  1 62  ? -1.648  -41.956  -44.554 1.00 62.94  ? 62  ASN A ND2 1 
ATOM   426   N N   . ILE A  1 63  ? -1.838  -46.890  -44.688 1.00 54.83  ? 63  ILE A N   1 
ATOM   427   C CA  . ILE A  1 63  ? -1.964  -47.861  -45.764 1.00 51.31  ? 63  ILE A CA  1 
ATOM   428   C C   . ILE A  1 63  ? -1.371  -47.324  -47.065 1.00 46.15  ? 63  ILE A C   1 
ATOM   429   O O   . ILE A  1 63  ? -0.581  -48.002  -47.719 1.00 46.53  ? 63  ILE A O   1 
ATOM   430   C CB  . ILE A  1 63  ? -3.431  -48.260  -45.993 1.00 54.97  ? 63  ILE A CB  1 
ATOM   431   C CG1 . ILE A  1 63  ? -4.018  -48.886  -44.727 1.00 41.41  ? 63  ILE A CG1 1 
ATOM   432   C CG2 . ILE A  1 63  ? -3.538  -49.230  -47.149 1.00 49.01  ? 63  ILE A CG2 1 
ATOM   433   C CD1 . ILE A  1 63  ? -3.403  -50.218  -44.368 1.00 58.23  ? 63  ILE A CD1 1 
ATOM   434   N N   . ALA A  1 64  ? -1.745  -46.101  -47.426 1.00 49.83  ? 64  ALA A N   1 
ATOM   435   C CA  . ALA A  1 64  ? -1.254  -45.479  -48.651 1.00 52.61  ? 64  ALA A CA  1 
ATOM   436   C C   . ALA A  1 64  ? 0.271   -45.506  -48.734 1.00 58.60  ? 64  ALA A C   1 
ATOM   437   O O   . ALA A  1 64  ? 0.841   -46.014  -49.700 1.00 59.29  ? 64  ALA A O   1 
ATOM   438   C CB  . ALA A  1 64  ? -1.767  -44.050  -48.763 1.00 45.96  ? 64  ALA A CB  1 
ATOM   439   N N   . GLY A  1 65  ? 0.926   -44.957  -47.716 1.00 52.31  ? 65  GLY A N   1 
ATOM   440   C CA  . GLY A  1 65  ? 2.375   -44.904  -47.681 1.00 44.45  ? 65  GLY A CA  1 
ATOM   441   C C   . GLY A  1 65  ? 3.019   -46.277  -47.728 1.00 50.26  ? 65  GLY A C   1 
ATOM   442   O O   . GLY A  1 65  ? 4.023   -46.478  -48.411 1.00 56.80  ? 65  GLY A O   1 
ATOM   443   N N   . TRP A  1 66  ? 2.436   -47.226  -47.004 1.00 50.86  ? 66  TRP A N   1 
ATOM   444   C CA  . TRP A  1 66  ? 2.993   -48.572  -46.912 1.00 54.58  ? 66  TRP A CA  1 
ATOM   445   C C   . TRP A  1 66  ? 2.988   -49.319  -48.245 1.00 46.50  ? 66  TRP A C   1 
ATOM   446   O O   . TRP A  1 66  ? 3.976   -49.958  -48.605 1.00 61.23  ? 66  TRP A O   1 
ATOM   447   C CB  . TRP A  1 66  ? 2.257   -49.386  -45.842 1.00 54.73  ? 66  TRP A CB  1 
ATOM   448   C CG  . TRP A  1 66  ? 2.470   -50.865  -45.961 1.00 55.55  ? 66  TRP A CG  1 
ATOM   449   C CD1 . TRP A  1 66  ? 3.650   -51.537  -45.825 1.00 67.86  ? 66  TRP A CD1 1 
ATOM   450   C CD2 . TRP A  1 66  ? 1.473   -51.857  -46.234 1.00 61.72  ? 66  TRP A CD2 1 
ATOM   451   N NE1 . TRP A  1 66  ? 3.450   -52.885  -46.002 1.00 69.19  ? 66  TRP A NE1 1 
ATOM   452   C CE2 . TRP A  1 66  ? 2.122   -53.108  -46.253 1.00 61.06  ? 66  TRP A CE2 1 
ATOM   453   C CE3 . TRP A  1 66  ? 0.094   -51.809  -46.464 1.00 59.82  ? 66  TRP A CE3 1 
ATOM   454   C CZ2 . TRP A  1 66  ? 1.440   -54.300  -46.494 1.00 55.62  ? 66  TRP A CZ2 1 
ATOM   455   C CZ3 . TRP A  1 66  ? -0.581  -52.994  -46.703 1.00 58.95  ? 66  TRP A CZ3 1 
ATOM   456   C CH2 . TRP A  1 66  ? 0.093   -54.222  -46.716 1.00 58.67  ? 66  TRP A CH2 1 
ATOM   457   N N   . ILE A  1 67  ? 1.879   -49.239  -48.975 1.00 47.36  ? 67  ILE A N   1 
ATOM   458   C CA  . ILE A  1 67  ? 1.752   -49.970  -50.232 1.00 60.34  ? 67  ILE A CA  1 
ATOM   459   C C   . ILE A  1 67  ? 2.487   -49.282  -51.378 1.00 62.79  ? 67  ILE A C   1 
ATOM   460   O O   . ILE A  1 67  ? 3.094   -49.944  -52.219 1.00 56.14  ? 67  ILE A O   1 
ATOM   461   C CB  . ILE A  1 67  ? 0.283   -50.165  -50.641 1.00 46.09  ? 67  ILE A CB  1 
ATOM   462   C CG1 . ILE A  1 67  ? -0.585  -50.442  -49.418 1.00 69.72  ? 67  ILE A CG1 1 
ATOM   463   C CG2 . ILE A  1 67  ? 0.161   -51.298  -51.647 1.00 53.37  ? 67  ILE A CG2 1 
ATOM   464   C CD1 . ILE A  1 67  ? -2.039  -50.635  -49.756 1.00 90.36  ? 67  ILE A CD1 1 
ATOM   465   N N   . LEU A  1 68  ? 2.420   -47.956  -51.420 1.00 48.62  ? 68  LEU A N   1 
ATOM   466   C CA  . LEU A  1 68  ? 3.102   -47.203  -52.467 1.00 53.48  ? 68  LEU A CA  1 
ATOM   467   C C   . LEU A  1 68  ? 4.614   -47.318  -52.325 1.00 60.66  ? 68  LEU A C   1 
ATOM   468   O O   . LEU A  1 68  ? 5.345   -47.284  -53.314 1.00 56.23  ? 68  LEU A O   1 
ATOM   469   C CB  . LEU A  1 68  ? 2.678   -45.734  -52.451 1.00 48.22  ? 68  LEU A CB  1 
ATOM   470   C CG  . LEU A  1 68  ? 1.292   -45.434  -53.021 1.00 54.22  ? 68  LEU A CG  1 
ATOM   471   C CD1 . LEU A  1 68  ? 1.067   -43.934  -53.102 1.00 49.90  ? 68  LEU A CD1 1 
ATOM   472   C CD2 . LEU A  1 68  ? 1.136   -46.076  -54.390 1.00 31.68  ? 68  LEU A CD2 1 
ATOM   473   N N   . GLY A  1 69  ? 5.076   -47.457  -51.087 1.00 64.05  ? 69  GLY A N   1 
ATOM   474   C CA  . GLY A  1 69  ? 6.494   -47.591  -50.819 1.00 61.71  ? 69  GLY A CA  1 
ATOM   475   C C   . GLY A  1 69  ? 7.151   -46.270  -50.473 1.00 70.32  ? 69  GLY A C   1 
ATOM   476   O O   . GLY A  1 69  ? 8.254   -45.977  -50.934 1.00 76.75  ? 69  GLY A O   1 
ATOM   477   N N   . ASN A  1 70  ? 6.468   -45.467  -49.663 1.00 70.35  ? 70  ASN A N   1 
ATOM   478   C CA  . ASN A  1 70  ? 7.030   -44.211  -49.184 1.00 76.69  ? 70  ASN A CA  1 
ATOM   479   C C   . ASN A  1 70  ? 8.388   -44.465  -48.544 1.00 85.87  ? 70  ASN A C   1 
ATOM   480   O O   . ASN A  1 70  ? 8.539   -45.400  -47.758 1.00 82.79  ? 70  ASN A O   1 
ATOM   481   C CB  . ASN A  1 70  ? 6.078   -43.552  -48.182 1.00 76.54  ? 70  ASN A CB  1 
ATOM   482   C CG  . ASN A  1 70  ? 6.494   -42.138  -47.816 1.00 77.14  ? 70  ASN A CG  1 
ATOM   483   O OD1 . ASN A  1 70  ? 7.656   -41.876  -47.507 1.00 74.62  ? 70  ASN A OD1 1 
ATOM   484   N ND2 . ASN A  1 70  ? 5.536   -41.218  -47.836 1.00 80.86  ? 70  ASN A ND2 1 
ATOM   485   N N   . PRO A  1 71  ? 9.388   -43.642  -48.892 1.00 97.73  ? 71  PRO A N   1 
ATOM   486   C CA  . PRO A  1 71  ? 10.746  -43.798  -48.362 1.00 86.16  ? 71  PRO A CA  1 
ATOM   487   C C   . PRO A  1 71  ? 10.774  -43.988  -46.846 1.00 91.89  ? 71  PRO A C   1 
ATOM   488   O O   . PRO A  1 71  ? 11.669  -44.659  -46.335 1.00 110.48 ? 71  PRO A O   1 
ATOM   489   C CB  . PRO A  1 71  ? 11.416  -42.479  -48.745 1.00 81.46  ? 71  PRO A CB  1 
ATOM   490   C CG  . PRO A  1 71  ? 10.722  -42.073  -49.998 1.00 92.79  ? 71  PRO A CG  1 
ATOM   491   C CD  . PRO A  1 71  ? 9.293   -42.525  -49.849 1.00 95.75  ? 71  PRO A CD  1 
ATOM   492   N N   . GLU A  1 72  ? 9.808   -43.411  -46.139 1.00 92.83  ? 72  GLU A N   1 
ATOM   493   C CA  . GLU A  1 72  ? 9.753   -43.555  -44.687 1.00 98.85  ? 72  GLU A CA  1 
ATOM   494   C C   . GLU A  1 72  ? 9.194   -44.908  -44.268 1.00 89.71  ? 72  GLU A C   1 
ATOM   495   O O   . GLU A  1 72  ? 9.615   -45.479  -43.265 1.00 87.85  ? 72  GLU A O   1 
ATOM   496   C CB  . GLU A  1 72  ? 8.925   -42.436  -44.058 1.00 97.44  ? 72  GLU A CB  1 
ATOM   497   C CG  . GLU A  1 72  ? 9.529   -41.069  -44.254 1.00 109.64 ? 72  GLU A CG  1 
ATOM   498   C CD  . GLU A  1 72  ? 11.009  -41.040  -43.937 1.00 120.55 ? 72  GLU A CD  1 
ATOM   499   O OE1 . GLU A  1 72  ? 11.431  -41.748  -42.999 1.00 110.17 ? 72  GLU A OE1 1 
ATOM   500   O OE2 . GLU A  1 72  ? 11.750  -40.309  -44.628 1.00 117.40 ? 72  GLU A OE2 1 
ATOM   501   N N   . CYS A  1 73  ? 8.240   -45.416  -45.036 1.00 102.68 ? 73  CYS A N   1 
ATOM   502   C CA  . CYS A  1 73  ? 7.611   -46.686  -44.719 1.00 109.81 ? 73  CYS A CA  1 
ATOM   503   C C   . CYS A  1 73  ? 8.515   -47.861  -45.083 1.00 120.18 ? 73  CYS A C   1 
ATOM   504   O O   . CYS A  1 73  ? 8.136   -48.718  -45.875 1.00 119.57 ? 73  CYS A O   1 
ATOM   505   C CB  . CYS A  1 73  ? 6.272   -46.794  -45.450 1.00 85.09  ? 73  CYS A CB  1 
ATOM   506   S SG  . CYS A  1 73  ? 5.141   -45.414  -45.139 1.00 93.40  ? 73  CYS A SG  1 
ATOM   507   N N   . GLU A  1 74  ? 9.711   -47.897  -44.506 1.00 141.29 ? 74  GLU A N   1 
ATOM   508   C CA  . GLU A  1 74  ? 10.713  -48.866  -44.922 1.00 150.60 ? 74  GLU A CA  1 
ATOM   509   C C   . GLU A  1 74  ? 10.583  -50.100  -44.070 1.00 160.93 ? 74  GLU A C   1 
ATOM   510   O O   . GLU A  1 74  ? 10.541  -51.232  -44.571 1.00 157.74 ? 74  GLU A O   1 
ATOM   511   C CB  . GLU A  1 74  ? 12.119  -48.293  -44.714 1.00 155.20 ? 74  GLU A CB  1 
ATOM   512   C CG  . GLU A  1 74  ? 13.135  -48.706  -45.769 1.00 163.96 ? 74  GLU A CG  1 
ATOM   513   C CD  . GLU A  1 74  ? 13.957  -47.534  -46.299 1.00 169.02 ? 74  GLU A CD  1 
ATOM   514   O OE1 . GLU A  1 74  ? 13.625  -46.362  -46.012 1.00 165.38 ? 74  GLU A OE1 1 
ATOM   515   O OE2 . GLU A  1 74  ? 14.941  -47.793  -47.020 1.00 164.68 ? 74  GLU A OE2 1 
ATOM   516   N N   . SER A  1 75  ? 10.528  -49.875  -42.760 1.00 153.10 ? 75  SER A N   1 
ATOM   517   C CA  . SER A  1 75  ? 10.896  -50.938  -41.804 1.00 169.37 ? 75  SER A CA  1 
ATOM   518   C C   . SER A  1 75  ? 9.831   -51.520  -40.913 1.00 177.94 ? 75  SER A C   1 
ATOM   519   O O   . SER A  1 75  ? 9.967   -51.442  -39.700 1.00 178.03 ? 75  SER A O   1 
ATOM   520   C CB  . SER A  1 75  ? 12.054  -50.473  -40.890 1.00 168.93 ? 75  SER A CB  1 
ATOM   521   O OG  . SER A  1 75  ? 11.620  -49.433  -39.986 1.00 162.66 ? 75  SER A OG  1 
ATOM   522   N N   . LEU A  1 76  ? 8.824   -52.143  -41.510 1.00 195.73 ? 76  LEU A N   1 
ATOM   523   C CA  . LEU A  1 76  ? 7.748   -52.758  -40.756 1.00 196.25 ? 76  LEU A CA  1 
ATOM   524   C C   . LEU A  1 76  ? 7.211   -53.970  -41.483 1.00 198.22 ? 76  LEU A C   1 
ATOM   525   O O   . LEU A  1 76  ? 6.454   -54.786  -40.937 1.00 196.47 ? 76  LEU A O   1 
ATOM   526   C CB  . LEU A  1 76  ? 6.567   -51.816  -40.675 1.00 186.12 ? 76  LEU A CB  1 
ATOM   527   C CG  . LEU A  1 76  ? 6.299   -51.117  -39.352 1.00 172.62 ? 76  LEU A CG  1 
ATOM   528   C CD1 . LEU A  1 76  ? 5.078   -50.262  -39.558 1.00 133.94 ? 76  LEU A CD1 1 
ATOM   529   C CD2 . LEU A  1 76  ? 6.099   -52.126  -38.222 1.00 178.19 ? 76  LEU A CD2 1 
ATOM   530   N N   . SER A  1 77  ? 7.581   -54.060  -42.746 1.00 189.24 ? 77  SER A N   1 
ATOM   531   C CA  . SER A  1 77  ? 6.894   -54.932  -43.669 1.00 177.19 ? 77  SER A CA  1 
ATOM   532   C C   . SER A  1 77  ? 7.751   -56.132  -44.016 1.00 182.12 ? 77  SER A C   1 
ATOM   533   O O   . SER A  1 77  ? 8.282   -56.212  -45.119 1.00 162.40 ? 77  SER A O   1 
ATOM   534   C CB  . SER A  1 77  ? 6.565   -54.169  -44.954 1.00 148.30 ? 77  SER A CB  1 
ATOM   535   O OG  . SER A  1 77  ? 7.761   -53.824  -45.628 1.00 137.65 ? 77  SER A OG  1 
ATOM   536   N N   . THR A  1 78  ? 7.923   -57.049  -43.076 1.00 233.52 ? 78  THR A N   1 
ATOM   537   C CA  . THR A  1 78  ? 8.434   -58.361  -43.437 1.00 225.44 ? 78  THR A CA  1 
ATOM   538   C C   . THR A  1 78  ? 7.478   -59.421  -42.899 1.00 223.91 ? 78  THR A C   1 
ATOM   539   O O   . THR A  1 78  ? 7.747   -60.105  -41.913 1.00 215.79 ? 78  THR A O   1 
ATOM   540   C CB  . THR A  1 78  ? 9.898   -58.603  -42.977 1.00 221.82 ? 78  THR A CB  1 
ATOM   541   O OG1 . THR A  1 78  ? 10.029  -59.938  -42.465 1.00 232.62 ? 78  THR A OG1 1 
ATOM   542   N N   . ALA A  1 79  ? 6.345   -59.533  -43.580 1.00 206.53 ? 79  ALA A N   1 
ATOM   543   C CA  . ALA A  1 79  ? 5.223   -60.349  -43.139 1.00 179.33 ? 79  ALA A CA  1 
ATOM   544   C C   . ALA A  1 79  ? 4.711   -61.213  -44.275 1.00 163.70 ? 79  ALA A C   1 
ATOM   545   O O   . ALA A  1 79  ? 5.198   -61.127  -45.401 1.00 150.99 ? 79  ALA A O   1 
ATOM   546   C CB  . ALA A  1 79  ? 4.058   -59.463  -42.720 1.00 170.47 ? 79  ALA A CB  1 
ATOM   547   N N   . SER A  1 80  ? 3.706   -62.028  -43.971 1.00 100.30 ? 80  SER A N   1 
ATOM   548   C CA  . SER A  1 80  ? 3.117   -62.934  -44.944 1.00 88.73  ? 80  SER A CA  1 
ATOM   549   C C   . SER A  1 80  ? 1.600   -62.922  -44.826 1.00 79.36  ? 80  SER A C   1 
ATOM   550   O O   . SER A  1 80  ? 0.886   -63.278  -45.764 1.00 69.21  ? 80  SER A O   1 
ATOM   551   C CB  . SER A  1 80  ? 3.655   -64.332  -44.640 1.00 101.91 ? 80  SER A CB  1 
ATOM   552   O OG  . SER A  1 80  ? 5.067   -64.318  -44.526 1.00 117.38 ? 80  SER A OG  1 
ATOM   553   N N   . SER A  1 81  ? 1.118   -62.499  -43.662 1.00 75.05  ? 81  SER A N   1 
ATOM   554   C CA  . SER A  1 81  ? -0.311  -62.466  -43.385 1.00 70.40  ? 81  SER A CA  1 
ATOM   555   C C   . SER A  1 81  ? -0.614  -61.635  -42.147 1.00 65.32  ? 81  SER A C   1 
ATOM   556   O O   . SER A  1 81  ? 0.267   -61.385  -41.324 1.00 52.90  ? 81  SER A O   1 
ATOM   557   C CB  . SER A  1 81  ? -0.842  -63.884  -43.184 1.00 67.57  ? 81  SER A CB  1 
ATOM   558   O OG  . SER A  1 81  ? -0.151  -64.546  -42.139 1.00 66.31  ? 81  SER A OG  1 
ATOM   559   N N   . TRP A  1 82  ? -1.867  -61.213  -42.018 1.00 58.51  ? 82  TRP A N   1 
ATOM   560   C CA  . TRP A  1 82  ? -2.311  -60.492  -40.832 1.00 46.89  ? 82  TRP A CA  1 
ATOM   561   C C   . TRP A  1 82  ? -3.824  -60.580  -40.658 1.00 46.24  ? 82  TRP A C   1 
ATOM   562   O O   . TRP A  1 82  ? -4.573  -60.607  -41.635 1.00 60.32  ? 82  TRP A O   1 
ATOM   563   C CB  . TRP A  1 82  ? -1.854  -59.030  -40.872 1.00 48.30  ? 82  TRP A CB  1 
ATOM   564   C CG  . TRP A  1 82  ? -2.256  -58.298  -42.112 1.00 52.93  ? 82  TRP A CG  1 
ATOM   565   C CD1 . TRP A  1 82  ? -3.442  -57.664  -42.341 1.00 55.72  ? 82  TRP A CD1 1 
ATOM   566   C CD2 . TRP A  1 82  ? -1.468  -58.112  -43.294 1.00 52.98  ? 82  TRP A CD2 1 
ATOM   567   N NE1 . TRP A  1 82  ? -3.443  -57.100  -43.593 1.00 47.65  ? 82  TRP A NE1 1 
ATOM   568   C CE2 . TRP A  1 82  ? -2.243  -57.360  -44.199 1.00 50.30  ? 82  TRP A CE2 1 
ATOM   569   C CE3 . TRP A  1 82  ? -0.183  -58.510  -43.676 1.00 50.72  ? 82  TRP A CE3 1 
ATOM   570   C CZ2 . TRP A  1 82  ? -1.776  -56.998  -45.461 1.00 52.97  ? 82  TRP A CZ2 1 
ATOM   571   C CZ3 . TRP A  1 82  ? 0.278   -58.150  -44.930 1.00 53.98  ? 82  TRP A CZ3 1 
ATOM   572   C CH2 . TRP A  1 82  ? -0.516  -57.403  -45.807 1.00 43.34  ? 82  TRP A CH2 1 
ATOM   573   N N   . SER A  1 83  ? -4.262  -60.634  -39.404 1.00 43.74  ? 83  SER A N   1 
ATOM   574   C CA  . SER A  1 83  ? -5.680  -60.737  -39.084 1.00 52.24  ? 83  SER A CA  1 
ATOM   575   C C   . SER A  1 83  ? -6.389  -59.400  -39.265 1.00 47.36  ? 83  SER A C   1 
ATOM   576   O O   . SER A  1 83  ? -7.542  -59.351  -39.690 1.00 54.75  ? 83  SER A O   1 
ATOM   577   C CB  . SER A  1 83  ? -5.866  -61.245  -37.654 1.00 52.22  ? 83  SER A CB  1 
ATOM   578   O OG  . SER A  1 83  ? -5.090  -60.486  -36.743 1.00 45.70  ? 83  SER A OG  1 
ATOM   579   N N   . TYR A  1 84  ? -5.692  -58.318  -38.934 1.00 45.46  ? 84  TYR A N   1 
ATOM   580   C CA  . TYR A  1 84  ? -6.228  -56.974  -39.114 1.00 47.12  ? 84  TYR A CA  1 
ATOM   581   C C   . TYR A  1 84  ? -5.094  -55.961  -39.201 1.00 48.23  ? 84  TYR A C   1 
ATOM   582   O O   . TYR A  1 84  ? -3.931  -56.304  -38.998 1.00 55.24  ? 84  TYR A O   1 
ATOM   583   C CB  . TYR A  1 84  ? -7.191  -56.611  -37.980 1.00 46.82  ? 84  TYR A CB  1 
ATOM   584   C CG  . TYR A  1 84  ? -6.552  -56.537  -36.611 1.00 46.36  ? 84  TYR A CG  1 
ATOM   585   C CD1 . TYR A  1 84  ? -6.203  -55.314  -36.052 1.00 37.69  ? 84  TYR A CD1 1 
ATOM   586   C CD2 . TYR A  1 84  ? -6.302  -57.689  -35.876 1.00 47.57  ? 84  TYR A CD2 1 
ATOM   587   C CE1 . TYR A  1 84  ? -5.624  -55.241  -34.800 1.00 38.16  ? 84  TYR A CE1 1 
ATOM   588   C CE2 . TYR A  1 84  ? -5.721  -57.625  -34.622 1.00 39.15  ? 84  TYR A CE2 1 
ATOM   589   C CZ  . TYR A  1 84  ? -5.385  -56.398  -34.090 1.00 43.64  ? 84  TYR A CZ  1 
ATOM   590   O OH  . TYR A  1 84  ? -4.805  -56.324  -32.844 1.00 41.62  ? 84  TYR A OH  1 
ATOM   591   N N   . ILE A  1 85  ? -5.434  -54.714  -39.505 1.00 39.67  ? 85  ILE A N   1 
ATOM   592   C CA  . ILE A  1 85  ? -4.427  -53.673  -39.676 1.00 41.19  ? 85  ILE A CA  1 
ATOM   593   C C   . ILE A  1 85  ? -4.533  -52.601  -38.598 1.00 42.65  ? 85  ILE A C   1 
ATOM   594   O O   . ILE A  1 85  ? -5.625  -52.129  -38.280 1.00 45.54  ? 85  ILE A O   1 
ATOM   595   C CB  . ILE A  1 85  ? -4.532  -53.015  -41.064 1.00 48.22  ? 85  ILE A CB  1 
ATOM   596   C CG1 . ILE A  1 85  ? -4.272  -54.049  -42.161 1.00 42.46  ? 85  ILE A CG1 1 
ATOM   597   C CG2 . ILE A  1 85  ? -3.560  -51.849  -41.180 1.00 38.12  ? 85  ILE A CG2 1 
ATOM   598   C CD1 . ILE A  1 85  ? -4.428  -53.505  -43.561 1.00 43.02  ? 85  ILE A CD1 1 
ATOM   599   N N   . VAL A  1 86  ? -3.389  -52.222  -38.037 1.00 45.09  ? 86  VAL A N   1 
ATOM   600   C CA  . VAL A  1 86  ? -3.349  -51.190  -37.010 1.00 41.25  ? 86  VAL A CA  1 
ATOM   601   C C   . VAL A  1 86  ? -2.658  -49.933  -37.522 1.00 46.45  ? 86  VAL A C   1 
ATOM   602   O O   . VAL A  1 86  ? -1.542  -49.988  -38.041 1.00 48.79  ? 86  VAL A O   1 
ATOM   603   C CB  . VAL A  1 86  ? -2.627  -51.675  -35.741 1.00 48.76  ? 86  VAL A CB  1 
ATOM   604   C CG1 . VAL A  1 86  ? -2.630  -50.582  -34.685 1.00 34.92  ? 86  VAL A CG1 1 
ATOM   605   C CG2 . VAL A  1 86  ? -3.285  -52.933  -35.207 1.00 49.20  ? 86  VAL A CG2 1 
ATOM   606   N N   . GLU A  1 87  ? -3.335  -48.801  -37.374 1.00 55.63  ? 87  GLU A N   1 
ATOM   607   C CA  . GLU A  1 87  ? -2.792  -47.512  -37.771 1.00 45.49  ? 87  GLU A CA  1 
ATOM   608   C C   . GLU A  1 87  ? -2.759  -46.603  -36.551 1.00 52.87  ? 87  GLU A C   1 
ATOM   609   O O   . GLU A  1 87  ? -3.708  -46.573  -35.771 1.00 66.79  ? 87  GLU A O   1 
ATOM   610   C CB  . GLU A  1 87  ? -3.671  -46.887  -38.855 1.00 54.36  ? 87  GLU A CB  1 
ATOM   611   C CG  . GLU A  1 87  ? -2.928  -46.435  -40.099 1.00 56.16  ? 87  GLU A CG  1 
ATOM   612   C CD  . GLU A  1 87  ? -3.870  -45.940  -41.181 1.00 65.19  ? 87  GLU A CD  1 
ATOM   613   O OE1 . GLU A  1 87  ? -3.588  -46.178  -42.374 1.00 69.67  ? 87  GLU A OE1 1 
ATOM   614   O OE2 . GLU A  1 87  ? -4.899  -45.322  -40.837 1.00 64.19  ? 87  GLU A OE2 1 
ATOM   615   N N   . THR A  1 88  ? -1.666  -45.868  -36.377 1.00 65.67  ? 88  THR A N   1 
ATOM   616   C CA  . THR A  1 88  ? -1.571  -44.931  -35.266 1.00 76.04  ? 88  THR A CA  1 
ATOM   617   C C   . THR A  1 88  ? -2.172  -43.591  -35.669 1.00 78.43  ? 88  THR A C   1 
ATOM   618   O O   . THR A  1 88  ? -2.011  -43.155  -36.807 1.00 84.40  ? 88  THR A O   1 
ATOM   619   C CB  . THR A  1 88  ? -0.116  -44.724  -34.809 1.00 80.77  ? 88  THR A CB  1 
ATOM   620   O OG1 . THR A  1 88  ? 0.615   -44.035  -35.830 1.00 88.91  ? 88  THR A OG1 1 
ATOM   621   C CG2 . THR A  1 88  ? 0.549   -46.063  -34.518 1.00 63.28  ? 88  THR A CG2 1 
ATOM   622   N N   . PRO A  1 89  ? -2.875  -42.935  -34.735 1.00 96.13  ? 89  PRO A N   1 
ATOM   623   C CA  . PRO A  1 89  ? -3.516  -41.644  -35.008 1.00 98.16  ? 89  PRO A CA  1 
ATOM   624   C C   . PRO A  1 89  ? -2.502  -40.596  -35.450 1.00 106.79 ? 89  PRO A C   1 
ATOM   625   O O   . PRO A  1 89  ? -2.884  -39.547  -35.969 1.00 110.72 ? 89  PRO A O   1 
ATOM   626   C CB  . PRO A  1 89  ? -4.109  -41.254  -33.650 1.00 85.89  ? 89  PRO A CB  1 
ATOM   627   C CG  . PRO A  1 89  ? -4.264  -42.540  -32.915 1.00 94.98  ? 89  PRO A CG  1 
ATOM   628   C CD  . PRO A  1 89  ? -3.116  -43.393  -33.356 1.00 101.87 ? 89  PRO A CD  1 
ATOM   629   N N   . SER A  1 90  ? -1.222  -40.885  -35.245 1.00 108.89 ? 90  SER A N   1 
ATOM   630   C CA  . SER A  1 90  ? -0.161  -39.938  -35.562 1.00 108.80 ? 90  SER A CA  1 
ATOM   631   C C   . SER A  1 90  ? 0.628   -40.361  -36.794 1.00 121.12 ? 90  SER A C   1 
ATOM   632   O O   . SER A  1 90  ? 1.784   -39.977  -36.962 1.00 132.82 ? 90  SER A O   1 
ATOM   633   C CB  . SER A  1 90  ? 0.786   -39.785  -34.371 1.00 120.10 ? 90  SER A CB  1 
ATOM   634   O OG  . SER A  1 90  ? 1.764   -38.791  -34.623 1.00 143.62 ? 90  SER A OG  1 
ATOM   635   N N   . SER A  1 91  ? 0.004   -41.160  -37.651 1.00 109.30 ? 91  SER A N   1 
ATOM   636   C CA  . SER A  1 91  ? 0.648   -41.585  -38.886 1.00 96.39  ? 91  SER A CA  1 
ATOM   637   C C   . SER A  1 91  ? 0.225   -40.681  -40.034 1.00 108.18 ? 91  SER A C   1 
ATOM   638   O O   . SER A  1 91  ? -0.967  -40.520  -40.299 1.00 110.07 ? 91  SER A O   1 
ATOM   639   C CB  . SER A  1 91  ? 0.301   -43.038  -39.201 1.00 89.68  ? 91  SER A CB  1 
ATOM   640   O OG  . SER A  1 91  ? -1.102  -43.232  -39.233 1.00 91.44  ? 91  SER A OG  1 
ATOM   641   N N   . ASP A  1 92  ? 1.205   -40.093  -40.713 1.00 120.23 ? 92  ASP A N   1 
ATOM   642   C CA  . ASP A  1 92  ? 0.925   -39.152  -41.793 1.00 123.89 ? 92  ASP A CA  1 
ATOM   643   C C   . ASP A  1 92  ? 1.815   -39.359  -43.017 1.00 114.18 ? 92  ASP A C   1 
ATOM   644   O O   . ASP A  1 92  ? 1.652   -38.678  -44.030 1.00 122.68 ? 92  ASP A O   1 
ATOM   645   C CB  . ASP A  1 92  ? 1.057   -37.712  -41.293 1.00 141.70 ? 92  ASP A CB  1 
ATOM   646   C CG  . ASP A  1 92  ? -0.012  -37.344  -40.282 1.00 151.86 ? 92  ASP A CG  1 
ATOM   647   O OD1 . ASP A  1 92  ? -1.070  -38.006  -40.260 1.00 154.24 ? 92  ASP A OD1 1 
ATOM   648   O OD2 . ASP A  1 92  ? 0.203   -36.385  -39.513 1.00 153.39 ? 92  ASP A OD2 1 
ATOM   649   N N   . ASN A  1 93  ? 2.757   -40.291  -42.923 1.00 106.23 ? 93  ASN A N   1 
ATOM   650   C CA  . ASN A  1 93  ? 3.599   -40.620  -44.067 1.00 108.12 ? 93  ASN A CA  1 
ATOM   651   C C   . ASN A  1 93  ? 2.848   -41.468  -45.090 1.00 96.37  ? 93  ASN A C   1 
ATOM   652   O O   . ASN A  1 93  ? 3.015   -42.686  -45.143 1.00 84.20  ? 93  ASN A O   1 
ATOM   653   C CB  . ASN A  1 93  ? 4.880   -41.329  -43.622 1.00 107.90 ? 93  ASN A CB  1 
ATOM   654   C CG  . ASN A  1 93  ? 5.860   -40.392  -42.937 1.00 114.14 ? 93  ASN A CG  1 
ATOM   655   O OD1 . ASN A  1 93  ? 6.322   -40.662  -41.828 1.00 118.86 ? 93  ASN A OD1 1 
ATOM   656   N ND2 . ASN A  1 93  ? 6.183   -39.283  -43.600 1.00 114.00 ? 93  ASN A ND2 1 
ATOM   657   N N   . GLY A  1 94  ? 2.014   -40.815  -45.894 1.00 99.01  ? 94  GLY A N   1 
ATOM   658   C CA  . GLY A  1 94  ? 1.261   -41.493  -46.932 1.00 86.60  ? 94  GLY A CA  1 
ATOM   659   C C   . GLY A  1 94  ? 1.735   -41.082  -48.311 1.00 82.53  ? 94  GLY A C   1 
ATOM   660   O O   . GLY A  1 94  ? 2.868   -41.369  -48.696 1.00 74.34  ? 94  GLY A O   1 
ATOM   661   N N   . THR A  1 95  ? 0.869   -40.404  -49.057 1.00 66.61  ? 95  THR A N   1 
ATOM   662   C CA  . THR A  1 95  ? 1.230   -39.912  -50.381 1.00 68.66  ? 95  THR A CA  1 
ATOM   663   C C   . THR A  1 95  ? 2.018   -38.609  -50.288 1.00 67.97  ? 95  THR A C   1 
ATOM   664   O O   . THR A  1 95  ? 1.441   -37.529  -50.161 1.00 78.25  ? 95  THR A O   1 
ATOM   665   C CB  . THR A  1 95  ? -0.011  -39.706  -51.272 1.00 63.44  ? 95  THR A CB  1 
ATOM   666   O OG1 . THR A  1 95  ? -1.029  -39.024  -50.529 1.00 60.53  ? 95  THR A OG1 1 
ATOM   667   C CG2 . THR A  1 95  ? -0.552  -41.046  -51.745 1.00 63.26  ? 95  THR A CG2 1 
ATOM   668   N N   . CYS A  1 96  ? 3.342   -38.724  -50.351 1.00 67.34  ? 96  CYS A N   1 
ATOM   669   C CA  . CYS A  1 96  ? 4.223   -37.565  -50.258 1.00 70.77  ? 96  CYS A CA  1 
ATOM   670   C C   . CYS A  1 96  ? 4.054   -36.609  -51.437 1.00 67.97  ? 96  CYS A C   1 
ATOM   671   O O   . CYS A  1 96  ? 4.213   -35.399  -51.289 1.00 63.52  ? 96  CYS A O   1 
ATOM   672   C CB  . CYS A  1 96  ? 5.683   -38.007  -50.121 1.00 66.39  ? 96  CYS A CB  1 
ATOM   673   S SG  . CYS A  1 96  ? 6.135   -39.426  -51.142 1.00 80.12  ? 96  CYS A SG  1 
ATOM   674   N N   . TYR A  1 97  ? 3.736   -37.152  -52.608 1.00 62.85  ? 97  TYR A N   1 
ATOM   675   C CA  . TYR A  1 97  ? 3.403   -36.313  -53.752 1.00 57.96  ? 97  TYR A CA  1 
ATOM   676   C C   . TYR A  1 97  ? 1.891   -36.133  -53.813 1.00 60.20  ? 97  TYR A C   1 
ATOM   677   O O   . TYR A  1 97  ? 1.147   -37.113  -53.857 1.00 71.19  ? 97  TYR A O   1 
ATOM   678   C CB  . TYR A  1 97  ? 3.923   -36.917  -55.058 1.00 61.91  ? 97  TYR A CB  1 
ATOM   679   C CG  . TYR A  1 97  ? 4.005   -35.921  -56.196 1.00 61.56  ? 97  TYR A CG  1 
ATOM   680   C CD1 . TYR A  1 97  ? 5.228   -35.413  -56.613 1.00 67.40  ? 97  TYR A CD1 1 
ATOM   681   C CD2 . TYR A  1 97  ? 2.859   -35.479  -56.843 1.00 63.12  ? 97  TYR A CD2 1 
ATOM   682   C CE1 . TYR A  1 97  ? 5.309   -34.499  -57.649 1.00 65.31  ? 97  TYR A CE1 1 
ATOM   683   C CE2 . TYR A  1 97  ? 2.929   -34.565  -57.880 1.00 62.52  ? 97  TYR A CE2 1 
ATOM   684   C CZ  . TYR A  1 97  ? 4.156   -34.079  -58.278 1.00 62.20  ? 97  TYR A CZ  1 
ATOM   685   O OH  . TYR A  1 97  ? 4.230   -33.169  -59.308 1.00 58.64  ? 97  TYR A OH  1 
ATOM   686   N N   . PRO A  1 98  ? 1.433   -34.873  -53.810 1.00 56.38  ? 98  PRO A N   1 
ATOM   687   C CA  . PRO A  1 98  ? 0.004   -34.544  -53.770 1.00 47.48  ? 98  PRO A CA  1 
ATOM   688   C C   . PRO A  1 98  ? -0.770  -35.228  -54.888 1.00 60.58  ? 98  PRO A C   1 
ATOM   689   O O   . PRO A  1 98  ? -0.271  -35.330  -56.008 1.00 55.02  ? 98  PRO A O   1 
ATOM   690   C CB  . PRO A  1 98  ? -0.012  -33.028  -53.979 1.00 54.12  ? 98  PRO A CB  1 
ATOM   691   C CG  . PRO A  1 98  ? 1.322   -32.573  -53.528 1.00 65.15  ? 98  PRO A CG  1 
ATOM   692   C CD  . PRO A  1 98  ? 2.275   -33.668  -53.884 1.00 65.64  ? 98  PRO A CD  1 
ATOM   693   N N   . GLY A  1 99  ? -1.976  -35.690  -54.581 1.00 60.90  ? 99  GLY A N   1 
ATOM   694   C CA  . GLY A  1 99  ? -2.804  -36.354  -55.568 1.00 58.21  ? 99  GLY A CA  1 
ATOM   695   C C   . GLY A  1 99  ? -3.946  -37.126  -54.943 1.00 63.47  ? 99  GLY A C   1 
ATOM   696   O O   . GLY A  1 99  ? -4.079  -37.181  -53.720 1.00 57.66  ? 99  GLY A O   1 
ATOM   697   N N   . ASP A  1 100 ? -4.772  -37.728  -55.791 1.00 63.97  ? 100 ASP A N   1 
ATOM   698   C CA  . ASP A  1 100 ? -5.934  -38.471  -55.327 1.00 56.55  ? 100 ASP A CA  1 
ATOM   699   C C   . ASP A  1 100 ? -5.680  -39.972  -55.393 1.00 48.16  ? 100 ASP A C   1 
ATOM   700   O O   . ASP A  1 100 ? -5.177  -40.482  -56.393 1.00 47.54  ? 100 ASP A O   1 
ATOM   701   C CB  . ASP A  1 100 ? -7.162  -38.110  -56.167 1.00 63.75  ? 100 ASP A CB  1 
ATOM   702   C CG  . ASP A  1 100 ? -8.460  -38.548  -55.521 1.00 84.16  ? 100 ASP A CG  1 
ATOM   703   O OD1 . ASP A  1 100 ? -8.458  -38.810  -54.300 1.00 100.64 ? 100 ASP A OD1 1 
ATOM   704   O OD2 . ASP A  1 100 ? -9.485  -38.623  -56.231 1.00 78.57  ? 100 ASP A OD2 1 
ATOM   705   N N   . PHE A  1 101 ? -6.021  -40.674  -54.317 1.00 48.49  ? 101 PHE A N   1 
ATOM   706   C CA  . PHE A  1 101 ? -5.925  -42.128  -54.295 1.00 50.92  ? 101 PHE A CA  1 
ATOM   707   C C   . PHE A  1 101 ? -7.300  -42.711  -54.598 1.00 43.15  ? 101 PHE A C   1 
ATOM   708   O O   . PHE A  1 101 ? -8.163  -42.776  -53.723 1.00 41.90  ? 101 PHE A O   1 
ATOM   709   C CB  . PHE A  1 101 ? -5.429  -42.618  -52.933 1.00 38.55  ? 101 PHE A CB  1 
ATOM   710   C CG  . PHE A  1 101 ? -4.728  -43.948  -52.983 1.00 39.04  ? 101 PHE A CG  1 
ATOM   711   C CD1 . PHE A  1 101 ? -3.413  -44.068  -52.564 1.00 43.38  ? 101 PHE A CD1 1 
ATOM   712   C CD2 . PHE A  1 101 ? -5.379  -45.074  -53.457 1.00 50.74  ? 101 PHE A CD2 1 
ATOM   713   C CE1 . PHE A  1 101 ? -2.763  -45.289  -52.609 1.00 39.65  ? 101 PHE A CE1 1 
ATOM   714   C CE2 . PHE A  1 101 ? -4.734  -46.297  -53.507 1.00 38.30  ? 101 PHE A CE2 1 
ATOM   715   C CZ  . PHE A  1 101 ? -3.425  -46.404  -53.082 1.00 32.43  ? 101 PHE A CZ  1 
ATOM   716   N N   . ILE A  1 102 ? -7.502  -43.127  -55.844 1.00 35.30  ? 102 ILE A N   1 
ATOM   717   C CA  . ILE A  1 102 ? -8.806  -43.601  -56.296 1.00 38.88  ? 102 ILE A CA  1 
ATOM   718   C C   . ILE A  1 102 ? -9.238  -44.874  -55.576 1.00 38.28  ? 102 ILE A C   1 
ATOM   719   O O   . ILE A  1 102 ? -8.476  -45.836  -55.485 1.00 46.80  ? 102 ILE A O   1 
ATOM   720   C CB  . ILE A  1 102 ? -8.813  -43.854  -57.815 1.00 49.59  ? 102 ILE A CB  1 
ATOM   721   C CG1 . ILE A  1 102 ? -8.213  -42.656  -58.553 1.00 48.10  ? 102 ILE A CG1 1 
ATOM   722   C CG2 . ILE A  1 102 ? -10.224 -44.149  -58.303 1.00 32.88  ? 102 ILE A CG2 1 
ATOM   723   C CD1 . ILE A  1 102 ? -8.931  -41.350  -58.291 1.00 43.20  ? 102 ILE A CD1 1 
ATOM   724   N N   . ASP A  1 103 ? -10.468 -44.870  -55.070 1.00 44.07  ? 103 ASP A N   1 
ATOM   725   C CA  . ASP A  1 103 ? -11.011 -46.013  -54.344 1.00 40.66  ? 103 ASP A CA  1 
ATOM   726   C C   . ASP A  1 103 ? -10.068 -46.440  -53.226 1.00 41.95  ? 103 ASP A C   1 
ATOM   727   O O   . ASP A  1 103 ? -9.788  -47.626  -53.053 1.00 45.54  ? 103 ASP A O   1 
ATOM   728   C CB  . ASP A  1 103 ? -11.266 -47.181  -55.298 1.00 44.39  ? 103 ASP A CB  1 
ATOM   729   C CG  . ASP A  1 103 ? -12.288 -46.848  -56.367 1.00 52.53  ? 103 ASP A CG  1 
ATOM   730   O OD1 . ASP A  1 103 ? -13.199 -46.039  -56.092 1.00 64.01  ? 103 ASP A OD1 1 
ATOM   731   O OD2 . ASP A  1 103 ? -12.183 -47.399  -57.483 1.00 54.92  ? 103 ASP A OD2 1 
ATOM   732   N N   . TYR A  1 104 ? -9.583  -45.462  -52.469 1.00 44.68  ? 104 TYR A N   1 
ATOM   733   C CA  . TYR A  1 104 ? -8.622  -45.711  -51.401 1.00 35.20  ? 104 TYR A CA  1 
ATOM   734   C C   . TYR A  1 104 ? -9.235  -46.502  -50.250 1.00 43.20  ? 104 TYR A C   1 
ATOM   735   O O   . TYR A  1 104 ? -8.677  -47.508  -49.812 1.00 36.25  ? 104 TYR A O   1 
ATOM   736   C CB  . TYR A  1 104 ? -8.043  -44.389  -50.891 1.00 29.14  ? 104 TYR A CB  1 
ATOM   737   C CG  . TYR A  1 104 ? -7.069  -44.539  -49.746 1.00 41.37  ? 104 TYR A CG  1 
ATOM   738   C CD1 . TYR A  1 104 ? -5.990  -45.408  -49.837 1.00 38.56  ? 104 TYR A CD1 1 
ATOM   739   C CD2 . TYR A  1 104 ? -7.218  -43.800  -48.581 1.00 33.99  ? 104 TYR A CD2 1 
ATOM   740   C CE1 . TYR A  1 104 ? -5.094  -45.546  -48.793 1.00 33.39  ? 104 TYR A CE1 1 
ATOM   741   C CE2 . TYR A  1 104 ? -6.326  -43.929  -47.533 1.00 40.67  ? 104 TYR A CE2 1 
ATOM   742   C CZ  . TYR A  1 104 ? -5.266  -44.803  -47.644 1.00 37.49  ? 104 TYR A CZ  1 
ATOM   743   O OH  . TYR A  1 104 ? -4.378  -44.934  -46.602 1.00 49.47  ? 104 TYR A OH  1 
ATOM   744   N N   . GLU A  1 105 ? -10.385 -46.042  -49.766 1.00 44.55  ? 105 GLU A N   1 
ATOM   745   C CA  . GLU A  1 105 ? -11.071 -46.710  -48.666 1.00 42.14  ? 105 GLU A CA  1 
ATOM   746   C C   . GLU A  1 105 ? -11.370 -48.163  -49.020 1.00 46.67  ? 105 GLU A C   1 
ATOM   747   O O   . GLU A  1 105 ? -11.312 -49.045  -48.164 1.00 42.64  ? 105 GLU A O   1 
ATOM   748   C CB  . GLU A  1 105 ? -12.362 -45.971  -48.303 1.00 42.99  ? 105 GLU A CB  1 
ATOM   749   C CG  . GLU A  1 105 ? -12.158 -44.518  -47.901 1.00 40.41  ? 105 GLU A CG  1 
ATOM   750   C CD  . GLU A  1 105 ? -11.814 -43.626  -49.080 1.00 60.55  ? 105 GLU A CD  1 
ATOM   751   O OE1 . GLU A  1 105 ? -12.311 -43.893  -50.194 1.00 70.17  ? 105 GLU A OE1 1 
ATOM   752   O OE2 . GLU A  1 105 ? -11.051 -42.656  -48.893 1.00 56.91  ? 105 GLU A OE2 1 
ATOM   753   N N   . GLU A  1 106 ? -11.686 -48.406  -50.288 1.00 38.49  ? 106 GLU A N   1 
ATOM   754   C CA  . GLU A  1 106 ? -11.932 -49.761  -50.766 1.00 32.04  ? 106 GLU A CA  1 
ATOM   755   C C   . GLU A  1 106 ? -10.668 -50.605  -50.682 1.00 35.02  ? 106 GLU A C   1 
ATOM   756   O O   . GLU A  1 106 ? -10.694 -51.735  -50.196 1.00 40.86  ? 106 GLU A O   1 
ATOM   757   C CB  . GLU A  1 106 ? -12.463 -49.738  -52.200 1.00 39.81  ? 106 GLU A CB  1 
ATOM   758   C CG  . GLU A  1 106 ? -13.965 -49.538  -52.286 1.00 51.78  ? 106 GLU A CG  1 
ATOM   759   C CD  . GLU A  1 106 ? -14.740 -50.747  -51.790 1.00 52.77  ? 106 GLU A CD  1 
ATOM   760   O OE1 . GLU A  1 106 ? -14.300 -51.886  -52.052 1.00 57.12  ? 106 GLU A OE1 1 
ATOM   761   O OE2 . GLU A  1 106 ? -15.794 -50.559  -51.145 1.00 45.98  ? 106 GLU A OE2 1 
ATOM   762   N N   . LEU A  1 107 ? -9.561  -50.044  -51.152 1.00 43.16  ? 107 LEU A N   1 
ATOM   763   C CA  . LEU A  1 107 ? -8.276  -50.722  -51.085 1.00 44.85  ? 107 LEU A CA  1 
ATOM   764   C C   . LEU A  1 107 ? -7.987  -51.169  -49.654 1.00 40.98  ? 107 LEU A C   1 
ATOM   765   O O   . LEU A  1 107 ? -7.654  -52.328  -49.408 1.00 40.01  ? 107 LEU A O   1 
ATOM   766   C CB  . LEU A  1 107 ? -7.168  -49.785  -51.559 1.00 40.88  ? 107 LEU A CB  1 
ATOM   767   C CG  . LEU A  1 107 ? -6.032  -50.383  -52.392 1.00 54.40  ? 107 LEU A CG  1 
ATOM   768   C CD1 . LEU A  1 107 ? -4.714  -49.691  -52.073 1.00 41.84  ? 107 LEU A CD1 1 
ATOM   769   C CD2 . LEU A  1 107 ? -5.945  -51.896  -52.248 1.00 40.20  ? 107 LEU A CD2 1 
ATOM   770   N N   . ARG A  1 108 ? -8.126  -50.237  -48.717 1.00 31.55  ? 108 ARG A N   1 
ATOM   771   C CA  . ARG A  1 108 ? -7.886  -50.506  -47.303 1.00 41.48  ? 108 ARG A CA  1 
ATOM   772   C C   . ARG A  1 108 ? -8.750  -51.653  -46.783 1.00 46.24  ? 108 ARG A C   1 
ATOM   773   O O   . ARG A  1 108 ? -8.272  -52.521  -46.052 1.00 41.63  ? 108 ARG A O   1 
ATOM   774   C CB  . ARG A  1 108 ? -8.147  -49.244  -46.479 1.00 40.78  ? 108 ARG A CB  1 
ATOM   775   C CG  . ARG A  1 108 ? -7.283  -48.055  -46.873 1.00 39.82  ? 108 ARG A CG  1 
ATOM   776   C CD  . ARG A  1 108 ? -7.785  -46.770  -46.233 1.00 39.67  ? 108 ARG A CD  1 
ATOM   777   N NE  . ARG A  1 108 ? -7.846  -46.868  -44.778 1.00 48.00  ? 108 ARG A NE  1 
ATOM   778   C CZ  . ARG A  1 108 ? -6.892  -46.440  -43.957 1.00 48.31  ? 108 ARG A CZ  1 
ATOM   779   N NH1 . ARG A  1 108 ? -5.797  -45.876  -44.447 1.00 38.10  ? 108 ARG A NH1 1 
ATOM   780   N NH2 . ARG A  1 108 ? -7.035  -46.572  -42.645 1.00 45.27  ? 108 ARG A NH2 1 
ATOM   781   N N   . GLU A  1 109 ? -10.025 -51.647  -47.159 1.00 45.05  ? 109 GLU A N   1 
ATOM   782   C CA  . GLU A  1 109 ? -10.957 -52.686  -46.735 1.00 44.02  ? 109 GLU A CA  1 
ATOM   783   C C   . GLU A  1 109 ? -10.517 -54.057  -47.237 1.00 44.20  ? 109 GLU A C   1 
ATOM   784   O O   . GLU A  1 109 ? -10.616 -55.053  -46.521 1.00 38.75  ? 109 GLU A O   1 
ATOM   785   C CB  . GLU A  1 109 ? -12.366 -52.371  -47.240 1.00 44.18  ? 109 GLU A CB  1 
ATOM   786   C CG  . GLU A  1 109 ? -13.425 -53.374  -46.813 1.00 59.53  ? 109 GLU A CG  1 
ATOM   787   C CD  . GLU A  1 109 ? -13.716 -53.322  -45.325 1.00 72.18  ? 109 GLU A CD  1 
ATOM   788   O OE1 . GLU A  1 109 ? -12.983 -52.625  -44.592 1.00 81.11  ? 109 GLU A OE1 1 
ATOM   789   O OE2 . GLU A  1 109 ? -14.682 -53.978  -44.886 1.00 74.15  ? 109 GLU A OE2 1 
ATOM   790   N N   . GLN A  1 110 ? -10.031 -54.100  -48.474 1.00 41.80  ? 110 GLN A N   1 
ATOM   791   C CA  . GLN A  1 110 ? -9.591  -55.350  -49.083 1.00 50.77  ? 110 GLN A CA  1 
ATOM   792   C C   . GLN A  1 110 ? -8.282  -55.834  -48.465 1.00 49.28  ? 110 GLN A C   1 
ATOM   793   O O   . GLN A  1 110 ? -8.043  -57.036  -48.361 1.00 48.85  ? 110 GLN A O   1 
ATOM   794   C CB  . GLN A  1 110 ? -9.419  -55.177  -50.595 1.00 49.02  ? 110 GLN A CB  1 
ATOM   795   C CG  . GLN A  1 110 ? -10.530 -54.382  -51.257 1.00 51.87  ? 110 GLN A CG  1 
ATOM   796   C CD  . GLN A  1 110 ? -11.293 -55.179  -52.293 1.00 56.55  ? 110 GLN A CD  1 
ATOM   797   O OE1 . GLN A  1 110 ? -11.051 -56.370  -52.482 1.00 66.75  ? 110 GLN A OE1 1 
ATOM   798   N NE2 . GLN A  1 110 ? -12.223 -54.522  -52.973 1.00 54.43  ? 110 GLN A NE2 1 
ATOM   799   N N   . LEU A  1 111 ? -7.437  -54.891  -48.059 1.00 52.49  ? 111 LEU A N   1 
ATOM   800   C CA  . LEU A  1 111 ? -6.144  -55.215  -47.465 1.00 40.79  ? 111 LEU A CA  1 
ATOM   801   C C   . LEU A  1 111 ? -6.251  -55.480  -45.969 1.00 42.19  ? 111 LEU A C   1 
ATOM   802   O O   . LEU A  1 111 ? -5.295  -55.939  -45.346 1.00 45.79  ? 111 LEU A O   1 
ATOM   803   C CB  . LEU A  1 111 ? -5.152  -54.075  -47.698 1.00 40.88  ? 111 LEU A CB  1 
ATOM   804   C CG  . LEU A  1 111 ? -4.040  -54.275  -48.728 1.00 36.44  ? 111 LEU A CG  1 
ATOM   805   C CD1 . LEU A  1 111 ? -4.096  -55.660  -49.347 1.00 58.09  ? 111 LEU A CD1 1 
ATOM   806   C CD2 . LEU A  1 111 ? -4.115  -53.203  -49.794 1.00 47.78  ? 111 LEU A CD2 1 
ATOM   807   N N   . SER A  1 112 ? -7.415  -55.186  -45.397 1.00 40.51  ? 112 SER A N   1 
ATOM   808   C CA  . SER A  1 112 ? -7.606  -55.265  -43.951 1.00 43.87  ? 112 SER A CA  1 
ATOM   809   C C   . SER A  1 112 ? -7.190  -56.617  -43.374 1.00 46.36  ? 112 SER A C   1 
ATOM   810   O O   . SER A  1 112 ? -6.647  -56.687  -42.273 1.00 48.14  ? 112 SER A O   1 
ATOM   811   C CB  . SER A  1 112 ? -9.057  -54.954  -43.577 1.00 48.12  ? 112 SER A CB  1 
ATOM   812   O OG  . SER A  1 112 ? -9.929  -55.986  -44.002 1.00 47.17  ? 112 SER A OG  1 
ATOM   813   N N   . SER A  1 113 ? -7.452  -57.688  -44.114 1.00 46.79  ? 113 SER A N   1 
ATOM   814   C CA  . SER A  1 113 ? -7.013  -59.014  -43.698 1.00 47.06  ? 113 SER A CA  1 
ATOM   815   C C   . SER A  1 113 ? -6.505  -59.812  -44.891 1.00 52.49  ? 113 SER A C   1 
ATOM   816   O O   . SER A  1 113 ? -7.193  -59.945  -45.906 1.00 56.66  ? 113 SER A O   1 
ATOM   817   C CB  . SER A  1 113 ? -8.139  -59.768  -42.991 1.00 67.49  ? 113 SER A CB  1 
ATOM   818   O OG  . SER A  1 113 ? -7.658  -60.963  -42.399 1.00 60.62  ? 113 SER A OG  1 
ATOM   819   N N   . VAL A  1 114 ? -5.294  -60.341  -44.758 1.00 53.98  ? 114 VAL A N   1 
ATOM   820   C CA  . VAL A  1 114 ? -4.632  -61.030  -45.855 1.00 63.72  ? 114 VAL A CA  1 
ATOM   821   C C   . VAL A  1 114 ? -4.113  -62.399  -45.429 1.00 64.38  ? 114 VAL A C   1 
ATOM   822   O O   . VAL A  1 114 ? -3.483  -62.538  -44.380 1.00 47.19  ? 114 VAL A O   1 
ATOM   823   C CB  . VAL A  1 114 ? -3.467  -60.185  -46.402 1.00 61.84  ? 114 VAL A CB  1 
ATOM   824   C CG1 . VAL A  1 114 ? -2.172  -60.990  -46.409 1.00 65.15  ? 114 VAL A CG1 1 
ATOM   825   C CG2 . VAL A  1 114 ? -3.806  -59.640  -47.789 1.00 55.34  ? 114 VAL A CG2 1 
ATOM   826   N N   . SER A  1 115 ? -4.390  -63.410  -46.245 1.00 72.67  ? 115 SER A N   1 
ATOM   827   C CA  . SER A  1 115 ? -3.924  -64.761  -45.962 1.00 82.69  ? 115 SER A CA  1 
ATOM   828   C C   . SER A  1 115 ? -2.443  -64.889  -46.315 1.00 84.54  ? 115 SER A C   1 
ATOM   829   O O   . SER A  1 115 ? -1.616  -65.143  -45.445 1.00 87.90  ? 115 SER A O   1 
ATOM   830   C CB  . SER A  1 115 ? -4.760  -65.794  -46.720 1.00 86.59  ? 115 SER A CB  1 
ATOM   831   O OG  . SER A  1 115 ? -4.734  -67.045  -46.057 1.00 85.38  ? 115 SER A OG  1 
ATOM   832   N N   . SER A  1 116 ? -2.110  -64.718  -47.592 1.00 86.82  ? 116 SER A N   1 
ATOM   833   C CA  . SER A  1 116 ? -0.708  -64.640  -48.003 1.00 84.42  ? 116 SER A CA  1 
ATOM   834   C C   . SER A  1 116 ? -0.434  -63.336  -48.735 1.00 87.63  ? 116 SER A C   1 
ATOM   835   O O   . SER A  1 116 ? -1.288  -62.829  -49.463 1.00 89.23  ? 116 SER A O   1 
ATOM   836   C CB  . SER A  1 116 ? -0.305  -65.822  -48.887 1.00 91.39  ? 116 SER A CB  1 
ATOM   837   O OG  . SER A  1 116 ? -0.961  -65.774  -50.140 1.00 100.80 ? 116 SER A OG  1 
ATOM   838   N N   . PHE A  1 117 ? 0.771   -62.809  -48.551 1.00 78.42  ? 117 PHE A N   1 
ATOM   839   C CA  . PHE A  1 117 ? 1.124   -61.501  -49.080 1.00 63.88  ? 117 PHE A CA  1 
ATOM   840   C C   . PHE A  1 117 ? 2.621   -61.428  -49.359 1.00 61.79  ? 117 PHE A C   1 
ATOM   841   O O   . PHE A  1 117 ? 3.423   -61.343  -48.430 1.00 72.57  ? 117 PHE A O   1 
ATOM   842   C CB  . PHE A  1 117 ? 0.733   -60.427  -48.064 1.00 57.18  ? 117 PHE A CB  1 
ATOM   843   C CG  . PHE A  1 117 ? 0.721   -59.034  -48.618 1.00 62.62  ? 117 PHE A CG  1 
ATOM   844   C CD1 . PHE A  1 117 ? 1.867   -58.258  -48.602 1.00 57.83  ? 117 PHE A CD1 1 
ATOM   845   C CD2 . PHE A  1 117 ? -0.442  -58.494  -49.142 1.00 69.31  ? 117 PHE A CD2 1 
ATOM   846   C CE1 . PHE A  1 117 ? 1.856   -56.972  -49.107 1.00 49.57  ? 117 PHE A CE1 1 
ATOM   847   C CE2 . PHE A  1 117 ? -0.459  -57.210  -49.649 1.00 53.33  ? 117 PHE A CE2 1 
ATOM   848   C CZ  . PHE A  1 117 ? 0.691   -56.448  -49.632 1.00 49.11  ? 117 PHE A CZ  1 
ATOM   849   N N   . GLU A  1 118 ? 2.996   -61.471  -50.635 1.00 68.79  ? 118 GLU A N   1 
ATOM   850   C CA  . GLU A  1 118 ? 4.400   -61.339  -51.013 1.00 75.67  ? 118 GLU A CA  1 
ATOM   851   C C   . GLU A  1 118 ? 4.605   -60.227  -52.030 1.00 64.71  ? 118 GLU A C   1 
ATOM   852   O O   . GLU A  1 118 ? 3.858   -60.099  -53.000 1.00 66.15  ? 118 GLU A O   1 
ATOM   853   C CB  . GLU A  1 118 ? 4.973   -62.657  -51.550 1.00 87.70  ? 118 GLU A CB  1 
ATOM   854   C CG  . GLU A  1 118 ? 4.582   -63.000  -52.985 1.00 96.89  ? 118 GLU A CG  1 
ATOM   855   C CD  . GLU A  1 118 ? 5.599   -63.905  -53.665 1.00 120.70 ? 118 GLU A CD  1 
ATOM   856   O OE1 . GLU A  1 118 ? 6.542   -64.356  -52.982 1.00 136.66 ? 118 GLU A OE1 1 
ATOM   857   O OE2 . GLU A  1 118 ? 5.461   -64.162  -54.880 1.00 119.99 ? 118 GLU A OE2 1 
ATOM   858   N N   . ARG A  1 119 ? 5.629   -59.420  -51.801 1.00 67.50  ? 119 ARG A N   1 
ATOM   859   C CA  . ARG A  1 119 ? 5.942   -58.344  -52.717 1.00 62.44  ? 119 ARG A CA  1 
ATOM   860   C C   . ARG A  1 119 ? 7.029   -58.754  -53.709 1.00 60.27  ? 119 ARG A C   1 
ATOM   861   O O   . ARG A  1 119 ? 8.160   -59.035  -53.317 1.00 86.08  ? 119 ARG A O   1 
ATOM   862   C CB  . ARG A  1 119 ? 6.391   -57.124  -51.936 1.00 61.60  ? 119 ARG A CB  1 
ATOM   863   C CG  . ARG A  1 119 ? 6.726   -55.962  -52.815 1.00 64.43  ? 119 ARG A CG  1 
ATOM   864   C CD  . ARG A  1 119 ? 7.414   -54.873  -52.007 1.00 76.00  ? 119 ARG A CD  1 
ATOM   865   N NE  . ARG A  1 119 ? 8.770   -55.279  -51.633 1.00 82.39  ? 119 ARG A NE  1 
ATOM   866   C CZ  . ARG A  1 119 ? 9.880   -54.647  -52.015 1.00 98.06  ? 119 ARG A CZ  1 
ATOM   867   N NH1 . ARG A  1 119 ? 11.058  -55.105  -51.622 1.00 107.77 ? 119 ARG A NH1 1 
ATOM   868   N NH2 . ARG A  1 119 ? 9.825   -53.557  -52.781 1.00 86.19  ? 119 ARG A NH2 1 
ATOM   869   N N   . PHE A  1 120 ? 6.682   -58.789  -54.992 1.00 65.62  ? 120 PHE A N   1 
ATOM   870   C CA  . PHE A  1 120 ? 7.634   -59.172  -56.030 1.00 64.29  ? 120 PHE A CA  1 
ATOM   871   C C   . PHE A  1 120 ? 7.785   -58.057  -57.055 1.00 67.23  ? 120 PHE A C   1 
ATOM   872   O O   . PHE A  1 120 ? 6.872   -57.255  -57.251 1.00 68.88  ? 120 PHE A O   1 
ATOM   873   C CB  . PHE A  1 120 ? 7.194   -60.466  -56.721 1.00 63.86  ? 120 PHE A CB  1 
ATOM   874   C CG  . PHE A  1 120 ? 5.947   -60.321  -57.549 1.00 64.15  ? 120 PHE A CG  1 
ATOM   875   C CD1 . PHE A  1 120 ? 6.028   -60.122  -58.917 1.00 71.84  ? 120 PHE A CD1 1 
ATOM   876   C CD2 . PHE A  1 120 ? 4.695   -60.386  -56.960 1.00 77.90  ? 120 PHE A CD2 1 
ATOM   877   C CE1 . PHE A  1 120 ? 4.886   -59.989  -59.682 1.00 71.12  ? 120 PHE A CE1 1 
ATOM   878   C CE2 . PHE A  1 120 ? 3.547   -60.253  -57.721 1.00 68.16  ? 120 PHE A CE2 1 
ATOM   879   C CZ  . PHE A  1 120 ? 3.644   -60.054  -59.084 1.00 65.22  ? 120 PHE A CZ  1 
ATOM   880   N N   . GLU A  1 121 ? 8.945   -58.007  -57.700 1.00 71.30  ? 121 GLU A N   1 
ATOM   881   C CA  . GLU A  1 121 ? 9.199   -57.019  -58.737 1.00 66.05  ? 121 GLU A CA  1 
ATOM   882   C C   . GLU A  1 121 ? 8.509   -57.444  -60.029 1.00 68.85  ? 121 GLU A C   1 
ATOM   883   O O   . GLU A  1 121 ? 8.956   -58.367  -60.709 1.00 80.34  ? 121 GLU A O   1 
ATOM   884   C CB  . GLU A  1 121 ? 10.703  -56.855  -58.959 1.00 77.24  ? 121 GLU A CB  1 
ATOM   885   C CG  . GLU A  1 121 ? 11.090  -55.588  -59.700 1.00 88.73  ? 121 GLU A CG  1 
ATOM   886   C CD  . GLU A  1 121 ? 12.591  -55.380  -59.753 1.00 102.39 ? 121 GLU A CD  1 
ATOM   887   O OE1 . GLU A  1 121 ? 13.336  -56.364  -59.563 1.00 109.41 ? 121 GLU A OE1 1 
ATOM   888   O OE2 . GLU A  1 121 ? 13.027  -54.232  -59.985 1.00 93.88  ? 121 GLU A OE2 1 
ATOM   889   N N   . ILE A  1 122 ? 7.409   -56.771  -60.352 1.00 65.02  ? 122 ILE A N   1 
ATOM   890   C CA  . ILE A  1 122 ? 6.643   -57.084  -61.553 1.00 71.39  ? 122 ILE A CA  1 
ATOM   891   C C   . ILE A  1 122 ? 7.339   -56.557  -62.807 1.00 82.30  ? 122 ILE A C   1 
ATOM   892   O O   . ILE A  1 122 ? 7.374   -57.230  -63.837 1.00 82.67  ? 122 ILE A O   1 
ATOM   893   C CB  . ILE A  1 122 ? 5.208   -56.525  -61.466 1.00 69.91  ? 122 ILE A CB  1 
ATOM   894   C CG1 . ILE A  1 122 ? 4.453   -56.774  -62.774 1.00 60.40  ? 122 ILE A CG1 1 
ATOM   895   C CG2 . ILE A  1 122 ? 5.229   -55.042  -61.128 1.00 75.70  ? 122 ILE A CG2 1 
ATOM   896   C CD1 . ILE A  1 122 ? 3.025   -56.275  -62.755 1.00 52.87  ? 122 ILE A CD1 1 
ATOM   897   N N   . PHE A  1 123 ? 7.893   -55.353  -62.711 1.00 80.58  ? 123 PHE A N   1 
ATOM   898   C CA  . PHE A  1 123 ? 8.675   -54.782  -63.800 1.00 68.20  ? 123 PHE A CA  1 
ATOM   899   C C   . PHE A  1 123 ? 10.039  -54.333  -63.294 1.00 86.37  ? 123 PHE A C   1 
ATOM   900   O O   . PHE A  1 123 ? 10.177  -53.226  -62.775 1.00 87.80  ? 123 PHE A O   1 
ATOM   901   C CB  . PHE A  1 123 ? 7.944   -53.600  -64.441 1.00 76.54  ? 123 PHE A CB  1 
ATOM   902   C CG  . PHE A  1 123 ? 6.642   -53.968  -65.091 1.00 74.53  ? 123 PHE A CG  1 
ATOM   903   C CD1 . PHE A  1 123 ? 5.457   -53.383  -64.679 1.00 68.37  ? 123 PHE A CD1 1 
ATOM   904   C CD2 . PHE A  1 123 ? 6.603   -54.903  -66.112 1.00 73.68  ? 123 PHE A CD2 1 
ATOM   905   C CE1 . PHE A  1 123 ? 4.258   -53.719  -65.276 1.00 69.13  ? 123 PHE A CE1 1 
ATOM   906   C CE2 . PHE A  1 123 ? 5.406   -55.245  -66.712 1.00 73.69  ? 123 PHE A CE2 1 
ATOM   907   C CZ  . PHE A  1 123 ? 4.232   -54.652  -66.293 1.00 74.86  ? 123 PHE A CZ  1 
ATOM   908   N N   . PRO A  1 124 ? 11.054  -55.197  -63.435 1.00 100.20 ? 124 PRO A N   1 
ATOM   909   C CA  . PRO A  1 124 ? 12.420  -54.861  -63.022 1.00 96.12  ? 124 PRO A CA  1 
ATOM   910   C C   . PRO A  1 124 ? 12.875  -53.557  -63.661 1.00 98.12  ? 124 PRO A C   1 
ATOM   911   O O   . PRO A  1 124 ? 12.743  -53.397  -64.872 1.00 98.57  ? 124 PRO A O   1 
ATOM   912   C CB  . PRO A  1 124 ? 13.240  -56.032  -63.561 1.00 109.67 ? 124 PRO A CB  1 
ATOM   913   C CG  . PRO A  1 124 ? 12.279  -57.164  -63.593 1.00 107.83 ? 124 PRO A CG  1 
ATOM   914   C CD  . PRO A  1 124 ? 10.963  -56.562  -63.981 1.00 100.73 ? 124 PRO A CD  1 
ATOM   915   N N   . LYS A  1 125 ? 13.402  -52.642  -62.857 1.00 96.64  ? 125 LYS A N   1 
ATOM   916   C CA  . LYS A  1 125 ? 13.750  -51.311  -63.339 1.00 99.12  ? 125 LYS A CA  1 
ATOM   917   C C   . LYS A  1 125 ? 14.620  -51.320  -64.581 1.00 123.16 ? 125 LYS A C   1 
ATOM   918   O O   . LYS A  1 125 ? 14.458  -50.481  -65.471 1.00 120.63 ? 125 LYS A O   1 
ATOM   919   C CB  . LYS A  1 125 ? 14.453  -50.510  -62.245 1.00 98.41  ? 125 LYS A CB  1 
ATOM   920   C CG  . LYS A  1 125 ? 14.782  -49.086  -62.654 1.00 95.40  ? 125 LYS A CG  1 
ATOM   921   C CD  . LYS A  1 125 ? 15.014  -48.179  -61.454 1.00 92.34  ? 125 LYS A CD  1 
ATOM   922   C CE  . LYS A  1 125 ? 16.270  -48.554  -60.685 1.00 102.01 ? 125 LYS A CE  1 
ATOM   923   N NZ  . LYS A  1 125 ? 16.536  -47.611  -59.557 1.00 92.20  ? 125 LYS A NZ  1 
ATOM   924   N N   . THR A  1 126 ? 15.527  -52.283  -64.652 1.00 270.75 ? 126 THR A N   1 
ATOM   925   C CA  . THR A  1 126 ? 16.621  -52.197  -65.606 1.00 264.17 ? 126 THR A CA  1 
ATOM   926   C C   . THR A  1 126 ? 16.458  -52.871  -66.959 1.00 265.30 ? 126 THR A C   1 
ATOM   927   O O   . THR A  1 126 ? 17.198  -52.552  -67.881 1.00 264.45 ? 126 THR A O   1 
ATOM   928   C CB  . THR A  1 126 ? 17.925  -52.660  -64.945 1.00 140.81 ? 126 THR A CB  1 
ATOM   929   O OG1 . THR A  1 126 ? 17.690  -53.870  -64.205 1.00 141.09 ? 126 THR A OG1 1 
ATOM   930   C CG2 . THR A  1 126 ? 18.376  -51.580  -63.996 1.00 139.95 ? 126 THR A CG2 1 
ATOM   931   N N   . SER A  1 127 ? 15.498  -53.776  -67.087 1.00 120.49 ? 127 SER A N   1 
ATOM   932   C CA  . SER A  1 127 ? 15.337  -54.507  -68.327 1.00 112.09 ? 127 SER A CA  1 
ATOM   933   C C   . SER A  1 127 ? 14.010  -54.188  -69.036 1.00 110.82 ? 127 SER A C   1 
ATOM   934   O O   . SER A  1 127 ? 13.846  -54.446  -70.233 1.00 116.98 ? 127 SER A O   1 
ATOM   935   C CB  . SER A  1 127 ? 15.493  -56.002  -68.060 1.00 121.02 ? 127 SER A CB  1 
ATOM   936   O OG  . SER A  1 127 ? 14.568  -56.435  -67.073 1.00 112.85 ? 127 SER A OG  1 
ATOM   937   N N   . SER A  1 128 ? 13.098  -53.557  -68.303 1.00 113.62 ? 128 SER A N   1 
ATOM   938   C CA  . SER A  1 128 ? 11.733  -53.347  -68.769 1.00 100.85 ? 128 SER A CA  1 
ATOM   939   C C   . SER A  1 128 ? 11.510  -51.987  -69.424 1.00 94.40  ? 128 SER A C   1 
ATOM   940   O O   . SER A  1 128 ? 10.698  -51.859  -70.345 1.00 84.92  ? 128 SER A O   1 
ATOM   941   C CB  . SER A  1 128 ? 10.755  -53.542  -67.608 1.00 91.52  ? 128 SER A CB  1 
ATOM   942   O OG  . SER A  1 128 ? 10.786  -54.882  -67.146 1.00 84.01  ? 128 SER A OG  1 
ATOM   943   N N   . TRP A  1 129 ? 12.219  -50.972  -68.942 1.00 96.97  ? 129 TRP A N   1 
ATOM   944   C CA  . TRP A  1 129 ? 12.114  -49.640  -69.524 1.00 100.21 ? 129 TRP A CA  1 
ATOM   945   C C   . TRP A  1 129 ? 13.432  -49.219  -70.171 1.00 100.36 ? 129 TRP A C   1 
ATOM   946   O O   . TRP A  1 129 ? 14.191  -48.439  -69.596 1.00 90.71  ? 129 TRP A O   1 
ATOM   947   C CB  . TRP A  1 129 ? 11.675  -48.612  -68.475 1.00 102.93 ? 129 TRP A CB  1 
ATOM   948   C CG  . TRP A  1 129 ? 10.576  -49.100  -67.581 1.00 91.22  ? 129 TRP A CG  1 
ATOM   949   C CD1 . TRP A  1 129 ? 10.604  -49.185  -66.220 1.00 87.83  ? 129 TRP A CD1 1 
ATOM   950   C CD2 . TRP A  1 129 ? 9.292   -49.587  -67.987 1.00 79.09  ? 129 TRP A CD2 1 
ATOM   951   N NE1 . TRP A  1 129 ? 9.415   -49.688  -65.752 1.00 85.36  ? 129 TRP A NE1 1 
ATOM   952   C CE2 . TRP A  1 129 ? 8.592   -49.944  -66.817 1.00 79.68  ? 129 TRP A CE2 1 
ATOM   953   C CE3 . TRP A  1 129 ? 8.664   -49.753  -69.225 1.00 76.44  ? 129 TRP A CE3 1 
ATOM   954   C CZ2 . TRP A  1 129 ? 7.299   -50.457  -66.848 1.00 83.56  ? 129 TRP A CZ2 1 
ATOM   955   C CZ3 . TRP A  1 129 ? 7.381   -50.261  -69.254 1.00 79.04  ? 129 TRP A CZ3 1 
ATOM   956   C CH2 . TRP A  1 129 ? 6.712   -50.608  -68.074 1.00 86.04  ? 129 TRP A CH2 1 
ATOM   957   N N   . PRO A  1 130 ? 13.700  -49.734  -71.380 1.00 110.90 ? 130 PRO A N   1 
ATOM   958   C CA  . PRO A  1 130 ? 14.946  -49.464  -72.105 1.00 104.65 ? 130 PRO A CA  1 
ATOM   959   C C   . PRO A  1 130 ? 14.901  -48.191  -72.944 1.00 109.67 ? 130 PRO A C   1 
ATOM   960   O O   . PRO A  1 130 ? 15.956  -47.660  -73.290 1.00 117.22 ? 130 PRO A O   1 
ATOM   961   C CB  . PRO A  1 130 ? 15.081  -50.677  -73.024 1.00 109.21 ? 130 PRO A CB  1 
ATOM   962   C CG  . PRO A  1 130 ? 13.683  -51.143  -73.254 1.00 106.31 ? 130 PRO A CG  1 
ATOM   963   C CD  . PRO A  1 130 ? 12.830  -50.680  -72.101 1.00 115.03 ? 130 PRO A CD  1 
ATOM   964   N N   . ASN A  1 131 ? 13.703  -47.720  -73.274 1.00 120.44 ? 131 ASN A N   1 
ATOM   965   C CA  . ASN A  1 131 ? 13.551  -46.542  -74.122 1.00 125.12 ? 131 ASN A CA  1 
ATOM   966   C C   . ASN A  1 131 ? 13.150  -45.310  -73.319 1.00 106.64 ? 131 ASN A C   1 
ATOM   967   O O   . ASN A  1 131 ? 12.623  -44.343  -73.870 1.00 96.84  ? 131 ASN A O   1 
ATOM   968   C CB  . ASN A  1 131 ? 12.519  -46.798  -75.227 1.00 124.07 ? 131 ASN A CB  1 
ATOM   969   C CG  . ASN A  1 131 ? 12.685  -48.157  -75.877 1.00 132.66 ? 131 ASN A CG  1 
ATOM   970   O OD1 . ASN A  1 131 ? 13.325  -49.048  -75.324 1.00 133.28 ? 131 ASN A OD1 1 
ATOM   971   N ND2 . ASN A  1 131 ? 12.100  -48.325  -77.056 1.00 134.72 ? 131 ASN A ND2 1 
ATOM   972   N N   . HIS A  1 132 ? 13.398  -45.356  -72.013 1.00 86.27  ? 132 HIS A N   1 
ATOM   973   C CA  . HIS A  1 132 ? 12.998  -44.285  -71.109 1.00 74.33  ? 132 HIS A CA  1 
ATOM   974   C C   . HIS A  1 132 ? 13.943  -44.232  -69.916 1.00 79.46  ? 132 HIS A C   1 
ATOM   975   O O   . HIS A  1 132 ? 14.562  -45.237  -69.563 1.00 92.44  ? 132 HIS A O   1 
ATOM   976   C CB  . HIS A  1 132 ? 11.569  -44.517  -70.620 1.00 78.43  ? 132 HIS A CB  1 
ATOM   977   C CG  . HIS A  1 132 ? 10.595  -44.802  -71.719 1.00 81.80  ? 132 HIS A CG  1 
ATOM   978   N ND1 . HIS A  1 132 ? 9.760   -43.839  -72.242 1.00 83.13  ? 132 HIS A ND1 1 
ATOM   979   C CD2 . HIS A  1 132 ? 10.332  -45.941  -72.403 1.00 74.40  ? 132 HIS A CD2 1 
ATOM   980   C CE1 . HIS A  1 132 ? 9.021   -44.374  -73.198 1.00 78.99  ? 132 HIS A CE1 1 
ATOM   981   N NE2 . HIS A  1 132 ? 9.348   -45.647  -73.316 1.00 66.86  ? 132 HIS A NE2 1 
ATOM   982   N N   . ASP A  1 133 ? 14.050  -43.062  -69.295 1.00 71.87  ? 133 ASP A N   1 
ATOM   983   C CA  . ASP A  1 133 ? 14.909  -42.904  -68.128 1.00 81.54  ? 133 ASP A CA  1 
ATOM   984   C C   . ASP A  1 133 ? 14.184  -43.335  -66.857 1.00 82.81  ? 133 ASP A C   1 
ATOM   985   O O   . ASP A  1 133 ? 13.150  -42.773  -66.501 1.00 74.68  ? 133 ASP A O   1 
ATOM   986   C CB  . ASP A  1 133 ? 15.411  -41.464  -68.008 1.00 82.96  ? 133 ASP A CB  1 
ATOM   987   C CG  . ASP A  1 133 ? 16.570  -41.328  -67.038 1.00 105.09 ? 133 ASP A CG  1 
ATOM   988   O OD1 . ASP A  1 133 ? 16.502  -41.912  -65.936 1.00 100.40 ? 133 ASP A OD1 1 
ATOM   989   O OD2 . ASP A  1 133 ? 17.551  -40.633  -67.378 1.00 113.50 ? 133 ASP A OD2 1 
ATOM   990   N N   . SER A  1 134 ? 14.732  -44.340  -66.182 1.00 82.61  ? 134 SER A N   1 
ATOM   991   C CA  . SER A  1 134 ? 14.126  -44.863  -64.964 1.00 78.12  ? 134 SER A CA  1 
ATOM   992   C C   . SER A  1 134 ? 14.938  -44.484  -63.729 1.00 80.37  ? 134 SER A C   1 
ATOM   993   O O   . SER A  1 134 ? 14.936  -45.202  -62.729 1.00 91.63  ? 134 SER A O   1 
ATOM   994   C CB  . SER A  1 134 ? 13.977  -46.384  -65.056 1.00 82.84  ? 134 SER A CB  1 
ATOM   995   O OG  . SER A  1 134 ? 15.208  -46.999  -65.399 1.00 97.94  ? 134 SER A OG  1 
ATOM   996   N N   . ASN A  1 135 ? 15.625  -43.348  -63.803 1.00 82.89  ? 135 ASN A N   1 
ATOM   997   C CA  . ASN A  1 135 ? 16.501  -42.912  -62.721 1.00 95.03  ? 135 ASN A CA  1 
ATOM   998   C C   . ASN A  1 135 ? 16.253  -41.472  -62.274 1.00 94.98  ? 135 ASN A C   1 
ATOM   999   O O   . ASN A  1 135 ? 16.509  -41.121  -61.123 1.00 105.37 ? 135 ASN A O   1 
ATOM   1000  C CB  . ASN A  1 135 ? 17.967  -43.090  -63.125 1.00 105.37 ? 135 ASN A CB  1 
ATOM   1001  C CG  . ASN A  1 135 ? 18.344  -44.545  -63.331 1.00 101.15 ? 135 ASN A CG  1 
ATOM   1002  O OD1 . ASN A  1 135 ? 18.011  -45.405  -62.516 1.00 85.01  ? 135 ASN A OD1 1 
ATOM   1003  N ND2 . ASN A  1 135 ? 19.047  -44.827  -64.422 1.00 89.87  ? 135 ASN A ND2 1 
ATOM   1004  N N   . LYS A  1 136 ? 15.752  -40.645  -63.187 1.00 86.88  ? 136 LYS A N   1 
ATOM   1005  C CA  . LYS A  1 136 ? 15.550  -39.224  -62.911 1.00 100.70 ? 136 LYS A CA  1 
ATOM   1006  C C   . LYS A  1 136 ? 14.214  -38.945  -62.234 1.00 100.05 ? 136 LYS A C   1 
ATOM   1007  O O   . LYS A  1 136 ? 13.850  -37.789  -62.018 1.00 97.65  ? 136 LYS A O   1 
ATOM   1008  C CB  . LYS A  1 136 ? 15.643  -38.413  -64.204 1.00 110.92 ? 136 LYS A CB  1 
ATOM   1009  C CG  . LYS A  1 136 ? 16.948  -38.600  -64.944 1.00 116.35 ? 136 LYS A CG  1 
ATOM   1010  C CD  . LYS A  1 136 ? 17.603  -37.272  -65.262 1.00 120.18 ? 136 LYS A CD  1 
ATOM   1011  C CE  . LYS A  1 136 ? 19.096  -37.458  -65.443 1.00 143.20 ? 136 LYS A CE  1 
ATOM   1012  N NZ  . LYS A  1 136 ? 19.704  -38.104  -64.244 1.00 144.87 ? 136 LYS A NZ  1 
ATOM   1013  N N   . GLY A  1 137 ? 13.492  -40.007  -61.898 1.00 86.70  ? 137 GLY A N   1 
ATOM   1014  C CA  . GLY A  1 137 ? 12.154  -39.877  -61.351 1.00 79.99  ? 137 GLY A CA  1 
ATOM   1015  C C   . GLY A  1 137 ? 12.112  -39.678  -59.850 1.00 77.82  ? 137 GLY A C   1 
ATOM   1016  O O   . GLY A  1 137 ? 11.621  -40.536  -59.116 1.00 82.56  ? 137 GLY A O   1 
ATOM   1017  N N   . VAL A  1 138 ? 12.621  -38.541  -59.390 1.00 63.78  ? 138 VAL A N   1 
ATOM   1018  C CA  . VAL A  1 138 ? 12.601  -38.216  -57.969 1.00 72.47  ? 138 VAL A CA  1 
ATOM   1019  C C   . VAL A  1 138 ? 12.012  -36.828  -57.749 1.00 72.63  ? 138 VAL A C   1 
ATOM   1020  O O   . VAL A  1 138 ? 11.784  -36.084  -58.702 1.00 76.39  ? 138 VAL A O   1 
ATOM   1021  C CB  . VAL A  1 138 ? 14.008  -38.280  -57.353 1.00 80.02  ? 138 VAL A CB  1 
ATOM   1022  C CG1 . VAL A  1 138 ? 14.625  -39.650  -57.591 1.00 86.52  ? 138 VAL A CG1 1 
ATOM   1023  C CG2 . VAL A  1 138 ? 14.890  -37.185  -57.931 1.00 82.77  ? 138 VAL A CG2 1 
ATOM   1024  N N   . THR A  1 139 ? 11.770  -36.484  -56.489 1.00 62.78  ? 139 THR A N   1 
ATOM   1025  C CA  . THR A  1 139 ? 11.141  -35.213  -56.157 1.00 72.11  ? 139 THR A CA  1 
ATOM   1026  C C   . THR A  1 139 ? 11.417  -34.810  -54.715 1.00 78.67  ? 139 THR A C   1 
ATOM   1027  O O   . THR A  1 139 ? 11.678  -35.657  -53.861 1.00 74.52  ? 139 THR A O   1 
ATOM   1028  C CB  . THR A  1 139 ? 9.618   -35.270  -56.378 1.00 80.76  ? 139 THR A CB  1 
ATOM   1029  O OG1 . THR A  1 139 ? 9.013   -34.075  -55.869 1.00 67.68  ? 139 THR A OG1 1 
ATOM   1030  C CG2 . THR A  1 139 ? 9.022   -36.477  -55.665 1.00 82.64  ? 139 THR A CG2 1 
ATOM   1031  N N   . ALA A  1 140 ? 11.357  -33.509  -54.451 1.00 91.11  ? 140 ALA A N   1 
ATOM   1032  C CA  . ALA A  1 140 ? 11.557  -32.989  -53.106 1.00 89.33  ? 140 ALA A CA  1 
ATOM   1033  C C   . ALA A  1 140 ? 10.365  -33.331  -52.218 1.00 90.19  ? 140 ALA A C   1 
ATOM   1034  O O   . ALA A  1 140 ? 10.430  -33.196  -50.997 1.00 87.06  ? 140 ALA A O   1 
ATOM   1035  C CB  . ALA A  1 140 ? 11.774  -31.485  -53.148 1.00 95.37  ? 140 ALA A CB  1 
ATOM   1036  N N   . ALA A  1 141 ? 9.280   -33.776  -52.843 1.00 89.05  ? 141 ALA A N   1 
ATOM   1037  C CA  . ALA A  1 141 ? 8.064   -34.127  -52.120 1.00 85.29  ? 141 ALA A CA  1 
ATOM   1038  C C   . ALA A  1 141 ? 8.224   -35.430  -51.341 1.00 85.39  ? 141 ALA A C   1 
ATOM   1039  O O   . ALA A  1 141 ? 7.653   -35.589  -50.264 1.00 87.27  ? 141 ALA A O   1 
ATOM   1040  C CB  . ALA A  1 141 ? 6.886   -34.221  -53.080 1.00 82.52  ? 141 ALA A CB  1 
ATOM   1041  N N   . CYS A  1 142 ? 9.001   -36.361  -51.890 1.00 72.27  ? 142 CYS A N   1 
ATOM   1042  C CA  . CYS A  1 142 ? 9.232   -37.654  -51.244 1.00 79.89  ? 142 CYS A CA  1 
ATOM   1043  C C   . CYS A  1 142 ? 10.690  -37.810  -50.805 1.00 81.24  ? 142 CYS A C   1 
ATOM   1044  O O   . CYS A  1 142 ? 11.433  -38.610  -51.374 1.00 73.85  ? 142 CYS A O   1 
ATOM   1045  C CB  . CYS A  1 142 ? 8.834   -38.802  -52.179 1.00 89.02  ? 142 CYS A CB  1 
ATOM   1046  S SG  . CYS A  1 142 ? 7.125   -38.742  -52.778 1.00 103.39 ? 142 CYS A SG  1 
ATOM   1047  N N   . PRO A  1 143 ? 11.095  -37.049  -49.775 1.00 84.40  ? 143 PRO A N   1 
ATOM   1048  C CA  . PRO A  1 143 ? 12.487  -36.939  -49.321 1.00 88.28  ? 143 PRO A CA  1 
ATOM   1049  C C   . PRO A  1 143 ? 13.008  -38.155  -48.561 1.00 98.32  ? 143 PRO A C   1 
ATOM   1050  O O   . PRO A  1 143 ? 12.361  -38.620  -47.627 1.00 104.68 ? 143 PRO A O   1 
ATOM   1051  C CB  . PRO A  1 143 ? 12.458  -35.721  -48.386 1.00 95.53  ? 143 PRO A CB  1 
ATOM   1052  C CG  . PRO A  1 143 ? 11.132  -35.058  -48.621 1.00 94.53  ? 143 PRO A CG  1 
ATOM   1053  C CD  . PRO A  1 143 ? 10.211  -36.157  -49.012 1.00 92.23  ? 143 PRO A CD  1 
ATOM   1054  N N   . HIS A  1 144 ? 14.175  -38.654  -48.953 1.00 106.35 ? 144 HIS A N   1 
ATOM   1055  C CA  . HIS A  1 144 ? 14.867  -39.661  -48.157 1.00 121.53 ? 144 HIS A CA  1 
ATOM   1056  C C   . HIS A  1 144 ? 16.156  -39.062  -47.604 1.00 131.49 ? 144 HIS A C   1 
ATOM   1057  O O   . HIS A  1 144 ? 17.173  -38.997  -48.298 1.00 127.80 ? 144 HIS A O   1 
ATOM   1058  C CB  . HIS A  1 144 ? 15.154  -40.921  -48.976 1.00 113.92 ? 144 HIS A CB  1 
ATOM   1059  C CG  . HIS A  1 144 ? 15.278  -42.162  -48.148 1.00 120.74 ? 144 HIS A CG  1 
ATOM   1060  N ND1 . HIS A  1 144 ? 16.233  -43.129  -48.387 1.00 125.04 ? 144 HIS A ND1 1 
ATOM   1061  C CD2 . HIS A  1 144 ? 14.571  -42.592  -47.075 1.00 122.45 ? 144 HIS A CD2 1 
ATOM   1062  C CE1 . HIS A  1 144 ? 16.104  -44.101  -47.502 1.00 127.75 ? 144 HIS A CE1 1 
ATOM   1063  N NE2 . HIS A  1 144 ? 15.104  -43.800  -46.695 1.00 125.42 ? 144 HIS A NE2 1 
ATOM   1064  N N   . ALA A  1 145 ? 16.096  -38.612  -46.354 1.00 112.90 ? 145 ALA A N   1 
ATOM   1065  C CA  . ALA A  1 145 ? 17.224  -37.945  -45.714 1.00 118.65 ? 145 ALA A CA  1 
ATOM   1066  C C   . ALA A  1 145 ? 17.765  -36.814  -46.584 1.00 123.68 ? 145 ALA A C   1 
ATOM   1067  O O   . ALA A  1 145 ? 18.862  -36.914  -47.132 1.00 116.04 ? 145 ALA A O   1 
ATOM   1068  C CB  . ALA A  1 145 ? 18.323  -38.944  -45.390 1.00 104.90 ? 145 ALA A CB  1 
ATOM   1069  N N   . GLY A  1 146 ? 16.986  -35.745  -46.710 1.00 135.29 ? 146 GLY A N   1 
ATOM   1070  C CA  . GLY A  1 146 ? 17.395  -34.586  -47.483 1.00 133.90 ? 146 GLY A CA  1 
ATOM   1071  C C   . GLY A  1 146 ? 17.292  -34.781  -48.985 1.00 132.25 ? 146 GLY A C   1 
ATOM   1072  O O   . GLY A  1 146 ? 16.725  -33.946  -49.689 1.00 132.27 ? 146 GLY A O   1 
ATOM   1073  N N   . ALA A  1 147 ? 17.844  -35.885  -49.478 1.00 120.90 ? 147 ALA A N   1 
ATOM   1074  C CA  . ALA A  1 147 ? 17.872  -36.163  -50.911 1.00 120.76 ? 147 ALA A CA  1 
ATOM   1075  C C   . ALA A  1 147 ? 16.473  -36.346  -51.491 1.00 115.39 ? 147 ALA A C   1 
ATOM   1076  O O   . ALA A  1 147 ? 15.567  -36.801  -50.797 1.00 110.16 ? 147 ALA A O   1 
ATOM   1077  C CB  . ALA A  1 147 ? 18.723  -37.392  -51.192 1.00 120.25 ? 147 ALA A CB  1 
ATOM   1078  N N   . LYS A  1 148 ? 16.314  -35.988  -52.765 1.00 97.34  ? 148 LYS A N   1 
ATOM   1079  C CA  . LYS A  1 148 ? 15.053  -36.167  -53.484 1.00 96.41  ? 148 LYS A CA  1 
ATOM   1080  C C   . LYS A  1 148 ? 14.880  -37.615  -53.942 1.00 100.17 ? 148 LYS A C   1 
ATOM   1081  O O   . LYS A  1 148 ? 15.684  -38.132  -54.718 1.00 90.16  ? 148 LYS A O   1 
ATOM   1082  C CB  . LYS A  1 148 ? 14.971  -35.229  -54.691 1.00 87.89  ? 148 LYS A CB  1 
ATOM   1083  C CG  . LYS A  1 148 ? 15.072  -33.749  -54.362 1.00 98.95  ? 148 LYS A CG  1 
ATOM   1084  C CD  . LYS A  1 148 ? 14.916  -32.909  -55.622 1.00 105.95 ? 148 LYS A CD  1 
ATOM   1085  C CE  . LYS A  1 148 ? 15.916  -33.332  -56.689 1.00 103.34 ? 148 LYS A CE  1 
ATOM   1086  N NZ  . LYS A  1 148 ? 15.726  -32.590  -57.967 1.00 102.42 ? 148 LYS A NZ  1 
ATOM   1087  N N   . SER A  1 149 ? 13.816  -38.252  -53.466 1.00 104.10 ? 149 SER A N   1 
ATOM   1088  C CA  . SER A  1 149 ? 13.571  -39.667  -53.701 1.00 94.02  ? 149 SER A CA  1 
ATOM   1089  C C   . SER A  1 149 ? 12.162  -39.859  -54.245 1.00 88.02  ? 149 SER A C   1 
ATOM   1090  O O   . SER A  1 149 ? 11.562  -38.926  -54.779 1.00 74.20  ? 149 SER A O   1 
ATOM   1091  C CB  . SER A  1 149 ? 13.746  -40.453  -52.398 1.00 92.95  ? 149 SER A CB  1 
ATOM   1092  O OG  . SER A  1 149 ? 13.765  -41.851  -52.630 1.00 103.10 ? 149 SER A OG  1 
ATOM   1093  N N   . PHE A  1 150 ? 11.634  -41.069  -54.097 1.00 91.29  ? 150 PHE A N   1 
ATOM   1094  C CA  . PHE A  1 150 ? 10.322  -41.399  -54.631 1.00 79.88  ? 150 PHE A CA  1 
ATOM   1095  C C   . PHE A  1 150 ? 9.813   -42.689  -53.999 1.00 72.86  ? 150 PHE A C   1 
ATOM   1096  O O   . PHE A  1 150 ? 10.514  -43.314  -53.204 1.00 76.61  ? 150 PHE A O   1 
ATOM   1097  C CB  . PHE A  1 150 ? 10.407  -41.547  -56.151 1.00 69.43  ? 150 PHE A CB  1 
ATOM   1098  C CG  . PHE A  1 150 ? 9.074   -41.560  -56.838 1.00 63.74  ? 150 PHE A CG  1 
ATOM   1099  C CD1 . PHE A  1 150 ? 8.251   -40.447  -56.800 1.00 59.05  ? 150 PHE A CD1 1 
ATOM   1100  C CD2 . PHE A  1 150 ? 8.650   -42.678  -57.536 1.00 60.93  ? 150 PHE A CD2 1 
ATOM   1101  C CE1 . PHE A  1 150 ? 7.026   -40.453  -57.436 1.00 51.20  ? 150 PHE A CE1 1 
ATOM   1102  C CE2 . PHE A  1 150 ? 7.426   -42.689  -58.175 1.00 61.64  ? 150 PHE A CE2 1 
ATOM   1103  C CZ  . PHE A  1 150 ? 6.613   -41.575  -58.125 1.00 54.40  ? 150 PHE A CZ  1 
ATOM   1104  N N   . TYR A  1 151 ? 8.592   -43.081  -54.347 1.00 75.49  ? 151 TYR A N   1 
ATOM   1105  C CA  . TYR A  1 151 ? 8.035   -44.336  -53.862 1.00 68.28  ? 151 TYR A CA  1 
ATOM   1106  C C   . TYR A  1 151 ? 8.898   -45.497  -54.346 1.00 64.37  ? 151 TYR A C   1 
ATOM   1107  O O   . TYR A  1 151 ? 9.365   -45.498  -55.484 1.00 56.67  ? 151 TYR A O   1 
ATOM   1108  C CB  . TYR A  1 151 ? 6.596   -44.511  -54.348 1.00 68.11  ? 151 TYR A CB  1 
ATOM   1109  C CG  . TYR A  1 151 ? 5.684   -43.353  -54.010 1.00 52.65  ? 151 TYR A CG  1 
ATOM   1110  C CD1 . TYR A  1 151 ? 5.146   -43.216  -52.737 1.00 55.74  ? 151 TYR A CD1 1 
ATOM   1111  C CD2 . TYR A  1 151 ? 5.354   -42.402  -54.966 1.00 50.68  ? 151 TYR A CD2 1 
ATOM   1112  C CE1 . TYR A  1 151 ? 4.310   -42.160  -52.424 1.00 54.22  ? 151 TYR A CE1 1 
ATOM   1113  C CE2 . TYR A  1 151 ? 4.519   -41.343  -54.663 1.00 49.65  ? 151 TYR A CE2 1 
ATOM   1114  C CZ  . TYR A  1 151 ? 3.999   -41.227  -53.391 1.00 55.86  ? 151 TYR A CZ  1 
ATOM   1115  O OH  . TYR A  1 151 ? 3.167   -40.174  -53.084 1.00 50.39  ? 151 TYR A OH  1 
ATOM   1116  N N   . LYS A  1 152 ? 9.109   -46.480  -53.478 1.00 70.37  ? 152 LYS A N   1 
ATOM   1117  C CA  . LYS A  1 152 ? 9.943   -47.628  -53.814 1.00 74.05  ? 152 LYS A CA  1 
ATOM   1118  C C   . LYS A  1 152 ? 9.249   -48.557  -54.805 1.00 66.27  ? 152 LYS A C   1 
ATOM   1119  O O   . LYS A  1 152 ? 9.879   -49.087  -55.721 1.00 72.93  ? 152 LYS A O   1 
ATOM   1120  C CB  . LYS A  1 152 ? 10.317  -48.407  -52.550 1.00 67.60  ? 152 LYS A CB  1 
ATOM   1121  C CG  . LYS A  1 152 ? 11.098  -47.600  -51.525 1.00 97.55  ? 152 LYS A CG  1 
ATOM   1122  C CD  . LYS A  1 152 ? 12.420  -47.114  -52.094 1.00 118.82 ? 152 LYS A CD  1 
ATOM   1123  C CE  . LYS A  1 152 ? 13.210  -46.333  -51.057 1.00 128.88 ? 152 LYS A CE  1 
ATOM   1124  N NZ  . LYS A  1 152 ? 14.495  -45.821  -51.608 1.00 130.88 ? 152 LYS A NZ  1 
ATOM   1125  N N   . ASN A  1 153 ? 7.947   -48.744  -54.617 1.00 63.96  ? 153 ASN A N   1 
ATOM   1126  C CA  . ASN A  1 153 ? 7.185   -49.701  -55.412 1.00 63.81  ? 153 ASN A CA  1 
ATOM   1127  C C   . ASN A  1 153 ? 6.721   -49.153  -56.759 1.00 59.08  ? 153 ASN A C   1 
ATOM   1128  O O   . ASN A  1 153 ? 6.053   -49.849  -57.523 1.00 59.12  ? 153 ASN A O   1 
ATOM   1129  C CB  . ASN A  1 153 ? 5.994   -50.224  -54.607 1.00 53.82  ? 153 ASN A CB  1 
ATOM   1130  C CG  . ASN A  1 153 ? 6.419   -50.922  -53.330 1.00 59.78  ? 153 ASN A CG  1 
ATOM   1131  O OD1 . ASN A  1 153 ? 7.547   -51.400  -53.219 1.00 72.15  ? 153 ASN A OD1 1 
ATOM   1132  N ND2 . ASN A  1 153 ? 5.517   -50.984  -52.359 1.00 70.02  ? 153 ASN A ND2 1 
ATOM   1133  N N   . LEU A  1 154 ? 7.079   -47.906  -57.047 1.00 68.01  ? 154 LEU A N   1 
ATOM   1134  C CA  . LEU A  1 154 ? 6.734   -47.285  -58.321 1.00 69.10  ? 154 LEU A CA  1 
ATOM   1135  C C   . LEU A  1 154 ? 7.947   -46.592  -58.935 1.00 68.04  ? 154 LEU A C   1 
ATOM   1136  O O   . LEU A  1 154 ? 8.857   -46.168  -58.222 1.00 76.17  ? 154 LEU A O   1 
ATOM   1137  C CB  . LEU A  1 154 ? 5.595   -46.279  -58.140 1.00 66.46  ? 154 LEU A CB  1 
ATOM   1138  C CG  . LEU A  1 154 ? 4.260   -46.820  -57.621 1.00 57.91  ? 154 LEU A CG  1 
ATOM   1139  C CD1 . LEU A  1 154 ? 3.308   -45.678  -57.301 1.00 52.76  ? 154 LEU A CD1 1 
ATOM   1140  C CD2 . LEU A  1 154 ? 3.637   -47.779  -58.623 1.00 59.89  ? 154 LEU A CD2 1 
ATOM   1141  N N   . ILE A  1 155 ? 7.957   -46.483  -60.260 1.00 64.96  ? 155 ILE A N   1 
ATOM   1142  C CA  . ILE A  1 155 ? 9.035   -45.796  -60.964 1.00 78.11  ? 155 ILE A CA  1 
ATOM   1143  C C   . ILE A  1 155 ? 8.493   -44.660  -61.821 1.00 64.55  ? 155 ILE A C   1 
ATOM   1144  O O   . ILE A  1 155 ? 7.657   -44.878  -62.697 1.00 62.56  ? 155 ILE A O   1 
ATOM   1145  C CB  . ILE A  1 155 ? 9.838   -46.756  -61.861 1.00 79.74  ? 155 ILE A CB  1 
ATOM   1146  C CG1 . ILE A  1 155 ? 10.497  -47.849  -61.018 1.00 79.73  ? 155 ILE A CG1 1 
ATOM   1147  C CG2 . ILE A  1 155 ? 10.889  -45.988  -62.650 1.00 65.43  ? 155 ILE A CG2 1 
ATOM   1148  C CD1 . ILE A  1 155 ? 11.295  -48.843  -61.828 1.00 95.22  ? 155 ILE A CD1 1 
ATOM   1149  N N   . TRP A  1 156 ? 8.972   -43.447  -61.564 1.00 64.62  ? 156 TRP A N   1 
ATOM   1150  C CA  . TRP A  1 156 ? 8.522   -42.281  -62.313 1.00 67.02  ? 156 TRP A CA  1 
ATOM   1151  C C   . TRP A  1 156 ? 9.307   -42.145  -63.612 1.00 66.23  ? 156 TRP A C   1 
ATOM   1152  O O   . TRP A  1 156 ? 10.399  -41.575  -63.641 1.00 77.77  ? 156 TRP A O   1 
ATOM   1153  C CB  . TRP A  1 156 ? 8.641   -41.010  -61.471 1.00 64.62  ? 156 TRP A CB  1 
ATOM   1154  C CG  . TRP A  1 156 ? 7.980   -39.816  -62.092 1.00 66.92  ? 156 TRP A CG  1 
ATOM   1155  C CD1 . TRP A  1 156 ? 7.403   -39.746  -63.328 1.00 63.26  ? 156 TRP A CD1 1 
ATOM   1156  C CD2 . TRP A  1 156 ? 7.831   -38.518  -61.506 1.00 62.77  ? 156 TRP A CD2 1 
ATOM   1157  N NE1 . TRP A  1 156 ? 6.904   -38.486  -63.547 1.00 53.23  ? 156 TRP A NE1 1 
ATOM   1158  C CE2 . TRP A  1 156 ? 7.153   -37.712  -62.444 1.00 57.06  ? 156 TRP A CE2 1 
ATOM   1159  C CE3 . TRP A  1 156 ? 8.204   -37.959  -60.280 1.00 63.61  ? 156 TRP A CE3 1 
ATOM   1160  C CZ2 . TRP A  1 156 ? 6.842   -36.378  -62.193 1.00 71.80  ? 156 TRP A CZ2 1 
ATOM   1161  C CZ3 . TRP A  1 156 ? 7.894   -36.635  -60.033 1.00 68.76  ? 156 TRP A CZ3 1 
ATOM   1162  C CH2 . TRP A  1 156 ? 7.220   -35.859  -60.985 1.00 75.83  ? 156 TRP A CH2 1 
ATOM   1163  N N   . LEU A  1 157 ? 8.726   -42.671  -64.684 1.00 54.85  ? 157 LEU A N   1 
ATOM   1164  C CA  . LEU A  1 157 ? 9.379   -42.728  -65.985 1.00 60.13  ? 157 LEU A CA  1 
ATOM   1165  C C   . LEU A  1 157 ? 9.396   -41.373  -66.685 1.00 67.57  ? 157 LEU A C   1 
ATOM   1166  O O   . LEU A  1 157 ? 8.347   -40.837  -67.044 1.00 72.28  ? 157 LEU A O   1 
ATOM   1167  C CB  . LEU A  1 157 ? 8.661   -43.749  -66.869 1.00 56.04  ? 157 LEU A CB  1 
ATOM   1168  C CG  . LEU A  1 157 ? 9.461   -44.904  -67.470 1.00 64.05  ? 157 LEU A CG  1 
ATOM   1169  C CD1 . LEU A  1 157 ? 10.100  -45.748  -66.395 1.00 71.04  ? 157 LEU A CD1 1 
ATOM   1170  C CD2 . LEU A  1 157 ? 8.554   -45.752  -68.325 1.00 57.53  ? 157 LEU A CD2 1 
ATOM   1171  N N   . VAL A  1 158 ? 10.590  -40.825  -66.878 1.00 72.23  ? 158 VAL A N   1 
ATOM   1172  C CA  . VAL A  1 158 ? 10.743  -39.588  -67.632 1.00 71.22  ? 158 VAL A CA  1 
ATOM   1173  C C   . VAL A  1 158 ? 11.408  -39.887  -68.968 1.00 75.79  ? 158 VAL A C   1 
ATOM   1174  O O   . VAL A  1 158 ? 11.960  -40.972  -69.168 1.00 83.70  ? 158 VAL A O   1 
ATOM   1175  C CB  . VAL A  1 158 ? 11.580  -38.544  -66.869 1.00 67.36  ? 158 VAL A CB  1 
ATOM   1176  C CG1 . VAL A  1 158 ? 10.920  -38.197  -65.546 1.00 72.28  ? 158 VAL A CG1 1 
ATOM   1177  C CG2 . VAL A  1 158 ? 12.999  -39.048  -66.653 1.00 83.03  ? 158 VAL A CG2 1 
ATOM   1178  N N   . LYS A  1 159 ? 11.349  -38.926  -69.882 1.00 87.34  ? 159 LYS A N   1 
ATOM   1179  C CA  . LYS A  1 159 ? 11.905  -39.121  -71.213 1.00 97.02  ? 159 LYS A CA  1 
ATOM   1180  C C   . LYS A  1 159 ? 13.425  -39.078  -71.202 1.00 97.34  ? 159 LYS A C   1 
ATOM   1181  O O   . LYS A  1 159 ? 14.042  -38.212  -70.578 1.00 82.51  ? 159 LYS A O   1 
ATOM   1182  C CB  . LYS A  1 159 ? 11.365  -38.081  -72.191 1.00 96.50  ? 159 LYS A CB  1 
ATOM   1183  C CG  . LYS A  1 159 ? 11.975  -36.709  -72.019 1.00 94.70  ? 159 LYS A CG  1 
ATOM   1184  C CD  . LYS A  1 159 ? 11.641  -35.810  -73.186 1.00 98.30  ? 159 LYS A CD  1 
ATOM   1185  C CE  . LYS A  1 159 ? 11.978  -34.370  -72.857 1.00 98.53  ? 159 LYS A CE  1 
ATOM   1186  N NZ  . LYS A  1 159 ? 13.267  -34.292  -72.123 1.00 108.45 ? 159 LYS A NZ  1 
ATOM   1187  N N   . LYS A  1 160 ? 14.014  -40.035  -71.905 1.00 104.37 ? 160 LYS A N   1 
ATOM   1188  C CA  . LYS A  1 160 ? 15.455  -40.154  -72.015 1.00 114.12 ? 160 LYS A CA  1 
ATOM   1189  C C   . LYS A  1 160 ? 15.980  -39.177  -73.064 1.00 119.89 ? 160 LYS A C   1 
ATOM   1190  O O   . LYS A  1 160 ? 15.715  -39.336  -74.256 1.00 114.79 ? 160 LYS A O   1 
ATOM   1191  C CB  . LYS A  1 160 ? 15.815  -41.601  -72.376 1.00 101.71 ? 160 LYS A CB  1 
ATOM   1192  C CG  . LYS A  1 160 ? 17.287  -41.863  -72.616 1.00 103.39 ? 160 LYS A CG  1 
ATOM   1193  C CD  . LYS A  1 160 ? 17.722  -41.375  -73.984 1.00 117.86 ? 160 LYS A CD  1 
ATOM   1194  C CE  . LYS A  1 160 ? 19.099  -40.748  -73.926 1.00 115.73 ? 160 LYS A CE  1 
ATOM   1195  N NZ  . LYS A  1 160 ? 19.021  -39.272  -74.076 1.00 117.72 ? 160 LYS A NZ  1 
ATOM   1196  N N   . GLY A  1 161 ? 16.713  -38.164  -72.610 1.00 120.04 ? 161 GLY A N   1 
ATOM   1197  C CA  . GLY A  1 161 ? 17.323  -37.181  -73.493 1.00 117.02 ? 161 GLY A CA  1 
ATOM   1198  C C   . GLY A  1 161 ? 16.543  -36.748  -74.722 1.00 126.81 ? 161 GLY A C   1 
ATOM   1199  O O   . GLY A  1 161 ? 16.995  -36.936  -75.852 1.00 134.13 ? 161 GLY A O   1 
ATOM   1200  N N   . ASN A  1 162 ? 15.366  -36.172  -74.495 1.00 122.70 ? 162 ASN A N   1 
ATOM   1201  C CA  . ASN A  1 162 ? 14.569  -35.594  -75.570 1.00 137.42 ? 162 ASN A CA  1 
ATOM   1202  C C   . ASN A  1 162 ? 13.788  -36.631  -76.369 1.00 134.35 ? 162 ASN A C   1 
ATOM   1203  O O   . ASN A  1 162 ? 13.485  -36.410  -77.540 1.00 124.41 ? 162 ASN A O   1 
ATOM   1204  C CB  . ASN A  1 162 ? 15.408  -34.746  -76.522 1.00 151.80 ? 162 ASN A CB  1 
ATOM   1205  C CG  . ASN A  1 162 ? 15.247  -33.263  -76.281 1.00 155.10 ? 162 ASN A CG  1 
ATOM   1206  O OD1 . ASN A  1 162 ? 15.834  -32.442  -76.984 1.00 169.49 ? 162 ASN A OD1 1 
ATOM   1207  N ND2 . ASN A  1 162 ? 14.443  -32.909  -75.285 1.00 146.11 ? 162 ASN A ND2 1 
ATOM   1208  N N   . SER A  1 163 ? 13.458  -37.756  -75.749 1.00 135.49 ? 163 SER A N   1 
ATOM   1209  C CA  . SER A  1 163 ? 12.705  -38.785  -76.450 1.00 136.15 ? 163 SER A CA  1 
ATOM   1210  C C   . SER A  1 163 ? 11.758  -39.504  -75.497 1.00 122.81 ? 163 SER A C   1 
ATOM   1211  O O   . SER A  1 163 ? 12.139  -39.855  -74.385 1.00 113.30 ? 163 SER A O   1 
ATOM   1212  C CB  . SER A  1 163 ? 13.661  -39.788  -77.103 1.00 124.84 ? 163 SER A CB  1 
ATOM   1213  O OG  . SER A  1 163 ? 13.183  -40.205  -78.370 1.00 116.96 ? 163 SER A OG  1 
ATOM   1214  N N   . TYR A  1 164 ? 10.518  -39.705  -75.928 1.00 99.29  ? 164 TYR A N   1 
ATOM   1215  C CA  . TYR A  1 164 ? 9.589   -40.544  -75.181 1.00 93.17  ? 164 TYR A CA  1 
ATOM   1216  C C   . TYR A  1 164 ? 8.726   -41.342  -76.159 1.00 86.53  ? 164 TYR A C   1 
ATOM   1217  O O   . TYR A  1 164 ? 7.602   -40.946  -76.479 1.00 75.23  ? 164 TYR A O   1 
ATOM   1218  C CB  . TYR A  1 164 ? 8.731   -39.716  -74.214 1.00 96.81  ? 164 TYR A CB  1 
ATOM   1219  C CG  . TYR A  1 164 ? 7.947   -40.561  -73.230 1.00 86.71  ? 164 TYR A CG  1 
ATOM   1220  C CD1 . TYR A  1 164 ? 7.896   -40.242  -71.878 1.00 85.44  ? 164 TYR A CD1 1 
ATOM   1221  C CD2 . TYR A  1 164 ? 7.271   -41.691  -73.658 1.00 78.60  ? 164 TYR A CD2 1 
ATOM   1222  C CE1 . TYR A  1 164 ? 7.179   -41.027  -70.988 1.00 81.56  ? 164 TYR A CE1 1 
ATOM   1223  C CE2 . TYR A  1 164 ? 6.562   -42.475  -72.785 1.00 76.93  ? 164 TYR A CE2 1 
ATOM   1224  C CZ  . TYR A  1 164 ? 6.517   -42.145  -71.453 1.00 83.86  ? 164 TYR A CZ  1 
ATOM   1225  O OH  . TYR A  1 164 ? 5.798   -42.943  -70.592 1.00 76.16  ? 164 TYR A OH  1 
ATOM   1226  N N   . PRO A  1 165 ? 9.256   -42.478  -76.639 1.00 73.48  ? 165 PRO A N   1 
ATOM   1227  C CA  . PRO A  1 165 ? 8.499   -43.300  -77.584 1.00 81.65  ? 165 PRO A CA  1 
ATOM   1228  C C   . PRO A  1 165 ? 7.328   -43.934  -76.862 1.00 86.92  ? 165 PRO A C   1 
ATOM   1229  O O   . PRO A  1 165 ? 7.400   -44.115  -75.646 1.00 79.22  ? 165 PRO A O   1 
ATOM   1230  C CB  . PRO A  1 165 ? 9.487   -44.411  -77.965 1.00 78.21  ? 165 PRO A CB  1 
ATOM   1231  C CG  . PRO A  1 165 ? 10.807  -44.052  -77.308 1.00 95.70  ? 165 PRO A CG  1 
ATOM   1232  C CD  . PRO A  1 165 ? 10.462  -43.170  -76.157 1.00 80.37  ? 165 PRO A CD  1 
ATOM   1233  N N   . LYS A  1 166 ? 6.268   -44.274  -77.583 1.00 71.36  ? 166 LYS A N   1 
ATOM   1234  C CA  . LYS A  1 166 ? 5.168   -44.985  -76.956 1.00 80.77  ? 166 LYS A CA  1 
ATOM   1235  C C   . LYS A  1 166 ? 5.709   -46.255  -76.311 1.00 90.28  ? 166 LYS A C   1 
ATOM   1236  O O   . LYS A  1 166 ? 6.324   -47.083  -76.982 1.00 81.17  ? 166 LYS A O   1 
ATOM   1237  C CB  . LYS A  1 166 ? 4.092   -45.336  -77.983 1.00 74.62  ? 166 LYS A CB  1 
ATOM   1238  C CG  . LYS A  1 166 ? 3.247   -46.538  -77.593 1.00 87.10  ? 166 LYS A CG  1 
ATOM   1239  C CD  . LYS A  1 166 ? 2.420   -47.041  -78.761 1.00 98.35  ? 166 LYS A CD  1 
ATOM   1240  C CE  . LYS A  1 166 ? 1.301   -46.075  -79.100 1.00 99.28  ? 166 LYS A CE  1 
ATOM   1241  N NZ  . LYS A  1 166 ? 0.397   -46.637  -80.138 1.00 111.41 ? 166 LYS A NZ  1 
ATOM   1242  N N   . LEU A  1 167 ? 5.508   -46.400  -75.006 1.00 90.90  ? 167 LEU A N   1 
ATOM   1243  C CA  . LEU A  1 167 ? 5.899   -47.634  -74.335 1.00 85.78  ? 167 LEU A CA  1 
ATOM   1244  C C   . LEU A  1 167 ? 4.725   -48.602  -74.296 1.00 84.24  ? 167 LEU A C   1 
ATOM   1245  O O   . LEU A  1 167 ? 3.567   -48.186  -74.343 1.00 77.42  ? 167 LEU A O   1 
ATOM   1246  C CB  . LEU A  1 167 ? 6.447   -47.373  -72.927 1.00 66.82  ? 167 LEU A CB  1 
ATOM   1247  C CG  . LEU A  1 167 ? 5.568   -46.778  -71.821 1.00 76.89  ? 167 LEU A CG  1 
ATOM   1248  C CD1 . LEU A  1 167 ? 4.342   -47.627  -71.494 1.00 77.00  ? 167 LEU A CD1 1 
ATOM   1249  C CD2 . LEU A  1 167 ? 6.410   -46.566  -70.577 1.00 74.00  ? 167 LEU A CD2 1 
ATOM   1250  N N   . SER A  1 168 ? 5.027   -49.893  -74.214 1.00 82.21  ? 168 SER A N   1 
ATOM   1251  C CA  . SER A  1 168 ? 3.986   -50.911  -74.210 1.00 78.57  ? 168 SER A CA  1 
ATOM   1252  C C   . SER A  1 168 ? 4.439   -52.184  -73.501 1.00 78.79  ? 168 SER A C   1 
ATOM   1253  O O   . SER A  1 168 ? 4.863   -53.148  -74.139 1.00 103.06 ? 168 SER A O   1 
ATOM   1254  C CB  . SER A  1 168 ? 3.544   -51.226  -75.641 1.00 88.04  ? 168 SER A CB  1 
ATOM   1255  O OG  . SER A  1 168 ? 2.256   -51.817  -75.661 1.00 88.21  ? 168 SER A OG  1 
ATOM   1256  N N   . LYS A  1 169 ? 4.351   -52.175  -72.175 1.00 70.83  ? 169 LYS A N   1 
ATOM   1257  C CA  . LYS A  1 169 ? 4.674   -53.345  -71.371 1.00 80.90  ? 169 LYS A CA  1 
ATOM   1258  C C   . LYS A  1 169 ? 3.394   -54.014  -70.889 1.00 83.03  ? 169 LYS A C   1 
ATOM   1259  O O   . LYS A  1 169 ? 2.371   -53.355  -70.710 1.00 82.77  ? 169 LYS A O   1 
ATOM   1260  C CB  . LYS A  1 169 ? 5.531   -52.947  -70.170 1.00 72.62  ? 169 LYS A CB  1 
ATOM   1261  C CG  . LYS A  1 169 ? 6.995   -53.345  -70.272 1.00 84.15  ? 169 LYS A CG  1 
ATOM   1262  C CD  . LYS A  1 169 ? 7.180   -54.840  -70.078 1.00 95.05  ? 169 LYS A CD  1 
ATOM   1263  C CE  . LYS A  1 169 ? 8.640   -55.183  -69.840 1.00 100.40 ? 169 LYS A CE  1 
ATOM   1264  N NZ  . LYS A  1 169 ? 9.511   -54.736  -70.962 1.00 106.53 ? 169 LYS A NZ  1 
ATOM   1265  N N   . SER A  1 170 ? 3.455   -55.324  -70.681 1.00 94.07  ? 170 SER A N   1 
ATOM   1266  C CA  . SER A  1 170 ? 2.307   -56.067  -70.178 1.00 92.12  ? 170 SER A CA  1 
ATOM   1267  C C   . SER A  1 170 ? 2.743   -57.315  -69.418 1.00 77.13  ? 170 SER A C   1 
ATOM   1268  O O   . SER A  1 170 ? 3.501   -58.137  -69.932 1.00 85.06  ? 170 SER A O   1 
ATOM   1269  C CB  . SER A  1 170 ? 1.357   -56.437  -71.320 1.00 87.61  ? 170 SER A CB  1 
ATOM   1270  O OG  . SER A  1 170 ? 2.028   -57.169  -72.330 1.00 112.15 ? 170 SER A OG  1 
ATOM   1271  N N   . TYR A  1 171 ? 2.257   -57.440  -68.188 1.00 70.24  ? 171 TYR A N   1 
ATOM   1272  C CA  . TYR A  1 171 ? 2.591   -58.567  -67.326 1.00 76.84  ? 171 TYR A CA  1 
ATOM   1273  C C   . TYR A  1 171 ? 1.412   -59.530  -67.208 1.00 70.01  ? 171 TYR A C   1 
ATOM   1274  O O   . TYR A  1 171 ? 0.259   -59.105  -67.153 1.00 63.67  ? 171 TYR A O   1 
ATOM   1275  C CB  . TYR A  1 171 ? 3.003   -58.059  -65.942 1.00 75.26  ? 171 TYR A CB  1 
ATOM   1276  C CG  . TYR A  1 171 ? 2.879   -59.082  -64.837 1.00 65.70  ? 171 TYR A CG  1 
ATOM   1277  C CD1 . TYR A  1 171 ? 3.951   -59.892  -64.490 1.00 72.04  ? 171 TYR A CD1 1 
ATOM   1278  C CD2 . TYR A  1 171 ? 1.691   -59.233  -64.136 1.00 72.40  ? 171 TYR A CD2 1 
ATOM   1279  C CE1 . TYR A  1 171 ? 3.842   -60.823  -63.478 1.00 75.30  ? 171 TYR A CE1 1 
ATOM   1280  C CE2 . TYR A  1 171 ? 1.571   -60.165  -63.124 1.00 73.44  ? 171 TYR A CE2 1 
ATOM   1281  C CZ  . TYR A  1 171 ? 2.650   -60.958  -62.800 1.00 76.82  ? 171 TYR A CZ  1 
ATOM   1282  O OH  . TYR A  1 171 ? 2.539   -61.889  -61.793 1.00 82.94  ? 171 TYR A OH  1 
ATOM   1283  N N   . ILE A  1 172 ? 1.705   -60.826  -67.169 1.00 76.09  ? 172 ILE A N   1 
ATOM   1284  C CA  . ILE A  1 172 ? 0.667   -61.842  -67.032 1.00 80.25  ? 172 ILE A CA  1 
ATOM   1285  C C   . ILE A  1 172 ? 0.774   -62.558  -65.687 1.00 79.59  ? 172 ILE A C   1 
ATOM   1286  O O   . ILE A  1 172 ? 1.843   -63.028  -65.310 1.00 73.92  ? 172 ILE A O   1 
ATOM   1287  C CB  . ILE A  1 172 ? 0.727   -62.874  -68.176 1.00 75.11  ? 172 ILE A CB  1 
ATOM   1288  C CG1 . ILE A  1 172 ? -0.419  -63.879  -68.048 1.00 78.11  ? 172 ILE A CG1 1 
ATOM   1289  C CG2 . ILE A  1 172 ? 2.072   -63.587  -68.183 1.00 88.69  ? 172 ILE A CG2 1 
ATOM   1290  C CD1 . ILE A  1 172 ? -1.201  -64.076  -69.329 1.00 87.09  ? 172 ILE A CD1 1 
ATOM   1291  N N   . ASN A  1 173 ? -0.338  -62.642  -64.967 1.00 69.85  ? 173 ASN A N   1 
ATOM   1292  C CA  . ASN A  1 173 ? -0.336  -63.227  -63.630 1.00 77.86  ? 173 ASN A CA  1 
ATOM   1293  C C   . ASN A  1 173 ? -0.024  -64.723  -63.629 1.00 85.28  ? 173 ASN A C   1 
ATOM   1294  O O   . ASN A  1 173 ? -0.915  -65.551  -63.818 1.00 75.70  ? 173 ASN A O   1 
ATOM   1295  C CB  . ASN A  1 173 ? -1.668  -62.963  -62.924 1.00 71.09  ? 173 ASN A CB  1 
ATOM   1296  C CG  . ASN A  1 173 ? -1.629  -63.326  -61.453 1.00 75.82  ? 173 ASN A CG  1 
ATOM   1297  O OD1 . ASN A  1 173 ? -0.622  -63.826  -60.954 1.00 82.68  ? 173 ASN A OD1 1 
ATOM   1298  N ND2 . ASN A  1 173 ? -2.727  -63.073  -60.750 1.00 71.61  ? 173 ASN A ND2 1 
ATOM   1299  N N   . ASP A  1 174 ? 1.243   -65.063  -63.411 1.00 95.57  ? 174 ASP A N   1 
ATOM   1300  C CA  . ASP A  1 174 ? 1.659   -66.460  -63.357 1.00 94.66  ? 174 ASP A CA  1 
ATOM   1301  C C   . ASP A  1 174 ? 1.542   -67.013  -61.942 1.00 97.21  ? 174 ASP A C   1 
ATOM   1302  O O   . ASP A  1 174 ? 1.842   -68.179  -61.701 1.00 114.03 ? 174 ASP A O   1 
ATOM   1303  C CB  . ASP A  1 174 ? 3.094   -66.625  -63.864 1.00 102.53 ? 174 ASP A CB  1 
ATOM   1304  C CG  . ASP A  1 174 ? 4.102   -65.875  -63.014 1.00 119.33 ? 174 ASP A CG  1 
ATOM   1305  O OD1 . ASP A  1 174 ? 4.744   -66.506  -62.146 1.00 129.81 ? 174 ASP A OD1 1 
ATOM   1306  O OD2 . ASP A  1 174 ? 4.249   -64.652  -63.211 1.00 113.83 ? 174 ASP A OD2 1 
ATOM   1307  N N   . LYS A  1 175 ? 1.112   -66.166  -61.012 1.00 85.33  ? 175 LYS A N   1 
ATOM   1308  C CA  . LYS A  1 175 ? 0.891   -66.584  -59.633 1.00 84.52  ? 175 LYS A CA  1 
ATOM   1309  C C   . LYS A  1 175 ? -0.412  -67.378  -59.539 1.00 96.18  ? 175 LYS A C   1 
ATOM   1310  O O   . LYS A  1 175 ? -1.152  -67.485  -60.517 1.00 100.40 ? 175 LYS A O   1 
ATOM   1311  C CB  . LYS A  1 175 ? 0.839   -65.368  -58.706 1.00 72.57  ? 175 LYS A CB  1 
ATOM   1312  C CG  . LYS A  1 175 ? 2.024   -64.416  -58.836 1.00 75.47  ? 175 LYS A CG  1 
ATOM   1313  C CD  . LYS A  1 175 ? 3.307   -65.010  -58.270 1.00 73.13  ? 175 LYS A CD  1 
ATOM   1314  C CE  . LYS A  1 175 ? 4.440   -63.990  -58.297 1.00 69.06  ? 175 LYS A CE  1 
ATOM   1315  N NZ  . LYS A  1 175 ? 5.696   -64.511  -57.688 1.00 94.22  ? 175 LYS A NZ  1 
ATOM   1316  N N   . GLY A  1 176 ? -0.681  -67.943  -58.366 1.00 71.42  ? 176 GLY A N   1 
ATOM   1317  C CA  . GLY A  1 176 ? -1.897  -68.710  -58.148 1.00 97.90  ? 176 GLY A CA  1 
ATOM   1318  C C   . GLY A  1 176 ? -2.827  -67.964  -57.222 1.00 97.99  ? 176 GLY A C   1 
ATOM   1319  O O   . GLY A  1 176 ? -3.724  -68.537  -56.601 1.00 101.74 ? 176 GLY A O   1 
ATOM   1320  N N   . LYS A  1 177 ? -2.592  -66.663  -57.138 1.00 90.31  ? 177 LYS A N   1 
ATOM   1321  C CA  . LYS A  1 177 ? -3.365  -65.777  -56.295 1.00 78.91  ? 177 LYS A CA  1 
ATOM   1322  C C   . LYS A  1 177 ? -3.448  -64.444  -57.014 1.00 71.59  ? 177 LYS A C   1 
ATOM   1323  O O   . LYS A  1 177 ? -2.631  -64.155  -57.889 1.00 81.07  ? 177 LYS A O   1 
ATOM   1324  C CB  . LYS A  1 177 ? -2.669  -65.610  -54.946 1.00 72.27  ? 177 LYS A CB  1 
ATOM   1325  C CG  . LYS A  1 177 ? -1.199  -65.238  -55.067 1.00 73.24  ? 177 LYS A CG  1 
ATOM   1326  C CD  . LYS A  1 177 ? -0.500  -65.266  -53.719 1.00 76.34  ? 177 LYS A CD  1 
ATOM   1327  C CE  . LYS A  1 177 ? -0.374  -66.684  -53.189 1.00 88.51  ? 177 LYS A CE  1 
ATOM   1328  N NZ  . LYS A  1 177 ? 0.441   -67.545  -54.089 1.00 101.25 ? 177 LYS A NZ  1 
ATOM   1329  N N   . GLU A  1 178 ? -4.439  -63.637  -56.656 1.00 59.86  ? 178 GLU A N   1 
ATOM   1330  C CA  . GLU A  1 178 ? -4.587  -62.320  -57.254 1.00 66.14  ? 178 GLU A CA  1 
ATOM   1331  C C   . GLU A  1 178 ? -3.314  -61.513  -57.056 1.00 71.12  ? 178 GLU A C   1 
ATOM   1332  O O   . GLU A  1 178 ? -2.572  -61.734  -56.099 1.00 60.11  ? 178 GLU A O   1 
ATOM   1333  C CB  . GLU A  1 178 ? -5.766  -61.584  -56.627 1.00 67.55  ? 178 GLU A CB  1 
ATOM   1334  C CG  . GLU A  1 178 ? -7.096  -62.290  -56.792 1.00 89.05  ? 178 GLU A CG  1 
ATOM   1335  C CD  . GLU A  1 178 ? -8.194  -61.636  -55.984 1.00 88.30  ? 178 GLU A CD  1 
ATOM   1336  O OE1 . GLU A  1 178 ? -7.954  -61.339  -54.795 1.00 84.66  ? 178 GLU A OE1 1 
ATOM   1337  O OE2 . GLU A  1 178 ? -9.293  -61.419  -56.534 1.00 87.05  ? 178 GLU A OE2 1 
ATOM   1338  N N   . VAL A  1 179 ? -3.061  -60.581  -57.966 1.00 57.13  ? 179 VAL A N   1 
ATOM   1339  C CA  . VAL A  1 179 ? -1.920  -59.687  -57.836 1.00 60.47  ? 179 VAL A CA  1 
ATOM   1340  C C   . VAL A  1 179 ? -2.376  -58.235  -57.808 1.00 55.49  ? 179 VAL A C   1 
ATOM   1341  O O   . VAL A  1 179 ? -3.010  -57.754  -58.747 1.00 50.67  ? 179 VAL A O   1 
ATOM   1342  C CB  . VAL A  1 179 ? -0.906  -59.879  -58.978 1.00 56.89  ? 179 VAL A CB  1 
ATOM   1343  C CG1 . VAL A  1 179 ? 0.106   -58.744  -58.980 1.00 60.38  ? 179 VAL A CG1 1 
ATOM   1344  C CG2 . VAL A  1 179 ? -0.209  -61.223  -58.846 1.00 54.81  ? 179 VAL A CG2 1 
ATOM   1345  N N   . LEU A  1 180 ? -2.057  -57.544  -56.719 1.00 46.08  ? 180 LEU A N   1 
ATOM   1346  C CA  . LEU A  1 180 ? -2.379  -56.131  -56.596 1.00 49.06  ? 180 LEU A CA  1 
ATOM   1347  C C   . LEU A  1 180 ? -1.358  -55.293  -57.352 1.00 49.05  ? 180 LEU A C   1 
ATOM   1348  O O   . LEU A  1 180 ? -0.187  -55.240  -56.977 1.00 53.01  ? 180 LEU A O   1 
ATOM   1349  C CB  . LEU A  1 180 ? -2.406  -55.712  -55.126 1.00 45.23  ? 180 LEU A CB  1 
ATOM   1350  C CG  . LEU A  1 180 ? -2.645  -54.223  -54.864 1.00 38.38  ? 180 LEU A CG  1 
ATOM   1351  C CD1 . LEU A  1 180 ? -4.085  -53.848  -55.174 1.00 41.59  ? 180 LEU A CD1 1 
ATOM   1352  C CD2 . LEU A  1 180 ? -2.299  -53.870  -53.427 1.00 41.02  ? 180 LEU A CD2 1 
ATOM   1353  N N   . VAL A  1 181 ? -1.803  -54.645  -58.422 1.00 49.05  ? 181 VAL A N   1 
ATOM   1354  C CA  . VAL A  1 181 ? -0.929  -53.776  -59.197 1.00 51.68  ? 181 VAL A CA  1 
ATOM   1355  C C   . VAL A  1 181 ? -1.301  -52.316  -58.978 1.00 42.31  ? 181 VAL A C   1 
ATOM   1356  O O   . VAL A  1 181 ? -2.460  -51.932  -59.129 1.00 48.63  ? 181 VAL A O   1 
ATOM   1357  C CB  . VAL A  1 181 ? -1.003  -54.092  -60.701 1.00 40.98  ? 181 VAL A CB  1 
ATOM   1358  C CG1 . VAL A  1 181 ? 0.051   -53.301  -61.458 1.00 51.57  ? 181 VAL A CG1 1 
ATOM   1359  C CG2 . VAL A  1 181 ? -0.820  -55.581  -60.938 1.00 49.95  ? 181 VAL A CG2 1 
ATOM   1360  N N   . LEU A  1 182 ? -0.314  -51.505  -58.612 1.00 45.36  ? 182 LEU A N   1 
ATOM   1361  C CA  . LEU A  1 182 ? -0.534  -50.077  -58.431 1.00 50.81  ? 182 LEU A CA  1 
ATOM   1362  C C   . LEU A  1 182 ? 0.251   -49.274  -59.459 1.00 44.70  ? 182 LEU A C   1 
ATOM   1363  O O   . LEU A  1 182 ? 1.351   -49.658  -59.853 1.00 55.18  ? 182 LEU A O   1 
ATOM   1364  C CB  . LEU A  1 182 ? -0.145  -49.638  -57.018 1.00 45.17  ? 182 LEU A CB  1 
ATOM   1365  C CG  . LEU A  1 182 ? -0.977  -50.212  -55.871 1.00 53.99  ? 182 LEU A CG  1 
ATOM   1366  C CD1 . LEU A  1 182 ? -0.154  -51.205  -55.070 1.00 50.61  ? 182 LEU A CD1 1 
ATOM   1367  C CD2 . LEU A  1 182 ? -1.500  -49.097  -54.976 1.00 52.96  ? 182 LEU A CD2 1 
ATOM   1368  N N   . TRP A  1 183 ? -0.327  -48.161  -59.893 1.00 49.68  ? 183 TRP A N   1 
ATOM   1369  C CA  . TRP A  1 183 ? 0.342   -47.269  -60.828 1.00 52.74  ? 183 TRP A CA  1 
ATOM   1370  C C   . TRP A  1 183 ? -0.140  -45.841  -60.614 1.00 47.48  ? 183 TRP A C   1 
ATOM   1371  O O   . TRP A  1 183 ? -1.119  -45.609  -59.905 1.00 45.91  ? 183 TRP A O   1 
ATOM   1372  C CB  . TRP A  1 183 ? 0.095   -47.708  -62.273 1.00 54.46  ? 183 TRP A CB  1 
ATOM   1373  C CG  . TRP A  1 183 ? -1.307  -47.483  -62.751 1.00 49.94  ? 183 TRP A CG  1 
ATOM   1374  C CD1 . TRP A  1 183 ? -1.785  -46.380  -63.398 1.00 44.82  ? 183 TRP A CD1 1 
ATOM   1375  C CD2 . TRP A  1 183 ? -2.413  -48.386  -62.629 1.00 60.35  ? 183 TRP A CD2 1 
ATOM   1376  N NE1 . TRP A  1 183 ? -3.119  -46.539  -63.683 1.00 47.86  ? 183 TRP A NE1 1 
ATOM   1377  C CE2 . TRP A  1 183 ? -3.529  -47.762  -63.222 1.00 49.02  ? 183 TRP A CE2 1 
ATOM   1378  C CE3 . TRP A  1 183 ? -2.568  -49.660  -62.075 1.00 47.93  ? 183 TRP A CE3 1 
ATOM   1379  C CZ2 . TRP A  1 183 ? -4.782  -48.369  -63.276 1.00 49.02  ? 183 TRP A CZ2 1 
ATOM   1380  C CZ3 . TRP A  1 183 ? -3.813  -50.261  -62.130 1.00 53.33  ? 183 TRP A CZ3 1 
ATOM   1381  C CH2 . TRP A  1 183 ? -4.903  -49.615  -62.726 1.00 58.74  ? 183 TRP A CH2 1 
ATOM   1382  N N   . GLY A  1 184 ? 0.550   -44.887  -61.226 1.00 48.95  ? 184 GLY A N   1 
ATOM   1383  C CA  . GLY A  1 184 ? 0.207   -43.489  -61.057 1.00 44.11  ? 184 GLY A CA  1 
ATOM   1384  C C   . GLY A  1 184 ? 0.131   -42.725  -62.362 1.00 50.91  ? 184 GLY A C   1 
ATOM   1385  O O   . GLY A  1 184 ? 0.826   -43.045  -63.326 1.00 53.90  ? 184 GLY A O   1 
ATOM   1386  N N   . ILE A  1 185 ? -0.729  -41.714  -62.392 1.00 47.52  ? 185 ILE A N   1 
ATOM   1387  C CA  . ILE A  1 185 ? -0.820  -40.817  -63.533 1.00 42.60  ? 185 ILE A CA  1 
ATOM   1388  C C   . ILE A  1 185 ? -0.413  -39.421  -63.086 1.00 47.34  ? 185 ILE A C   1 
ATOM   1389  O O   . ILE A  1 185 ? -1.094  -38.804  -62.267 1.00 46.49  ? 185 ILE A O   1 
ATOM   1390  C CB  . ILE A  1 185 ? -2.246  -40.765  -64.106 1.00 50.46  ? 185 ILE A CB  1 
ATOM   1391  C CG1 . ILE A  1 185 ? -2.755  -42.175  -64.409 1.00 46.78  ? 185 ILE A CG1 1 
ATOM   1392  C CG2 . ILE A  1 185 ? -2.287  -39.894  -65.353 1.00 42.18  ? 185 ILE A CG2 1 
ATOM   1393  C CD1 . ILE A  1 185 ? -1.903  -42.930  -65.404 1.00 46.83  ? 185 ILE A CD1 1 
ATOM   1394  N N   . HIS A  1 186 ? 0.702   -38.929  -63.613 1.00 58.02  ? 186 HIS A N   1 
ATOM   1395  C CA  . HIS A  1 186 ? 1.205   -37.619  -63.219 1.00 57.53  ? 186 HIS A CA  1 
ATOM   1396  C C   . HIS A  1 186 ? 0.600   -36.495  -64.051 1.00 51.60  ? 186 HIS A C   1 
ATOM   1397  O O   . HIS A  1 186 ? 0.567   -36.562  -65.280 1.00 53.84  ? 186 HIS A O   1 
ATOM   1398  C CB  . HIS A  1 186 ? 2.734   -37.569  -63.293 1.00 63.64  ? 186 HIS A CB  1 
ATOM   1399  C CG  . HIS A  1 186 ? 3.305   -36.222  -62.986 1.00 67.08  ? 186 HIS A CG  1 
ATOM   1400  N ND1 . HIS A  1 186 ? 3.898   -35.425  -63.944 1.00 61.99  ? 186 HIS A ND1 1 
ATOM   1401  C CD2 . HIS A  1 186 ? 3.362   -35.518  -61.828 1.00 62.94  ? 186 HIS A CD2 1 
ATOM   1402  C CE1 . HIS A  1 186 ? 4.301   -34.298  -63.388 1.00 65.75  ? 186 HIS A CE1 1 
ATOM   1403  N NE2 . HIS A  1 186 ? 3.989   -34.327  -62.109 1.00 59.41  ? 186 HIS A NE2 1 
ATOM   1404  N N   . HIS A  1 187 ? 0.116   -35.464  -63.367 1.00 61.92  ? 187 HIS A N   1 
ATOM   1405  C CA  . HIS A  1 187 ? -0.432  -34.289  -64.028 1.00 49.94  ? 187 HIS A CA  1 
ATOM   1406  C C   . HIS A  1 187 ? 0.436   -33.072  -63.724 1.00 67.81  ? 187 HIS A C   1 
ATOM   1407  O O   . HIS A  1 187 ? 0.309   -32.465  -62.660 1.00 71.06  ? 187 HIS A O   1 
ATOM   1408  C CB  . HIS A  1 187 ? -1.871  -34.037  -63.571 1.00 48.88  ? 187 HIS A CB  1 
ATOM   1409  C CG  . HIS A  1 187 ? -2.775  -35.216  -63.743 1.00 58.39  ? 187 HIS A CG  1 
ATOM   1410  N ND1 . HIS A  1 187 ? -3.458  -35.468  -64.916 1.00 56.13  ? 187 HIS A ND1 1 
ATOM   1411  C CD2 . HIS A  1 187 ? -3.114  -36.214  -62.891 1.00 64.14  ? 187 HIS A CD2 1 
ATOM   1412  C CE1 . HIS A  1 187 ? -4.174  -36.568  -64.777 1.00 57.62  ? 187 HIS A CE1 1 
ATOM   1413  N NE2 . HIS A  1 187 ? -3.985  -37.040  -63.561 1.00 63.15  ? 187 HIS A NE2 1 
ATOM   1414  N N   . PRO A  1 188 ? 1.330   -32.720  -64.659 1.00 62.28  ? 188 PRO A N   1 
ATOM   1415  C CA  . PRO A  1 188 ? 2.247   -31.587  -64.497 1.00 63.70  ? 188 PRO A CA  1 
ATOM   1416  C C   . PRO A  1 188 ? 1.506   -30.273  -64.272 1.00 64.21  ? 188 PRO A C   1 
ATOM   1417  O O   . PRO A  1 188 ? 0.325   -30.164  -64.601 1.00 56.72  ? 188 PRO A O   1 
ATOM   1418  C CB  . PRO A  1 188 ? 2.994   -31.549  -65.833 1.00 63.22  ? 188 PRO A CB  1 
ATOM   1419  C CG  . PRO A  1 188 ? 2.908   -32.942  -66.348 1.00 63.98  ? 188 PRO A CG  1 
ATOM   1420  C CD  . PRO A  1 188 ? 1.559   -33.435  -65.925 1.00 56.12  ? 188 PRO A CD  1 
ATOM   1421  N N   . SER A  1 189 ? 2.204   -29.288  -63.718 1.00 68.03  ? 189 SER A N   1 
ATOM   1422  C CA  . SER A  1 189 ? 1.597   -28.002  -63.396 1.00 63.38  ? 189 SER A CA  1 
ATOM   1423  C C   . SER A  1 189 ? 1.524   -27.085  -64.612 1.00 69.96  ? 189 SER A C   1 
ATOM   1424  O O   . SER A  1 189 ? 0.547   -26.360  -64.797 1.00 68.10  ? 189 SER A O   1 
ATOM   1425  C CB  . SER A  1 189 ? 2.370   -27.317  -62.267 1.00 65.22  ? 189 SER A CB  1 
ATOM   1426  O OG  . SER A  1 189 ? 3.739   -27.169  -62.602 1.00 74.54  ? 189 SER A OG  1 
ATOM   1427  N N   . THR A  1 190 ? 2.563   -27.123  -65.439 1.00 75.68  ? 190 THR A N   1 
ATOM   1428  C CA  . THR A  1 190 ? 2.639   -26.261  -66.611 1.00 76.31  ? 190 THR A CA  1 
ATOM   1429  C C   . THR A  1 190 ? 2.978   -27.047  -67.874 1.00 74.99  ? 190 THR A C   1 
ATOM   1430  O O   . THR A  1 190 ? 3.591   -28.112  -67.807 1.00 77.81  ? 190 THR A O   1 
ATOM   1431  C CB  . THR A  1 190 ? 3.675   -25.138  -66.409 1.00 77.22  ? 190 THR A CB  1 
ATOM   1432  O OG1 . THR A  1 190 ? 4.263   -24.793  -67.669 1.00 102.85 ? 190 THR A OG1 1 
ATOM   1433  C CG2 . THR A  1 190 ? 4.771   -25.591  -65.455 1.00 75.47  ? 190 THR A CG2 1 
ATOM   1434  N N   . SER A  1 191 ? 2.569   -26.518  -69.024 1.00 88.42  ? 191 SER A N   1 
ATOM   1435  C CA  . SER A  1 191 ? 2.852   -27.158  -70.304 1.00 87.50  ? 191 SER A CA  1 
ATOM   1436  C C   . SER A  1 191 ? 4.355   -27.215  -70.558 1.00 78.16  ? 191 SER A C   1 
ATOM   1437  O O   . SER A  1 191 ? 4.833   -28.043  -71.333 1.00 75.67  ? 191 SER A O   1 
ATOM   1438  C CB  . SER A  1 191 ? 2.148   -26.421  -71.445 1.00 78.76  ? 191 SER A CB  1 
ATOM   1439  O OG  . SER A  1 191 ? 2.603   -25.083  -71.549 1.00 90.09  ? 191 SER A OG  1 
ATOM   1440  N N   . ALA A  1 192 ? 5.093   -26.325  -69.902 1.00 83.42  ? 192 ALA A N   1 
ATOM   1441  C CA  . ALA A  1 192 ? 6.548   -26.332  -69.982 1.00 94.10  ? 192 ALA A CA  1 
ATOM   1442  C C   . ALA A  1 192 ? 7.101   -27.524  -69.211 1.00 93.97  ? 192 ALA A C   1 
ATOM   1443  O O   . ALA A  1 192 ? 8.048   -28.175  -69.651 1.00 90.08  ? 192 ALA A O   1 
ATOM   1444  C CB  . ALA A  1 192 ? 7.118   -25.031  -69.439 1.00 92.92  ? 192 ALA A CB  1 
ATOM   1445  N N   . ASP A  1 193 ? 6.501   -27.804  -68.058 1.00 93.41  ? 193 ASP A N   1 
ATOM   1446  C CA  . ASP A  1 193 ? 6.873   -28.966  -67.261 1.00 85.71  ? 193 ASP A CA  1 
ATOM   1447  C C   . ASP A  1 193 ? 6.527   -30.257  -67.993 1.00 74.44  ? 193 ASP A C   1 
ATOM   1448  O O   . ASP A  1 193 ? 7.205   -31.273  -67.836 1.00 66.00  ? 193 ASP A O   1 
ATOM   1449  C CB  . ASP A  1 193 ? 6.170   -28.938  -65.901 1.00 82.44  ? 193 ASP A CB  1 
ATOM   1450  C CG  . ASP A  1 193 ? 7.047   -28.377  -64.800 1.00 108.27 ? 193 ASP A CG  1 
ATOM   1451  O OD1 . ASP A  1 193 ? 7.753   -27.376  -65.045 1.00 108.06 ? 193 ASP A OD1 1 
ATOM   1452  O OD2 . ASP A  1 193 ? 7.028   -28.939  -63.684 1.00 131.83 ? 193 ASP A OD2 1 
ATOM   1453  N N   . GLN A  1 194 ? 5.465   -30.209  -68.792 1.00 71.82  ? 194 GLN A N   1 
ATOM   1454  C CA  . GLN A  1 194 ? 5.011   -31.373  -69.545 1.00 70.84  ? 194 GLN A CA  1 
ATOM   1455  C C   . GLN A  1 194 ? 6.054   -31.831  -70.560 1.00 79.94  ? 194 GLN A C   1 
ATOM   1456  O O   . GLN A  1 194 ? 6.488   -32.983  -70.537 1.00 78.77  ? 194 GLN A O   1 
ATOM   1457  C CB  . GLN A  1 194 ? 3.687   -31.071  -70.252 1.00 78.17  ? 194 GLN A CB  1 
ATOM   1458  C CG  . GLN A  1 194 ? 3.261   -32.124  -71.267 1.00 76.08  ? 194 GLN A CG  1 
ATOM   1459  C CD  . GLN A  1 194 ? 2.832   -33.428  -70.622 1.00 79.80  ? 194 GLN A CD  1 
ATOM   1460  O OE1 . GLN A  1 194 ? 2.715   -34.455  -71.291 1.00 78.76  ? 194 GLN A OE1 1 
ATOM   1461  N NE2 . GLN A  1 194 ? 2.591   -33.393  -69.318 1.00 69.45  ? 194 GLN A NE2 1 
ATOM   1462  N N   . GLN A  1 195 ? 6.451   -30.927  -71.449 1.00 109.87 ? 195 GLN A N   1 
ATOM   1463  C CA  . GLN A  1 195 ? 7.446   -31.246  -72.468 1.00 118.36 ? 195 GLN A CA  1 
ATOM   1464  C C   . GLN A  1 195 ? 8.828   -31.441  -71.851 1.00 105.93 ? 195 GLN A C   1 
ATOM   1465  O O   . GLN A  1 195 ? 9.675   -32.137  -72.410 1.00 96.40  ? 195 GLN A O   1 
ATOM   1466  C CB  . GLN A  1 195 ? 7.482   -30.162  -73.548 1.00 117.26 ? 195 GLN A CB  1 
ATOM   1467  C CG  . GLN A  1 195 ? 7.683   -28.753  -73.018 1.00 142.54 ? 195 GLN A CG  1 
ATOM   1468  C CD  . GLN A  1 195 ? 7.520   -27.698  -74.096 1.00 160.83 ? 195 GLN A CD  1 
ATOM   1469  O OE1 . GLN A  1 195 ? 7.668   -26.503  -73.839 1.00 147.63 ? 195 GLN A OE1 1 
ATOM   1470  N NE2 . GLN A  1 195 ? 7.212   -28.136  -75.311 1.00 166.58 ? 195 GLN A NE2 1 
ATOM   1471  N N   . SER A  1 196 ? 9.046   -30.824  -70.694 1.00 85.30  ? 196 SER A N   1 
ATOM   1472  C CA  . SER A  1 196 ? 10.298  -30.988  -69.967 1.00 81.36  ? 196 SER A CA  1 
ATOM   1473  C C   . SER A  1 196 ? 10.445  -32.419  -69.467 1.00 93.00  ? 196 SER A C   1 
ATOM   1474  O O   . SER A  1 196 ? 11.551  -32.958  -69.406 1.00 93.89  ? 196 SER A O   1 
ATOM   1475  C CB  . SER A  1 196 ? 10.361  -30.018  -68.785 1.00 80.06  ? 196 SER A CB  1 
ATOM   1476  O OG  . SER A  1 196 ? 11.502  -30.265  -67.982 1.00 87.57  ? 196 SER A OG  1 
ATOM   1477  N N   . LEU A  1 197 ? 9.318   -33.030  -69.115 1.00 94.28  ? 197 LEU A N   1 
ATOM   1478  C CA  . LEU A  1 197 ? 9.316   -34.366  -68.530 1.00 81.72  ? 197 LEU A CA  1 
ATOM   1479  C C   . LEU A  1 197 ? 9.105   -35.477  -69.556 1.00 81.52  ? 197 LEU A C   1 
ATOM   1480  O O   . LEU A  1 197 ? 9.766   -36.513  -69.497 1.00 79.67  ? 197 LEU A O   1 
ATOM   1481  C CB  . LEU A  1 197 ? 8.255   -34.463  -67.429 1.00 74.63  ? 197 LEU A CB  1 
ATOM   1482  C CG  . LEU A  1 197 ? 8.621   -33.875  -66.065 1.00 73.71  ? 197 LEU A CG  1 
ATOM   1483  C CD1 . LEU A  1 197 ? 7.390   -33.753  -65.179 1.00 69.85  ? 197 LEU A CD1 1 
ATOM   1484  C CD2 . LEU A  1 197 ? 9.689   -34.723  -65.391 1.00 70.71  ? 197 LEU A CD2 1 
ATOM   1485  N N   . TYR A  1 198 ? 8.187   -35.264  -70.494 1.00 79.09  ? 198 TYR A N   1 
ATOM   1486  C CA  . TYR A  1 198 ? 7.821   -36.320  -71.432 1.00 83.73  ? 198 TYR A CA  1 
ATOM   1487  C C   . TYR A  1 198 ? 7.621   -35.228  -72.488 1.00 91.90  ? 198 TYR A C   1 
ATOM   1488  O O   . TYR A  1 198 ? 6.597   -34.544  -72.492 1.00 89.73  ? 198 TYR A O   1 
ATOM   1489  C CB  . TYR A  1 198 ? 6.434   -36.877  -71.084 1.00 97.30  ? 198 TYR A CB  1 
ATOM   1490  C CG  . TYR A  1 198 ? 6.159   -36.941  -69.594 1.00 83.43  ? 198 TYR A CG  1 
ATOM   1491  C CD1 . TYR A  1 198 ? 5.342   -36.001  -68.980 1.00 69.14  ? 198 TYR A CD1 1 
ATOM   1492  C CD2 . TYR A  1 198 ? 6.724   -37.933  -68.801 1.00 79.25  ? 198 TYR A CD2 1 
ATOM   1493  C CE1 . TYR A  1 198 ? 5.089   -36.049  -67.620 1.00 76.60  ? 198 TYR A CE1 1 
ATOM   1494  C CE2 . TYR A  1 198 ? 6.477   -37.989  -67.439 1.00 71.92  ? 198 TYR A CE2 1 
ATOM   1495  C CZ  . TYR A  1 198 ? 5.659   -37.044  -66.856 1.00 72.42  ? 198 TYR A CZ  1 
ATOM   1496  O OH  . TYR A  1 198 ? 5.409   -37.093  -65.504 1.00 69.60  ? 198 TYR A OH  1 
ATOM   1497  N N   . GLN A  1 199 ? 8.599   -35.075  -73.380 1.00 97.96  ? 199 GLN A N   1 
ATOM   1498  C CA  . GLN A  1 199 ? 8.524   -34.113  -74.488 1.00 102.01 ? 199 GLN A CA  1 
ATOM   1499  C C   . GLN A  1 199 ? 7.266   -33.813  -75.292 1.00 96.45  ? 199 GLN A C   1 
ATOM   1500  O O   . GLN A  1 199 ? 7.096   -32.712  -75.814 1.00 98.54  ? 199 GLN A O   1 
ATOM   1501  C CB  . GLN A  1 199 ? 9.326   -35.074  -75.370 1.00 113.31 ? 199 GLN A CB  1 
ATOM   1502  C CG  . GLN A  1 199 ? 10.643  -34.513  -75.899 1.00 122.05 ? 199 GLN A CG  1 
ATOM   1503  C CD  . GLN A  1 199 ? 10.502  -33.145  -76.539 1.00 121.65 ? 199 GLN A CD  1 
ATOM   1504  O OE1 . GLN A  1 199 ? 9.757   -32.966  -77.504 1.00 122.88 ? 199 GLN A OE1 1 
ATOM   1505  N NE2 . GLN A  1 199 ? 11.226  -32.168  -76.003 1.00 109.80 ? 199 GLN A NE2 1 
ATOM   1506  N N   . ASN A  1 200 ? 6.395   -34.810  -75.399 1.00 102.24 ? 200 ASN A N   1 
ATOM   1507  C CA  . ASN A  1 200 ? 5.173   -34.692  -76.179 1.00 97.37  ? 200 ASN A CA  1 
ATOM   1508  C C   . ASN A  1 200 ? 4.198   -33.824  -75.392 1.00 102.66 ? 200 ASN A C   1 
ATOM   1509  O O   . ASN A  1 200 ? 4.175   -33.862  -74.162 1.00 111.20 ? 200 ASN A O   1 
ATOM   1510  C CB  . ASN A  1 200 ? 4.566   -36.069  -76.446 1.00 98.45  ? 200 ASN A CB  1 
ATOM   1511  C CG  . ASN A  1 200 ? 5.603   -37.087  -76.887 1.00 98.77  ? 200 ASN A CG  1 
ATOM   1512  O OD1 . ASN A  1 200 ? 6.733   -36.732  -77.228 1.00 111.66 ? 200 ASN A OD1 1 
ATOM   1513  N ND2 . ASN A  1 200 ? 5.226   -38.360  -76.878 1.00 94.40  ? 200 ASN A ND2 1 
ATOM   1514  N N   . ALA A  1 201 ? 3.399   -33.036  -76.105 1.00 93.78  ? 201 ALA A N   1 
ATOM   1515  C CA  . ALA A  1 201 ? 2.452   -32.131  -75.465 1.00 91.71  ? 201 ALA A CA  1 
ATOM   1516  C C   . ALA A  1 201 ? 1.101   -32.803  -75.246 1.00 101.20 ? 201 ALA A C   1 
ATOM   1517  O O   . ALA A  1 201 ? 0.480   -32.640  -74.196 1.00 104.96 ? 201 ALA A O   1 
ATOM   1518  C CB  . ALA A  1 201 ? 2.292   -30.862  -76.289 1.00 92.77  ? 201 ALA A CB  1 
ATOM   1519  N N   . ASP A  1 202 ? 0.651   -33.557  -76.243 1.00 102.90 ? 202 ASP A N   1 
ATOM   1520  C CA  . ASP A  1 202 ? -0.622  -34.262  -76.155 1.00 103.50 ? 202 ASP A CA  1 
ATOM   1521  C C   . ASP A  1 202 ? -0.384  -35.757  -75.962 1.00 96.65  ? 202 ASP A C   1 
ATOM   1522  O O   . ASP A  1 202 ? -0.156  -36.487  -76.926 1.00 93.15  ? 202 ASP A O   1 
ATOM   1523  C CB  . ASP A  1 202 ? -1.455  -34.015  -77.414 1.00 119.99 ? 202 ASP A CB  1 
ATOM   1524  C CG  . ASP A  1 202 ? -2.930  -34.288  -77.201 1.00 128.49 ? 202 ASP A CG  1 
ATOM   1525  O OD1 . ASP A  1 202 ? -3.470  -33.865  -76.157 1.00 127.48 ? 202 ASP A OD1 1 
ATOM   1526  O OD2 . ASP A  1 202 ? -3.553  -34.917  -78.082 1.00 124.15 ? 202 ASP A OD2 1 
ATOM   1527  N N   . THR A  1 203 ? -0.440  -36.206  -74.711 1.00 89.24  ? 203 THR A N   1 
ATOM   1528  C CA  . THR A  1 203 ? -0.125  -37.592  -74.375 1.00 77.39  ? 203 THR A CA  1 
ATOM   1529  C C   . THR A  1 203 ? -1.324  -38.336  -73.793 1.00 73.55  ? 203 THR A C   1 
ATOM   1530  O O   . THR A  1 203 ? -2.365  -37.738  -73.521 1.00 77.83  ? 203 THR A O   1 
ATOM   1531  C CB  . THR A  1 203 ? 1.033   -37.667  -73.364 1.00 74.03  ? 203 THR A CB  1 
ATOM   1532  O OG1 . THR A  1 203 ? 0.640   -37.032  -72.142 1.00 66.05  ? 203 THR A OG1 1 
ATOM   1533  C CG2 . THR A  1 203 ? 2.268   -36.974  -73.915 1.00 74.15  ? 203 THR A CG2 1 
ATOM   1534  N N   . TYR A  1 204 ? -1.166  -39.644  -73.597 1.00 72.08  ? 204 TYR A N   1 
ATOM   1535  C CA  . TYR A  1 204 ? -2.226  -40.475  -73.029 1.00 69.59  ? 204 TYR A CA  1 
ATOM   1536  C C   . TYR A  1 204 ? -1.671  -41.730  -72.358 1.00 71.75  ? 204 TYR A C   1 
ATOM   1537  O O   . TYR A  1 204 ? -0.671  -42.293  -72.807 1.00 64.96  ? 204 TYR A O   1 
ATOM   1538  C CB  . TYR A  1 204 ? -3.220  -40.892  -74.115 1.00 68.31  ? 204 TYR A CB  1 
ATOM   1539  C CG  . TYR A  1 204 ? -2.704  -41.990  -75.023 1.00 76.33  ? 204 TYR A CG  1 
ATOM   1540  C CD1 . TYR A  1 204 ? -2.931  -43.329  -74.727 1.00 71.57  ? 204 TYR A CD1 1 
ATOM   1541  C CD2 . TYR A  1 204 ? -1.988  -41.688  -76.174 1.00 79.01  ? 204 TYR A CD2 1 
ATOM   1542  C CE1 . TYR A  1 204 ? -2.460  -44.334  -75.552 1.00 78.50  ? 204 TYR A CE1 1 
ATOM   1543  C CE2 . TYR A  1 204 ? -1.514  -42.687  -77.005 1.00 86.03  ? 204 TYR A CE2 1 
ATOM   1544  C CZ  . TYR A  1 204 ? -1.753  -44.008  -76.689 1.00 88.15  ? 204 TYR A CZ  1 
ATOM   1545  O OH  . TYR A  1 204 ? -1.283  -45.005  -77.512 1.00 90.29  ? 204 TYR A OH  1 
ATOM   1546  N N   . VAL A  1 205 ? -2.334  -42.168  -71.290 1.00 62.37  ? 205 VAL A N   1 
ATOM   1547  C CA  . VAL A  1 205 ? -2.011  -43.436  -70.641 1.00 60.63  ? 205 VAL A CA  1 
ATOM   1548  C C   . VAL A  1 205 ? -3.188  -44.395  -70.761 1.00 61.76  ? 205 VAL A C   1 
ATOM   1549  O O   . VAL A  1 205 ? -4.337  -43.989  -70.615 1.00 63.04  ? 205 VAL A O   1 
ATOM   1550  C CB  . VAL A  1 205 ? -1.737  -43.253  -69.139 1.00 52.22  ? 205 VAL A CB  1 
ATOM   1551  C CG1 . VAL A  1 205 ? -1.182  -44.548  -68.534 1.00 52.26  ? 205 VAL A CG1 1 
ATOM   1552  C CG2 . VAL A  1 205 ? -0.808  -42.070  -68.898 1.00 63.44  ? 205 VAL A CG2 1 
ATOM   1553  N N   . PHE A  1 206 ? -2.908  -45.667  -71.019 1.00 61.10  ? 206 PHE A N   1 
ATOM   1554  C CA  . PHE A  1 206 ? -3.962  -46.677  -71.038 1.00 63.82  ? 206 PHE A CA  1 
ATOM   1555  C C   . PHE A  1 206 ? -3.561  -47.918  -70.239 1.00 69.76  ? 206 PHE A C   1 
ATOM   1556  O O   . PHE A  1 206 ? -2.480  -48.474  -70.434 1.00 70.48  ? 206 PHE A O   1 
ATOM   1557  C CB  . PHE A  1 206 ? -4.341  -47.040  -72.478 1.00 59.37  ? 206 PHE A CB  1 
ATOM   1558  C CG  . PHE A  1 206 ? -5.283  -48.208  -72.587 1.00 72.18  ? 206 PHE A CG  1 
ATOM   1559  C CD1 . PHE A  1 206 ? -4.810  -49.457  -72.948 1.00 67.21  ? 206 PHE A CD1 1 
ATOM   1560  C CD2 . PHE A  1 206 ? -6.639  -48.058  -72.339 1.00 77.42  ? 206 PHE A CD2 1 
ATOM   1561  C CE1 . PHE A  1 206 ? -5.663  -50.536  -73.057 1.00 70.98  ? 206 PHE A CE1 1 
ATOM   1562  C CE2 . PHE A  1 206 ? -7.499  -49.136  -72.445 1.00 66.69  ? 206 PHE A CE2 1 
ATOM   1563  C CZ  . PHE A  1 206 ? -7.009  -50.376  -72.805 1.00 80.00  ? 206 PHE A CZ  1 
ATOM   1564  N N   . VAL A  1 207 ? -4.435  -48.330  -69.324 1.00 56.76  ? 207 VAL A N   1 
ATOM   1565  C CA  . VAL A  1 207 ? -4.212  -49.525  -68.517 1.00 61.96  ? 207 VAL A CA  1 
ATOM   1566  C C   . VAL A  1 207 ? -5.390  -50.478  -68.672 1.00 70.94  ? 207 VAL A C   1 
ATOM   1567  O O   . VAL A  1 207 ? -6.535  -50.105  -68.414 1.00 73.65  ? 207 VAL A O   1 
ATOM   1568  C CB  . VAL A  1 207 ? -4.046  -49.189  -67.023 1.00 53.25  ? 207 VAL A CB  1 
ATOM   1569  C CG1 . VAL A  1 207 ? -3.845  -50.463  -66.218 1.00 42.18  ? 207 VAL A CG1 1 
ATOM   1570  C CG2 . VAL A  1 207 ? -2.883  -48.232  -66.816 1.00 60.02  ? 207 VAL A CG2 1 
ATOM   1571  N N   . GLY A  1 208 ? -5.110  -51.707  -69.093 1.00 66.59  ? 208 GLY A N   1 
ATOM   1572  C CA  . GLY A  1 208 ? -6.167  -52.669  -69.339 1.00 62.07  ? 208 GLY A CA  1 
ATOM   1573  C C   . GLY A  1 208 ? -5.842  -54.100  -68.961 1.00 72.94  ? 208 GLY A C   1 
ATOM   1574  O O   . GLY A  1 208 ? -4.709  -54.556  -69.102 1.00 77.90  ? 208 GLY A O   1 
ATOM   1575  N N   . SER A  1 209 ? -6.854  -54.807  -68.469 1.00 65.84  ? 209 SER A N   1 
ATOM   1576  C CA  . SER A  1 209 ? -6.756  -56.235  -68.203 1.00 67.51  ? 209 SER A CA  1 
ATOM   1577  C C   . SER A  1 209 ? -7.981  -56.912  -68.802 1.00 76.36  ? 209 SER A C   1 
ATOM   1578  O O   . SER A  1 209 ? -8.653  -56.338  -69.658 1.00 80.78  ? 209 SER A O   1 
ATOM   1579  C CB  . SER A  1 209 ? -6.683  -56.506  -66.700 1.00 71.64  ? 209 SER A CB  1 
ATOM   1580  O OG  . SER A  1 209 ? -7.920  -56.227  -66.068 1.00 59.06  ? 209 SER A OG  1 
ATOM   1581  N N   . SER A  1 210 ? -8.277  -58.126  -68.353 1.00 92.33  ? 210 SER A N   1 
ATOM   1582  C CA  . SER A  1 210 ? -9.463  -58.830  -68.826 1.00 97.20  ? 210 SER A CA  1 
ATOM   1583  C C   . SER A  1 210 ? -10.732 -58.125  -68.358 1.00 102.42 ? 210 SER A C   1 
ATOM   1584  O O   . SER A  1 210 ? -11.783 -58.236  -68.987 1.00 86.64  ? 210 SER A O   1 
ATOM   1585  C CB  . SER A  1 210 ? -9.464  -60.282  -68.345 1.00 102.51 ? 210 SER A CB  1 
ATOM   1586  O OG  . SER A  1 210 ? -8.428  -61.025  -68.961 1.00 123.75 ? 210 SER A OG  1 
ATOM   1587  N N   . ARG A  1 211 ? -10.621 -57.394  -67.254 1.00 88.95  ? 211 ARG A N   1 
ATOM   1588  C CA  . ARG A  1 211 ? -11.775 -56.739  -66.650 1.00 94.79  ? 211 ARG A CA  1 
ATOM   1589  C C   . ARG A  1 211 ? -11.610 -55.220  -66.600 1.00 92.53  ? 211 ARG A C   1 
ATOM   1590  O O   . ARG A  1 211 ? -12.573 -54.477  -66.791 1.00 105.34 ? 211 ARG A O   1 
ATOM   1591  C CB  . ARG A  1 211 ? -12.012 -57.292  -65.243 1.00 92.97  ? 211 ARG A CB  1 
ATOM   1592  C CG  . ARG A  1 211 ? -10.894 -56.976  -64.265 1.00 104.77 ? 211 ARG A CG  1 
ATOM   1593  C CD  . ARG A  1 211 ? -10.891 -57.923  -63.077 1.00 125.75 ? 211 ARG A CD  1 
ATOM   1594  N NE  . ARG A  1 211 ? -12.229 -58.135  -62.535 1.00 136.13 ? 211 ARG A NE  1 
ATOM   1595  C CZ  . ARG A  1 211 ? -12.474 -58.669  -61.343 1.00 127.43 ? 211 ARG A CZ  1 
ATOM   1596  N NH1 . ARG A  1 211 ? -11.468 -59.035  -60.560 1.00 115.61 ? 211 ARG A NH1 1 
ATOM   1597  N NH2 . ARG A  1 211 ? -13.723 -58.829  -60.929 1.00 120.07 ? 211 ARG A NH2 1 
ATOM   1598  N N   . TYR A  1 212 ? -10.387 -54.766  -66.345 1.00 86.61  ? 212 TYR A N   1 
ATOM   1599  C CA  . TYR A  1 212 ? -10.103 -53.340  -66.225 1.00 68.29  ? 212 TYR A CA  1 
ATOM   1600  C C   . TYR A  1 212 ? -9.765  -52.732  -67.582 1.00 70.38  ? 212 TYR A C   1 
ATOM   1601  O O   . TYR A  1 212 ? -9.159  -53.386  -68.430 1.00 79.94  ? 212 TYR A O   1 
ATOM   1602  C CB  . TYR A  1 212 ? -8.950  -53.110  -65.244 1.00 60.18  ? 212 TYR A CB  1 
ATOM   1603  C CG  . TYR A  1 212 ? -8.760  -51.666  -64.836 1.00 69.12  ? 212 TYR A CG  1 
ATOM   1604  C CD1 . TYR A  1 212 ? -9.318  -51.177  -63.662 1.00 61.82  ? 212 TYR A CD1 1 
ATOM   1605  C CD2 . TYR A  1 212 ? -8.021  -50.793  -65.623 1.00 71.23  ? 212 TYR A CD2 1 
ATOM   1606  C CE1 . TYR A  1 212 ? -9.146  -49.859  -63.284 1.00 67.59  ? 212 TYR A CE1 1 
ATOM   1607  C CE2 . TYR A  1 212 ? -7.845  -49.472  -65.253 1.00 62.01  ? 212 TYR A CE2 1 
ATOM   1608  C CZ  . TYR A  1 212 ? -8.409  -49.011  -64.083 1.00 65.28  ? 212 TYR A CZ  1 
ATOM   1609  O OH  . TYR A  1 212 ? -8.236  -47.698  -63.710 1.00 59.84  ? 212 TYR A OH  1 
ATOM   1610  N N   . SER A  1 213 ? -10.160 -51.478  -67.783 1.00 56.56  ? 213 SER A N   1 
ATOM   1611  C CA  . SER A  1 213 ? -9.878  -50.780  -69.032 1.00 64.51  ? 213 SER A CA  1 
ATOM   1612  C C   . SER A  1 213 ? -10.175 -49.298  -68.827 1.00 68.95  ? 213 SER A C   1 
ATOM   1613  O O   . SER A  1 213 ? -11.298 -48.923  -68.491 1.00 77.56  ? 213 SER A O   1 
ATOM   1614  C CB  . SER A  1 213 ? -10.671 -51.401  -70.184 1.00 57.86  ? 213 SER A CB  1 
ATOM   1615  O OG  . SER A  1 213 ? -10.338 -50.793  -71.420 1.00 62.70  ? 213 SER A OG  1 
ATOM   1616  N N   . LYS A  1 214 ? -9.165  -48.456  -69.028 1.00 60.26  ? 214 LYS A N   1 
ATOM   1617  C CA  . LYS A  1 214 ? -9.362  -47.015  -68.927 1.00 67.09  ? 214 LYS A CA  1 
ATOM   1618  C C   . LYS A  1 214 ? -8.211  -46.249  -69.569 1.00 77.06  ? 214 LYS A C   1 
ATOM   1619  O O   . LYS A  1 214 ? -7.042  -46.607  -69.417 1.00 66.75  ? 214 LYS A O   1 
ATOM   1620  C CB  . LYS A  1 214 ? -9.603  -46.513  -67.501 1.00 62.77  ? 214 LYS A CB  1 
ATOM   1621  C CG  . LYS A  1 214 ? -9.977  -45.039  -67.432 1.00 73.35  ? 214 LYS A CG  1 
ATOM   1622  C CD  . LYS A  1 214 ? -11.073 -44.791  -66.408 1.00 85.72  ? 214 LYS A CD  1 
ATOM   1623  C CE  . LYS A  1 214 ? -10.515 -44.238  -65.108 1.00 90.97  ? 214 LYS A CE  1 
ATOM   1624  N NZ  . LYS A  1 214 ? -10.040 -42.834  -65.259 1.00 90.26  ? 214 LYS A NZ  1 
ATOM   1625  N N   . LYS A  1 215 ? -8.562  -45.190  -70.291 1.00 68.28  ? 215 LYS A N   1 
ATOM   1626  C CA  . LYS A  1 215 ? -7.588  -44.326  -70.939 1.00 67.66  ? 215 LYS A CA  1 
ATOM   1627  C C   . LYS A  1 215 ? -7.500  -43.010  -70.176 1.00 65.20  ? 215 LYS A C   1 
ATOM   1628  O O   . LYS A  1 215 ? -8.519  -42.391  -69.873 1.00 71.24  ? 215 LYS A O   1 
ATOM   1629  C CB  . LYS A  1 215 ? -7.997  -44.073  -72.390 1.00 72.71  ? 215 LYS A CB  1 
ATOM   1630  C CG  . LYS A  1 215 ? -6.976  -43.311  -73.213 1.00 74.93  ? 215 LYS A CG  1 
ATOM   1631  C CD  . LYS A  1 215 ? -7.420  -43.204  -74.663 1.00 81.50  ? 215 LYS A CD  1 
ATOM   1632  C CE  . LYS A  1 215 ? -6.296  -42.684  -75.543 1.00 99.95  ? 215 LYS A CE  1 
ATOM   1633  N NZ  . LYS A  1 215 ? -6.697  -42.596  -76.976 1.00 90.32  ? 215 LYS A NZ  1 
ATOM   1634  N N   . PHE A  1 216 ? -6.280  -42.588  -69.862 1.00 61.88  ? 216 PHE A N   1 
ATOM   1635  C CA  . PHE A  1 216 ? -6.071  -41.389  -69.061 1.00 62.30  ? 216 PHE A CA  1 
ATOM   1636  C C   . PHE A  1 216 ? -5.522  -40.232  -69.886 1.00 63.07  ? 216 PHE A C   1 
ATOM   1637  O O   . PHE A  1 216 ? -4.595  -40.400  -70.679 1.00 69.14  ? 216 PHE A O   1 
ATOM   1638  C CB  . PHE A  1 216 ? -5.126  -41.682  -67.894 1.00 70.94  ? 216 PHE A CB  1 
ATOM   1639  C CG  . PHE A  1 216 ? -5.586  -42.804  -67.009 1.00 67.42  ? 216 PHE A CG  1 
ATOM   1640  C CD1 . PHE A  1 216 ? -5.195  -44.108  -67.263 1.00 67.33  ? 216 PHE A CD1 1 
ATOM   1641  C CD2 . PHE A  1 216 ? -6.409  -42.556  -65.923 1.00 61.66  ? 216 PHE A CD2 1 
ATOM   1642  C CE1 . PHE A  1 216 ? -5.616  -45.144  -66.451 1.00 64.66  ? 216 PHE A CE1 1 
ATOM   1643  C CE2 . PHE A  1 216 ? -6.833  -43.588  -65.107 1.00 73.54  ? 216 PHE A CE2 1 
ATOM   1644  C CZ  . PHE A  1 216 ? -6.436  -44.883  -65.372 1.00 63.86  ? 216 PHE A CZ  1 
ATOM   1645  N N   . LYS A  1 217 ? -6.106  -39.055  -69.691 1.00 67.39  ? 217 LYS A N   1 
ATOM   1646  C CA  . LYS A  1 217 ? -5.604  -37.834  -70.304 1.00 63.75  ? 217 LYS A CA  1 
ATOM   1647  C C   . LYS A  1 217 ? -5.065  -36.899  -69.230 1.00 68.33  ? 217 LYS A C   1 
ATOM   1648  O O   . LYS A  1 217 ? -5.800  -36.492  -68.330 1.00 68.74  ? 217 LYS A O   1 
ATOM   1649  C CB  . LYS A  1 217 ? -6.705  -37.140  -71.108 1.00 74.46  ? 217 LYS A CB  1 
ATOM   1650  C CG  . LYS A  1 217 ? -6.666  -37.434  -72.598 1.00 76.52  ? 217 LYS A CG  1 
ATOM   1651  C CD  . LYS A  1 217 ? -5.400  -36.877  -73.232 1.00 90.45  ? 217 LYS A CD  1 
ATOM   1652  C CE  . LYS A  1 217 ? -5.378  -37.116  -74.733 1.00 97.26  ? 217 LYS A CE  1 
ATOM   1653  N NZ  . LYS A  1 217 ? -4.168  -36.527  -75.370 1.00 107.46 ? 217 LYS A NZ  1 
ATOM   1654  N N   . PRO A  1 218 ? -3.770  -36.564  -69.316 1.00 73.81  ? 218 PRO A N   1 
ATOM   1655  C CA  . PRO A  1 218 ? -3.125  -35.669  -68.350 1.00 69.74  ? 218 PRO A CA  1 
ATOM   1656  C C   . PRO A  1 218 ? -3.824  -34.315  -68.271 1.00 72.77  ? 218 PRO A C   1 
ATOM   1657  O O   . PRO A  1 218 ? -4.023  -33.660  -69.293 1.00 62.08  ? 218 PRO A O   1 
ATOM   1658  C CB  . PRO A  1 218 ? -1.714  -35.502  -68.919 1.00 65.57  ? 218 PRO A CB  1 
ATOM   1659  C CG  . PRO A  1 218 ? -1.488  -36.729  -69.733 1.00 69.86  ? 218 PRO A CG  1 
ATOM   1660  C CD  . PRO A  1 218 ? -2.823  -37.063  -70.327 1.00 74.03  ? 218 PRO A CD  1 
ATOM   1661  N N   . GLU A  1 219 ? -4.193  -33.908  -67.061 1.00 73.74  ? 219 GLU A N   1 
ATOM   1662  C CA  . GLU A  1 219 ? -4.842  -32.622  -66.846 1.00 58.86  ? 219 GLU A CA  1 
ATOM   1663  C C   . GLU A  1 219 ? -3.823  -31.598  -66.363 1.00 62.92  ? 219 GLU A C   1 
ATOM   1664  O O   . GLU A  1 219 ? -3.522  -31.521  -65.173 1.00 59.90  ? 219 GLU A O   1 
ATOM   1665  C CB  . GLU A  1 219 ? -5.979  -32.762  -65.834 1.00 57.32  ? 219 GLU A CB  1 
ATOM   1666  C CG  . GLU A  1 219 ? -7.015  -33.807  -66.216 1.00 71.15  ? 219 GLU A CG  1 
ATOM   1667  C CD  . GLU A  1 219 ? -8.127  -33.932  -65.193 1.00 81.54  ? 219 GLU A CD  1 
ATOM   1668  O OE1 . GLU A  1 219 ? -8.029  -33.295  -64.123 1.00 67.66  ? 219 GLU A OE1 1 
ATOM   1669  O OE2 . GLU A  1 219 ? -9.100  -34.668  -65.460 1.00 84.48  ? 219 GLU A OE2 1 
ATOM   1670  N N   . ILE A  1 220 ? -3.296  -30.814  -67.296 1.00 71.08  ? 220 ILE A N   1 
ATOM   1671  C CA  . ILE A  1 220 ? -2.234  -29.860  -66.994 1.00 67.43  ? 220 ILE A CA  1 
ATOM   1672  C C   . ILE A  1 220 ? -2.777  -28.519  -66.508 1.00 61.10  ? 220 ILE A C   1 
ATOM   1673  O O   . ILE A  1 220 ? -3.502  -27.834  -67.229 1.00 62.96  ? 220 ILE A O   1 
ATOM   1674  C CB  . ILE A  1 220 ? -1.337  -29.631  -68.223 1.00 60.24  ? 220 ILE A CB  1 
ATOM   1675  C CG1 . ILE A  1 220 ? -0.742  -30.959  -68.695 1.00 61.38  ? 220 ILE A CG1 1 
ATOM   1676  C CG2 . ILE A  1 220 ? -0.241  -28.627  -67.903 1.00 66.64  ? 220 ILE A CG2 1 
ATOM   1677  C CD1 . ILE A  1 220 ? -0.085  -30.888  -70.055 1.00 83.87  ? 220 ILE A CD1 1 
ATOM   1678  N N   . ALA A  1 221 ? -2.414  -28.150  -65.282 1.00 57.65  ? 221 ALA A N   1 
ATOM   1679  C CA  . ALA A  1 221 ? -2.855  -26.891  -64.691 1.00 55.28  ? 221 ALA A CA  1 
ATOM   1680  C C   . ALA A  1 221 ? -2.129  -26.614  -63.377 1.00 68.28  ? 221 ALA A C   1 
ATOM   1681  O O   . ALA A  1 221 ? -1.399  -27.465  -62.869 1.00 66.97  ? 221 ALA A O   1 
ATOM   1682  C CB  . ALA A  1 221 ? -4.360  -26.903  -64.474 1.00 52.84  ? 221 ALA A CB  1 
ATOM   1683  N N   . ILE A  1 222 ? -2.337  -25.420  -62.831 1.00 76.72  ? 222 ILE A N   1 
ATOM   1684  C CA  . ILE A  1 222 ? -1.685  -25.022  -61.587 1.00 75.86  ? 222 ILE A CA  1 
ATOM   1685  C C   . ILE A  1 222 ? -2.588  -25.234  -60.375 1.00 70.79  ? 222 ILE A C   1 
ATOM   1686  O O   . ILE A  1 222 ? -3.595  -24.544  -60.211 1.00 78.99  ? 222 ILE A O   1 
ATOM   1687  C CB  . ILE A  1 222 ? -1.246  -23.545  -61.627 1.00 83.87  ? 222 ILE A CB  1 
ATOM   1688  C CG1 . ILE A  1 222 ? -0.286  -23.304  -62.793 1.00 80.81  ? 222 ILE A CG1 1 
ATOM   1689  C CG2 . ILE A  1 222 ? -0.597  -23.148  -60.310 1.00 55.77  ? 222 ILE A CG2 1 
ATOM   1690  C CD1 . ILE A  1 222 ? 0.993   -24.104  -62.703 1.00 81.91  ? 222 ILE A CD1 1 
ATOM   1691  N N   . ARG A  1 223 ? -2.222  -26.192  -59.530 1.00 60.75  ? 223 ARG A N   1 
ATOM   1692  C CA  . ARG A  1 223 ? -2.943  -26.435  -58.286 1.00 67.96  ? 223 ARG A CA  1 
ATOM   1693  C C   . ARG A  1 223 ? -2.249  -25.734  -57.124 1.00 70.63  ? 223 ARG A C   1 
ATOM   1694  O O   . ARG A  1 223 ? -1.031  -25.557  -57.143 1.00 74.28  ? 223 ARG A O   1 
ATOM   1695  C CB  . ARG A  1 223 ? -3.034  -27.934  -57.992 1.00 63.04  ? 223 ARG A CB  1 
ATOM   1696  C CG  . ARG A  1 223 ? -3.932  -28.726  -58.928 1.00 60.29  ? 223 ARG A CG  1 
ATOM   1697  C CD  . ARG A  1 223 ? -3.205  -29.156  -60.191 1.00 56.02  ? 223 ARG A CD  1 
ATOM   1698  N NE  . ARG A  1 223 ? -3.935  -30.208  -60.892 1.00 53.35  ? 223 ARG A NE  1 
ATOM   1699  C CZ  . ARG A  1 223 ? -3.546  -30.756  -62.038 1.00 56.42  ? 223 ARG A CZ  1 
ATOM   1700  N NH1 . ARG A  1 223 ? -2.428  -30.351  -62.625 1.00 61.79  ? 223 ARG A NH1 1 
ATOM   1701  N NH2 . ARG A  1 223 ? -4.277  -31.710  -62.598 1.00 55.89  ? 223 ARG A NH2 1 
ATOM   1702  N N   . PRO A  1 224 ? -3.026  -25.333  -56.107 1.00 67.17  ? 224 PRO A N   1 
ATOM   1703  C CA  . PRO A  1 224 ? -2.460  -24.728  -54.897 1.00 69.62  ? 224 PRO A CA  1 
ATOM   1704  C C   . PRO A  1 224 ? -1.371  -25.615  -54.309 1.00 72.54  ? 224 PRO A C   1 
ATOM   1705  O O   . PRO A  1 224 ? -1.590  -26.810  -54.110 1.00 67.29  ? 224 PRO A O   1 
ATOM   1706  C CB  . PRO A  1 224 ? -3.658  -24.662  -53.950 1.00 60.47  ? 224 PRO A CB  1 
ATOM   1707  C CG  . PRO A  1 224 ? -4.833  -24.558  -54.855 1.00 77.87  ? 224 PRO A CG  1 
ATOM   1708  C CD  . PRO A  1 224 ? -4.497  -25.395  -56.056 1.00 70.15  ? 224 PRO A CD  1 
ATOM   1709  N N   . LYS A  1 225 ? -0.210  -25.029  -54.036 1.00 88.19  ? 225 LYS A N   1 
ATOM   1710  C CA  . LYS A  1 225 ? 0.948   -25.789  -53.583 1.00 87.52  ? 225 LYS A CA  1 
ATOM   1711  C C   . LYS A  1 225 ? 0.681   -26.637  -52.345 1.00 87.26  ? 225 LYS A C   1 
ATOM   1712  O O   . LYS A  1 225 ? 0.297   -26.127  -51.292 1.00 86.47  ? 225 LYS A O   1 
ATOM   1713  C CB  . LYS A  1 225 ? 2.139   -24.861  -53.332 1.00 97.89  ? 225 LYS A CB  1 
ATOM   1714  C CG  . LYS A  1 225 ? 2.747   -24.280  -54.595 1.00 117.15 ? 225 LYS A CG  1 
ATOM   1715  C CD  . LYS A  1 225 ? 3.941   -23.400  -54.274 1.00 129.32 ? 225 LYS A CD  1 
ATOM   1716  C CE  . LYS A  1 225 ? 4.575   -22.844  -55.537 1.00 142.52 ? 225 LYS A CE  1 
ATOM   1717  N NZ  . LYS A  1 225 ? 5.028   -23.928  -56.452 1.00 145.56 ? 225 LYS A NZ  1 
ATOM   1718  N N   . VAL A  1 226 ? 0.885   -27.941  -52.492 1.00 70.89  ? 226 VAL A N   1 
ATOM   1719  C CA  . VAL A  1 226 ? 0.889   -28.860  -51.367 1.00 70.97  ? 226 VAL A CA  1 
ATOM   1720  C C   . VAL A  1 226 ? 2.226   -29.583  -51.390 1.00 74.01  ? 226 VAL A C   1 
ATOM   1721  O O   . VAL A  1 226 ? 2.491   -30.378  -52.288 1.00 75.56  ? 226 VAL A O   1 
ATOM   1722  C CB  . VAL A  1 226 ? -0.254  -29.886  -51.459 1.00 69.11  ? 226 VAL A CB  1 
ATOM   1723  C CG1 . VAL A  1 226 ? -0.202  -30.844  -50.279 1.00 61.64  ? 226 VAL A CG1 1 
ATOM   1724  C CG2 . VAL A  1 226 ? -1.599  -29.178  -51.515 1.00 67.14  ? 226 VAL A CG2 1 
ATOM   1725  N N   . ARG A  1 227 ? 3.078   -29.287  -50.415 1.00 85.29  ? 227 ARG A N   1 
ATOM   1726  C CA  . ARG A  1 227 ? 4.423   -29.848  -50.384 1.00 75.36  ? 227 ARG A CA  1 
ATOM   1727  C C   . ARG A  1 227 ? 5.241   -29.394  -51.591 1.00 80.37  ? 227 ARG A C   1 
ATOM   1728  O O   . ARG A  1 227 ? 5.963   -30.188  -52.195 1.00 74.49  ? 227 ARG A O   1 
ATOM   1729  C CB  . ARG A  1 227 ? 4.372   -31.376  -50.324 1.00 66.33  ? 227 ARG A CB  1 
ATOM   1730  C CG  . ARG A  1 227 ? 3.806   -31.933  -49.029 1.00 67.69  ? 227 ARG A CG  1 
ATOM   1731  C CD  . ARG A  1 227 ? 3.584   -33.431  -49.135 1.00 74.23  ? 227 ARG A CD  1 
ATOM   1732  N NE  . ARG A  1 227 ? 4.125   -34.157  -47.990 1.00 68.12  ? 227 ARG A NE  1 
ATOM   1733  C CZ  . ARG A  1 227 ? 5.405   -34.486  -47.858 1.00 81.23  ? 227 ARG A CZ  1 
ATOM   1734  N NH1 . ARG A  1 227 ? 6.275   -34.143  -48.796 1.00 88.40  ? 227 ARG A NH1 1 
ATOM   1735  N NH2 . ARG A  1 227 ? 5.818   -35.150  -46.786 1.00 74.09  ? 227 ARG A NH2 1 
ATOM   1736  N N   . ASP A  1 228 ? 5.107   -28.117  -51.943 1.00 90.91  ? 228 ASP A N   1 
ATOM   1737  C CA  . ASP A  1 228 ? 5.921   -27.501  -52.991 1.00 98.17  ? 228 ASP A CA  1 
ATOM   1738  C C   . ASP A  1 228 ? 5.501   -27.860  -54.415 1.00 99.46  ? 228 ASP A C   1 
ATOM   1739  O O   . ASP A  1 228 ? 6.010   -27.287  -55.378 1.00 110.01 ? 228 ASP A O   1 
ATOM   1740  C CB  . ASP A  1 228 ? 7.402   -27.832  -52.787 1.00 122.58 ? 228 ASP A CB  1 
ATOM   1741  C CG  . ASP A  1 228 ? 8.147   -26.739  -52.053 1.00 150.52 ? 228 ASP A CG  1 
ATOM   1742  O OD1 . ASP A  1 228 ? 8.343   -25.661  -52.646 1.00 152.09 ? 228 ASP A OD1 1 
ATOM   1743  O OD2 . ASP A  1 228 ? 8.545   -26.959  -50.890 1.00 161.78 ? 228 ASP A OD2 1 
ATOM   1744  N N   . GLN A  1 229 ? 4.575   -28.804  -54.551 1.00 85.11  ? 229 GLN A N   1 
ATOM   1745  C CA  . GLN A  1 229 ? 4.150   -29.255  -55.871 1.00 81.32  ? 229 GLN A CA  1 
ATOM   1746  C C   . GLN A  1 229 ? 2.848   -28.590  -56.306 1.00 75.23  ? 229 GLN A C   1 
ATOM   1747  O O   . GLN A  1 229 ? 1.835   -28.674  -55.612 1.00 80.86  ? 229 GLN A O   1 
ATOM   1748  C CB  . GLN A  1 229 ? 3.993   -30.777  -55.892 1.00 75.94  ? 229 GLN A CB  1 
ATOM   1749  C CG  . GLN A  1 229 ? 5.141   -31.531  -55.237 1.00 68.29  ? 229 GLN A CG  1 
ATOM   1750  C CD  . GLN A  1 229 ? 6.483   -31.224  -55.871 1.00 73.03  ? 229 GLN A CD  1 
ATOM   1751  O OE1 . GLN A  1 229 ? 6.577   -30.991  -57.076 1.00 68.58  ? 229 GLN A OE1 1 
ATOM   1752  N NE2 . GLN A  1 229 ? 7.534   -31.228  -55.059 1.00 89.02  ? 229 GLN A NE2 1 
ATOM   1753  N N   . GLU A  1 230 ? 2.884   -27.924  -57.456 1.00 75.78  ? 230 GLU A N   1 
ATOM   1754  C CA  . GLU A  1 230 ? 1.685   -27.331  -58.037 1.00 74.73  ? 230 GLU A CA  1 
ATOM   1755  C C   . GLU A  1 230 ? 1.017   -28.338  -58.963 1.00 75.11  ? 230 GLU A C   1 
ATOM   1756  O O   . GLU A  1 230 ? -0.105  -28.131  -59.425 1.00 79.54  ? 230 GLU A O   1 
ATOM   1757  C CB  . GLU A  1 230 ? 2.028   -26.053  -58.804 1.00 83.61  ? 230 GLU A CB  1 
ATOM   1758  N N   . GLY A  1 231 ? 1.725   -29.429  -59.235 1.00 56.73  ? 231 GLY A N   1 
ATOM   1759  C CA  . GLY A  1 231 ? 1.182   -30.515  -60.027 1.00 61.91  ? 231 GLY A CA  1 
ATOM   1760  C C   . GLY A  1 231 ? 0.577   -31.576  -59.130 1.00 67.27  ? 231 GLY A C   1 
ATOM   1761  O O   . GLY A  1 231 ? 0.776   -31.559  -57.916 1.00 59.97  ? 231 GLY A O   1 
ATOM   1762  N N   . ARG A  1 232 ? -0.168  -32.500  -59.726 1.00 63.35  ? 232 ARG A N   1 
ATOM   1763  C CA  . ARG A  1 232 ? -0.805  -33.568  -58.966 1.00 57.67  ? 232 ARG A CA  1 
ATOM   1764  C C   . ARG A  1 232 ? -0.410  -34.938  -59.498 1.00 58.84  ? 232 ARG A C   1 
ATOM   1765  O O   . ARG A  1 232 ? 0.114   -35.060  -60.605 1.00 54.06  ? 232 ARG A O   1 
ATOM   1766  C CB  . ARG A  1 232 ? -2.327  -33.415  -58.992 1.00 60.81  ? 232 ARG A CB  1 
ATOM   1767  C CG  . ARG A  1 232 ? -2.849  -32.247  -58.174 1.00 57.93  ? 232 ARG A CG  1 
ATOM   1768  C CD  . ARG A  1 232 ? -2.529  -32.427  -56.700 1.00 53.51  ? 232 ARG A CD  1 
ATOM   1769  N NE  . ARG A  1 232 ? -2.991  -31.298  -55.899 1.00 63.64  ? 232 ARG A NE  1 
ATOM   1770  C CZ  . ARG A  1 232 ? -2.286  -30.191  -55.699 1.00 67.97  ? 232 ARG A CZ  1 
ATOM   1771  N NH1 . ARG A  1 232 ? -1.085  -30.060  -56.247 1.00 59.32  ? 232 ARG A NH1 1 
ATOM   1772  N NH2 . ARG A  1 232 ? -2.781  -29.211  -54.955 1.00 69.14  ? 232 ARG A NH2 1 
ATOM   1773  N N   . MET A  1 233 ? -0.665  -35.968  -58.699 1.00 63.08  ? 233 MET A N   1 
ATOM   1774  C CA  . MET A  1 233 ? -0.396  -37.339  -59.109 1.00 60.18  ? 233 MET A CA  1 
ATOM   1775  C C   . MET A  1 233 ? -1.475  -38.270  -58.570 1.00 53.00  ? 233 MET A C   1 
ATOM   1776  O O   . MET A  1 233 ? -1.548  -38.523  -57.369 1.00 49.35  ? 233 MET A O   1 
ATOM   1777  C CB  . MET A  1 233 ? 0.986   -37.786  -58.628 1.00 53.17  ? 233 MET A CB  1 
ATOM   1778  C CG  . MET A  1 233 ? 1.416   -39.145  -59.155 1.00 57.81  ? 233 MET A CG  1 
ATOM   1779  S SD  . MET A  1 233 ? 3.100   -39.586  -58.681 1.00 76.69  ? 233 MET A SD  1 
ATOM   1780  C CE  . MET A  1 233 ? 4.040   -38.315  -59.525 1.00 64.29  ? 233 MET A CE  1 
ATOM   1781  N N   . ASN A  1 234 ? -2.321  -38.766  -59.467 1.00 53.86  ? 234 ASN A N   1 
ATOM   1782  C CA  . ASN A  1 234 ? -3.391  -39.677  -59.082 1.00 53.33  ? 234 ASN A CA  1 
ATOM   1783  C C   . ASN A  1 234 ? -2.914  -41.123  -59.036 1.00 47.56  ? 234 ASN A C   1 
ATOM   1784  O O   . ASN A  1 234 ? -2.182  -41.575  -59.917 1.00 44.95  ? 234 ASN A O   1 
ATOM   1785  C CB  . ASN A  1 234 ? -4.586  -39.539  -60.027 1.00 44.13  ? 234 ASN A CB  1 
ATOM   1786  C CG  . ASN A  1 234 ? -5.283  -38.201  -59.891 1.00 45.00  ? 234 ASN A CG  1 
ATOM   1787  O OD1 . ASN A  1 234 ? -4.928  -37.387  -59.039 1.00 49.63  ? 234 ASN A OD1 1 
ATOM   1788  N ND2 . ASN A  1 234 ? -6.283  -37.967  -60.732 1.00 59.69  ? 234 ASN A ND2 1 
ATOM   1789  N N   . TYR A  1 235 ? -3.333  -41.844  -58.002 1.00 36.94  ? 235 TYR A N   1 
ATOM   1790  C CA  . TYR A  1 235 ? -2.897  -43.219  -57.803 1.00 39.15  ? 235 TYR A CA  1 
ATOM   1791  C C   . TYR A  1 235 ? -4.028  -44.202  -58.069 1.00 43.88  ? 235 TYR A C   1 
ATOM   1792  O O   . TYR A  1 235 ? -5.132  -44.055  -57.543 1.00 47.96  ? 235 TYR A O   1 
ATOM   1793  C CB  . TYR A  1 235 ? -2.346  -43.401  -56.388 1.00 44.02  ? 235 TYR A CB  1 
ATOM   1794  C CG  . TYR A  1 235 ? -1.292  -42.379  -56.030 1.00 56.52  ? 235 TYR A CG  1 
ATOM   1795  C CD1 . TYR A  1 235 ? -1.630  -41.214  -55.355 1.00 48.86  ? 235 TYR A CD1 1 
ATOM   1796  C CD2 . TYR A  1 235 ? 0.037   -42.569  -56.385 1.00 44.45  ? 235 TYR A CD2 1 
ATOM   1797  C CE1 . TYR A  1 235 ? -0.673  -40.272  -55.033 1.00 52.90  ? 235 TYR A CE1 1 
ATOM   1798  C CE2 . TYR A  1 235 ? 1.002   -41.633  -56.067 1.00 47.65  ? 235 TYR A CE2 1 
ATOM   1799  C CZ  . TYR A  1 235 ? 0.642   -40.486  -55.391 1.00 53.69  ? 235 TYR A CZ  1 
ATOM   1800  O OH  . TYR A  1 235 ? 1.599   -39.550  -55.073 1.00 47.66  ? 235 TYR A OH  1 
ATOM   1801  N N   . TYR A  1 236 ? -3.743  -45.202  -58.894 1.00 41.95  ? 236 TYR A N   1 
ATOM   1802  C CA  . TYR A  1 236 ? -4.739  -46.198  -59.262 1.00 47.02  ? 236 TYR A CA  1 
ATOM   1803  C C   . TYR A  1 236 ? -4.263  -47.600  -58.909 1.00 53.39  ? 236 TYR A C   1 
ATOM   1804  O O   . TYR A  1 236 ? -3.064  -47.847  -58.780 1.00 50.41  ? 236 TYR A O   1 
ATOM   1805  C CB  . TYR A  1 236 ? -5.051  -46.110  -60.756 1.00 37.68  ? 236 TYR A CB  1 
ATOM   1806  C CG  . TYR A  1 236 ? -5.665  -44.794  -61.174 1.00 53.89  ? 236 TYR A CG  1 
ATOM   1807  C CD1 . TYR A  1 236 ? -4.869  -43.692  -61.456 1.00 49.88  ? 236 TYR A CD1 1 
ATOM   1808  C CD2 . TYR A  1 236 ? -7.041  -44.654  -61.288 1.00 54.32  ? 236 TYR A CD2 1 
ATOM   1809  C CE1 . TYR A  1 236 ? -5.427  -42.487  -61.838 1.00 54.40  ? 236 TYR A CE1 1 
ATOM   1810  C CE2 . TYR A  1 236 ? -7.608  -43.454  -61.670 1.00 56.70  ? 236 TYR A CE2 1 
ATOM   1811  C CZ  . TYR A  1 236 ? -6.798  -42.374  -61.942 1.00 56.47  ? 236 TYR A CZ  1 
ATOM   1812  O OH  . TYR A  1 236 ? -7.360  -41.177  -62.322 1.00 52.45  ? 236 TYR A OH  1 
ATOM   1813  N N   . TRP A  1 237 ? -5.211  -48.516  -58.754 1.00 51.98  ? 237 TRP A N   1 
ATOM   1814  C CA  . TRP A  1 237 ? -4.886  -49.896  -58.432 1.00 40.46  ? 237 TRP A CA  1 
ATOM   1815  C C   . TRP A  1 237 ? -5.928  -50.845  -58.996 1.00 38.09  ? 237 TRP A C   1 
ATOM   1816  O O   . TRP A  1 237 ? -7.027  -50.432  -59.366 1.00 49.61  ? 237 TRP A O   1 
ATOM   1817  C CB  . TRP A  1 237 ? -4.785  -50.088  -56.920 1.00 38.48  ? 237 TRP A CB  1 
ATOM   1818  C CG  . TRP A  1 237 ? -6.075  -49.853  -56.198 1.00 42.27  ? 237 TRP A CG  1 
ATOM   1819  C CD1 . TRP A  1 237 ? -6.520  -48.672  -55.681 1.00 44.59  ? 237 TRP A CD1 1 
ATOM   1820  C CD2 . TRP A  1 237 ? -7.087  -50.825  -55.905 1.00 48.25  ? 237 TRP A CD2 1 
ATOM   1821  N NE1 . TRP A  1 237 ? -7.745  -48.846  -55.085 1.00 44.03  ? 237 TRP A NE1 1 
ATOM   1822  C CE2 . TRP A  1 237 ? -8.116  -50.159  -55.209 1.00 47.27  ? 237 TRP A CE2 1 
ATOM   1823  C CE3 . TRP A  1 237 ? -7.223  -52.193  -56.164 1.00 54.90  ? 237 TRP A CE3 1 
ATOM   1824  C CZ2 . TRP A  1 237 ? -9.265  -50.814  -54.769 1.00 51.32  ? 237 TRP A CZ2 1 
ATOM   1825  C CZ3 . TRP A  1 237 ? -8.365  -52.841  -55.726 1.00 56.61  ? 237 TRP A CZ3 1 
ATOM   1826  C CH2 . TRP A  1 237 ? -9.371  -52.151  -55.036 1.00 51.41  ? 237 TRP A CH2 1 
ATOM   1827  N N   . THR A  1 238 ? -5.574  -52.122  -59.052 1.00 45.96  ? 238 THR A N   1 
ATOM   1828  C CA  . THR A  1 238 ? -6.479  -53.144  -59.545 1.00 48.75  ? 238 THR A CA  1 
ATOM   1829  C C   . THR A  1 238 ? -5.958  -54.524  -59.167 1.00 49.92  ? 238 THR A C   1 
ATOM   1830  O O   . THR A  1 238 ? -4.775  -54.694  -58.869 1.00 50.11  ? 238 THR A O   1 
ATOM   1831  C CB  . THR A  1 238 ? -6.650  -53.059  -61.073 1.00 51.98  ? 238 THR A CB  1 
ATOM   1832  O OG1 . THR A  1 238 ? -7.677  -53.965  -61.493 1.00 57.50  ? 238 THR A OG1 1 
ATOM   1833  C CG2 . THR A  1 238 ? -5.350  -53.409  -61.775 1.00 47.64  ? 238 THR A CG2 1 
ATOM   1834  N N   . LEU A  1 239 ? -6.854  -55.504  -59.171 1.00 60.57  ? 239 LEU A N   1 
ATOM   1835  C CA  . LEU A  1 239 ? -6.501  -56.878  -58.844 1.00 63.07  ? 239 LEU A CA  1 
ATOM   1836  C C   . LEU A  1 239 ? -6.616  -57.761  -60.077 1.00 62.11  ? 239 LEU A C   1 
ATOM   1837  O O   . LEU A  1 239 ? -7.719  -58.107  -60.494 1.00 73.62  ? 239 LEU A O   1 
ATOM   1838  C CB  . LEU A  1 239 ? -7.419  -57.415  -57.744 1.00 59.11  ? 239 LEU A CB  1 
ATOM   1839  C CG  . LEU A  1 239 ? -7.318  -56.746  -56.373 1.00 44.69  ? 239 LEU A CG  1 
ATOM   1840  C CD1 . LEU A  1 239 ? -8.380  -57.284  -55.430 1.00 59.83  ? 239 LEU A CD1 1 
ATOM   1841  C CD2 . LEU A  1 239 ? -5.933  -56.955  -55.796 1.00 50.72  ? 239 LEU A CD2 1 
ATOM   1842  N N   . VAL A  1 240 ? -5.479  -58.124  -60.660 1.00 60.93  ? 240 VAL A N   1 
ATOM   1843  C CA  . VAL A  1 240 ? -5.485  -58.989  -61.833 1.00 69.43  ? 240 VAL A CA  1 
ATOM   1844  C C   . VAL A  1 240 ? -5.551  -60.459  -61.449 1.00 61.45  ? 240 VAL A C   1 
ATOM   1845  O O   . VAL A  1 240 ? -4.715  -60.955  -60.697 1.00 57.14  ? 240 VAL A O   1 
ATOM   1846  C CB  . VAL A  1 240 ? -4.289  -58.720  -62.768 1.00 64.04  ? 240 VAL A CB  1 
ATOM   1847  C CG1 . VAL A  1 240 ? -3.271  -57.814  -62.088 1.00 58.10  ? 240 VAL A CG1 1 
ATOM   1848  C CG2 . VAL A  1 240 ? -3.670  -60.031  -63.235 1.00 68.00  ? 240 VAL A CG2 1 
ATOM   1849  N N   . GLU A  1 241 ? -6.556  -61.142  -61.985 1.00 69.36  ? 241 GLU A N   1 
ATOM   1850  C CA  . GLU A  1 241 ? -6.821  -62.539  -61.670 1.00 67.54  ? 241 GLU A CA  1 
ATOM   1851  C C   . GLU A  1 241 ? -5.689  -63.461  -62.112 1.00 72.65  ? 241 GLU A C   1 
ATOM   1852  O O   . GLU A  1 241 ? -4.946  -63.140  -63.039 1.00 78.85  ? 241 GLU A O   1 
ATOM   1853  C CB  . GLU A  1 241 ? -8.124  -62.972  -62.342 1.00 83.93  ? 241 GLU A CB  1 
ATOM   1854  C CG  . GLU A  1 241 ? -9.322  -62.112  -61.976 1.00 100.86 ? 241 GLU A CG  1 
ATOM   1855  C CD  . GLU A  1 241 ? -9.845  -62.413  -60.589 1.00 121.98 ? 241 GLU A CD  1 
ATOM   1856  O OE1 . GLU A  1 241 ? -10.402 -61.500  -59.946 1.00 128.42 ? 241 GLU A OE1 1 
ATOM   1857  O OE2 . GLU A  1 241 ? -9.694  -63.568  -60.141 1.00 130.70 ? 241 GLU A OE2 1 
ATOM   1858  N N   . PRO A  1 242 ? -5.554  -64.617  -61.443 1.00 86.45  ? 242 PRO A N   1 
ATOM   1859  C CA  . PRO A  1 242 ? -4.586  -65.636  -61.859 1.00 87.39  ? 242 PRO A CA  1 
ATOM   1860  C C   . PRO A  1 242 ? -4.827  -66.049  -63.306 1.00 84.97  ? 242 PRO A C   1 
ATOM   1861  O O   . PRO A  1 242 ? -5.957  -66.376  -63.666 1.00 70.46  ? 242 PRO A O   1 
ATOM   1862  C CB  . PRO A  1 242 ? -4.892  -66.809  -60.924 1.00 67.18  ? 242 PRO A CB  1 
ATOM   1863  C CG  . PRO A  1 242 ? -5.484  -66.181  -59.716 1.00 71.28  ? 242 PRO A CG  1 
ATOM   1864  C CD  . PRO A  1 242 ? -6.269  -65.003  -60.215 1.00 75.82  ? 242 PRO A CD  1 
ATOM   1865  N N   . GLY A  1 243 ? -3.778  -66.029  -64.121 1.00 77.71  ? 243 GLY A N   1 
ATOM   1866  C CA  . GLY A  1 243 ? -3.897  -66.384  -65.523 1.00 80.08  ? 243 GLY A CA  1 
ATOM   1867  C C   . GLY A  1 243 ? -4.312  -65.209  -66.388 1.00 78.07  ? 243 GLY A C   1 
ATOM   1868  O O   . GLY A  1 243 ? -4.396  -65.323  -67.611 1.00 82.40  ? 243 GLY A O   1 
ATOM   1869  N N   . ASP A  1 244 ? -4.577  -64.076  -65.746 1.00 80.64  ? 244 ASP A N   1 
ATOM   1870  C CA  . ASP A  1 244 ? -4.952  -62.858  -66.453 1.00 70.81  ? 244 ASP A CA  1 
ATOM   1871  C C   . ASP A  1 244 ? -3.720  -61.978  -66.624 1.00 70.99  ? 244 ASP A C   1 
ATOM   1872  O O   . ASP A  1 244 ? -2.752  -62.108  -65.878 1.00 73.99  ? 244 ASP A O   1 
ATOM   1873  C CB  . ASP A  1 244 ? -6.037  -62.113  -65.670 1.00 72.68  ? 244 ASP A CB  1 
ATOM   1874  C CG  . ASP A  1 244 ? -6.661  -60.979  -66.462 1.00 88.64  ? 244 ASP A CG  1 
ATOM   1875  O OD1 . ASP A  1 244 ? -7.565  -60.307  -65.920 1.00 94.26  ? 244 ASP A OD1 1 
ATOM   1876  O OD2 . ASP A  1 244 ? -6.257  -60.759  -67.622 1.00 81.78  ? 244 ASP A OD2 1 
ATOM   1877  N N   . LYS A  1 245 ? -3.749  -61.092  -67.613 1.00 72.90  ? 245 LYS A N   1 
ATOM   1878  C CA  . LYS A  1 245 ? -2.640  -60.171  -67.824 1.00 74.20  ? 245 LYS A CA  1 
ATOM   1879  C C   . LYS A  1 245 ? -3.119  -58.725  -67.870 1.00 66.99  ? 245 LYS A C   1 
ATOM   1880  O O   . LYS A  1 245 ? -4.242  -58.441  -68.287 1.00 66.98  ? 245 LYS A O   1 
ATOM   1881  C CB  . LYS A  1 245 ? -1.869  -60.519  -69.100 1.00 82.98  ? 245 LYS A CB  1 
ATOM   1882  C CG  . LYS A  1 245 ? -2.561  -60.115  -70.389 1.00 84.87  ? 245 LYS A CG  1 
ATOM   1883  C CD  . LYS A  1 245 ? -1.707  -60.464  -71.600 1.00 83.69  ? 245 LYS A CD  1 
ATOM   1884  C CE  . LYS A  1 245 ? -2.363  -60.009  -72.893 1.00 102.36 ? 245 LYS A CE  1 
ATOM   1885  N NZ  . LYS A  1 245 ? -1.594  -60.440  -74.092 1.00 87.22  ? 245 LYS A NZ  1 
ATOM   1886  N N   . ILE A  1 246 ? -2.258  -57.817  -67.428 1.00 64.19  ? 246 ILE A N   1 
ATOM   1887  C CA  . ILE A  1 246 ? -2.567  -56.396  -67.448 1.00 64.04  ? 246 ILE A CA  1 
ATOM   1888  C C   . ILE A  1 246 ? -1.574  -55.661  -68.341 1.00 70.65  ? 246 ILE A C   1 
ATOM   1889  O O   . ILE A  1 246 ? -0.361  -55.840  -68.220 1.00 67.68  ? 246 ILE A O   1 
ATOM   1890  C CB  . ILE A  1 246 ? -2.548  -55.794  -66.031 1.00 57.23  ? 246 ILE A CB  1 
ATOM   1891  C CG1 . ILE A  1 246 ? -2.880  -54.302  -66.077 1.00 60.51  ? 246 ILE A CG1 1 
ATOM   1892  C CG2 . ILE A  1 246 ? -1.199  -56.028  -65.367 1.00 51.94  ? 246 ILE A CG2 1 
ATOM   1893  C CD1 . ILE A  1 246 ? -2.837  -53.629  -64.723 1.00 53.32  ? 246 ILE A CD1 1 
ATOM   1894  N N   . THR A  1 247 ? -2.100  -54.843  -69.245 1.00 81.39  ? 247 THR A N   1 
ATOM   1895  C CA  . THR A  1 247 ? -1.273  -54.113  -70.196 1.00 77.35  ? 247 THR A CA  1 
ATOM   1896  C C   . THR A  1 247 ? -1.192  -52.630  -69.860 1.00 69.06  ? 247 THR A C   1 
ATOM   1897  O O   . THR A  1 247 ? -2.165  -52.029  -69.407 1.00 74.70  ? 247 THR A O   1 
ATOM   1898  C CB  . THR A  1 247 ? -1.797  -54.273  -71.640 1.00 73.75  ? 247 THR A CB  1 
ATOM   1899  O OG1 . THR A  1 247 ? -1.525  -55.602  -72.103 1.00 88.89  ? 247 THR A OG1 1 
ATOM   1900  N N   . PHE A  1 248 ? -0.018  -52.049  -70.079 1.00 71.38  ? 248 PHE A N   1 
ATOM   1901  C CA  . PHE A  1 248 ? 0.155   -50.609  -69.955 1.00 72.49  ? 248 PHE A CA  1 
ATOM   1902  C C   . PHE A  1 248 ? 0.620   -50.043  -71.288 1.00 73.13  ? 248 PHE A C   1 
ATOM   1903  O O   . PHE A  1 248 ? 1.277   -50.732  -72.070 1.00 74.02  ? 248 PHE A O   1 
ATOM   1904  C CB  . PHE A  1 248 ? 1.147   -50.269  -68.842 1.00 50.94  ? 248 PHE A CB  1 
ATOM   1905  C CG  . PHE A  1 248 ? 0.715   -50.743  -67.483 1.00 63.37  ? 248 PHE A CG  1 
ATOM   1906  C CD1 . PHE A  1 248 ? 0.884   -52.069  -67.113 1.00 64.49  ? 248 PHE A CD1 1 
ATOM   1907  C CD2 . PHE A  1 248 ? 0.142   -49.865  -66.575 1.00 64.27  ? 248 PHE A CD2 1 
ATOM   1908  C CE1 . PHE A  1 248 ? 0.490   -52.510  -65.867 1.00 55.24  ? 248 PHE A CE1 1 
ATOM   1909  C CE2 . PHE A  1 248 ? -0.254  -50.300  -65.325 1.00 58.17  ? 248 PHE A CE2 1 
ATOM   1910  C CZ  . PHE A  1 248 ? -0.080  -51.624  -64.972 1.00 53.64  ? 248 PHE A CZ  1 
ATOM   1911  N N   . GLU A  1 249 ? 0.266   -48.789  -71.545 1.00 66.60  ? 249 GLU A N   1 
ATOM   1912  C CA  . GLU A  1 249 ? 0.544   -48.152  -72.822 1.00 75.39  ? 249 GLU A CA  1 
ATOM   1913  C C   . GLU A  1 249 ? 0.506   -46.650  -72.617 1.00 72.59  ? 249 GLU A C   1 
ATOM   1914  O O   . GLU A  1 249 ? -0.544  -46.083  -72.315 1.00 73.76  ? 249 GLU A O   1 
ATOM   1915  C CB  . GLU A  1 249 ? -0.500  -48.571  -73.858 1.00 77.24  ? 249 GLU A CB  1 
ATOM   1916  C CG  . GLU A  1 249 ? -0.298  -47.980  -75.244 1.00 95.21  ? 249 GLU A CG  1 
ATOM   1917  C CD  . GLU A  1 249 ? -1.323  -48.493  -76.238 1.00 106.75 ? 249 GLU A CD  1 
ATOM   1918  O OE1 . GLU A  1 249 ? -1.595  -47.792  -77.234 1.00 108.61 ? 249 GLU A OE1 1 
ATOM   1919  O OE2 . GLU A  1 249 ? -1.862  -49.599  -76.018 1.00 93.64  ? 249 GLU A OE2 1 
ATOM   1920  N N   . ALA A  1 250 ? 1.652   -46.002  -72.774 1.00 70.82  ? 250 ALA A N   1 
ATOM   1921  C CA  . ALA A  1 250 ? 1.749   -44.589  -72.447 1.00 64.77  ? 250 ALA A CA  1 
ATOM   1922  C C   . ALA A  1 250 ? 2.661   -43.833  -73.395 1.00 77.84  ? 250 ALA A C   1 
ATOM   1923  O O   . ALA A  1 250 ? 3.672   -44.359  -73.863 1.00 84.67  ? 250 ALA A O   1 
ATOM   1924  C CB  . ALA A  1 250 ? 2.223   -44.416  -71.012 1.00 65.22  ? 250 ALA A CB  1 
ATOM   1925  N N   . THR A  1 251 ? 2.282   -42.593  -73.676 1.00 72.75  ? 251 THR A N   1 
ATOM   1926  C CA  . THR A  1 251 ? 3.136   -41.671  -74.403 1.00 65.42  ? 251 THR A CA  1 
ATOM   1927  C C   . THR A  1 251 ? 3.692   -40.641  -73.422 1.00 68.59  ? 251 THR A C   1 
ATOM   1928  O O   . THR A  1 251 ? 4.210   -39.601  -73.826 1.00 77.68  ? 251 THR A O   1 
ATOM   1929  C CB  . THR A  1 251 ? 2.369   -40.963  -75.535 1.00 68.79  ? 251 THR A CB  1 
ATOM   1930  O OG1 . THR A  1 251 ? 1.132   -40.450  -75.027 1.00 75.90  ? 251 THR A OG1 1 
ATOM   1931  C CG2 . THR A  1 251 ? 2.075   -41.933  -76.670 1.00 65.15  ? 251 THR A CG2 1 
ATOM   1932  N N   . GLY A  1 252 ? 3.576   -40.942  -72.130 1.00 73.56  ? 252 GLY A N   1 
ATOM   1933  C CA  . GLY A  1 252 ? 4.084   -40.071  -71.083 1.00 72.94  ? 252 GLY A CA  1 
ATOM   1934  C C   . GLY A  1 252 ? 3.192   -40.014  -69.854 1.00 72.47  ? 252 GLY A C   1 
ATOM   1935  O O   . GLY A  1 252 ? 2.085   -40.538  -69.858 1.00 73.83  ? 252 GLY A O   1 
ATOM   1936  N N   . ASN A  1 253 ? 3.678   -39.381  -68.793 1.00 71.87  ? 253 ASN A N   1 
ATOM   1937  C CA  . ASN A  1 253 ? 2.859   -39.146  -67.606 1.00 63.38  ? 253 ASN A CA  1 
ATOM   1938  C C   . ASN A  1 253 ? 2.502   -40.411  -66.825 1.00 65.59  ? 253 ASN A C   1 
ATOM   1939  O O   . ASN A  1 253 ? 1.650   -40.373  -65.938 1.00 59.30  ? 253 ASN A O   1 
ATOM   1940  C CB  . ASN A  1 253 ? 1.567   -38.415  -67.987 1.00 60.04  ? 253 ASN A CB  1 
ATOM   1941  C CG  . ASN A  1 253 ? 1.820   -37.135  -68.758 1.00 60.94  ? 253 ASN A CG  1 
ATOM   1942  O OD1 . ASN A  1 253 ? 1.602   -36.037  -68.247 1.00 65.21  ? 253 ASN A OD1 1 
ATOM   1943  N ND2 . ASN A  1 253 ? 2.275   -37.268  -69.998 1.00 62.34  ? 253 ASN A ND2 1 
ATOM   1944  N N   . LEU A  1 254 ? 3.144   -41.529  -67.150 1.00 70.12  ? 254 LEU A N   1 
ATOM   1945  C CA  . LEU A  1 254 ? 2.834   -42.792  -66.483 1.00 58.96  ? 254 LEU A CA  1 
ATOM   1946  C C   . LEU A  1 254 ? 3.863   -43.180  -65.425 1.00 49.29  ? 254 LEU A C   1 
ATOM   1947  O O   . LEU A  1 254 ? 4.997   -43.533  -65.748 1.00 62.23  ? 254 LEU A O   1 
ATOM   1948  C CB  . LEU A  1 254 ? 2.687   -43.928  -67.501 1.00 55.89  ? 254 LEU A CB  1 
ATOM   1949  C CG  . LEU A  1 254 ? 2.488   -45.329  -66.914 1.00 55.43  ? 254 LEU A CG  1 
ATOM   1950  C CD1 . LEU A  1 254 ? 1.250   -45.381  -66.031 1.00 57.95  ? 254 LEU A CD1 1 
ATOM   1951  C CD2 . LEU A  1 254 ? 2.409   -46.379  -68.013 1.00 53.60  ? 254 LEU A CD2 1 
ATOM   1952  N N   . VAL A  1 255 ? 3.460   -43.109  -64.160 1.00 43.63  ? 255 VAL A N   1 
ATOM   1953  C CA  . VAL A  1 255 ? 4.272   -43.634  -63.071 1.00 43.82  ? 255 VAL A CA  1 
ATOM   1954  C C   . VAL A  1 255 ? 4.064   -45.142  -63.014 1.00 55.48  ? 255 VAL A C   1 
ATOM   1955  O O   . VAL A  1 255 ? 3.108   -45.625  -62.408 1.00 56.67  ? 255 VAL A O   1 
ATOM   1956  C CB  . VAL A  1 255 ? 3.887   -43.010  -61.718 1.00 49.79  ? 255 VAL A CB  1 
ATOM   1957  C CG1 . VAL A  1 255 ? 4.754   -43.579  -60.603 1.00 55.90  ? 255 VAL A CG1 1 
ATOM   1958  C CG2 . VAL A  1 255 ? 4.011   -41.494  -61.777 1.00 42.70  ? 255 VAL A CG2 1 
ATOM   1959  N N   . VAL A  1 256 ? 4.962   -45.880  -63.658 1.00 63.81  ? 256 VAL A N   1 
ATOM   1960  C CA  . VAL A  1 256 ? 4.797   -47.319  -63.835 1.00 55.89  ? 256 VAL A CA  1 
ATOM   1961  C C   . VAL A  1 256 ? 5.032   -48.112  -62.554 1.00 56.94  ? 256 VAL A C   1 
ATOM   1962  O O   . VAL A  1 256 ? 5.775   -47.679  -61.673 1.00 61.78  ? 256 VAL A O   1 
ATOM   1963  C CB  . VAL A  1 256 ? 5.739   -47.858  -64.928 1.00 63.85  ? 256 VAL A CB  1 
ATOM   1964  C CG1 . VAL A  1 256 ? 5.506   -47.121  -66.236 1.00 64.95  ? 256 VAL A CG1 1 
ATOM   1965  C CG2 . VAL A  1 256 ? 7.190   -47.728  -64.488 1.00 67.56  ? 256 VAL A CG2 1 
ATOM   1966  N N   . PRO A  1 257 ? 4.386   -49.282  -62.451 1.00 56.38  ? 257 PRO A N   1 
ATOM   1967  C CA  . PRO A  1 257 ? 4.586   -50.199  -61.326 1.00 48.53  ? 257 PRO A CA  1 
ATOM   1968  C C   . PRO A  1 257 ? 5.986   -50.799  -61.355 1.00 58.61  ? 257 PRO A C   1 
ATOM   1969  O O   . PRO A  1 257 ? 6.499   -51.109  -62.430 1.00 64.83  ? 257 PRO A O   1 
ATOM   1970  C CB  . PRO A  1 257 ? 3.553   -51.303  -61.584 1.00 53.70  ? 257 PRO A CB  1 
ATOM   1971  C CG  . PRO A  1 257 ? 2.560   -50.704  -62.523 1.00 53.00  ? 257 PRO A CG  1 
ATOM   1972  C CD  . PRO A  1 257 ? 3.340   -49.757  -63.371 1.00 49.63  ? 257 PRO A CD  1 
ATOM   1973  N N   . ARG A  1 258 ? 6.595   -50.951  -60.185 1.00 71.30  ? 258 ARG A N   1 
ATOM   1974  C CA  . ARG A  1 258 ? 7.871   -51.643  -60.074 1.00 64.54  ? 258 ARG A CA  1 
ATOM   1975  C C   . ARG A  1 258 ? 7.660   -52.935  -59.296 1.00 61.07  ? 258 ARG A C   1 
ATOM   1976  O O   . ARG A  1 258 ? 8.064   -54.012  -59.734 1.00 65.39  ? 258 ARG A O   1 
ATOM   1977  C CB  . ARG A  1 258 ? 8.912   -50.759  -59.383 1.00 59.87  ? 258 ARG A CB  1 
ATOM   1978  C CG  . ARG A  1 258 ? 10.273  -51.417  -59.213 1.00 67.80  ? 258 ARG A CG  1 
ATOM   1979  C CD  . ARG A  1 258 ? 11.249  -50.497  -58.496 1.00 70.69  ? 258 ARG A CD  1 
ATOM   1980  N NE  . ARG A  1 258 ? 12.269  -51.249  -57.770 1.00 85.13  ? 258 ARG A NE  1 
ATOM   1981  C CZ  . ARG A  1 258 ? 13.483  -51.517  -58.240 1.00 95.76  ? 258 ARG A CZ  1 
ATOM   1982  N NH1 . ARG A  1 258 ? 13.840  -51.089  -59.441 1.00 91.65  ? 258 ARG A NH1 1 
ATOM   1983  N NH2 . ARG A  1 258 ? 14.342  -52.211  -57.506 1.00 99.00  ? 258 ARG A NH2 1 
ATOM   1984  N N   . TYR A  1 259 ? 7.014   -52.817  -58.141 1.00 59.22  ? 259 TYR A N   1 
ATOM   1985  C CA  . TYR A  1 259 ? 6.660   -53.978  -57.336 1.00 55.45  ? 259 TYR A CA  1 
ATOM   1986  C C   . TYR A  1 259 ? 5.150   -54.172  -57.296 1.00 63.06  ? 259 TYR A C   1 
ATOM   1987  O O   . TYR A  1 259 ? 4.392   -53.211  -57.157 1.00 58.93  ? 259 TYR A O   1 
ATOM   1988  C CB  . TYR A  1 259 ? 7.193   -53.831  -55.910 1.00 59.83  ? 259 TYR A CB  1 
ATOM   1989  C CG  . TYR A  1 259 ? 8.693   -53.968  -55.791 1.00 76.97  ? 259 TYR A CG  1 
ATOM   1990  C CD1 . TYR A  1 259 ? 9.524   -52.868  -55.944 1.00 72.47  ? 259 TYR A CD1 1 
ATOM   1991  C CD2 . TYR A  1 259 ? 9.277   -55.198  -55.520 1.00 86.57  ? 259 TYR A CD2 1 
ATOM   1992  C CE1 . TYR A  1 259 ? 10.895  -52.988  -55.833 1.00 86.75  ? 259 TYR A CE1 1 
ATOM   1993  C CE2 . TYR A  1 259 ? 10.649  -55.328  -55.408 1.00 84.49  ? 259 TYR A CE2 1 
ATOM   1994  C CZ  . TYR A  1 259 ? 11.453  -54.220  -55.566 1.00 88.80  ? 259 TYR A CZ  1 
ATOM   1995  O OH  . TYR A  1 259 ? 12.820  -54.342  -55.456 1.00 89.92  ? 259 TYR A OH  1 
ATOM   1996  N N   . ALA A  1 260 ? 4.721   -55.423  -57.425 1.00 62.56  ? 260 ALA A N   1 
ATOM   1997  C CA  . ALA A  1 260 ? 3.319   -55.779  -57.255 1.00 53.85  ? 260 ALA A CA  1 
ATOM   1998  C C   . ALA A  1 260 ? 3.186   -56.656  -56.017 1.00 60.88  ? 260 ALA A C   1 
ATOM   1999  O O   . ALA A  1 260 ? 4.160   -56.867  -55.294 1.00 62.12  ? 260 ALA A O   1 
ATOM   2000  C CB  . ALA A  1 260 ? 2.798   -56.500  -58.484 1.00 55.94  ? 260 ALA A CB  1 
ATOM   2001  N N   . PHE A  1 261 ? 1.987   -57.172  -55.771 1.00 63.37  ? 261 PHE A N   1 
ATOM   2002  C CA  . PHE A  1 261 ? 1.762   -57.984  -54.582 1.00 48.96  ? 261 PHE A CA  1 
ATOM   2003  C C   . PHE A  1 261 ? 0.914   -59.223  -54.856 1.00 56.17  ? 261 PHE A C   1 
ATOM   2004  O O   . PHE A  1 261 ? -0.288  -59.121  -55.099 1.00 64.01  ? 261 PHE A O   1 
ATOM   2005  C CB  . PHE A  1 261 ? 1.114   -57.145  -53.477 1.00 45.34  ? 261 PHE A CB  1 
ATOM   2006  C CG  . PHE A  1 261 ? 1.920   -55.942  -53.074 1.00 47.52  ? 261 PHE A CG  1 
ATOM   2007  C CD1 . PHE A  1 261 ? 1.709   -54.715  -53.681 1.00 52.24  ? 261 PHE A CD1 1 
ATOM   2008  C CD2 . PHE A  1 261 ? 2.885   -56.038  -52.087 1.00 45.46  ? 261 PHE A CD2 1 
ATOM   2009  C CE1 . PHE A  1 261 ? 2.448   -53.606  -53.311 1.00 56.51  ? 261 PHE A CE1 1 
ATOM   2010  C CE2 . PHE A  1 261 ? 3.627   -54.932  -51.711 1.00 34.48  ? 261 PHE A CE2 1 
ATOM   2011  C CZ  . PHE A  1 261 ? 3.408   -53.715  -52.325 1.00 55.17  ? 261 PHE A CZ  1 
ATOM   2012  N N   . ALA A  1 262 ? 1.550   -60.390  -54.820 1.00 68.22  ? 262 ALA A N   1 
ATOM   2013  C CA  . ALA A  1 262 ? 0.819   -61.650  -54.848 1.00 63.54  ? 262 ALA A CA  1 
ATOM   2014  C C   . ALA A  1 262 ? 0.036   -61.739  -53.548 1.00 71.12  ? 262 ALA A C   1 
ATOM   2015  O O   . ALA A  1 262 ? 0.609   -61.634  -52.463 1.00 65.78  ? 262 ALA A O   1 
ATOM   2016  C CB  . ALA A  1 262 ? 1.773   -62.820  -54.984 1.00 73.50  ? 262 ALA A CB  1 
ATOM   2017  N N   . MET A  1 263 ? -1.274  -61.925  -53.655 1.00 61.42  ? 263 MET A N   1 
ATOM   2018  C CA  . MET A  1 263 ? -2.144  -61.729  -52.505 1.00 65.71  ? 263 MET A CA  1 
ATOM   2019  C C   . MET A  1 263 ? -3.347  -62.665  -52.475 1.00 65.72  ? 263 MET A C   1 
ATOM   2020  O O   . MET A  1 263 ? -4.063  -62.811  -53.465 1.00 76.75  ? 263 MET A O   1 
ATOM   2021  C CB  . MET A  1 263 ? -2.623  -60.277  -52.478 1.00 65.37  ? 263 MET A CB  1 
ATOM   2022  C CG  . MET A  1 263 ? -3.401  -59.893  -51.240 1.00 65.09  ? 263 MET A CG  1 
ATOM   2023  S SD  . MET A  1 263 ? -4.037  -58.212  -51.351 1.00 77.80  ? 263 MET A SD  1 
ATOM   2024  C CE  . MET A  1 263 ? -5.235  -58.382  -52.671 1.00 71.84  ? 263 MET A CE  1 
ATOM   2025  N N   . GLU A  1 264 ? -3.557  -63.294  -51.324 1.00 61.90  ? 264 GLU A N   1 
ATOM   2026  C CA  . GLU A  1 264 ? -4.754  -64.086  -51.079 1.00 74.45  ? 264 GLU A CA  1 
ATOM   2027  C C   . GLU A  1 264 ? -5.475  -63.502  -49.875 1.00 71.18  ? 264 GLU A C   1 
ATOM   2028  O O   . GLU A  1 264 ? -4.969  -63.552  -48.757 1.00 67.66  ? 264 GLU A O   1 
ATOM   2029  C CB  . GLU A  1 264 ? -4.391  -65.548  -50.824 1.00 75.33  ? 264 GLU A CB  1 
ATOM   2030  C CG  . GLU A  1 264 ? -4.841  -66.495  -51.923 1.00 101.85 ? 264 GLU A CG  1 
ATOM   2031  C CD  . GLU A  1 264 ? -4.055  -67.791  -51.933 1.00 120.27 ? 264 GLU A CD  1 
ATOM   2032  O OE1 . GLU A  1 264 ? -4.669  -68.861  -52.126 1.00 118.24 ? 264 GLU A OE1 1 
ATOM   2033  O OE2 . GLU A  1 264 ? -2.821  -67.739  -51.747 1.00 127.17 ? 264 GLU A OE2 1 
ATOM   2034  N N   . ARG A  1 265 ? -6.654  -62.938  -50.110 1.00 73.03  ? 265 ARG A N   1 
ATOM   2035  C CA  . ARG A  1 265 ? -7.376  -62.227  -49.063 1.00 74.42  ? 265 ARG A CA  1 
ATOM   2036  C C   . ARG A  1 265 ? -8.611  -62.971  -48.565 1.00 78.82  ? 265 ARG A C   1 
ATOM   2037  O O   . ARG A  1 265 ? -9.315  -63.625  -49.335 1.00 85.73  ? 265 ARG A O   1 
ATOM   2038  C CB  . ARG A  1 265 ? -7.762  -60.826  -49.544 1.00 61.74  ? 265 ARG A CB  1 
ATOM   2039  C CG  . ARG A  1 265 ? -8.101  -60.753  -51.024 1.00 71.67  ? 265 ARG A CG  1 
ATOM   2040  C CD  . ARG A  1 265 ? -8.477  -59.340  -51.440 1.00 77.90  ? 265 ARG A CD  1 
ATOM   2041  N NE  . ARG A  1 265 ? -9.917  -59.189  -51.630 1.00 74.80  ? 265 ARG A NE  1 
ATOM   2042  C CZ  . ARG A  1 265 ? -10.538 -59.375  -52.791 1.00 70.28  ? 265 ARG A CZ  1 
ATOM   2043  N NH1 . ARG A  1 265 ? -9.845  -59.718  -53.867 1.00 75.83  ? 265 ARG A NH1 1 
ATOM   2044  N NH2 . ARG A  1 265 ? -11.851 -59.217  -52.877 1.00 78.28  ? 265 ARG A NH2 1 
ATOM   2045  N N   . ASN A  1 266 ? -8.857  -62.864  -47.264 1.00 76.25  ? 266 ASN A N   1 
ATOM   2046  C CA  . ASN A  1 266 ? -10.072 -63.389  -46.658 1.00 98.44  ? 266 ASN A CA  1 
ATOM   2047  C C   . ASN A  1 266 ? -10.954 -62.250  -46.163 1.00 87.44  ? 266 ASN A C   1 
ATOM   2048  O O   . ASN A  1 266 ? -10.495 -61.366  -45.443 1.00 81.06  ? 266 ASN A O   1 
ATOM   2049  C CB  . ASN A  1 266 ? -9.736  -64.351  -45.517 1.00 109.36 ? 266 ASN A CB  1 
ATOM   2050  C CG  . ASN A  1 266 ? -8.402  -64.039  -44.865 1.00 97.44  ? 266 ASN A CG  1 
ATOM   2051  O OD1 . ASN A  1 266 ? -7.534  -64.906  -44.758 1.00 84.67  ? 266 ASN A OD1 1 
ATOM   2052  N ND2 . ASN A  1 266 ? -8.229  -62.795  -44.432 1.00 89.40  ? 266 ASN A ND2 1 
ATOM   2053  N N   . ALA A  1 267 ? -12.220 -62.273  -46.560 1.00 83.00  ? 267 ALA A N   1 
ATOM   2054  C CA  . ALA A  1 267 ? -13.138 -61.185  -46.245 1.00 105.05 ? 267 ALA A CA  1 
ATOM   2055  C C   . ALA A  1 267 ? -13.479 -61.116  -44.759 1.00 93.19  ? 267 ALA A C   1 
ATOM   2056  O O   . ALA A  1 267 ? -13.417 -62.120  -44.048 1.00 79.46  ? 267 ALA A O   1 
ATOM   2057  C CB  . ALA A  1 267 ? -14.410 -61.315  -47.072 1.00 105.88 ? 267 ALA A CB  1 
ATOM   2058  N N   . GLY A  1 268 ? -13.825 -59.918  -44.294 1.00 94.47  ? 268 GLY A N   1 
ATOM   2059  C CA  . GLY A  1 268 ? -14.397 -59.753  -42.971 1.00 99.77  ? 268 GLY A CA  1 
ATOM   2060  C C   . GLY A  1 268 ? -13.485 -59.334  -41.831 1.00 99.73  ? 268 GLY A C   1 
ATOM   2061  O O   . GLY A  1 268 ? -13.598 -59.865  -40.729 1.00 92.43  ? 268 GLY A O   1 
ATOM   2062  N N   . SER A  1 269 ? -12.591 -58.382  -42.077 1.00 79.16  ? 269 SER A N   1 
ATOM   2063  C CA  . SER A  1 269 ? -11.804 -57.796  -40.993 1.00 66.12  ? 269 SER A CA  1 
ATOM   2064  C C   . SER A  1 269 ? -11.946 -56.279  -40.999 1.00 62.91  ? 269 SER A C   1 
ATOM   2065  O O   . SER A  1 269 ? -12.904 -55.744  -41.554 1.00 74.61  ? 269 SER A O   1 
ATOM   2066  C CB  . SER A  1 269 ? -10.333 -58.198  -41.093 1.00 62.50  ? 269 SER A CB  1 
ATOM   2067  O OG  . SER A  1 269 ? -9.604  -57.728  -39.971 1.00 52.89  ? 269 SER A OG  1 
ATOM   2068  N N   . GLY A  1 270 ? -10.997 -55.585  -40.380 1.00 45.13  ? 270 GLY A N   1 
ATOM   2069  C CA  . GLY A  1 270 ? -11.059 -54.139  -40.307 1.00 48.59  ? 270 GLY A CA  1 
ATOM   2070  C C   . GLY A  1 270 ? -9.726  -53.469  -40.046 1.00 44.13  ? 270 GLY A C   1 
ATOM   2071  O O   . GLY A  1 270 ? -8.673  -54.106  -40.079 1.00 50.73  ? 270 GLY A O   1 
ATOM   2072  N N   . ILE A  1 271 ? -9.781  -52.167  -39.787 1.00 51.91  ? 271 ILE A N   1 
ATOM   2073  C CA  . ILE A  1 271 ? -8.589  -51.372  -39.529 1.00 36.93  ? 271 ILE A CA  1 
ATOM   2074  C C   . ILE A  1 271 ? -8.781  -50.548  -38.264 1.00 40.54  ? 271 ILE A C   1 
ATOM   2075  O O   . ILE A  1 271 ? -9.667  -49.697  -38.197 1.00 66.33  ? 271 ILE A O   1 
ATOM   2076  C CB  . ILE A  1 271 ? -8.292  -50.426  -40.703 1.00 36.99  ? 271 ILE A CB  1 
ATOM   2077  C CG1 . ILE A  1 271 ? -8.057  -51.231  -41.982 1.00 46.07  ? 271 ILE A CG1 1 
ATOM   2078  C CG2 . ILE A  1 271 ? -7.095  -49.542  -40.387 1.00 48.73  ? 271 ILE A CG2 1 
ATOM   2079  C CD1 . ILE A  1 271 ? -8.327  -50.455  -43.248 1.00 54.49  ? 271 ILE A CD1 1 
ATOM   2080  N N   . ILE A  1 272 ? -7.951  -50.809  -37.260 1.00 41.07  ? 272 ILE A N   1 
ATOM   2081  C CA  . ILE A  1 272 ? -8.046  -50.098  -35.992 1.00 48.22  ? 272 ILE A CA  1 
ATOM   2082  C C   . ILE A  1 272 ? -7.043  -48.953  -35.917 1.00 48.68  ? 272 ILE A C   1 
ATOM   2083  O O   . ILE A  1 272 ? -5.842  -49.155  -36.096 1.00 46.50  ? 272 ILE A O   1 
ATOM   2084  C CB  . ILE A  1 272 ? -7.820  -51.041  -34.795 1.00 45.04  ? 272 ILE A CB  1 
ATOM   2085  C CG1 . ILE A  1 272 ? -8.913  -52.111  -34.743 1.00 49.12  ? 272 ILE A CG1 1 
ATOM   2086  C CG2 . ILE A  1 272 ? -7.786  -50.255  -33.495 1.00 45.30  ? 272 ILE A CG2 1 
ATOM   2087  C CD1 . ILE A  1 272 ? -8.840  -53.000  -33.521 1.00 50.86  ? 272 ILE A CD1 1 
ATOM   2088  N N   . ILE A  1 273 ? -7.546  -47.750  -35.660 1.00 51.68  ? 273 ILE A N   1 
ATOM   2089  C CA  . ILE A  1 273 ? -6.688  -46.593  -35.447 1.00 58.58  ? 273 ILE A CA  1 
ATOM   2090  C C   . ILE A  1 273 ? -6.514  -46.367  -33.950 1.00 65.71  ? 273 ILE A C   1 
ATOM   2091  O O   . ILE A  1 273 ? -7.403  -45.836  -33.284 1.00 73.14  ? 273 ILE A O   1 
ATOM   2092  C CB  . ILE A  1 273 ? -7.258  -45.317  -36.101 1.00 59.17  ? 273 ILE A CB  1 
ATOM   2093  C CG1 . ILE A  1 273 ? -7.402  -45.498  -37.615 1.00 56.96  ? 273 ILE A CG1 1 
ATOM   2094  C CG2 . ILE A  1 273 ? -6.369  -44.122  -35.795 1.00 66.45  ? 273 ILE A CG2 1 
ATOM   2095  C CD1 . ILE A  1 273 ? -8.645  -46.255  -38.037 1.00 74.29  ? 273 ILE A CD1 1 
ATOM   2096  N N   . SER A  1 274 ? -5.365  -46.778  -33.426 1.00 68.57  ? 274 SER A N   1 
ATOM   2097  C CA  . SER A  1 274 ? -5.121  -46.733  -31.991 1.00 62.16  ? 274 SER A CA  1 
ATOM   2098  C C   . SER A  1 274 ? -3.644  -46.551  -31.661 1.00 70.45  ? 274 SER A C   1 
ATOM   2099  O O   . SER A  1 274 ? -2.770  -46.899  -32.455 1.00 74.52  ? 274 SER A O   1 
ATOM   2100  C CB  . SER A  1 274 ? -5.649  -48.010  -31.329 1.00 63.71  ? 274 SER A CB  1 
ATOM   2101  O OG  . SER A  1 274 ? -5.068  -48.205  -30.051 1.00 66.49  ? 274 SER A OG  1 
ATOM   2102  N N   . ASP A  1 275 ? -3.378  -46.001  -30.481 1.00 90.49  ? 275 ASP A N   1 
ATOM   2103  C CA  . ASP A  1 275 ? -2.014  -45.843  -29.993 1.00 91.90  ? 275 ASP A CA  1 
ATOM   2104  C C   . ASP A  1 275 ? -1.585  -47.075  -29.208 1.00 79.11  ? 275 ASP A C   1 
ATOM   2105  O O   . ASP A  1 275 ? -0.394  -47.342  -29.057 1.00 94.93  ? 275 ASP A O   1 
ATOM   2106  C CB  . ASP A  1 275 ? -1.903  -44.610  -29.094 1.00 106.10 ? 275 ASP A CB  1 
ATOM   2107  C CG  . ASP A  1 275 ? -2.270  -43.327  -29.810 1.00 125.12 ? 275 ASP A CG  1 
ATOM   2108  O OD1 . ASP A  1 275 ? -3.392  -42.825  -29.589 1.00 140.92 ? 275 ASP A OD1 1 
ATOM   2109  O OD2 . ASP A  1 275 ? -1.436  -42.816  -30.588 1.00 120.51 ? 275 ASP A OD2 1 
ATOM   2110  N N   . THR A  1 276 ? -2.569  -47.818  -28.708 1.00 73.05  ? 276 THR A N   1 
ATOM   2111  C CA  . THR A  1 276 ? -2.321  -48.961  -27.835 1.00 72.68  ? 276 THR A CA  1 
ATOM   2112  C C   . THR A  1 276 ? -1.242  -49.880  -28.401 1.00 74.41  ? 276 THR A C   1 
ATOM   2113  O O   . THR A  1 276 ? -1.179  -50.102  -29.611 1.00 68.63  ? 276 THR A O   1 
ATOM   2114  C CB  . THR A  1 276 ? -3.618  -49.761  -27.587 1.00 62.87  ? 276 THR A CB  1 
ATOM   2115  O OG1 . THR A  1 276 ? -4.680  -48.860  -27.252 1.00 53.91  ? 276 THR A OG1 1 
ATOM   2116  C CG2 . THR A  1 276 ? -3.438  -50.766  -26.457 1.00 61.20  ? 276 THR A CG2 1 
ATOM   2117  N N   . PRO A  1 277 ? -0.379  -50.402  -27.518 1.00 80.03  ? 277 PRO A N   1 
ATOM   2118  C CA  . PRO A  1 277 ? 0.748   -51.274  -27.868 1.00 76.27  ? 277 PRO A CA  1 
ATOM   2119  C C   . PRO A  1 277 ? 0.321   -52.595  -28.499 1.00 71.22  ? 277 PRO A C   1 
ATOM   2120  O O   . PRO A  1 277 ? -0.617  -53.237  -28.024 1.00 70.39  ? 277 PRO A O   1 
ATOM   2121  C CB  . PRO A  1 277 ? 1.409   -51.549  -26.513 1.00 87.07  ? 277 PRO A CB  1 
ATOM   2122  C CG  . PRO A  1 277 ? 0.983   -50.424  -25.640 1.00 90.43  ? 277 PRO A CG  1 
ATOM   2123  C CD  . PRO A  1 277 ? -0.395  -50.074  -26.082 1.00 75.22  ? 277 PRO A CD  1 
ATOM   2124  N N   . VAL A  1 278 ? 1.013   -52.991  -29.562 1.00 66.69  ? 278 VAL A N   1 
ATOM   2125  C CA  . VAL A  1 278 ? 0.839   -54.317  -30.138 1.00 75.98  ? 278 VAL A CA  1 
ATOM   2126  C C   . VAL A  1 278 ? 1.522   -55.326  -29.223 1.00 79.62  ? 278 VAL A C   1 
ATOM   2127  O O   . VAL A  1 278 ? 2.568   -55.037  -28.642 1.00 82.32  ? 278 VAL A O   1 
ATOM   2128  C CB  . VAL A  1 278 ? 1.449   -54.403  -31.547 1.00 68.26  ? 278 VAL A CB  1 
ATOM   2129  C CG1 . VAL A  1 278 ? 2.905   -53.971  -31.517 1.00 89.07  ? 278 VAL A CG1 1 
ATOM   2130  C CG2 . VAL A  1 278 ? 1.314   -55.813  -32.105 1.00 58.76  ? 278 VAL A CG2 1 
ATOM   2131  N N   . HIS A  1 279 ? 0.930   -56.507  -29.088 1.00 83.52  ? 279 HIS A N   1 
ATOM   2132  C CA  . HIS A  1 279 ? 1.435   -57.492  -28.139 1.00 80.10  ? 279 HIS A CA  1 
ATOM   2133  C C   . HIS A  1 279 ? 1.427   -58.916  -28.678 1.00 85.38  ? 279 HIS A C   1 
ATOM   2134  O O   . HIS A  1 279 ? 0.684   -59.242  -29.605 1.00 93.18  ? 279 HIS A O   1 
ATOM   2135  C CB  . HIS A  1 279 ? 0.628   -57.433  -26.840 1.00 89.25  ? 279 HIS A CB  1 
ATOM   2136  C CG  . HIS A  1 279 ? 1.334   -56.733  -25.719 1.00 99.31  ? 279 HIS A CG  1 
ATOM   2137  N ND1 . HIS A  1 279 ? 1.940   -57.413  -24.687 1.00 97.83  ? 279 HIS A ND1 1 
ATOM   2138  C CD2 . HIS A  1 279 ? 1.529   -55.418  -25.472 1.00 100.11 ? 279 HIS A CD2 1 
ATOM   2139  C CE1 . HIS A  1 279 ? 2.479   -56.546  -23.847 1.00 112.46 ? 279 HIS A CE1 1 
ATOM   2140  N NE2 . HIS A  1 279 ? 2.242   -55.325  -24.303 1.00 103.23 ? 279 HIS A NE2 1 
ATOM   2141  N N   . ASP A  1 280 ? 2.265   -59.758  -28.083 1.00 88.90  ? 280 ASP A N   1 
ATOM   2142  C CA  . ASP A  1 280 ? 2.262   -61.185  -28.373 1.00 102.31 ? 280 ASP A CA  1 
ATOM   2143  C C   . ASP A  1 280 ? 1.279   -61.885  -27.443 1.00 96.88  ? 280 ASP A C   1 
ATOM   2144  O O   . ASP A  1 280 ? 1.678   -62.505  -26.457 1.00 116.11 ? 280 ASP A O   1 
ATOM   2145  C CB  . ASP A  1 280 ? 3.661   -61.774  -28.187 1.00 108.18 ? 280 ASP A CB  1 
ATOM   2146  C CG  . ASP A  1 280 ? 3.693   -63.282  -28.375 1.00 123.90 ? 280 ASP A CG  1 
ATOM   2147  O OD1 . ASP A  1 280 ? 2.740   -63.838  -28.961 1.00 116.03 ? 280 ASP A OD1 1 
ATOM   2148  O OD2 . ASP A  1 280 ? 4.678   -63.912  -27.938 1.00 133.11 ? 280 ASP A OD2 1 
ATOM   2149  N N   . CYS A  1 281 ? -0.009  -61.776  -27.754 1.00 89.22  ? 281 CYS A N   1 
ATOM   2150  C CA  . CYS A  1 281 ? -1.046  -62.385  -26.927 1.00 89.85  ? 281 CYS A CA  1 
ATOM   2151  C C   . CYS A  1 281 ? -2.209  -62.865  -27.775 1.00 80.63  ? 281 CYS A C   1 
ATOM   2152  O O   . CYS A  1 281 ? -2.375  -62.433  -28.911 1.00 85.11  ? 281 CYS A O   1 
ATOM   2153  C CB  . CYS A  1 281 ? -1.548  -61.408  -25.877 1.00 79.24  ? 281 CYS A CB  1 
ATOM   2154  S SG  . CYS A  1 281 ? -2.087  -59.839  -26.558 1.00 124.59 ? 281 CYS A SG  1 
ATOM   2155  N N   . ASN A  1 282 ? -3.017  -63.756  -27.213 1.00 78.88  ? 282 ASN A N   1 
ATOM   2156  C CA  . ASN A  1 282 ? -4.170  -64.299  -27.918 1.00 71.32  ? 282 ASN A CA  1 
ATOM   2157  C C   . ASN A  1 282 ? -5.475  -63.643  -27.477 1.00 74.47  ? 282 ASN A C   1 
ATOM   2158  O O   . ASN A  1 282 ? -5.688  -63.406  -26.289 1.00 75.33  ? 282 ASN A O   1 
ATOM   2159  C CB  . ASN A  1 282 ? -4.251  -65.816  -27.719 1.00 82.16  ? 282 ASN A CB  1 
ATOM   2160  C CG  . ASN A  1 282 ? -3.894  -66.590  -28.975 1.00 97.85  ? 282 ASN A CG  1 
ATOM   2161  O OD1 . ASN A  1 282 ? -4.152  -66.134  -30.088 1.00 102.99 ? 282 ASN A OD1 1 
ATOM   2162  N ND2 . ASN A  1 282 ? -3.308  -67.771  -28.802 1.00 119.80 ? 282 ASN A ND2 1 
ATOM   2163  N N   . THR A  1 283 ? -6.344  -63.349  -28.439 1.00 73.50  ? 283 THR A N   1 
ATOM   2164  C CA  . THR A  1 283 ? -7.663  -62.808  -28.134 1.00 68.35  ? 283 THR A CA  1 
ATOM   2165  C C   . THR A  1 283 ? -8.690  -63.252  -29.169 1.00 61.03  ? 283 THR A C   1 
ATOM   2166  O O   . THR A  1 283 ? -8.341  -63.592  -30.300 1.00 66.10  ? 283 THR A O   1 
ATOM   2167  C CB  . THR A  1 283 ? -7.654  -61.269  -28.065 1.00 62.56  ? 283 THR A CB  1 
ATOM   2168  O OG1 . THR A  1 283 ? -8.864  -60.809  -27.452 1.00 41.10  ? 283 THR A OG1 1 
ATOM   2169  C CG2 . THR A  1 283 ? -7.535  -60.667  -29.459 1.00 53.42  ? 283 THR A CG2 1 
ATOM   2170  N N   . THR A  1 284 ? -9.957  -63.251  -28.771 1.00 52.99  ? 284 THR A N   1 
ATOM   2171  C CA  . THR A  1 284 ? -11.045 -63.586  -29.678 1.00 58.28  ? 284 THR A CA  1 
ATOM   2172  C C   . THR A  1 284 ? -11.839 -62.339  -30.040 1.00 57.85  ? 284 THR A C   1 
ATOM   2173  O O   . THR A  1 284 ? -12.672 -62.359  -30.946 1.00 52.87  ? 284 THR A O   1 
ATOM   2174  C CB  . THR A  1 284 ? -12.006 -64.600  -29.053 1.00 52.11  ? 284 THR A CB  1 
ATOM   2175  O OG1 . THR A  1 284 ? -13.016 -64.941  -30.007 1.00 70.00  ? 284 THR A OG1 1 
ATOM   2176  C CG2 . THR A  1 284 ? -12.671 -64.006  -27.822 1.00 54.40  ? 284 THR A CG2 1 
ATOM   2177  N N   . CYS A  1 285 ? -11.581 -61.256  -29.317 1.00 43.60  ? 285 CYS A N   1 
ATOM   2178  C CA  . CYS A  1 285 ? -12.269 -59.994  -29.551 1.00 39.25  ? 285 CYS A CA  1 
ATOM   2179  C C   . CYS A  1 285 ? -11.316 -58.828  -29.319 1.00 43.50  ? 285 CYS A C   1 
ATOM   2180  O O   . CYS A  1 285 ? -10.694 -58.725  -28.261 1.00 49.20  ? 285 CYS A O   1 
ATOM   2181  C CB  . CYS A  1 285 ? -13.489 -59.876  -28.638 1.00 42.81  ? 285 CYS A CB  1 
ATOM   2182  S SG  . CYS A  1 285 ? -14.376 -58.306  -28.772 1.00 63.58  ? 285 CYS A SG  1 
ATOM   2183  N N   . GLN A  1 286 ? -11.205 -57.952  -30.312 1.00 42.77  ? 286 GLN A N   1 
ATOM   2184  C CA  . GLN A  1 286 ? -10.251 -56.852  -30.253 1.00 35.09  ? 286 GLN A CA  1 
ATOM   2185  C C   . GLN A  1 286 ? -10.925 -55.488  -30.372 1.00 49.46  ? 286 GLN A C   1 
ATOM   2186  O O   . GLN A  1 286 ? -11.737 -55.261  -31.269 1.00 48.99  ? 286 GLN A O   1 
ATOM   2187  C CB  . GLN A  1 286 ? -9.197  -57.006  -31.353 1.00 38.42  ? 286 GLN A CB  1 
ATOM   2188  C CG  . GLN A  1 286 ? -8.064  -56.000  -31.262 1.00 38.95  ? 286 GLN A CG  1 
ATOM   2189  C CD  . GLN A  1 286 ? -7.279  -56.134  -29.973 1.00 54.60  ? 286 GLN A CD  1 
ATOM   2190  O OE1 . GLN A  1 286 ? -6.703  -57.184  -29.690 1.00 55.79  ? 286 GLN A OE1 1 
ATOM   2191  N NE2 . GLN A  1 286 ? -7.250  -55.067  -29.183 1.00 45.61  ? 286 GLN A NE2 1 
ATOM   2192  N N   . THR A  1 287 ? -10.577 -54.584  -29.460 1.00 49.10  ? 287 THR A N   1 
ATOM   2193  C CA  . THR A  1 287 ? -11.060 -53.209  -29.509 1.00 41.60  ? 287 THR A CA  1 
ATOM   2194  C C   . THR A  1 287 ? -9.871  -52.261  -29.616 1.00 45.12  ? 287 THR A C   1 
ATOM   2195  O O   . THR A  1 287 ? -8.742  -52.645  -29.312 1.00 50.91  ? 287 THR A O   1 
ATOM   2196  C CB  . THR A  1 287 ? -11.875 -52.844  -28.251 1.00 47.42  ? 287 THR A CB  1 
ATOM   2197  O OG1 . THR A  1 287 ? -11.008 -52.277  -27.260 1.00 37.55  ? 287 THR A OG1 1 
ATOM   2198  C CG2 . THR A  1 287 ? -12.570 -54.071  -27.683 1.00 39.65  ? 287 THR A CG2 1 
ATOM   2199  N N   . PRO A  1 288 ? -10.119 -51.018  -30.056 1.00 56.02  ? 288 PRO A N   1 
ATOM   2200  C CA  . PRO A  1 288 ? -9.059  -50.010  -30.165 1.00 55.72  ? 288 PRO A CA  1 
ATOM   2201  C C   . PRO A  1 288 ? -8.375  -49.726  -28.828 1.00 53.63  ? 288 PRO A C   1 
ATOM   2202  O O   . PRO A  1 288 ? -7.221  -49.298  -28.813 1.00 52.70  ? 288 PRO A O   1 
ATOM   2203  C CB  . PRO A  1 288 ? -9.811  -48.765  -30.642 1.00 52.92  ? 288 PRO A CB  1 
ATOM   2204  C CG  . PRO A  1 288 ? -11.004 -49.298  -31.353 1.00 42.60  ? 288 PRO A CG  1 
ATOM   2205  C CD  . PRO A  1 288 ? -11.400 -50.532  -30.599 1.00 52.01  ? 288 PRO A CD  1 
ATOM   2206  N N   . LYS A  1 289 ? -9.079  -49.962  -27.725 1.00 55.17  ? 289 LYS A N   1 
ATOM   2207  C CA  . LYS A  1 289 ? -8.541  -49.682  -26.397 1.00 56.22  ? 289 LYS A CA  1 
ATOM   2208  C C   . LYS A  1 289 ? -7.763  -50.870  -25.839 1.00 50.13  ? 289 LYS A C   1 
ATOM   2209  O O   . LYS A  1 289 ? -6.844  -50.703  -25.037 1.00 60.45  ? 289 LYS A O   1 
ATOM   2210  C CB  . LYS A  1 289 ? -9.669  -49.291  -25.438 1.00 55.85  ? 289 LYS A CB  1 
ATOM   2211  C CG  . LYS A  1 289 ? -10.462 -48.076  -25.895 1.00 66.03  ? 289 LYS A CG  1 
ATOM   2212  C CD  . LYS A  1 289 ? -11.726 -47.868  -25.072 1.00 69.68  ? 289 LYS A CD  1 
ATOM   2213  C CE  . LYS A  1 289 ? -11.417 -47.383  -23.666 1.00 71.79  ? 289 LYS A CE  1 
ATOM   2214  N NZ  . LYS A  1 289 ? -12.659 -47.018  -22.927 1.00 77.77  ? 289 LYS A NZ  1 
ATOM   2215  N N   . GLY A  1 290 ? -8.139  -52.069  -26.271 1.00 44.24  ? 290 GLY A N   1 
ATOM   2216  C CA  . GLY A  1 290 ? -7.507  -53.289  -25.806 1.00 48.42  ? 290 GLY A CA  1 
ATOM   2217  C C   . GLY A  1 290 ? -8.357  -54.503  -26.124 1.00 49.54  ? 290 GLY A C   1 
ATOM   2218  O O   . GLY A  1 290 ? -9.497  -54.371  -26.566 1.00 61.41  ? 290 GLY A O   1 
ATOM   2219  N N   . ALA A  1 291 ? -7.803  -55.689  -25.898 1.00 53.42  ? 291 ALA A N   1 
ATOM   2220  C CA  . ALA A  1 291 ? -8.507  -56.931  -26.197 1.00 52.87  ? 291 ALA A CA  1 
ATOM   2221  C C   . ALA A  1 291 ? -9.462  -57.320  -25.073 1.00 59.20  ? 291 ALA A C   1 
ATOM   2222  O O   . ALA A  1 291 ? -9.323  -56.861  -23.940 1.00 47.37  ? 291 ALA A O   1 
ATOM   2223  C CB  . ALA A  1 291 ? -7.514  -58.051  -26.461 1.00 43.16  ? 291 ALA A CB  1 
ATOM   2224  N N   . ILE A  1 292 ? -10.433 -58.169  -25.398 1.00 51.32  ? 292 ILE A N   1 
ATOM   2225  C CA  . ILE A  1 292 ? -11.379 -58.666  -24.406 1.00 46.04  ? 292 ILE A CA  1 
ATOM   2226  C C   . ILE A  1 292 ? -11.332 -60.186  -24.298 1.00 72.24  ? 292 ILE A C   1 
ATOM   2227  O O   . ILE A  1 292 ? -11.655 -60.901  -25.247 1.00 77.97  ? 292 ILE A O   1 
ATOM   2228  C CB  . ILE A  1 292 ? -12.822 -58.231  -24.716 1.00 57.50  ? 292 ILE A CB  1 
ATOM   2229  C CG1 . ILE A  1 292 ? -12.940 -56.708  -24.682 1.00 47.80  ? 292 ILE A CG1 1 
ATOM   2230  C CG2 . ILE A  1 292 ? -13.786 -58.853  -23.720 1.00 70.85  ? 292 ILE A CG2 1 
ATOM   2231  C CD1 . ILE A  1 292 ? -14.337 -56.198  -24.961 1.00 52.79  ? 292 ILE A CD1 1 
ATOM   2232  N N   . ASN A  1 293 ? -10.920 -60.664  -23.130 1.00 112.71 ? 293 ASN A N   1 
ATOM   2233  C CA  . ASN A  1 293 ? -10.889 -62.087  -22.825 1.00 119.50 ? 293 ASN A CA  1 
ATOM   2234  C C   . ASN A  1 293 ? -12.098 -62.419  -21.960 1.00 118.35 ? 293 ASN A C   1 
ATOM   2235  O O   . ASN A  1 293 ? -12.026 -62.349  -20.735 1.00 123.51 ? 293 ASN A O   1 
ATOM   2236  C CB  . ASN A  1 293 ? -9.589  -62.419  -22.088 1.00 126.12 ? 293 ASN A CB  1 
ATOM   2237  C CG  . ASN A  1 293 ? -9.464  -63.890  -21.740 1.00 139.85 ? 293 ASN A CG  1 
ATOM   2238  O OD1 . ASN A  1 293 ? -10.274 -64.714  -22.161 1.00 124.88 ? 293 ASN A OD1 1 
ATOM   2239  N ND2 . ASN A  1 293 ? -8.437  -64.226  -20.965 1.00 140.75 ? 293 ASN A ND2 1 
ATOM   2240  N N   . THR A  1 294 ? -13.215 -62.767  -22.595 1.00 87.92  ? 294 THR A N   1 
ATOM   2241  C CA  . THR A  1 294 ? -14.479 -62.872  -21.869 1.00 94.83  ? 294 THR A CA  1 
ATOM   2242  C C   . THR A  1 294 ? -15.415 -63.990  -22.317 1.00 86.97  ? 294 THR A C   1 
ATOM   2243  O O   . THR A  1 294 ? -15.380 -64.438  -23.464 1.00 85.06  ? 294 THR A O   1 
ATOM   2244  C CB  . THR A  1 294 ? -15.269 -61.553  -21.947 1.00 89.73  ? 294 THR A CB  1 
ATOM   2245  O OG1 . THR A  1 294 ? -16.355 -61.589  -21.013 1.00 78.26  ? 294 THR A OG1 1 
ATOM   2246  N N   . SER A  1 295 ? -16.262 -64.420  -21.387 1.00 72.03  ? 295 SER A N   1 
ATOM   2247  C CA  . SER A  1 295 ? -17.338 -65.357  -21.672 1.00 81.42  ? 295 SER A CA  1 
ATOM   2248  C C   . SER A  1 295 ? -18.675 -64.635  -21.559 1.00 62.63  ? 295 SER A C   1 
ATOM   2249  O O   . SER A  1 295 ? -19.698 -65.120  -22.039 1.00 62.20  ? 295 SER A O   1 
ATOM   2250  C CB  . SER A  1 295 ? -17.301 -66.531  -20.692 1.00 83.50  ? 295 SER A CB  1 
ATOM   2251  O OG  . SER A  1 295 ? -16.928 -67.732  -21.343 1.00 106.89 ? 295 SER A OG  1 
ATOM   2252  N N   . LEU A  1 296 ? -18.652 -63.469  -20.919 1.00 51.43  ? 296 LEU A N   1 
ATOM   2253  C CA  . LEU A  1 296 ? -19.863 -62.689  -20.681 1.00 51.12  ? 296 LEU A CA  1 
ATOM   2254  C C   . LEU A  1 296 ? -20.522 -62.234  -21.982 1.00 51.88  ? 296 LEU A C   1 
ATOM   2255  O O   . LEU A  1 296 ? -19.840 -61.967  -22.972 1.00 52.17  ? 296 LEU A O   1 
ATOM   2256  C CB  . LEU A  1 296 ? -19.556 -61.484  -19.787 1.00 45.94  ? 296 LEU A CB  1 
ATOM   2257  C CG  . LEU A  1 296 ? -18.914 -61.810  -18.436 1.00 55.33  ? 296 LEU A CG  1 
ATOM   2258  C CD1 . LEU A  1 296 ? -18.729 -60.549  -17.604 1.00 60.95  ? 296 LEU A CD1 1 
ATOM   2259  C CD2 . LEU A  1 296 ? -19.746 -62.834  -17.679 1.00 47.78  ? 296 LEU A CD2 1 
ATOM   2260  N N   . PRO A  1 297 ? -21.860 -62.147  -21.978 1.00 50.86  ? 297 PRO A N   1 
ATOM   2261  C CA  . PRO A  1 297 ? -22.655 -61.823  -23.168 1.00 46.54  ? 297 PRO A CA  1 
ATOM   2262  C C   . PRO A  1 297 ? -22.536 -60.362  -23.594 1.00 53.42  ? 297 PRO A C   1 
ATOM   2263  O O   . PRO A  1 297 ? -22.766 -60.054  -24.763 1.00 53.37  ? 297 PRO A O   1 
ATOM   2264  C CB  . PRO A  1 297 ? -24.095 -62.111  -22.718 1.00 45.24  ? 297 PRO A CB  1 
ATOM   2265  C CG  . PRO A  1 297 ? -23.972 -62.920  -21.461 1.00 62.11  ? 297 PRO A CG  1 
ATOM   2266  C CD  . PRO A  1 297 ? -22.714 -62.447  -20.818 1.00 55.33  ? 297 PRO A CD  1 
ATOM   2267  N N   . PHE A  1 298 ? -22.187 -59.477  -22.665 1.00 50.90  ? 298 PHE A N   1 
ATOM   2268  C CA  . PHE A  1 298 ? -22.189 -58.047  -22.958 1.00 47.58  ? 298 PHE A CA  1 
ATOM   2269  C C   . PHE A  1 298 ? -20.923 -57.332  -22.493 1.00 47.59  ? 298 PHE A C   1 
ATOM   2270  O O   . PHE A  1 298 ? -20.323 -57.696  -21.482 1.00 55.97  ? 298 PHE A O   1 
ATOM   2271  C CB  . PHE A  1 298 ? -23.419 -57.380  -22.335 1.00 42.05  ? 298 PHE A CB  1 
ATOM   2272  C CG  . PHE A  1 298 ? -24.684 -58.176  -22.489 1.00 42.85  ? 298 PHE A CG  1 
ATOM   2273  C CD1 . PHE A  1 298 ? -25.363 -58.201  -23.696 1.00 39.91  ? 298 PHE A CD1 1 
ATOM   2274  C CD2 . PHE A  1 298 ? -25.196 -58.898  -21.423 1.00 41.53  ? 298 PHE A CD2 1 
ATOM   2275  C CE1 . PHE A  1 298 ? -26.528 -58.934  -23.837 1.00 44.82  ? 298 PHE A CE1 1 
ATOM   2276  C CE2 . PHE A  1 298 ? -26.360 -59.631  -21.558 1.00 48.57  ? 298 PHE A CE2 1 
ATOM   2277  C CZ  . PHE A  1 298 ? -27.026 -59.649  -22.766 1.00 38.68  ? 298 PHE A CZ  1 
ATOM   2278  N N   . GLN A  1 299 ? -20.530 -56.308  -23.243 1.00 47.44  ? 299 GLN A N   1 
ATOM   2279  C CA  . GLN A  1 299 ? -19.380 -55.485  -22.891 1.00 40.59  ? 299 GLN A CA  1 
ATOM   2280  C C   . GLN A  1 299 ? -19.696 -54.010  -23.121 1.00 43.64  ? 299 GLN A C   1 
ATOM   2281  O O   . GLN A  1 299 ? -20.413 -53.660  -24.057 1.00 71.78  ? 299 GLN A O   1 
ATOM   2282  C CB  . GLN A  1 299 ? -18.150 -55.906  -23.701 1.00 38.81  ? 299 GLN A CB  1 
ATOM   2283  C CG  . GLN A  1 299 ? -18.331 -55.841  -25.212 1.00 44.92  ? 299 GLN A CG  1 
ATOM   2284  C CD  . GLN A  1 299 ? -18.083 -54.455  -25.779 1.00 45.17  ? 299 GLN A CD  1 
ATOM   2285  O OE1 . GLN A  1 299 ? -17.607 -53.559  -25.081 1.00 38.68  ? 299 GLN A OE1 1 
ATOM   2286  N NE2 . GLN A  1 299 ? -18.399 -54.274  -27.056 1.00 42.08  ? 299 GLN A NE2 1 
ATOM   2287  N N   . ASN A  1 300 ? -19.165 -53.148  -22.259 1.00 45.82  ? 300 ASN A N   1 
ATOM   2288  C CA  . ASN A  1 300 ? -19.392 -51.712  -22.379 1.00 43.47  ? 300 ASN A CA  1 
ATOM   2289  C C   . ASN A  1 300 ? -18.092 -50.950  -22.602 1.00 36.37  ? 300 ASN A C   1 
ATOM   2290  O O   . ASN A  1 300 ? -18.010 -49.748  -22.347 1.00 37.34  ? 300 ASN A O   1 
ATOM   2291  C CB  . ASN A  1 300 ? -20.109 -51.172  -21.138 1.00 38.97  ? 300 ASN A CB  1 
ATOM   2292  C CG  . ASN A  1 300 ? -19.257 -51.263  -19.886 1.00 48.98  ? 300 ASN A CG  1 
ATOM   2293  O OD1 . ASN A  1 300 ? -18.208 -51.907  -19.878 1.00 56.98  ? 300 ASN A OD1 1 
ATOM   2294  N ND2 . ASN A  1 300 ? -19.707 -50.616  -18.817 1.00 43.49  ? 300 ASN A ND2 1 
ATOM   2295  N N   . ILE A  1 301 ? -17.078 -51.661  -23.082 1.00 38.26  ? 301 ILE A N   1 
ATOM   2296  C CA  . ILE A  1 301 ? -15.760 -51.078  -23.293 1.00 43.99  ? 301 ILE A CA  1 
ATOM   2297  C C   . ILE A  1 301 ? -15.721 -50.179  -24.523 1.00 41.07  ? 301 ILE A C   1 
ATOM   2298  O O   . ILE A  1 301 ? -15.340 -49.012  -24.435 1.00 42.66  ? 301 ILE A O   1 
ATOM   2299  C CB  . ILE A  1 301 ? -14.679 -52.167  -23.432 1.00 47.97  ? 301 ILE A CB  1 
ATOM   2300  C CG1 . ILE A  1 301 ? -14.555 -52.964  -22.131 1.00 36.08  ? 301 ILE A CG1 1 
ATOM   2301  C CG2 . ILE A  1 301 ? -13.342 -51.548  -23.815 1.00 39.23  ? 301 ILE A CG2 1 
ATOM   2302  C CD1 . ILE A  1 301 ? -13.601 -54.132  -22.218 1.00 58.08  ? 301 ILE A CD1 1 
ATOM   2303  N N   . HIS A  1 302 ? -16.116 -50.725  -25.668 1.00 45.27  ? 302 HIS A N   1 
ATOM   2304  C CA  . HIS A  1 302 ? -16.045 -49.982  -26.921 1.00 47.63  ? 302 HIS A CA  1 
ATOM   2305  C C   . HIS A  1 302 ? -17.024 -50.533  -27.955 1.00 48.63  ? 302 HIS A C   1 
ATOM   2306  O O   . HIS A  1 302 ? -17.203 -51.747  -28.062 1.00 52.13  ? 302 HIS A O   1 
ATOM   2307  C CB  . HIS A  1 302 ? -14.619 -50.023  -27.473 1.00 42.64  ? 302 HIS A CB  1 
ATOM   2308  C CG  . HIS A  1 302 ? -14.304 -48.906  -28.418 1.00 50.61  ? 302 HIS A CG  1 
ATOM   2309  N ND1 . HIS A  1 302 ? -14.679 -48.923  -29.744 1.00 50.14  ? 302 HIS A ND1 1 
ATOM   2310  C CD2 . HIS A  1 302 ? -13.643 -47.739  -28.229 1.00 47.63  ? 302 HIS A CD2 1 
ATOM   2311  C CE1 . HIS A  1 302 ? -14.266 -47.813  -30.330 1.00 52.80  ? 302 HIS A CE1 1 
ATOM   2312  N NE2 . HIS A  1 302 ? -13.635 -47.079  -29.433 1.00 40.60  ? 302 HIS A NE2 1 
ATOM   2313  N N   . PRO A  1 303 ? -17.664 -49.633  -28.718 1.00 41.91  ? 303 PRO A N   1 
ATOM   2314  C CA  . PRO A  1 303 ? -18.625 -49.986  -29.770 1.00 40.00  ? 303 PRO A CA  1 
ATOM   2315  C C   . PRO A  1 303 ? -17.953 -50.636  -30.976 1.00 44.52  ? 303 PRO A C   1 
ATOM   2316  O O   . PRO A  1 303 ? -18.453 -51.637  -31.491 1.00 43.90  ? 303 PRO A O   1 
ATOM   2317  C CB  . PRO A  1 303 ? -19.219 -48.630  -30.175 1.00 38.57  ? 303 PRO A CB  1 
ATOM   2318  C CG  . PRO A  1 303 ? -18.897 -47.705  -29.044 1.00 48.14  ? 303 PRO A CG  1 
ATOM   2319  C CD  . PRO A  1 303 ? -17.584 -48.178  -28.517 1.00 50.53  ? 303 PRO A CD  1 
ATOM   2320  N N   . ILE A  1 304 ? -16.839 -50.067  -31.424 1.00 37.93  ? 304 ILE A N   1 
ATOM   2321  C CA  . ILE A  1 304 ? -16.102 -50.626  -32.552 1.00 45.53  ? 304 ILE A CA  1 
ATOM   2322  C C   . ILE A  1 304 ? -15.290 -51.834  -32.100 1.00 43.03  ? 304 ILE A C   1 
ATOM   2323  O O   . ILE A  1 304 ? -14.462 -51.735  -31.195 1.00 53.39  ? 304 ILE A O   1 
ATOM   2324  C CB  . ILE A  1 304 ? -15.178 -49.587  -33.214 1.00 39.77  ? 304 ILE A CB  1 
ATOM   2325  C CG1 . ILE A  1 304 ? -15.994 -48.609  -34.063 1.00 36.08  ? 304 ILE A CG1 1 
ATOM   2326  C CG2 . ILE A  1 304 ? -14.146 -50.278  -34.089 1.00 58.39  ? 304 ILE A CG2 1 
ATOM   2327  C CD1 . ILE A  1 304 ? -16.978 -47.770  -33.276 1.00 57.32  ? 304 ILE A CD1 1 
ATOM   2328  N N   . THR A  1 305 ? -15.534 -52.973  -32.737 1.00 37.81  ? 305 THR A N   1 
ATOM   2329  C CA  . THR A  1 305 ? -14.955 -54.231  -32.289 1.00 29.65  ? 305 THR A CA  1 
ATOM   2330  C C   . THR A  1 305 ? -14.610 -55.128  -33.474 1.00 53.16  ? 305 THR A C   1 
ATOM   2331  O O   . THR A  1 305 ? -15.233 -55.039  -34.532 1.00 56.79  ? 305 THR A O   1 
ATOM   2332  C CB  . THR A  1 305 ? -15.936 -54.973  -31.357 1.00 43.21  ? 305 THR A CB  1 
ATOM   2333  O OG1 . THR A  1 305 ? -15.235 -55.481  -30.216 1.00 65.98  ? 305 THR A OG1 1 
ATOM   2334  C CG2 . THR A  1 305 ? -16.625 -56.118  -32.094 1.00 43.70  ? 305 THR A CG2 1 
ATOM   2335  N N   . ILE A  1 306 ? -13.609 -55.985  -33.294 1.00 46.61  ? 306 ILE A N   1 
ATOM   2336  C CA  . ILE A  1 306 ? -13.246 -56.957  -34.320 1.00 41.09  ? 306 ILE A CA  1 
ATOM   2337  C C   . ILE A  1 306 ? -13.142 -58.359  -33.733 1.00 38.64  ? 306 ILE A C   1 
ATOM   2338  O O   . ILE A  1 306 ? -12.586 -58.548  -32.652 1.00 45.26  ? 306 ILE A O   1 
ATOM   2339  C CB  . ILE A  1 306 ? -11.913 -56.607  -35.004 1.00 32.61  ? 306 ILE A CB  1 
ATOM   2340  C CG1 . ILE A  1 306 ? -11.930 -55.166  -35.514 1.00 43.91  ? 306 ILE A CG1 1 
ATOM   2341  C CG2 . ILE A  1 306 ? -11.643 -57.565  -36.150 1.00 35.55  ? 306 ILE A CG2 1 
ATOM   2342  C CD1 . ILE A  1 306 ? -10.725 -54.805  -36.358 1.00 38.17  ? 306 ILE A CD1 1 
ATOM   2343  N N   . GLY A  1 307 ? -13.679 -59.338  -34.453 1.00 44.56  ? 307 GLY A N   1 
ATOM   2344  C CA  . GLY A  1 307 ? -13.658 -60.719  -34.005 1.00 46.99  ? 307 GLY A CA  1 
ATOM   2345  C C   . GLY A  1 307 ? -15.028 -61.212  -33.583 1.00 48.48  ? 307 GLY A C   1 
ATOM   2346  O O   . GLY A  1 307 ? -16.047 -60.742  -34.091 1.00 62.85  ? 307 GLY A O   1 
ATOM   2347  N N   . LYS A  1 308 ? -15.051 -62.150  -32.640 1.00 48.27  ? 308 LYS A N   1 
ATOM   2348  C CA  . LYS A  1 308 ? -16.299 -62.695  -32.117 1.00 50.34  ? 308 LYS A CA  1 
ATOM   2349  C C   . LYS A  1 308 ? -16.521 -62.135  -30.721 1.00 41.15  ? 308 LYS A C   1 
ATOM   2350  O O   . LYS A  1 308 ? -16.092 -62.733  -29.733 1.00 57.88  ? 308 LYS A O   1 
ATOM   2351  C CB  . LYS A  1 308 ? -16.221 -64.221  -32.060 1.00 52.63  ? 308 LYS A CB  1 
ATOM   2352  C CG  . LYS A  1 308 ? -17.538 -64.926  -31.760 1.00 68.31  ? 308 LYS A CG  1 
ATOM   2353  C CD  . LYS A  1 308 ? -17.331 -66.004  -30.701 1.00 78.93  ? 308 LYS A CD  1 
ATOM   2354  C CE  . LYS A  1 308 ? -18.451 -67.035  -30.696 1.00 75.32  ? 308 LYS A CE  1 
ATOM   2355  N NZ  . LYS A  1 308 ? -18.440 -67.862  -31.931 1.00 91.10  ? 308 LYS A NZ  1 
ATOM   2356  N N   . CYS A  1 309 ? -17.200 -60.994  -30.640 1.00 57.70  ? 309 CYS A N   1 
ATOM   2357  C CA  . CYS A  1 309 ? -17.239 -60.220  -29.404 1.00 52.11  ? 309 CYS A CA  1 
ATOM   2358  C C   . CYS A  1 309 ? -18.596 -60.202  -28.706 1.00 44.66  ? 309 CYS A C   1 
ATOM   2359  O O   . CYS A  1 309 ? -19.630 -60.439  -29.331 1.00 50.54  ? 309 CYS A O   1 
ATOM   2360  C CB  . CYS A  1 309 ? -16.790 -58.786  -29.688 1.00 38.21  ? 309 CYS A CB  1 
ATOM   2361  S SG  . CYS A  1 309 ? -15.223 -58.683  -30.578 1.00 71.32  ? 309 CYS A SG  1 
ATOM   2362  N N   . PRO A  1 310 ? -18.587 -59.918  -27.394 1.00 45.88  ? 310 PRO A N   1 
ATOM   2363  C CA  . PRO A  1 310 ? -19.822 -59.691  -26.642 1.00 44.43  ? 310 PRO A CA  1 
ATOM   2364  C C   . PRO A  1 310 ? -20.531 -58.480  -27.222 1.00 44.85  ? 310 PRO A C   1 
ATOM   2365  O O   . PRO A  1 310 ? -19.894 -57.661  -27.884 1.00 43.21  ? 310 PRO A O   1 
ATOM   2366  C CB  . PRO A  1 310 ? -19.321 -59.375  -25.229 1.00 35.89  ? 310 PRO A CB  1 
ATOM   2367  C CG  . PRO A  1 310 ? -17.960 -59.977  -25.161 1.00 49.73  ? 310 PRO A CG  1 
ATOM   2368  C CD  . PRO A  1 310 ? -17.394 -59.830  -26.537 1.00 42.50  ? 310 PRO A CD  1 
ATOM   2369  N N   . LYS A  1 311 ? -21.829 -58.365  -26.981 1.00 45.60  ? 311 LYS A N   1 
ATOM   2370  C CA  . LYS A  1 311 ? -22.594 -57.266  -27.545 1.00 39.67  ? 311 LYS A CA  1 
ATOM   2371  C C   . LYS A  1 311 ? -22.330 -55.964  -26.796 1.00 36.87  ? 311 LYS A C   1 
ATOM   2372  O O   . LYS A  1 311 ? -22.256 -55.951  -25.567 1.00 46.43  ? 311 LYS A O   1 
ATOM   2373  C CB  . LYS A  1 311 ? -24.082 -57.605  -27.538 1.00 36.46  ? 311 LYS A CB  1 
ATOM   2374  C CG  . LYS A  1 311 ? -24.734 -57.454  -28.894 1.00 39.79  ? 311 LYS A CG  1 
ATOM   2375  C CD  . LYS A  1 311 ? -23.925 -58.124  -29.993 1.00 32.60  ? 311 LYS A CD  1 
ATOM   2376  C CE  . LYS A  1 311 ? -24.420 -59.530  -30.277 1.00 43.35  ? 311 LYS A CE  1 
ATOM   2377  N NZ  . LYS A  1 311 ? -23.902 -60.029  -31.581 1.00 47.20  ? 311 LYS A NZ  1 
ATOM   2378  N N   . TYR A  1 312 ? -22.177 -54.871  -27.538 1.00 37.48  ? 312 TYR A N   1 
ATOM   2379  C CA  . TYR A  1 312 ? -21.914 -53.577  -26.919 1.00 36.19  ? 312 TYR A CA  1 
ATOM   2380  C C   . TYR A  1 312 ? -23.166 -53.002  -26.267 1.00 42.69  ? 312 TYR A C   1 
ATOM   2381  O O   . TYR A  1 312 ? -24.212 -52.878  -26.904 1.00 54.08  ? 312 TYR A O   1 
ATOM   2382  C CB  . TYR A  1 312 ? -21.339 -52.578  -27.924 1.00 30.27  ? 312 TYR A CB  1 
ATOM   2383  C CG  . TYR A  1 312 ? -21.099 -51.213  -27.319 1.00 36.22  ? 312 TYR A CG  1 
ATOM   2384  C CD1 . TYR A  1 312 ? -20.138 -51.031  -26.334 1.00 39.66  ? 312 TYR A CD1 1 
ATOM   2385  C CD2 . TYR A  1 312 ? -21.838 -50.110  -27.724 1.00 44.89  ? 312 TYR A CD2 1 
ATOM   2386  C CE1 . TYR A  1 312 ? -19.918 -49.789  -25.770 1.00 33.45  ? 312 TYR A CE1 1 
ATOM   2387  C CE2 . TYR A  1 312 ? -21.623 -48.863  -27.166 1.00 37.39  ? 312 TYR A CE2 1 
ATOM   2388  C CZ  . TYR A  1 312 ? -20.662 -48.709  -26.190 1.00 42.38  ? 312 TYR A CZ  1 
ATOM   2389  O OH  . TYR A  1 312 ? -20.445 -47.470  -25.631 1.00 47.09  ? 312 TYR A OH  1 
ATOM   2390  N N   . VAL A  1 313 ? -23.045 -52.651  -24.992 1.00 47.25  ? 313 VAL A N   1 
ATOM   2391  C CA  . VAL A  1 313 ? -24.165 -52.119  -24.230 1.00 39.43  ? 313 VAL A CA  1 
ATOM   2392  C C   . VAL A  1 313 ? -23.762 -50.839  -23.505 1.00 36.09  ? 313 VAL A C   1 
ATOM   2393  O O   . VAL A  1 313 ? -22.615 -50.686  -23.085 1.00 49.66  ? 313 VAL A O   1 
ATOM   2394  C CB  . VAL A  1 313 ? -24.686 -53.153  -23.211 1.00 45.13  ? 313 VAL A CB  1 
ATOM   2395  C CG1 . VAL A  1 313 ? -25.796 -52.558  -22.368 1.00 56.37  ? 313 VAL A CG1 1 
ATOM   2396  C CG2 . VAL A  1 313 ? -25.175 -54.401  -23.929 1.00 48.49  ? 313 VAL A CG2 1 
ATOM   2397  N N   . LYS A  1 314 ? -24.713 -49.921  -23.365 1.00 44.73  ? 314 LYS A N   1 
ATOM   2398  C CA  . LYS A  1 314 ? -24.458 -48.630  -22.738 1.00 46.63  ? 314 LYS A CA  1 
ATOM   2399  C C   . LYS A  1 314 ? -24.580 -48.726  -21.221 1.00 44.11  ? 314 LYS A C   1 
ATOM   2400  O O   . LYS A  1 314 ? -24.445 -47.729  -20.511 1.00 54.04  ? 314 LYS A O   1 
ATOM   2401  C CB  . LYS A  1 314 ? -25.442 -47.593  -23.278 1.00 42.06  ? 314 LYS A CB  1 
ATOM   2402  C CG  . LYS A  1 314 ? -24.992 -46.151  -23.135 1.00 55.88  ? 314 LYS A CG  1 
ATOM   2403  C CD  . LYS A  1 314 ? -25.997 -45.227  -23.794 1.00 87.65  ? 314 LYS A CD  1 
ATOM   2404  C CE  . LYS A  1 314 ? -26.295 -45.683  -25.214 1.00 94.91  ? 314 LYS A CE  1 
ATOM   2405  N NZ  . LYS A  1 314 ? -27.569 -45.111  -25.731 1.00 76.57  ? 314 LYS A NZ  1 
ATOM   2406  N N   . SER A  1 315 ? -24.835 -49.934  -20.730 1.00 48.27  ? 315 SER A N   1 
ATOM   2407  C CA  . SER A  1 315 ? -25.020 -50.161  -19.302 1.00 50.57  ? 315 SER A CA  1 
ATOM   2408  C C   . SER A  1 315 ? -23.747 -49.897  -18.508 1.00 51.69  ? 315 SER A C   1 
ATOM   2409  O O   . SER A  1 315 ? -22.638 -50.048  -19.020 1.00 46.66  ? 315 SER A O   1 
ATOM   2410  C CB  . SER A  1 315 ? -25.500 -51.590  -19.045 1.00 52.63  ? 315 SER A CB  1 
ATOM   2411  O OG  . SER A  1 315 ? -26.771 -51.814  -19.626 1.00 72.72  ? 315 SER A OG  1 
ATOM   2412  N N   . THR A  1 316 ? -23.921 -49.501  -17.253 1.00 58.21  ? 316 THR A N   1 
ATOM   2413  C CA  . THR A  1 316 ? -22.801 -49.305  -16.342 1.00 52.08  ? 316 THR A CA  1 
ATOM   2414  C C   . THR A  1 316 ? -22.577 -50.569  -15.524 1.00 54.75  ? 316 THR A C   1 
ATOM   2415  O O   . THR A  1 316 ? -21.444 -50.918  -15.194 1.00 66.96  ? 316 THR A O   1 
ATOM   2416  C CB  . THR A  1 316 ? -23.050 -48.122  -15.391 1.00 60.84  ? 316 THR A CB  1 
ATOM   2417  O OG1 . THR A  1 316 ? -22.143 -48.199  -14.284 1.00 75.97  ? 316 THR A OG1 1 
ATOM   2418  C CG2 . THR A  1 316 ? -24.478 -48.151  -14.866 1.00 68.88  ? 316 THR A CG2 1 
ATOM   2419  N N   . LYS A  1 317 ? -23.672 -51.250  -15.203 1.00 65.62  ? 317 LYS A N   1 
ATOM   2420  C CA  . LYS A  1 317 ? -23.612 -52.502  -14.462 1.00 62.21  ? 317 LYS A CA  1 
ATOM   2421  C C   . LYS A  1 317 ? -24.780 -53.406  -14.833 1.00 58.48  ? 317 LYS A C   1 
ATOM   2422  O O   . LYS A  1 317 ? -25.889 -52.934  -15.086 1.00 56.85  ? 317 LYS A O   1 
ATOM   2423  C CB  . LYS A  1 317 ? -23.609 -52.237  -12.955 1.00 64.70  ? 317 LYS A CB  1 
ATOM   2424  C CG  . LYS A  1 317 ? -24.763 -51.372  -12.477 1.00 77.47  ? 317 LYS A CG  1 
ATOM   2425  C CD  . LYS A  1 317 ? -24.772 -51.240  -10.961 1.00 99.01  ? 317 LYS A CD  1 
ATOM   2426  C CE  . LYS A  1 317 ? -25.092 -52.566  -10.290 1.00 92.97  ? 317 LYS A CE  1 
ATOM   2427  N NZ  . LYS A  1 317 ? -25.149 -52.439  -8.808  1.00 73.38  ? 317 LYS A NZ  1 
ATOM   2428  N N   . LEU A  1 318 ? -24.519 -54.708  -14.869 1.00 62.89  ? 318 LEU A N   1 
ATOM   2429  C CA  . LEU A  1 318 ? -25.548 -55.698  -15.152 1.00 51.34  ? 318 LEU A CA  1 
ATOM   2430  C C   . LEU A  1 318 ? -25.442 -56.854  -14.171 1.00 52.88  ? 318 LEU A C   1 
ATOM   2431  O O   . LEU A  1 318 ? -25.314 -58.009  -14.578 1.00 58.94  ? 318 LEU A O   1 
ATOM   2432  C CB  . LEU A  1 318 ? -25.405 -56.230  -16.578 1.00 47.53  ? 318 LEU A CB  1 
ATOM   2433  C CG  . LEU A  1 318 ? -25.815 -55.305  -17.724 1.00 51.93  ? 318 LEU A CG  1 
ATOM   2434  C CD1 . LEU A  1 318 ? -25.430 -55.920  -19.061 1.00 51.29  ? 318 LEU A CD1 1 
ATOM   2435  C CD2 . LEU A  1 318 ? -27.307 -55.018  -17.669 1.00 36.24  ? 318 LEU A CD2 1 
ATOM   2436  N N   . ARG A  1 319 ? -25.492 -56.546  -12.879 1.00 60.44  ? 319 ARG A N   1 
ATOM   2437  C CA  . ARG A  1 319 ? -25.339 -57.584  -11.866 1.00 58.32  ? 319 ARG A CA  1 
ATOM   2438  C C   . ARG A  1 319 ? -26.573 -58.478  -11.791 1.00 49.71  ? 319 ARG A C   1 
ATOM   2439  O O   . ARG A  1 319 ? -27.702 -58.000  -11.669 1.00 36.85  ? 319 ARG A O   1 
ATOM   2440  C CB  . ARG A  1 319 ? -24.990 -56.991  -10.495 1.00 66.40  ? 319 ARG A CB  1 
ATOM   2441  C CG  . ARG A  1 319 ? -24.721 -58.045  -9.421  1.00 64.14  ? 319 ARG A CG  1 
ATOM   2442  C CD  . ARG A  1 319 ? -23.838 -57.530  -8.283  1.00 67.11  ? 319 ARG A CD  1 
ATOM   2443  N NE  . ARG A  1 319 ? -22.414 -57.547  -8.616  1.00 77.40  ? 319 ARG A NE  1 
ATOM   2444  C CZ  . ARG A  1 319 ? -21.688 -58.654  -8.750  1.00 78.18  ? 319 ARG A CZ  1 
ATOM   2445  N NH1 . ARG A  1 319 ? -22.249 -59.847  -8.605  1.00 77.63  ? 319 ARG A NH1 1 
ATOM   2446  N NH2 . ARG A  1 319 ? -20.398 -58.574  -9.045  1.00 84.95  ? 319 ARG A NH2 1 
ATOM   2447  N N   . LEU A  1 320 ? -26.337 -59.782  -11.885 1.00 54.30  ? 320 LEU A N   1 
ATOM   2448  C CA  . LEU A  1 320 ? -27.394 -60.779  -11.879 1.00 47.29  ? 320 LEU A CA  1 
ATOM   2449  C C   . LEU A  1 320 ? -27.428 -61.441  -10.510 1.00 54.96  ? 320 LEU A C   1 
ATOM   2450  O O   . LEU A  1 320 ? -26.402 -61.899  -10.024 1.00 61.92  ? 320 LEU A O   1 
ATOM   2451  C CB  . LEU A  1 320 ? -27.098 -61.827  -12.952 1.00 51.53  ? 320 LEU A CB  1 
ATOM   2452  C CG  . LEU A  1 320 ? -28.184 -62.832  -13.331 1.00 57.55  ? 320 LEU A CG  1 
ATOM   2453  C CD1 . LEU A  1 320 ? -29.363 -62.106  -13.954 1.00 46.04  ? 320 LEU A CD1 1 
ATOM   2454  C CD2 . LEU A  1 320 ? -27.640 -63.887  -14.288 1.00 46.50  ? 320 LEU A CD2 1 
ATOM   2455  N N   . ALA A  1 321 ? -28.594 -61.492  -9.879  1.00 49.83  ? 321 ALA A N   1 
ATOM   2456  C CA  . ALA A  1 321 ? -28.686 -62.107  -8.559  1.00 51.03  ? 321 ALA A CA  1 
ATOM   2457  C C   . ALA A  1 321 ? -28.612 -63.631  -8.657  1.00 56.62  ? 321 ALA A C   1 
ATOM   2458  O O   . ALA A  1 321 ? -29.331 -64.242  -9.448  1.00 62.45  ? 321 ALA A O   1 
ATOM   2459  C CB  . ALA A  1 321 ? -29.959 -61.671  -7.847  1.00 41.43  ? 321 ALA A CB  1 
ATOM   2460  N N   . THR A  1 322 ? -27.729 -64.240  -7.868  1.00 61.78  ? 322 THR A N   1 
ATOM   2461  C CA  . THR A  1 322 ? -27.635 -65.700  -7.806  1.00 58.98  ? 322 THR A CA  1 
ATOM   2462  C C   . THR A  1 322 ? -28.129 -66.235  -6.471  1.00 59.48  ? 322 THR A C   1 
ATOM   2463  O O   . THR A  1 322 ? -28.797 -67.266  -6.413  1.00 49.78  ? 322 THR A O   1 
ATOM   2464  C CB  . THR A  1 322 ? -26.196 -66.219  -8.006  1.00 62.67  ? 322 THR A CB  1 
ATOM   2465  O OG1 . THR A  1 322 ? -25.320 -65.604  -7.054  1.00 72.36  ? 322 THR A OG1 1 
ATOM   2466  C CG2 . THR A  1 322 ? -25.708 -65.939  -9.408  1.00 68.05  ? 322 THR A CG2 1 
ATOM   2467  N N   . GLY A  1 323 ? -27.770 -65.540  -5.397  1.00 67.34  ? 323 GLY A N   1 
ATOM   2468  C CA  . GLY A  1 323 ? -28.229 -65.902  -4.070  1.00 66.58  ? 323 GLY A CA  1 
ATOM   2469  C C   . GLY A  1 323 ? -29.618 -65.353  -3.813  1.00 68.49  ? 323 GLY A C   1 
ATOM   2470  O O   . GLY A  1 323 ? -30.337 -65.002  -4.749  1.00 62.21  ? 323 GLY A O   1 
ATOM   2471  N N   . LEU A  1 324 ? -29.989 -65.277  -2.539  1.00 61.61  ? 324 LEU A N   1 
ATOM   2472  C CA  . LEU A  1 324 ? -31.292 -64.761  -2.134  1.00 56.96  ? 324 LEU A CA  1 
ATOM   2473  C C   . LEU A  1 324 ? -31.172 -63.361  -1.536  1.00 67.19  ? 324 LEU A C   1 
ATOM   2474  O O   . LEU A  1 324 ? -30.192 -62.660  -1.782  1.00 79.39  ? 324 LEU A O   1 
ATOM   2475  C CB  . LEU A  1 324 ? -31.954 -65.706  -1.125  1.00 63.32  ? 324 LEU A CB  1 
ATOM   2476  C CG  . LEU A  1 324 ? -31.090 -66.279  0.001   1.00 72.38  ? 324 LEU A CG  1 
ATOM   2477  C CD1 . LEU A  1 324 ? -31.962 -66.752  1.145   1.00 76.45  ? 324 LEU A CD1 1 
ATOM   2478  C CD2 . LEU A  1 324 ? -30.224 -67.417  -0.511  1.00 62.97  ? 324 LEU A CD2 1 
ATOM   2479  N N   . ARG A  1 325 ? -32.184 -62.960  -0.766  1.00 62.13  ? 325 ARG A N   1 
ATOM   2480  C CA  . ARG A  1 325 ? -32.144 -61.706  -0.016  1.00 67.83  ? 325 ARG A CA  1 
ATOM   2481  C C   . ARG A  1 325 ? -31.008 -61.751  1.013   1.00 79.58  ? 325 ARG A C   1 
ATOM   2482  O O   . ARG A  1 325 ? -30.269 -62.735  1.075   1.00 79.87  ? 325 ARG A O   1 
ATOM   2483  C CB  . ARG A  1 325 ? -33.486 -61.419  0.659   1.00 67.34  ? 325 ARG A CB  1 
ATOM   2484  C CG  . ARG A  1 325 ? -34.489 -60.688  -0.231  1.00 60.87  ? 325 ARG A CG  1 
ATOM   2485  C CD  . ARG A  1 325 ? -34.640 -59.222  0.167   1.00 78.67  ? 325 ARG A CD  1 
ATOM   2486  N NE  . ARG A  1 325 ? -35.964 -58.940  0.720   1.00 85.51  ? 325 ARG A NE  1 
ATOM   2487  C CZ  . ARG A  1 325 ? -37.013 -58.533  0.008   1.00 90.88  ? 325 ARG A CZ  1 
ATOM   2488  N NH1 . ARG A  1 325 ? -36.911 -58.349  -1.303  1.00 80.08  ? 325 ARG A NH1 1 
ATOM   2489  N NH2 . ARG A  1 325 ? -38.171 -58.307  0.612   1.00 85.36  ? 325 ARG A NH2 1 
ATOM   2490  N N   . ASN A  1 326 ? -30.846 -60.681  1.790   1.00 86.94  ? 326 ASN A N   1 
ATOM   2491  C CA  . ASN A  1 326 ? -29.809 -60.649  2.825   1.00 86.70  ? 326 ASN A CA  1 
ATOM   2492  C C   . ASN A  1 326 ? -30.226 -59.887  4.081   1.00 97.38  ? 326 ASN A C   1 
ATOM   2493  O O   . ASN A  1 326 ? -30.798 -58.797  4.025   1.00 98.40  ? 326 ASN A O   1 
ATOM   2494  C CB  . ASN A  1 326 ? -28.482 -60.113  2.282   1.00 99.40  ? 326 ASN A CB  1 
ATOM   2495  C CG  . ASN A  1 326 ? -27.292 -60.507  3.152   1.00 102.30 ? 326 ASN A CG  1 
ATOM   2496  O OD1 . ASN A  1 326 ? -27.251 -61.604  3.713   1.00 98.14  ? 326 ASN A OD1 1 
ATOM   2497  N ND2 . ASN A  1 326 ? -26.315 -59.614  3.257   1.00 105.34 ? 326 ASN A ND2 1 
ATOM   2498  N N   . ILE A  1 327 ? -29.895 -60.471  5.220   1.00 106.08 ? 327 ILE A N   1 
ATOM   2499  C CA  . ILE A  1 327 ? -30.499 -60.082  6.472   1.00 99.13  ? 327 ILE A CA  1 
ATOM   2500  C C   . ILE A  1 327 ? -29.443 -60.264  7.564   1.00 92.50  ? 327 ILE A C   1 
ATOM   2501  O O   . ILE A  1 327 ? -28.283 -60.544  7.264   1.00 76.06  ? 327 ILE A O   1 
ATOM   2502  C CB  . ILE A  1 327 ? -31.777 -60.954  6.686   1.00 84.44  ? 327 ILE A CB  1 
ATOM   2503  C CG1 . ILE A  1 327 ? -33.028 -60.224  6.161   1.00 73.60  ? 327 ILE A CG1 1 
ATOM   2504  C CG2 . ILE A  1 327 ? -31.923 -61.437  8.124   1.00 93.62  ? 327 ILE A CG2 1 
ATOM   2505  C CD1 . ILE A  1 327 ? -33.592 -60.760  4.814   1.00 61.99  ? 327 ILE A CD1 1 
ATOM   2506  N N   . GLY B  2 1   ? -41.011 -62.824  -1.432  1.00 100.71 ? 1   GLY B N   1 
ATOM   2507  C CA  . GLY B  2 1   ? -41.632 -61.762  -2.200  1.00 81.26  ? 1   GLY B CA  1 
ATOM   2508  C C   . GLY B  2 1   ? -42.937 -62.173  -2.855  1.00 68.20  ? 1   GLY B C   1 
ATOM   2509  O O   . GLY B  2 1   ? -43.876 -61.380  -2.929  1.00 75.56  ? 1   GLY B O   1 
ATOM   2510  N N   . LEU B  2 2   ? -43.002 -63.414  -3.328  1.00 65.95  ? 2   LEU B N   1 
ATOM   2511  C CA  . LEU B  2 2   ? -44.183 -63.889  -4.042  1.00 67.75  ? 2   LEU B CA  1 
ATOM   2512  C C   . LEU B  2 2   ? -44.875 -65.063  -3.348  1.00 66.76  ? 2   LEU B C   1 
ATOM   2513  O O   . LEU B  2 2   ? -46.076 -65.270  -3.519  1.00 61.61  ? 2   LEU B O   1 
ATOM   2514  C CB  . LEU B  2 2   ? -43.824 -64.267  -5.481  1.00 68.21  ? 2   LEU B CB  1 
ATOM   2515  C CG  . LEU B  2 2   ? -44.967 -64.155  -6.492  1.00 70.80  ? 2   LEU B CG  1 
ATOM   2516  C CD1 . LEU B  2 2   ? -45.477 -62.720  -6.566  1.00 58.54  ? 2   LEU B CD1 1 
ATOM   2517  C CD2 . LEU B  2 2   ? -44.532 -64.649  -7.862  1.00 43.99  ? 2   LEU B CD2 1 
ATOM   2518  N N   . PHE B  2 3   ? -44.119 -65.830  -2.568  1.00 74.06  ? 3   PHE B N   1 
ATOM   2519  C CA  . PHE B  2 3   ? -44.674 -67.000  -1.891  1.00 75.03  ? 3   PHE B CA  1 
ATOM   2520  C C   . PHE B  2 3   ? -44.872 -66.783  -0.391  1.00 85.29  ? 3   PHE B C   1 
ATOM   2521  O O   . PHE B  2 3   ? -45.221 -67.713  0.336   1.00 88.85  ? 3   PHE B O   1 
ATOM   2522  C CB  . PHE B  2 3   ? -43.805 -68.235  -2.142  1.00 76.99  ? 3   PHE B CB  1 
ATOM   2523  C CG  . PHE B  2 3   ? -43.877 -68.749  -3.552  1.00 79.10  ? 3   PHE B CG  1 
ATOM   2524  C CD1 . PHE B  2 3   ? -43.034 -68.249  -4.530  1.00 77.98  ? 3   PHE B CD1 1 
ATOM   2525  C CD2 . PHE B  2 3   ? -44.789 -69.732  -3.900  1.00 80.18  ? 3   PHE B CD2 1 
ATOM   2526  C CE1 . PHE B  2 3   ? -43.098 -68.719  -5.827  1.00 75.41  ? 3   PHE B CE1 1 
ATOM   2527  C CE2 . PHE B  2 3   ? -44.858 -70.206  -5.196  1.00 75.71  ? 3   PHE B CE2 1 
ATOM   2528  C CZ  . PHE B  2 3   ? -44.011 -69.698  -6.161  1.00 74.38  ? 3   PHE B CZ  1 
ATOM   2529  N N   . GLY B  2 4   ? -44.645 -65.555  0.064   1.00 80.05  ? 4   GLY B N   1 
ATOM   2530  C CA  . GLY B  2 4   ? -44.892 -65.185  1.447   1.00 74.19  ? 4   GLY B CA  1 
ATOM   2531  C C   . GLY B  2 4   ? -43.867 -65.674  2.454   1.00 75.92  ? 4   GLY B C   1 
ATOM   2532  O O   . GLY B  2 4   ? -43.941 -65.331  3.634   1.00 79.72  ? 4   GLY B O   1 
ATOM   2533  N N   . ALA B  2 5   ? -42.903 -66.467  1.996   1.00 80.04  ? 5   ALA B N   1 
ATOM   2534  C CA  . ALA B  2 5   ? -41.925 -67.073  2.897   1.00 68.11  ? 5   ALA B CA  1 
ATOM   2535  C C   . ALA B  2 5   ? -40.770 -66.136  3.255   1.00 69.14  ? 5   ALA B C   1 
ATOM   2536  O O   . ALA B  2 5   ? -40.703 -65.621  4.371   1.00 68.78  ? 5   ALA B O   1 
ATOM   2537  C CB  . ALA B  2 5   ? -41.395 -68.375  2.311   1.00 59.03  ? 5   ALA B CB  1 
ATOM   2538  N N   . ILE B  2 6   ? -39.859 -65.929  2.310   1.00 71.31  ? 6   ILE B N   1 
ATOM   2539  C CA  . ILE B  2 6   ? -38.698 -65.077  2.543   1.00 57.83  ? 6   ILE B CA  1 
ATOM   2540  C C   . ILE B  2 6   ? -39.117 -63.620  2.700   1.00 71.88  ? 6   ILE B C   1 
ATOM   2541  O O   . ILE B  2 6   ? -39.806 -63.067  1.843   1.00 75.22  ? 6   ILE B O   1 
ATOM   2542  C CB  . ILE B  2 6   ? -37.661 -65.204  1.411   1.00 58.04  ? 6   ILE B CB  1 
ATOM   2543  C CG1 . ILE B  2 6   ? -37.194 -66.655  1.285   1.00 54.16  ? 6   ILE B CG1 1 
ATOM   2544  C CG2 . ILE B  2 6   ? -36.477 -64.286  1.665   1.00 52.18  ? 6   ILE B CG2 1 
ATOM   2545  C CD1 . ILE B  2 6   ? -36.045 -66.847  0.320   1.00 54.35  ? 6   ILE B CD1 1 
ATOM   2546  N N   . ALA B  2 7   ? -38.695 -63.008  3.803   1.00 68.04  ? 7   ALA B N   1 
ATOM   2547  C CA  . ALA B  2 7   ? -39.118 -61.656  4.149   1.00 66.63  ? 7   ALA B CA  1 
ATOM   2548  C C   . ALA B  2 7   ? -40.628 -61.616  4.367   1.00 75.33  ? 7   ALA B C   1 
ATOM   2549  O O   . ALA B  2 7   ? -41.263 -60.573  4.213   1.00 83.50  ? 7   ALA B O   1 
ATOM   2550  C CB  . ALA B  2 7   ? -38.698 -60.665  3.073   1.00 64.67  ? 7   ALA B CB  1 
ATOM   2551  N N   . GLY B  2 8   ? -41.192 -62.767  4.723   1.00 68.77  ? 8   GLY B N   1 
ATOM   2552  C CA  . GLY B  2 8   ? -42.614 -62.887  4.995   1.00 74.31  ? 8   GLY B CA  1 
ATOM   2553  C C   . GLY B  2 8   ? -42.872 -63.351  6.417   1.00 89.99  ? 8   GLY B C   1 
ATOM   2554  O O   . GLY B  2 8   ? -42.513 -62.659  7.370   1.00 91.25  ? 8   GLY B O   1 
ATOM   2555  N N   . PHE B  2 9   ? -43.490 -64.520  6.568   1.00 69.77  ? 9   PHE B N   1 
ATOM   2556  C CA  . PHE B  2 9   ? -43.750 -65.067  7.899   1.00 69.67  ? 9   PHE B CA  1 
ATOM   2557  C C   . PHE B  2 9   ? -42.470 -65.593  8.545   1.00 82.17  ? 9   PHE B C   1 
ATOM   2558  O O   . PHE B  2 9   ? -42.400 -65.765  9.762   1.00 99.21  ? 9   PHE B O   1 
ATOM   2559  C CB  . PHE B  2 9   ? -44.847 -66.140  7.873   1.00 76.24  ? 9   PHE B CB  1 
ATOM   2560  C CG  . PHE B  2 9   ? -44.568 -67.289  6.945   1.00 76.62  ? 9   PHE B CG  1 
ATOM   2561  C CD1 . PHE B  2 9   ? -43.653 -68.271  7.286   1.00 84.28  ? 9   PHE B CD1 1 
ATOM   2562  C CD2 . PHE B  2 9   ? -45.247 -67.403  5.743   1.00 89.09  ? 9   PHE B CD2 1 
ATOM   2563  C CE1 . PHE B  2 9   ? -43.406 -69.335  6.436   1.00 84.60  ? 9   PHE B CE1 1 
ATOM   2564  C CE2 . PHE B  2 9   ? -45.005 -68.464  4.891   1.00 88.48  ? 9   PHE B CE2 1 
ATOM   2565  C CZ  . PHE B  2 9   ? -44.083 -69.430  5.237   1.00 93.21  ? 9   PHE B CZ  1 
ATOM   2566  N N   . ILE B  2 10  ? -41.468 -65.856  7.712   1.00 75.62  ? 10  ILE B N   1 
ATOM   2567  C CA  . ILE B  2 10  ? -40.105 -66.074  8.176   1.00 73.68  ? 10  ILE B CA  1 
ATOM   2568  C C   . ILE B  2 10  ? -39.336 -64.806  7.830   1.00 76.14  ? 10  ILE B C   1 
ATOM   2569  O O   . ILE B  2 10  ? -38.909 -64.632  6.694   1.00 78.31  ? 10  ILE B O   1 
ATOM   2570  C CB  . ILE B  2 10  ? -39.436 -67.265  7.461   1.00 64.58  ? 10  ILE B CB  1 
ATOM   2571  C CG1 . ILE B  2 10  ? -40.347 -68.494  7.470   1.00 65.05  ? 10  ILE B CG1 1 
ATOM   2572  C CG2 . ILE B  2 10  ? -38.093 -67.590  8.100   1.00 60.51  ? 10  ILE B CG2 1 
ATOM   2573  C CD1 . ILE B  2 10  ? -39.744 -69.696  6.776   1.00 65.19  ? 10  ILE B CD1 1 
ATOM   2574  N N   . GLU B  2 11  ? -39.176 -63.915  8.805   1.00 85.51  ? 11  GLU B N   1 
ATOM   2575  C CA  . GLU B  2 11  ? -38.627 -62.580  8.554   1.00 93.88  ? 11  GLU B CA  1 
ATOM   2576  C C   . GLU B  2 11  ? -37.104 -62.532  8.448   1.00 80.12  ? 11  GLU B C   1 
ATOM   2577  O O   . GLU B  2 11  ? -36.548 -61.524  8.002   1.00 77.64  ? 11  GLU B O   1 
ATOM   2578  C CB  . GLU B  2 11  ? -39.056 -61.610  9.660   1.00 110.07 ? 11  GLU B CB  1 
ATOM   2579  C CG  . GLU B  2 11  ? -40.531 -61.646  10.017  1.00 124.70 ? 11  GLU B CG  1 
ATOM   2580  C CD  . GLU B  2 11  ? -40.761 -61.740  11.515  1.00 152.94 ? 11  GLU B CD  1 
ATOM   2581  O OE1 . GLU B  2 11  ? -41.927 -61.910  11.926  1.00 158.68 ? 11  GLU B OE1 1 
ATOM   2582  O OE2 . GLU B  2 11  ? -39.778 -61.651  12.283  1.00 153.47 ? 11  GLU B OE2 1 
ATOM   2583  N N   . GLY B  2 12  ? -36.430 -63.601  8.865   1.00 76.96  ? 12  GLY B N   1 
ATOM   2584  C CA  . GLY B  2 12  ? -34.982 -63.562  8.996   1.00 76.66  ? 12  GLY B CA  1 
ATOM   2585  C C   . GLY B  2 12  ? -34.192 -64.745  8.462   1.00 74.18  ? 12  GLY B C   1 
ATOM   2586  O O   . GLY B  2 12  ? -34.661 -65.883  8.466   1.00 76.70  ? 12  GLY B O   1 
ATOM   2587  N N   . GLY B  2 13  ? -32.974 -64.467  8.003   1.00 72.40  ? 13  GLY B N   1 
ATOM   2588  C CA  . GLY B  2 13  ? -32.070 -65.505  7.541   1.00 73.88  ? 13  GLY B CA  1 
ATOM   2589  C C   . GLY B  2 13  ? -31.029 -65.857  8.586   1.00 79.14  ? 13  GLY B C   1 
ATOM   2590  O O   . GLY B  2 13  ? -30.867 -65.138  9.573   1.00 81.49  ? 13  GLY B O   1 
ATOM   2591  N N   . TRP B  2 14  ? -30.319 -66.959  8.366   1.00 80.29  ? 14  TRP B N   1 
ATOM   2592  C CA  . TRP B  2 14  ? -29.357 -67.455  9.346   1.00 76.32  ? 14  TRP B CA  1 
ATOM   2593  C C   . TRP B  2 14  ? -27.905 -67.350  8.886   1.00 83.80  ? 14  TRP B C   1 
ATOM   2594  O O   . TRP B  2 14  ? -27.406 -68.214  8.162   1.00 79.50  ? 14  TRP B O   1 
ATOM   2595  C CB  . TRP B  2 14  ? -29.681 -68.903  9.727   1.00 77.93  ? 14  TRP B CB  1 
ATOM   2596  C CG  . TRP B  2 14  ? -31.071 -69.070  10.243  1.00 72.85  ? 14  TRP B CG  1 
ATOM   2597  C CD1 . TRP B  2 14  ? -31.827 -68.124  10.866  1.00 74.70  ? 14  TRP B CD1 1 
ATOM   2598  C CD2 . TRP B  2 14  ? -31.874 -70.255  10.189  1.00 65.91  ? 14  TRP B CD2 1 
ATOM   2599  N NE1 . TRP B  2 14  ? -33.055 -68.643  11.198  1.00 72.24  ? 14  TRP B NE1 1 
ATOM   2600  C CE2 . TRP B  2 14  ? -33.108 -69.951  10.794  1.00 72.09  ? 14  TRP B CE2 1 
ATOM   2601  C CE3 . TRP B  2 14  ? -31.671 -71.542  9.685   1.00 69.37  ? 14  TRP B CE3 1 
ATOM   2602  C CZ2 . TRP B  2 14  ? -34.133 -70.887  10.910  1.00 79.32  ? 14  TRP B CZ2 1 
ATOM   2603  C CZ3 . TRP B  2 14  ? -32.690 -72.468  9.804   1.00 79.61  ? 14  TRP B CZ3 1 
ATOM   2604  C CH2 . TRP B  2 14  ? -33.902 -72.138  10.412  1.00 88.77  ? 14  TRP B CH2 1 
ATOM   2605  N N   . THR B  2 15  ? -27.226 -66.295  9.325   1.00 90.49  ? 15  THR B N   1 
ATOM   2606  C CA  . THR B  2 15  ? -25.791 -66.176  9.117   1.00 89.34  ? 15  THR B CA  1 
ATOM   2607  C C   . THR B  2 15  ? -25.134 -67.452  9.627   1.00 99.35  ? 15  THR B C   1 
ATOM   2608  O O   . THR B  2 15  ? -24.092 -67.880  9.125   1.00 100.44 ? 15  THR B O   1 
ATOM   2609  C CB  . THR B  2 15  ? -25.210 -64.965  9.876   1.00 86.77  ? 15  THR B CB  1 
ATOM   2610  O OG1 . THR B  2 15  ? -25.378 -65.153  11.287  1.00 117.72 ? 15  THR B OG1 1 
ATOM   2611  C CG2 . THR B  2 15  ? -25.916 -63.683  9.457   1.00 93.61  ? 15  THR B CG2 1 
ATOM   2612  N N   . GLY B  2 16  ? -25.777 -68.061  10.620  1.00 93.55  ? 16  GLY B N   1 
ATOM   2613  C CA  . GLY B  2 16  ? -25.299 -69.282  11.239  1.00 102.66 ? 16  GLY B CA  1 
ATOM   2614  C C   . GLY B  2 16  ? -25.238 -70.480  10.310  1.00 94.15  ? 16  GLY B C   1 
ATOM   2615  O O   . GLY B  2 16  ? -24.287 -71.256  10.364  1.00 106.05 ? 16  GLY B O   1 
ATOM   2616  N N   . MET B  2 17  ? -26.250 -70.641  9.462   1.00 93.34  ? 17  MET B N   1 
ATOM   2617  C CA  . MET B  2 17  ? -26.276 -71.760  8.524   1.00 93.87  ? 17  MET B CA  1 
ATOM   2618  C C   . MET B  2 17  ? -25.452 -71.447  7.280   1.00 98.02  ? 17  MET B C   1 
ATOM   2619  O O   . MET B  2 17  ? -25.839 -70.611  6.465   1.00 104.03 ? 17  MET B O   1 
ATOM   2620  C CB  . MET B  2 17  ? -27.713 -72.108  8.132   1.00 86.00  ? 17  MET B CB  1 
ATOM   2621  C CG  . MET B  2 17  ? -27.827 -73.294  7.189   1.00 101.00 ? 17  MET B CG  1 
ATOM   2622  S SD  . MET B  2 17  ? -29.538 -73.715  6.813   1.00 105.97 ? 17  MET B SD  1 
ATOM   2623  C CE  . MET B  2 17  ? -30.139 -72.161  6.157   1.00 91.03  ? 17  MET B CE  1 
ATOM   2624  N N   . VAL B  2 18  ? -24.318 -72.125  7.138   1.00 104.96 ? 18  VAL B N   1 
ATOM   2625  C CA  . VAL B  2 18  ? -23.389 -71.848  6.047   1.00 113.73 ? 18  VAL B CA  1 
ATOM   2626  C C   . VAL B  2 18  ? -23.159 -73.071  5.165   1.00 113.27 ? 18  VAL B C   1 
ATOM   2627  O O   . VAL B  2 18  ? -22.212 -73.110  4.379   1.00 113.36 ? 18  VAL B O   1 
ATOM   2628  C CB  . VAL B  2 18  ? -22.029 -71.370  6.587   1.00 116.86 ? 18  VAL B CB  1 
ATOM   2629  C CG1 . VAL B  2 18  ? -22.201 -70.103  7.411   1.00 106.04 ? 18  VAL B CG1 1 
ATOM   2630  C CG2 . VAL B  2 18  ? -21.377 -72.465  7.418   1.00 112.53 ? 18  VAL B CG2 1 
ATOM   2631  N N   . ASP B  2 19  ? -24.030 -74.065  5.296   1.00 120.86 ? 19  ASP B N   1 
ATOM   2632  C CA  . ASP B  2 19  ? -23.886 -75.310  4.551   1.00 123.50 ? 19  ASP B CA  1 
ATOM   2633  C C   . ASP B  2 19  ? -24.653 -75.264  3.232   1.00 115.61 ? 19  ASP B C   1 
ATOM   2634  O O   . ASP B  2 19  ? -24.245 -75.877  2.246   1.00 113.47 ? 19  ASP B O   1 
ATOM   2635  C CB  . ASP B  2 19  ? -24.366 -76.491  5.395   1.00 137.31 ? 19  ASP B CB  1 
ATOM   2636  C CG  . ASP B  2 19  ? -23.780 -76.484  6.794   1.00 145.22 ? 19  ASP B CG  1 
ATOM   2637  O OD1 . ASP B  2 19  ? -22.674 -75.934  6.976   1.00 149.95 ? 19  ASP B OD1 1 
ATOM   2638  O OD2 . ASP B  2 19  ? -24.428 -77.031  7.711   1.00 140.07 ? 19  ASP B OD2 1 
ATOM   2639  N N   . GLY B  2 20  ? -25.766 -74.536  3.222   1.00 102.17 ? 20  GLY B N   1 
ATOM   2640  C CA  . GLY B  2 20  ? -26.596 -74.428  2.036   1.00 89.07  ? 20  GLY B CA  1 
ATOM   2641  C C   . GLY B  2 20  ? -27.487 -73.199  2.045   1.00 87.33  ? 20  GLY B C   1 
ATOM   2642  O O   . GLY B  2 20  ? -27.333 -72.321  2.893   1.00 86.64  ? 20  GLY B O   1 
ATOM   2643  N N   . TRP B  2 21  ? -28.422 -73.136  1.101   1.00 76.89  ? 21  TRP B N   1 
ATOM   2644  C CA  . TRP B  2 21  ? -29.322 -71.989  0.988   1.00 76.09  ? 21  TRP B CA  1 
ATOM   2645  C C   . TRP B  2 21  ? -30.540 -72.124  1.895   1.00 65.90  ? 21  TRP B C   1 
ATOM   2646  O O   . TRP B  2 21  ? -30.996 -71.150  2.498   1.00 64.15  ? 21  TRP B O   1 
ATOM   2647  C CB  . TRP B  2 21  ? -29.766 -71.788  -0.465  1.00 80.73  ? 21  TRP B CB  1 
ATOM   2648  C CG  . TRP B  2 21  ? -28.763 -71.041  -1.294  1.00 75.59  ? 21  TRP B CG  1 
ATOM   2649  C CD1 . TRP B  2 21  ? -27.834 -70.149  -0.843  1.00 71.45  ? 21  TRP B CD1 1 
ATOM   2650  C CD2 . TRP B  2 21  ? -28.597 -71.106  -2.717  1.00 72.00  ? 21  TRP B CD2 1 
ATOM   2651  N NE1 . TRP B  2 21  ? -27.095 -69.662  -1.893  1.00 71.47  ? 21  TRP B NE1 1 
ATOM   2652  C CE2 . TRP B  2 21  ? -27.544 -70.233  -3.055  1.00 68.55  ? 21  TRP B CE2 1 
ATOM   2653  C CE3 . TRP B  2 21  ? -29.234 -71.820  -3.737  1.00 65.16  ? 21  TRP B CE3 1 
ATOM   2654  C CZ2 . TRP B  2 21  ? -27.114 -70.054  -4.368  1.00 64.74  ? 21  TRP B CZ2 1 
ATOM   2655  C CZ3 . TRP B  2 21  ? -28.804 -71.641  -5.041  1.00 59.81  ? 21  TRP B CZ3 1 
ATOM   2656  C CH2 . TRP B  2 21  ? -27.755 -70.765  -5.344  1.00 62.63  ? 21  TRP B CH2 1 
ATOM   2657  N N   . TYR B  2 22  ? -31.068 -73.339  1.973   1.00 72.49  ? 22  TYR B N   1 
ATOM   2658  C CA  . TYR B  2 22  ? -32.187 -73.631  2.856   1.00 78.63  ? 22  TYR B CA  1 
ATOM   2659  C C   . TYR B  2 22  ? -31.813 -74.788  3.772   1.00 88.34  ? 22  TYR B C   1 
ATOM   2660  O O   . TYR B  2 22  ? -31.087 -75.699  3.364   1.00 94.27  ? 22  TYR B O   1 
ATOM   2661  C CB  . TYR B  2 22  ? -33.445 -73.965  2.049   1.00 80.72  ? 22  TYR B CB  1 
ATOM   2662  C CG  . TYR B  2 22  ? -33.402 -73.470  0.622   1.00 80.90  ? 22  TYR B CG  1 
ATOM   2663  C CD1 . TYR B  2 22  ? -32.990 -74.306  -0.405  1.00 76.00  ? 22  TYR B CD1 1 
ATOM   2664  C CD2 . TYR B  2 22  ? -33.767 -72.168  0.302   1.00 76.20  ? 22  TYR B CD2 1 
ATOM   2665  C CE1 . TYR B  2 22  ? -32.944 -73.864  -1.713  1.00 70.14  ? 22  TYR B CE1 1 
ATOM   2666  C CE2 . TYR B  2 22  ? -33.724 -71.715  -1.006  1.00 71.39  ? 22  TYR B CE2 1 
ATOM   2667  C CZ  . TYR B  2 22  ? -33.312 -72.569  -2.010  1.00 72.03  ? 22  TYR B CZ  1 
ATOM   2668  O OH  . TYR B  2 22  ? -33.266 -72.128  -3.315  1.00 57.75  ? 22  TYR B OH  1 
ATOM   2669  N N   . GLY B  2 23  ? -32.306 -74.737  5.008   1.00 116.26 ? 23  GLY B N   1 
ATOM   2670  C CA  . GLY B  2 23  ? -31.967 -75.720  6.024   1.00 121.49 ? 23  GLY B CA  1 
ATOM   2671  C C   . GLY B  2 23  ? -32.510 -75.403  7.412   1.00 121.40 ? 23  GLY B C   1 
ATOM   2672  O O   . GLY B  2 23  ? -32.876 -74.265  7.714   1.00 109.53 ? 23  GLY B O   1 
ATOM   2673  N N   . TYR B  2 24  ? -32.527 -76.418  8.271   1.00 107.66 ? 24  TYR B N   1 
ATOM   2674  C CA  . TYR B  2 24  ? -33.246 -76.357  9.543   1.00 95.84  ? 24  TYR B CA  1 
ATOM   2675  C C   . TYR B  2 24  ? -32.412 -75.888  10.740  1.00 98.25  ? 24  TYR B C   1 
ATOM   2676  O O   . TYR B  2 24  ? -31.196 -75.736  10.647  1.00 88.99  ? 24  TYR B O   1 
ATOM   2677  C CB  . TYR B  2 24  ? -33.840 -77.733  9.859   1.00 91.82  ? 24  TYR B CB  1 
ATOM   2678  C CG  . TYR B  2 24  ? -34.370 -78.478  8.651   1.00 84.00  ? 24  TYR B CG  1 
ATOM   2679  C CD1 . TYR B  2 24  ? -33.506 -79.084  7.744   1.00 83.01  ? 24  TYR B CD1 1 
ATOM   2680  C CD2 . TYR B  2 24  ? -35.735 -78.587  8.424   1.00 85.03  ? 24  TYR B CD2 1 
ATOM   2681  C CE1 . TYR B  2 24  ? -33.988 -79.766  6.638   1.00 89.18  ? 24  TYR B CE1 1 
ATOM   2682  C CE2 . TYR B  2 24  ? -36.226 -79.263  7.319   1.00 87.90  ? 24  TYR B CE2 1 
ATOM   2683  C CZ  . TYR B  2 24  ? -35.348 -79.851  6.431   1.00 92.19  ? 24  TYR B CZ  1 
ATOM   2684  O OH  . TYR B  2 24  ? -35.828 -80.529  5.334   1.00 84.35  ? 24  TYR B OH  1 
ATOM   2685  N N   . HIS B  2 25  ? -33.091 -75.650  11.861  1.00 102.23 ? 25  HIS B N   1 
ATOM   2686  C CA  . HIS B  2 25  ? -32.434 -75.408  13.144  1.00 98.70  ? 25  HIS B CA  1 
ATOM   2687  C C   . HIS B  2 25  ? -33.176 -76.114  14.278  1.00 113.91 ? 25  HIS B C   1 
ATOM   2688  O O   . HIS B  2 25  ? -34.186 -75.623  14.787  1.00 106.26 ? 25  HIS B O   1 
ATOM   2689  C CB  . HIS B  2 25  ? -32.318 -73.919  13.448  1.00 103.05 ? 25  HIS B CB  1 
ATOM   2690  C CG  . HIS B  2 25  ? -31.911 -73.635  14.858  1.00 115.76 ? 25  HIS B CG  1 
ATOM   2691  N ND1 . HIS B  2 25  ? -32.821 -73.311  15.842  1.00 111.12 ? 25  HIS B ND1 1 
ATOM   2692  C CD2 . HIS B  2 25  ? -30.698 -73.655  15.458  1.00 108.68 ? 25  HIS B CD2 1 
ATOM   2693  C CE1 . HIS B  2 25  ? -32.183 -73.128  16.983  1.00 113.94 ? 25  HIS B CE1 1 
ATOM   2694  N NE2 . HIS B  2 25  ? -30.895 -73.330  16.780  1.00 117.38 ? 25  HIS B NE2 1 
ATOM   2695  N N   . HIS B  2 26  ? -32.656 -77.273  14.661  1.00 128.68 ? 26  HIS B N   1 
ATOM   2696  C CA  . HIS B  2 26  ? -33.285 -78.126  15.654  1.00 123.51 ? 26  HIS B CA  1 
ATOM   2697  C C   . HIS B  2 26  ? -33.000 -77.575  17.048  1.00 131.04 ? 26  HIS B C   1 
ATOM   2698  O O   . HIS B  2 26  ? -32.064 -76.803  17.230  1.00 130.89 ? 26  HIS B O   1 
ATOM   2699  C CB  . HIS B  2 26  ? -32.767 -79.556  15.499  1.00 123.33 ? 26  HIS B CB  1 
ATOM   2700  C CG  . HIS B  2 26  ? -31.406 -79.771  16.077  1.00 129.02 ? 26  HIS B CG  1 
ATOM   2701  N ND1 . HIS B  2 26  ? -30.247 -79.455  15.400  1.00 128.60 ? 26  HIS B ND1 1 
ATOM   2702  C CD2 . HIS B  2 26  ? -31.017 -80.281  17.270  1.00 143.62 ? 26  HIS B CD2 1 
ATOM   2703  C CE1 . HIS B  2 26  ? -29.205 -79.755  16.153  1.00 140.07 ? 26  HIS B CE1 1 
ATOM   2704  N NE2 . HIS B  2 26  ? -29.643 -80.257  17.292  1.00 148.03 ? 26  HIS B NE2 1 
ATOM   2705  N N   . GLN B  2 27  ? -33.806 -77.967  18.027  1.00 160.01 ? 27  GLN B N   1 
ATOM   2706  C CA  . GLN B  2 27  ? -33.659 -77.455  19.386  1.00 163.13 ? 27  GLN B CA  1 
ATOM   2707  C C   . GLN B  2 27  ? -34.110 -78.504  20.396  1.00 162.44 ? 27  GLN B C   1 
ATOM   2708  O O   . GLN B  2 27  ? -35.012 -78.256  21.196  1.00 159.40 ? 27  GLN B O   1 
ATOM   2709  C CB  . GLN B  2 27  ? -34.474 -76.167  19.559  1.00 165.18 ? 27  GLN B CB  1 
ATOM   2710  C CG  . GLN B  2 27  ? -34.483 -75.559  20.964  1.00 167.40 ? 27  GLN B CG  1 
ATOM   2711  C CD  . GLN B  2 27  ? -33.102 -75.170  21.447  1.00 173.17 ? 27  GLN B CD  1 
ATOM   2712  O OE1 . GLN B  2 27  ? -32.729 -73.998  21.421  1.00 170.60 ? 27  GLN B OE1 1 
ATOM   2713  N NE2 . GLN B  2 27  ? -32.335 -76.156  21.894  1.00 178.41 ? 27  GLN B NE2 1 
ATOM   2714  N N   . ASN B  2 28  ? -33.497 -79.685  20.346  1.00 161.70 ? 28  ASN B N   1 
ATOM   2715  C CA  . ASN B  2 28  ? -33.925 -80.782  21.205  1.00 162.61 ? 28  ASN B CA  1 
ATOM   2716  C C   . ASN B  2 28  ? -33.028 -80.944  22.414  1.00 166.15 ? 28  ASN B C   1 
ATOM   2717  O O   . ASN B  2 28  ? -32.234 -80.061  22.720  1.00 165.64 ? 28  ASN B O   1 
ATOM   2718  C CB  . ASN B  2 28  ? -34.099 -82.099  20.428  1.00 146.58 ? 28  ASN B CB  1 
ATOM   2719  C CG  . ASN B  2 28  ? -32.779 -82.766  20.062  1.00 145.16 ? 28  ASN B CG  1 
ATOM   2720  O OD1 . ASN B  2 28  ? -32.771 -83.902  19.584  1.00 138.97 ? 28  ASN B OD1 1 
ATOM   2721  N ND2 . ASN B  2 28  ? -31.665 -82.069  20.277  1.00 148.84 ? 28  ASN B ND2 1 
ATOM   2722  N N   . GLU B  2 29  ? -33.169 -82.065  23.106  1.00 152.44 ? 29  GLU B N   1 
ATOM   2723  C CA  . GLU B  2 29  ? -32.495 -82.255  24.379  1.00 154.26 ? 29  GLU B CA  1 
ATOM   2724  C C   . GLU B  2 29  ? -31.035 -82.685  24.206  1.00 153.75 ? 29  GLU B C   1 
ATOM   2725  O O   . GLU B  2 29  ? -30.284 -82.765  25.179  1.00 144.48 ? 29  GLU B O   1 
ATOM   2726  C CB  . GLU B  2 29  ? -33.252 -83.281  25.217  1.00 166.80 ? 29  GLU B CB  1 
ATOM   2727  C CG  . GLU B  2 29  ? -34.764 -83.089  25.296  1.00 166.61 ? 29  GLU B CG  1 
ATOM   2728  C CD  . GLU B  2 29  ? -35.491 -84.388  25.616  1.00 179.07 ? 29  GLU B CD  1 
ATOM   2729  O OE1 . GLU B  2 29  ? -35.014 -85.452  25.171  1.00 176.34 ? 29  GLU B OE1 1 
ATOM   2730  O OE2 . GLU B  2 29  ? -36.532 -84.353  26.308  1.00 176.86 ? 29  GLU B OE2 1 
ATOM   2731  N N   . GLN B  2 30  ? -30.636 -82.960  22.968  1.00 167.48 ? 30  GLN B N   1 
ATOM   2732  C CA  . GLN B  2 30  ? -29.257 -83.343  22.683  1.00 156.73 ? 30  GLN B CA  1 
ATOM   2733  C C   . GLN B  2 30  ? -28.444 -82.183  22.119  1.00 163.53 ? 30  GLN B C   1 
ATOM   2734  O O   . GLN B  2 30  ? -27.302 -82.366  21.700  1.00 165.65 ? 30  GLN B O   1 
ATOM   2735  C CB  . GLN B  2 30  ? -29.205 -84.524  21.715  1.00 147.23 ? 30  GLN B CB  1 
ATOM   2736  C CG  . GLN B  2 30  ? -29.701 -85.824  22.302  1.00 138.02 ? 30  GLN B CG  1 
ATOM   2737  C CD  . GLN B  2 30  ? -30.819 -86.424  21.485  1.00 144.44 ? 30  GLN B CD  1 
ATOM   2738  O OE1 . GLN B  2 30  ? -30.580 -87.171  20.536  1.00 141.14 ? 30  GLN B OE1 1 
ATOM   2739  N NE2 . GLN B  2 30  ? -32.052 -86.092  21.842  1.00 149.27 ? 30  GLN B NE2 1 
ATOM   2740  N N   . GLY B  2 31  ? -29.031 -80.991  22.103  1.00 175.01 ? 31  GLY B N   1 
ATOM   2741  C CA  . GLY B  2 31  ? -28.322 -79.814  21.635  1.00 171.16 ? 31  GLY B CA  1 
ATOM   2742  C C   . GLY B  2 31  ? -29.068 -79.029  20.575  1.00 164.81 ? 31  GLY B C   1 
ATOM   2743  O O   . GLY B  2 31  ? -30.222 -79.325  20.267  1.00 160.52 ? 31  GLY B O   1 
ATOM   2744  N N   . SER B  2 32  ? -28.403 -78.023  20.016  1.00 160.02 ? 32  SER B N   1 
ATOM   2745  C CA  . SER B  2 32  ? -28.998 -77.177  18.989  1.00 150.74 ? 32  SER B CA  1 
ATOM   2746  C C   . SER B  2 32  ? -28.108 -77.144  17.752  1.00 146.28 ? 32  SER B C   1 
ATOM   2747  O O   . SER B  2 32  ? -27.245 -78.004  17.578  1.00 148.67 ? 32  SER B O   1 
ATOM   2748  C CB  . SER B  2 32  ? -29.198 -75.758  19.521  1.00 143.55 ? 32  SER B CB  1 
ATOM   2749  O OG  . SER B  2 32  ? -29.927 -75.768  20.735  1.00 151.63 ? 32  SER B OG  1 
ATOM   2750  N N   . GLY B  2 33  ? -28.321 -76.149  16.896  1.00 148.01 ? 33  GLY B N   1 
ATOM   2751  C CA  . GLY B  2 33  ? -27.496 -75.975  15.715  1.00 142.65 ? 33  GLY B CA  1 
ATOM   2752  C C   . GLY B  2 33  ? -28.284 -75.875  14.423  1.00 122.92 ? 33  GLY B C   1 
ATOM   2753  O O   . GLY B  2 33  ? -29.487 -76.132  14.393  1.00 110.86 ? 33  GLY B O   1 
ATOM   2754  N N   . TYR B  2 34  ? -27.595 -75.498  13.350  1.00 108.21 ? 34  TYR B N   1 
ATOM   2755  C CA  . TYR B  2 34  ? -28.215 -75.386  12.035  1.00 93.29  ? 34  TYR B CA  1 
ATOM   2756  C C   . TYR B  2 34  ? -27.770 -76.529  11.128  1.00 92.45  ? 34  TYR B C   1 
ATOM   2757  O O   . TYR B  2 34  ? -26.635 -76.996  11.215  1.00 89.38  ? 34  TYR B O   1 
ATOM   2758  C CB  . TYR B  2 34  ? -27.852 -74.050  11.382  1.00 94.78  ? 34  TYR B CB  1 
ATOM   2759  C CG  . TYR B  2 34  ? -28.135 -72.835  12.237  1.00 94.99  ? 34  TYR B CG  1 
ATOM   2760  C CD1 . TYR B  2 34  ? -27.181 -72.346  13.120  1.00 83.67  ? 34  TYR B CD1 1 
ATOM   2761  C CD2 . TYR B  2 34  ? -29.351 -72.170  12.154  1.00 91.39  ? 34  TYR B CD2 1 
ATOM   2762  C CE1 . TYR B  2 34  ? -27.432 -71.234  13.901  1.00 91.98  ? 34  TYR B CE1 1 
ATOM   2763  C CE2 . TYR B  2 34  ? -29.611 -71.056  12.931  1.00 83.39  ? 34  TYR B CE2 1 
ATOM   2764  C CZ  . TYR B  2 34  ? -28.648 -70.593  13.802  1.00 86.33  ? 34  TYR B CZ  1 
ATOM   2765  O OH  . TYR B  2 34  ? -28.902 -69.485  14.578  1.00 76.51  ? 34  TYR B OH  1 
ATOM   2766  N N   . ALA B  2 35  ? -28.669 -76.973  10.256  1.00 103.64 ? 35  ALA B N   1 
ATOM   2767  C CA  . ALA B  2 35  ? -28.352 -78.020  9.291   1.00 99.74  ? 35  ALA B CA  1 
ATOM   2768  C C   . ALA B  2 35  ? -29.042 -77.748  7.958   1.00 105.13 ? 35  ALA B C   1 
ATOM   2769  O O   . ALA B  2 35  ? -30.268 -77.790  7.866   1.00 110.64 ? 35  ALA B O   1 
ATOM   2770  C CB  . ALA B  2 35  ? -28.753 -79.383  9.832   1.00 108.14 ? 35  ALA B CB  1 
ATOM   2771  N N   . ALA B  2 36  ? -28.250 -77.470  6.928   1.00 91.43  ? 36  ALA B N   1 
ATOM   2772  C CA  . ALA B  2 36  ? -28.792 -77.153  5.612   1.00 100.75 ? 36  ALA B CA  1 
ATOM   2773  C C   . ALA B  2 36  ? -29.381 -78.382  4.928   1.00 94.85  ? 36  ALA B C   1 
ATOM   2774  O O   . ALA B  2 36  ? -28.813 -79.472  4.991   1.00 101.70 ? 36  ALA B O   1 
ATOM   2775  C CB  . ALA B  2 36  ? -27.725 -76.520  4.737   1.00 105.26 ? 36  ALA B CB  1 
ATOM   2776  N N   . ASP B  2 37  ? -30.525 -78.197  4.276   1.00 93.62  ? 37  ASP B N   1 
ATOM   2777  C CA  . ASP B  2 37  ? -31.179 -79.282  3.558   1.00 95.60  ? 37  ASP B CA  1 
ATOM   2778  C C   . ASP B  2 37  ? -30.342 -79.703  2.359   1.00 101.21 ? 37  ASP B C   1 
ATOM   2779  O O   . ASP B  2 37  ? -30.055 -78.899  1.473   1.00 91.13  ? 37  ASP B O   1 
ATOM   2780  C CB  . ASP B  2 37  ? -32.579 -78.869  3.103   1.00 79.55  ? 37  ASP B CB  1 
ATOM   2781  C CG  . ASP B  2 37  ? -33.340 -80.010  2.456   1.00 95.80  ? 37  ASP B CG  1 
ATOM   2782  O OD1 . ASP B  2 37  ? -34.454 -79.769  1.949   1.00 110.77 ? 37  ASP B OD1 1 
ATOM   2783  O OD2 . ASP B  2 37  ? -32.827 -81.149  2.455   1.00 109.51 ? 37  ASP B OD2 1 
ATOM   2784  N N   . LEU B  2 38  ? -29.960 -80.973  2.338   1.00 109.46 ? 38  LEU B N   1 
ATOM   2785  C CA  . LEU B  2 38  ? -29.058 -81.485  1.318   1.00 123.44 ? 38  LEU B CA  1 
ATOM   2786  C C   . LEU B  2 38  ? -29.664 -81.444  -0.086  1.00 114.14 ? 38  LEU B C   1 
ATOM   2787  O O   . LEU B  2 38  ? -29.135 -80.782  -0.979  1.00 104.58 ? 38  LEU B O   1 
ATOM   2788  C CB  . LEU B  2 38  ? -28.631 -82.911  1.668   1.00 147.34 ? 38  LEU B CB  1 
ATOM   2789  C CG  . LEU B  2 38  ? -27.159 -83.259  1.444   1.00 158.48 ? 38  LEU B CG  1 
ATOM   2790  C CD1 . LEU B  2 38  ? -26.884 -84.697  1.858   1.00 157.43 ? 38  LEU B CD1 1 
ATOM   2791  C CD2 . LEU B  2 38  ? -26.752 -83.011  -0.001  1.00 157.53 ? 38  LEU B CD2 1 
ATOM   2792  N N   . LYS B  2 39  ? -30.774 -82.150  -0.276  1.00 136.16 ? 39  LYS B N   1 
ATOM   2793  C CA  . LYS B  2 39  ? -31.384 -82.281  -1.598  1.00 138.78 ? 39  LYS B CA  1 
ATOM   2794  C C   . LYS B  2 39  ? -31.876 -80.953  -2.174  1.00 136.02 ? 39  LYS B C   1 
ATOM   2795  O O   . LYS B  2 39  ? -31.735 -80.700  -3.371  1.00 128.73 ? 39  LYS B O   1 
ATOM   2796  C CB  . LYS B  2 39  ? -32.531 -83.295  -1.561  1.00 149.50 ? 39  LYS B CB  1 
ATOM   2797  C CG  . LYS B  2 39  ? -33.126 -83.604  -2.926  1.00 167.07 ? 39  LYS B CG  1 
ATOM   2798  C CD  . LYS B  2 39  ? -34.141 -84.732  -2.845  1.00 180.20 ? 39  LYS B CD  1 
ATOM   2799  C CE  . LYS B  2 39  ? -34.660 -85.107  -4.223  1.00 182.41 ? 39  LYS B CE  1 
ATOM   2800  N NZ  . LYS B  2 39  ? -35.590 -86.269  -4.167  1.00 175.63 ? 39  LYS B NZ  1 
ATOM   2801  N N   . SER B  2 40  ? -32.452 -80.111  -1.324  1.00 107.93 ? 40  SER B N   1 
ATOM   2802  C CA  . SER B  2 40  ? -33.021 -78.845  -1.775  1.00 94.79  ? 40  SER B CA  1 
ATOM   2803  C C   . SER B  2 40  ? -31.947 -77.872  -2.256  1.00 84.02  ? 40  SER B C   1 
ATOM   2804  O O   . SER B  2 40  ? -32.023 -77.354  -3.370  1.00 84.48  ? 40  SER B O   1 
ATOM   2805  C CB  . SER B  2 40  ? -33.856 -78.205  -0.663  1.00 91.88  ? 40  SER B CB  1 
ATOM   2806  O OG  . SER B  2 40  ? -34.580 -77.088  -1.148  1.00 99.81  ? 40  SER B OG  1 
ATOM   2807  N N   . THR B  2 41  ? -30.950 -77.627  -1.412  1.00 87.18  ? 41  THR B N   1 
ATOM   2808  C CA  . THR B  2 41  ? -29.871 -76.705  -1.751  1.00 85.31  ? 41  THR B CA  1 
ATOM   2809  C C   . THR B  2 41  ? -29.124 -77.150  -3.004  1.00 88.67  ? 41  THR B C   1 
ATOM   2810  O O   . THR B  2 41  ? -28.730 -76.324  -3.829  1.00 78.01  ? 41  THR B O   1 
ATOM   2811  C CB  . THR B  2 41  ? -28.866 -76.557  -0.592  1.00 71.88  ? 41  THR B CB  1 
ATOM   2812  O OG1 . THR B  2 41  ? -29.520 -75.964  0.537   1.00 86.47  ? 41  THR B OG1 1 
ATOM   2813  C CG2 . THR B  2 41  ? -27.697 -75.679  -1.011  1.00 75.62  ? 41  THR B CG2 1 
ATOM   2814  N N   . GLN B  2 42  ? -28.936 -78.457  -3.145  1.00 98.82  ? 42  GLN B N   1 
ATOM   2815  C CA  . GLN B  2 42  ? -28.212 -79.002  -4.288  1.00 101.81 ? 42  GLN B CA  1 
ATOM   2816  C C   . GLN B  2 42  ? -28.937 -78.722  -5.602  1.00 92.74  ? 42  GLN B C   1 
ATOM   2817  O O   . GLN B  2 42  ? -28.324 -78.282  -6.575  1.00 88.42  ? 42  GLN B O   1 
ATOM   2818  C CB  . GLN B  2 42  ? -27.980 -80.505  -4.118  1.00 104.94 ? 42  GLN B CB  1 
ATOM   2819  C CG  . GLN B  2 42  ? -27.093 -81.110  -5.193  1.00 111.94 ? 42  GLN B CG  1 
ATOM   2820  C CD  . GLN B  2 42  ? -25.734 -80.442  -5.267  1.00 119.70 ? 42  GLN B CD  1 
ATOM   2821  O OE1 . GLN B  2 42  ? -25.218 -79.944  -4.266  1.00 123.59 ? 42  GLN B OE1 1 
ATOM   2822  N NE2 . GLN B  2 42  ? -25.145 -80.430  -6.457  1.00 119.65 ? 42  GLN B NE2 1 
ATOM   2823  N N   . ASN B  2 43  ? -30.241 -78.978  -5.626  1.00 83.38  ? 43  ASN B N   1 
ATOM   2824  C CA  . ASN B  2 43  ? -31.045 -78.726  -6.818  1.00 86.78  ? 43  ASN B CA  1 
ATOM   2825  C C   . ASN B  2 43  ? -31.052 -77.254  -7.219  1.00 85.74  ? 43  ASN B C   1 
ATOM   2826  O O   . ASN B  2 43  ? -30.888 -76.923  -8.394  1.00 77.47  ? 43  ASN B O   1 
ATOM   2827  C CB  . ASN B  2 43  ? -32.480 -79.222  -6.623  1.00 86.49  ? 43  ASN B CB  1 
ATOM   2828  C CG  . ASN B  2 43  ? -32.694 -80.618  -7.172  1.00 99.66  ? 43  ASN B CG  1 
ATOM   2829  O OD1 . ASN B  2 43  ? -32.122 -81.589  -6.677  1.00 109.45 ? 43  ASN B OD1 1 
ATOM   2830  N ND2 . ASN B  2 43  ? -33.525 -80.725  -8.203  1.00 102.74 ? 43  ASN B ND2 1 
ATOM   2831  N N   . ALA B  2 44  ? -31.245 -76.377  -6.240  1.00 81.48  ? 44  ALA B N   1 
ATOM   2832  C CA  . ALA B  2 44  ? -31.254 -74.941  -6.491  1.00 67.64  ? 44  ALA B CA  1 
ATOM   2833  C C   . ALA B  2 44  ? -29.960 -74.500  -7.165  1.00 67.32  ? 44  ALA B C   1 
ATOM   2834  O O   . ALA B  2 44  ? -29.986 -73.804  -8.180  1.00 74.00  ? 44  ALA B O   1 
ATOM   2835  C CB  . ALA B  2 44  ? -31.469 -74.175  -5.195  1.00 62.12  ? 44  ALA B CB  1 
ATOM   2836  N N   . ILE B  2 45  ? -28.830 -74.912  -6.598  1.00 67.03  ? 45  ILE B N   1 
ATOM   2837  C CA  . ILE B  2 45  ? -27.525 -74.589  -7.166  1.00 74.33  ? 45  ILE B CA  1 
ATOM   2838  C C   . ILE B  2 45  ? -27.425 -75.040  -8.620  1.00 71.32  ? 45  ILE B C   1 
ATOM   2839  O O   . ILE B  2 45  ? -27.019 -74.271  -9.490  1.00 70.33  ? 45  ILE B O   1 
ATOM   2840  C CB  . ILE B  2 45  ? -26.378 -75.222  -6.354  1.00 76.92  ? 45  ILE B CB  1 
ATOM   2841  C CG1 . ILE B  2 45  ? -26.196 -74.485  -5.026  1.00 73.74  ? 45  ILE B CG1 1 
ATOM   2842  C CG2 . ILE B  2 45  ? -25.082 -75.196  -7.149  1.00 73.69  ? 45  ILE B CG2 1 
ATOM   2843  C CD1 . ILE B  2 45  ? -25.016 -74.972  -4.214  1.00 81.98  ? 45  ILE B CD1 1 
ATOM   2844  N N   . ASP B  2 46  ? -27.800 -76.290  -8.876  1.00 76.60  ? 46  ASP B N   1 
ATOM   2845  C CA  . ASP B  2 46  ? -27.774 -76.837  -10.228 1.00 75.13  ? 46  ASP B CA  1 
ATOM   2846  C C   . ASP B  2 46  ? -28.631 -76.017  -11.187 1.00 71.90  ? 46  ASP B C   1 
ATOM   2847  O O   . ASP B  2 46  ? -28.190 -75.665  -12.281 1.00 70.55  ? 46  ASP B O   1 
ATOM   2848  C CB  . ASP B  2 46  ? -28.243 -78.294  -10.228 1.00 80.50  ? 46  ASP B CB  1 
ATOM   2849  C CG  . ASP B  2 46  ? -27.215 -79.239  -9.637  1.00 100.90 ? 46  ASP B CG  1 
ATOM   2850  O OD1 . ASP B  2 46  ? -26.036 -78.843  -9.526  1.00 98.72  ? 46  ASP B OD1 1 
ATOM   2851  O OD2 . ASP B  2 46  ? -27.585 -80.381  -9.291  1.00 111.76 ? 46  ASP B OD2 1 
ATOM   2852  N N   . GLU B  2 47  ? -29.857 -75.714  -10.771 1.00 71.64  ? 47  GLU B N   1 
ATOM   2853  C CA  . GLU B  2 47  ? -30.799 -75.005  -11.631 1.00 58.70  ? 47  GLU B CA  1 
ATOM   2854  C C   . GLU B  2 47  ? -30.441 -73.531  -11.819 1.00 61.38  ? 47  GLU B C   1 
ATOM   2855  O O   . GLU B  2 47  ? -30.591 -72.986  -12.912 1.00 59.13  ? 47  GLU B O   1 
ATOM   2856  C CB  . GLU B  2 47  ? -32.230 -75.161  -11.110 1.00 53.58  ? 47  GLU B CB  1 
ATOM   2857  C CG  . GLU B  2 47  ? -32.740 -76.595  -11.162 1.00 68.24  ? 47  GLU B CG  1 
ATOM   2858  C CD  . GLU B  2 47  ? -34.221 -76.708  -10.858 1.00 82.86  ? 47  GLU B CD  1 
ATOM   2859  O OE1 . GLU B  2 47  ? -34.785 -75.765  -10.265 1.00 73.76  ? 47  GLU B OE1 1 
ATOM   2860  O OE2 . GLU B  2 47  ? -34.821 -77.744  -11.214 1.00 90.76  ? 47  GLU B OE2 1 
ATOM   2861  N N   . ILE B  2 48  ? -29.969 -72.889  -10.755 1.00 49.39  ? 48  ILE B N   1 
ATOM   2862  C CA  . ILE B  2 48  ? -29.510 -71.508  -10.853 1.00 50.11  ? 48  ILE B CA  1 
ATOM   2863  C C   . ILE B  2 48  ? -28.274 -71.432  -11.743 1.00 56.95  ? 48  ILE B C   1 
ATOM   2864  O O   . ILE B  2 48  ? -28.120 -70.499  -12.532 1.00 57.26  ? 48  ILE B O   1 
ATOM   2865  C CB  . ILE B  2 48  ? -29.200 -70.902  -9.471  1.00 59.81  ? 48  ILE B CB  1 
ATOM   2866  C CG1 . ILE B  2 48  ? -30.497 -70.670  -8.695  1.00 59.67  ? 48  ILE B CG1 1 
ATOM   2867  C CG2 . ILE B  2 48  ? -28.437 -69.593  -9.618  1.00 44.84  ? 48  ILE B CG2 1 
ATOM   2868  C CD1 . ILE B  2 48  ? -31.478 -69.763  -9.407  1.00 56.40  ? 48  ILE B CD1 1 
ATOM   2869  N N   . THR B  2 49  ? -27.398 -72.424  -11.613 1.00 59.80  ? 49  THR B N   1 
ATOM   2870  C CA  . THR B  2 49  ? -26.226 -72.528  -12.473 1.00 62.06  ? 49  THR B CA  1 
ATOM   2871  C C   . THR B  2 49  ? -26.654 -72.620  -13.932 1.00 66.24  ? 49  THR B C   1 
ATOM   2872  O O   . THR B  2 49  ? -26.173 -71.869  -14.781 1.00 63.21  ? 49  THR B O   1 
ATOM   2873  C CB  . THR B  2 49  ? -25.372 -73.760  -12.122 1.00 61.20  ? 49  THR B CB  1 
ATOM   2874  O OG1 . THR B  2 49  ? -24.765 -73.573  -10.838 1.00 74.54  ? 49  THR B OG1 1 
ATOM   2875  C CG2 . THR B  2 49  ? -24.282 -73.969  -13.163 1.00 47.64  ? 49  THR B CG2 1 
ATOM   2876  N N   . ASN B  2 50  ? -27.565 -73.546  -14.214 1.00 55.63  ? 50  ASN B N   1 
ATOM   2877  C CA  . ASN B  2 50  ? -28.093 -73.722  -15.561 1.00 60.69  ? 50  ASN B CA  1 
ATOM   2878  C C   . ASN B  2 50  ? -28.691 -72.423  -16.089 1.00 61.29  ? 50  ASN B C   1 
ATOM   2879  O O   . ASN B  2 50  ? -28.550 -72.094  -17.267 1.00 62.44  ? 50  ASN B O   1 
ATOM   2880  C CB  . ASN B  2 50  ? -29.146 -74.831  -15.578 1.00 59.76  ? 50  ASN B CB  1 
ATOM   2881  C CG  . ASN B  2 50  ? -29.522 -75.256  -16.983 1.00 63.40  ? 50  ASN B CG  1 
ATOM   2882  O OD1 . ASN B  2 50  ? -28.919 -76.167  -17.550 1.00 68.44  ? 50  ASN B OD1 1 
ATOM   2883  N ND2 . ASN B  2 50  ? -30.526 -74.599  -17.552 1.00 56.83  ? 50  ASN B ND2 1 
ATOM   2884  N N   . LYS B  2 51  ? -29.355 -71.689  -15.203 1.00 59.59  ? 51  LYS B N   1 
ATOM   2885  C CA  . LYS B  2 51  ? -29.954 -70.407  -15.550 1.00 54.55  ? 51  LYS B CA  1 
ATOM   2886  C C   . LYS B  2 51  ? -28.897 -69.428  -16.045 1.00 54.93  ? 51  LYS B C   1 
ATOM   2887  O O   . LYS B  2 51  ? -29.043 -68.826  -17.109 1.00 47.29  ? 51  LYS B O   1 
ATOM   2888  C CB  . LYS B  2 51  ? -30.687 -69.827  -14.339 1.00 57.16  ? 51  LYS B CB  1 
ATOM   2889  C CG  . LYS B  2 51  ? -31.350 -68.484  -14.584 1.00 49.01  ? 51  LYS B CG  1 
ATOM   2890  C CD  . LYS B  2 51  ? -32.315 -68.153  -13.458 1.00 56.28  ? 51  LYS B CD  1 
ATOM   2891  C CE  . LYS B  2 51  ? -33.107 -66.893  -13.756 1.00 59.31  ? 51  LYS B CE  1 
ATOM   2892  N NZ  . LYS B  2 51  ? -34.349 -66.813  -12.938 1.00 62.79  ? 51  LYS B NZ  1 
ATOM   2893  N N   . VAL B  2 52  ? -27.830 -69.278  -15.266 1.00 50.90  ? 52  VAL B N   1 
ATOM   2894  C CA  . VAL B  2 52  ? -26.742 -68.373  -15.618 1.00 47.29  ? 52  VAL B CA  1 
ATOM   2895  C C   . VAL B  2 52  ? -26.059 -68.806  -16.912 1.00 55.61  ? 52  VAL B C   1 
ATOM   2896  O O   . VAL B  2 52  ? -25.716 -67.974  -17.752 1.00 58.50  ? 52  VAL B O   1 
ATOM   2897  C CB  . VAL B  2 52  ? -25.694 -68.291  -14.494 1.00 40.93  ? 52  VAL B CB  1 
ATOM   2898  C CG1 . VAL B  2 52  ? -24.609 -67.287  -14.852 1.00 38.72  ? 52  VAL B CG1 1 
ATOM   2899  C CG2 . VAL B  2 52  ? -26.359 -67.916  -13.178 1.00 45.47  ? 52  VAL B CG2 1 
ATOM   2900  N N   . ASN B  2 53  ? -25.865 -70.112  -17.068 1.00 51.46  ? 53  ASN B N   1 
ATOM   2901  C CA  . ASN B  2 53  ? -25.246 -70.654  -18.274 1.00 62.09  ? 53  ASN B CA  1 
ATOM   2902  C C   . ASN B  2 53  ? -26.061 -70.372  -19.530 1.00 66.50  ? 53  ASN B C   1 
ATOM   2903  O O   . ASN B  2 53  ? -25.502 -70.109  -20.592 1.00 69.53  ? 53  ASN B O   1 
ATOM   2904  C CB  . ASN B  2 53  ? -25.002 -72.158  -18.134 1.00 66.83  ? 53  ASN B CB  1 
ATOM   2905  C CG  . ASN B  2 53  ? -23.737 -72.476  -17.362 1.00 73.13  ? 53  ASN B CG  1 
ATOM   2906  O OD1 . ASN B  2 53  ? -22.953 -71.585  -17.036 1.00 57.95  ? 53  ASN B OD1 1 
ATOM   2907  N ND2 . ASN B  2 53  ? -23.527 -73.755  -17.072 1.00 70.09  ? 53  ASN B ND2 1 
ATOM   2908  N N   . SER B  2 54  ? -27.383 -70.428  -19.406 1.00 58.17  ? 54  SER B N   1 
ATOM   2909  C CA  . SER B  2 54  ? -28.265 -70.191  -20.546 1.00 50.73  ? 54  SER B CA  1 
ATOM   2910  C C   . SER B  2 54  ? -28.133 -68.766  -21.071 1.00 56.10  ? 54  SER B C   1 
ATOM   2911  O O   . SER B  2 54  ? -27.906 -68.553  -22.262 1.00 62.82  ? 54  SER B O   1 
ATOM   2912  C CB  . SER B  2 54  ? -29.720 -70.482  -20.173 1.00 51.05  ? 54  SER B CB  1 
ATOM   2913  O OG  . SER B  2 54  ? -29.898 -71.848  -19.842 1.00 59.90  ? 54  SER B OG  1 
ATOM   2914  N N   . VAL B  2 55  ? -28.279 -67.794  -20.176 1.00 49.78  ? 55  VAL B N   1 
ATOM   2915  C CA  . VAL B  2 55  ? -28.161 -66.386  -20.538 1.00 47.26  ? 55  VAL B CA  1 
ATOM   2916  C C   . VAL B  2 55  ? -26.845 -66.112  -21.260 1.00 56.14  ? 55  VAL B C   1 
ATOM   2917  O O   . VAL B  2 55  ? -26.767 -65.238  -22.124 1.00 49.87  ? 55  VAL B O   1 
ATOM   2918  C CB  . VAL B  2 55  ? -28.263 -65.477  -19.296 1.00 43.12  ? 55  VAL B CB  1 
ATOM   2919  C CG1 . VAL B  2 55  ? -27.980 -64.029  -19.666 1.00 52.10  ? 55  VAL B CG1 1 
ATOM   2920  C CG2 . VAL B  2 55  ? -29.632 -65.611  -18.652 1.00 39.18  ? 55  VAL B CG2 1 
ATOM   2921  N N   . ILE B  2 56  ? -25.815 -66.873  -20.906 1.00 51.08  ? 56  ILE B N   1 
ATOM   2922  C CA  . ILE B  2 56  ? -24.489 -66.698  -21.488 1.00 50.37  ? 56  ILE B CA  1 
ATOM   2923  C C   . ILE B  2 56  ? -24.285 -67.535  -22.750 1.00 55.88  ? 56  ILE B C   1 
ATOM   2924  O O   . ILE B  2 56  ? -23.868 -67.018  -23.786 1.00 52.03  ? 56  ILE B O   1 
ATOM   2925  C CB  . ILE B  2 56  ? -23.385 -67.059  -20.472 1.00 57.00  ? 56  ILE B CB  1 
ATOM   2926  C CG1 . ILE B  2 56  ? -23.389 -66.071  -19.303 1.00 56.78  ? 56  ILE B CG1 1 
ATOM   2927  C CG2 . ILE B  2 56  ? -22.023 -67.083  -21.149 1.00 54.68  ? 56  ILE B CG2 1 
ATOM   2928  C CD1 . ILE B  2 56  ? -22.379 -66.400  -18.225 1.00 53.94  ? 56  ILE B CD1 1 
ATOM   2929  N N   . GLU B  2 57  ? -24.586 -68.826  -22.655 1.00 51.31  ? 57  GLU B N   1 
ATOM   2930  C CA  . GLU B  2 57  ? -24.286 -69.776  -23.722 1.00 53.43  ? 57  GLU B CA  1 
ATOM   2931  C C   . GLU B  2 57  ? -25.049 -69.487  -25.013 1.00 53.70  ? 57  GLU B C   1 
ATOM   2932  O O   . GLU B  2 57  ? -24.577 -69.804  -26.106 1.00 59.81  ? 57  GLU B O   1 
ATOM   2933  C CB  . GLU B  2 57  ? -24.562 -71.207  -23.250 1.00 69.16  ? 57  GLU B CB  1 
ATOM   2934  C CG  . GLU B  2 57  ? -23.898 -72.286  -24.090 1.00 106.08 ? 57  GLU B CG  1 
ATOM   2935  C CD  . GLU B  2 57  ? -24.857 -72.957  -25.054 1.00 115.43 ? 57  GLU B CD  1 
ATOM   2936  O OE1 . GLU B  2 57  ? -26.069 -73.009  -24.754 1.00 102.84 ? 57  GLU B OE1 1 
ATOM   2937  O OE2 . GLU B  2 57  ? -24.396 -73.441  -26.109 1.00 102.94 ? 57  GLU B OE2 1 
ATOM   2938  N N   . LYS B  2 58  ? -26.225 -68.881  -24.883 1.00 52.85  ? 58  LYS B N   1 
ATOM   2939  C CA  . LYS B  2 58  ? -27.067 -68.581  -26.038 1.00 50.21  ? 58  LYS B CA  1 
ATOM   2940  C C   . LYS B  2 58  ? -26.557 -67.395  -26.854 1.00 53.33  ? 58  LYS B C   1 
ATOM   2941  O O   . LYS B  2 58  ? -27.151 -67.029  -27.870 1.00 55.43  ? 58  LYS B O   1 
ATOM   2942  C CB  . LYS B  2 58  ? -28.517 -68.347  -25.606 1.00 48.66  ? 58  LYS B CB  1 
ATOM   2943  C CG  . LYS B  2 58  ? -29.208 -69.590  -25.062 1.00 57.90  ? 58  LYS B CG  1 
ATOM   2944  C CD  . LYS B  2 58  ? -29.188 -70.720  -26.078 1.00 59.18  ? 58  LYS B CD  1 
ATOM   2945  C CE  . LYS B  2 58  ? -29.852 -71.970  -25.525 1.00 61.88  ? 58  LYS B CE  1 
ATOM   2946  N NZ  . LYS B  2 58  ? -29.840 -73.085  -26.511 1.00 62.23  ? 58  LYS B NZ  1 
ATOM   2947  N N   . MET B  2 59  ? -25.454 -66.799  -26.411 1.00 48.11  ? 59  MET B N   1 
ATOM   2948  C CA  . MET B  2 59  ? -24.856 -65.685  -27.136 1.00 46.55  ? 59  MET B CA  1 
ATOM   2949  C C   . MET B  2 59  ? -23.721 -66.160  -28.037 1.00 62.36  ? 59  MET B C   1 
ATOM   2950  O O   . MET B  2 59  ? -22.554 -66.139  -27.642 1.00 75.12  ? 59  MET B O   1 
ATOM   2951  C CB  . MET B  2 59  ? -24.348 -64.618  -26.163 1.00 61.41  ? 59  MET B CB  1 
ATOM   2952  C CG  . MET B  2 59  ? -23.939 -63.321  -26.834 1.00 59.41  ? 59  MET B CG  1 
ATOM   2953  S SD  . MET B  2 59  ? -25.316 -62.494  -27.659 1.00 68.12  ? 59  MET B SD  1 
ATOM   2954  C CE  . MET B  2 59  ? -25.735 -61.231  -26.456 1.00 48.30  ? 59  MET B CE  1 
ATOM   2955  N N   . ASN B  2 60  ? -24.067 -66.593  -29.245 1.00 58.65  ? 60  ASN B N   1 
ATOM   2956  C CA  . ASN B  2 60  ? -23.059 -66.964  -30.228 1.00 72.87  ? 60  ASN B CA  1 
ATOM   2957  C C   . ASN B  2 60  ? -22.996 -65.919  -31.342 1.00 65.79  ? 60  ASN B C   1 
ATOM   2958  O O   . ASN B  2 60  ? -23.802 -65.923  -32.273 1.00 72.55  ? 60  ASN B O   1 
ATOM   2959  C CB  . ASN B  2 60  ? -23.309 -68.377  -30.774 1.00 86.39  ? 60  ASN B CB  1 
ATOM   2960  C CG  . ASN B  2 60  ? -24.442 -68.429  -31.779 1.00 114.72 ? 60  ASN B CG  1 
ATOM   2961  O OD1 . ASN B  2 60  ? -24.213 -68.347  -32.985 1.00 117.36 ? 60  ASN B OD1 1 
ATOM   2962  N ND2 . ASN B  2 60  ? -25.669 -68.573  -31.290 1.00 103.75 ? 60  ASN B ND2 1 
ATOM   2963  N N   . THR B  2 61  ? -22.037 -65.008  -31.224 1.00 61.33  ? 61  THR B N   1 
ATOM   2964  C CA  . THR B  2 61  ? -21.942 -63.874  -32.132 1.00 64.93  ? 61  THR B CA  1 
ATOM   2965  C C   . THR B  2 61  ? -21.202 -64.215  -33.420 1.00 65.77  ? 61  THR B C   1 
ATOM   2966  O O   . THR B  2 61  ? -20.398 -65.147  -33.463 1.00 55.97  ? 61  THR B O   1 
ATOM   2967  C CB  . THR B  2 61  ? -21.253 -62.674  -31.456 1.00 69.86  ? 61  THR B CB  1 
ATOM   2968  O OG1 . THR B  2 61  ? -19.948 -63.060  -31.009 1.00 83.35  ? 61  THR B OG1 1 
ATOM   2969  C CG2 . THR B  2 61  ? -22.069 -62.199  -30.264 1.00 52.30  ? 61  THR B CG2 1 
ATOM   2970  N N   . GLN B  2 62  ? -21.488 -63.454  -34.470 1.00 66.68  ? 62  GLN B N   1 
ATOM   2971  C CA  . GLN B  2 62  ? -20.811 -63.614  -35.747 1.00 69.04  ? 62  GLN B CA  1 
ATOM   2972  C C   . GLN B  2 62  ? -19.456 -62.925  -35.702 1.00 67.85  ? 62  GLN B C   1 
ATOM   2973  O O   . GLN B  2 62  ? -19.247 -62.001  -34.914 1.00 55.33  ? 62  GLN B O   1 
ATOM   2974  C CB  . GLN B  2 62  ? -21.653 -63.011  -36.871 1.00 61.73  ? 62  GLN B CB  1 
ATOM   2975  C CG  . GLN B  2 62  ? -22.973 -63.716  -37.113 1.00 46.59  ? 62  GLN B CG  1 
ATOM   2976  C CD  . GLN B  2 62  ? -22.786 -65.121  -37.645 1.00 70.59  ? 62  GLN B CD  1 
ATOM   2977  O OE1 . GLN B  2 62  ? -22.502 -66.051  -36.890 1.00 82.41  ? 62  GLN B OE1 1 
ATOM   2978  N NE2 . GLN B  2 62  ? -22.944 -65.284  -38.954 1.00 67.15  ? 62  GLN B NE2 1 
ATOM   2979  N N   . PHE B  2 63  ? -18.533 -63.375  -36.545 1.00 67.43  ? 63  PHE B N   1 
ATOM   2980  C CA  . PHE B  2 63  ? -17.265 -62.678  -36.691 1.00 59.28  ? 63  PHE B CA  1 
ATOM   2981  C C   . PHE B  2 63  ? -17.477 -61.459  -37.574 1.00 51.82  ? 63  PHE B C   1 
ATOM   2982  O O   . PHE B  2 63  ? -17.630 -61.580  -38.789 1.00 69.39  ? 63  PHE B O   1 
ATOM   2983  C CB  . PHE B  2 63  ? -16.196 -63.582  -37.302 1.00 60.93  ? 63  PHE B CB  1 
ATOM   2984  C CG  . PHE B  2 63  ? -14.833 -62.949  -37.358 1.00 66.21  ? 63  PHE B CG  1 
ATOM   2985  C CD1 . PHE B  2 63  ? -13.865 -63.275  -36.423 1.00 56.97  ? 63  PHE B CD1 1 
ATOM   2986  C CD2 . PHE B  2 63  ? -14.524 -62.020  -38.338 1.00 61.12  ? 63  PHE B CD2 1 
ATOM   2987  C CE1 . PHE B  2 63  ? -12.612 -62.692  -36.469 1.00 63.43  ? 63  PHE B CE1 1 
ATOM   2988  C CE2 . PHE B  2 63  ? -13.273 -61.433  -38.386 1.00 64.14  ? 63  PHE B CE2 1 
ATOM   2989  C CZ  . PHE B  2 63  ? -12.317 -61.769  -37.452 1.00 61.44  ? 63  PHE B CZ  1 
ATOM   2990  N N   . THR B  2 64  ? -17.494 -60.284  -36.957 1.00 46.16  ? 64  THR B N   1 
ATOM   2991  C CA  . THR B  2 64  ? -17.699 -59.046  -37.694 1.00 70.72  ? 64  THR B CA  1 
ATOM   2992  C C   . THR B  2 64  ? -16.718 -57.971  -37.259 1.00 47.36  ? 64  THR B C   1 
ATOM   2993  O O   . THR B  2 64  ? -16.306 -57.919  -36.101 1.00 32.53  ? 64  THR B O   1 
ATOM   2994  C CB  . THR B  2 64  ? -19.130 -58.507  -37.512 1.00 71.11  ? 64  THR B CB  1 
ATOM   2995  O OG1 . THR B  2 64  ? -19.504 -58.596  -36.131 1.00 56.09  ? 64  THR B OG1 1 
ATOM   2996  C CG2 . THR B  2 64  ? -20.115 -59.308  -38.351 1.00 65.83  ? 64  THR B CG2 1 
ATOM   2997  N N   . ALA B  2 65  ? -16.342 -57.114  -38.200 1.00 47.75  ? 65  ALA B N   1 
ATOM   2998  C CA  . ALA B  2 65  ? -15.510 -55.968  -37.879 1.00 45.35  ? 65  ALA B CA  1 
ATOM   2999  C C   . ALA B  2 65  ? -16.341 -54.699  -37.943 1.00 47.74  ? 65  ALA B C   1 
ATOM   3000  O O   . ALA B  2 65  ? -16.415 -54.044  -38.984 1.00 46.48  ? 65  ALA B O   1 
ATOM   3001  C CB  . ALA B  2 65  ? -14.331 -55.880  -38.823 1.00 46.50  ? 65  ALA B CB  1 
ATOM   3002  N N   . VAL B  2 66  ? -16.977 -54.364  -36.826 1.00 38.03  ? 66  VAL B N   1 
ATOM   3003  C CA  . VAL B  2 66  ? -17.707 -53.112  -36.722 1.00 39.80  ? 66  VAL B CA  1 
ATOM   3004  C C   . VAL B  2 66  ? -16.767 -51.993  -37.167 1.00 52.01  ? 66  VAL B C   1 
ATOM   3005  O O   . VAL B  2 66  ? -15.544 -52.162  -37.178 1.00 74.20  ? 66  VAL B O   1 
ATOM   3006  C CB  . VAL B  2 66  ? -18.155 -52.845  -35.275 1.00 34.09  ? 66  VAL B CB  1 
ATOM   3007  C CG1 . VAL B  2 66  ? -19.230 -51.761  -35.237 1.00 34.26  ? 66  VAL B CG1 1 
ATOM   3008  C CG2 . VAL B  2 66  ? -18.615 -54.142  -34.607 1.00 40.66  ? 66  VAL B CG2 1 
ATOM   3009  N N   . GLY B  2 67  ? -17.332 -50.863  -37.572 1.00 44.32  ? 67  GLY B N   1 
ATOM   3010  C CA  . GLY B  2 67  ? -16.524 -49.715  -37.932 1.00 58.42  ? 67  GLY B CA  1 
ATOM   3011  C C   . GLY B  2 67  ? -16.062 -49.740  -39.371 1.00 52.26  ? 67  GLY B C   1 
ATOM   3012  O O   . GLY B  2 67  ? -15.427 -50.693  -39.823 1.00 34.68  ? 67  GLY B O   1 
ATOM   3013  N N   . LYS B  2 68  ? -16.387 -48.673  -40.089 1.00 53.27  ? 68  LYS B N   1 
ATOM   3014  C CA  . LYS B  2 68  ? -16.039 -48.551  -41.492 1.00 32.93  ? 68  LYS B CA  1 
ATOM   3015  C C   . LYS B  2 68  ? -15.413 -47.186  -41.721 1.00 47.66  ? 68  LYS B C   1 
ATOM   3016  O O   . LYS B  2 68  ? -15.457 -46.321  -40.846 1.00 47.95  ? 68  LYS B O   1 
ATOM   3017  C CB  . LYS B  2 68  ? -17.290 -48.723  -42.351 1.00 54.65  ? 68  LYS B CB  1 
ATOM   3018  C CG  . LYS B  2 68  ? -17.996 -50.054  -42.135 1.00 50.33  ? 68  LYS B CG  1 
ATOM   3019  C CD  . LYS B  2 68  ? -17.513 -51.102  -43.125 1.00 57.02  ? 68  LYS B CD  1 
ATOM   3020  C CE  . LYS B  2 68  ? -17.904 -52.509  -42.699 1.00 66.38  ? 68  LYS B CE  1 
ATOM   3021  N NZ  . LYS B  2 68  ? -16.915 -53.095  -41.750 1.00 62.51  ? 68  LYS B NZ  1 
ATOM   3022  N N   . GLU B  2 69  ? -14.823 -46.998  -42.894 1.00 49.19  ? 69  GLU B N   1 
ATOM   3023  C CA  . GLU B  2 69  ? -14.176 -45.737  -43.222 1.00 39.20  ? 69  GLU B CA  1 
ATOM   3024  C C   . GLU B  2 69  ? -14.824 -45.113  -44.448 1.00 40.68  ? 69  GLU B C   1 
ATOM   3025  O O   . GLU B  2 69  ? -14.986 -45.769  -45.475 1.00 43.25  ? 69  GLU B O   1 
ATOM   3026  C CB  . GLU B  2 69  ? -12.683 -45.954  -43.462 1.00 50.29  ? 69  GLU B CB  1 
ATOM   3027  C CG  . GLU B  2 69  ? -11.936 -46.486  -42.250 1.00 64.49  ? 69  GLU B CG  1 
ATOM   3028  C CD  . GLU B  2 69  ? -10.501 -46.850  -42.567 1.00 67.94  ? 69  GLU B CD  1 
ATOM   3029  O OE1 . GLU B  2 69  ? -10.218 -47.163  -43.742 1.00 67.66  ? 69  GLU B OE1 1 
ATOM   3030  O OE2 . GLU B  2 69  ? -9.660  -46.828  -41.644 1.00 63.30  ? 69  GLU B OE2 1 
ATOM   3031  N N   . PHE B  2 70  ? -15.202 -43.845  -44.329 1.00 40.57  ? 70  PHE B N   1 
ATOM   3032  C CA  . PHE B  2 70  ? -15.829 -43.125  -45.429 1.00 36.55  ? 70  PHE B CA  1 
ATOM   3033  C C   . PHE B  2 70  ? -15.160 -41.771  -45.629 1.00 45.01  ? 70  PHE B C   1 
ATOM   3034  O O   . PHE B  2 70  ? -14.779 -41.110  -44.662 1.00 50.87  ? 70  PHE B O   1 
ATOM   3035  C CB  . PHE B  2 70  ? -17.323 -42.931  -45.159 1.00 43.15  ? 70  PHE B CB  1 
ATOM   3036  C CG  . PHE B  2 70  ? -18.054 -44.204  -44.835 1.00 41.09  ? 70  PHE B CG  1 
ATOM   3037  C CD1 . PHE B  2 70  ? -18.472 -45.055  -45.845 1.00 32.02  ? 70  PHE B CD1 1 
ATOM   3038  C CD2 . PHE B  2 70  ? -18.330 -44.546  -43.521 1.00 37.40  ? 70  PHE B CD2 1 
ATOM   3039  C CE1 . PHE B  2 70  ? -19.148 -46.225  -45.550 1.00 39.58  ? 70  PHE B CE1 1 
ATOM   3040  C CE2 . PHE B  2 70  ? -19.005 -45.714  -43.220 1.00 31.84  ? 70  PHE B CE2 1 
ATOM   3041  C CZ  . PHE B  2 70  ? -19.415 -46.554  -44.236 1.00 33.64  ? 70  PHE B CZ  1 
ATOM   3042  N N   . ASN B  2 71  ? -15.014 -41.360  -46.884 1.00 38.40  ? 71  ASN B N   1 
ATOM   3043  C CA  . ASN B  2 71  ? -14.437 -40.055  -47.185 1.00 41.77  ? 71  ASN B CA  1 
ATOM   3044  C C   . ASN B  2 71  ? -15.457 -38.931  -47.018 1.00 42.27  ? 71  ASN B C   1 
ATOM   3045  O O   . ASN B  2 71  ? -16.632 -39.183  -46.751 1.00 45.34  ? 71  ASN B O   1 
ATOM   3046  C CB  . ASN B  2 71  ? -13.821 -40.033  -48.588 1.00 50.19  ? 71  ASN B CB  1 
ATOM   3047  C CG  . ASN B  2 71  ? -14.838 -40.301  -49.679 1.00 52.80  ? 71  ASN B CG  1 
ATOM   3048  O OD1 . ASN B  2 71  ? -15.886 -39.657  -49.742 1.00 63.19  ? 71  ASN B OD1 1 
ATOM   3049  N ND2 . ASN B  2 71  ? -14.528 -41.250  -50.554 1.00 51.64  ? 71  ASN B ND2 1 
ATOM   3050  N N   . HIS B  2 72  ? -14.997 -37.695  -47.180 1.00 43.87  ? 72  HIS B N   1 
ATOM   3051  C CA  . HIS B  2 72  ? -15.826 -36.518  -46.934 1.00 55.87  ? 72  HIS B CA  1 
ATOM   3052  C C   . HIS B  2 72  ? -17.080 -36.466  -47.805 1.00 48.01  ? 72  HIS B C   1 
ATOM   3053  O O   . HIS B  2 72  ? -18.045 -35.781  -47.469 1.00 58.87  ? 72  HIS B O   1 
ATOM   3054  C CB  . HIS B  2 72  ? -15.001 -35.243  -47.127 1.00 60.52  ? 72  HIS B CB  1 
ATOM   3055  C CG  . HIS B  2 72  ? -14.397 -35.118  -48.489 1.00 77.35  ? 72  HIS B CG  1 
ATOM   3056  N ND1 . HIS B  2 72  ? -13.213 -35.730  -48.840 1.00 83.11  ? 72  HIS B ND1 1 
ATOM   3057  C CD2 . HIS B  2 72  ? -14.813 -34.448  -49.592 1.00 79.64  ? 72  HIS B CD2 1 
ATOM   3058  C CE1 . HIS B  2 72  ? -12.926 -35.445  -50.097 1.00 82.86  ? 72  HIS B CE1 1 
ATOM   3059  N NE2 . HIS B  2 72  ? -13.880 -34.669  -50.576 1.00 75.78  ? 72  HIS B NE2 1 
ATOM   3060  N N   . LEU B  2 73  ? -17.062 -37.190  -48.920 1.00 46.59  ? 73  LEU B N   1 
ATOM   3061  C CA  . LEU B  2 73  ? -18.196 -37.206  -49.839 1.00 38.41  ? 73  LEU B CA  1 
ATOM   3062  C C   . LEU B  2 73  ? -19.068 -38.445  -49.660 1.00 39.99  ? 73  LEU B C   1 
ATOM   3063  O O   . LEU B  2 73  ? -19.834 -38.811  -50.552 1.00 44.95  ? 73  LEU B O   1 
ATOM   3064  C CB  . LEU B  2 73  ? -17.716 -37.105  -51.290 1.00 44.86  ? 73  LEU B CB  1 
ATOM   3065  C CG  . LEU B  2 73  ? -17.162 -35.744  -51.717 1.00 50.19  ? 73  LEU B CG  1 
ATOM   3066  C CD1 . LEU B  2 73  ? -16.587 -35.808  -53.122 1.00 45.88  ? 73  LEU B CD1 1 
ATOM   3067  C CD2 . LEU B  2 73  ? -18.245 -34.680  -51.624 1.00 47.93  ? 73  LEU B CD2 1 
ATOM   3068  N N   . GLU B  2 74  ? -18.948 -39.086  -48.502 1.00 41.94  ? 74  GLU B N   1 
ATOM   3069  C CA  . GLU B  2 74  ? -19.739 -40.270  -48.189 1.00 34.16  ? 74  GLU B CA  1 
ATOM   3070  C C   . GLU B  2 74  ? -20.354 -40.155  -46.797 1.00 42.92  ? 74  GLU B C   1 
ATOM   3071  O O   . GLU B  2 74  ? -20.534 -41.154  -46.103 1.00 45.95  ? 74  GLU B O   1 
ATOM   3072  C CB  . GLU B  2 74  ? -18.875 -41.529  -48.282 1.00 32.44  ? 74  GLU B CB  1 
ATOM   3073  C CG  . GLU B  2 74  ? -18.371 -41.841  -49.682 1.00 39.18  ? 74  GLU B CG  1 
ATOM   3074  C CD  . GLU B  2 74  ? -17.425 -43.027  -49.706 1.00 61.76  ? 74  GLU B CD  1 
ATOM   3075  O OE1 . GLU B  2 74  ? -16.474 -43.045  -48.896 1.00 51.44  ? 74  GLU B OE1 1 
ATOM   3076  O OE2 . GLU B  2 74  ? -17.631 -43.938  -50.536 1.00 36.90  ? 74  GLU B OE2 1 
ATOM   3077  N N   . LYS B  2 75  ? -20.675 -38.928  -46.398 1.00 40.80  ? 75  LYS B N   1 
ATOM   3078  C CA  . LYS B  2 75  ? -21.242 -38.666  -45.079 1.00 43.13  ? 75  LYS B CA  1 
ATOM   3079  C C   . LYS B  2 75  ? -22.573 -39.388  -44.876 1.00 42.18  ? 75  LYS B C   1 
ATOM   3080  O O   . LYS B  2 75  ? -22.971 -39.666  -43.741 1.00 42.05  ? 75  LYS B O   1 
ATOM   3081  C CB  . LYS B  2 75  ? -21.423 -37.160  -44.869 1.00 40.19  ? 75  LYS B CB  1 
ATOM   3082  C CG  . LYS B  2 75  ? -22.138 -36.792  -43.579 1.00 53.81  ? 75  LYS B CG  1 
ATOM   3083  C CD  . LYS B  2 75  ? -21.375 -37.286  -42.361 1.00 49.76  ? 75  LYS B CD  1 
ATOM   3084  C CE  . LYS B  2 75  ? -20.156 -36.424  -42.084 1.00 71.35  ? 75  LYS B CE  1 
ATOM   3085  N NZ  . LYS B  2 75  ? -19.423 -36.880  -40.869 1.00 89.57  ? 75  LYS B NZ  1 
ATOM   3086  N N   . ARG B  2 76  ? -23.251 -39.694  -45.980 1.00 36.47  ? 76  ARG B N   1 
ATOM   3087  C CA  . ARG B  2 76  ? -24.577 -40.308  -45.927 1.00 41.26  ? 76  ARG B CA  1 
ATOM   3088  C C   . ARG B  2 76  ? -24.512 -41.782  -45.521 1.00 34.78  ? 76  ARG B C   1 
ATOM   3089  O O   . ARG B  2 76  ? -25.223 -42.209  -44.614 1.00 35.76  ? 76  ARG B O   1 
ATOM   3090  C CB  . ARG B  2 76  ? -25.316 -40.140  -47.263 1.00 29.30  ? 76  ARG B CB  1 
ATOM   3091  C CG  . ARG B  2 76  ? -25.564 -38.688  -47.676 1.00 31.14  ? 76  ARG B CG  1 
ATOM   3092  C CD  . ARG B  2 76  ? -26.310 -38.586  -49.007 1.00 43.95  ? 76  ARG B CD  1 
ATOM   3093  N NE  . ARG B  2 76  ? -25.565 -39.201  -50.103 1.00 45.64  ? 76  ARG B NE  1 
ATOM   3094  C CZ  . ARG B  2 76  ? -26.123 -39.766  -51.170 1.00 36.44  ? 76  ARG B CZ  1 
ATOM   3095  N NH1 . ARG B  2 76  ? -27.438 -39.804  -51.302 1.00 42.82  ? 76  ARG B NH1 1 
ATOM   3096  N NH2 . ARG B  2 76  ? -25.364 -40.304  -52.109 1.00 30.43  ? 76  ARG B NH2 1 
ATOM   3097  N N   . ILE B  2 77  ? -23.659 -42.556  -46.185 1.00 37.97  ? 77  ILE B N   1 
ATOM   3098  C CA  . ILE B  2 77  ? -23.463 -43.951  -45.806 1.00 35.62  ? 77  ILE B CA  1 
ATOM   3099  C C   . ILE B  2 77  ? -22.772 -44.036  -44.448 1.00 32.38  ? 77  ILE B C   1 
ATOM   3100  O O   . ILE B  2 77  ? -22.962 -44.997  -43.704 1.00 29.07  ? 77  ILE B O   1 
ATOM   3101  C CB  . ILE B  2 77  ? -22.655 -44.733  -46.863 1.00 28.28  ? 77  ILE B CB  1 
ATOM   3102  C CG1 . ILE B  2 77  ? -21.519 -43.871  -47.415 1.00 56.93  ? 77  ILE B CG1 1 
ATOM   3103  C CG2 . ILE B  2 77  ? -23.561 -45.180  -48.000 1.00 35.73  ? 77  ILE B CG2 1 
ATOM   3104  C CD1 . ILE B  2 77  ? -20.734 -44.529  -48.530 1.00 57.29  ? 77  ILE B CD1 1 
ATOM   3105  N N   . GLU B  2 78  ? -21.974 -43.021  -44.129 1.00 28.81  ? 78  GLU B N   1 
ATOM   3106  C CA  . GLU B  2 78  ? -21.350 -42.932  -42.816 1.00 36.01  ? 78  GLU B CA  1 
ATOM   3107  C C   . GLU B  2 78  ? -22.424 -42.828  -41.739 1.00 34.32  ? 78  GLU B C   1 
ATOM   3108  O O   . GLU B  2 78  ? -22.322 -43.454  -40.685 1.00 34.82  ? 78  GLU B O   1 
ATOM   3109  C CB  . GLU B  2 78  ? -20.409 -41.728  -42.738 1.00 36.96  ? 78  GLU B CB  1 
ATOM   3110  C CG  . GLU B  2 78  ? -19.705 -41.602  -41.395 1.00 45.70  ? 78  GLU B CG  1 
ATOM   3111  C CD  . GLU B  2 78  ? -18.856 -40.351  -41.281 1.00 69.75  ? 78  GLU B CD  1 
ATOM   3112  O OE1 . GLU B  2 78  ? -18.379 -39.850  -42.321 1.00 85.35  ? 78  GLU B OE1 1 
ATOM   3113  O OE2 . GLU B  2 78  ? -18.663 -39.870  -40.145 1.00 78.03  ? 78  GLU B OE2 1 
ATOM   3114  N N   . ASN B  2 79  ? -23.455 -42.033  -42.013 1.00 36.60  ? 79  ASN B N   1 
ATOM   3115  C CA  . ASN B  2 79  ? -24.570 -41.876  -41.086 1.00 38.67  ? 79  ASN B CA  1 
ATOM   3116  C C   . ASN B  2 79  ? -25.493 -43.090  -41.082 1.00 36.35  ? 79  ASN B C   1 
ATOM   3117  O O   . ASN B  2 79  ? -26.047 -43.453  -40.045 1.00 37.56  ? 79  ASN B O   1 
ATOM   3118  C CB  . ASN B  2 79  ? -25.355 -40.599  -41.395 1.00 33.82  ? 79  ASN B CB  1 
ATOM   3119  C CG  . ASN B  2 79  ? -24.646 -39.350  -40.906 1.00 52.18  ? 79  ASN B CG  1 
ATOM   3120  O OD1 . ASN B  2 79  ? -23.907 -39.388  -39.922 1.00 52.51  ? 79  ASN B OD1 1 
ATOM   3121  N ND2 . ASN B  2 79  ? -24.872 -38.233  -41.590 1.00 53.12  ? 79  ASN B ND2 1 
ATOM   3122  N N   . LEU B  2 80  ? -25.657 -43.714  -42.245 1.00 16.64  ? 80  LEU B N   1 
ATOM   3123  C CA  . LEU B  2 80  ? -26.411 -44.956  -42.330 1.00 18.43  ? 80  LEU B CA  1 
ATOM   3124  C C   . LEU B  2 80  ? -25.739 -45.963  -41.409 1.00 45.21  ? 80  LEU B C   1 
ATOM   3125  O O   . LEU B  2 80  ? -26.388 -46.597  -40.577 1.00 41.16  ? 80  LEU B O   1 
ATOM   3126  C CB  . LEU B  2 80  ? -26.414 -45.487  -43.764 1.00 33.55  ? 80  LEU B CB  1 
ATOM   3127  C CG  . LEU B  2 80  ? -27.562 -46.406  -44.201 1.00 38.31  ? 80  LEU B CG  1 
ATOM   3128  C CD1 . LEU B  2 80  ? -27.131 -47.259  -45.388 1.00 33.01  ? 80  LEU B CD1 1 
ATOM   3129  C CD2 . LEU B  2 80  ? -28.057 -47.286  -43.063 1.00 28.12  ? 80  LEU B CD2 1 
ATOM   3130  N N   . ASN B  2 81  ? -24.425 -46.092  -41.564 1.00 44.82  ? 81  ASN B N   1 
ATOM   3131  C CA  . ASN B  2 81  ? -23.623 -46.971  -40.723 1.00 23.33  ? 81  ASN B CA  1 
ATOM   3132  C C   . ASN B  2 81  ? -23.758 -46.630  -39.244 1.00 31.07  ? 81  ASN B C   1 
ATOM   3133  O O   . ASN B  2 81  ? -23.907 -47.517  -38.404 1.00 40.12  ? 81  ASN B O   1 
ATOM   3134  C CB  . ASN B  2 81  ? -22.153 -46.904  -41.141 1.00 38.28  ? 81  ASN B CB  1 
ATOM   3135  C CG  . ASN B  2 81  ? -21.258 -47.755  -40.263 1.00 39.99  ? 81  ASN B CG  1 
ATOM   3136  O OD1 . ASN B  2 81  ? -21.376 -48.980  -40.238 1.00 39.41  ? 81  ASN B OD1 1 
ATOM   3137  N ND2 . ASN B  2 81  ? -20.353 -47.108  -39.538 1.00 32.60  ? 81  ASN B ND2 1 
ATOM   3138  N N   . LYS B  2 82  ? -23.698 -45.342  -38.926 1.00 31.69  ? 82  LYS B N   1 
ATOM   3139  C CA  . LYS B  2 82  ? -23.865 -44.899  -37.548 1.00 41.81  ? 82  LYS B CA  1 
ATOM   3140  C C   . LYS B  2 82  ? -25.245 -45.280  -37.023 1.00 45.77  ? 82  LYS B C   1 
ATOM   3141  O O   . LYS B  2 82  ? -25.398 -45.628  -35.852 1.00 39.02  ? 82  LYS B O   1 
ATOM   3142  C CB  . LYS B  2 82  ? -23.657 -43.389  -37.431 1.00 43.10  ? 82  LYS B CB  1 
ATOM   3143  C CG  . LYS B  2 82  ? -24.043 -42.829  -36.072 1.00 53.22  ? 82  LYS B CG  1 
ATOM   3144  C CD  . LYS B  2 82  ? -23.816 -41.331  -35.990 1.00 62.54  ? 82  LYS B CD  1 
ATOM   3145  C CE  . LYS B  2 82  ? -24.443 -40.754  -34.730 1.00 87.67  ? 82  LYS B CE  1 
ATOM   3146  N NZ  . LYS B  2 82  ? -23.960 -41.439  -33.499 1.00 70.84  ? 82  LYS B NZ  1 
ATOM   3147  N N   . LYS B  2 83  ? -26.246 -45.214  -37.895 1.00 41.92  ? 83  LYS B N   1 
ATOM   3148  C CA  . LYS B  2 83  ? -27.610 -45.555  -37.506 1.00 38.39  ? 83  LYS B CA  1 
ATOM   3149  C C   . LYS B  2 83  ? -27.737 -47.028  -37.129 1.00 33.96  ? 83  LYS B C   1 
ATOM   3150  O O   . LYS B  2 83  ? -28.367 -47.364  -36.127 1.00 31.45  ? 83  LYS B O   1 
ATOM   3151  C CB  . LYS B  2 83  ? -28.610 -45.202  -38.613 1.00 27.79  ? 83  LYS B CB  1 
ATOM   3152  C CG  . LYS B  2 83  ? -30.042 -45.591  -38.268 1.00 35.25  ? 83  LYS B CG  1 
ATOM   3153  C CD  . LYS B  2 83  ? -31.064 -44.951  -39.196 1.00 34.30  ? 83  LYS B CD  1 
ATOM   3154  C CE  . LYS B  2 83  ? -31.071 -45.601  -40.569 1.00 32.19  ? 83  LYS B CE  1 
ATOM   3155  N NZ  . LYS B  2 83  ? -32.258 -45.180  -41.364 1.00 32.35  ? 83  LYS B NZ  1 
ATOM   3156  N N   . VAL B  2 84  ? -27.138 -47.904  -37.930 1.00 25.28  ? 84  VAL B N   1 
ATOM   3157  C CA  . VAL B  2 84  ? -27.216 -49.337  -37.663 1.00 35.96  ? 84  VAL B CA  1 
ATOM   3158  C C   . VAL B  2 84  ? -26.450 -49.699  -36.393 1.00 36.82  ? 84  VAL B C   1 
ATOM   3159  O O   . VAL B  2 84  ? -26.790 -50.664  -35.707 1.00 38.20  ? 84  VAL B O   1 
ATOM   3160  C CB  . VAL B  2 84  ? -26.708 -50.181  -38.852 1.00 30.19  ? 84  VAL B CB  1 
ATOM   3161  C CG1 . VAL B  2 84  ? -25.211 -50.012  -39.034 1.00 47.52  ? 84  VAL B CG1 1 
ATOM   3162  C CG2 . VAL B  2 84  ? -27.055 -51.645  -38.642 1.00 42.73  ? 84  VAL B CG2 1 
ATOM   3163  N N   . ASP B  2 85  ? -25.421 -48.918  -36.081 1.00 36.46  ? 85  ASP B N   1 
ATOM   3164  C CA  . ASP B  2 85  ? -24.663 -49.109  -34.849 1.00 26.99  ? 85  ASP B CA  1 
ATOM   3165  C C   . ASP B  2 85  ? -25.456 -48.626  -33.640 1.00 32.11  ? 85  ASP B C   1 
ATOM   3166  O O   . ASP B  2 85  ? -25.486 -49.286  -32.601 1.00 38.34  ? 85  ASP B O   1 
ATOM   3167  C CB  . ASP B  2 85  ? -23.322 -48.376  -34.919 1.00 35.25  ? 85  ASP B CB  1 
ATOM   3168  C CG  . ASP B  2 85  ? -22.295 -49.115  -35.752 1.00 48.22  ? 85  ASP B CG  1 
ATOM   3169  O OD1 . ASP B  2 85  ? -22.524 -50.301  -36.065 1.00 45.93  ? 85  ASP B OD1 1 
ATOM   3170  O OD2 . ASP B  2 85  ? -21.255 -48.509  -36.087 1.00 54.36  ? 85  ASP B OD2 1 
ATOM   3171  N N   . ASP B  2 86  ? -26.093 -47.468  -33.781 1.00 32.35  ? 86  ASP B N   1 
ATOM   3172  C CA  . ASP B  2 86  ? -26.892 -46.898  -32.702 1.00 31.42  ? 86  ASP B CA  1 
ATOM   3173  C C   . ASP B  2 86  ? -28.178 -47.685  -32.482 1.00 39.99  ? 86  ASP B C   1 
ATOM   3174  O O   . ASP B  2 86  ? -28.749 -47.668  -31.392 1.00 42.97  ? 86  ASP B O   1 
ATOM   3175  C CB  . ASP B  2 86  ? -27.214 -45.430  -32.988 1.00 46.45  ? 86  ASP B CB  1 
ATOM   3176  C CG  . ASP B  2 86  ? -26.021 -44.520  -32.775 1.00 67.07  ? 86  ASP B CG  1 
ATOM   3177  O OD1 . ASP B  2 86  ? -25.037 -44.967  -32.149 1.00 71.98  ? 86  ASP B OD1 1 
ATOM   3178  O OD2 . ASP B  2 86  ? -26.071 -43.358  -33.228 1.00 69.40  ? 86  ASP B OD2 1 
ATOM   3179  N N   . GLY B  2 87  ? -28.632 -48.373  -33.525 1.00 35.61  ? 87  GLY B N   1 
ATOM   3180  C CA  . GLY B  2 87  ? -29.820 -49.199  -33.429 1.00 24.59  ? 87  GLY B CA  1 
ATOM   3181  C C   . GLY B  2 87  ? -29.559 -50.441  -32.601 1.00 34.69  ? 87  GLY B C   1 
ATOM   3182  O O   . GLY B  2 87  ? -30.277 -50.722  -31.640 1.00 35.62  ? 87  GLY B O   1 
ATOM   3183  N N   . PHE B  2 88  ? -28.525 -51.186  -32.977 1.00 30.90  ? 88  PHE B N   1 
ATOM   3184  C CA  . PHE B  2 88  ? -28.135 -52.379  -32.237 1.00 33.60  ? 88  PHE B CA  1 
ATOM   3185  C C   . PHE B  2 88  ? -27.794 -52.023  -30.795 1.00 36.83  ? 88  PHE B C   1 
ATOM   3186  O O   . PHE B  2 88  ? -28.065 -52.794  -29.875 1.00 38.97  ? 88  PHE B O   1 
ATOM   3187  C CB  . PHE B  2 88  ? -26.942 -53.065  -32.906 1.00 36.25  ? 88  PHE B CB  1 
ATOM   3188  C CG  . PHE B  2 88  ? -27.259 -53.668  -34.244 1.00 29.54  ? 88  PHE B CG  1 
ATOM   3189  C CD1 . PHE B  2 88  ? -26.262 -53.864  -35.185 1.00 23.97  ? 88  PHE B CD1 1 
ATOM   3190  C CD2 . PHE B  2 88  ? -28.555 -54.039  -34.562 1.00 32.76  ? 88  PHE B CD2 1 
ATOM   3191  C CE1 . PHE B  2 88  ? -26.550 -54.420  -36.416 1.00 33.01  ? 88  PHE B CE1 1 
ATOM   3192  C CE2 . PHE B  2 88  ? -28.851 -54.595  -35.792 1.00 39.54  ? 88  PHE B CE2 1 
ATOM   3193  C CZ  . PHE B  2 88  ? -27.847 -54.785  -36.721 1.00 38.14  ? 88  PHE B CZ  1 
ATOM   3194  N N   . LEU B  2 89  ? -27.202 -50.848  -30.608 1.00 30.35  ? 89  LEU B N   1 
ATOM   3195  C CA  . LEU B  2 89  ? -26.838 -50.374  -29.279 1.00 25.31  ? 89  LEU B CA  1 
ATOM   3196  C C   . LEU B  2 89  ? -28.068 -50.200  -28.397 1.00 31.39  ? 89  LEU B C   1 
ATOM   3197  O O   . LEU B  2 89  ? -28.065 -50.587  -27.229 1.00 38.67  ? 89  LEU B O   1 
ATOM   3198  C CB  . LEU B  2 89  ? -26.069 -49.054  -29.370 1.00 28.56  ? 89  LEU B CB  1 
ATOM   3199  C CG  . LEU B  2 89  ? -25.746 -48.382  -28.034 1.00 34.17  ? 89  LEU B CG  1 
ATOM   3200  C CD1 . LEU B  2 89  ? -25.062 -49.360  -27.092 1.00 41.13  ? 89  LEU B CD1 1 
ATOM   3201  C CD2 . LEU B  2 89  ? -24.887 -47.145  -28.245 1.00 38.00  ? 89  LEU B CD2 1 
ATOM   3202  N N   . ASP B  2 90  ? -29.120 -49.618  -28.962 1.00 32.54  ? 90  ASP B N   1 
ATOM   3203  C CA  . ASP B  2 90  ? -30.352 -49.376  -28.218 1.00 30.26  ? 90  ASP B CA  1 
ATOM   3204  C C   . ASP B  2 90  ? -31.118 -50.665  -27.927 1.00 32.60  ? 90  ASP B C   1 
ATOM   3205  O O   . ASP B  2 90  ? -31.664 -50.838  -26.838 1.00 35.61  ? 90  ASP B O   1 
ATOM   3206  C CB  . ASP B  2 90  ? -31.244 -48.379  -28.961 1.00 32.83  ? 90  ASP B CB  1 
ATOM   3207  C CG  . ASP B  2 90  ? -30.743 -46.951  -28.846 1.00 51.15  ? 90  ASP B CG  1 
ATOM   3208  O OD1 . ASP B  2 90  ? -29.964 -46.667  -27.911 1.00 63.53  ? 90  ASP B OD1 1 
ATOM   3209  O OD2 . ASP B  2 90  ? -31.130 -46.112  -29.686 1.00 66.08  ? 90  ASP B OD2 1 
ATOM   3210  N N   . ILE B  2 91  ? -31.157 -51.565  -28.905 1.00 36.71  ? 91  ILE B N   1 
ATOM   3211  C CA  . ILE B  2 91  ? -31.832 -52.847  -28.737 1.00 29.77  ? 91  ILE B CA  1 
ATOM   3212  C C   . ILE B  2 91  ? -31.173 -53.676  -27.642 1.00 39.64  ? 91  ILE B C   1 
ATOM   3213  O O   . ILE B  2 91  ? -31.836 -54.132  -26.709 1.00 37.36  ? 91  ILE B O   1 
ATOM   3214  C CB  . ILE B  2 91  ? -31.828 -53.664  -30.042 1.00 28.17  ? 91  ILE B CB  1 
ATOM   3215  C CG1 . ILE B  2 91  ? -32.652 -52.957  -31.119 1.00 26.44  ? 91  ILE B CG1 1 
ATOM   3216  C CG2 . ILE B  2 91  ? -32.371 -55.063  -29.795 1.00 47.21  ? 91  ILE B CG2 1 
ATOM   3217  C CD1 . ILE B  2 91  ? -32.651 -53.669  -32.454 1.00 46.32  ? 91  ILE B CD1 1 
ATOM   3218  N N   . TRP B  2 92  ? -29.863 -53.866  -27.761 1.00 33.36  ? 92  TRP B N   1 
ATOM   3219  C CA  . TRP B  2 92  ? -29.122 -54.704  -26.826 1.00 32.21  ? 92  TRP B CA  1 
ATOM   3220  C C   . TRP B  2 92  ? -29.100 -54.144  -25.409 1.00 33.97  ? 92  TRP B C   1 
ATOM   3221  O O   . TRP B  2 92  ? -29.239 -54.890  -24.441 1.00 36.91  ? 92  TRP B O   1 
ATOM   3222  C CB  . TRP B  2 92  ? -27.700 -54.956  -27.332 1.00 31.77  ? 92  TRP B CB  1 
ATOM   3223  C CG  . TRP B  2 92  ? -27.653 -55.983  -28.412 1.00 28.40  ? 92  TRP B CG  1 
ATOM   3224  C CD1 . TRP B  2 92  ? -27.301 -55.791  -29.716 1.00 29.64  ? 92  TRP B CD1 1 
ATOM   3225  C CD2 . TRP B  2 92  ? -27.997 -57.366  -28.288 1.00 27.11  ? 92  TRP B CD2 1 
ATOM   3226  N NE1 . TRP B  2 92  ? -27.391 -56.975  -30.409 1.00 47.70  ? 92  TRP B NE1 1 
ATOM   3227  C CE2 . TRP B  2 92  ? -27.817 -57.957  -29.553 1.00 34.97  ? 92  TRP B CE2 1 
ATOM   3228  C CE3 . TRP B  2 92  ? -28.433 -58.164  -27.226 1.00 35.97  ? 92  TRP B CE3 1 
ATOM   3229  C CZ2 . TRP B  2 92  ? -28.058 -59.310  -29.785 1.00 34.33  ? 92  TRP B CZ2 1 
ATOM   3230  C CZ3 . TRP B  2 92  ? -28.671 -59.505  -27.458 1.00 36.94  ? 92  TRP B CZ3 1 
ATOM   3231  C CH2 . TRP B  2 92  ? -28.484 -60.064  -28.727 1.00 38.91  ? 92  TRP B CH2 1 
ATOM   3232  N N   . THR B  2 93  ? -28.927 -52.833  -25.288 1.00 31.09  ? 93  THR B N   1 
ATOM   3233  C CA  . THR B  2 93  ? -28.945 -52.191  -23.979 1.00 32.19  ? 93  THR B CA  1 
ATOM   3234  C C   . THR B  2 93  ? -30.288 -52.413  -23.295 1.00 32.68  ? 93  THR B C   1 
ATOM   3235  O O   . THR B  2 93  ? -30.348 -52.855  -22.148 1.00 34.43  ? 93  THR B O   1 
ATOM   3236  C CB  . THR B  2 93  ? -28.675 -50.679  -24.080 1.00 33.81  ? 93  THR B CB  1 
ATOM   3237  O OG1 . THR B  2 93  ? -27.353 -50.459  -24.589 1.00 36.45  ? 93  THR B OG1 1 
ATOM   3238  C CG2 . THR B  2 93  ? -28.801 -50.023  -22.712 1.00 33.38  ? 93  THR B CG2 1 
ATOM   3239  N N   . TYR B  2 94  ? -31.365 -52.111  -24.011 1.00 36.27  ? 94  TYR B N   1 
ATOM   3240  C CA  . TYR B  2 94  ? -32.710 -52.239  -23.463 1.00 32.81  ? 94  TYR B CA  1 
ATOM   3241  C C   . TYR B  2 94  ? -33.035 -53.683  -23.086 1.00 34.38  ? 94  TYR B C   1 
ATOM   3242  O O   . TYR B  2 94  ? -33.532 -53.949  -21.993 1.00 30.87  ? 94  TYR B O   1 
ATOM   3243  C CB  . TYR B  2 94  ? -33.746 -51.699  -24.452 1.00 26.60  ? 94  TYR B CB  1 
ATOM   3244  C CG  . TYR B  2 94  ? -35.143 -51.602  -23.882 1.00 35.77  ? 94  TYR B CG  1 
ATOM   3245  C CD1 . TYR B  2 94  ? -35.489 -50.574  -23.015 1.00 34.37  ? 94  TYR B CD1 1 
ATOM   3246  C CD2 . TYR B  2 94  ? -36.118 -52.533  -24.214 1.00 39.64  ? 94  TYR B CD2 1 
ATOM   3247  C CE1 . TYR B  2 94  ? -36.764 -50.478  -22.490 1.00 30.70  ? 94  TYR B CE1 1 
ATOM   3248  C CE2 . TYR B  2 94  ? -37.396 -52.446  -23.695 1.00 41.55  ? 94  TYR B CE2 1 
ATOM   3249  C CZ  . TYR B  2 94  ? -37.714 -51.416  -22.834 1.00 46.64  ? 94  TYR B CZ  1 
ATOM   3250  O OH  . TYR B  2 94  ? -38.984 -51.323  -22.313 1.00 56.00  ? 94  TYR B OH  1 
ATOM   3251  N N   . ASN B  2 95  ? -32.750 -54.613  -23.992 1.00 35.04  ? 95  ASN B N   1 
ATOM   3252  C CA  . ASN B  2 95  ? -33.035 -56.022  -23.744 1.00 30.11  ? 95  ASN B CA  1 
ATOM   3253  C C   . ASN B  2 95  ? -32.222 -56.596  -22.589 1.00 38.38  ? 95  ASN B C   1 
ATOM   3254  O O   . ASN B  2 95  ? -32.752 -57.322  -21.748 1.00 43.92  ? 95  ASN B O   1 
ATOM   3255  C CB  . ASN B  2 95  ? -32.815 -56.850  -25.011 1.00 35.61  ? 95  ASN B CB  1 
ATOM   3256  C CG  . ASN B  2 95  ? -33.884 -56.607  -26.055 1.00 45.24  ? 95  ASN B CG  1 
ATOM   3257  O OD1 . ASN B  2 95  ? -34.678 -55.674  -25.940 1.00 36.52  ? 95  ASN B OD1 1 
ATOM   3258  N ND2 . ASN B  2 95  ? -33.913 -57.450  -27.081 1.00 51.48  ? 95  ASN B ND2 1 
ATOM   3259  N N   . ALA B  2 96  ? -30.934 -56.268  -22.553 1.00 32.02  ? 96  ALA B N   1 
ATOM   3260  C CA  . ALA B  2 96  ? -30.049 -56.754  -21.500 1.00 39.18  ? 96  ALA B CA  1 
ATOM   3261  C C   . ALA B  2 96  ? -30.489 -56.229  -20.140 1.00 41.77  ? 96  ALA B C   1 
ATOM   3262  O O   . ALA B  2 96  ? -30.558 -56.979  -19.166 1.00 43.29  ? 96  ALA B O   1 
ATOM   3263  C CB  . ALA B  2 96  ? -28.613 -56.349  -21.787 1.00 41.20  ? 96  ALA B CB  1 
ATOM   3264  N N   . GLU B  2 97  ? -30.783 -54.935  -20.082 1.00 29.21  ? 97  GLU B N   1 
ATOM   3265  C CA  . GLU B  2 97  ? -31.249 -54.316  -18.848 1.00 37.98  ? 97  GLU B CA  1 
ATOM   3266  C C   . GLU B  2 97  ? -32.516 -54.989  -18.336 1.00 45.16  ? 97  GLU B C   1 
ATOM   3267  O O   . GLU B  2 97  ? -32.629 -55.284  -17.148 1.00 44.21  ? 97  GLU B O   1 
ATOM   3268  C CB  . GLU B  2 97  ? -31.503 -52.821  -19.047 1.00 39.06  ? 97  GLU B CB  1 
ATOM   3269  C CG  . GLU B  2 97  ? -30.250 -51.991  -19.271 1.00 36.29  ? 97  GLU B CG  1 
ATOM   3270  C CD  . GLU B  2 97  ? -29.450 -51.769  -18.001 1.00 53.30  ? 97  GLU B CD  1 
ATOM   3271  O OE1 . GLU B  2 97  ? -28.581 -50.872  -17.999 1.00 57.61  ? 97  GLU B OE1 1 
ATOM   3272  O OE2 . GLU B  2 97  ? -29.690 -52.483  -17.005 1.00 76.57  ? 97  GLU B OE2 1 
ATOM   3273  N N   . LEU B  2 98  ? -33.471 -55.233  -19.226 1.00 41.55  ? 98  LEU B N   1 
ATOM   3274  C CA  . LEU B  2 98  ? -34.735 -55.821  -18.796 1.00 33.30  ? 98  LEU B CA  1 
ATOM   3275  C C   . LEU B  2 98  ? -34.640 -57.325  -18.563 1.00 44.63  ? 98  LEU B C   1 
ATOM   3276  O O   . LEU B  2 98  ? -35.357 -57.870  -17.726 1.00 44.57  ? 98  LEU B O   1 
ATOM   3277  C CB  . LEU B  2 98  ? -35.876 -55.494  -19.765 1.00 31.02  ? 98  LEU B CB  1 
ATOM   3278  C CG  . LEU B  2 98  ? -36.747 -54.305  -19.352 1.00 38.43  ? 98  LEU B CG  1 
ATOM   3279  C CD1 . LEU B  2 98  ? -36.302 -53.018  -20.023 1.00 42.50  ? 98  LEU B CD1 1 
ATOM   3280  C CD2 . LEU B  2 98  ? -38.219 -54.592  -19.585 1.00 63.16  ? 98  LEU B CD2 1 
ATOM   3281  N N   . LEU B  2 99  ? -33.757 -57.993  -19.297 1.00 43.03  ? 99  LEU B N   1 
ATOM   3282  C CA  . LEU B  2 99  ? -33.532 -59.414  -19.072 1.00 43.97  ? 99  LEU B CA  1 
ATOM   3283  C C   . LEU B  2 99  ? -33.083 -59.642  -17.637 1.00 39.38  ? 99  LEU B C   1 
ATOM   3284  O O   . LEU B  2 99  ? -33.592 -60.527  -16.953 1.00 37.85  ? 99  LEU B O   1 
ATOM   3285  C CB  . LEU B  2 99  ? -32.481 -59.962  -20.035 1.00 42.30  ? 99  LEU B CB  1 
ATOM   3286  C CG  . LEU B  2 99  ? -32.182 -61.453  -19.873 1.00 50.23  ? 99  LEU B CG  1 
ATOM   3287  C CD1 . LEU B  2 99  ? -33.432 -62.281  -20.139 1.00 44.20  ? 99  LEU B CD1 1 
ATOM   3288  C CD2 . LEU B  2 99  ? -31.045 -61.881  -20.789 1.00 51.87  ? 99  LEU B CD2 1 
ATOM   3289  N N   . VAL B  2 100 ? -32.124 -58.836  -17.189 1.00 34.97  ? 100 VAL B N   1 
ATOM   3290  C CA  . VAL B  2 100 ? -31.609 -58.943  -15.829 1.00 44.08  ? 100 VAL B CA  1 
ATOM   3291  C C   . VAL B  2 100 ? -32.693 -58.637  -14.810 1.00 40.61  ? 100 VAL B C   1 
ATOM   3292  O O   . VAL B  2 100 ? -32.883 -59.384  -13.851 1.00 44.19  ? 100 VAL B O   1 
ATOM   3293  C CB  . VAL B  2 100 ? -30.423 -57.995  -15.590 1.00 35.27  ? 100 VAL B CB  1 
ATOM   3294  C CG1 . VAL B  2 100 ? -30.096 -57.923  -14.107 1.00 42.06  ? 100 VAL B CG1 1 
ATOM   3295  C CG2 . VAL B  2 100 ? -29.214 -58.452  -16.387 1.00 34.07  ? 100 VAL B CG2 1 
ATOM   3296  N N   . LEU B  2 101 ? -33.400 -57.530  -15.012 1.00 42.96  ? 101 LEU B N   1 
ATOM   3297  C CA  . LEU B  2 101 ? -34.484 -57.179  -14.112 1.00 42.77  ? 101 LEU B CA  1 
ATOM   3298  C C   . LEU B  2 101 ? -35.434 -58.366  -13.999 1.00 41.20  ? 101 LEU B C   1 
ATOM   3299  O O   . LEU B  2 101 ? -35.548 -58.971  -12.936 1.00 49.47  ? 101 LEU B O   1 
ATOM   3300  C CB  . LEU B  2 101 ? -35.212 -55.916  -14.579 1.00 37.47  ? 101 LEU B CB  1 
ATOM   3301  C CG  . LEU B  2 101 ? -34.399 -54.617  -14.523 1.00 41.64  ? 101 LEU B CG  1 
ATOM   3302  C CD1 . LEU B  2 101 ? -35.289 -53.413  -14.783 1.00 47.85  ? 101 LEU B CD1 1 
ATOM   3303  C CD2 . LEU B  2 101 ? -33.691 -54.470  -13.183 1.00 35.62  ? 101 LEU B CD2 1 
ATOM   3304  N N   . LEU B  2 102 ? -36.073 -58.726  -15.109 1.00 43.62  ? 102 LEU B N   1 
ATOM   3305  C CA  . LEU B  2 102 ? -37.041 -59.825  -15.117 1.00 47.95  ? 102 LEU B CA  1 
ATOM   3306  C C   . LEU B  2 102 ? -36.527 -61.101  -14.459 1.00 43.67  ? 102 LEU B C   1 
ATOM   3307  O O   . LEU B  2 102 ? -37.217 -61.698  -13.634 1.00 51.88  ? 102 LEU B O   1 
ATOM   3308  C CB  . LEU B  2 102 ? -37.495 -60.149  -16.539 1.00 47.56  ? 102 LEU B CB  1 
ATOM   3309  C CG  . LEU B  2 102 ? -38.200 -59.032  -17.310 1.00 68.98  ? 102 LEU B CG  1 
ATOM   3310  C CD1 . LEU B  2 102 ? -38.858 -59.590  -18.564 1.00 88.42  ? 102 LEU B CD1 1 
ATOM   3311  C CD2 . LEU B  2 102 ? -39.184 -58.245  -16.446 1.00 58.06  ? 102 LEU B CD2 1 
ATOM   3312  N N   . GLU B  2 103 ? -35.324 -61.524  -14.835 1.00 34.39  ? 103 GLU B N   1 
ATOM   3313  C CA  . GLU B  2 103 ? -34.749 -62.757  -14.301 1.00 49.25  ? 103 GLU B CA  1 
ATOM   3314  C C   . GLU B  2 103 ? -34.459 -62.673  -12.807 1.00 47.16  ? 103 GLU B C   1 
ATOM   3315  O O   . GLU B  2 103 ? -34.637 -63.649  -12.079 1.00 51.76  ? 103 GLU B O   1 
ATOM   3316  C CB  . GLU B  2 103 ? -33.484 -63.149  -15.066 1.00 42.13  ? 103 GLU B CB  1 
ATOM   3317  C CG  . GLU B  2 103 ? -33.766 -63.702  -16.450 1.00 61.37  ? 103 GLU B CG  1 
ATOM   3318  C CD  . GLU B  2 103 ? -34.870 -64.739  -16.437 1.00 82.00  ? 103 GLU B CD  1 
ATOM   3319  O OE1 . GLU B  2 103 ? -34.601 -65.894  -16.048 1.00 79.00  ? 103 GLU B OE1 1 
ATOM   3320  O OE2 . GLU B  2 103 ? -36.011 -64.396  -16.812 1.00 74.64  ? 103 GLU B OE2 1 
ATOM   3321  N N   . ASN B  2 104 ? -34.008 -61.508  -12.355 1.00 35.94  ? 104 ASN B N   1 
ATOM   3322  C CA  . ASN B  2 104 ? -33.760 -61.297  -10.935 1.00 38.14  ? 104 ASN B CA  1 
ATOM   3323  C C   . ASN B  2 104 ? -35.026 -61.471  -10.095 1.00 48.13  ? 104 ASN B C   1 
ATOM   3324  O O   . ASN B  2 104 ? -34.958 -61.976  -8.976  1.00 55.04  ? 104 ASN B O   1 
ATOM   3325  C CB  . ASN B  2 104 ? -33.118 -59.927  -10.688 1.00 28.57  ? 104 ASN B CB  1 
ATOM   3326  C CG  . ASN B  2 104 ? -31.623 -59.923  -10.969 1.00 40.74  ? 104 ASN B CG  1 
ATOM   3327  O OD1 . ASN B  2 104 ? -31.023 -60.970  -11.220 1.00 45.55  ? 104 ASN B OD1 1 
ATOM   3328  N ND2 . ASN B  2 104 ? -31.013 -58.744  -10.920 1.00 48.16  ? 104 ASN B ND2 1 
ATOM   3329  N N   . GLU B  2 105 ? -36.170 -61.058  -10.645 1.00 41.10  ? 105 GLU B N   1 
ATOM   3330  C CA  . GLU B  2 105 ? -37.467 -61.209  -9.975  1.00 45.45  ? 105 GLU B CA  1 
ATOM   3331  C C   . GLU B  2 105 ? -37.914 -62.659  -9.949  1.00 51.83  ? 105 GLU B C   1 
ATOM   3332  O O   . GLU B  2 105 ? -38.650 -63.083  -9.054  1.00 61.24  ? 105 GLU B O   1 
ATOM   3333  C CB  . GLU B  2 105 ? -38.555 -60.396  -10.671 1.00 54.10  ? 105 GLU B CB  1 
ATOM   3334  C CG  . GLU B  2 105 ? -39.917 -60.533  -10.019 1.00 66.57  ? 105 GLU B CG  1 
ATOM   3335  C CD  . GLU B  2 105 ? -39.890 -60.091  -8.574  1.00 99.16  ? 105 GLU B CD  1 
ATOM   3336  O OE1 . GLU B  2 105 ? -39.148 -59.134  -8.268  1.00 91.70  ? 105 GLU B OE1 1 
ATOM   3337  O OE2 . GLU B  2 105 ? -40.601 -60.698  -7.745  1.00 103.28 ? 105 GLU B OE2 1 
ATOM   3338  N N   . ARG B  2 106 ? -37.478 -63.414  -10.947 1.00 45.26  ? 106 ARG B N   1 
ATOM   3339  C CA  . ARG B  2 106 ? -37.806 -64.826  -11.019 1.00 54.40  ? 106 ARG B CA  1 
ATOM   3340  C C   . ARG B  2 106 ? -36.906 -65.628  -10.084 1.00 58.22  ? 106 ARG B C   1 
ATOM   3341  O O   . ARG B  2 106 ? -37.337 -66.615  -9.491  1.00 62.64  ? 106 ARG B O   1 
ATOM   3342  C CB  . ARG B  2 106 ? -37.694 -65.329  -12.459 1.00 55.18  ? 106 ARG B CB  1 
ATOM   3343  C CG  . ARG B  2 106 ? -38.753 -64.753  -13.389 1.00 55.79  ? 106 ARG B CG  1 
ATOM   3344  C CD  . ARG B  2 106 ? -38.882 -65.581  -14.654 1.00 72.79  ? 106 ARG B CD  1 
ATOM   3345  N NE  . ARG B  2 106 ? -39.128 -66.987  -14.347 1.00 77.75  ? 106 ARG B NE  1 
ATOM   3346  C CZ  . ARG B  2 106 ? -40.308 -67.475  -13.981 1.00 87.40  ? 106 ARG B CZ  1 
ATOM   3347  N NH1 . ARG B  2 106 ? -41.357 -66.670  -13.872 1.00 82.45  ? 106 ARG B NH1 1 
ATOM   3348  N NH2 . ARG B  2 106 ? -40.441 -68.768  -13.719 1.00 83.52  ? 106 ARG B NH2 1 
ATOM   3349  N N   . THR B  2 107 ? -35.661 -65.183  -9.939  1.00 49.55  ? 107 THR B N   1 
ATOM   3350  C CA  . THR B  2 107 ? -34.681 -65.893  -9.119  1.00 50.66  ? 107 THR B CA  1 
ATOM   3351  C C   . THR B  2 107 ? -35.024 -65.859  -7.627  1.00 54.80  ? 107 THR B C   1 
ATOM   3352  O O   . THR B  2 107 ? -34.996 -66.889  -6.955  1.00 57.37  ? 107 THR B O   1 
ATOM   3353  C CB  . THR B  2 107 ? -33.253 -65.354  -9.348  1.00 56.37  ? 107 THR B CB  1 
ATOM   3354  O OG1 . THR B  2 107 ? -32.887 -65.537  -10.721 1.00 58.37  ? 107 THR B OG1 1 
ATOM   3355  C CG2 . THR B  2 107 ? -32.257 -66.090  -8.464  1.00 48.82  ? 107 THR B CG2 1 
ATOM   3356  N N   . LEU B  2 108 ? -35.338 -64.671  -7.118  1.00 50.02  ? 108 LEU B N   1 
ATOM   3357  C CA  . LEU B  2 108 ? -35.807 -64.497  -5.743  1.00 46.60  ? 108 LEU B CA  1 
ATOM   3358  C C   . LEU B  2 108 ? -37.123 -65.233  -5.494  1.00 53.16  ? 108 LEU B C   1 
ATOM   3359  O O   . LEU B  2 108 ? -37.307 -65.839  -4.440  1.00 57.51  ? 108 LEU B O   1 
ATOM   3360  C CB  . LEU B  2 108 ? -35.981 -63.010  -5.410  1.00 44.34  ? 108 LEU B CB  1 
ATOM   3361  C CG  . LEU B  2 108 ? -34.759 -62.115  -5.622  1.00 45.49  ? 108 LEU B CG  1 
ATOM   3362  C CD1 . LEU B  2 108 ? -35.039 -60.680  -5.190  1.00 46.81  ? 108 LEU B CD1 1 
ATOM   3363  C CD2 . LEU B  2 108 ? -33.571 -62.681  -4.869  1.00 47.63  ? 108 LEU B CD2 1 
ATOM   3364  N N   . ASP B  2 109 ? -38.043 -65.170  -6.453  1.00 49.02  ? 109 ASP B N   1 
ATOM   3365  C CA  . ASP B  2 109 ? -39.305 -65.895  -6.330  1.00 51.80  ? 109 ASP B CA  1 
ATOM   3366  C C   . ASP B  2 109 ? -39.051 -67.398  -6.319  1.00 54.48  ? 109 ASP B C   1 
ATOM   3367  O O   . ASP B  2 109 ? -39.770 -68.156  -5.668  1.00 55.29  ? 109 ASP B O   1 
ATOM   3368  C CB  . ASP B  2 109 ? -40.270 -65.526  -7.461  1.00 59.95  ? 109 ASP B CB  1 
ATOM   3369  C CG  . ASP B  2 109 ? -40.906 -64.163  -7.264  1.00 80.50  ? 109 ASP B CG  1 
ATOM   3370  O OD1 . ASP B  2 109 ? -40.776 -63.598  -6.158  1.00 80.74  ? 109 ASP B OD1 1 
ATOM   3371  O OD2 . ASP B  2 109 ? -41.541 -63.660  -8.214  1.00 77.63  ? 109 ASP B OD2 1 
ATOM   3372  N N   . TYR B  2 110 ? -38.019 -67.820  -7.042  1.00 50.80  ? 110 TYR B N   1 
ATOM   3373  C CA  . TYR B  2 110 ? -37.628 -69.224  -7.078  1.00 45.37  ? 110 TYR B CA  1 
ATOM   3374  C C   . TYR B  2 110 ? -37.133 -69.686  -5.712  1.00 65.76  ? 110 TYR B C   1 
ATOM   3375  O O   . TYR B  2 110 ? -37.534 -70.742  -5.221  1.00 54.66  ? 110 TYR B O   1 
ATOM   3376  C CB  . TYR B  2 110 ? -36.546 -69.450  -8.136  1.00 42.90  ? 110 TYR B CB  1 
ATOM   3377  C CG  . TYR B  2 110 ? -35.916 -70.823  -8.087  1.00 48.79  ? 110 TYR B CG  1 
ATOM   3378  C CD1 . TYR B  2 110 ? -36.504 -71.904  -8.730  1.00 42.70  ? 110 TYR B CD1 1 
ATOM   3379  C CD2 . TYR B  2 110 ? -34.728 -71.037  -7.400  1.00 47.06  ? 110 TYR B CD2 1 
ATOM   3380  C CE1 . TYR B  2 110 ? -35.929 -73.160  -8.688  1.00 38.52  ? 110 TYR B CE1 1 
ATOM   3381  C CE2 . TYR B  2 110 ? -34.147 -72.288  -7.352  1.00 59.83  ? 110 TYR B CE2 1 
ATOM   3382  C CZ  . TYR B  2 110 ? -34.750 -73.346  -7.997  1.00 57.28  ? 110 TYR B CZ  1 
ATOM   3383  O OH  . TYR B  2 110 ? -34.170 -74.593  -7.949  1.00 64.72  ? 110 TYR B OH  1 
ATOM   3384  N N   . HIS B  2 111 ? -36.259 -68.891  -5.103  1.00 57.76  ? 111 HIS B N   1 
ATOM   3385  C CA  . HIS B  2 111 ? -35.750 -69.198  -3.772  1.00 53.90  ? 111 HIS B CA  1 
ATOM   3386  C C   . HIS B  2 111 ? -36.866 -69.136  -2.737  1.00 63.40  ? 111 HIS B C   1 
ATOM   3387  O O   . HIS B  2 111 ? -36.993 -70.022  -1.892  1.00 58.12  ? 111 HIS B O   1 
ATOM   3388  C CB  . HIS B  2 111 ? -34.621 -68.239  -3.388  1.00 43.94  ? 111 HIS B CB  1 
ATOM   3389  C CG  . HIS B  2 111 ? -33.355 -68.466  -4.131  1.00 50.09  ? 111 HIS B CG  1 
ATOM   3390  N ND1 . HIS B  2 111 ? -32.589 -69.621  -3.984  1.00 58.04  ? 111 HIS B ND1 1 
ATOM   3391  C CD2 . HIS B  2 111 ? -32.676 -67.707  -5.026  1.00 56.02  ? 111 HIS B CD2 1 
ATOM   3392  C CE1 . HIS B  2 111 ? -31.533 -69.551  -4.749  1.00 61.51  ? 111 HIS B CE1 1 
ATOM   3393  N NE2 . HIS B  2 111 ? -31.554 -68.393  -5.401  1.00 57.75  ? 111 HIS B NE2 1 
ATOM   3394  N N   . ASP B  2 112 ? -37.671 -68.082  -2.811  1.00 51.98  ? 112 ASP B N   1 
ATOM   3395  C CA  . ASP B  2 112 ? -38.812 -67.918  -1.921  1.00 47.99  ? 112 ASP B CA  1 
ATOM   3396  C C   . ASP B  2 112 ? -39.694 -69.160  -1.973  1.00 54.48  ? 112 ASP B C   1 
ATOM   3397  O O   . ASP B  2 112 ? -40.195 -69.628  -0.950  1.00 62.21  ? 112 ASP B O   1 
ATOM   3398  C CB  . ASP B  2 112 ? -39.622 -66.685  -2.327  1.00 67.46  ? 112 ASP B CB  1 
ATOM   3399  C CG  . ASP B  2 112 ? -40.696 -66.334  -1.319  1.00 64.56  ? 112 ASP B CG  1 
ATOM   3400  O OD1 . ASP B  2 112 ? -41.637 -65.601  -1.683  1.00 66.87  ? 112 ASP B OD1 1 
ATOM   3401  O OD2 . ASP B  2 112 ? -40.598 -66.790  -0.162  1.00 77.66  ? 112 ASP B OD2 1 
ATOM   3402  N N   . SER B  2 113 ? -39.872 -69.691  -3.178  1.00 61.66  ? 113 SER B N   1 
ATOM   3403  C CA  . SER B  2 113 ? -40.693 -70.875  -3.395  1.00 57.44  ? 113 SER B CA  1 
ATOM   3404  C C   . SER B  2 113 ? -40.143 -72.100  -2.671  1.00 63.22  ? 113 SER B C   1 
ATOM   3405  O O   . SER B  2 113 ? -40.878 -72.805  -1.980  1.00 66.12  ? 113 SER B O   1 
ATOM   3406  C CB  . SER B  2 113 ? -40.810 -71.167  -4.891  1.00 48.94  ? 113 SER B CB  1 
ATOM   3407  O OG  . SER B  2 113 ? -41.411 -72.429  -5.119  1.00 68.64  ? 113 SER B OG  1 
ATOM   3408  N N   . ASN B  2 114 ? -38.849 -72.352  -2.837  1.00 53.42  ? 114 ASN B N   1 
ATOM   3409  C CA  . ASN B  2 114 ? -38.213 -73.515  -2.227  1.00 64.73  ? 114 ASN B CA  1 
ATOM   3410  C C   . ASN B  2 114 ? -38.349 -73.528  -0.708  1.00 68.55  ? 114 ASN B C   1 
ATOM   3411  O O   . ASN B  2 114 ? -38.527 -74.585  -0.103  1.00 70.52  ? 114 ASN B O   1 
ATOM   3412  C CB  . ASN B  2 114 ? -36.741 -73.599  -2.636  1.00 62.16  ? 114 ASN B CB  1 
ATOM   3413  C CG  . ASN B  2 114 ? -36.566 -73.824  -4.124  1.00 70.92  ? 114 ASN B CG  1 
ATOM   3414  O OD1 . ASN B  2 114 ? -37.480 -74.290  -4.805  1.00 74.07  ? 114 ASN B OD1 1 
ATOM   3415  N ND2 . ASN B  2 114 ? -35.386 -73.496  -4.638  1.00 70.87  ? 114 ASN B ND2 1 
ATOM   3416  N N   . VAL B  2 115 ? -38.265 -72.351  -0.097  1.00 65.88  ? 115 VAL B N   1 
ATOM   3417  C CA  . VAL B  2 115 ? -38.463 -72.222  1.341   1.00 61.39  ? 115 VAL B CA  1 
ATOM   3418  C C   . VAL B  2 115 ? -39.887 -72.619  1.712   1.00 59.59  ? 115 VAL B C   1 
ATOM   3419  O O   . VAL B  2 115 ? -40.102 -73.497  2.548   1.00 65.72  ? 115 VAL B O   1 
ATOM   3420  C CB  . VAL B  2 115 ? -38.195 -70.785  1.824   1.00 61.48  ? 115 VAL B CB  1 
ATOM   3421  C CG1 . VAL B  2 115 ? -38.600 -70.630  3.282   1.00 68.84  ? 115 VAL B CG1 1 
ATOM   3422  C CG2 . VAL B  2 115 ? -36.731 -70.423  1.627   1.00 50.95  ? 115 VAL B CG2 1 
ATOM   3423  N N   . LYS B  2 116 ? -40.855 -71.961  1.081   1.00 55.75  ? 116 LYS B N   1 
ATOM   3424  C CA  . LYS B  2 116 ? -42.268 -72.268  1.279   1.00 61.76  ? 116 LYS B CA  1 
ATOM   3425  C C   . LYS B  2 116 ? -42.529 -73.764  1.151   1.00 67.10  ? 116 LYS B C   1 
ATOM   3426  O O   . LYS B  2 116 ? -43.263 -74.348  1.948   1.00 67.90  ? 116 LYS B O   1 
ATOM   3427  C CB  . LYS B  2 116 ? -43.113 -71.506  0.257   1.00 64.19  ? 116 LYS B CB  1 
ATOM   3428  C CG  . LYS B  2 116 ? -44.564 -71.958  0.163   1.00 55.85  ? 116 LYS B CG  1 
ATOM   3429  C CD  . LYS B  2 116 ? -45.476 -71.132  1.057   1.00 77.92  ? 116 LYS B CD  1 
ATOM   3430  C CE  . LYS B  2 116 ? -46.940 -71.413  0.750   1.00 90.20  ? 116 LYS B CE  1 
ATOM   3431  N NZ  . LYS B  2 116 ? -47.857 -70.480  1.462   1.00 110.61 ? 116 LYS B NZ  1 
ATOM   3432  N N   . ASN B  2 117 ? -41.922 -74.378  0.141   1.00 59.49  ? 117 ASN B N   1 
ATOM   3433  C CA  . ASN B  2 117 ? -42.088 -75.806  -0.102  1.00 72.08  ? 117 ASN B CA  1 
ATOM   3434  C C   . ASN B  2 117 ? -41.487 -76.664  1.004   1.00 73.77  ? 117 ASN B C   1 
ATOM   3435  O O   . ASN B  2 117 ? -42.061 -77.680  1.394   1.00 76.99  ? 117 ASN B O   1 
ATOM   3436  C CB  . ASN B  2 117 ? -41.488 -76.193  -1.453  1.00 64.31  ? 117 ASN B CB  1 
ATOM   3437  C CG  . ASN B  2 117 ? -42.374 -75.800  -2.614  1.00 58.14  ? 117 ASN B CG  1 
ATOM   3438  O OD1 . ASN B  2 117 ? -43.547 -75.477  -2.430  1.00 48.00  ? 117 ASN B OD1 1 
ATOM   3439  N ND2 . ASN B  2 117 ? -41.821 -75.832  -3.821  1.00 78.73  ? 117 ASN B ND2 1 
ATOM   3440  N N   . LEU B  2 118 ? -40.327 -76.252  1.501   1.00 72.10  ? 118 LEU B N   1 
ATOM   3441  C CA  . LEU B  2 118 ? -39.671 -76.967  2.585   1.00 64.58  ? 118 LEU B CA  1 
ATOM   3442  C C   . LEU B  2 118 ? -40.542 -76.904  3.833   1.00 64.94  ? 118 LEU B C   1 
ATOM   3443  O O   . LEU B  2 118 ? -40.724 -77.902  4.530   1.00 74.13  ? 118 LEU B O   1 
ATOM   3444  C CB  . LEU B  2 118 ? -38.294 -76.366  2.864   1.00 72.09  ? 118 LEU B CB  1 
ATOM   3445  C CG  . LEU B  2 118 ? -37.223 -77.352  3.329   1.00 80.94  ? 118 LEU B CG  1 
ATOM   3446  C CD1 . LEU B  2 118 ? -37.160 -78.536  2.378   1.00 78.64  ? 118 LEU B CD1 1 
ATOM   3447  C CD2 . LEU B  2 118 ? -35.870 -76.667  3.431   1.00 83.05  ? 118 LEU B CD2 1 
ATOM   3448  N N   . TYR B  2 119 ? -41.083 -75.720  4.102   1.00 64.99  ? 119 TYR B N   1 
ATOM   3449  C CA  . TYR B  2 119 ? -41.989 -75.522  5.225   1.00 70.95  ? 119 TYR B CA  1 
ATOM   3450  C C   . TYR B  2 119 ? -43.223 -76.408  5.093   1.00 74.11  ? 119 TYR B C   1 
ATOM   3451  O O   . TYR B  2 119 ? -43.595 -77.113  6.030   1.00 87.59  ? 119 TYR B O   1 
ATOM   3452  C CB  . TYR B  2 119 ? -42.408 -74.053  5.317   1.00 72.14  ? 119 TYR B CB  1 
ATOM   3453  C CG  . TYR B  2 119 ? -43.417 -73.766  6.407   1.00 82.23  ? 119 TYR B CG  1 
ATOM   3454  C CD1 . TYR B  2 119 ? -43.005 -73.420  7.687   1.00 87.41  ? 119 TYR B CD1 1 
ATOM   3455  C CD2 . TYR B  2 119 ? -44.781 -73.840  6.156   1.00 82.39  ? 119 TYR B CD2 1 
ATOM   3456  C CE1 . TYR B  2 119 ? -43.923 -73.157  8.686   1.00 95.29  ? 119 TYR B CE1 1 
ATOM   3457  C CE2 . TYR B  2 119 ? -45.705 -73.578  7.148   1.00 97.07  ? 119 TYR B CE2 1 
ATOM   3458  C CZ  . TYR B  2 119 ? -45.271 -73.237  8.411   1.00 101.17 ? 119 TYR B CZ  1 
ATOM   3459  O OH  . TYR B  2 119 ? -46.190 -72.977  9.401   1.00 101.17 ? 119 TYR B OH  1 
ATOM   3460  N N   . GLU B  2 120 ? -43.851 -76.368  3.922   1.00 85.02  ? 120 GLU B N   1 
ATOM   3461  C CA  . GLU B  2 120 ? -45.054 -77.154  3.666   1.00 87.28  ? 120 GLU B CA  1 
ATOM   3462  C C   . GLU B  2 120 ? -44.805 -78.655  3.786   1.00 74.10  ? 120 GLU B C   1 
ATOM   3463  O O   . GLU B  2 120 ? -45.623 -79.383  4.347   1.00 95.47  ? 120 GLU B O   1 
ATOM   3464  C CB  . GLU B  2 120 ? -45.632 -76.824  2.287   1.00 93.18  ? 120 GLU B CB  1 
ATOM   3465  C CG  . GLU B  2 120 ? -46.524 -75.593  2.266   1.00 99.84  ? 120 GLU B CG  1 
ATOM   3466  C CD  . GLU B  2 120 ? -47.832 -75.807  3.007   1.00 124.77 ? 120 GLU B CD  1 
ATOM   3467  O OE1 . GLU B  2 120 ? -48.242 -76.974  3.170   1.00 118.60 ? 120 GLU B OE1 1 
ATOM   3468  O OE2 . GLU B  2 120 ? -48.452 -74.806  3.424   1.00 133.93 ? 120 GLU B OE2 1 
ATOM   3469  N N   . LYS B  2 121 ? -43.676 -79.115  3.256   1.00 72.17  ? 121 LYS B N   1 
ATOM   3470  C CA  . LYS B  2 121 ? -43.347 -80.537  3.289   1.00 92.14  ? 121 LYS B CA  1 
ATOM   3471  C C   . LYS B  2 121 ? -43.247 -81.055  4.721   1.00 96.05  ? 121 LYS B C   1 
ATOM   3472  O O   . LYS B  2 121 ? -43.605 -82.198  5.004   1.00 99.92  ? 121 LYS B O   1 
ATOM   3473  C CB  . LYS B  2 121 ? -42.046 -80.813  2.533   1.00 87.28  ? 121 LYS B CB  1 
ATOM   3474  C CG  . LYS B  2 121 ? -41.723 -82.291  2.396   1.00 107.16 ? 121 LYS B CG  1 
ATOM   3475  C CD  . LYS B  2 121 ? -40.438 -82.518  1.618   1.00 117.99 ? 121 LYS B CD  1 
ATOM   3476  C CE  . LYS B  2 121 ? -40.142 -84.002  1.477   1.00 123.55 ? 121 LYS B CE  1 
ATOM   3477  N NZ  . LYS B  2 121 ? -38.870 -84.253  0.747   1.00 130.24 ? 121 LYS B NZ  1 
ATOM   3478  N N   . VAL B  2 122 ? -42.755 -80.208  5.620   1.00 97.47  ? 122 VAL B N   1 
ATOM   3479  C CA  . VAL B  2 122 ? -42.669 -80.556  7.033   1.00 93.51  ? 122 VAL B CA  1 
ATOM   3480  C C   . VAL B  2 122 ? -44.046 -80.500  7.679   1.00 96.76  ? 122 VAL B C   1 
ATOM   3481  O O   . VAL B  2 122 ? -44.422 -81.385  8.448   1.00 117.83 ? 122 VAL B O   1 
ATOM   3482  C CB  . VAL B  2 122 ? -41.730 -79.599  7.794   1.00 83.66  ? 122 VAL B CB  1 
ATOM   3483  C CG1 . VAL B  2 122 ? -41.983 -79.680  9.293   1.00 97.46  ? 122 VAL B CG1 1 
ATOM   3484  C CG2 . VAL B  2 122 ? -40.276 -79.906  7.467   1.00 80.48  ? 122 VAL B CG2 1 
ATOM   3485  N N   . ARG B  2 123 ? -44.797 -79.455  7.350   1.00 82.44  ? 123 ARG B N   1 
ATOM   3486  C CA  . ARG B  2 123 ? -46.103 -79.223  7.953   1.00 95.07  ? 123 ARG B CA  1 
ATOM   3487  C C   . ARG B  2 123 ? -47.128 -80.293  7.582   1.00 95.25  ? 123 ARG B C   1 
ATOM   3488  O O   . ARG B  2 123 ? -47.879 -80.756  8.435   1.00 109.57 ? 123 ARG B O   1 
ATOM   3489  C CB  . ARG B  2 123 ? -46.636 -77.842  7.573   1.00 99.25  ? 123 ARG B CB  1 
ATOM   3490  C CG  . ARG B  2 123 ? -47.847 -77.426  8.382   1.00 100.32 ? 123 ARG B CG  1 
ATOM   3491  C CD  . ARG B  2 123 ? -48.782 -76.546  7.577   1.00 111.25 ? 123 ARG B CD  1 
ATOM   3492  N NE  . ARG B  2 123 ? -49.408 -77.264  6.472   1.00 124.66 ? 123 ARG B NE  1 
ATOM   3493  C CZ  . ARG B  2 123 ? -50.545 -76.891  5.895   1.00 138.36 ? 123 ARG B CZ  1 
ATOM   3494  N NH1 . ARG B  2 123 ? -51.184 -75.813  6.328   1.00 128.97 ? 123 ARG B NH1 1 
ATOM   3495  N NH2 . ARG B  2 123 ? -51.050 -77.594  4.891   1.00 142.79 ? 123 ARG B NH2 1 
ATOM   3496  N N   . SER B  2 124 ? -47.172 -80.680  6.311   1.00 106.62 ? 124 SER B N   1 
ATOM   3497  C CA  . SER B  2 124 ? -48.112 -81.710  5.876   1.00 120.50 ? 124 SER B CA  1 
ATOM   3498  C C   . SER B  2 124 ? -47.596 -83.091  6.240   1.00 124.22 ? 124 SER B C   1 
ATOM   3499  O O   . SER B  2 124 ? -48.020 -84.101  5.673   1.00 128.72 ? 124 SER B O   1 
ATOM   3500  C CB  . SER B  2 124 ? -48.361 -81.627  4.371   1.00 123.26 ? 124 SER B CB  1 
ATOM   3501  O OG  . SER B  2 124 ? -47.165 -81.837  3.642   1.00 124.35 ? 124 SER B OG  1 
ATOM   3502  N N   . GLN B  2 125 ? -46.677 -83.127  7.194   1.00 114.75 ? 125 GLN B N   1 
ATOM   3503  C CA  . GLN B  2 125 ? -46.064 -84.374  7.609   1.00 112.31 ? 125 GLN B CA  1 
ATOM   3504  C C   . GLN B  2 125 ? -46.192 -84.514  9.128   1.00 124.88 ? 125 GLN B C   1 
ATOM   3505  O O   . GLN B  2 125 ? -46.591 -85.567  9.637   1.00 124.73 ? 125 GLN B O   1 
ATOM   3506  C CB  . GLN B  2 125 ? -44.610 -84.414  7.158   1.00 95.06  ? 125 GLN B CB  1 
ATOM   3507  C CG  . GLN B  2 125 ? -43.940 -85.745  7.357   1.00 103.57 ? 125 GLN B CG  1 
ATOM   3508  C CD  . GLN B  2 125 ? -42.510 -85.735  6.879   1.00 124.59 ? 125 GLN B CD  1 
ATOM   3509  O OE1 . GLN B  2 125 ? -41.835 -84.707  6.926   1.00 119.77 ? 125 GLN B OE1 1 
ATOM   3510  N NE2 . GLN B  2 125 ? -42.036 -86.882  6.412   1.00 133.28 ? 125 GLN B NE2 1 
ATOM   3511  N N   . LEU B  2 126 ? -45.872 -83.448  9.857   1.00 121.33 ? 126 LEU B N   1 
ATOM   3512  C CA  . LEU B  2 126 ? -46.378 -83.319  11.214  1.00 108.54 ? 126 LEU B CA  1 
ATOM   3513  C C   . LEU B  2 126 ? -47.707 -82.620  11.079  1.00 119.68 ? 126 LEU B C   1 
ATOM   3514  O O   . LEU B  2 126 ? -47.769 -81.492  10.598  1.00 127.63 ? 126 LEU B O   1 
ATOM   3515  C CB  . LEU B  2 126 ? -45.466 -82.449  12.080  1.00 111.07 ? 126 LEU B CB  1 
ATOM   3516  C CG  . LEU B  2 126 ? -43.979 -82.229  11.729  1.00 108.17 ? 126 LEU B CG  1 
ATOM   3517  C CD1 . LEU B  2 126 ? -43.462 -81.006  12.458  1.00 110.04 ? 126 LEU B CD1 1 
ATOM   3518  C CD2 . LEU B  2 126 ? -43.073 -83.439  11.982  1.00 103.65 ? 126 LEU B CD2 1 
ATOM   3519  N N   . LYS B  2 127 ? -48.770 -83.286  11.498  1.00 117.39 ? 127 LYS B N   1 
ATOM   3520  C CA  . LYS B  2 127 ? -50.083 -82.668  11.475  1.00 119.03 ? 127 LYS B CA  1 
ATOM   3521  C C   . LYS B  2 127 ? -50.535 -82.312  12.895  1.00 140.27 ? 127 LYS B C   1 
ATOM   3522  O O   . LYS B  2 127 ? -50.333 -81.190  13.363  1.00 133.92 ? 127 LYS B O   1 
ATOM   3523  C CB  . LYS B  2 127 ? -51.094 -83.579  10.789  1.00 116.56 ? 127 LYS B CB  1 
ATOM   3524  C CG  . LYS B  2 127 ? -50.594 -84.035  9.414   1.00 117.77 ? 127 LYS B CG  1 
ATOM   3525  C CD  . LYS B  2 127 ? -50.663 -85.550  9.251   1.00 113.26 ? 127 LYS B CD  1 
ATOM   3526  C CE  . LYS B  2 127 ? -50.093 -85.973  7.898   1.00 128.15 ? 127 LYS B CE  1 
ATOM   3527  N NZ  . LYS B  2 127 ? -50.191 -87.442  7.646   1.00 127.82 ? 127 LYS B NZ  1 
ATOM   3528  N N   . ASN B  2 128 ? -51.121 -83.279  13.590  1.00 161.05 ? 128 ASN B N   1 
ATOM   3529  C CA  . ASN B  2 128 ? -51.515 -83.089  14.979  1.00 162.16 ? 128 ASN B CA  1 
ATOM   3530  C C   . ASN B  2 128 ? -50.330 -83.164  15.934  1.00 162.98 ? 128 ASN B C   1 
ATOM   3531  O O   . ASN B  2 128 ? -50.351 -82.545  16.993  1.00 165.40 ? 128 ASN B O   1 
ATOM   3532  C CB  . ASN B  2 128 ? -52.583 -84.108  15.362  1.00 159.79 ? 128 ASN B CB  1 
ATOM   3533  C CG  . ASN B  2 128 ? -53.898 -83.856  14.650  1.00 169.44 ? 128 ASN B CG  1 
ATOM   3534  O OD1 . ASN B  2 128 ? -54.366 -82.718  14.569  1.00 170.75 ? 128 ASN B OD1 1 
ATOM   3535  N ND2 . ASN B  2 128 ? -54.507 -84.918  14.138  1.00 177.05 ? 128 ASN B ND2 1 
ATOM   3536  N N   . ASN B  2 129 ? -49.295 -83.907  15.552  1.00 182.03 ? 129 ASN B N   1 
ATOM   3537  C CA  . ASN B  2 129 ? -48.161 -84.163  16.438  1.00 190.98 ? 129 ASN B CA  1 
ATOM   3538  C C   . ASN B  2 129 ? -47.344 -82.919  16.784  1.00 188.37 ? 129 ASN B C   1 
ATOM   3539  O O   . ASN B  2 129 ? -46.361 -83.003  17.519  1.00 176.41 ? 129 ASN B O   1 
ATOM   3540  C CB  . ASN B  2 129 ? -47.256 -85.244  15.843  1.00 179.01 ? 129 ASN B CB  1 
ATOM   3541  C CG  . ASN B  2 129 ? -47.966 -86.576  15.685  1.00 171.62 ? 129 ASN B CG  1 
ATOM   3542  O OD1 . ASN B  2 129 ? -47.353 -87.578  15.320  1.00 165.53 ? 129 ASN B OD1 1 
ATOM   3543  N ND2 . ASN B  2 129 ? -49.265 -86.594  15.966  1.00 178.24 ? 129 ASN B ND2 1 
ATOM   3544  N N   . ALA B  2 130 ? -47.754 -81.770  16.255  1.00 161.03 ? 130 ALA B N   1 
ATOM   3545  C CA  . ALA B  2 130 ? -47.073 -80.509  16.533  1.00 146.70 ? 130 ALA B CA  1 
ATOM   3546  C C   . ALA B  2 130 ? -47.937 -79.329  16.100  1.00 130.58 ? 130 ALA B C   1 
ATOM   3547  O O   . ALA B  2 130 ? -48.942 -79.509  15.413  1.00 132.46 ? 130 ALA B O   1 
ATOM   3548  C CB  . ALA B  2 130 ? -45.723 -80.467  15.835  1.00 140.20 ? 130 ALA B CB  1 
ATOM   3549  N N   . LYS B  2 131 ? -47.544 -78.124  16.500  1.00 142.53 ? 131 LYS B N   1 
ATOM   3550  C CA  . LYS B  2 131 ? -48.304 -76.928  16.151  1.00 157.68 ? 131 LYS B CA  1 
ATOM   3551  C C   . LYS B  2 131 ? -47.426 -75.862  15.503  1.00 165.49 ? 131 LYS B C   1 
ATOM   3552  O O   . LYS B  2 131 ? -46.236 -75.756  15.800  1.00 150.71 ? 131 LYS B O   1 
ATOM   3553  C CB  . LYS B  2 131 ? -48.994 -76.344  17.387  1.00 150.97 ? 131 LYS B CB  1 
ATOM   3554  C CG  . LYS B  2 131 ? -48.045 -75.677  18.371  1.00 157.07 ? 131 LYS B CG  1 
ATOM   3555  C CD  . LYS B  2 131 ? -48.799 -74.783  19.341  1.00 157.47 ? 131 LYS B CD  1 
ATOM   3556  C CE  . LYS B  2 131 ? -47.845 -73.990  20.220  1.00 152.69 ? 131 LYS B CE  1 
ATOM   3557  N NZ  . LYS B  2 131 ? -48.563 -73.000  21.070  1.00 145.51 ? 131 LYS B NZ  1 
ATOM   3558  N N   . GLU B  2 132 ? -48.025 -75.073  14.616  1.00 165.58 ? 132 GLU B N   1 
ATOM   3559  C CA  . GLU B  2 132 ? -47.327 -73.961  13.987  1.00 150.60 ? 132 GLU B CA  1 
ATOM   3560  C C   . GLU B  2 132 ? -47.210 -72.797  14.960  1.00 149.26 ? 132 GLU B C   1 
ATOM   3561  O O   . GLU B  2 132 ? -48.150 -72.496  15.695  1.00 158.59 ? 132 GLU B O   1 
ATOM   3562  C CB  . GLU B  2 132 ? -48.075 -73.494  12.739  1.00 156.03 ? 132 GLU B CB  1 
ATOM   3563  C CG  . GLU B  2 132 ? -48.277 -74.556  11.677  1.00 153.48 ? 132 GLU B CG  1 
ATOM   3564  C CD  . GLU B  2 132 ? -49.105 -74.046  10.516  1.00 161.89 ? 132 GLU B CD  1 
ATOM   3565  O OE1 . GLU B  2 132 ? -49.558 -74.870  9.697   1.00 159.67 ? 132 GLU B OE1 1 
ATOM   3566  O OE2 . GLU B  2 132 ? -49.311 -72.817  10.427  1.00 165.93 ? 132 GLU B OE2 1 
ATOM   3567  N N   . ILE B  2 133 ? -46.055 -72.141  14.960  1.00 136.61 ? 133 ILE B N   1 
ATOM   3568  C CA  . ILE B  2 133 ? -45.861 -70.942  15.764  1.00 150.85 ? 133 ILE B CA  1 
ATOM   3569  C C   . ILE B  2 133 ? -46.239 -69.711  14.949  1.00 153.36 ? 133 ILE B C   1 
ATOM   3570  O O   . ILE B  2 133 ? -46.767 -68.735  15.482  1.00 158.67 ? 133 ILE B O   1 
ATOM   3571  C CB  . ILE B  2 133 ? -44.403 -70.807  16.241  1.00 149.31 ? 133 ILE B CB  1 
ATOM   3572  C CG1 . ILE B  2 133 ? -44.016 -71.993  17.126  1.00 145.89 ? 133 ILE B CG1 1 
ATOM   3573  C CG2 . ILE B  2 133 ? -44.211 -69.506  17.002  1.00 142.93 ? 133 ILE B CG2 1 
ATOM   3574  C CD1 . ILE B  2 133 ? -44.732 -72.019  18.459  1.00 154.36 ? 133 ILE B CD1 1 
ATOM   3575  N N   . GLY B  2 134 ? -45.972 -69.770  13.648  1.00 140.88 ? 134 GLY B N   1 
ATOM   3576  C CA  . GLY B  2 134 ? -46.258 -68.662  12.757  1.00 133.80 ? 134 GLY B CA  1 
ATOM   3577  C C   . GLY B  2 134 ? -44.983 -68.044  12.219  1.00 121.46 ? 134 GLY B C   1 
ATOM   3578  O O   . GLY B  2 134 ? -45.001 -67.331  11.216  1.00 110.97 ? 134 GLY B O   1 
ATOM   3579  N N   . ASN B  2 135 ? -43.870 -68.322  12.891  1.00 112.46 ? 135 ASN B N   1 
ATOM   3580  C CA  . ASN B  2 135 ? -42.574 -67.784  12.492  1.00 100.54 ? 135 ASN B CA  1 
ATOM   3581  C C   . ASN B  2 135 ? -41.780 -68.801  11.679  1.00 96.57  ? 135 ASN B C   1 
ATOM   3582  O O   . ASN B  2 135 ? -40.548 -68.821  11.699  1.00 71.87  ? 135 ASN B O   1 
ATOM   3583  C CB  . ASN B  2 135 ? -41.776 -67.352  13.721  1.00 108.56 ? 135 ASN B CB  1 
ATOM   3584  C CG  . ASN B  2 135 ? -40.597 -66.469  13.367  1.00 122.88 ? 135 ASN B CG  1 
ATOM   3585  O OD1 . ASN B  2 135 ? -40.440 -66.055  12.218  1.00 111.57 ? 135 ASN B OD1 1 
ATOM   3586  N ND2 . ASN B  2 135 ? -39.764 -66.171  14.357  1.00 140.15 ? 135 ASN B ND2 1 
ATOM   3587  N N   . GLY B  2 136 ? -42.502 -69.649  10.958  1.00 94.86  ? 136 GLY B N   1 
ATOM   3588  C CA  . GLY B  2 136 ? -41.879 -70.718  10.197  1.00 90.77  ? 136 GLY B CA  1 
ATOM   3589  C C   . GLY B  2 136 ? -41.309 -71.801  11.111  1.00 108.56 ? 136 GLY B C   1 
ATOM   3590  O O   . GLY B  2 136 ? -40.467 -72.618  10.700  1.00 104.09 ? 136 GLY B O   1 
ATOM   3591  N N   . CYS B  2 137 ? -41.781 -71.810  12.357  1.00 134.68 ? 137 CYS B N   1 
ATOM   3592  C CA  . CYS B  2 137 ? -41.314 -72.752  13.363  1.00 124.13 ? 137 CYS B CA  1 
ATOM   3593  C C   . CYS B  2 137 ? -42.445 -73.608  13.922  1.00 126.67 ? 137 CYS B C   1 
ATOM   3594  O O   . CYS B  2 137 ? -43.555 -73.125  14.106  1.00 127.45 ? 137 CYS B O   1 
ATOM   3595  C CB  . CYS B  2 137 ? -40.615 -71.970  14.479  1.00 114.40 ? 137 CYS B CB  1 
ATOM   3596  S SG  . CYS B  2 137 ? -39.727 -72.950  15.664  1.00 143.50 ? 137 CYS B SG  1 
ATOM   3597  N N   . PHE B  2 138 ? -42.141 -74.866  14.230  1.00 118.31 ? 138 PHE B N   1 
ATOM   3598  C CA  . PHE B  2 138 ? -43.127 -75.779  14.795  1.00 133.24 ? 138 PHE B CA  1 
ATOM   3599  C C   . PHE B  2 138 ? -42.773 -76.136  16.235  1.00 143.84 ? 138 PHE B C   1 
ATOM   3600  O O   . PHE B  2 138 ? -41.607 -76.073  16.626  1.00 137.40 ? 138 PHE B O   1 
ATOM   3601  C CB  . PHE B  2 138 ? -43.211 -77.065  13.968  1.00 127.71 ? 138 PHE B CB  1 
ATOM   3602  C CG  . PHE B  2 138 ? -43.641 -76.851  12.543  1.00 121.02 ? 138 PHE B CG  1 
ATOM   3603  C CD1 . PHE B  2 138 ? -42.721 -76.503  11.567  1.00 109.39 ? 138 PHE B CD1 1 
ATOM   3604  C CD2 . PHE B  2 138 ? -44.967 -77.010  12.179  1.00 119.77 ? 138 PHE B CD2 1 
ATOM   3605  C CE1 . PHE B  2 138 ? -43.120 -76.310  10.254  1.00 111.16 ? 138 PHE B CE1 1 
ATOM   3606  C CE2 . PHE B  2 138 ? -45.371 -76.820  10.872  1.00 105.68 ? 138 PHE B CE2 1 
ATOM   3607  C CZ  . PHE B  2 138 ? -44.448 -76.470  9.909   1.00 108.11 ? 138 PHE B CZ  1 
ATOM   3608  N N   . GLU B  2 139 ? -43.783 -76.499  17.020  1.00 155.64 ? 139 GLU B N   1 
ATOM   3609  C CA  . GLU B  2 139 ? -43.556 -76.987  18.373  1.00 142.41 ? 139 GLU B CA  1 
ATOM   3610  C C   . GLU B  2 139 ? -44.120 -78.392  18.552  1.00 136.12 ? 139 GLU B C   1 
ATOM   3611  O O   . GLU B  2 139 ? -45.315 -78.627  18.366  1.00 140.03 ? 139 GLU B O   1 
ATOM   3612  C CB  . GLU B  2 139 ? -44.153 -76.036  19.410  1.00 147.72 ? 139 GLU B CB  1 
ATOM   3613  C CG  . GLU B  2 139 ? -43.945 -76.514  20.836  1.00 170.70 ? 139 GLU B CG  1 
ATOM   3614  C CD  . GLU B  2 139 ? -44.258 -75.454  21.871  1.00 170.67 ? 139 GLU B CD  1 
ATOM   3615  O OE1 . GLU B  2 139 ? -44.630 -74.328  21.482  1.00 153.45 ? 139 GLU B OE1 1 
ATOM   3616  O OE2 . GLU B  2 139 ? -44.126 -75.748  23.078  1.00 173.12 ? 139 GLU B OE2 1 
ATOM   3617  N N   . PHE B  2 140 ? -43.246 -79.322  18.921  1.00 160.21 ? 140 PHE B N   1 
ATOM   3618  C CA  . PHE B  2 140 ? -43.628 -80.719  19.084  1.00 168.98 ? 140 PHE B CA  1 
ATOM   3619  C C   . PHE B  2 140 ? -44.407 -80.969  20.371  1.00 174.74 ? 140 PHE B C   1 
ATOM   3620  O O   . PHE B  2 140 ? -44.047 -80.466  21.435  1.00 171.93 ? 140 PHE B O   1 
ATOM   3621  C CB  . PHE B  2 140 ? -42.387 -81.616  19.067  1.00 170.51 ? 140 PHE B CB  1 
ATOM   3622  C CG  . PHE B  2 140 ? -41.695 -81.675  17.736  1.00 165.93 ? 140 PHE B CG  1 
ATOM   3623  C CD1 . PHE B  2 140 ? -40.584 -80.890  17.480  1.00 163.26 ? 140 PHE B CD1 1 
ATOM   3624  C CD2 . PHE B  2 140 ? -42.154 -82.522  16.741  1.00 164.45 ? 140 PHE B CD2 1 
ATOM   3625  C CE1 . PHE B  2 140 ? -39.944 -80.948  16.256  1.00 158.40 ? 140 PHE B CE1 1 
ATOM   3626  C CE2 . PHE B  2 140 ? -41.519 -82.583  15.516  1.00 159.41 ? 140 PHE B CE2 1 
ATOM   3627  C CZ  . PHE B  2 140 ? -40.413 -81.795  15.273  1.00 154.15 ? 140 PHE B CZ  1 
ATOM   3628  N N   . TYR B  2 141 ? -45.477 -81.752  20.267  1.00 154.67 ? 141 TYR B N   1 
ATOM   3629  C CA  . TYR B  2 141 ? -46.181 -82.236  21.446  1.00 150.33 ? 141 TYR B CA  1 
ATOM   3630  C C   . TYR B  2 141 ? -45.557 -83.550  21.877  1.00 142.86 ? 141 TYR B C   1 
ATOM   3631  O O   . TYR B  2 141 ? -45.752 -84.009  23.002  1.00 157.35 ? 141 TYR B O   1 
ATOM   3632  C CB  . TYR B  2 141 ? -47.664 -82.460  21.154  1.00 149.68 ? 141 TYR B CB  1 
ATOM   3633  C CG  . TYR B  2 141 ? -48.430 -81.204  20.824  1.00 141.41 ? 141 TYR B CG  1 
ATOM   3634  C CD1 . TYR B  2 141 ? -49.258 -81.149  19.712  1.00 129.61 ? 141 TYR B CD1 1 
ATOM   3635  C CD2 . TYR B  2 141 ? -48.323 -80.073  21.621  1.00 135.00 ? 141 TYR B CD2 1 
ATOM   3636  C CE1 . TYR B  2 141 ? -49.963 -80.004  19.406  1.00 128.65 ? 141 TYR B CE1 1 
ATOM   3637  C CE2 . TYR B  2 141 ? -49.022 -78.923  21.322  1.00 130.64 ? 141 TYR B CE2 1 
ATOM   3638  C CZ  . TYR B  2 141 ? -49.841 -78.894  20.213  1.00 132.53 ? 141 TYR B CZ  1 
ATOM   3639  O OH  . TYR B  2 141 ? -50.541 -77.750  19.909  1.00 127.37 ? 141 TYR B OH  1 
ATOM   3640  N N   . HIS B  2 142 ? -44.808 -84.155  20.964  1.00 157.26 ? 142 HIS B N   1 
ATOM   3641  C CA  . HIS B  2 142 ? -44.194 -85.448  21.217  1.00 152.55 ? 142 HIS B CA  1 
ATOM   3642  C C   . HIS B  2 142 ? -42.678 -85.332  21.172  1.00 154.43 ? 142 HIS B C   1 
ATOM   3643  O O   . HIS B  2 142 ? -42.107 -84.918  20.162  1.00 163.87 ? 142 HIS B O   1 
ATOM   3644  C CB  . HIS B  2 142 ? -44.653 -86.470  20.182  1.00 149.71 ? 142 HIS B CB  1 
ATOM   3645  C CG  . HIS B  2 142 ? -43.580 -86.863  19.212  1.00 155.43 ? 142 HIS B CG  1 
ATOM   3646  N ND1 . HIS B  2 142 ? -42.635 -87.817  19.502  1.00 156.61 ? 142 HIS B ND1 1 
ATOM   3647  C CD2 . HIS B  2 142 ? -43.299 -86.417  17.967  1.00 160.67 ? 142 HIS B CD2 1 
ATOM   3648  C CE1 . HIS B  2 142 ? -41.816 -87.955  18.473  1.00 157.46 ? 142 HIS B CE1 1 
ATOM   3649  N NE2 . HIS B  2 142 ? -42.203 -87.107  17.525  1.00 161.62 ? 142 HIS B NE2 1 
ATOM   3650  N N   . LYS B  2 143 ? -42.032 -85.713  22.270  1.00 151.21 ? 143 LYS B N   1 
ATOM   3651  C CA  . LYS B  2 143 ? -40.578 -85.619  22.384  1.00 148.15 ? 143 LYS B CA  1 
ATOM   3652  C C   . LYS B  2 143 ? -39.849 -86.068  21.124  1.00 146.93 ? 143 LYS B C   1 
ATOM   3653  O O   . LYS B  2 143 ? -39.837 -87.251  20.772  1.00 142.70 ? 143 LYS B O   1 
ATOM   3654  C CB  . LYS B  2 143 ? -40.067 -86.400  23.595  1.00 149.70 ? 143 LYS B CB  1 
ATOM   3655  C CG  . LYS B  2 143 ? -40.459 -85.795  24.939  1.00 154.00 ? 143 LYS B CG  1 
ATOM   3656  C CD  . LYS B  2 143 ? -39.483 -84.715  25.404  1.00 163.30 ? 143 LYS B CD  1 
ATOM   3657  C CE  . LYS B  2 143 ? -39.752 -83.369  24.746  1.00 158.66 ? 143 LYS B CE  1 
ATOM   3658  N NZ  . LYS B  2 143 ? -38.804 -82.318  25.215  1.00 150.69 ? 143 LYS B NZ  1 
ATOM   3659  N N   . CYS B  2 144 ? -39.228 -85.101  20.460  1.00 152.68 ? 144 CYS B N   1 
ATOM   3660  C CA  . CYS B  2 144 ? -38.493 -85.354  19.230  1.00 162.82 ? 144 CYS B CA  1 
ATOM   3661  C C   . CYS B  2 144 ? -36.983 -85.206  19.385  1.00 152.43 ? 144 CYS B C   1 
ATOM   3662  O O   . CYS B  2 144 ? -36.448 -84.101  19.286  1.00 150.64 ? 144 CYS B O   1 
ATOM   3663  C CB  . CYS B  2 144 ? -38.965 -84.422  18.125  1.00 160.52 ? 144 CYS B CB  1 
ATOM   3664  S SG  . CYS B  2 144 ? -40.058 -85.190  16.935  1.00 167.41 ? 144 CYS B SG  1 
ATOM   3665  N N   . ASP B  2 145 ? -36.293 -86.322  19.593  1.00 171.15 ? 145 ASP B N   1 
ATOM   3666  C CA  . ASP B  2 145 ? -34.838 -86.299  19.693  1.00 174.80 ? 145 ASP B CA  1 
ATOM   3667  C C   . ASP B  2 145 ? -34.164 -86.206  18.317  1.00 169.63 ? 145 ASP B C   1 
ATOM   3668  O O   . ASP B  2 145 ? -34.806 -85.840  17.335  1.00 177.93 ? 145 ASP B O   1 
ATOM   3669  C CB  . ASP B  2 145 ? -34.324 -87.494  20.507  1.00 191.42 ? 145 ASP B CB  1 
ATOM   3670  C CG  . ASP B  2 145 ? -34.966 -88.812  20.105  1.00 192.71 ? 145 ASP B CG  1 
ATOM   3671  O OD1 . ASP B  2 145 ? -34.377 -89.868  20.422  1.00 181.01 ? 145 ASP B OD1 1 
ATOM   3672  O OD2 . ASP B  2 145 ? -36.047 -88.804  19.485  1.00 190.43 ? 145 ASP B OD2 1 
ATOM   3673  N N   . ASN B  2 146 ? -32.873 -86.528  18.258  1.00 156.90 ? 146 ASN B N   1 
ATOM   3674  C CA  . ASN B  2 146 ? -32.070 -86.357  17.040  1.00 150.26 ? 146 ASN B CA  1 
ATOM   3675  C C   . ASN B  2 146 ? -32.469 -87.254  15.869  1.00 158.79 ? 146 ASN B C   1 
ATOM   3676  O O   . ASN B  2 146 ? -32.578 -86.792  14.732  1.00 166.57 ? 146 ASN B O   1 
ATOM   3677  C CB  . ASN B  2 146 ? -30.583 -86.564  17.344  1.00 129.46 ? 146 ASN B CB  1 
ATOM   3678  C CG  . ASN B  2 146 ? -29.972 -85.407  18.103  1.00 131.98 ? 146 ASN B CG  1 
ATOM   3679  O OD1 . ASN B  2 146 ? -28.822 -85.476  18.539  1.00 137.27 ? 146 ASN B OD1 1 
ATOM   3680  N ND2 . ASN B  2 146 ? -30.736 -84.335  18.265  1.00 134.52 ? 146 ASN B ND2 1 
ATOM   3681  N N   . THR B  2 147 ? -32.651 -88.540  16.139  1.00 171.49 ? 147 THR B N   1 
ATOM   3682  C CA  . THR B  2 147 ? -33.144 -89.443  15.111  1.00 177.26 ? 147 THR B CA  1 
ATOM   3683  C C   . THR B  2 147 ? -34.632 -89.213  14.897  1.00 173.44 ? 147 THR B C   1 
ATOM   3684  O O   . THR B  2 147 ? -35.215 -89.707  13.930  1.00 171.83 ? 147 THR B O   1 
ATOM   3685  C CB  . THR B  2 147 ? -32.939 -90.913  15.484  1.00 174.90 ? 147 THR B CB  1 
ATOM   3686  O OG1 . THR B  2 147 ? -33.717 -91.214  16.648  1.00 181.91 ? 147 THR B OG1 1 
ATOM   3687  N N   . CYS B  2 148 ? -35.251 -88.463  15.799  1.00 157.38 ? 148 CYS B N   1 
ATOM   3688  C CA  . CYS B  2 148 ? -36.620 -88.025  15.579  1.00 160.19 ? 148 CYS B CA  1 
ATOM   3689  C C   . CYS B  2 148 ? -36.634 -86.732  14.756  1.00 168.94 ? 148 CYS B C   1 
ATOM   3690  O O   . CYS B  2 148 ? -37.628 -86.366  14.125  1.00 168.44 ? 148 CYS B O   1 
ATOM   3691  C CB  . CYS B  2 148 ? -37.347 -87.869  16.924  1.00 158.86 ? 148 CYS B CB  1 
ATOM   3692  S SG  . CYS B  2 148 ? -38.475 -86.444  16.986  1.00 169.02 ? 148 CYS B SG  1 
ATOM   3693  N N   . MET B  2 149 ? -35.522 -86.018  14.820  1.00 167.59 ? 149 MET B N   1 
ATOM   3694  C CA  . MET B  2 149 ? -35.276 -84.937  13.884  1.00 154.90 ? 149 MET B CA  1 
ATOM   3695  C C   . MET B  2 149 ? -35.369 -85.420  12.435  1.00 147.85 ? 149 MET B C   1 
ATOM   3696  O O   . MET B  2 149 ? -36.323 -85.114  11.718  1.00 146.75 ? 149 MET B O   1 
ATOM   3697  C CB  . MET B  2 149 ? -33.898 -84.309  14.120  1.00 146.81 ? 149 MET B CB  1 
ATOM   3698  C CG  . MET B  2 149 ? -33.905 -83.263  15.205  1.00 143.94 ? 149 MET B CG  1 
ATOM   3699  S SD  . MET B  2 149 ? -35.608 -82.743  15.494  1.00 148.32 ? 149 MET B SD  1 
ATOM   3700  C CE  . MET B  2 149 ? -35.369 -81.259  16.460  1.00 135.32 ? 149 MET B CE  1 
ATOM   3701  N N   . GLU B  2 150 ? -34.381 -86.211  12.029  1.00 202.73 ? 150 GLU B N   1 
ATOM   3702  C CA  . GLU B  2 150 ? -34.194 -86.603  10.629  1.00 204.47 ? 150 GLU B CA  1 
ATOM   3703  C C   . GLU B  2 150 ? -35.430 -87.154  9.921   1.00 205.58 ? 150 GLU B C   1 
ATOM   3704  O O   . GLU B  2 150 ? -35.698 -86.793  8.776   1.00 203.44 ? 150 GLU B O   1 
ATOM   3705  C CB  . GLU B  2 150 ? -33.057 -87.622  10.509  1.00 209.25 ? 150 GLU B CB  1 
ATOM   3706  C CG  . GLU B  2 150 ? -31.878 -87.154  9.672   1.00 215.63 ? 150 GLU B CG  1 
ATOM   3707  C CD  . GLU B  2 150 ? -30.879 -86.346  10.473  1.00 217.84 ? 150 GLU B CD  1 
ATOM   3708  O OE1 . GLU B  2 150 ? -30.181 -85.499  9.879   1.00 209.60 ? 150 GLU B OE1 1 
ATOM   3709  O OE2 . GLU B  2 150 ? -30.793 -86.560  11.700  1.00 214.44 ? 150 GLU B OE2 1 
ATOM   3710  N N   . SER B  2 151 ? -36.166 -88.041  10.585  1.00 169.77 ? 151 SER B N   1 
ATOM   3711  C CA  . SER B  2 151 ? -37.348 -88.643  9.972   1.00 168.00 ? 151 SER B CA  1 
ATOM   3712  C C   . SER B  2 151 ? -38.147 -87.572  9.231   1.00 161.79 ? 151 SER B C   1 
ATOM   3713  O O   . SER B  2 151 ? -38.795 -87.842  8.218   1.00 171.16 ? 151 SER B O   1 
ATOM   3714  C CB  . SER B  2 151 ? -38.213 -89.349  11.020  1.00 167.36 ? 151 SER B CB  1 
ATOM   3715  O OG  . SER B  2 151 ? -38.856 -88.415  11.871  1.00 164.82 ? 151 SER B OG  1 
ATOM   3716  N N   . VAL B  2 152 ? -38.066 -86.348  9.745   1.00 136.25 ? 152 VAL B N   1 
ATOM   3717  C CA  . VAL B  2 152 ? -38.658 -85.180  9.109   1.00 133.72 ? 152 VAL B CA  1 
ATOM   3718  C C   . VAL B  2 152 ? -37.817 -84.715  7.915   1.00 133.07 ? 152 VAL B C   1 
ATOM   3719  O O   . VAL B  2 152 ? -38.346 -84.504  6.824   1.00 121.75 ? 152 VAL B O   1 
ATOM   3720  C CB  . VAL B  2 152 ? -38.801 -84.022  10.112  1.00 116.84 ? 152 VAL B CB  1 
ATOM   3721  C CG1 . VAL B  2 152 ? -39.698 -82.936  9.546   1.00 99.88  ? 152 VAL B CG1 1 
ATOM   3722  C CG2 . VAL B  2 152 ? -39.350 -84.535  11.438  1.00 125.81 ? 152 VAL B CG2 1 
ATOM   3723  N N   . LYS B  2 153 ? -36.510 -84.556  8.121   1.00 127.18 ? 153 LYS B N   1 
ATOM   3724  C CA  . LYS B  2 153 ? -35.607 -84.154  7.040   1.00 122.44 ? 153 LYS B CA  1 
ATOM   3725  C C   . LYS B  2 153 ? -35.604 -85.159  5.890   1.00 143.90 ? 153 LYS B C   1 
ATOM   3726  O O   . LYS B  2 153 ? -35.869 -84.801  4.742   1.00 152.22 ? 153 LYS B O   1 
ATOM   3727  C CB  . LYS B  2 153 ? -34.176 -83.952  7.552   1.00 115.45 ? 153 LYS B CB  1 
ATOM   3728  C CG  . LYS B  2 153 ? -34.003 -82.793  8.520   1.00 101.69 ? 153 LYS B CG  1 
ATOM   3729  C CD  . LYS B  2 153 ? -32.530 -82.511  8.787   1.00 108.05 ? 153 LYS B CD  1 
ATOM   3730  C CE  . LYS B  2 153 ? -32.351 -81.416  9.826   1.00 102.74 ? 153 LYS B CE  1 
ATOM   3731  N NZ  . LYS B  2 153 ? -32.896 -81.816  11.152  1.00 112.64 ? 153 LYS B NZ  1 
ATOM   3732  N N   . ASN B  2 154 ? -35.291 -86.414  6.201   1.00 197.56 ? 154 ASN B N   1 
ATOM   3733  C CA  . ASN B  2 154 ? -35.310 -87.480  5.204   1.00 204.39 ? 154 ASN B CA  1 
ATOM   3734  C C   . ASN B  2 154 ? -36.676 -87.614  4.541   1.00 205.68 ? 154 ASN B C   1 
ATOM   3735  O O   . ASN B  2 154 ? -36.817 -88.285  3.519   1.00 210.95 ? 154 ASN B O   1 
ATOM   3736  C CB  . ASN B  2 154 ? -34.905 -88.818  5.829   1.00 211.25 ? 154 ASN B CB  1 
ATOM   3737  C CG  . ASN B  2 154 ? -33.417 -88.909  6.104   1.00 210.18 ? 154 ASN B CG  1 
ATOM   3738  O OD1 . ASN B  2 154 ? -32.943 -88.499  7.163   1.00 211.47 ? 154 ASN B OD1 1 
ATOM   3739  N ND2 . ASN B  2 154 ? -32.671 -89.455  5.150   1.00 207.28 ? 154 ASN B ND2 1 
ATOM   3740  N N   . GLY B  2 155 ? -37.679 -86.971  5.129   1.00 169.57 ? 155 GLY B N   1 
ATOM   3741  C CA  . GLY B  2 155 ? -39.032 -87.031  4.608   1.00 167.26 ? 155 GLY B CA  1 
ATOM   3742  C C   . GLY B  2 155 ? -39.703 -88.346  4.950   1.00 174.19 ? 155 GLY B C   1 
ATOM   3743  O O   . GLY B  2 155 ? -40.844 -88.593  4.563   1.00 166.94 ? 155 GLY B O   1 
ATOM   3744  N N   . THR B  2 156 ? -38.986 -89.194  5.679   1.00 191.76 ? 156 THR B N   1 
ATOM   3745  C CA  . THR B  2 156 ? -39.519 -90.478  6.121   1.00 194.67 ? 156 THR B CA  1 
ATOM   3746  C C   . THR B  2 156 ? -39.984 -90.399  7.573   1.00 178.60 ? 156 THR B C   1 
ATOM   3747  O O   . THR B  2 156 ? -39.292 -90.857  8.483   1.00 172.22 ? 156 THR B O   1 
ATOM   3748  C CB  . THR B  2 156 ? -38.473 -91.597  5.989   1.00 203.82 ? 156 THR B CB  1 
ATOM   3749  O OG1 . THR B  2 156 ? -37.272 -91.215  6.671   1.00 198.42 ? 156 THR B OG1 1 
ATOM   3750  C CG2 . THR B  2 156 ? -38.152 -91.858  4.524   1.00 208.40 ? 156 THR B CG2 1 
ATOM   3751  N N   . TYR B  2 157 ? -41.159 -89.813  7.777   1.00 164.56 ? 157 TYR B N   1 
ATOM   3752  C CA  . TYR B  2 157 ? -41.704 -89.607  9.111   1.00 155.88 ? 157 TYR B CA  1 
ATOM   3753  C C   . TYR B  2 157 ? -42.856 -90.569  9.356   1.00 164.32 ? 157 TYR B C   1 
ATOM   3754  O O   . TYR B  2 157 ? -43.874 -90.518  8.666   1.00 153.59 ? 157 TYR B O   1 
ATOM   3755  C CB  . TYR B  2 157 ? -42.193 -88.160  9.258   1.00 149.57 ? 157 TYR B CB  1 
ATOM   3756  C CG  . TYR B  2 157 ? -42.637 -87.771  10.652  1.00 136.94 ? 157 TYR B CG  1 
ATOM   3757  C CD1 . TYR B  2 157 ? -41.736 -87.238  11.564  1.00 138.99 ? 157 TYR B CD1 1 
ATOM   3758  C CD2 . TYR B  2 157 ? -43.958 -87.920  11.050  1.00 130.93 ? 157 TYR B CD2 1 
ATOM   3759  C CE1 . TYR B  2 157 ? -42.134 -86.876  12.834  1.00 132.37 ? 157 TYR B CE1 1 
ATOM   3760  C CE2 . TYR B  2 157 ? -44.367 -87.562  12.322  1.00 134.74 ? 157 TYR B CE2 1 
ATOM   3761  C CZ  . TYR B  2 157 ? -43.449 -87.039  13.210  1.00 128.72 ? 157 TYR B CZ  1 
ATOM   3762  O OH  . TYR B  2 157 ? -43.840 -86.676  14.479  1.00 115.65 ? 157 TYR B OH  1 
ATOM   3763  N N   . ASP B  2 158 ? -42.695 -91.451  10.337  1.00 156.33 ? 158 ASP B N   1 
ATOM   3764  C CA  . ASP B  2 158 ? -43.756 -92.384  10.699  1.00 148.09 ? 158 ASP B CA  1 
ATOM   3765  C C   . ASP B  2 158 ? -44.956 -91.620  11.243  1.00 125.69 ? 158 ASP B C   1 
ATOM   3766  O O   . ASP B  2 158 ? -44.954 -90.389  11.269  1.00 141.54 ? 158 ASP B O   1 
ATOM   3767  C CB  . ASP B  2 158 ? -43.261 -93.375  11.752  1.00 125.26 ? 158 ASP B CB  1 
ATOM   3768  C CG  . ASP B  2 158 ? -41.836 -93.819  11.505  1.00 138.67 ? 158 ASP B CG  1 
ATOM   3769  O OD1 . ASP B  2 158 ? -41.630 -95.002  11.163  1.00 122.62 ? 158 ASP B OD1 1 
ATOM   3770  O OD2 . ASP B  2 158 ? -40.922 -92.982  11.654  1.00 123.37 ? 158 ASP B OD2 1 
ATOM   3771  N N   . TYR B  2 159 ? -45.986 -92.342  11.676  1.00 122.04 ? 159 TYR B N   1 
ATOM   3772  C CA  . TYR B  2 159 ? -47.094 -91.688  12.373  1.00 125.17 ? 159 TYR B CA  1 
ATOM   3773  C C   . TYR B  2 159 ? -47.813 -92.554  13.420  1.00 143.49 ? 159 TYR B C   1 
ATOM   3774  O O   . TYR B  2 159 ? -49.031 -92.740  13.347  1.00 144.30 ? 159 TYR B O   1 
ATOM   3775  C CB  . TYR B  2 159 ? -48.095 -91.069  11.383  1.00 117.12 ? 159 TYR B CB  1 
ATOM   3776  C CG  . TYR B  2 159 ? -48.717 -89.798  11.923  1.00 96.68  ? 159 TYR B CG  1 
ATOM   3777  C CD1 . TYR B  2 159 ? -47.970 -88.633  12.032  1.00 103.36 ? 159 TYR B CD1 1 
ATOM   3778  C CD2 . TYR B  2 159 ? -50.040 -89.766  12.337  1.00 100.07 ? 159 TYR B CD2 1 
ATOM   3779  C CE1 . TYR B  2 159 ? -48.524 -87.469  12.535  1.00 107.82 ? 159 TYR B CE1 1 
ATOM   3780  C CE2 . TYR B  2 159 ? -50.605 -88.604  12.842  1.00 108.96 ? 159 TYR B CE2 1 
ATOM   3781  C CZ  . TYR B  2 159 ? -49.842 -87.459  12.939  1.00 109.76 ? 159 TYR B CZ  1 
ATOM   3782  O OH  . TYR B  2 159 ? -50.392 -86.301  13.440  1.00 110.11 ? 159 TYR B OH  1 
ATOM   3783  N N   . PRO B  2 160 ? -47.067 -93.041  14.429  1.00 154.71 ? 160 PRO B N   1 
ATOM   3784  C CA  . PRO B  2 160 ? -47.647 -93.871  15.493  1.00 169.61 ? 160 PRO B CA  1 
ATOM   3785  C C   . PRO B  2 160 ? -47.913 -93.132  16.809  1.00 161.34 ? 160 PRO B C   1 
ATOM   3786  O O   . PRO B  2 160 ? -48.329 -93.777  17.775  1.00 159.18 ? 160 PRO B O   1 
ATOM   3787  C CB  . PRO B  2 160 ? -46.524 -94.871  15.800  1.00 179.40 ? 160 PRO B CB  1 
ATOM   3788  C CG  . PRO B  2 160 ? -45.265 -94.347  15.084  1.00 166.27 ? 160 PRO B CG  1 
ATOM   3789  C CD  . PRO B  2 160 ? -45.607 -92.959  14.572  1.00 162.14 ? 160 PRO B CD  1 
ATOM   3790  N N   . LYS B  2 161 ? -47.682 -91.826  16.873  1.00 138.92 ? 161 LYS B N   1 
ATOM   3791  C CA  . LYS B  2 161 ? -47.449 -91.208  18.179  1.00 120.05 ? 161 LYS B CA  1 
ATOM   3792  C C   . LYS B  2 161 ? -48.543 -90.360  18.845  1.00 127.37 ? 161 LYS B C   1 
ATOM   3793  O O   . LYS B  2 161 ? -49.461 -89.862  18.199  1.00 89.76  ? 161 LYS B O   1 
ATOM   3794  C CB  . LYS B  2 161 ? -46.185 -90.377  18.103  1.00 71.87  ? 161 LYS B CB  1 
ATOM   3795  C CG  . LYS B  2 161 ? -45.052 -91.067  17.368  1.00 103.20 ? 161 LYS B CG  1 
ATOM   3796  C CD  . LYS B  2 161 ? -43.814 -90.165  17.361  1.00 98.93  ? 161 LYS B CD  1 
ATOM   3797  C CE  . LYS B  2 161 ? -42.528 -90.970  17.634  1.00 117.69 ? 161 LYS B CE  1 
ATOM   3798  N NZ  . LYS B  2 161 ? -41.249 -90.372  17.112  1.00 79.14  ? 161 LYS B NZ  1 
ATOM   3799  N N   . TYR B  2 162 ? -48.431 -90.250  20.168  1.00 145.99 ? 162 TYR B N   1 
ATOM   3800  C CA  . TYR B  2 162 ? -48.950 -89.122  20.940  1.00 125.28 ? 162 TYR B CA  1 
ATOM   3801  C C   . TYR B  2 162 ? -48.174 -89.054  22.250  1.00 88.36  ? 162 TYR B C   1 
ATOM   3802  O O   . TYR B  2 162 ? -47.255 -89.842  22.471  1.00 60.91  ? 162 TYR B O   1 
ATOM   3803  C CB  . TYR B  2 162 ? -50.451 -89.213  21.216  1.00 109.49 ? 162 TYR B CB  1 
ATOM   3804  C CG  . TYR B  2 162 ? -50.938 -88.086  22.099  1.00 124.79 ? 162 TYR B CG  1 
ATOM   3805  C CD1 . TYR B  2 162 ? -50.611 -88.052  23.448  1.00 111.06 ? 162 TYR B CD1 1 
ATOM   3806  C CD2 . TYR B  2 162 ? -51.708 -87.052  21.586  1.00 118.36 ? 162 TYR B CD2 1 
ATOM   3807  C CE1 . TYR B  2 162 ? -51.034 -87.028  24.259  1.00 113.80 ? 162 TYR B CE1 1 
ATOM   3808  C CE2 . TYR B  2 162 ? -52.142 -86.020  22.395  1.00 96.62  ? 162 TYR B CE2 1 
ATOM   3809  C CZ  . TYR B  2 162 ? -51.800 -86.016  23.731  1.00 112.95 ? 162 TYR B CZ  1 
ATOM   3810  O OH  . TYR B  2 162 ? -52.222 -84.998  24.550  1.00 89.53  ? 162 TYR B OH  1 
ATOM   3811  N N   . ASP C  1 7   ? -69.432 -60.812  13.734  1.00 152.48 ? 7   ASP C N   1 
ATOM   3812  C CA  . ASP C  1 7   ? -68.718 -62.064  13.963  1.00 159.40 ? 7   ASP C CA  1 
ATOM   3813  C C   . ASP C  1 7   ? -68.134 -62.648  12.678  1.00 173.55 ? 7   ASP C C   1 
ATOM   3814  O O   . ASP C  1 7   ? -67.906 -63.854  12.580  1.00 175.08 ? 7   ASP C O   1 
ATOM   3815  C CB  . ASP C  1 7   ? -69.619 -63.086  14.663  1.00 143.88 ? 7   ASP C CB  1 
ATOM   3816  C CG  . ASP C  1 7   ? -71.050 -63.046  14.162  1.00 146.84 ? 7   ASP C CG  1 
ATOM   3817  O OD1 . ASP C  1 7   ? -71.497 -64.041  13.554  1.00 123.35 ? 7   ASP C OD1 1 
ATOM   3818  O OD2 . ASP C  1 7   ? -71.730 -62.021  14.381  1.00 151.41 ? 7   ASP C OD2 1 
ATOM   3819  N N   . THR C  1 8   ? -67.902 -61.785  11.694  1.00 179.08 ? 8   THR C N   1 
ATOM   3820  C CA  . THR C  1 8   ? -67.187 -62.178  10.485  1.00 176.88 ? 8   THR C CA  1 
ATOM   3821  C C   . THR C  1 8   ? -66.167 -61.114  10.102  1.00 164.03 ? 8   THR C C   1 
ATOM   3822  O O   . THR C  1 8   ? -66.438 -59.916  10.195  1.00 162.06 ? 8   THR C O   1 
ATOM   3823  C CB  . THR C  1 8   ? -68.128 -62.393  9.279   1.00 175.66 ? 8   THR C CB  1 
ATOM   3824  O OG1 . THR C  1 8   ? -68.562 -61.125  8.773   1.00 174.54 ? 8   THR C OG1 1 
ATOM   3825  C CG2 . THR C  1 8   ? -69.333 -63.233  9.665   1.00 184.94 ? 8   THR C CG2 1 
ATOM   3826  N N   . LEU C  1 9   ? -64.990 -61.563  9.682   1.00 151.52 ? 9   LEU C N   1 
ATOM   3827  C CA  . LEU C  1 9   ? -63.999 -60.678  9.090   1.00 125.51 ? 9   LEU C CA  1 
ATOM   3828  C C   . LEU C  1 9   ? -63.571 -61.244  7.746   1.00 119.28 ? 9   LEU C C   1 
ATOM   3829  O O   . LEU C  1 9   ? -62.926 -62.289  7.684   1.00 103.96 ? 9   LEU C O   1 
ATOM   3830  C CB  . LEU C  1 9   ? -62.781 -60.516  9.998   1.00 130.65 ? 9   LEU C CB  1 
ATOM   3831  C CG  . LEU C  1 9   ? -61.651 -59.705  9.358   1.00 118.74 ? 9   LEU C CG  1 
ATOM   3832  C CD1 . LEU C  1 9   ? -62.140 -58.342  8.870   1.00 112.94 ? 9   LEU C CD1 1 
ATOM   3833  C CD2 . LEU C  1 9   ? -60.475 -59.568  10.310  1.00 105.26 ? 9   LEU C CD2 1 
ATOM   3834  N N   . CYS C  1 10  ? -63.937 -60.555  6.671   1.00 125.64 ? 10  CYS C N   1 
ATOM   3835  C CA  . CYS C  1 10  ? -63.636 -61.040  5.329   1.00 113.71 ? 10  CYS C CA  1 
ATOM   3836  C C   . CYS C  1 10  ? -62.530 -60.238  4.660   1.00 95.38  ? 10  CYS C C   1 
ATOM   3837  O O   . CYS C  1 10  ? -62.176 -59.150  5.111   1.00 91.94  ? 10  CYS C O   1 
ATOM   3838  C CB  . CYS C  1 10  ? -64.894 -61.042  4.461   1.00 103.40 ? 10  CYS C CB  1 
ATOM   3839  S SG  . CYS C  1 10  ? -66.134 -62.247  4.982   1.00 128.26 ? 10  CYS C SG  1 
ATOM   3840  N N   . ILE C  1 11  ? -61.987 -60.787  3.579   1.00 89.81  ? 11  ILE C N   1 
ATOM   3841  C CA  . ILE C  1 11  ? -60.872 -60.161  2.883   1.00 96.32  ? 11  ILE C CA  1 
ATOM   3842  C C   . ILE C  1 11  ? -61.120 -60.094  1.382   1.00 93.21  ? 11  ILE C C   1 
ATOM   3843  O O   . ILE C  1 11  ? -61.618 -61.047  0.781   1.00 93.11  ? 11  ILE C O   1 
ATOM   3844  C CB  . ILE C  1 11  ? -59.558 -60.914  3.147   1.00 94.34  ? 11  ILE C CB  1 
ATOM   3845  C CG1 . ILE C  1 11  ? -59.325 -61.054  4.652   1.00 91.45  ? 11  ILE C CG1 1 
ATOM   3846  C CG2 . ILE C  1 11  ? -58.390 -60.200  2.485   1.00 91.89  ? 11  ILE C CG2 1 
ATOM   3847  C CD1 . ILE C  1 11  ? -57.995 -61.670  5.005   1.00 79.91  ? 11  ILE C CD1 1 
ATOM   3848  N N   . GLY C  1 12  ? -60.770 -58.962  0.782   1.00 114.32 ? 12  GLY C N   1 
ATOM   3849  C CA  . GLY C  1 12  ? -60.972 -58.771  -0.640  1.00 112.19 ? 12  GLY C CA  1 
ATOM   3850  C C   . GLY C  1 12  ? -60.106 -57.689  -1.251  1.00 109.01 ? 12  GLY C C   1 
ATOM   3851  O O   . GLY C  1 12  ? -59.197 -57.160  -0.611  1.00 101.76 ? 12  GLY C O   1 
ATOM   3852  N N   . TYR C  1 13  ? -60.404 -57.361  -2.504  1.00 85.32  ? 13  TYR C N   1 
ATOM   3853  C CA  . TYR C  1 13  ? -59.630 -56.394  -3.269  1.00 81.36  ? 13  TYR C CA  1 
ATOM   3854  C C   . TYR C  1 13  ? -60.493 -55.244  -3.795  1.00 74.79  ? 13  TYR C C   1 
ATOM   3855  O O   . TYR C  1 13  ? -61.606 -55.031  -3.317  1.00 77.37  ? 13  TYR C O   1 
ATOM   3856  C CB  . TYR C  1 13  ? -58.899 -57.094  -4.418  1.00 63.90  ? 13  TYR C CB  1 
ATOM   3857  C CG  . TYR C  1 13  ? -59.667 -58.246  -5.031  1.00 59.52  ? 13  TYR C CG  1 
ATOM   3858  C CD1 . TYR C  1 13  ? -60.407 -58.074  -6.192  1.00 61.40  ? 13  TYR C CD1 1 
ATOM   3859  C CD2 . TYR C  1 13  ? -59.645 -59.508  -4.451  1.00 51.42  ? 13  TYR C CD2 1 
ATOM   3860  C CE1 . TYR C  1 13  ? -61.111 -59.123  -6.755  1.00 50.95  ? 13  TYR C CE1 1 
ATOM   3861  C CE2 . TYR C  1 13  ? -60.344 -60.563  -5.006  1.00 63.99  ? 13  TYR C CE2 1 
ATOM   3862  C CZ  . TYR C  1 13  ? -61.074 -60.364  -6.158  1.00 61.32  ? 13  TYR C CZ  1 
ATOM   3863  O OH  . TYR C  1 13  ? -61.770 -61.411  -6.717  1.00 56.99  ? 13  TYR C OH  1 
ATOM   3864  N N   . HIS C  1 14  ? -59.981 -54.514  -4.784  1.00 79.37  ? 14  HIS C N   1 
ATOM   3865  C CA  . HIS C  1 14  ? -60.654 -53.314  -5.286  1.00 70.66  ? 14  HIS C CA  1 
ATOM   3866  C C   . HIS C  1 14  ? -61.484 -53.576  -6.542  1.00 79.78  ? 14  HIS C C   1 
ATOM   3867  O O   . HIS C  1 14  ? -61.303 -54.585  -7.223  1.00 86.29  ? 14  HIS C O   1 
ATOM   3868  C CB  . HIS C  1 14  ? -59.629 -52.206  -5.559  1.00 83.05  ? 14  HIS C CB  1 
ATOM   3869  C CG  . HIS C  1 14  ? -60.240 -50.891  -5.949  1.00 86.66  ? 14  HIS C CG  1 
ATOM   3870  N ND1 . HIS C  1 14  ? -60.589 -49.932  -5.022  1.00 97.73  ? 14  HIS C ND1 1 
ATOM   3871  C CD2 . HIS C  1 14  ? -60.549 -50.377  -7.159  1.00 94.32  ? 14  HIS C CD2 1 
ATOM   3872  C CE1 . HIS C  1 14  ? -61.095 -48.884  -5.647  1.00 108.76 ? 14  HIS C CE1 1 
ATOM   3873  N NE2 . HIS C  1 14  ? -61.083 -49.126  -6.946  1.00 104.76 ? 14  HIS C NE2 1 
ATOM   3874  N N   . ALA C  1 15  ? -62.397 -52.653  -6.834  1.00 68.78  ? 15  ALA C N   1 
ATOM   3875  C CA  . ALA C  1 15  ? -63.202 -52.693  -8.050  1.00 75.85  ? 15  ALA C CA  1 
ATOM   3876  C C   . ALA C  1 15  ? -63.712 -51.289  -8.358  1.00 73.82  ? 15  ALA C C   1 
ATOM   3877  O O   . ALA C  1 15  ? -63.778 -50.441  -7.468  1.00 79.86  ? 15  ALA C O   1 
ATOM   3878  C CB  . ALA C  1 15  ? -64.363 -53.661  -7.895  1.00 65.48  ? 15  ALA C CB  1 
ATOM   3879  N N   . ASN C  1 16  ? -64.071 -51.040  -9.614  1.00 72.44  ? 16  ASN C N   1 
ATOM   3880  C CA  . ASN C  1 16  ? -64.517 -49.710  -10.016 1.00 92.21  ? 16  ASN C CA  1 
ATOM   3881  C C   . ASN C  1 16  ? -65.238 -49.677  -11.362 1.00 98.64  ? 16  ASN C C   1 
ATOM   3882  O O   . ASN C  1 16  ? -65.563 -50.718  -11.935 1.00 96.18  ? 16  ASN C O   1 
ATOM   3883  C CB  . ASN C  1 16  ? -63.335 -48.737  -10.033 1.00 97.26  ? 16  ASN C CB  1 
ATOM   3884  C CG  . ASN C  1 16  ? -62.204 -49.211  -10.923 1.00 94.72  ? 16  ASN C CG  1 
ATOM   3885  O OD1 . ASN C  1 16  ? -62.370 -50.135  -11.719 1.00 90.57  ? 16  ASN C OD1 1 
ATOM   3886  N ND2 . ASN C  1 16  ? -61.043 -48.578  -10.793 1.00 86.76  ? 16  ASN C ND2 1 
ATOM   3887  N N   . ASN C  1 17  ? -65.478 -48.467  -11.855 1.00 91.73  ? 17  ASN C N   1 
ATOM   3888  C CA  . ASN C  1 17  ? -66.180 -48.254  -13.114 1.00 99.10  ? 17  ASN C CA  1 
ATOM   3889  C C   . ASN C  1 17  ? -65.236 -48.296  -14.312 1.00 112.26 ? 17  ASN C C   1 
ATOM   3890  O O   . ASN C  1 17  ? -65.567 -47.804  -15.390 1.00 122.71 ? 17  ASN C O   1 
ATOM   3891  C CB  . ASN C  1 17  ? -66.906 -46.907  -13.081 1.00 124.27 ? 17  ASN C CB  1 
ATOM   3892  C CG  . ASN C  1 17  ? -65.950 -45.735  -12.912 1.00 132.59 ? 17  ASN C CG  1 
ATOM   3893  O OD1 . ASN C  1 17  ? -64.756 -45.853  -13.185 1.00 132.98 ? 17  ASN C OD1 1 
ATOM   3894  N ND2 . ASN C  1 17  ? -66.471 -44.597  -12.467 1.00 143.96 ? 17  ASN C ND2 1 
ATOM   3895  N N   . SER C  1 18  ? -64.058 -48.880  -14.115 1.00 103.75 ? 18  SER C N   1 
ATOM   3896  C CA  . SER C  1 18  ? -63.039 -48.909  -15.158 1.00 90.04  ? 18  SER C CA  1 
ATOM   3897  C C   . SER C  1 18  ? -63.417 -49.851  -16.296 1.00 83.72  ? 18  SER C C   1 
ATOM   3898  O O   . SER C  1 18  ? -63.882 -50.968  -16.067 1.00 75.48  ? 18  SER C O   1 
ATOM   3899  C CB  . SER C  1 18  ? -61.681 -49.306  -14.573 1.00 92.34  ? 18  SER C CB  1 
ATOM   3900  O OG  . SER C  1 18  ? -60.652 -49.180  -15.539 1.00 80.42  ? 18  SER C OG  1 
ATOM   3901  N N   . THR C  1 19  ? -63.215 -49.386  -17.525 1.00 89.83  ? 19  THR C N   1 
ATOM   3902  C CA  . THR C  1 19  ? -63.473 -50.197  -18.707 1.00 93.09  ? 19  THR C CA  1 
ATOM   3903  C C   . THR C  1 19  ? -62.161 -50.555  -19.392 1.00 89.48  ? 19  THR C C   1 
ATOM   3904  O O   . THR C  1 19  ? -62.147 -51.246  -20.411 1.00 91.67  ? 19  THR C O   1 
ATOM   3905  C CB  . THR C  1 19  ? -64.390 -49.466  -19.703 1.00 89.48  ? 19  THR C CB  1 
ATOM   3906  O OG1 . THR C  1 19  ? -63.839 -48.178  -20.007 1.00 87.53  ? 19  THR C OG1 1 
ATOM   3907  C CG2 . THR C  1 19  ? -65.779 -49.287  -19.112 1.00 98.24  ? 19  THR C CG2 1 
ATOM   3908  N N   . ASP C  1 20  ? -61.060 -50.074  -18.823 1.00 79.46  ? 20  ASP C N   1 
ATOM   3909  C CA  . ASP C  1 20  ? -59.731 -50.368  -19.342 1.00 68.59  ? 20  ASP C CA  1 
ATOM   3910  C C   . ASP C  1 20  ? -59.542 -51.865  -19.532 1.00 64.51  ? 20  ASP C C   1 
ATOM   3911  O O   . ASP C  1 20  ? -59.841 -52.657  -18.639 1.00 79.91  ? 20  ASP C O   1 
ATOM   3912  C CB  . ASP C  1 20  ? -58.652 -49.834  -18.396 1.00 80.43  ? 20  ASP C CB  1 
ATOM   3913  C CG  . ASP C  1 20  ? -58.593 -48.321  -18.373 1.00 87.78  ? 20  ASP C CG  1 
ATOM   3914  O OD1 . ASP C  1 20  ? -57.848 -47.768  -17.535 1.00 74.75  ? 20  ASP C OD1 1 
ATOM   3915  O OD2 . ASP C  1 20  ? -59.288 -47.684  -19.192 1.00 79.38  ? 20  ASP C OD2 1 
ATOM   3916  N N   . THR C  1 21  ? -59.046 -52.249  -20.702 1.00 66.14  ? 21  THR C N   1 
ATOM   3917  C CA  . THR C  1 21  ? -58.749 -53.647  -20.972 1.00 64.51  ? 21  THR C CA  1 
ATOM   3918  C C   . THR C  1 21  ? -57.313 -53.826  -21.439 1.00 62.59  ? 21  THR C C   1 
ATOM   3919  O O   . THR C  1 21  ? -56.811 -53.056  -22.258 1.00 70.76  ? 21  THR C O   1 
ATOM   3920  C CB  . THR C  1 21  ? -59.701 -54.250  -22.021 1.00 68.96  ? 21  THR C CB  1 
ATOM   3921  O OG1 . THR C  1 21  ? -59.764 -53.390  -23.166 1.00 83.06  ? 21  THR C OG1 1 
ATOM   3922  C CG2 . THR C  1 21  ? -61.093 -54.419  -21.440 1.00 68.80  ? 21  THR C CG2 1 
ATOM   3923  N N   . VAL C  1 22  ? -56.656 -54.847  -20.902 1.00 62.52  ? 22  VAL C N   1 
ATOM   3924  C CA  . VAL C  1 22  ? -55.306 -55.188  -21.316 1.00 46.31  ? 22  VAL C CA  1 
ATOM   3925  C C   . VAL C  1 22  ? -55.258 -56.646  -21.743 1.00 53.84  ? 22  VAL C C   1 
ATOM   3926  O O   . VAL C  1 22  ? -56.200 -57.405  -21.514 1.00 56.66  ? 22  VAL C O   1 
ATOM   3927  C CB  . VAL C  1 22  ? -54.291 -54.976  -20.178 1.00 51.18  ? 22  VAL C CB  1 
ATOM   3928  C CG1 . VAL C  1 22  ? -54.495 -53.616  -19.532 1.00 46.13  ? 22  VAL C CG1 1 
ATOM   3929  C CG2 . VAL C  1 22  ? -54.415 -56.084  -19.144 1.00 44.46  ? 22  VAL C CG2 1 
ATOM   3930  N N   . ASP C  1 23  ? -54.153 -57.030  -22.368 1.00 44.92  ? 23  ASP C N   1 
ATOM   3931  C CA  . ASP C  1 23  ? -53.929 -58.414  -22.752 1.00 47.78  ? 23  ASP C CA  1 
ATOM   3932  C C   . ASP C  1 23  ? -52.790 -59.007  -21.952 1.00 44.10  ? 23  ASP C C   1 
ATOM   3933  O O   . ASP C  1 23  ? -51.869 -58.301  -21.547 1.00 39.16  ? 23  ASP C O   1 
ATOM   3934  C CB  . ASP C  1 23  ? -53.584 -58.514  -24.233 1.00 61.65  ? 23  ASP C CB  1 
ATOM   3935  C CG  . ASP C  1 23  ? -54.779 -58.307  -25.121 1.00 74.10  ? 23  ASP C CG  1 
ATOM   3936  O OD1 . ASP C  1 23  ? -55.868 -57.995  -24.594 1.00 86.21  ? 23  ASP C OD1 1 
ATOM   3937  O OD2 . ASP C  1 23  ? -54.624 -58.462  -26.351 1.00 78.29  ? 23  ASP C OD2 1 
ATOM   3938  N N   . THR C  1 24  ? -52.855 -60.314  -21.738 1.00 48.66  ? 24  THR C N   1 
ATOM   3939  C CA  . THR C  1 24  ? -51.770 -61.039  -21.106 1.00 51.32  ? 24  THR C CA  1 
ATOM   3940  C C   . THR C  1 24  ? -51.335 -62.153  -22.045 1.00 49.60  ? 24  THR C C   1 
ATOM   3941  O O   . THR C  1 24  ? -51.871 -62.289  -23.145 1.00 47.75  ? 24  THR C O   1 
ATOM   3942  C CB  . THR C  1 24  ? -52.206 -61.642  -19.762 1.00 66.58  ? 24  THR C CB  1 
ATOM   3943  O OG1 . THR C  1 24  ? -53.150 -62.694  -19.992 1.00 69.14  ? 24  THR C OG1 1 
ATOM   3944  C CG2 . THR C  1 24  ? -52.846 -60.576  -18.886 1.00 55.82  ? 24  THR C CG2 1 
ATOM   3945  N N   . VAL C  1 25  ? -50.364 -62.946  -21.612 1.00 58.28  ? 25  VAL C N   1 
ATOM   3946  C CA  . VAL C  1 25  ? -49.906 -64.081  -22.397 1.00 59.10  ? 25  VAL C CA  1 
ATOM   3947  C C   . VAL C  1 25  ? -50.985 -65.154  -22.416 1.00 60.14  ? 25  VAL C C   1 
ATOM   3948  O O   . VAL C  1 25  ? -51.165 -65.856  -23.411 1.00 54.65  ? 25  VAL C O   1 
ATOM   3949  C CB  . VAL C  1 25  ? -48.628 -64.685  -21.799 1.00 52.41  ? 25  VAL C CB  1 
ATOM   3950  C CG1 . VAL C  1 25  ? -47.859 -65.457  -22.859 1.00 48.05  ? 25  VAL C CG1 1 
ATOM   3951  C CG2 . VAL C  1 25  ? -47.763 -63.590  -21.209 1.00 61.54  ? 25  VAL C CG2 1 
ATOM   3952  N N   . LEU C  1 26  ? -51.710 -65.265  -21.307 1.00 57.46  ? 26  LEU C N   1 
ATOM   3953  C CA  . LEU C  1 26  ? -52.693 -66.328  -21.126 1.00 55.05  ? 26  LEU C CA  1 
ATOM   3954  C C   . LEU C  1 26  ? -54.116 -65.934  -21.506 1.00 60.83  ? 26  LEU C C   1 
ATOM   3955  O O   . LEU C  1 26  ? -54.946 -66.798  -21.786 1.00 59.70  ? 26  LEU C O   1 
ATOM   3956  C CB  . LEU C  1 26  ? -52.687 -66.799  -19.672 1.00 49.88  ? 26  LEU C CB  1 
ATOM   3957  C CG  . LEU C  1 26  ? -51.601 -67.782  -19.232 1.00 57.62  ? 26  LEU C CG  1 
ATOM   3958  C CD1 . LEU C  1 26  ? -50.376 -67.730  -20.136 1.00 66.98  ? 26  LEU C CD1 1 
ATOM   3959  C CD2 . LEU C  1 26  ? -51.234 -67.547  -17.775 1.00 48.14  ? 26  LEU C CD2 1 
ATOM   3960  N N   . GLU C  1 27  ? -54.404 -64.637  -21.510 1.00 64.33  ? 27  GLU C N   1 
ATOM   3961  C CA  . GLU C  1 27  ? -55.780 -64.181  -21.681 1.00 54.59  ? 27  GLU C CA  1 
ATOM   3962  C C   . GLU C  1 27  ? -55.878 -62.860  -22.445 1.00 61.93  ? 27  GLU C C   1 
ATOM   3963  O O   . GLU C  1 27  ? -55.014 -61.994  -22.320 1.00 63.84  ? 27  GLU C O   1 
ATOM   3964  C CB  . GLU C  1 27  ? -56.453 -64.053  -20.312 1.00 70.24  ? 27  GLU C CB  1 
ATOM   3965  C CG  . GLU C  1 27  ? -57.969 -64.087  -20.336 1.00 83.41  ? 27  GLU C CG  1 
ATOM   3966  C CD  . GLU C  1 27  ? -58.554 -64.304  -18.955 1.00 103.48 ? 27  GLU C CD  1 
ATOM   3967  O OE1 . GLU C  1 27  ? -59.761 -64.045  -18.765 1.00 99.92  ? 27  GLU C OE1 1 
ATOM   3968  O OE2 . GLU C  1 27  ? -57.800 -64.733  -18.056 1.00 100.33 ? 27  GLU C OE2 1 
ATOM   3969  N N   . LYS C  1 28  ? -56.940 -62.717  -23.235 1.00 62.99  ? 28  LYS C N   1 
ATOM   3970  C CA  . LYS C  1 28  ? -57.168 -61.502  -24.014 1.00 63.80  ? 28  LYS C CA  1 
ATOM   3971  C C   . LYS C  1 28  ? -58.267 -60.623  -23.420 1.00 62.41  ? 28  LYS C C   1 
ATOM   3972  O O   . LYS C  1 28  ? -59.119 -61.099  -22.670 1.00 70.44  ? 28  LYS C O   1 
ATOM   3973  C CB  . LYS C  1 28  ? -57.509 -61.848  -25.466 1.00 68.59  ? 28  LYS C CB  1 
ATOM   3974  C CG  . LYS C  1 28  ? -56.303 -61.974  -26.382 1.00 71.79  ? 28  LYS C CG  1 
ATOM   3975  C CD  . LYS C  1 28  ? -56.728 -62.282  -27.810 1.00 86.83  ? 28  LYS C CD  1 
ATOM   3976  C CE  . LYS C  1 28  ? -55.601 -62.011  -28.795 1.00 96.39  ? 28  LYS C CE  1 
ATOM   3977  N NZ  . LYS C  1 28  ? -54.350 -62.732  -28.433 1.00 89.24  ? 28  LYS C NZ  1 
ATOM   3978  N N   . ASN C  1 29  ? -58.237 -59.339  -23.769 1.00 70.65  ? 29  ASN C N   1 
ATOM   3979  C CA  . ASN C  1 29  ? -59.224 -58.369  -23.294 1.00 66.79  ? 29  ASN C CA  1 
ATOM   3980  C C   . ASN C  1 29  ? -59.664 -58.582  -21.846 1.00 71.33  ? 29  ASN C C   1 
ATOM   3981  O O   . ASN C  1 29  ? -60.828 -58.879  -21.574 1.00 80.86  ? 29  ASN C O   1 
ATOM   3982  C CB  . ASN C  1 29  ? -60.435 -58.325  -24.232 1.00 70.56  ? 29  ASN C CB  1 
ATOM   3983  C CG  . ASN C  1 29  ? -60.163 -57.529  -25.501 1.00 98.76  ? 29  ASN C CG  1 
ATOM   3984  O OD1 . ASN C  1 29  ? -60.128 -56.300  -25.473 1.00 99.46  ? 29  ASN C OD1 1 
ATOM   3985  N ND2 . ASN C  1 29  ? -59.969 -58.229  -26.620 1.00 99.24  ? 29  ASN C ND2 1 
ATOM   3986  N N   . VAL C  1 30  ? -58.717 -58.431  -20.925 1.00 69.73  ? 30  VAL C N   1 
ATOM   3987  C CA  . VAL C  1 30  ? -58.999 -58.523  -19.498 1.00 56.00  ? 30  VAL C CA  1 
ATOM   3988  C C   . VAL C  1 30  ? -59.192 -57.129  -18.912 1.00 52.51  ? 30  VAL C C   1 
ATOM   3989  O O   . VAL C  1 30  ? -58.307 -56.279  -19.009 1.00 54.72  ? 30  VAL C O   1 
ATOM   3990  C CB  . VAL C  1 30  ? -57.857 -59.228  -18.739 1.00 52.35  ? 30  VAL C CB  1 
ATOM   3991  C CG1 . VAL C  1 30  ? -58.103 -59.175  -17.238 1.00 46.15  ? 30  VAL C CG1 1 
ATOM   3992  C CG2 . VAL C  1 30  ? -57.708 -60.666  -19.215 1.00 54.89  ? 30  VAL C CG2 1 
ATOM   3993  N N   . THR C  1 31  ? -60.352 -56.899  -18.307 1.00 60.21  ? 31  THR C N   1 
ATOM   3994  C CA  . THR C  1 31  ? -60.659 -55.603  -17.713 1.00 65.67  ? 31  THR C CA  1 
ATOM   3995  C C   . THR C  1 31  ? -59.905 -55.400  -16.404 1.00 60.23  ? 31  THR C C   1 
ATOM   3996  O O   . THR C  1 31  ? -59.996 -56.219  -15.490 1.00 72.14  ? 31  THR C O   1 
ATOM   3997  C CB  . THR C  1 31  ? -62.169 -55.440  -17.459 1.00 65.64  ? 31  THR C CB  1 
ATOM   3998  O OG1 . THR C  1 31  ? -62.882 -55.601  -18.692 1.00 56.46  ? 31  THR C OG1 1 
ATOM   3999  C CG2 . THR C  1 31  ? -62.468 -54.065  -16.880 1.00 53.47  ? 31  THR C CG2 1 
ATOM   4000  N N   . VAL C  1 32  ? -59.161 -54.303  -16.319 1.00 55.27  ? 32  VAL C N   1 
ATOM   4001  C CA  . VAL C  1 32  ? -58.385 -53.998  -15.124 1.00 60.73  ? 32  VAL C CA  1 
ATOM   4002  C C   . VAL C  1 32  ? -58.838 -52.690  -14.482 1.00 59.96  ? 32  VAL C C   1 
ATOM   4003  O O   . VAL C  1 32  ? -59.436 -51.837  -15.138 1.00 67.52  ? 32  VAL C O   1 
ATOM   4004  C CB  . VAL C  1 32  ? -56.878 -53.920  -15.432 1.00 60.65  ? 32  VAL C CB  1 
ATOM   4005  C CG1 . VAL C  1 32  ? -56.336 -55.297  -15.790 1.00 51.61  ? 32  VAL C CG1 1 
ATOM   4006  C CG2 . VAL C  1 32  ? -56.613 -52.915  -16.547 1.00 52.70  ? 32  VAL C CG2 1 
ATOM   4007  N N   . THR C  1 33  ? -58.547 -52.542  -13.194 1.00 59.18  ? 33  THR C N   1 
ATOM   4008  C CA  . THR C  1 33  ? -58.938 -51.355  -12.442 1.00 65.84  ? 33  THR C CA  1 
ATOM   4009  C C   . THR C  1 33  ? -58.151 -50.123  -12.881 1.00 64.06  ? 33  THR C C   1 
ATOM   4010  O O   . THR C  1 33  ? -58.702 -49.026  -12.972 1.00 75.75  ? 33  THR C O   1 
ATOM   4011  C CB  . THR C  1 33  ? -58.743 -51.560  -10.927 1.00 62.85  ? 33  THR C CB  1 
ATOM   4012  O OG1 . THR C  1 33  ? -57.362 -51.827  -10.651 1.00 60.60  ? 33  THR C OG1 1 
ATOM   4013  C CG2 . THR C  1 33  ? -59.585 -52.726  -10.435 1.00 67.44  ? 33  THR C CG2 1 
ATOM   4014  N N   . HIS C  1 34  ? -56.863 -50.311  -13.147 1.00 65.45  ? 34  HIS C N   1 
ATOM   4015  C CA  . HIS C  1 34  ? -55.994 -49.208  -13.544 1.00 60.30  ? 34  HIS C CA  1 
ATOM   4016  C C   . HIS C  1 34  ? -54.964 -49.656  -14.577 1.00 65.47  ? 34  HIS C C   1 
ATOM   4017  O O   . HIS C  1 34  ? -54.599 -50.831  -14.633 1.00 63.33  ? 34  HIS C O   1 
ATOM   4018  C CB  . HIS C  1 34  ? -55.285 -48.624  -12.321 1.00 64.94  ? 34  HIS C CB  1 
ATOM   4019  C CG  . HIS C  1 34  ? -56.217 -48.179  -11.239 1.00 81.52  ? 34  HIS C CG  1 
ATOM   4020  N ND1 . HIS C  1 34  ? -56.871 -49.064  -10.407 1.00 72.84  ? 34  HIS C ND1 1 
ATOM   4021  C CD2 . HIS C  1 34  ? -56.603 -46.941  -10.845 1.00 87.40  ? 34  HIS C CD2 1 
ATOM   4022  C CE1 . HIS C  1 34  ? -57.621 -48.391  -9.554  1.00 80.33  ? 34  HIS C CE1 1 
ATOM   4023  N NE2 . HIS C  1 34  ? -57.476 -47.103  -9.797  1.00 97.95  ? 34  HIS C NE2 1 
ATOM   4024  N N   . SER C  1 35  ? -54.497 -48.714  -15.390 1.00 71.46  ? 35  SER C N   1 
ATOM   4025  C CA  . SER C  1 35  ? -53.502 -49.014  -16.415 1.00 63.31  ? 35  SER C CA  1 
ATOM   4026  C C   . SER C  1 35  ? -52.880 -47.748  -16.996 1.00 54.73  ? 35  SER C C   1 
ATOM   4027  O O   . SER C  1 35  ? -53.377 -46.642  -16.784 1.00 67.33  ? 35  SER C O   1 
ATOM   4028  C CB  . SER C  1 35  ? -54.122 -49.850  -17.537 1.00 62.40  ? 35  SER C CB  1 
ATOM   4029  O OG  . SER C  1 35  ? -55.187 -49.156  -18.163 1.00 68.12  ? 35  SER C OG  1 
ATOM   4030  N N   . VAL C  1 36  ? -51.783 -47.924  -17.727 1.00 53.13  ? 36  VAL C N   1 
ATOM   4031  C CA  . VAL C  1 36  ? -51.115 -46.817  -18.399 1.00 59.73  ? 36  VAL C CA  1 
ATOM   4032  C C   . VAL C  1 36  ? -50.777 -47.214  -19.828 1.00 56.04  ? 36  VAL C C   1 
ATOM   4033  O O   . VAL C  1 36  ? -50.616 -48.396  -20.127 1.00 50.71  ? 36  VAL C O   1 
ATOM   4034  C CB  . VAL C  1 36  ? -49.815 -46.414  -17.679 1.00 49.94  ? 36  VAL C CB  1 
ATOM   4035  C CG1 . VAL C  1 36  ? -50.105 -46.019  -16.241 1.00 58.60  ? 36  VAL C CG1 1 
ATOM   4036  C CG2 . VAL C  1 36  ? -48.804 -47.550  -17.733 1.00 52.68  ? 36  VAL C CG2 1 
ATOM   4037  N N   . ASN C  1 37  ? -50.671 -46.228  -20.711 1.00 62.12  ? 37  ASN C N   1 
ATOM   4038  C CA  . ASN C  1 37  ? -50.300 -46.500  -22.092 1.00 61.18  ? 37  ASN C CA  1 
ATOM   4039  C C   . ASN C  1 37  ? -48.815 -46.240  -22.323 1.00 55.47  ? 37  ASN C C   1 
ATOM   4040  O O   . ASN C  1 37  ? -48.316 -45.149  -22.048 1.00 58.26  ? 37  ASN C O   1 
ATOM   4041  C CB  . ASN C  1 37  ? -51.147 -45.669  -23.059 1.00 53.97  ? 37  ASN C CB  1 
ATOM   4042  C CG  . ASN C  1 37  ? -51.126 -46.220  -24.473 1.00 61.99  ? 37  ASN C CG  1 
ATOM   4043  O OD1 . ASN C  1 37  ? -51.622 -45.588  -25.406 1.00 80.03  ? 37  ASN C OD1 1 
ATOM   4044  N ND2 . ASN C  1 37  ? -50.553 -47.407  -24.637 1.00 60.38  ? 37  ASN C ND2 1 
ATOM   4045  N N   . LEU C  1 38  ? -48.112 -47.253  -22.819 1.00 48.03  ? 38  LEU C N   1 
ATOM   4046  C CA  . LEU C  1 38  ? -46.684 -47.136  -23.090 1.00 42.76  ? 38  LEU C CA  1 
ATOM   4047  C C   . LEU C  1 38  ? -46.438 -46.630  -24.507 1.00 40.03  ? 38  LEU C C   1 
ATOM   4048  O O   . LEU C  1 38  ? -45.307 -46.316  -24.880 1.00 42.45  ? 38  LEU C O   1 
ATOM   4049  C CB  . LEU C  1 38  ? -45.989 -48.484  -22.884 1.00 37.92  ? 38  LEU C CB  1 
ATOM   4050  C CG  . LEU C  1 38  ? -45.908 -49.009  -21.448 1.00 35.92  ? 38  LEU C CG  1 
ATOM   4051  C CD1 . LEU C  1 38  ? -45.483 -50.471  -21.431 1.00 54.70  ? 38  LEU C CD1 1 
ATOM   4052  C CD2 . LEU C  1 38  ? -44.959 -48.158  -20.617 1.00 40.51  ? 38  LEU C CD2 1 
ATOM   4053  N N   . LEU C  1 39  ? -47.508 -46.550  -25.291 1.00 46.96  ? 39  LEU C N   1 
ATOM   4054  C CA  . LEU C  1 39  ? -47.410 -46.134  -26.683 1.00 42.67  ? 39  LEU C CA  1 
ATOM   4055  C C   . LEU C  1 39  ? -47.875 -44.696  -26.889 1.00 53.62  ? 39  LEU C C   1 
ATOM   4056  O O   . LEU C  1 39  ? -49.022 -44.355  -26.597 1.00 63.88  ? 39  LEU C O   1 
ATOM   4057  C CB  . LEU C  1 39  ? -48.220 -47.073  -27.577 1.00 46.33  ? 39  LEU C CB  1 
ATOM   4058  C CG  . LEU C  1 39  ? -48.291 -46.678  -29.052 1.00 44.80  ? 39  LEU C CG  1 
ATOM   4059  C CD1 . LEU C  1 39  ? -46.898 -46.591  -29.660 1.00 50.75  ? 39  LEU C CD1 1 
ATOM   4060  C CD2 . LEU C  1 39  ? -49.162 -47.656  -29.820 1.00 50.34  ? 39  LEU C CD2 1 
ATOM   4061  N N   . GLU C  1 40  ? -46.977 -43.859  -27.397 1.00 51.90  ? 40  GLU C N   1 
ATOM   4062  C CA  . GLU C  1 40  ? -47.322 -42.487  -27.741 1.00 51.06  ? 40  GLU C CA  1 
ATOM   4063  C C   . GLU C  1 40  ? -47.881 -42.434  -29.158 1.00 54.41  ? 40  GLU C C   1 
ATOM   4064  O O   . GLU C  1 40  ? -47.248 -42.905  -30.104 1.00 46.86  ? 40  GLU C O   1 
ATOM   4065  C CB  . GLU C  1 40  ? -46.101 -41.575  -27.617 1.00 44.10  ? 40  GLU C CB  1 
ATOM   4066  C CG  . GLU C  1 40  ? -46.378 -40.113  -27.943 1.00 56.90  ? 40  GLU C CG  1 
ATOM   4067  C CD  . GLU C  1 40  ? -47.396 -39.484  -27.009 1.00 71.43  ? 40  GLU C CD  1 
ATOM   4068  O OE1 . GLU C  1 40  ? -47.013 -38.582  -26.234 1.00 74.13  ? 40  GLU C OE1 1 
ATOM   4069  O OE2 . GLU C  1 40  ? -48.577 -39.890  -27.048 1.00 78.51  ? 40  GLU C OE2 1 
ATOM   4070  N N   . ASP C  1 41  ? -49.071 -41.861  -29.298 1.00 58.98  ? 41  ASP C N   1 
ATOM   4071  C CA  . ASP C  1 41  ? -49.749 -41.801  -30.587 1.00 58.00  ? 41  ASP C CA  1 
ATOM   4072  C C   . ASP C  1 41  ? -50.351 -40.423  -30.828 1.00 59.58  ? 41  ASP C C   1 
ATOM   4073  O O   . ASP C  1 41  ? -51.427 -40.302  -31.413 1.00 78.02  ? 41  ASP C O   1 
ATOM   4074  C CB  . ASP C  1 41  ? -50.847 -42.865  -30.654 1.00 67.15  ? 41  ASP C CB  1 
ATOM   4075  C CG  . ASP C  1 41  ? -51.841 -42.750  -29.512 1.00 94.11  ? 41  ASP C CG  1 
ATOM   4076  O OD1 . ASP C  1 41  ? -51.695 -41.830  -28.679 1.00 90.18  ? 41  ASP C OD1 1 
ATOM   4077  O OD2 . ASP C  1 41  ? -52.770 -43.582  -29.445 1.00 95.65  ? 41  ASP C OD2 1 
ATOM   4078  N N   . LYS C  1 42  ? -49.651 -39.387  -30.380 1.00 65.18  ? 42  LYS C N   1 
ATOM   4079  C CA  . LYS C  1 42  ? -50.182 -38.031  -30.438 1.00 64.10  ? 42  LYS C CA  1 
ATOM   4080  C C   . LYS C  1 42  ? -49.079 -36.999  -30.646 1.00 57.98  ? 42  LYS C C   1 
ATOM   4081  O O   . LYS C  1 42  ? -48.238 -36.791  -29.775 1.00 69.26  ? 42  LYS C O   1 
ATOM   4082  C CB  . LYS C  1 42  ? -50.947 -37.723  -29.151 1.00 76.75  ? 42  LYS C CB  1 
ATOM   4083  C CG  . LYS C  1 42  ? -52.258 -36.987  -29.353 1.00 102.84 ? 42  LYS C CG  1 
ATOM   4084  C CD  . LYS C  1 42  ? -53.161 -37.186  -28.149 1.00 120.56 ? 42  LYS C CD  1 
ATOM   4085  C CE  . LYS C  1 42  ? -53.387 -38.668  -27.886 1.00 112.15 ? 42  LYS C CE  1 
ATOM   4086  N NZ  . LYS C  1 42  ? -54.182 -38.905  -26.651 1.00 105.79 ? 42  LYS C NZ  1 
ATOM   4087  N N   . HIS C  1 43  ? -49.092 -36.353  -31.806 1.00 47.85  ? 43  HIS C N   1 
ATOM   4088  C CA  . HIS C  1 43  ? -48.126 -35.307  -32.113 1.00 45.87  ? 43  HIS C CA  1 
ATOM   4089  C C   . HIS C  1 43  ? -48.821 -33.950  -32.102 1.00 54.50  ? 43  HIS C C   1 
ATOM   4090  O O   . HIS C  1 43  ? -50.043 -33.873  -32.220 1.00 55.32  ? 43  HIS C O   1 
ATOM   4091  C CB  . HIS C  1 43  ? -47.498 -35.561  -33.479 1.00 49.99  ? 43  HIS C CB  1 
ATOM   4092  C CG  . HIS C  1 43  ? -48.492 -35.609  -34.595 1.00 56.32  ? 43  HIS C CG  1 
ATOM   4093  N ND1 . HIS C  1 43  ? -48.729 -34.535  -35.427 1.00 59.52  ? 43  HIS C ND1 1 
ATOM   4094  C CD2 . HIS C  1 43  ? -49.324 -36.594  -35.008 1.00 55.47  ? 43  HIS C CD2 1 
ATOM   4095  C CE1 . HIS C  1 43  ? -49.656 -34.861  -36.309 1.00 59.34  ? 43  HIS C CE1 1 
ATOM   4096  N NE2 . HIS C  1 43  ? -50.034 -36.105  -36.077 1.00 56.63  ? 43  HIS C NE2 1 
ATOM   4097  N N   . ASN C  1 44  ? -48.044 -32.880  -31.962 1.00 55.46  ? 44  ASN C N   1 
ATOM   4098  C CA  . ASN C  1 44  ? -48.619 -31.540  -31.895 1.00 52.08  ? 44  ASN C CA  1 
ATOM   4099  C C   . ASN C  1 44  ? -48.863 -30.922  -33.271 1.00 58.56  ? 44  ASN C C   1 
ATOM   4100  O O   . ASN C  1 44  ? -49.365 -29.802  -33.380 1.00 59.40  ? 44  ASN C O   1 
ATOM   4101  C CB  . ASN C  1 44  ? -47.759 -30.617  -31.025 1.00 50.56  ? 44  ASN C CB  1 
ATOM   4102  C CG  . ASN C  1 44  ? -46.368 -30.397  -31.591 1.00 64.52  ? 44  ASN C CG  1 
ATOM   4103  O OD1 . ASN C  1 44  ? -45.543 -29.718  -30.981 1.00 70.11  ? 44  ASN C OD1 1 
ATOM   4104  N ND2 . ASN C  1 44  ? -46.100 -30.969  -32.760 1.00 64.97  ? 44  ASN C ND2 1 
ATOM   4105  N N   . GLY C  1 45  ? -48.509 -31.664  -34.315 1.00 59.07  ? 45  GLY C N   1 
ATOM   4106  C CA  . GLY C  1 45  ? -48.726 -31.222  -35.680 1.00 56.74  ? 45  GLY C CA  1 
ATOM   4107  C C   . GLY C  1 45  ? -47.959 -29.962  -36.030 1.00 55.88  ? 45  GLY C C   1 
ATOM   4108  O O   . GLY C  1 45  ? -48.366 -29.204  -36.909 1.00 50.95  ? 45  GLY C O   1 
ATOM   4109  N N   . LYS C  1 46  ? -46.847 -29.737  -35.338 1.00 64.03  ? 46  LYS C N   1 
ATOM   4110  C CA  . LYS C  1 46  ? -45.997 -28.585  -35.605 1.00 67.06  ? 46  LYS C CA  1 
ATOM   4111  C C   . LYS C  1 46  ? -44.581 -29.030  -35.915 1.00 51.18  ? 46  LYS C C   1 
ATOM   4112  O O   . LYS C  1 46  ? -44.063 -29.953  -35.288 1.00 53.69  ? 46  LYS C O   1 
ATOM   4113  C CB  . LYS C  1 46  ? -45.934 -27.667  -34.387 1.00 72.99  ? 46  LYS C CB  1 
ATOM   4114  C CG  . LYS C  1 46  ? -47.247 -27.075  -33.938 1.00 77.00  ? 46  LYS C CG  1 
ATOM   4115  C CD  . LYS C  1 46  ? -47.098 -26.548  -32.522 1.00 91.79  ? 46  LYS C CD  1 
ATOM   4116  C CE  . LYS C  1 46  ? -48.079 -25.435  -32.229 1.00 102.99 ? 46  LYS C CE  1 
ATOM   4117  N NZ  . LYS C  1 46  ? -48.195 -25.189  -30.765 1.00 99.69  ? 46  LYS C NZ  1 
ATOM   4118  N N   . LEU C  1 47  ? -43.951 -28.364  -36.873 1.00 51.54  ? 47  LEU C N   1 
ATOM   4119  C CA  . LEU C  1 47  ? -42.523 -28.538  -37.086 1.00 48.88  ? 47  LEU C CA  1 
ATOM   4120  C C   . LEU C  1 47  ? -41.777 -27.592  -36.152 1.00 53.42  ? 47  LEU C C   1 
ATOM   4121  O O   . LEU C  1 47  ? -41.566 -26.422  -36.476 1.00 50.82  ? 47  LEU C O   1 
ATOM   4122  C CB  . LEU C  1 47  ? -42.151 -28.267  -38.541 1.00 39.76  ? 47  LEU C CB  1 
ATOM   4123  C CG  . LEU C  1 47  ? -42.808 -29.200  -39.559 1.00 48.63  ? 47  LEU C CG  1 
ATOM   4124  C CD1 . LEU C  1 47  ? -42.141 -29.063  -40.920 1.00 43.63  ? 47  LEU C CD1 1 
ATOM   4125  C CD2 . LEU C  1 47  ? -42.789 -30.649  -39.079 1.00 43.49  ? 47  LEU C CD2 1 
ATOM   4126  N N   . CYS C  1 48  ? -41.390 -28.108  -34.988 1.00 52.81  ? 48  CYS C N   1 
ATOM   4127  C CA  . CYS C  1 48  ? -40.790 -27.297  -33.930 1.00 58.08  ? 48  CYS C CA  1 
ATOM   4128  C C   . CYS C  1 48  ? -39.262 -27.266  -33.983 1.00 57.39  ? 48  CYS C C   1 
ATOM   4129  O O   . CYS C  1 48  ? -38.642 -27.930  -34.817 1.00 53.10  ? 48  CYS C O   1 
ATOM   4130  C CB  . CYS C  1 48  ? -41.236 -27.808  -32.556 1.00 47.11  ? 48  CYS C CB  1 
ATOM   4131  S SG  . CYS C  1 48  ? -43.015 -28.089  -32.383 1.00 85.45  ? 48  CYS C SG  1 
ATOM   4132  N N   . LYS C  1 49  ? -38.664 -26.487  -33.082 1.00 57.26  ? 49  LYS C N   1 
ATOM   4133  C CA  . LYS C  1 49  ? -37.211 -26.403  -32.986 1.00 58.05  ? 49  LYS C CA  1 
ATOM   4134  C C   . LYS C  1 49  ? -36.699 -27.614  -32.229 1.00 49.84  ? 49  LYS C C   1 
ATOM   4135  O O   . LYS C  1 49  ? -37.376 -28.144  -31.346 1.00 55.81  ? 49  LYS C O   1 
ATOM   4136  C CB  . LYS C  1 49  ? -36.764 -25.117  -32.288 1.00 60.74  ? 49  LYS C CB  1 
ATOM   4137  C CG  . LYS C  1 49  ? -37.523 -23.871  -32.715 1.00 64.14  ? 49  LYS C CG  1 
ATOM   4138  C CD  . LYS C  1 49  ? -36.996 -22.630  -32.000 1.00 70.84  ? 49  LYS C CD  1 
ATOM   4139  C CE  . LYS C  1 49  ? -38.119 -21.832  -31.352 1.00 84.53  ? 49  LYS C CE  1 
ATOM   4140  N NZ  . LYS C  1 49  ? -37.584 -20.778  -30.442 1.00 86.73  ? 49  LYS C NZ  1 
ATOM   4141  N N   . LEU C  1 50  ? -35.495 -28.051  -32.572 1.00 58.66  ? 50  LEU C N   1 
ATOM   4142  C CA  . LEU C  1 50  ? -35.036 -29.371  -32.152 1.00 68.54  ? 50  LEU C CA  1 
ATOM   4143  C C   . LEU C  1 50  ? -34.217 -29.422  -30.860 1.00 79.02  ? 50  LEU C C   1 
ATOM   4144  O O   . LEU C  1 50  ? -34.463 -30.260  -30.004 1.00 92.46  ? 50  LEU C O   1 
ATOM   4145  C CB  . LEU C  1 50  ? -34.229 -30.025  -33.277 1.00 56.27  ? 50  LEU C CB  1 
ATOM   4146  C CG  . LEU C  1 50  ? -34.396 -31.530  -33.523 1.00 56.94  ? 50  LEU C CG  1 
ATOM   4147  C CD1 . LEU C  1 50  ? -33.333 -32.074  -34.482 1.00 52.54  ? 50  LEU C CD1 1 
ATOM   4148  C CD2 . LEU C  1 50  ? -34.370 -32.281  -32.215 1.00 60.07  ? 50  LEU C CD2 1 
ATOM   4149  N N   . ARG C  1 51  ? -33.250 -28.525  -30.728 1.00 70.71  ? 51  ARG C N   1 
ATOM   4150  C CA  . ARG C  1 51  ? -32.572 -28.305  -29.454 1.00 82.81  ? 51  ARG C CA  1 
ATOM   4151  C C   . ARG C  1 51  ? -33.208 -27.057  -28.860 1.00 90.65  ? 51  ARG C C   1 
ATOM   4152  O O   . ARG C  1 51  ? -34.126 -27.132  -28.042 1.00 106.13 ? 51  ARG C O   1 
ATOM   4153  C CB  . ARG C  1 51  ? -31.073 -28.055  -29.627 1.00 97.43  ? 51  ARG C CB  1 
ATOM   4154  C CG  . ARG C  1 51  ? -30.418 -28.974  -30.614 1.00 111.49 ? 51  ARG C CG  1 
ATOM   4155  C CD  . ARG C  1 51  ? -28.940 -29.089  -30.334 1.00 145.44 ? 51  ARG C CD  1 
ATOM   4156  N NE  . ARG C  1 51  ? -28.686 -29.739  -29.052 1.00 156.74 ? 51  ARG C NE  1 
ATOM   4157  C CZ  . ARG C  1 51  ? -27.963 -29.208  -28.070 1.00 144.56 ? 51  ARG C CZ  1 
ATOM   4158  N NH1 . ARG C  1 51  ? -27.411 -28.012  -28.217 1.00 132.49 ? 51  ARG C NH1 1 
ATOM   4159  N NH2 . ARG C  1 51  ? -27.787 -29.880  -26.941 1.00 128.22 ? 51  ARG C NH2 1 
ATOM   4160  N N   . GLY C  1 52  ? -32.688 -25.908  -29.281 1.00 76.06  ? 52  GLY C N   1 
ATOM   4161  C CA  . GLY C  1 52  ? -33.276 -24.608  -29.011 1.00 80.27  ? 52  GLY C CA  1 
ATOM   4162  C C   . GLY C  1 52  ? -33.220 -23.782  -30.283 1.00 83.01  ? 52  GLY C C   1 
ATOM   4163  O O   . GLY C  1 52  ? -33.699 -22.650  -30.333 1.00 86.51  ? 52  GLY C O   1 
ATOM   4164  N N   . VAL C  1 53  ? -32.632 -24.366  -31.323 1.00 79.52  ? 53  VAL C N   1 
ATOM   4165  C CA  . VAL C  1 53  ? -32.484 -23.690  -32.609 1.00 59.86  ? 53  VAL C CA  1 
ATOM   4166  C C   . VAL C  1 53  ? -33.518 -24.146  -33.633 1.00 47.91  ? 53  VAL C C   1 
ATOM   4167  O O   . VAL C  1 53  ? -33.901 -25.312  -33.668 1.00 50.80  ? 53  VAL C O   1 
ATOM   4168  C CB  . VAL C  1 53  ? -31.058 -23.858  -33.185 1.00 46.08  ? 53  VAL C CB  1 
ATOM   4169  C CG1 . VAL C  1 53  ? -30.254 -24.846  -32.344 1.00 45.36  ? 53  VAL C CG1 1 
ATOM   4170  C CG2 . VAL C  1 53  ? -31.117 -24.278  -34.643 1.00 45.14  ? 53  VAL C CG2 1 
ATOM   4171  N N   . ALA C  1 54  ? -33.945 -23.216  -34.479 1.00 57.38  ? 54  ALA C N   1 
ATOM   4172  C CA  . ALA C  1 54  ? -35.038 -23.462  -35.412 1.00 58.44  ? 54  ALA C CA  1 
ATOM   4173  C C   . ALA C  1 54  ? -34.609 -24.182  -36.690 1.00 54.03  ? 54  ALA C C   1 
ATOM   4174  O O   . ALA C  1 54  ? -33.440 -24.134  -37.078 1.00 53.79  ? 54  ALA C O   1 
ATOM   4175  C CB  . ALA C  1 54  ? -35.727 -22.152  -35.753 1.00 57.17  ? 54  ALA C CB  1 
ATOM   4176  N N   . PRO C  1 55  ? -35.564 -24.855  -37.351 1.00 48.95  ? 55  PRO C N   1 
ATOM   4177  C CA  . PRO C  1 55  ? -35.301 -25.478  -38.651 1.00 39.36  ? 55  PRO C CA  1 
ATOM   4178  C C   . PRO C  1 55  ? -35.181 -24.431  -39.750 1.00 38.63  ? 55  PRO C C   1 
ATOM   4179  O O   . PRO C  1 55  ? -35.706 -23.326  -39.608 1.00 56.25  ? 55  PRO C O   1 
ATOM   4180  C CB  . PRO C  1 55  ? -36.551 -26.329  -38.887 1.00 42.95  ? 55  PRO C CB  1 
ATOM   4181  C CG  . PRO C  1 55  ? -37.618 -25.651  -38.100 1.00 42.62  ? 55  PRO C CG  1 
ATOM   4182  C CD  . PRO C  1 55  ? -36.927 -25.143  -36.869 1.00 46.32  ? 55  PRO C CD  1 
ATOM   4183  N N   . LEU C  1 56  ? -34.493 -24.778  -40.832 1.00 42.78  ? 56  LEU C N   1 
ATOM   4184  C CA  . LEU C  1 56  ? -34.390 -23.900  -41.989 1.00 43.41  ? 56  LEU C CA  1 
ATOM   4185  C C   . LEU C  1 56  ? -35.486 -24.247  -42.989 1.00 45.09  ? 56  LEU C C   1 
ATOM   4186  O O   . LEU C  1 56  ? -35.415 -25.271  -43.668 1.00 53.99  ? 56  LEU C O   1 
ATOM   4187  C CB  . LEU C  1 56  ? -33.016 -24.038  -42.645 1.00 40.65  ? 56  LEU C CB  1 
ATOM   4188  C CG  . LEU C  1 56  ? -32.761 -23.204  -43.902 1.00 41.81  ? 56  LEU C CG  1 
ATOM   4189  C CD1 . LEU C  1 56  ? -32.819 -21.718  -43.584 1.00 56.58  ? 56  LEU C CD1 1 
ATOM   4190  C CD2 . LEU C  1 56  ? -31.421 -23.571  -44.518 1.00 43.83  ? 56  LEU C CD2 1 
ATOM   4191  N N   . HIS C  1 57  ? -36.505 -23.396  -43.071 1.00 53.14  ? 57  HIS C N   1 
ATOM   4192  C CA  . HIS C  1 57  ? -37.634 -23.643  -43.961 1.00 53.32  ? 57  HIS C CA  1 
ATOM   4193  C C   . HIS C  1 57  ? -37.437 -22.923  -45.290 1.00 50.99  ? 57  HIS C C   1 
ATOM   4194  O O   . HIS C  1 57  ? -37.285 -21.702  -45.328 1.00 55.77  ? 57  HIS C O   1 
ATOM   4195  C CB  . HIS C  1 57  ? -38.942 -23.196  -43.306 1.00 54.14  ? 57  HIS C CB  1 
ATOM   4196  C CG  . HIS C  1 57  ? -40.164 -23.780  -43.941 1.00 61.79  ? 57  HIS C CG  1 
ATOM   4197  N ND1 . HIS C  1 57  ? -40.724 -23.268  -45.091 1.00 61.94  ? 57  HIS C ND1 1 
ATOM   4198  C CD2 . HIS C  1 57  ? -40.937 -24.834  -43.584 1.00 64.12  ? 57  HIS C CD2 1 
ATOM   4199  C CE1 . HIS C  1 57  ? -41.787 -23.982  -45.417 1.00 71.15  ? 57  HIS C CE1 1 
ATOM   4200  N NE2 . HIS C  1 57  ? -41.937 -24.938  -44.520 1.00 66.81  ? 57  HIS C NE2 1 
ATOM   4201  N N   . LEU C  1 58  ? -37.447 -23.686  -46.378 1.00 52.45  ? 58  LEU C N   1 
ATOM   4202  C CA  . LEU C  1 58  ? -37.156 -23.141  -47.700 1.00 66.02  ? 58  LEU C CA  1 
ATOM   4203  C C   . LEU C  1 58  ? -38.409 -22.718  -48.456 1.00 72.90  ? 58  LEU C C   1 
ATOM   4204  O O   . LEU C  1 58  ? -38.325 -22.020  -49.466 1.00 73.69  ? 58  LEU C O   1 
ATOM   4205  C CB  . LEU C  1 58  ? -36.370 -24.153  -48.532 1.00 59.50  ? 58  LEU C CB  1 
ATOM   4206  C CG  . LEU C  1 58  ? -35.057 -24.629  -47.909 1.00 50.67  ? 58  LEU C CG  1 
ATOM   4207  C CD1 . LEU C  1 58  ? -34.315 -25.543  -48.869 1.00 56.19  ? 58  LEU C CD1 1 
ATOM   4208  C CD2 . LEU C  1 58  ? -34.186 -23.453  -47.484 1.00 53.28  ? 58  LEU C CD2 1 
ATOM   4209  N N   . GLY C  1 59  ? -39.569 -23.148  -47.971 1.00 63.57  ? 59  GLY C N   1 
ATOM   4210  C CA  . GLY C  1 59  ? -40.829 -22.785  -48.591 1.00 62.33  ? 59  GLY C CA  1 
ATOM   4211  C C   . GLY C  1 59  ? -40.980 -23.313  -50.005 1.00 74.05  ? 59  GLY C C   1 
ATOM   4212  O O   . GLY C  1 59  ? -41.018 -24.523  -50.224 1.00 84.93  ? 59  GLY C O   1 
ATOM   4213  N N   . LYS C  1 60  ? -41.061 -22.400  -50.967 1.00 79.41  ? 60  LYS C N   1 
ATOM   4214  C CA  . LYS C  1 60  ? -41.299 -22.765  -52.360 1.00 95.58  ? 60  LYS C CA  1 
ATOM   4215  C C   . LYS C  1 60  ? -40.031 -23.258  -53.058 1.00 88.03  ? 60  LYS C C   1 
ATOM   4216  O O   . LYS C  1 60  ? -40.080 -23.709  -54.202 1.00 96.95  ? 60  LYS C O   1 
ATOM   4217  C CB  . LYS C  1 60  ? -41.889 -21.576  -53.125 1.00 96.74  ? 60  LYS C CB  1 
ATOM   4218  C CG  . LYS C  1 60  ? -42.452 -21.928  -54.493 1.00 125.92 ? 60  LYS C CG  1 
ATOM   4219  C CD  . LYS C  1 60  ? -43.651 -22.857  -54.374 1.00 138.24 ? 60  LYS C CD  1 
ATOM   4220  C CE  . LYS C  1 60  ? -44.797 -22.189  -53.630 1.00 149.59 ? 60  LYS C CE  1 
ATOM   4221  N NZ  . LYS C  1 60  ? -45.981 -23.085  -53.515 1.00 134.37 ? 60  LYS C NZ  1 
ATOM   4222  N N   . CYS C  1 61  ? -38.899 -23.175  -52.367 1.00 73.42  ? 61  CYS C N   1 
ATOM   4223  C CA  . CYS C  1 61  ? -37.622 -23.565  -52.957 1.00 68.21  ? 61  CYS C CA  1 
ATOM   4224  C C   . CYS C  1 61  ? -37.066 -24.851  -52.354 1.00 71.75  ? 61  CYS C C   1 
ATOM   4225  O O   . CYS C  1 61  ? -37.477 -25.273  -51.272 1.00 75.46  ? 61  CYS C O   1 
ATOM   4226  C CB  . CYS C  1 61  ? -36.596 -22.440  -52.799 1.00 60.75  ? 61  CYS C CB  1 
ATOM   4227  S SG  . CYS C  1 61  ? -37.037 -20.894  -53.621 1.00 82.35  ? 61  CYS C SG  1 
ATOM   4228  N N   . ASN C  1 62  ? -36.132 -25.472  -53.067 1.00 56.80  ? 62  ASN C N   1 
ATOM   4229  C CA  . ASN C  1 62  ? -35.401 -26.619  -52.546 1.00 62.92  ? 62  ASN C CA  1 
ATOM   4230  C C   . ASN C  1 62  ? -33.941 -26.249  -52.308 1.00 58.89  ? 62  ASN C C   1 
ATOM   4231  O O   . ASN C  1 62  ? -33.504 -25.162  -52.687 1.00 54.82  ? 62  ASN C O   1 
ATOM   4232  C CB  . ASN C  1 62  ? -35.515 -27.821  -53.490 1.00 66.15  ? 62  ASN C CB  1 
ATOM   4233  C CG  . ASN C  1 62  ? -35.010 -27.520  -54.889 1.00 57.55  ? 62  ASN C CG  1 
ATOM   4234  O OD1 . ASN C  1 62  ? -34.194 -26.621  -55.089 1.00 59.16  ? 62  ASN C OD1 1 
ATOM   4235  N ND2 . ASN C  1 62  ? -35.491 -28.280  -55.866 1.00 57.17  ? 62  ASN C ND2 1 
ATOM   4236  N N   . ILE C  1 63  ? -33.191 -27.148  -51.680 1.00 46.78  ? 63  ILE C N   1 
ATOM   4237  C CA  . ILE C  1 63  ? -31.792 -26.886  -51.352 1.00 45.31  ? 63  ILE C CA  1 
ATOM   4238  C C   . ILE C  1 63  ? -31.028 -26.298  -52.537 1.00 41.29  ? 63  ILE C C   1 
ATOM   4239  O O   . ILE C  1 63  ? -30.342 -25.285  -52.403 1.00 43.80  ? 63  ILE C O   1 
ATOM   4240  C CB  . ILE C  1 63  ? -31.078 -28.161  -50.865 1.00 53.32  ? 63  ILE C CB  1 
ATOM   4241  C CG1 . ILE C  1 63  ? -31.765 -28.713  -49.615 1.00 44.87  ? 63  ILE C CG1 1 
ATOM   4242  C CG2 . ILE C  1 63  ? -29.623 -27.870  -50.564 1.00 42.35  ? 63  ILE C CG2 1 
ATOM   4243  C CD1 . ILE C  1 63  ? -31.638 -27.813  -48.405 1.00 56.85  ? 63  ILE C CD1 1 
ATOM   4244  N N   . ALA C  1 64  ? -31.156 -26.934  -53.697 1.00 41.46  ? 64  ALA C N   1 
ATOM   4245  C CA  . ALA C  1 64  ? -30.473 -26.480  -54.903 1.00 45.90  ? 64  ALA C CA  1 
ATOM   4246  C C   . ALA C  1 64  ? -30.737 -25.004  -55.186 1.00 53.02  ? 64  ALA C C   1 
ATOM   4247  O O   . ALA C  1 64  ? -29.805 -24.210  -55.318 1.00 51.68  ? 64  ALA C O   1 
ATOM   4248  C CB  . ALA C  1 64  ? -30.886 -27.330  -56.094 1.00 43.86  ? 64  ALA C CB  1 
ATOM   4249  N N   . GLY C  1 65  ? -32.012 -24.644  -55.280 1.00 46.71  ? 65  GLY C N   1 
ATOM   4250  C CA  . GLY C  1 65  ? -32.397 -23.274  -55.566 1.00 48.73  ? 65  GLY C CA  1 
ATOM   4251  C C   . GLY C  1 65  ? -31.907 -22.296  -54.517 1.00 56.03  ? 65  GLY C C   1 
ATOM   4252  O O   . GLY C  1 65  ? -31.463 -21.195  -54.844 1.00 66.07  ? 65  GLY C O   1 
ATOM   4253  N N   . TRP C  1 66  ? -31.984 -22.699  -53.253 1.00 47.48  ? 66  TRP C N   1 
ATOM   4254  C CA  . TRP C  1 66  ? -31.596 -21.827  -52.149 1.00 54.43  ? 66  TRP C CA  1 
ATOM   4255  C C   . TRP C  1 66  ? -30.110 -21.474  -52.153 1.00 48.15  ? 66  TRP C C   1 
ATOM   4256  O O   . TRP C  1 66  ? -29.746 -20.317  -51.955 1.00 61.08  ? 66  TRP C O   1 
ATOM   4257  C CB  . TRP C  1 66  ? -31.996 -22.441  -50.803 1.00 53.00  ? 66  TRP C CB  1 
ATOM   4258  C CG  . TRP C  1 66  ? -31.289 -21.829  -49.630 1.00 58.85  ? 66  TRP C CG  1 
ATOM   4259  C CD1 . TRP C  1 66  ? -31.381 -20.537  -49.198 1.00 70.35  ? 66  TRP C CD1 1 
ATOM   4260  C CD2 . TRP C  1 66  ? -30.386 -22.488  -48.734 1.00 56.85  ? 66  TRP C CD2 1 
ATOM   4261  N NE1 . TRP C  1 66  ? -30.587 -20.350  -48.092 1.00 62.20  ? 66  TRP C NE1 1 
ATOM   4262  C CE2 . TRP C  1 66  ? -29.967 -21.533  -47.786 1.00 54.35  ? 66  TRP C CE2 1 
ATOM   4263  C CE3 . TRP C  1 66  ? -29.892 -23.792  -48.641 1.00 58.53  ? 66  TRP C CE3 1 
ATOM   4264  C CZ2 . TRP C  1 66  ? -29.076 -21.842  -46.760 1.00 57.57  ? 66  TRP C CZ2 1 
ATOM   4265  C CZ3 . TRP C  1 66  ? -29.007 -24.096  -47.622 1.00 55.23  ? 66  TRP C CZ3 1 
ATOM   4266  C CH2 . TRP C  1 66  ? -28.609 -23.125  -46.695 1.00 52.27  ? 66  TRP C CH2 1 
ATOM   4267  N N   . ILE C  1 67  ? -29.255 -22.467  -52.382 1.00 49.73  ? 67  ILE C N   1 
ATOM   4268  C CA  . ILE C  1 67  ? -27.812 -22.244  -52.335 1.00 57.02  ? 67  ILE C CA  1 
ATOM   4269  C C   . ILE C  1 67  ? -27.285 -21.589  -53.607 1.00 57.53  ? 67  ILE C C   1 
ATOM   4270  O O   . ILE C  1 67  ? -26.399 -20.737  -53.549 1.00 52.26  ? 67  ILE C O   1 
ATOM   4271  C CB  . ILE C  1 67  ? -27.034 -23.549  -52.105 1.00 43.38  ? 67  ILE C CB  1 
ATOM   4272  C CG1 . ILE C  1 67  ? -27.777 -24.456  -51.128 1.00 68.51  ? 67  ILE C CG1 1 
ATOM   4273  C CG2 . ILE C  1 67  ? -25.637 -23.246  -51.589 1.00 46.70  ? 67  ILE C CG2 1 
ATOM   4274  C CD1 . ILE C  1 67  ? -27.067 -25.757  -50.869 1.00 83.07  ? 67  ILE C CD1 1 
ATOM   4275  N N   . LEU C  1 68  ? -27.818 -21.996  -54.754 1.00 54.27  ? 68  LEU C N   1 
ATOM   4276  C CA  . LEU C  1 68  ? -27.397 -21.418  -56.025 1.00 52.66  ? 68  LEU C CA  1 
ATOM   4277  C C   . LEU C  1 68  ? -27.810 -19.956  -56.126 1.00 58.72  ? 68  LEU C C   1 
ATOM   4278  O O   . LEU C  1 68  ? -27.129 -19.150  -56.761 1.00 59.30  ? 68  LEU C O   1 
ATOM   4279  C CB  . LEU C  1 68  ? -27.963 -22.212  -57.205 1.00 44.20  ? 68  LEU C CB  1 
ATOM   4280  C CG  . LEU C  1 68  ? -27.297 -23.558  -57.490 1.00 50.91  ? 68  LEU C CG  1 
ATOM   4281  C CD1 . LEU C  1 68  ? -27.840 -24.158  -58.777 1.00 42.52  ? 68  LEU C CD1 1 
ATOM   4282  C CD2 . LEU C  1 68  ? -25.788 -23.392  -57.574 1.00 36.44  ? 68  LEU C CD2 1 
ATOM   4283  N N   . GLY C  1 69  ? -28.927 -19.619  -55.492 1.00 58.68  ? 69  GLY C N   1 
ATOM   4284  C CA  . GLY C  1 69  ? -29.419 -18.255  -55.494 1.00 60.96  ? 69  GLY C CA  1 
ATOM   4285  C C   . GLY C  1 69  ? -30.457 -18.010  -56.571 1.00 70.33  ? 69  GLY C C   1 
ATOM   4286  O O   . GLY C  1 69  ? -30.440 -16.974  -57.234 1.00 75.04  ? 69  GLY C O   1 
ATOM   4287  N N   . ASN C  1 70  ? -31.358 -18.970  -56.750 1.00 67.65  ? 70  ASN C N   1 
ATOM   4288  C CA  . ASN C  1 70  ? -32.456 -18.815  -57.695 1.00 76.82  ? 70  ASN C CA  1 
ATOM   4289  C C   . ASN C  1 70  ? -33.210 -17.523  -57.402 1.00 85.32  ? 70  ASN C C   1 
ATOM   4290  O O   . ASN C  1 70  ? -33.516 -17.233  -56.245 1.00 75.80  ? 70  ASN C O   1 
ATOM   4291  C CB  . ASN C  1 70  ? -33.400 -20.019  -57.618 1.00 75.76  ? 70  ASN C CB  1 
ATOM   4292  C CG  . ASN C  1 70  ? -34.432 -20.031  -58.733 1.00 79.03  ? 70  ASN C CG  1 
ATOM   4293  O OD1 . ASN C  1 70  ? -35.083 -19.023  -59.007 1.00 79.40  ? 70  ASN C OD1 1 
ATOM   4294  N ND2 . ASN C  1 70  ? -34.594 -21.183  -59.374 1.00 71.23  ? 70  ASN C ND2 1 
ATOM   4295  N N   . PRO C  1 71  ? -33.496 -16.733  -58.448 1.00 97.70  ? 71  PRO C N   1 
ATOM   4296  C CA  . PRO C  1 71  ? -34.183 -15.445  -58.297 1.00 84.66  ? 71  PRO C CA  1 
ATOM   4297  C C   . PRO C  1 71  ? -35.426 -15.538  -57.416 1.00 87.96  ? 71  PRO C C   1 
ATOM   4298  O O   . PRO C  1 71  ? -35.796 -14.558  -56.767 1.00 107.46 ? 71  PRO C O   1 
ATOM   4299  C CB  . PRO C  1 71  ? -34.580 -15.100  -59.732 1.00 87.14  ? 71  PRO C CB  1 
ATOM   4300  C CG  . PRO C  1 71  ? -33.519 -15.729  -60.560 1.00 87.26  ? 71  PRO C CG  1 
ATOM   4301  C CD  . PRO C  1 71  ? -33.130 -17.000  -59.851 1.00 87.07  ? 71  PRO C CD  1 
ATOM   4302  N N   . GLU C  1 72  ? -36.055 -16.709  -57.388 1.00 85.53  ? 72  GLU C N   1 
ATOM   4303  C CA  . GLU C  1 72  ? -37.274 -16.907  -56.605 1.00 94.73  ? 72  GLU C CA  1 
ATOM   4304  C C   . GLU C  1 72  ? -37.044 -17.378  -55.157 1.00 86.67  ? 72  GLU C C   1 
ATOM   4305  O O   . GLU C  1 72  ? -37.994 -17.505  -54.388 1.00 76.42  ? 72  GLU C O   1 
ATOM   4306  C CB  . GLU C  1 72  ? -38.216 -17.886  -57.319 1.00 92.11  ? 72  GLU C CB  1 
ATOM   4307  C CG  . GLU C  1 72  ? -38.617 -17.485  -58.738 1.00 108.93 ? 72  GLU C CG  1 
ATOM   4308  C CD  . GLU C  1 72  ? -39.519 -16.265  -58.774 1.00 125.68 ? 72  GLU C CD  1 
ATOM   4309  O OE1 . GLU C  1 72  ? -40.151 -15.966  -57.740 1.00 123.24 ? 72  GLU C OE1 1 
ATOM   4310  O OE2 . GLU C  1 72  ? -39.597 -15.610  -59.835 1.00 113.44 ? 72  GLU C OE2 1 
ATOM   4311  N N   . CYS C  1 73  ? -35.794 -17.618  -54.778 1.00 92.40  ? 73  CYS C N   1 
ATOM   4312  C CA  . CYS C  1 73  ? -35.485 -18.186  -53.464 1.00 100.69 ? 73  CYS C CA  1 
ATOM   4313  C C   . CYS C  1 73  ? -34.863 -17.162  -52.496 1.00 113.72 ? 73  CYS C C   1 
ATOM   4314  O O   . CYS C  1 73  ? -33.746 -17.343  -52.028 1.00 117.02 ? 73  CYS C O   1 
ATOM   4315  C CB  . CYS C  1 73  ? -34.503 -19.341  -53.656 1.00 83.81  ? 73  CYS C CB  1 
ATOM   4316  S SG  . CYS C  1 73  ? -35.203 -20.812  -54.495 1.00 89.58  ? 73  CYS C SG  1 
ATOM   4317  N N   . GLU C  1 74  ? -35.604 -16.129  -52.133 1.00 132.65 ? 74  GLU C N   1 
ATOM   4318  C CA  . GLU C  1 74  ? -34.985 -14.848  -51.844 1.00 145.27 ? 74  GLU C CA  1 
ATOM   4319  C C   . GLU C  1 74  ? -35.636 -14.355  -50.559 1.00 152.66 ? 74  GLU C C   1 
ATOM   4320  O O   . GLU C  1 74  ? -36.326 -13.318  -50.472 1.00 147.39 ? 74  GLU C O   1 
ATOM   4321  C CB  . GLU C  1 74  ? -35.222 -14.039  -53.099 1.00 146.36 ? 74  GLU C CB  1 
ATOM   4322  C CG  . GLU C  1 74  ? -35.191 -12.553  -53.159 1.00 148.56 ? 74  GLU C CG  1 
ATOM   4323  C CD  . GLU C  1 74  ? -36.077 -12.264  -54.264 1.00 156.83 ? 74  GLU C CD  1 
ATOM   4324  O OE1 . GLU C  1 74  ? -37.202 -12.662  -53.986 1.00 155.39 ? 74  GLU C OE1 1 
ATOM   4325  O OE2 . GLU C  1 74  ? -35.729 -11.824  -55.382 1.00 151.72 ? 74  GLU C OE2 1 
ATOM   4326  N N   . SER C  1 75  ? -35.415 -15.187  -49.546 1.00 150.08 ? 75  SER C N   1 
ATOM   4327  C CA  . SER C  1 75  ? -36.305 -15.227  -48.394 1.00 167.41 ? 75  SER C CA  1 
ATOM   4328  C C   . SER C  1 75  ? -35.846 -14.420  -47.184 1.00 176.91 ? 75  SER C C   1 
ATOM   4329  O O   . SER C  1 75  ? -35.411 -14.965  -46.161 1.00 174.13 ? 75  SER C O   1 
ATOM   4330  C CB  . SER C  1 75  ? -36.585 -16.662  -47.996 1.00 163.26 ? 75  SER C CB  1 
ATOM   4331  O OG  . SER C  1 75  ? -36.492 -17.492  -49.134 1.00 154.09 ? 75  SER C OG  1 
ATOM   4332  N N   . LEU C  1 76  ? -36.020 -13.108  -47.316 1.00 187.83 ? 76  LEU C N   1 
ATOM   4333  C CA  . LEU C  1 76  ? -35.818 -12.138  -46.248 1.00 182.79 ? 76  LEU C CA  1 
ATOM   4334  C C   . LEU C  1 76  ? -34.474 -12.363  -45.574 1.00 184.36 ? 76  LEU C C   1 
ATOM   4335  O O   . LEU C  1 76  ? -34.285 -11.985  -44.436 1.00 179.27 ? 76  LEU C O   1 
ATOM   4336  C CB  . LEU C  1 76  ? -36.937 -12.208  -45.219 1.00 174.35 ? 76  LEU C CB  1 
ATOM   4337  C CG  . LEU C  1 76  ? -37.029 -11.024  -44.260 1.00 158.37 ? 76  LEU C CG  1 
ATOM   4338  C CD1 . LEU C  1 76  ? -37.128 -9.720   -45.036 1.00 131.78 ? 76  LEU C CD1 1 
ATOM   4339  C CD2 . LEU C  1 76  ? -38.206 -11.184  -43.312 1.00 156.42 ? 76  LEU C CD2 1 
ATOM   4340  N N   . SER C  1 77  ? -33.552 -13.009  -46.279 1.00 219.00 ? 77  SER C N   1 
ATOM   4341  C CA  . SER C  1 77  ? -32.111 -12.833  -46.051 1.00 210.81 ? 77  SER C CA  1 
ATOM   4342  C C   . SER C  1 77  ? -31.457 -13.538  -44.837 1.00 195.06 ? 77  SER C C   1 
ATOM   4343  O O   . SER C  1 77  ? -30.233 -13.420  -44.628 1.00 180.10 ? 77  SER C O   1 
ATOM   4344  C CB  . SER C  1 77  ? -31.719 -11.325  -46.201 1.00 199.30 ? 77  SER C CB  1 
ATOM   4345  O OG  . SER C  1 77  ? -31.875 -10.522  -45.036 1.00 169.85 ? 77  SER C OG  1 
ATOM   4346  N N   . THR C  1 78  ? -32.268 -14.316  -44.131 1.00 214.91 ? 78  THR C N   1 
ATOM   4347  C CA  . THR C  1 78  ? -31.893 -15.602  -43.574 1.00 208.83 ? 78  THR C CA  1 
ATOM   4348  C C   . THR C  1 78  ? -31.034 -15.601  -42.315 1.00 201.34 ? 78  THR C C   1 
ATOM   4349  O O   . THR C  1 78  ? -30.989 -14.634  -41.556 1.00 196.18 ? 78  THR C O   1 
ATOM   4350  C CB  . THR C  1 78  ? -30.945 -16.355  -44.538 1.00 197.11 ? 78  THR C CB  1 
ATOM   4351  O OG1 . THR C  1 78  ? -31.010 -15.761  -45.840 1.00 200.86 ? 78  THR C OG1 1 
ATOM   4352  C CG2 . THR C  1 78  ? -31.337 -17.822  -44.633 1.00 144.25 ? 78  THR C CG2 1 
ATOM   4353  N N   . ALA C  1 79  ? -30.368 -16.735  -42.118 1.00 170.19 ? 79  ALA C N   1 
ATOM   4354  C CA  . ALA C  1 79  ? -29.857 -17.160  -40.851 1.00 144.35 ? 79  ALA C CA  1 
ATOM   4355  C C   . ALA C  1 79  ? -28.369 -17.255  -40.482 1.00 124.94 ? 79  ALA C C   1 
ATOM   4356  O O   . ALA C  1 79  ? -27.512 -16.667  -41.147 1.00 118.11 ? 79  ALA C O   1 
ATOM   4357  C CB  . ALA C  1 79  ? -30.519 -18.525  -40.752 1.00 129.00 ? 79  ALA C CB  1 
ATOM   4358  N N   . SER C  1 80  ? -28.095 -17.929  -39.357 1.00 84.71  ? 80  SER C N   1 
ATOM   4359  C CA  . SER C  1 80  ? -26.723 -18.193  -38.913 1.00 80.20  ? 80  SER C CA  1 
ATOM   4360  C C   . SER C  1 80  ? -26.604 -19.663  -38.518 1.00 68.40  ? 80  SER C C   1 
ATOM   4361  O O   . SER C  1 80  ? -25.504 -20.208  -38.408 1.00 67.90  ? 80  SER C O   1 
ATOM   4362  C CB  . SER C  1 80  ? -26.332 -17.309  -37.722 1.00 87.80  ? 80  SER C CB  1 
ATOM   4363  O OG  . SER C  1 80  ? -27.000 -17.703  -36.526 1.00 96.43  ? 80  SER C OG  1 
ATOM   4364  N N   . SER C  1 81  ? -27.751 -20.308  -38.316 1.00 59.45  ? 81  SER C N   1 
ATOM   4365  C CA  . SER C  1 81  ? -27.768 -21.721  -37.940 1.00 52.27  ? 81  SER C CA  1 
ATOM   4366  C C   . SER C  1 81  ? -29.148 -22.386  -38.000 1.00 48.06  ? 81  SER C C   1 
ATOM   4367  O O   . SER C  1 81  ? -30.179 -21.714  -37.968 1.00 45.37  ? 81  SER C O   1 
ATOM   4368  C CB  . SER C  1 81  ? -27.188 -21.888  -36.537 1.00 58.70  ? 81  SER C CB  1 
ATOM   4369  O OG  . SER C  1 81  ? -27.970 -21.200  -35.576 1.00 59.33  ? 81  SER C OG  1 
ATOM   4370  N N   . TRP C  1 82  ? -29.154 -23.715  -38.068 1.00 36.97  ? 82  TRP C N   1 
ATOM   4371  C CA  . TRP C  1 82  ? -30.397 -24.485  -38.048 1.00 46.44  ? 82  TRP C CA  1 
ATOM   4372  C C   . TRP C  1 82  ? -30.171 -25.939  -37.627 1.00 42.39  ? 82  TRP C C   1 
ATOM   4373  O O   . TRP C  1 82  ? -29.138 -26.532  -37.935 1.00 37.11  ? 82  TRP C O   1 
ATOM   4374  C CB  . TRP C  1 82  ? -31.114 -24.422  -39.404 1.00 45.27  ? 82  TRP C CB  1 
ATOM   4375  C CG  . TRP C  1 82  ? -30.270 -24.854  -40.563 1.00 37.59  ? 82  TRP C CG  1 
ATOM   4376  C CD1 . TRP C  1 82  ? -30.079 -26.130  -41.010 1.00 44.40  ? 82  TRP C CD1 1 
ATOM   4377  C CD2 . TRP C  1 82  ? -29.505 -24.008  -41.428 1.00 39.69  ? 82  TRP C CD2 1 
ATOM   4378  N NE1 . TRP C  1 82  ? -29.239 -26.129  -42.097 1.00 40.11  ? 82  TRP C NE1 1 
ATOM   4379  C CE2 . TRP C  1 82  ? -28.872 -24.839  -42.374 1.00 41.38  ? 82  TRP C CE2 1 
ATOM   4380  C CE3 . TRP C  1 82  ? -29.291 -22.628  -41.494 1.00 43.61  ? 82  TRP C CE3 1 
ATOM   4381  C CZ2 . TRP C  1 82  ? -28.041 -24.335  -43.373 1.00 42.77  ? 82  TRP C CZ2 1 
ATOM   4382  C CZ3 . TRP C  1 82  ? -28.466 -22.130  -42.485 1.00 45.39  ? 82  TRP C CZ3 1 
ATOM   4383  C CH2 . TRP C  1 82  ? -27.851 -22.982  -43.412 1.00 37.25  ? 82  TRP C CH2 1 
ATOM   4384  N N   . SER C  1 83  ? -31.143 -26.502  -36.916 1.00 44.39  ? 83  SER C N   1 
ATOM   4385  C CA  . SER C  1 83  ? -31.047 -27.872  -36.422 1.00 42.66  ? 83  SER C CA  1 
ATOM   4386  C C   . SER C  1 83  ? -31.329 -28.881  -37.526 1.00 41.37  ? 83  SER C C   1 
ATOM   4387  O O   . SER C  1 83  ? -30.731 -29.956  -37.567 1.00 42.80  ? 83  SER C O   1 
ATOM   4388  C CB  . SER C  1 83  ? -32.016 -28.082  -35.260 1.00 41.03  ? 83  SER C CB  1 
ATOM   4389  O OG  . SER C  1 83  ? -33.314 -27.623  -35.593 1.00 51.54  ? 83  SER C OG  1 
ATOM   4390  N N   . TYR C  1 84  ? -32.248 -28.529  -38.419 1.00 37.49  ? 84  TYR C N   1 
ATOM   4391  C CA  . TYR C  1 84  ? -32.562 -29.368  -39.567 1.00 35.19  ? 84  TYR C CA  1 
ATOM   4392  C C   . TYR C  1 84  ? -33.183 -28.530  -40.678 1.00 39.70  ? 84  TYR C C   1 
ATOM   4393  O O   . TYR C  1 84  ? -33.456 -27.345  -40.491 1.00 44.90  ? 84  TYR C O   1 
ATOM   4394  C CB  . TYR C  1 84  ? -33.491 -30.517  -39.166 1.00 38.93  ? 84  TYR C CB  1 
ATOM   4395  C CG  . TYR C  1 84  ? -34.853 -30.083  -38.674 1.00 35.60  ? 84  TYR C CG  1 
ATOM   4396  C CD1 . TYR C  1 84  ? -35.958 -30.119  -39.513 1.00 43.01  ? 84  TYR C CD1 1 
ATOM   4397  C CD2 . TYR C  1 84  ? -35.036 -29.646  -37.368 1.00 35.59  ? 84  TYR C CD2 1 
ATOM   4398  C CE1 . TYR C  1 84  ? -37.205 -29.730  -39.068 1.00 42.78  ? 84  TYR C CE1 1 
ATOM   4399  C CE2 . TYR C  1 84  ? -36.281 -29.254  -36.914 1.00 34.51  ? 84  TYR C CE2 1 
ATOM   4400  C CZ  . TYR C  1 84  ? -37.362 -29.298  -37.769 1.00 40.31  ? 84  TYR C CZ  1 
ATOM   4401  O OH  . TYR C  1 84  ? -38.604 -28.908  -37.326 1.00 46.43  ? 84  TYR C OH  1 
ATOM   4402  N N   . ILE C  1 85  ? -33.399 -29.145  -41.834 1.00 33.36  ? 85  ILE C N   1 
ATOM   4403  C CA  . ILE C  1 85  ? -33.940 -28.430  -42.983 1.00 41.21  ? 85  ILE C CA  1 
ATOM   4404  C C   . ILE C  1 85  ? -35.329 -28.934  -43.355 1.00 45.49  ? 85  ILE C C   1 
ATOM   4405  O O   . ILE C  1 85  ? -35.571 -30.140  -43.400 1.00 40.21  ? 85  ILE C O   1 
ATOM   4406  C CB  . ILE C  1 85  ? -33.005 -28.539  -44.202 1.00 38.77  ? 85  ILE C CB  1 
ATOM   4407  C CG1 . ILE C  1 85  ? -31.661 -27.878  -43.893 1.00 31.74  ? 85  ILE C CG1 1 
ATOM   4408  C CG2 . ILE C  1 85  ? -33.644 -27.903  -45.427 1.00 39.38  ? 85  ILE C CG2 1 
ATOM   4409  C CD1 . ILE C  1 85  ? -30.640 -28.024  -44.997 1.00 37.21  ? 85  ILE C CD1 1 
ATOM   4410  N N   . VAL C  1 86  ? -36.238 -28.001  -43.616 1.00 42.34  ? 86  VAL C N   1 
ATOM   4411  C CA  . VAL C  1 86  ? -37.596 -28.346  -44.015 1.00 45.24  ? 86  VAL C CA  1 
ATOM   4412  C C   . VAL C  1 86  ? -37.864 -27.957  -45.464 1.00 42.73  ? 86  VAL C C   1 
ATOM   4413  O O   . VAL C  1 86  ? -37.648 -26.813  -45.864 1.00 50.93  ? 86  VAL C O   1 
ATOM   4414  C CB  . VAL C  1 86  ? -38.643 -27.669  -43.113 1.00 43.91  ? 86  VAL C CB  1 
ATOM   4415  C CG1 . VAL C  1 86  ? -40.042 -28.076  -43.539 1.00 39.84  ? 86  VAL C CG1 1 
ATOM   4416  C CG2 . VAL C  1 86  ? -38.402 -28.032  -41.660 1.00 46.89  ? 86  VAL C CG2 1 
ATOM   4417  N N   . GLU C  1 87  ? -38.333 -28.924  -46.243 1.00 43.79  ? 87  GLU C N   1 
ATOM   4418  C CA  . GLU C  1 87  ? -38.682 -28.698  -47.637 1.00 48.38  ? 87  GLU C CA  1 
ATOM   4419  C C   . GLU C  1 87  ? -40.153 -29.038  -47.830 1.00 62.58  ? 87  GLU C C   1 
ATOM   4420  O O   . GLU C  1 87  ? -40.636 -30.036  -47.298 1.00 59.41  ? 87  GLU C O   1 
ATOM   4421  C CB  . GLU C  1 87  ? -37.824 -29.583  -48.541 1.00 50.98  ? 87  GLU C CB  1 
ATOM   4422  C CG  . GLU C  1 87  ? -37.099 -28.847  -49.653 1.00 63.08  ? 87  GLU C CG  1 
ATOM   4423  C CD  . GLU C  1 87  ? -36.165 -29.755  -50.429 1.00 63.35  ? 87  GLU C CD  1 
ATOM   4424  O OE1 . GLU C  1 87  ? -35.091 -29.283  -50.855 1.00 62.66  ? 87  GLU C OE1 1 
ATOM   4425  O OE2 . GLU C  1 87  ? -36.500 -30.946  -50.603 1.00 55.70  ? 87  GLU C OE2 1 
ATOM   4426  N N   . THR C  1 88  ? -40.870 -28.209  -48.579 1.00 67.74  ? 88  THR C N   1 
ATOM   4427  C CA  . THR C  1 88  ? -42.271 -28.489  -48.866 1.00 69.07  ? 88  THR C CA  1 
ATOM   4428  C C   . THR C  1 88  ? -42.377 -29.373  -50.101 1.00 74.46  ? 88  THR C C   1 
ATOM   4429  O O   . THR C  1 88  ? -41.610 -29.212  -51.050 1.00 83.76  ? 88  THR C O   1 
ATOM   4430  C CB  . THR C  1 88  ? -43.085 -27.199  -49.083 1.00 80.47  ? 88  THR C CB  1 
ATOM   4431  O OG1 . THR C  1 88  ? -42.664 -26.561  -50.295 1.00 89.31  ? 88  THR C OG1 1 
ATOM   4432  C CG2 . THR C  1 88  ? -42.894 -26.244  -47.913 1.00 68.19  ? 88  THR C CG2 1 
ATOM   4433  N N   . PRO C  1 89  ? -43.328 -30.318  -50.090 1.00 95.65  ? 89  PRO C N   1 
ATOM   4434  C CA  . PRO C  1 89  ? -43.523 -31.235  -51.218 1.00 95.87  ? 89  PRO C CA  1 
ATOM   4435  C C   . PRO C  1 89  ? -43.822 -30.482  -52.510 1.00 102.49 ? 89  PRO C C   1 
ATOM   4436  O O   . PRO C  1 89  ? -43.766 -31.066  -53.592 1.00 103.29 ? 89  PRO C O   1 
ATOM   4437  C CB  . PRO C  1 89  ? -44.747 -32.053  -50.795 1.00 86.31  ? 89  PRO C CB  1 
ATOM   4438  C CG  . PRO C  1 89  ? -44.778 -31.955  -49.307 1.00 88.18  ? 89  PRO C CG  1 
ATOM   4439  C CD  . PRO C  1 89  ? -44.269 -30.584  -48.990 1.00 96.80  ? 89  PRO C CD  1 
ATOM   4440  N N   . SER C  1 90  ? -44.131 -29.195  -52.392 1.00 96.33  ? 90  SER C N   1 
ATOM   4441  C CA  . SER C  1 90  ? -44.507 -28.385  -53.545 1.00 102.20 ? 90  SER C CA  1 
ATOM   4442  C C   . SER C  1 90  ? -43.421 -27.378  -53.916 1.00 113.48 ? 90  SER C C   1 
ATOM   4443  O O   . SER C  1 90  ? -43.700 -26.352  -54.536 1.00 127.64 ? 90  SER C O   1 
ATOM   4444  C CB  . SER C  1 90  ? -45.825 -27.658  -53.270 1.00 116.08 ? 90  SER C CB  1 
ATOM   4445  O OG  . SER C  1 90  ? -46.283 -26.973  -54.422 1.00 137.75 ? 90  SER C OG  1 
ATOM   4446  N N   . SER C  1 91  ? -42.183 -27.676  -53.534 1.00 113.87 ? 91  SER C N   1 
ATOM   4447  C CA  . SER C  1 91  ? -41.057 -26.799  -53.840 1.00 105.25 ? 91  SER C CA  1 
ATOM   4448  C C   . SER C  1 91  ? -40.315 -27.285  -55.081 1.00 110.06 ? 91  SER C C   1 
ATOM   4449  O O   . SER C  1 91  ? -39.737 -28.372  -55.083 1.00 104.59 ? 91  SER C O   1 
ATOM   4450  C CB  . SER C  1 91  ? -40.099 -26.722  -52.650 1.00 91.83  ? 91  SER C CB  1 
ATOM   4451  O OG  . SER C  1 91  ? -39.570 -27.999  -52.339 1.00 91.57  ? 91  SER C OG  1 
ATOM   4452  N N   . ASP C  1 92  ? -40.331 -26.475  -56.135 1.00 120.19 ? 92  ASP C N   1 
ATOM   4453  C CA  . ASP C  1 92  ? -39.732 -26.869  -57.407 1.00 127.60 ? 92  ASP C CA  1 
ATOM   4454  C C   . ASP C  1 92  ? -38.779 -25.820  -57.964 1.00 116.55 ? 92  ASP C C   1 
ATOM   4455  O O   . ASP C  1 92  ? -38.171 -26.017  -59.018 1.00 125.53 ? 92  ASP C O   1 
ATOM   4456  C CB  . ASP C  1 92  ? -40.820 -27.171  -58.436 1.00 144.54 ? 92  ASP C CB  1 
ATOM   4457  C CG  . ASP C  1 92  ? -41.637 -28.391  -58.073 1.00 152.85 ? 92  ASP C CG  1 
ATOM   4458  O OD1 . ASP C  1 92  ? -41.140 -29.229  -57.292 1.00 154.86 ? 92  ASP C OD1 1 
ATOM   4459  O OD2 . ASP C  1 92  ? -42.776 -28.514  -58.569 1.00 153.50 ? 92  ASP C OD2 1 
ATOM   4460  N N   . ASN C  1 93  ? -38.655 -24.702  -57.262 1.00 100.23 ? 93  ASN C N   1 
ATOM   4461  C CA  . ASN C  1 93  ? -37.727 -23.663  -57.682 1.00 107.49 ? 93  ASN C CA  1 
ATOM   4462  C C   . ASN C  1 93  ? -36.286 -23.993  -57.296 1.00 94.55  ? 93  ASN C C   1 
ATOM   4463  O O   . ASN C  1 93  ? -35.760 -23.476  -56.309 1.00 83.40  ? 93  ASN C O   1 
ATOM   4464  C CB  . ASN C  1 93  ? -38.159 -22.298  -57.142 1.00 103.90 ? 93  ASN C CB  1 
ATOM   4465  C CG  . ASN C  1 93  ? -39.278 -21.679  -57.965 1.00 108.05 ? 93  ASN C CG  1 
ATOM   4466  O OD1 . ASN C  1 93  ? -40.300 -21.252  -57.428 1.00 110.59 ? 93  ASN C OD1 1 
ATOM   4467  N ND2 . ASN C  1 93  ? -39.084 -21.633  -59.283 1.00 103.89 ? 93  ASN C ND2 1 
ATOM   4468  N N   . GLY C  1 94  ? -35.665 -24.866  -58.088 1.00 92.74  ? 94  GLY C N   1 
ATOM   4469  C CA  . GLY C  1 94  ? -34.283 -25.269  -57.890 1.00 81.93  ? 94  GLY C CA  1 
ATOM   4470  C C   . GLY C  1 94  ? -33.404 -24.839  -59.050 1.00 84.27  ? 94  GLY C C   1 
ATOM   4471  O O   . GLY C  1 94  ? -33.156 -23.648  -59.234 1.00 86.79  ? 94  GLY C O   1 
ATOM   4472  N N   . THR C  1 95  ? -32.936 -25.802  -59.839 1.00 68.80  ? 95  THR C N   1 
ATOM   4473  C CA  . THR C  1 95  ? -32.156 -25.482  -61.028 1.00 72.93  ? 95  THR C CA  1 
ATOM   4474  C C   . THR C  1 95  ? -33.062 -24.983  -62.148 1.00 69.27  ? 95  THR C C   1 
ATOM   4475  O O   . THR C  1 95  ? -33.696 -25.776  -62.844 1.00 72.64  ? 95  THR C O   1 
ATOM   4476  C CB  . THR C  1 95  ? -31.355 -26.697  -61.530 1.00 58.89  ? 95  THR C CB  1 
ATOM   4477  O OG1 . THR C  1 95  ? -30.529 -27.195  -60.470 1.00 47.55  ? 95  THR C OG1 1 
ATOM   4478  N N   . CYS C  1 96  ? -33.128 -23.665  -62.310 1.00 68.23  ? 96  CYS C N   1 
ATOM   4479  C CA  . CYS C  1 96  ? -33.867 -23.079  -63.420 1.00 66.21  ? 96  CYS C CA  1 
ATOM   4480  C C   . CYS C  1 96  ? -33.186 -23.379  -64.755 1.00 63.28  ? 96  CYS C C   1 
ATOM   4481  O O   . CYS C  1 96  ? -33.855 -23.516  -65.779 1.00 62.91  ? 96  CYS C O   1 
ATOM   4482  C CB  . CYS C  1 96  ? -34.058 -21.574  -63.218 1.00 64.46  ? 96  CYS C CB  1 
ATOM   4483  S SG  . CYS C  1 96  ? -32.599 -20.690  -62.612 1.00 82.91  ? 96  CYS C SG  1 
ATOM   4484  N N   . TYR C  1 97  ? -31.860 -23.495  -64.741 1.00 60.32  ? 97  TYR C N   1 
ATOM   4485  C CA  . TYR C  1 97  ? -31.130 -23.886  -65.943 1.00 58.85  ? 97  TYR C CA  1 
ATOM   4486  C C   . TYR C  1 97  ? -30.825 -25.384  -65.917 1.00 56.31  ? 97  TYR C C   1 
ATOM   4487  O O   . TYR C  1 97  ? -30.163 -25.876  -65.003 1.00 61.17  ? 97  TYR C O   1 
ATOM   4488  C CB  . TYR C  1 97  ? -29.844 -23.070  -66.112 1.00 60.38  ? 97  TYR C CB  1 
ATOM   4489  C CG  . TYR C  1 97  ? -29.286 -23.122  -67.519 1.00 60.33  ? 97  TYR C CG  1 
ATOM   4490  C CD1 . TYR C  1 97  ? -29.144 -21.970  -68.281 1.00 64.34  ? 97  TYR C CD1 1 
ATOM   4491  C CD2 . TYR C  1 97  ? -28.923 -24.330  -68.092 1.00 62.42  ? 97  TYR C CD2 1 
ATOM   4492  C CE1 . TYR C  1 97  ? -28.643 -22.027  -69.570 1.00 77.05  ? 97  TYR C CE1 1 
ATOM   4493  C CE2 . TYR C  1 97  ? -28.427 -24.396  -69.373 1.00 60.05  ? 97  TYR C CE2 1 
ATOM   4494  C CZ  . TYR C  1 97  ? -28.286 -23.245  -70.108 1.00 66.55  ? 97  TYR C CZ  1 
ATOM   4495  O OH  . TYR C  1 97  ? -27.785 -23.327  -71.386 1.00 63.57  ? 97  TYR C OH  1 
ATOM   4496  N N   . PRO C  1 98  ? -31.320 -26.116  -66.924 1.00 60.97  ? 98  PRO C N   1 
ATOM   4497  C CA  . PRO C  1 98  ? -31.165 -27.573  -66.988 1.00 48.93  ? 98  PRO C CA  1 
ATOM   4498  C C   . PRO C  1 98  ? -29.715 -27.989  -66.801 1.00 61.90  ? 98  PRO C C   1 
ATOM   4499  O O   . PRO C  1 98  ? -28.816 -27.340  -67.333 1.00 68.19  ? 98  PRO C O   1 
ATOM   4500  C CB  . PRO C  1 98  ? -31.612 -27.910  -68.411 1.00 50.45  ? 98  PRO C CB  1 
ATOM   4501  C CG  . PRO C  1 98  ? -32.526 -26.814  -68.786 1.00 68.10  ? 98  PRO C CG  1 
ATOM   4502  C CD  . PRO C  1 98  ? -32.014 -25.581  -68.107 1.00 70.15  ? 98  PRO C CD  1 
ATOM   4503  N N   . GLY C  1 99  ? -29.494 -29.067  -66.059 1.00 60.61  ? 99  GLY C N   1 
ATOM   4504  C CA  . GLY C  1 99  ? -28.150 -29.550  -65.812 1.00 53.70  ? 99  GLY C CA  1 
ATOM   4505  C C   . GLY C  1 99  ? -28.092 -30.516  -64.649 1.00 61.85  ? 99  GLY C C   1 
ATOM   4506  O O   . GLY C  1 99  ? -29.101 -30.781  -63.995 1.00 49.85  ? 99  GLY C O   1 
ATOM   4507  N N   . ASP C  1 100 ? -26.900 -31.040  -64.387 1.00 69.36  ? 100 ASP C N   1 
ATOM   4508  C CA  . ASP C  1 100 ? -26.712 -32.013  -63.322 1.00 60.40  ? 100 ASP C CA  1 
ATOM   4509  C C   . ASP C  1 100 ? -26.044 -31.375  -62.109 1.00 54.85  ? 100 ASP C C   1 
ATOM   4510  O O   . ASP C  1 100 ? -25.054 -30.657  -62.241 1.00 60.01  ? 100 ASP C O   1 
ATOM   4511  C CB  . ASP C  1 100 ? -25.874 -33.190  -63.825 1.00 63.13  ? 100 ASP C CB  1 
ATOM   4512  C CG  . ASP C  1 100 ? -25.949 -34.394  -62.909 1.00 88.68  ? 100 ASP C CG  1 
ATOM   4513  O OD1 . ASP C  1 100 ? -26.894 -34.465  -62.096 1.00 99.48  ? 100 ASP C OD1 1 
ATOM   4514  O OD2 . ASP C  1 100 ? -25.066 -35.272  -63.007 1.00 91.72  ? 100 ASP C OD2 1 
ATOM   4515  N N   . PHE C  1 101 ? -26.596 -31.635  -60.928 1.00 37.89  ? 101 PHE C N   1 
ATOM   4516  C CA  . PHE C  1 101 ? -26.000 -31.164  -59.685 1.00 44.63  ? 101 PHE C CA  1 
ATOM   4517  C C   . PHE C  1 101 ? -25.172 -32.292  -59.082 1.00 44.26  ? 101 PHE C C   1 
ATOM   4518  O O   . PHE C  1 101 ? -25.709 -33.189  -58.433 1.00 50.90  ? 101 PHE C O   1 
ATOM   4519  C CB  . PHE C  1 101 ? -27.084 -30.721  -58.701 1.00 39.61  ? 101 PHE C CB  1 
ATOM   4520  C CG  . PHE C  1 101 ? -26.615 -29.704  -57.698 1.00 41.14  ? 101 PHE C CG  1 
ATOM   4521  C CD1 . PHE C  1 101 ? -27.242 -28.473  -57.597 1.00 43.17  ? 101 PHE C CD1 1 
ATOM   4522  C CD2 . PHE C  1 101 ? -25.544 -29.973  -56.862 1.00 44.32  ? 101 PHE C CD2 1 
ATOM   4523  C CE1 . PHE C  1 101 ? -26.815 -27.533  -56.678 1.00 33.95  ? 101 PHE C CE1 1 
ATOM   4524  C CE2 . PHE C  1 101 ? -25.111 -29.036  -55.942 1.00 41.71  ? 101 PHE C CE2 1 
ATOM   4525  C CZ  . PHE C  1 101 ? -25.748 -27.815  -55.851 1.00 28.98  ? 101 PHE C CZ  1 
ATOM   4526  N N   . ILE C  1 102 ? -23.863 -32.243  -59.302 1.00 36.90  ? 102 ILE C N   1 
ATOM   4527  C CA  . ILE C  1 102 ? -22.970 -33.318  -58.881 1.00 37.79  ? 102 ILE C CA  1 
ATOM   4528  C C   . ILE C  1 102 ? -22.942 -33.484  -57.365 1.00 36.08  ? 102 ILE C C   1 
ATOM   4529  O O   . ILE C  1 102 ? -22.771 -32.513  -56.628 1.00 42.24  ? 102 ILE C O   1 
ATOM   4530  C CB  . ILE C  1 102 ? -21.538 -33.082  -59.391 1.00 52.38  ? 102 ILE C CB  1 
ATOM   4531  C CG1 . ILE C  1 102 ? -21.559 -32.736  -60.880 1.00 50.82  ? 102 ILE C CG1 1 
ATOM   4532  C CG2 . ILE C  1 102 ? -20.665 -34.300  -59.121 1.00 38.87  ? 102 ILE C CG2 1 
ATOM   4533  C CD1 . ILE C  1 102 ? -22.179 -33.805  -61.751 1.00 49.39  ? 102 ILE C CD1 1 
ATOM   4534  N N   . ASP C  1 103 ? -23.107 -34.723  -56.909 1.00 44.52  ? 103 ASP C N   1 
ATOM   4535  C CA  . ASP C  1 103 ? -23.100 -35.025  -55.481 1.00 42.80  ? 103 ASP C CA  1 
ATOM   4536  C C   . ASP C  1 103 ? -24.095 -34.146  -54.733 1.00 41.19  ? 103 ASP C C   1 
ATOM   4537  O O   . ASP C  1 103 ? -23.783 -33.599  -53.674 1.00 41.74  ? 103 ASP C O   1 
ATOM   4538  C CB  . ASP C  1 103 ? -21.695 -34.844  -54.901 1.00 46.62  ? 103 ASP C CB  1 
ATOM   4539  C CG  . ASP C  1 103 ? -20.687 -35.804  -55.502 1.00 47.94  ? 103 ASP C CG  1 
ATOM   4540  O OD1 . ASP C  1 103 ? -21.088 -36.918  -55.899 1.00 50.23  ? 103 ASP C OD1 1 
ATOM   4541  O OD2 . ASP C  1 103 ? -19.492 -35.447  -55.573 1.00 57.90  ? 103 ASP C OD2 1 
ATOM   4542  N N   . TYR C  1 104 ? -25.293 -34.015  -55.292 1.00 35.15  ? 104 TYR C N   1 
ATOM   4543  C CA  . TYR C  1 104 ? -26.325 -33.158  -54.722 1.00 35.39  ? 104 TYR C CA  1 
ATOM   4544  C C   . TYR C  1 104 ? -26.830 -33.684  -53.382 1.00 38.84  ? 104 TYR C C   1 
ATOM   4545  O O   . TYR C  1 104 ? -26.893 -32.945  -52.399 1.00 39.97  ? 104 TYR C O   1 
ATOM   4546  C CB  . TYR C  1 104 ? -27.487 -33.005  -55.706 1.00 32.41  ? 104 TYR C CB  1 
ATOM   4547  C CG  . TYR C  1 104 ? -28.632 -32.168  -55.184 1.00 34.60  ? 104 TYR C CG  1 
ATOM   4548  C CD1 . TYR C  1 104 ? -28.409 -30.904  -54.656 1.00 32.29  ? 104 TYR C CD1 1 
ATOM   4549  C CD2 . TYR C  1 104 ? -29.939 -32.636  -55.233 1.00 31.96  ? 104 TYR C CD2 1 
ATOM   4550  C CE1 . TYR C  1 104 ? -29.453 -30.134  -54.180 1.00 34.66  ? 104 TYR C CE1 1 
ATOM   4551  C CE2 . TYR C  1 104 ? -30.990 -31.873  -54.762 1.00 39.06  ? 104 TYR C CE2 1 
ATOM   4552  C CZ  . TYR C  1 104 ? -30.742 -30.623  -54.237 1.00 34.98  ? 104 TYR C CZ  1 
ATOM   4553  O OH  . TYR C  1 104 ? -31.785 -29.858  -53.768 1.00 47.32  ? 104 TYR C OH  1 
ATOM   4554  N N   . GLU C  1 105 ? -27.189 -34.963  -53.347 1.00 32.66  ? 105 GLU C N   1 
ATOM   4555  C CA  . GLU C  1 105 ? -27.696 -35.575  -52.125 1.00 37.91  ? 105 GLU C CA  1 
ATOM   4556  C C   . GLU C  1 105 ? -26.669 -35.461  -51.005 1.00 41.04  ? 105 GLU C C   1 
ATOM   4557  O O   . GLU C  1 105 ? -27.023 -35.287  -49.840 1.00 38.04  ? 105 GLU C O   1 
ATOM   4558  C CB  . GLU C  1 105 ? -28.063 -37.041  -52.360 1.00 35.75  ? 105 GLU C CB  1 
ATOM   4559  C CG  . GLU C  1 105 ? -29.081 -37.262  -53.466 1.00 34.76  ? 105 GLU C CG  1 
ATOM   4560  C CD  . GLU C  1 105 ? -28.500 -37.027  -54.846 1.00 58.36  ? 105 GLU C CD  1 
ATOM   4561  O OE1 . GLU C  1 105 ? -27.299 -37.308  -55.040 1.00 63.99  ? 105 GLU C OE1 1 
ATOM   4562  O OE2 . GLU C  1 105 ? -29.243 -36.565  -55.738 1.00 44.43  ? 105 GLU C OE2 1 
ATOM   4563  N N   . GLU C  1 106 ? -25.393 -35.557  -51.363 1.00 40.11  ? 106 GLU C N   1 
ATOM   4564  C CA  . GLU C  1 106 ? -24.321 -35.381  -50.392 1.00 35.12  ? 106 GLU C CA  1 
ATOM   4565  C C   . GLU C  1 106 ? -24.318 -33.963  -49.832 1.00 36.73  ? 106 GLU C C   1 
ATOM   4566  O O   . GLU C  1 106 ? -24.237 -33.768  -48.621 1.00 38.53  ? 106 GLU C O   1 
ATOM   4567  C CB  . GLU C  1 106 ? -22.964 -35.721  -51.010 1.00 33.19  ? 106 GLU C CB  1 
ATOM   4568  C CG  . GLU C  1 106 ? -22.618 -37.200  -50.948 1.00 60.45  ? 106 GLU C CG  1 
ATOM   4569  C CD  . GLU C  1 106 ? -22.356 -37.680  -49.529 1.00 54.38  ? 106 GLU C CD  1 
ATOM   4570  O OE1 . GLU C  1 106 ? -21.737 -36.926  -48.747 1.00 53.09  ? 106 GLU C OE1 1 
ATOM   4571  O OE2 . GLU C  1 106 ? -22.764 -38.813  -49.197 1.00 42.47  ? 106 GLU C OE2 1 
ATOM   4572  N N   . LEU C  1 107 ? -24.417 -32.977  -50.717 1.00 47.22  ? 107 LEU C N   1 
ATOM   4573  C CA  . LEU C  1 107 ? -24.446 -31.581  -50.300 1.00 46.24  ? 107 LEU C CA  1 
ATOM   4574  C C   . LEU C  1 107 ? -25.583 -31.327  -49.317 1.00 39.75  ? 107 LEU C C   1 
ATOM   4575  O O   . LEU C  1 107 ? -25.398 -30.673  -48.289 1.00 42.21  ? 107 LEU C O   1 
ATOM   4576  C CB  . LEU C  1 107 ? -24.594 -30.666  -51.516 1.00 38.19  ? 107 LEU C CB  1 
ATOM   4577  C CG  . LEU C  1 107 ? -24.536 -29.168  -51.219 1.00 40.53  ? 107 LEU C CG  1 
ATOM   4578  C CD1 . LEU C  1 107 ? -23.234 -28.796  -50.520 1.00 38.85  ? 107 LEU C CD1 1 
ATOM   4579  C CD2 . LEU C  1 107 ? -24.726 -28.365  -52.493 1.00 44.24  ? 107 LEU C CD2 1 
ATOM   4580  N N   . ARG C  1 108 ? -26.760 -31.850  -49.643 1.00 30.91  ? 108 ARG C N   1 
ATOM   4581  C CA  . ARG C  1 108 ? -27.936 -31.697  -48.797 1.00 41.46  ? 108 ARG C CA  1 
ATOM   4582  C C   . ARG C  1 108 ? -27.686 -32.268  -47.407 1.00 37.97  ? 108 ARG C C   1 
ATOM   4583  O O   . ARG C  1 108 ? -28.041 -31.655  -46.401 1.00 37.89  ? 108 ARG C O   1 
ATOM   4584  C CB  . ARG C  1 108 ? -29.142 -32.389  -49.435 1.00 35.61  ? 108 ARG C CB  1 
ATOM   4585  C CG  . ARG C  1 108 ? -29.538 -31.831  -50.791 1.00 39.60  ? 108 ARG C CG  1 
ATOM   4586  C CD  . ARG C  1 108 ? -30.551 -32.732  -51.478 1.00 46.20  ? 108 ARG C CD  1 
ATOM   4587  N NE  . ARG C  1 108 ? -31.760 -32.914  -50.680 1.00 51.37  ? 108 ARG C NE  1 
ATOM   4588  C CZ  . ARG C  1 108 ? -32.870 -32.197  -50.826 1.00 45.94  ? 108 ARG C CZ  1 
ATOM   4589  N NH1 . ARG C  1 108 ? -32.932 -31.244  -51.744 1.00 42.38  ? 108 ARG C NH1 1 
ATOM   4590  N NH2 . ARG C  1 108 ? -33.921 -32.435  -50.053 1.00 38.56  ? 108 ARG C NH2 1 
ATOM   4591  N N   . GLU C  1 109 ? -27.072 -33.447  -47.359 1.00 43.88  ? 109 GLU C N   1 
ATOM   4592  C CA  . GLU C  1 109 ? -26.777 -34.110  -46.094 1.00 42.05  ? 109 GLU C CA  1 
ATOM   4593  C C   . GLU C  1 109 ? -25.835 -33.272  -45.237 1.00 39.31  ? 109 GLU C C   1 
ATOM   4594  O O   . GLU C  1 109 ? -25.998 -33.186  -44.019 1.00 33.30  ? 109 GLU C O   1 
ATOM   4595  C CB  . GLU C  1 109 ? -26.165 -35.490  -46.348 1.00 36.89  ? 109 GLU C CB  1 
ATOM   4596  C CG  . GLU C  1 109 ? -25.841 -36.279  -45.087 1.00 54.44  ? 109 GLU C CG  1 
ATOM   4597  C CD  . GLU C  1 109 ? -27.082 -36.760  -44.358 1.00 69.92  ? 109 GLU C CD  1 
ATOM   4598  O OE1 . GLU C  1 109 ? -28.197 -36.336  -44.728 1.00 81.20  ? 109 GLU C OE1 1 
ATOM   4599  O OE2 . GLU C  1 109 ? -26.941 -37.565  -43.414 1.00 66.61  ? 109 GLU C OE2 1 
ATOM   4600  N N   . GLN C  1 110 ? -24.850 -32.656  -45.883 1.00 35.55  ? 110 GLN C N   1 
ATOM   4601  C CA  . GLN C  1 110 ? -23.867 -31.834  -45.186 1.00 42.42  ? 110 GLN C CA  1 
ATOM   4602  C C   . GLN C  1 110 ? -24.488 -30.527  -44.700 1.00 52.12  ? 110 GLN C C   1 
ATOM   4603  O O   . GLN C  1 110 ? -24.109 -30.002  -43.653 1.00 58.52  ? 110 GLN C O   1 
ATOM   4604  C CB  . GLN C  1 110 ? -22.675 -31.537  -46.100 1.00 41.54  ? 110 GLN C CB  1 
ATOM   4605  C CG  . GLN C  1 110 ? -22.199 -32.733  -46.907 1.00 46.40  ? 110 GLN C CG  1 
ATOM   4606  C CD  . GLN C  1 110 ? -20.779 -33.142  -46.580 1.00 56.38  ? 110 GLN C CD  1 
ATOM   4607  O OE1 . GLN C  1 110 ? -20.153 -32.592  -45.674 1.00 68.45  ? 110 GLN C OE1 1 
ATOM   4608  N NE2 . GLN C  1 110 ? -20.261 -34.117  -47.319 1.00 50.71  ? 110 GLN C NE2 1 
ATOM   4609  N N   . LEU C  1 111 ? -25.441 -30.006  -45.466 1.00 50.77  ? 111 LEU C N   1 
ATOM   4610  C CA  . LEU C  1 111 ? -26.113 -28.756  -45.120 1.00 34.40  ? 111 LEU C CA  1 
ATOM   4611  C C   . LEU C  1 111 ? -27.262 -28.968  -44.139 1.00 36.04  ? 111 LEU C C   1 
ATOM   4612  O O   . LEU C  1 111 ? -27.801 -28.008  -43.589 1.00 43.78  ? 111 LEU C O   1 
ATOM   4613  C CB  . LEU C  1 111 ? -26.648 -28.074  -46.380 1.00 40.62  ? 111 LEU C CB  1 
ATOM   4614  C CG  . LEU C  1 111 ? -25.889 -26.861  -46.922 1.00 39.17  ? 111 LEU C CG  1 
ATOM   4615  C CD1 . LEU C  1 111 ? -24.752 -26.459  -45.998 1.00 56.06  ? 111 LEU C CD1 1 
ATOM   4616  C CD2 . LEU C  1 111 ? -25.379 -27.136  -48.322 1.00 36.03  ? 111 LEU C CD2 1 
ATOM   4617  N N   . SER C  1 112 ? -27.632 -30.227  -43.925 1.00 41.31  ? 112 SER C N   1 
ATOM   4618  C CA  . SER C  1 112 ? -28.802 -30.564  -43.119 1.00 40.55  ? 112 SER C CA  1 
ATOM   4619  C C   . SER C  1 112 ? -28.803 -29.873  -41.757 1.00 35.95  ? 112 SER C C   1 
ATOM   4620  O O   . SER C  1 112 ? -29.852 -29.458  -41.264 1.00 44.38  ? 112 SER C O   1 
ATOM   4621  C CB  . SER C  1 112 ? -28.913 -32.079  -42.942 1.00 46.00  ? 112 SER C CB  1 
ATOM   4622  O OG  . SER C  1 112 ? -27.886 -32.569  -42.100 1.00 41.23  ? 112 SER C OG  1 
ATOM   4623  N N   . SER C  1 113 ? -27.629 -29.756  -41.147 1.00 41.13  ? 113 SER C N   1 
ATOM   4624  C CA  . SER C  1 113 ? -27.504 -29.039  -39.884 1.00 46.60  ? 113 SER C CA  1 
ATOM   4625  C C   . SER C  1 113 ? -26.232 -28.203  -39.859 1.00 56.14  ? 113 SER C C   1 
ATOM   4626  O O   . SER C  1 113 ? -25.134 -28.708  -40.102 1.00 52.56  ? 113 SER C O   1 
ATOM   4627  C CB  . SER C  1 113 ? -27.532 -30.007  -38.701 1.00 54.88  ? 113 SER C CB  1 
ATOM   4628  O OG  . SER C  1 113 ? -27.605 -29.307  -37.471 1.00 46.78  ? 113 SER C OG  1 
ATOM   4629  N N   . VAL C  1 114 ? -26.392 -26.918  -39.562 1.00 51.69  ? 114 VAL C N   1 
ATOM   4630  C CA  . VAL C  1 114 ? -25.289 -25.972  -39.610 1.00 56.16  ? 114 VAL C CA  1 
ATOM   4631  C C   . VAL C  1 114 ? -25.187 -25.180  -38.312 1.00 55.76  ? 114 VAL C C   1 
ATOM   4632  O O   . VAL C  1 114 ? -26.188 -24.683  -37.795 1.00 54.30  ? 114 VAL C O   1 
ATOM   4633  C CB  . VAL C  1 114 ? -25.448 -25.009  -40.803 1.00 57.90  ? 114 VAL C CB  1 
ATOM   4634  C CG1 . VAL C  1 114 ? -25.390 -23.557  -40.341 1.00 58.67  ? 114 VAL C CG1 1 
ATOM   4635  C CG2 . VAL C  1 114 ? -24.401 -25.308  -41.874 1.00 50.54  ? 114 VAL C CG2 1 
ATOM   4636  N N   . SER C  1 115 ? -23.973 -25.076  -37.783 1.00 62.04  ? 115 SER C N   1 
ATOM   4637  C CA  . SER C  1 115 ? -23.746 -24.369  -36.530 1.00 72.42  ? 115 SER C CA  1 
ATOM   4638  C C   . SER C  1 115 ? -23.672 -22.864  -36.766 1.00 69.32  ? 115 SER C C   1 
ATOM   4639  O O   . SER C  1 115 ? -24.347 -22.086  -36.092 1.00 77.39  ? 115 SER C O   1 
ATOM   4640  C CB  . SER C  1 115 ? -22.467 -24.867  -35.857 1.00 76.00  ? 115 SER C CB  1 
ATOM   4641  O OG  . SER C  1 115 ? -22.427 -24.473  -34.498 1.00 82.91  ? 115 SER C OG  1 
ATOM   4642  N N   . SER C  1 116 ? -22.839 -22.461  -37.721 1.00 66.73  ? 116 SER C N   1 
ATOM   4643  C CA  . SER C  1 116 ? -22.779 -21.069  -38.156 1.00 74.64  ? 116 SER C CA  1 
ATOM   4644  C C   . SER C  1 116 ? -22.709 -21.013  -39.677 1.00 80.09  ? 116 SER C C   1 
ATOM   4645  O O   . SER C  1 116 ? -22.044 -21.835  -40.306 1.00 81.50  ? 116 SER C O   1 
ATOM   4646  C CB  . SER C  1 116 ? -21.595 -20.332  -37.526 1.00 75.66  ? 116 SER C CB  1 
ATOM   4647  O OG  . SER C  1 116 ? -20.360 -20.887  -37.939 1.00 98.23  ? 116 SER C OG  1 
ATOM   4648  N N   . PHE C  1 117 ? -23.402 -20.042  -40.262 1.00 70.60  ? 117 PHE C N   1 
ATOM   4649  C CA  . PHE C  1 117 ? -23.584 -19.993  -41.706 1.00 58.59  ? 117 PHE C CA  1 
ATOM   4650  C C   . PHE C  1 117 ? -23.692 -18.550  -42.177 1.00 55.22  ? 117 PHE C C   1 
ATOM   4651  O O   . PHE C  1 117 ? -24.729 -17.910  -42.002 1.00 63.07  ? 117 PHE C O   1 
ATOM   4652  C CB  . PHE C  1 117 ? -24.855 -20.758  -42.089 1.00 55.05  ? 117 PHE C CB  1 
ATOM   4653  C CG  . PHE C  1 117 ? -24.978 -21.055  -43.560 1.00 51.45  ? 117 PHE C CG  1 
ATOM   4654  C CD1 . PHE C  1 117 ? -25.595 -20.157  -44.416 1.00 41.85  ? 117 PHE C CD1 1 
ATOM   4655  C CD2 . PHE C  1 117 ? -24.494 -22.244  -44.083 1.00 48.74  ? 117 PHE C CD2 1 
ATOM   4656  C CE1 . PHE C  1 117 ? -25.716 -20.434  -45.769 1.00 40.97  ? 117 PHE C CE1 1 
ATOM   4657  C CE2 . PHE C  1 117 ? -24.611 -22.527  -45.434 1.00 51.83  ? 117 PHE C CE2 1 
ATOM   4658  C CZ  . PHE C  1 117 ? -25.223 -21.620  -46.278 1.00 53.12  ? 117 PHE C CZ  1 
ATOM   4659  N N   . GLU C  1 118 ? -22.620 -18.034  -42.769 1.00 61.41  ? 118 GLU C N   1 
ATOM   4660  C CA  . GLU C  1 118 ? -22.654 -16.685  -43.322 1.00 68.45  ? 118 GLU C CA  1 
ATOM   4661  C C   . GLU C  1 118 ? -22.310 -16.672  -44.809 1.00 55.81  ? 118 GLU C C   1 
ATOM   4662  O O   . GLU C  1 118 ? -21.428 -17.400  -45.266 1.00 56.30  ? 118 GLU C O   1 
ATOM   4663  C CB  . GLU C  1 118 ? -21.733 -15.739  -42.547 1.00 81.68  ? 118 GLU C CB  1 
ATOM   4664  C CG  . GLU C  1 118 ? -20.276 -15.800  -42.965 1.00 90.17  ? 118 GLU C CG  1 
ATOM   4665  C CD  . GLU C  1 118 ? -19.545 -14.497  -42.706 1.00 110.01 ? 118 GLU C CD  1 
ATOM   4666  O OE1 . GLU C  1 118 ? -20.166 -13.564  -42.153 1.00 126.39 ? 118 GLU C OE1 1 
ATOM   4667  O OE2 . GLU C  1 118 ? -18.351 -14.404  -43.059 1.00 101.73 ? 118 GLU C OE2 1 
ATOM   4668  N N   . ARG C  1 119 ? -23.021 -15.833  -45.553 1.00 59.40  ? 119 ARG C N   1 
ATOM   4669  C CA  . ARG C  1 119 ? -22.864 -15.739  -46.997 1.00 55.90  ? 119 ARG C CA  1 
ATOM   4670  C C   . ARG C  1 119 ? -22.098 -14.475  -47.372 1.00 52.31  ? 119 ARG C C   1 
ATOM   4671  O O   . ARG C  1 119 ? -22.587 -13.362  -47.180 1.00 64.83  ? 119 ARG C O   1 
ATOM   4672  C CB  . ARG C  1 119 ? -24.241 -15.750  -47.664 1.00 57.71  ? 119 ARG C CB  1 
ATOM   4673  C CG  . ARG C  1 119 ? -24.268 -15.272  -49.106 1.00 59.35  ? 119 ARG C CG  1 
ATOM   4674  C CD  . ARG C  1 119 ? -25.705 -15.176  -49.605 1.00 70.20  ? 119 ARG C CD  1 
ATOM   4675  N NE  . ARG C  1 119 ? -25.808 -14.420  -50.851 1.00 77.07  ? 119 ARG C NE  1 
ATOM   4676  C CZ  . ARG C  1 119 ? -25.995 -13.105  -50.922 1.00 86.32  ? 119 ARG C CZ  1 
ATOM   4677  N NH1 . ARG C  1 119 ? -26.103 -12.375  -49.818 1.00 93.53  ? 119 ARG C NH1 1 
ATOM   4678  N NH2 . ARG C  1 119 ? -26.073 -12.517  -52.106 1.00 84.40  ? 119 ARG C NH2 1 
ATOM   4679  N N   . PHE C  1 120 ? -20.894 -14.653  -47.904 1.00 54.17  ? 120 PHE C N   1 
ATOM   4680  C CA  . PHE C  1 120 ? -20.045 -13.523  -48.258 1.00 55.07  ? 120 PHE C CA  1 
ATOM   4681  C C   . PHE C  1 120 ? -19.675 -13.546  -49.735 1.00 52.81  ? 120 PHE C C   1 
ATOM   4682  O O   . PHE C  1 120 ? -19.637 -14.605  -50.360 1.00 51.99  ? 120 PHE C O   1 
ATOM   4683  C CB  . PHE C  1 120 ? -18.774 -13.519  -47.406 1.00 56.06  ? 120 PHE C CB  1 
ATOM   4684  C CG  . PHE C  1 120 ? -17.837 -14.656  -47.708 1.00 58.08  ? 120 PHE C CG  1 
ATOM   4685  C CD1 . PHE C  1 120 ? -16.756 -14.474  -48.555 1.00 61.18  ? 120 PHE C CD1 1 
ATOM   4686  C CD2 . PHE C  1 120 ? -18.037 -15.904  -47.144 1.00 68.37  ? 120 PHE C CD2 1 
ATOM   4687  C CE1 . PHE C  1 120 ? -15.891 -15.517  -48.832 1.00 53.85  ? 120 PHE C CE1 1 
ATOM   4688  C CE2 . PHE C  1 120 ? -17.177 -16.951  -47.418 1.00 61.78  ? 120 PHE C CE2 1 
ATOM   4689  C CZ  . PHE C  1 120 ? -16.102 -16.757  -48.263 1.00 55.07  ? 120 PHE C CZ  1 
ATOM   4690  N N   . GLU C  1 121 ? -19.401 -12.369  -50.288 1.00 60.85  ? 121 GLU C N   1 
ATOM   4691  C CA  . GLU C  1 121 ? -18.989 -12.265  -51.679 1.00 57.13  ? 121 GLU C CA  1 
ATOM   4692  C C   . GLU C  1 121 ? -17.526 -12.670  -51.818 1.00 60.64  ? 121 GLU C C   1 
ATOM   4693  O O   . GLU C  1 121 ? -16.625 -11.926  -51.428 1.00 71.85  ? 121 GLU C O   1 
ATOM   4694  C CB  . GLU C  1 121 ? -19.203 -10.842  -52.198 1.00 67.84  ? 121 GLU C CB  1 
ATOM   4695  C CG  . GLU C  1 121 ? -19.166 -10.718  -53.713 1.00 82.20  ? 121 GLU C CG  1 
ATOM   4696  C CD  . GLU C  1 121 ? -19.492 -9.316   -54.190 1.00 91.64  ? 121 GLU C CD  1 
ATOM   4697  O OE1 . GLU C  1 121 ? -19.447 -8.379   -53.365 1.00 95.13  ? 121 GLU C OE1 1 
ATOM   4698  O OE2 . GLU C  1 121 ? -19.801 -9.151   -55.390 1.00 88.57  ? 121 GLU C OE2 1 
ATOM   4699  N N   . ILE C  1 122 ? -17.297 -13.859  -52.366 1.00 62.95  ? 122 ILE C N   1 
ATOM   4700  C CA  . ILE C  1 122 ? -15.944 -14.377  -52.541 1.00 62.15  ? 122 ILE C CA  1 
ATOM   4701  C C   . ILE C  1 122 ? -15.241 -13.702  -53.715 1.00 72.90  ? 122 ILE C C   1 
ATOM   4702  O O   . ILE C  1 122 ? -14.054 -13.382  -53.641 1.00 66.79  ? 122 ILE C O   1 
ATOM   4703  C CB  . ILE C  1 122 ? -15.948 -15.908  -52.734 1.00 58.28  ? 122 ILE C CB  1 
ATOM   4704  C CG1 . ILE C  1 122 ? -14.535 -16.417  -53.023 1.00 57.97  ? 122 ILE C CG1 1 
ATOM   4705  C CG2 . ILE C  1 122 ? -16.904 -16.306  -53.849 1.00 57.72  ? 122 ILE C CG2 1 
ATOM   4706  C CD1 . ILE C  1 122 ? -14.453 -17.917  -53.193 1.00 52.47  ? 122 ILE C CD1 1 
ATOM   4707  N N   . PHE C  1 123 ? -15.980 -13.486  -54.798 1.00 76.13  ? 123 PHE C N   1 
ATOM   4708  C CA  . PHE C  1 123 ? -15.460 -12.755  -55.945 1.00 59.89  ? 123 PHE C CA  1 
ATOM   4709  C C   . PHE C  1 123 ? -16.403 -11.618  -56.325 1.00 74.75  ? 123 PHE C C   1 
ATOM   4710  O O   . PHE C  1 123 ? -17.377 -11.833  -57.045 1.00 69.12  ? 123 PHE C O   1 
ATOM   4711  C CB  . PHE C  1 123 ? -15.259 -13.685  -57.145 1.00 61.32  ? 123 PHE C CB  1 
ATOM   4712  C CG  . PHE C  1 123 ? -14.240 -14.764  -56.916 1.00 63.22  ? 123 PHE C CG  1 
ATOM   4713  C CD1 . PHE C  1 123 ? -14.589 -16.099  -57.030 1.00 65.09  ? 123 PHE C CD1 1 
ATOM   4714  C CD2 . PHE C  1 123 ? -12.935 -14.444  -56.584 1.00 68.39  ? 123 PHE C CD2 1 
ATOM   4715  C CE1 . PHE C  1 123 ? -13.654 -17.095  -56.821 1.00 62.28  ? 123 PHE C CE1 1 
ATOM   4716  C CE2 . PHE C  1 123 ? -11.995 -15.436  -56.372 1.00 71.73  ? 123 PHE C CE2 1 
ATOM   4717  C CZ  . PHE C  1 123 ? -12.356 -16.763  -56.491 1.00 62.87  ? 123 PHE C CZ  1 
ATOM   4718  N N   . PRO C  1 124 ? -16.119 -10.402  -55.834 1.00 86.75  ? 124 PRO C N   1 
ATOM   4719  C CA  . PRO C  1 124 ? -16.924 -9.221   -56.172 1.00 84.86  ? 124 PRO C CA  1 
ATOM   4720  C C   . PRO C  1 124 ? -17.034 -9.034   -57.683 1.00 88.05  ? 124 PRO C C   1 
ATOM   4721  O O   . PRO C  1 124 ? -16.021 -9.133   -58.370 1.00 82.30  ? 124 PRO C O   1 
ATOM   4722  C CB  . PRO C  1 124 ? -16.123 -8.069   -55.562 1.00 96.24  ? 124 PRO C CB  1 
ATOM   4723  C CG  . PRO C  1 124 ? -15.344 -8.692   -54.457 1.00 95.24  ? 124 PRO C CG  1 
ATOM   4724  C CD  . PRO C  1 124 ? -15.008 -10.077  -54.923 1.00 85.67  ? 124 PRO C CD  1 
ATOM   4725  N N   . LYS C  1 125 ? -18.235 -8.756   -58.184 1.00 84.73  ? 125 LYS C N   1 
ATOM   4726  C CA  . LYS C  1 125 ? -18.479 -8.692   -59.623 1.00 94.64  ? 125 LYS C CA  1 
ATOM   4727  C C   . LYS C  1 125 ? -17.647 -7.631   -60.346 1.00 107.18 ? 125 LYS C C   1 
ATOM   4728  O O   . LYS C  1 125 ? -17.331 -7.787   -61.528 1.00 94.10  ? 125 LYS C O   1 
ATOM   4729  C CB  . LYS C  1 125 ? -19.969 -8.465   -59.904 1.00 85.31  ? 125 LYS C CB  1 
ATOM   4730  C CG  . LYS C  1 125 ? -20.335 -8.519   -61.376 1.00 92.60  ? 125 LYS C CG  1 
ATOM   4731  C CD  . LYS C  1 125 ? -21.831 -8.691   -61.597 1.00 88.24  ? 125 LYS C CD  1 
ATOM   4732  C CE  . LYS C  1 125 ? -22.622 -7.477   -61.134 1.00 93.39  ? 125 LYS C CE  1 
ATOM   4733  N NZ  . LYS C  1 125 ? -24.077 -7.603   -61.446 1.00 91.10  ? 125 LYS C NZ  1 
ATOM   4734  N N   . THR C  1 126 ? -17.270 -6.569   -59.639 1.00 165.26 ? 126 THR C N   1 
ATOM   4735  C CA  . THR C  1 126 ? -16.721 -5.368   -60.282 1.00 165.27 ? 126 THR C CA  1 
ATOM   4736  C C   . THR C  1 126 ? -15.216 -5.129   -60.182 1.00 168.19 ? 126 THR C C   1 
ATOM   4737  O O   . THR C  1 126 ? -14.749 -4.038   -60.501 1.00 180.38 ? 126 THR C O   1 
ATOM   4738  C CB  . THR C  1 126 ? -17.329 -4.118   -59.629 1.00 131.02 ? 126 THR C CB  1 
ATOM   4739  O OG1 . THR C  1 126 ? -17.616 -4.398   -58.249 1.00 120.19 ? 126 THR C OG1 1 
ATOM   4740  N N   . SER C  1 127 ? -14.459 -6.110   -59.725 1.00 109.53 ? 127 SER C N   1 
ATOM   4741  C CA  . SER C  1 127 ? -13.047 -5.889   -59.520 1.00 100.50 ? 127 SER C CA  1 
ATOM   4742  C C   . SER C  1 127 ? -12.362 -7.197   -59.902 1.00 95.51  ? 127 SER C C   1 
ATOM   4743  O O   . SER C  1 127 ? -11.224 -7.230   -60.379 1.00 104.72 ? 127 SER C O   1 
ATOM   4744  C CB  . SER C  1 127 ? -12.797 -5.452   -58.078 1.00 105.83 ? 127 SER C CB  1 
ATOM   4745  O OG  . SER C  1 127 ? -13.360 -6.375   -57.159 1.00 92.94  ? 127 SER C OG  1 
ATOM   4746  N N   . SER C  1 128 ? -13.115 -8.277   -59.740 1.00 95.04  ? 128 SER C N   1 
ATOM   4747  C CA  . SER C  1 128 ? -12.822 -9.531   -60.405 1.00 84.18  ? 128 SER C CA  1 
ATOM   4748  C C   . SER C  1 128 ? -13.375 -9.324   -61.807 1.00 86.22  ? 128 SER C C   1 
ATOM   4749  O O   . SER C  1 128 ? -14.231 -8.465   -62.024 1.00 88.23  ? 128 SER C O   1 
ATOM   4750  C CB  . SER C  1 128 ? -13.446 -10.693  -59.635 1.00 79.97  ? 128 SER C CB  1 
ATOM   4751  O OG  . SER C  1 128 ? -13.460 -10.393  -58.247 1.00 79.29  ? 128 SER C OG  1 
ATOM   4752  N N   . TRP C  1 129 ? -12.872 -10.101  -62.760 1.00 91.74  ? 129 TRP C N   1 
ATOM   4753  C CA  . TRP C  1 129 ? -13.360 -10.076  -64.141 1.00 91.22  ? 129 TRP C CA  1 
ATOM   4754  C C   . TRP C  1 129 ? -13.285 -8.729   -64.878 1.00 88.69  ? 129 TRP C C   1 
ATOM   4755  O O   . TRP C  1 129 ? -14.311 -8.198   -65.297 1.00 90.43  ? 129 TRP C O   1 
ATOM   4756  C CB  . TRP C  1 129 ? -14.812 -10.574  -64.120 1.00 96.61  ? 129 TRP C CB  1 
ATOM   4757  C CG  . TRP C  1 129 ? -15.110 -11.522  -62.993 1.00 81.89  ? 129 TRP C CG  1 
ATOM   4758  C CD1 . TRP C  1 129 ? -16.163 -11.463  -62.129 1.00 71.79  ? 129 TRP C CD1 1 
ATOM   4759  C CD2 . TRP C  1 129 ? -14.337 -12.664  -62.609 1.00 77.33  ? 129 TRP C CD2 1 
ATOM   4760  N NE1 . TRP C  1 129 ? -16.099 -12.506  -61.237 1.00 75.79  ? 129 TRP C NE1 1 
ATOM   4761  C CE2 . TRP C  1 129 ? -14.987 -13.257  -61.510 1.00 72.65  ? 129 TRP C CE2 1 
ATOM   4762  C CE3 . TRP C  1 129 ? -13.161 -13.246  -63.092 1.00 73.88  ? 129 TRP C CE3 1 
ATOM   4763  C CZ2 . TRP C  1 129 ? -14.501 -14.400  -60.886 1.00 78.52  ? 129 TRP C CZ2 1 
ATOM   4764  C CZ3 . TRP C  1 129 ? -12.681 -14.378  -62.474 1.00 64.18  ? 129 TRP C CZ3 1 
ATOM   4765  C CH2 . TRP C  1 129 ? -13.350 -14.945  -61.381 1.00 73.96  ? 129 TRP C CH2 1 
ATOM   4766  N N   . PRO C  1 130 ? -12.072 -8.173   -65.040 1.00 99.00  ? 130 PRO C N   1 
ATOM   4767  C CA  . PRO C  1 130 ? -11.898 -6.923   -65.790 1.00 98.15  ? 130 PRO C CA  1 
ATOM   4768  C C   . PRO C  1 130 ? -11.692 -7.191   -67.275 1.00 99.92  ? 130 PRO C C   1 
ATOM   4769  O O   . PRO C  1 130 ? -11.672 -6.259   -68.079 1.00 104.00 ? 130 PRO C O   1 
ATOM   4770  C CB  . PRO C  1 130 ? -10.604 -6.343   -65.207 1.00 98.63  ? 130 PRO C CB  1 
ATOM   4771  C CG  . PRO C  1 130 ? -10.217 -7.253   -64.064 1.00 96.85  ? 130 PRO C CG  1 
ATOM   4772  C CD  . PRO C  1 130 ? -10.828 -8.569   -64.369 1.00 106.56 ? 130 PRO C CD  1 
ATOM   4773  N N   . ASN C  1 131 ? -11.520 -8.461   -67.623 1.00 104.90 ? 131 ASN C N   1 
ATOM   4774  C CA  . ASN C  1 131 ? -11.278 -8.863   -69.002 1.00 107.80 ? 131 ASN C CA  1 
ATOM   4775  C C   . ASN C  1 131 ? -12.446 -9.655   -69.574 1.00 98.24  ? 131 ASN C C   1 
ATOM   4776  O O   . ASN C  1 131 ? -12.360 -10.199  -70.674 1.00 91.28  ? 131 ASN C O   1 
ATOM   4777  C CB  . ASN C  1 131 ? -9.999  -9.695   -69.088 1.00 116.72 ? 131 ASN C CB  1 
ATOM   4778  C CG  . ASN C  1 131 ? -8.765  -8.908   -68.698 1.00 125.57 ? 131 ASN C CG  1 
ATOM   4779  O OD1 . ASN C  1 131 ? -8.773  -7.677   -68.704 1.00 129.61 ? 131 ASN C OD1 1 
ATOM   4780  N ND2 . ASN C  1 131 ? -7.694  -9.616   -68.362 1.00 121.54 ? 131 ASN C ND2 1 
ATOM   4781  N N   . HIS C  1 132 ? -13.536 -9.719   -68.817 1.00 88.33  ? 132 HIS C N   1 
ATOM   4782  C CA  . HIS C  1 132 ? -14.712 -10.475  -69.229 1.00 78.62  ? 132 HIS C CA  1 
ATOM   4783  C C   . HIS C  1 132 ? -15.981 -9.721   -68.857 1.00 82.07  ? 132 HIS C C   1 
ATOM   4784  O O   . HIS C  1 132 ? -15.979 -8.906   -67.935 1.00 83.05  ? 132 HIS C O   1 
ATOM   4785  C CB  . HIS C  1 132 ? -14.713 -11.855  -68.568 1.00 75.02  ? 132 HIS C CB  1 
ATOM   4786  C CG  . HIS C  1 132 ? -13.413 -12.586  -68.696 1.00 73.13  ? 132 HIS C CG  1 
ATOM   4787  N ND1 . HIS C  1 132 ? -13.213 -13.597  -69.612 1.00 70.75  ? 132 HIS C ND1 1 
ATOM   4788  C CD2 . HIS C  1 132 ? -12.244 -12.449  -68.029 1.00 66.37  ? 132 HIS C CD2 1 
ATOM   4789  C CE1 . HIS C  1 132 ? -11.980 -14.053  -69.500 1.00 72.71  ? 132 HIS C CE1 1 
ATOM   4790  N NE2 . HIS C  1 132 ? -11.368 -13.371  -68.545 1.00 69.02  ? 132 HIS C NE2 1 
ATOM   4791  N N   . ASP C  1 133 ? -17.064 -9.993   -69.576 1.00 72.16  ? 133 ASP C N   1 
ATOM   4792  C CA  . ASP C  1 133 ? -18.340 -9.345   -69.302 1.00 79.65  ? 133 ASP C CA  1 
ATOM   4793  C C   . ASP C  1 133 ? -19.092 -10.095  -68.208 1.00 79.77  ? 133 ASP C C   1 
ATOM   4794  O O   . ASP C  1 133 ? -19.418 -11.273  -68.358 1.00 78.98  ? 133 ASP C O   1 
ATOM   4795  C CB  . ASP C  1 133 ? -19.183 -9.264   -70.576 1.00 82.84  ? 133 ASP C CB  1 
ATOM   4796  C CG  . ASP C  1 133 ? -20.367 -8.326   -70.434 1.00 97.90  ? 133 ASP C CG  1 
ATOM   4797  O OD1 . ASP C  1 133 ? -21.058 -8.383   -69.396 1.00 92.35  ? 133 ASP C OD1 1 
ATOM   4798  O OD2 . ASP C  1 133 ? -20.609 -7.532   -71.368 1.00 111.24 ? 133 ASP C OD2 1 
ATOM   4799  N N   . SER C  1 134 ? -19.360 -9.405   -67.105 1.00 77.80  ? 134 SER C N   1 
ATOM   4800  C CA  . SER C  1 134 ? -20.045 -10.009  -65.968 1.00 72.25  ? 134 SER C CA  1 
ATOM   4801  C C   . SER C  1 134 ? -21.467 -9.476   -65.839 1.00 74.35  ? 134 SER C C   1 
ATOM   4802  O O   . SER C  1 134 ? -22.021 -9.410   -64.742 1.00 74.18  ? 134 SER C O   1 
ATOM   4803  C CB  . SER C  1 134 ? -19.266 -9.739   -64.681 1.00 81.09  ? 134 SER C CB  1 
ATOM   4804  O OG  . SER C  1 134 ? -19.028 -8.353   -64.516 1.00 87.41  ? 134 SER C OG  1 
ATOM   4805  N N   . ASN C  1 135 ? -22.055 -9.102   -66.971 1.00 86.98  ? 135 ASN C N   1 
ATOM   4806  C CA  . ASN C  1 135 ? -23.379 -8.496   -66.982 1.00 90.64  ? 135 ASN C CA  1 
ATOM   4807  C C   . ASN C  1 135 ? -24.331 -9.164   -67.970 1.00 89.42  ? 135 ASN C C   1 
ATOM   4808  O O   . ASN C  1 135 ? -25.547 -9.139   -67.784 1.00 101.11 ? 135 ASN C O   1 
ATOM   4809  C CB  . ASN C  1 135 ? -23.270 -7.002   -67.291 1.00 101.08 ? 135 ASN C CB  1 
ATOM   4810  C CG  . ASN C  1 135 ? -22.567 -6.230   -66.192 1.00 95.69  ? 135 ASN C CG  1 
ATOM   4811  O OD1 . ASN C  1 135 ? -22.847 -6.418   -65.009 1.00 77.76  ? 135 ASN C OD1 1 
ATOM   4812  N ND2 . ASN C  1 135 ? -21.650 -5.350   -66.580 1.00 84.05  ? 135 ASN C ND2 1 
ATOM   4813  N N   . LYS C  1 136 ? -23.771 -9.763   -69.016 1.00 84.29  ? 136 LYS C N   1 
ATOM   4814  C CA  . LYS C  1 136 ? -24.577 -10.362  -70.076 1.00 93.36  ? 136 LYS C CA  1 
ATOM   4815  C C   . LYS C  1 136 ? -24.999 -11.793  -69.763 1.00 98.28  ? 136 LYS C C   1 
ATOM   4816  O O   . LYS C  1 136 ? -25.644 -12.448  -70.582 1.00 90.50  ? 136 LYS C O   1 
ATOM   4817  C CB  . LYS C  1 136 ? -23.824 -10.321  -71.406 1.00 106.75 ? 136 LYS C CB  1 
ATOM   4818  C CG  . LYS C  1 136 ? -23.440 -8.922   -71.833 1.00 112.18 ? 136 LYS C CG  1 
ATOM   4819  C CD  . LYS C  1 136 ? -23.928 -8.612   -73.232 1.00 120.74 ? 136 LYS C CD  1 
ATOM   4820  C CE  . LYS C  1 136 ? -24.022 -7.115   -73.429 1.00 140.77 ? 136 LYS C CE  1 
ATOM   4821  N NZ  . LYS C  1 136 ? -24.925 -6.499   -72.415 1.00 139.81 ? 136 LYS C NZ  1 
ATOM   4822  N N   . GLY C  1 137 ? -24.644 -12.269  -68.575 1.00 89.88  ? 137 GLY C N   1 
ATOM   4823  C CA  . GLY C  1 137 ? -24.921 -13.641  -68.192 1.00 76.67  ? 137 GLY C CA  1 
ATOM   4824  C C   . GLY C  1 137 ? -26.308 -13.874  -67.623 1.00 71.16  ? 137 GLY C C   1 
ATOM   4825  O O   . GLY C  1 137 ? -26.456 -14.174  -66.438 1.00 74.22  ? 137 GLY C O   1 
ATOM   4826  N N   . VAL C  1 138 ? -27.328 -13.740  -68.465 1.00 72.55  ? 138 VAL C N   1 
ATOM   4827  C CA  . VAL C  1 138 ? -28.699 -14.023  -68.051 1.00 70.30  ? 138 VAL C CA  1 
ATOM   4828  C C   . VAL C  1 138 ? -29.376 -14.983  -69.023 1.00 69.74  ? 138 VAL C C   1 
ATOM   4829  O O   . VAL C  1 138 ? -28.827 -15.302  -70.078 1.00 74.07  ? 138 VAL C O   1 
ATOM   4830  C CB  . VAL C  1 138 ? -29.546 -12.741  -67.937 1.00 80.37  ? 138 VAL C CB  1 
ATOM   4831  C CG1 . VAL C  1 138 ? -28.903 -11.765  -66.963 1.00 85.32  ? 138 VAL C CG1 1 
ATOM   4832  C CG2 . VAL C  1 138 ? -29.739 -12.106  -69.306 1.00 78.78  ? 138 VAL C CG2 1 
ATOM   4833  N N   . THR C  1 139 ? -30.573 -15.437  -68.666 1.00 59.18  ? 139 THR C N   1 
ATOM   4834  C CA  . THR C  1 139 ? -31.288 -16.412  -69.480 1.00 78.75  ? 139 THR C CA  1 
ATOM   4835  C C   . THR C  1 139 ? -32.784 -16.422  -69.186 1.00 83.15  ? 139 THR C C   1 
ATOM   4836  O O   . THR C  1 139 ? -33.214 -16.068  -68.088 1.00 75.06  ? 139 THR C O   1 
ATOM   4837  C CB  . THR C  1 139 ? -30.729 -17.832  -69.269 1.00 86.21  ? 139 THR C CB  1 
ATOM   4838  O OG1 . THR C  1 139 ? -31.571 -18.783  -69.933 1.00 74.23  ? 139 THR C OG1 1 
ATOM   4839  C CG2 . THR C  1 139 ? -30.671 -18.166  -67.787 1.00 79.60  ? 139 THR C CG2 1 
ATOM   4840  N N   . ALA C  1 140 ? -33.571 -16.832  -70.176 1.00 98.57  ? 140 ALA C N   1 
ATOM   4841  C CA  . ALA C  1 140 ? -35.015 -16.943  -70.015 1.00 93.02  ? 140 ALA C CA  1 
ATOM   4842  C C   . ALA C  1 140 ? -35.363 -18.104  -69.092 1.00 97.12  ? 140 ALA C C   1 
ATOM   4843  O O   . ALA C  1 140 ? -36.503 -18.236  -68.645 1.00 87.12  ? 140 ALA C O   1 
ATOM   4844  C CB  . ALA C  1 140 ? -35.688 -17.120  -71.367 1.00 92.72  ? 140 ALA C CB  1 
ATOM   4845  N N   . ALA C  1 141 ? -34.372 -18.945  -68.812 1.00 97.43  ? 141 ALA C N   1 
ATOM   4846  C CA  . ALA C  1 141 ? -34.565 -20.100  -67.942 1.00 87.82  ? 141 ALA C CA  1 
ATOM   4847  C C   . ALA C  1 141 ? -34.697 -19.680  -66.482 1.00 81.72  ? 141 ALA C C   1 
ATOM   4848  O O   . ALA C  1 141 ? -35.439 -20.293  -65.718 1.00 74.81  ? 141 ALA C O   1 
ATOM   4849  C CB  . ALA C  1 141 ? -33.421 -21.087  -68.109 1.00 83.51  ? 141 ALA C CB  1 
ATOM   4850  N N   . CYS C  1 142 ? -33.973 -18.634  -66.099 1.00 79.03  ? 142 CYS C N   1 
ATOM   4851  C CA  . CYS C  1 142 ? -34.031 -18.127  -64.732 1.00 84.11  ? 142 CYS C CA  1 
ATOM   4852  C C   . CYS C  1 142 ? -34.658 -16.737  -64.707 1.00 81.84  ? 142 CYS C C   1 
ATOM   4853  O O   . CYS C  1 142 ? -33.960 -15.741  -64.530 1.00 77.87  ? 142 CYS C O   1 
ATOM   4854  C CB  . CYS C  1 142 ? -32.630 -18.085  -64.119 1.00 93.12  ? 142 CYS C CB  1 
ATOM   4855  S SG  . CYS C  1 142 ? -31.758 -19.669  -64.152 1.00 99.04  ? 142 CYS C SG  1 
ATOM   4856  N N   . PRO C  1 143 ? -35.987 -16.671  -64.884 1.00 88.22  ? 143 PRO C N   1 
ATOM   4857  C CA  . PRO C  1 143 ? -36.703 -15.400  -65.022 1.00 88.96  ? 143 PRO C CA  1 
ATOM   4858  C C   . PRO C  1 143 ? -36.977 -14.715  -63.690 1.00 97.18  ? 143 PRO C C   1 
ATOM   4859  O O   . PRO C  1 143 ? -37.421 -15.356  -62.737 1.00 96.47  ? 143 PRO C O   1 
ATOM   4860  C CB  . PRO C  1 143 ? -38.040 -15.816  -65.657 1.00 91.18  ? 143 PRO C CB  1 
ATOM   4861  C CG  . PRO C  1 143 ? -37.899 -17.279  -66.006 1.00 93.73  ? 143 PRO C CG  1 
ATOM   4862  C CD  . PRO C  1 143 ? -36.891 -17.816  -65.054 1.00 95.13  ? 143 PRO C CD  1 
ATOM   4863  N N   . HIS C  1 144 ? -36.712 -13.415  -63.639 1.00 99.59  ? 144 HIS C N   1 
ATOM   4864  C CA  . HIS C  1 144 ? -37.114 -12.600  -62.504 1.00 105.64 ? 144 HIS C CA  1 
ATOM   4865  C C   . HIS C  1 144 ? -38.152 -11.588  -62.976 1.00 120.44 ? 144 HIS C C   1 
ATOM   4866  O O   . HIS C  1 144 ? -37.810 -10.554  -63.550 1.00 121.84 ? 144 HIS C O   1 
ATOM   4867  C CB  . HIS C  1 144 ? -35.909 -11.895  -61.882 1.00 97.21  ? 144 HIS C CB  1 
ATOM   4868  C CG  . HIS C  1 144 ? -36.093 -11.554  -60.437 1.00 109.34 ? 144 HIS C CG  1 
ATOM   4869  N ND1 . HIS C  1 144 ? -35.676 -10.358  -59.893 1.00 124.33 ? 144 HIS C ND1 1 
ATOM   4870  C CD2 . HIS C  1 144 ? -36.659 -12.250  -59.424 1.00 107.08 ? 144 HIS C CD2 1 
ATOM   4871  C CE1 . HIS C  1 144 ? -35.970 -10.337  -58.605 1.00 123.08 ? 144 HIS C CE1 1 
ATOM   4872  N NE2 . HIS C  1 144 ? -36.568 -11.473  -58.296 1.00 110.92 ? 144 HIS C NE2 1 
ATOM   4873  N N   . ALA C  1 145 ? -39.422 -11.906  -62.745 1.00 119.99 ? 145 ALA C N   1 
ATOM   4874  C CA  . ALA C  1 145 ? -40.529 -11.076  -63.202 1.00 122.04 ? 145 ALA C CA  1 
ATOM   4875  C C   . ALA C  1 145 ? -40.391 -10.753  -64.685 1.00 126.60 ? 145 ALA C C   1 
ATOM   4876  O O   . ALA C  1 145 ? -40.110 -9.614   -65.058 1.00 115.37 ? 145 ALA C O   1 
ATOM   4877  C CB  . ALA C  1 145 ? -40.615 -9.799   -62.380 1.00 107.83 ? 145 ALA C CB  1 
ATOM   4878  N N   . GLY C  1 146 ? -40.583 -11.765  -65.526 1.00 142.58 ? 146 GLY C N   1 
ATOM   4879  C CA  . GLY C  1 146 ? -40.515 -11.590  -66.965 1.00 140.69 ? 146 GLY C CA  1 
ATOM   4880  C C   . GLY C  1 146 ? -39.103 -11.456  -67.503 1.00 143.00 ? 146 GLY C C   1 
ATOM   4881  O O   . GLY C  1 146 ? -38.733 -12.126  -68.467 1.00 143.77 ? 146 GLY C O   1 
ATOM   4882  N N   . ALA C  1 147 ? -38.313 -10.588  -66.879 1.00 117.90 ? 147 ALA C N   1 
ATOM   4883  C CA  . ALA C  1 147 ? -36.951 -10.326  -67.332 1.00 119.66 ? 147 ALA C CA  1 
ATOM   4884  C C   . ALA C  1 147 ? -36.050 -11.552  -67.205 1.00 111.92 ? 147 ALA C C   1 
ATOM   4885  O O   . ALA C  1 147 ? -36.225 -12.374  -66.305 1.00 108.60 ? 147 ALA C O   1 
ATOM   4886  C CB  . ALA C  1 147 ? -36.358 -9.149   -66.570 1.00 122.22 ? 147 ALA C CB  1 
ATOM   4887  N N   . LYS C  1 148 ? -35.086 -11.666  -68.114 1.00 90.50  ? 148 LYS C N   1 
ATOM   4888  C CA  . LYS C  1 148 ? -34.125 -12.763  -68.085 1.00 89.20  ? 148 LYS C CA  1 
ATOM   4889  C C   . LYS C  1 148 ? -33.080 -12.523  -67.005 1.00 96.65  ? 148 LYS C C   1 
ATOM   4890  O O   . LYS C  1 148 ? -32.317 -11.560  -67.075 1.00 91.03  ? 148 LYS C O   1 
ATOM   4891  C CB  . LYS C  1 148 ? -33.435 -12.913  -69.443 1.00 85.26  ? 148 LYS C CB  1 
ATOM   4892  C CG  . LYS C  1 148 ? -34.371 -13.233  -70.597 1.00 104.53 ? 148 LYS C CG  1 
ATOM   4893  C CD  . LYS C  1 148 ? -33.590 -13.451  -71.884 1.00 108.31 ? 148 LYS C CD  1 
ATOM   4894  C CE  . LYS C  1 148 ? -32.713 -12.251  -72.206 1.00 108.59 ? 148 LYS C CE  1 
ATOM   4895  N NZ  . LYS C  1 148 ? -31.887 -12.468  -73.426 1.00 110.53 ? 148 LYS C NZ  1 
ATOM   4896  N N   . SER C  1 149 ? -33.042 -13.401  -66.008 1.00 92.42  ? 149 SER C N   1 
ATOM   4897  C CA  . SER C  1 149 ? -32.106 -13.249  -64.900 1.00 84.79  ? 149 SER C CA  1 
ATOM   4898  C C   . SER C  1 149 ? -31.182 -14.458  -64.772 1.00 92.38  ? 149 SER C C   1 
ATOM   4899  O O   . SER C  1 149 ? -30.965 -15.192  -65.737 1.00 82.89  ? 149 SER C O   1 
ATOM   4900  C CB  . SER C  1 149 ? -32.862 -13.014  -63.591 1.00 85.92  ? 149 SER C CB  1 
ATOM   4901  O OG  . SER C  1 149 ? -31.991 -12.566  -62.567 1.00 101.69 ? 149 SER C OG  1 
ATOM   4902  N N   . PHE C  1 150 ? -30.640 -14.658  -63.575 1.00 85.28  ? 150 PHE C N   1 
ATOM   4903  C CA  . PHE C  1 150 ? -29.720 -15.759  -63.318 1.00 64.67  ? 150 PHE C CA  1 
ATOM   4904  C C   . PHE C  1 150 ? -29.585 -15.984  -61.816 1.00 72.49  ? 150 PHE C C   1 
ATOM   4905  O O   . PHE C  1 150 ? -30.173 -15.253  -61.019 1.00 82.74  ? 150 PHE C O   1 
ATOM   4906  C CB  . PHE C  1 150 ? -28.351 -15.457  -63.933 1.00 66.10  ? 150 PHE C CB  1 
ATOM   4907  C CG  . PHE C  1 150 ? -27.444 -16.650  -64.015 1.00 57.35  ? 150 PHE C CG  1 
ATOM   4908  C CD1 . PHE C  1 150 ? -27.776 -17.734  -64.810 1.00 57.32  ? 150 PHE C CD1 1 
ATOM   4909  C CD2 . PHE C  1 150 ? -26.251 -16.683  -63.312 1.00 63.10  ? 150 PHE C CD2 1 
ATOM   4910  C CE1 . PHE C  1 150 ? -26.944 -18.832  -64.893 1.00 51.44  ? 150 PHE C CE1 1 
ATOM   4911  C CE2 . PHE C  1 150 ? -25.413 -17.779  -63.392 1.00 68.36  ? 150 PHE C CE2 1 
ATOM   4912  C CZ  . PHE C  1 150 ? -25.761 -18.855  -64.184 1.00 59.59  ? 150 PHE C CZ  1 
ATOM   4913  N N   . TYR C  1 151 ? -28.818 -16.999  -61.433 1.00 73.33  ? 151 TYR C N   1 
ATOM   4914  C CA  . TYR C  1 151 ? -28.561 -17.264  -60.023 1.00 61.48  ? 151 TYR C CA  1 
ATOM   4915  C C   . TYR C  1 151 ? -27.829 -16.079  -59.403 1.00 58.73  ? 151 TYR C C   1 
ATOM   4916  O O   . TYR C  1 151 ? -26.944 -15.494  -60.027 1.00 63.48  ? 151 TYR C O   1 
ATOM   4917  C CB  . TYR C  1 151 ? -27.733 -18.539  -59.854 1.00 64.68  ? 151 TYR C CB  1 
ATOM   4918  C CG  . TYR C  1 151 ? -28.331 -19.757  -60.524 1.00 53.56  ? 151 TYR C CG  1 
ATOM   4919  C CD1 . TYR C  1 151 ? -29.388 -20.445  -59.942 1.00 54.18  ? 151 TYR C CD1 1 
ATOM   4920  C CD2 . TYR C  1 151 ? -27.835 -20.221  -61.734 1.00 51.95  ? 151 TYR C CD2 1 
ATOM   4921  C CE1 . TYR C  1 151 ? -29.936 -21.558  -60.550 1.00 50.79  ? 151 TYR C CE1 1 
ATOM   4922  C CE2 . TYR C  1 151 ? -28.376 -21.334  -62.350 1.00 46.60  ? 151 TYR C CE2 1 
ATOM   4923  C CZ  . TYR C  1 151 ? -29.426 -21.999  -61.753 1.00 50.54  ? 151 TYR C CZ  1 
ATOM   4924  O OH  . TYR C  1 151 ? -29.971 -23.107  -62.360 1.00 56.67  ? 151 TYR C OH  1 
ATOM   4925  N N   . LYS C  1 152 ? -28.202 -15.727  -58.178 1.00 52.19  ? 152 LYS C N   1 
ATOM   4926  C CA  . LYS C  1 152 ? -27.598 -14.591  -57.492 1.00 65.64  ? 152 LYS C CA  1 
ATOM   4927  C C   . LYS C  1 152 ? -26.172 -14.894  -57.048 1.00 64.84  ? 152 LYS C C   1 
ATOM   4928  O O   . LYS C  1 152 ? -25.290 -14.040  -57.132 1.00 66.97  ? 152 LYS C O   1 
ATOM   4929  C CB  . LYS C  1 152 ? -28.440 -14.185  -56.282 1.00 62.55  ? 152 LYS C CB  1 
ATOM   4930  C CG  . LYS C  1 152 ? -29.856 -13.756  -56.624 1.00 92.07  ? 152 LYS C CG  1 
ATOM   4931  C CD  . LYS C  1 152 ? -29.859 -12.550  -57.549 1.00 119.51 ? 152 LYS C CD  1 
ATOM   4932  C CE  . LYS C  1 152 ? -31.276 -12.111  -57.876 1.00 125.18 ? 152 LYS C CE  1 
ATOM   4933  N NZ  . LYS C  1 152 ? -31.294 -10.943  -58.799 1.00 123.84 ? 152 LYS C NZ  1 
ATOM   4934  N N   . ASN C  1 153 ? -25.952 -16.118  -56.579 1.00 56.60  ? 153 ASN C N   1 
ATOM   4935  C CA  . ASN C  1 153 ? -24.663 -16.501  -56.011 1.00 59.21  ? 153 ASN C CA  1 
ATOM   4936  C C   . ASN C  1 153 ? -23.632 -16.937  -57.047 1.00 59.58  ? 153 ASN C C   1 
ATOM   4937  O O   . ASN C  1 153 ? -22.514 -17.317  -56.699 1.00 58.24  ? 153 ASN C O   1 
ATOM   4938  C CB  . ASN C  1 153 ? -24.854 -17.596  -54.960 1.00 49.27  ? 153 ASN C CB  1 
ATOM   4939  C CG  . ASN C  1 153 ? -25.749 -17.153  -53.820 1.00 64.25  ? 153 ASN C CG  1 
ATOM   4940  O OD1 . ASN C  1 153 ? -25.896 -15.959  -53.559 1.00 69.18  ? 153 ASN C OD1 1 
ATOM   4941  N ND2 . ASN C  1 153 ? -26.352 -18.115  -53.135 1.00 63.19  ? 153 ASN C ND2 1 
ATOM   4942  N N   . LEU C  1 154 ? -24.010 -16.879  -58.320 1.00 57.91  ? 154 LEU C N   1 
ATOM   4943  C CA  . LEU C  1 154 ? -23.097 -17.222  -59.404 1.00 58.86  ? 154 LEU C CA  1 
ATOM   4944  C C   . LEU C  1 154 ? -23.144 -16.167  -60.503 1.00 63.58  ? 154 LEU C C   1 
ATOM   4945  O O   . LEU C  1 154 ? -24.158 -15.493  -60.684 1.00 73.76  ? 154 LEU C O   1 
ATOM   4946  C CB  . LEU C  1 154 ? -23.441 -18.595  -59.985 1.00 62.02  ? 154 LEU C CB  1 
ATOM   4947  C CG  . LEU C  1 154 ? -23.342 -19.800  -59.047 1.00 53.36  ? 154 LEU C CG  1 
ATOM   4948  C CD1 . LEU C  1 154 ? -23.900 -21.044  -59.718 1.00 49.39  ? 154 LEU C CD1 1 
ATOM   4949  C CD2 . LEU C  1 154 ? -21.905 -20.026  -58.604 1.00 58.66  ? 154 LEU C CD2 1 
ATOM   4950  N N   . ILE C  1 155 ? -22.044 -16.025  -61.233 1.00 67.49  ? 155 ILE C N   1 
ATOM   4951  C CA  . ILE C  1 155 ? -21.990 -15.094  -62.353 1.00 71.12  ? 155 ILE C CA  1 
ATOM   4952  C C   . ILE C  1 155 ? -21.625 -15.819  -63.642 1.00 58.89  ? 155 ILE C C   1 
ATOM   4953  O O   . ILE C  1 155 ? -20.574 -16.452  -63.732 1.00 51.95  ? 155 ILE C O   1 
ATOM   4954  C CB  . ILE C  1 155 ? -20.971 -13.967  -62.108 1.00 75.27  ? 155 ILE C CB  1 
ATOM   4955  C CG1 . ILE C  1 155 ? -21.372 -13.141  -60.885 1.00 78.00  ? 155 ILE C CG1 1 
ATOM   4956  C CG2 . ILE C  1 155 ? -20.863 -13.078  -63.335 1.00 57.09  ? 155 ILE C CG2 1 
ATOM   4957  C CD1 . ILE C  1 155 ? -20.409 -12.021  -60.566 1.00 91.68  ? 155 ILE C CD1 1 
ATOM   4958  N N   . TRP C  1 156 ? -22.499 -15.727  -64.638 1.00 60.12  ? 156 TRP C N   1 
ATOM   4959  C CA  . TRP C  1 156 ? -22.249 -16.367  -65.923 1.00 57.68  ? 156 TRP C CA  1 
ATOM   4960  C C   . TRP C  1 156 ? -21.375 -15.476  -66.803 1.00 60.97  ? 156 TRP C C   1 
ATOM   4961  O O   . TRP C  1 156 ? -21.879 -14.638  -67.550 1.00 76.21  ? 156 TRP C O   1 
ATOM   4962  C CB  . TRP C  1 156 ? -23.569 -16.688  -66.627 1.00 60.20  ? 156 TRP C CB  1 
ATOM   4963  C CG  . TRP C  1 156 ? -23.407 -17.550  -67.839 1.00 57.74  ? 156 TRP C CG  1 
ATOM   4964  C CD1 . TRP C  1 156 ? -22.235 -17.962  -68.398 1.00 63.42  ? 156 TRP C CD1 1 
ATOM   4965  C CD2 . TRP C  1 156 ? -24.453 -18.104  -68.647 1.00 61.32  ? 156 TRP C CD2 1 
ATOM   4966  N NE1 . TRP C  1 156 ? -22.481 -18.741  -69.501 1.00 61.70  ? 156 TRP C NE1 1 
ATOM   4967  C CE2 . TRP C  1 156 ? -23.836 -18.843  -69.677 1.00 61.17  ? 156 TRP C CE2 1 
ATOM   4968  C CE3 . TRP C  1 156 ? -25.850 -18.047  -68.601 1.00 56.43  ? 156 TRP C CE3 1 
ATOM   4969  C CZ2 . TRP C  1 156 ? -24.566 -19.519  -70.652 1.00 67.95  ? 156 TRP C CZ2 1 
ATOM   4970  C CZ3 . TRP C  1 156 ? -26.573 -18.721  -69.571 1.00 61.21  ? 156 TRP C CZ3 1 
ATOM   4971  C CH2 . TRP C  1 156 ? -25.929 -19.447  -70.582 1.00 66.40  ? 156 TRP C CH2 1 
ATOM   4972  N N   . LEU C  1 157 ? -20.064 -15.663  -66.705 1.00 54.24  ? 157 LEU C N   1 
ATOM   4973  C CA  . LEU C  1 157 ? -19.110 -14.873  -67.475 1.00 51.93  ? 157 LEU C CA  1 
ATOM   4974  C C   . LEU C  1 157 ? -19.183 -15.176  -68.965 1.00 65.32  ? 157 LEU C C   1 
ATOM   4975  O O   . LEU C  1 157 ? -19.128 -16.335  -69.373 1.00 73.38  ? 157 LEU C O   1 
ATOM   4976  C CB  . LEU C  1 157 ? -17.692 -15.141  -66.980 1.00 56.16  ? 157 LEU C CB  1 
ATOM   4977  C CG  . LEU C  1 157 ? -17.017 -14.038  -66.164 1.00 61.79  ? 157 LEU C CG  1 
ATOM   4978  C CD1 . LEU C  1 157 ? -18.020 -13.242  -65.341 1.00 63.14  ? 157 LEU C CD1 1 
ATOM   4979  C CD2 . LEU C  1 157 ? -15.913 -14.623  -65.295 1.00 53.24  ? 157 LEU C CD2 1 
ATOM   4980  N N   . VAL C  1 158 ? -19.296 -14.126  -69.772 1.00 69.61  ? 158 VAL C N   1 
ATOM   4981  C CA  . VAL C  1 158 ? -19.278 -14.264  -71.223 1.00 69.40  ? 158 VAL C CA  1 
ATOM   4982  C C   . VAL C  1 158 ? -18.160 -13.414  -71.816 1.00 76.98  ? 158 VAL C C   1 
ATOM   4983  O O   . VAL C  1 158 ? -17.556 -12.597  -71.121 1.00 74.80  ? 158 VAL C O   1 
ATOM   4984  C CB  . VAL C  1 158 ? -20.621 -13.850  -71.851 1.00 69.35  ? 158 VAL C CB  1 
ATOM   4985  C CG1 . VAL C  1 158 ? -21.739 -14.755  -71.355 1.00 78.29  ? 158 VAL C CG1 1 
ATOM   4986  C CG2 . VAL C  1 158 ? -20.926 -12.393  -71.540 1.00 77.05  ? 158 VAL C CG2 1 
ATOM   4987  N N   . LYS C  1 159 ? -17.890 -13.607  -73.103 1.00 84.05  ? 159 LYS C N   1 
ATOM   4988  C CA  . LYS C  1 159 ? -16.815 -12.886  -73.773 1.00 94.09  ? 159 LYS C CA  1 
ATOM   4989  C C   . LYS C  1 159 ? -17.088 -11.385  -73.817 1.00 94.19  ? 159 LYS C C   1 
ATOM   4990  O O   . LYS C  1 159 ? -18.218 -10.954  -74.049 1.00 76.84  ? 159 LYS C O   1 
ATOM   4991  C CB  . LYS C  1 159 ? -16.610 -13.421  -75.192 1.00 89.97  ? 159 LYS C CB  1 
ATOM   4992  C CG  . LYS C  1 159 ? -17.744 -13.097  -76.151 1.00 85.14  ? 159 LYS C CG  1 
ATOM   4993  C CD  . LYS C  1 159 ? -17.402 -13.518  -77.570 1.00 95.90  ? 159 LYS C CD  1 
ATOM   4994  C CE  . LYS C  1 159 ? -18.481 -13.088  -78.550 1.00 98.66  ? 159 LYS C CE  1 
ATOM   4995  N NZ  . LYS C  1 159 ? -18.168 -13.512  -79.943 1.00 101.26 ? 159 LYS C NZ  1 
ATOM   4996  N N   . LYS C  1 160 ? -16.044 -10.595  -73.591 1.00 94.38  ? 160 LYS C N   1 
ATOM   4997  C CA  . LYS C  1 160 ? -16.157 -9.143   -73.653 1.00 106.19 ? 160 LYS C CA  1 
ATOM   4998  C C   . LYS C  1 160 ? -15.839 -8.627   -75.051 1.00 112.16 ? 160 LYS C C   1 
ATOM   4999  O O   . LYS C  1 160 ? -14.677 -8.411   -75.395 1.00 102.98 ? 160 LYS C O   1 
ATOM   5000  C CB  . LYS C  1 160 ? -15.232 -8.482   -72.629 1.00 96.37  ? 160 LYS C CB  1 
ATOM   5001  C CG  . LYS C  1 160 ? -15.219 -6.963   -72.705 1.00 98.16  ? 160 LYS C CG  1 
ATOM   5002  C CD  . LYS C  1 160 ? -14.308 -6.360   -71.650 1.00 103.46 ? 160 LYS C CD  1 
ATOM   5003  C CE  . LYS C  1 160 ? -14.716 -6.803   -70.256 1.00 111.82 ? 160 LYS C CE  1 
ATOM   5004  N NZ  . LYS C  1 160 ? -14.025 -6.017   -69.199 1.00 114.36 ? 160 LYS C NZ  1 
ATOM   5005  N N   . GLY C  1 161 ? -16.881 -8.436   -75.854 1.00 118.17 ? 161 GLY C N   1 
ATOM   5006  C CA  . GLY C  1 161 ? -16.732 -7.896   -77.193 1.00 109.14 ? 161 GLY C CA  1 
ATOM   5007  C C   . GLY C  1 161 ? -15.700 -8.623   -78.033 1.00 117.38 ? 161 GLY C C   1 
ATOM   5008  O O   . GLY C  1 161 ? -14.709 -8.030   -78.462 1.00 119.63 ? 161 GLY C O   1 
ATOM   5009  N N   . ASN C  1 162 ? -15.936 -9.912   -78.265 1.00 111.79 ? 162 ASN C N   1 
ATOM   5010  C CA  . ASN C  1 162 ? -15.062 -10.731  -79.103 1.00 121.63 ? 162 ASN C CA  1 
ATOM   5011  C C   . ASN C  1 162 ? -13.745 -11.119  -78.440 1.00 121.48 ? 162 ASN C C   1 
ATOM   5012  O O   . ASN C  1 162 ? -12.754 -11.364  -79.125 1.00 121.16 ? 162 ASN C O   1 
ATOM   5013  C CB  . ASN C  1 162 ? -14.780 -10.036  -80.440 1.00 136.53 ? 162 ASN C CB  1 
ATOM   5014  C CG  . ASN C  1 162 ? -15.587 -10.617  -81.580 1.00 149.15 ? 162 ASN C CG  1 
ATOM   5015  O OD1 . ASN C  1 162 ? -15.462 -10.188  -82.727 1.00 167.37 ? 162 ASN C OD1 1 
ATOM   5016  N ND2 . ASN C  1 162 ? -16.419 -11.604  -81.271 1.00 139.92 ? 162 ASN C ND2 1 
ATOM   5017  N N   . SER C  1 163 ? -13.730 -11.184  -77.112 1.00 120.49 ? 163 SER C N   1 
ATOM   5018  C CA  . SER C  1 163 ? -12.509 -11.545  -76.401 1.00 118.84 ? 163 SER C CA  1 
ATOM   5019  C C   . SER C  1 163 ? -12.782 -12.316  -75.114 1.00 107.67 ? 163 SER C C   1 
ATOM   5020  O O   . SER C  1 163 ? -13.475 -11.830  -74.221 1.00 103.20 ? 163 SER C O   1 
ATOM   5021  C CB  . SER C  1 163 ? -11.675 -10.296  -76.098 1.00 112.74 ? 163 SER C CB  1 
ATOM   5022  O OG  . SER C  1 163 ? -10.389 -10.645  -75.615 1.00 102.77 ? 163 SER C OG  1 
ATOM   5023  N N   . TYR C  1 164 ? -12.235 -13.524  -75.032 1.00 91.54  ? 164 TYR C N   1 
ATOM   5024  C CA  . TYR C  1 164 ? -12.287 -14.308  -73.807 1.00 83.47  ? 164 TYR C CA  1 
ATOM   5025  C C   . TYR C  1 164 ? -10.898 -14.849  -73.502 1.00 82.53  ? 164 TYR C C   1 
ATOM   5026  O O   . TYR C  1 164 ? -10.568 -15.976  -73.873 1.00 74.49  ? 164 TYR C O   1 
ATOM   5027  C CB  . TYR C  1 164 ? -13.280 -15.462  -73.929 1.00 90.51  ? 164 TYR C CB  1 
ATOM   5028  C CG  . TYR C  1 164 ? -13.697 -16.050  -72.600 1.00 87.02  ? 164 TYR C CG  1 
ATOM   5029  C CD1 . TYR C  1 164 ? -15.016 -15.982  -72.172 1.00 77.88  ? 164 TYR C CD1 1 
ATOM   5030  C CD2 . TYR C  1 164 ? -12.769 -16.661  -71.767 1.00 77.77  ? 164 TYR C CD2 1 
ATOM   5031  C CE1 . TYR C  1 164 ? -15.401 -16.515  -70.958 1.00 70.12  ? 164 TYR C CE1 1 
ATOM   5032  C CE2 . TYR C  1 164 ? -13.144 -17.194  -70.551 1.00 72.81  ? 164 TYR C CE2 1 
ATOM   5033  C CZ  . TYR C  1 164 ? -14.460 -17.119  -70.151 1.00 77.86  ? 164 TYR C CZ  1 
ATOM   5034  O OH  . TYR C  1 164 ? -14.837 -17.651  -68.940 1.00 74.14  ? 164 TYR C OH  1 
ATOM   5035  N N   . PRO C  1 165 ? -10.074 -14.033  -72.832 1.00 72.91  ? 165 PRO C N   1 
ATOM   5036  C CA  . PRO C  1 165 ? -8.706  -14.396  -72.458 1.00 82.88  ? 165 PRO C CA  1 
ATOM   5037  C C   . PRO C  1 165 ? -8.717  -15.376  -71.294 1.00 76.11  ? 165 PRO C C   1 
ATOM   5038  O O   . PRO C  1 165 ? -9.647  -15.346  -70.490 1.00 70.11  ? 165 PRO C O   1 
ATOM   5039  C CB  . PRO C  1 165 ? -8.101  -13.062  -71.998 1.00 77.84  ? 165 PRO C CB  1 
ATOM   5040  C CG  . PRO C  1 165 ? -9.078  -11.997  -72.432 1.00 89.00  ? 165 PRO C CG  1 
ATOM   5041  C CD  . PRO C  1 165 ? -10.407 -12.662  -72.420 1.00 67.58  ? 165 PRO C CD  1 
ATOM   5042  N N   . LYS C  1 166 ? -7.704  -16.232  -71.207 1.00 66.80  ? 166 LYS C N   1 
ATOM   5043  C CA  . LYS C  1 166 ? -7.587  -17.138  -70.073 1.00 80.47  ? 166 LYS C CA  1 
ATOM   5044  C C   . LYS C  1 166 ? -7.712  -16.359  -68.772 1.00 88.45  ? 166 LYS C C   1 
ATOM   5045  O O   . LYS C  1 166 ? -6.892  -15.488  -68.482 1.00 77.19  ? 166 LYS C O   1 
ATOM   5046  C CB  . LYS C  1 166 ? -6.247  -17.877  -70.097 1.00 69.55  ? 166 LYS C CB  1 
ATOM   5047  C CG  . LYS C  1 166 ? -5.870  -18.485  -68.752 1.00 81.88  ? 166 LYS C CG  1 
ATOM   5048  C CD  . LYS C  1 166 ? -4.448  -19.022  -68.741 1.00 94.14  ? 166 LYS C CD  1 
ATOM   5049  C CE  . LYS C  1 166 ? -4.337  -20.328  -69.508 1.00 98.67  ? 166 LYS C CE  1 
ATOM   5050  N NZ  . LYS C  1 166 ? -2.987  -20.940  -69.357 1.00 104.74 ? 166 LYS C NZ  1 
ATOM   5051  N N   . LEU C  1 167 ? -8.743  -16.663  -67.992 1.00 82.91  ? 167 LEU C N   1 
ATOM   5052  C CA  . LEU C  1 167 ? -8.881  -16.047  -66.680 1.00 79.91  ? 167 LEU C CA  1 
ATOM   5053  C C   . LEU C  1 167 ? -8.231  -16.928  -65.624 1.00 77.82  ? 167 LEU C C   1 
ATOM   5054  O O   . LEU C  1 167 ? -8.097  -18.138  -65.809 1.00 65.71  ? 167 LEU C O   1 
ATOM   5055  C CB  . LEU C  1 167 ? -10.348 -15.760  -66.339 1.00 58.12  ? 167 LEU C CB  1 
ATOM   5056  C CG  . LEU C  1 167 ? -11.376 -16.882  -66.153 1.00 66.45  ? 167 LEU C CG  1 
ATOM   5057  C CD1 . LEU C  1 167 ? -11.009 -17.864  -65.042 1.00 68.66  ? 167 LEU C CD1 1 
ATOM   5058  C CD2 . LEU C  1 167 ? -12.743 -16.264  -65.891 1.00 60.33  ? 167 LEU C CD2 1 
ATOM   5059  N N   . SER C  1 168 ? -7.821  -16.320  -64.519 1.00 69.78  ? 168 SER C N   1 
ATOM   5060  C CA  . SER C  1 168 ? -7.141  -17.070  -63.477 1.00 70.67  ? 168 SER C CA  1 
ATOM   5061  C C   . SER C  1 168 ? -7.250  -16.379  -62.122 1.00 77.65  ? 168 SER C C   1 
ATOM   5062  O O   . SER C  1 168 ? -6.343  -15.664  -61.693 1.00 93.97  ? 168 SER C O   1 
ATOM   5063  C CB  . SER C  1 168 ? -5.681  -17.302  -63.863 1.00 78.56  ? 168 SER C CB  1 
ATOM   5064  O OG  . SER C  1 168 ? -5.170  -18.465  -63.235 1.00 92.59  ? 168 SER C OG  1 
ATOM   5065  N N   . LYS C  1 169 ? -8.383  -16.599  -61.464 1.00 69.99  ? 169 LYS C N   1 
ATOM   5066  C CA  . LYS C  1 169 ? -8.633  -16.072  -60.132 1.00 68.20  ? 169 LYS C CA  1 
ATOM   5067  C C   . LYS C  1 169 ? -8.465  -17.184  -59.108 1.00 74.21  ? 169 LYS C C   1 
ATOM   5068  O O   . LYS C  1 169 ? -8.613  -18.362  -59.429 1.00 70.24  ? 169 LYS C O   1 
ATOM   5069  C CB  . LYS C  1 169 ? -10.050 -15.504  -60.046 1.00 56.04  ? 169 LYS C CB  1 
ATOM   5070  C CG  . LYS C  1 169 ? -10.126 -13.988  -59.999 1.00 76.96  ? 169 LYS C CG  1 
ATOM   5071  C CD  . LYS C  1 169 ? -9.647  -13.450  -58.661 1.00 77.88  ? 169 LYS C CD  1 
ATOM   5072  C CE  . LYS C  1 169 ? -10.007 -11.982  -58.498 1.00 88.68  ? 169 LYS C CE  1 
ATOM   5073  N NZ  . LYS C  1 169 ? -9.430  -11.140  -59.582 1.00 101.30 ? 169 LYS C NZ  1 
ATOM   5074  N N   . SER C  1 170 ? -8.157  -16.808  -57.873 1.00 81.96  ? 170 SER C N   1 
ATOM   5075  C CA  . SER C  1 170 ? -7.976  -17.785  -56.810 1.00 66.53  ? 170 SER C CA  1 
ATOM   5076  C C   . SER C  1 170 ? -8.163  -17.143  -55.443 1.00 63.88  ? 170 SER C C   1 
ATOM   5077  O O   . SER C  1 170 ? -7.511  -16.153  -55.113 1.00 74.46  ? 170 SER C O   1 
ATOM   5078  C CB  . SER C  1 170 ? -6.598  -18.438  -56.915 1.00 66.27  ? 170 SER C CB  1 
ATOM   5079  O OG  . SER C  1 170 ? -5.583  -17.461  -57.058 1.00 97.95  ? 170 SER C OG  1 
ATOM   5080  N N   . TYR C  1 171 ? -9.064  -17.716  -54.654 1.00 62.65  ? 171 TYR C N   1 
ATOM   5081  C CA  . TYR C  1 171 ? -9.379  -17.192  -53.333 1.00 61.27  ? 171 TYR C CA  1 
ATOM   5082  C C   . TYR C  1 171 ? -8.794  -18.073  -52.237 1.00 60.78  ? 171 TYR C C   1 
ATOM   5083  O O   . TYR C  1 171 ? -8.774  -19.297  -52.360 1.00 58.38  ? 171 TYR C O   1 
ATOM   5084  C CB  . TYR C  1 171 ? -10.895 -17.080  -53.165 1.00 65.84  ? 171 TYR C CB  1 
ATOM   5085  C CG  . TYR C  1 171 ? -11.360 -17.064  -51.728 1.00 64.06  ? 171 TYR C CG  1 
ATOM   5086  C CD1 . TYR C  1 171 ? -11.484 -15.871  -51.031 1.00 64.15  ? 171 TYR C CD1 1 
ATOM   5087  C CD2 . TYR C  1 171 ? -11.683 -18.244  -51.071 1.00 63.73  ? 171 TYR C CD2 1 
ATOM   5088  C CE1 . TYR C  1 171 ? -11.912 -15.853  -49.718 1.00 64.86  ? 171 TYR C CE1 1 
ATOM   5089  C CE2 . TYR C  1 171 ? -12.111 -18.236  -49.760 1.00 64.92  ? 171 TYR C CE2 1 
ATOM   5090  C CZ  . TYR C  1 171 ? -12.223 -17.039  -49.088 1.00 68.24  ? 171 TYR C CZ  1 
ATOM   5091  O OH  . TYR C  1 171 ? -12.650 -17.029  -47.780 1.00 72.76  ? 171 TYR C OH  1 
ATOM   5092  N N   . ILE C  1 172 ? -8.319  -17.446  -51.166 1.00 62.50  ? 172 ILE C N   1 
ATOM   5093  C CA  . ILE C  1 172 ? -7.774  -18.186  -50.034 1.00 60.51  ? 172 ILE C CA  1 
ATOM   5094  C C   . ILE C  1 172 ? -8.664  -18.039  -48.804 1.00 65.08  ? 172 ILE C C   1 
ATOM   5095  O O   . ILE C  1 172 ? -9.075  -16.935  -48.449 1.00 66.83  ? 172 ILE C O   1 
ATOM   5096  C CB  . ILE C  1 172 ? -6.334  -17.747  -49.700 1.00 64.02  ? 172 ILE C CB  1 
ATOM   5097  C CG1 . ILE C  1 172 ? -5.771  -18.601  -48.563 1.00 74.09  ? 172 ILE C CG1 1 
ATOM   5098  C CG2 . ILE C  1 172 ? -6.290  -16.269  -49.343 1.00 80.05  ? 172 ILE C CG2 1 
ATOM   5099  C CD1 . ILE C  1 172 ? -4.411  -19.180  -48.855 1.00 76.05  ? 172 ILE C CD1 1 
ATOM   5100  N N   . ASN C  1 173 ? -8.960  -19.164  -48.162 1.00 66.25  ? 173 ASN C N   1 
ATOM   5101  C CA  . ASN C  1 173 ? -9.862  -19.185  -47.017 1.00 61.90  ? 173 ASN C CA  1 
ATOM   5102  C C   . ASN C  1 173 ? -9.265  -18.517  -45.781 1.00 72.93  ? 173 ASN C C   1 
ATOM   5103  O O   . ASN C  1 173 ? -8.529  -19.143  -45.019 1.00 69.06  ? 173 ASN C O   1 
ATOM   5104  C CB  . ASN C  1 173 ? -10.279 -20.622  -46.693 1.00 59.33  ? 173 ASN C CB  1 
ATOM   5105  C CG  . ASN C  1 173 ? -11.407 -20.688  -45.683 1.00 68.70  ? 173 ASN C CG  1 
ATOM   5106  O OD1 . ASN C  1 173 ? -11.862 -19.663  -45.177 1.00 75.19  ? 173 ASN C OD1 1 
ATOM   5107  N ND2 . ASN C  1 173 ? -11.867 -21.898  -45.388 1.00 66.54  ? 173 ASN C ND2 1 
ATOM   5108  N N   . ASP C  1 174 ? -9.590  -17.243  -45.590 1.00 92.76  ? 174 ASP C N   1 
ATOM   5109  C CA  . ASP C  1 174 ? -9.098  -16.488  -44.445 1.00 90.74  ? 174 ASP C CA  1 
ATOM   5110  C C   . ASP C  1 174 ? -10.041 -16.615  -43.253 1.00 87.62  ? 174 ASP C C   1 
ATOM   5111  O O   . ASP C  1 174 ? -9.777  -16.074  -42.180 1.00 94.65  ? 174 ASP C O   1 
ATOM   5112  C CB  . ASP C  1 174 ? -8.909  -15.015  -44.813 1.00 95.75  ? 174 ASP C CB  1 
ATOM   5113  C CG  . ASP C  1 174 ? -10.175 -14.385  -45.360 1.00 116.97 ? 174 ASP C CG  1 
ATOM   5114  O OD1 . ASP C  1 174 ? -10.887 -13.711  -44.586 1.00 122.59 ? 174 ASP C OD1 1 
ATOM   5115  O OD2 . ASP C  1 174 ? -10.457 -14.564  -46.563 1.00 115.77 ? 174 ASP C OD2 1 
ATOM   5116  N N   . LYS C  1 175 ? -11.143 -17.332  -43.452 1.00 77.80  ? 175 LYS C N   1 
ATOM   5117  C CA  . LYS C  1 175 ? -12.103 -17.575  -42.383 1.00 77.17  ? 175 LYS C CA  1 
ATOM   5118  C C   . LYS C  1 175 ? -11.548 -18.609  -41.406 1.00 76.90  ? 175 LYS C C   1 
ATOM   5119  O O   . LYS C  1 175 ? -10.509 -19.219  -41.659 1.00 76.81  ? 175 LYS C O   1 
ATOM   5120  C CB  . LYS C  1 175 ? -13.433 -18.066  -42.962 1.00 67.81  ? 175 LYS C CB  1 
ATOM   5121  C CG  . LYS C  1 175 ? -14.005 -17.193  -44.072 1.00 64.77  ? 175 LYS C CG  1 
ATOM   5122  C CD  . LYS C  1 175 ? -14.518 -15.861  -43.544 1.00 60.82  ? 175 LYS C CD  1 
ATOM   5123  C CE  . LYS C  1 175 ? -15.218 -15.068  -44.642 1.00 64.68  ? 175 LYS C CE  1 
ATOM   5124  N NZ  . LYS C  1 175 ? -15.817 -13.802  -44.133 1.00 89.42  ? 175 LYS C NZ  1 
ATOM   5125  N N   . GLY C  1 176 ? -12.243 -18.802  -40.289 1.00 54.75  ? 176 GLY C N   1 
ATOM   5126  C CA  . GLY C  1 176 ? -11.851 -19.801  -39.311 1.00 82.06  ? 176 GLY C CA  1 
ATOM   5127  C C   . GLY C  1 176 ? -12.734 -21.028  -39.410 1.00 84.93  ? 176 GLY C C   1 
ATOM   5128  O O   . GLY C  1 176 ? -12.815 -21.835  -38.483 1.00 90.76  ? 176 GLY C O   1 
ATOM   5129  N N   . LYS C  1 177 ? -13.398 -21.161  -40.553 1.00 78.97  ? 177 LYS C N   1 
ATOM   5130  C CA  . LYS C  1 177 ? -14.334 -22.248  -40.792 1.00 65.07  ? 177 LYS C CA  1 
ATOM   5131  C C   . LYS C  1 177 ? -14.301 -22.618  -42.269 1.00 51.56  ? 177 LYS C C   1 
ATOM   5132  O O   . LYS C  1 177 ? -13.854 -21.829  -43.100 1.00 60.02  ? 177 LYS C O   1 
ATOM   5133  C CB  . LYS C  1 177 ? -15.743 -21.815  -40.390 1.00 68.49  ? 177 LYS C CB  1 
ATOM   5134  C CG  . LYS C  1 177 ? -16.180 -20.505  -41.030 1.00 61.51  ? 177 LYS C CG  1 
ATOM   5135  C CD  . LYS C  1 177 ? -17.506 -20.013  -40.472 1.00 71.09  ? 177 LYS C CD  1 
ATOM   5136  C CE  . LYS C  1 177 ? -17.372 -19.571  -39.023 1.00 81.62  ? 177 LYS C CE  1 
ATOM   5137  N NZ  . LYS C  1 177 ? -16.418 -18.438  -38.862 1.00 85.36  ? 177 LYS C NZ  1 
ATOM   5138  N N   . GLU C  1 178 ? -14.769 -23.818  -42.595 1.00 50.75  ? 178 GLU C N   1 
ATOM   5139  C CA  . GLU C  1 178 ? -14.821 -24.252  -43.986 1.00 50.96  ? 178 GLU C CA  1 
ATOM   5140  C C   . GLU C  1 178 ? -15.640 -23.271  -44.814 1.00 58.27  ? 178 GLU C C   1 
ATOM   5141  O O   . GLU C  1 178 ? -16.544 -22.614  -44.299 1.00 55.83  ? 178 GLU C O   1 
ATOM   5142  C CB  . GLU C  1 178 ? -15.441 -25.643  -44.093 1.00 60.36  ? 178 GLU C CB  1 
ATOM   5143  C CG  . GLU C  1 178 ? -14.687 -26.734  -43.359 1.00 82.44  ? 178 GLU C CG  1 
ATOM   5144  C CD  . GLU C  1 178 ? -15.428 -28.055  -43.389 1.00 85.62  ? 178 GLU C CD  1 
ATOM   5145  O OE1 . GLU C  1 178 ? -16.663 -28.044  -43.204 1.00 74.14  ? 178 GLU C OE1 1 
ATOM   5146  O OE2 . GLU C  1 178 ? -14.778 -29.102  -43.596 1.00 97.13  ? 178 GLU C OE2 1 
ATOM   5147  N N   . VAL C  1 179 ? -15.322 -23.176  -46.099 1.00 52.58  ? 179 VAL C N   1 
ATOM   5148  C CA  . VAL C  1 179 ? -16.090 -22.335  -47.006 1.00 52.90  ? 179 VAL C CA  1 
ATOM   5149  C C   . VAL C  1 179 ? -16.655 -23.154  -48.158 1.00 43.92  ? 179 VAL C C   1 
ATOM   5150  O O   . VAL C  1 179 ? -15.910 -23.789  -48.905 1.00 40.48  ? 179 VAL C O   1 
ATOM   5151  C CB  . VAL C  1 179 ? -15.244 -21.180  -47.571 1.00 50.51  ? 179 VAL C CB  1 
ATOM   5152  C CG1 . VAL C  1 179 ? -15.974 -20.504  -48.722 1.00 53.27  ? 179 VAL C CG1 1 
ATOM   5153  C CG2 . VAL C  1 179 ? -14.916 -20.179  -46.475 1.00 52.89  ? 179 VAL C CG2 1 
ATOM   5154  N N   . LEU C  1 180 ? -17.977 -23.142  -48.292 1.00 39.09  ? 180 LEU C N   1 
ATOM   5155  C CA  . LEU C  1 180 ? -18.640 -23.834  -49.388 1.00 39.63  ? 180 LEU C CA  1 
ATOM   5156  C C   . LEU C  1 180 ? -18.587 -22.990  -50.653 1.00 37.38  ? 180 LEU C C   1 
ATOM   5157  O O   . LEU C  1 180 ? -19.203 -21.927  -50.724 1.00 52.72  ? 180 LEU C O   1 
ATOM   5158  C CB  . LEU C  1 180 ? -20.096 -24.134  -49.031 1.00 36.25  ? 180 LEU C CB  1 
ATOM   5159  C CG  . LEU C  1 180 ? -20.929 -24.792  -50.133 1.00 40.81  ? 180 LEU C CG  1 
ATOM   5160  C CD1 . LEU C  1 180 ? -20.482 -26.229  -50.358 1.00 39.50  ? 180 LEU C CD1 1 
ATOM   5161  C CD2 . LEU C  1 180 ? -22.412 -24.732  -49.796 1.00 32.47  ? 180 LEU C CD2 1 
ATOM   5162  N N   . VAL C  1 181 ? -17.846 -23.463  -51.648 1.00 34.26  ? 181 VAL C N   1 
ATOM   5163  C CA  . VAL C  1 181 ? -17.752 -22.759  -52.918 1.00 41.99  ? 181 VAL C CA  1 
ATOM   5164  C C   . VAL C  1 181 ? -18.494 -23.526  -54.005 1.00 47.70  ? 181 VAL C C   1 
ATOM   5165  O O   . VAL C  1 181 ? -18.250 -24.714  -54.214 1.00 45.48  ? 181 VAL C O   1 
ATOM   5166  C CB  . VAL C  1 181 ? -16.290 -22.562  -53.354 1.00 40.48  ? 181 VAL C CB  1 
ATOM   5167  C CG1 . VAL C  1 181 ? -16.224 -21.665  -54.580 1.00 38.22  ? 181 VAL C CG1 1 
ATOM   5168  C CG2 . VAL C  1 181 ? -15.472 -21.973  -52.217 1.00 43.88  ? 181 VAL C CG2 1 
ATOM   5169  N N   . LEU C  1 182 ? -19.405 -22.845  -54.689 1.00 52.37  ? 182 LEU C N   1 
ATOM   5170  C CA  . LEU C  1 182 ? -20.135 -23.454  -55.792 1.00 48.99  ? 182 LEU C CA  1 
ATOM   5171  C C   . LEU C  1 182 ? -19.771 -22.791  -57.113 1.00 44.97  ? 182 LEU C C   1 
ATOM   5172  O O   . LEU C  1 182 ? -19.510 -21.589  -57.165 1.00 52.02  ? 182 LEU C O   1 
ATOM   5173  C CB  . LEU C  1 182 ? -21.645 -23.368  -55.562 1.00 35.03  ? 182 LEU C CB  1 
ATOM   5174  C CG  . LEU C  1 182 ? -22.198 -24.136  -54.362 1.00 48.00  ? 182 LEU C CG  1 
ATOM   5175  C CD1 . LEU C  1 182 ? -22.625 -23.174  -53.267 1.00 55.75  ? 182 LEU C CD1 1 
ATOM   5176  C CD2 . LEU C  1 182 ? -23.360 -25.023  -54.782 1.00 48.09  ? 182 LEU C CD2 1 
ATOM   5177  N N   . TRP C  1 183 ? -19.749 -23.584  -58.177 1.00 42.54  ? 183 TRP C N   1 
ATOM   5178  C CA  . TRP C  1 183 ? -19.482 -23.063  -59.509 1.00 49.29  ? 183 TRP C CA  1 
ATOM   5179  C C   . TRP C  1 183 ? -20.194 -23.914  -60.550 1.00 47.39  ? 183 TRP C C   1 
ATOM   5180  O O   . TRP C  1 183 ? -20.700 -24.992  -60.240 1.00 50.34  ? 183 TRP C O   1 
ATOM   5181  C CB  . TRP C  1 183 ? -17.978 -23.021  -59.786 1.00 49.13  ? 183 TRP C CB  1 
ATOM   5182  C CG  . TRP C  1 183 ? -17.348 -24.369  -59.963 1.00 43.28  ? 183 TRP C CG  1 
ATOM   5183  C CD1 . TRP C  1 183 ? -17.167 -25.039  -61.137 1.00 48.01  ? 183 TRP C CD1 1 
ATOM   5184  C CD2 . TRP C  1 183 ? -16.805 -25.207  -58.935 1.00 54.05  ? 183 TRP C CD2 1 
ATOM   5185  N NE1 . TRP C  1 183 ? -16.548 -26.243  -60.905 1.00 45.75  ? 183 TRP C NE1 1 
ATOM   5186  C CE2 . TRP C  1 183 ? -16.315 -26.370  -59.561 1.00 50.83  ? 183 TRP C CE2 1 
ATOM   5187  C CE3 . TRP C  1 183 ? -16.687 -25.088  -57.547 1.00 52.90  ? 183 TRP C CE3 1 
ATOM   5188  C CZ2 . TRP C  1 183 ? -15.717 -27.407  -58.847 1.00 46.07  ? 183 TRP C CZ2 1 
ATOM   5189  C CZ3 . TRP C  1 183 ? -16.093 -26.118  -56.840 1.00 45.15  ? 183 TRP C CZ3 1 
ATOM   5190  C CH2 . TRP C  1 183 ? -15.616 -27.262  -57.491 1.00 45.84  ? 183 TRP C CH2 1 
ATOM   5191  N N   . GLY C  1 184 ? -20.236 -23.427  -61.785 1.00 45.99  ? 184 GLY C N   1 
ATOM   5192  C CA  . GLY C  1 184 ? -20.919 -24.137  -62.848 1.00 46.93  ? 184 GLY C CA  1 
ATOM   5193  C C   . GLY C  1 184 ? -20.098 -24.262  -64.114 1.00 47.61  ? 184 GLY C C   1 
ATOM   5194  O O   . GLY C  1 184 ? -19.265 -23.409  -64.417 1.00 49.83  ? 184 GLY C O   1 
ATOM   5195  N N   . ILE C  1 185 ? -20.330 -25.343  -64.850 1.00 47.01  ? 185 ILE C N   1 
ATOM   5196  C CA  . ILE C  1 185 ? -19.712 -25.534  -66.153 1.00 36.13  ? 185 ILE C CA  1 
ATOM   5197  C C   . ILE C  1 185 ? -20.807 -25.561  -67.208 1.00 43.91  ? 185 ILE C C   1 
ATOM   5198  O O   . ILE C  1 185 ? -21.625 -26.480  -67.236 1.00 49.40  ? 185 ILE C O   1 
ATOM   5199  C CB  . ILE C  1 185 ? -18.924 -26.852  -66.222 1.00 44.31  ? 185 ILE C CB  1 
ATOM   5200  C CG1 . ILE C  1 185 ? -17.919 -26.935  -65.072 1.00 43.95  ? 185 ILE C CG1 1 
ATOM   5201  C CG2 . ILE C  1 185 ? -18.221 -26.981  -67.565 1.00 43.04  ? 185 ILE C CG2 1 
ATOM   5202  C CD1 . ILE C  1 185 ? -16.907 -25.816  -65.070 1.00 45.49  ? 185 ILE C CD1 1 
ATOM   5203  N N   . HIS C  1 186 ? -20.832 -24.549  -68.068 1.00 51.53  ? 186 HIS C N   1 
ATOM   5204  C CA  . HIS C  1 186 ? -21.868 -24.461  -69.089 1.00 53.84  ? 186 HIS C CA  1 
ATOM   5205  C C   . HIS C  1 186 ? -21.503 -25.232  -70.353 1.00 47.79  ? 186 HIS C C   1 
ATOM   5206  O O   . HIS C  1 186 ? -20.399 -25.097  -70.882 1.00 50.56  ? 186 HIS C O   1 
ATOM   5207  C CB  . HIS C  1 186 ? -22.182 -23.003  -69.432 1.00 59.39  ? 186 HIS C CB  1 
ATOM   5208  C CG  . HIS C  1 186 ? -23.165 -22.848  -70.549 1.00 61.90  ? 186 HIS C CG  1 
ATOM   5209  N ND1 . HIS C  1 186 ? -22.814 -22.357  -71.789 1.00 62.95  ? 186 HIS C ND1 1 
ATOM   5210  C CD2 . HIS C  1 186 ? -24.487 -23.136  -70.621 1.00 59.85  ? 186 HIS C CD2 1 
ATOM   5211  C CE1 . HIS C  1 186 ? -23.878 -22.341  -72.571 1.00 65.17  ? 186 HIS C CE1 1 
ATOM   5212  N NE2 . HIS C  1 186 ? -24.905 -22.808  -71.888 1.00 56.54  ? 186 HIS C NE2 1 
ATOM   5213  N N   . HIS C  1 187 ? -22.441 -26.045  -70.826 1.00 52.28  ? 187 HIS C N   1 
ATOM   5214  C CA  . HIS C  1 187 ? -22.261 -26.802  -72.056 1.00 54.63  ? 187 HIS C CA  1 
ATOM   5215  C C   . HIS C  1 187 ? -23.258 -26.320  -73.104 1.00 64.14  ? 187 HIS C C   1 
ATOM   5216  O O   . HIS C  1 187 ? -24.424 -26.715  -73.085 1.00 68.15  ? 187 HIS C O   1 
ATOM   5217  C CB  . HIS C  1 187 ? -22.451 -28.298  -71.800 1.00 56.64  ? 187 HIS C CB  1 
ATOM   5218  C CG  . HIS C  1 187 ? -21.572 -28.844  -70.714 1.00 52.06  ? 187 HIS C CG  1 
ATOM   5219  N ND1 . HIS C  1 187 ? -20.296 -29.302  -70.952 1.00 57.38  ? 187 HIS C ND1 1 
ATOM   5220  C CD2 . HIS C  1 187 ? -21.790 -29.004  -69.390 1.00 60.66  ? 187 HIS C CD2 1 
ATOM   5221  C CE1 . HIS C  1 187 ? -19.761 -29.721  -69.819 1.00 65.97  ? 187 HIS C CE1 1 
ATOM   5222  N NE2 . HIS C  1 187 ? -20.651 -29.551  -68.852 1.00 63.52  ? 187 HIS C NE2 1 
ATOM   5223  N N   . PRO C  1 188 ? -22.800 -25.451  -74.018 1.00 63.37  ? 188 PRO C N   1 
ATOM   5224  C CA  . PRO C  1 188 ? -23.644 -24.887  -75.077 1.00 66.26  ? 188 PRO C CA  1 
ATOM   5225  C C   . PRO C  1 188 ? -24.254 -25.966  -75.967 1.00 72.68  ? 188 PRO C C   1 
ATOM   5226  O O   . PRO C  1 188 ? -23.751 -27.089  -76.016 1.00 61.30  ? 188 PRO C O   1 
ATOM   5227  C CB  . PRO C  1 188 ? -22.664 -24.031  -75.884 1.00 64.82  ? 188 PRO C CB  1 
ATOM   5228  C CG  . PRO C  1 188 ? -21.584 -23.691  -74.920 1.00 67.34  ? 188 PRO C CG  1 
ATOM   5229  C CD  . PRO C  1 188 ? -21.434 -24.905  -74.055 1.00 61.50  ? 188 PRO C CD  1 
ATOM   5230  N N   . SER C  1 189 ? -25.328 -25.617  -76.667 1.00 72.56  ? 189 SER C N   1 
ATOM   5231  C CA  . SER C  1 189 ? -26.035 -26.571  -77.512 1.00 69.06  ? 189 SER C CA  1 
ATOM   5232  C C   . SER C  1 189 ? -25.366 -26.740  -78.873 1.00 76.85  ? 189 SER C C   1 
ATOM   5233  O O   . SER C  1 189 ? -25.296 -27.848  -79.406 1.00 77.78  ? 189 SER C O   1 
ATOM   5234  C CB  . SER C  1 189 ? -27.495 -26.148  -77.688 1.00 69.79  ? 189 SER C CB  1 
ATOM   5235  O OG  . SER C  1 189 ? -27.587 -24.832  -78.202 1.00 78.75  ? 189 SER C OG  1 
ATOM   5236  N N   . THR C  1 190 ? -24.872 -25.641  -79.430 1.00 85.27  ? 190 THR C N   1 
ATOM   5237  C CA  . THR C  1 190 ? -24.244 -25.674  -80.746 1.00 82.16  ? 190 THR C CA  1 
ATOM   5238  C C   . THR C  1 190 ? -22.881 -24.987  -80.739 1.00 76.51  ? 190 THR C C   1 
ATOM   5239  O O   . THR C  1 190 ? -22.616 -24.123  -79.903 1.00 80.35  ? 190 THR C O   1 
ATOM   5240  C CB  . THR C  1 190 ? -25.143 -25.021  -81.812 1.00 77.59  ? 190 THR C CB  1 
ATOM   5241  O OG1 . THR C  1 190 ? -24.334 -24.306  -82.753 1.00 107.19 ? 190 THR C OG1 1 
ATOM   5242  N N   . SER C  1 191 ? -22.020 -25.379  -81.673 1.00 86.63  ? 191 SER C N   1 
ATOM   5243  C CA  . SER C  1 191 ? -20.691 -24.788  -81.786 1.00 90.39  ? 191 SER C CA  1 
ATOM   5244  C C   . SER C  1 191 ? -20.785 -23.303  -82.118 1.00 81.94  ? 191 SER C C   1 
ATOM   5245  O O   . SER C  1 191 ? -19.857 -22.539  -81.856 1.00 86.36  ? 191 SER C O   1 
ATOM   5246  C CB  . SER C  1 191 ? -19.860 -25.518  -82.844 1.00 85.89  ? 191 SER C CB  1 
ATOM   5247  O OG  . SER C  1 191 ? -20.448 -25.401  -84.128 1.00 98.51  ? 191 SER C OG  1 
ATOM   5248  N N   . ALA C  1 192 ? -21.911 -22.903  -82.700 1.00 86.33  ? 192 ALA C N   1 
ATOM   5249  C CA  . ALA C  1 192 ? -22.165 -21.497  -82.988 1.00 94.78  ? 192 ALA C CA  1 
ATOM   5250  C C   . ALA C  1 192 ? -22.439 -20.745  -81.692 1.00 97.01  ? 192 ALA C C   1 
ATOM   5251  O O   . ALA C  1 192 ? -22.006 -19.606  -81.520 1.00 92.21  ? 192 ALA C O   1 
ATOM   5252  C CB  . ALA C  1 192 ? -23.334 -21.352  -83.948 1.00 101.89 ? 192 ALA C CB  1 
ATOM   5253  N N   . ASP C  1 193 ? -23.162 -21.391  -80.782 1.00 102.22 ? 193 ASP C N   1 
ATOM   5254  C CA  . ASP C  1 193 ? -23.430 -20.819  -79.468 1.00 89.81  ? 193 ASP C CA  1 
ATOM   5255  C C   . ASP C  1 193 ? -22.154 -20.737  -78.640 1.00 71.99  ? 193 ASP C C   1 
ATOM   5256  O O   . ASP C  1 193 ? -22.007 -19.854  -77.795 1.00 56.15  ? 193 ASP C O   1 
ATOM   5257  C CB  . ASP C  1 193 ? -24.482 -21.644  -78.723 1.00 87.97  ? 193 ASP C CB  1 
ATOM   5258  C CG  . ASP C  1 193 ? -25.881 -21.078  -78.871 1.00 104.52 ? 193 ASP C CG  1 
ATOM   5259  O OD1 . ASP C  1 193 ? -26.243 -20.660  -79.990 1.00 115.89 ? 193 ASP C OD1 1 
ATOM   5260  O OD2 . ASP C  1 193 ? -26.620 -21.053  -77.865 1.00 126.05 ? 193 ASP C OD2 1 
ATOM   5261  N N   . GLN C  1 194 ? -21.236 -21.665  -78.888 1.00 71.03  ? 194 GLN C N   1 
ATOM   5262  C CA  . GLN C  1 194 ? -19.967 -21.708  -78.172 1.00 77.88  ? 194 GLN C CA  1 
ATOM   5263  C C   . GLN C  1 194 ? -19.120 -20.470  -78.451 1.00 88.08  ? 194 GLN C C   1 
ATOM   5264  O O   . GLN C  1 194 ? -18.729 -19.756  -77.529 1.00 85.74  ? 194 GLN C O   1 
ATOM   5265  C CB  . GLN C  1 194 ? -19.187 -22.972  -78.541 1.00 75.30  ? 194 GLN C CB  1 
ATOM   5266  C CG  . GLN C  1 194 ? -17.748 -22.990  -78.045 1.00 74.69  ? 194 GLN C CG  1 
ATOM   5267  C CD  . GLN C  1 194 ? -17.643 -23.138  -76.539 1.00 76.29  ? 194 GLN C CD  1 
ATOM   5268  O OE1 . GLN C  1 194 ? -16.580 -22.924  -75.955 1.00 82.98  ? 194 GLN C OE1 1 
ATOM   5269  N NE2 . GLN C  1 194 ? -18.746 -23.507  -75.901 1.00 62.42  ? 194 GLN C NE2 1 
ATOM   5270  N N   . GLN C  1 195 ? -18.836 -20.224  -79.726 1.00 104.87 ? 195 GLN C N   1 
ATOM   5271  C CA  . GLN C  1 195 ? -18.036 -19.069  -80.119 1.00 115.50 ? 195 GLN C CA  1 
ATOM   5272  C C   . GLN C  1 195 ? -18.803 -17.765  -79.907 1.00 105.05 ? 195 GLN C C   1 
ATOM   5273  O O   . GLN C  1 195 ? -18.205 -16.701  -79.749 1.00 103.27 ? 195 GLN C O   1 
ATOM   5274  C CB  . GLN C  1 195 ? -17.578 -19.197  -81.574 1.00 117.39 ? 195 GLN C CB  1 
ATOM   5275  C CG  . GLN C  1 195 ? -18.704 -19.426  -82.567 1.00 138.28 ? 195 GLN C CG  1 
ATOM   5276  C CD  . GLN C  1 195 ? -18.194 -19.735  -83.962 1.00 156.20 ? 195 GLN C CD  1 
ATOM   5277  O OE1 . GLN C  1 195 ? -18.977 -19.933  -84.892 1.00 151.62 ? 195 GLN C OE1 1 
ATOM   5278  N NE2 . GLN C  1 195 ? -16.876 -19.780  -84.114 1.00 157.56 ? 195 GLN C NE2 1 
ATOM   5279  N N   . SER C  1 196 ? -20.128 -17.856  -79.900 1.00 77.98  ? 196 SER C N   1 
ATOM   5280  C CA  . SER C  1 196 ? -20.973 -16.698  -79.636 1.00 76.37  ? 196 SER C CA  1 
ATOM   5281  C C   . SER C  1 196 ? -20.811 -16.244  -78.193 1.00 91.16  ? 196 SER C C   1 
ATOM   5282  O O   . SER C  1 196 ? -20.866 -15.051  -77.892 1.00 97.94  ? 196 SER C O   1 
ATOM   5283  C CB  . SER C  1 196 ? -22.439 -17.033  -79.909 1.00 75.67  ? 196 SER C CB  1 
ATOM   5284  O OG  . SER C  1 196 ? -23.287 -15.976  -79.494 1.00 90.44  ? 196 SER C OG  1 
ATOM   5285  N N   . LEU C  1 197 ? -20.607 -17.211  -77.304 1.00 87.06  ? 197 LEU C N   1 
ATOM   5286  C CA  . LEU C  1 197 ? -20.499 -16.934  -75.876 1.00 77.18  ? 197 LEU C CA  1 
ATOM   5287  C C   . LEU C  1 197 ? -19.058 -16.726  -75.402 1.00 75.43  ? 197 LEU C C   1 
ATOM   5288  O O   . LEU C  1 197 ? -18.792 -15.828  -74.603 1.00 73.83  ? 197 LEU C O   1 
ATOM   5289  C CB  . LEU C  1 197 ? -21.174 -18.044  -75.063 1.00 83.82  ? 197 LEU C CB  1 
ATOM   5290  C CG  . LEU C  1 197 ? -22.703 -18.009  -74.992 1.00 73.61  ? 197 LEU C CG  1 
ATOM   5291  C CD1 . LEU C  1 197 ? -23.254 -19.326  -74.464 1.00 69.15  ? 197 LEU C CD1 1 
ATOM   5292  C CD2 . LEU C  1 197 ? -23.165 -16.844  -74.130 1.00 69.85  ? 197 LEU C CD2 1 
ATOM   5293  N N   . TYR C  1 198 ? -18.128 -17.541  -75.893 1.00 68.20  ? 198 TYR C N   1 
ATOM   5294  C CA  . TYR C  1 198 ? -16.748 -17.463  -75.415 1.00 77.71  ? 198 TYR C CA  1 
ATOM   5295  C C   . TYR C  1 198 ? -15.762 -16.959  -76.471 1.00 91.23  ? 198 TYR C C   1 
ATOM   5296  O O   . TYR C  1 198 ? -14.712 -16.411  -76.134 1.00 94.65  ? 198 TYR C O   1 
ATOM   5297  C CB  . TYR C  1 198 ? -16.306 -18.810  -74.835 1.00 89.71  ? 198 TYR C CB  1 
ATOM   5298  C CG  . TYR C  1 198 ? -17.331 -19.401  -73.893 1.00 80.35  ? 198 TYR C CG  1 
ATOM   5299  C CD1 . TYR C  1 198 ? -18.016 -20.564  -74.220 1.00 73.54  ? 198 TYR C CD1 1 
ATOM   5300  C CD2 . TYR C  1 198 ? -17.635 -18.779  -72.688 1.00 72.66  ? 198 TYR C CD2 1 
ATOM   5301  C CE1 . TYR C  1 198 ? -18.961 -21.100  -73.367 1.00 77.71  ? 198 TYR C CE1 1 
ATOM   5302  C CE2 . TYR C  1 198 ? -18.581 -19.307  -71.830 1.00 72.21  ? 198 TYR C CE2 1 
ATOM   5303  C CZ  . TYR C  1 198 ? -19.240 -20.468  -72.176 1.00 75.67  ? 198 TYR C CZ  1 
ATOM   5304  O OH  . TYR C  1 198 ? -20.181 -21.005  -71.330 1.00 75.72  ? 198 TYR C OH  1 
ATOM   5305  N N   . GLN C  1 199 ? -16.129 -17.117  -77.740 1.00 92.82  ? 199 GLN C N   1 
ATOM   5306  C CA  . GLN C  1 199 ? -15.306 -16.649  -78.850 1.00 99.84  ? 199 GLN C CA  1 
ATOM   5307  C C   . GLN C  1 199 ? -14.156 -17.570  -79.230 1.00 96.95  ? 199 GLN C C   1 
ATOM   5308  O O   . GLN C  1 199 ? -13.471 -17.356  -80.230 1.00 105.58 ? 199 GLN C O   1 
ATOM   5309  C CB  . GLN C  1 199 ? -14.499 -15.417  -78.437 1.00 110.05 ? 199 GLN C CB  1 
ATOM   5310  C CG  . GLN C  1 199 ? -13.230 -15.206  -79.247 1.00 115.74 ? 199 GLN C CG  1 
ATOM   5311  C CD  . GLN C  1 199 ? -13.505 -14.622  -80.619 1.00 116.57 ? 199 GLN C CD  1 
ATOM   5312  O OE1 . GLN C  1 199 ? -12.671 -14.706  -81.520 1.00 120.74 ? 199 GLN C OE1 1 
ATOM   5313  N NE2 . GLN C  1 199 ? -14.680 -14.027  -80.784 1.00 105.05 ? 199 GLN C NE2 1 
ATOM   5314  N N   . ASN C  1 200 ? -13.956 -18.599  -78.416 1.00 96.11  ? 200 ASN C N   1 
ATOM   5315  C CA  . ASN C  1 200 ? -12.912 -19.594  -78.648 1.00 99.70  ? 200 ASN C CA  1 
ATOM   5316  C C   . ASN C  1 200 ? -13.729 -20.869  -78.898 1.00 102.38 ? 200 ASN C C   1 
ATOM   5317  O O   . ASN C  1 200 ? -14.927 -20.898  -78.613 1.00 102.08 ? 200 ASN C O   1 
ATOM   5318  C CB  . ASN C  1 200 ? -11.905 -19.768  -77.497 1.00 98.24  ? 200 ASN C CB  1 
ATOM   5319  C CG  . ASN C  1 200 ? -11.523 -18.441  -76.857 1.00 92.53  ? 200 ASN C CG  1 
ATOM   5320  O OD1 . ASN C  1 200 ? -12.391 -17.664  -76.465 1.00 106.88 ? 200 ASN C OD1 1 
ATOM   5321  N ND2 . ASN C  1 200 ? -10.225 -18.168  -76.766 1.00 82.91  ? 200 ASN C ND2 1 
ATOM   5322  N N   . ALA C  1 201 ? -13.105 -21.909  -79.447 1.00 94.63  ? 201 ALA C N   1 
ATOM   5323  C CA  . ALA C  1 201 ? -13.829 -23.151  -79.729 1.00 89.21  ? 201 ALA C CA  1 
ATOM   5324  C C   . ALA C  1 201 ? -13.445 -24.245  -78.745 1.00 103.23 ? 201 ALA C C   1 
ATOM   5325  O O   . ALA C  1 201 ? -14.284 -24.753  -78.001 1.00 103.84 ? 201 ALA C O   1 
ATOM   5326  C CB  . ALA C  1 201 ? -13.576 -23.613  -81.153 1.00 93.58  ? 201 ALA C CB  1 
ATOM   5327  N N   . ASP C  1 202 ? -12.168 -24.609  -78.760 1.00 106.92 ? 202 ASP C N   1 
ATOM   5328  C CA  . ASP C  1 202 ? -11.650 -25.637  -77.872 1.00 104.53 ? 202 ASP C CA  1 
ATOM   5329  C C   . ASP C  1 202 ? -11.233 -25.012  -76.545 1.00 95.19  ? 202 ASP C C   1 
ATOM   5330  O O   . ASP C  1 202 ? -10.130 -24.481  -76.421 1.00 96.37  ? 202 ASP C O   1 
ATOM   5331  C CB  . ASP C  1 202 ? -10.455 -26.330  -78.525 1.00 109.12 ? 202 ASP C CB  1 
ATOM   5332  C CG  . ASP C  1 202 ? -10.205 -27.714  -77.966 1.00 125.46 ? 202 ASP C CG  1 
ATOM   5333  O OD1 . ASP C  1 202 ? -11.185 -28.456  -77.748 1.00 128.89 ? 202 ASP C OD1 1 
ATOM   5334  O OD2 . ASP C  1 202 ? -9.025  -28.061  -77.753 1.00 128.69 ? 202 ASP C OD2 1 
ATOM   5335  N N   . THR C  1 203 ? -12.119 -25.075  -75.556 1.00 86.96  ? 203 THR C N   1 
ATOM   5336  C CA  . THR C  1 203 ? -11.868 -24.438  -74.268 1.00 79.95  ? 203 THR C CA  1 
ATOM   5337  C C   . THR C  1 203 ? -11.771 -25.454  -73.138 1.00 67.46  ? 203 THR C C   1 
ATOM   5338  O O   . THR C  1 203 ? -12.031 -26.640  -73.331 1.00 73.42  ? 203 THR C O   1 
ATOM   5339  C CB  . THR C  1 203 ? -12.977 -23.431  -73.921 1.00 77.53  ? 203 THR C CB  1 
ATOM   5340  O OG1 . THR C  1 203 ? -14.228 -24.120  -73.813 1.00 69.85  ? 203 THR C OG1 1 
ATOM   5341  C CG2 . THR C  1 203 ? -13.082 -22.363  -74.996 1.00 77.07  ? 203 THR C CG2 1 
ATOM   5342  N N   . TYR C  1 204 ? -11.400 -24.978  -71.954 1.00 66.01  ? 204 TYR C N   1 
ATOM   5343  C CA  . TYR C  1 204 ? -11.306 -25.841  -70.785 1.00 69.34  ? 204 TYR C CA  1 
ATOM   5344  C C   . TYR C  1 204 ? -11.494 -25.048  -69.498 1.00 69.71  ? 204 TYR C C   1 
ATOM   5345  O O   . TYR C  1 204 ? -11.245 -23.844  -69.453 1.00 65.74  ? 204 TYR C O   1 
ATOM   5346  C CB  . TYR C  1 204 ? -9.957  -26.560  -70.753 1.00 67.18  ? 204 TYR C CB  1 
ATOM   5347  C CG  . TYR C  1 204 ? -8.800  -25.676  -70.342 1.00 73.80  ? 204 TYR C CG  1 
ATOM   5348  C CD1 . TYR C  1 204 ? -8.412  -25.580  -69.012 1.00 70.38  ? 204 TYR C CD1 1 
ATOM   5349  C CD2 . TYR C  1 204 ? -8.094  -24.939  -71.284 1.00 76.99  ? 204 TYR C CD2 1 
ATOM   5350  C CE1 . TYR C  1 204 ? -7.356  -24.775  -68.631 1.00 79.59  ? 204 TYR C CE1 1 
ATOM   5351  C CE2 . TYR C  1 204 ? -7.036  -24.131  -70.913 1.00 79.64  ? 204 TYR C CE2 1 
ATOM   5352  C CZ  . TYR C  1 204 ? -6.672  -24.053  -69.585 1.00 89.09  ? 204 TYR C CZ  1 
ATOM   5353  O OH  . TYR C  1 204 ? -5.619  -23.250  -69.211 1.00 90.08  ? 204 TYR C OH  1 
ATOM   5354  N N   . VAL C  1 205 ? -11.938 -25.738  -68.454 1.00 62.76  ? 205 VAL C N   1 
ATOM   5355  C CA  . VAL C  1 205 ? -12.072 -25.138  -67.135 1.00 57.02  ? 205 VAL C CA  1 
ATOM   5356  C C   . VAL C  1 205 ? -11.329 -26.004  -66.125 1.00 53.80  ? 205 VAL C C   1 
ATOM   5357  O O   . VAL C  1 205 ? -11.383 -27.229  -66.196 1.00 59.23  ? 205 VAL C O   1 
ATOM   5358  C CB  . VAL C  1 205 ? -13.547 -25.028  -66.715 1.00 48.76  ? 205 VAL C CB  1 
ATOM   5359  C CG1 . VAL C  1 205 ? -13.667 -24.320  -65.372 1.00 49.76  ? 205 VAL C CG1 1 
ATOM   5360  C CG2 . VAL C  1 205 ? -14.355 -24.312  -67.789 1.00 57.05  ? 205 VAL C CG2 1 
ATOM   5361  N N   . PHE C  1 206 ? -10.618 -25.374  -65.197 1.00 50.54  ? 206 PHE C N   1 
ATOM   5362  C CA  . PHE C  1 206 ? -9.911  -26.124  -64.166 1.00 54.34  ? 206 PHE C CA  1 
ATOM   5363  C C   . PHE C  1 206 ? -10.094 -25.524  -62.777 1.00 57.34  ? 206 PHE C C   1 
ATOM   5364  O O   . PHE C  1 206 ? -9.800  -24.350  -62.549 1.00 58.78  ? 206 PHE C O   1 
ATOM   5365  C CB  . PHE C  1 206 ? -8.422  -26.245  -64.492 1.00 57.74  ? 206 PHE C CB  1 
ATOM   5366  C CG  . PHE C  1 206 ? -7.606  -26.811  -63.368 1.00 63.76  ? 206 PHE C CG  1 
ATOM   5367  C CD1 . PHE C  1 206 ? -6.951  -25.973  -62.482 1.00 66.97  ? 206 PHE C CD1 1 
ATOM   5368  C CD2 . PHE C  1 206 ? -7.505  -28.180  -63.186 1.00 65.55  ? 206 PHE C CD2 1 
ATOM   5369  C CE1 . PHE C  1 206 ? -6.204  -26.487  -61.443 1.00 64.18  ? 206 PHE C CE1 1 
ATOM   5370  C CE2 . PHE C  1 206 ? -6.759  -28.701  -62.147 1.00 62.76  ? 206 PHE C CE2 1 
ATOM   5371  C CZ  . PHE C  1 206 ? -6.108  -27.853  -61.275 1.00 71.60  ? 206 PHE C CZ  1 
ATOM   5372  N N   . VAL C  1 207 ? -10.579 -26.346  -61.852 1.00 56.17  ? 207 VAL C N   1 
ATOM   5373  C CA  . VAL C  1 207 ? -10.775 -25.928  -60.471 1.00 52.98  ? 207 VAL C CA  1 
ATOM   5374  C C   . VAL C  1 207 ? -9.941  -26.795  -59.537 1.00 56.45  ? 207 VAL C C   1 
ATOM   5375  O O   . VAL C  1 207 ? -10.039 -28.022  -59.562 1.00 59.85  ? 207 VAL C O   1 
ATOM   5376  C CB  . VAL C  1 207 ? -12.253 -26.024  -60.060 1.00 38.29  ? 207 VAL C CB  1 
ATOM   5377  C CG1 . VAL C  1 207 ? -12.434 -25.547  -58.632 1.00 37.80  ? 207 VAL C CG1 1 
ATOM   5378  C CG2 . VAL C  1 207 ? -13.117 -25.212  -61.010 1.00 51.65  ? 207 VAL C CG2 1 
ATOM   5379  N N   . GLY C  1 208 ? -9.120  -26.154  -58.712 1.00 57.12  ? 208 GLY C N   1 
ATOM   5380  C CA  . GLY C  1 208 ? -8.239  -26.883  -57.820 1.00 57.66  ? 208 GLY C CA  1 
ATOM   5381  C C   . GLY C  1 208 ? -8.027  -26.246  -56.460 1.00 55.74  ? 208 GLY C C   1 
ATOM   5382  O O   . GLY C  1 208 ? -7.998  -25.024  -56.325 1.00 58.59  ? 208 GLY C O   1 
ATOM   5383  N N   . SER C  1 209 ? -7.886  -27.094  -55.446 1.00 61.87  ? 209 SER C N   1 
ATOM   5384  C CA  . SER C  1 209 ? -7.510  -26.662  -54.107 1.00 60.84  ? 209 SER C CA  1 
ATOM   5385  C C   . SER C  1 209 ? -6.421  -27.599  -53.597 1.00 64.36  ? 209 SER C C   1 
ATOM   5386  O O   . SER C  1 209 ? -5.810  -28.326  -54.380 1.00 63.68  ? 209 SER C O   1 
ATOM   5387  C CB  . SER C  1 209 ? -8.715  -26.685  -53.167 1.00 53.78  ? 209 SER C CB  1 
ATOM   5388  O OG  . SER C  1 209 ? -9.134  -28.012  -52.904 1.00 66.15  ? 209 SER C OG  1 
ATOM   5389  N N   . SER C  1 210 ? -6.175  -27.588  -52.292 1.00 75.92  ? 210 SER C N   1 
ATOM   5390  C CA  . SER C  1 210 ? -5.185  -28.487  -51.707 1.00 72.62  ? 210 SER C CA  1 
ATOM   5391  C C   . SER C  1 210 ? -5.618  -29.937  -51.876 1.00 81.46  ? 210 SER C C   1 
ATOM   5392  O O   . SER C  1 210 ? -4.788  -30.847  -51.922 1.00 68.96  ? 210 SER C O   1 
ATOM   5393  C CB  . SER C  1 210 ? -4.975  -28.175  -50.225 1.00 79.34  ? 210 SER C CB  1 
ATOM   5394  O OG  . SER C  1 210 ? -4.352  -26.915  -50.054 1.00 99.22  ? 210 SER C OG  1 
ATOM   5395  N N   . ARG C  1 211 ? -6.928  -30.140  -51.972 1.00 76.30  ? 211 ARG C N   1 
ATOM   5396  C CA  . ARG C  1 211 ? -7.496  -31.472  -52.112 1.00 86.95  ? 211 ARG C CA  1 
ATOM   5397  C C   . ARG C  1 211 ? -8.110  -31.649  -53.493 1.00 84.24  ? 211 ARG C C   1 
ATOM   5398  O O   . ARG C  1 211 ? -7.748  -32.558  -54.237 1.00 98.23  ? 211 ARG C O   1 
ATOM   5399  C CB  . ARG C  1 211 ? -8.577  -31.697  -51.049 1.00 99.67  ? 211 ARG C CB  1 
ATOM   5400  C CG  . ARG C  1 211 ? -8.293  -31.030  -49.708 1.00 105.65 ? 211 ARG C CG  1 
ATOM   5401  C CD  . ARG C  1 211 ? -9.576  -30.821  -48.891 1.00 121.48 ? 211 ARG C CD  1 
ATOM   5402  N NE  . ARG C  1 211 ? -10.080 -32.049  -48.275 1.00 135.71 ? 211 ARG C NE  1 
ATOM   5403  C CZ  . ARG C  1 211 ? -11.336 -32.228  -47.871 1.00 122.92 ? 211 ARG C CZ  1 
ATOM   5404  N NH1 . ARG C  1 211 ? -12.234 -31.264  -48.027 1.00 105.97 ? 211 ARG C NH1 1 
ATOM   5405  N NH2 . ARG C  1 211 ? -11.698 -33.378  -47.319 1.00 114.38 ? 211 ARG C NH2 1 
ATOM   5406  N N   . TYR C  1 212 ? -9.043  -30.766  -53.828 1.00 83.88  ? 212 TYR C N   1 
ATOM   5407  C CA  . TYR C  1 212 ? -9.841  -30.917  -55.039 1.00 66.06  ? 212 TYR C CA  1 
ATOM   5408  C C   . TYR C  1 212 ? -9.060  -30.519  -56.294 1.00 63.48  ? 212 TYR C C   1 
ATOM   5409  O O   . TYR C  1 212 ? -8.389  -29.490  -56.317 1.00 70.91  ? 212 TYR C O   1 
ATOM   5410  C CB  . TYR C  1 212 ? -11.143 -30.121  -54.911 1.00 53.16  ? 212 TYR C CB  1 
ATOM   5411  C CG  . TYR C  1 212 ? -12.067 -30.244  -56.097 1.00 60.86  ? 212 TYR C CG  1 
ATOM   5412  C CD1 . TYR C  1 212 ? -13.262 -30.946  -56.009 1.00 53.85  ? 212 TYR C CD1 1 
ATOM   5413  C CD2 . TYR C  1 212 ? -11.750 -29.644  -57.304 1.00 61.26  ? 212 TYR C CD2 1 
ATOM   5414  C CE1 . TYR C  1 212 ? -14.107 -31.049  -57.098 1.00 54.14  ? 212 TYR C CE1 1 
ATOM   5415  C CE2 . TYR C  1 212 ? -12.580 -29.744  -58.387 1.00 61.06  ? 212 TYR C CE2 1 
ATOM   5416  C CZ  . TYR C  1 212 ? -13.754 -30.443  -58.285 1.00 59.80  ? 212 TYR C CZ  1 
ATOM   5417  O OH  . TYR C  1 212 ? -14.560 -30.522  -59.392 1.00 54.22  ? 212 TYR C OH  1 
ATOM   5418  N N   . SER C  1 213 ? -9.144  -31.346  -57.333 1.00 55.90  ? 213 SER C N   1 
ATOM   5419  C CA  . SER C  1 213 ? -8.495  -31.036  -58.604 1.00 61.33  ? 213 SER C CA  1 
ATOM   5420  C C   . SER C  1 213 ? -9.165  -31.715  -59.799 1.00 61.47  ? 213 SER C C   1 
ATOM   5421  O O   . SER C  1 213 ? -9.153  -32.943  -59.912 1.00 73.73  ? 213 SER C O   1 
ATOM   5422  C CB  . SER C  1 213 ? -7.013  -31.410  -58.561 1.00 57.16  ? 213 SER C CB  1 
ATOM   5423  O OG  . SER C  1 213 ? -6.378  -31.089  -59.788 1.00 52.02  ? 213 SER C OG  1 
ATOM   5424  N N   . LYS C  1 214 ? -9.737  -30.916  -60.697 1.00 59.90  ? 214 LYS C N   1 
ATOM   5425  C CA  . LYS C  1 214 ? -10.352 -31.464  -61.904 1.00 58.19  ? 214 LYS C CA  1 
ATOM   5426  C C   . LYS C  1 214 ? -10.397 -30.488  -63.083 1.00 70.47  ? 214 LYS C C   1 
ATOM   5427  O O   . LYS C  1 214 ? -10.630 -29.290  -62.913 1.00 58.00  ? 214 LYS C O   1 
ATOM   5428  C CB  . LYS C  1 214 ? -11.755 -32.005  -61.609 1.00 55.37  ? 214 LYS C CB  1 
ATOM   5429  C CG  . LYS C  1 214 ? -12.383 -32.742  -62.785 1.00 66.95  ? 214 LYS C CG  1 
ATOM   5430  C CD  . LYS C  1 214 ? -13.135 -33.986  -62.333 1.00 89.01  ? 214 LYS C CD  1 
ATOM   5431  C CE  . LYS C  1 214 ? -14.638 -33.756  -62.287 1.00 91.65  ? 214 LYS C CE  1 
ATOM   5432  N NZ  . LYS C  1 214 ? -15.237 -33.647  -63.649 1.00 85.53  ? 214 LYS C NZ  1 
ATOM   5433  N N   . LYS C  1 215 ? -10.172 -31.024  -64.279 1.00 67.48  ? 215 LYS C N   1 
ATOM   5434  C CA  . LYS C  1 215 ? -10.210 -30.246  -65.512 1.00 54.99  ? 215 LYS C CA  1 
ATOM   5435  C C   . LYS C  1 215 ? -11.467 -30.591  -66.305 1.00 55.65  ? 215 LYS C C   1 
ATOM   5436  O O   . LYS C  1 215 ? -11.761 -31.763  -66.539 1.00 65.74  ? 215 LYS C O   1 
ATOM   5437  C CB  . LYS C  1 215 ? -8.963  -30.532  -66.350 1.00 70.09  ? 215 LYS C CB  1 
ATOM   5438  C CG  . LYS C  1 215 ? -8.813  -29.661  -67.587 1.00 71.71  ? 215 LYS C CG  1 
ATOM   5439  C CD  . LYS C  1 215 ? -7.499  -29.957  -68.293 1.00 80.89  ? 215 LYS C CD  1 
ATOM   5440  C CE  . LYS C  1 215 ? -7.176  -28.909  -69.345 1.00 90.62  ? 215 LYS C CE  1 
ATOM   5441  N NZ  . LYS C  1 215 ? -5.808  -29.099  -69.903 1.00 77.77  ? 215 LYS C NZ  1 
ATOM   5442  N N   . PHE C  1 216 ? -12.205 -29.567  -66.718 1.00 60.22  ? 216 PHE C N   1 
ATOM   5443  C CA  . PHE C  1 216 ? -13.475 -29.768  -67.406 1.00 58.96  ? 216 PHE C CA  1 
ATOM   5444  C C   . PHE C  1 216 ? -13.395 -29.448  -68.895 1.00 64.62  ? 216 PHE C C   1 
ATOM   5445  O O   . PHE C  1 216 ? -12.846 -28.421  -69.296 1.00 61.14  ? 216 PHE C O   1 
ATOM   5446  C CB  . PHE C  1 216 ? -14.573 -28.920  -66.758 1.00 61.95  ? 216 PHE C CB  1 
ATOM   5447  C CG  . PHE C  1 216 ? -14.744 -29.172  -65.289 1.00 66.00  ? 216 PHE C CG  1 
ATOM   5448  C CD1 . PHE C  1 216 ? -14.034 -28.430  -64.360 1.00 63.66  ? 216 PHE C CD1 1 
ATOM   5449  C CD2 . PHE C  1 216 ? -15.615 -30.148  -64.836 1.00 58.50  ? 216 PHE C CD2 1 
ATOM   5450  C CE1 . PHE C  1 216 ? -14.189 -28.658  -63.006 1.00 63.84  ? 216 PHE C CE1 1 
ATOM   5451  C CE2 . PHE C  1 216 ? -15.774 -30.381  -63.483 1.00 67.41  ? 216 PHE C CE2 1 
ATOM   5452  C CZ  . PHE C  1 216 ? -15.059 -29.634  -62.567 1.00 62.29  ? 216 PHE C CZ  1 
ATOM   5453  N N   . LYS C  1 217 ? -13.950 -30.341  -69.708 1.00 68.56  ? 217 LYS C N   1 
ATOM   5454  C CA  . LYS C  1 217 ? -14.068 -30.111  -71.141 1.00 62.82  ? 217 LYS C CA  1 
ATOM   5455  C C   . LYS C  1 217 ? -15.535 -29.963  -71.523 1.00 66.11  ? 217 LYS C C   1 
ATOM   5456  O O   . LYS C  1 217 ? -16.328 -30.883  -71.325 1.00 66.13  ? 217 LYS C O   1 
ATOM   5457  C CB  . LYS C  1 217 ? -13.429 -31.255  -71.930 1.00 75.66  ? 217 LYS C CB  1 
ATOM   5458  C CG  . LYS C  1 217 ? -12.015 -30.969  -72.408 1.00 76.58  ? 217 LYS C CG  1 
ATOM   5459  C CD  . LYS C  1 217 ? -11.999 -29.831  -73.417 1.00 80.28  ? 217 LYS C CD  1 
ATOM   5460  C CE  . LYS C  1 217 ? -10.595 -29.566  -73.936 1.00 99.73  ? 217 LYS C CE  1 
ATOM   5461  N NZ  . LYS C  1 217 ? -10.575 -28.481  -74.957 1.00 103.98 ? 217 LYS C NZ  1 
ATOM   5462  N N   . PRO C  1 218 ? -15.901 -28.793  -72.067 1.00 73.88  ? 218 PRO C N   1 
ATOM   5463  C CA  . PRO C  1 218 ? -17.280 -28.521  -72.484 1.00 74.37  ? 218 PRO C CA  1 
ATOM   5464  C C   . PRO C  1 218 ? -17.778 -29.547  -73.496 1.00 72.21  ? 218 PRO C C   1 
ATOM   5465  O O   . PRO C  1 218 ? -17.138 -29.766  -74.524 1.00 69.70  ? 218 PRO C O   1 
ATOM   5466  C CB  . PRO C  1 218 ? -17.179 -27.142  -73.141 1.00 65.53  ? 218 PRO C CB  1 
ATOM   5467  C CG  . PRO C  1 218 ? -15.983 -26.514  -72.517 1.00 72.96  ? 218 PRO C CG  1 
ATOM   5468  C CD  . PRO C  1 218 ? -15.018 -27.636  -72.287 1.00 68.09  ? 218 PRO C CD  1 
ATOM   5469  N N   . GLU C  1 219 ? -18.912 -30.170  -73.197 1.00 79.54  ? 219 GLU C N   1 
ATOM   5470  C CA  . GLU C  1 219 ? -19.510 -31.146  -74.096 1.00 68.99  ? 219 GLU C CA  1 
ATOM   5471  C C   . GLU C  1 219 ? -20.605 -30.478  -74.918 1.00 63.96  ? 219 GLU C C   1 
ATOM   5472  O O   . GLU C  1 219 ? -21.721 -30.300  -74.445 1.00 65.75  ? 219 GLU C O   1 
ATOM   5473  C CB  . GLU C  1 219 ? -20.078 -32.321  -73.297 1.00 65.57  ? 219 GLU C CB  1 
ATOM   5474  C CG  . GLU C  1 219 ? -19.056 -32.997  -72.392 1.00 77.27  ? 219 GLU C CG  1 
ATOM   5475  C CD  . GLU C  1 219 ? -19.642 -34.143  -71.589 1.00 84.86  ? 219 GLU C CD  1 
ATOM   5476  O OE1 . GLU C  1 219 ? -20.875 -34.334  -71.629 1.00 81.29  ? 219 GLU C OE1 1 
ATOM   5477  O OE2 . GLU C  1 219 ? -18.865 -34.853  -70.916 1.00 77.01  ? 219 GLU C OE2 1 
ATOM   5478  N N   . ILE C  1 220 ? -20.279 -30.101  -76.149 1.00 77.31  ? 220 ILE C N   1 
ATOM   5479  C CA  . ILE C  1 220 ? -21.210 -29.356  -76.993 1.00 70.85  ? 220 ILE C CA  1 
ATOM   5480  C C   . ILE C  1 220 ? -22.113 -30.271  -77.821 1.00 65.44  ? 220 ILE C C   1 
ATOM   5481  O O   . ILE C  1 220 ? -21.631 -31.055  -78.637 1.00 71.52  ? 220 ILE C O   1 
ATOM   5482  C CB  . ILE C  1 220 ? -20.456 -28.398  -77.935 1.00 65.39  ? 220 ILE C CB  1 
ATOM   5483  C CG1 . ILE C  1 220 ? -19.613 -27.412  -77.122 1.00 64.26  ? 220 ILE C CG1 1 
ATOM   5484  C CG2 . ILE C  1 220 ? -21.432 -27.660  -78.836 1.00 73.33  ? 220 ILE C CG2 1 
ATOM   5485  C CD1 . ILE C  1 220 ? -18.590 -26.654  -77.942 1.00 84.47  ? 220 ILE C CD1 1 
ATOM   5486  N N   . ALA C  1 221 ? -23.423 -30.161  -77.612 1.00 59.12  ? 221 ALA C N   1 
ATOM   5487  C CA  . ALA C  1 221 ? -24.390 -30.970  -78.352 1.00 61.32  ? 221 ALA C CA  1 
ATOM   5488  C C   . ALA C  1 221 ? -25.820 -30.471  -78.147 1.00 72.98  ? 221 ALA C C   1 
ATOM   5489  O O   . ALA C  1 221 ? -26.053 -29.528  -77.397 1.00 76.00  ? 221 ALA C O   1 
ATOM   5490  C CB  . ALA C  1 221 ? -24.276 -32.431  -77.949 1.00 62.43  ? 221 ALA C CB  1 
ATOM   5491  N N   . ILE C  1 222 ? -26.774 -31.109  -78.818 1.00 76.71  ? 222 ILE C N   1 
ATOM   5492  C CA  . ILE C  1 222 ? -28.179 -30.734  -78.682 1.00 78.65  ? 222 ILE C CA  1 
ATOM   5493  C C   . ILE C  1 222 ? -28.938 -31.698  -77.774 1.00 74.66  ? 222 ILE C C   1 
ATOM   5494  O O   . ILE C  1 222 ? -29.114 -32.871  -78.106 1.00 72.94  ? 222 ILE C O   1 
ATOM   5495  C CB  . ILE C  1 222 ? -28.891 -30.666  -80.052 1.00 91.21  ? 222 ILE C CB  1 
ATOM   5496  C CG1 . ILE C  1 222 ? -28.206 -29.647  -80.966 1.00 83.53  ? 222 ILE C CG1 1 
ATOM   5497  C CG2 . ILE C  1 222 ? -30.357 -30.315  -79.871 1.00 79.62  ? 222 ILE C CG2 1 
ATOM   5498  C CD1 . ILE C  1 222 ? -28.211 -28.235  -80.424 1.00 90.45  ? 222 ILE C CD1 1 
ATOM   5499  N N   . ARG C  1 223 ? -29.387 -31.195  -76.628 1.00 71.45  ? 223 ARG C N   1 
ATOM   5500  C CA  . ARG C  1 223 ? -30.188 -31.990  -75.704 1.00 78.68  ? 223 ARG C CA  1 
ATOM   5501  C C   . ARG C  1 223 ? -31.656 -31.602  -75.803 1.00 77.72  ? 223 ARG C C   1 
ATOM   5502  O O   . ARG C  1 223 ? -31.980 -30.457  -76.109 1.00 81.22  ? 223 ARG C O   1 
ATOM   5503  C CB  . ARG C  1 223 ? -29.719 -31.799  -74.261 1.00 69.74  ? 223 ARG C CB  1 
ATOM   5504  C CG  . ARG C  1 223 ? -28.269 -32.154  -73.999 1.00 63.02  ? 223 ARG C CG  1 
ATOM   5505  C CD  . ARG C  1 223 ? -27.317 -31.067  -74.468 1.00 56.24  ? 223 ARG C CD  1 
ATOM   5506  N NE  . ARG C  1 223 ? -26.024 -31.201  -73.809 1.00 63.93  ? 223 ARG C NE  1 
ATOM   5507  C CZ  . ARG C  1 223 ? -24.914 -30.576  -74.182 1.00 61.40  ? 223 ARG C CZ  1 
ATOM   5508  N NH1 . ARG C  1 223 ? -24.915 -29.761  -75.227 1.00 70.21  ? 223 ARG C NH1 1 
ATOM   5509  N NH2 . ARG C  1 223 ? -23.796 -30.774  -73.504 1.00 64.21  ? 223 ARG C NH2 1 
ATOM   5510  N N   . PRO C  1 224 ? -32.551 -32.561  -75.531 1.00 70.65  ? 224 PRO C N   1 
ATOM   5511  C CA  . PRO C  1 224 ? -33.997 -32.324  -75.514 1.00 70.68  ? 224 PRO C CA  1 
ATOM   5512  C C   . PRO C  1 224 ? -34.346 -31.111  -74.665 1.00 79.58  ? 224 PRO C C   1 
ATOM   5513  O O   . PRO C  1 224 ? -33.954 -31.041  -73.501 1.00 80.46  ? 224 PRO C O   1 
ATOM   5514  C CB  . PRO C  1 224 ? -34.544 -33.590  -74.857 1.00 70.73  ? 224 PRO C CB  1 
ATOM   5515  C CG  . PRO C  1 224 ? -33.549 -34.639  -75.194 1.00 77.22  ? 224 PRO C CG  1 
ATOM   5516  C CD  . PRO C  1 224 ? -32.215 -33.952  -75.182 1.00 76.22  ? 224 PRO C CD  1 
ATOM   5517  N N   . LYS C  1 225 ? -35.087 -30.173  -75.241 1.00 87.24  ? 225 LYS C N   1 
ATOM   5518  C CA  . LYS C  1 225 ? -35.393 -28.921  -74.561 1.00 80.98  ? 225 LYS C CA  1 
ATOM   5519  C C   . LYS C  1 225 ? -36.024 -29.109  -73.188 1.00 80.82  ? 225 LYS C C   1 
ATOM   5520  O O   . LYS C  1 225 ? -37.066 -29.748  -73.046 1.00 79.84  ? 225 LYS C O   1 
ATOM   5521  C CB  . LYS C  1 225 ? -36.290 -28.041  -75.431 1.00 95.75  ? 225 LYS C CB  1 
ATOM   5522  C CG  . LYS C  1 225 ? -35.586 -27.477  -76.644 1.00 117.49 ? 225 LYS C CG  1 
ATOM   5523  C CD  . LYS C  1 225 ? -36.512 -26.608  -77.466 1.00 128.54 ? 225 LYS C CD  1 
ATOM   5524  C CE  . LYS C  1 225 ? -35.787 -26.057  -78.677 1.00 141.53 ? 225 LYS C CE  1 
ATOM   5525  N NZ  . LYS C  1 225 ? -34.636 -25.200  -78.281 1.00 141.29 ? 225 LYS C NZ  1 
ATOM   5526  N N   . VAL C  1 226 ? -35.369 -28.547  -72.179 1.00 74.59  ? 226 VAL C N   1 
ATOM   5527  C CA  . VAL C  1 226 ? -35.941 -28.438  -70.848 1.00 77.10  ? 226 VAL C CA  1 
ATOM   5528  C C   . VAL C  1 226 ? -35.908 -26.965  -70.470 1.00 76.75  ? 226 VAL C C   1 
ATOM   5529  O O   . VAL C  1 226 ? -34.838 -26.397  -70.265 1.00 75.12  ? 226 VAL C O   1 
ATOM   5530  C CB  . VAL C  1 226 ? -35.146 -29.254  -69.815 1.00 75.77  ? 226 VAL C CB  1 
ATOM   5531  C CG1 . VAL C  1 226 ? -35.763 -29.102  -68.431 1.00 61.41  ? 226 VAL C CG1 1 
ATOM   5532  C CG2 . VAL C  1 226 ? -35.092 -30.719  -70.223 1.00 69.74  ? 226 VAL C CG2 1 
ATOM   5533  N N   . ARG C  1 227 ? -37.078 -26.341  -70.401 1.00 81.63  ? 227 ARG C N   1 
ATOM   5534  C CA  . ARG C  1 227 ? -37.157 -24.908  -70.148 1.00 77.32  ? 227 ARG C CA  1 
ATOM   5535  C C   . ARG C  1 227 ? -36.479 -24.122  -71.267 1.00 84.46  ? 227 ARG C C   1 
ATOM   5536  O O   . ARG C  1 227 ? -35.780 -23.140  -71.013 1.00 84.61  ? 227 ARG C O   1 
ATOM   5537  C CB  . ARG C  1 227 ? -36.527 -24.561  -68.799 1.00 68.20  ? 227 ARG C CB  1 
ATOM   5538  C CG  . ARG C  1 227 ? -37.272 -25.125  -67.601 1.00 66.40  ? 227 ARG C CG  1 
ATOM   5539  C CD  . ARG C  1 227 ? -36.455 -24.952  -66.336 1.00 69.44  ? 227 ARG C CD  1 
ATOM   5540  N NE  . ARG C  1 227 ? -37.231 -24.367  -65.248 1.00 59.08  ? 227 ARG C NE  1 
ATOM   5541  C CZ  . ARG C  1 227 ? -37.487 -23.068  -65.132 1.00 80.86  ? 227 ARG C CZ  1 
ATOM   5542  N NH1 . ARG C  1 227 ? -37.040 -22.219  -66.047 1.00 89.59  ? 227 ARG C NH1 1 
ATOM   5543  N NH2 . ARG C  1 227 ? -38.194 -22.619  -64.107 1.00 76.44  ? 227 ARG C NH2 1 
ATOM   5544  N N   . ASP C  1 228 ? -36.679 -24.578  -72.501 1.00 88.76  ? 228 ASP C N   1 
ATOM   5545  C CA  . ASP C  1 228 ? -36.223 -23.865  -73.694 1.00 99.97  ? 228 ASP C CA  1 
ATOM   5546  C C   . ASP C  1 228 ? -34.735 -23.973  -73.990 1.00 95.81  ? 228 ASP C C   1 
ATOM   5547  O O   . ASP C  1 228 ? -34.269 -23.507  -75.030 1.00 110.40 ? 228 ASP C O   1 
ATOM   5548  C CB  . ASP C  1 228 ? -36.622 -22.395  -73.626 1.00 128.94 ? 228 ASP C CB  1 
ATOM   5549  C CG  . ASP C  1 228 ? -37.951 -22.139  -74.272 1.00 155.53 ? 228 ASP C CG  1 
ATOM   5550  O OD1 . ASP C  1 228 ? -38.027 -22.246  -75.515 1.00 160.45 ? 228 ASP C OD1 1 
ATOM   5551  O OD2 . ASP C  1 228 ? -38.918 -21.838  -73.542 1.00 164.65 ? 228 ASP C OD2 1 
ATOM   5552  N N   . GLN C  1 229 ? -33.990 -24.584  -73.080 1.00 82.30  ? 229 GLN C N   1 
ATOM   5553  C CA  . GLN C  1 229 ? -32.553 -24.700  -73.258 1.00 88.58  ? 229 GLN C CA  1 
ATOM   5554  C C   . GLN C  1 229 ? -32.181 -26.066  -73.819 1.00 81.53  ? 229 GLN C C   1 
ATOM   5555  O O   . GLN C  1 229 ? -32.518 -27.100  -73.240 1.00 77.71  ? 229 GLN C O   1 
ATOM   5556  C CB  . GLN C  1 229 ? -31.832 -24.447  -71.934 1.00 76.09  ? 229 GLN C CB  1 
ATOM   5557  C CG  . GLN C  1 229 ? -32.354 -23.236  -71.173 1.00 74.16  ? 229 GLN C CG  1 
ATOM   5558  C CD  . GLN C  1 229 ? -32.245 -21.948  -71.968 1.00 75.93  ? 229 GLN C CD  1 
ATOM   5559  O OE1 . GLN C  1 229 ? -31.325 -21.774  -72.768 1.00 81.15  ? 229 GLN C OE1 1 
ATOM   5560  N NE2 . GLN C  1 229 ? -33.183 -21.035  -71.745 1.00 85.74  ? 229 GLN C NE2 1 
ATOM   5561  N N   . GLU C  1 230 ? -31.501 -26.062  -74.960 1.00 78.74  ? 230 GLU C N   1 
ATOM   5562  C CA  . GLU C  1 230 ? -30.980 -27.290  -75.544 1.00 74.06  ? 230 GLU C CA  1 
ATOM   5563  C C   . GLU C  1 230 ? -29.583 -27.560  -75.004 1.00 75.95  ? 230 GLU C C   1 
ATOM   5564  O O   . GLU C  1 230 ? -29.027 -28.638  -75.206 1.00 82.78  ? 230 GLU C O   1 
ATOM   5565  C CB  . GLU C  1 230 ? -30.949 -27.199  -77.069 1.00 94.19  ? 230 GLU C CB  1 
ATOM   5566  C CG  . GLU C  1 230 ? -32.320 -27.170  -77.716 1.00 98.24  ? 230 GLU C CG  1 
ATOM   5567  C CD  . GLU C  1 230 ? -32.251 -27.133  -79.230 1.00 113.83 ? 230 GLU C CD  1 
ATOM   5568  O OE1 . GLU C  1 230 ? -32.613 -28.144  -79.867 1.00 104.19 ? 230 GLU C OE1 1 
ATOM   5569  O OE2 . GLU C  1 230 ? -31.835 -26.093  -79.783 1.00 103.42 ? 230 GLU C OE2 1 
ATOM   5570  N N   . GLY C  1 231 ? -29.021 -26.565  -74.325 1.00 64.62  ? 231 GLY C N   1 
ATOM   5571  C CA  . GLY C  1 231 ? -27.734 -26.713  -73.673 1.00 65.61  ? 231 GLY C CA  1 
ATOM   5572  C C   . GLY C  1 231 ? -27.921 -27.107  -72.222 1.00 65.47  ? 231 GLY C C   1 
ATOM   5573  O O   . GLY C  1 231 ? -29.040 -27.077  -71.710 1.00 64.02  ? 231 GLY C O   1 
ATOM   5574  N N   . ARG C  1 232 ? -26.828 -27.465  -71.554 1.00 58.26  ? 232 ARG C N   1 
ATOM   5575  C CA  . ARG C  1 232 ? -26.891 -27.904  -70.163 1.00 58.03  ? 232 ARG C CA  1 
ATOM   5576  C C   . ARG C  1 232 ? -25.833 -27.212  -69.312 1.00 56.54  ? 232 ARG C C   1 
ATOM   5577  O O   . ARG C  1 232 ? -24.825 -26.728  -69.829 1.00 48.46  ? 232 ARG C O   1 
ATOM   5578  C CB  . ARG C  1 232 ? -26.712 -29.421  -70.074 1.00 60.07  ? 232 ARG C CB  1 
ATOM   5579  C CG  . ARG C  1 232 ? -27.745 -30.227  -70.850 1.00 59.83  ? 232 ARG C CG  1 
ATOM   5580  C CD  . ARG C  1 232 ? -28.934 -30.608  -69.978 1.00 55.47  ? 232 ARG C CD  1 
ATOM   5581  N NE  . ARG C  1 232 ? -30.005 -31.212  -70.764 1.00 62.19  ? 232 ARG C NE  1 
ATOM   5582  C CZ  . ARG C  1 232 ? -30.889 -30.506  -71.458 1.00 70.06  ? 232 ARG C CZ  1 
ATOM   5583  N NH1 . ARG C  1 232 ? -30.815 -29.182  -71.463 1.00 71.09  ? 232 ARG C NH1 1 
ATOM   5584  N NH2 . ARG C  1 232 ? -31.840 -31.113  -72.150 1.00 74.55  ? 232 ARG C NH2 1 
ATOM   5585  N N   . MET C  1 233 ? -26.069 -27.171  -68.005 1.00 56.83  ? 233 MET C N   1 
ATOM   5586  C CA  . MET C  1 233 ? -25.135 -26.551  -67.077 1.00 58.11  ? 233 MET C CA  1 
ATOM   5587  C C   . MET C  1 233 ? -24.975 -27.444  -65.847 1.00 59.65  ? 233 MET C C   1 
ATOM   5588  O O   . MET C  1 233 ? -25.920 -27.626  -65.076 1.00 52.10  ? 233 MET C O   1 
ATOM   5589  C CB  . MET C  1 233 ? -25.634 -25.157  -66.679 1.00 48.11  ? 233 MET C CB  1 
ATOM   5590  C CG  . MET C  1 233 ? -24.595 -24.272  -66.010 1.00 51.07  ? 233 MET C CG  1 
ATOM   5591  S SD  . MET C  1 233 ? -25.133 -22.551  -65.873 1.00 69.34  ? 233 MET C SD  1 
ATOM   5592  C CE  . MET C  1 233 ? -25.409 -22.134  -67.597 1.00 67.98  ? 233 MET C CE  1 
ATOM   5593  N N   . ASN C  1 234 ? -23.785 -28.014  -65.677 1.00 49.39  ? 234 ASN C N   1 
ATOM   5594  C CA  . ASN C  1 234 ? -23.508 -28.853  -64.517 1.00 49.07  ? 234 ASN C CA  1 
ATOM   5595  C C   . ASN C  1 234 ? -23.022 -28.015  -63.345 1.00 49.09  ? 234 ASN C C   1 
ATOM   5596  O O   . ASN C  1 234 ? -22.243 -27.077  -63.520 1.00 47.74  ? 234 ASN C O   1 
ATOM   5597  C CB  . ASN C  1 234 ? -22.488 -29.940  -64.861 1.00 50.70  ? 234 ASN C CB  1 
ATOM   5598  C CG  . ASN C  1 234 ? -23.019 -30.935  -65.875 1.00 54.36  ? 234 ASN C CG  1 
ATOM   5599  O OD1 . ASN C  1 234 ? -24.189 -30.885  -66.253 1.00 47.39  ? 234 ASN C OD1 1 
ATOM   5600  N ND2 . ASN C  1 234 ? -22.160 -31.844  -66.322 1.00 61.51  ? 234 ASN C ND2 1 
ATOM   5601  N N   . TYR C  1 235 ? -23.493 -28.351  -62.149 1.00 43.94  ? 235 TYR C N   1 
ATOM   5602  C CA  . TYR C  1 235 ? -23.155 -27.587  -60.957 1.00 41.70  ? 235 TYR C CA  1 
ATOM   5603  C C   . TYR C  1 235 ? -22.241 -28.387  -60.039 1.00 46.82  ? 235 TYR C C   1 
ATOM   5604  O O   . TYR C  1 235 ? -22.506 -29.551  -59.739 1.00 47.74  ? 235 TYR C O   1 
ATOM   5605  C CB  . TYR C  1 235 ? -24.427 -27.163  -60.222 1.00 42.13  ? 235 TYR C CB  1 
ATOM   5606  C CG  . TYR C  1 235 ? -25.430 -26.466  -61.117 1.00 57.17  ? 235 TYR C CG  1 
ATOM   5607  C CD1 . TYR C  1 235 ? -26.444 -27.180  -61.743 1.00 55.79  ? 235 TYR C CD1 1 
ATOM   5608  C CD2 . TYR C  1 235 ? -25.357 -25.098  -61.344 1.00 48.96  ? 235 TYR C CD2 1 
ATOM   5609  C CE1 . TYR C  1 235 ? -27.359 -26.551  -62.565 1.00 48.85  ? 235 TYR C CE1 1 
ATOM   5610  C CE2 . TYR C  1 235 ? -26.268 -24.460  -62.164 1.00 54.95  ? 235 TYR C CE2 1 
ATOM   5611  C CZ  . TYR C  1 235 ? -27.267 -25.191  -62.772 1.00 54.55  ? 235 TYR C CZ  1 
ATOM   5612  O OH  . TYR C  1 235 ? -28.177 -24.561  -63.590 1.00 56.08  ? 235 TYR C OH  1 
ATOM   5613  N N   . TYR C  1 236 ? -21.157 -27.755  -59.604 1.00 41.78  ? 236 TYR C N   1 
ATOM   5614  C CA  . TYR C  1 236 ? -20.180 -28.416  -58.750 1.00 39.61  ? 236 TYR C CA  1 
ATOM   5615  C C   . TYR C  1 236 ? -19.933 -27.615  -57.476 1.00 44.83  ? 236 TYR C C   1 
ATOM   5616  O O   . TYR C  1 236 ? -20.148 -26.401  -57.441 1.00 42.26  ? 236 TYR C O   1 
ATOM   5617  C CB  . TYR C  1 236 ? -18.868 -28.623  -59.506 1.00 36.46  ? 236 TYR C CB  1 
ATOM   5618  C CG  . TYR C  1 236 ? -19.011 -29.415  -60.785 1.00 48.74  ? 236 TYR C CG  1 
ATOM   5619  C CD1 . TYR C  1 236 ? -19.426 -28.803  -61.958 1.00 49.06  ? 236 TYR C CD1 1 
ATOM   5620  C CD2 . TYR C  1 236 ? -18.717 -30.769  -60.822 1.00 46.76  ? 236 TYR C CD2 1 
ATOM   5621  C CE1 . TYR C  1 236 ? -19.553 -29.519  -63.127 1.00 51.12  ? 236 TYR C CE1 1 
ATOM   5622  C CE2 . TYR C  1 236 ? -18.840 -31.491  -61.989 1.00 48.27  ? 236 TYR C CE2 1 
ATOM   5623  C CZ  . TYR C  1 236 ? -19.261 -30.861  -63.137 1.00 52.15  ? 236 TYR C CZ  1 
ATOM   5624  O OH  . TYR C  1 236 ? -19.386 -31.574  -64.304 1.00 46.74  ? 236 TYR C OH  1 
ATOM   5625  N N   . TRP C  1 237 ? -19.486 -28.303  -56.430 1.00 46.26  ? 237 TRP C N   1 
ATOM   5626  C CA  . TRP C  1 237 ? -19.212 -27.658  -55.154 1.00 39.34  ? 237 TRP C CA  1 
ATOM   5627  C C   . TRP C  1 237 ? -18.057 -28.357  -54.453 1.00 35.49  ? 237 TRP C C   1 
ATOM   5628  O O   . TRP C  1 237 ? -17.673 -29.466  -54.824 1.00 48.34  ? 237 TRP C O   1 
ATOM   5629  C CB  . TRP C  1 237 ? -20.454 -27.684  -54.261 1.00 38.22  ? 237 TRP C CB  1 
ATOM   5630  C CG  . TRP C  1 237 ? -20.890 -29.070  -53.910 1.00 43.45  ? 237 TRP C CG  1 
ATOM   5631  C CD1 . TRP C  1 237 ? -21.741 -29.864  -54.620 1.00 45.64  ? 237 TRP C CD1 1 
ATOM   5632  C CD2 . TRP C  1 237 ? -20.493 -29.831  -52.763 1.00 42.18  ? 237 TRP C CD2 1 
ATOM   5633  N NE1 . TRP C  1 237 ? -21.901 -31.073  -53.986 1.00 45.92  ? 237 TRP C NE1 1 
ATOM   5634  C CE2 . TRP C  1 237 ? -21.145 -31.078  -52.844 1.00 42.60  ? 237 TRP C CE2 1 
ATOM   5635  C CE3 . TRP C  1 237 ? -19.651 -29.579  -51.676 1.00 44.69  ? 237 TRP C CE3 1 
ATOM   5636  C CZ2 . TRP C  1 237 ? -20.981 -32.069  -51.879 1.00 50.02  ? 237 TRP C CZ2 1 
ATOM   5637  C CZ3 . TRP C  1 237 ? -19.489 -30.565  -50.719 1.00 47.71  ? 237 TRP C CZ3 1 
ATOM   5638  C CH2 . TRP C  1 237 ? -20.151 -31.794  -50.827 1.00 40.60  ? 237 TRP C CH2 1 
ATOM   5639  N N   . THR C  1 238 ? -17.510 -27.700  -53.437 1.00 34.72  ? 238 THR C N   1 
ATOM   5640  C CA  . THR C  1 238 ? -16.428 -28.267  -52.641 1.00 38.59  ? 238 THR C CA  1 
ATOM   5641  C C   . THR C  1 238 ? -16.299 -27.491  -51.336 1.00 45.79  ? 238 THR C C   1 
ATOM   5642  O O   . THR C  1 238 ? -16.853 -26.400  -51.200 1.00 49.68  ? 238 THR C O   1 
ATOM   5643  C CB  . THR C  1 238 ? -15.083 -28.245  -53.403 1.00 46.97  ? 238 THR C CB  1 
ATOM   5644  O OG1 . THR C  1 238 ? -14.075 -28.900  -52.623 1.00 52.67  ? 238 THR C OG1 1 
ATOM   5645  C CG2 . THR C  1 238 ? -14.650 -26.814  -53.696 1.00 40.98  ? 238 THR C CG2 1 
ATOM   5646  N N   . LEU C  1 239 ? -15.583 -28.056  -50.371 1.00 43.91  ? 239 LEU C N   1 
ATOM   5647  C CA  . LEU C  1 239 ? -15.384 -27.387  -49.092 1.00 47.69  ? 239 LEU C CA  1 
ATOM   5648  C C   . LEU C  1 239 ? -13.914 -27.026  -48.888 1.00 58.73  ? 239 LEU C C   1 
ATOM   5649  O O   . LEU C  1 239 ? -13.073 -27.900  -48.680 1.00 77.63  ? 239 LEU C O   1 
ATOM   5650  C CB  . LEU C  1 239 ? -15.900 -28.256  -47.941 1.00 54.22  ? 239 LEU C CB  1 
ATOM   5651  C CG  . LEU C  1 239 ? -17.420 -28.444  -47.877 1.00 43.09  ? 239 LEU C CG  1 
ATOM   5652  C CD1 . LEU C  1 239 ? -17.816 -29.441  -46.796 1.00 58.52  ? 239 LEU C CD1 1 
ATOM   5653  C CD2 . LEU C  1 239 ? -18.111 -27.109  -47.651 1.00 50.66  ? 239 LEU C CD2 1 
ATOM   5654  N N   . VAL C  1 240 ? -13.609 -25.733  -48.957 1.00 53.48  ? 240 VAL C N   1 
ATOM   5655  C CA  . VAL C  1 240 ? -12.240 -25.255  -48.787 1.00 55.82  ? 240 VAL C CA  1 
ATOM   5656  C C   . VAL C  1 240 ? -11.873 -25.167  -47.308 1.00 54.72  ? 240 VAL C C   1 
ATOM   5657  O O   . VAL C  1 240 ? -12.522 -24.458  -46.537 1.00 56.87  ? 240 VAL C O   1 
ATOM   5658  C CB  . VAL C  1 240 ? -12.033 -23.870  -49.434 1.00 51.21  ? 240 VAL C CB  1 
ATOM   5659  C CG1 . VAL C  1 240 ? -10.568 -23.457  -49.350 1.00 61.02  ? 240 VAL C CG1 1 
ATOM   5660  C CG2 . VAL C  1 240 ? -12.507 -23.876  -50.876 1.00 40.33  ? 240 VAL C CG2 1 
ATOM   5661  N N   . GLU C  1 241 ? -10.836 -25.897  -46.914 1.00 57.04  ? 241 GLU C N   1 
ATOM   5662  C CA  . GLU C  1 241 ? -10.384 -25.892  -45.530 1.00 65.11  ? 241 GLU C CA  1 
ATOM   5663  C C   . GLU C  1 241 ? -9.860  -24.514  -45.151 1.00 70.83  ? 241 GLU C C   1 
ATOM   5664  O O   . GLU C  1 241 ? -9.387  -23.769  -46.009 1.00 63.02  ? 241 GLU C O   1 
ATOM   5665  C CB  . GLU C  1 241 ? -9.295  -26.947  -45.319 1.00 80.57  ? 241 GLU C CB  1 
ATOM   5666  C CG  . GLU C  1 241 ? -9.744  -28.368  -45.618 1.00 95.19  ? 241 GLU C CG  1 
ATOM   5667  C CD  . GLU C  1 241 ? -10.722 -28.899  -44.588 1.00 116.07 ? 241 GLU C CD  1 
ATOM   5668  O OE1 . GLU C  1 241 ? -11.562 -29.751  -44.947 1.00 116.64 ? 241 GLU C OE1 1 
ATOM   5669  O OE2 . GLU C  1 241 ? -10.651 -28.465  -43.419 1.00 125.84 ? 241 GLU C OE2 1 
ATOM   5670  N N   . PRO C  1 242 ? -9.959  -24.164  -43.862 1.00 79.46  ? 242 PRO C N   1 
ATOM   5671  C CA  . PRO C  1 242 ? -9.387  -22.907  -43.371 1.00 70.90  ? 242 PRO C CA  1 
ATOM   5672  C C   . PRO C  1 242 ? -7.895  -22.849  -43.672 1.00 70.79  ? 242 PRO C C   1 
ATOM   5673  O O   . PRO C  1 242 ? -7.176  -23.800  -43.370 1.00 67.14  ? 242 PRO C O   1 
ATOM   5674  C CB  . PRO C  1 242 ? -9.617  -22.989  -41.861 1.00 46.88  ? 242 PRO C CB  1 
ATOM   5675  C CG  . PRO C  1 242 ? -10.798 -23.884  -41.710 1.00 58.57  ? 242 PRO C CG  1 
ATOM   5676  C CD  . PRO C  1 242 ? -10.682 -24.897  -42.809 1.00 62.01  ? 242 PRO C CD  1 
ATOM   5677  N N   . GLY C  1 243 ? -7.443  -21.750  -44.267 1.00 67.19  ? 243 GLY C N   1 
ATOM   5678  C CA  . GLY C  1 243 ? -6.040  -21.595  -44.609 1.00 68.28  ? 243 GLY C CA  1 
ATOM   5679  C C   . GLY C  1 243 ? -5.706  -22.195  -45.960 1.00 63.72  ? 243 GLY C C   1 
ATOM   5680  O O   . GLY C  1 243 ? -4.573  -22.098  -46.432 1.00 78.99  ? 243 GLY C O   1 
ATOM   5681  N N   . ASP C  1 244 ? -6.699  -22.822  -46.581 1.00 65.29  ? 244 ASP C N   1 
ATOM   5682  C CA  . ASP C  1 244 ? -6.536  -23.413  -47.902 1.00 63.83  ? 244 ASP C CA  1 
ATOM   5683  C C   . ASP C  1 244 ? -7.061  -22.446  -48.958 1.00 56.55  ? 244 ASP C C   1 
ATOM   5684  O O   . ASP C  1 244 ? -7.874  -21.574  -48.656 1.00 65.13  ? 244 ASP C O   1 
ATOM   5685  C CB  . ASP C  1 244 ? -7.291  -24.742  -47.977 1.00 68.01  ? 244 ASP C CB  1 
ATOM   5686  C CG  . ASP C  1 244 ? -6.954  -25.541  -49.222 1.00 81.29  ? 244 ASP C CG  1 
ATOM   5687  O OD1 . ASP C  1 244 ? -7.513  -26.647  -49.384 1.00 89.82  ? 244 ASP C OD1 1 
ATOM   5688  O OD2 . ASP C  1 244 ? -6.132  -25.071  -50.036 1.00 68.50  ? 244 ASP C OD2 1 
ATOM   5689  N N   . LYS C  1 245 ? -6.592  -22.593  -50.192 1.00 54.04  ? 245 LYS C N   1 
ATOM   5690  C CA  . LYS C  1 245 ? -7.063  -21.742  -51.279 1.00 65.02  ? 245 LYS C CA  1 
ATOM   5691  C C   . LYS C  1 245 ? -7.554  -22.565  -52.465 1.00 57.13  ? 245 LYS C C   1 
ATOM   5692  O O   . LYS C  1 245 ? -7.083  -23.678  -52.702 1.00 64.27  ? 245 LYS C O   1 
ATOM   5693  C CB  . LYS C  1 245 ? -5.964  -20.778  -51.730 1.00 79.34  ? 245 LYS C CB  1 
ATOM   5694  C CG  . LYS C  1 245 ? -4.888  -21.421  -52.585 1.00 72.62  ? 245 LYS C CG  1 
ATOM   5695  C CD  . LYS C  1 245 ? -3.823  -20.414  -52.974 1.00 79.36  ? 245 LYS C CD  1 
ATOM   5696  C CE  . LYS C  1 245 ? -2.780  -21.042  -53.879 1.00 88.87  ? 245 LYS C CE  1 
ATOM   5697  N NZ  . LYS C  1 245 ? -1.590  -20.165  -54.033 1.00 84.01  ? 245 LYS C NZ  1 
ATOM   5698  N N   . ILE C  1 246 ? -8.504  -22.005  -53.205 1.00 53.16  ? 246 ILE C N   1 
ATOM   5699  C CA  . ILE C  1 246 ? -9.056  -22.667  -54.380 1.00 50.82  ? 246 ILE C CA  1 
ATOM   5700  C C   . ILE C  1 246 ? -8.838  -21.811  -55.626 1.00 57.38  ? 246 ILE C C   1 
ATOM   5701  O O   . ILE C  1 246 ? -9.098  -20.608  -55.618 1.00 50.15  ? 246 ILE C O   1 
ATOM   5702  C CB  . ILE C  1 246 ? -10.557 -22.966  -54.203 1.00 54.44  ? 246 ILE C CB  1 
ATOM   5703  C CG1 . ILE C  1 246 ? -11.111 -23.686  -55.434 1.00 58.85  ? 246 ILE C CG1 1 
ATOM   5704  C CG2 . ILE C  1 246 ? -11.331 -21.685  -53.931 1.00 41.74  ? 246 ILE C CG2 1 
ATOM   5705  C CD1 . ILE C  1 246 ? -12.600 -23.952  -55.364 1.00 45.07  ? 246 ILE C CD1 1 
ATOM   5706  N N   . THR C  1 247 ? -8.356  -22.440  -56.693 1.00 68.22  ? 247 THR C N   1 
ATOM   5707  C CA  . THR C  1 247 ? -8.018  -21.727  -57.919 1.00 71.81  ? 247 THR C CA  1 
ATOM   5708  C C   . THR C  1 247 ? -8.982  -22.031  -59.062 1.00 63.64  ? 247 THR C C   1 
ATOM   5709  O O   . THR C  1 247 ? -9.375  -23.179  -59.271 1.00 61.07  ? 247 THR C O   1 
ATOM   5710  C CB  . THR C  1 247 ? -6.583  -22.058  -58.379 1.00 70.70  ? 247 THR C CB  1 
ATOM   5711  O OG1 . THR C  1 247 ? -5.641  -21.439  -57.493 1.00 75.14  ? 247 THR C OG1 1 
ATOM   5712  C CG2 . THR C  1 247 ? -6.342  -21.554  -59.796 1.00 82.45  ? 247 THR C CG2 1 
ATOM   5713  N N   . PHE C  1 248 ? -9.358  -20.988  -59.796 1.00 65.09  ? 248 PHE C N   1 
ATOM   5714  C CA  . PHE C  1 248 ? -10.172 -21.135  -60.996 1.00 64.52  ? 248 PHE C CA  1 
ATOM   5715  C C   . PHE C  1 248 ? -9.381  -20.703  -62.228 1.00 66.65  ? 248 PHE C C   1 
ATOM   5716  O O   . PHE C  1 248 ? -8.700  -19.677  -62.213 1.00 76.01  ? 248 PHE C O   1 
ATOM   5717  C CB  . PHE C  1 248 ? -11.463 -20.322  -60.879 1.00 46.23  ? 248 PHE C CB  1 
ATOM   5718  C CG  . PHE C  1 248 ? -12.439 -20.874  -59.878 1.00 49.24  ? 248 PHE C CG  1 
ATOM   5719  C CD1 . PHE C  1 248 ? -12.300 -20.597  -58.529 1.00 50.76  ? 248 PHE C CD1 1 
ATOM   5720  C CD2 . PHE C  1 248 ? -13.500 -21.664  -60.288 1.00 52.21  ? 248 PHE C CD2 1 
ATOM   5721  C CE1 . PHE C  1 248 ? -13.197 -21.102  -57.606 1.00 46.55  ? 248 PHE C CE1 1 
ATOM   5722  C CE2 . PHE C  1 248 ? -14.401 -22.172  -59.370 1.00 52.68  ? 248 PHE C CE2 1 
ATOM   5723  C CZ  . PHE C  1 248 ? -14.249 -21.890  -58.028 1.00 45.63  ? 248 PHE C CZ  1 
ATOM   5724  N N   . GLU C  1 249 ? -9.475  -21.492  -63.293 1.00 58.58  ? 249 GLU C N   1 
ATOM   5725  C CA  . GLU C  1 249 ? -8.715  -21.236  -64.511 1.00 59.46  ? 249 GLU C CA  1 
ATOM   5726  C C   . GLU C  1 249 ? -9.496  -21.682  -65.743 1.00 60.25  ? 249 GLU C C   1 
ATOM   5727  O O   . GLU C  1 249 ? -9.651  -22.878  -65.992 1.00 66.76  ? 249 GLU C O   1 
ATOM   5728  C CB  . GLU C  1 249 ? -7.365  -21.954  -64.447 1.00 70.69  ? 249 GLU C CB  1 
ATOM   5729  C CG  . GLU C  1 249 ? -6.519  -21.824  -65.701 1.00 89.43  ? 249 GLU C CG  1 
ATOM   5730  C CD  . GLU C  1 249 ? -5.188  -22.541  -65.575 1.00 98.31  ? 249 GLU C CD  1 
ATOM   5731  O OE1 . GLU C  1 249 ? -4.576  -22.853  -66.617 1.00 110.26 ? 249 GLU C OE1 1 
ATOM   5732  O OE2 . GLU C  1 249 ? -4.757  -22.799  -64.431 1.00 85.81  ? 249 GLU C OE2 1 
ATOM   5733  N N   . ALA C  1 250 ? -9.980  -20.716  -66.518 1.00 65.01  ? 250 ALA C N   1 
ATOM   5734  C CA  . ALA C  1 250 ? -10.876 -21.021  -67.628 1.00 61.87  ? 250 ALA C CA  1 
ATOM   5735  C C   . ALA C  1 250 ? -10.575 -20.246  -68.910 1.00 74.79  ? 250 ALA C C   1 
ATOM   5736  O O   . ALA C  1 250 ? -10.163 -19.087  -68.873 1.00 66.72  ? 250 ALA C O   1 
ATOM   5737  C CB  . ALA C  1 250 ? -12.322 -20.793  -67.208 1.00 55.30  ? 250 ALA C CB  1 
ATOM   5738  N N   . THR C  1 251 ? -10.793 -20.907  -70.042 1.00 71.07  ? 251 THR C N   1 
ATOM   5739  C CA  . THR C  1 251 ? -10.754 -20.251  -71.342 1.00 63.25  ? 251 THR C CA  1 
ATOM   5740  C C   . THR C  1 251 ? -12.184 -20.100  -71.844 1.00 67.21  ? 251 THR C C   1 
ATOM   5741  O O   . THR C  1 251 ? -12.424 -19.837  -73.024 1.00 72.34  ? 251 THR C O   1 
ATOM   5742  C CB  . THR C  1 251 ? -9.930  -21.055  -72.359 1.00 62.15  ? 251 THR C CB  1 
ATOM   5743  O OG1 . THR C  1 251 ? -10.333 -22.429  -72.320 1.00 73.16  ? 251 THR C OG1 1 
ATOM   5744  C CG2 . THR C  1 251 ? -8.449  -20.965  -72.030 1.00 61.33  ? 251 THR C CG2 1 
ATOM   5745  N N   . GLY C  1 252 ? -13.131 -20.272  -70.927 1.00 66.90  ? 252 GLY C N   1 
ATOM   5746  C CA  . GLY C  1 252 ? -14.542 -20.171  -71.242 1.00 66.62  ? 252 GLY C CA  1 
ATOM   5747  C C   . GLY C  1 252 ? -15.371 -21.228  -70.537 1.00 69.06  ? 252 GLY C C   1 
ATOM   5748  O O   . GLY C  1 252 ? -14.830 -22.152  -69.928 1.00 68.02  ? 252 GLY C O   1 
ATOM   5749  N N   . ASN C  1 253 ? -16.690 -21.078  -70.616 1.00 61.70  ? 253 ASN C N   1 
ATOM   5750  C CA  . ASN C  1 253 ? -17.638 -22.073  -70.115 1.00 56.48  ? 253 ASN C CA  1 
ATOM   5751  C C   . ASN C  1 253 ? -17.746 -22.155  -68.593 1.00 63.72  ? 253 ASN C C   1 
ATOM   5752  O O   . ASN C  1 253 ? -18.382 -23.060  -68.055 1.00 60.71  ? 253 ASN C O   1 
ATOM   5753  C CB  . ASN C  1 253 ? -17.339 -23.452  -70.712 1.00 61.88  ? 253 ASN C CB  1 
ATOM   5754  C CG  . ASN C  1 253 ? -17.330 -23.441  -72.230 1.00 60.35  ? 253 ASN C CG  1 
ATOM   5755  O OD1 . ASN C  1 253 ? -18.231 -23.980  -72.872 1.00 63.11  ? 253 ASN C OD1 1 
ATOM   5756  N ND2 . ASN C  1 253 ? -16.313 -22.818  -72.811 1.00 56.66  ? 253 ASN C ND2 1 
ATOM   5757  N N   . LEU C  1 254 ? -17.144 -21.195  -67.903 1.00 68.01  ? 254 LEU C N   1 
ATOM   5758  C CA  . LEU C  1 254 ? -17.109 -21.224  -66.447 1.00 54.08  ? 254 LEU C CA  1 
ATOM   5759  C C   . LEU C  1 254 ? -18.109 -20.271  -65.790 1.00 50.06  ? 254 LEU C C   1 
ATOM   5760  O O   . LEU C  1 254 ? -17.940 -19.054  -65.838 1.00 60.81  ? 254 LEU C O   1 
ATOM   5761  C CB  . LEU C  1 254 ? -15.695 -20.906  -65.955 1.00 55.58  ? 254 LEU C CB  1 
ATOM   5762  C CG  . LEU C  1 254 ? -15.547 -20.781  -64.440 1.00 50.29  ? 254 LEU C CG  1 
ATOM   5763  C CD1 . LEU C  1 254 ? -15.978 -22.073  -63.771 1.00 56.14  ? 254 LEU C CD1 1 
ATOM   5764  C CD2 . LEU C  1 254 ? -14.127 -20.411  -64.044 1.00 46.56  ? 254 LEU C CD2 1 
ATOM   5765  N N   . VAL C  1 255 ? -19.148 -20.824  -65.173 1.00 50.26  ? 255 VAL C N   1 
ATOM   5766  C CA  . VAL C  1 255 ? -20.024 -20.029  -64.317 1.00 43.43  ? 255 VAL C CA  1 
ATOM   5767  C C   . VAL C  1 255 ? -19.348 -19.800  -62.970 1.00 51.52  ? 255 VAL C C   1 
ATOM   5768  O O   . VAL C  1 255 ? -19.457 -20.623  -62.058 1.00 50.15  ? 255 VAL C O   1 
ATOM   5769  C CB  . VAL C  1 255 ? -21.365 -20.723  -64.086 1.00 44.22  ? 255 VAL C CB  1 
ATOM   5770  C CG1 . VAL C  1 255 ? -22.287 -19.838  -63.243 1.00 48.63  ? 255 VAL C CG1 1 
ATOM   5771  C CG2 . VAL C  1 255 ? -21.998 -21.062  -65.413 1.00 43.31  ? 255 VAL C CG2 1 
ATOM   5772  N N   . VAL C  1 256 ? -18.650 -18.676  -62.850 1.00 58.59  ? 256 VAL C N   1 
ATOM   5773  C CA  . VAL C  1 256 ? -17.827 -18.407  -61.677 1.00 52.62  ? 256 VAL C CA  1 
ATOM   5774  C C   . VAL C  1 256 ? -18.655 -18.129  -60.429 1.00 52.59  ? 256 VAL C C   1 
ATOM   5775  O O   . VAL C  1 256 ? -19.780 -17.639  -60.515 1.00 56.45  ? 256 VAL C O   1 
ATOM   5776  C CB  . VAL C  1 256 ? -16.868 -17.228  -61.923 1.00 56.83  ? 256 VAL C CB  1 
ATOM   5777  C CG1 . VAL C  1 256 ? -16.002 -17.502  -63.141 1.00 54.91  ? 256 VAL C CG1 1 
ATOM   5778  C CG2 . VAL C  1 256 ? -17.650 -15.936  -62.099 1.00 64.80  ? 256 VAL C CG2 1 
ATOM   5779  N N   . PRO C  1 257 ? -18.094 -18.459  -59.258 1.00 48.29  ? 257 PRO C N   1 
ATOM   5780  C CA  . PRO C  1 257 ? -18.724 -18.170  -57.968 1.00 45.27  ? 257 PRO C CA  1 
ATOM   5781  C C   . PRO C  1 257 ? -18.758 -16.669  -57.721 1.00 50.73  ? 257 PRO C C   1 
ATOM   5782  O O   . PRO C  1 257 ? -17.814 -15.970  -58.086 1.00 57.45  ? 257 PRO C O   1 
ATOM   5783  C CB  . PRO C  1 257 ? -17.779 -18.834  -56.959 1.00 43.67  ? 257 PRO C CB  1 
ATOM   5784  C CG  . PRO C  1 257 ? -16.992 -19.825  -57.748 1.00 54.67  ? 257 PRO C CG  1 
ATOM   5785  C CD  . PRO C  1 257 ? -16.846 -19.225  -59.105 1.00 44.96  ? 257 PRO C CD  1 
ATOM   5786  N N   . ARG C  1 258 ? -19.837 -16.180  -57.121 1.00 55.54  ? 258 ARG C N   1 
ATOM   5787  C CA  . ARG C  1 258 ? -19.905 -14.788  -56.695 1.00 56.03  ? 258 ARG C CA  1 
ATOM   5788  C C   . ARG C  1 258 ? -19.956 -14.741  -55.174 1.00 51.63  ? 258 ARG C C   1 
ATOM   5789  O O   . ARG C  1 258 ? -19.191 -14.019  -54.537 1.00 55.76  ? 258 ARG C O   1 
ATOM   5790  C CB  . ARG C  1 258 ? -21.127 -14.091  -57.298 1.00 55.56  ? 258 ARG C CB  1 
ATOM   5791  C CG  . ARG C  1 258 ? -21.320 -12.647  -56.847 1.00 60.99  ? 258 ARG C CG  1 
ATOM   5792  C CD  . ARG C  1 258 ? -22.539 -12.035  -57.523 1.00 65.92  ? 258 ARG C CD  1 
ATOM   5793  N NE  . ARG C  1 258 ? -23.115 -10.927  -56.763 1.00 72.79  ? 258 ARG C NE  1 
ATOM   5794  C CZ  . ARG C  1 258 ? -22.867 -9.644   -57.003 1.00 84.13  ? 258 ARG C CZ  1 
ATOM   5795  N NH1 . ARG C  1 258 ? -22.047 -9.298   -57.982 1.00 90.04  ? 258 ARG C NH1 1 
ATOM   5796  N NH2 . ARG C  1 258 ? -23.441 -8.705   -56.263 1.00 88.71  ? 258 ARG C NH2 1 
ATOM   5797  N N   . TYR C  1 259 ? -20.859 -15.530  -54.600 1.00 50.08  ? 259 TYR C N   1 
ATOM   5798  C CA  . TYR C  1 259 ? -20.977 -15.648  -53.153 1.00 50.97  ? 259 TYR C CA  1 
ATOM   5799  C C   . TYR C  1 259 ? -20.614 -17.050  -52.687 1.00 57.32  ? 259 TYR C C   1 
ATOM   5800  O O   . TYR C  1 259 ? -21.069 -18.039  -53.259 1.00 59.08  ? 259 TYR C O   1 
ATOM   5801  C CB  . TYR C  1 259 ? -22.404 -15.344  -52.703 1.00 57.39  ? 259 TYR C CB  1 
ATOM   5802  C CG  . TYR C  1 259 ? -22.798 -13.892  -52.783 1.00 73.06  ? 259 TYR C CG  1 
ATOM   5803  C CD1 . TYR C  1 259 ? -23.347 -13.365  -53.942 1.00 70.92  ? 259 TYR C CD1 1 
ATOM   5804  C CD2 . TYR C  1 259 ? -22.638 -13.051  -51.690 1.00 75.14  ? 259 TYR C CD2 1 
ATOM   5805  C CE1 . TYR C  1 259 ? -23.717 -12.039  -54.015 1.00 77.97  ? 259 TYR C CE1 1 
ATOM   5806  C CE2 . TYR C  1 259 ? -23.004 -11.724  -51.753 1.00 75.20  ? 259 TYR C CE2 1 
ATOM   5807  C CZ  . TYR C  1 259 ? -23.544 -11.223  -52.917 1.00 79.99  ? 259 TYR C CZ  1 
ATOM   5808  O OH  . TYR C  1 259 ? -23.913 -9.900   -52.978 1.00 85.84  ? 259 TYR C OH  1 
ATOM   5809  N N   . ALA C  1 260 ? -19.802 -17.129  -51.640 1.00 54.78  ? 260 ALA C N   1 
ATOM   5810  C CA  . ALA C  1 260 ? -19.502 -18.403  -51.002 1.00 44.20  ? 260 ALA C CA  1 
ATOM   5811  C C   . ALA C  1 260 ? -20.164 -18.450  -49.630 1.00 48.62  ? 260 ALA C C   1 
ATOM   5812  O O   . ALA C  1 260 ? -20.924 -17.550  -49.272 1.00 49.63  ? 260 ALA C O   1 
ATOM   5813  C CB  . ALA C  1 260 ? -18.003 -18.600  -50.884 1.00 49.52  ? 260 ALA C CB  1 
ATOM   5814  N N   . PHE C  1 261 ? -19.877 -19.493  -48.858 1.00 51.92  ? 261 PHE C N   1 
ATOM   5815  C CA  . PHE C  1 261 ? -20.500 -19.641  -47.548 1.00 40.37  ? 261 PHE C CA  1 
ATOM   5816  C C   . PHE C  1 261 ? -19.528 -20.098  -46.463 1.00 45.30  ? 261 PHE C C   1 
ATOM   5817  O O   . PHE C  1 261 ? -19.102 -21.254  -46.447 1.00 60.84  ? 261 PHE C O   1 
ATOM   5818  C CB  . PHE C  1 261 ? -21.682 -20.612  -47.624 1.00 38.33  ? 261 PHE C CB  1 
ATOM   5819  C CG  . PHE C  1 261 ? -22.745 -20.202  -48.603 1.00 44.39  ? 261 PHE C CG  1 
ATOM   5820  C CD1 . PHE C  1 261 ? -22.710 -20.651  -49.913 1.00 47.39  ? 261 PHE C CD1 1 
ATOM   5821  C CD2 . PHE C  1 261 ? -23.780 -19.369  -48.213 1.00 44.81  ? 261 PHE C CD2 1 
ATOM   5822  C CE1 . PHE C  1 261 ? -23.689 -20.276  -50.816 1.00 54.00  ? 261 PHE C CE1 1 
ATOM   5823  C CE2 . PHE C  1 261 ? -24.762 -18.991  -49.110 1.00 38.48  ? 261 PHE C CE2 1 
ATOM   5824  C CZ  . PHE C  1 261 ? -24.716 -19.444  -50.414 1.00 46.34  ? 261 PHE C CZ  1 
ATOM   5825  N N   . ALA C  1 262 ? -19.179 -19.185  -45.561 1.00 53.05  ? 262 ALA C N   1 
ATOM   5826  C CA  . ALA C  1 262 ? -18.432 -19.550  -44.364 1.00 55.41  ? 262 ALA C CA  1 
ATOM   5827  C C   . ALA C  1 262 ? -19.345 -20.423  -43.518 1.00 58.48  ? 262 ALA C C   1 
ATOM   5828  O O   . ALA C  1 262 ? -20.457 -20.020  -43.177 1.00 55.54  ? 262 ALA C O   1 
ATOM   5829  C CB  . ALA C  1 262 ? -18.010 -18.313  -43.598 1.00 62.61  ? 262 ALA C CB  1 
ATOM   5830  N N   . MET C  1 263 ? -18.879 -21.620  -43.182 1.00 51.66  ? 263 MET C N   1 
ATOM   5831  C CA  . MET C  1 263 ? -19.773 -22.636  -42.646 1.00 56.60  ? 263 MET C CA  1 
ATOM   5832  C C   . MET C  1 263 ? -19.119 -23.558  -41.622 1.00 55.80  ? 263 MET C C   1 
ATOM   5833  O O   . MET C  1 263 ? -18.045 -24.110  -41.858 1.00 63.84  ? 263 MET C O   1 
ATOM   5834  C CB  . MET C  1 263 ? -20.337 -23.467  -43.800 1.00 57.54  ? 263 MET C CB  1 
ATOM   5835  C CG  . MET C  1 263 ? -21.393 -24.474  -43.401 1.00 55.54  ? 263 MET C CG  1 
ATOM   5836  S SD  . MET C  1 263 ? -21.882 -25.510  -44.791 1.00 73.55  ? 263 MET C SD  1 
ATOM   5837  C CE  . MET C  1 263 ? -20.379 -26.445  -45.069 1.00 64.98  ? 263 MET C CE  1 
ATOM   5838  N N   . GLU C  1 264 ? -19.785 -23.720  -40.484 1.00 53.53  ? 264 GLU C N   1 
ATOM   5839  C CA  . GLU C  1 264 ? -19.379 -24.692  -39.479 1.00 58.18  ? 264 GLU C CA  1 
ATOM   5840  C C   . GLU C  1 264 ? -20.514 -25.684  -39.272 1.00 60.07  ? 264 GLU C C   1 
ATOM   5841  O O   . GLU C  1 264 ? -21.580 -25.321  -38.780 1.00 68.02  ? 264 GLU C O   1 
ATOM   5842  C CB  . GLU C  1 264 ? -19.033 -23.995  -38.164 1.00 62.37  ? 264 GLU C CB  1 
ATOM   5843  C CG  . GLU C  1 264 ? -17.554 -24.034  -37.816 1.00 87.11  ? 264 GLU C CG  1 
ATOM   5844  C CD  . GLU C  1 264 ? -17.158 -22.947  -36.837 1.00 105.01 ? 264 GLU C CD  1 
ATOM   5845  O OE1 . GLU C  1 264 ? -16.380 -23.238  -35.904 1.00 107.98 ? 264 GLU C OE1 1 
ATOM   5846  O OE2 . GLU C  1 264 ? -17.628 -21.801  -36.999 1.00 111.92 ? 264 GLU C OE2 1 
ATOM   5847  N N   . ARG C  1 265 ? -20.285 -26.934  -39.657 1.00 65.51  ? 265 ARG C N   1 
ATOM   5848  C CA  . ARG C  1 265 ? -21.344 -27.935  -39.642 1.00 67.46  ? 265 ARG C CA  1 
ATOM   5849  C C   . ARG C  1 265 ? -21.174 -28.989  -38.554 1.00 66.92  ? 265 ARG C C   1 
ATOM   5850  O O   . ARG C  1 265 ? -20.060 -29.414  -38.247 1.00 67.30  ? 265 ARG C O   1 
ATOM   5851  C CB  . ARG C  1 265 ? -21.459 -28.608  -41.012 1.00 56.81  ? 265 ARG C CB  1 
ATOM   5852  C CG  . ARG C  1 265 ? -20.131 -28.778  -41.731 1.00 59.77  ? 265 ARG C CG  1 
ATOM   5853  C CD  . ARG C  1 265 ? -20.312 -29.451  -43.082 1.00 65.69  ? 265 ARG C CD  1 
ATOM   5854  N NE  . ARG C  1 265 ? -19.897 -30.850  -43.055 1.00 71.14  ? 265 ARG C NE  1 
ATOM   5855  C CZ  . ARG C  1 265 ? -18.668 -31.267  -43.340 1.00 71.57  ? 265 ARG C CZ  1 
ATOM   5856  N NH1 . ARG C  1 265 ? -17.731 -30.391  -43.675 1.00 71.03  ? 265 ARG C NH1 1 
ATOM   5857  N NH2 . ARG C  1 265 ? -18.374 -32.558  -43.291 1.00 78.04  ? 265 ARG C NH2 1 
ATOM   5858  N N   . ASN C  1 266 ? -22.297 -29.395  -37.974 1.00 73.51  ? 266 ASN C N   1 
ATOM   5859  C CA  . ASN C  1 266 ? -22.328 -30.498  -37.026 1.00 81.78  ? 266 ASN C CA  1 
ATOM   5860  C C   . ASN C  1 266 ? -23.065 -31.686  -37.629 1.00 81.01  ? 266 ASN C C   1 
ATOM   5861  O O   . ASN C  1 266 ? -24.158 -31.540  -38.175 1.00 80.03  ? 266 ASN C O   1 
ATOM   5862  C CB  . ASN C  1 266 ? -22.978 -30.062  -35.712 1.00 96.41  ? 266 ASN C CB  1 
ATOM   5863  C CG  . ASN C  1 266 ? -23.964 -28.925  -35.898 1.00 85.46  ? 266 ASN C CG  1 
ATOM   5864  O OD1 . ASN C  1 266 ? -23.845 -27.876  -35.264 1.00 67.21  ? 266 ASN C OD1 1 
ATOM   5865  N ND2 . ASN C  1 266 ? -24.941 -29.124  -36.775 1.00 88.04  ? 266 ASN C ND2 1 
ATOM   5866  N N   . ALA C  1 267 ? -22.457 -32.862  -37.537 1.00 77.66  ? 267 ALA C N   1 
ATOM   5867  C CA  . ALA C  1 267 ? -22.993 -34.051  -38.188 1.00 93.33  ? 267 ALA C CA  1 
ATOM   5868  C C   . ALA C  1 267 ? -24.238 -34.593  -37.493 1.00 87.96  ? 267 ALA C C   1 
ATOM   5869  O O   . ALA C  1 267 ? -24.432 -34.388  -36.294 1.00 74.12  ? 267 ALA C O   1 
ATOM   5870  C CB  . ALA C  1 267 ? -21.923 -35.130  -38.265 1.00 97.41  ? 267 ALA C CB  1 
ATOM   5871  N N   . GLY C  1 268 ? -25.086 -35.275  -38.258 1.00 86.85  ? 268 GLY C N   1 
ATOM   5872  C CA  . GLY C  1 268 ? -26.150 -36.077  -37.680 1.00 93.97  ? 268 GLY C CA  1 
ATOM   5873  C C   . GLY C  1 268 ? -27.580 -35.565  -37.717 1.00 91.28  ? 268 GLY C C   1 
ATOM   5874  O O   . GLY C  1 268 ? -28.392 -35.978  -36.890 1.00 87.21  ? 268 GLY C O   1 
ATOM   5875  N N   . SER C  1 269 ? -27.910 -34.687  -38.659 1.00 73.11  ? 269 SER C N   1 
ATOM   5876  C CA  . SER C  1 269 ? -29.298 -34.246  -38.798 1.00 61.10  ? 269 SER C CA  1 
ATOM   5877  C C   . SER C  1 269 ? -29.932 -34.800  -40.070 1.00 61.81  ? 269 SER C C   1 
ATOM   5878  O O   . SER C  1 269 ? -29.490 -35.821  -40.595 1.00 71.91  ? 269 SER C O   1 
ATOM   5879  C CB  . SER C  1 269 ? -29.406 -32.721  -38.767 1.00 55.95  ? 269 SER C CB  1 
ATOM   5880  O OG  . SER C  1 269 ? -30.764 -32.312  -38.734 1.00 43.44  ? 269 SER C OG  1 
ATOM   5881  N N   . GLY C  1 270 ? -30.970 -34.128  -40.559 1.00 47.11  ? 270 GLY C N   1 
ATOM   5882  C CA  . GLY C  1 270 ? -31.667 -34.582  -41.747 1.00 47.47  ? 270 GLY C CA  1 
ATOM   5883  C C   . GLY C  1 270 ? -32.493 -33.512  -42.432 1.00 36.68  ? 270 GLY C C   1 
ATOM   5884  O O   . GLY C  1 270 ? -32.408 -32.330  -42.099 1.00 40.87  ? 270 GLY C O   1 
ATOM   5885  N N   . ILE C  1 271 ? -33.297 -33.939  -43.399 1.00 39.12  ? 271 ILE C N   1 
ATOM   5886  C CA  . ILE C  1 271 ? -34.146 -33.036  -44.163 1.00 34.02  ? 271 ILE C CA  1 
ATOM   5887  C C   . ILE C  1 271 ? -35.565 -33.583  -44.223 1.00 42.39  ? 271 ILE C C   1 
ATOM   5888  O O   . ILE C  1 271 ? -35.798 -34.666  -44.761 1.00 60.20  ? 271 ILE C O   1 
ATOM   5889  C CB  . ILE C  1 271 ? -33.614 -32.859  -45.594 1.00 38.85  ? 271 ILE C CB  1 
ATOM   5890  C CG1 . ILE C  1 271 ? -32.195 -32.289  -45.561 1.00 35.39  ? 271 ILE C CG1 1 
ATOM   5891  C CG2 . ILE C  1 271 ? -34.544 -31.966  -46.405 1.00 48.30  ? 271 ILE C CG2 1 
ATOM   5892  C CD1 . ILE C  1 271 ? -31.392 -32.579  -46.806 1.00 46.11  ? 271 ILE C CD1 1 
ATOM   5893  N N   . ILE C  1 272 ? -36.510 -32.835  -43.666 1.00 48.22  ? 272 ILE C N   1 
ATOM   5894  C CA  . ILE C  1 272 ? -37.904 -33.257  -43.651 1.00 51.31  ? 272 ILE C CA  1 
ATOM   5895  C C   . ILE C  1 272 ? -38.699 -32.604  -44.774 1.00 46.33  ? 272 ILE C C   1 
ATOM   5896  O O   . ILE C  1 272 ? -38.724 -31.380  -44.899 1.00 47.04  ? 272 ILE C O   1 
ATOM   5897  C CB  . ILE C  1 272 ? -38.581 -32.931  -42.306 1.00 37.74  ? 272 ILE C CB  1 
ATOM   5898  C CG1 . ILE C  1 272 ? -37.899 -33.691  -41.168 1.00 43.93  ? 272 ILE C CG1 1 
ATOM   5899  C CG2 . ILE C  1 272 ? -40.059 -33.274  -42.358 1.00 49.87  ? 272 ILE C CG2 1 
ATOM   5900  C CD1 . ILE C  1 272 ? -38.581 -33.523  -39.826 1.00 52.81  ? 272 ILE C CD1 1 
ATOM   5901  N N   . ILE C  1 273 ? -39.340 -33.430  -45.594 1.00 48.35  ? 273 ILE C N   1 
ATOM   5902  C CA  . ILE C  1 273 ? -40.234 -32.934  -46.631 1.00 51.48  ? 273 ILE C CA  1 
ATOM   5903  C C   . ILE C  1 273 ? -41.670 -32.998  -46.126 1.00 57.66  ? 273 ILE C C   1 
ATOM   5904  O O   . ILE C  1 273 ? -42.275 -34.070  -46.080 1.00 52.47  ? 273 ILE C O   1 
ATOM   5905  C CB  . ILE C  1 273 ? -40.110 -33.741  -47.938 1.00 52.42  ? 273 ILE C CB  1 
ATOM   5906  C CG1 . ILE C  1 273 ? -38.684 -33.661  -48.492 1.00 57.82  ? 273 ILE C CG1 1 
ATOM   5907  C CG2 . ILE C  1 273 ? -41.105 -33.236  -48.972 1.00 66.97  ? 273 ILE C CG2 1 
ATOM   5908  C CD1 . ILE C  1 273 ? -37.699 -34.592  -47.812 1.00 72.60  ? 273 ILE C CD1 1 
ATOM   5909  N N   . SER C  1 274 ? -42.208 -31.846  -45.740 1.00 66.22  ? 274 SER C N   1 
ATOM   5910  C CA  . SER C  1 274 ? -43.529 -31.788  -45.128 1.00 64.20  ? 274 SER C CA  1 
ATOM   5911  C C   . SER C  1 274 ? -44.228 -30.455  -45.378 1.00 67.74  ? 274 SER C C   1 
ATOM   5912  O O   . SER C  1 274 ? -43.580 -29.434  -45.610 1.00 73.07  ? 274 SER C O   1 
ATOM   5913  C CB  . SER C  1 274 ? -43.420 -32.041  -43.623 1.00 58.35  ? 274 SER C CB  1 
ATOM   5914  O OG  . SER C  1 274 ? -44.579 -31.593  -42.944 1.00 65.98  ? 274 SER C OG  1 
ATOM   5915  N N   . ASP C  1 275 ? -45.557 -30.477  -45.329 1.00 85.28  ? 275 ASP C N   1 
ATOM   5916  C CA  . ASP C  1 275 ? -46.358 -29.268  -45.466 1.00 84.12  ? 275 ASP C CA  1 
ATOM   5917  C C   . ASP C  1 275 ? -46.588 -28.640  -44.096 1.00 76.23  ? 275 ASP C C   1 
ATOM   5918  O O   . ASP C  1 275 ? -46.876 -27.448  -43.987 1.00 89.75  ? 275 ASP C O   1 
ATOM   5919  C CB  . ASP C  1 275 ? -47.706 -29.588  -46.117 1.00 105.80 ? 275 ASP C CB  1 
ATOM   5920  C CG  . ASP C  1 275 ? -47.559 -30.200  -47.496 1.00 122.61 ? 275 ASP C CG  1 
ATOM   5921  O OD1 . ASP C  1 275 ? -47.712 -31.433  -47.620 1.00 135.71 ? 275 ASP C OD1 1 
ATOM   5922  O OD2 . ASP C  1 275 ? -47.296 -29.447  -48.458 1.00 106.75 ? 275 ASP C OD2 1 
ATOM   5923  N N   . THR C  1 276 ? -46.458 -29.461  -43.058 1.00 70.35  ? 276 THR C N   1 
ATOM   5924  C CA  . THR C  1 276 ? -46.682 -29.039  -41.677 1.00 66.61  ? 276 THR C CA  1 
ATOM   5925  C C   . THR C  1 276 ? -46.084 -27.666  -41.375 1.00 67.50  ? 276 THR C C   1 
ATOM   5926  O O   . THR C  1 276 ? -44.961 -27.368  -41.782 1.00 58.99  ? 276 THR C O   1 
ATOM   5927  C CB  . THR C  1 276 ? -46.106 -30.073  -40.686 1.00 59.14  ? 276 THR C CB  1 
ATOM   5928  O OG1 . THR C  1 276 ? -46.689 -31.357  -40.940 1.00 60.06  ? 276 THR C OG1 1 
ATOM   5929  C CG2 . THR C  1 276 ? -46.389 -29.666  -39.247 1.00 58.27  ? 276 THR C CG2 1 
ATOM   5930  N N   . PRO C  1 277 ? -46.844 -26.824  -40.658 1.00 69.60  ? 277 PRO C N   1 
ATOM   5931  C CA  . PRO C  1 277 ? -46.425 -25.467  -40.290 1.00 65.54  ? 277 PRO C CA  1 
ATOM   5932  C C   . PRO C  1 277 ? -45.197 -25.447  -39.385 1.00 65.71  ? 277 PRO C C   1 
ATOM   5933  O O   . PRO C  1 277 ? -45.110 -26.238  -38.445 1.00 71.95  ? 277 PRO C O   1 
ATOM   5934  C CB  . PRO C  1 277 ? -47.634 -24.924  -39.518 1.00 74.78  ? 277 PRO C CB  1 
ATOM   5935  C CG  . PRO C  1 277 ? -48.785 -25.750  -39.970 1.00 89.97  ? 277 PRO C CG  1 
ATOM   5936  C CD  . PRO C  1 277 ? -48.222 -27.111  -40.224 1.00 72.66  ? 277 PRO C CD  1 
ATOM   5937  N N   . VAL C  1 278 ? -44.261 -24.548  -39.672 1.00 60.79  ? 278 VAL C N   1 
ATOM   5938  C CA  . VAL C  1 278 ? -43.134 -24.309  -38.781 1.00 65.85  ? 278 VAL C CA  1 
ATOM   5939  C C   . VAL C  1 278 ? -43.630 -23.503  -37.586 1.00 66.92  ? 278 VAL C C   1 
ATOM   5940  O O   . VAL C  1 278 ? -44.505 -22.648  -37.729 1.00 76.81  ? 278 VAL C O   1 
ATOM   5941  C CB  . VAL C  1 278 ? -41.997 -23.547  -39.491 1.00 66.11  ? 278 VAL C CB  1 
ATOM   5942  C CG1 . VAL C  1 278 ? -42.523 -22.264  -40.117 1.00 86.04  ? 278 VAL C CG1 1 
ATOM   5943  C CG2 . VAL C  1 278 ? -40.863 -23.251  -38.519 1.00 46.64  ? 278 VAL C CG2 1 
ATOM   5944  N N   . HIS C  1 279 ? -43.080 -23.777  -36.408 1.00 68.42  ? 279 HIS C N   1 
ATOM   5945  C CA  . HIS C  1 279 ? -43.580 -23.157  -35.187 1.00 71.42  ? 279 HIS C CA  1 
ATOM   5946  C C   . HIS C  1 279 ? -42.488 -22.730  -34.216 1.00 73.41  ? 279 HIS C C   1 
ATOM   5947  O O   . HIS C  1 279 ? -41.373 -23.249  -34.242 1.00 78.44  ? 279 HIS C O   1 
ATOM   5948  C CB  . HIS C  1 279 ? -44.553 -24.100  -34.478 1.00 82.45  ? 279 HIS C CB  1 
ATOM   5949  C CG  . HIS C  1 279 ? -45.992 -23.761  -34.703 1.00 95.34  ? 279 HIS C CG  1 
ATOM   5950  N ND1 . HIS C  1 279 ? -46.757 -23.112  -33.759 1.00 98.36  ? 279 HIS C ND1 1 
ATOM   5951  C CD2 . HIS C  1 279 ? -46.803 -23.969  -35.767 1.00 94.67  ? 279 HIS C CD2 1 
ATOM   5952  C CE1 . HIS C  1 279 ? -47.980 -22.942  -34.229 1.00 107.34 ? 279 HIS C CE1 1 
ATOM   5953  N NE2 . HIS C  1 279 ? -48.033 -23.453  -35.447 1.00 97.64  ? 279 HIS C NE2 1 
ATOM   5954  N N   . ASP C  1 280 ? -42.828 -21.775  -33.357 1.00 81.54  ? 280 ASP C N   1 
ATOM   5955  C CA  . ASP C  1 280 ? -41.953 -21.368  -32.268 1.00 89.71  ? 280 ASP C CA  1 
ATOM   5956  C C   . ASP C  1 280 ? -42.234 -22.225  -31.038 1.00 93.38  ? 280 ASP C C   1 
ATOM   5957  O O   . ASP C  1 280 ? -42.921 -21.790  -30.115 1.00 121.31 ? 280 ASP C O   1 
ATOM   5958  C CB  . ASP C  1 280 ? -42.167 -19.889  -31.935 1.00 105.17 ? 280 ASP C CB  1 
ATOM   5959  C CG  . ASP C  1 280 ? -41.361 -19.437  -30.731 1.00 117.19 ? 280 ASP C CG  1 
ATOM   5960  O OD1 . ASP C  1 280 ? -40.393 -20.136  -30.368 1.00 116.62 ? 280 ASP C OD1 1 
ATOM   5961  O OD2 . ASP C  1 280 ? -41.693 -18.384  -30.146 1.00 118.97 ? 280 ASP C OD2 1 
ATOM   5962  N N   . CYS C  1 281 ? -41.705 -23.446  -31.037 1.00 80.70  ? 281 CYS C N   1 
ATOM   5963  C CA  . CYS C  1 281 ? -41.898 -24.379  -29.932 1.00 84.72  ? 281 CYS C CA  1 
ATOM   5964  C C   . CYS C  1 281 ? -40.647 -25.253  -29.723 1.00 74.02  ? 281 CYS C C   1 
ATOM   5965  O O   . CYS C  1 281 ? -39.839 -25.418  -30.632 1.00 70.23  ? 281 CYS C O   1 
ATOM   5966  C CB  . CYS C  1 281 ? -43.139 -25.248  -30.176 1.00 78.18  ? 281 CYS C CB  1 
ATOM   5967  S SG  . CYS C  1 281 ? -43.122 -26.166  -31.738 1.00 114.47 ? 281 CYS C SG  1 
ATOM   5968  N N   . ASN C  1 282 ? -40.493 -25.790  -28.514 1.00 69.08  ? 282 ASN C N   1 
ATOM   5969  C CA  . ASN C  1 282 ? -39.397 -26.693  -28.171 1.00 57.77  ? 282 ASN C CA  1 
ATOM   5970  C C   . ASN C  1 282 ? -39.804 -28.166  -28.326 1.00 66.58  ? 282 ASN C C   1 
ATOM   5971  O O   . ASN C  1 282 ? -40.861 -28.558  -27.841 1.00 73.43  ? 282 ASN C O   1 
ATOM   5972  C CB  . ASN C  1 282 ? -38.948 -26.417  -26.731 1.00 77.25  ? 282 ASN C CB  1 
ATOM   5973  C CG  . ASN C  1 282 ? -38.670 -24.949  -26.474 1.00 95.57  ? 282 ASN C CG  1 
ATOM   5974  O OD1 . ASN C  1 282 ? -38.339 -24.185  -27.388 1.00 89.28  ? 282 ASN C OD1 1 
ATOM   5975  N ND2 . ASN C  1 282 ? -38.799 -24.550  -25.206 1.00 109.59 ? 282 ASN C ND2 1 
ATOM   5976  N N   . THR C  1 283 ? -38.959 -28.986  -28.955 1.00 66.25  ? 283 THR C N   1 
ATOM   5977  C CA  . THR C  1 283 ? -39.202 -30.434  -29.030 1.00 62.34  ? 283 THR C CA  1 
ATOM   5978  C C   . THR C  1 283 ? -37.891 -31.206  -28.944 1.00 46.63  ? 283 THR C C   1 
ATOM   5979  O O   . THR C  1 283 ? -36.835 -30.659  -29.236 1.00 53.04  ? 283 THR C O   1 
ATOM   5980  C CB  . THR C  1 283 ? -39.940 -30.857  -30.325 1.00 52.10  ? 283 THR C CB  1 
ATOM   5981  O OG1 . THR C  1 283 ? -40.322 -32.236  -30.228 1.00 43.48  ? 283 THR C OG1 1 
ATOM   5982  C CG2 . THR C  1 283 ? -39.042 -30.689  -31.536 1.00 46.18  ? 283 THR C CG2 1 
ATOM   5983  N N   . THR C  1 284 ? -37.957 -32.471  -28.539 1.00 39.99  ? 284 THR C N   1 
ATOM   5984  C CA  . THR C  1 284 ? -36.766 -33.319  -28.479 1.00 52.47  ? 284 THR C CA  1 
ATOM   5985  C C   . THR C  1 284 ? -36.807 -34.371  -29.583 1.00 50.46  ? 284 THR C C   1 
ATOM   5986  O O   . THR C  1 284 ? -35.820 -35.065  -29.841 1.00 46.34  ? 284 THR C O   1 
ATOM   5987  C CB  . THR C  1 284 ? -36.633 -34.029  -27.114 1.00 52.52  ? 284 THR C CB  1 
ATOM   5988  O OG1 . THR C  1 284 ? -35.354 -34.671  -27.022 1.00 51.72  ? 284 THR C OG1 1 
ATOM   5989  C CG2 . THR C  1 284 ? -37.731 -35.068  -26.948 1.00 49.35  ? 284 THR C CG2 1 
ATOM   5990  N N   . CYS C  1 285 ? -37.963 -34.482  -30.229 1.00 44.58  ? 285 CYS C N   1 
ATOM   5991  C CA  . CYS C  1 285 ? -38.164 -35.441  -31.307 1.00 40.36  ? 285 CYS C CA  1 
ATOM   5992  C C   . CYS C  1 285 ? -39.095 -34.855  -32.365 1.00 37.43  ? 285 CYS C C   1 
ATOM   5993  O O   . CYS C  1 285 ? -40.190 -34.388  -32.049 1.00 42.93  ? 285 CYS C O   1 
ATOM   5994  C CB  . CYS C  1 285 ? -38.740 -36.747  -30.756 1.00 36.14  ? 285 CYS C CB  1 
ATOM   5995  S SG  . CYS C  1 285 ? -39.101 -37.994  -32.011 1.00 71.10  ? 285 CYS C SG  1 
ATOM   5996  N N   . GLN C  1 286 ? -38.657 -34.881  -33.620 1.00 44.93  ? 286 GLN C N   1 
ATOM   5997  C CA  . GLN C  1 286 ? -39.413 -34.262  -34.703 1.00 37.07  ? 286 GLN C CA  1 
ATOM   5998  C C   . GLN C  1 286 ? -39.761 -35.245  -35.819 1.00 38.47  ? 286 GLN C C   1 
ATOM   5999  O O   . GLN C  1 286 ? -38.901 -35.977  -36.309 1.00 48.18  ? 286 GLN C O   1 
ATOM   6000  C CB  . GLN C  1 286 ? -38.637 -33.075  -35.281 1.00 34.61  ? 286 GLN C CB  1 
ATOM   6001  C CG  . GLN C  1 286 ? -39.418 -32.263  -36.298 1.00 38.28  ? 286 GLN C CG  1 
ATOM   6002  C CD  . GLN C  1 286 ? -40.652 -31.625  -35.697 1.00 50.55  ? 286 GLN C CD  1 
ATOM   6003  O OE1 . GLN C  1 286 ? -40.560 -30.835  -34.757 1.00 53.42  ? 286 GLN C OE1 1 
ATOM   6004  N NE2 . GLN C  1 286 ? -41.817 -31.966  -36.235 1.00 43.27  ? 286 GLN C NE2 1 
ATOM   6005  N N   . THR C  1 287 ? -41.031 -35.252  -36.215 1.00 41.37  ? 287 THR C N   1 
ATOM   6006  C CA  . THR C  1 287 ? -41.484 -36.067  -37.335 1.00 40.67  ? 287 THR C CA  1 
ATOM   6007  C C   . THR C  1 287 ? -42.079 -35.164  -38.410 1.00 48.11  ? 287 THR C C   1 
ATOM   6008  O O   . THR C  1 287 ? -42.434 -34.018  -38.132 1.00 50.87  ? 287 THR C O   1 
ATOM   6009  C CB  . THR C  1 287 ? -42.550 -37.094  -36.901 1.00 44.74  ? 287 THR C CB  1 
ATOM   6010  O OG1 . THR C  1 287 ? -43.858 -36.530  -37.063 1.00 44.77  ? 287 THR C OG1 1 
ATOM   6011  C CG2 . THR C  1 287 ? -42.345 -37.506  -35.449 1.00 34.88  ? 287 THR C CG2 1 
ATOM   6012  N N   . PRO C  1 288 ? -42.183 -35.675  -39.646 1.00 49.41  ? 288 PRO C N   1 
ATOM   6013  C CA  . PRO C  1 288 ? -42.786 -34.921  -40.751 1.00 47.59  ? 288 PRO C CA  1 
ATOM   6014  C C   . PRO C  1 288 ? -44.223 -34.488  -40.459 1.00 46.09  ? 288 PRO C C   1 
ATOM   6015  O O   . PRO C  1 288 ? -44.681 -33.482  -41.000 1.00 42.64  ? 288 PRO C O   1 
ATOM   6016  C CB  . PRO C  1 288 ? -42.766 -35.925  -41.905 1.00 53.85  ? 288 PRO C CB  1 
ATOM   6017  C CG  . PRO C  1 288 ? -41.631 -36.836  -41.587 1.00 42.07  ? 288 PRO C CG  1 
ATOM   6018  C CD  . PRO C  1 288 ? -41.625 -36.963  -40.095 1.00 39.02  ? 288 PRO C CD  1 
ATOM   6019  N N   . LYS C  1 289 ? -44.921 -35.241  -39.615 1.00 50.28  ? 289 LYS C N   1 
ATOM   6020  C CA  . LYS C  1 289 ? -46.319 -34.952  -39.305 1.00 47.64  ? 289 LYS C CA  1 
ATOM   6021  C C   . LYS C  1 289 ? -46.452 -33.962  -38.153 1.00 45.32  ? 289 LYS C C   1 
ATOM   6022  O O   . LYS C  1 289 ? -47.430 -33.217  -38.070 1.00 55.14  ? 289 LYS C O   1 
ATOM   6023  C CB  . LYS C  1 289 ? -47.067 -36.248  -38.980 1.00 48.87  ? 289 LYS C CB  1 
ATOM   6024  C CG  . LYS C  1 289 ? -47.026 -37.273  -40.103 1.00 60.97  ? 289 LYS C CG  1 
ATOM   6025  C CD  . LYS C  1 289 ? -47.544 -38.633  -39.660 1.00 59.27  ? 289 LYS C CD  1 
ATOM   6026  C CE  . LYS C  1 289 ? -49.050 -38.630  -39.461 1.00 76.14  ? 289 LYS C CE  1 
ATOM   6027  N NZ  . LYS C  1 289 ? -49.570 -40.004  -39.212 1.00 81.78  ? 289 LYS C NZ  1 
ATOM   6028  N N   . GLY C  1 290 ? -45.462 -33.958  -37.267 1.00 43.47  ? 290 GLY C N   1 
ATOM   6029  C CA  . GLY C  1 290 ? -45.473 -33.088  -36.106 1.00 45.42  ? 290 GLY C CA  1 
ATOM   6030  C C   . GLY C  1 290 ? -44.473 -33.546  -35.063 1.00 43.91  ? 290 GLY C C   1 
ATOM   6031  O O   . GLY C  1 290 ? -43.888 -34.621  -35.185 1.00 47.76  ? 290 GLY C O   1 
ATOM   6032  N N   . ALA C  1 291 ? -44.277 -32.731  -34.033 1.00 47.85  ? 291 ALA C N   1 
ATOM   6033  C CA  . ALA C  1 291 ? -43.311 -33.041  -32.985 1.00 43.56  ? 291 ALA C CA  1 
ATOM   6034  C C   . ALA C  1 291 ? -43.898 -33.971  -31.928 1.00 47.56  ? 291 ALA C C   1 
ATOM   6035  O O   . ALA C  1 291 ? -45.116 -34.066  -31.777 1.00 45.12  ? 291 ALA C O   1 
ATOM   6036  C CB  . ALA C  1 291 ? -42.800 -31.762  -32.342 1.00 36.53  ? 291 ALA C CB  1 
ATOM   6037  N N   . ILE C  1 292 ? -43.022 -34.655  -31.199 1.00 49.43  ? 292 ILE C N   1 
ATOM   6038  C CA  . ILE C  1 292 ? -43.452 -35.548  -30.131 1.00 49.32  ? 292 ILE C CA  1 
ATOM   6039  C C   . ILE C  1 292 ? -42.887 -35.126  -28.776 1.00 63.69  ? 292 ILE C C   1 
ATOM   6040  O O   . ILE C  1 292 ? -41.676 -35.148  -28.559 1.00 60.70  ? 292 ILE C O   1 
ATOM   6041  C CB  . ILE C  1 292 ? -43.050 -37.008  -30.409 1.00 49.28  ? 292 ILE C CB  1 
ATOM   6042  C CG1 . ILE C  1 292 ? -43.694 -37.505  -31.704 1.00 41.33  ? 292 ILE C CG1 1 
ATOM   6043  C CG2 . ILE C  1 292 ? -43.463 -37.897  -29.253 1.00 60.28  ? 292 ILE C CG2 1 
ATOM   6044  C CD1 . ILE C  1 292 ? -43.380 -38.953  -32.021 1.00 51.42  ? 292 ILE C CD1 1 
ATOM   6045  N N   . ASN C  1 293 ? -43.781 -34.739  -27.874 1.00 86.19  ? 293 ASN C N   1 
ATOM   6046  C CA  . ASN C  1 293 ? -43.418 -34.392  -26.507 1.00 96.41  ? 293 ASN C CA  1 
ATOM   6047  C C   . ASN C  1 293 ? -43.768 -35.558  -25.589 1.00 95.44  ? 293 ASN C C   1 
ATOM   6048  O O   . ASN C  1 293 ? -44.887 -35.638  -25.086 1.00 106.58 ? 293 ASN C O   1 
ATOM   6049  C CB  . ASN C  1 293 ? -44.179 -33.134  -26.080 1.00 108.56 ? 293 ASN C CB  1 
ATOM   6050  C CG  . ASN C  1 293 ? -43.856 -32.703  -24.664 1.00 121.19 ? 293 ASN C CG  1 
ATOM   6051  O OD1 . ASN C  1 293 ? -42.936 -33.225  -24.036 1.00 117.36 ? 293 ASN C OD1 1 
ATOM   6052  N ND2 . ASN C  1 293 ? -44.615 -31.738  -24.154 1.00 114.56 ? 293 ASN C ND2 1 
ATOM   6053  N N   . THR C  1 294 ? -42.822 -36.467  -25.370 1.00 73.89  ? 294 THR C N   1 
ATOM   6054  C CA  . THR C  1 294 ? -43.156 -37.720  -24.699 1.00 96.67  ? 294 THR C CA  1 
ATOM   6055  C C   . THR C  1 294 ? -42.065 -38.275  -23.781 1.00 90.06  ? 294 THR C C   1 
ATOM   6056  O O   . THR C  1 294 ? -40.887 -37.950  -23.917 1.00 75.38  ? 294 THR C O   1 
ATOM   6057  C CB  . THR C  1 294 ? -43.526 -38.804  -25.731 1.00 88.50  ? 294 THR C CB  1 
ATOM   6058  O OG1 . THR C  1 294 ? -44.131 -39.921  -25.069 1.00 82.67  ? 294 THR C OG1 1 
ATOM   6059  C CG2 . THR C  1 294 ? -42.289 -39.265  -26.475 1.00 73.71  ? 294 THR C CG2 1 
ATOM   6060  N N   . SER C  1 295 ? -42.483 -39.118  -22.842 1.00 69.11  ? 295 SER C N   1 
ATOM   6061  C CA  . SER C  1 295 ? -41.562 -39.865  -21.994 1.00 69.32  ? 295 SER C CA  1 
ATOM   6062  C C   . SER C  1 295 ? -41.661 -41.346  -22.335 1.00 59.39  ? 295 SER C C   1 
ATOM   6063  O O   . SER C  1 295 ? -40.798 -42.145  -21.967 1.00 57.44  ? 295 SER C O   1 
ATOM   6064  C CB  . SER C  1 295 ? -41.889 -39.645  -20.517 1.00 72.33  ? 295 SER C CB  1 
ATOM   6065  O OG  . SER C  1 295 ? -40.879 -38.882  -19.881 1.00 99.28  ? 295 SER C OG  1 
ATOM   6066  N N   . LEU C  1 296 ? -42.723 -41.698  -23.053 1.00 52.10  ? 296 LEU C N   1 
ATOM   6067  C CA  . LEU C  1 296 ? -43.001 -43.083  -23.409 1.00 48.91  ? 296 LEU C CA  1 
ATOM   6068  C C   . LEU C  1 296 ? -41.921 -43.676  -24.310 1.00 43.41  ? 296 LEU C C   1 
ATOM   6069  O O   . LEU C  1 296 ? -41.336 -42.976  -25.136 1.00 42.19  ? 296 LEU C O   1 
ATOM   6070  C CB  . LEU C  1 296 ? -44.375 -43.194  -24.074 1.00 49.04  ? 296 LEU C CB  1 
ATOM   6071  C CG  . LEU C  1 296 ? -45.541 -42.636  -23.254 1.00 45.13  ? 296 LEU C CG  1 
ATOM   6072  C CD1 . LEU C  1 296 ? -46.862 -42.893  -23.958 1.00 50.81  ? 296 LEU C CD1 1 
ATOM   6073  C CD2 . LEU C  1 296 ? -45.553 -43.234  -21.856 1.00 51.38  ? 296 LEU C CD2 1 
ATOM   6074  N N   . PRO C  1 297 ? -41.657 -44.979  -24.143 1.00 37.07  ? 297 PRO C N   1 
ATOM   6075  C CA  . PRO C  1 297 ? -40.591 -45.691  -24.854 1.00 41.05  ? 297 PRO C CA  1 
ATOM   6076  C C   . PRO C  1 297 ? -40.904 -45.913  -26.330 1.00 49.83  ? 297 PRO C C   1 
ATOM   6077  O O   . PRO C  1 297 ? -39.981 -46.071  -27.129 1.00 45.15  ? 297 PRO C O   1 
ATOM   6078  C CB  . PRO C  1 297 ? -40.532 -47.046  -24.133 1.00 39.95  ? 297 PRO C CB  1 
ATOM   6079  C CG  . PRO C  1 297 ? -41.286 -46.853  -22.850 1.00 55.48  ? 297 PRO C CG  1 
ATOM   6080  C CD  . PRO C  1 297 ? -42.333 -45.843  -23.165 1.00 45.71  ? 297 PRO C CD  1 
ATOM   6081  N N   . PHE C  1 298 ? -42.184 -45.929  -26.690 1.00 43.21  ? 298 PHE C N   1 
ATOM   6082  C CA  . PHE C  1 298 ? -42.563 -46.271  -28.056 1.00 42.93  ? 298 PHE C CA  1 
ATOM   6083  C C   . PHE C  1 298 ? -43.557 -45.297  -28.684 1.00 39.30  ? 298 PHE C C   1 
ATOM   6084  O O   . PHE C  1 298 ? -44.372 -44.680  -27.994 1.00 46.52  ? 298 PHE C O   1 
ATOM   6085  C CB  . PHE C  1 298 ? -43.110 -47.698  -28.111 1.00 40.83  ? 298 PHE C CB  1 
ATOM   6086  C CG  . PHE C  1 298 ? -42.327 -48.674  -27.281 1.00 41.68  ? 298 PHE C CG  1 
ATOM   6087  C CD1 . PHE C  1 298 ? -41.107 -49.162  -27.723 1.00 32.69  ? 298 PHE C CD1 1 
ATOM   6088  C CD2 . PHE C  1 298 ? -42.808 -49.099  -26.055 1.00 40.65  ? 298 PHE C CD2 1 
ATOM   6089  C CE1 . PHE C  1 298 ? -40.385 -50.057  -26.957 1.00 40.12  ? 298 PHE C CE1 1 
ATOM   6090  C CE2 . PHE C  1 298 ? -42.092 -49.994  -25.285 1.00 46.82  ? 298 PHE C CE2 1 
ATOM   6091  C CZ  . PHE C  1 298 ? -40.879 -50.474  -25.736 1.00 39.85  ? 298 PHE C CZ  1 
ATOM   6092  N N   . GLN C  1 299 ? -43.471 -45.173  -30.005 1.00 39.32  ? 299 GLN C N   1 
ATOM   6093  C CA  . GLN C  1 299 ? -44.332 -44.283  -30.774 1.00 36.51  ? 299 GLN C CA  1 
ATOM   6094  C C   . GLN C  1 299 ? -44.759 -44.973  -32.064 1.00 40.12  ? 299 GLN C C   1 
ATOM   6095  O O   . GLN C  1 299 ? -43.993 -45.744  -32.646 1.00 69.41  ? 299 GLN C O   1 
ATOM   6096  C CB  . GLN C  1 299 ? -43.595 -42.977  -31.089 1.00 30.07  ? 299 GLN C CB  1 
ATOM   6097  C CG  . GLN C  1 299 ? -42.243 -43.159  -31.794 1.00 39.98  ? 299 GLN C CG  1 
ATOM   6098  C CD  . GLN C  1 299 ? -42.294 -42.802  -33.268 1.00 43.78  ? 299 GLN C CD  1 
ATOM   6099  O OE1 . GLN C  1 299 ? -43.367 -42.755  -33.866 1.00 40.86  ? 299 GLN C OE1 1 
ATOM   6100  N NE2 . GLN C  1 299 ? -41.132 -42.557  -33.862 1.00 38.67  ? 299 GLN C NE2 1 
ATOM   6101  N N   . ASN C  1 300 ? -45.988 -44.714  -32.499 1.00 43.28  ? 300 ASN C N   1 
ATOM   6102  C CA  . ASN C  1 300 ? -46.487 -45.290  -33.743 1.00 41.92  ? 300 ASN C CA  1 
ATOM   6103  C C   . ASN C  1 300 ? -46.917 -44.211  -34.729 1.00 33.63  ? 300 ASN C C   1 
ATOM   6104  O O   . ASN C  1 300 ? -47.672 -44.474  -35.663 1.00 43.24  ? 300 ASN C O   1 
ATOM   6105  C CB  . ASN C  1 300 ? -47.643 -46.256  -33.472 1.00 32.66  ? 300 ASN C CB  1 
ATOM   6106  C CG  . ASN C  1 300 ? -48.877 -45.557  -32.936 1.00 42.23  ? 300 ASN C CG  1 
ATOM   6107  O OD1 . ASN C  1 300 ? -48.839 -44.373  -32.598 1.00 47.85  ? 300 ASN C OD1 1 
ATOM   6108  N ND2 . ASN C  1 300 ? -49.982 -46.290  -32.852 1.00 39.15  ? 300 ASN C ND2 1 
ATOM   6109  N N   . ILE C  1 301 ? -46.422 -42.997  -34.512 1.00 37.06  ? 301 ILE C N   1 
ATOM   6110  C CA  . ILE C  1 301 ? -46.780 -41.859  -35.348 1.00 39.36  ? 301 ILE C CA  1 
ATOM   6111  C C   . ILE C  1 301 ? -46.111 -41.919  -36.717 1.00 43.72  ? 301 ILE C C   1 
ATOM   6112  O O   . ILE C  1 301 ? -46.786 -41.889  -37.745 1.00 49.58  ? 301 ILE C O   1 
ATOM   6113  C CB  . ILE C  1 301 ? -46.410 -40.527  -34.670 1.00 48.97  ? 301 ILE C CB  1 
ATOM   6114  C CG1 . ILE C  1 301 ? -47.219 -40.341  -33.384 1.00 34.69  ? 301 ILE C CG1 1 
ATOM   6115  C CG2 . ILE C  1 301 ? -46.639 -39.364  -35.623 1.00 37.46  ? 301 ILE C CG2 1 
ATOM   6116  C CD1 . ILE C  1 301 ? -46.843 -39.104  -32.599 1.00 51.00  ? 301 ILE C CD1 1 
ATOM   6117  N N   . HIS C  1 302 ? -44.784 -42.003  -36.727 1.00 44.70  ? 302 HIS C N   1 
ATOM   6118  C CA  . HIS C  1 302 ? -44.036 -41.984  -37.978 1.00 45.65  ? 302 HIS C CA  1 
ATOM   6119  C C   . HIS C  1 302 ? -42.674 -42.659  -37.831 1.00 45.43  ? 302 HIS C C   1 
ATOM   6120  O O   . HIS C  1 302 ? -41.999 -42.488  -36.816 1.00 47.74  ? 302 HIS C O   1 
ATOM   6121  C CB  . HIS C  1 302 ? -43.857 -40.543  -38.460 1.00 35.61  ? 302 HIS C CB  1 
ATOM   6122  C CG  . HIS C  1 302 ? -43.604 -40.423  -39.929 1.00 47.79  ? 302 HIS C CG  1 
ATOM   6123  N ND1 . HIS C  1 302 ? -42.360 -40.615  -40.490 1.00 48.72  ? 302 HIS C ND1 1 
ATOM   6124  C CD2 . HIS C  1 302 ? -44.437 -40.124  -40.956 1.00 50.18  ? 302 HIS C CD2 1 
ATOM   6125  C CE1 . HIS C  1 302 ? -42.436 -40.442  -41.798 1.00 53.39  ? 302 HIS C CE1 1 
ATOM   6126  N NE2 . HIS C  1 302 ? -43.687 -40.143  -42.105 1.00 43.87  ? 302 HIS C NE2 1 
ATOM   6127  N N   . PRO C  1 303 ? -42.270 -43.433  -38.851 1.00 48.09  ? 303 PRO C N   1 
ATOM   6128  C CA  . PRO C  1 303 ? -40.986 -44.142  -38.877 1.00 38.77  ? 303 PRO C CA  1 
ATOM   6129  C C   . PRO C  1 303 ? -39.804 -43.187  -39.011 1.00 42.69  ? 303 PRO C C   1 
ATOM   6130  O O   . PRO C  1 303 ? -38.819 -43.326  -38.285 1.00 37.75  ? 303 PRO C O   1 
ATOM   6131  C CB  . PRO C  1 303 ? -41.092 -45.019  -40.132 1.00 32.72  ? 303 PRO C CB  1 
ATOM   6132  C CG  . PRO C  1 303 ? -42.552 -45.084  -40.447 1.00 54.63  ? 303 PRO C CG  1 
ATOM   6133  C CD  . PRO C  1 303 ? -43.100 -43.762  -40.021 1.00 52.93  ? 303 PRO C CD  1 
ATOM   6134  N N   . ILE C  1 304 ? -39.899 -42.235  -39.934 1.00 36.27  ? 304 ILE C N   1 
ATOM   6135  C CA  . ILE C  1 304 ? -38.840 -41.249  -40.121 1.00 37.82  ? 304 ILE C CA  1 
ATOM   6136  C C   . ILE C  1 304 ? -38.890 -40.205  -39.013 1.00 39.79  ? 304 ILE C C   1 
ATOM   6137  O O   . ILE C  1 304 ? -39.912 -39.551  -38.807 1.00 55.36  ? 304 ILE C O   1 
ATOM   6138  C CB  . ILE C  1 304 ? -38.927 -40.559  -41.495 1.00 35.72  ? 304 ILE C CB  1 
ATOM   6139  C CG1 . ILE C  1 304 ? -38.433 -41.498  -42.599 1.00 27.06  ? 304 ILE C CG1 1 
ATOM   6140  C CG2 . ILE C  1 304 ? -38.095 -39.289  -41.502 1.00 49.65  ? 304 ILE C CG2 1 
ATOM   6141  C CD1 . ILE C  1 304 ? -39.274 -42.744  -42.786 1.00 49.47  ? 304 ILE C CD1 1 
ATOM   6142  N N   . THR C  1 305 ? -37.778 -40.054  -38.302 1.00 36.84  ? 305 THR C N   1 
ATOM   6143  C CA  . THR C  1 305 ? -37.745 -39.222  -37.109 1.00 31.02  ? 305 THR C CA  1 
ATOM   6144  C C   . THR C  1 305 ? -36.398 -38.516  -36.967 1.00 45.00  ? 305 THR C C   1 
ATOM   6145  O O   . THR C  1 305 ? -35.381 -38.995  -37.470 1.00 48.24  ? 305 THR C O   1 
ATOM   6146  C CB  . THR C  1 305 ? -38.012 -40.073  -35.849 1.00 39.23  ? 305 THR C CB  1 
ATOM   6147  O OG1 . THR C  1 305 ? -38.947 -39.402  -34.996 1.00 53.41  ? 305 THR C OG1 1 
ATOM   6148  C CG2 . THR C  1 305 ? -36.716 -40.344  -35.090 1.00 37.44  ? 305 THR C CG2 1 
ATOM   6149  N N   . ILE C  1 306 ? -36.396 -37.373  -36.288 1.00 35.32  ? 306 ILE C N   1 
ATOM   6150  C CA  . ILE C  1 306 ? -35.158 -36.647  -36.021 1.00 40.09  ? 306 ILE C CA  1 
ATOM   6151  C C   . ILE C  1 306 ? -35.060 -36.241  -34.552 1.00 44.74  ? 306 ILE C C   1 
ATOM   6152  O O   . ILE C  1 306 ? -36.029 -35.760  -33.965 1.00 38.86  ? 306 ILE C O   1 
ATOM   6153  C CB  . ILE C  1 306 ? -35.023 -35.389  -36.903 1.00 31.49  ? 306 ILE C CB  1 
ATOM   6154  C CG1 . ILE C  1 306 ? -35.197 -35.744  -38.381 1.00 39.25  ? 306 ILE C CG1 1 
ATOM   6155  C CG2 . ILE C  1 306 ? -33.676 -34.723  -36.676 1.00 28.80  ? 306 ILE C CG2 1 
ATOM   6156  C CD1 . ILE C  1 306 ? -34.908 -34.592  -39.320 1.00 37.08  ? 306 ILE C CD1 1 
ATOM   6157  N N   . GLY C  1 307 ? -33.883 -36.439  -33.964 1.00 44.71  ? 307 GLY C N   1 
ATOM   6158  C CA  . GLY C  1 307 ? -33.657 -36.106  -32.569 1.00 39.54  ? 307 GLY C CA  1 
ATOM   6159  C C   . GLY C  1 307 ? -33.507 -37.340  -31.703 1.00 46.24  ? 307 GLY C C   1 
ATOM   6160  O O   . GLY C  1 307 ? -33.112 -38.402  -32.184 1.00 56.48  ? 307 GLY C O   1 
ATOM   6161  N N   . LYS C  1 308 ? -33.810 -37.197  -30.417 1.00 48.34  ? 308 LYS C N   1 
ATOM   6162  C CA  . LYS C  1 308 ? -33.822 -38.330  -29.500 1.00 46.88  ? 308 LYS C CA  1 
ATOM   6163  C C   . LYS C  1 308 ? -35.262 -38.789  -29.305 1.00 42.80  ? 308 LYS C C   1 
ATOM   6164  O O   . LYS C  1 308 ? -35.998 -38.227  -28.494 1.00 51.25  ? 308 LYS C O   1 
ATOM   6165  C CB  . LYS C  1 308 ? -33.194 -37.951  -28.158 1.00 47.29  ? 308 LYS C CB  1 
ATOM   6166  C CG  . LYS C  1 308 ? -33.148 -39.097  -27.163 1.00 70.15  ? 308 LYS C CG  1 
ATOM   6167  C CD  . LYS C  1 308 ? -32.554 -38.677  -25.829 1.00 77.37  ? 308 LYS C CD  1 
ATOM   6168  C CE  . LYS C  1 308 ? -31.080 -38.334  -25.957 1.00 78.42  ? 308 LYS C CE  1 
ATOM   6169  N NZ  . LYS C  1 308 ? -30.346 -38.619  -24.691 1.00 85.05  ? 308 LYS C NZ  1 
ATOM   6170  N N   . CYS C  1 309 ? -35.660 -39.813  -30.051 1.00 45.67  ? 309 CYS C N   1 
ATOM   6171  C CA  . CYS C  1 309 ? -37.068 -40.179  -30.140 1.00 48.67  ? 309 CYS C CA  1 
ATOM   6172  C C   . CYS C  1 309 ? -37.381 -41.566  -29.592 1.00 40.60  ? 309 CYS C C   1 
ATOM   6173  O O   . CYS C  1 309 ? -36.499 -42.420  -29.500 1.00 45.29  ? 309 CYS C O   1 
ATOM   6174  C CB  . CYS C  1 309 ? -37.532 -40.084  -31.595 1.00 35.17  ? 309 CYS C CB  1 
ATOM   6175  S SG  . CYS C  1 309 ? -37.167 -38.495  -32.374 1.00 62.35  ? 309 CYS C SG  1 
ATOM   6176  N N   . PRO C  1 310 ? -38.651 -41.789  -29.220 1.00 35.49  ? 310 PRO C N   1 
ATOM   6177  C CA  . PRO C  1 310 ? -39.123 -43.124  -28.846 1.00 40.39  ? 310 PRO C CA  1 
ATOM   6178  C C   . PRO C  1 310 ? -39.014 -44.050  -30.044 1.00 43.32  ? 310 PRO C C   1 
ATOM   6179  O O   . PRO C  1 310 ? -38.998 -43.582  -31.183 1.00 46.49  ? 310 PRO C O   1 
ATOM   6180  C CB  . PRO C  1 310 ? -40.599 -42.894  -28.508 1.00 35.59  ? 310 PRO C CB  1 
ATOM   6181  C CG  . PRO C  1 310 ? -40.706 -41.447  -28.210 1.00 35.46  ? 310 PRO C CG  1 
ATOM   6182  C CD  . PRO C  1 310 ? -39.709 -40.775  -29.095 1.00 31.39  ? 310 PRO C CD  1 
ATOM   6183  N N   . LYS C  1 311 ? -38.946 -45.350  -29.794 1.00 43.73  ? 311 LYS C N   1 
ATOM   6184  C CA  . LYS C  1 311 ? -38.784 -46.309  -30.874 1.00 42.06  ? 311 LYS C CA  1 
ATOM   6185  C C   . LYS C  1 311 ? -40.074 -46.468  -31.674 1.00 39.52  ? 311 LYS C C   1 
ATOM   6186  O O   . LYS C  1 311 ? -41.163 -46.522  -31.102 1.00 53.87  ? 311 LYS C O   1 
ATOM   6187  C CB  . LYS C  1 311 ? -38.319 -47.652  -30.315 1.00 35.33  ? 311 LYS C CB  1 
ATOM   6188  C CG  . LYS C  1 311 ? -37.076 -48.183  -30.994 1.00 36.67  ? 311 LYS C CG  1 
ATOM   6189  C CD  . LYS C  1 311 ? -35.990 -47.122  -31.102 1.00 36.93  ? 311 LYS C CD  1 
ATOM   6190  C CE  . LYS C  1 311 ? -35.047 -47.154  -29.912 1.00 38.48  ? 311 LYS C CE  1 
ATOM   6191  N NZ  . LYS C  1 311 ? -33.799 -46.387  -30.192 1.00 42.21  ? 311 LYS C NZ  1 
ATOM   6192  N N   . TYR C  1 312 ? -39.952 -46.532  -32.997 1.00 35.05  ? 312 TYR C N   1 
ATOM   6193  C CA  . TYR C  1 312 ? -41.126 -46.678  -33.852 1.00 33.47  ? 312 TYR C CA  1 
ATOM   6194  C C   . TYR C  1 312 ? -41.674 -48.100  -33.826 1.00 33.78  ? 312 TYR C C   1 
ATOM   6195  O O   . TYR C  1 312 ? -40.953 -49.062  -34.093 1.00 42.03  ? 312 TYR C O   1 
ATOM   6196  C CB  . TYR C  1 312 ? -40.828 -46.257  -35.293 1.00 29.16  ? 312 TYR C CB  1 
ATOM   6197  C CG  . TYR C  1 312 ? -42.011 -46.449  -36.215 1.00 38.21  ? 312 TYR C CG  1 
ATOM   6198  C CD1 . TYR C  1 312 ? -43.166 -45.697  -36.057 1.00 33.72  ? 312 TYR C CD1 1 
ATOM   6199  C CD2 . TYR C  1 312 ? -41.977 -47.389  -37.237 1.00 41.35  ? 312 TYR C CD2 1 
ATOM   6200  C CE1 . TYR C  1 312 ? -44.254 -45.871  -36.890 1.00 35.47  ? 312 TYR C CE1 1 
ATOM   6201  C CE2 . TYR C  1 312 ? -43.060 -47.570  -38.076 1.00 38.89  ? 312 TYR C CE2 1 
ATOM   6202  C CZ  . TYR C  1 312 ? -44.195 -46.809  -37.898 1.00 41.87  ? 312 TYR C CZ  1 
ATOM   6203  O OH  . TYR C  1 312 ? -45.275 -46.985  -38.732 1.00 45.04  ? 312 TYR C OH  1 
ATOM   6204  N N   . VAL C  1 313 ? -42.958 -48.220  -33.506 1.00 45.12  ? 313 VAL C N   1 
ATOM   6205  C CA  . VAL C  1 313 ? -43.609 -49.520  -33.414 1.00 38.31  ? 313 VAL C CA  1 
ATOM   6206  C C   . VAL C  1 313 ? -44.890 -49.571  -34.247 1.00 37.76  ? 313 VAL C C   1 
ATOM   6207  O O   . VAL C  1 313 ? -45.589 -48.567  -34.395 1.00 38.60  ? 313 VAL C O   1 
ATOM   6208  C CB  . VAL C  1 313 ? -43.921 -49.886  -31.950 1.00 32.68  ? 313 VAL C CB  1 
ATOM   6209  C CG1 . VAL C  1 313 ? -44.659 -51.206  -31.880 1.00 49.55  ? 313 VAL C CG1 1 
ATOM   6210  C CG2 . VAL C  1 313 ? -42.639 -49.954  -31.137 1.00 41.60  ? 313 VAL C CG2 1 
ATOM   6211  N N   . LYS C  1 314 ? -45.185 -50.748  -34.790 1.00 43.71  ? 314 LYS C N   1 
ATOM   6212  C CA  . LYS C  1 314 ? -46.352 -50.950  -35.639 1.00 47.52  ? 314 LYS C CA  1 
ATOM   6213  C C   . LYS C  1 314 ? -47.606 -51.179  -34.801 1.00 47.97  ? 314 LYS C C   1 
ATOM   6214  O O   . LYS C  1 314 ? -48.694 -51.386  -35.341 1.00 60.45  ? 314 LYS C O   1 
ATOM   6215  C CB  . LYS C  1 314 ? -46.121 -52.155  -36.549 1.00 49.93  ? 314 LYS C CB  1 
ATOM   6216  C CG  . LYS C  1 314 ? -46.360 -51.897  -38.025 1.00 53.02  ? 314 LYS C CG  1 
ATOM   6217  C CD  . LYS C  1 314 ? -45.872 -53.078  -38.852 1.00 86.28  ? 314 LYS C CD  1 
ATOM   6218  C CE  . LYS C  1 314 ? -44.422 -53.417  -38.533 1.00 85.67  ? 314 LYS C CE  1 
ATOM   6219  N NZ  . LYS C  1 314 ? -44.178 -54.884  -38.531 1.00 72.29  ? 314 LYS C NZ  1 
ATOM   6220  N N   . SER C  1 315 ? -47.447 -51.141  -33.482 1.00 50.27  ? 315 SER C N   1 
ATOM   6221  C CA  . SER C  1 315 ? -48.552 -51.418  -32.571 1.00 52.16  ? 315 SER C CA  1 
ATOM   6222  C C   . SER C  1 315 ? -49.653 -50.366  -32.646 1.00 47.53  ? 315 SER C C   1 
ATOM   6223  O O   . SER C  1 315 ? -49.400 -49.204  -32.963 1.00 36.70  ? 315 SER C O   1 
ATOM   6224  C CB  . SER C  1 315 ? -48.042 -51.530  -31.134 1.00 51.20  ? 315 SER C CB  1 
ATOM   6225  O OG  . SER C  1 315 ? -47.164 -52.631  -30.990 1.00 66.68  ? 315 SER C OG  1 
ATOM   6226  N N   . THR C  1 316 ? -50.877 -50.788  -32.354 1.00 52.79  ? 316 THR C N   1 
ATOM   6227  C CA  . THR C  1 316 ? -52.009 -49.874  -32.288 1.00 59.91  ? 316 THR C CA  1 
ATOM   6228  C C   . THR C  1 316 ? -52.219 -49.427  -30.847 1.00 51.94  ? 316 THR C C   1 
ATOM   6229  O O   . THR C  1 316 ? -52.617 -48.291  -30.586 1.00 51.29  ? 316 THR C O   1 
ATOM   6230  C CB  . THR C  1 316 ? -53.295 -50.532  -32.817 1.00 59.96  ? 316 THR C CB  1 
ATOM   6231  O OG1 . THR C  1 316 ? -54.434 -49.773  -32.390 1.00 70.74  ? 316 THR C OG1 1 
ATOM   6232  C CG2 . THR C  1 316 ? -53.416 -51.955  -32.293 1.00 69.71  ? 316 THR C CG2 1 
ATOM   6233  N N   . LYS C  1 317 ? -51.941 -50.333  -29.916 1.00 59.72  ? 317 LYS C N   1 
ATOM   6234  C CA  . LYS C  1 317 ? -52.045 -50.037  -28.495 1.00 53.10  ? 317 LYS C CA  1 
ATOM   6235  C C   . LYS C  1 317 ? -51.059 -50.873  -27.685 1.00 51.61  ? 317 LYS C C   1 
ATOM   6236  O O   . LYS C  1 317 ? -50.790 -52.030  -28.013 1.00 54.84  ? 317 LYS C O   1 
ATOM   6237  C CB  . LYS C  1 317 ? -53.472 -50.281  -28.000 1.00 59.41  ? 317 LYS C CB  1 
ATOM   6238  C CG  . LYS C  1 317 ? -54.014 -51.664  -28.326 1.00 80.64  ? 317 LYS C CG  1 
ATOM   6239  C CD  . LYS C  1 317 ? -55.384 -51.881  -27.706 1.00 96.58  ? 317 LYS C CD  1 
ATOM   6240  C CE  . LYS C  1 317 ? -55.306 -51.907  -26.188 1.00 98.18  ? 317 LYS C CE  1 
ATOM   6241  N NZ  . LYS C  1 317 ? -56.651 -52.056  -25.567 1.00 77.44  ? 317 LYS C NZ  1 
ATOM   6242  N N   . LEU C  1 318 ? -50.517 -50.273  -26.630 1.00 46.54  ? 318 LEU C N   1 
ATOM   6243  C CA  . LEU C  1 318 ? -49.616 -50.969  -25.720 1.00 49.79  ? 318 LEU C CA  1 
ATOM   6244  C C   . LEU C  1 318 ? -50.006 -50.671  -24.278 1.00 46.31  ? 318 LEU C C   1 
ATOM   6245  O O   . LEU C  1 318 ? -49.202 -50.154  -23.503 1.00 51.39  ? 318 LEU C O   1 
ATOM   6246  C CB  . LEU C  1 318 ? -48.166 -50.547  -25.965 1.00 44.86  ? 318 LEU C CB  1 
ATOM   6247  C CG  . LEU C  1 318 ? -47.499 -51.039  -27.251 1.00 47.66  ? 318 LEU C CG  1 
ATOM   6248  C CD1 . LEU C  1 318 ? -46.160 -50.348  -27.461 1.00 45.69  ? 318 LEU C CD1 1 
ATOM   6249  C CD2 . LEU C  1 318 ? -47.330 -52.552  -27.227 1.00 38.87  ? 318 LEU C CD2 1 
ATOM   6250  N N   . ARG C  1 319 ? -51.245 -50.999  -23.926 1.00 57.84  ? 319 ARG C N   1 
ATOM   6251  C CA  . ARG C  1 319 ? -51.766 -50.690  -22.599 1.00 54.81  ? 319 ARG C CA  1 
ATOM   6252  C C   . ARG C  1 319 ? -51.185 -51.611  -21.527 1.00 41.49  ? 319 ARG C C   1 
ATOM   6253  O O   . ARG C  1 319 ? -51.344 -52.831  -21.581 1.00 36.17  ? 319 ARG C O   1 
ATOM   6254  C CB  . ARG C  1 319 ? -53.296 -50.739  -22.594 1.00 61.82  ? 319 ARG C CB  1 
ATOM   6255  C CG  . ARG C  1 319 ? -53.927 -50.288  -21.287 1.00 58.63  ? 319 ARG C CG  1 
ATOM   6256  C CD  . ARG C  1 319 ? -55.260 -49.593  -21.523 1.00 63.42  ? 319 ARG C CD  1 
ATOM   6257  N NE  . ARG C  1 319 ? -55.090 -48.270  -22.118 1.00 73.16  ? 319 ARG C NE  1 
ATOM   6258  C CZ  . ARG C  1 319 ? -54.889 -47.157  -21.419 1.00 73.48  ? 319 ARG C CZ  1 
ATOM   6259  N NH1 . ARG C  1 319 ? -54.829 -47.206  -20.095 1.00 67.27  ? 319 ARG C NH1 1 
ATOM   6260  N NH2 . ARG C  1 319 ? -54.745 -45.995  -22.041 1.00 75.32  ? 319 ARG C NH2 1 
ATOM   6261  N N   . LEU C  1 320 ? -50.513 -51.005  -20.553 1.00 44.58  ? 320 LEU C N   1 
ATOM   6262  C CA  . LEU C  1 320 ? -49.828 -51.738  -19.496 1.00 43.35  ? 320 LEU C CA  1 
ATOM   6263  C C   . LEU C  1 320 ? -50.646 -51.732  -18.209 1.00 41.34  ? 320 LEU C C   1 
ATOM   6264  O O   . LEU C  1 320 ? -50.940 -50.673  -17.655 1.00 52.44  ? 320 LEU C O   1 
ATOM   6265  C CB  . LEU C  1 320 ? -48.457 -51.112  -19.241 1.00 48.56  ? 320 LEU C CB  1 
ATOM   6266  C CG  . LEU C  1 320 ? -47.487 -51.856  -18.324 1.00 50.25  ? 320 LEU C CG  1 
ATOM   6267  C CD1 . LEU C  1 320 ? -46.978 -53.119  -19.000 1.00 40.84  ? 320 LEU C CD1 1 
ATOM   6268  C CD2 . LEU C  1 320 ? -46.327 -50.950  -17.944 1.00 41.03  ? 320 LEU C CD2 1 
ATOM   6269  N N   . ALA C  1 321 ? -51.007 -52.920  -17.734 1.00 35.81  ? 321 ALA C N   1 
ATOM   6270  C CA  . ALA C  1 321 ? -51.820 -53.054  -16.530 1.00 44.92  ? 321 ALA C CA  1 
ATOM   6271  C C   . ALA C  1 321 ? -51.072 -52.600  -15.280 1.00 53.44  ? 321 ALA C C   1 
ATOM   6272  O O   . ALA C  1 321 ? -49.960 -53.054  -15.012 1.00 57.62  ? 321 ALA C O   1 
ATOM   6273  C CB  . ALA C  1 321 ? -52.296 -54.489  -16.370 1.00 32.54  ? 321 ALA C CB  1 
ATOM   6274  N N   . THR C  1 322 ? -51.691 -51.705  -14.517 1.00 58.56  ? 322 THR C N   1 
ATOM   6275  C CA  . THR C  1 322 ? -51.107 -51.222  -13.272 1.00 50.09  ? 322 THR C CA  1 
ATOM   6276  C C   . THR C  1 322 ? -51.922 -51.696  -12.075 1.00 55.65  ? 322 THR C C   1 
ATOM   6277  O O   . THR C  1 322 ? -51.370 -52.027  -11.025 1.00 60.08  ? 322 THR C O   1 
ATOM   6278  C CB  . THR C  1 322 ? -51.014 -49.685  -13.247 1.00 49.36  ? 322 THR C CB  1 
ATOM   6279  O OG1 . THR C  1 322 ? -52.322 -49.121  -13.399 1.00 58.86  ? 322 THR C OG1 1 
ATOM   6280  C CG2 . THR C  1 322 ? -50.119 -49.187  -14.371 1.00 61.40  ? 322 THR C CG2 1 
ATOM   6281  N N   . GLY C  1 323 ? -53.241 -51.727  -12.239 1.00 55.08  ? 323 GLY C N   1 
ATOM   6282  C CA  . GLY C  1 323 ? -54.128 -52.201  -11.195 1.00 57.42  ? 323 GLY C CA  1 
ATOM   6283  C C   . GLY C  1 323 ? -54.357 -53.696  -11.296 1.00 57.59  ? 323 GLY C C   1 
ATOM   6284  O O   . GLY C  1 323 ? -53.568 -54.414  -11.910 1.00 51.26  ? 323 GLY C O   1 
ATOM   6285  N N   . LEU C  1 324 ? -55.441 -54.167  -10.690 1.00 57.29  ? 324 LEU C N   1 
ATOM   6286  C CA  . LEU C  1 324 ? -55.783 -55.583  -10.727 1.00 56.08  ? 324 LEU C CA  1 
ATOM   6287  C C   . LEU C  1 324 ? -57.082 -55.809  -11.490 1.00 59.41  ? 324 LEU C C   1 
ATOM   6288  O O   . LEU C  1 324 ? -57.716 -54.858  -11.946 1.00 72.96  ? 324 LEU C O   1 
ATOM   6289  C CB  . LEU C  1 324 ? -55.906 -56.149  -9.311  1.00 66.94  ? 324 LEU C CB  1 
ATOM   6290  C CG  . LEU C  1 324 ? -56.820 -55.393  -8.345  1.00 60.46  ? 324 LEU C CG  1 
ATOM   6291  C CD1 . LEU C  1 324 ? -57.318 -56.314  -7.248  1.00 72.28  ? 324 LEU C CD1 1 
ATOM   6292  C CD2 . LEU C  1 324 ? -56.106 -54.188  -7.756  1.00 57.52  ? 324 LEU C CD2 1 
ATOM   6293  N N   . ARG C  1 325 ? -57.472 -57.072  -11.625 1.00 57.86  ? 325 ARG C N   1 
ATOM   6294  C CA  . ARG C  1 325 ? -58.712 -57.418  -12.312 1.00 60.47  ? 325 ARG C CA  1 
ATOM   6295  C C   . ARG C  1 325 ? -59.884 -56.577  -11.824 1.00 70.30  ? 325 ARG C C   1 
ATOM   6296  O O   . ARG C  1 325 ? -59.868 -56.058  -10.707 1.00 78.72  ? 325 ARG C O   1 
ATOM   6297  C CB  . ARG C  1 325 ? -59.035 -58.902  -12.134 1.00 62.69  ? 325 ARG C CB  1 
ATOM   6298  C CG  . ARG C  1 325 ? -58.386 -59.809  -13.162 1.00 64.76  ? 325 ARG C CG  1 
ATOM   6299  C CD  . ARG C  1 325 ? -58.753 -61.263  -12.914 1.00 77.43  ? 325 ARG C CD  1 
ATOM   6300  N NE  . ARG C  1 325 ? -58.324 -62.124  -14.011 1.00 90.11  ? 325 ARG C NE  1 
ATOM   6301  C CZ  . ARG C  1 325 ? -58.970 -62.229  -15.167 1.00 90.64  ? 325 ARG C CZ  1 
ATOM   6302  N NH1 . ARG C  1 325 ? -60.071 -61.521  -15.380 1.00 70.66  ? 325 ARG C NH1 1 
ATOM   6303  N NH2 . ARG C  1 325 ? -58.513 -63.038  -16.113 1.00 84.41  ? 325 ARG C NH2 1 
ATOM   6304  N N   . ASN C  1 326 ? -60.904 -56.457  -12.667 1.00 79.70  ? 326 ASN C N   1 
ATOM   6305  C CA  . ASN C  1 326 ? -62.079 -55.653  -12.350 1.00 83.01  ? 326 ASN C CA  1 
ATOM   6306  C C   . ASN C  1 326 ? -63.368 -56.482  -12.373 1.00 84.71  ? 326 ASN C C   1 
ATOM   6307  O O   . ASN C  1 326 ? -63.723 -57.085  -13.388 1.00 83.96  ? 326 ASN C O   1 
ATOM   6308  C CB  . ASN C  1 326 ? -62.179 -54.475  -13.322 1.00 91.54  ? 326 ASN C CB  1 
ATOM   6309  C CG  . ASN C  1 326 ? -63.015 -53.334  -12.778 1.00 95.35  ? 326 ASN C CG  1 
ATOM   6310  O OD1 . ASN C  1 326 ? -63.012 -53.056  -11.578 1.00 92.64  ? 326 ASN C OD1 1 
ATOM   6311  N ND2 . ASN C  1 326 ? -63.733 -52.658  -13.664 1.00 99.54  ? 326 ASN C ND2 1 
ATOM   6312  N N   . ILE C  1 327 ? -64.066 -56.520  -11.245 1.00 91.44  ? 327 ILE C N   1 
ATOM   6313  C CA  . ILE C  1 327 ? -65.260 -57.342  -11.131 1.00 84.17  ? 327 ILE C CA  1 
ATOM   6314  C C   . ILE C  1 327 ? -66.157 -56.778  -10.040 1.00 88.21  ? 327 ILE C C   1 
ATOM   6315  O O   . ILE C  1 327 ? -67.129 -56.080  -10.317 1.00 76.54  ? 327 ILE C O   1 
ATOM   6316  C CB  . ILE C  1 327 ? -64.913 -58.811  -10.768 1.00 80.18  ? 327 ILE C CB  1 
ATOM   6317  C CG1 . ILE C  1 327 ? -63.610 -59.270  -11.438 1.00 63.66  ? 327 ILE C CG1 1 
ATOM   6318  C CG2 . ILE C  1 327 ? -66.083 -59.743  -11.097 1.00 84.85  ? 327 ILE C CG2 1 
ATOM   6319  C CD1 . ILE C  1 327 ? -62.904 -60.374  -10.684 1.00 56.30  ? 327 ILE C CD1 1 
ATOM   6320  N N   . GLY D  2 1   ? -55.338 -65.577  -10.915 1.00 84.51  ? 1   GLY D N   1 
ATOM   6321  C CA  . GLY D  2 1   ? -55.379 -66.725  -11.801 1.00 88.21  ? 1   GLY D CA  1 
ATOM   6322  C C   . GLY D  2 1   ? -54.365 -67.795  -11.440 1.00 84.17  ? 1   GLY D C   1 
ATOM   6323  O O   . GLY D  2 1   ? -54.628 -68.987  -11.599 1.00 71.26  ? 1   GLY D O   1 
ATOM   6324  N N   . LEU D  2 2   ? -53.206 -67.371  -10.944 1.00 73.70  ? 2   LEU D N   1 
ATOM   6325  C CA  . LEU D  2 2   ? -52.121 -68.303  -10.651 1.00 71.96  ? 2   LEU D CA  1 
ATOM   6326  C C   . LEU D  2 2   ? -52.094 -68.754  -9.191  1.00 65.19  ? 2   LEU D C   1 
ATOM   6327  O O   . LEU D  2 2   ? -51.628 -69.850  -8.884  1.00 62.28  ? 2   LEU D O   1 
ATOM   6328  C CB  . LEU D  2 2   ? -50.771 -67.693  -11.032 1.00 62.69  ? 2   LEU D CB  1 
ATOM   6329  C CG  . LEU D  2 2   ? -49.684 -68.705  -11.395 1.00 60.87  ? 2   LEU D CG  1 
ATOM   6330  C CD1 . LEU D  2 2   ? -50.104 -69.529  -12.606 1.00 61.45  ? 2   LEU D CD1 1 
ATOM   6331  C CD2 . LEU D  2 2   ? -48.358 -68.006  -11.644 1.00 43.15  ? 2   LEU D CD2 1 
ATOM   6332  N N   . PHE D  2 3   ? -52.586 -67.908  -8.293  1.00 60.92  ? 3   PHE D N   1 
ATOM   6333  C CA  . PHE D  2 3   ? -52.602 -68.243  -6.872  1.00 67.55  ? 3   PHE D CA  1 
ATOM   6334  C C   . PHE D  2 3   ? -53.996 -68.643  -6.392  1.00 83.39  ? 3   PHE D C   1 
ATOM   6335  O O   . PHE D  2 3   ? -54.205 -68.896  -5.205  1.00 79.14  ? 3   PHE D O   1 
ATOM   6336  C CB  . PHE D  2 3   ? -52.042 -67.091  -6.035  1.00 68.48  ? 3   PHE D CB  1 
ATOM   6337  C CG  . PHE D  2 3   ? -50.567 -66.869  -6.223  1.00 69.87  ? 3   PHE D CG  1 
ATOM   6338  C CD1 . PHE D  2 3   ? -50.099 -66.066  -7.250  1.00 66.58  ? 3   PHE D CD1 1 
ATOM   6339  C CD2 . PHE D  2 3   ? -49.649 -67.466  -5.375  1.00 72.87  ? 3   PHE D CD2 1 
ATOM   6340  C CE1 . PHE D  2 3   ? -48.743 -65.862  -7.427  1.00 64.14  ? 3   PHE D CE1 1 
ATOM   6341  C CE2 . PHE D  2 3   ? -48.292 -67.265  -5.547  1.00 70.58  ? 3   PHE D CE2 1 
ATOM   6342  C CZ  . PHE D  2 3   ? -47.839 -66.462  -6.574  1.00 67.88  ? 3   PHE D CZ  1 
ATOM   6343  N N   . GLY D  2 4   ? -54.943 -68.698  -7.324  1.00 79.10  ? 4   GLY D N   1 
ATOM   6344  C CA  . GLY D  2 4   ? -56.279 -69.191  -7.042  1.00 69.47  ? 4   GLY D CA  1 
ATOM   6345  C C   . GLY D  2 4   ? -57.157 -68.258  -6.230  1.00 77.42  ? 4   GLY D C   1 
ATOM   6346  O O   . GLY D  2 4   ? -58.308 -68.583  -5.936  1.00 75.81  ? 4   GLY D O   1 
ATOM   6347  N N   . ALA D  2 5   ? -56.623 -67.097  -5.867  1.00 79.81  ? 5   ALA D N   1 
ATOM   6348  C CA  . ALA D  2 5   ? -57.366 -66.142  -5.050  1.00 72.28  ? 5   ALA D CA  1 
ATOM   6349  C C   . ALA D  2 5   ? -58.329 -65.301  -5.883  1.00 66.04  ? 5   ALA D C   1 
ATOM   6350  O O   . ALA D  2 5   ? -59.544 -65.491  -5.822  1.00 63.19  ? 5   ALA D O   1 
ATOM   6351  C CB  . ALA D  2 5   ? -56.410 -65.249  -4.271  1.00 66.57  ? 5   ALA D CB  1 
ATOM   6352  N N   . ILE D  2 6   ? -57.782 -64.369  -6.657  1.00 72.44  ? 6   ILE D N   1 
ATOM   6353  C CA  . ILE D  2 6   ? -58.596 -63.487  -7.486  1.00 61.63  ? 6   ILE D CA  1 
ATOM   6354  C C   . ILE D  2 6   ? -59.262 -64.262  -8.618  1.00 67.66  ? 6   ILE D C   1 
ATOM   6355  O O   . ILE D  2 6   ? -58.596 -64.966  -9.378  1.00 71.33  ? 6   ILE D O   1 
ATOM   6356  C CB  . ILE D  2 6   ? -57.768 -62.324  -8.062  1.00 53.71  ? 6   ILE D CB  1 
ATOM   6357  C CG1 . ILE D  2 6   ? -57.151 -61.503  -6.928  1.00 47.13  ? 6   ILE D CG1 1 
ATOM   6358  C CG2 . ILE D  2 6   ? -58.632 -61.441  -8.949  1.00 53.04  ? 6   ILE D CG2 1 
ATOM   6359  C CD1 . ILE D  2 6   ? -56.456 -60.243  -7.391  1.00 54.95  ? 6   ILE D CD1 1 
ATOM   6360  N N   . ALA D  2 7   ? -60.581 -64.124  -8.722  1.00 61.04  ? 7   ALA D N   1 
ATOM   6361  C CA  . ALA D  2 7   ? -61.367 -64.902  -9.672  1.00 60.22  ? 7   ALA D CA  1 
ATOM   6362  C C   . ALA D  2 7   ? -61.251 -66.391  -9.360  1.00 77.36  ? 7   ALA D C   1 
ATOM   6363  O O   . ALA D  2 7   ? -61.413 -67.237  -10.240 1.00 78.98  ? 7   ALA D O   1 
ATOM   6364  C CB  . ALA D  2 7   ? -60.928 -64.613  -11.100 1.00 58.22  ? 7   ALA D CB  1 
ATOM   6365  N N   . GLY D  2 8   ? -60.965 -66.699  -8.098  1.00 80.77  ? 8   GLY D N   1 
ATOM   6366  C CA  . GLY D  2 8   ? -60.846 -68.071  -7.639  1.00 81.17  ? 8   GLY D CA  1 
ATOM   6367  C C   . GLY D  2 8   ? -61.843 -68.377  -6.538  1.00 97.97  ? 8   GLY D C   1 
ATOM   6368  O O   . GLY D  2 8   ? -63.053 -68.311  -6.758  1.00 93.52  ? 8   GLY D O   1 
ATOM   6369  N N   . PHE D  2 9   ? -61.344 -68.712  -5.351  1.00 71.80  ? 9   PHE D N   1 
ATOM   6370  C CA  . PHE D  2 9   ? -62.228 -68.967  -4.216  1.00 73.94  ? 9   PHE D CA  1 
ATOM   6371  C C   . PHE D  2 9   ? -62.831 -67.666  -3.688  1.00 79.01  ? 9   PHE D C   1 
ATOM   6372  O O   . PHE D  2 9   ? -63.835 -67.680  -2.976  1.00 99.11  ? 9   PHE D O   1 
ATOM   6373  C CB  . PHE D  2 9   ? -61.523 -69.758  -3.105  1.00 80.48  ? 9   PHE D CB  1 
ATOM   6374  C CG  . PHE D  2 9   ? -60.275 -69.105  -2.577  1.00 73.80  ? 9   PHE D CG  1 
ATOM   6375  C CD1 . PHE D  2 9   ? -60.352 -68.025  -1.714  1.00 75.61  ? 9   PHE D CD1 1 
ATOM   6376  C CD2 . PHE D  2 9   ? -59.025 -69.594  -2.919  1.00 80.93  ? 9   PHE D CD2 1 
ATOM   6377  C CE1 . PHE D  2 9   ? -59.206 -67.431  -1.219  1.00 77.32  ? 9   PHE D CE1 1 
ATOM   6378  C CE2 . PHE D  2 9   ? -57.876 -69.005  -2.427  1.00 85.88  ? 9   PHE D CE2 1 
ATOM   6379  C CZ  . PHE D  2 9   ? -57.966 -67.922  -1.576  1.00 86.46  ? 9   PHE D CZ  1 
ATOM   6380  N N   . ILE D  2 10  ? -62.207 -66.547  -4.042  1.00 63.02  ? 10  ILE D N   1 
ATOM   6381  C CA  . ILE D  2 10  ? -62.809 -65.235  -3.838  1.00 70.21  ? 10  ILE D CA  1 
ATOM   6382  C C   . ILE D  2 10  ? -63.306 -64.748  -5.194  1.00 74.32  ? 10  ILE D C   1 
ATOM   6383  O O   . ILE D  2 10  ? -62.566 -64.125  -5.956  1.00 73.86  ? 10  ILE D O   1 
ATOM   6384  C CB  . ILE D  2 10  ? -61.813 -64.223  -3.247  1.00 63.80  ? 10  ILE D CB  1 
ATOM   6385  C CG1 . ILE D  2 10  ? -61.118 -64.812  -2.018  1.00 64.96  ? 10  ILE D CG1 1 
ATOM   6386  C CG2 . ILE D  2 10  ? -62.523 -62.928  -2.883  1.00 49.21  ? 10  ILE D CG2 1 
ATOM   6387  C CD1 . ILE D  2 10  ? -60.141 -63.866  -1.356  1.00 65.39  ? 10  ILE D CD1 1 
ATOM   6388  N N   . GLU D  2 11  ? -64.568 -65.044  -5.485  1.00 99.56  ? 11  GLU D N   1 
ATOM   6389  C CA  . GLU D  2 11  ? -65.124 -64.896  -6.827  1.00 98.18  ? 11  GLU D CA  1 
ATOM   6390  C C   . GLU D  2 11  ? -65.157 -63.466  -7.360  1.00 88.82  ? 11  GLU D C   1 
ATOM   6391  O O   . GLU D  2 11  ? -64.946 -63.241  -8.552  1.00 93.53  ? 11  GLU D O   1 
ATOM   6392  C CB  . GLU D  2 11  ? -66.532 -65.492  -6.875  1.00 118.43 ? 11  GLU D CB  1 
ATOM   6393  C CG  . GLU D  2 11  ? -66.603 -66.938  -6.417  1.00 134.28 ? 11  GLU D CG  1 
ATOM   6394  C CD  . GLU D  2 11  ? -68.024 -67.460  -6.356  1.00 166.53 ? 11  GLU D CD  1 
ATOM   6395  O OE1 . GLU D  2 11  ? -68.212 -68.631  -5.964  1.00 170.19 ? 11  GLU D OE1 1 
ATOM   6396  O OE2 . GLU D  2 11  ? -68.953 -66.699  -6.699  1.00 157.65 ? 11  GLU D OE2 1 
ATOM   6397  N N   . GLY D  2 12  ? -65.428 -62.503  -6.488  1.00 77.01  ? 12  GLY D N   1 
ATOM   6398  C CA  . GLY D  2 12  ? -65.641 -61.142  -6.943  1.00 71.44  ? 12  GLY D CA  1 
ATOM   6399  C C   . GLY D  2 12  ? -64.879 -60.065  -6.202  1.00 68.39  ? 12  GLY D C   1 
ATOM   6400  O O   . GLY D  2 12  ? -64.277 -60.307  -5.155  1.00 73.26  ? 12  GLY D O   1 
ATOM   6401  N N   . GLY D  2 13  ? -64.915 -58.861  -6.763  1.00 62.07  ? 13  GLY D N   1 
ATOM   6402  C CA  . GLY D  2 13  ? -64.281 -57.709  -6.157  1.00 62.40  ? 13  GLY D CA  1 
ATOM   6403  C C   . GLY D  2 13  ? -65.268 -56.803  -5.446  1.00 65.99  ? 13  GLY D C   1 
ATOM   6404  O O   . GLY D  2 13  ? -66.478 -57.000  -5.544  1.00 73.82  ? 13  GLY D O   1 
ATOM   6405  N N   . TRP D  2 14  ? -64.754 -55.807  -4.730  1.00 61.99  ? 14  TRP D N   1 
ATOM   6406  C CA  . TRP D  2 14  ? -65.605 -54.891  -3.978  1.00 65.14  ? 14  TRP D CA  1 
ATOM   6407  C C   . TRP D  2 14  ? -65.518 -53.456  -4.486  1.00 74.33  ? 14  TRP D C   1 
ATOM   6408  O O   . TRP D  2 14  ? -64.544 -52.752  -4.220  1.00 81.51  ? 14  TRP D O   1 
ATOM   6409  C CB  . TRP D  2 14  ? -65.255 -54.924  -2.489  1.00 73.55  ? 14  TRP D CB  1 
ATOM   6410  C CG  . TRP D  2 14  ? -65.424 -56.267  -1.856  1.00 74.65  ? 14  TRP D CG  1 
ATOM   6411  C CD1 . TRP D  2 14  ? -66.271 -57.260  -2.252  1.00 70.93  ? 14  TRP D CD1 1 
ATOM   6412  C CD2 . TRP D  2 14  ? -64.739 -56.761  -0.699  1.00 66.42  ? 14  TRP D CD2 1 
ATOM   6413  N NE1 . TRP D  2 14  ? -66.149 -58.345  -1.419  1.00 62.38  ? 14  TRP D NE1 1 
ATOM   6414  C CE2 . TRP D  2 14  ? -65.216 -58.064  -0.457  1.00 72.29  ? 14  TRP D CE2 1 
ATOM   6415  C CE3 . TRP D  2 14  ? -63.765 -56.229  0.153   1.00 66.38  ? 14  TRP D CE3 1 
ATOM   6416  C CZ2 . TRP D  2 14  ? -64.753 -58.844  0.600   1.00 74.68  ? 14  TRP D CZ2 1 
ATOM   6417  C CZ3 . TRP D  2 14  ? -63.308 -57.005  1.203   1.00 83.85  ? 14  TRP D CZ3 1 
ATOM   6418  C CH2 . TRP D  2 14  ? -63.802 -58.298  1.418   1.00 82.07  ? 14  TRP D CH2 1 
ATOM   6419  N N   . THR D  2 15  ? -66.546 -53.026  -5.210  1.00 72.94  ? 15  THR D N   1 
ATOM   6420  C CA  . THR D  2 15  ? -66.654 -51.636  -5.626  1.00 84.26  ? 15  THR D CA  1 
ATOM   6421  C C   . THR D  2 15  ? -66.685 -50.749  -4.387  1.00 92.02  ? 15  THR D C   1 
ATOM   6422  O O   . THR D  2 15  ? -66.284 -49.586  -4.427  1.00 91.99  ? 15  THR D O   1 
ATOM   6423  C CB  . THR D  2 15  ? -67.936 -51.395  -6.442  1.00 85.18  ? 15  THR D CB  1 
ATOM   6424  O OG1 . THR D  2 15  ? -69.081 -51.648  -5.619  1.00 103.44 ? 15  THR D OG1 1 
ATOM   6425  C CG2 . THR D  2 15  ? -67.978 -52.312  -7.656  1.00 81.17  ? 15  THR D CG2 1 
ATOM   6426  N N   . GLY D  2 16  ? -67.160 -51.320  -3.283  1.00 90.05  ? 16  GLY D N   1 
ATOM   6427  C CA  . GLY D  2 16  ? -67.305 -50.594  -2.035  1.00 96.28  ? 16  GLY D CA  1 
ATOM   6428  C C   . GLY D  2 16  ? -65.998 -50.122  -1.428  1.00 93.63  ? 16  GLY D C   1 
ATOM   6429  O O   . GLY D  2 16  ? -65.923 -49.019  -0.887  1.00 94.87  ? 16  GLY D O   1 
ATOM   6430  N N   . MET D  2 17  ? -64.966 -50.956  -1.507  1.00 86.31  ? 17  MET D N   1 
ATOM   6431  C CA  . MET D  2 17  ? -63.662 -50.597  -0.961  1.00 86.19  ? 17  MET D CA  1 
ATOM   6432  C C   . MET D  2 17  ? -62.876 -49.738  -1.946  1.00 90.52  ? 17  MET D C   1 
ATOM   6433  O O   . MET D  2 17  ? -62.429 -50.220  -2.987  1.00 91.91  ? 17  MET D O   1 
ATOM   6434  C CB  . MET D  2 17  ? -62.863 -51.846  -0.590  1.00 74.45  ? 17  MET D CB  1 
ATOM   6435  C CG  . MET D  2 17  ? -61.517 -51.542  0.046   1.00 93.58  ? 17  MET D CG  1 
ATOM   6436  S SD  . MET D  2 17  ? -60.652 -53.021  0.600   1.00 91.10  ? 17  MET D SD  1 
ATOM   6437  C CE  . MET D  2 17  ? -60.572 -53.946  -0.925  1.00 84.88  ? 17  MET D CE  1 
ATOM   6438  N N   . VAL D  2 18  ? -62.709 -48.463  -1.607  1.00 102.99 ? 18  VAL D N   1 
ATOM   6439  C CA  . VAL D  2 18  ? -62.066 -47.507  -2.502  1.00 109.29 ? 18  VAL D CA  1 
ATOM   6440  C C   . VAL D  2 18  ? -60.825 -46.884  -1.873  1.00 103.07 ? 18  VAL D C   1 
ATOM   6441  O O   . VAL D  2 18  ? -60.321 -45.867  -2.350  1.00 107.16 ? 18  VAL D O   1 
ATOM   6442  C CB  . VAL D  2 18  ? -63.036 -46.379  -2.893  1.00 111.83 ? 18  VAL D CB  1 
ATOM   6443  C CG1 . VAL D  2 18  ? -64.264 -46.953  -3.583  1.00 100.83 ? 18  VAL D CG1 1 
ATOM   6444  C CG2 . VAL D  2 18  ? -63.437 -45.578  -1.664  1.00 106.20 ? 18  VAL D CG2 1 
ATOM   6445  N N   . ASP D  2 19  ? -60.334 -47.498  -0.802  1.00 100.62 ? 19  ASP D N   1 
ATOM   6446  C CA  . ASP D  2 19  ? -59.182 -46.969  -0.081  1.00 109.69 ? 19  ASP D CA  1 
ATOM   6447  C C   . ASP D  2 19  ? -57.877 -47.564  -0.599  1.00 105.12 ? 19  ASP D C   1 
ATOM   6448  O O   . ASP D  2 19  ? -56.835 -46.909  -0.582  1.00 97.62  ? 19  ASP D O   1 
ATOM   6449  C CB  . ASP D  2 19  ? -59.323 -47.244  1.417   1.00 122.58 ? 19  ASP D CB  1 
ATOM   6450  C CG  . ASP D  2 19  ? -60.682 -46.845  1.957   1.00 132.11 ? 19  ASP D CG  1 
ATOM   6451  O OD1 . ASP D  2 19  ? -61.311 -45.933  1.379   1.00 139.25 ? 19  ASP D OD1 1 
ATOM   6452  O OD2 . ASP D  2 19  ? -61.122 -47.443  2.961   1.00 127.19 ? 19  ASP D OD2 1 
ATOM   6453  N N   . GLY D  2 20  ? -57.941 -48.809  -1.060  1.00 103.45 ? 20  GLY D N   1 
ATOM   6454  C CA  . GLY D  2 20  ? -56.764 -49.497  -1.557  1.00 84.19  ? 20  GLY D CA  1 
ATOM   6455  C C   . GLY D  2 20  ? -57.095 -50.659  -2.473  1.00 74.26  ? 20  GLY D C   1 
ATOM   6456  O O   . GLY D  2 20  ? -58.247 -50.846  -2.866  1.00 66.04  ? 20  GLY D O   1 
ATOM   6457  N N   . TRP D  2 21  ? -56.078 -51.445  -2.813  1.00 72.73  ? 21  TRP D N   1 
ATOM   6458  C CA  . TRP D  2 21  ? -56.255 -52.581  -3.709  1.00 71.47  ? 21  TRP D CA  1 
ATOM   6459  C C   . TRP D  2 21  ? -56.722 -53.836  -2.982  1.00 62.14  ? 21  TRP D C   1 
ATOM   6460  O O   . TRP D  2 21  ? -57.520 -54.599  -3.514  1.00 62.22  ? 21  TRP D O   1 
ATOM   6461  C CB  . TRP D  2 21  ? -54.968 -52.871  -4.480  1.00 74.80  ? 21  TRP D CB  1 
ATOM   6462  C CG  . TRP D  2 21  ? -54.782 -51.993  -5.672  1.00 69.83  ? 21  TRP D CG  1 
ATOM   6463  C CD1 . TRP D  2 21  ? -55.758 -51.357  -6.381  1.00 53.85  ? 21  TRP D CD1 1 
ATOM   6464  C CD2 . TRP D  2 21  ? -53.543 -51.665  -6.311  1.00 64.69  ? 21  TRP D CD2 1 
ATOM   6465  N NE1 . TRP D  2 21  ? -55.204 -50.648  -7.418  1.00 63.46  ? 21  TRP D NE1 1 
ATOM   6466  C CE2 . TRP D  2 21  ? -53.845 -50.821  -7.397  1.00 57.06  ? 21  TRP D CE2 1 
ATOM   6467  C CE3 . TRP D  2 21  ? -52.208 -52.001  -6.068  1.00 63.68  ? 21  TRP D CE3 1 
ATOM   6468  C CZ2 . TRP D  2 21  ? -52.862 -50.307  -8.239  1.00 63.05  ? 21  TRP D CZ2 1 
ATOM   6469  C CZ3 . TRP D  2 21  ? -51.233 -51.490  -6.905  1.00 60.98  ? 21  TRP D CZ3 1 
ATOM   6470  C CH2 . TRP D  2 21  ? -51.564 -50.652  -7.977  1.00 56.54  ? 21  TRP D CH2 1 
ATOM   6471  N N   . TYR D  2 22  ? -56.212 -54.052  -1.774  1.00 70.45  ? 22  TYR D N   1 
ATOM   6472  C CA  . TYR D  2 22  ? -56.633 -55.188  -0.961  1.00 74.49  ? 22  TYR D CA  1 
ATOM   6473  C C   . TYR D  2 22  ? -57.057 -54.698  0.418   1.00 80.37  ? 22  TYR D C   1 
ATOM   6474  O O   . TYR D  2 22  ? -56.507 -53.723  0.929   1.00 90.85  ? 22  TYR D O   1 
ATOM   6475  C CB  . TYR D  2 22  ? -55.502 -56.211  -0.830  1.00 76.12  ? 22  TYR D CB  1 
ATOM   6476  C CG  . TYR D  2 22  ? -54.463 -56.128  -1.925  1.00 76.46  ? 22  TYR D CG  1 
ATOM   6477  C CD1 . TYR D  2 22  ? -53.292 -55.405  -1.739  1.00 71.32  ? 22  TYR D CD1 1 
ATOM   6478  C CD2 . TYR D  2 22  ? -54.651 -56.769  -3.142  1.00 68.57  ? 22  TYR D CD2 1 
ATOM   6479  C CE1 . TYR D  2 22  ? -52.338 -55.323  -2.733  1.00 66.82  ? 22  TYR D CE1 1 
ATOM   6480  C CE2 . TYR D  2 22  ? -53.701 -56.692  -4.143  1.00 67.59  ? 22  TYR D CE2 1 
ATOM   6481  C CZ  . TYR D  2 22  ? -52.547 -55.967  -3.933  1.00 70.13  ? 22  TYR D CZ  1 
ATOM   6482  O OH  . TYR D  2 22  ? -51.597 -55.885  -4.924  1.00 59.53  ? 22  TYR D OH  1 
ATOM   6483  N N   . GLY D  2 23  ? -58.034 -55.371  1.017   1.00 102.77 ? 23  GLY D N   1 
ATOM   6484  C CA  . GLY D  2 23  ? -58.532 -54.978  2.324   1.00 107.74 ? 23  GLY D CA  1 
ATOM   6485  C C   . GLY D  2 23  ? -59.515 -55.962  2.929   1.00 104.02 ? 23  GLY D C   1 
ATOM   6486  O O   . GLY D  2 23  ? -59.619 -57.105  2.483   1.00 90.47  ? 23  GLY D O   1 
ATOM   6487  N N   . TYR D  2 24  ? -60.244 -55.512  3.946   1.00 85.19  ? 24  TYR D N   1 
ATOM   6488  C CA  . TYR D  2 24  ? -61.170 -56.375  4.673   1.00 86.27  ? 24  TYR D CA  1 
ATOM   6489  C C   . TYR D  2 24  ? -62.588 -55.813  4.702   1.00 94.24  ? 24  TYR D C   1 
ATOM   6490  O O   . TYR D  2 24  ? -62.829 -54.673  4.307   1.00 89.95  ? 24  TYR D O   1 
ATOM   6491  C CB  . TYR D  2 24  ? -60.696 -56.574  6.115   1.00 81.30  ? 24  TYR D CB  1 
ATOM   6492  C CG  . TYR D  2 24  ? -59.206 -56.773  6.273   1.00 77.46  ? 24  TYR D CG  1 
ATOM   6493  C CD1 . TYR D  2 24  ? -58.345 -55.686  6.344   1.00 84.60  ? 24  TYR D CD1 1 
ATOM   6494  C CD2 . TYR D  2 24  ? -58.662 -58.047  6.374   1.00 75.80  ? 24  TYR D CD2 1 
ATOM   6495  C CE1 . TYR D  2 24  ? -56.984 -55.861  6.496   1.00 87.53  ? 24  TYR D CE1 1 
ATOM   6496  C CE2 . TYR D  2 24  ? -57.301 -58.232  6.527   1.00 75.67  ? 24  TYR D CE2 1 
ATOM   6497  C CZ  . TYR D  2 24  ? -56.467 -57.135  6.588   1.00 84.51  ? 24  TYR D CZ  1 
ATOM   6498  O OH  . TYR D  2 24  ? -55.111 -57.312  6.740   1.00 80.92  ? 24  TYR D OH  1 
ATOM   6499  N N   . HIS D  2 25  ? -63.523 -56.628  5.182   1.00 89.37  ? 25  HIS D N   1 
ATOM   6500  C CA  . HIS D  2 25  ? -64.888 -56.182  5.442   1.00 98.87  ? 25  HIS D CA  1 
ATOM   6501  C C   . HIS D  2 25  ? -65.431 -56.866  6.691   1.00 110.61 ? 25  HIS D C   1 
ATOM   6502  O O   . HIS D  2 25  ? -65.920 -57.994  6.636   1.00 92.78  ? 25  HIS D O   1 
ATOM   6503  C CB  . HIS D  2 25  ? -65.802 -56.454  4.247   1.00 100.44 ? 25  HIS D CB  1 
ATOM   6504  C CG  . HIS D  2 25  ? -67.259 -56.296  4.557   1.00 106.35 ? 25  HIS D CG  1 
ATOM   6505  N ND1 . HIS D  2 25  ? -68.076 -57.366  4.846   1.00 99.87  ? 25  HIS D ND1 1 
ATOM   6506  C CD2 . HIS D  2 25  ? -68.042 -55.194  4.631   1.00 92.83  ? 25  HIS D CD2 1 
ATOM   6507  C CE1 . HIS D  2 25  ? -69.302 -56.932  5.081   1.00 103.61 ? 25  HIS D CE1 1 
ATOM   6508  N NE2 . HIS D  2 25  ? -69.307 -55.616  4.957   1.00 107.75 ? 25  HIS D NE2 1 
ATOM   6509  N N   . HIS D  2 26  ? -65.334 -56.172  7.818   1.00 128.58 ? 26  HIS D N   1 
ATOM   6510  C CA  . HIS D  2 26  ? -65.750 -56.710  9.104   1.00 127.91 ? 26  HIS D CA  1 
ATOM   6511  C C   . HIS D  2 26  ? -67.271 -56.708  9.210   1.00 133.73 ? 26  HIS D C   1 
ATOM   6512  O O   . HIS D  2 26  ? -67.949 -56.021  8.450   1.00 135.02 ? 26  HIS D O   1 
ATOM   6513  C CB  . HIS D  2 26  ? -65.143 -55.871  10.218  1.00 124.42 ? 26  HIS D CB  1 
ATOM   6514  C CG  . HIS D  2 26  ? -65.820 -54.553  10.409  1.00 123.35 ? 26  HIS D CG  1 
ATOM   6515  N ND1 . HIS D  2 26  ? -65.573 -53.461  9.603   1.00 125.55 ? 26  HIS D ND1 1 
ATOM   6516  C CD2 . HIS D  2 26  ? -66.739 -54.149  11.319  1.00 139.55 ? 26  HIS D CD2 1 
ATOM   6517  C CE1 . HIS D  2 26  ? -66.312 -52.443  10.008  1.00 134.47 ? 26  HIS D CE1 1 
ATOM   6518  N NE2 . HIS D  2 26  ? -67.027 -52.833  11.045  1.00 148.49 ? 26  HIS D NE2 1 
ATOM   6519  N N   . GLN D  2 27  ? -67.805 -57.468  10.160  1.00 140.80 ? 27  GLN D N   1 
ATOM   6520  C CA  . GLN D  2 27  ? -69.251 -57.603  10.306  1.00 145.47 ? 27  GLN D CA  1 
ATOM   6521  C C   . GLN D  2 27  ? -69.622 -57.962  11.746  1.00 145.53 ? 27  GLN D C   1 
ATOM   6522  O O   . GLN D  2 27  ? -70.295 -58.963  11.994  1.00 137.18 ? 27  GLN D O   1 
ATOM   6523  C CB  . GLN D  2 27  ? -69.782 -58.655  9.326   1.00 140.75 ? 27  GLN D CB  1 
ATOM   6524  C CG  . GLN D  2 27  ? -71.267 -58.994  9.438   1.00 140.75 ? 27  GLN D CG  1 
ATOM   6525  C CD  . GLN D  2 27  ? -72.170 -57.828  9.091   1.00 151.60 ? 27  GLN D CD  1 
ATOM   6526  O OE1 . GLN D  2 27  ? -72.727 -57.765  7.996   1.00 149.86 ? 27  GLN D OE1 1 
ATOM   6527  N NE2 . GLN D  2 27  ? -72.321 -56.899  10.026  1.00 152.64 ? 27  GLN D NE2 1 
ATOM   6528  N N   . ASN D  2 28  ? -69.173 -57.141  12.693  1.00 157.70 ? 28  ASN D N   1 
ATOM   6529  C CA  . ASN D  2 28  ? -69.449 -57.383  14.104  1.00 155.57 ? 28  ASN D CA  1 
ATOM   6530  C C   . ASN D  2 28  ? -70.588 -56.519  14.631  1.00 162.22 ? 28  ASN D C   1 
ATOM   6531  O O   . ASN D  2 28  ? -71.315 -55.893  13.860  1.00 165.39 ? 28  ASN D O   1 
ATOM   6532  C CB  . ASN D  2 28  ? -68.190 -57.207  14.959  1.00 138.18 ? 28  ASN D CB  1 
ATOM   6533  C CG  . ASN D  2 28  ? -67.756 -55.750  15.092  1.00 134.26 ? 28  ASN D CG  1 
ATOM   6534  O OD1 . ASN D  2 28  ? -66.825 -55.440  15.837  1.00 127.97 ? 28  ASN D OD1 1 
ATOM   6535  N ND2 . ASN D  2 28  ? -68.425 -54.855  14.373  1.00 142.74 ? 28  ASN D ND2 1 
ATOM   6536  N N   . GLU D  2 29  ? -70.721 -56.478  15.951  1.00 152.15 ? 29  GLU D N   1 
ATOM   6537  C CA  . GLU D  2 29  ? -71.865 -55.852  16.603  1.00 152.64 ? 29  GLU D CA  1 
ATOM   6538  C C   . GLU D  2 29  ? -71.831 -54.322  16.588  1.00 146.86 ? 29  GLU D C   1 
ATOM   6539  O O   . GLU D  2 29  ? -72.816 -53.675  16.940  1.00 131.35 ? 29  GLU D O   1 
ATOM   6540  C CB  . GLU D  2 29  ? -71.969 -56.358  18.041  1.00 161.91 ? 29  GLU D CB  1 
ATOM   6541  C CG  . GLU D  2 29  ? -71.946 -57.880  18.164  1.00 163.02 ? 29  GLU D CG  1 
ATOM   6542  C CD  . GLU D  2 29  ? -71.427 -58.353  19.512  1.00 170.24 ? 29  GLU D CD  1 
ATOM   6543  O OE1 . GLU D  2 29  ? -70.647 -57.609  20.141  1.00 164.27 ? 29  GLU D OE1 1 
ATOM   6544  O OE2 . GLU D  2 29  ? -71.792 -59.469  19.939  1.00 165.67 ? 29  GLU D OE2 1 
ATOM   6545  N N   . GLN D  2 30  ? -70.704 -53.746  16.182  1.00 150.01 ? 30  GLN D N   1 
ATOM   6546  C CA  . GLN D  2 30  ? -70.579 -52.292  16.143  1.00 142.20 ? 30  GLN D CA  1 
ATOM   6547  C C   . GLN D  2 30  ? -70.754 -51.725  14.738  1.00 145.57 ? 30  GLN D C   1 
ATOM   6548  O O   . GLN D  2 30  ? -70.553 -50.532  14.515  1.00 140.36 ? 30  GLN D O   1 
ATOM   6549  C CB  . GLN D  2 30  ? -69.240 -51.842  16.728  1.00 127.16 ? 30  GLN D CB  1 
ATOM   6550  C CG  . GLN D  2 30  ? -69.124 -52.044  18.225  1.00 118.55 ? 30  GLN D CG  1 
ATOM   6551  C CD  . GLN D  2 30  ? -67.922 -52.878  18.596  1.00 126.02 ? 30  GLN D CD  1 
ATOM   6552  O OE1 . GLN D  2 30  ? -66.845 -52.350  18.870  1.00 116.04 ? 30  GLN D OE1 1 
ATOM   6553  N NE2 . GLN D  2 30  ? -68.097 -54.193  18.601  1.00 130.10 ? 30  GLN D NE2 1 
ATOM   6554  N N   . GLY D  2 31  ? -71.127 -52.578  13.791  1.00 168.09 ? 31  GLY D N   1 
ATOM   6555  C CA  . GLY D  2 31  ? -71.370 -52.129  12.432  1.00 170.71 ? 31  GLY D CA  1 
ATOM   6556  C C   . GLY D  2 31  ? -70.613 -52.918  11.382  1.00 160.96 ? 31  GLY D C   1 
ATOM   6557  O O   . GLY D  2 31  ? -69.977 -53.925  11.689  1.00 151.94 ? 31  GLY D O   1 
ATOM   6558  N N   . SER D  2 32  ? -70.685 -52.455  10.138  1.00 149.95 ? 32  SER D N   1 
ATOM   6559  C CA  . SER D  2 32  ? -70.011 -53.115  9.026   1.00 140.06 ? 32  SER D CA  1 
ATOM   6560  C C   . SER D  2 32  ? -69.124 -52.123  8.282   1.00 135.02 ? 32  SER D C   1 
ATOM   6561  O O   . SER D  2 32  ? -68.782 -51.067  8.813   1.00 134.83 ? 32  SER D O   1 
ATOM   6562  C CB  . SER D  2 32  ? -71.036 -53.717  8.064   1.00 128.03 ? 32  SER D CB  1 
ATOM   6563  O OG  . SER D  2 32  ? -71.942 -54.563  8.749   1.00 132.35 ? 32  SER D OG  1 
ATOM   6564  N N   . GLY D  2 33  ? -68.757 -52.467  7.051   1.00 133.59 ? 33  GLY D N   1 
ATOM   6565  C CA  . GLY D  2 33  ? -67.965 -51.578  6.220   1.00 131.69 ? 33  GLY D CA  1 
ATOM   6566  C C   . GLY D  2 33  ? -66.704 -52.216  5.668   1.00 112.47 ? 33  GLY D C   1 
ATOM   6567  O O   . GLY D  2 33  ? -66.322 -53.315  6.071   1.00 100.80 ? 33  GLY D O   1 
ATOM   6568  N N   . TYR D  2 34  ? -66.058 -51.518  4.739   1.00 103.98 ? 34  TYR D N   1 
ATOM   6569  C CA  . TYR D  2 34  ? -64.817 -51.994  4.140   1.00 89.08  ? 34  TYR D CA  1 
ATOM   6570  C C   . TYR D  2 34  ? -63.627 -51.186  4.647   1.00 91.36  ? 34  TYR D C   1 
ATOM   6571  O O   . TYR D  2 34  ? -63.745 -49.988  4.909   1.00 94.38  ? 34  TYR D O   1 
ATOM   6572  C CB  . TYR D  2 34  ? -64.884 -51.895  2.614   1.00 88.61  ? 34  TYR D CB  1 
ATOM   6573  C CG  . TYR D  2 34  ? -66.092 -52.562  1.994   1.00 83.69  ? 34  TYR D CG  1 
ATOM   6574  C CD1 . TYR D  2 34  ? -67.278 -51.864  1.813   1.00 71.86  ? 34  TYR D CD1 1 
ATOM   6575  C CD2 . TYR D  2 34  ? -66.042 -53.886  1.578   1.00 76.84  ? 34  TYR D CD2 1 
ATOM   6576  C CE1 . TYR D  2 34  ? -68.382 -52.466  1.243   1.00 83.74  ? 34  TYR D CE1 1 
ATOM   6577  C CE2 . TYR D  2 34  ? -67.142 -54.497  1.006   1.00 64.40  ? 34  TYR D CE2 1 
ATOM   6578  C CZ  . TYR D  2 34  ? -68.309 -53.783  0.841   1.00 76.24  ? 34  TYR D CZ  1 
ATOM   6579  O OH  . TYR D  2 34  ? -69.408 -54.386  0.273   1.00 72.59  ? 34  TYR D OH  1 
ATOM   6580  N N   . ALA D  2 35  ? -62.481 -51.845  4.779   1.00 86.71  ? 35  ALA D N   1 
ATOM   6581  C CA  . ALA D  2 35  ? -61.253 -51.177  5.194   1.00 89.07  ? 35  ALA D CA  1 
ATOM   6582  C C   . ALA D  2 35  ? -60.051 -51.756  4.456   1.00 92.09  ? 35  ALA D C   1 
ATOM   6583  O O   . ALA D  2 35  ? -59.693 -52.917  4.650   1.00 99.22  ? 35  ALA D O   1 
ATOM   6584  C CB  . ALA D  2 35  ? -61.065 -51.293  6.698   1.00 93.26  ? 35  ALA D CB  1 
ATOM   6585  N N   . ALA D  2 36  ? -59.430 -50.941  3.610   1.00 78.53  ? 36  ALA D N   1 
ATOM   6586  C CA  . ALA D  2 36  ? -58.290 -51.388  2.818   1.00 87.54  ? 36  ALA D CA  1 
ATOM   6587  C C   . ALA D  2 36  ? -57.045 -51.572  3.678   1.00 85.57  ? 36  ALA D C   1 
ATOM   6588  O O   . ALA D  2 36  ? -56.765 -50.764  4.564   1.00 92.77  ? 36  ALA D O   1 
ATOM   6589  C CB  . ALA D  2 36  ? -58.014 -50.411  1.689   1.00 95.00  ? 36  ALA D CB  1 
ATOM   6590  N N   . ASP D  2 37  ? -56.302 -52.641  3.410   1.00 84.22  ? 37  ASP D N   1 
ATOM   6591  C CA  . ASP D  2 37  ? -55.072 -52.921  4.138   1.00 80.23  ? 37  ASP D CA  1 
ATOM   6592  C C   . ASP D  2 37  ? -54.017 -51.873  3.815   1.00 90.52  ? 37  ASP D C   1 
ATOM   6593  O O   . ASP D  2 37  ? -53.639 -51.688  2.658   1.00 90.99  ? 37  ASP D O   1 
ATOM   6594  C CB  . ASP D  2 37  ? -54.547 -54.316  3.801   1.00 76.47  ? 37  ASP D CB  1 
ATOM   6595  C CG  . ASP D  2 37  ? -53.334 -54.697  4.627   1.00 91.26  ? 37  ASP D CG  1 
ATOM   6596  O OD1 . ASP D  2 37  ? -52.748 -55.766  4.363   1.00 102.75 ? 37  ASP D OD1 1 
ATOM   6597  O OD2 . ASP D  2 37  ? -52.966 -53.929  5.541   1.00 99.28  ? 37  ASP D OD2 1 
ATOM   6598  N N   . LEU D  2 38  ? -53.540 -51.194  4.850   1.00 102.15 ? 38  LEU D N   1 
ATOM   6599  C CA  . LEU D  2 38  ? -52.617 -50.082  4.677   1.00 114.75 ? 38  LEU D CA  1 
ATOM   6600  C C   . LEU D  2 38  ? -51.270 -50.514  4.096   1.00 108.96 ? 38  LEU D C   1 
ATOM   6601  O O   . LEU D  2 38  ? -50.877 -50.063  3.020   1.00 96.68  ? 38  LEU D O   1 
ATOM   6602  C CB  . LEU D  2 38  ? -52.412 -49.362  6.011   1.00 137.47 ? 38  LEU D CB  1 
ATOM   6603  C CG  . LEU D  2 38  ? -52.377 -47.834  5.968   1.00 151.05 ? 38  LEU D CG  1 
ATOM   6604  C CD1 . LEU D  2 38  ? -52.189 -47.269  7.369   1.00 145.38 ? 38  LEU D CD1 1 
ATOM   6605  C CD2 . LEU D  2 38  ? -51.296 -47.336  5.019   1.00 150.36 ? 38  LEU D CD2 1 
ATOM   6606  N N   . LYS D  2 39  ? -50.568 -51.390  4.808   1.00 164.88 ? 39  LYS D N   1 
ATOM   6607  C CA  . LYS D  2 39  ? -49.219 -51.793  4.416   1.00 163.70 ? 39  LYS D CA  1 
ATOM   6608  C C   . LYS D  2 39  ? -49.168 -52.524  3.075   1.00 161.97 ? 39  LYS D C   1 
ATOM   6609  O O   . LYS D  2 39  ? -48.246 -52.319  2.285   1.00 160.85 ? 39  LYS D O   1 
ATOM   6610  C CB  . LYS D  2 39  ? -48.577 -52.655  5.508   1.00 178.44 ? 39  LYS D CB  1 
ATOM   6611  C CG  . LYS D  2 39  ? -47.117 -52.994  5.249   1.00 196.86 ? 39  LYS D CG  1 
ATOM   6612  C CD  . LYS D  2 39  ? -46.495 -53.703  6.441   1.00 218.99 ? 39  LYS D CD  1 
ATOM   6613  C CE  . LYS D  2 39  ? -45.011 -53.947  6.223   1.00 220.25 ? 39  LYS D CE  1 
ATOM   6614  N NZ  . LYS D  2 39  ? -44.370 -54.564  7.417   1.00 205.49 ? 39  LYS D NZ  1 
ATOM   6615  N N   . SER D  2 40  ? -50.158 -53.374  2.821   1.00 104.21 ? 40  SER D N   1 
ATOM   6616  C CA  . SER D  2 40  ? -50.176 -54.179  1.603   1.00 92.36  ? 40  SER D CA  1 
ATOM   6617  C C   . SER D  2 40  ? -50.390 -53.326  0.355   1.00 81.23  ? 40  SER D C   1 
ATOM   6618  O O   . SER D  2 40  ? -49.615 -53.403  -0.599  1.00 78.12  ? 40  SER D O   1 
ATOM   6619  C CB  . SER D  2 40  ? -51.252 -55.264  1.693   1.00 82.32  ? 40  SER D CB  1 
ATOM   6620  O OG  . SER D  2 40  ? -51.136 -56.188  0.625   1.00 88.70  ? 40  SER D OG  1 
ATOM   6621  N N   . THR D  2 41  ? -51.444 -52.517  0.365   1.00 75.25  ? 41  THR D N   1 
ATOM   6622  C CA  . THR D  2 41  ? -51.764 -51.665  -0.775  1.00 74.20  ? 41  THR D CA  1 
ATOM   6623  C C   . THR D  2 41  ? -50.632 -50.691  -1.085  1.00 78.28  ? 41  THR D C   1 
ATOM   6624  O O   . THR D  2 41  ? -50.341 -50.414  -2.249  1.00 73.88  ? 41  THR D O   1 
ATOM   6625  C CB  . THR D  2 41  ? -53.064 -50.872  -0.543  1.00 70.43  ? 41  THR D CB  1 
ATOM   6626  O OG1 . THR D  2 41  ? -54.168 -51.780  -0.434  1.00 72.31  ? 41  THR D OG1 1 
ATOM   6627  C CG2 . THR D  2 41  ? -53.316 -49.913  -1.698  1.00 64.37  ? 41  THR D CG2 1 
ATOM   6628  N N   . GLN D  2 42  ? -49.994 -50.177  -0.039  1.00 92.30  ? 42  GLN D N   1 
ATOM   6629  C CA  . GLN D  2 42  ? -48.912 -49.214  -0.207  1.00 89.57  ? 42  GLN D CA  1 
ATOM   6630  C C   . GLN D  2 42  ? -47.718 -49.828  -0.934  1.00 82.32  ? 42  GLN D C   1 
ATOM   6631  O O   . GLN D  2 42  ? -47.178 -49.233  -1.867  1.00 81.28  ? 42  GLN D O   1 
ATOM   6632  C CB  . GLN D  2 42  ? -48.475 -48.646  1.145   1.00 96.32  ? 42  GLN D CB  1 
ATOM   6633  C CG  . GLN D  2 42  ? -47.459 -47.522  1.035   1.00 105.77 ? 42  GLN D CG  1 
ATOM   6634  C CD  . GLN D  2 42  ? -47.964 -46.365  0.195   1.00 114.70 ? 42  GLN D CD  1 
ATOM   6635  O OE1 . GLN D  2 42  ? -49.165 -46.100  0.140   1.00 115.70 ? 42  GLN D OE1 1 
ATOM   6636  N NE2 . GLN D  2 42  ? -47.047 -45.668  -0.465  1.00 109.73 ? 42  GLN D NE2 1 
ATOM   6637  N N   . ASN D  2 43  ? -47.311 -51.019  -0.504  1.00 78.92  ? 43  ASN D N   1 
ATOM   6638  C CA  . ASN D  2 43  ? -46.199 -51.721  -1.137  1.00 80.54  ? 43  ASN D CA  1 
ATOM   6639  C C   . ASN D  2 43  ? -46.464 -52.038  -2.605  1.00 76.06  ? 43  ASN D C   1 
ATOM   6640  O O   . ASN D  2 43  ? -45.604 -51.825  -3.458  1.00 67.66  ? 43  ASN D O   1 
ATOM   6641  C CB  . ASN D  2 43  ? -45.859 -53.004  -0.376  1.00 84.91  ? 43  ASN D CB  1 
ATOM   6642  C CG  . ASN D  2 43  ? -44.731 -52.810  0.620   1.00 92.97  ? 43  ASN D CG  1 
ATOM   6643  O OD1 . ASN D  2 43  ? -44.870 -52.079  1.600   1.00 109.45 ? 43  ASN D OD1 1 
ATOM   6644  N ND2 . ASN D  2 43  ? -43.605 -53.469  0.372   1.00 89.40  ? 43  ASN D ND2 1 
ATOM   6645  N N   . ALA D  2 44  ? -47.658 -52.549  -2.891  1.00 76.85  ? 44  ALA D N   1 
ATOM   6646  C CA  . ALA D  2 44  ? -48.042 -52.876  -4.259  1.00 63.01  ? 44  ALA D CA  1 
ATOM   6647  C C   . ALA D  2 44  ? -47.900 -51.658  -5.165  1.00 60.73  ? 44  ALA D C   1 
ATOM   6648  O O   . ALA D  2 44  ? -47.282 -51.732  -6.226  1.00 61.92  ? 44  ALA D O   1 
ATOM   6649  C CB  . ALA D  2 44  ? -49.465 -53.409  -4.299  1.00 53.79  ? 44  ALA D CB  1 
ATOM   6650  N N   . ILE D  2 45  ? -48.475 -50.538  -4.737  1.00 57.58  ? 45  ILE D N   1 
ATOM   6651  C CA  . ILE D  2 45  ? -48.388 -49.294  -5.494  1.00 68.05  ? 45  ILE D CA  1 
ATOM   6652  C C   . ILE D  2 45  ? -46.938 -48.919  -5.782  1.00 67.57  ? 45  ILE D C   1 
ATOM   6653  O O   . ILE D  2 45  ? -46.583 -48.612  -6.920  1.00 68.96  ? 45  ILE D O   1 
ATOM   6654  C CB  . ILE D  2 45  ? -49.080 -48.131  -4.757  1.00 68.78  ? 45  ILE D CB  1 
ATOM   6655  C CG1 . ILE D  2 45  ? -50.600 -48.285  -4.830  1.00 63.53  ? 45  ILE D CG1 1 
ATOM   6656  C CG2 . ILE D  2 45  ? -48.658 -46.797  -5.351  1.00 67.88  ? 45  ILE D CG2 1 
ATOM   6657  C CD1 . ILE D  2 45  ? -51.362 -47.128  -4.219  1.00 82.81  ? 45  ILE D CD1 1 
ATOM   6658  N N   . ASP D  2 46  ? -46.104 -48.947  -4.747  1.00 68.71  ? 46  ASP D N   1 
ATOM   6659  C CA  . ASP D  2 46  ? -44.689 -48.628  -4.895  1.00 66.89  ? 46  ASP D CA  1 
ATOM   6660  C C   . ASP D  2 46  ? -44.007 -49.539  -5.911  1.00 66.32  ? 46  ASP D C   1 
ATOM   6661  O O   . ASP D  2 46  ? -43.291 -49.071  -6.796  1.00 70.98  ? 46  ASP D O   1 
ATOM   6662  C CB  . ASP D  2 46  ? -43.971 -48.722  -3.546  1.00 73.97  ? 46  ASP D CB  1 
ATOM   6663  C CG  . ASP D  2 46  ? -44.319 -47.575  -2.617  1.00 94.05  ? 46  ASP D CG  1 
ATOM   6664  O OD1 . ASP D  2 46  ? -44.841 -46.549  -3.103  1.00 97.06  ? 46  ASP D OD1 1 
ATOM   6665  O OD2 . ASP D  2 46  ? -44.063 -47.697  -1.400  1.00 92.81  ? 46  ASP D OD2 1 
ATOM   6666  N N   . GLU D  2 47  ? -44.235 -50.842  -5.781  1.00 63.88  ? 47  GLU D N   1 
ATOM   6667  C CA  . GLU D  2 47  ? -43.578 -51.822  -6.641  1.00 55.14  ? 47  GLU D CA  1 
ATOM   6668  C C   . GLU D  2 47  ? -44.115 -51.812  -8.072  1.00 57.07  ? 47  GLU D C   1 
ATOM   6669  O O   . GLU D  2 47  ? -43.351 -51.959  -9.026  1.00 52.49  ? 47  GLU D O   1 
ATOM   6670  C CB  . GLU D  2 47  ? -43.664 -53.224  -6.032  1.00 49.99  ? 47  GLU D CB  1 
ATOM   6671  C CG  . GLU D  2 47  ? -42.896 -53.364  -4.725  1.00 68.74  ? 47  GLU D CG  1 
ATOM   6672  C CD  . GLU D  2 47  ? -42.807 -54.798  -4.243  1.00 71.55  ? 47  GLU D CD  1 
ATOM   6673  O OE1 . GLU D  2 47  ? -43.618 -55.633  -4.694  1.00 66.42  ? 47  GLU D OE1 1 
ATOM   6674  O OE2 . GLU D  2 47  ? -41.923 -55.089  -3.409  1.00 82.03  ? 47  GLU D OE2 1 
ATOM   6675  N N   . ILE D  2 48  ? -45.425 -51.640  -8.221  1.00 51.38  ? 48  ILE D N   1 
ATOM   6676  C CA  . ILE D  2 48  ? -46.022 -51.520  -9.546  1.00 43.18  ? 48  ILE D CA  1 
ATOM   6677  C C   . ILE D  2 48  ? -45.533 -50.246  -10.225 1.00 52.55  ? 48  ILE D C   1 
ATOM   6678  O O   . ILE D  2 48  ? -45.264 -50.233  -11.426 1.00 50.86  ? 48  ILE D O   1 
ATOM   6679  C CB  . ILE D  2 48  ? -47.562 -51.525  -9.488  1.00 47.96  ? 48  ILE D CB  1 
ATOM   6680  C CG1 . ILE D  2 48  ? -48.073 -52.918  -9.115  1.00 54.02  ? 48  ILE D CG1 1 
ATOM   6681  C CG2 . ILE D  2 48  ? -48.149 -51.096  -10.825 1.00 40.20  ? 48  ILE D CG2 1 
ATOM   6682  C CD1 . ILE D  2 48  ? -47.632 -54.007  -10.071 1.00 51.81  ? 48  ILE D CD1 1 
ATOM   6683  N N   . THR D  2 49  ? -45.417 -49.175  -9.445  1.00 47.90  ? 49  THR D N   1 
ATOM   6684  C CA  . THR D  2 49  ? -44.868 -47.922  -9.944  1.00 45.80  ? 49  THR D CA  1 
ATOM   6685  C C   . THR D  2 49  ? -43.456 -48.145  -10.467 1.00 54.07  ? 49  THR D C   1 
ATOM   6686  O O   . THR D  2 49  ? -43.133 -47.775  -11.596 1.00 51.15  ? 49  THR D O   1 
ATOM   6687  C CB  . THR D  2 49  ? -44.827 -46.845  -8.846  1.00 52.48  ? 49  THR D CB  1 
ATOM   6688  O OG1 . THR D  2 49  ? -46.164 -46.460  -8.500  1.00 57.20  ? 49  THR D OG1 1 
ATOM   6689  C CG2 . THR D  2 49  ? -44.059 -45.622  -9.326  1.00 45.80  ? 49  THR D CG2 1 
ATOM   6690  N N   . ASN D  2 50  ? -42.620 -48.756  -9.636  1.00 45.43  ? 50  ASN D N   1 
ATOM   6691  C CA  . ASN D  2 50  ? -41.248 -49.065  -10.013 1.00 56.23  ? 50  ASN D CA  1 
ATOM   6692  C C   . ASN D  2 50  ? -41.201 -49.898  -11.290 1.00 51.56  ? 50  ASN D C   1 
ATOM   6693  O O   . ASN D  2 50  ? -40.335 -49.701  -12.143 1.00 45.98  ? 50  ASN D O   1 
ATOM   6694  C CB  . ASN D  2 50  ? -40.541 -49.801  -8.874  1.00 58.51  ? 50  ASN D CB  1 
ATOM   6695  C CG  . ASN D  2 50  ? -39.043 -49.890  -9.078  1.00 62.73  ? 50  ASN D CG  1 
ATOM   6696  O OD1 . ASN D  2 50  ? -38.294 -49.010  -8.653  1.00 68.40  ? 50  ASN D OD1 1 
ATOM   6697  N ND2 . ASN D  2 50  ? -38.598 -50.956  -9.729  1.00 52.41  ? 50  ASN D ND2 1 
ATOM   6698  N N   . LYS D  2 51  ? -42.145 -50.825  -11.413 1.00 50.92  ? 51  LYS D N   1 
ATOM   6699  C CA  . LYS D  2 51  ? -42.252 -51.671  -12.595 1.00 51.95  ? 51  LYS D CA  1 
ATOM   6700  C C   . LYS D  2 51  ? -42.459 -50.831  -13.850 1.00 50.26  ? 51  LYS D C   1 
ATOM   6701  O O   . LYS D  2 51  ? -41.747 -50.991  -14.841 1.00 45.47  ? 51  LYS D O   1 
ATOM   6702  C CB  . LYS D  2 51  ? -43.406 -52.661  -12.427 1.00 53.49  ? 51  LYS D CB  1 
ATOM   6703  C CG  . LYS D  2 51  ? -43.604 -53.609  -13.596 1.00 41.99  ? 51  LYS D CG  1 
ATOM   6704  C CD  . LYS D  2 51  ? -44.544 -54.740  -13.211 1.00 54.09  ? 51  LYS D CD  1 
ATOM   6705  C CE  . LYS D  2 51  ? -44.649 -55.777  -14.313 1.00 52.17  ? 51  LYS D CE  1 
ATOM   6706  N NZ  . LYS D  2 51  ? -45.151 -57.081  -13.797 1.00 57.69  ? 51  LYS D NZ  1 
ATOM   6707  N N   . VAL D  2 52  ? -43.437 -49.933  -13.796 1.00 47.06  ? 52  VAL D N   1 
ATOM   6708  C CA  . VAL D  2 52  ? -43.745 -49.060  -14.923 1.00 43.75  ? 52  VAL D CA  1 
ATOM   6709  C C   . VAL D  2 52  ? -42.566 -48.151  -15.255 1.00 51.40  ? 52  VAL D C   1 
ATOM   6710  O O   . VAL D  2 52  ? -42.250 -47.934  -16.425 1.00 60.92  ? 52  VAL D O   1 
ATOM   6711  C CB  . VAL D  2 52  ? -44.989 -48.196  -14.641 1.00 39.01  ? 52  VAL D CB  1 
ATOM   6712  C CG1 . VAL D  2 52  ? -45.325 -47.337  -15.849 1.00 37.07  ? 52  VAL D CG1 1 
ATOM   6713  C CG2 . VAL D  2 52  ? -46.170 -49.077  -14.265 1.00 44.00  ? 52  VAL D CG2 1 
ATOM   6714  N N   . ASN D  2 53  ? -41.918 -47.623  -14.221 1.00 44.74  ? 53  ASN D N   1 
ATOM   6715  C CA  . ASN D  2 53  ? -40.760 -46.757  -14.410 1.00 49.27  ? 53  ASN D CA  1 
ATOM   6716  C C   . ASN D  2 53  ? -39.599 -47.465  -15.101 1.00 59.68  ? 53  ASN D C   1 
ATOM   6717  O O   . ASN D  2 53  ? -38.900 -46.868  -15.916 1.00 56.13  ? 53  ASN D O   1 
ATOM   6718  C CB  . ASN D  2 53  ? -40.295 -46.169  -13.076 1.00 59.10  ? 53  ASN D CB  1 
ATOM   6719  C CG  . ASN D  2 53  ? -41.108 -44.961  -12.655 1.00 67.58  ? 53  ASN D CG  1 
ATOM   6720  O OD1 . ASN D  2 53  ? -41.938 -44.459  -13.414 1.00 56.75  ? 53  ASN D OD1 1 
ATOM   6721  N ND2 . ASN D  2 53  ? -40.869 -44.482  -11.439 1.00 72.68  ? 53  ASN D ND2 1 
ATOM   6722  N N   . SER D  2 54  ? -39.396 -48.736  -14.771 1.00 53.71  ? 54  SER D N   1 
ATOM   6723  C CA  . SER D  2 54  ? -38.309 -49.511  -15.360 1.00 41.74  ? 54  SER D CA  1 
ATOM   6724  C C   . SER D  2 54  ? -38.482 -49.665  -16.869 1.00 48.31  ? 54  SER D C   1 
ATOM   6725  O O   . SER D  2 54  ? -37.578 -49.346  -17.643 1.00 45.63  ? 54  SER D O   1 
ATOM   6726  C CB  . SER D  2 54  ? -38.206 -50.885  -14.695 1.00 42.43  ? 54  SER D CB  1 
ATOM   6727  O OG  . SER D  2 54  ? -37.876 -50.763  -13.323 1.00 55.77  ? 54  SER D OG  1 
ATOM   6728  N N   . VAL D  2 55  ? -39.648 -50.153  -17.279 1.00 44.08  ? 55  VAL D N   1 
ATOM   6729  C CA  . VAL D  2 55  ? -39.950 -50.343  -18.694 1.00 44.84  ? 55  VAL D CA  1 
ATOM   6730  C C   . VAL D  2 55  ? -39.722 -49.057  -19.485 1.00 48.50  ? 55  VAL D C   1 
ATOM   6731  O O   . VAL D  2 55  ? -39.369 -49.095  -20.664 1.00 48.54  ? 55  VAL D O   1 
ATOM   6732  C CB  . VAL D  2 55  ? -41.403 -50.821  -18.897 1.00 46.00  ? 55  VAL D CB  1 
ATOM   6733  C CG1 . VAL D  2 55  ? -41.749 -50.871  -20.379 1.00 48.34  ? 55  VAL D CG1 1 
ATOM   6734  C CG2 . VAL D  2 55  ? -41.611 -52.180  -18.247 1.00 32.58  ? 55  VAL D CG2 1 
ATOM   6735  N N   . ILE D  2 56  ? -39.915 -47.921  -18.824 1.00 50.97  ? 56  ILE D N   1 
ATOM   6736  C CA  . ILE D  2 56  ? -39.759 -46.619  -19.462 1.00 43.46  ? 56  ILE D CA  1 
ATOM   6737  C C   . ILE D  2 56  ? -38.337 -46.074  -19.343 1.00 48.35  ? 56  ILE D C   1 
ATOM   6738  O O   . ILE D  2 56  ? -37.727 -45.680  -20.337 1.00 42.86  ? 56  ILE D O   1 
ATOM   6739  C CB  . ILE D  2 56  ? -40.731 -45.584  -18.860 1.00 39.20  ? 56  ILE D CB  1 
ATOM   6740  C CG1 . ILE D  2 56  ? -42.179 -45.967  -19.168 1.00 46.56  ? 56  ILE D CG1 1 
ATOM   6741  C CG2 . ILE D  2 56  ? -40.421 -44.191  -19.384 1.00 39.79  ? 56  ILE D CG2 1 
ATOM   6742  C CD1 . ILE D  2 56  ? -43.200 -45.043  -18.541 1.00 46.42  ? 56  ILE D CD1 1 
ATOM   6743  N N   . GLU D  2 57  ? -37.816 -46.058  -18.120 1.00 46.23  ? 57  GLU D N   1 
ATOM   6744  C CA  . GLU D  2 57  ? -36.537 -45.416  -17.826 1.00 49.60  ? 57  GLU D CA  1 
ATOM   6745  C C   . GLU D  2 57  ? -35.359 -46.066  -18.549 1.00 47.27  ? 57  GLU D C   1 
ATOM   6746  O O   . GLU D  2 57  ? -34.365 -45.404  -18.849 1.00 58.56  ? 57  GLU D O   1 
ATOM   6747  C CB  . GLU D  2 57  ? -36.290 -45.399  -16.314 1.00 68.38  ? 57  GLU D CB  1 
ATOM   6748  C CG  . GLU D  2 57  ? -35.233 -44.405  -15.861 1.00 98.16  ? 57  GLU D CG  1 
ATOM   6749  C CD  . GLU D  2 57  ? -33.893 -45.055  -15.579 1.00 105.74 ? 57  GLU D CD  1 
ATOM   6750  O OE1 . GLU D  2 57  ? -33.872 -46.249  -15.212 1.00 95.47  ? 57  GLU D OE1 1 
ATOM   6751  O OE2 . GLU D  2 57  ? -32.859 -44.367  -15.715 1.00 93.60  ? 57  GLU D OE2 1 
ATOM   6752  N N   . LYS D  2 58  ? -35.476 -47.361  -18.830 1.00 45.54  ? 58  LYS D N   1 
ATOM   6753  C CA  . LYS D  2 58  ? -34.402 -48.111  -19.476 1.00 42.64  ? 58  LYS D CA  1 
ATOM   6754  C C   . LYS D  2 58  ? -34.285 -47.829  -20.973 1.00 49.97  ? 58  LYS D C   1 
ATOM   6755  O O   . LYS D  2 58  ? -33.426 -48.398  -21.651 1.00 45.48  ? 58  LYS D O   1 
ATOM   6756  C CB  . LYS D  2 58  ? -34.576 -49.613  -19.234 1.00 36.58  ? 58  LYS D CB  1 
ATOM   6757  C CG  . LYS D  2 58  ? -34.376 -50.035  -17.790 1.00 49.61  ? 58  LYS D CG  1 
ATOM   6758  C CD  . LYS D  2 58  ? -33.003 -49.629  -17.284 1.00 48.92  ? 58  LYS D CD  1 
ATOM   6759  C CE  . LYS D  2 58  ? -32.820 -50.026  -15.831 1.00 54.90  ? 58  LYS D CE  1 
ATOM   6760  N NZ  . LYS D  2 58  ? -31.484 -49.628  -15.312 1.00 52.92  ? 58  LYS D NZ  1 
ATOM   6761  N N   . MET D  2 59  ? -35.137 -46.946  -21.485 1.00 43.74  ? 59  MET D N   1 
ATOM   6762  C CA  . MET D  2 59  ? -35.098 -46.602  -22.901 1.00 44.21  ? 59  MET D CA  1 
ATOM   6763  C C   . MET D  2 59  ? -34.380 -45.277  -23.146 1.00 52.75  ? 59  MET D C   1 
ATOM   6764  O O   . MET D  2 59  ? -35.030 -44.249  -23.336 1.00 73.03  ? 59  MET D O   1 
ATOM   6765  C CB  . MET D  2 59  ? -36.516 -46.547  -23.480 1.00 61.42  ? 59  MET D CB  1 
ATOM   6766  C CG  . MET D  2 59  ? -36.566 -46.310  -24.976 1.00 53.49  ? 59  MET D CG  1 
ATOM   6767  S SD  . MET D  2 59  ? -35.621 -47.533  -25.908 1.00 59.07  ? 59  MET D SD  1 
ATOM   6768  C CE  . MET D  2 59  ? -36.940 -48.411  -26.749 1.00 45.60  ? 59  MET D CE  1 
ATOM   6769  N N   . ASN D  2 60  ? -33.048 -45.297  -23.134 1.00 59.14  ? 60  ASN D N   1 
ATOM   6770  C CA  . ASN D  2 60  ? -32.273 -44.113  -23.501 1.00 68.12  ? 60  ASN D CA  1 
ATOM   6771  C C   . ASN D  2 60  ? -31.758 -44.233  -24.931 1.00 56.41  ? 60  ASN D C   1 
ATOM   6772  O O   . ASN D  2 60  ? -30.779 -44.934  -25.197 1.00 63.26  ? 60  ASN D O   1 
ATOM   6773  C CB  . ASN D  2 60  ? -31.112 -43.879  -22.533 1.00 85.62  ? 60  ASN D CB  1 
ATOM   6774  C CG  . ASN D  2 60  ? -30.449 -42.525  -22.731 1.00 99.02  ? 60  ASN D CG  1 
ATOM   6775  O OD1 . ASN D  2 60  ? -31.120 -41.517  -22.956 1.00 101.36 ? 60  ASN D OD1 1 
ATOM   6776  N ND2 . ASN D  2 60  ? -29.126 -42.496  -22.638 1.00 94.02  ? 60  ASN D ND2 1 
ATOM   6777  N N   . THR D  2 61  ? -32.431 -43.542  -25.844 1.00 60.46  ? 61  THR D N   1 
ATOM   6778  C CA  . THR D  2 61  ? -32.133 -43.627  -27.265 1.00 61.48  ? 61  THR D CA  1 
ATOM   6779  C C   . THR D  2 61  ? -31.006 -42.684  -27.673 1.00 56.20  ? 61  THR D C   1 
ATOM   6780  O O   . THR D  2 61  ? -30.743 -41.681  -27.007 1.00 50.40  ? 61  THR D O   1 
ATOM   6781  C CB  . THR D  2 61  ? -33.383 -43.315  -28.107 1.00 61.70  ? 61  THR D CB  1 
ATOM   6782  O OG1 . THR D  2 61  ? -33.881 -42.014  -27.766 1.00 59.63  ? 61  THR D OG1 1 
ATOM   6783  C CG2 . THR D  2 61  ? -34.471 -44.345  -27.847 1.00 49.64  ? 61  THR D CG2 1 
ATOM   6784  N N   . GLN D  2 62  ? -30.341 -43.022  -28.771 1.00 59.06  ? 62  GLN D N   1 
ATOM   6785  C CA  . GLN D  2 62  ? -29.287 -42.183  -29.319 1.00 66.52  ? 62  GLN D CA  1 
ATOM   6786  C C   . GLN D  2 62  ? -29.904 -41.046  -30.115 1.00 57.44  ? 62  GLN D C   1 
ATOM   6787  O O   . GLN D  2 62  ? -31.038 -41.152  -30.580 1.00 56.50  ? 62  GLN D O   1 
ATOM   6788  C CB  . GLN D  2 62  ? -28.375 -43.007  -30.229 1.00 58.08  ? 62  GLN D CB  1 
ATOM   6789  C CG  . GLN D  2 62  ? -27.579 -44.079  -29.511 1.00 45.73  ? 62  GLN D CG  1 
ATOM   6790  C CD  . GLN D  2 62  ? -26.562 -43.497  -28.552 1.00 60.08  ? 62  GLN D CD  1 
ATOM   6791  O OE1 . GLN D  2 62  ? -26.902 -43.081  -27.445 1.00 73.59  ? 62  GLN D OE1 1 
ATOM   6792  N NE2 . GLN D  2 62  ? -25.304 -43.461  -28.975 1.00 56.58  ? 62  GLN D NE2 1 
ATOM   6793  N N   . PHE D  2 63  ? -29.162 -39.955  -30.269 1.00 55.48  ? 63  PHE D N   1 
ATOM   6794  C CA  . PHE D  2 63  ? -29.599 -38.883  -31.149 1.00 53.00  ? 63  PHE D CA  1 
ATOM   6795  C C   . PHE D  2 63  ? -29.294 -39.272  -32.587 1.00 44.65  ? 63  PHE D C   1 
ATOM   6796  O O   . PHE D  2 63  ? -28.140 -39.258  -33.015 1.00 64.46  ? 63  PHE D O   1 
ATOM   6797  C CB  . PHE D  2 63  ? -28.913 -37.562  -30.807 1.00 50.82  ? 63  PHE D CB  1 
ATOM   6798  C CG  . PHE D  2 63  ? -29.418 -36.396  -31.611 1.00 60.11  ? 63  PHE D CG  1 
ATOM   6799  C CD1 . PHE D  2 63  ? -30.312 -35.493  -31.060 1.00 47.14  ? 63  PHE D CD1 1 
ATOM   6800  C CD2 . PHE D  2 63  ? -29.009 -36.210  -32.922 1.00 50.48  ? 63  PHE D CD2 1 
ATOM   6801  C CE1 . PHE D  2 63  ? -30.781 -34.422  -31.797 1.00 48.77  ? 63  PHE D CE1 1 
ATOM   6802  C CE2 . PHE D  2 63  ? -29.476 -35.143  -33.664 1.00 55.44  ? 63  PHE D CE2 1 
ATOM   6803  C CZ  . PHE D  2 63  ? -30.363 -34.248  -33.101 1.00 52.14  ? 63  PHE D CZ  1 
ATOM   6804  N N   . THR D  2 64  ? -30.334 -39.629  -33.328 1.00 34.94  ? 64  THR D N   1 
ATOM   6805  C CA  . THR D  2 64  ? -30.168 -40.053  -34.707 1.00 56.32  ? 64  THR D CA  1 
ATOM   6806  C C   . THR D  2 64  ? -31.220 -39.429  -35.605 1.00 46.87  ? 64  THR D C   1 
ATOM   6807  O O   . THR D  2 64  ? -32.360 -39.212  -35.193 1.00 40.11  ? 64  THR D O   1 
ATOM   6808  C CB  . THR D  2 64  ? -30.246 -41.586  -34.845 1.00 58.73  ? 64  THR D CB  1 
ATOM   6809  O OG1 . THR D  2 64  ? -31.330 -42.085  -34.052 1.00 50.76  ? 64  THR D OG1 1 
ATOM   6810  C CG2 . THR D  2 64  ? -28.951 -42.230  -34.381 1.00 61.80  ? 64  THR D CG2 1 
ATOM   6811  N N   . ALA D  2 65  ? -30.823 -39.135  -36.836 1.00 42.17  ? 65  ALA D N   1 
ATOM   6812  C CA  . ALA D  2 65  ? -31.758 -38.672  -37.845 1.00 40.23  ? 65  ALA D CA  1 
ATOM   6813  C C   . ALA D  2 65  ? -31.993 -39.784  -38.855 1.00 43.13  ? 65  ALA D C   1 
ATOM   6814  O O   . ALA D  2 65  ? -31.356 -39.821  -39.908 1.00 43.20  ? 65  ALA D O   1 
ATOM   6815  C CB  . ALA D  2 65  ? -31.226 -37.431  -38.533 1.00 40.27  ? 65  ALA D CB  1 
ATOM   6816  N N   . VAL D  2 66  ? -32.891 -40.703  -38.521 1.00 37.16  ? 66  VAL D N   1 
ATOM   6817  C CA  . VAL D  2 66  ? -33.287 -41.738  -39.462 1.00 33.30  ? 66  VAL D CA  1 
ATOM   6818  C C   . VAL D  2 66  ? -33.831 -41.072  -40.715 1.00 46.77  ? 66  VAL D C   1 
ATOM   6819  O O   . VAL D  2 66  ? -34.320 -39.945  -40.660 1.00 59.77  ? 66  VAL D O   1 
ATOM   6820  C CB  . VAL D  2 66  ? -34.338 -42.691  -38.854 1.00 35.43  ? 66  VAL D CB  1 
ATOM   6821  C CG1 . VAL D  2 66  ? -35.154 -41.978  -37.791 1.00 39.99  ? 66  VAL D CG1 1 
ATOM   6822  C CG2 . VAL D  2 66  ? -35.232 -43.283  -39.939 1.00 35.23  ? 66  VAL D CG2 1 
ATOM   6823  N N   . GLY D  2 67  ? -33.733 -41.763  -41.844 1.00 38.38  ? 67  GLY D N   1 
ATOM   6824  C CA  . GLY D  2 67  ? -34.168 -41.201  -43.105 1.00 60.12  ? 67  GLY D CA  1 
ATOM   6825  C C   . GLY D  2 67  ? -33.002 -40.586  -43.850 1.00 47.11  ? 67  GLY D C   1 
ATOM   6826  O O   . GLY D  2 67  ? -32.341 -39.674  -43.352 1.00 34.20  ? 67  GLY D O   1 
ATOM   6827  N N   . LYS D  2 68  ? -32.746 -41.099  -45.047 1.00 44.94  ? 68  LYS D N   1 
ATOM   6828  C CA  . LYS D  2 68  ? -31.647 -40.621  -45.871 1.00 37.19  ? 68  LYS D CA  1 
ATOM   6829  C C   . LYS D  2 68  ? -32.158 -40.323  -47.274 1.00 43.30  ? 68  LYS D C   1 
ATOM   6830  O O   . LYS D  2 68  ? -33.270 -40.712  -47.633 1.00 38.72  ? 68  LYS D O   1 
ATOM   6831  C CB  . LYS D  2 68  ? -30.532 -41.667  -45.923 1.00 44.25  ? 68  LYS D CB  1 
ATOM   6832  C CG  . LYS D  2 68  ? -29.983 -42.054  -44.556 1.00 41.29  ? 68  LYS D CG  1 
ATOM   6833  C CD  . LYS D  2 68  ? -28.780 -41.205  -44.179 1.00 46.67  ? 68  LYS D CD  1 
ATOM   6834  C CE  . LYS D  2 68  ? -28.483 -41.284  -42.689 1.00 53.27  ? 68  LYS D CE  1 
ATOM   6835  N NZ  . LYS D  2 68  ? -29.257 -40.273  -41.916 1.00 57.07  ? 68  LYS D NZ  1 
ATOM   6836  N N   . GLU D  2 69  ? -31.349 -39.630  -48.064 1.00 46.74  ? 69  GLU D N   1 
ATOM   6837  C CA  . GLU D  2 69  ? -31.732 -39.292  -49.427 1.00 42.32  ? 69  GLU D CA  1 
ATOM   6838  C C   . GLU D  2 69  ? -30.781 -39.949  -50.415 1.00 37.36  ? 69  GLU D C   1 
ATOM   6839  O O   . GLU D  2 69  ? -29.568 -39.869  -50.257 1.00 43.96  ? 69  GLU D O   1 
ATOM   6840  C CB  . GLU D  2 69  ? -31.737 -37.776  -49.620 1.00 48.54  ? 69  GLU D CB  1 
ATOM   6841  C CG  . GLU D  2 69  ? -32.716 -37.047  -48.716 1.00 61.19  ? 69  GLU D CG  1 
ATOM   6842  C CD  . GLU D  2 69  ? -32.576 -35.542  -48.797 1.00 68.30  ? 69  GLU D CD  1 
ATOM   6843  O OE1 . GLU D  2 69  ? -31.469 -35.066  -49.125 1.00 66.98  ? 69  GLU D OE1 1 
ATOM   6844  O OE2 . GLU D  2 69  ? -33.570 -34.835  -48.527 1.00 57.30  ? 69  GLU D OE2 1 
ATOM   6845  N N   . PHE D  2 70  ? -31.339 -40.608  -51.424 1.00 38.92  ? 70  PHE D N   1 
ATOM   6846  C CA  . PHE D  2 70  ? -30.535 -41.258  -52.448 1.00 41.02  ? 70  PHE D CA  1 
ATOM   6847  C C   . PHE D  2 70  ? -31.080 -40.931  -53.831 1.00 43.08  ? 70  PHE D C   1 
ATOM   6848  O O   . PHE D  2 70  ? -32.293 -40.843  -54.026 1.00 44.00  ? 70  PHE D O   1 
ATOM   6849  C CB  . PHE D  2 70  ? -30.523 -42.774  -52.247 1.00 43.17  ? 70  PHE D CB  1 
ATOM   6850  C CG  . PHE D  2 70  ? -30.104 -43.205  -50.871 1.00 43.14  ? 70  PHE D CG  1 
ATOM   6851  C CD1 . PHE D  2 70  ? -28.765 -43.278  -50.528 1.00 34.13  ? 70  PHE D CD1 1 
ATOM   6852  C CD2 . PHE D  2 70  ? -31.053 -43.550  -49.924 1.00 40.79  ? 70  PHE D CD2 1 
ATOM   6853  C CE1 . PHE D  2 70  ? -28.381 -43.680  -49.261 1.00 36.96  ? 70  PHE D CE1 1 
ATOM   6854  C CE2 . PHE D  2 70  ? -30.675 -43.953  -48.657 1.00 33.42  ? 70  PHE D CE2 1 
ATOM   6855  C CZ  . PHE D  2 70  ? -29.338 -44.019  -48.326 1.00 31.03  ? 70  PHE D CZ  1 
ATOM   6856  N N   . ASN D  2 71  ? -30.178 -40.756  -54.790 1.00 37.35  ? 71  ASN D N   1 
ATOM   6857  C CA  . ASN D  2 71  ? -30.574 -40.466  -56.161 1.00 43.95  ? 71  ASN D CA  1 
ATOM   6858  C C   . ASN D  2 71  ? -30.964 -41.735  -56.908 1.00 46.13  ? 71  ASN D C   1 
ATOM   6859  O O   . ASN D  2 71  ? -30.822 -42.840  -56.387 1.00 41.71  ? 71  ASN D O   1 
ATOM   6860  C CB  . ASN D  2 71  ? -29.457 -39.729  -56.901 1.00 41.36  ? 71  ASN D CB  1 
ATOM   6861  C CG  . ASN D  2 71  ? -28.159 -40.512  -56.926 1.00 48.63  ? 71  ASN D CG  1 
ATOM   6862  O OD1 . ASN D  2 71  ? -28.144 -41.706  -57.226 1.00 56.05  ? 71  ASN D OD1 1 
ATOM   6863  N ND2 . ASN D  2 71  ? -27.059 -39.839  -56.614 1.00 58.84  ? 71  ASN D ND2 1 
ATOM   6864  N N   . HIS D  2 72  ? -31.446 -41.568  -58.135 1.00 45.53  ? 72  HIS D N   1 
ATOM   6865  C CA  . HIS D  2 72  ? -31.976 -42.681  -58.919 1.00 55.42  ? 72  HIS D CA  1 
ATOM   6866  C C   . HIS D  2 72  ? -30.965 -43.802  -59.157 1.00 53.08  ? 72  HIS D C   1 
ATOM   6867  O O   . HIS D  2 72  ? -31.348 -44.934  -59.451 1.00 53.54  ? 72  HIS D O   1 
ATOM   6868  C CB  . HIS D  2 72  ? -32.517 -42.172  -60.257 1.00 57.04  ? 72  HIS D CB  1 
ATOM   6869  C CG  . HIS D  2 72  ? -31.496 -41.465  -61.091 1.00 80.91  ? 72  HIS D CG  1 
ATOM   6870  N ND1 . HIS D  2 72  ? -31.171 -40.138  -60.903 1.00 88.75  ? 72  HIS D ND1 1 
ATOM   6871  C CD2 . HIS D  2 72  ? -30.727 -41.898  -62.118 1.00 80.03  ? 72  HIS D CD2 1 
ATOM   6872  C CE1 . HIS D  2 72  ? -30.246 -39.785  -61.777 1.00 91.14  ? 72  HIS D CE1 1 
ATOM   6873  N NE2 . HIS D  2 72  ? -29.959 -40.835  -62.526 1.00 74.10  ? 72  HIS D NE2 1 
ATOM   6874  N N   . LEU D  2 73  ? -29.680 -43.488  -59.034 1.00 41.58  ? 73  LEU D N   1 
ATOM   6875  C CA  . LEU D  2 73  ? -28.629 -44.476  -59.262 1.00 47.58  ? 73  LEU D CA  1 
ATOM   6876  C C   . LEU D  2 73  ? -28.080 -45.049  -57.957 1.00 47.84  ? 73  LEU D C   1 
ATOM   6877  O O   . LEU D  2 73  ? -26.997 -45.634  -57.931 1.00 45.95  ? 73  LEU D O   1 
ATOM   6878  C CB  . LEU D  2 73  ? -27.496 -43.873  -60.096 1.00 51.75  ? 73  LEU D CB  1 
ATOM   6879  C CG  . LEU D  2 73  ? -27.815 -43.609  -61.568 1.00 58.50  ? 73  LEU D CG  1 
ATOM   6880  C CD1 . LEU D  2 73  ? -26.669 -42.869  -62.242 1.00 56.16  ? 73  LEU D CD1 1 
ATOM   6881  C CD2 . LEU D  2 73  ? -28.119 -44.914  -62.290 1.00 46.15  ? 73  LEU D CD2 1 
ATOM   6882  N N   . GLU D  2 74  ? -28.835 -44.879  -56.878 1.00 39.07  ? 74  GLU D N   1 
ATOM   6883  C CA  . GLU D  2 74  ? -28.439 -45.398  -55.575 1.00 35.67  ? 74  GLU D CA  1 
ATOM   6884  C C   . GLU D  2 74  ? -29.576 -46.188  -54.936 1.00 46.50  ? 74  GLU D C   1 
ATOM   6885  O O   . GLU D  2 74  ? -29.751 -46.169  -53.719 1.00 40.70  ? 74  GLU D O   1 
ATOM   6886  C CB  . GLU D  2 74  ? -28.009 -44.254  -54.655 1.00 36.02  ? 74  GLU D CB  1 
ATOM   6887  C CG  . GLU D  2 74  ? -26.756 -43.533  -55.116 1.00 35.77  ? 74  GLU D CG  1 
ATOM   6888  C CD  . GLU D  2 74  ? -26.422 -42.336  -54.253 1.00 55.06  ? 74  GLU D CD  1 
ATOM   6889  O OE1 . GLU D  2 74  ? -27.322 -41.503  -54.012 1.00 46.88  ? 74  GLU D OE1 1 
ATOM   6890  O OE2 . GLU D  2 74  ? -25.255 -42.225  -53.822 1.00 49.29  ? 74  GLU D OE2 1 
ATOM   6891  N N   . LYS D  2 75  ? -30.345 -46.886  -55.766 1.00 39.80  ? 75  LYS D N   1 
ATOM   6892  C CA  . LYS D  2 75  ? -31.510 -47.631  -55.299 1.00 44.27  ? 75  LYS D CA  1 
ATOM   6893  C C   . LYS D  2 75  ? -31.123 -48.761  -54.347 1.00 40.92  ? 75  LYS D C   1 
ATOM   6894  O O   . LYS D  2 75  ? -31.909 -49.153  -53.483 1.00 38.23  ? 75  LYS D O   1 
ATOM   6895  C CB  . LYS D  2 75  ? -32.293 -48.189  -56.492 1.00 41.94  ? 75  LYS D CB  1 
ATOM   6896  C CG  . LYS D  2 75  ? -33.459 -49.086  -56.109 1.00 59.49  ? 75  LYS D CG  1 
ATOM   6897  C CD  . LYS D  2 75  ? -34.479 -48.352  -55.248 1.00 62.73  ? 75  LYS D CD  1 
ATOM   6898  C CE  . LYS D  2 75  ? -35.342 -47.410  -56.076 1.00 73.84  ? 75  LYS D CE  1 
ATOM   6899  N NZ  . LYS D  2 75  ? -36.379 -46.736  -55.243 1.00 87.09  ? 75  LYS D NZ  1 
ATOM   6900  N N   . ARG D  2 76  ? -29.908 -49.278  -54.508 1.00 42.01  ? 76  ARG D N   1 
ATOM   6901  C CA  . ARG D  2 76  ? -29.434 -50.397  -53.697 1.00 41.58  ? 76  ARG D CA  1 
ATOM   6902  C C   . ARG D  2 76  ? -29.147 -50.001  -52.247 1.00 41.38  ? 76  ARG D C   1 
ATOM   6903  O O   . ARG D  2 76  ? -29.567 -50.692  -51.321 1.00 42.16  ? 76  ARG D O   1 
ATOM   6904  C CB  . ARG D  2 76  ? -28.208 -51.054  -54.338 1.00 35.11  ? 76  ARG D CB  1 
ATOM   6905  C CG  . ARG D  2 76  ? -28.531 -51.883  -55.575 1.00 36.32  ? 76  ARG D CG  1 
ATOM   6906  C CD  . ARG D  2 76  ? -27.277 -52.426  -56.238 1.00 33.52  ? 76  ARG D CD  1 
ATOM   6907  N NE  . ARG D  2 76  ? -26.357 -51.360  -56.620 1.00 36.65  ? 76  ARG D NE  1 
ATOM   6908  C CZ  . ARG D  2 76  ? -25.047 -51.399  -56.407 1.00 34.74  ? 76  ARG D CZ  1 
ATOM   6909  N NH1 . ARG D  2 76  ? -24.499 -52.449  -55.819 1.00 44.04  ? 76  ARG D NH1 1 
ATOM   6910  N NH2 . ARG D  2 76  ? -24.278 -50.388  -56.775 1.00 40.52  ? 76  ARG D NH2 1 
ATOM   6911  N N   . ILE D  2 77  ? -28.441 -48.891  -52.049 1.00 39.31  ? 77  ILE D N   1 
ATOM   6912  C CA  . ILE D  2 77  ? -28.209 -48.387  -50.698 1.00 37.77  ? 77  ILE D CA  1 
ATOM   6913  C C   . ILE D  2 77  ? -29.506 -47.855  -50.097 1.00 30.39  ? 77  ILE D C   1 
ATOM   6914  O O   . ILE D  2 77  ? -29.697 -47.890  -48.883 1.00 37.44  ? 77  ILE D O   1 
ATOM   6915  C CB  . ILE D  2 77  ? -27.108 -47.299  -50.649 1.00 30.03  ? 77  ILE D CB  1 
ATOM   6916  C CG1 . ILE D  2 77  ? -27.214 -46.353  -51.847 1.00 53.67  ? 77  ILE D CG1 1 
ATOM   6917  C CG2 . ILE D  2 77  ? -25.730 -47.937  -50.623 1.00 39.40  ? 77  ILE D CG2 1 
ATOM   6918  C CD1 . ILE D  2 77  ? -26.123 -45.297  -51.888 1.00 57.33  ? 77  ILE D CD1 1 
ATOM   6919  N N   . GLU D  2 78  ? -30.396 -47.366  -50.955 1.00 32.34  ? 78  GLU D N   1 
ATOM   6920  C CA  . GLU D  2 78  ? -31.714 -46.935  -50.514 1.00 33.18  ? 78  GLU D CA  1 
ATOM   6921  C C   . GLU D  2 78  ? -32.471 -48.123  -49.931 1.00 37.37  ? 78  GLU D C   1 
ATOM   6922  O O   . GLU D  2 78  ? -33.151 -47.999  -48.914 1.00 38.23  ? 78  GLU D O   1 
ATOM   6923  C CB  . GLU D  2 78  ? -32.502 -46.324  -51.674 1.00 35.55  ? 78  GLU D CB  1 
ATOM   6924  C CG  . GLU D  2 78  ? -33.883 -45.830  -51.279 1.00 43.43  ? 78  GLU D CG  1 
ATOM   6925  C CD  . GLU D  2 78  ? -34.691 -45.329  -52.461 1.00 72.52  ? 78  GLU D CD  1 
ATOM   6926  O OE1 . GLU D  2 78  ? -34.085 -44.872  -53.453 1.00 81.84  ? 78  GLU D OE1 1 
ATOM   6927  O OE2 . GLU D  2 78  ? -35.937 -45.391  -52.393 1.00 84.74  ? 78  GLU D OE2 1 
ATOM   6928  N N   . ASN D  2 79  ? -32.342 -49.276  -50.581 1.00 39.04  ? 79  ASN D N   1 
ATOM   6929  C CA  . ASN D  2 79  ? -32.986 -50.497  -50.110 1.00 37.38  ? 79  ASN D CA  1 
ATOM   6930  C C   . ASN D  2 79  ? -32.280 -51.096  -48.898 1.00 40.97  ? 79  ASN D C   1 
ATOM   6931  O O   . ASN D  2 79  ? -32.920 -51.676  -48.022 1.00 47.12  ? 79  ASN D O   1 
ATOM   6932  C CB  . ASN D  2 79  ? -33.093 -51.525  -51.238 1.00 35.41  ? 79  ASN D CB  1 
ATOM   6933  C CG  . ASN D  2 79  ? -34.203 -51.199  -52.217 1.00 55.56  ? 79  ASN D CG  1 
ATOM   6934  O OD1 . ASN D  2 79  ? -35.210 -50.592  -51.851 1.00 57.17  ? 79  ASN D OD1 1 
ATOM   6935  N ND2 . ASN D  2 79  ? -34.028 -51.606  -53.469 1.00 57.72  ? 79  ASN D ND2 1 
ATOM   6936  N N   . LEU D  2 80  ? -30.959 -50.956  -48.853 1.00 38.03  ? 80  LEU D N   1 
ATOM   6937  C CA  . LEU D  2 80  ? -30.200 -51.367  -47.680 1.00 34.33  ? 80  LEU D CA  1 
ATOM   6938  C C   . LEU D  2 80  ? -30.726 -50.575  -46.490 1.00 37.78  ? 80  LEU D C   1 
ATOM   6939  O O   . LEU D  2 80  ? -31.050 -51.138  -45.443 1.00 32.59  ? 80  LEU D O   1 
ATOM   6940  C CB  . LEU D  2 80  ? -28.711 -51.081  -47.879 1.00 31.35  ? 80  LEU D CB  1 
ATOM   6941  C CG  . LEU D  2 80  ? -27.691 -51.918  -47.098 1.00 37.34  ? 80  LEU D CG  1 
ATOM   6942  C CD1 . LEU D  2 80  ? -26.382 -51.156  -46.961 1.00 27.89  ? 80  LEU D CD1 1 
ATOM   6943  C CD2 . LEU D  2 80  ? -28.215 -52.324  -45.730 1.00 35.32  ? 80  LEU D CD2 1 
ATOM   6944  N N   . ASN D  2 81  ? -30.812 -49.261  -46.670 1.00 35.06  ? 81  ASN D N   1 
ATOM   6945  C CA  . ASN D  2 81  ? -31.350 -48.367  -45.652 1.00 29.11  ? 81  ASN D CA  1 
ATOM   6946  C C   . ASN D  2 81  ? -32.772 -48.746  -45.251 1.00 38.94  ? 81  ASN D C   1 
ATOM   6947  O O   . ASN D  2 81  ? -33.111 -48.752  -44.069 1.00 35.04  ? 81  ASN D O   1 
ATOM   6948  C CB  . ASN D  2 81  ? -31.314 -46.920  -46.146 1.00 29.90  ? 81  ASN D CB  1 
ATOM   6949  C CG  . ASN D  2 81  ? -31.917 -45.950  -45.149 1.00 40.46  ? 81  ASN D CG  1 
ATOM   6950  O OD1 . ASN D  2 81  ? -31.405 -45.780  -44.044 1.00 47.08  ? 81  ASN D OD1 1 
ATOM   6951  N ND2 . ASN D  2 81  ? -33.012 -45.307  -45.538 1.00 39.08  ? 81  ASN D ND2 1 
ATOM   6952  N N   . LYS D  2 82  ? -33.604 -49.053  -46.240 1.00 34.42  ? 82  LYS D N   1 
ATOM   6953  C CA  . LYS D  2 82  ? -34.971 -49.478  -45.969 1.00 37.42  ? 82  LYS D CA  1 
ATOM   6954  C C   . LYS D  2 82  ? -34.983 -50.775  -45.168 1.00 41.49  ? 82  LYS D C   1 
ATOM   6955  O O   . LYS D  2 82  ? -35.843 -50.978  -44.310 1.00 38.69  ? 82  LYS D O   1 
ATOM   6956  C CB  . LYS D  2 82  ? -35.757 -49.656  -47.270 1.00 32.61  ? 82  LYS D CB  1 
ATOM   6957  C CG  . LYS D  2 82  ? -37.102 -50.334  -47.075 1.00 48.92  ? 82  LYS D CG  1 
ATOM   6958  C CD  . LYS D  2 82  ? -37.859 -50.478  -48.382 1.00 52.61  ? 82  LYS D CD  1 
ATOM   6959  C CE  . LYS D  2 82  ? -39.087 -51.358  -48.202 1.00 84.98  ? 82  LYS D CE  1 
ATOM   6960  N NZ  . LYS D  2 82  ? -39.976 -50.865  -47.112 1.00 75.17  ? 82  LYS D NZ  1 
ATOM   6961  N N   . LYS D  2 83  ? -34.024 -51.651  -45.450 1.00 40.53  ? 83  LYS D N   1 
ATOM   6962  C CA  . LYS D  2 83  ? -33.937 -52.925  -44.747 1.00 38.17  ? 83  LYS D CA  1 
ATOM   6963  C C   . LYS D  2 83  ? -33.619 -52.731  -43.268 1.00 38.48  ? 83  LYS D C   1 
ATOM   6964  O O   . LYS D  2 83  ? -34.223 -53.374  -42.410 1.00 34.18  ? 83  LYS D O   1 
ATOM   6965  C CB  . LYS D  2 83  ? -32.900 -53.848  -45.392 1.00 31.84  ? 83  LYS D CB  1 
ATOM   6966  C CG  . LYS D  2 83  ? -32.751 -55.177  -44.664 1.00 35.60  ? 83  LYS D CG  1 
ATOM   6967  C CD  . LYS D  2 83  ? -31.981 -56.206  -45.476 1.00 28.76  ? 83  LYS D CD  1 
ATOM   6968  C CE  . LYS D  2 83  ? -30.492 -55.909  -45.507 1.00 37.33  ? 83  LYS D CE  1 
ATOM   6969  N NZ  . LYS D  2 83  ? -29.727 -57.067  -46.049 1.00 40.90  ? 83  LYS D NZ  1 
ATOM   6970  N N   . VAL D  2 84  ? -32.673 -51.846  -42.971 1.00 33.39  ? 84  VAL D N   1 
ATOM   6971  C CA  . VAL D  2 84  ? -32.285 -51.601  -41.586 1.00 34.30  ? 84  VAL D CA  1 
ATOM   6972  C C   . VAL D  2 84  ? -33.416 -50.925  -40.814 1.00 33.52  ? 84  VAL D C   1 
ATOM   6973  O O   . VAL D  2 84  ? -33.544 -51.100  -39.602 1.00 38.29  ? 84  VAL D O   1 
ATOM   6974  C CB  . VAL D  2 84  ? -30.987 -50.770  -41.481 1.00 26.45  ? 84  VAL D CB  1 
ATOM   6975  C CG1 . VAL D  2 84  ? -31.217 -49.346  -41.952 1.00 42.19  ? 84  VAL D CG1 1 
ATOM   6976  C CG2 . VAL D  2 84  ? -30.470 -50.779  -40.053 1.00 44.08  ? 84  VAL D CG2 1 
ATOM   6977  N N   . ASP D  2 85  ? -34.239 -50.160  -41.524 1.00 30.43  ? 85  ASP D N   1 
ATOM   6978  C CA  . ASP D  2 85  ? -35.406 -49.527  -40.919 1.00 26.98  ? 85  ASP D CA  1 
ATOM   6979  C C   . ASP D  2 85  ? -36.509 -50.546  -40.655 1.00 36.00  ? 85  ASP D C   1 
ATOM   6980  O O   . ASP D  2 85  ? -37.137 -50.533  -39.596 1.00 38.77  ? 85  ASP D O   1 
ATOM   6981  C CB  . ASP D  2 85  ? -35.937 -48.402  -41.810 1.00 27.96  ? 85  ASP D CB  1 
ATOM   6982  C CG  . ASP D  2 85  ? -35.122 -47.130  -41.693 1.00 46.68  ? 85  ASP D CG  1 
ATOM   6983  O OD1 . ASP D  2 85  ? -34.312 -47.026  -40.749 1.00 46.96  ? 85  ASP D OD1 1 
ATOM   6984  O OD2 . ASP D  2 85  ? -35.298 -46.232  -42.543 1.00 60.26  ? 85  ASP D OD2 1 
ATOM   6985  N N   . ASP D  2 86  ? -36.743 -51.426  -41.623 1.00 34.93  ? 86  ASP D N   1 
ATOM   6986  C CA  . ASP D  2 86  ? -37.767 -52.457  -41.489 1.00 27.98  ? 86  ASP D CA  1 
ATOM   6987  C C   . ASP D  2 86  ? -37.354 -53.523  -40.481 1.00 38.42  ? 86  ASP D C   1 
ATOM   6988  O O   . ASP D  2 86  ? -38.201 -54.190  -39.887 1.00 39.13  ? 86  ASP D O   1 
ATOM   6989  C CB  . ASP D  2 86  ? -38.067 -53.101  -42.844 1.00 44.06  ? 86  ASP D CB  1 
ATOM   6990  C CG  . ASP D  2 86  ? -38.885 -52.200  -43.748 1.00 68.56  ? 86  ASP D CG  1 
ATOM   6991  O OD1 . ASP D  2 86  ? -39.455 -51.210  -43.244 1.00 74.53  ? 86  ASP D OD1 1 
ATOM   6992  O OD2 . ASP D  2 86  ? -38.963 -52.486  -44.962 1.00 74.89  ? 86  ASP D OD2 1 
ATOM   6993  N N   . GLY D  2 87  ? -36.048 -53.677  -40.294 1.00 45.61  ? 87  GLY D N   1 
ATOM   6994  C CA  . GLY D  2 87  ? -35.524 -54.626  -39.330 1.00 36.56  ? 87  GLY D CA  1 
ATOM   6995  C C   . GLY D  2 87  ? -35.773 -54.163  -37.909 1.00 35.71  ? 87  GLY D C   1 
ATOM   6996  O O   . GLY D  2 87  ? -36.335 -54.898  -37.097 1.00 40.57  ? 87  GLY D O   1 
ATOM   6997  N N   . PHE D  2 88  ? -35.353 -52.939  -37.608 1.00 30.64  ? 88  PHE D N   1 
ATOM   6998  C CA  . PHE D  2 88  ? -35.580 -52.355  -36.292 1.00 31.26  ? 88  PHE D CA  1 
ATOM   6999  C C   . PHE D  2 88  ? -37.071 -52.272  -35.993 1.00 36.60  ? 88  PHE D C   1 
ATOM   7000  O O   . PHE D  2 88  ? -37.495 -52.430  -34.849 1.00 43.47  ? 88  PHE D O   1 
ATOM   7001  C CB  . PHE D  2 88  ? -34.951 -50.963  -36.199 1.00 32.46  ? 88  PHE D CB  1 
ATOM   7002  C CG  . PHE D  2 88  ? -33.451 -50.971  -36.243 1.00 40.36  ? 88  PHE D CG  1 
ATOM   7003  C CD1 . PHE D  2 88  ? -32.752 -49.854  -36.671 1.00 30.10  ? 88  PHE D CD1 1 
ATOM   7004  C CD2 . PHE D  2 88  ? -32.739 -52.095  -35.860 1.00 37.02  ? 88  PHE D CD2 1 
ATOM   7005  C CE1 . PHE D  2 88  ? -31.371 -49.858  -36.711 1.00 27.91  ? 88  PHE D CE1 1 
ATOM   7006  C CE2 . PHE D  2 88  ? -31.359 -52.105  -35.899 1.00 36.73  ? 88  PHE D CE2 1 
ATOM   7007  C CZ  . PHE D  2 88  ? -30.674 -50.985  -36.325 1.00 36.25  ? 88  PHE D CZ  1 
ATOM   7008  N N   . LEU D  2 89  ? -37.860 -52.020  -37.032 1.00 36.33  ? 89  LEU D N   1 
ATOM   7009  C CA  . LEU D  2 89  ? -39.308 -51.938  -36.890 1.00 31.44  ? 89  LEU D CA  1 
ATOM   7010  C C   . LEU D  2 89  ? -39.890 -53.270  -36.427 1.00 38.57  ? 89  LEU D C   1 
ATOM   7011  O O   . LEU D  2 89  ? -40.736 -53.309  -35.535 1.00 39.20  ? 89  LEU D O   1 
ATOM   7012  C CB  . LEU D  2 89  ? -39.953 -51.510  -38.210 1.00 32.31  ? 89  LEU D CB  1 
ATOM   7013  C CG  . LEU D  2 89  ? -41.482 -51.498  -38.236 1.00 40.22  ? 89  LEU D CG  1 
ATOM   7014  C CD1 . LEU D  2 89  ? -42.035 -50.711  -37.058 1.00 38.35  ? 89  LEU D CD1 1 
ATOM   7015  C CD2 . LEU D  2 89  ? -42.001 -50.939  -39.553 1.00 33.03  ? 89  LEU D CD2 1 
ATOM   7016  N N   . ASP D  2 90  ? -39.429 -54.357  -37.037 1.00 31.72  ? 90  ASP D N   1 
ATOM   7017  C CA  . ASP D  2 90  ? -39.922 -55.690  -36.704 1.00 30.62  ? 90  ASP D CA  1 
ATOM   7018  C C   . ASP D  2 90  ? -39.471 -56.148  -35.319 1.00 32.82  ? 90  ASP D C   1 
ATOM   7019  O O   . ASP D  2 90  ? -40.239 -56.766  -34.583 1.00 37.84  ? 90  ASP D O   1 
ATOM   7020  C CB  . ASP D  2 90  ? -39.495 -56.706  -37.767 1.00 35.63  ? 90  ASP D CB  1 
ATOM   7021  C CG  . ASP D  2 90  ? -40.314 -56.596  -39.039 1.00 58.14  ? 90  ASP D CG  1 
ATOM   7022  O OD1 . ASP D  2 90  ? -41.432 -56.043  -38.979 1.00 67.49  ? 90  ASP D OD1 1 
ATOM   7023  O OD2 . ASP D  2 90  ? -39.845 -57.068  -40.096 1.00 65.90  ? 90  ASP D OD2 1 
ATOM   7024  N N   . ILE D  2 91  ? -38.225 -55.845  -34.970 1.00 32.29  ? 91  ILE D N   1 
ATOM   7025  C CA  . ILE D  2 91  ? -37.691 -56.207  -33.662 1.00 37.59  ? 91  ILE D CA  1 
ATOM   7026  C C   . ILE D  2 91  ? -38.441 -55.493  -32.543 1.00 42.33  ? 91  ILE D C   1 
ATOM   7027  O O   . ILE D  2 91  ? -38.932 -56.126  -31.608 1.00 39.93  ? 91  ILE D O   1 
ATOM   7028  C CB  . ILE D  2 91  ? -36.194 -55.866  -33.545 1.00 36.53  ? 91  ILE D CB  1 
ATOM   7029  C CG1 . ILE D  2 91  ? -35.373 -56.697  -34.533 1.00 32.53  ? 91  ILE D CG1 1 
ATOM   7030  C CG2 . ILE D  2 91  ? -35.705 -56.089  -32.120 1.00 41.01  ? 91  ILE D CG2 1 
ATOM   7031  C CD1 . ILE D  2 91  ? -33.898 -56.370  -34.520 1.00 46.20  ? 91  ILE D CD1 1 
ATOM   7032  N N   . TRP D  2 92  ? -38.528 -54.171  -32.648 1.00 33.96  ? 92  TRP D N   1 
ATOM   7033  C CA  . TRP D  2 92  ? -39.153 -53.358  -31.611 1.00 22.99  ? 92  TRP D CA  1 
ATOM   7034  C C   . TRP D  2 92  ? -40.645 -53.627  -31.451 1.00 31.20  ? 92  TRP D C   1 
ATOM   7035  O O   . TRP D  2 92  ? -41.158 -53.655  -30.333 1.00 44.48  ? 92  TRP D O   1 
ATOM   7036  C CB  . TRP D  2 92  ? -38.901 -51.872  -31.866 1.00 29.82  ? 92  TRP D CB  1 
ATOM   7037  C CG  . TRP D  2 92  ? -37.525 -51.453  -31.476 1.00 36.99  ? 92  TRP D CG  1 
ATOM   7038  C CD1 . TRP D  2 92  ? -36.531 -51.017  -32.302 1.00 32.96  ? 92  TRP D CD1 1 
ATOM   7039  C CD2 . TRP D  2 92  ? -36.979 -51.452  -30.153 1.00 32.21  ? 92  TRP D CD2 1 
ATOM   7040  N NE1 . TRP D  2 92  ? -35.401 -50.733  -31.572 1.00 36.34  ? 92  TRP D NE1 1 
ATOM   7041  C CE2 . TRP D  2 92  ? -35.651 -50.994  -30.250 1.00 36.53  ? 92  TRP D CE2 1 
ATOM   7042  C CE3 . TRP D  2 92  ? -37.486 -51.791  -28.895 1.00 32.63  ? 92  TRP D CE3 1 
ATOM   7043  C CZ2 . TRP D  2 92  ? -34.824 -50.865  -29.137 1.00 33.92  ? 92  TRP D CZ2 1 
ATOM   7044  C CZ3 . TRP D  2 92  ? -36.664 -51.664  -27.792 1.00 42.59  ? 92  TRP D CZ3 1 
ATOM   7045  C CH2 . TRP D  2 92  ? -35.348 -51.204  -27.920 1.00 40.17  ? 92  TRP D CH2 1 
ATOM   7046  N N   . THR D  2 93  ? -41.339 -53.822  -32.567 1.00 36.97  ? 93  THR D N   1 
ATOM   7047  C CA  . THR D  2 93  ? -42.759 -54.140  -32.521 1.00 32.01  ? 93  THR D CA  1 
ATOM   7048  C C   . THR D  2 93  ? -42.984 -55.457  -31.788 1.00 33.60  ? 93  THR D C   1 
ATOM   7049  O O   . THR D  2 93  ? -43.776 -55.528  -30.848 1.00 36.86  ? 93  THR D O   1 
ATOM   7050  C CB  . THR D  2 93  ? -43.371 -54.232  -33.930 1.00 35.51  ? 93  THR D CB  1 
ATOM   7051  O OG1 . THR D  2 93  ? -43.313 -52.948  -34.564 1.00 34.79  ? 93  THR D OG1 1 
ATOM   7052  C CG2 . THR D  2 93  ? -44.821 -54.684  -33.849 1.00 37.21  ? 93  THR D CG2 1 
ATOM   7053  N N   . TYR D  2 94  ? -42.273 -56.495  -32.217 1.00 39.49  ? 94  TYR D N   1 
ATOM   7054  C CA  . TYR D  2 94  ? -42.413 -57.819  -31.620 1.00 36.41  ? 94  TYR D CA  1 
ATOM   7055  C C   . TYR D  2 94  ? -42.057 -57.811  -30.137 1.00 35.00  ? 94  TYR D C   1 
ATOM   7056  O O   . TYR D  2 94  ? -42.811 -58.324  -29.310 1.00 37.02  ? 94  TYR D O   1 
ATOM   7057  C CB  . TYR D  2 94  ? -41.549 -58.840  -32.365 1.00 28.97  ? 94  TYR D CB  1 
ATOM   7058  C CG  . TYR D  2 94  ? -41.792 -60.271  -31.940 1.00 36.61  ? 94  TYR D CG  1 
ATOM   7059  C CD1 . TYR D  2 94  ? -42.927 -60.954  -32.357 1.00 37.46  ? 94  TYR D CD1 1 
ATOM   7060  C CD2 . TYR D  2 94  ? -40.887 -60.941  -31.126 1.00 42.37  ? 94  TYR D CD2 1 
ATOM   7061  C CE1 . TYR D  2 94  ? -43.157 -62.261  -31.974 1.00 43.73  ? 94  TYR D CE1 1 
ATOM   7062  C CE2 . TYR D  2 94  ? -41.108 -62.251  -30.739 1.00 36.86  ? 94  TYR D CE2 1 
ATOM   7063  C CZ  . TYR D  2 94  ? -42.245 -62.905  -31.166 1.00 49.95  ? 94  TYR D CZ  1 
ATOM   7064  O OH  . TYR D  2 94  ? -42.473 -64.207  -30.785 1.00 51.45  ? 94  TYR D OH  1 
ATOM   7065  N N   . ASN D  2 95  ? -40.910 -57.228  -29.804 1.00 31.09  ? 95  ASN D N   1 
ATOM   7066  C CA  . ASN D  2 95  ? -40.460 -57.175  -28.416 1.00 38.90  ? 95  ASN D CA  1 
ATOM   7067  C C   . ASN D  2 95  ? -41.406 -56.387  -27.514 1.00 38.95  ? 95  ASN D C   1 
ATOM   7068  O O   . ASN D  2 95  ? -41.718 -56.817  -26.405 1.00 44.09  ? 95  ASN D O   1 
ATOM   7069  C CB  . ASN D  2 95  ? -39.040 -56.609  -28.324 1.00 41.54  ? 95  ASN D CB  1 
ATOM   7070  C CG  . ASN D  2 95  ? -37.991 -57.580  -28.831 1.00 49.84  ? 95  ASN D CG  1 
ATOM   7071  O OD1 . ASN D  2 95  ? -38.308 -58.554  -29.512 1.00 48.49  ? 95  ASN D OD1 1 
ATOM   7072  N ND2 . ASN D  2 95  ? -36.732 -57.317  -28.499 1.00 54.45  ? 95  ASN D ND2 1 
ATOM   7073  N N   . ALA D  2 96  ? -41.861 -55.235  -27.996 1.00 32.51  ? 96  ALA D N   1 
ATOM   7074  C CA  . ALA D  2 96  ? -42.774 -54.395  -27.229 1.00 37.64  ? 96  ALA D CA  1 
ATOM   7075  C C   . ALA D  2 96  ? -44.107 -55.098  -26.979 1.00 42.59  ? 96  ALA D C   1 
ATOM   7076  O O   . ALA D  2 96  ? -44.651 -55.041  -25.876 1.00 43.86  ? 96  ALA D O   1 
ATOM   7077  C CB  . ALA D  2 96  ? -42.995 -53.067  -27.936 1.00 36.11  ? 96  ALA D CB  1 
ATOM   7078  N N   . GLU D  2 97  ? -44.627 -55.757  -28.010 1.00 36.03  ? 97  GLU D N   1 
ATOM   7079  C CA  . GLU D  2 97  ? -45.882 -56.494  -27.898 1.00 40.89  ? 97  GLU D CA  1 
ATOM   7080  C C   . GLU D  2 97  ? -45.765 -57.628  -26.882 1.00 41.20  ? 97  GLU D C   1 
ATOM   7081  O O   . GLU D  2 97  ? -46.624 -57.788  -26.014 1.00 38.87  ? 97  GLU D O   1 
ATOM   7082  C CB  . GLU D  2 97  ? -46.298 -57.053  -29.262 1.00 44.01  ? 97  GLU D CB  1 
ATOM   7083  C CG  . GLU D  2 97  ? -46.699 -55.998  -30.289 1.00 39.53  ? 97  GLU D CG  1 
ATOM   7084  C CD  . GLU D  2 97  ? -48.085 -55.430  -30.044 1.00 56.52  ? 97  GLU D CD  1 
ATOM   7085  O OE1 . GLU D  2 97  ? -48.648 -54.810  -30.971 1.00 59.25  ? 97  GLU D OE1 1 
ATOM   7086  O OE2 . GLU D  2 97  ? -48.618 -55.609  -28.928 1.00 70.97  ? 97  GLU D OE2 1 
ATOM   7087  N N   . LEU D  2 98  ? -44.697 -58.411  -26.997 1.00 35.12  ? 98  LEU D N   1 
ATOM   7088  C CA  . LEU D  2 98  ? -44.455 -59.527  -26.087 1.00 36.95  ? 98  LEU D CA  1 
ATOM   7089  C C   . LEU D  2 98  ? -44.164 -59.056  -24.665 1.00 43.78  ? 98  LEU D C   1 
ATOM   7090  O O   . LEU D  2 98  ? -44.596 -59.682  -23.698 1.00 40.37  ? 98  LEU D O   1 
ATOM   7091  C CB  . LEU D  2 98  ? -43.299 -60.393  -26.594 1.00 32.37  ? 98  LEU D CB  1 
ATOM   7092  C CG  . LEU D  2 98  ? -43.647 -61.608  -27.458 1.00 36.61  ? 98  LEU D CG  1 
ATOM   7093  C CD1 . LEU D  2 98  ? -44.116 -62.776  -26.600 1.00 60.43  ? 98  LEU D CD1 1 
ATOM   7094  C CD2 . LEU D  2 98  ? -44.679 -61.257  -28.521 1.00 44.38  ? 98  LEU D CD2 1 
ATOM   7095  N N   . LEU D  2 99  ? -43.429 -57.955  -24.542 1.00 43.30  ? 99  LEU D N   1 
ATOM   7096  C CA  . LEU D  2 99  ? -43.085 -57.410  -23.232 1.00 48.53  ? 99  LEU D CA  1 
ATOM   7097  C C   . LEU D  2 99  ? -44.336 -57.076  -22.428 1.00 45.40  ? 99  LEU D C   1 
ATOM   7098  O O   . LEU D  2 99  ? -44.441 -57.421  -21.251 1.00 50.01  ? 99  LEU D O   1 
ATOM   7099  C CB  . LEU D  2 99  ? -42.214 -56.160  -23.370 1.00 45.48  ? 99  LEU D CB  1 
ATOM   7100  C CG  . LEU D  2 99  ? -41.789 -55.517  -22.047 1.00 44.53  ? 99  LEU D CG  1 
ATOM   7101  C CD1 . LEU D  2 99  ? -40.924 -56.476  -21.241 1.00 38.90  ? 99  LEU D CD1 1 
ATOM   7102  C CD2 . LEU D  2 99  ? -41.060 -54.201  -22.280 1.00 44.04  ? 99  LEU D CD2 1 
ATOM   7103  N N   . VAL D  2 100 ? -45.278 -56.397  -23.072 1.00 36.70  ? 100 VAL D N   1 
ATOM   7104  C CA  . VAL D  2 100 ? -46.530 -56.026  -22.426 1.00 42.79  ? 100 VAL D CA  1 
ATOM   7105  C C   . VAL D  2 100 ? -47.328 -57.260  -22.014 1.00 40.12  ? 100 VAL D C   1 
ATOM   7106  O O   . VAL D  2 100 ? -47.792 -57.353  -20.879 1.00 47.86  ? 100 VAL D O   1 
ATOM   7107  C CB  . VAL D  2 100 ? -47.390 -55.131  -23.338 1.00 33.28  ? 100 VAL D CB  1 
ATOM   7108  C CG1 . VAL D  2 100 ? -48.788 -54.980  -22.766 1.00 42.89  ? 100 VAL D CG1 1 
ATOM   7109  C CG2 . VAL D  2 100 ? -46.731 -53.772  -23.520 1.00 36.43  ? 100 VAL D CG2 1 
ATOM   7110  N N   . LEU D  2 101 ? -47.483 -58.205  -22.937 1.00 40.60  ? 101 LEU D N   1 
ATOM   7111  C CA  . LEU D  2 101 ? -48.200 -59.442  -22.648 1.00 41.83  ? 101 LEU D CA  1 
ATOM   7112  C C   . LEU D  2 101 ? -47.580 -60.157  -21.453 1.00 46.41  ? 101 LEU D C   1 
ATOM   7113  O O   . LEU D  2 101 ? -48.270 -60.506  -20.496 1.00 47.39  ? 101 LEU D O   1 
ATOM   7114  C CB  . LEU D  2 101 ? -48.191 -60.371  -23.864 1.00 36.66  ? 101 LEU D CB  1 
ATOM   7115  C CG  . LEU D  2 101 ? -48.897 -59.889  -25.132 1.00 41.34  ? 101 LEU D CG  1 
ATOM   7116  C CD1 . LEU D  2 101 ? -48.964 -61.011  -26.155 1.00 48.31  ? 101 LEU D CD1 1 
ATOM   7117  C CD2 . LEU D  2 101 ? -50.290 -59.378  -24.814 1.00 36.79  ? 101 LEU D CD2 1 
ATOM   7118  N N   . LEU D  2 102 ? -46.269 -60.363  -21.516 1.00 44.10  ? 102 LEU D N   1 
ATOM   7119  C CA  . LEU D  2 102 ? -45.545 -61.083  -20.474 1.00 45.49  ? 102 LEU D CA  1 
ATOM   7120  C C   . LEU D  2 102 ? -45.627 -60.379  -19.122 1.00 47.26  ? 102 LEU D C   1 
ATOM   7121  O O   . LEU D  2 102 ? -45.746 -61.032  -18.085 1.00 41.77  ? 102 LEU D O   1 
ATOM   7122  C CB  . LEU D  2 102 ? -44.083 -61.266  -20.879 1.00 43.55  ? 102 LEU D CB  1 
ATOM   7123  C CG  . LEU D  2 102 ? -43.045 -60.708  -19.903 1.00 62.05  ? 102 LEU D CG  1 
ATOM   7124  C CD1 . LEU D  2 102 ? -42.465 -61.820  -19.051 1.00 56.28  ? 102 LEU D CD1 1 
ATOM   7125  C CD2 . LEU D  2 102 ? -41.945 -59.985  -20.652 1.00 78.20  ? 102 LEU D CD2 1 
ATOM   7126  N N   . GLU D  2 103 ? -45.565 -59.051  -19.135 1.00 43.76  ? 103 GLU D N   1 
ATOM   7127  C CA  . GLU D  2 103 ? -45.595 -58.282  -17.894 1.00 42.77  ? 103 GLU D CA  1 
ATOM   7128  C C   . GLU D  2 103 ? -46.996 -58.184  -17.294 1.00 46.49  ? 103 GLU D C   1 
ATOM   7129  O O   . GLU D  2 103 ? -47.162 -58.255  -16.076 1.00 53.10  ? 103 GLU D O   1 
ATOM   7130  C CB  . GLU D  2 103 ? -45.004 -56.886  -18.103 1.00 35.87  ? 103 GLU D CB  1 
ATOM   7131  C CG  . GLU D  2 103 ? -43.488 -56.880  -18.212 1.00 64.20  ? 103 GLU D CG  1 
ATOM   7132  C CD  . GLU D  2 103 ? -42.823 -57.690  -17.111 1.00 83.79  ? 103 GLU D CD  1 
ATOM   7133  O OE1 . GLU D  2 103 ? -42.731 -57.191  -15.971 1.00 80.81  ? 103 GLU D OE1 1 
ATOM   7134  O OE2 . GLU D  2 103 ? -42.391 -58.829  -17.386 1.00 83.84  ? 103 GLU D OE2 1 
ATOM   7135  N N   . ASN D  2 104 ? -47.997 -58.016  -18.151 1.00 44.58  ? 104 ASN D N   1 
ATOM   7136  C CA  . ASN D  2 104 ? -49.377 -57.906  -17.703 1.00 44.08  ? 104 ASN D CA  1 
ATOM   7137  C C   . ASN D  2 104 ? -49.818 -59.164  -16.987 1.00 52.57  ? 104 ASN D C   1 
ATOM   7138  O O   . ASN D  2 104 ? -50.624 -59.118  -16.058 1.00 52.48  ? 104 ASN D O   1 
ATOM   7139  C CB  . ASN D  2 104 ? -50.296 -57.649  -18.893 1.00 27.24  ? 104 ASN D CB  1 
ATOM   7140  C CG  . ASN D  2 104 ? -50.324 -56.202  -19.291 1.00 37.80  ? 104 ASN D CG  1 
ATOM   7141  O OD1 . ASN D  2 104 ? -49.927 -55.338  -18.519 1.00 40.21  ? 104 ASN D OD1 1 
ATOM   7142  N ND2 . ASN D  2 104 ? -50.800 -55.923  -20.494 1.00 40.54  ? 104 ASN D ND2 1 
ATOM   7143  N N   . GLU D  2 105 ? -49.288 -60.292  -17.445 1.00 42.02  ? 105 GLU D N   1 
ATOM   7144  C CA  . GLU D  2 105 ? -49.614 -61.591  -16.882 1.00 45.99  ? 105 GLU D CA  1 
ATOM   7145  C C   . GLU D  2 105 ? -48.867 -61.810  -15.575 1.00 52.41  ? 105 GLU D C   1 
ATOM   7146  O O   . GLU D  2 105 ? -49.324 -62.561  -14.716 1.00 52.37  ? 105 GLU D O   1 
ATOM   7147  C CB  . GLU D  2 105 ? -49.292 -62.693  -17.892 1.00 50.42  ? 105 GLU D CB  1 
ATOM   7148  C CG  . GLU D  2 105 ? -49.225 -64.102  -17.327 1.00 61.98  ? 105 GLU D CG  1 
ATOM   7149  C CD  . GLU D  2 105 ? -47.882 -64.745  -17.623 1.00 95.41  ? 105 GLU D CD  1 
ATOM   7150  O OE1 . GLU D  2 105 ? -47.116 -64.124  -18.392 1.00 93.33  ? 105 GLU D OE1 1 
ATOM   7151  O OE2 . GLU D  2 105 ? -47.595 -65.843  -17.093 1.00 102.43 ? 105 GLU D OE2 1 
ATOM   7152  N N   . ARG D  2 106 ? -47.729 -61.137  -15.421 1.00 53.73  ? 106 ARG D N   1 
ATOM   7153  C CA  . ARG D  2 106 ? -46.995 -61.153  -14.161 1.00 52.25  ? 106 ARG D CA  1 
ATOM   7154  C C   . ARG D  2 106 ? -47.634 -60.203  -13.155 1.00 57.02  ? 106 ARG D C   1 
ATOM   7155  O O   . ARG D  2 106 ? -47.638 -60.470  -11.955 1.00 65.61  ? 106 ARG D O   1 
ATOM   7156  C CB  . ARG D  2 106 ? -45.529 -60.762  -14.372 1.00 47.54  ? 106 ARG D CB  1 
ATOM   7157  C CG  . ARG D  2 106 ? -44.688 -61.805  -15.093 1.00 55.10  ? 106 ARG D CG  1 
ATOM   7158  C CD  . ARG D  2 106 ? -43.197 -61.534  -14.914 1.00 72.65  ? 106 ARG D CD  1 
ATOM   7159  N NE  . ARG D  2 106 ? -42.817 -61.471  -13.504 1.00 68.93  ? 106 ARG D NE  1 
ATOM   7160  C CZ  . ARG D  2 106 ? -42.671 -62.534  -12.720 1.00 81.84  ? 106 ARG D CZ  1 
ATOM   7161  N NH1 . ARG D  2 106 ? -42.881 -63.752  -13.202 1.00 80.83  ? 106 ARG D NH1 1 
ATOM   7162  N NH2 . ARG D  2 106 ? -42.321 -62.381  -11.450 1.00 90.44  ? 106 ARG D NH2 1 
ATOM   7163  N N   . THR D  2 107 ? -48.169 -59.091  -13.651 1.00 44.21  ? 107 THR D N   1 
ATOM   7164  C CA  . THR D  2 107 ? -48.786 -58.085  -12.794 1.00 44.38  ? 107 THR D CA  1 
ATOM   7165  C C   . THR D  2 107 ? -50.060 -58.616  -12.145 1.00 54.15  ? 107 THR D C   1 
ATOM   7166  O O   . THR D  2 107 ? -50.310 -58.378  -10.964 1.00 51.73  ? 107 THR D O   1 
ATOM   7167  C CB  . THR D  2 107 ? -49.103 -56.798  -13.576 1.00 46.34  ? 107 THR D CB  1 
ATOM   7168  O OG1 . THR D  2 107 ? -47.883 -56.205  -14.036 1.00 43.38  ? 107 THR D OG1 1 
ATOM   7169  C CG2 . THR D  2 107 ? -49.835 -55.804  -12.691 1.00 40.47  ? 107 THR D CG2 1 
ATOM   7170  N N   . LEU D  2 108 ? -50.863 -59.335  -12.922 1.00 54.44  ? 108 LEU D N   1 
ATOM   7171  C CA  . LEU D  2 108 ? -52.080 -59.939  -12.394 1.00 49.05  ? 108 LEU D CA  1 
ATOM   7172  C C   . LEU D  2 108 ? -51.748 -61.021  -11.371 1.00 47.23  ? 108 LEU D C   1 
ATOM   7173  O O   . LEU D  2 108 ? -52.393 -61.118  -10.327 1.00 53.01  ? 108 LEU D O   1 
ATOM   7174  C CB  . LEU D  2 108 ? -52.939 -60.512  -13.524 1.00 43.41  ? 108 LEU D CB  1 
ATOM   7175  C CG  . LEU D  2 108 ? -53.480 -59.489  -14.526 1.00 49.92  ? 108 LEU D CG  1 
ATOM   7176  C CD1 . LEU D  2 108 ? -54.434 -60.147  -15.512 1.00 39.49  ? 108 LEU D CD1 1 
ATOM   7177  C CD2 . LEU D  2 108 ? -54.167 -58.340  -13.802 1.00 48.94  ? 108 LEU D CD2 1 
ATOM   7178  N N   . ASP D  2 109 ? -50.737 -61.830  -11.673 1.00 44.87  ? 109 ASP D N   1 
ATOM   7179  C CA  . ASP D  2 109 ? -50.284 -62.862  -10.748 1.00 51.22  ? 109 ASP D CA  1 
ATOM   7180  C C   . ASP D  2 109 ? -49.711 -62.240  -9.479  1.00 50.29  ? 109 ASP D C   1 
ATOM   7181  O O   . ASP D  2 109 ? -49.797 -62.822  -8.399  1.00 52.13  ? 109 ASP D O   1 
ATOM   7182  C CB  . ASP D  2 109 ? -49.245 -63.767  -11.411 1.00 57.52  ? 109 ASP D CB  1 
ATOM   7183  C CG  . ASP D  2 109 ? -49.858 -64.711  -12.426 1.00 73.45  ? 109 ASP D CG  1 
ATOM   7184  O OD1 . ASP D  2 109 ? -51.101 -64.833  -12.451 1.00 78.83  ? 109 ASP D OD1 1 
ATOM   7185  O OD2 . ASP D  2 109 ? -49.097 -65.336  -13.195 1.00 69.75  ? 109 ASP D OD2 1 
ATOM   7186  N N   . TYR D  2 110 ? -49.128 -61.054  -9.618  1.00 54.33  ? 110 TYR D N   1 
ATOM   7187  C CA  . TYR D  2 110 ? -48.586 -60.329  -8.474  1.00 47.56  ? 110 TYR D CA  1 
ATOM   7188  C C   . TYR D  2 110 ? -49.698 -59.904  -7.522  1.00 61.58  ? 110 TYR D C   1 
ATOM   7189  O O   . TYR D  2 110 ? -49.591 -60.087  -6.309  1.00 57.37  ? 110 TYR D O   1 
ATOM   7190  C CB  . TYR D  2 110 ? -47.793 -59.106  -8.939  1.00 39.64  ? 110 TYR D CB  1 
ATOM   7191  C CG  . TYR D  2 110 ? -47.391 -58.174  -7.817  1.00 43.33  ? 110 TYR D CG  1 
ATOM   7192  C CD1 . TYR D  2 110 ? -46.232 -58.395  -7.085  1.00 44.28  ? 110 TYR D CD1 1 
ATOM   7193  C CD2 . TYR D  2 110 ? -48.170 -57.071  -7.493  1.00 42.25  ? 110 TYR D CD2 1 
ATOM   7194  C CE1 . TYR D  2 110 ? -45.862 -57.545  -6.059  1.00 37.27  ? 110 TYR D CE1 1 
ATOM   7195  C CE2 . TYR D  2 110 ? -47.808 -56.216  -6.471  1.00 49.05  ? 110 TYR D CE2 1 
ATOM   7196  C CZ  . TYR D  2 110 ? -46.654 -56.458  -5.757  1.00 55.11  ? 110 TYR D CZ  1 
ATOM   7197  O OH  . TYR D  2 110 ? -46.293 -55.608  -4.738  1.00 64.82  ? 110 TYR D OH  1 
ATOM   7198  N N   . HIS D  2 111 ? -50.764 -59.334  -8.077  1.00 52.20  ? 111 HIS D N   1 
ATOM   7199  C CA  . HIS D  2 111 ? -51.913 -58.922  -7.280  1.00 45.03  ? 111 HIS D CA  1 
ATOM   7200  C C   . HIS D  2 111 ? -52.612 -60.133  -6.675  1.00 54.07  ? 111 HIS D C   1 
ATOM   7201  O O   . HIS D  2 111 ? -52.948 -60.142  -5.490  1.00 54.77  ? 111 HIS D O   1 
ATOM   7202  C CB  . HIS D  2 111 ? -52.902 -58.115  -8.124  1.00 44.14  ? 111 HIS D CB  1 
ATOM   7203  C CG  . HIS D  2 111 ? -52.415 -56.741  -8.477  1.00 52.21  ? 111 HIS D CG  1 
ATOM   7204  N ND1 . HIS D  2 111 ? -52.245 -55.752  -7.536  1.00 57.61  ? 111 HIS D ND1 1 
ATOM   7205  C CD2 . HIS D  2 111 ? -52.075 -56.196  -9.668  1.00 53.47  ? 111 HIS D CD2 1 
ATOM   7206  C CE1 . HIS D  2 111 ? -51.812 -54.652  -8.130  1.00 59.78  ? 111 HIS D CE1 1 
ATOM   7207  N NE2 . HIS D  2 111 ? -51.702 -54.895  -9.424  1.00 51.64  ? 111 HIS D NE2 1 
ATOM   7208  N N   . ASP D  2 112 ? -52.828 -61.153  -7.499  1.00 49.39  ? 112 ASP D N   1 
ATOM   7209  C CA  . ASP D  2 112 ? -53.435 -62.395  -7.043  1.00 46.27  ? 112 ASP D CA  1 
ATOM   7210  C C   . ASP D  2 112 ? -52.675 -62.927  -5.834  1.00 48.14  ? 112 ASP D C   1 
ATOM   7211  O O   . ASP D  2 112 ? -53.272 -63.395  -4.865  1.00 53.37  ? 112 ASP D O   1 
ATOM   7212  C CB  . ASP D  2 112 ? -53.417 -63.431  -8.168  1.00 57.70  ? 112 ASP D CB  1 
ATOM   7213  C CG  . ASP D  2 112 ? -54.229 -64.665  -7.837  1.00 64.30  ? 112 ASP D CG  1 
ATOM   7214  O OD1 . ASP D  2 112 ? -54.026 -65.706  -8.495  1.00 71.73  ? 112 ASP D OD1 1 
ATOM   7215  O OD2 . ASP D  2 112 ? -55.070 -64.595  -6.919  1.00 75.85  ? 112 ASP D OD2 1 
ATOM   7216  N N   . SER D  2 113 ? -51.350 -62.839  -5.902  1.00 62.91  ? 113 SER D N   1 
ATOM   7217  C CA  . SER D  2 113 ? -50.480 -63.308  -4.831  1.00 51.28  ? 113 SER D CA  1 
ATOM   7218  C C   . SER D  2 113 ? -50.728 -62.568  -3.521  1.00 60.27  ? 113 SER D C   1 
ATOM   7219  O O   . SER D  2 113 ? -50.900 -63.188  -2.471  1.00 67.14  ? 113 SER D O   1 
ATOM   7220  C CB  . SER D  2 113 ? -49.014 -63.159  -5.241  1.00 47.58  ? 113 SER D CB  1 
ATOM   7221  O OG  . SER D  2 113 ? -48.150 -63.397  -4.143  1.00 74.33  ? 113 SER D OG  1 
ATOM   7222  N N   . ASN D  2 114 ? -50.741 -61.240  -3.587  1.00 52.40  ? 114 ASN D N   1 
ATOM   7223  C CA  . ASN D  2 114 ? -50.926 -60.416  -2.398  1.00 62.03  ? 114 ASN D CA  1 
ATOM   7224  C C   . ASN D  2 114 ? -52.231 -60.717  -1.668  1.00 60.31  ? 114 ASN D C   1 
ATOM   7225  O O   . ASN D  2 114 ? -52.283 -60.694  -0.438  1.00 63.48  ? 114 ASN D O   1 
ATOM   7226  C CB  . ASN D  2 114 ? -50.842 -58.931  -2.756  1.00 53.05  ? 114 ASN D CB  1 
ATOM   7227  C CG  . ASN D  2 114 ? -49.472 -58.535  -3.270  1.00 62.89  ? 114 ASN D CG  1 
ATOM   7228  O OD1 . ASN D  2 114 ? -48.484 -59.229  -3.031  1.00 71.27  ? 114 ASN D OD1 1 
ATOM   7229  N ND2 . ASN D  2 114 ? -49.406 -57.415  -3.978  1.00 67.02  ? 114 ASN D ND2 1 
ATOM   7230  N N   . VAL D  2 115 ? -53.282 -60.999  -2.431  1.00 52.44  ? 115 VAL D N   1 
ATOM   7231  C CA  . VAL D  2 115 ? -54.561 -61.386  -1.850  1.00 56.37  ? 115 VAL D CA  1 
ATOM   7232  C C   . VAL D  2 115 ? -54.414 -62.703  -1.096  1.00 55.77  ? 115 VAL D C   1 
ATOM   7233  O O   . VAL D  2 115 ? -54.722 -62.788  0.093   1.00 71.15  ? 115 VAL D O   1 
ATOM   7234  C CB  . VAL D  2 115 ? -55.650 -61.535  -2.928  1.00 55.47  ? 115 VAL D CB  1 
ATOM   7235  C CG1 . VAL D  2 115 ? -56.917 -62.122  -2.326  1.00 60.77  ? 115 VAL D CG1 1 
ATOM   7236  C CG2 . VAL D  2 115 ? -55.933 -60.193  -3.582  1.00 38.87  ? 115 VAL D CG2 1 
ATOM   7237  N N   . LYS D  2 116 ? -53.939 -63.725  -1.801  1.00 50.65  ? 116 LYS D N   1 
ATOM   7238  C CA  . LYS D  2 116 ? -53.682 -65.034  -1.210  1.00 60.24  ? 116 LYS D CA  1 
ATOM   7239  C C   . LYS D  2 116 ? -52.873 -64.914  0.077   1.00 69.16  ? 116 LYS D C   1 
ATOM   7240  O O   . LYS D  2 116 ? -53.170 -65.574  1.073   1.00 67.76  ? 116 LYS D O   1 
ATOM   7241  C CB  . LYS D  2 116 ? -52.937 -65.920  -2.210  1.00 60.70  ? 116 LYS D CB  1 
ATOM   7242  C CG  . LYS D  2 116 ? -52.350 -67.194  -1.619  1.00 62.28  ? 116 LYS D CG  1 
ATOM   7243  C CD  . LYS D  2 116 ? -53.292 -68.378  -1.772  1.00 72.97  ? 116 LYS D CD  1 
ATOM   7244  C CE  . LYS D  2 116 ? -52.587 -69.682  -1.427  1.00 88.66  ? 116 LYS D CE  1 
ATOM   7245  N NZ  . LYS D  2 116 ? -53.412 -70.877  -1.759  1.00 103.28 ? 116 LYS D NZ  1 
ATOM   7246  N N   . ASN D  2 117 ? -51.848 -64.069  0.048   1.00 61.57  ? 117 ASN D N   1 
ATOM   7247  C CA  . ASN D  2 117 ? -50.994 -63.857  1.211   1.00 67.22  ? 117 ASN D CA  1 
ATOM   7248  C C   . ASN D  2 117 ? -51.733 -63.192  2.366   1.00 74.32  ? 117 ASN D C   1 
ATOM   7249  O O   . ASN D  2 117 ? -51.523 -63.538  3.529   1.00 84.13  ? 117 ASN D O   1 
ATOM   7250  C CB  . ASN D  2 117 ? -49.760 -63.036  0.832   1.00 61.22  ? 117 ASN D CB  1 
ATOM   7251  C CG  . ASN D  2 117 ? -48.737 -63.845  0.062   1.00 58.36  ? 117 ASN D CG  1 
ATOM   7252  O OD1 . ASN D  2 117 ? -48.832 -65.070  -0.022  1.00 60.94  ? 117 ASN D OD1 1 
ATOM   7253  N ND2 . ASN D  2 117 ? -47.746 -63.165  -0.503  1.00 75.91  ? 117 ASN D ND2 1 
ATOM   7254  N N   . LEU D  2 118 ? -52.596 -62.236  2.041   1.00 62.30  ? 118 LEU D N   1 
ATOM   7255  C CA  . LEU D  2 118 ? -53.384 -61.548  3.054   1.00 59.99  ? 118 LEU D CA  1 
ATOM   7256  C C   . LEU D  2 118 ? -54.336 -62.535  3.717   1.00 64.83  ? 118 LEU D C   1 
ATOM   7257  O O   . LEU D  2 118 ? -54.510 -62.528  4.935   1.00 82.17  ? 118 LEU D O   1 
ATOM   7258  C CB  . LEU D  2 118 ? -54.166 -60.391  2.430   1.00 70.27  ? 118 LEU D CB  1 
ATOM   7259  C CG  . LEU D  2 118 ? -54.395 -59.183  3.337   1.00 73.53  ? 118 LEU D CG  1 
ATOM   7260  C CD1 . LEU D  2 118 ? -53.074 -58.723  3.932   1.00 71.22  ? 118 LEU D CD1 1 
ATOM   7261  C CD2 . LEU D  2 118 ? -55.068 -58.054  2.573   1.00 77.11  ? 118 LEU D CD2 1 
ATOM   7262  N N   . TYR D  2 119 ? -54.944 -63.389  2.900   1.00 57.32  ? 119 TYR D N   1 
ATOM   7263  C CA  . TYR D  2 119 ? -55.832 -64.433  3.393   1.00 66.76  ? 119 TYR D CA  1 
ATOM   7264  C C   . TYR D  2 119 ? -55.083 -65.386  4.317   1.00 71.19  ? 119 TYR D C   1 
ATOM   7265  O O   . TYR D  2 119 ? -55.534 -65.676  5.425   1.00 87.14  ? 119 TYR D O   1 
ATOM   7266  C CB  . TYR D  2 119 ? -56.438 -65.208  2.221   1.00 63.13  ? 119 TYR D CB  1 
ATOM   7267  C CG  . TYR D  2 119 ? -57.305 -66.375  2.635   1.00 85.07  ? 119 TYR D CG  1 
ATOM   7268  C CD1 . TYR D  2 119 ? -58.667 -66.211  2.849   1.00 87.69  ? 119 TYR D CD1 1 
ATOM   7269  C CD2 . TYR D  2 119 ? -56.762 -67.642  2.808   1.00 75.70  ? 119 TYR D CD2 1 
ATOM   7270  C CE1 . TYR D  2 119 ? -59.464 -67.274  3.227   1.00 88.73  ? 119 TYR D CE1 1 
ATOM   7271  C CE2 . TYR D  2 119 ? -57.551 -68.711  3.186   1.00 87.87  ? 119 TYR D CE2 1 
ATOM   7272  C CZ  . TYR D  2 119 ? -58.901 -68.522  3.393   1.00 97.98  ? 119 TYR D CZ  1 
ATOM   7273  O OH  . TYR D  2 119 ? -59.690 -69.584  3.770   1.00 107.22 ? 119 TYR D OH  1 
ATOM   7274  N N   . GLU D  2 120 ? -53.934 -65.868  3.852   1.00 78.20  ? 120 GLU D N   1 
ATOM   7275  C CA  . GLU D  2 120 ? -53.121 -66.804  4.622   1.00 77.53  ? 120 GLU D CA  1 
ATOM   7276  C C   . GLU D  2 120 ? -52.649 -66.215  5.947   1.00 75.91  ? 120 GLU D C   1 
ATOM   7277  O O   . GLU D  2 120 ? -52.674 -66.889  6.976   1.00 82.38  ? 120 GLU D O   1 
ATOM   7278  C CB  . GLU D  2 120 ? -51.918 -67.272  3.799   1.00 94.50  ? 120 GLU D CB  1 
ATOM   7279  C CG  . GLU D  2 120 ? -52.212 -68.451  2.888   1.00 101.47 ? 120 GLU D CG  1 
ATOM   7280  C CD  . GLU D  2 120 ? -52.475 -69.729  3.661   1.00 129.10 ? 120 GLU D CD  1 
ATOM   7281  O OE1 . GLU D  2 120 ? -52.009 -69.834  4.816   1.00 123.99 ? 120 GLU D OE1 1 
ATOM   7282  O OE2 . GLU D  2 120 ? -53.144 -70.630  3.113   1.00 136.67 ? 120 GLU D OE2 1 
ATOM   7283  N N   . LYS D  2 121 ? -52.217 -64.958  5.918   1.00 79.63  ? 121 LYS D N   1 
ATOM   7284  C CA  . LYS D  2 121 ? -51.714 -64.300  7.119   1.00 85.92  ? 121 LYS D CA  1 
ATOM   7285  C C   . LYS D  2 121 ? -52.779 -64.241  8.210   1.00 92.61  ? 121 LYS D C   1 
ATOM   7286  O O   . LYS D  2 121 ? -52.470 -64.334  9.398   1.00 98.96  ? 121 LYS D O   1 
ATOM   7287  C CB  . LYS D  2 121 ? -51.207 -62.894  6.796   1.00 85.39  ? 121 LYS D CB  1 
ATOM   7288  C CG  . LYS D  2 121 ? -50.544 -62.200  7.974   1.00 102.62 ? 121 LYS D CG  1 
ATOM   7289  C CD  . LYS D  2 121 ? -50.036 -60.820  7.600   1.00 105.78 ? 121 LYS D CD  1 
ATOM   7290  C CE  . LYS D  2 121 ? -49.348 -60.156  8.781   1.00 117.38 ? 121 LYS D CE  1 
ATOM   7291  N NZ  . LYS D  2 121 ? -48.868 -58.786  8.452   1.00 131.12 ? 121 LYS D NZ  1 
ATOM   7292  N N   . VAL D  2 122 ? -54.033 -64.085  7.799   1.00 97.60  ? 122 VAL D N   1 
ATOM   7293  C CA  . VAL D  2 122 ? -55.151 -64.082  8.735   1.00 97.47  ? 122 VAL D CA  1 
ATOM   7294  C C   . VAL D  2 122 ? -55.457 -65.497  9.211   1.00 102.55 ? 122 VAL D C   1 
ATOM   7295  O O   . VAL D  2 122 ? -55.693 -65.729  10.397  1.00 123.40 ? 122 VAL D O   1 
ATOM   7296  C CB  . VAL D  2 122 ? -56.420 -63.484  8.096   1.00 85.75  ? 122 VAL D CB  1 
ATOM   7297  C CG1 . VAL D  2 122 ? -57.659 -63.890  8.884   1.00 98.53  ? 122 VAL D CG1 1 
ATOM   7298  C CG2 . VAL D  2 122 ? -56.305 -61.970  8.001   1.00 76.15  ? 122 VAL D CG2 1 
ATOM   7299  N N   . ARG D  2 123 ? -55.442 -66.439  8.274   1.00 80.84  ? 123 ARG D N   1 
ATOM   7300  C CA  . ARG D  2 123 ? -55.805 -67.821  8.560   1.00 94.56  ? 123 ARG D CA  1 
ATOM   7301  C C   . ARG D  2 123 ? -54.804 -68.510  9.483   1.00 99.21  ? 123 ARG D C   1 
ATOM   7302  O O   . ARG D  2 123 ? -55.191 -69.192  10.425  1.00 109.90 ? 123 ARG D O   1 
ATOM   7303  C CB  . ARG D  2 123 ? -55.941 -68.617  7.264   1.00 87.73  ? 123 ARG D CB  1 
ATOM   7304  C CG  . ARG D  2 123 ? -56.592 -69.971  7.452   1.00 97.51  ? 123 ARG D CG  1 
ATOM   7305  C CD  . ARG D  2 123 ? -56.023 -70.993  6.491   1.00 108.01 ? 123 ARG D CD  1 
ATOM   7306  N NE  . ARG D  2 123 ? -54.620 -71.278  6.768   1.00 120.48 ? 123 ARG D NE  1 
ATOM   7307  C CZ  . ARG D  2 123 ? -53.994 -72.385  6.383   1.00 129.34 ? 123 ARG D CZ  1 
ATOM   7308  N NH1 . ARG D  2 123 ? -54.652 -73.319  5.709   1.00 124.69 ? 123 ARG D NH1 1 
ATOM   7309  N NH2 . ARG D  2 123 ? -52.714 -72.562  6.678   1.00 133.26 ? 123 ARG D NH2 1 
ATOM   7310  N N   . SER D  2 124 ? -53.516 -68.343  9.208   1.00 102.14 ? 124 SER D N   1 
ATOM   7311  C CA  . SER D  2 124 ? -52.491 -68.948  10.054  1.00 111.37 ? 124 SER D CA  1 
ATOM   7312  C C   . SER D  2 124 ? -52.331 -68.160  11.352  1.00 115.99 ? 124 SER D C   1 
ATOM   7313  O O   . SER D  2 124 ? -51.325 -68.282  12.054  1.00 121.85 ? 124 SER D O   1 
ATOM   7314  C CB  . SER D  2 124 ? -51.157 -69.039  9.311   1.00 121.33 ? 124 SER D CB  1 
ATOM   7315  O OG  . SER D  2 124 ? -50.645 -67.751  9.020   1.00 117.93 ? 124 SER D OG  1 
ATOM   7316  N N   . GLN D  2 125 ? -53.344 -67.358  11.660  1.00 112.06 ? 125 GLN D N   1 
ATOM   7317  C CA  . GLN D  2 125 ? -53.359 -66.528  12.855  1.00 112.06 ? 125 GLN D CA  1 
ATOM   7318  C C   . GLN D  2 125 ? -54.562 -66.957  13.700  1.00 119.11 ? 125 GLN D C   1 
ATOM   7319  O O   . GLN D  2 125 ? -54.398 -67.481  14.810  1.00 118.23 ? 125 GLN D O   1 
ATOM   7320  C CB  . GLN D  2 125 ? -53.465 -65.057  12.468  1.00 90.73  ? 125 GLN D CB  1 
ATOM   7321  C CG  . GLN D  2 125 ? -52.458 -64.147  13.151  1.00 99.55  ? 125 GLN D CG  1 
ATOM   7322  C CD  . GLN D  2 125 ? -52.639 -62.712  12.729  1.00 111.09 ? 125 GLN D CD  1 
ATOM   7323  O OE1 . GLN D  2 125 ? -53.713 -62.328  12.276  1.00 113.21 ? 125 GLN D OE1 1 
ATOM   7324  N NE2 . GLN D  2 125 ? -51.590 -61.911  12.865  1.00 113.49 ? 125 GLN D NE2 1 
ATOM   7325  N N   . LEU D  2 126 ? -55.771 -66.754  13.182  1.00 113.36 ? 126 LEU D N   1 
ATOM   7326  C CA  . LEU D  2 126 ? -56.913 -67.464  13.734  1.00 113.34 ? 126 LEU D CA  1 
ATOM   7327  C C   . LEU D  2 126 ? -56.758 -68.883  13.244  1.00 133.69 ? 126 LEU D C   1 
ATOM   7328  O O   . LEU D  2 126 ? -56.711 -69.120  12.042  1.00 156.26 ? 126 LEU D O   1 
ATOM   7329  C CB  . LEU D  2 126 ? -58.231 -66.901  13.199  1.00 107.76 ? 126 LEU D CB  1 
ATOM   7330  C CG  . LEU D  2 126 ? -58.309 -65.484  12.578  1.00 99.65  ? 126 LEU D CG  1 
ATOM   7331  C CD1 . LEU D  2 126 ? -59.560 -65.346  11.730  1.00 100.27 ? 126 LEU D CD1 1 
ATOM   7332  C CD2 . LEU D  2 126 ? -58.200 -64.314  13.573  1.00 101.66 ? 126 LEU D CD2 1 
ATOM   7333  N N   . LYS D  2 127 ? -56.661 -69.822  14.171  1.00 123.45 ? 127 LYS D N   1 
ATOM   7334  C CA  . LYS D  2 127 ? -56.577 -71.226  13.810  1.00 120.18 ? 127 LYS D CA  1 
ATOM   7335  C C   . LYS D  2 127 ? -57.862 -71.942  14.235  1.00 141.65 ? 127 LYS D C   1 
ATOM   7336  O O   . LYS D  2 127 ? -58.778 -72.137  13.434  1.00 127.33 ? 127 LYS D O   1 
ATOM   7337  C CB  . LYS D  2 127 ? -55.356 -71.872  14.453  1.00 119.91 ? 127 LYS D CB  1 
ATOM   7338  C CG  . LYS D  2 127 ? -54.072 -71.094  14.140  1.00 117.66 ? 127 LYS D CG  1 
ATOM   7339  C CD  . LYS D  2 127 ? -53.235 -70.846  15.394  1.00 124.59 ? 127 LYS D CD  1 
ATOM   7340  C CE  . LYS D  2 127 ? -52.016 -69.979  15.069  1.00 130.60 ? 127 LYS D CE  1 
ATOM   7341  N NZ  . LYS D  2 127 ? -51.129 -69.716  16.245  1.00 125.65 ? 127 LYS D NZ  1 
ATOM   7342  N N   . ASN D  2 128 ? -57.950 -72.293  15.513  1.00 160.81 ? 128 ASN D N   1 
ATOM   7343  C CA  . ASN D  2 128 ? -59.165 -72.887  16.051  1.00 161.10 ? 128 ASN D CA  1 
ATOM   7344  C C   . ASN D  2 128 ? -60.236 -71.848  16.357  1.00 162.68 ? 128 ASN D C   1 
ATOM   7345  O O   . ASN D  2 128 ? -61.422 -72.151  16.300  1.00 152.33 ? 128 ASN D O   1 
ATOM   7346  C CB  . ASN D  2 128 ? -58.845 -73.713  17.291  1.00 154.48 ? 128 ASN D CB  1 
ATOM   7347  C CG  . ASN D  2 128 ? -58.064 -74.969  16.959  1.00 158.00 ? 128 ASN D CG  1 
ATOM   7348  O OD1 . ASN D  2 128 ? -58.387 -75.683  16.007  1.00 153.27 ? 128 ASN D OD1 1 
ATOM   7349  N ND2 . ASN D  2 128 ? -57.036 -75.250  17.748  1.00 171.10 ? 128 ASN D ND2 1 
ATOM   7350  N N   . ASN D  2 129 ? -59.815 -70.624  16.663  1.00 223.81 ? 129 ASN D N   1 
ATOM   7351  C CA  . ASN D  2 129 ? -60.734 -69.581  17.113  1.00 229.19 ? 129 ASN D CA  1 
ATOM   7352  C C   . ASN D  2 129 ? -61.741 -69.138  16.053  1.00 216.45 ? 129 ASN D C   1 
ATOM   7353  O O   . ASN D  2 129 ? -62.569 -68.264  16.305  1.00 216.23 ? 129 ASN D O   1 
ATOM   7354  C CB  . ASN D  2 129 ? -59.949 -68.378  17.638  1.00 225.81 ? 129 ASN D CB  1 
ATOM   7355  C CG  . ASN D  2 129 ? -59.072 -68.728  18.828  1.00 222.75 ? 129 ASN D CG  1 
ATOM   7356  O OD1 . ASN D  2 129 ? -58.448 -67.855  19.429  1.00 218.80 ? 129 ASN D OD1 1 
ATOM   7357  N ND2 . ASN D  2 129 ? -59.024 -70.010  19.175  1.00 229.82 ? 129 ASN D ND2 1 
ATOM   7358  N N   . ALA D  2 130 ? -61.668 -69.742  14.871  1.00 150.86 ? 130 ALA D N   1 
ATOM   7359  C CA  . ALA D  2 130 ? -62.591 -69.426  13.785  1.00 138.97 ? 130 ALA D CA  1 
ATOM   7360  C C   . ALA D  2 130 ? -62.523 -70.490  12.696  1.00 124.57 ? 130 ALA D C   1 
ATOM   7361  O O   . ALA D  2 130 ? -61.621 -71.327  12.695  1.00 124.08 ? 130 ALA D O   1 
ATOM   7362  C CB  . ALA D  2 130 ? -62.284 -68.053  13.208  1.00 129.28 ? 130 ALA D CB  1 
ATOM   7363  N N   . LYS D  2 131 ? -63.476 -70.458  11.769  1.00 126.10 ? 131 LYS D N   1 
ATOM   7364  C CA  . LYS D  2 131 ? -63.516 -71.443  10.692  1.00 138.91 ? 131 LYS D CA  1 
ATOM   7365  C C   . LYS D  2 131 ? -63.587 -70.786  9.318   1.00 154.30 ? 131 LYS D C   1 
ATOM   7366  O O   . LYS D  2 131 ? -64.155 -69.705  9.162   1.00 148.11 ? 131 LYS D O   1 
ATOM   7367  C CB  . LYS D  2 131 ? -64.704 -72.390  10.869  1.00 136.06 ? 131 LYS D CB  1 
ATOM   7368  C CG  . LYS D  2 131 ? -66.054 -71.753  10.576  1.00 146.64 ? 131 LYS D CG  1 
ATOM   7369  C CD  . LYS D  2 131 ? -67.125 -72.809  10.355  1.00 146.29 ? 131 LYS D CD  1 
ATOM   7370  C CE  . LYS D  2 131 ? -68.433 -72.182  9.898   1.00 135.39 ? 131 LYS D CE  1 
ATOM   7371  N NZ  . LYS D  2 131 ? -69.446 -73.211  9.533   1.00 136.08 ? 131 LYS D NZ  1 
ATOM   7372  N N   . GLU D  2 132 ? -63.008 -71.450  8.323   1.00 192.43 ? 132 GLU D N   1 
ATOM   7373  C CA  . GLU D  2 132 ? -63.073 -70.978  6.947   1.00 180.18 ? 132 GLU D CA  1 
ATOM   7374  C C   . GLU D  2 132 ? -64.449 -71.259  6.357   1.00 182.50 ? 132 GLU D C   1 
ATOM   7375  O O   . GLU D  2 132 ? -65.027 -72.321  6.590   1.00 186.42 ? 132 GLU D O   1 
ATOM   7376  C CB  . GLU D  2 132 ? -62.013 -71.671  6.090   1.00 188.87 ? 132 GLU D CB  1 
ATOM   7377  C CG  . GLU D  2 132 ? -60.585 -71.482  6.562   1.00 191.39 ? 132 GLU D CG  1 
ATOM   7378  C CD  . GLU D  2 132 ? -59.600 -72.268  5.720   1.00 196.68 ? 132 GLU D CD  1 
ATOM   7379  O OE1 . GLU D  2 132 ? -58.432 -72.401  6.135   1.00 186.21 ? 132 GLU D OE1 1 
ATOM   7380  O OE2 . GLU D  2 132 ? -59.999 -72.761  4.644   1.00 194.90 ? 132 GLU D OE2 1 
ATOM   7381  N N   . ILE D  2 133 ? -64.968 -70.307  5.591   1.00 157.59 ? 133 ILE D N   1 
ATOM   7382  C CA  . ILE D  2 133 ? -66.226 -70.503  4.882   1.00 165.77 ? 133 ILE D CA  1 
ATOM   7383  C C   . ILE D  2 133 ? -65.952 -71.070  3.494   1.00 163.90 ? 133 ILE D C   1 
ATOM   7384  O O   . ILE D  2 133 ? -66.722 -71.878  2.975   1.00 165.71 ? 133 ILE D O   1 
ATOM   7385  C CB  . ILE D  2 133 ? -67.014 -69.186  4.746   1.00 158.32 ? 133 ILE D CB  1 
ATOM   7386  C CG1 . ILE D  2 133 ? -67.373 -68.630  6.125   1.00 161.94 ? 133 ILE D CG1 1 
ATOM   7387  C CG2 . ILE D  2 133 ? -68.276 -69.405  3.928   1.00 150.95 ? 133 ILE D CG2 1 
ATOM   7388  C CD1 . ILE D  2 133 ? -68.381 -69.470  6.878   1.00 173.08 ? 133 ILE D CD1 1 
ATOM   7389  N N   . GLY D  2 134 ? -64.841 -70.644  2.901   1.00 142.62 ? 134 GLY D N   1 
ATOM   7390  C CA  . GLY D  2 134 ? -64.466 -71.085  1.571   1.00 136.16 ? 134 GLY D CA  1 
ATOM   7391  C C   . GLY D  2 134 ? -64.526 -69.950  0.568   1.00 123.09 ? 134 GLY D C   1 
ATOM   7392  O O   . GLY D  2 134 ? -63.928 -70.022  -0.506  1.00 103.31 ? 134 GLY D O   1 
ATOM   7393  N N   . ASN D  2 135 ? -65.252 -68.896  0.925   1.00 105.13 ? 135 ASN D N   1 
ATOM   7394  C CA  . ASN D  2 135 ? -65.391 -67.730  0.063   1.00 92.59  ? 135 ASN D CA  1 
ATOM   7395  C C   . ASN D  2 135 ? -64.413 -66.631  0.464   1.00 94.94  ? 135 ASN D C   1 
ATOM   7396  O O   . ASN D  2 135 ? -64.676 -65.445  0.266   1.00 87.69  ? 135 ASN D O   1 
ATOM   7397  C CB  . ASN D  2 135 ? -66.827 -67.203  0.112   1.00 97.86  ? 135 ASN D CB  1 
ATOM   7398  C CG  . ASN D  2 135 ? -67.131 -66.226  -1.007  1.00 108.85 ? 135 ASN D CG  1 
ATOM   7399  O OD1 . ASN D  2 135 ? -66.319 -66.027  -1.911  1.00 97.79  ? 135 ASN D OD1 1 
ATOM   7400  N ND2 . ASN D  2 135 ? -68.308 -65.613  -0.954  1.00 122.60 ? 135 ASN D ND2 1 
ATOM   7401  N N   . GLY D  2 136 ? -63.282 -67.036  1.031   1.00 92.72  ? 136 GLY D N   1 
ATOM   7402  C CA  . GLY D  2 136 ? -62.286 -66.091  1.500   1.00 84.55  ? 136 GLY D CA  1 
ATOM   7403  C C   . GLY D  2 136 ? -62.741 -65.368  2.753   1.00 100.43 ? 136 GLY D C   1 
ATOM   7404  O O   . GLY D  2 136 ? -62.196 -64.324  3.111   1.00 99.94  ? 136 GLY D O   1 
ATOM   7405  N N   . CYS D  2 137 ? -63.747 -65.927  3.420   1.00 142.71 ? 137 CYS D N   1 
ATOM   7406  C CA  . CYS D  2 137 ? -64.286 -65.330  4.637   1.00 145.70 ? 137 CYS D CA  1 
ATOM   7407  C C   . CYS D  2 137 ? -64.257 -66.304  5.811   1.00 142.67 ? 137 CYS D C   1 
ATOM   7408  O O   . CYS D  2 137 ? -64.481 -67.503  5.645   1.00 139.61 ? 137 CYS D O   1 
ATOM   7409  C CB  . CYS D  2 137 ? -65.712 -64.827  4.406   1.00 137.72 ? 137 CYS D CB  1 
ATOM   7410  S SG  . CYS D  2 137 ? -65.829 -63.383  3.324   1.00 153.75 ? 137 CYS D SG  1 
ATOM   7411  N N   . PHE D  2 138 ? -63.981 -65.776  6.999   1.00 127.92 ? 138 PHE D N   1 
ATOM   7412  C CA  . PHE D  2 138 ? -63.904 -66.585  8.209   1.00 141.39 ? 138 PHE D CA  1 
ATOM   7413  C C   . PHE D  2 138 ? -65.102 -66.327  9.116   1.00 157.22 ? 138 PHE D C   1 
ATOM   7414  O O   . PHE D  2 138 ? -65.726 -65.268  9.047   1.00 158.32 ? 138 PHE D O   1 
ATOM   7415  C CB  . PHE D  2 138 ? -62.616 -66.274  8.974   1.00 137.29 ? 138 PHE D CB  1 
ATOM   7416  C CG  . PHE D  2 138 ? -61.361 -66.567  8.202   1.00 121.64 ? 138 PHE D CG  1 
ATOM   7417  C CD1 . PHE D  2 138 ? -60.854 -65.646  7.299   1.00 112.40 ? 138 PHE D CD1 1 
ATOM   7418  C CD2 . PHE D  2 138 ? -60.680 -67.757  8.389   1.00 114.13 ? 138 PHE D CD2 1 
ATOM   7419  C CE1 . PHE D  2 138 ? -59.697 -65.912  6.592   1.00 105.59 ? 138 PHE D CE1 1 
ATOM   7420  C CE2 . PHE D  2 138 ? -59.522 -68.029  7.685   1.00 101.38 ? 138 PHE D CE2 1 
ATOM   7421  C CZ  . PHE D  2 138 ? -59.030 -67.105  6.786   1.00 105.73 ? 138 PHE D CZ  1 
ATOM   7422  N N   . GLU D  2 139 ? -65.420 -67.298  9.967   1.00 166.62 ? 139 GLU D N   1 
ATOM   7423  C CA  . GLU D  2 139 ? -66.458 -67.113  10.976  1.00 157.76 ? 139 GLU D CA  1 
ATOM   7424  C C   . GLU D  2 139 ? -65.899 -67.331  12.378  1.00 145.89 ? 139 GLU D C   1 
ATOM   7425  O O   . GLU D  2 139 ? -65.376 -68.401  12.690  1.00 147.25 ? 139 GLU D O   1 
ATOM   7426  C CB  . GLU D  2 139 ? -67.649 -68.041  10.729  1.00 159.95 ? 139 GLU D CB  1 
ATOM   7427  C CG  . GLU D  2 139 ? -68.757 -67.885  11.762  1.00 181.56 ? 139 GLU D CG  1 
ATOM   7428  C CD  . GLU D  2 139 ? -70.046 -68.571  11.357  1.00 186.53 ? 139 GLU D CD  1 
ATOM   7429  O OE1 . GLU D  2 139 ? -70.088 -69.163  10.258  1.00 172.47 ? 139 GLU D OE1 1 
ATOM   7430  O OE2 . GLU D  2 139 ? -71.019 -68.515  12.138  1.00 184.01 ? 139 GLU D OE2 1 
ATOM   7431  N N   . PHE D  2 140 ? -66.017 -66.308  13.217  1.00 180.44 ? 140 PHE D N   1 
ATOM   7432  C CA  . PHE D  2 140 ? -65.483 -66.355  14.573  1.00 190.44 ? 140 PHE D CA  1 
ATOM   7433  C C   . PHE D  2 140 ? -66.344 -67.194  15.510  1.00 198.55 ? 140 PHE D C   1 
ATOM   7434  O O   . PHE D  2 140 ? -67.572 -67.097  15.496  1.00 195.56 ? 140 PHE D O   1 
ATOM   7435  C CB  . PHE D  2 140 ? -65.355 -64.940  15.144  1.00 193.15 ? 140 PHE D CB  1 
ATOM   7436  C CG  . PHE D  2 140 ? -64.304 -64.103  14.474  1.00 187.74 ? 140 PHE D CG  1 
ATOM   7437  C CD1 . PHE D  2 140 ? -64.645 -63.205  13.476  1.00 190.83 ? 140 PHE D CD1 1 
ATOM   7438  C CD2 . PHE D  2 140 ? -62.975 -64.210  14.847  1.00 183.20 ? 140 PHE D CD2 1 
ATOM   7439  C CE1 . PHE D  2 140 ? -63.678 -62.431  12.862  1.00 186.89 ? 140 PHE D CE1 1 
ATOM   7440  C CE2 . PHE D  2 140 ? -62.005 -63.440  14.237  1.00 178.90 ? 140 PHE D CE2 1 
ATOM   7441  C CZ  . PHE D  2 140 ? -62.356 -62.549  13.243  1.00 177.95 ? 140 PHE D CZ  1 
ATOM   7442  N N   . TYR D  2 141 ? -65.693 -68.018  16.324  1.00 156.40 ? 141 TYR D N   1 
ATOM   7443  C CA  . TYR D  2 141 ? -66.376 -68.705  17.411  1.00 151.10 ? 141 TYR D CA  1 
ATOM   7444  C C   . TYR D  2 141 ? -66.319 -67.822  18.647  1.00 145.42 ? 141 TYR D C   1 
ATOM   7445  O O   . TYR D  2 141 ? -67.062 -68.023  19.607  1.00 153.75 ? 141 TYR D O   1 
ATOM   7446  C CB  . TYR D  2 141 ? -65.718 -70.052  17.715  1.00 152.75 ? 141 TYR D CB  1 
ATOM   7447  C CG  . TYR D  2 141 ? -65.796 -71.057  16.590  1.00 146.82 ? 141 TYR D CG  1 
ATOM   7448  C CD1 . TYR D  2 141 ? -64.663 -71.735  16.160  1.00 143.02 ? 141 TYR D CD1 1 
ATOM   7449  C CD2 . TYR D  2 141 ? -67.001 -71.327  15.956  1.00 136.64 ? 141 TYR D CD2 1 
ATOM   7450  C CE1 . TYR D  2 141 ? -64.729 -72.656  15.134  1.00 139.91 ? 141 TYR D CE1 1 
ATOM   7451  C CE2 . TYR D  2 141 ? -67.077 -72.246  14.928  1.00 136.33 ? 141 TYR D CE2 1 
ATOM   7452  C CZ  . TYR D  2 141 ? -65.937 -72.908  14.520  1.00 138.50 ? 141 TYR D CZ  1 
ATOM   7453  O OH  . TYR D  2 141 ? -66.006 -73.824  13.496  1.00 125.43 ? 141 TYR D OH  1 
ATOM   7454  N N   . HIS D  2 142 ? -65.425 -66.839  18.612  1.00 146.91 ? 142 HIS D N   1 
ATOM   7455  C CA  . HIS D  2 142 ? -65.216 -65.948  19.745  1.00 147.44 ? 142 HIS D CA  1 
ATOM   7456  C C   . HIS D  2 142 ? -65.568 -64.510  19.384  1.00 150.63 ? 142 HIS D C   1 
ATOM   7457  O O   . HIS D  2 142 ? -64.989 -63.927  18.467  1.00 159.84 ? 142 HIS D O   1 
ATOM   7458  C CB  . HIS D  2 142 ? -63.774 -66.063  20.248  1.00 147.09 ? 142 HIS D CB  1 
ATOM   7459  C CG  . HIS D  2 142 ? -62.950 -64.829  20.043  1.00 153.72 ? 142 HIS D CG  1 
ATOM   7460  N ND1 . HIS D  2 142 ? -62.784 -63.874  21.024  1.00 154.47 ? 142 HIS D ND1 1 
ATOM   7461  C CD2 . HIS D  2 142 ? -62.218 -64.408  18.984  1.00 153.31 ? 142 HIS D CD2 1 
ATOM   7462  C CE1 . HIS D  2 142 ? -61.997 -62.913  20.574  1.00 150.63 ? 142 HIS D CE1 1 
ATOM   7463  N NE2 . HIS D  2 142 ? -61.642 -63.211  19.338  1.00 155.78 ? 142 HIS D NE2 1 
ATOM   7464  N N   . LYS D  2 143 ? -66.536 -63.951  20.106  1.00 137.59 ? 143 LYS D N   1 
ATOM   7465  C CA  . LYS D  2 143 ? -67.014 -62.598  19.842  1.00 137.28 ? 143 LYS D CA  1 
ATOM   7466  C C   . LYS D  2 143 ? -65.860 -61.644  19.567  1.00 136.75 ? 143 LYS D C   1 
ATOM   7467  O O   . LYS D  2 143 ? -65.049 -61.360  20.448  1.00 128.11 ? 143 LYS D O   1 
ATOM   7468  C CB  . LYS D  2 143 ? -67.855 -62.083  21.011  1.00 134.87 ? 143 LYS D CB  1 
ATOM   7469  C CG  . LYS D  2 143 ? -69.208 -62.762  21.171  1.00 134.69 ? 143 LYS D CG  1 
ATOM   7470  C CD  . LYS D  2 143 ? -70.270 -62.133  20.277  1.00 140.91 ? 143 LYS D CD  1 
ATOM   7471  C CE  . LYS D  2 143 ? -70.186 -62.634  18.843  1.00 137.91 ? 143 LYS D CE  1 
ATOM   7472  N NZ  . LYS D  2 143 ? -71.245 -62.031  17.987  1.00 129.01 ? 143 LYS D NZ  1 
ATOM   7473  N N   . CYS D  2 144 ? -65.792 -61.156  18.334  1.00 152.68 ? 144 CYS D N   1 
ATOM   7474  C CA  . CYS D  2 144 ? -64.713 -60.269  17.927  1.00 161.97 ? 144 CYS D CA  1 
ATOM   7475  C C   . CYS D  2 144 ? -65.238 -58.886  17.561  1.00 155.39 ? 144 CYS D C   1 
ATOM   7476  O O   . CYS D  2 144 ? -65.732 -58.670  16.455  1.00 152.96 ? 144 CYS D O   1 
ATOM   7477  C CB  . CYS D  2 144 ? -63.941 -60.868  16.751  1.00 163.98 ? 144 CYS D CB  1 
ATOM   7478  S SG  . CYS D  2 144 ? -62.417 -59.990  16.341  1.00 169.31 ? 144 CYS D SG  1 
ATOM   7479  N N   . ASP D  2 145 ? -65.128 -57.955  18.502  1.00 177.96 ? 145 ASP D N   1 
ATOM   7480  C CA  . ASP D  2 145 ? -65.538 -56.575  18.270  1.00 181.26 ? 145 ASP D CA  1 
ATOM   7481  C C   . ASP D  2 145 ? -64.506 -55.806  17.444  1.00 170.65 ? 145 ASP D C   1 
ATOM   7482  O O   . ASP D  2 145 ? -63.628 -56.404  16.823  1.00 172.58 ? 145 ASP D O   1 
ATOM   7483  C CB  . ASP D  2 145 ? -65.833 -55.858  19.594  1.00 195.15 ? 145 ASP D CB  1 
ATOM   7484  C CG  . ASP D  2 145 ? -64.797 -56.146  20.666  1.00 192.67 ? 145 ASP D CG  1 
ATOM   7485  O OD1 . ASP D  2 145 ? -64.747 -55.387  21.656  1.00 183.43 ? 145 ASP D OD1 1 
ATOM   7486  O OD2 . ASP D  2 145 ? -64.036 -57.126  20.528  1.00 188.01 ? 145 ASP D OD2 1 
ATOM   7487  N N   . ASN D  2 146 ? -64.622 -54.481  17.437  1.00 143.20 ? 146 ASN D N   1 
ATOM   7488  C CA  . ASN D  2 146 ? -63.780 -53.631  16.595  1.00 135.18 ? 146 ASN D CA  1 
ATOM   7489  C C   . ASN D  2 146 ? -62.287 -53.713  16.900  1.00 144.52 ? 146 ASN D C   1 
ATOM   7490  O O   . ASN D  2 146 ? -61.463 -53.765  15.986  1.00 158.82 ? 146 ASN D O   1 
ATOM   7491  C CB  . ASN D  2 146 ? -64.244 -52.174  16.667  1.00 120.83 ? 146 ASN D CB  1 
ATOM   7492  C CG  . ASN D  2 146 ? -65.554 -51.944  15.943  1.00 121.60 ? 146 ASN D CG  1 
ATOM   7493  O OD1 . ASN D  2 146 ? -66.139 -50.864  16.022  1.00 118.83 ? 146 ASN D OD1 1 
ATOM   7494  N ND2 . ASN D  2 146 ? -66.022 -52.960  15.228  1.00 126.05 ? 146 ASN D ND2 1 
ATOM   7495  N N   . THR D  2 147 ? -61.939 -53.712  18.181  1.00 199.47 ? 147 THR D N   1 
ATOM   7496  C CA  . THR D  2 147 ? -60.539 -53.771  18.584  1.00 204.83 ? 147 THR D CA  1 
ATOM   7497  C C   . THR D  2 147 ? -60.010 -55.197  18.533  1.00 206.45 ? 147 THR D C   1 
ATOM   7498  O O   . THR D  2 147 ? -58.808 -55.428  18.655  1.00 204.47 ? 147 THR D O   1 
ATOM   7499  C CB  . THR D  2 147 ? -60.336 -53.230  19.997  1.00 196.59 ? 147 THR D CB  1 
ATOM   7500  O OG1 . THR D  2 147 ? -61.022 -54.075  20.928  1.00 205.78 ? 147 THR D OG1 1 
ATOM   7501  N N   . CYS D  2 148 ? -60.916 -56.155  18.377  1.00 160.59 ? 148 CYS D N   1 
ATOM   7502  C CA  . CYS D  2 148 ? -60.513 -57.527  18.124  1.00 159.89 ? 148 CYS D CA  1 
ATOM   7503  C C   . CYS D  2 148 ? -60.145 -57.613  16.653  1.00 164.42 ? 148 CYS D C   1 
ATOM   7504  O O   . CYS D  2 148 ? -59.100 -58.149  16.286  1.00 164.91 ? 148 CYS D O   1 
ATOM   7505  C CB  . CYS D  2 148 ? -61.652 -58.493  18.447  1.00 157.09 ? 148 CYS D CB  1 
ATOM   7506  S SG  . CYS D  2 148 ? -61.309 -60.218  18.029  1.00 152.22 ? 148 CYS D SG  1 
ATOM   7507  N N   . MET D  2 149 ? -61.015 -57.054  15.819  1.00 165.28 ? 149 MET D N   1 
ATOM   7508  C CA  . MET D  2 149 ? -60.797 -56.992  14.380  1.00 149.43 ? 149 MET D CA  1 
ATOM   7509  C C   . MET D  2 149 ? -59.462 -56.340  14.032  1.00 142.23 ? 149 MET D C   1 
ATOM   7510  O O   . MET D  2 149 ? -58.876 -56.630  12.990  1.00 132.19 ? 149 MET D O   1 
ATOM   7511  C CB  . MET D  2 149 ? -61.936 -56.221  13.710  1.00 142.81 ? 149 MET D CB  1 
ATOM   7512  C CG  . MET D  2 149 ? -63.274 -56.941  13.719  1.00 142.95 ? 149 MET D CG  1 
ATOM   7513  S SD  . MET D  2 149 ? -63.250 -58.456  12.744  1.00 133.24 ? 149 MET D SD  1 
ATOM   7514  C CE  . MET D  2 149 ? -64.990 -58.879  12.736  1.00 134.61 ? 149 MET D CE  1 
ATOM   7515  N N   . GLU D  2 150 ? -58.989 -55.458  14.907  1.00 174.93 ? 150 GLU D N   1 
ATOM   7516  C CA  . GLU D  2 150 ? -57.750 -54.726  14.664  1.00 178.10 ? 150 GLU D CA  1 
ATOM   7517  C C   . GLU D  2 150 ? -56.524 -55.607  14.882  1.00 180.16 ? 150 GLU D C   1 
ATOM   7518  O O   . GLU D  2 150 ? -55.574 -55.566  14.101  1.00 178.02 ? 150 GLU D O   1 
ATOM   7519  C CB  . GLU D  2 150 ? -57.669 -53.495  15.570  1.00 185.95 ? 150 GLU D CB  1 
ATOM   7520  C CG  . GLU D  2 150 ? -57.333 -52.197  14.847  1.00 192.93 ? 150 GLU D CG  1 
ATOM   7521  C CD  . GLU D  2 150 ? -58.557 -51.517  14.262  1.00 191.40 ? 150 GLU D CD  1 
ATOM   7522  O OE1 . GLU D  2 150 ? -58.505 -50.290  14.031  1.00 191.85 ? 150 GLU D OE1 1 
ATOM   7523  O OE2 . GLU D  2 150 ? -59.575 -52.206  14.042  1.00 185.19 ? 150 GLU D OE2 1 
ATOM   7524  N N   . SER D  2 151 ? -56.552 -56.398  15.951  1.00 177.08 ? 151 SER D N   1 
ATOM   7525  C CA  . SER D  2 151 ? -55.437 -57.277  16.288  1.00 172.09 ? 151 SER D CA  1 
ATOM   7526  C C   . SER D  2 151 ? -55.083 -58.180  15.114  1.00 163.79 ? 151 SER D C   1 
ATOM   7527  O O   . SER D  2 151 ? -53.939 -58.613  14.970  1.00 170.28 ? 151 SER D O   1 
ATOM   7528  C CB  . SER D  2 151 ? -55.776 -58.125  17.515  1.00 172.29 ? 151 SER D CB  1 
ATOM   7529  O OG  . SER D  2 151 ? -56.827 -59.033  17.235  1.00 168.92 ? 151 SER D OG  1 
ATOM   7530  N N   . VAL D  2 152 ? -56.074 -58.459  14.276  1.00 136.11 ? 152 VAL D N   1 
ATOM   7531  C CA  . VAL D  2 152 ? -55.866 -59.268  13.085  1.00 130.53 ? 152 VAL D CA  1 
ATOM   7532  C C   . VAL D  2 152 ? -55.199 -58.438  11.996  1.00 128.42 ? 152 VAL D C   1 
ATOM   7533  O O   . VAL D  2 152 ? -54.284 -58.905  11.321  1.00 116.13 ? 152 VAL D O   1 
ATOM   7534  C CB  . VAL D  2 152 ? -57.194 -59.813  12.541  1.00 116.71 ? 152 VAL D CB  1 
ATOM   7535  C CG1 . VAL D  2 152 ? -56.935 -60.898  11.507  1.00 92.84  ? 152 VAL D CG1 1 
ATOM   7536  C CG2 . VAL D  2 152 ? -58.050 -60.347  13.677  1.00 119.73 ? 152 VAL D CG2 1 
ATOM   7537  N N   . LYS D  2 153 ? -55.664 -57.205  11.828  1.00 129.12 ? 153 LYS D N   1 
ATOM   7538  C CA  . LYS D  2 153 ? -55.117 -56.313  10.810  1.00 124.04 ? 153 LYS D CA  1 
ATOM   7539  C C   . LYS D  2 153 ? -53.665 -55.956  11.114  1.00 144.86 ? 153 LYS D C   1 
ATOM   7540  O O   . LYS D  2 153 ? -52.771 -56.191  10.301  1.00 147.35 ? 153 LYS D O   1 
ATOM   7541  N N   . ASN D  2 154 ? -53.440 -55.384  12.293  1.00 187.47 ? 154 ASN D N   1 
ATOM   7542  C CA  . ASN D  2 154 ? -52.095 -55.067  12.760  1.00 203.47 ? 154 ASN D CA  1 
ATOM   7543  C C   . ASN D  2 154 ? -51.189 -56.295  12.797  1.00 204.58 ? 154 ASN D C   1 
ATOM   7544  O O   . ASN D  2 154 ? -49.972 -56.178  12.936  1.00 212.31 ? 154 ASN D O   1 
ATOM   7545  C CB  . ASN D  2 154 ? -52.156 -54.415  14.143  1.00 213.08 ? 154 ASN D CB  1 
ATOM   7546  C CG  . ASN D  2 154 ? -52.736 -53.016  14.100  1.00 217.53 ? 154 ASN D CG  1 
ATOM   7547  O OD1 . ASN D  2 154 ? -53.952 -52.831  14.145  1.00 221.33 ? 154 ASN D OD1 1 
ATOM   7548  N ND2 . ASN D  2 154 ? -51.863 -52.020  14.006  1.00 216.56 ? 154 ASN D ND2 1 
ATOM   7549  N N   . GLY D  2 155 ? -51.794 -57.471  12.665  1.00 161.79 ? 155 GLY D N   1 
ATOM   7550  C CA  . GLY D  2 155 ? -51.056 -58.719  12.689  1.00 153.81 ? 155 GLY D CA  1 
ATOM   7551  C C   . GLY D  2 155 ? -50.661 -59.105  14.100  1.00 158.69 ? 155 GLY D C   1 
ATOM   7552  O O   . GLY D  2 155 ? -49.950 -60.086  14.310  1.00 148.77 ? 155 GLY D O   1 
ATOM   7553  N N   . THR D  2 156 ? -51.125 -58.324  15.070  1.00 192.71 ? 156 THR D N   1 
ATOM   7554  C CA  . THR D  2 156 ? -50.839 -58.579  16.477  1.00 194.36 ? 156 THR D CA  1 
ATOM   7555  C C   . THR D  2 156 ? -52.040 -59.226  17.158  1.00 178.03 ? 156 THR D C   1 
ATOM   7556  O O   . THR D  2 156 ? -52.839 -58.547  17.803  1.00 178.16 ? 156 THR D O   1 
ATOM   7557  C CB  . THR D  2 156 ? -50.466 -57.279  17.215  1.00 205.62 ? 156 THR D CB  1 
ATOM   7558  O OG1 . THR D  2 156 ? -51.481 -56.292  16.992  1.00 203.34 ? 156 THR D OG1 1 
ATOM   7559  C CG2 . THR D  2 156 ? -49.135 -56.745  16.708  1.00 208.26 ? 156 THR D CG2 1 
ATOM   7560  N N   . TYR D  2 157 ? -52.158 -60.543  17.016  1.00 150.43 ? 157 TYR D N   1 
ATOM   7561  C CA  . TYR D  2 157 ? -53.338 -61.264  17.483  1.00 151.04 ? 157 TYR D CA  1 
ATOM   7562  C C   . TYR D  2 157 ? -53.014 -62.329  18.528  1.00 166.90 ? 157 TYR D C   1 
ATOM   7563  O O   . TYR D  2 157 ? -52.332 -63.314  18.238  1.00 157.99 ? 157 TYR D O   1 
ATOM   7564  C CB  . TYR D  2 157 ? -54.065 -61.904  16.298  1.00 133.90 ? 157 TYR D CB  1 
ATOM   7565  C CG  . TYR D  2 157 ? -55.334 -62.635  16.670  1.00 127.40 ? 157 TYR D CG  1 
ATOM   7566  C CD1 . TYR D  2 157 ? -56.578 -62.050  16.475  1.00 127.72 ? 157 TYR D CD1 1 
ATOM   7567  C CD2 . TYR D  2 157 ? -55.290 -63.913  17.214  1.00 124.47 ? 157 TYR D CD2 1 
ATOM   7568  C CE1 . TYR D  2 157 ? -57.742 -62.716  16.811  1.00 122.57 ? 157 TYR D CE1 1 
ATOM   7569  C CE2 . TYR D  2 157 ? -56.447 -64.586  17.554  1.00 128.67 ? 157 TYR D CE2 1 
ATOM   7570  C CZ  . TYR D  2 157 ? -57.670 -63.984  17.350  1.00 123.19 ? 157 TYR D CZ  1 
ATOM   7571  O OH  . TYR D  2 157 ? -58.825 -64.652  17.687  1.00 112.89 ? 157 TYR D OH  1 
ATOM   7572  N N   . ASP D  2 158 ? -53.528 -62.133  19.738  1.00 241.25 ? 158 ASP D N   1 
ATOM   7573  C CA  . ASP D  2 158 ? -53.285 -63.065  20.833  1.00 257.62 ? 158 ASP D CA  1 
ATOM   7574  C C   . ASP D  2 158 ? -54.141 -64.319  20.697  1.00 252.19 ? 158 ASP D C   1 
ATOM   7575  O O   . ASP D  2 158 ? -55.347 -64.248  20.455  1.00 239.71 ? 158 ASP D O   1 
ATOM   7576  C CB  . ASP D  2 158 ? -53.525 -62.383  22.181  1.00 267.72 ? 158 ASP D CB  1 
ATOM   7577  C CG  . ASP D  2 158 ? -53.426 -63.344  23.353  1.00 242.79 ? 158 ASP D CG  1 
ATOM   7578  O OD1 . ASP D  2 158 ? -54.460 -63.578  24.013  1.00 234.67 ? 158 ASP D OD1 1 
ATOM   7579  O OD2 . ASP D  2 158 ? -52.319 -63.857  23.622  1.00 230.57 ? 158 ASP D OD2 1 
ATOM   7580  N N   . TYR D  2 159 ? -53.500 -65.472  20.846  1.00 232.56 ? 159 TYR D N   1 
ATOM   7581  C CA  . TYR D  2 159 ? -54.176 -66.748  20.643  1.00 227.77 ? 159 TYR D CA  1 
ATOM   7582  C C   . TYR D  2 159 ? -54.892 -67.368  21.858  1.00 232.60 ? 159 TYR D C   1 
ATOM   7583  O O   . TYR D  2 159 ? -55.799 -68.176  21.676  1.00 228.60 ? 159 TYR D O   1 
ATOM   7584  C CB  . TYR D  2 159 ? -53.208 -67.800  20.086  1.00 217.29 ? 159 TYR D CB  1 
ATOM   7585  C CG  . TYR D  2 159 ? -53.909 -69.050  19.610  1.00 207.37 ? 159 TYR D CG  1 
ATOM   7586  C CD1 . TYR D  2 159 ? -53.648 -70.282  20.193  1.00 212.77 ? 159 TYR D CD1 1 
ATOM   7587  C CD2 . TYR D  2 159 ? -54.848 -68.995  18.587  1.00 193.38 ? 159 TYR D CD2 1 
ATOM   7588  C CE1 . TYR D  2 159 ? -54.295 -71.429  19.765  1.00 208.38 ? 159 TYR D CE1 1 
ATOM   7589  C CE2 . TYR D  2 159 ? -55.501 -70.137  18.153  1.00 188.98 ? 159 TYR D CE2 1 
ATOM   7590  C CZ  . TYR D  2 159 ? -55.220 -71.350  18.746  1.00 188.26 ? 159 TYR D CZ  1 
ATOM   7591  O OH  . TYR D  2 159 ? -55.866 -72.487  18.319  1.00 160.00 ? 159 TYR D OH  1 
ATOM   7592  N N   . PRO D  2 160 ? -54.480 -67.003  23.089  1.00 235.05 ? 160 PRO D N   1 
ATOM   7593  C CA  . PRO D  2 160 ? -55.130 -67.478  24.319  1.00 223.24 ? 160 PRO D CA  1 
ATOM   7594  C C   . PRO D  2 160 ? -56.556 -66.932  24.426  1.00 209.22 ? 160 PRO D C   1 
ATOM   7595  O O   . PRO D  2 160 ? -56.820 -66.058  25.252  1.00 200.69 ? 160 PRO D O   1 
ATOM   7596  C CB  . PRO D  2 160 ? -54.251 -66.870  25.413  1.00 189.05 ? 160 PRO D CB  1 
ATOM   7597  C CG  . PRO D  2 160 ? -52.887 -66.896  24.832  1.00 187.82 ? 160 PRO D CG  1 
ATOM   7598  C CD  . PRO D  2 160 ? -53.067 -66.614  23.362  1.00 223.91 ? 160 PRO D CD  1 
ATOM   7599  N N   . LYS D  2 161 ? -57.455 -67.450  23.593  1.00 188.83 ? 161 LYS D N   1 
ATOM   7600  C CA  . LYS D  2 161 ? -58.853 -67.024  23.571  1.00 165.78 ? 161 LYS D CA  1 
ATOM   7601  C C   . LYS D  2 161 ? -59.794 -68.115  23.056  1.00 156.37 ? 161 LYS D C   1 
ATOM   7602  O O   . LYS D  2 161 ? -60.948 -67.852  22.730  1.00 144.72 ? 161 LYS D O   1 
ATOM   7603  C CB  . LYS D  2 161 ? -59.009 -65.715  22.795  1.00 164.73 ? 161 LYS D CB  1 
ATOM   7604  C CG  . LYS D  2 161 ? -58.740 -64.455  23.603  1.00 152.28 ? 161 LYS D CG  1 
ATOM   7605  C CD  . LYS D  2 161 ? -59.523 -64.460  24.909  1.00 146.42 ? 161 LYS D CD  1 
ATOM   7606  C CE  . LYS D  2 161 ? -59.787 -63.049  25.413  1.00 121.00 ? 161 LYS D CE  1 
ATOM   7607  N NZ  . LYS D  2 161 ? -60.780 -62.333  24.562  1.00 103.37 ? 161 LYS D NZ  1 
ATOM   7608  N N   . TYR D  2 162 ? -59.292 -69.340  22.980  1.00 167.71 ? 162 TYR D N   1 
ATOM   7609  C CA  . TYR D  2 162 ? -60.090 -70.463  22.508  1.00 167.09 ? 162 TYR D CA  1 
ATOM   7610  C C   . TYR D  2 162 ? -61.371 -70.671  23.323  1.00 165.50 ? 162 TYR D C   1 
ATOM   7611  O O   . TYR D  2 162 ? -61.332 -70.717  24.554  1.00 173.50 ? 162 TYR D O   1 
ATOM   7612  C CB  . TYR D  2 162 ? -59.234 -71.729  22.485  1.00 156.91 ? 162 TYR D CB  1 
ATOM   7613  C CG  . TYR D  2 162 ? -59.935 -72.935  21.916  1.00 157.86 ? 162 TYR D CG  1 
ATOM   7614  C CD1 . TYR D  2 162 ? -59.904 -73.207  20.554  1.00 165.69 ? 162 TYR D CD1 1 
ATOM   7615  C CD2 . TYR D  2 162 ? -60.626 -73.807  22.742  1.00 148.27 ? 162 TYR D CD2 1 
ATOM   7616  C CE1 . TYR D  2 162 ? -60.547 -74.312  20.035  1.00 167.60 ? 162 TYR D CE1 1 
ATOM   7617  C CE2 . TYR D  2 162 ? -61.269 -74.911  22.234  1.00 146.46 ? 162 TYR D CE2 1 
ATOM   7618  C CZ  . TYR D  2 162 ? -61.228 -75.160  20.881  1.00 162.36 ? 162 TYR D CZ  1 
ATOM   7619  O OH  . TYR D  2 162 ? -61.872 -76.264  20.377  1.00 166.15 ? 162 TYR D OH  1 
ATOM   7620  N N   . ASP E  1 7   ? -62.340 -95.382  -0.230  1.00 149.04 ? 7   ASP E N   1 
ATOM   7621  C CA  . ASP E  1 7   ? -63.210 -94.365  -0.801  1.00 154.34 ? 7   ASP E CA  1 
ATOM   7622  C C   . ASP E  1 7   ? -62.504 -93.021  -0.733  1.00 148.19 ? 7   ASP E C   1 
ATOM   7623  O O   . ASP E  1 7   ? -63.124 -91.987  -0.515  1.00 142.87 ? 7   ASP E O   1 
ATOM   7624  C CB  . ASP E  1 7   ? -64.553 -94.351  -0.074  1.00 152.50 ? 7   ASP E CB  1 
ATOM   7625  C CG  . ASP E  1 7   ? -65.176 -95.737  0.008   1.00 153.02 ? 7   ASP E CG  1 
ATOM   7626  O OD1 . ASP E  1 7   ? -64.435 -96.731  -0.154  1.00 140.63 ? 7   ASP E OD1 1 
ATOM   7627  O OD2 . ASP E  1 7   ? -66.401 -95.838  0.227   1.00 150.65 ? 7   ASP E OD2 1 
ATOM   7628  N N   . THR E  1 8   ? -61.190 -93.060  -0.923  1.00 148.88 ? 8   THR E N   1 
ATOM   7629  C CA  . THR E  1 8   ? -60.362 -91.859  -0.919  1.00 152.87 ? 8   THR E CA  1 
ATOM   7630  C C   . THR E  1 8   ? -60.744 -90.878  -2.025  1.00 135.65 ? 8   THR E C   1 
ATOM   7631  O O   . THR E  1 8   ? -61.488 -91.228  -2.945  1.00 120.82 ? 8   THR E O   1 
ATOM   7632  C CB  . THR E  1 8   ? -58.868 -92.218  -1.086  1.00 139.18 ? 8   THR E CB  1 
ATOM   7633  O OG1 . THR E  1 8   ? -58.746 -93.577  -1.523  1.00 113.26 ? 8   THR E OG1 1 
ATOM   7634  C CG2 . THR E  1 8   ? -58.127 -92.055  0.229   1.00 135.52 ? 8   THR E CG2 1 
ATOM   7635  N N   . LEU E  1 9   ? -60.243 -89.647  -1.921  1.00 147.87 ? 9   LEU E N   1 
ATOM   7636  C CA  . LEU E  1 9   ? -60.240 -88.736  -3.063  1.00 140.25 ? 9   LEU E CA  1 
ATOM   7637  C C   . LEU E  1 9   ? -58.826 -88.368  -3.480  1.00 127.65 ? 9   LEU E C   1 
ATOM   7638  O O   . LEU E  1 9   ? -58.152 -87.523  -2.888  1.00 123.53 ? 9   LEU E O   1 
ATOM   7639  C CB  . LEU E  1 9   ? -61.090 -87.483  -2.863  1.00 123.93 ? 9   LEU E CB  1 
ATOM   7640  C CG  . LEU E  1 9   ? -62.121 -87.428  -3.996  1.00 96.93  ? 9   LEU E CG  1 
ATOM   7641  C CD1 . LEU E  1 9   ? -62.711 -86.048  -4.227  1.00 97.18  ? 9   LEU E CD1 1 
ATOM   7642  C CD2 . LEU E  1 9   ? -61.482 -87.958  -5.267  1.00 93.87  ? 9   LEU E CD2 1 
ATOM   7643  N N   . CYS E  1 10  ? -58.407 -89.046  -4.536  1.00 113.04 ? 10  CYS E N   1 
ATOM   7644  C CA  . CYS E  1 10  ? -57.107 -88.875  -5.153  1.00 108.74 ? 10  CYS E CA  1 
ATOM   7645  C C   . CYS E  1 10  ? -57.119 -87.715  -6.143  1.00 106.50 ? 10  CYS E C   1 
ATOM   7646  O O   . CYS E  1 10  ? -57.961 -87.668  -7.042  1.00 89.41  ? 10  CYS E O   1 
ATOM   7647  C CB  . CYS E  1 10  ? -56.759 -90.130  -5.924  1.00 109.01 ? 10  CYS E CB  1 
ATOM   7648  S SG  . CYS E  1 10  ? -55.637 -91.212  -5.053  1.00 137.88 ? 10  CYS E SG  1 
ATOM   7649  N N   . ILE E  1 11  ? -56.186 -86.780  -5.999  1.00 121.40 ? 11  ILE E N   1 
ATOM   7650  C CA  . ILE E  1 11  ? -56.025 -85.716  -6.988  1.00 104.41 ? 11  ILE E CA  1 
ATOM   7651  C C   . ILE E  1 11  ? -54.716 -85.879  -7.753  1.00 95.61  ? 11  ILE E C   1 
ATOM   7652  O O   . ILE E  1 11  ? -53.784 -86.527  -7.278  1.00 106.39 ? 11  ILE E O   1 
ATOM   7653  C CB  . ILE E  1 11  ? -56.096 -84.313  -6.337  1.00 99.50  ? 11  ILE E CB  1 
ATOM   7654  C CG1 . ILE E  1 11  ? -57.526 -83.763  -6.434  1.00 107.72 ? 11  ILE E CG1 1 
ATOM   7655  C CG2 . ILE E  1 11  ? -55.119 -83.361  -7.000  1.00 92.77  ? 11  ILE E CG2 1 
ATOM   7656  C CD1 . ILE E  1 11  ? -57.620 -82.242  -6.500  1.00 93.08  ? 11  ILE E CD1 1 
ATOM   7657  N N   . GLY E  1 12  ? -54.659 -85.303  -8.948  1.00 119.15 ? 12  GLY E N   1 
ATOM   7658  C CA  . GLY E  1 12  ? -53.422 -85.270  -9.698  1.00 116.77 ? 12  GLY E CA  1 
ATOM   7659  C C   . GLY E  1 12  ? -53.535 -84.695  -11.095 1.00 108.19 ? 12  GLY E C   1 
ATOM   7660  O O   . GLY E  1 12  ? -54.505 -84.017  -11.433 1.00 97.88  ? 12  GLY E O   1 
ATOM   7661  N N   . TYR E  1 13  ? -52.529 -84.982  -11.913 1.00 92.33  ? 13  TYR E N   1 
ATOM   7662  C CA  . TYR E  1 13  ? -52.455 -84.440  -13.262 1.00 84.68  ? 13  TYR E CA  1 
ATOM   7663  C C   . TYR E  1 13  ? -52.320 -85.530  -14.324 1.00 80.17  ? 13  TYR E C   1 
ATOM   7664  O O   . TYR E  1 13  ? -52.507 -86.714  -14.042 1.00 79.08  ? 13  TYR E O   1 
ATOM   7665  C CB  . TYR E  1 13  ? -51.296 -83.449  -13.360 1.00 71.60  ? 13  TYR E CB  1 
ATOM   7666  C CG  . TYR E  1 13  ? -50.090 -83.855  -12.546 1.00 69.34  ? 13  TYR E CG  1 
ATOM   7667  C CD1 . TYR E  1 13  ? -49.038 -84.546  -13.129 1.00 65.92  ? 13  TYR E CD1 1 
ATOM   7668  C CD2 . TYR E  1 13  ? -50.009 -83.556  -11.192 1.00 59.30  ? 13  TYR E CD2 1 
ATOM   7669  C CE1 . TYR E  1 13  ? -47.939 -84.921  -12.391 1.00 66.11  ? 13  TYR E CE1 1 
ATOM   7670  C CE2 . TYR E  1 13  ? -48.913 -83.929  -10.445 1.00 60.63  ? 13  TYR E CE2 1 
ATOM   7671  C CZ  . TYR E  1 13  ? -47.881 -84.611  -11.051 1.00 70.17  ? 13  TYR E CZ  1 
ATOM   7672  O OH  . TYR E  1 13  ? -46.782 -84.986  -10.320 1.00 71.07  ? 13  TYR E OH  1 
ATOM   7673  N N   . HIS E  1 14  ? -51.984 -85.113  -15.542 1.00 88.80  ? 14  HIS E N   1 
ATOM   7674  C CA  . HIS E  1 14  ? -51.947 -86.004  -16.701 1.00 72.38  ? 14  HIS E CA  1 
ATOM   7675  C C   . HIS E  1 14  ? -50.567 -86.606  -16.958 1.00 88.18  ? 14  HIS E C   1 
ATOM   7676  O O   . HIS E  1 14  ? -49.552 -86.091  -16.491 1.00 97.42  ? 14  HIS E O   1 
ATOM   7677  C CB  . HIS E  1 14  ? -52.419 -85.253  -17.952 1.00 87.72  ? 14  HIS E CB  1 
ATOM   7678  C CG  . HIS E  1 14  ? -52.536 -86.116  -19.170 1.00 96.25  ? 14  HIS E CG  1 
ATOM   7679  N ND1 . HIS E  1 14  ? -53.695 -86.784  -19.499 1.00 107.14 ? 14  HIS E ND1 1 
ATOM   7680  C CD2 . HIS E  1 14  ? -51.642 -86.417  -20.143 1.00 101.61 ? 14  HIS E CD2 1 
ATOM   7681  C CE1 . HIS E  1 14  ? -53.511 -87.462  -20.618 1.00 113.00 ? 14  HIS E CE1 1 
ATOM   7682  N NE2 . HIS E  1 14  ? -52.272 -87.256  -21.029 1.00 102.75 ? 14  HIS E NE2 1 
ATOM   7683  N N   . ALA E  1 15  ? -50.549 -87.703  -17.712 1.00 78.68  ? 15  ALA E N   1 
ATOM   7684  C CA  . ALA E  1 15  ? -49.314 -88.352  -18.140 1.00 80.17  ? 15  ALA E CA  1 
ATOM   7685  C C   . ALA E  1 15  ? -49.575 -89.150  -19.418 1.00 84.27  ? 15  ALA E C   1 
ATOM   7686  O O   . ALA E  1 15  ? -50.722 -89.480  -19.718 1.00 93.47  ? 15  ALA E O   1 
ATOM   7687  C CB  . ALA E  1 15  ? -48.782 -89.256  -17.043 1.00 75.21  ? 15  ALA E CB  1 
ATOM   7688  N N   . ASN E  1 16  ? -48.521 -89.457  -20.170 1.00 89.48  ? 16  ASN E N   1 
ATOM   7689  C CA  . ASN E  1 16  ? -48.680 -90.174  -21.437 1.00 102.95 ? 16  ASN E CA  1 
ATOM   7690  C C   . ASN E  1 16  ? -47.379 -90.749  -22.000 1.00 102.31 ? 16  ASN E C   1 
ATOM   7691  O O   . ASN E  1 16  ? -46.345 -90.740  -21.332 1.00 95.52  ? 16  ASN E O   1 
ATOM   7692  C CB  . ASN E  1 16  ? -49.339 -89.267  -22.478 1.00 104.46 ? 16  ASN E CB  1 
ATOM   7693  C CG  . ASN E  1 16  ? -48.567 -87.982  -22.702 1.00 101.23 ? 16  ASN E CG  1 
ATOM   7694  O OD1 . ASN E  1 16  ? -47.418 -87.853  -22.282 1.00 101.83 ? 16  ASN E OD1 1 
ATOM   7695  N ND2 . ASN E  1 16  ? -49.198 -87.021  -23.366 1.00 90.78  ? 16  ASN E ND2 1 
ATOM   7696  N N   . ASN E  1 17  ? -47.440 -91.247  -23.233 1.00 107.11 ? 17  ASN E N   1 
ATOM   7697  C CA  . ASN E  1 17  ? -46.264 -91.816  -23.887 1.00 110.81 ? 17  ASN E CA  1 
ATOM   7698  C C   . ASN E  1 17  ? -45.423 -90.776  -24.615 1.00 127.15 ? 17  ASN E C   1 
ATOM   7699  O O   . ASN E  1 17  ? -44.645 -91.110  -25.508 1.00 134.30 ? 17  ASN E O   1 
ATOM   7700  C CB  . ASN E  1 17  ? -46.655 -92.944  -24.849 1.00 133.60 ? 17  ASN E CB  1 
ATOM   7701  C CG  . ASN E  1 17  ? -47.613 -92.491  -25.937 1.00 144.21 ? 17  ASN E CG  1 
ATOM   7702  O OD1 . ASN E  1 17  ? -47.581 -91.345  -26.390 1.00 147.54 ? 17  ASN E OD1 1 
ATOM   7703  N ND2 . ASN E  1 17  ? -48.472 -93.406  -26.368 1.00 154.20 ? 17  ASN E ND2 1 
ATOM   7704  N N   . SER E  1 18  ? -45.578 -89.516  -24.225 1.00 114.58 ? 18  SER E N   1 
ATOM   7705  C CA  . SER E  1 18  ? -44.860 -88.428  -24.874 1.00 100.10 ? 18  SER E CA  1 
ATOM   7706  C C   . SER E  1 18  ? -43.369 -88.472  -24.559 1.00 93.58  ? 18  SER E C   1 
ATOM   7707  O O   . SER E  1 18  ? -42.968 -88.666  -23.410 1.00 85.38  ? 18  SER E O   1 
ATOM   7708  C CB  . SER E  1 18  ? -45.445 -87.075  -24.466 1.00 99.22  ? 18  SER E CB  1 
ATOM   7709  O OG  . SER E  1 18  ? -44.880 -86.024  -25.230 1.00 88.33  ? 18  SER E OG  1 
ATOM   7710  N N   . THR E  1 19  ? -42.553 -88.295  -25.592 1.00 104.01 ? 19  THR E N   1 
ATOM   7711  C CA  . THR E  1 19  ? -41.107 -88.242  -25.433 1.00 105.51 ? 19  THR E CA  1 
ATOM   7712  C C   . THR E  1 19  ? -40.609 -86.826  -25.693 1.00 94.84  ? 19  THR E C   1 
ATOM   7713  O O   . THR E  1 19  ? -39.412 -86.550  -25.610 1.00 93.02  ? 19  THR E O   1 
ATOM   7714  C CB  . THR E  1 19  ? -40.398 -89.220  -26.385 1.00 100.86 ? 19  THR E CB  1 
ATOM   7715  O OG1 . THR E  1 19  ? -40.832 -88.978  -27.729 1.00 106.22 ? 19  THR E OG1 1 
ATOM   7716  C CG2 . THR E  1 19  ? -40.720 -90.657  -26.007 1.00 107.32 ? 19  THR E CG2 1 
ATOM   7717  N N   . ASP E  1 20  ? -41.542 -85.933  -26.012 1.00 85.43  ? 20  ASP E N   1 
ATOM   7718  C CA  . ASP E  1 20  ? -41.221 -84.531  -26.241 1.00 79.58  ? 20  ASP E CA  1 
ATOM   7719  C C   . ASP E  1 20  ? -40.418 -83.963  -25.081 1.00 78.09  ? 20  ASP E C   1 
ATOM   7720  O O   . ASP E  1 20  ? -40.779 -84.139  -23.917 1.00 87.55  ? 20  ASP E O   1 
ATOM   7721  C CB  . ASP E  1 20  ? -42.498 -83.709  -26.426 1.00 86.88  ? 20  ASP E CB  1 
ATOM   7722  C CG  . ASP E  1 20  ? -43.217 -84.029  -27.720 1.00 91.16  ? 20  ASP E CG  1 
ATOM   7723  O OD1 . ASP E  1 20  ? -44.346 -83.530  -27.909 1.00 77.96  ? 20  ASP E OD1 1 
ATOM   7724  O OD2 . ASP E  1 20  ? -42.655 -84.776  -28.548 1.00 93.45  ? 20  ASP E OD2 1 
ATOM   7725  N N   . THR E  1 21  ? -39.324 -83.284  -25.404 1.00 72.11  ? 21  THR E N   1 
ATOM   7726  C CA  . THR E  1 21  ? -38.513 -82.630  -24.387 1.00 72.22  ? 21  THR E CA  1 
ATOM   7727  C C   . THR E  1 21  ? -38.319 -81.156  -24.711 1.00 62.52  ? 21  THR E C   1 
ATOM   7728  O O   . THR E  1 21  ? -38.069 -80.786  -25.859 1.00 74.94  ? 21  THR E O   1 
ATOM   7729  C CB  . THR E  1 21  ? -37.136 -83.302  -24.228 1.00 81.25  ? 21  THR E CB  1 
ATOM   7730  O OG1 . THR E  1 21  ? -36.531 -83.469  -25.516 1.00 97.10  ? 21  THR E OG1 1 
ATOM   7731  C CG2 . THR E  1 21  ? -37.280 -84.662  -23.558 1.00 77.38  ? 21  THR E CG2 1 
ATOM   7732  N N   . VAL E  1 22  ? -38.447 -80.317  -23.690 1.00 66.31  ? 22  VAL E N   1 
ATOM   7733  C CA  . VAL E  1 22  ? -38.219 -78.890  -23.843 1.00 57.70  ? 22  VAL E CA  1 
ATOM   7734  C C   . VAL E  1 22  ? -37.174 -78.432  -22.836 1.00 61.78  ? 22  VAL E C   1 
ATOM   7735  O O   . VAL E  1 22  ? -36.828 -79.167  -21.911 1.00 67.98  ? 22  VAL E O   1 
ATOM   7736  C CB  . VAL E  1 22  ? -39.509 -78.080  -23.624 1.00 50.76  ? 22  VAL E CB  1 
ATOM   7737  C CG1 . VAL E  1 22  ? -40.652 -78.677  -24.427 1.00 54.84  ? 22  VAL E CG1 1 
ATOM   7738  C CG2 . VAL E  1 22  ? -39.861 -78.031  -22.146 1.00 43.64  ? 22  VAL E CG2 1 
ATOM   7739  N N   . ASP E  1 23  ? -36.669 -77.220  -23.023 1.00 55.26  ? 23  ASP E N   1 
ATOM   7740  C CA  . ASP E  1 23  ? -35.731 -76.636  -22.075 1.00 52.84  ? 23  ASP E CA  1 
ATOM   7741  C C   . ASP E  1 23  ? -36.368 -75.452  -21.362 1.00 53.43  ? 23  ASP E C   1 
ATOM   7742  O O   . ASP E  1 23  ? -37.212 -74.755  -21.925 1.00 61.07  ? 23  ASP E O   1 
ATOM   7743  C CB  . ASP E  1 23  ? -34.448 -76.194  -22.781 1.00 67.90  ? 23  ASP E CB  1 
ATOM   7744  C CG  . ASP E  1 23  ? -33.583 -77.361  -23.210 1.00 78.19  ? 23  ASP E CG  1 
ATOM   7745  O OD1 . ASP E  1 23  ? -34.005 -78.521  -23.019 1.00 86.20  ? 23  ASP E OD1 1 
ATOM   7746  O OD2 . ASP E  1 23  ? -32.476 -77.117  -23.736 1.00 85.46  ? 23  ASP E OD2 1 
ATOM   7747  N N   . THR E  1 24  ? -35.967 -75.239  -20.115 1.00 50.49  ? 24  THR E N   1 
ATOM   7748  C CA  . THR E  1 24  ? -36.404 -74.078  -19.357 1.00 57.25  ? 24  THR E CA  1 
ATOM   7749  C C   . THR E  1 24  ? -35.176 -73.296  -18.925 1.00 54.72  ? 24  THR E C   1 
ATOM   7750  O O   . THR E  1 24  ? -34.050 -73.667  -19.251 1.00 46.47  ? 24  THR E O   1 
ATOM   7751  C CB  . THR E  1 24  ? -37.209 -74.478  -18.108 1.00 68.27  ? 24  THR E CB  1 
ATOM   7752  O OG1 . THR E  1 24  ? -36.341 -75.104  -17.155 1.00 67.01  ? 24  THR E OG1 1 
ATOM   7753  C CG2 . THR E  1 24  ? -38.332 -75.437  -18.477 1.00 58.49  ? 24  THR E CG2 1 
ATOM   7754  N N   . VAL E  1 25  ? -35.392 -72.213  -18.190 1.00 64.57  ? 25  VAL E N   1 
ATOM   7755  C CA  . VAL E  1 25  ? -34.287 -71.412  -17.691 1.00 62.83  ? 25  VAL E CA  1 
ATOM   7756  C C   . VAL E  1 25  ? -33.545 -72.191  -16.616 1.00 62.26  ? 25  VAL E C   1 
ATOM   7757  O O   . VAL E  1 25  ? -32.324 -72.098  -16.492 1.00 51.84  ? 25  VAL E O   1 
ATOM   7758  C CB  . VAL E  1 25  ? -34.788 -70.094  -17.084 1.00 54.67  ? 25  VAL E CB  1 
ATOM   7759  C CG1 . VAL E  1 25  ? -33.694 -69.041  -17.129 1.00 52.79  ? 25  VAL E CG1 1 
ATOM   7760  C CG2 . VAL E  1 25  ? -36.019 -69.613  -17.826 1.00 60.58  ? 25  VAL E CG2 1 
ATOM   7761  N N   . LEU E  1 26  ? -34.296 -72.976  -15.850 1.00 62.34  ? 26  LEU E N   1 
ATOM   7762  C CA  . LEU E  1 26  ? -33.755 -73.653  -14.679 1.00 62.08  ? 26  LEU E CA  1 
ATOM   7763  C C   . LEU E  1 26  ? -33.359 -75.102  -14.944 1.00 63.63  ? 26  LEU E C   1 
ATOM   7764  O O   . LEU E  1 26  ? -32.570 -75.677  -14.195 1.00 69.15  ? 26  LEU E O   1 
ATOM   7765  C CB  . LEU E  1 26  ? -34.766 -73.604  -13.533 1.00 53.60  ? 26  LEU E CB  1 
ATOM   7766  C CG  . LEU E  1 26  ? -35.398 -72.235  -13.275 1.00 60.67  ? 26  LEU E CG  1 
ATOM   7767  C CD1 . LEU E  1 26  ? -36.391 -72.308  -12.125 1.00 45.78  ? 26  LEU E CD1 1 
ATOM   7768  C CD2 . LEU E  1 26  ? -34.339 -71.165  -13.027 1.00 67.14  ? 26  LEU E CD2 1 
ATOM   7769  N N   . GLU E  1 27  ? -33.901 -75.691  -16.004 1.00 71.06  ? 27  GLU E N   1 
ATOM   7770  C CA  . GLU E  1 27  ? -33.697 -77.116  -16.249 1.00 64.64  ? 27  GLU E CA  1 
ATOM   7771  C C   . GLU E  1 27  ? -33.613 -77.458  -17.737 1.00 68.66  ? 27  GLU E C   1 
ATOM   7772  O O   . GLU E  1 27  ? -34.284 -76.844  -18.567 1.00 63.96  ? 27  GLU E O   1 
ATOM   7773  C CB  . GLU E  1 27  ? -34.814 -77.919  -15.579 1.00 72.39  ? 27  GLU E CB  1 
ATOM   7774  C CG  . GLU E  1 27  ? -34.464 -79.365  -15.278 1.00 90.44  ? 27  GLU E CG  1 
ATOM   7775  C CD  . GLU E  1 27  ? -35.456 -80.011  -14.330 1.00 109.55 ? 27  GLU E CD  1 
ATOM   7776  O OE1 . GLU E  1 27  ? -35.484 -81.257  -14.249 1.00 104.33 ? 27  GLU E OE1 1 
ATOM   7777  O OE2 . GLU E  1 27  ? -36.211 -79.269  -13.666 1.00 106.51 ? 27  GLU E OE2 1 
ATOM   7778  N N   . LYS E  1 28  ? -32.780 -78.443  -18.064 1.00 71.83  ? 28  LYS E N   1 
ATOM   7779  C CA  . LYS E  1 28  ? -32.612 -78.892  -19.444 1.00 68.87  ? 28  LYS E CA  1 
ATOM   7780  C C   . LYS E  1 28  ? -33.312 -80.224  -19.702 1.00 76.30  ? 28  LYS E C   1 
ATOM   7781  O O   . LYS E  1 28  ? -33.580 -80.986  -18.773 1.00 83.50  ? 28  LYS E O   1 
ATOM   7782  C CB  . LYS E  1 28  ? -31.127 -79.009  -19.797 1.00 69.40  ? 28  LYS E CB  1 
ATOM   7783  C CG  . LYS E  1 28  ? -30.503 -77.728  -20.328 1.00 73.88  ? 28  LYS E CG  1 
ATOM   7784  C CD  . LYS E  1 28  ? -29.036 -77.933  -20.675 1.00 80.24  ? 28  LYS E CD  1 
ATOM   7785  C CE  . LYS E  1 28  ? -28.520 -76.825  -21.581 1.00 95.79  ? 28  LYS E CE  1 
ATOM   7786  N NZ  . LYS E  1 28  ? -28.757 -75.472  -21.007 1.00 94.72  ? 28  LYS E NZ  1 
ATOM   7787  N N   . ASN E  1 29  ? -33.597 -80.494  -20.973 1.00 79.43  ? 29  ASN E N   1 
ATOM   7788  C CA  . ASN E  1 29  ? -34.252 -81.734  -21.388 1.00 73.90  ? 29  ASN E CA  1 
ATOM   7789  C C   . ASN E  1 29  ? -35.324 -82.230  -20.421 1.00 78.72  ? 29  ASN E C   1 
ATOM   7790  O O   . ASN E  1 29  ? -35.190 -83.295  -19.818 1.00 85.27  ? 29  ASN E O   1 
ATOM   7791  C CB  . ASN E  1 29  ? -33.218 -82.831  -21.654 1.00 75.94  ? 29  ASN E CB  1 
ATOM   7792  C CG  . ASN E  1 29  ? -32.508 -82.648  -22.981 1.00 108.71 ? 29  ASN E CG  1 
ATOM   7793  O OD1 . ASN E  1 29  ? -33.110 -82.799  -24.045 1.00 105.85 ? 29  ASN E OD1 1 
ATOM   7794  N ND2 . ASN E  1 29  ? -31.222 -82.319  -22.927 1.00 109.68 ? 29  ASN E ND2 1 
ATOM   7795  N N   . VAL E  1 30  ? -36.387 -81.447  -20.281 1.00 72.52  ? 30  VAL E N   1 
ATOM   7796  C CA  . VAL E  1 30  ? -37.512 -81.826  -19.438 1.00 58.46  ? 30  VAL E CA  1 
ATOM   7797  C C   . VAL E  1 30  ? -38.613 -82.455  -20.283 1.00 68.11  ? 30  VAL E C   1 
ATOM   7798  O O   . VAL E  1 30  ? -39.137 -81.829  -21.204 1.00 67.35  ? 30  VAL E O   1 
ATOM   7799  C CB  . VAL E  1 30  ? -38.079 -80.614  -18.676 1.00 61.00  ? 30  VAL E CB  1 
ATOM   7800  C CG1 . VAL E  1 30  ? -39.366 -80.989  -17.957 1.00 52.04  ? 30  VAL E CG1 1 
ATOM   7801  C CG2 . VAL E  1 30  ? -37.045 -80.074  -17.696 1.00 65.36  ? 30  VAL E CG2 1 
ATOM   7802  N N   . THR E  1 31  ? -38.956 -83.701  -19.977 1.00 78.00  ? 31  THR E N   1 
ATOM   7803  C CA  . THR E  1 31  ? -40.002 -84.381  -20.729 1.00 69.04  ? 31  THR E CA  1 
ATOM   7804  C C   . THR E  1 31  ? -41.370 -83.786  -20.395 1.00 63.07  ? 31  THR E C   1 
ATOM   7805  O O   . THR E  1 31  ? -41.702 -83.553  -19.226 1.00 68.88  ? 31  THR E O   1 
ATOM   7806  C CB  . THR E  1 31  ? -39.984 -85.905  -20.509 1.00 75.78  ? 31  THR E CB  1 
ATOM   7807  O OG1 . THR E  1 31  ? -38.712 -86.429  -20.908 1.00 74.77  ? 31  THR E OG1 1 
ATOM   7808  C CG2 . THR E  1 31  ? -41.069 -86.580  -21.333 1.00 68.55  ? 31  THR E CG2 1 
ATOM   7809  N N   . VAL E  1 32  ? -42.148 -83.536  -21.445 1.00 72.71  ? 32  VAL E N   1 
ATOM   7810  C CA  . VAL E  1 32  ? -43.374 -82.763  -21.346 1.00 72.00  ? 32  VAL E CA  1 
ATOM   7811  C C   . VAL E  1 32  ? -44.506 -83.436  -22.114 1.00 66.60  ? 32  VAL E C   1 
ATOM   7812  O O   . VAL E  1 32  ? -44.270 -84.041  -23.158 1.00 72.23  ? 32  VAL E O   1 
ATOM   7813  C CB  . VAL E  1 32  ? -43.131 -81.354  -21.904 1.00 65.32  ? 32  VAL E CB  1 
ATOM   7814  C CG1 . VAL E  1 32  ? -43.820 -81.191  -23.255 1.00 61.06  ? 32  VAL E CG1 1 
ATOM   7815  C CG2 . VAL E  1 32  ? -43.548 -80.289  -20.882 1.00 58.21  ? 32  VAL E CG2 1 
ATOM   7816  N N   . THR E  1 33  ? -45.727 -83.340  -21.591 1.00 72.38  ? 33  THR E N   1 
ATOM   7817  C CA  . THR E  1 33  ? -46.852 -84.079  -22.157 1.00 65.90  ? 33  THR E CA  1 
ATOM   7818  C C   . THR E  1 33  ? -47.206 -83.613  -23.563 1.00 71.94  ? 33  THR E C   1 
ATOM   7819  O O   . THR E  1 33  ? -47.507 -84.424  -24.438 1.00 83.19  ? 33  THR E O   1 
ATOM   7820  C CB  . THR E  1 33  ? -48.109 -84.003  -21.268 1.00 74.20  ? 33  THR E CB  1 
ATOM   7821  O OG1 . THR E  1 33  ? -48.526 -82.639  -21.135 1.00 77.25  ? 33  THR E OG1 1 
ATOM   7822  C CG2 . THR E  1 33  ? -47.827 -84.591  -19.895 1.00 76.18  ? 33  THR E CG2 1 
ATOM   7823  N N   . HIS E  1 34  ? -47.164 -82.304  -23.777 1.00 78.86  ? 34  HIS E N   1 
ATOM   7824  C CA  . HIS E  1 34  ? -47.521 -81.731  -25.067 1.00 71.98  ? 34  HIS E CA  1 
ATOM   7825  C C   . HIS E  1 34  ? -46.639 -80.528  -25.364 1.00 72.91  ? 34  HIS E C   1 
ATOM   7826  O O   . HIS E  1 34  ? -46.155 -79.867  -24.448 1.00 72.38  ? 34  HIS E O   1 
ATOM   7827  C CB  . HIS E  1 34  ? -48.990 -81.305  -25.073 1.00 72.63  ? 34  HIS E CB  1 
ATOM   7828  C CG  . HIS E  1 34  ? -49.945 -82.417  -24.768 1.00 85.84  ? 34  HIS E CG  1 
ATOM   7829  N ND1 . HIS E  1 34  ? -50.132 -82.908  -23.495 1.00 79.89  ? 34  HIS E ND1 1 
ATOM   7830  C CD2 . HIS E  1 34  ? -50.774 -83.126  -25.571 1.00 89.18  ? 34  HIS E CD2 1 
ATOM   7831  C CE1 . HIS E  1 34  ? -51.029 -83.878  -23.526 1.00 88.88  ? 34  HIS E CE1 1 
ATOM   7832  N NE2 . HIS E  1 34  ? -51.435 -84.029  -24.774 1.00 100.41 ? 34  HIS E NE2 1 
ATOM   7833  N N   . SER E  1 35  ? -46.437 -80.243  -26.645 1.00 69.94  ? 35  SER E N   1 
ATOM   7834  C CA  . SER E  1 35  ? -45.628 -79.101  -27.047 1.00 62.28  ? 35  SER E CA  1 
ATOM   7835  C C   . SER E  1 35  ? -45.797 -78.781  -28.527 1.00 60.29  ? 35  SER E C   1 
ATOM   7836  O O   . SER E  1 35  ? -46.376 -79.562  -29.282 1.00 65.35  ? 35  SER E O   1 
ATOM   7837  C CB  . SER E  1 35  ? -44.151 -79.340  -26.714 1.00 65.60  ? 35  SER E CB  1 
ATOM   7838  O OG  . SER E  1 35  ? -43.737 -80.637  -27.107 1.00 76.34  ? 35  SER E OG  1 
ATOM   7839  N N   . VAL E  1 36  ? -45.295 -77.618  -28.927 1.00 68.23  ? 36  VAL E N   1 
ATOM   7840  C CA  . VAL E  1 36  ? -45.350 -77.188  -30.316 1.00 63.01  ? 36  VAL E CA  1 
ATOM   7841  C C   . VAL E  1 36  ? -43.997 -76.632  -30.731 1.00 61.75  ? 36  VAL E C   1 
ATOM   7842  O O   . VAL E  1 36  ? -43.231 -76.156  -29.894 1.00 65.43  ? 36  VAL E O   1 
ATOM   7843  C CB  . VAL E  1 36  ? -46.414 -76.097  -30.528 1.00 54.86  ? 36  VAL E CB  1 
ATOM   7844  C CG1 . VAL E  1 36  ? -47.783 -76.601  -30.103 1.00 64.21  ? 36  VAL E CG1 1 
ATOM   7845  C CG2 . VAL E  1 36  ? -46.042 -74.839  -29.757 1.00 58.44  ? 36  VAL E CG2 1 
ATOM   7846  N N   . ASN E  1 37  ? -43.701 -76.695  -32.022 1.00 66.24  ? 37  ASN E N   1 
ATOM   7847  C CA  . ASN E  1 37  ? -42.453 -76.143  -32.527 1.00 63.43  ? 37  ASN E CA  1 
ATOM   7848  C C   . ASN E  1 37  ? -42.664 -74.750  -33.108 1.00 57.46  ? 37  ASN E C   1 
ATOM   7849  O O   . ASN E  1 37  ? -43.504 -74.556  -33.986 1.00 61.08  ? 37  ASN E O   1 
ATOM   7850  C CB  . ASN E  1 37  ? -41.832 -77.071  -33.571 1.00 61.51  ? 37  ASN E CB  1 
ATOM   7851  C CG  . ASN E  1 37  ? -40.360 -76.794  -33.786 1.00 69.68  ? 37  ASN E CG  1 
ATOM   7852  O OD1 . ASN E  1 37  ? -39.729 -77.366  -34.676 1.00 81.59  ? 37  ASN E OD1 1 
ATOM   7853  N ND2 . ASN E  1 37  ? -39.802 -75.911  -32.965 1.00 57.70  ? 37  ASN E ND2 1 
ATOM   7854  N N   . LEU E  1 38  ? -41.907 -73.781  -32.606 1.00 56.25  ? 38  LEU E N   1 
ATOM   7855  C CA  . LEU E  1 38  ? -42.007 -72.406  -33.081 1.00 45.93  ? 38  LEU E CA  1 
ATOM   7856  C C   . LEU E  1 38  ? -41.054 -72.162  -34.243 1.00 48.89  ? 38  LEU E C   1 
ATOM   7857  O O   . LEU E  1 38  ? -41.095 -71.112  -34.885 1.00 51.63  ? 38  LEU E O   1 
ATOM   7858  C CB  . LEU E  1 38  ? -41.713 -71.422  -31.945 1.00 37.08  ? 38  LEU E CB  1 
ATOM   7859  C CG  . LEU E  1 38  ? -42.747 -71.336  -30.819 1.00 40.42  ? 38  LEU E CG  1 
ATOM   7860  C CD1 . LEU E  1 38  ? -42.187 -70.573  -29.627 1.00 64.76  ? 38  LEU E CD1 1 
ATOM   7861  C CD2 . LEU E  1 38  ? -44.035 -70.695  -31.314 1.00 45.16  ? 38  LEU E CD2 1 
ATOM   7862  N N   . LEU E  1 39  ? -40.199 -73.143  -34.511 1.00 49.02  ? 39  LEU E N   1 
ATOM   7863  C CA  . LEU E  1 39  ? -39.198 -73.020  -35.563 1.00 52.02  ? 39  LEU E CA  1 
ATOM   7864  C C   . LEU E  1 39  ? -39.572 -73.810  -36.811 1.00 62.64  ? 39  LEU E C   1 
ATOM   7865  O O   . LEU E  1 39  ? -39.732 -75.030  -36.763 1.00 67.97  ? 39  LEU E O   1 
ATOM   7866  C CB  . LEU E  1 39  ? -37.832 -73.479  -35.053 1.00 45.87  ? 39  LEU E CB  1 
ATOM   7867  C CG  . LEU E  1 39  ? -36.717 -73.501  -36.098 1.00 53.06  ? 39  LEU E CG  1 
ATOM   7868  C CD1 . LEU E  1 39  ? -36.507 -72.117  -36.693 1.00 56.12  ? 39  LEU E CD1 1 
ATOM   7869  C CD2 . LEU E  1 39  ? -35.433 -74.037  -35.490 1.00 53.93  ? 39  LEU E CD2 1 
ATOM   7870  N N   . GLU E  1 40  ? -39.706 -73.105  -37.929 1.00 64.97  ? 40  GLU E N   1 
ATOM   7871  C CA  . GLU E  1 40  ? -39.957 -73.750  -39.210 1.00 57.07  ? 40  GLU E CA  1 
ATOM   7872  C C   . GLU E  1 40  ? -38.637 -74.174  -39.844 1.00 59.92  ? 40  GLU E C   1 
ATOM   7873  O O   . GLU E  1 40  ? -37.722 -73.365  -39.997 1.00 57.65  ? 40  GLU E O   1 
ATOM   7874  C CB  . GLU E  1 40  ? -40.721 -72.813  -40.147 1.00 48.87  ? 40  GLU E CB  1 
ATOM   7875  C CG  . GLU E  1 40  ? -41.040 -73.415  -41.508 1.00 61.88  ? 40  GLU E CG  1 
ATOM   7876  C CD  . GLU E  1 40  ? -41.937 -74.636  -41.416 1.00 78.00  ? 40  GLU E CD  1 
ATOM   7877  O OE1 . GLU E  1 40  ? -43.093 -74.560  -41.882 1.00 86.11  ? 40  GLU E OE1 1 
ATOM   7878  O OE2 . GLU E  1 40  ? -41.489 -75.672  -40.879 1.00 75.13  ? 40  GLU E OE2 1 
ATOM   7879  N N   . ASP E  1 41  ? -38.545 -75.448  -40.205 1.00 65.02  ? 41  ASP E N   1 
ATOM   7880  C CA  . ASP E  1 41  ? -37.323 -75.998  -40.776 1.00 67.49  ? 41  ASP E CA  1 
ATOM   7881  C C   . ASP E  1 41  ? -37.642 -76.883  -41.972 1.00 68.54  ? 41  ASP E C   1 
ATOM   7882  O O   . ASP E  1 41  ? -36.978 -77.893  -42.203 1.00 87.23  ? 41  ASP E O   1 
ATOM   7883  C CB  . ASP E  1 41  ? -36.561 -76.802  -39.720 1.00 80.49  ? 41  ASP E CB  1 
ATOM   7884  C CG  . ASP E  1 41  ? -37.417 -77.878  -39.074 1.00 96.23  ? 41  ASP E CG  1 
ATOM   7885  O OD1 . ASP E  1 41  ? -38.589 -78.036  -39.476 1.00 86.70  ? 41  ASP E OD1 1 
ATOM   7886  O OD2 . ASP E  1 41  ? -36.916 -78.566  -38.160 1.00 96.46  ? 41  ASP E OD2 1 
ATOM   7887  N N   . LYS E  1 42  ? -38.661 -76.497  -42.732 1.00 67.51  ? 42  LYS E N   1 
ATOM   7888  C CA  . LYS E  1 42  ? -39.131 -77.320  -43.838 1.00 77.22  ? 42  LYS E CA  1 
ATOM   7889  C C   . LYS E  1 42  ? -39.643 -76.479  -45.001 1.00 76.31  ? 42  LYS E C   1 
ATOM   7890  O O   . LYS E  1 42  ? -40.645 -75.775  -44.881 1.00 64.70  ? 42  LYS E O   1 
ATOM   7891  C CB  . LYS E  1 42  ? -40.228 -78.266  -43.353 1.00 84.47  ? 42  LYS E CB  1 
ATOM   7892  C CG  . LYS E  1 42  ? -40.091 -79.692  -43.853 1.00 115.46 ? 42  LYS E CG  1 
ATOM   7893  C CD  . LYS E  1 42  ? -40.859 -80.643  -42.953 1.00 129.23 ? 42  LYS E CD  1 
ATOM   7894  C CE  . LYS E  1 42  ? -40.369 -80.533  -41.517 1.00 113.67 ? 42  LYS E CE  1 
ATOM   7895  N NZ  . LYS E  1 42  ? -41.179 -81.359  -40.582 1.00 117.77 ? 42  LYS E NZ  1 
ATOM   7896  N N   . HIS E  1 43  ? -38.944 -76.562  -46.126 1.00 63.99  ? 43  HIS E N   1 
ATOM   7897  C CA  . HIS E  1 43  ? -39.344 -75.858  -47.335 1.00 58.57  ? 43  HIS E CA  1 
ATOM   7898  C C   . HIS E  1 43  ? -39.807 -76.868  -48.379 1.00 70.69  ? 43  HIS E C   1 
ATOM   7899  O O   . HIS E  1 43  ? -39.446 -78.042  -48.314 1.00 81.86  ? 43  HIS E O   1 
ATOM   7900  C CB  . HIS E  1 43  ? -38.171 -75.046  -47.878 1.00 56.96  ? 43  HIS E CB  1 
ATOM   7901  C CG  . HIS E  1 43  ? -36.973 -75.873  -48.215 1.00 61.44  ? 43  HIS E CG  1 
ATOM   7902  N ND1 . HIS E  1 43  ? -36.666 -76.248  -49.506 1.00 72.03  ? 43  HIS E ND1 1 
ATOM   7903  C CD2 . HIS E  1 43  ? -36.008 -76.411  -47.430 1.00 60.99  ? 43  HIS E CD2 1 
ATOM   7904  C CE1 . HIS E  1 43  ? -35.563 -76.971  -49.502 1.00 78.17  ? 43  HIS E CE1 1 
ATOM   7905  N NE2 . HIS E  1 43  ? -35.144 -77.087  -48.254 1.00 77.41  ? 43  HIS E NE2 1 
ATOM   7906  N N   . ASN E  1 44  ? -40.606 -76.412  -49.338 1.00 65.10  ? 44  ASN E N   1 
ATOM   7907  C CA  . ASN E  1 44  ? -41.127 -77.302  -50.371 1.00 61.74  ? 44  ASN E CA  1 
ATOM   7908  C C   . ASN E  1 44  ? -40.134 -77.535  -51.505 1.00 59.42  ? 44  ASN E C   1 
ATOM   7909  O O   . ASN E  1 44  ? -40.397 -78.303  -52.430 1.00 59.58  ? 44  ASN E O   1 
ATOM   7910  C CB  . ASN E  1 44  ? -42.460 -76.786  -50.921 1.00 56.12  ? 44  ASN E CB  1 
ATOM   7911  C CG  . ASN E  1 44  ? -42.332 -75.436  -51.602 1.00 65.76  ? 44  ASN E CG  1 
ATOM   7912  O OD1 . ASN E  1 44  ? -43.329 -74.850  -52.026 1.00 66.48  ? 44  ASN E OD1 1 
ATOM   7913  N ND2 . ASN E  1 44  ? -41.108 -74.934  -51.711 1.00 70.92  ? 44  ASN E ND2 1 
ATOM   7914  N N   . GLY E  1 45  ? -38.992 -76.862  -51.422 1.00 64.05  ? 45  GLY E N   1 
ATOM   7915  C CA  . GLY E  1 45  ? -37.945 -77.003  -52.414 1.00 67.88  ? 45  GLY E CA  1 
ATOM   7916  C C   . GLY E  1 45  ? -38.381 -76.643  -53.817 1.00 68.74  ? 45  GLY E C   1 
ATOM   7917  O O   . GLY E  1 45  ? -37.887 -77.200  -54.798 1.00 66.93  ? 45  GLY E O   1 
ATOM   7918  N N   . LYS E  1 46  ? -39.316 -75.707  -53.907 1.00 72.40  ? 46  LYS E N   1 
ATOM   7919  C CA  . LYS E  1 46  ? -39.768 -75.195  -55.188 1.00 68.13  ? 46  LYS E CA  1 
ATOM   7920  C C   . LYS E  1 46  ? -39.559 -73.689  -55.221 1.00 61.16  ? 46  LYS E C   1 
ATOM   7921  O O   . LYS E  1 46  ? -39.781 -73.008  -54.220 1.00 64.40  ? 46  LYS E O   1 
ATOM   7922  C CB  . LYS E  1 46  ? -41.253 -75.498  -55.385 1.00 74.49  ? 46  LYS E CB  1 
ATOM   7923  C CG  . LYS E  1 46  ? -41.607 -76.974  -55.427 1.00 77.77  ? 46  LYS E CG  1 
ATOM   7924  C CD  . LYS E  1 46  ? -43.114 -77.156  -55.344 1.00 101.74 ? 46  LYS E CD  1 
ATOM   7925  C CE  . LYS E  1 46  ? -43.520 -78.605  -55.543 1.00 115.41 ? 46  LYS E CE  1 
ATOM   7926  N NZ  . LYS E  1 46  ? -44.986 -78.777  -55.347 1.00 116.15 ? 46  LYS E NZ  1 
ATOM   7927  N N   . LEU E  1 47  ? -39.121 -73.170  -56.361 1.00 63.82  ? 47  LEU E N   1 
ATOM   7928  C CA  . LEU E  1 47  ? -39.128 -71.729  -56.575 1.00 61.52  ? 47  LEU E CA  1 
ATOM   7929  C C   . LEU E  1 47  ? -40.517 -71.321  -57.041 1.00 54.85  ? 47  LEU E C   1 
ATOM   7930  O O   . LEU E  1 47  ? -40.821 -71.379  -58.231 1.00 69.48  ? 47  LEU E O   1 
ATOM   7931  C CB  . LEU E  1 47  ? -38.083 -71.324  -57.611 1.00 58.10  ? 47  LEU E CB  1 
ATOM   7932  C CG  . LEU E  1 47  ? -36.740 -70.849  -57.049 1.00 51.06  ? 47  LEU E CG  1 
ATOM   7933  C CD1 . LEU E  1 47  ? -36.418 -71.510  -55.716 1.00 54.26  ? 47  LEU E CD1 1 
ATOM   7934  C CD2 . LEU E  1 47  ? -35.629 -71.061  -58.064 1.00 53.68  ? 47  LEU E CD2 1 
ATOM   7935  N N   . CYS E  1 48  ? -41.353 -70.915  -56.089 1.00 60.38  ? 48  CYS E N   1 
ATOM   7936  C CA  . CYS E  1 48  ? -42.761 -70.633  -56.349 1.00 68.55  ? 48  CYS E CA  1 
ATOM   7937  C C   . CYS E  1 48  ? -43.028 -69.167  -56.673 1.00 51.63  ? 48  CYS E C   1 
ATOM   7938  O O   . CYS E  1 48  ? -42.128 -68.325  -56.608 1.00 55.34  ? 48  CYS E O   1 
ATOM   7939  C CB  . CYS E  1 48  ? -43.610 -71.038  -55.140 1.00 58.94  ? 48  CYS E CB  1 
ATOM   7940  S SG  . CYS E  1 48  ? -43.331 -72.723  -54.544 1.00 65.67  ? 48  CYS E SG  1 
ATOM   7941  N N   . LYS E  1 49  ? -44.280 -68.876  -57.016 1.00 62.26  ? 49  LYS E N   1 
ATOM   7942  C CA  . LYS E  1 49  ? -44.702 -67.511  -57.291 1.00 64.24  ? 49  LYS E CA  1 
ATOM   7943  C C   . LYS E  1 49  ? -44.887 -66.771  -55.979 1.00 59.54  ? 49  LYS E C   1 
ATOM   7944  O O   . LYS E  1 49  ? -45.305 -67.349  -54.974 1.00 71.56  ? 49  LYS E O   1 
ATOM   7945  C CB  . LYS E  1 49  ? -46.001 -67.484  -58.096 1.00 64.60  ? 49  LYS E CB  1 
ATOM   7946  C CG  . LYS E  1 49  ? -46.006 -68.410  -59.301 1.00 70.71  ? 49  LYS E CG  1 
ATOM   7947  C CD  . LYS E  1 49  ? -47.321 -68.319  -60.068 1.00 81.10  ? 49  LYS E CD  1 
ATOM   7948  C CE  . LYS E  1 49  ? -48.046 -69.656  -60.096 1.00 93.63  ? 49  LYS E CE  1 
ATOM   7949  N NZ  . LYS E  1 49  ? -49.500 -69.487  -60.382 1.00 105.27 ? 49  LYS E NZ  1 
ATOM   7950  N N   . LEU E  1 50  ? -44.582 -65.482  -55.999 1.00 64.43  ? 50  LEU E N   1 
ATOM   7951  C CA  . LEU E  1 50  ? -44.481 -64.714  -54.770 1.00 67.33  ? 50  LEU E CA  1 
ATOM   7952  C C   . LEU E  1 50  ? -45.753 -64.032  -54.254 1.00 86.31  ? 50  LEU E C   1 
ATOM   7953  O O   . LEU E  1 50  ? -46.077 -64.128  -53.075 1.00 112.51 ? 50  LEU E O   1 
ATOM   7954  C CB  . LEU E  1 50  ? -43.401 -63.644  -54.933 1.00 67.96  ? 50  LEU E CB  1 
ATOM   7955  C CG  . LEU E  1 50  ? -42.986 -62.871  -53.674 1.00 64.36  ? 50  LEU E CG  1 
ATOM   7956  C CD1 . LEU E  1 50  ? -43.222 -63.685  -52.413 1.00 56.11  ? 50  LEU E CD1 1 
ATOM   7957  C CD2 . LEU E  1 50  ? -41.536 -62.384  -53.754 1.00 56.48  ? 50  LEU E CD2 1 
ATOM   7958  N N   . ARG E  1 51  ? -46.468 -63.353  -55.141 1.00 70.63  ? 51  ARG E N   1 
ATOM   7959  C CA  . ARG E  1 51  ? -47.791 -62.842  -54.814 1.00 94.71  ? 51  ARG E CA  1 
ATOM   7960  C C   . ARG E  1 51  ? -48.755 -63.829  -55.458 1.00 94.87  ? 51  ARG E C   1 
ATOM   7961  O O   . ARG E  1 51  ? -49.246 -64.755  -54.818 1.00 121.94 ? 51  ARG E O   1 
ATOM   7962  C CB  . ARG E  1 51  ? -48.034 -61.444  -55.381 1.00 117.50 ? 51  ARG E CB  1 
ATOM   7963  C CG  . ARG E  1 51  ? -46.915 -60.478  -55.106 1.00 127.65 ? 51  ARG E CG  1 
ATOM   7964  C CD  . ARG E  1 51  ? -47.420 -59.056  -55.129 1.00 158.01 ? 51  ARG E CD  1 
ATOM   7965  N NE  . ARG E  1 51  ? -48.289 -58.772  -53.991 1.00 168.70 ? 51  ARG E NE  1 
ATOM   7966  C CZ  . ARG E  1 51  ? -49.531 -58.306  -54.090 1.00 160.47 ? 51  ARG E CZ  1 
ATOM   7967  N NH1 . ARG E  1 51  ? -50.063 -58.062  -55.280 1.00 147.37 ? 51  ARG E NH1 1 
ATOM   7968  N NH2 . ARG E  1 51  ? -50.241 -58.076  -52.994 1.00 148.21 ? 51  ARG E NH2 1 
ATOM   7969  N N   . GLY E  1 52  ? -49.023 -63.601  -56.737 1.00 77.72  ? 52  GLY E N   1 
ATOM   7970  C CA  . GLY E  1 52  ? -49.712 -64.548  -57.593 1.00 96.69  ? 52  GLY E CA  1 
ATOM   7971  C C   . GLY E  1 52  ? -48.938 -64.501  -58.892 1.00 97.30  ? 52  GLY E C   1 
ATOM   7972  O O   . GLY E  1 52  ? -49.288 -65.137  -59.887 1.00 102.09 ? 52  GLY E O   1 
ATOM   7973  N N   . VAL E  1 53  ? -47.861 -63.722  -58.860 1.00 92.69  ? 53  VAL E N   1 
ATOM   7974  C CA  . VAL E  1 53  ? -47.015 -63.502  -60.023 1.00 77.71  ? 53  VAL E CA  1 
ATOM   7975  C C   . VAL E  1 53  ? -45.823 -64.456  -60.023 1.00 50.30  ? 53  VAL E C   1 
ATOM   7976  O O   . VAL E  1 53  ? -45.221 -64.720  -58.982 1.00 57.28  ? 53  VAL E O   1 
ATOM   7977  C CB  . VAL E  1 53  ? -46.494 -62.052  -60.067 1.00 67.18  ? 53  VAL E CB  1 
ATOM   7978  C CG1 . VAL E  1 53  ? -45.738 -61.799  -61.366 1.00 67.48  ? 53  VAL E CG1 1 
ATOM   7979  C CG2 . VAL E  1 53  ? -47.646 -61.063  -59.893 1.00 56.29  ? 53  VAL E CG2 1 
ATOM   7980  N N   . ALA E  1 54  ? -45.488 -64.973  -61.200 1.00 55.54  ? 54  ALA E N   1 
ATOM   7981  C CA  . ALA E  1 54  ? -44.385 -65.915  -61.332 1.00 60.65  ? 54  ALA E CA  1 
ATOM   7982  C C   . ALA E  1 54  ? -43.044 -65.198  -61.433 1.00 60.54  ? 54  ALA E C   1 
ATOM   7983  O O   . ALA E  1 54  ? -42.981 -64.041  -61.848 1.00 60.69  ? 54  ALA E O   1 
ATOM   7984  C CB  . ALA E  1 54  ? -44.598 -66.812  -62.540 1.00 70.46  ? 54  ALA E CB  1 
ATOM   7985  N N   . PRO E  1 55  ? -41.965 -65.887  -61.040 1.00 47.13  ? 55  PRO E N   1 
ATOM   7986  C CA  . PRO E  1 55  ? -40.607 -65.353  -61.178 1.00 46.08  ? 55  PRO E CA  1 
ATOM   7987  C C   . PRO E  1 55  ? -40.137 -65.410  -62.626 1.00 50.26  ? 55  PRO E C   1 
ATOM   7988  O O   . PRO E  1 55  ? -40.631 -66.228  -63.402 1.00 57.79  ? 55  PRO E O   1 
ATOM   7989  C CB  . PRO E  1 55  ? -39.772 -66.310  -60.326 1.00 41.82  ? 55  PRO E CB  1 
ATOM   7990  C CG  . PRO E  1 55  ? -40.541 -67.587  -60.343 1.00 48.21  ? 55  PRO E CG  1 
ATOM   7991  C CD  . PRO E  1 55  ? -41.981 -67.172  -60.320 1.00 47.54  ? 55  PRO E CD  1 
ATOM   7992  N N   . LEU E  1 56  ? -39.197 -64.542  -62.980 1.00 50.81  ? 56  LEU E N   1 
ATOM   7993  C CA  . LEU E  1 56  ? -38.596 -64.559  -64.307 1.00 44.01  ? 56  LEU E CA  1 
ATOM   7994  C C   . LEU E  1 56  ? -37.354 -65.444  -64.293 1.00 55.05  ? 56  LEU E C   1 
ATOM   7995  O O   . LEU E  1 56  ? -36.322 -65.069  -63.737 1.00 58.59  ? 56  LEU E O   1 
ATOM   7996  C CB  . LEU E  1 56  ? -38.229 -63.140  -64.744 1.00 54.39  ? 56  LEU E CB  1 
ATOM   7997  C CG  . LEU E  1 56  ? -37.577 -62.981  -66.120 1.00 57.05  ? 56  LEU E CG  1 
ATOM   7998  C CD1 . LEU E  1 56  ? -38.527 -63.424  -67.223 1.00 62.93  ? 56  LEU E CD1 1 
ATOM   7999  C CD2 . LEU E  1 56  ? -37.134 -61.542  -66.336 1.00 53.26  ? 56  LEU E CD2 1 
ATOM   8000  N N   . HIS E  1 57  ? -37.461 -66.622  -64.899 1.00 60.51  ? 57  HIS E N   1 
ATOM   8001  C CA  . HIS E  1 57  ? -36.352 -67.569  -64.923 1.00 57.42  ? 57  HIS E CA  1 
ATOM   8002  C C   . HIS E  1 57  ? -35.567 -67.444  -66.224 1.00 67.68  ? 57  HIS E C   1 
ATOM   8003  O O   . HIS E  1 57  ? -36.121 -67.602  -67.312 1.00 74.03  ? 57  HIS E O   1 
ATOM   8004  C CB  . HIS E  1 57  ? -36.865 -68.998  -64.750 1.00 62.83  ? 57  HIS E CB  1 
ATOM   8005  C CG  . HIS E  1 57  ? -35.805 -69.975  -64.353 1.00 69.00  ? 57  HIS E CG  1 
ATOM   8006  N ND1 . HIS E  1 57  ? -34.935 -70.543  -65.260 1.00 73.83  ? 57  HIS E ND1 1 
ATOM   8007  C CD2 . HIS E  1 57  ? -35.473 -70.490  -63.144 1.00 69.25  ? 57  HIS E CD2 1 
ATOM   8008  C CE1 . HIS E  1 57  ? -34.115 -71.362  -64.627 1.00 79.91  ? 57  HIS E CE1 1 
ATOM   8009  N NE2 . HIS E  1 57  ? -34.420 -71.347  -63.343 1.00 76.84  ? 57  HIS E NE2 1 
ATOM   8010  N N   . LEU E  1 58  ? -34.272 -67.167  -66.104 1.00 68.61  ? 58  LEU E N   1 
ATOM   8011  C CA  . LEU E  1 58  ? -33.434 -66.899  -67.268 1.00 74.25  ? 58  LEU E CA  1 
ATOM   8012  C C   . LEU E  1 58  ? -32.723 -68.143  -67.785 1.00 80.17  ? 58  LEU E C   1 
ATOM   8013  O O   . LEU E  1 58  ? -32.183 -68.141  -68.891 1.00 81.07  ? 58  LEU E O   1 
ATOM   8014  C CB  . LEU E  1 58  ? -32.406 -65.816  -66.944 1.00 67.05  ? 58  LEU E CB  1 
ATOM   8015  C CG  . LEU E  1 58  ? -32.988 -64.497  -66.435 1.00 56.82  ? 58  LEU E CG  1 
ATOM   8016  C CD1 . LEU E  1 58  ? -31.885 -63.472  -66.234 1.00 56.07  ? 58  LEU E CD1 1 
ATOM   8017  C CD2 . LEU E  1 58  ? -34.067 -63.969  -67.373 1.00 66.75  ? 58  LEU E CD2 1 
ATOM   8018  N N   . GLY E  1 59  ? -32.717 -69.200  -66.981 1.00 80.67  ? 59  GLY E N   1 
ATOM   8019  C CA  . GLY E  1 59  ? -32.096 -70.449  -67.380 1.00 75.58  ? 59  GLY E CA  1 
ATOM   8020  C C   . GLY E  1 59  ? -30.598 -70.339  -67.592 1.00 80.37  ? 59  GLY E C   1 
ATOM   8021  O O   . GLY E  1 59  ? -29.848 -70.063  -66.657 1.00 91.46  ? 59  GLY E O   1 
ATOM   8022  N N   . LYS E  1 60  ? -30.163 -70.551  -68.830 1.00 89.14  ? 60  LYS E N   1 
ATOM   8023  C CA  . LYS E  1 60  ? -28.740 -70.570  -69.154 1.00 101.20 ? 60  LYS E CA  1 
ATOM   8024  C C   . LYS E  1 60  ? -28.154 -69.165  -69.289 1.00 95.27  ? 60  LYS E C   1 
ATOM   8025  O O   . LYS E  1 60  ? -26.945 -69.001  -69.450 1.00 106.79 ? 60  LYS E O   1 
ATOM   8026  C CB  . LYS E  1 60  ? -28.500 -71.362  -70.443 1.00 105.40 ? 60  LYS E CB  1 
ATOM   8027  C CG  . LYS E  1 60  ? -27.040 -71.693  -70.712 1.00 144.32 ? 60  LYS E CG  1 
ATOM   8028  C CD  . LYS E  1 60  ? -26.481 -72.628  -69.652 1.00 157.39 ? 60  LYS E CD  1 
ATOM   8029  C CE  . LYS E  1 60  ? -27.204 -73.966  -69.657 1.00 173.34 ? 60  LYS E CE  1 
ATOM   8030  N NZ  . LYS E  1 60  ? -26.659 -74.896  -68.629 1.00 159.15 ? 60  LYS E NZ  1 
ATOM   8031  N N   . CYS E  1 61  ? -29.012 -68.152  -69.219 1.00 87.34  ? 61  CYS E N   1 
ATOM   8032  C CA  . CYS E  1 61  ? -28.570 -66.772  -69.388 1.00 78.69  ? 61  CYS E CA  1 
ATOM   8033  C C   . CYS E  1 61  ? -28.620 -65.980  -68.085 1.00 80.47  ? 61  CYS E C   1 
ATOM   8034  O O   . CYS E  1 61  ? -29.285 -66.376  -67.127 1.00 86.83  ? 61  CYS E O   1 
ATOM   8035  C CB  . CYS E  1 61  ? -29.416 -66.065  -70.449 1.00 68.64  ? 61  CYS E CB  1 
ATOM   8036  S SG  . CYS E  1 61  ? -29.330 -66.798  -72.098 1.00 94.34  ? 61  CYS E SG  1 
ATOM   8037  N N   . ASN E  1 62  ? -27.905 -64.860  -68.060 1.00 64.42  ? 62  ASN E N   1 
ATOM   8038  C CA  . ASN E  1 62  ? -27.985 -63.920  -66.949 1.00 61.21  ? 62  ASN E CA  1 
ATOM   8039  C C   . ASN E  1 62  ? -28.658 -62.626  -67.398 1.00 56.22  ? 62  ASN E C   1 
ATOM   8040  O O   . ASN E  1 62  ? -28.940 -62.449  -68.583 1.00 57.41  ? 62  ASN E O   1 
ATOM   8041  C CB  . ASN E  1 62  ? -26.597 -63.643  -66.363 1.00 71.67  ? 62  ASN E CB  1 
ATOM   8042  C CG  . ASN E  1 62  ? -25.622 -63.106  -67.392 1.00 72.03  ? 62  ASN E CG  1 
ATOM   8043  O OD1 . ASN E  1 62  ? -26.020 -62.537  -68.408 1.00 77.03  ? 62  ASN E OD1 1 
ATOM   8044  N ND2 . ASN E  1 62  ? -24.332 -63.280  -67.129 1.00 67.33  ? 62  ASN E ND2 1 
ATOM   8045  N N   . ILE E  1 63  ? -28.918 -61.728  -66.453 1.00 51.35  ? 63  ILE E N   1 
ATOM   8046  C CA  . ILE E  1 63  ? -29.604 -60.475  -66.757 1.00 58.65  ? 63  ILE E CA  1 
ATOM   8047  C C   . ILE E  1 63  ? -29.000 -59.773  -67.973 1.00 52.36  ? 63  ILE E C   1 
ATOM   8048  O O   . ILE E  1 63  ? -29.719 -59.370  -68.887 1.00 60.07  ? 63  ILE E O   1 
ATOM   8049  C CB  . ILE E  1 63  ? -29.592 -59.515  -65.552 1.00 52.43  ? 63  ILE E CB  1 
ATOM   8050  C CG1 . ILE E  1 63  ? -30.313 -60.147  -64.361 1.00 50.63  ? 63  ILE E CG1 1 
ATOM   8051  C CG2 . ILE E  1 63  ? -30.250 -58.199  -65.916 1.00 52.16  ? 63  ILE E CG2 1 
ATOM   8052  C CD1 . ILE E  1 63  ? -31.793 -60.367  -64.590 1.00 61.12  ? 63  ILE E CD1 1 
ATOM   8053  N N   . ALA E  1 64  ? -27.678 -59.639  -67.981 1.00 49.50  ? 64  ALA E N   1 
ATOM   8054  C CA  . ALA E  1 64  ? -26.977 -58.980  -69.077 1.00 53.27  ? 64  ALA E CA  1 
ATOM   8055  C C   . ALA E  1 64  ? -27.352 -59.575  -70.432 1.00 59.54  ? 64  ALA E C   1 
ATOM   8056  O O   . ALA E  1 64  ? -27.782 -58.859  -71.337 1.00 60.54  ? 64  ALA E O   1 
ATOM   8057  C CB  . ALA E  1 64  ? -25.472 -59.053  -68.862 1.00 54.16  ? 64  ALA E CB  1 
ATOM   8058  N N   . GLY E  1 65  ? -27.187 -60.887  -70.566 1.00 55.15  ? 65  GLY E N   1 
ATOM   8059  C CA  . GLY E  1 65  ? -27.488 -61.568  -71.811 1.00 56.53  ? 65  GLY E CA  1 
ATOM   8060  C C   . GLY E  1 65  ? -28.937 -61.422  -72.233 1.00 63.84  ? 65  GLY E C   1 
ATOM   8061  O O   . GLY E  1 65  ? -29.235 -61.225  -73.411 1.00 74.14  ? 65  GLY E O   1 
ATOM   8062  N N   . TRP E  1 66  ? -29.840 -61.514  -71.262 1.00 57.42  ? 66  TRP E N   1 
ATOM   8063  C CA  . TRP E  1 66  ? -31.272 -61.453  -71.532 1.00 60.21  ? 66  TRP E CA  1 
ATOM   8064  C C   . TRP E  1 66  ? -31.729 -60.102  -72.084 1.00 55.94  ? 66  TRP E C   1 
ATOM   8065  O O   . TRP E  1 66  ? -32.515 -60.048  -73.030 1.00 70.58  ? 66  TRP E O   1 
ATOM   8066  C CB  . TRP E  1 66  ? -32.065 -61.808  -70.272 1.00 64.37  ? 66  TRP E CB  1 
ATOM   8067  C CG  . TRP E  1 66  ? -33.499 -61.394  -70.334 1.00 68.22  ? 66  TRP E CG  1 
ATOM   8068  C CD1 . TRP E  1 66  ? -34.446 -61.856  -71.198 1.00 70.30  ? 66  TRP E CD1 1 
ATOM   8069  C CD2 . TRP E  1 66  ? -34.154 -60.438  -69.492 1.00 64.03  ? 66  TRP E CD2 1 
ATOM   8070  N NE1 . TRP E  1 66  ? -35.648 -61.243  -70.951 1.00 70.30  ? 66  TRP E NE1 1 
ATOM   8071  C CE2 . TRP E  1 66  ? -35.498 -60.368  -69.907 1.00 65.27  ? 66  TRP E CE2 1 
ATOM   8072  C CE3 . TRP E  1 66  ? -33.736 -59.633  -68.428 1.00 63.81  ? 66  TRP E CE3 1 
ATOM   8073  C CZ2 . TRP E  1 66  ? -36.426 -59.526  -69.298 1.00 64.17  ? 66  TRP E CZ2 1 
ATOM   8074  C CZ3 . TRP E  1 66  ? -34.659 -58.797  -67.824 1.00 63.93  ? 66  TRP E CZ3 1 
ATOM   8075  C CH2 . TRP E  1 66  ? -35.988 -58.751  -68.261 1.00 62.42  ? 66  TRP E CH2 1 
ATOM   8076  N N   . ILE E  1 67  ? -31.239 -59.015  -71.495 1.00 51.72  ? 67  ILE E N   1 
ATOM   8077  C CA  . ILE E  1 67  ? -31.661 -57.680  -71.909 1.00 68.27  ? 67  ILE E CA  1 
ATOM   8078  C C   . ILE E  1 67  ? -30.962 -57.226  -73.186 1.00 67.79  ? 67  ILE E C   1 
ATOM   8079  O O   . ILE E  1 67  ? -31.576 -56.592  -74.044 1.00 64.15  ? 67  ILE E O   1 
ATOM   8080  C CB  . ILE E  1 67  ? -31.414 -56.629  -70.814 1.00 58.69  ? 67  ILE E CB  1 
ATOM   8081  C CG1 . ILE E  1 67  ? -31.698 -57.212  -69.433 1.00 78.80  ? 67  ILE E CG1 1 
ATOM   8082  C CG2 . ILE E  1 67  ? -32.274 -55.398  -71.058 1.00 50.61  ? 67  ILE E CG2 1 
ATOM   8083  C CD1 . ILE E  1 67  ? -31.476 -56.228  -68.316 1.00 86.19  ? 67  ILE E CD1 1 
ATOM   8084  N N   . LEU E  1 68  ? -29.677 -57.539  -73.305 1.00 63.43  ? 68  LEU E N   1 
ATOM   8085  C CA  . LEU E  1 68  ? -28.918 -57.163  -74.492 1.00 67.31  ? 68  LEU E CA  1 
ATOM   8086  C C   . LEU E  1 68  ? -29.414 -57.913  -75.722 1.00 72.47  ? 68  LEU E C   1 
ATOM   8087  O O   . LEU E  1 68  ? -29.352 -57.402  -76.840 1.00 59.91  ? 68  LEU E O   1 
ATOM   8088  C CB  . LEU E  1 68  ? -27.422 -57.410  -74.288 1.00 55.65  ? 68  LEU E CB  1 
ATOM   8089  C CG  . LEU E  1 68  ? -26.698 -56.406  -73.391 1.00 61.69  ? 68  LEU E CG  1 
ATOM   8090  C CD1 . LEU E  1 68  ? -25.199 -56.660  -73.414 1.00 59.89  ? 68  LEU E CD1 1 
ATOM   8091  C CD2 . LEU E  1 68  ? -27.009 -54.986  -73.834 1.00 43.81  ? 68  LEU E CD2 1 
ATOM   8092  N N   . GLY E  1 69  ? -29.910 -59.126  -75.507 1.00 69.06  ? 69  GLY E N   1 
ATOM   8093  C CA  . GLY E  1 69  ? -30.426 -59.936  -76.593 1.00 67.42  ? 69  GLY E CA  1 
ATOM   8094  C C   . GLY E  1 69  ? -29.394 -60.898  -77.145 1.00 79.48  ? 69  GLY E C   1 
ATOM   8095  O O   . GLY E  1 69  ? -29.288 -61.079  -78.358 1.00 86.15  ? 69  GLY E O   1 
ATOM   8096  N N   . ASN E  1 70  ? -28.624 -61.513  -76.252 1.00 76.99  ? 70  ASN E N   1 
ATOM   8097  C CA  . ASN E  1 70  ? -27.657 -62.525  -76.650 1.00 82.65  ? 70  ASN E CA  1 
ATOM   8098  C C   . ASN E  1 70  ? -28.347 -63.595  -77.487 1.00 92.58  ? 70  ASN E C   1 
ATOM   8099  O O   . ASN E  1 70  ? -29.426 -64.064  -77.126 1.00 94.43  ? 70  ASN E O   1 
ATOM   8100  C CB  . ASN E  1 70  ? -27.002 -63.149  -75.414 1.00 83.34  ? 70  ASN E CB  1 
ATOM   8101  C CG  . ASN E  1 70  ? -25.826 -64.044  -75.759 1.00 86.88  ? 70  ASN E CG  1 
ATOM   8102  O OD1 . ASN E  1 70  ? -25.908 -64.887  -76.652 1.00 88.53  ? 70  ASN E OD1 1 
ATOM   8103  N ND2 . ASN E  1 70  ? -24.723 -63.872  -75.040 1.00 86.26  ? 70  ASN E ND2 1 
ATOM   8104  N N   . PRO E  1 71  ? -27.736 -63.970  -78.619 1.00 106.45 ? 71  PRO E N   1 
ATOM   8105  C CA  . PRO E  1 71  ? -28.317 -64.970  -79.522 1.00 104.25 ? 71  PRO E CA  1 
ATOM   8106  C C   . PRO E  1 71  ? -28.797 -66.228  -78.798 1.00 99.41  ? 71  PRO E C   1 
ATOM   8107  O O   . PRO E  1 71  ? -29.727 -66.881  -79.267 1.00 116.14 ? 71  PRO E O   1 
ATOM   8108  C CB  . PRO E  1 71  ? -27.153 -65.308  -80.454 1.00 101.60 ? 71  PRO E CB  1 
ATOM   8109  C CG  . PRO E  1 71  ? -26.350 -64.055  -80.502 1.00 99.43  ? 71  PRO E CG  1 
ATOM   8110  C CD  . PRO E  1 71  ? -26.465 -63.430  -79.136 1.00 98.75  ? 71  PRO E CD  1 
ATOM   8111  N N   . GLU E  1 72  ? -28.176 -66.554  -77.668 1.00 95.62  ? 72  GLU E N   1 
ATOM   8112  C CA  . GLU E  1 72  ? -28.503 -67.778  -76.941 1.00 108.20 ? 72  GLU E CA  1 
ATOM   8113  C C   . GLU E  1 72  ? -29.570 -67.571  -75.869 1.00 103.85 ? 72  GLU E C   1 
ATOM   8114  O O   . GLU E  1 72  ? -30.028 -68.529  -75.247 1.00 95.55  ? 72  GLU E O   1 
ATOM   8115  C CB  . GLU E  1 72  ? -27.243 -68.376  -76.314 1.00 95.91  ? 72  GLU E CB  1 
ATOM   8116  C CG  . GLU E  1 72  ? -26.155 -68.705  -77.318 1.00 113.60 ? 72  GLU E CG  1 
ATOM   8117  C CD  . GLU E  1 72  ? -26.526 -69.857  -78.232 1.00 132.14 ? 72  GLU E CD  1 
ATOM   8118  O OE1 . GLU E  1 72  ? -27.373 -70.685  -77.834 1.00 125.90 ? 72  GLU E OE1 1 
ATOM   8119  O OE2 . GLU E  1 72  ? -25.967 -69.939  -79.346 1.00 127.06 ? 72  GLU E OE2 1 
ATOM   8120  N N   . CYS E  1 73  ? -29.956 -66.319  -75.649 1.00 110.49 ? 73  CYS E N   1 
ATOM   8121  C CA  . CYS E  1 73  ? -31.004 -66.002  -74.686 1.00 113.24 ? 73  CYS E CA  1 
ATOM   8122  C C   . CYS E  1 73  ? -32.322 -65.773  -75.417 1.00 125.59 ? 73  CYS E C   1 
ATOM   8123  O O   . CYS E  1 73  ? -33.106 -64.894  -75.060 1.00 132.64 ? 73  CYS E O   1 
ATOM   8124  C CB  . CYS E  1 73  ? -30.623 -64.768  -73.867 1.00 98.33  ? 73  CYS E CB  1 
ATOM   8125  S SG  . CYS E  1 73  ? -29.091 -64.957  -72.923 1.00 96.16  ? 73  CYS E SG  1 
ATOM   8126  N N   . GLU E  1 74  ? -32.554 -66.590  -76.438 1.00 135.81 ? 74  GLU E N   1 
ATOM   8127  C CA  . GLU E  1 74  ? -33.688 -66.429  -77.340 1.00 154.13 ? 74  GLU E CA  1 
ATOM   8128  C C   . GLU E  1 74  ? -35.042 -66.651  -76.663 1.00 160.19 ? 74  GLU E C   1 
ATOM   8129  O O   . GLU E  1 74  ? -35.832 -65.719  -76.500 1.00 159.00 ? 74  GLU E O   1 
ATOM   8130  C CB  . GLU E  1 74  ? -33.533 -67.394  -78.518 1.00 157.10 ? 74  GLU E CB  1 
ATOM   8131  C CG  . GLU E  1 74  ? -34.030 -66.857  -79.846 1.00 167.16 ? 74  GLU E CG  1 
ATOM   8132  C CD  . GLU E  1 74  ? -33.024 -67.070  -80.960 1.00 172.30 ? 74  GLU E CD  1 
ATOM   8133  O OE1 . GLU E  1 74  ? -31.890 -67.500  -80.659 1.00 165.97 ? 74  GLU E OE1 1 
ATOM   8134  O OE2 . GLU E  1 74  ? -33.362 -66.804  -82.132 1.00 167.24 ? 74  GLU E OE2 1 
ATOM   8135  N N   . SER E  1 75  ? -35.288 -67.898  -76.271 1.00 164.95 ? 75  SER E N   1 
ATOM   8136  C CA  . SER E  1 75  ? -36.579 -68.347  -75.758 1.00 178.32 ? 75  SER E CA  1 
ATOM   8137  C C   . SER E  1 75  ? -37.366 -67.843  -74.560 1.00 183.96 ? 75  SER E C   1 
ATOM   8138  O O   . SER E  1 75  ? -38.443 -68.375  -74.251 1.00 185.67 ? 75  SER E O   1 
ATOM   8139  C CB  . SER E  1 75  ? -36.650 -69.865  -75.872 1.00 182.39 ? 75  SER E CB  1 
ATOM   8140  O OG  . SER E  1 75  ? -35.484 -70.434  -75.301 1.00 166.95 ? 75  SER E OG  1 
ATOM   8141  N N   . LEU E  1 76  ? -36.863 -66.796  -73.914 1.00 198.67 ? 76  LEU E N   1 
ATOM   8142  C CA  . LEU E  1 76  ? -37.516 -66.320  -72.704 1.00 199.28 ? 76  LEU E CA  1 
ATOM   8143  C C   . LEU E  1 76  ? -38.514 -65.171  -72.492 1.00 198.37 ? 76  LEU E C   1 
ATOM   8144  O O   . LEU E  1 76  ? -39.719 -65.408  -72.351 1.00 197.72 ? 76  LEU E O   1 
ATOM   8145  C CB  . LEU E  1 76  ? -36.157 -65.953  -72.123 1.00 189.69 ? 76  LEU E CB  1 
ATOM   8146  C CG  . LEU E  1 76  ? -35.831 -66.770  -70.867 1.00 179.17 ? 76  LEU E CG  1 
ATOM   8147  C CD1 . LEU E  1 76  ? -36.756 -67.981  -70.739 1.00 183.65 ? 76  LEU E CD1 1 
ATOM   8148  C CD2 . LEU E  1 76  ? -34.364 -67.180  -70.830 1.00 147.73 ? 76  LEU E CD2 1 
ATOM   8149  N N   . SER E  1 77  ? -38.022 -63.934  -72.423 1.00 163.06 ? 77  SER E N   1 
ATOM   8150  C CA  . SER E  1 77  ? -38.910 -62.802  -72.164 1.00 150.62 ? 77  SER E CA  1 
ATOM   8151  C C   . SER E  1 77  ? -40.028 -62.732  -73.193 1.00 170.99 ? 77  SER E C   1 
ATOM   8152  O O   . SER E  1 77  ? -39.790 -62.393  -74.363 1.00 176.72 ? 77  SER E O   1 
ATOM   8153  C CB  . SER E  1 77  ? -38.146 -61.468  -72.119 1.00 140.47 ? 77  SER E CB  1 
ATOM   8154  O OG  . SER E  1 77  ? -39.014 -60.387  -71.829 1.00 124.27 ? 77  SER E OG  1 
ATOM   8155  N N   . THR E  1 78  ? -41.224 -63.017  -72.678 1.00 224.21 ? 78  THR E N   1 
ATOM   8156  C CA  . THR E  1 78  ? -42.486 -63.188  -73.354 1.00 226.56 ? 78  THR E CA  1 
ATOM   8157  C C   . THR E  1 78  ? -43.357 -62.671  -72.210 1.00 218.95 ? 78  THR E C   1 
ATOM   8158  O O   . THR E  1 78  ? -44.591 -62.536  -72.274 1.00 215.46 ? 78  THR E O   1 
ATOM   8159  C CB  . THR E  1 78  ? -42.716 -64.694  -73.574 1.00 212.58 ? 78  THR E CB  1 
ATOM   8160  O OG1 . THR E  1 78  ? -42.168 -65.100  -74.835 1.00 213.52 ? 78  THR E OG1 1 
ATOM   8161  C CG2 . THR E  1 78  ? -44.188 -65.088  -73.461 1.00 194.42 ? 78  THR E CG2 1 
ATOM   8162  N N   . ALA E  1 79  ? -42.633 -62.334  -71.150 1.00 173.03 ? 79  ALA E N   1 
ATOM   8163  C CA  . ALA E  1 79  ? -43.188 -61.957  -69.862 1.00 148.16 ? 79  ALA E CA  1 
ATOM   8164  C C   . ALA E  1 79  ? -43.678 -60.526  -69.833 1.00 131.72 ? 79  ALA E C   1 
ATOM   8165  O O   . ALA E  1 79  ? -43.061 -59.619  -70.403 1.00 130.51 ? 79  ALA E O   1 
ATOM   8166  C CB  . ALA E  1 79  ? -42.146 -62.171  -68.765 1.00 139.93 ? 79  ALA E CB  1 
ATOM   8167  N N   . SER E  1 80  ? -44.805 -60.349  -69.160 1.00 100.04 ? 80  SER E N   1 
ATOM   8168  C CA  . SER E  1 80  ? -45.414 -59.052  -68.983 1.00 89.63  ? 80  SER E CA  1 
ATOM   8169  C C   . SER E  1 80  ? -45.043 -58.523  -67.603 1.00 76.16  ? 80  SER E C   1 
ATOM   8170  O O   . SER E  1 80  ? -45.035 -57.315  -67.373 1.00 70.94  ? 80  SER E O   1 
ATOM   8171  C CB  . SER E  1 80  ? -46.929 -59.183  -69.122 1.00 105.51 ? 80  SER E CB  1 
ATOM   8172  O OG  . SER E  1 80  ? -47.264 -59.921  -70.287 1.00 125.74 ? 80  SER E OG  1 
ATOM   8173  N N   . SER E  1 81  ? -44.722 -59.436  -66.691 1.00 74.50  ? 81  SER E N   1 
ATOM   8174  C CA  . SER E  1 81  ? -44.385 -59.064  -65.322 1.00 71.33  ? 81  SER E CA  1 
ATOM   8175  C C   . SER E  1 81  ? -43.755 -60.222  -64.556 1.00 62.98  ? 81  SER E C   1 
ATOM   8176  O O   . SER E  1 81  ? -43.867 -61.378  -64.959 1.00 58.00  ? 81  SER E O   1 
ATOM   8177  C CB  . SER E  1 81  ? -45.635 -58.588  -64.584 1.00 70.28  ? 81  SER E CB  1 
ATOM   8178  O OG  . SER E  1 81  ? -46.631 -59.596  -64.571 1.00 67.00  ? 81  SER E OG  1 
ATOM   8179  N N   . TRP E  1 82  ? -43.095 -59.902  -63.447 1.00 45.78  ? 82  TRP E N   1 
ATOM   8180  C CA  . TRP E  1 82  ? -42.522 -60.921  -62.573 1.00 55.15  ? 82  TRP E CA  1 
ATOM   8181  C C   . TRP E  1 82  ? -42.269 -60.384  -61.166 1.00 52.41  ? 82  TRP E C   1 
ATOM   8182  O O   . TRP E  1 82  ? -41.936 -59.212  -60.986 1.00 55.06  ? 82  TRP E O   1 
ATOM   8183  C CB  . TRP E  1 82  ? -41.236 -61.503  -63.169 1.00 52.08  ? 82  TRP E CB  1 
ATOM   8184  C CG  . TRP E  1 82  ? -40.199 -60.480  -63.505 1.00 50.44  ? 82  TRP E CG  1 
ATOM   8185  C CD1 . TRP E  1 82  ? -39.270 -59.947  -62.662 1.00 46.47  ? 82  TRP E CD1 1 
ATOM   8186  C CD2 . TRP E  1 82  ? -39.976 -59.874  -64.783 1.00 54.48  ? 82  TRP E CD2 1 
ATOM   8187  N NE1 . TRP E  1 82  ? -38.485 -59.042  -63.334 1.00 48.03  ? 82  TRP E NE1 1 
ATOM   8188  C CE2 . TRP E  1 82  ? -38.898 -58.979  -64.639 1.00 50.72  ? 82  TRP E CE2 1 
ATOM   8189  C CE3 . TRP E  1 82  ? -40.585 -59.999  -66.035 1.00 51.61  ? 82  TRP E CE3 1 
ATOM   8190  C CZ2 . TRP E  1 82  ? -38.416 -58.214  -65.698 1.00 51.72  ? 82  TRP E CZ2 1 
ATOM   8191  C CZ3 . TRP E  1 82  ? -40.106 -59.239  -67.085 1.00 57.59  ? 82  TRP E CZ3 1 
ATOM   8192  C CH2 . TRP E  1 82  ? -39.033 -58.357  -66.911 1.00 45.79  ? 82  TRP E CH2 1 
ATOM   8193  N N   . SER E  1 83  ? -42.440 -61.251  -60.173 1.00 47.87  ? 83  SER E N   1 
ATOM   8194  C CA  . SER E  1 83  ? -42.273 -60.869  -58.776 1.00 52.52  ? 83  SER E CA  1 
ATOM   8195  C C   . SER E  1 83  ? -40.801 -60.802  -58.386 1.00 47.89  ? 83  SER E C   1 
ATOM   8196  O O   . SER E  1 83  ? -40.404 -59.974  -57.568 1.00 54.11  ? 83  SER E O   1 
ATOM   8197  C CB  . SER E  1 83  ? -43.017 -61.847  -57.866 1.00 47.25  ? 83  SER E CB  1 
ATOM   8198  O OG  . SER E  1 83  ? -42.681 -63.187  -58.182 1.00 50.23  ? 83  SER E OG  1 
ATOM   8199  N N   . TYR E  1 84  ? -39.999 -61.686  -58.969 1.00 43.98  ? 84  TYR E N   1 
ATOM   8200  C CA  . TYR E  1 84  ? -38.557 -61.677  -58.749 1.00 41.99  ? 84  TYR E CA  1 
ATOM   8201  C C   . TYR E  1 84  ? -37.849 -62.387  -59.896 1.00 48.49  ? 84  TYR E C   1 
ATOM   8202  O O   . TYR E  1 84  ? -38.494 -62.972  -60.764 1.00 56.24  ? 84  TYR E O   1 
ATOM   8203  C CB  . TYR E  1 84  ? -38.200 -62.323  -57.406 1.00 47.43  ? 84  TYR E CB  1 
ATOM   8204  C CG  . TYR E  1 84  ? -38.554 -63.789  -57.303 1.00 51.44  ? 84  TYR E CG  1 
ATOM   8205  C CD1 . TYR E  1 84  ? -37.597 -64.772  -57.519 1.00 40.65  ? 84  TYR E CD1 1 
ATOM   8206  C CD2 . TYR E  1 84  ? -39.846 -64.190  -56.987 1.00 50.85  ? 84  TYR E CD2 1 
ATOM   8207  C CE1 . TYR E  1 84  ? -37.917 -66.113  -57.424 1.00 40.47  ? 84  TYR E CE1 1 
ATOM   8208  C CE2 . TYR E  1 84  ? -40.175 -65.529  -56.892 1.00 39.59  ? 84  TYR E CE2 1 
ATOM   8209  C CZ  . TYR E  1 84  ? -39.207 -66.486  -57.111 1.00 39.81  ? 84  TYR E CZ  1 
ATOM   8210  O OH  . TYR E  1 84  ? -39.527 -67.820  -57.018 1.00 43.21  ? 84  TYR E OH  1 
ATOM   8211  N N   . ILE E  1 85  ? -36.522 -62.329  -59.899 1.00 40.94  ? 85  ILE E N   1 
ATOM   8212  C CA  . ILE E  1 85  ? -35.740 -62.923  -60.976 1.00 52.63  ? 85  ILE E CA  1 
ATOM   8213  C C   . ILE E  1 85  ? -34.910 -64.108  -60.493 1.00 53.63  ? 85  ILE E C   1 
ATOM   8214  O O   . ILE E  1 85  ? -34.265 -64.043  -59.446 1.00 50.54  ? 85  ILE E O   1 
ATOM   8215  C CB  . ILE E  1 85  ? -34.820 -61.882  -61.641 1.00 46.59  ? 85  ILE E CB  1 
ATOM   8216  C CG1 . ILE E  1 85  ? -35.657 -60.773  -62.281 1.00 44.80  ? 85  ILE E CG1 1 
ATOM   8217  C CG2 . ILE E  1 85  ? -33.926 -62.543  -62.678 1.00 49.78  ? 85  ILE E CG2 1 
ATOM   8218  C CD1 . ILE E  1 85  ? -34.836 -59.665  -62.899 1.00 50.93  ? 85  ILE E CD1 1 
ATOM   8219  N N   . VAL E  1 86  ? -34.936 -65.191  -61.262 1.00 48.94  ? 86  VAL E N   1 
ATOM   8220  C CA  . VAL E  1 86  ? -34.162 -66.380  -60.929 1.00 50.37  ? 86  VAL E CA  1 
ATOM   8221  C C   . VAL E  1 86  ? -33.030 -66.599  -61.925 1.00 50.41  ? 86  VAL E C   1 
ATOM   8222  O O   . VAL E  1 86  ? -33.248 -66.632  -63.136 1.00 60.21  ? 86  VAL E O   1 
ATOM   8223  C CB  . VAL E  1 86  ? -35.042 -67.642  -60.889 1.00 51.85  ? 86  VAL E CB  1 
ATOM   8224  C CG1 . VAL E  1 86  ? -34.208 -68.852  -60.502 1.00 41.64  ? 86  VAL E CG1 1 
ATOM   8225  C CG2 . VAL E  1 86  ? -36.194 -67.454  -59.917 1.00 53.95  ? 86  VAL E CG2 1 
ATOM   8226  N N   . GLU E  1 87  ? -31.820 -66.744  -61.399 1.00 51.68  ? 87  GLU E N   1 
ATOM   8227  C CA  . GLU E  1 87  ? -30.646 -67.013  -62.215 1.00 56.41  ? 87  GLU E CA  1 
ATOM   8228  C C   . GLU E  1 87  ? -30.033 -68.330  -61.764 1.00 64.88  ? 87  GLU E C   1 
ATOM   8229  O O   . GLU E  1 87  ? -29.934 -68.591  -60.567 1.00 69.71  ? 87  GLU E O   1 
ATOM   8230  C CB  . GLU E  1 87  ? -29.627 -65.887  -62.052 1.00 61.08  ? 87  GLU E CB  1 
ATOM   8231  C CG  . GLU E  1 87  ? -29.162 -65.256  -63.352 1.00 67.60  ? 87  GLU E CG  1 
ATOM   8232  C CD  . GLU E  1 87  ? -28.246 -64.070  -63.120 1.00 72.73  ? 87  GLU E CD  1 
ATOM   8233  O OE1 . GLU E  1 87  ? -28.302 -63.109  -63.914 1.00 76.31  ? 87  GLU E OE1 1 
ATOM   8234  O OE2 . GLU E  1 87  ? -27.477 -64.093  -62.135 1.00 69.83  ? 87  GLU E OE2 1 
ATOM   8235  N N   . THR E  1 88  ? -29.632 -69.165  -62.715 1.00 81.13  ? 88  THR E N   1 
ATOM   8236  C CA  . THR E  1 88  ? -28.977 -70.421  -62.373 1.00 84.37  ? 88  THR E CA  1 
ATOM   8237  C C   . THR E  1 88  ? -27.481 -70.192  -62.208 1.00 82.79  ? 88  THR E C   1 
ATOM   8238  O O   . THR E  1 88  ? -26.884 -69.414  -62.950 1.00 95.12  ? 88  THR E O   1 
ATOM   8239  C CB  . THR E  1 88  ? -29.217 -71.504  -63.440 1.00 85.97  ? 88  THR E CB  1 
ATOM   8240  O OG1 . THR E  1 88  ? -28.534 -71.152  -64.649 1.00 93.88  ? 88  THR E OG1 1 
ATOM   8241  C CG2 . THR E  1 88  ? -30.705 -71.654  -63.721 1.00 76.91  ? 88  THR E CG2 1 
ATOM   8242  N N   . PRO E  1 89  ? -26.869 -70.867  -61.224 1.00 106.40 ? 89  PRO E N   1 
ATOM   8243  C CA  . PRO E  1 89  ? -25.434 -70.720  -60.960 1.00 106.41 ? 89  PRO E CA  1 
ATOM   8244  C C   . PRO E  1 89  ? -24.598 -71.078  -62.184 1.00 114.66 ? 89  PRO E C   1 
ATOM   8245  O O   . PRO E  1 89  ? -23.406 -70.774  -62.228 1.00 112.51 ? 89  PRO E O   1 
ATOM   8246  C CB  . PRO E  1 89  ? -25.180 -71.733  -59.838 1.00 93.01  ? 89  PRO E CB  1 
ATOM   8247  C CG  . PRO E  1 89  ? -26.508 -71.926  -59.188 1.00 100.04 ? 89  PRO E CG  1 
ATOM   8248  C CD  . PRO E  1 89  ? -27.512 -71.807  -60.291 1.00 108.29 ? 89  PRO E CD  1 
ATOM   8249  N N   . SER E  1 90  ? -25.226 -71.715  -63.168 1.00 115.00 ? 90  SER E N   1 
ATOM   8250  C CA  . SER E  1 90  ? -24.521 -72.176  -64.357 1.00 113.62 ? 90  SER E CA  1 
ATOM   8251  C C   . SER E  1 90  ? -24.872 -71.345  -65.588 1.00 129.37 ? 90  SER E C   1 
ATOM   8252  O O   . SER E  1 90  ? -24.742 -71.811  -66.721 1.00 145.15 ? 90  SER E O   1 
ATOM   8253  C CB  . SER E  1 90  ? -24.832 -73.652  -64.615 1.00 125.39 ? 90  SER E CB  1 
ATOM   8254  O OG  . SER E  1 90  ? -24.061 -74.160  -65.689 1.00 149.65 ? 90  SER E OG  1 
ATOM   8255  N N   . SER E  1 91  ? -25.379 -70.149  -65.371 1.00 127.12 ? 91  SER E N   1 
ATOM   8256  C CA  . SER E  1 91  ? -25.755 -69.295  -66.468 1.00 113.69 ? 91  SER E CA  1 
ATOM   8257  C C   . SER E  1 91  ? -24.528 -68.486  -66.724 1.00 121.33 ? 91  SER E C   1 
ATOM   8258  O O   . SER E  1 91  ? -23.749 -68.269  -65.827 1.00 120.09 ? 91  SER E O   1 
ATOM   8259  C CB  . SER E  1 91  ? -26.904 -68.409  -66.045 1.00 100.04 ? 91  SER E CB  1 
ATOM   8260  O OG  . SER E  1 91  ? -27.484 -68.903  -64.858 1.00 103.60 ? 91  SER E OG  1 
ATOM   8261  N N   . ASP E  1 92  ? -24.314 -68.056  -67.948 1.00 134.33 ? 92  ASP E N   1 
ATOM   8262  C CA  . ASP E  1 92  ? -23.072 -67.375  -68.229 1.00 137.82 ? 92  ASP E CA  1 
ATOM   8263  C C   . ASP E  1 92  ? -23.119 -66.733  -69.599 1.00 128.16 ? 92  ASP E C   1 
ATOM   8264  O O   . ASP E  1 92  ? -22.302 -65.912  -69.934 1.00 135.40 ? 92  ASP E O   1 
ATOM   8265  C CB  . ASP E  1 92  ? -21.912 -68.364  -68.104 1.00 159.50 ? 92  ASP E CB  1 
ATOM   8266  C CG  . ASP E  1 92  ? -21.054 -68.116  -66.878 1.00 158.69 ? 92  ASP E CG  1 
ATOM   8267  O OD1 . ASP E  1 92  ? -21.394 -67.234  -66.072 1.00 157.52 ? 92  ASP E OD1 1 
ATOM   8268  O OD2 . ASP E  1 92  ? -20.023 -68.795  -66.728 1.00 158.97 ? 92  ASP E OD2 1 
ATOM   8269  N N   . ASN E  1 93  ? -24.106 -67.102  -70.382 1.00 112.62 ? 93  ASN E N   1 
ATOM   8270  C CA  . ASN E  1 93  ? -24.367 -66.415  -71.639 1.00 114.43 ? 93  ASN E CA  1 
ATOM   8271  C C   . ASN E  1 93  ? -24.828 -64.980  -71.393 1.00 103.40 ? 93  ASN E C   1 
ATOM   8272  O O   . ASN E  1 93  ? -26.022 -64.682  -71.422 1.00 94.92  ? 93  ASN E O   1 
ATOM   8273  C CB  . ASN E  1 93  ? -25.375 -67.188  -72.495 1.00 111.27 ? 93  ASN E CB  1 
ATOM   8274  C CG  . ASN E  1 93  ? -24.778 -68.450  -73.112 1.00 120.87 ? 93  ASN E CG  1 
ATOM   8275  O OD1 . ASN E  1 93  ? -25.244 -69.559  -72.848 1.00 121.59 ? 93  ASN E OD1 1 
ATOM   8276  N ND2 . ASN E  1 93  ? -23.761 -68.280  -73.963 1.00 121.66 ? 93  ASN E ND2 1 
ATOM   8277  N N   . GLY E  1 94  ? -23.865 -64.099  -71.136 1.00 105.22 ? 94  GLY E N   1 
ATOM   8278  C CA  . GLY E  1 94  ? -24.141 -62.692  -70.914 1.00 94.67  ? 94  GLY E CA  1 
ATOM   8279  C C   . GLY E  1 94  ? -23.587 -61.836  -72.037 1.00 93.02  ? 94  GLY E C   1 
ATOM   8280  O O   . GLY E  1 94  ? -24.058 -61.912  -73.171 1.00 85.81  ? 94  GLY E O   1 
ATOM   8281  N N   . THR E  1 95  ? -22.583 -61.022  -71.726 1.00 78.55  ? 95  THR E N   1 
ATOM   8282  C CA  . THR E  1 95  ? -21.946 -60.184  -72.738 1.00 80.68  ? 95  THR E CA  1 
ATOM   8283  C C   . THR E  1 95  ? -20.916 -60.977  -73.537 1.00 79.81  ? 95  THR E C   1 
ATOM   8284  O O   . THR E  1 95  ? -19.772 -61.134  -73.112 1.00 83.03  ? 95  THR E O   1 
ATOM   8285  C CB  . THR E  1 95  ? -21.269 -58.946  -72.117 1.00 60.80  ? 95  THR E CB  1 
ATOM   8286  O OG1 . THR E  1 95  ? -20.587 -59.321  -70.914 1.00 62.17  ? 95  THR E OG1 1 
ATOM   8287  N N   . CYS E  1 96  ? -21.333 -61.473  -74.698 1.00 75.89  ? 96  CYS E N   1 
ATOM   8288  C CA  . CYS E  1 96  ? -20.460 -62.268  -75.556 1.00 80.12  ? 96  CYS E CA  1 
ATOM   8289  C C   . CYS E  1 96  ? -19.279 -61.460  -76.089 1.00 80.44  ? 96  CYS E C   1 
ATOM   8290  O O   . CYS E  1 96  ? -18.191 -61.999  -76.288 1.00 79.37  ? 96  CYS E O   1 
ATOM   8291  C CB  . CYS E  1 96  ? -21.255 -62.888  -76.708 1.00 75.26  ? 96  CYS E CB  1 
ATOM   8292  S SG  . CYS E  1 96  ? -22.497 -61.798  -77.433 1.00 95.39  ? 96  CYS E SG  1 
ATOM   8293  N N   . TYR E  1 97  ? -19.493 -60.170  -76.326 1.00 70.75  ? 97  TYR E N   1 
ATOM   8294  C CA  . TYR E  1 97  ? -18.392 -59.289  -76.693 1.00 69.46  ? 97  TYR E CA  1 
ATOM   8295  C C   . TYR E  1 97  ? -17.837 -58.641  -75.432 1.00 70.47  ? 97  TYR E C   1 
ATOM   8296  O O   . TYR E  1 97  ? -18.572 -57.991  -74.688 1.00 73.88  ? 97  TYR E O   1 
ATOM   8297  C CB  . TYR E  1 97  ? -18.840 -58.219  -77.692 1.00 71.97  ? 97  TYR E CB  1 
ATOM   8298  C CG  . TYR E  1 97  ? -17.691 -57.569  -78.436 1.00 71.00  ? 97  TYR E CG  1 
ATOM   8299  C CD1 . TYR E  1 97  ? -17.424 -57.894  -79.760 1.00 76.58  ? 97  TYR E CD1 1 
ATOM   8300  C CD2 . TYR E  1 97  ? -16.868 -56.640  -77.812 1.00 72.48  ? 97  TYR E CD2 1 
ATOM   8301  C CE1 . TYR E  1 97  ? -16.375 -57.307  -80.443 1.00 78.21  ? 97  TYR E CE1 1 
ATOM   8302  C CE2 . TYR E  1 97  ? -15.815 -56.049  -78.487 1.00 72.48  ? 97  TYR E CE2 1 
ATOM   8303  C CZ  . TYR E  1 97  ? -15.573 -56.386  -79.802 1.00 75.48  ? 97  TYR E CZ  1 
ATOM   8304  O OH  . TYR E  1 97  ? -14.528 -55.801  -80.480 1.00 68.82  ? 97  TYR E OH  1 
ATOM   8305  N N   . PRO E  1 98  ? -16.533 -58.824  -75.186 1.00 68.62  ? 98  PRO E N   1 
ATOM   8306  C CA  . PRO E  1 98  ? -15.883 -58.318  -73.974 1.00 60.17  ? 98  PRO E CA  1 
ATOM   8307  C C   . PRO E  1 98  ? -16.118 -56.830  -73.789 1.00 69.94  ? 98  PRO E C   1 
ATOM   8308  O O   . PRO E  1 98  ? -16.155 -56.075  -74.762 1.00 66.61  ? 98  PRO E O   1 
ATOM   8309  C CB  . PRO E  1 98  ? -14.398 -58.570  -74.240 1.00 58.91  ? 98  PRO E CB  1 
ATOM   8310  C CG  . PRO E  1 98  ? -14.370 -59.657  -75.233 1.00 74.80  ? 98  PRO E CG  1 
ATOM   8311  C CD  . PRO E  1 98  ? -15.575 -59.470  -76.096 1.00 74.95  ? 98  PRO E CD  1 
ATOM   8312  N N   . GLY E  1 99  ? -16.265 -56.427  -72.534 1.00 73.50  ? 99  GLY E N   1 
ATOM   8313  C CA  . GLY E  1 99  ? -16.491 -55.043  -72.175 1.00 66.69  ? 99  GLY E CA  1 
ATOM   8314  C C   . GLY E  1 99  ? -17.111 -54.987  -70.798 1.00 66.38  ? 99  GLY E C   1 
ATOM   8315  O O   . GLY E  1 99  ? -17.400 -56.032  -70.215 1.00 66.55  ? 99  GLY E O   1 
ATOM   8316  N N   . ASP E  1 100 ? -17.314 -53.788  -70.259 1.00 64.47  ? 100 ASP E N   1 
ATOM   8317  C CA  . ASP E  1 100 ? -17.976 -53.695  -68.959 1.00 63.28  ? 100 ASP E CA  1 
ATOM   8318  C C   . ASP E  1 100 ? -19.315 -52.962  -68.991 1.00 59.89  ? 100 ASP E C   1 
ATOM   8319  O O   . ASP E  1 100 ? -19.504 -51.977  -69.712 1.00 58.39  ? 100 ASP E O   1 
ATOM   8320  C CB  . ASP E  1 100 ? -17.042 -53.189  -67.839 1.00 65.31  ? 100 ASP E CB  1 
ATOM   8321  C CG  . ASP E  1 100 ? -16.895 -51.676  -67.813 1.00 87.41  ? 100 ASP E CG  1 
ATOM   8322  O OD1 . ASP E  1 100 ? -16.141 -51.133  -68.644 1.00 95.22  ? 100 ASP E OD1 1 
ATOM   8323  O OD2 . ASP E  1 100 ? -17.506 -51.027  -66.938 1.00 91.69  ? 100 ASP E OD2 1 
ATOM   8324  N N   . PHE E  1 101 ? -20.235 -53.493  -68.195 1.00 49.98  ? 101 PHE E N   1 
ATOM   8325  C CA  . PHE E  1 101 ? -21.618 -53.060  -68.144 1.00 53.61  ? 101 PHE E CA  1 
ATOM   8326  C C   . PHE E  1 101 ? -21.760 -52.026  -67.038 1.00 51.41  ? 101 PHE E C   1 
ATOM   8327  O O   . PHE E  1 101 ? -21.786 -52.371  -65.857 1.00 59.68  ? 101 PHE E O   1 
ATOM   8328  C CB  . PHE E  1 101 ? -22.491 -54.274  -67.823 1.00 44.95  ? 101 PHE E CB  1 
ATOM   8329  C CG  . PHE E  1 101 ? -23.901 -54.171  -68.327 1.00 48.86  ? 101 PHE E CG  1 
ATOM   8330  C CD1 . PHE E  1 101 ? -24.386 -55.087  -69.246 1.00 48.27  ? 101 PHE E CD1 1 
ATOM   8331  C CD2 . PHE E  1 101 ? -24.746 -53.169  -67.879 1.00 52.81  ? 101 PHE E CD2 1 
ATOM   8332  C CE1 . PHE E  1 101 ? -25.687 -55.006  -69.711 1.00 46.02  ? 101 PHE E CE1 1 
ATOM   8333  C CE2 . PHE E  1 101 ? -26.048 -53.082  -68.342 1.00 43.45  ? 101 PHE E CE2 1 
ATOM   8334  C CZ  . PHE E  1 101 ? -26.518 -54.002  -69.259 1.00 41.63  ? 101 PHE E CZ  1 
ATOM   8335  N N   . ILE E  1 102 ? -21.845 -50.758  -67.422 1.00 37.75  ? 102 ILE E N   1 
ATOM   8336  C CA  . ILE E  1 102 ? -21.875 -49.674  -66.448 1.00 40.15  ? 102 ILE E CA  1 
ATOM   8337  C C   . ILE E  1 102 ? -23.122 -49.751  -65.572 1.00 44.00  ? 102 ILE E C   1 
ATOM   8338  O O   . ILE E  1 102 ? -24.233 -49.914  -66.073 1.00 41.01  ? 102 ILE E O   1 
ATOM   8339  C CB  . ILE E  1 102 ? -21.807 -48.302  -67.141 1.00 55.22  ? 102 ILE E CB  1 
ATOM   8340  C CG1 . ILE E  1 102 ? -20.683 -48.288  -68.180 1.00 58.62  ? 102 ILE E CG1 1 
ATOM   8341  C CG2 . ILE E  1 102 ? -21.632 -47.187  -66.116 1.00 43.28  ? 102 ILE E CG2 1 
ATOM   8342  C CD1 . ILE E  1 102 ? -19.308 -48.546  -67.604 1.00 53.48  ? 102 ILE E CD1 1 
ATOM   8343  N N   . ASP E  1 103 ? -22.927 -49.638  -64.261 1.00 48.11  ? 103 ASP E N   1 
ATOM   8344  C CA  . ASP E  1 103 ? -24.034 -49.701  -63.312 1.00 40.40  ? 103 ASP E CA  1 
ATOM   8345  C C   . ASP E  1 103 ? -24.887 -50.946  -63.538 1.00 44.04  ? 103 ASP E C   1 
ATOM   8346  O O   . ASP E  1 103 ? -26.115 -50.875  -63.555 1.00 53.14  ? 103 ASP E O   1 
ATOM   8347  C CB  . ASP E  1 103 ? -24.899 -48.444  -63.417 1.00 49.04  ? 103 ASP E CB  1 
ATOM   8348  C CG  . ASP E  1 103 ? -24.131 -47.181  -63.083 1.00 56.78  ? 103 ASP E CG  1 
ATOM   8349  O OD1 . ASP E  1 103 ? -23.206 -47.251  -62.248 1.00 58.57  ? 103 ASP E OD1 1 
ATOM   8350  O OD2 . ASP E  1 103 ? -24.455 -46.118  -63.652 1.00 56.25  ? 103 ASP E OD2 1 
ATOM   8351  N N   . TYR E  1 104 ? -24.223 -52.084  -63.709 1.00 45.86  ? 104 TYR E N   1 
ATOM   8352  C CA  . TYR E  1 104 ? -24.902 -53.345  -63.985 1.00 45.88  ? 104 TYR E CA  1 
ATOM   8353  C C   . TYR E  1 104 ? -25.735 -53.817  -62.796 1.00 49.68  ? 104 TYR E C   1 
ATOM   8354  O O   . TYR E  1 104 ? -26.916 -54.136  -62.943 1.00 39.21  ? 104 TYR E O   1 
ATOM   8355  C CB  . TYR E  1 104 ? -23.883 -54.417  -64.381 1.00 47.72  ? 104 TYR E CB  1 
ATOM   8356  C CG  . TYR E  1 104 ? -24.482 -55.774  -64.673 1.00 46.71  ? 104 TYR E CG  1 
ATOM   8357  C CD1 . TYR E  1 104 ? -25.529 -55.913  -65.574 1.00 40.70  ? 104 TYR E CD1 1 
ATOM   8358  C CD2 . TYR E  1 104 ? -23.985 -56.918  -64.064 1.00 40.75  ? 104 TYR E CD2 1 
ATOM   8359  C CE1 . TYR E  1 104 ? -26.075 -57.153  -65.848 1.00 46.04  ? 104 TYR E CE1 1 
ATOM   8360  C CE2 . TYR E  1 104 ? -24.523 -58.162  -64.333 1.00 52.54  ? 104 TYR E CE2 1 
ATOM   8361  C CZ  . TYR E  1 104 ? -25.568 -58.273  -65.226 1.00 45.01  ? 104 TYR E CZ  1 
ATOM   8362  O OH  . TYR E  1 104 ? -26.106 -59.510  -65.498 1.00 56.32  ? 104 TYR E OH  1 
ATOM   8363  N N   . GLU E  1 105 ? -25.116 -53.857  -61.621 1.00 47.12  ? 105 GLU E N   1 
ATOM   8364  C CA  . GLU E  1 105 ? -25.797 -54.305  -60.412 1.00 49.53  ? 105 GLU E CA  1 
ATOM   8365  C C   . GLU E  1 105 ? -27.035 -53.459  -60.148 1.00 51.90  ? 105 GLU E C   1 
ATOM   8366  O O   . GLU E  1 105 ? -28.057 -53.966  -59.683 1.00 48.50  ? 105 GLU E O   1 
ATOM   8367  C CB  . GLU E  1 105 ? -24.856 -54.255  -59.207 1.00 42.86  ? 105 GLU E CB  1 
ATOM   8368  C CG  . GLU E  1 105 ? -23.593 -55.086  -59.367 1.00 47.95  ? 105 GLU E CG  1 
ATOM   8369  C CD  . GLU E  1 105 ? -22.614 -54.473  -60.349 1.00 69.65  ? 105 GLU E CD  1 
ATOM   8370  O OE1 . GLU E  1 105 ? -22.566 -53.228  -60.441 1.00 71.58  ? 105 GLU E OE1 1 
ATOM   8371  O OE2 . GLU E  1 105 ? -21.892 -55.235  -61.026 1.00 62.72  ? 105 GLU E OE2 1 
ATOM   8372  N N   . GLU E  1 106 ? -26.936 -52.168  -60.445 1.00 44.48  ? 106 GLU E N   1 
ATOM   8373  C CA  . GLU E  1 106 ? -28.073 -51.265  -60.315 1.00 36.18  ? 106 GLU E CA  1 
ATOM   8374  C C   . GLU E  1 106 ? -29.203 -51.666  -61.258 1.00 40.48  ? 106 GLU E C   1 
ATOM   8375  O O   . GLU E  1 106 ? -30.356 -51.766  -60.846 1.00 37.15  ? 106 GLU E O   1 
ATOM   8376  C CB  . GLU E  1 106 ? -27.651 -49.816  -60.573 1.00 36.27  ? 106 GLU E CB  1 
ATOM   8377  C CG  . GLU E  1 106 ? -27.093 -49.110  -59.349 1.00 54.59  ? 106 GLU E CG  1 
ATOM   8378  C CD  . GLU E  1 106 ? -28.154 -48.856  -58.294 1.00 50.25  ? 106 GLU E CD  1 
ATOM   8379  O OE1 . GLU E  1 106 ? -29.296 -48.515  -58.667 1.00 57.29  ? 106 GLU E OE1 1 
ATOM   8380  O OE2 . GLU E  1 106 ? -27.846 -48.990  -57.091 1.00 46.94  ? 106 GLU E OE2 1 
ATOM   8381  N N   . LEU E  1 107 ? -28.864 -51.900  -62.521 1.00 48.19  ? 107 LEU E N   1 
ATOM   8382  C CA  . LEU E  1 107 ? -29.854 -52.293  -63.517 1.00 49.30  ? 107 LEU E CA  1 
ATOM   8383  C C   . LEU E  1 107 ? -30.622 -53.528  -63.067 1.00 46.29  ? 107 LEU E C   1 
ATOM   8384  O O   . LEU E  1 107 ? -31.848 -53.591  -63.179 1.00 48.76  ? 107 LEU E O   1 
ATOM   8385  C CB  . LEU E  1 107 ? -29.173 -52.570  -64.855 1.00 44.83  ? 107 LEU E CB  1 
ATOM   8386  C CG  . LEU E  1 107 ? -30.119 -52.910  -66.006 1.00 44.16  ? 107 LEU E CG  1 
ATOM   8387  C CD1 . LEU E  1 107 ? -31.147 -51.807  -66.208 1.00 40.72  ? 107 LEU E CD1 1 
ATOM   8388  C CD2 . LEU E  1 107 ? -29.340 -53.180  -67.282 1.00 49.46  ? 107 LEU E CD2 1 
ATOM   8389  N N   . ARG E  1 108 ? -29.884 -54.507  -62.556 1.00 35.16  ? 108 ARG E N   1 
ATOM   8390  C CA  . ARG E  1 108 ? -30.465 -55.763  -62.102 1.00 44.05  ? 108 ARG E CA  1 
ATOM   8391  C C   . ARG E  1 108 ? -31.427 -55.535  -60.941 1.00 48.87  ? 108 ARG E C   1 
ATOM   8392  O O   . ARG E  1 108 ? -32.487 -56.156  -60.871 1.00 49.45  ? 108 ARG E O   1 
ATOM   8393  C CB  . ARG E  1 108 ? -29.358 -56.720  -61.667 1.00 40.33  ? 108 ARG E CB  1 
ATOM   8394  C CG  . ARG E  1 108 ? -28.204 -56.837  -62.645 1.00 46.91  ? 108 ARG E CG  1 
ATOM   8395  C CD  . ARG E  1 108 ? -27.008 -57.491  -61.972 1.00 48.16  ? 108 ARG E CD  1 
ATOM   8396  N NE  . ARG E  1 108 ? -27.383 -58.745  -61.326 1.00 44.68  ? 108 ARG E NE  1 
ATOM   8397  C CZ  . ARG E  1 108 ? -27.351 -59.930  -61.927 1.00 52.86  ? 108 ARG E CZ  1 
ATOM   8398  N NH1 . ARG E  1 108 ? -26.957 -60.027  -63.186 1.00 54.37  ? 108 ARG E NH1 1 
ATOM   8399  N NH2 . ARG E  1 108 ? -27.710 -61.022  -61.269 1.00 47.10  ? 108 ARG E NH2 1 
ATOM   8400  N N   . GLU E  1 109 ? -31.047 -54.646  -60.029 1.00 47.21  ? 109 GLU E N   1 
ATOM   8401  C CA  . GLU E  1 109 ? -31.885 -54.317  -58.882 1.00 40.36  ? 109 GLU E CA  1 
ATOM   8402  C C   . GLU E  1 109 ? -33.196 -53.688  -59.338 1.00 44.89  ? 109 GLU E C   1 
ATOM   8403  O O   . GLU E  1 109 ? -34.261 -53.970  -58.786 1.00 45.93  ? 109 GLU E O   1 
ATOM   8404  C CB  . GLU E  1 109 ? -31.145 -53.363  -57.942 1.00 41.30  ? 109 GLU E CB  1 
ATOM   8405  C CG  . GLU E  1 109 ? -31.921 -52.973  -56.691 1.00 59.20  ? 109 GLU E CG  1 
ATOM   8406  C CD  . GLU E  1 109 ? -32.112 -54.130  -55.728 1.00 72.70  ? 109 GLU E CD  1 
ATOM   8407  O OE1 . GLU E  1 109 ? -31.766 -55.274  -56.089 1.00 73.98  ? 109 GLU E OE1 1 
ATOM   8408  O OE2 . GLU E  1 109 ? -32.606 -53.894  -54.605 1.00 79.04  ? 109 GLU E OE2 1 
ATOM   8409  N N   . GLN E  1 110 ? -33.110 -52.836  -60.355 1.00 43.89  ? 110 GLN E N   1 
ATOM   8410  C CA  . GLN E  1 110 ? -34.280 -52.156  -60.894 1.00 42.13  ? 110 GLN E CA  1 
ATOM   8411  C C   . GLN E  1 110 ? -35.171 -53.123  -61.671 1.00 49.78  ? 110 GLN E C   1 
ATOM   8412  O O   . GLN E  1 110 ? -36.393 -52.982  -61.679 1.00 63.81  ? 110 GLN E O   1 
ATOM   8413  C CB  . GLN E  1 110 ? -33.854 -50.995  -61.796 1.00 54.90  ? 110 GLN E CB  1 
ATOM   8414  C CG  . GLN E  1 110 ? -32.704 -50.165  -61.244 1.00 57.24  ? 110 GLN E CG  1 
ATOM   8415  C CD  . GLN E  1 110 ? -33.087 -48.725  -60.969 1.00 59.23  ? 110 GLN E CD  1 
ATOM   8416  O OE1 . GLN E  1 110 ? -34.246 -48.337  -61.119 1.00 68.36  ? 110 GLN E OE1 1 
ATOM   8417  N NE2 . GLN E  1 110 ? -32.111 -47.922  -60.563 1.00 48.85  ? 110 GLN E NE2 1 
ATOM   8418  N N   . LEU E  1 111 ? -34.552 -54.103  -62.324 1.00 47.64  ? 111 LEU E N   1 
ATOM   8419  C CA  . LEU E  1 111 ? -35.286 -55.093  -63.107 1.00 45.91  ? 111 LEU E CA  1 
ATOM   8420  C C   . LEU E  1 111 ? -35.812 -56.240  -62.251 1.00 48.01  ? 111 LEU E C   1 
ATOM   8421  O O   . LEU E  1 111 ? -36.617 -57.048  -62.713 1.00 50.09  ? 111 LEU E O   1 
ATOM   8422  C CB  . LEU E  1 111 ? -34.399 -55.664  -64.214 1.00 47.11  ? 111 LEU E CB  1 
ATOM   8423  C CG  . LEU E  1 111 ? -34.633 -55.181  -65.647 1.00 46.72  ? 111 LEU E CG  1 
ATOM   8424  C CD1 . LEU E  1 111 ? -35.841 -54.265  -65.733 1.00 61.98  ? 111 LEU E CD1 1 
ATOM   8425  C CD2 . LEU E  1 111 ? -33.394 -54.495  -66.184 1.00 48.98  ? 111 LEU E CD2 1 
ATOM   8426  N N   . SER E  1 112 ? -35.350 -56.311  -61.007 1.00 53.40  ? 112 SER E N   1 
ATOM   8427  C CA  . SER E  1 112 ? -35.670 -57.437  -60.134 1.00 40.03  ? 112 SER E CA  1 
ATOM   8428  C C   . SER E  1 112 ? -37.169 -57.733  -60.091 1.00 43.50  ? 112 SER E C   1 
ATOM   8429  O O   . SER E  1 112 ? -37.578 -58.885  -59.948 1.00 50.17  ? 112 SER E O   1 
ATOM   8430  C CB  . SER E  1 112 ? -35.125 -57.202  -58.721 1.00 45.24  ? 112 SER E CB  1 
ATOM   8431  O OG  . SER E  1 112 ? -35.813 -56.150  -58.065 1.00 54.38  ? 112 SER E OG  1 
ATOM   8432  N N   . SER E  1 113 ? -37.983 -56.689  -60.217 1.00 51.87  ? 113 SER E N   1 
ATOM   8433  C CA  . SER E  1 113 ? -39.432 -56.844  -60.213 1.00 56.08  ? 113 SER E CA  1 
ATOM   8434  C C   . SER E  1 113 ? -40.095 -55.789  -61.079 1.00 56.38  ? 113 SER E C   1 
ATOM   8435  O O   . SER E  1 113 ? -40.016 -54.596  -60.794 1.00 50.93  ? 113 SER E O   1 
ATOM   8436  C CB  . SER E  1 113 ? -39.986 -56.759  -58.792 1.00 54.51  ? 113 SER E CB  1 
ATOM   8437  O OG  . SER E  1 113 ? -41.353 -57.130  -58.761 1.00 53.77  ? 113 SER E OG  1 
ATOM   8438  N N   . VAL E  1 114 ? -40.749 -56.229  -62.143 1.00 50.30  ? 114 VAL E N   1 
ATOM   8439  C CA  . VAL E  1 114 ? -41.494 -55.302  -62.974 1.00 63.10  ? 114 VAL E CA  1 
ATOM   8440  C C   . VAL E  1 114 ? -42.980 -55.617  -62.930 1.00 65.97  ? 114 VAL E C   1 
ATOM   8441  O O   . VAL E  1 114 ? -43.386 -56.770  -62.762 1.00 61.05  ? 114 VAL E O   1 
ATOM   8442  C CB  . VAL E  1 114 ? -41.007 -55.299  -64.435 1.00 66.47  ? 114 VAL E CB  1 
ATOM   8443  C CG1 . VAL E  1 114 ? -39.508 -55.031  -64.492 1.00 53.87  ? 114 VAL E CG1 1 
ATOM   8444  C CG2 . VAL E  1 114 ? -41.387 -56.604  -65.131 1.00 66.51  ? 114 VAL E CG2 1 
ATOM   8445  N N   . SER E  1 115 ? -43.783 -54.570  -63.070 1.00 72.82  ? 115 SER E N   1 
ATOM   8446  C CA  . SER E  1 115 ? -45.230 -54.688  -63.058 1.00 79.35  ? 115 SER E CA  1 
ATOM   8447  C C   . SER E  1 115 ? -45.700 -54.922  -64.493 1.00 85.15  ? 115 SER E C   1 
ATOM   8448  O O   . SER E  1 115 ? -46.505 -55.816  -64.750 1.00 89.73  ? 115 SER E O   1 
ATOM   8449  C CB  . SER E  1 115 ? -45.847 -53.428  -62.449 1.00 78.01  ? 115 SER E CB  1 
ATOM   8450  O OG  . SER E  1 115 ? -47.105 -53.689  -61.850 1.00 94.40  ? 115 SER E OG  1 
ATOM   8451  N N   . SER E  1 116 ? -45.181 -54.129  -65.428 1.00 85.33  ? 116 SER E N   1 
ATOM   8452  C CA  . SER E  1 116 ? -45.370 -54.405  -66.853 1.00 85.23  ? 116 SER E CA  1 
ATOM   8453  C C   . SER E  1 116 ? -44.083 -54.232  -67.646 1.00 77.83  ? 116 SER E C   1 
ATOM   8454  O O   . SER E  1 116 ? -43.251 -53.378  -67.335 1.00 83.40  ? 116 SER E O   1 
ATOM   8455  C CB  . SER E  1 116 ? -46.454 -53.527  -67.461 1.00 98.21  ? 116 SER E CB  1 
ATOM   8456  O OG  . SER E  1 116 ? -46.024 -52.183  -67.565 1.00 114.39 ? 116 SER E OG  1 
ATOM   8457  N N   . PHE E  1 117 ? -43.946 -55.032  -68.695 1.00 73.91  ? 117 PHE E N   1 
ATOM   8458  C CA  . PHE E  1 117 ? -42.695 -55.116  -69.426 1.00 65.18  ? 117 PHE E CA  1 
ATOM   8459  C C   . PHE E  1 117 ? -42.948 -55.539  -70.869 1.00 65.15  ? 117 PHE E C   1 
ATOM   8460  O O   . PHE E  1 117 ? -43.196 -56.713  -71.147 1.00 72.59  ? 117 PHE E O   1 
ATOM   8461  C CB  . PHE E  1 117 ? -41.786 -56.127  -68.729 1.00 59.01  ? 117 PHE E CB  1 
ATOM   8462  C CG  . PHE E  1 117 ? -40.351 -56.046  -69.146 1.00 61.89  ? 117 PHE E CG  1 
ATOM   8463  C CD1 . PHE E  1 117 ? -39.886 -56.793  -70.212 1.00 57.99  ? 117 PHE E CD1 1 
ATOM   8464  C CD2 . PHE E  1 117 ? -39.463 -55.236  -68.459 1.00 60.95  ? 117 PHE E CD2 1 
ATOM   8465  C CE1 . PHE E  1 117 ? -38.563 -56.726  -70.595 1.00 56.42  ? 117 PHE E CE1 1 
ATOM   8466  C CE2 . PHE E  1 117 ? -38.138 -55.164  -68.838 1.00 58.33  ? 117 PHE E CE2 1 
ATOM   8467  C CZ  . PHE E  1 117 ? -37.689 -55.909  -69.908 1.00 57.10  ? 117 PHE E CZ  1 
ATOM   8468  N N   . GLU E  1 118 ? -42.895 -54.579  -71.786 1.00 73.57  ? 118 GLU E N   1 
ATOM   8469  C CA  . GLU E  1 118 ? -43.091 -54.879  -73.199 1.00 82.01  ? 118 GLU E CA  1 
ATOM   8470  C C   . GLU E  1 118 ? -41.915 -54.388  -74.036 1.00 71.62  ? 118 GLU E C   1 
ATOM   8471  O O   . GLU E  1 118 ? -41.468 -53.247  -73.900 1.00 68.05  ? 118 GLU E O   1 
ATOM   8472  C CB  . GLU E  1 118 ? -44.399 -54.278  -73.719 1.00 82.49  ? 118 GLU E CB  1 
ATOM   8473  C CG  . GLU E  1 118 ? -44.291 -52.823  -74.126 1.00 92.61  ? 118 GLU E CG  1 
ATOM   8474  C CD  . GLU E  1 118 ? -45.216 -52.469  -75.271 1.00 128.65 ? 118 GLU E CD  1 
ATOM   8475  O OE1 . GLU E  1 118 ? -45.999 -53.344  -75.698 1.00 139.90 ? 118 GLU E OE1 1 
ATOM   8476  O OE2 . GLU E  1 118 ? -45.159 -51.317  -75.747 1.00 129.03 ? 118 GLU E OE2 1 
ATOM   8477  N N   . ARG E  1 119 ? -41.429 -55.263  -74.907 1.00 71.90  ? 119 ARG E N   1 
ATOM   8478  C CA  . ARG E  1 119 ? -40.251 -54.992  -75.720 1.00 67.52  ? 119 ARG E CA  1 
ATOM   8479  C C   . ARG E  1 119 ? -40.634 -54.531  -77.124 1.00 72.06  ? 119 ARG E C   1 
ATOM   8480  O O   . ARG E  1 119 ? -41.187 -55.299  -77.911 1.00 86.29  ? 119 ARG E O   1 
ATOM   8481  C CB  . ARG E  1 119 ? -39.384 -56.251  -75.786 1.00 57.69  ? 119 ARG E CB  1 
ATOM   8482  C CG  . ARG E  1 119 ? -38.327 -56.256  -76.871 1.00 62.26  ? 119 ARG E CG  1 
ATOM   8483  C CD  . ARG E  1 119 ? -37.653 -57.619  -76.938 1.00 82.62  ? 119 ARG E CD  1 
ATOM   8484  N NE  . ARG E  1 119 ? -36.888 -57.792  -78.169 1.00 96.94  ? 119 ARG E NE  1 
ATOM   8485  C CZ  . ARG E  1 119 ? -37.411 -58.154  -79.338 1.00 109.83 ? 119 ARG E CZ  1 
ATOM   8486  N NH1 . ARG E  1 119 ? -38.714 -58.384  -79.457 1.00 112.52 ? 119 ARG E NH1 1 
ATOM   8487  N NH2 . ARG E  1 119 ? -36.623 -58.282  -80.394 1.00 101.49 ? 119 ARG E NH2 1 
ATOM   8488  N N   . PHE E  1 120 ? -40.336 -53.273  -77.434 1.00 72.37  ? 120 PHE E N   1 
ATOM   8489  C CA  . PHE E  1 120 ? -40.702 -52.699  -78.724 1.00 73.36  ? 120 PHE E CA  1 
ATOM   8490  C C   . PHE E  1 120 ? -39.480 -52.206  -79.487 1.00 71.55  ? 120 PHE E C   1 
ATOM   8491  O O   . PHE E  1 120 ? -38.459 -51.865  -78.890 1.00 72.11  ? 120 PHE E O   1 
ATOM   8492  C CB  . PHE E  1 120 ? -41.693 -51.548  -78.534 1.00 69.45  ? 120 PHE E CB  1 
ATOM   8493  C CG  . PHE E  1 120 ? -41.100 -50.343  -77.862 1.00 67.68  ? 120 PHE E CG  1 
ATOM   8494  C CD1 . PHE E  1 120 ? -40.658 -49.264  -78.610 1.00 75.27  ? 120 PHE E CD1 1 
ATOM   8495  C CD2 . PHE E  1 120 ? -40.984 -50.288  -76.483 1.00 78.39  ? 120 PHE E CD2 1 
ATOM   8496  C CE1 . PHE E  1 120 ? -40.112 -48.153  -77.995 1.00 76.04  ? 120 PHE E CE1 1 
ATOM   8497  C CE2 . PHE E  1 120 ? -40.439 -49.179  -75.862 1.00 72.22  ? 120 PHE E CE2 1 
ATOM   8498  C CZ  . PHE E  1 120 ? -40.002 -48.111  -76.620 1.00 73.00  ? 120 PHE E CZ  1 
ATOM   8499  N N   . GLU E  1 121 ? -39.592 -52.169  -80.810 1.00 77.52  ? 121 GLU E N   1 
ATOM   8500  C CA  . GLU E  1 121 ? -38.509 -51.682  -81.651 1.00 73.79  ? 121 GLU E CA  1 
ATOM   8501  C C   . GLU E  1 121 ? -38.488 -50.158  -81.631 1.00 75.10  ? 121 GLU E C   1 
ATOM   8502  O O   . GLU E  1 121 ? -39.333 -49.507  -82.245 1.00 87.30  ? 121 GLU E O   1 
ATOM   8503  C CB  . GLU E  1 121 ? -38.670 -52.197  -83.083 1.00 81.74  ? 121 GLU E CB  1 
ATOM   8504  C CG  . GLU E  1 121 ? -37.408 -52.108  -83.924 1.00 94.57  ? 121 GLU E CG  1 
ATOM   8505  C CD  . GLU E  1 121 ? -37.565 -52.775  -85.276 1.00 105.13 ? 121 GLU E CD  1 
ATOM   8506  O OE1 . GLU E  1 121 ? -38.720 -52.982  -85.707 1.00 111.88 ? 121 GLU E OE1 1 
ATOM   8507  O OE2 . GLU E  1 121 ? -36.536 -53.092  -85.909 1.00 105.13 ? 121 GLU E OE2 1 
ATOM   8508  N N   . ILE E  1 122 ? -37.523 -49.597  -80.909 1.00 73.68  ? 122 ILE E N   1 
ATOM   8509  C CA  . ILE E  1 122 ? -37.401 -48.149  -80.786 1.00 68.21  ? 122 ILE E CA  1 
ATOM   8510  C C   . ILE E  1 122 ? -36.830 -47.536  -82.059 1.00 72.77  ? 122 ILE E C   1 
ATOM   8511  O O   . ILE E  1 122 ? -37.282 -46.484  -82.510 1.00 84.86  ? 122 ILE E O   1 
ATOM   8512  C CB  . ILE E  1 122 ? -36.530 -47.756  -79.575 1.00 75.68  ? 122 ILE E CB  1 
ATOM   8513  C CG1 . ILE E  1 122 ? -36.325 -46.241  -79.531 1.00 64.89  ? 122 ILE E CG1 1 
ATOM   8514  C CG2 . ILE E  1 122 ? -35.192 -48.481  -79.618 1.00 71.72  ? 122 ILE E CG2 1 
ATOM   8515  C CD1 . ILE E  1 122 ? -35.525 -45.772  -78.335 1.00 51.96  ? 122 ILE E CD1 1 
ATOM   8516  N N   . PHE E  1 123 ? -35.833 -48.199  -82.635 1.00 86.74  ? 123 PHE E N   1 
ATOM   8517  C CA  . PHE E  1 123 ? -35.275 -47.777  -83.911 1.00 74.97  ? 123 PHE E CA  1 
ATOM   8518  C C   . PHE E  1 123 ? -35.288 -48.930  -84.904 1.00 80.85  ? 123 PHE E C   1 
ATOM   8519  O O   . PHE E  1 123 ? -34.370 -49.748  -84.921 1.00 82.97  ? 123 PHE E O   1 
ATOM   8520  C CB  . PHE E  1 123 ? -33.848 -47.249  -83.740 1.00 73.15  ? 123 PHE E CB  1 
ATOM   8521  C CG  . PHE E  1 123 ? -33.755 -46.019  -82.886 1.00 78.02  ? 123 PHE E CG  1 
ATOM   8522  C CD1 . PHE E  1 123 ? -32.991 -46.018  -81.731 1.00 69.95  ? 123 PHE E CD1 1 
ATOM   8523  C CD2 . PHE E  1 123 ? -34.438 -44.866  -83.233 1.00 79.48  ? 123 PHE E CD2 1 
ATOM   8524  C CE1 . PHE E  1 123 ? -32.905 -44.888  -80.942 1.00 70.13  ? 123 PHE E CE1 1 
ATOM   8525  C CE2 . PHE E  1 123 ? -34.357 -43.733  -82.448 1.00 75.95  ? 123 PHE E CE2 1 
ATOM   8526  C CZ  . PHE E  1 123 ? -33.590 -43.744  -81.301 1.00 71.69  ? 123 PHE E CZ  1 
ATOM   8527  N N   . PRO E  1 124 ? -36.338 -49.002  -85.736 1.00 98.21  ? 124 PRO E N   1 
ATOM   8528  C CA  . PRO E  1 124 ? -36.417 -50.039  -86.771 1.00 101.34 ? 124 PRO E CA  1 
ATOM   8529  C C   . PRO E  1 124 ? -35.170 -50.034  -87.647 1.00 100.54 ? 124 PRO E C   1 
ATOM   8530  O O   . PRO E  1 124 ? -34.761 -48.972  -88.109 1.00 98.16  ? 124 PRO E O   1 
ATOM   8531  C CB  . PRO E  1 124 ? -37.631 -49.613  -87.600 1.00 109.78 ? 124 PRO E CB  1 
ATOM   8532  C CG  . PRO E  1 124 ? -38.454 -48.780  -86.680 1.00 103.73 ? 124 PRO E CG  1 
ATOM   8533  C CD  . PRO E  1 124 ? -37.487 -48.081  -85.775 1.00 98.50  ? 124 PRO E CD  1 
ATOM   8534  N N   . LYS E  1 125 ? -34.580 -51.205  -87.867 1.00 97.34  ? 125 LYS E N   1 
ATOM   8535  C CA  . LYS E  1 125 ? -33.380 -51.325  -88.684 1.00 110.76 ? 125 LYS E CA  1 
ATOM   8536  C C   . LYS E  1 125 ? -33.487 -50.585  -90.009 1.00 125.05 ? 125 LYS E C   1 
ATOM   8537  O O   . LYS E  1 125 ? -32.645 -49.749  -90.333 1.00 125.87 ? 125 LYS E O   1 
ATOM   8538  C CB  . LYS E  1 125 ? -33.076 -52.798  -88.964 1.00 105.99 ? 125 LYS E CB  1 
ATOM   8539  C CG  . LYS E  1 125 ? -31.982 -53.377  -88.090 1.00 96.42  ? 125 LYS E CG  1 
ATOM   8540  C CD  . LYS E  1 125 ? -31.745 -54.864  -88.337 1.00 100.41 ? 125 LYS E CD  1 
ATOM   8541  C CE  . LYS E  1 125 ? -31.195 -55.143  -89.729 1.00 101.80 ? 125 LYS E CE  1 
ATOM   8542  N NZ  . LYS E  1 125 ? -30.880 -56.589  -89.936 1.00 99.01  ? 125 LYS E NZ  1 
ATOM   8543  N N   . THR E  1 126 ? -34.538 -50.882  -90.762 1.00 180.02 ? 126 THR E N   1 
ATOM   8544  C CA  . THR E  1 126 ? -34.585 -50.560  -92.187 1.00 180.66 ? 126 THR E CA  1 
ATOM   8545  C C   . THR E  1 126 ? -35.094 -49.170  -92.579 1.00 183.75 ? 126 THR E C   1 
ATOM   8546  O O   . THR E  1 126 ? -35.416 -48.944  -93.746 1.00 200.99 ? 126 THR E O   1 
ATOM   8547  C CB  . THR E  1 126 ? -35.498 -51.574  -92.910 1.00 145.57 ? 126 THR E CB  1 
ATOM   8548  O OG1 . THR E  1 126 ? -36.581 -51.939  -92.039 1.00 137.32 ? 126 THR E OG1 1 
ATOM   8549  N N   . SER E  1 127 ? -35.167 -48.245  -91.631 1.00 123.14 ? 127 SER E N   1 
ATOM   8550  C CA  . SER E  1 127 ? -35.640 -46.909  -91.940 1.00 113.11 ? 127 SER E CA  1 
ATOM   8551  C C   . SER E  1 127 ? -34.888 -45.846  -91.130 1.00 106.06 ? 127 SER E C   1 
ATOM   8552  O O   . SER E  1 127 ? -34.927 -44.659  -91.451 1.00 117.63 ? 127 SER E O   1 
ATOM   8553  C CB  . SER E  1 127 ? -37.148 -46.824  -91.716 1.00 123.49 ? 127 SER E CB  1 
ATOM   8554  O OG  . SER E  1 127 ? -37.477 -47.182  -90.383 1.00 110.42 ? 127 SER E OG  1 
ATOM   8555  N N   . SER E  1 128 ? -34.159 -46.288  -90.111 1.00 106.61 ? 128 SER E N   1 
ATOM   8556  C CA  . SER E  1 128 ? -33.510 -45.375  -89.177 1.00 97.24  ? 128 SER E CA  1 
ATOM   8557  C C   . SER E  1 128 ? -32.077 -45.065  -89.589 1.00 99.56  ? 128 SER E C   1 
ATOM   8558  O O   . SER E  1 128 ? -31.541 -44.001  -89.270 1.00 100.92 ? 128 SER E O   1 
ATOM   8559  C CB  . SER E  1 128 ? -33.537 -45.970  -87.768 1.00 96.05  ? 128 SER E CB  1 
ATOM   8560  O OG  . SER E  1 128 ? -34.862 -46.315  -87.399 1.00 86.94  ? 128 SER E OG  1 
ATOM   8561  N N   . TRP E  1 129 ? -31.467 -45.995  -90.313 1.00 101.12 ? 129 TRP E N   1 
ATOM   8562  C CA  . TRP E  1 129 ? -30.062 -45.872  -90.675 1.00 102.84 ? 129 TRP E CA  1 
ATOM   8563  C C   . TRP E  1 129 ? -29.842 -46.022  -92.178 1.00 106.92 ? 129 TRP E C   1 
ATOM   8564  O O   . TRP E  1 129 ? -29.398 -47.071  -92.646 1.00 107.17 ? 129 TRP E O   1 
ATOM   8565  C CB  . TRP E  1 129 ? -29.241 -46.899  -89.897 1.00 106.52 ? 129 TRP E CB  1 
ATOM   8566  C CG  . TRP E  1 129 ? -29.738 -47.079  -88.495 1.00 92.18  ? 129 TRP E CG  1 
ATOM   8567  C CD1 . TRP E  1 129 ? -30.314 -48.197  -87.965 1.00 86.26  ? 129 TRP E CD1 1 
ATOM   8568  C CD2 . TRP E  1 129 ? -29.730 -46.098  -87.452 1.00 89.42  ? 129 TRP E CD2 1 
ATOM   8569  N NE1 . TRP E  1 129 ? -30.652 -47.977  -86.652 1.00 86.70  ? 129 TRP E NE1 1 
ATOM   8570  C CE2 . TRP E  1 129 ? -30.305 -46.696  -86.313 1.00 89.49  ? 129 TRP E CE2 1 
ATOM   8571  C CE3 . TRP E  1 129 ? -29.286 -44.775  -87.368 1.00 83.88  ? 129 TRP E CE3 1 
ATOM   8572  C CZ2 . TRP E  1 129 ? -30.447 -46.016  -85.105 1.00 90.14  ? 129 TRP E CZ2 1 
ATOM   8573  C CZ3 . TRP E  1 129 ? -29.429 -44.102  -86.169 1.00 81.54  ? 129 TRP E CZ3 1 
ATOM   8574  C CH2 . TRP E  1 129 ? -30.004 -44.723  -85.054 1.00 88.77  ? 129 TRP E CH2 1 
ATOM   8575  N N   . PRO E  1 130 ? -30.152 -44.959  -92.937 1.00 118.41 ? 130 PRO E N   1 
ATOM   8576  C CA  . PRO E  1 130 ? -30.069 -44.917  -94.400 1.00 110.84 ? 130 PRO E CA  1 
ATOM   8577  C C   . PRO E  1 130 ? -28.690 -44.490  -94.889 1.00 119.53 ? 130 PRO E C   1 
ATOM   8578  O O   . PRO E  1 130 ? -28.396 -44.614  -96.078 1.00 121.38 ? 130 PRO E O   1 
ATOM   8579  C CB  . PRO E  1 130 ? -31.093 -43.833  -94.776 1.00 111.54 ? 130 PRO E CB  1 
ATOM   8580  C CG  . PRO E  1 130 ? -31.732 -43.383  -93.469 1.00 106.51 ? 130 PRO E CG  1 
ATOM   8581  C CD  . PRO E  1 130 ? -30.754 -43.731  -92.404 1.00 122.71 ? 130 PRO E CD  1 
ATOM   8582  N N   . ASN E  1 131 ? -27.864 -43.980  -93.983 1.00 119.23 ? 131 ASN E N   1 
ATOM   8583  C CA  . ASN E  1 131 ? -26.530 -43.512  -94.339 1.00 116.35 ? 131 ASN E CA  1 
ATOM   8584  C C   . ASN E  1 131 ? -25.440 -44.391  -93.740 1.00 108.28 ? 131 ASN E C   1 
ATOM   8585  O O   . ASN E  1 131 ? -24.253 -44.079  -93.832 1.00 108.07 ? 131 ASN E O   1 
ATOM   8586  C CB  . ASN E  1 131 ? -26.335 -42.061  -93.894 1.00 119.96 ? 131 ASN E CB  1 
ATOM   8587  C CG  . ASN E  1 131 ? -27.280 -41.105  -94.595 1.00 137.36 ? 131 ASN E CG  1 
ATOM   8588  O OD1 . ASN E  1 131 ? -27.830 -41.419  -95.651 1.00 136.91 ? 131 ASN E OD1 1 
ATOM   8589  N ND2 . ASN E  1 131 ? -27.471 -39.928  -94.011 1.00 143.42 ? 131 ASN E ND2 1 
ATOM   8590  N N   . HIS E  1 132 ? -25.854 -45.494  -93.125 1.00 98.18  ? 132 HIS E N   1 
ATOM   8591  C CA  . HIS E  1 132 ? -24.923 -46.410  -92.481 1.00 93.41  ? 132 HIS E CA  1 
ATOM   8592  C C   . HIS E  1 132 ? -25.339 -47.854  -92.733 1.00 97.81  ? 132 HIS E C   1 
ATOM   8593  O O   . HIS E  1 132 ? -26.509 -48.134  -92.994 1.00 96.07  ? 132 HIS E O   1 
ATOM   8594  C CB  . HIS E  1 132 ? -24.870 -46.136  -90.978 1.00 92.41  ? 132 HIS E CB  1 
ATOM   8595  C CG  . HIS E  1 132 ? -24.686 -44.690  -90.633 1.00 86.75  ? 132 HIS E CG  1 
ATOM   8596  N ND1 . HIS E  1 132 ? -23.472 -44.165  -90.249 1.00 84.05  ? 132 HIS E ND1 1 
ATOM   8597  C CD2 . HIS E  1 132 ? -25.564 -43.660  -90.621 1.00 78.24  ? 132 HIS E CD2 1 
ATOM   8598  C CE1 . HIS E  1 132 ? -23.611 -42.872  -90.011 1.00 89.74  ? 132 HIS E CE1 1 
ATOM   8599  N NE2 . HIS E  1 132 ? -24.869 -42.541  -90.230 1.00 76.29  ? 132 HIS E NE2 1 
ATOM   8600  N N   . ASP E  1 133 ? -24.378 -48.768  -92.653 1.00 83.10  ? 133 ASP E N   1 
ATOM   8601  C CA  . ASP E  1 133 ? -24.659 -50.182  -92.859 1.00 86.22  ? 133 ASP E CA  1 
ATOM   8602  C C   . ASP E  1 133 ? -25.126 -50.827  -91.558 1.00 93.57  ? 133 ASP E C   1 
ATOM   8603  O O   . ASP E  1 133 ? -24.402 -50.836  -90.563 1.00 90.91  ? 133 ASP E O   1 
ATOM   8604  C CB  . ASP E  1 133 ? -23.423 -50.903  -93.402 1.00 93.51  ? 133 ASP E CB  1 
ATOM   8605  C CG  . ASP E  1 133 ? -23.740 -52.285  -93.937 1.00 112.96 ? 133 ASP E CG  1 
ATOM   8606  O OD1 . ASP E  1 133 ? -24.489 -53.029  -93.269 1.00 116.47 ? 133 ASP E OD1 1 
ATOM   8607  O OD2 . ASP E  1 133 ? -23.238 -52.631  -95.027 1.00 123.22 ? 133 ASP E OD2 1 
ATOM   8608  N N   . SER E  1 134 ? -26.342 -51.362  -91.574 1.00 93.99  ? 134 SER E N   1 
ATOM   8609  C CA  . SER E  1 134 ? -26.925 -51.984  -90.392 1.00 91.39  ? 134 SER E CA  1 
ATOM   8610  C C   . SER E  1 134 ? -27.000 -53.499  -90.543 1.00 89.69  ? 134 SER E C   1 
ATOM   8611  O O   . SER E  1 134 ? -27.881 -54.146  -89.977 1.00 101.19 ? 134 SER E O   1 
ATOM   8612  C CB  . SER E  1 134 ? -28.319 -51.412  -90.125 1.00 87.14  ? 134 SER E CB  1 
ATOM   8613  O OG  . SER E  1 134 ? -29.138 -51.509  -91.277 1.00 90.06  ? 134 SER E OG  1 
ATOM   8614  N N   . ASN E  1 135 ? -26.068 -54.060  -91.307 1.00 88.58  ? 135 ASN E N   1 
ATOM   8615  C CA  . ASN E  1 135 ? -26.068 -55.491  -91.590 1.00 100.83 ? 135 ASN E CA  1 
ATOM   8616  C C   . ASN E  1 135 ? -24.718 -56.159  -91.334 1.00 102.07 ? 135 ASN E C   1 
ATOM   8617  O O   . ASN E  1 135 ? -24.654 -57.355  -91.051 1.00 115.48 ? 135 ASN E O   1 
ATOM   8618  C CB  . ASN E  1 135 ? -26.511 -55.744  -93.033 1.00 112.81 ? 135 ASN E CB  1 
ATOM   8619  C CG  . ASN E  1 135 ? -27.950 -55.336  -93.281 1.00 110.47 ? 135 ASN E CG  1 
ATOM   8620  O OD1 . ASN E  1 135 ? -28.841 -55.652  -92.493 1.00 90.62  ? 135 ASN E OD1 1 
ATOM   8621  N ND2 . ASN E  1 135 ? -28.186 -54.634  -94.384 1.00 103.73 ? 135 ASN E ND2 1 
ATOM   8622  N N   . LYS E  1 136 ? -23.644 -55.383  -91.433 1.00 97.08  ? 136 LYS E N   1 
ATOM   8623  C CA  . LYS E  1 136 ? -22.296 -55.926  -91.293 1.00 105.10 ? 136 LYS E CA  1 
ATOM   8624  C C   . LYS E  1 136 ? -21.844 -56.003  -89.838 1.00 108.14 ? 136 LYS E C   1 
ATOM   8625  O O   . LYS E  1 136 ? -20.711 -56.390  -89.554 1.00 110.75 ? 136 LYS E O   1 
ATOM   8626  C CB  . LYS E  1 136 ? -21.301 -55.096  -92.106 1.00 118.69 ? 136 LYS E CB  1 
ATOM   8627  C CG  . LYS E  1 136 ? -21.647 -55.014  -93.578 1.00 123.73 ? 136 LYS E CG  1 
ATOM   8628  C CD  . LYS E  1 136 ? -20.473 -55.405  -94.453 1.00 126.19 ? 136 LYS E CD  1 
ATOM   8629  C CE  . LYS E  1 136 ? -20.962 -55.847  -95.819 1.00 140.31 ? 136 LYS E CE  1 
ATOM   8630  N NZ  . LYS E  1 136 ? -21.955 -56.953  -95.696 1.00 149.82 ? 136 LYS E NZ  1 
ATOM   8631  N N   . GLY E  1 137 ? -22.736 -55.642  -88.923 1.00 95.43  ? 137 GLY E N   1 
ATOM   8632  C CA  . GLY E  1 137 ? -22.400 -55.590  -87.512 1.00 91.29  ? 137 GLY E CA  1 
ATOM   8633  C C   . GLY E  1 137 ? -22.504 -56.921  -86.790 1.00 89.15  ? 137 GLY E C   1 
ATOM   8634  O O   . GLY E  1 137 ? -23.362 -57.100  -85.926 1.00 86.65  ? 137 GLY E O   1 
ATOM   8635  N N   . VAL E  1 138 ? -21.626 -57.855  -87.140 1.00 86.33  ? 138 VAL E N   1 
ATOM   8636  C CA  . VAL E  1 138 ? -21.584 -59.150  -86.469 1.00 91.16  ? 138 VAL E CA  1 
ATOM   8637  C C   . VAL E  1 138 ? -20.168 -59.475  -86.002 1.00 87.65  ? 138 VAL E C   1 
ATOM   8638  O O   . VAL E  1 138 ? -19.219 -58.763  -86.331 1.00 86.36  ? 138 VAL E O   1 
ATOM   8639  C CB  . VAL E  1 138 ? -22.097 -60.282  -87.377 1.00 91.62  ? 138 VAL E CB  1 
ATOM   8640  C CG1 . VAL E  1 138 ? -23.505 -59.972  -87.864 1.00 91.49  ? 138 VAL E CG1 1 
ATOM   8641  C CG2 . VAL E  1 138 ? -21.152 -60.494  -88.550 1.00 88.57  ? 138 VAL E CG2 1 
ATOM   8642  N N   . THR E  1 139 ? -20.031 -60.552  -85.236 1.00 74.18  ? 139 THR E N   1 
ATOM   8643  C CA  . THR E  1 139 ? -18.738 -60.928  -84.676 1.00 87.07  ? 139 THR E CA  1 
ATOM   8644  C C   . THR E  1 139 ? -18.699 -62.397  -84.266 1.00 92.09  ? 139 THR E C   1 
ATOM   8645  O O   . THR E  1 139 ? -19.731 -62.998  -83.972 1.00 85.60  ? 139 THR E O   1 
ATOM   8646  C CB  . THR E  1 139 ? -18.382 -60.057  -83.455 1.00 89.37  ? 139 THR E CB  1 
ATOM   8647  O OG1 . THR E  1 139 ? -17.203 -60.572  -82.824 1.00 86.27  ? 139 THR E OG1 1 
ATOM   8648  C CG2 . THR E  1 139 ? -19.524 -60.056  -82.452 1.00 94.88  ? 139 THR E CG2 1 
ATOM   8649  N N   . ALA E  1 140 ? -17.498 -62.966  -84.247 1.00 103.28 ? 140 ALA E N   1 
ATOM   8650  C CA  . ALA E  1 140 ? -17.311 -64.349  -83.828 1.00 98.31  ? 140 ALA E CA  1 
ATOM   8651  C C   . ALA E  1 140 ? -17.512 -64.485  -82.323 1.00 105.72 ? 140 ALA E C   1 
ATOM   8652  O O   . ALA E  1 140 ? -17.621 -65.593  -81.799 1.00 106.59 ? 140 ALA E O   1 
ATOM   8653  C CB  . ALA E  1 140 ? -15.929 -64.840  -84.226 1.00 108.47 ? 140 ALA E CB  1 
ATOM   8654  N N   . ALA E  1 141 ? -17.559 -63.349  -81.636 1.00 100.87 ? 141 ALA E N   1 
ATOM   8655  C CA  . ALA E  1 141 ? -17.749 -63.331  -80.191 1.00 97.31  ? 141 ALA E CA  1 
ATOM   8656  C C   . ALA E  1 141 ? -19.183 -63.690  -79.813 1.00 93.73  ? 141 ALA E C   1 
ATOM   8657  O O   . ALA E  1 141 ? -19.422 -64.323  -78.788 1.00 95.70  ? 141 ALA E O   1 
ATOM   8658  C CB  . ALA E  1 141 ? -17.376 -61.969  -79.625 1.00 96.61  ? 141 ALA E CB  1 
ATOM   8659  N N   . CYS E  1 142 ? -20.135 -63.282  -80.645 1.00 88.40  ? 142 CYS E N   1 
ATOM   8660  C CA  . CYS E  1 142 ? -21.541 -63.584  -80.402 1.00 86.12  ? 142 CYS E CA  1 
ATOM   8661  C C   . CYS E  1 142 ? -22.073 -64.528  -81.473 1.00 90.00  ? 142 CYS E C   1 
ATOM   8662  O O   . CYS E  1 142 ? -22.810 -64.109  -82.364 1.00 84.05  ? 142 CYS E O   1 
ATOM   8663  C CB  . CYS E  1 142 ? -22.366 -62.296  -80.374 1.00 101.98 ? 142 CYS E CB  1 
ATOM   8664  S SG  . CYS E  1 142 ? -21.783 -61.064  -79.186 1.00 103.31 ? 142 CYS E SG  1 
ATOM   8665  N N   . PRO E  1 143 ? -21.700 -65.814  -81.385 1.00 91.81  ? 143 PRO E N   1 
ATOM   8666  C CA  . PRO E  1 143 ? -22.013 -66.804  -82.419 1.00 97.76  ? 143 PRO E CA  1 
ATOM   8667  C C   . PRO E  1 143 ? -23.427 -67.361  -82.305 1.00 108.33 ? 143 PRO E C   1 
ATOM   8668  O O   . PRO E  1 143 ? -23.866 -67.722  -81.214 1.00 114.17 ? 143 PRO E O   1 
ATOM   8669  C CB  . PRO E  1 143 ? -21.005 -67.932  -82.142 1.00 109.78 ? 143 PRO E CB  1 
ATOM   8670  C CG  . PRO E  1 143 ? -20.083 -67.413  -81.057 1.00 106.24 ? 143 PRO E CG  1 
ATOM   8671  C CD  . PRO E  1 143 ? -20.877 -66.398  -80.317 1.00 99.68  ? 143 PRO E CD  1 
ATOM   8672  N N   . HIS E  1 144 ? -24.126 -67.431  -83.433 1.00 120.18 ? 144 HIS E N   1 
ATOM   8673  C CA  . HIS E  1 144 ? -25.402 -68.128  -83.495 1.00 123.99 ? 144 HIS E CA  1 
ATOM   8674  C C   . HIS E  1 144 ? -25.243 -69.331  -84.417 1.00 135.09 ? 144 HIS E C   1 
ATOM   8675  O O   . HIS E  1 144 ? -25.278 -69.197  -85.641 1.00 130.27 ? 144 HIS E O   1 
ATOM   8676  C CB  . HIS E  1 144 ? -26.510 -67.199  -83.994 1.00 114.31 ? 144 HIS E CB  1 
ATOM   8677  C CG  . HIS E  1 144 ? -27.883 -67.605  -83.552 1.00 122.25 ? 144 HIS E CG  1 
ATOM   8678  N ND1 . HIS E  1 144 ? -28.983 -67.543  -84.380 1.00 128.63 ? 144 HIS E ND1 1 
ATOM   8679  C CD2 . HIS E  1 144 ? -28.331 -68.084  -82.367 1.00 124.58 ? 144 HIS E CD2 1 
ATOM   8680  C CE1 . HIS E  1 144 ? -30.050 -67.961  -83.724 1.00 130.76 ? 144 HIS E CE1 1 
ATOM   8681  N NE2 . HIS E  1 144 ? -29.682 -68.297  -82.500 1.00 126.27 ? 144 HIS E NE2 1 
ATOM   8682  N N   . ALA E  1 145 ? -25.047 -70.501  -83.817 1.00 139.66 ? 145 ALA E N   1 
ATOM   8683  C CA  . ALA E  1 145 ? -24.805 -71.728  -84.569 1.00 137.00 ? 145 ALA E CA  1 
ATOM   8684  C C   . ALA E  1 145 ? -23.689 -71.546  -85.593 1.00 146.41 ? 145 ALA E C   1 
ATOM   8685  O O   . ALA E  1 145 ? -23.938 -71.533  -86.799 1.00 134.78 ? 145 ALA E O   1 
ATOM   8686  C CB  . ALA E  1 145 ? -26.082 -72.198  -85.249 1.00 120.54 ? 145 ALA E CB  1 
ATOM   8687  N N   . GLY E  1 146 ? -22.461 -71.400  -85.106 1.00 199.45 ? 146 GLY E N   1 
ATOM   8688  C CA  . GLY E  1 146 ? -21.306 -71.251  -85.972 1.00 201.74 ? 146 GLY E CA  1 
ATOM   8689  C C   . GLY E  1 146 ? -21.176 -69.870  -86.588 1.00 200.38 ? 146 GLY E C   1 
ATOM   8690  O O   . GLY E  1 146 ? -20.109 -69.259  -86.542 1.00 197.37 ? 146 GLY E O   1 
ATOM   8691  N N   . ALA E  1 147 ? -22.267 -69.377  -87.166 1.00 143.50 ? 147 ALA E N   1 
ATOM   8692  C CA  . ALA E  1 147 ? -22.261 -68.085  -87.844 1.00 145.77 ? 147 ALA E CA  1 
ATOM   8693  C C   . ALA E  1 147 ? -21.987 -66.929  -86.886 1.00 133.03 ? 147 ALA E C   1 
ATOM   8694  O O   . ALA E  1 147 ? -22.355 -66.981  -85.712 1.00 128.68 ? 147 ALA E O   1 
ATOM   8695  C CB  . ALA E  1 147 ? -23.578 -67.867  -88.577 1.00 138.91 ? 147 ALA E CB  1 
ATOM   8696  N N   . LYS E  1 148 ? -21.336 -65.888  -87.397 1.00 117.23 ? 148 LYS E N   1 
ATOM   8697  C CA  . LYS E  1 148 ? -21.050 -64.695  -86.607 1.00 112.74 ? 148 LYS E CA  1 
ATOM   8698  C C   . LYS E  1 148 ? -22.304 -63.841  -86.466 1.00 111.99 ? 148 LYS E C   1 
ATOM   8699  O O   . LYS E  1 148 ? -22.829 -63.330  -87.455 1.00 99.17  ? 148 LYS E O   1 
ATOM   8700  C CB  . LYS E  1 148 ? -19.937 -63.871  -87.258 1.00 104.03 ? 148 LYS E CB  1 
ATOM   8701  C CG  . LYS E  1 148 ? -18.610 -64.596  -87.396 1.00 115.77 ? 148 LYS E CG  1 
ATOM   8702  C CD  . LYS E  1 148 ? -17.544 -63.675  -87.970 1.00 118.93 ? 148 LYS E CD  1 
ATOM   8703  C CE  . LYS E  1 148 ? -17.982 -63.092  -89.304 1.00 118.66 ? 148 LYS E CE  1 
ATOM   8704  N NZ  . LYS E  1 148 ? -16.984 -62.132  -89.851 1.00 118.00 ? 148 LYS E NZ  1 
ATOM   8705  N N   . SER E  1 149 ? -22.779 -63.685  -85.235 1.00 109.42 ? 149 SER E N   1 
ATOM   8706  C CA  . SER E  1 149 ? -23.997 -62.922  -84.986 1.00 104.86 ? 149 SER E CA  1 
ATOM   8707  C C   . SER E  1 149 ? -23.742 -61.742  -84.050 1.00 98.88  ? 149 SER E C   1 
ATOM   8708  O O   . SER E  1 149 ? -22.613 -61.267  -83.928 1.00 84.37  ? 149 SER E O   1 
ATOM   8709  C CB  . SER E  1 149 ? -25.088 -63.832  -84.416 1.00 98.42  ? 149 SER E CB  1 
ATOM   8710  O OG  . SER E  1 149 ? -26.353 -63.195  -84.443 1.00 113.13 ? 149 SER E OG  1 
ATOM   8711  N N   . PHE E  1 150 ? -24.799 -61.275  -83.395 1.00 100.88 ? 150 PHE E N   1 
ATOM   8712  C CA  . PHE E  1 150 ? -24.705 -60.139  -82.486 1.00 85.12  ? 150 PHE E CA  1 
ATOM   8713  C C   . PHE E  1 150 ? -25.939 -60.083  -81.592 1.00 83.05  ? 150 PHE E C   1 
ATOM   8714  O O   . PHE E  1 150 ? -26.859 -60.886  -81.744 1.00 83.46  ? 150 PHE E O   1 
ATOM   8715  C CB  . PHE E  1 150 ? -24.565 -58.838  -83.280 1.00 72.22  ? 150 PHE E CB  1 
ATOM   8716  C CG  . PHE E  1 150 ? -24.136 -57.663  -82.450 1.00 67.71  ? 150 PHE E CG  1 
ATOM   8717  C CD1 . PHE E  1 150 ? -22.890 -57.647  -81.846 1.00 63.54  ? 150 PHE E CD1 1 
ATOM   8718  C CD2 . PHE E  1 150 ? -24.969 -56.569  -82.286 1.00 67.41  ? 150 PHE E CD2 1 
ATOM   8719  C CE1 . PHE E  1 150 ? -22.487 -56.568  -81.085 1.00 59.13  ? 150 PHE E CE1 1 
ATOM   8720  C CE2 . PHE E  1 150 ? -24.571 -55.485  -81.526 1.00 73.04  ? 150 PHE E CE2 1 
ATOM   8721  C CZ  . PHE E  1 150 ? -23.328 -55.485  -80.925 1.00 62.90  ? 150 PHE E CZ  1 
ATOM   8722  N N   . TYR E  1 151 ? -25.952 -59.139  -80.656 1.00 88.90  ? 151 TYR E N   1 
ATOM   8723  C CA  . TYR E  1 151 ? -27.109 -58.948  -79.791 1.00 75.47  ? 151 TYR E CA  1 
ATOM   8724  C C   . TYR E  1 151 ? -28.325 -58.582  -80.634 1.00 72.40  ? 151 TYR E C   1 
ATOM   8725  O O   . TYR E  1 151 ? -28.217 -57.823  -81.597 1.00 79.26  ? 151 TYR E O   1 
ATOM   8726  C CB  . TYR E  1 151 ? -26.836 -57.852  -78.759 1.00 75.38  ? 151 TYR E CB  1 
ATOM   8727  C CG  . TYR E  1 151 ? -25.579 -58.070  -77.946 1.00 59.19  ? 151 TYR E CG  1 
ATOM   8728  C CD1 . TYR E  1 151 ? -25.565 -58.954  -76.876 1.00 66.51  ? 151 TYR E CD1 1 
ATOM   8729  C CD2 . TYR E  1 151 ? -24.409 -57.384  -78.243 1.00 57.35  ? 151 TYR E CD2 1 
ATOM   8730  C CE1 . TYR E  1 151 ? -24.419 -59.154  -76.128 1.00 65.01  ? 151 TYR E CE1 1 
ATOM   8731  C CE2 . TYR E  1 151 ? -23.258 -57.577  -77.501 1.00 52.78  ? 151 TYR E CE2 1 
ATOM   8732  C CZ  . TYR E  1 151 ? -23.269 -58.463  -76.445 1.00 66.86  ? 151 TYR E CZ  1 
ATOM   8733  O OH  . TYR E  1 151 ? -22.127 -58.660  -75.703 1.00 65.00  ? 151 TYR E OH  1 
ATOM   8734  N N   . LYS E  1 152 ? -29.482 -59.127  -80.272 1.00 67.04  ? 152 LYS E N   1 
ATOM   8735  C CA  . LYS E  1 152 ? -30.708 -58.883  -81.023 1.00 76.03  ? 152 LYS E CA  1 
ATOM   8736  C C   . LYS E  1 152 ? -31.243 -57.475  -80.785 1.00 77.05  ? 152 LYS E C   1 
ATOM   8737  O O   . LYS E  1 152 ? -31.740 -56.827  -81.706 1.00 86.43  ? 152 LYS E O   1 
ATOM   8738  C CB  . LYS E  1 152 ? -31.779 -59.911  -80.648 1.00 78.64  ? 152 LYS E CB  1 
ATOM   8739  C CG  . LYS E  1 152 ? -31.387 -61.351  -80.927 1.00 102.85 ? 152 LYS E CG  1 
ATOM   8740  C CD  . LYS E  1 152 ? -31.131 -61.578  -82.407 1.00 128.76 ? 152 LYS E CD  1 
ATOM   8741  C CE  . LYS E  1 152 ? -30.773 -63.028  -82.689 1.00 137.30 ? 152 LYS E CE  1 
ATOM   8742  N NZ  . LYS E  1 152 ? -30.494 -63.260  -84.132 1.00 135.61 ? 152 LYS E NZ  1 
ATOM   8743  N N   . ASN E  1 153 ? -31.134 -57.008  -79.546 1.00 68.56  ? 153 ASN E N   1 
ATOM   8744  C CA  . ASN E  1 153 ? -31.707 -55.725  -79.155 1.00 66.00  ? 153 ASN E CA  1 
ATOM   8745  C C   . ASN E  1 153 ? -30.812 -54.530  -79.470 1.00 63.38  ? 153 ASN E C   1 
ATOM   8746  O O   . ASN E  1 153 ? -31.161 -53.388  -79.173 1.00 64.19  ? 153 ASN E O   1 
ATOM   8747  C CB  . ASN E  1 153 ? -32.072 -55.742  -77.670 1.00 59.63  ? 153 ASN E CB  1 
ATOM   8748  C CG  . ASN E  1 153 ? -33.098 -56.807  -77.338 1.00 70.23  ? 153 ASN E CG  1 
ATOM   8749  O OD1 . ASN E  1 153 ? -33.838 -57.263  -78.210 1.00 80.64  ? 153 ASN E OD1 1 
ATOM   8750  N ND2 . ASN E  1 153 ? -33.149 -57.208  -76.074 1.00 76.03  ? 153 ASN E ND2 1 
ATOM   8751  N N   . LEU E  1 154 ? -29.660 -54.799  -80.075 1.00 65.62  ? 154 LEU E N   1 
ATOM   8752  C CA  . LEU E  1 154 ? -28.738 -53.741  -80.468 1.00 78.82  ? 154 LEU E CA  1 
ATOM   8753  C C   . LEU E  1 154 ? -28.249 -53.949  -81.895 1.00 75.07  ? 154 LEU E C   1 
ATOM   8754  O O   . LEU E  1 154 ? -28.218 -55.074  -82.394 1.00 84.45  ? 154 LEU E O   1 
ATOM   8755  C CB  . LEU E  1 154 ? -27.543 -53.683  -79.515 1.00 68.67  ? 154 LEU E CB  1 
ATOM   8756  C CG  . LEU E  1 154 ? -27.843 -53.382  -78.046 1.00 61.02  ? 154 LEU E CG  1 
ATOM   8757  C CD1 . LEU E  1 154 ? -26.593 -53.564  -77.198 1.00 63.67  ? 154 LEU E CD1 1 
ATOM   8758  C CD2 . LEU E  1 154 ? -28.409 -51.978  -77.887 1.00 70.41  ? 154 LEU E CD2 1 
ATOM   8759  N N   . ILE E  1 155 ? -27.871 -52.856  -82.548 1.00 78.35  ? 155 ILE E N   1 
ATOM   8760  C CA  . ILE E  1 155 ? -27.334 -52.922  -83.899 1.00 87.63  ? 155 ILE E CA  1 
ATOM   8761  C C   . ILE E  1 155 ? -25.969 -52.263  -83.965 1.00 78.41  ? 155 ILE E C   1 
ATOM   8762  O O   . ILE E  1 155 ? -25.819 -51.087  -83.634 1.00 74.10  ? 155 ILE E O   1 
ATOM   8763  C CB  . ILE E  1 155 ? -28.243 -52.221  -84.913 1.00 86.39  ? 155 ILE E CB  1 
ATOM   8764  C CG1 . ILE E  1 155 ? -29.615 -52.891  -84.952 1.00 88.40  ? 155 ILE E CG1 1 
ATOM   8765  C CG2 . ILE E  1 155 ? -27.597 -52.238  -86.292 1.00 71.82  ? 155 ILE E CG2 1 
ATOM   8766  C CD1 . ILE E  1 155 ? -30.650 -52.080  -85.681 1.00 102.21 ? 155 ILE E CD1 1 
ATOM   8767  N N   . TRP E  1 156 ? -24.975 -53.028  -84.399 1.00 75.08  ? 156 TRP E N   1 
ATOM   8768  C CA  . TRP E  1 156 ? -23.622 -52.514  -84.521 1.00 79.81  ? 156 TRP E CA  1 
ATOM   8769  C C   . TRP E  1 156 ? -23.439 -51.826  -85.868 1.00 85.53  ? 156 TRP E C   1 
ATOM   8770  O O   . TRP E  1 156 ? -23.085 -52.464  -86.858 1.00 97.05  ? 156 TRP E O   1 
ATOM   8771  C CB  . TRP E  1 156 ? -22.611 -53.648  -84.363 1.00 77.62  ? 156 TRP E CB  1 
ATOM   8772  C CG  . TRP E  1 156 ? -21.201 -53.174  -84.242 1.00 81.75  ? 156 TRP E CG  1 
ATOM   8773  C CD1 . TRP E  1 156 ? -20.755 -51.887  -84.346 1.00 76.54  ? 156 TRP E CD1 1 
ATOM   8774  C CD2 . TRP E  1 156 ? -20.046 -53.982  -83.991 1.00 80.57  ? 156 TRP E CD2 1 
ATOM   8775  N NE1 . TRP E  1 156 ? -19.392 -51.843  -84.177 1.00 89.88  ? 156 TRP E NE1 1 
ATOM   8776  C CE2 . TRP E  1 156 ? -18.933 -53.115  -83.958 1.00 81.14  ? 156 TRP E CE2 1 
ATOM   8777  C CE3 . TRP E  1 156 ? -19.844 -55.351  -83.793 1.00 82.33  ? 156 TRP E CE3 1 
ATOM   8778  C CZ2 . TRP E  1 156 ? -17.640 -53.574  -83.735 1.00 89.88  ? 156 TRP E CZ2 1 
ATOM   8779  C CZ3 . TRP E  1 156 ? -18.558 -55.805  -83.571 1.00 87.98  ? 156 TRP E CZ3 1 
ATOM   8780  C CH2 . TRP E  1 156 ? -17.471 -54.918  -83.544 1.00 93.24  ? 156 TRP E CH2 1 
ATOM   8781  N N   . LEU E  1 157 ? -23.687 -50.521  -85.899 1.00 69.33  ? 157 LEU E N   1 
ATOM   8782  C CA  . LEU E  1 157 ? -23.568 -49.755  -87.133 1.00 63.91  ? 157 LEU E CA  1 
ATOM   8783  C C   . LEU E  1 157 ? -22.118 -49.612  -87.573 1.00 74.14  ? 157 LEU E C   1 
ATOM   8784  O O   . LEU E  1 157 ? -21.248 -49.252  -86.780 1.00 75.44  ? 157 LEU E O   1 
ATOM   8785  C CB  . LEU E  1 157 ? -24.194 -48.369  -86.975 1.00 68.51  ? 157 LEU E CB  1 
ATOM   8786  C CG  . LEU E  1 157 ? -25.718 -48.308  -86.862 1.00 79.30  ? 157 LEU E CG  1 
ATOM   8787  C CD1 . LEU E  1 157 ? -26.191 -46.863  -86.923 1.00 76.29  ? 157 LEU E CD1 1 
ATOM   8788  C CD2 . LEU E  1 157 ? -26.392 -49.149  -87.939 1.00 78.96  ? 157 LEU E CD2 1 
ATOM   8789  N N   . VAL E  1 158 ? -21.870 -49.899  -88.846 1.00 84.63  ? 158 VAL E N   1 
ATOM   8790  C CA  . VAL E  1 158 ? -20.548 -49.722  -89.433 1.00 80.85  ? 158 VAL E CA  1 
ATOM   8791  C C   . VAL E  1 158 ? -20.643 -48.795  -90.639 1.00 86.15  ? 158 VAL E C   1 
ATOM   8792  O O   . VAL E  1 158 ? -21.739 -48.474  -91.099 1.00 88.62  ? 158 VAL E O   1 
ATOM   8793  C CB  . VAL E  1 158 ? -19.933 -51.065  -89.868 1.00 77.84  ? 158 VAL E CB  1 
ATOM   8794  C CG1 . VAL E  1 158 ? -19.731 -51.973  -88.665 1.00 78.19  ? 158 VAL E CG1 1 
ATOM   8795  C CG2 . VAL E  1 158 ? -20.811 -51.738  -90.911 1.00 87.01  ? 158 VAL E CG2 1 
ATOM   8796  N N   . LYS E  1 159 ? -19.494 -48.367  -91.152 1.00 100.40 ? 159 LYS E N   1 
ATOM   8797  C CA  . LYS E  1 159 ? -19.465 -47.443  -92.279 1.00 106.34 ? 159 LYS E CA  1 
ATOM   8798  C C   . LYS E  1 159 ? -20.063 -48.073  -93.533 1.00 99.96  ? 159 LYS E C   1 
ATOM   8799  O O   . LYS E  1 159 ? -19.831 -49.247  -93.822 1.00 90.65  ? 159 LYS E O   1 
ATOM   8800  C CB  . LYS E  1 159 ? -18.035 -46.977  -92.560 1.00 103.52 ? 159 LYS E CB  1 
ATOM   8801  C CG  . LYS E  1 159 ? -17.121 -48.071  -93.084 1.00 96.81  ? 159 LYS E CG  1 
ATOM   8802  C CD  . LYS E  1 159 ? -15.764 -47.514  -93.476 1.00 106.64 ? 159 LYS E CD  1 
ATOM   8803  C CE  . LYS E  1 159 ? -14.905 -48.577  -94.140 1.00 106.59 ? 159 LYS E CE  1 
ATOM   8804  N NZ  . LYS E  1 159 ? -13.567 -48.049  -94.524 1.00 115.64 ? 159 LYS E NZ  1 
ATOM   8805  N N   . LYS E  1 160 ? -20.838 -47.287  -94.273 1.00 110.98 ? 160 LYS E N   1 
ATOM   8806  C CA  . LYS E  1 160 ? -21.426 -47.752  -95.522 1.00 121.45 ? 160 LYS E CA  1 
ATOM   8807  C C   . LYS E  1 160 ? -20.512 -47.437  -96.698 1.00 128.59 ? 160 LYS E C   1 
ATOM   8808  O O   . LYS E  1 160 ? -20.537 -46.329  -97.233 1.00 125.76 ? 160 LYS E O   1 
ATOM   8809  C CB  . LYS E  1 160 ? -22.798 -47.115  -95.747 1.00 115.50 ? 160 LYS E CB  1 
ATOM   8810  C CG  . LYS E  1 160 ? -23.415 -47.456  -97.094 1.00 113.07 ? 160 LYS E CG  1 
ATOM   8811  C CD  . LYS E  1 160 ? -24.781 -46.818  -97.256 1.00 120.21 ? 160 LYS E CD  1 
ATOM   8812  C CE  . LYS E  1 160 ? -25.707 -47.221  -96.124 1.00 125.90 ? 160 LYS E CE  1 
ATOM   8813  N NZ  . LYS E  1 160 ? -27.118 -46.844  -96.402 1.00 130.41 ? 160 LYS E NZ  1 
ATOM   8814  N N   . GLY E  1 161 ? -19.706 -48.417  -97.093 1.00 131.56 ? 161 GLY E N   1 
ATOM   8815  C CA  . GLY E  1 161 ? -18.792 -48.251  -98.207 1.00 127.31 ? 161 GLY E CA  1 
ATOM   8816  C C   . GLY E  1 161 ? -17.905 -47.021  -98.191 1.00 133.01 ? 161 GLY E C   1 
ATOM   8817  O O   . GLY E  1 161 ? -17.944 -46.206  -99.113 1.00 129.19 ? 161 GLY E O   1 
ATOM   8818  N N   . ASN E  1 162 ? -17.112 -46.883  -97.132 1.00 129.42 ? 162 ASN E N   1 
ATOM   8819  C CA  . ASN E  1 162 ? -16.151 -45.788  -97.017 1.00 135.15 ? 162 ASN E CA  1 
ATOM   8820  C C   . ASN E  1 162 ? -16.826 -44.485  -96.594 1.00 131.79 ? 162 ASN E C   1 
ATOM   8821  O O   . ASN E  1 162 ? -16.332 -43.401  -96.902 1.00 132.72 ? 162 ASN E O   1 
ATOM   8822  C CB  . ASN E  1 162 ? -15.360 -45.560  -98.308 1.00 147.63 ? 162 ASN E CB  1 
ATOM   8823  C CG  . ASN E  1 162 ? -13.951 -46.110  -98.235 1.00 156.94 ? 162 ASN E CG  1 
ATOM   8824  O OD1 . ASN E  1 162 ? -13.177 -45.993  -99.184 1.00 178.16 ? 162 ASN E OD1 1 
ATOM   8825  N ND2 . ASN E  1 162 ? -13.608 -46.710  -97.101 1.00 143.29 ? 162 ASN E ND2 1 
ATOM   8826  N N   . SER E  1 163 ? -17.945 -44.585  -95.885 1.00 130.59 ? 163 SER E N   1 
ATOM   8827  C CA  . SER E  1 163 ? -18.647 -43.386  -95.440 1.00 130.94 ? 163 SER E CA  1 
ATOM   8828  C C   . SER E  1 163 ? -19.363 -43.575  -94.106 1.00 115.22 ? 163 SER E C   1 
ATOM   8829  O O   . SER E  1 163 ? -20.222 -44.445  -93.966 1.00 109.38 ? 163 SER E O   1 
ATOM   8830  C CB  . SER E  1 163 ? -19.639 -42.914  -96.508 1.00 125.74 ? 163 SER E CB  1 
ATOM   8831  O OG  . SER E  1 163 ? -20.150 -41.629  -96.197 1.00 112.76 ? 163 SER E OG  1 
ATOM   8832  N N   . TYR E  1 164 ? -18.995 -42.754  -93.129 1.00 93.16  ? 164 TYR E N   1 
ATOM   8833  C CA  . TYR E  1 164 ? -19.692 -42.720  -91.851 1.00 96.54  ? 164 TYR E CA  1 
ATOM   8834  C C   . TYR E  1 164 ? -19.990 -41.275  -91.476 1.00 92.19  ? 164 TYR E C   1 
ATOM   8835  O O   . TYR E  1 164 ? -19.227 -40.648  -90.740 1.00 71.08  ? 164 TYR E O   1 
ATOM   8836  C CB  . TYR E  1 164 ? -18.861 -43.382  -90.753 1.00 102.41 ? 164 TYR E CB  1 
ATOM   8837  C CG  . TYR E  1 164 ? -19.664 -43.760  -89.529 1.00 92.75  ? 164 TYR E CG  1 
ATOM   8838  C CD1 . TYR E  1 164 ? -19.799 -45.088  -89.147 1.00 85.38  ? 164 TYR E CD1 1 
ATOM   8839  C CD2 . TYR E  1 164 ? -20.298 -42.791  -88.763 1.00 88.48  ? 164 TYR E CD2 1 
ATOM   8840  C CE1 . TYR E  1 164 ? -20.534 -45.440  -88.032 1.00 82.32  ? 164 TYR E CE1 1 
ATOM   8841  C CE2 . TYR E  1 164 ? -21.038 -43.134  -87.649 1.00 87.26  ? 164 TYR E CE2 1 
ATOM   8842  C CZ  . TYR E  1 164 ? -21.152 -44.459  -87.288 1.00 89.70  ? 164 TYR E CZ  1 
ATOM   8843  O OH  . TYR E  1 164 ? -21.886 -44.805  -86.177 1.00 86.32  ? 164 TYR E OH  1 
ATOM   8844  N N   . PRO E  1 165 ? -21.104 -40.741  -91.994 1.00 81.49  ? 165 PRO E N   1 
ATOM   8845  C CA  . PRO E  1 165 ? -21.538 -39.363  -91.745 1.00 90.56  ? 165 PRO E CA  1 
ATOM   8846  C C   . PRO E  1 165 ? -22.092 -39.220  -90.336 1.00 90.19  ? 165 PRO E C   1 
ATOM   8847  O O   . PRO E  1 165 ? -22.620 -40.190  -89.794 1.00 80.44  ? 165 PRO E O   1 
ATOM   8848  C CB  . PRO E  1 165 ? -22.671 -39.162  -92.763 1.00 79.89  ? 165 PRO E CB  1 
ATOM   8849  C CG  . PRO E  1 165 ? -22.573 -40.326  -93.718 1.00 97.42  ? 165 PRO E CG  1 
ATOM   8850  C CD  . PRO E  1 165 ? -22.013 -41.442  -92.912 1.00 75.81  ? 165 PRO E CD  1 
ATOM   8851  N N   . LYS E  1 166 ? -21.972 -38.033  -89.749 1.00 72.23  ? 166 LYS E N   1 
ATOM   8852  C CA  . LYS E  1 166 ? -22.562 -37.791  -88.439 1.00 81.77  ? 166 LYS E CA  1 
ATOM   8853  C C   . LYS E  1 166 ? -24.020 -38.223  -88.438 1.00 91.61  ? 166 LYS E C   1 
ATOM   8854  O O   . LYS E  1 166 ? -24.830 -37.709  -89.212 1.00 83.06  ? 166 LYS E O   1 
ATOM   8855  C CB  . LYS E  1 166 ? -22.473 -36.316  -88.051 1.00 78.71  ? 166 LYS E CB  1 
ATOM   8856  C CG  . LYS E  1 166 ? -23.434 -35.938  -86.931 1.00 88.75  ? 166 LYS E CG  1 
ATOM   8857  C CD  . LYS E  1 166 ? -23.481 -34.437  -86.699 1.00 92.22  ? 166 LYS E CD  1 
ATOM   8858  C CE  . LYS E  1 166 ? -22.237 -33.942  -85.982 1.00 102.62 ? 166 LYS E CE  1 
ATOM   8859  N NZ  . LYS E  1 166 ? -22.357 -32.503  -85.617 1.00 116.51 ? 166 LYS E NZ  1 
ATOM   8860  N N   . LEU E  1 167 ? -24.352 -39.170  -87.571 1.00 95.62  ? 167 LEU E N   1 
ATOM   8861  C CA  . LEU E  1 167 ? -25.727 -39.626  -87.454 1.00 86.48  ? 167 LEU E CA  1 
ATOM   8862  C C   . LEU E  1 167 ? -26.412 -38.911  -86.293 1.00 75.14  ? 167 LEU E C   1 
ATOM   8863  O O   . LEU E  1 167 ? -25.756 -38.513  -85.331 1.00 69.34  ? 167 LEU E O   1 
ATOM   8864  C CB  . LEU E  1 167 ? -25.773 -41.155  -87.322 1.00 74.92  ? 167 LEU E CB  1 
ATOM   8865  C CG  . LEU E  1 167 ? -26.108 -41.935  -86.040 1.00 77.01  ? 167 LEU E CG  1 
ATOM   8866  C CD1 . LEU E  1 167 ? -25.634 -43.377  -86.188 1.00 78.57  ? 167 LEU E CD1 1 
ATOM   8867  C CD2 . LEU E  1 167 ? -25.591 -41.316  -84.748 1.00 82.03  ? 167 LEU E CD2 1 
ATOM   8868  N N   . SER E  1 168 ? -27.723 -38.724  -86.393 1.00 77.30  ? 168 SER E N   1 
ATOM   8869  C CA  . SER E  1 168 ? -28.445 -37.971  -85.375 1.00 79.06  ? 168 SER E CA  1 
ATOM   8870  C C   . SER E  1 168 ? -29.904 -38.401  -85.270 1.00 85.39  ? 168 SER E C   1 
ATOM   8871  O O   . SER E  1 168 ? -30.796 -37.763  -85.830 1.00 102.03 ? 168 SER E O   1 
ATOM   8872  C CB  . SER E  1 168 ? -28.350 -36.470  -85.655 1.00 87.72  ? 168 SER E CB  1 
ATOM   8873  O OG  . SER E  1 168 ? -28.609 -35.714  -84.485 1.00 98.79  ? 168 SER E OG  1 
ATOM   8874  N N   . LYS E  1 169 ? -30.134 -39.493  -84.549 1.00 81.50  ? 169 LYS E N   1 
ATOM   8875  C CA  . LYS E  1 169 ? -31.479 -39.990  -84.298 1.00 77.33  ? 169 LYS E CA  1 
ATOM   8876  C C   . LYS E  1 169 ? -31.901 -39.646  -82.877 1.00 81.12  ? 169 LYS E C   1 
ATOM   8877  O O   . LYS E  1 169 ? -31.064 -39.541  -81.981 1.00 85.72  ? 169 LYS E O   1 
ATOM   8878  C CB  . LYS E  1 169 ? -31.530 -41.506  -84.500 1.00 73.20  ? 169 LYS E CB  1 
ATOM   8879  C CG  . LYS E  1 169 ? -32.238 -41.956  -85.767 1.00 86.74  ? 169 LYS E CG  1 
ATOM   8880  C CD  . LYS E  1 169 ? -33.740 -41.748  -85.664 1.00 89.63  ? 169 LYS E CD  1 
ATOM   8881  C CE  . LYS E  1 169 ? -34.476 -42.480  -86.776 1.00 97.62  ? 169 LYS E CE  1 
ATOM   8882  N NZ  . LYS E  1 169 ? -34.038 -42.035  -88.126 1.00 105.34 ? 169 LYS E NZ  1 
ATOM   8883  N N   . SER E  1 170 ? -33.202 -39.468  -82.673 1.00 83.25  ? 170 SER E N   1 
ATOM   8884  C CA  . SER E  1 170 ? -33.729 -39.183  -81.344 1.00 81.12  ? 170 SER E CA  1 
ATOM   8885  C C   . SER E  1 170 ? -35.168 -39.671  -81.201 1.00 72.87  ? 170 SER E C   1 
ATOM   8886  O O   . SER E  1 170 ? -36.032 -39.339  -82.011 1.00 76.29  ? 170 SER E O   1 
ATOM   8887  C CB  . SER E  1 170 ? -33.634 -37.688  -81.028 1.00 86.48  ? 170 SER E CB  1 
ATOM   8888  O OG  . SER E  1 170 ? -34.286 -36.911  -82.016 1.00 104.08 ? 170 SER E OG  1 
ATOM   8889  N N   . TYR E  1 171 ? -35.411 -40.465  -80.164 1.00 76.75  ? 171 TYR E N   1 
ATOM   8890  C CA  . TYR E  1 171 ? -36.732 -41.025  -79.909 1.00 74.12  ? 171 TYR E CA  1 
ATOM   8891  C C   . TYR E  1 171 ? -37.398 -40.338  -78.724 1.00 70.28  ? 171 TYR E C   1 
ATOM   8892  O O   . TYR E  1 171 ? -36.734 -39.984  -77.750 1.00 70.51  ? 171 TYR E O   1 
ATOM   8893  C CB  . TYR E  1 171 ? -36.626 -42.532  -79.657 1.00 76.43  ? 171 TYR E CB  1 
ATOM   8894  C CG  . TYR E  1 171 ? -37.788 -43.119  -78.888 1.00 69.52  ? 171 TYR E CG  1 
ATOM   8895  C CD1 . TYR E  1 171 ? -38.913 -43.599  -79.545 1.00 68.47  ? 171 TYR E CD1 1 
ATOM   8896  C CD2 . TYR E  1 171 ? -37.755 -43.201  -77.501 1.00 73.08  ? 171 TYR E CD2 1 
ATOM   8897  C CE1 . TYR E  1 171 ? -39.975 -44.138  -78.843 1.00 76.98  ? 171 TYR E CE1 1 
ATOM   8898  C CE2 . TYR E  1 171 ? -38.811 -43.737  -76.791 1.00 73.23  ? 171 TYR E CE2 1 
ATOM   8899  C CZ  . TYR E  1 171 ? -39.918 -44.205  -77.466 1.00 81.00  ? 171 TYR E CZ  1 
ATOM   8900  O OH  . TYR E  1 171 ? -40.972 -44.741  -76.761 1.00 80.45  ? 171 TYR E OH  1 
ATOM   8901  N N   . ILE E  1 172 ? -38.711 -40.151  -78.811 1.00 69.19  ? 172 ILE E N   1 
ATOM   8902  C CA  . ILE E  1 172 ? -39.465 -39.539  -77.723 1.00 74.59  ? 172 ILE E CA  1 
ATOM   8903  C C   . ILE E  1 172 ? -40.429 -40.541  -77.089 1.00 75.98  ? 172 ILE E C   1 
ATOM   8904  O O   . ILE E  1 172 ? -41.177 -41.228  -77.785 1.00 74.61  ? 172 ILE E O   1 
ATOM   8905  C CB  . ILE E  1 172 ? -40.228 -38.280  -78.193 1.00 69.55  ? 172 ILE E CB  1 
ATOM   8906  C CG1 . ILE E  1 172 ? -40.904 -37.592  -77.006 1.00 78.37  ? 172 ILE E CG1 1 
ATOM   8907  C CG2 . ILE E  1 172 ? -41.241 -38.634  -79.272 1.00 91.29  ? 172 ILE E CG2 1 
ATOM   8908  C CD1 . ILE E  1 172 ? -40.680 -36.096  -76.962 1.00 83.06  ? 172 ILE E CD1 1 
ATOM   8909  N N   . ASN E  1 173 ? -40.398 -40.622  -75.762 1.00 72.54  ? 173 ASN E N   1 
ATOM   8910  C CA  . ASN E  1 173 ? -41.200 -41.596  -75.030 1.00 67.24  ? 173 ASN E CA  1 
ATOM   8911  C C   . ASN E  1 173 ? -42.697 -41.314  -75.110 1.00 83.46  ? 173 ASN E C   1 
ATOM   8912  O O   . ASN E  1 173 ? -43.237 -40.530  -74.328 1.00 79.25  ? 173 ASN E O   1 
ATOM   8913  C CB  . ASN E  1 173 ? -40.752 -41.672  -73.569 1.00 72.88  ? 173 ASN E CB  1 
ATOM   8914  C CG  . ASN E  1 173 ? -41.378 -42.836  -72.826 1.00 81.02  ? 173 ASN E CG  1 
ATOM   8915  O OD1 . ASN E  1 173 ? -42.196 -43.573  -73.377 1.00 81.40  ? 173 ASN E OD1 1 
ATOM   8916  N ND2 . ASN E  1 173 ? -40.994 -43.010  -71.567 1.00 72.70  ? 173 ASN E ND2 1 
ATOM   8917  N N   . ASP E  1 174 ? -43.358 -41.967  -76.060 1.00 93.20  ? 174 ASP E N   1 
ATOM   8918  C CA  . ASP E  1 174 ? -44.796 -41.825  -76.246 1.00 92.40  ? 174 ASP E CA  1 
ATOM   8919  C C   . ASP E  1 174 ? -45.546 -42.921  -75.501 1.00 93.20  ? 174 ASP E C   1 
ATOM   8920  O O   . ASP E  1 174 ? -46.733 -43.149  -75.741 1.00 110.17 ? 174 ASP E O   1 
ATOM   8921  C CB  . ASP E  1 174 ? -45.144 -41.904  -77.726 1.00 102.59 ? 174 ASP E CB  1 
ATOM   8922  C CG  . ASP E  1 174 ? -44.759 -43.234  -78.333 1.00 118.69 ? 174 ASP E CG  1 
ATOM   8923  O OD1 . ASP E  1 174 ? -45.625 -44.132  -78.402 1.00 125.33 ? 174 ASP E OD1 1 
ATOM   8924  O OD2 . ASP E  1 174 ? -43.584 -43.387  -78.725 1.00 119.99 ? 174 ASP E OD2 1 
ATOM   8925  N N   . LYS E  1 175 ? -44.843 -43.609  -74.609 1.00 90.41  ? 175 LYS E N   1 
ATOM   8926  C CA  . LYS E  1 175 ? -45.475 -44.597  -73.748 1.00 86.18  ? 175 LYS E CA  1 
ATOM   8927  C C   . LYS E  1 175 ? -45.949 -43.887  -72.489 1.00 90.77  ? 175 LYS E C   1 
ATOM   8928  O O   . LYS E  1 175 ? -45.637 -42.715  -72.279 1.00 92.03  ? 175 LYS E O   1 
ATOM   8929  C CB  . LYS E  1 175 ? -44.491 -45.711  -73.384 1.00 77.20  ? 175 LYS E CB  1 
ATOM   8930  C CG  . LYS E  1 175 ? -43.826 -46.392  -74.573 1.00 79.24  ? 175 LYS E CG  1 
ATOM   8931  C CD  . LYS E  1 175 ? -44.808 -47.234  -75.377 1.00 70.74  ? 175 LYS E CD  1 
ATOM   8932  C CE  . LYS E  1 175 ? -44.088 -48.008  -76.473 1.00 68.83  ? 175 LYS E CE  1 
ATOM   8933  N NZ  . LYS E  1 175 ? -44.997 -48.928  -77.209 1.00 93.16  ? 175 LYS E NZ  1 
ATOM   8934  N N   . GLY E  1 176 ? -46.702 -44.592  -71.654 1.00 73.03  ? 176 GLY E N   1 
ATOM   8935  C CA  . GLY E  1 176 ? -47.155 -44.034  -70.394 1.00 91.05  ? 176 GLY E CA  1 
ATOM   8936  C C   . GLY E  1 176 ? -46.322 -44.564  -69.247 1.00 90.79  ? 176 GLY E C   1 
ATOM   8937  O O   . GLY E  1 176 ? -46.699 -44.456  -68.081 1.00 93.10  ? 176 GLY E O   1 
ATOM   8938  N N   . LYS E  1 177 ? -45.179 -45.143  -69.592 1.00 87.31  ? 177 LYS E N   1 
ATOM   8939  C CA  . LYS E  1 177 ? -44.287 -45.738  -68.610 1.00 73.67  ? 177 LYS E CA  1 
ATOM   8940  C C   . LYS E  1 177 ? -42.848 -45.480  -69.018 1.00 67.80  ? 177 LYS E C   1 
ATOM   8941  O O   . LYS E  1 177 ? -42.569 -45.190  -70.180 1.00 75.20  ? 177 LYS E O   1 
ATOM   8942  C CB  . LYS E  1 177 ? -44.541 -47.240  -68.525 1.00 68.39  ? 177 LYS E CB  1 
ATOM   8943  C CG  . LYS E  1 177 ? -44.509 -47.933  -69.876 1.00 70.45  ? 177 LYS E CG  1 
ATOM   8944  C CD  . LYS E  1 177 ? -45.037 -49.352  -69.789 1.00 75.62  ? 177 LYS E CD  1 
ATOM   8945  C CE  . LYS E  1 177 ? -46.505 -49.369  -69.403 1.00 93.61  ? 177 LYS E CE  1 
ATOM   8946  N NZ  . LYS E  1 177 ? -47.368 -48.755  -70.447 1.00 96.37  ? 177 LYS E NZ  1 
ATOM   8947  N N   . GLU E  1 178 ? -41.934 -45.579  -68.061 1.00 64.93  ? 178 GLU E N   1 
ATOM   8948  C CA  . GLU E  1 178 ? -40.524 -45.393  -68.360 1.00 61.90  ? 178 GLU E CA  1 
ATOM   8949  C C   . GLU E  1 178 ? -40.106 -46.351  -69.464 1.00 64.20  ? 178 GLU E C   1 
ATOM   8950  O O   . GLU E  1 178 ? -40.698 -47.417  -69.630 1.00 65.81  ? 178 GLU E O   1 
ATOM   8951  C CB  . GLU E  1 178 ? -39.675 -45.636  -67.116 1.00 59.22  ? 178 GLU E CB  1 
ATOM   8952  C CG  . GLU E  1 178 ? -39.988 -44.706  -65.963 1.00 88.55  ? 178 GLU E CG  1 
ATOM   8953  C CD  . GLU E  1 178 ? -39.268 -45.108  -64.696 1.00 91.51  ? 178 GLU E CD  1 
ATOM   8954  O OE1 . GLU E  1 178 ? -39.288 -46.311  -64.363 1.00 89.84  ? 178 GLU E OE1 1 
ATOM   8955  O OE2 . GLU E  1 178 ? -38.683 -44.224  -64.035 1.00 95.98  ? 178 GLU E OE2 1 
ATOM   8956  N N   . VAL E  1 179 ? -39.093 -45.962  -70.226 1.00 52.74  ? 179 VAL E N   1 
ATOM   8957  C CA  . VAL E  1 179 ? -38.547 -46.832  -71.256 1.00 61.54  ? 179 VAL E CA  1 
ATOM   8958  C C   . VAL E  1 179 ? -37.063 -47.068  -71.020 1.00 61.64  ? 179 VAL E C   1 
ATOM   8959  O O   . VAL E  1 179 ? -36.273 -46.124  -70.972 1.00 54.48  ? 179 VAL E O   1 
ATOM   8960  C CB  . VAL E  1 179 ? -38.753 -46.253  -72.666 1.00 57.60  ? 179 VAL E CB  1 
ATOM   8961  C CG1 . VAL E  1 179 ? -37.910 -47.015  -73.674 1.00 59.09  ? 179 VAL E CG1 1 
ATOM   8962  C CG2 . VAL E  1 179 ? -40.224 -46.301  -73.049 1.00 63.10  ? 179 VAL E CG2 1 
ATOM   8963  N N   . LEU E  1 180 ? -36.692 -48.333  -70.861 1.00 53.94  ? 180 LEU E N   1 
ATOM   8964  C CA  . LEU E  1 180 ? -35.295 -48.700  -70.689 1.00 46.31  ? 180 LEU E CA  1 
ATOM   8965  C C   . LEU E  1 180 ? -34.599 -48.739  -72.040 1.00 49.37  ? 180 LEU E C   1 
ATOM   8966  O O   . LEU E  1 180 ? -34.901 -49.588  -72.878 1.00 62.46  ? 180 LEU E O   1 
ATOM   8967  C CB  . LEU E  1 180 ? -35.177 -50.065  -70.011 1.00 46.08  ? 180 LEU E CB  1 
ATOM   8968  C CG  . LEU E  1 180 ? -33.752 -50.594  -69.838 1.00 47.15  ? 180 LEU E CG  1 
ATOM   8969  C CD1 . LEU E  1 180 ? -33.013 -49.802  -68.770 1.00 43.16  ? 180 LEU E CD1 1 
ATOM   8970  C CD2 . LEU E  1 180 ? -33.767 -52.074  -69.493 1.00 46.10  ? 180 LEU E CD2 1 
ATOM   8971  N N   . VAL E  1 181 ? -33.669 -47.815  -72.251 1.00 50.82  ? 181 VAL E N   1 
ATOM   8972  C CA  . VAL E  1 181 ? -32.904 -47.780  -73.489 1.00 48.72  ? 181 VAL E CA  1 
ATOM   8973  C C   . VAL E  1 181 ? -31.465 -48.211  -73.237 1.00 54.23  ? 181 VAL E C   1 
ATOM   8974  O O   . VAL E  1 181 ? -30.788 -47.668  -72.365 1.00 55.34  ? 181 VAL E O   1 
ATOM   8975  C CB  . VAL E  1 181 ? -32.906 -46.377  -74.120 1.00 43.81  ? 181 VAL E CB  1 
ATOM   8976  C CG1 . VAL E  1 181 ? -32.257 -46.417  -75.494 1.00 55.71  ? 181 VAL E CG1 1 
ATOM   8977  C CG2 . VAL E  1 181 ? -34.325 -45.843  -74.217 1.00 46.21  ? 181 VAL E CG2 1 
ATOM   8978  N N   . LEU E  1 182 ? -31.005 -49.197  -73.999 1.00 55.85  ? 182 LEU E N   1 
ATOM   8979  C CA  . LEU E  1 182 ? -29.628 -49.659  -73.890 1.00 56.23  ? 182 LEU E CA  1 
ATOM   8980  C C   . LEU E  1 182 ? -28.854 -49.359  -75.165 1.00 51.96  ? 182 LEU E C   1 
ATOM   8981  O O   . LEU E  1 182 ? -29.403 -49.416  -76.265 1.00 61.45  ? 182 LEU E O   1 
ATOM   8982  C CB  . LEU E  1 182 ? -29.577 -51.158  -73.589 1.00 41.49  ? 182 LEU E CB  1 
ATOM   8983  C CG  . LEU E  1 182 ? -30.139 -51.599  -72.237 1.00 53.63  ? 182 LEU E CG  1 
ATOM   8984  C CD1 . LEU E  1 182 ? -31.442 -52.354  -72.426 1.00 65.88  ? 182 LEU E CD1 1 
ATOM   8985  C CD2 . LEU E  1 182 ? -29.129 -52.454  -71.488 1.00 52.20  ? 182 LEU E CD2 1 
ATOM   8986  N N   . TRP E  1 183 ? -27.577 -49.033  -75.007 1.00 54.01  ? 183 TRP E N   1 
ATOM   8987  C CA  . TRP E  1 183 ? -26.705 -48.788  -76.147 1.00 57.84  ? 183 TRP E CA  1 
ATOM   8988  C C   . TRP E  1 183 ? -25.272 -49.165  -75.800 1.00 44.71  ? 183 TRP E C   1 
ATOM   8989  O O   . TRP E  1 183 ? -24.948 -49.397  -74.636 1.00 50.28  ? 183 TRP E O   1 
ATOM   8990  C CB  . TRP E  1 183 ? -26.781 -47.324  -76.585 1.00 58.77  ? 183 TRP E CB  1 
ATOM   8991  C CG  . TRP E  1 183 ? -26.138 -46.368  -75.629 1.00 49.77  ? 183 TRP E CG  1 
ATOM   8992  C CD1 . TRP E  1 183 ? -24.848 -45.926  -75.659 1.00 49.67  ? 183 TRP E CD1 1 
ATOM   8993  C CD2 . TRP E  1 183 ? -26.755 -45.730  -74.505 1.00 54.26  ? 183 TRP E CD2 1 
ATOM   8994  N NE1 . TRP E  1 183 ? -24.622 -45.054  -74.622 1.00 49.49  ? 183 TRP E NE1 1 
ATOM   8995  C CE2 . TRP E  1 183 ? -25.777 -44.916  -73.899 1.00 57.95  ? 183 TRP E CE2 1 
ATOM   8996  C CE3 . TRP E  1 183 ? -28.038 -45.769  -73.951 1.00 56.13  ? 183 TRP E CE3 1 
ATOM   8997  C CZ2 . TRP E  1 183 ? -26.042 -44.148  -72.767 1.00 56.13  ? 183 TRP E CZ2 1 
ATOM   8998  C CZ3 . TRP E  1 183 ? -28.298 -45.005  -72.827 1.00 58.51  ? 183 TRP E CZ3 1 
ATOM   8999  C CH2 . TRP E  1 183 ? -27.305 -44.206  -72.247 1.00 55.68  ? 183 TRP E CH2 1 
ATOM   9000  N N   . GLY E  1 184 ? -24.416 -49.228  -76.813 1.00 48.96  ? 184 GLY E N   1 
ATOM   9001  C CA  . GLY E  1 184 ? -23.036 -49.621  -76.604 1.00 48.45  ? 184 GLY E CA  1 
ATOM   9002  C C   . GLY E  1 184 ? -22.038 -48.700  -77.274 1.00 55.23  ? 184 GLY E C   1 
ATOM   9003  O O   . GLY E  1 184 ? -22.315 -48.115  -78.320 1.00 50.91  ? 184 GLY E O   1 
ATOM   9004  N N   . ILE E  1 185 ? -20.870 -48.567  -76.656 1.00 57.15  ? 185 ILE E N   1 
ATOM   9005  C CA  . ILE E  1 185 ? -19.771 -47.814  -77.242 1.00 44.10  ? 185 ILE E CA  1 
ATOM   9006  C C   . ILE E  1 185 ? -18.632 -48.777  -77.541 1.00 53.19  ? 185 ILE E C   1 
ATOM   9007  O O   . ILE E  1 185 ? -18.050 -49.362  -76.627 1.00 55.05  ? 185 ILE E O   1 
ATOM   9008  C CB  . ILE E  1 185 ? -19.262 -46.717  -76.290 1.00 49.76  ? 185 ILE E CB  1 
ATOM   9009  C CG1 . ILE E  1 185 ? -20.420 -45.833  -75.825 1.00 50.14  ? 185 ILE E CG1 1 
ATOM   9010  C CG2 . ILE E  1 185 ? -18.183 -45.883  -76.967 1.00 52.35  ? 185 ILE E CG2 1 
ATOM   9011  C CD1 . ILE E  1 185 ? -21.150 -45.143  -76.953 1.00 50.63  ? 185 ILE E CD1 1 
ATOM   9012  N N   . HIS E  1 186 ? -18.320 -48.950  -78.821 1.00 55.89  ? 186 HIS E N   1 
ATOM   9013  C CA  . HIS E  1 186 ? -17.273 -49.883  -79.218 1.00 62.92  ? 186 HIS E CA  1 
ATOM   9014  C C   . HIS E  1 186 ? -15.894 -49.232  -79.233 1.00 58.34  ? 186 HIS E C   1 
ATOM   9015  O O   . HIS E  1 186 ? -15.707 -48.154  -79.799 1.00 64.94  ? 186 HIS E O   1 
ATOM   9016  C CB  . HIS E  1 186 ? -17.580 -50.506  -80.581 1.00 62.60  ? 186 HIS E CB  1 
ATOM   9017  C CG  . HIS E  1 186 ? -16.494 -51.403  -81.090 1.00 70.64  ? 186 HIS E CG  1 
ATOM   9018  N ND1 . HIS E  1 186 ? -15.709 -51.080  -82.176 1.00 69.30  ? 186 HIS E ND1 1 
ATOM   9019  C CD2 . HIS E  1 186 ? -16.052 -52.605  -80.651 1.00 65.80  ? 186 HIS E CD2 1 
ATOM   9020  C CE1 . HIS E  1 186 ? -14.836 -52.048  -82.389 1.00 76.18  ? 186 HIS E CE1 1 
ATOM   9021  N NE2 . HIS E  1 186 ? -15.023 -52.985  -81.477 1.00 66.02  ? 186 HIS E NE2 1 
ATOM   9022  N N   . HIS E  1 187 ? -14.933 -49.895  -78.600 1.00 61.62  ? 187 HIS E N   1 
ATOM   9023  C CA  . HIS E  1 187 ? -13.554 -49.426  -78.585 1.00 62.76  ? 187 HIS E CA  1 
ATOM   9024  C C   . HIS E  1 187 ? -12.665 -50.409  -79.338 1.00 74.98  ? 187 HIS E C   1 
ATOM   9025  O O   . HIS E  1 187 ? -12.263 -51.434  -78.788 1.00 74.12  ? 187 HIS E O   1 
ATOM   9026  C CB  . HIS E  1 187 ? -13.058 -49.259  -77.148 1.00 67.48  ? 187 HIS E CB  1 
ATOM   9027  C CG  . HIS E  1 187 ? -13.925 -48.377  -76.307 1.00 63.51  ? 187 HIS E CG  1 
ATOM   9028  N ND1 . HIS E  1 187 ? -13.777 -47.007  -76.262 1.00 64.02  ? 187 HIS E ND1 1 
ATOM   9029  C CD2 . HIS E  1 187 ? -14.953 -48.668  -75.473 1.00 64.85  ? 187 HIS E CD2 1 
ATOM   9030  C CE1 . HIS E  1 187 ? -14.673 -46.494  -75.441 1.00 72.75  ? 187 HIS E CE1 1 
ATOM   9031  N NE2 . HIS E  1 187 ? -15.400 -47.481  -74.948 1.00 72.71  ? 187 HIS E NE2 1 
ATOM   9032  N N   . PRO E  1 188 ? -12.363 -50.100  -80.608 1.00 72.71  ? 188 PRO E N   1 
ATOM   9033  C CA  . PRO E  1 188 ? -11.534 -50.960  -81.459 1.00 73.66  ? 188 PRO E CA  1 
ATOM   9034  C C   . PRO E  1 188 ? -10.152 -51.200  -80.862 1.00 74.15  ? 188 PRO E C   1 
ATOM   9035  O O   . PRO E  1 188 ? -9.702  -50.432  -80.011 1.00 72.26  ? 188 PRO E O   1 
ATOM   9036  C CB  . PRO E  1 188 ? -11.418 -50.156  -82.757 1.00 72.06  ? 188 PRO E CB  1 
ATOM   9037  C CG  . PRO E  1 188 ? -12.623 -49.284  -82.766 1.00 66.90  ? 188 PRO E CG  1 
ATOM   9038  C CD  . PRO E  1 188 ? -12.853 -48.916  -81.333 1.00 63.74  ? 188 PRO E CD  1 
ATOM   9039  N N   . SER E  1 189 ? -9.488  -52.259  -81.312 1.00 77.90  ? 189 SER E N   1 
ATOM   9040  C CA  . SER E  1 189 ? -8.181  -52.629  -80.784 1.00 75.70  ? 189 SER E CA  1 
ATOM   9041  C C   . SER E  1 189 ? -7.057  -51.817  -81.418 1.00 78.14  ? 189 SER E C   1 
ATOM   9042  O O   . SER E  1 189 ? -6.102  -51.431  -80.745 1.00 79.99  ? 189 SER E O   1 
ATOM   9043  C CB  . SER E  1 189 ? -7.930  -54.125  -80.988 1.00 77.39  ? 189 SER E CB  1 
ATOM   9044  O OG  . SER E  1 189 ? -8.064  -54.483  -82.352 1.00 87.99  ? 189 SER E OG  1 
ATOM   9045  N N   . THR E  1 190 ? -7.179  -51.558  -82.715 1.00 87.79  ? 190 THR E N   1 
ATOM   9046  C CA  . THR E  1 190 ? -6.148  -50.834  -83.451 1.00 88.86  ? 190 THR E CA  1 
ATOM   9047  C C   . THR E  1 190 ? -6.733  -49.682  -84.262 1.00 84.57  ? 190 THR E C   1 
ATOM   9048  O O   . THR E  1 190 ? -7.909  -49.700  -84.625 1.00 86.76  ? 190 THR E O   1 
ATOM   9049  C CB  . THR E  1 190 ? -5.365  -51.778  -84.384 1.00 90.34  ? 190 THR E CB  1 
ATOM   9050  O OG1 . THR E  1 190 ? -4.926  -51.055  -85.541 1.00 107.63 ? 190 THR E OG1 1 
ATOM   9051  C CG2 . THR E  1 190 ? -6.244  -52.937  -84.826 1.00 84.93  ? 190 THR E CG2 1 
ATOM   9052  N N   . SER E  1 191 ? -5.905  -48.678  -84.539 1.00 90.89  ? 191 SER E N   1 
ATOM   9053  C CA  . SER E  1 191 ? -6.334  -47.526  -85.324 1.00 92.65  ? 191 SER E CA  1 
ATOM   9054  C C   . SER E  1 191 ? -6.699  -47.948  -86.744 1.00 88.59  ? 191 SER E C   1 
ATOM   9055  O O   . SER E  1 191 ? -7.449  -47.257  -87.434 1.00 86.07  ? 191 SER E O   1 
ATOM   9056  C CB  . SER E  1 191 ? -5.245  -46.452  -85.350 1.00 81.60  ? 191 SER E CB  1 
ATOM   9057  O OG  . SER E  1 191 ? -4.065  -46.934  -85.968 1.00 99.92  ? 191 SER E OG  1 
ATOM   9058  N N   . ALA E  1 192 ? -6.161  -49.085  -87.173 1.00 95.87  ? 192 ALA E N   1 
ATOM   9059  C CA  . ALA E  1 192 ? -6.501  -49.647  -88.473 1.00 104.10 ? 192 ALA E CA  1 
ATOM   9060  C C   . ALA E  1 192 ? -7.916  -50.212  -88.438 1.00 103.24 ? 192 ALA E C   1 
ATOM   9061  O O   . ALA E  1 192 ? -8.673  -50.075  -89.398 1.00 93.39  ? 192 ALA E O   1 
ATOM   9062  C CB  . ALA E  1 192 ? -5.504  -50.726  -88.863 1.00 110.80 ? 192 ALA E CB  1 
ATOM   9063  N N   . ASP E  1 193 ? -8.264  -50.848  -87.324 1.00 107.54 ? 193 ASP E N   1 
ATOM   9064  C CA  . ASP E  1 193 ? -9.613  -51.363  -87.122 1.00 91.85  ? 193 ASP E CA  1 
ATOM   9065  C C   . ASP E  1 193 ? -10.618 -50.221  -87.025 1.00 85.97  ? 193 ASP E C   1 
ATOM   9066  O O   . ASP E  1 193 ? -11.773 -50.361  -87.426 1.00 78.16  ? 193 ASP E O   1 
ATOM   9067  C CB  . ASP E  1 193 ? -9.682  -52.220  -85.855 1.00 89.28  ? 193 ASP E CB  1 
ATOM   9068  C CG  . ASP E  1 193 ? -9.577  -53.704  -86.147 1.00 117.25 ? 193 ASP E CG  1 
ATOM   9069  O OD1 . ASP E  1 193 ? -8.754  -54.089  -87.004 1.00 119.29 ? 193 ASP E OD1 1 
ATOM   9070  O OD2 . ASP E  1 193 ? -10.319 -54.486  -85.515 1.00 136.73 ? 193 ASP E OD2 1 
ATOM   9071  N N   . GLN E  1 194 ? -10.167 -49.092  -86.488 1.00 83.15  ? 194 GLN E N   1 
ATOM   9072  C CA  . GLN E  1 194 ? -11.020 -47.920  -86.322 1.00 79.10  ? 194 GLN E CA  1 
ATOM   9073  C C   . GLN E  1 194 ? -11.508 -47.381  -87.662 1.00 88.87  ? 194 GLN E C   1 
ATOM   9074  O O   . GLN E  1 194 ? -12.712 -47.266  -87.892 1.00 89.67  ? 194 GLN E O   1 
ATOM   9075  C CB  . GLN E  1 194 ? -10.277 -46.824  -85.555 1.00 85.13  ? 194 GLN E CB  1 
ATOM   9076  C CG  . GLN E  1 194 ? -10.980 -45.473  -85.551 1.00 83.13  ? 194 GLN E CG  1 
ATOM   9077  C CD  . GLN E  1 194 ? -12.240 -45.462  -84.706 1.00 81.69  ? 194 GLN E CD  1 
ATOM   9078  O OE1 . GLN E  1 194 ? -13.058 -44.547  -84.805 1.00 76.15  ? 194 GLN E OE1 1 
ATOM   9079  N NE2 . GLN E  1 194 ? -12.402 -46.478  -83.868 1.00 72.53  ? 194 GLN E NE2 1 
ATOM   9080  N N   . GLN E  1 195 ? -10.570 -47.048  -88.542 1.00 110.56 ? 195 GLN E N   1 
ATOM   9081  C CA  . GLN E  1 195 ? -10.913 -46.521  -89.858 1.00 116.78 ? 195 GLN E CA  1 
ATOM   9082  C C   . GLN E  1 195 ? -11.548 -47.595  -90.738 1.00 113.89 ? 195 GLN E C   1 
ATOM   9083  O O   . GLN E  1 195 ? -12.300 -47.288  -91.662 1.00 111.55 ? 195 GLN E O   1 
ATOM   9084  C CB  . GLN E  1 195 ? -9.680  -45.921  -90.540 1.00 118.93 ? 195 GLN E CB  1 
ATOM   9085  C CG  . GLN E  1 195 ? -8.492  -46.864  -90.635 1.00 137.70 ? 195 GLN E CG  1 
ATOM   9086  C CD  . GLN E  1 195 ? -7.241  -46.173  -91.143 1.00 158.92 ? 195 GLN E CD  1 
ATOM   9087  O OE1 . GLN E  1 195 ? -6.190  -46.797  -91.294 1.00 151.18 ? 195 GLN E OE1 1 
ATOM   9088  N NE2 . GLN E  1 195 ? -7.348  -44.876  -91.408 1.00 167.08 ? 195 GLN E NE2 1 
ATOM   9089  N N   . SER E  1 196 ? -11.242 -48.854  -90.441 1.00 96.35  ? 196 SER E N   1 
ATOM   9090  C CA  . SER E  1 196 ? -11.830 -49.977  -91.161 1.00 88.56  ? 196 SER E CA  1 
ATOM   9091  C C   . SER E  1 196 ? -13.321 -50.073  -90.869 1.00 103.08 ? 196 SER E C   1 
ATOM   9092  O O   . SER E  1 196 ? -14.113 -50.451  -91.734 1.00 101.19 ? 196 SER E O   1 
ATOM   9093  C CB  . SER E  1 196 ? -11.144 -51.285  -90.765 1.00 85.09  ? 196 SER E CB  1 
ATOM   9094  O OG  . SER E  1 196 ? -11.806 -52.401  -91.333 1.00 98.22  ? 196 SER E OG  1 
ATOM   9095  N N   . LEU E  1 197 ? -13.695 -49.724  -89.643 1.00 99.40  ? 197 LEU E N   1 
ATOM   9096  C CA  . LEU E  1 197 ? -15.081 -49.820  -89.203 1.00 89.87  ? 197 LEU E CA  1 
ATOM   9097  C C   . LEU E  1 197 ? -15.871 -48.524  -89.399 1.00 90.89  ? 197 LEU E C   1 
ATOM   9098  O O   . LEU E  1 197 ? -17.024 -48.562  -89.827 1.00 80.59  ? 197 LEU E O   1 
ATOM   9099  C CB  . LEU E  1 197 ? -15.151 -50.266  -87.739 1.00 93.20  ? 197 LEU E CB  1 
ATOM   9100  C CG  . LEU E  1 197 ? -14.942 -51.756  -87.459 1.00 83.02  ? 197 LEU E CG  1 
ATOM   9101  C CD1 . LEU E  1 197 ? -14.705 -52.000  -85.976 1.00 73.79  ? 197 LEU E CD1 1 
ATOM   9102  C CD2 . LEU E  1 197 ? -16.133 -52.562  -87.955 1.00 76.26  ? 197 LEU E CD2 1 
ATOM   9103  N N   . TYR E  1 198 ? -15.269 -47.408  -89.005 1.00 90.96  ? 198 TYR E N   1 
ATOM   9104  C CA  . TYR E  1 198 ? -15.894 -46.096  -89.104 1.00 100.10 ? 198 TYR E CA  1 
ATOM   9105  C C   . TYR E  1 198 ? -14.766 -45.213  -89.593 1.00 108.94 ? 198 TYR E C   1 
ATOM   9106  O O   . TYR E  1 198 ? -13.911 -44.783  -88.818 1.00 97.79  ? 198 TYR E O   1 
ATOM   9107  C CB  . TYR E  1 198 ? -16.416 -45.640  -87.742 1.00 106.73 ? 198 TYR E CB  1 
ATOM   9108  C CG  . TYR E  1 198 ? -16.571 -46.761  -86.739 1.00 91.22  ? 198 TYR E CG  1 
ATOM   9109  C CD1 . TYR E  1 198 ? -15.522 -47.124  -85.905 1.00 90.01  ? 198 TYR E CD1 1 
ATOM   9110  C CD2 . TYR E  1 198 ? -17.768 -47.457  -86.625 1.00 88.75  ? 198 TYR E CD2 1 
ATOM   9111  C CE1 . TYR E  1 198 ? -15.659 -48.147  -84.987 1.00 90.09  ? 198 TYR E CE1 1 
ATOM   9112  C CE2 . TYR E  1 198 ? -17.915 -48.481  -85.710 1.00 83.78  ? 198 TYR E CE2 1 
ATOM   9113  C CZ  . TYR E  1 198 ? -16.858 -48.822  -84.894 1.00 92.55  ? 198 TYR E CZ  1 
ATOM   9114  O OH  . TYR E  1 198 ? -16.999 -49.842  -83.981 1.00 86.94  ? 198 TYR E OH  1 
ATOM   9115  N N   . GLN E  1 199 ? -14.728 -44.999  -90.905 1.00 103.27 ? 199 GLN E N   1 
ATOM   9116  C CA  . GLN E  1 199 ? -13.592 -44.379  -91.593 1.00 103.74 ? 199 GLN E CA  1 
ATOM   9117  C C   . GLN E  1 199 ? -12.812 -43.342  -90.781 1.00 103.64 ? 199 GLN E C   1 
ATOM   9118  O O   . GLN E  1 199 ? -11.594 -43.225  -90.917 1.00 106.78 ? 199 GLN E O   1 
ATOM   9119  C CB  . GLN E  1 199 ? -14.047 -43.786  -92.931 1.00 116.11 ? 199 GLN E CB  1 
ATOM   9120  C CG  . GLN E  1 199 ? -13.570 -44.562  -94.148 1.00 123.11 ? 199 GLN E CG  1 
ATOM   9121  C CD  . GLN E  1 199 ? -12.221 -44.086  -94.650 1.00 127.13 ? 199 GLN E CD  1 
ATOM   9122  O OE1 . GLN E  1 199 ? -11.891 -42.904  -94.552 1.00 130.92 ? 199 GLN E OE1 1 
ATOM   9123  N NE2 . GLN E  1 199 ? -11.433 -45.007  -95.192 1.00 118.38 ? 199 GLN E NE2 1 
ATOM   9124  N N   . ASN E  1 200 ? -13.519 -42.586  -89.951 1.00 111.57 ? 200 ASN E N   1 
ATOM   9125  C CA  . ASN E  1 200 ? -12.941 -41.452  -89.235 1.00 104.62 ? 200 ASN E CA  1 
ATOM   9126  C C   . ASN E  1 200 ? -12.002 -41.902  -88.111 1.00 101.59 ? 200 ASN E C   1 
ATOM   9127  O O   . ASN E  1 200 ? -12.248 -42.919  -87.461 1.00 100.94 ? 200 ASN E O   1 
ATOM   9128  C CB  . ASN E  1 200 ? -14.058 -40.555  -88.688 1.00 102.87 ? 200 ASN E CB  1 
ATOM   9129  C CG  . ASN E  1 200 ? -15.164 -40.335  -89.699 1.00 102.23 ? 200 ASN E CG  1 
ATOM   9130  O OD1 . ASN E  1 200 ? -14.998 -40.641  -90.878 1.00 106.73 ? 200 ASN E OD1 1 
ATOM   9131  N ND2 . ASN E  1 200 ? -16.301 -39.816  -89.246 1.00 99.77  ? 200 ASN E ND2 1 
ATOM   9132  N N   . ALA E  1 201 ? -10.920 -41.158  -87.896 1.00 101.25 ? 201 ALA E N   1 
ATOM   9133  C CA  . ALA E  1 201 ? -9.942  -41.520  -86.873 1.00 98.27  ? 201 ALA E CA  1 
ATOM   9134  C C   . ALA E  1 201 ? -10.315 -40.928  -85.518 1.00 100.54 ? 201 ALA E C   1 
ATOM   9135  O O   . ALA E  1 201 ? -10.224 -41.600  -84.492 1.00 100.58 ? 201 ALA E O   1 
ATOM   9136  C CB  . ALA E  1 201 ? -8.546  -41.077  -87.288 1.00 111.71 ? 201 ALA E CB  1 
ATOM   9137  N N   . ASP E  1 202 ? -10.736 -39.668  -85.523 1.00 110.52 ? 202 ASP E N   1 
ATOM   9138  C CA  . ASP E  1 202 ? -11.122 -38.987  -84.296 1.00 110.12 ? 202 ASP E CA  1 
ATOM   9139  C C   . ASP E  1 202 ? -12.637 -38.834  -84.236 1.00 102.64 ? 202 ASP E C   1 
ATOM   9140  O O   . ASP E  1 202 ? -13.200 -37.898  -84.806 1.00 108.36 ? 202 ASP E O   1 
ATOM   9141  C CB  . ASP E  1 202 ? -10.448 -37.617  -84.216 1.00 121.12 ? 202 ASP E CB  1 
ATOM   9142  C CG  . ASP E  1 202 ? -10.393 -37.077  -82.803 1.00 126.42 ? 202 ASP E CG  1 
ATOM   9143  O OD1 . ASP E  1 202 ? -10.064 -37.854  -81.882 1.00 120.35 ? 202 ASP E OD1 1 
ATOM   9144  O OD2 . ASP E  1 202 ? -10.671 -35.874  -82.616 1.00 128.75 ? 202 ASP E OD2 1 
ATOM   9145  N N   . THR E  1 203 ? -13.293 -39.761  -83.545 1.00 87.08  ? 203 THR E N   1 
ATOM   9146  C CA  . THR E  1 203 ? -14.748 -39.783  -83.481 1.00 79.46  ? 203 THR E CA  1 
ATOM   9147  C C   . THR E  1 203 ? -15.264 -39.542  -82.066 1.00 71.16  ? 203 THR E C   1 
ATOM   9148  O O   . THR E  1 203 ? -14.491 -39.480  -81.110 1.00 76.52  ? 203 THR E O   1 
ATOM   9149  C CB  . THR E  1 203 ? -15.308 -41.126  -83.980 1.00 78.39  ? 203 THR E CB  1 
ATOM   9150  O OG1 . THR E  1 203 ? -14.852 -42.180  -83.124 1.00 72.51  ? 203 THR E OG1 1 
ATOM   9151  C CG2 . THR E  1 203 ? -14.851 -41.399  -85.402 1.00 83.54  ? 203 THR E CG2 1 
ATOM   9152  N N   . TYR E  1 204 ? -16.581 -39.410  -81.950 1.00 71.97  ? 204 TYR E N   1 
ATOM   9153  C CA  . TYR E  1 204 ? -17.240 -39.216  -80.667 1.00 74.83  ? 204 TYR E CA  1 
ATOM   9154  C C   . TYR E  1 204 ? -18.685 -39.671  -80.776 1.00 77.24  ? 204 TYR E C   1 
ATOM   9155  O O   . TYR E  1 204 ? -19.263 -39.664  -81.861 1.00 71.52  ? 204 TYR E O   1 
ATOM   9156  C CB  . TYR E  1 204 ? -17.208 -37.739  -80.266 1.00 70.06  ? 204 TYR E CB  1 
ATOM   9157  C CG  . TYR E  1 204 ? -18.197 -36.875  -81.027 1.00 69.16  ? 204 TYR E CG  1 
ATOM   9158  C CD1 . TYR E  1 204 ? -19.476 -36.644  -80.532 1.00 73.83  ? 204 TYR E CD1 1 
ATOM   9159  C CD2 . TYR E  1 204 ? -17.852 -36.295  -82.239 1.00 73.66  ? 204 TYR E CD2 1 
ATOM   9160  C CE1 . TYR E  1 204 ? -20.382 -35.858  -81.225 1.00 79.73  ? 204 TYR E CE1 1 
ATOM   9161  C CE2 . TYR E  1 204 ? -18.750 -35.509  -82.938 1.00 81.04  ? 204 TYR E CE2 1 
ATOM   9162  C CZ  . TYR E  1 204 ? -20.013 -35.293  -82.428 1.00 91.10  ? 204 TYR E CZ  1 
ATOM   9163  O OH  . TYR E  1 204 ? -20.910 -34.511  -83.120 1.00 95.24  ? 204 TYR E OH  1 
ATOM   9164  N N   . VAL E  1 205 ? -19.266 -40.068  -79.650 1.00 61.58  ? 205 VAL E N   1 
ATOM   9165  C CA  . VAL E  1 205 ? -20.699 -40.325  -79.587 1.00 59.30  ? 205 VAL E CA  1 
ATOM   9166  C C   . VAL E  1 205 ? -21.289 -39.673  -78.350 1.00 64.16  ? 205 VAL E C   1 
ATOM   9167  O O   . VAL E  1 205 ? -20.665 -39.657  -77.292 1.00 62.62  ? 205 VAL E O   1 
ATOM   9168  C CB  . VAL E  1 205 ? -21.036 -41.830  -79.610 1.00 63.23  ? 205 VAL E CB  1 
ATOM   9169  C CG1 . VAL E  1 205 ? -19.768 -42.669  -79.493 1.00 64.13  ? 205 VAL E CG1 1 
ATOM   9170  C CG2 . VAL E  1 205 ? -22.045 -42.166  -78.519 1.00 64.08  ? 205 VAL E CG2 1 
ATOM   9171  N N   . PHE E  1 206 ? -22.501 -39.148  -78.491 1.00 61.14  ? 206 PHE E N   1 
ATOM   9172  C CA  . PHE E  1 206 ? -23.150 -38.405  -77.421 1.00 62.37  ? 206 PHE E CA  1 
ATOM   9173  C C   . PHE E  1 206 ? -24.594 -38.849  -77.223 1.00 69.74  ? 206 PHE E C   1 
ATOM   9174  O O   . PHE E  1 206 ? -25.380 -38.881  -78.169 1.00 60.02  ? 206 PHE E O   1 
ATOM   9175  C CB  . PHE E  1 206 ? -23.097 -36.907  -77.725 1.00 59.47  ? 206 PHE E CB  1 
ATOM   9176  C CG  . PHE E  1 206 ? -23.986 -36.072  -76.845 1.00 67.64  ? 206 PHE E CG  1 
ATOM   9177  C CD1 . PHE E  1 206 ? -25.257 -35.711  -77.263 1.00 69.19  ? 206 PHE E CD1 1 
ATOM   9178  C CD2 . PHE E  1 206 ? -23.547 -35.638  -75.605 1.00 73.92  ? 206 PHE E CD2 1 
ATOM   9179  C CE1 . PHE E  1 206 ? -26.076 -34.938  -76.458 1.00 73.83  ? 206 PHE E CE1 1 
ATOM   9180  C CE2 . PHE E  1 206 ? -24.361 -34.864  -74.795 1.00 63.49  ? 206 PHE E CE2 1 
ATOM   9181  C CZ  . PHE E  1 206 ? -25.627 -34.514  -75.223 1.00 79.23  ? 206 PHE E CZ  1 
ATOM   9182  N N   . VAL E  1 207 ? -24.937 -39.185  -75.985 1.00 67.90  ? 207 VAL E N   1 
ATOM   9183  C CA  . VAL E  1 207 ? -26.291 -39.607  -75.653 1.00 61.99  ? 207 VAL E CA  1 
ATOM   9184  C C   . VAL E  1 207 ? -26.880 -38.682  -74.597 1.00 64.90  ? 207 VAL E C   1 
ATOM   9185  O O   . VAL E  1 207 ? -26.308 -38.518  -73.519 1.00 62.74  ? 207 VAL E O   1 
ATOM   9186  C CB  . VAL E  1 207 ? -26.314 -41.050  -75.123 1.00 55.23  ? 207 VAL E CB  1 
ATOM   9187  C CG1 . VAL E  1 207 ? -27.736 -41.471  -74.789 1.00 49.84  ? 207 VAL E CG1 1 
ATOM   9188  C CG2 . VAL E  1 207 ? -25.697 -41.995  -76.139 1.00 55.72  ? 207 VAL E CG2 1 
ATOM   9189  N N   . GLY E  1 208 ? -28.023 -38.079  -74.904 1.00 65.80  ? 208 GLY E N   1 
ATOM   9190  C CA  . GLY E  1 208 ? -28.632 -37.131  -73.992 1.00 65.09  ? 208 GLY E CA  1 
ATOM   9191  C C   . GLY E  1 208 ? -30.144 -37.206  -73.917 1.00 66.95  ? 208 GLY E C   1 
ATOM   9192  O O   . GLY E  1 208 ? -30.818 -37.474  -74.910 1.00 67.46  ? 208 GLY E O   1 
ATOM   9193  N N   . SER E  1 209 ? -30.670 -36.975  -72.720 1.00 67.39  ? 209 SER E N   1 
ATOM   9194  C CA  . SER E  1 209 ? -32.104 -36.844  -72.509 1.00 66.66  ? 209 SER E CA  1 
ATOM   9195  C C   . SER E  1 209 ? -32.338 -35.612  -71.647 1.00 70.33  ? 209 SER E C   1 
ATOM   9196  O O   . SER E  1 209 ? -31.461 -34.755  -71.534 1.00 73.61  ? 209 SER E O   1 
ATOM   9197  C CB  . SER E  1 209 ? -32.670 -38.087  -71.821 1.00 72.24  ? 209 SER E CB  1 
ATOM   9198  O OG  . SER E  1 209 ? -32.250 -38.163  -70.470 1.00 63.07  ? 209 SER E OG  1 
ATOM   9199  N N   . SER E  1 210 ? -33.513 -35.520  -71.036 1.00 70.20  ? 210 SER E N   1 
ATOM   9200  C CA  . SER E  1 210 ? -33.809 -34.402  -70.150 1.00 76.21  ? 210 SER E CA  1 
ATOM   9201  C C   . SER E  1 210 ? -32.927 -34.446  -68.908 1.00 82.04  ? 210 SER E C   1 
ATOM   9202  O O   . SER E  1 210 ? -32.670 -33.418  -68.281 1.00 67.51  ? 210 SER E O   1 
ATOM   9203  C CB  . SER E  1 210 ? -35.284 -34.404  -69.746 1.00 83.51  ? 210 SER E CB  1 
ATOM   9204  O OG  . SER E  1 210 ? -36.119 -34.117  -70.853 1.00 113.46 ? 210 SER E OG  1 
ATOM   9205  N N   . ARG E  1 211 ? -32.459 -35.641  -68.563 1.00 73.10  ? 211 ARG E N   1 
ATOM   9206  C CA  . ARG E  1 211 ? -31.677 -35.836  -67.348 1.00 88.70  ? 211 ARG E CA  1 
ATOM   9207  C C   . ARG E  1 211 ? -30.282 -36.381  -67.648 1.00 87.20  ? 211 ARG E C   1 
ATOM   9208  O O   . ARG E  1 211 ? -29.308 -36.010  -66.993 1.00 109.81 ? 211 ARG E O   1 
ATOM   9209  C CB  . ARG E  1 211 ? -32.418 -36.778  -66.396 1.00 95.92  ? 211 ARG E CB  1 
ATOM   9210  C CG  . ARG E  1 211 ? -32.578 -38.193  -66.929 1.00 111.50 ? 211 ARG E CG  1 
ATOM   9211  C CD  . ARG E  1 211 ? -33.711 -38.934  -66.237 1.00 114.48 ? 211 ARG E CD  1 
ATOM   9212  N NE  . ARG E  1 211 ? -33.690 -38.751  -64.789 1.00 125.23 ? 211 ARG E NE  1 
ATOM   9213  C CZ  . ARG E  1 211 ? -34.371 -39.505  -63.933 1.00 131.26 ? 211 ARG E CZ  1 
ATOM   9214  N NH1 . ARG E  1 211 ? -35.119 -40.505  -64.378 1.00 127.76 ? 211 ARG E NH1 1 
ATOM   9215  N NH2 . ARG E  1 211 ? -34.297 -39.266  -62.631 1.00 119.00 ? 211 ARG E NH2 1 
ATOM   9216  N N   . TYR E  1 212 ? -30.193 -37.260  -68.641 1.00 71.53  ? 212 TYR E N   1 
ATOM   9217  C CA  . TYR E  1 212 ? -28.928 -37.894  -68.996 1.00 65.22  ? 212 TYR E CA  1 
ATOM   9218  C C   . TYR E  1 212 ? -28.170 -37.061  -70.025 1.00 68.04  ? 212 TYR E C   1 
ATOM   9219  O O   . TYR E  1 212 ? -28.775 -36.416  -70.879 1.00 73.96  ? 212 TYR E O   1 
ATOM   9220  C CB  . TYR E  1 212 ? -29.177 -39.303  -69.540 1.00 59.45  ? 212 TYR E CB  1 
ATOM   9221  C CG  . TYR E  1 212 ? -27.929 -40.145  -69.681 1.00 68.21  ? 212 TYR E CG  1 
ATOM   9222  C CD1 . TYR E  1 212 ? -27.552 -41.032  -68.681 1.00 64.34  ? 212 TYR E CD1 1 
ATOM   9223  C CD2 . TYR E  1 212 ? -27.130 -40.057  -70.813 1.00 63.61  ? 212 TYR E CD2 1 
ATOM   9224  C CE1 . TYR E  1 212 ? -26.414 -41.806  -68.803 1.00 59.52  ? 212 TYR E CE1 1 
ATOM   9225  C CE2 . TYR E  1 212 ? -25.989 -40.826  -70.944 1.00 62.27  ? 212 TYR E CE2 1 
ATOM   9226  C CZ  . TYR E  1 212 ? -25.636 -41.699  -69.936 1.00 62.45  ? 212 TYR E CZ  1 
ATOM   9227  O OH  . TYR E  1 212 ? -24.501 -42.468  -70.059 1.00 57.24  ? 212 TYR E OH  1 
ATOM   9228  N N   . SER E  1 213 ? -26.843 -37.077  -69.938 1.00 57.22  ? 213 SER E N   1 
ATOM   9229  C CA  . SER E  1 213 ? -26.007 -36.333  -70.874 1.00 61.89  ? 213 SER E CA  1 
ATOM   9230  C C   . SER E  1 213 ? -24.556 -36.767  -70.698 1.00 61.82  ? 213 SER E C   1 
ATOM   9231  O O   . SER E  1 213 ? -23.973 -36.586  -69.629 1.00 81.52  ? 213 SER E O   1 
ATOM   9232  C CB  . SER E  1 213 ? -26.192 -34.827  -70.678 1.00 63.47  ? 213 SER E CB  1 
ATOM   9233  O OG  . SER E  1 213 ? -25.443 -34.092  -71.631 1.00 59.27  ? 213 SER E OG  1 
ATOM   9234  N N   . LYS E  1 214 ? -23.976 -37.340  -71.747 1.00 55.40  ? 214 LYS E N   1 
ATOM   9235  C CA  . LYS E  1 214 ? -22.570 -37.725  -71.708 1.00 64.66  ? 214 LYS E CA  1 
ATOM   9236  C C   . LYS E  1 214 ? -21.993 -37.881  -73.111 1.00 77.31  ? 214 LYS E C   1 
ATOM   9237  O O   . LYS E  1 214 ? -22.649 -38.400  -74.015 1.00 65.65  ? 214 LYS E O   1 
ATOM   9238  C CB  . LYS E  1 214 ? -22.306 -38.987  -70.881 1.00 60.82  ? 214 LYS E CB  1 
ATOM   9239  C CG  . LYS E  1 214 ? -20.825 -39.284  -70.681 1.00 72.66  ? 214 LYS E CG  1 
ATOM   9240  C CD  . LYS E  1 214 ? -20.532 -39.735  -69.258 1.00 85.84  ? 214 LYS E CD  1 
ATOM   9241  C CE  . LYS E  1 214 ? -20.389 -41.244  -69.163 1.00 86.86  ? 214 LYS E CE  1 
ATOM   9242  N NZ  . LYS E  1 214 ? -19.136 -41.723  -69.810 1.00 90.58  ? 214 LYS E NZ  1 
ATOM   9243  N N   . LYS E  1 215 ? -20.758 -37.420  -73.277 1.00 74.27  ? 215 LYS E N   1 
ATOM   9244  C CA  . LYS E  1 215 ? -20.047 -37.532  -74.541 1.00 60.53  ? 215 LYS E CA  1 
ATOM   9245  C C   . LYS E  1 215 ? -18.958 -38.590  -74.411 1.00 64.49  ? 215 LYS E C   1 
ATOM   9246  O O   . LYS E  1 215 ? -18.175 -38.570  -73.462 1.00 68.98  ? 215 LYS E O   1 
ATOM   9247  C CB  . LYS E  1 215 ? -19.433 -36.185  -74.918 1.00 72.84  ? 215 LYS E CB  1 
ATOM   9248  C CG  . LYS E  1 215 ? -18.788 -36.145  -76.290 1.00 80.21  ? 215 LYS E CG  1 
ATOM   9249  C CD  . LYS E  1 215 ? -18.309 -34.740  -76.614 1.00 88.80  ? 215 LYS E CD  1 
ATOM   9250  C CE  . LYS E  1 215 ? -17.921 -34.606  -78.076 1.00 91.61  ? 215 LYS E CE  1 
ATOM   9251  N NZ  . LYS E  1 215 ? -17.630 -33.191  -78.438 1.00 94.52  ? 215 LYS E NZ  1 
ATOM   9252  N N   . PHE E  1 216 ? -18.914 -39.513  -75.365 1.00 66.80  ? 216 PHE E N   1 
ATOM   9253  C CA  . PHE E  1 216 ? -17.981 -40.632  -75.302 1.00 63.89  ? 216 PHE E CA  1 
ATOM   9254  C C   . PHE E  1 216 ? -16.849 -40.503  -76.313 1.00 63.81  ? 216 PHE E C   1 
ATOM   9255  O O   . PHE E  1 216 ? -17.076 -40.188  -77.482 1.00 64.83  ? 216 PHE E O   1 
ATOM   9256  C CB  . PHE E  1 216 ? -18.716 -41.956  -75.519 1.00 66.39  ? 216 PHE E CB  1 
ATOM   9257  C CG  . PHE E  1 216 ? -19.842 -42.190  -74.554 1.00 72.58  ? 216 PHE E CG  1 
ATOM   9258  C CD1 . PHE E  1 216 ? -21.128 -41.778  -74.858 1.00 61.70  ? 216 PHE E CD1 1 
ATOM   9259  C CD2 . PHE E  1 216 ? -19.614 -42.821  -73.342 1.00 63.86  ? 216 PHE E CD2 1 
ATOM   9260  C CE1 . PHE E  1 216 ? -22.167 -41.991  -73.973 1.00 64.80  ? 216 PHE E CE1 1 
ATOM   9261  C CE2 . PHE E  1 216 ? -20.649 -43.037  -72.453 1.00 66.12  ? 216 PHE E CE2 1 
ATOM   9262  C CZ  . PHE E  1 216 ? -21.927 -42.621  -72.769 1.00 68.06  ? 216 PHE E CZ  1 
ATOM   9263  N N   . LYS E  1 217 ? -15.629 -40.749  -75.850 1.00 70.48  ? 217 LYS E N   1 
ATOM   9264  C CA  . LYS E  1 217 ? -14.466 -40.789  -76.725 1.00 70.63  ? 217 LYS E CA  1 
ATOM   9265  C C   . LYS E  1 217 ? -13.911 -42.205  -76.787 1.00 69.82  ? 217 LYS E C   1 
ATOM   9266  O O   . LYS E  1 217 ? -13.504 -42.762  -75.766 1.00 77.98  ? 217 LYS E O   1 
ATOM   9267  C CB  . LYS E  1 217 ? -13.388 -39.819  -76.240 1.00 78.92  ? 217 LYS E CB  1 
ATOM   9268  C CG  . LYS E  1 217 ? -13.386 -38.481  -76.962 1.00 77.34  ? 217 LYS E CG  1 
ATOM   9269  C CD  . LYS E  1 217 ? -13.030 -38.653  -78.430 1.00 82.98  ? 217 LYS E CD  1 
ATOM   9270  C CE  . LYS E  1 217 ? -12.978 -37.315  -79.149 1.00 96.91  ? 217 LYS E CE  1 
ATOM   9271  N NZ  . LYS E  1 217 ? -12.581 -37.468  -80.577 1.00 110.12 ? 217 LYS E NZ  1 
ATOM   9272  N N   . PRO E  1 218 ? -13.903 -42.796  -77.990 1.00 74.70  ? 218 PRO E N   1 
ATOM   9273  C CA  . PRO E  1 218 ? -13.391 -44.155  -78.188 1.00 74.16  ? 218 PRO E CA  1 
ATOM   9274  C C   . PRO E  1 218 ? -11.953 -44.288  -77.709 1.00 74.33  ? 218 PRO E C   1 
ATOM   9275  O O   . PRO E  1 218 ? -11.084 -43.520  -78.122 1.00 77.36  ? 218 PRO E O   1 
ATOM   9276  C CB  . PRO E  1 218 ? -13.455 -44.333  -79.707 1.00 68.15  ? 218 PRO E CB  1 
ATOM   9277  C CG  . PRO E  1 218 ? -14.512 -43.389  -80.153 1.00 70.76  ? 218 PRO E CG  1 
ATOM   9278  C CD  . PRO E  1 218 ? -14.400 -42.205  -79.243 1.00 69.99  ? 218 PRO E CD  1 
ATOM   9279  N N   . GLU E  1 219 ? -11.712 -45.258  -76.836 1.00 73.76  ? 219 GLU E N   1 
ATOM   9280  C CA  . GLU E  1 219 ? -10.370 -45.535  -76.352 1.00 71.04  ? 219 GLU E CA  1 
ATOM   9281  C C   . GLU E  1 219 ? -9.777  -46.685  -77.159 1.00 70.76  ? 219 GLU E C   1 
ATOM   9282  O O   . GLU E  1 219 ? -10.099 -47.846  -76.931 1.00 63.35  ? 219 GLU E O   1 
ATOM   9283  C CB  . GLU E  1 219 ? -10.404 -45.869  -74.858 1.00 75.49  ? 219 GLU E CB  1 
ATOM   9284  C CG  . GLU E  1 219 ? -11.102 -44.806  -74.014 1.00 76.69  ? 219 GLU E CG  1 
ATOM   9285  C CD  . GLU E  1 219 ? -11.154 -45.155  -72.537 1.00 93.52  ? 219 GLU E CD  1 
ATOM   9286  O OE1 . GLU E  1 219 ? -10.778 -46.289  -72.174 1.00 86.97  ? 219 GLU E OE1 1 
ATOM   9287  O OE2 . GLU E  1 219 ? -11.574 -44.290  -71.739 1.00 89.85  ? 219 GLU E OE2 1 
ATOM   9288  N N   . ILE E  1 220 ? -8.923  -46.350  -78.119 1.00 82.03  ? 220 ILE E N   1 
ATOM   9289  C CA  . ILE E  1 220 ? -8.333  -47.346  -79.007 1.00 81.44  ? 220 ILE E CA  1 
ATOM   9290  C C   . ILE E  1 220 ? -7.023  -47.907  -78.462 1.00 64.04  ? 220 ILE E C   1 
ATOM   9291  O O   . ILE E  1 220 ? -6.044  -47.180  -78.300 1.00 68.93  ? 220 ILE E O   1 
ATOM   9292  C CB  . ILE E  1 220 ? -8.083  -46.762  -80.409 1.00 70.50  ? 220 ILE E CB  1 
ATOM   9293  C CG1 . ILE E  1 220 ? -9.396  -46.251  -81.007 1.00 64.80  ? 220 ILE E CG1 1 
ATOM   9294  C CG2 . ILE E  1 220 ? -7.442  -47.804  -81.313 1.00 73.93  ? 220 ILE E CG2 1 
ATOM   9295  C CD1 . ILE E  1 220 ? -9.217  -45.380  -82.231 1.00 81.69  ? 220 ILE E CD1 1 
ATOM   9296  N N   . ALA E  1 221 ? -7.011  -49.207  -78.187 1.00 57.09  ? 221 ALA E N   1 
ATOM   9297  C CA  . ALA E  1 221 ? -5.812  -49.872  -77.693 1.00 65.88  ? 221 ALA E CA  1 
ATOM   9298  C C   . ALA E  1 221 ? -5.957  -51.389  -77.741 1.00 74.23  ? 221 ALA E C   1 
ATOM   9299  O O   . ALA E  1 221 ? -7.040  -51.911  -78.006 1.00 73.47  ? 221 ALA E O   1 
ATOM   9300  C CB  . ALA E  1 221 ? -5.496  -49.412  -76.280 1.00 61.69  ? 221 ALA E CB  1 
ATOM   9301  N N   . ILE E  1 222 ? -4.860  -52.092  -77.482 1.00 79.35  ? 222 ILE E N   1 
ATOM   9302  C CA  . ILE E  1 222 ? -4.875  -53.550  -77.460 1.00 81.76  ? 222 ILE E CA  1 
ATOM   9303  C C   . ILE E  1 222 ? -5.073  -54.088  -76.045 1.00 83.79  ? 222 ILE E C   1 
ATOM   9304  O O   . ILE E  1 222 ? -4.169  -54.007  -75.214 1.00 82.75  ? 222 ILE E O   1 
ATOM   9305  C CB  . ILE E  1 222 ? -3.570  -54.138  -78.030 1.00 94.00  ? 222 ILE E CB  1 
ATOM   9306  C CG1 . ILE E  1 222 ? -3.348  -53.661  -79.465 1.00 95.58  ? 222 ILE E CG1 1 
ATOM   9307  C CG2 . ILE E  1 222 ? -3.603  -55.657  -77.970 1.00 76.31  ? 222 ILE E CG2 1 
ATOM   9308  C CD1 . ILE E  1 222 ? -4.456  -54.053  -80.414 1.00 91.55  ? 222 ILE E CD1 1 
ATOM   9309  N N   . ARG E  1 223 ? -6.257  -54.633  -75.774 1.00 73.80  ? 223 ARG E N   1 
ATOM   9310  C CA  . ARG E  1 223 ? -6.526  -55.295  -74.499 1.00 82.77  ? 223 ARG E CA  1 
ATOM   9311  C C   . ARG E  1 223 ? -6.353  -56.797  -74.633 1.00 81.66  ? 223 ARG E C   1 
ATOM   9312  O O   . ARG E  1 223 ? -6.671  -57.370  -75.677 1.00 88.70  ? 223 ARG E O   1 
ATOM   9313  C CB  . ARG E  1 223 ? -7.951  -55.020  -74.011 1.00 78.25  ? 223 ARG E CB  1 
ATOM   9314  C CG  . ARG E  1 223 ? -8.263  -53.571  -73.728 1.00 67.15  ? 223 ARG E CG  1 
ATOM   9315  C CD  . ARG E  1 223 ? -9.144  -52.978  -74.806 1.00 63.83  ? 223 ARG E CD  1 
ATOM   9316  N NE  . ARG E  1 223 ? -9.249  -51.535  -74.627 1.00 60.67  ? 223 ARG E NE  1 
ATOM   9317  C CZ  . ARG E  1 223 ? -9.806  -50.705  -75.499 1.00 67.15  ? 223 ARG E CZ  1 
ATOM   9318  N NH1 . ARG E  1 223 ? -10.322 -51.165  -76.630 1.00 71.81  ? 223 ARG E NH1 1 
ATOM   9319  N NH2 . ARG E  1 223 ? -9.842  -49.410  -75.235 1.00 71.83  ? 223 ARG E NH2 1 
ATOM   9320  N N   . PRO E  1 224 ? -5.871  -57.444  -73.563 1.00 76.58  ? 224 PRO E N   1 
ATOM   9321  C CA  . PRO E  1 224 ? -5.756  -58.902  -73.527 1.00 82.41  ? 224 PRO E CA  1 
ATOM   9322  C C   . PRO E  1 224 ? -6.981  -59.550  -74.152 1.00 77.26  ? 224 PRO E C   1 
ATOM   9323  O O   . PRO E  1 224 ? -8.100  -59.148  -73.848 1.00 82.02  ? 224 PRO E O   1 
ATOM   9324  C CB  . PRO E  1 224 ? -5.717  -59.198  -72.031 1.00 73.62  ? 224 PRO E CB  1 
ATOM   9325  C CG  . PRO E  1 224 ? -5.036  -58.004  -71.454 1.00 81.58  ? 224 PRO E CG  1 
ATOM   9326  C CD  . PRO E  1 224 ? -5.485  -56.829  -72.280 1.00 76.73  ? 224 PRO E CD  1 
ATOM   9327  N N   . LYS E  1 225 ? -6.772  -60.536  -75.016 1.00 88.26  ? 225 LYS E N   1 
ATOM   9328  C CA  . LYS E  1 225 ? -7.884  -61.169  -75.713 1.00 89.43  ? 225 LYS E CA  1 
ATOM   9329  C C   . LYS E  1 225 ? -8.832  -61.927  -74.792 1.00 87.54  ? 225 LYS E C   1 
ATOM   9330  O O   . LYS E  1 225 ? -8.414  -62.764  -73.992 1.00 85.46  ? 225 LYS E O   1 
ATOM   9331  C CB  . LYS E  1 225 ? -7.379  -62.086  -76.828 1.00 105.64 ? 225 LYS E CB  1 
ATOM   9332  C CG  . LYS E  1 225 ? -7.379  -61.416  -78.187 1.00 115.56 ? 225 LYS E CG  1 
ATOM   9333  C CD  . LYS E  1 225 ? -6.531  -62.160  -79.201 1.00 129.97 ? 225 LYS E CD  1 
ATOM   9334  C CE  . LYS E  1 225 ? -6.162  -61.226  -80.344 1.00 148.71 ? 225 LYS E CE  1 
ATOM   9335  N NZ  . LYS E  1 225 ? -5.272  -61.839  -81.364 1.00 147.33 ? 225 LYS E NZ  1 
ATOM   9336  N N   . VAL E  1 226 ? -10.114 -61.606  -74.913 1.00 77.93  ? 226 VAL E N   1 
ATOM   9337  C CA  . VAL E  1 226 ? -11.169 -62.341  -74.241 1.00 75.41  ? 226 VAL E CA  1 
ATOM   9338  C C   . VAL E  1 226 ? -12.174 -62.710  -75.318 1.00 83.83  ? 226 VAL E C   1 
ATOM   9339  O O   . VAL E  1 226 ? -12.830 -61.838  -75.883 1.00 86.83  ? 226 VAL E O   1 
ATOM   9340  C CB  . VAL E  1 226 ? -11.851 -61.485  -73.161 1.00 74.78  ? 226 VAL E CB  1 
ATOM   9341  C CG1 . VAL E  1 226 ? -12.983 -62.260  -72.499 1.00 69.38  ? 226 VAL E CG1 1 
ATOM   9342  C CG2 . VAL E  1 226 ? -10.835 -61.028  -72.126 1.00 71.92  ? 226 VAL E CG2 1 
ATOM   9343  N N   . ARG E  1 227 ? -12.394 -63.695  -76.110 1.00 90.76  ? 227 ARG E N   1 
ATOM   9344  C CA  . ARG E  1 227 ? -13.253 -64.144  -77.198 1.00 85.47  ? 227 ARG E CA  1 
ATOM   9345  C C   . ARG E  1 227 ? -12.773 -63.593  -78.542 1.00 92.15  ? 227 ARG E C   1 
ATOM   9346  O O   . ARG E  1 227 ? -13.578 -63.157  -79.365 1.00 96.71  ? 227 ARG E O   1 
ATOM   9347  C CB  . ARG E  1 227 ? -14.704 -63.732  -76.940 1.00 81.73  ? 227 ARG E CB  1 
ATOM   9348  C CG  . ARG E  1 227 ? -15.346 -64.427  -75.750 1.00 82.54  ? 227 ARG E CG  1 
ATOM   9349  C CD  . ARG E  1 227 ? -16.698 -63.815  -75.430 1.00 84.20  ? 227 ARG E CD  1 
ATOM   9350  N NE  . ARG E  1 227 ? -17.736 -64.826  -75.255 1.00 74.19  ? 227 ARG E NE  1 
ATOM   9351  C CZ  . ARG E  1 227 ? -18.380 -65.410  -76.260 1.00 83.75  ? 227 ARG E CZ  1 
ATOM   9352  N NH1 . ARG E  1 227 ? -18.084 -65.088  -77.510 1.00 95.03  ? 227 ARG E NH1 1 
ATOM   9353  N NH2 . ARG E  1 227 ? -19.314 -66.319  -76.017 1.00 85.90  ? 227 ARG E NH2 1 
ATOM   9354  N N   . ASP E  1 228 ? -11.458 -63.605  -78.745 1.00 100.05 ? 228 ASP E N   1 
ATOM   9355  C CA  . ASP E  1 228 ? -10.848 -63.229  -80.023 1.00 113.56 ? 228 ASP E CA  1 
ATOM   9356  C C   . ASP E  1 228 ? -10.821 -61.727  -80.311 1.00 108.26 ? 228 ASP E C   1 
ATOM   9357  O O   . ASP E  1 228 ? -10.212 -61.292  -81.289 1.00 122.50 ? 228 ASP E O   1 
ATOM   9358  C CB  . ASP E  1 228 ? -11.516 -63.973  -81.185 1.00 143.29 ? 228 ASP E CB  1 
ATOM   9359  C CG  . ASP E  1 228 ? -10.776 -65.238  -81.568 1.00 161.92 ? 228 ASP E CG  1 
ATOM   9360  O OD1 . ASP E  1 228 ? -9.623  -65.133  -82.037 1.00 165.98 ? 228 ASP E OD1 1 
ATOM   9361  O OD2 . ASP E  1 228 ? -11.348 -66.337  -81.408 1.00 168.10 ? 228 ASP E OD2 1 
ATOM   9362  N N   . GLN E  1 229 ? -11.472 -60.937  -79.465 1.00 92.77  ? 229 GLN E N   1 
ATOM   9363  C CA  . GLN E  1 229 ? -11.543 -59.496  -79.683 1.00 96.44  ? 229 GLN E CA  1 
ATOM   9364  C C   . GLN E  1 229 ? -10.517 -58.740  -78.840 1.00 89.02  ? 229 GLN E C   1 
ATOM   9365  O O   . GLN E  1 229 ? -10.489 -58.874  -77.617 1.00 93.71  ? 229 GLN E O   1 
ATOM   9366  C CB  . GLN E  1 229 ? -12.952 -58.980  -79.378 1.00 81.95  ? 229 GLN E CB  1 
ATOM   9367  C CG  . GLN E  1 229 ? -14.069 -59.834  -79.960 1.00 84.74  ? 229 GLN E CG  1 
ATOM   9368  C CD  . GLN E  1 229 ? -13.985 -59.964  -81.469 1.00 88.49  ? 229 GLN E CD  1 
ATOM   9369  O OE1 . GLN E  1 229 ? -13.551 -59.044  -82.161 1.00 89.48  ? 229 GLN E OE1 1 
ATOM   9370  N NE2 . GLN E  1 229 ? -14.408 -61.112  -81.987 1.00 89.96  ? 229 GLN E NE2 1 
ATOM   9371  N N   . GLU E  1 230 ? -9.673  -57.949  -79.499 1.00 84.01  ? 230 GLU E N   1 
ATOM   9372  C CA  . GLU E  1 230 ? -8.718  -57.094  -78.800 1.00 81.83  ? 230 GLU E CA  1 
ATOM   9373  C C   . GLU E  1 230 ? -9.346  -55.730  -78.550 1.00 85.43  ? 230 GLU E C   1 
ATOM   9374  O O   . GLU E  1 230 ? -8.812  -54.913  -77.799 1.00 84.42  ? 230 GLU E O   1 
ATOM   9375  C CB  . GLU E  1 230 ? -7.434  -56.925  -79.611 1.00 99.67  ? 230 GLU E CB  1 
ATOM   9376  C CG  . GLU E  1 230 ? -7.281  -57.912  -80.747 1.00 113.67 ? 230 GLU E CG  1 
ATOM   9377  C CD  . GLU E  1 230 ? -6.015  -57.684  -81.548 1.00 106.61 ? 230 GLU E CD  1 
ATOM   9378  O OE1 . GLU E  1 230 ? -6.111  -57.563  -82.787 1.00 107.21 ? 230 GLU E OE1 1 
ATOM   9379  O OE2 . GLU E  1 230 ? -4.926  -57.621  -80.940 1.00 118.02 ? 230 GLU E OE2 1 
ATOM   9380  N N   . GLY E  1 231 ? -10.478 -55.488  -79.201 1.00 70.13  ? 231 GLY E N   1 
ATOM   9381  C CA  . GLY E  1 231 ? -11.235 -54.271  -78.987 1.00 71.63  ? 231 GLY E CA  1 
ATOM   9382  C C   . GLY E  1 231 ? -12.309 -54.495  -77.943 1.00 74.33  ? 231 GLY E C   1 
ATOM   9383  O O   . GLY E  1 231 ? -12.622 -55.635  -77.605 1.00 71.58  ? 231 GLY E O   1 
ATOM   9384  N N   . ARG E  1 232 ? -12.880 -53.408  -77.437 1.00 64.37  ? 232 ARG E N   1 
ATOM   9385  C CA  . ARG E  1 232 ? -13.917 -53.502  -76.417 1.00 59.38  ? 232 ARG E CA  1 
ATOM   9386  C C   . ARG E  1 232 ? -15.229 -52.889  -76.888 1.00 65.25  ? 232 ARG E C   1 
ATOM   9387  O O   . ARG E  1 232 ? -15.294 -52.277  -77.955 1.00 60.46  ? 232 ARG E O   1 
ATOM   9388  C CB  . ARG E  1 232 ? -13.468 -52.813  -75.125 1.00 64.94  ? 232 ARG E CB  1 
ATOM   9389  C CG  . ARG E  1 232 ? -12.322 -53.502  -74.405 1.00 60.85  ? 232 ARG E CG  1 
ATOM   9390  C CD  . ARG E  1 232 ? -12.770 -54.799  -73.755 1.00 60.93  ? 232 ARG E CD  1 
ATOM   9391  N NE  . ARG E  1 232 ? -11.640 -55.679  -73.478 1.00 77.07  ? 232 ARG E NE  1 
ATOM   9392  C CZ  . ARG E  1 232 ? -11.181 -56.592  -74.329 1.00 77.95  ? 232 ARG E CZ  1 
ATOM   9393  N NH1 . ARG E  1 232 ? -11.757 -56.751  -75.513 1.00 70.99  ? 232 ARG E NH1 1 
ATOM   9394  N NH2 . ARG E  1 232 ? -10.147 -57.348  -73.996 1.00 77.26  ? 232 ARG E NH2 1 
ATOM   9395  N N   . MET E  1 233 ? -16.271 -53.061  -76.082 1.00 71.57  ? 233 MET E N   1 
ATOM   9396  C CA  . MET E  1 233 ? -17.565 -52.448  -76.348 1.00 63.56  ? 233 MET E CA  1 
ATOM   9397  C C   . MET E  1 233 ? -18.285 -52.162  -75.033 1.00 66.66  ? 233 MET E C   1 
ATOM   9398  O O   . MET E  1 233 ? -18.769 -53.079  -74.366 1.00 63.86  ? 233 MET E O   1 
ATOM   9399  C CB  . MET E  1 233 ? -18.420 -53.351  -77.242 1.00 58.12  ? 233 MET E CB  1 
ATOM   9400  C CG  . MET E  1 233 ? -19.715 -52.711  -77.730 1.00 64.09  ? 233 MET E CG  1 
ATOM   9401  S SD  . MET E  1 233 ? -20.608 -53.738  -78.916 1.00 87.96  ? 233 MET E SD  1 
ATOM   9402  C CE  . MET E  1 233 ? -19.452 -53.767  -80.285 1.00 74.98  ? 233 MET E CE  1 
ATOM   9403  N N   . ASN E  1 234 ? -18.339 -50.887  -74.659 1.00 62.45  ? 234 ASN E N   1 
ATOM   9404  C CA  . ASN E  1 234 ? -19.024 -50.470  -73.440 1.00 62.99  ? 234 ASN E CA  1 
ATOM   9405  C C   . ASN E  1 234 ? -20.525 -50.344  -73.665 1.00 53.99  ? 234 ASN E C   1 
ATOM   9406  O O   . ASN E  1 234 ? -20.963 -49.804  -74.680 1.00 55.81  ? 234 ASN E O   1 
ATOM   9407  C CB  . ASN E  1 234 ? -18.466 -49.137  -72.936 1.00 60.19  ? 234 ASN E CB  1 
ATOM   9408  C CG  . ASN E  1 234 ? -17.067 -49.263  -72.363 1.00 55.85  ? 234 ASN E CG  1 
ATOM   9409  O OD1 . ASN E  1 234 ? -16.521 -50.357  -72.265 1.00 61.41  ? 234 ASN E OD1 1 
ATOM   9410  N ND2 . ASN E  1 234 ? -16.484 -48.137  -71.973 1.00 57.77  ? 234 ASN E ND2 1 
ATOM   9411  N N   . TYR E  1 235 ? -21.310 -50.840  -72.714 1.00 52.61  ? 235 TYR E N   1 
ATOM   9412  C CA  . TYR E  1 235 ? -22.763 -50.809  -72.835 1.00 44.25  ? 235 TYR E CA  1 
ATOM   9413  C C   . TYR E  1 235 ? -23.380 -49.804  -71.872 1.00 47.84  ? 235 TYR E C   1 
ATOM   9414  O O   . TYR E  1 235 ? -23.072 -49.800  -70.680 1.00 57.37  ? 235 TYR E O   1 
ATOM   9415  C CB  . TYR E  1 235 ? -23.348 -52.203  -72.605 1.00 52.51  ? 235 TYR E CB  1 
ATOM   9416  C CG  . TYR E  1 235 ? -22.700 -53.262  -73.464 1.00 69.84  ? 235 TYR E CG  1 
ATOM   9417  C CD1 . TYR E  1 235 ? -21.636 -54.015  -72.985 1.00 54.83  ? 235 TYR E CD1 1 
ATOM   9418  C CD2 . TYR E  1 235 ? -23.139 -53.497  -74.760 1.00 59.66  ? 235 TYR E CD2 1 
ATOM   9419  C CE1 . TYR E  1 235 ? -21.035 -54.979  -73.768 1.00 52.94  ? 235 TYR E CE1 1 
ATOM   9420  C CE2 . TYR E  1 235 ? -22.543 -54.459  -75.551 1.00 60.64  ? 235 TYR E CE2 1 
ATOM   9421  C CZ  . TYR E  1 235 ? -21.492 -55.197  -75.050 1.00 58.45  ? 235 TYR E CZ  1 
ATOM   9422  O OH  . TYR E  1 235 ? -20.895 -56.156  -75.834 1.00 67.90  ? 235 TYR E OH  1 
ATOM   9423  N N   . TYR E  1 236 ? -24.251 -48.952  -72.399 1.00 42.72  ? 236 TYR E N   1 
ATOM   9424  C CA  . TYR E  1 236 ? -24.893 -47.918  -71.599 1.00 47.22  ? 236 TYR E CA  1 
ATOM   9425  C C   . TYR E  1 236 ? -26.410 -48.027  -71.675 1.00 54.78  ? 236 TYR E C   1 
ATOM   9426  O O   . TYR E  1 236 ? -26.955 -48.601  -72.617 1.00 60.16  ? 236 TYR E O   1 
ATOM   9427  C CB  . TYR E  1 236 ? -24.445 -46.531  -72.063 1.00 38.03  ? 236 TYR E CB  1 
ATOM   9428  C CG  . TYR E  1 236 ? -22.966 -46.278  -71.888 1.00 53.81  ? 236 TYR E CG  1 
ATOM   9429  C CD1 . TYR E  1 236 ? -22.051 -46.706  -72.840 1.00 56.31  ? 236 TYR E CD1 1 
ATOM   9430  C CD2 . TYR E  1 236 ? -22.484 -45.610  -70.770 1.00 54.38  ? 236 TYR E CD2 1 
ATOM   9431  C CE1 . TYR E  1 236 ? -20.697 -46.478  -72.684 1.00 59.49  ? 236 TYR E CE1 1 
ATOM   9432  C CE2 . TYR E  1 236 ? -21.132 -45.376  -70.605 1.00 65.08  ? 236 TYR E CE2 1 
ATOM   9433  C CZ  . TYR E  1 236 ? -20.243 -45.813  -71.564 1.00 70.44  ? 236 TYR E CZ  1 
ATOM   9434  O OH  . TYR E  1 236 ? -18.896 -45.581  -71.402 1.00 61.07  ? 236 TYR E OH  1 
ATOM   9435  N N   . TRP E  1 237 ? -27.087 -47.470  -70.678 1.00 54.52  ? 237 TRP E N   1 
ATOM   9436  C CA  . TRP E  1 237 ? -28.542 -47.497  -70.637 1.00 47.93  ? 237 TRP E CA  1 
ATOM   9437  C C   . TRP E  1 237 ? -29.086 -46.289  -69.893 1.00 49.22  ? 237 TRP E C   1 
ATOM   9438  O O   . TRP E  1 237 ? -28.354 -45.604  -69.178 1.00 55.89  ? 237 TRP E O   1 
ATOM   9439  C CB  . TRP E  1 237 ? -29.034 -48.778  -69.966 1.00 47.37  ? 237 TRP E CB  1 
ATOM   9440  C CG  . TRP E  1 237 ? -28.637 -48.886  -68.524 1.00 50.06  ? 237 TRP E CG  1 
ATOM   9441  C CD1 . TRP E  1 237 ? -27.499 -49.453  -68.030 1.00 46.66  ? 237 TRP E CD1 1 
ATOM   9442  C CD2 . TRP E  1 237 ? -29.378 -48.418  -67.389 1.00 47.56  ? 237 TRP E CD2 1 
ATOM   9443  N NE1 . TRP E  1 237 ? -27.484 -49.367  -66.659 1.00 40.92  ? 237 TRP E NE1 1 
ATOM   9444  C CE2 . TRP E  1 237 ? -28.626 -48.735  -66.241 1.00 50.59  ? 237 TRP E CE2 1 
ATOM   9445  C CE3 . TRP E  1 237 ? -30.603 -47.761  -67.233 1.00 45.52  ? 237 TRP E CE3 1 
ATOM   9446  C CZ2 . TRP E  1 237 ? -29.058 -48.419  -64.954 1.00 59.28  ? 237 TRP E CZ2 1 
ATOM   9447  C CZ3 . TRP E  1 237 ? -31.030 -47.448  -65.954 1.00 47.42  ? 237 TRP E CZ3 1 
ATOM   9448  C CH2 . TRP E  1 237 ? -30.259 -47.778  -64.831 1.00 49.73  ? 237 TRP E CH2 1 
ATOM   9449  N N   . THR E  1 238 ? -30.379 -46.038  -70.058 1.00 47.44  ? 238 THR E N   1 
ATOM   9450  C CA  . THR E  1 238 ? -31.026 -44.914  -69.400 1.00 46.32  ? 238 THR E CA  1 
ATOM   9451  C C   . THR E  1 238 ? -32.541 -45.041  -69.494 1.00 49.75  ? 238 THR E C   1 
ATOM   9452  O O   . THR E  1 238 ? -33.062 -45.748  -70.357 1.00 56.39  ? 238 THR E O   1 
ATOM   9453  C CB  . THR E  1 238 ? -30.582 -43.574  -70.014 1.00 53.15  ? 238 THR E CB  1 
ATOM   9454  O OG1 . THR E  1 238 ? -31.036 -42.493  -69.192 1.00 49.23  ? 238 THR E OG1 1 
ATOM   9455  C CG2 . THR E  1 238 ? -31.141 -43.418  -71.421 1.00 48.79  ? 238 THR E CG2 1 
ATOM   9456  N N   . LEU E  1 239 ? -33.246 -44.355  -68.601 1.00 52.49  ? 239 LEU E N   1 
ATOM   9457  C CA  . LEU E  1 239 ? -34.702 -44.417  -68.574 1.00 57.65  ? 239 LEU E CA  1 
ATOM   9458  C C   . LEU E  1 239 ? -35.336 -43.105  -69.031 1.00 66.80  ? 239 LEU E C   1 
ATOM   9459  O O   . LEU E  1 239 ? -35.311 -42.104  -68.312 1.00 74.45  ? 239 LEU E O   1 
ATOM   9460  C CB  . LEU E  1 239 ? -35.198 -44.795  -67.176 1.00 60.41  ? 239 LEU E CB  1 
ATOM   9461  C CG  . LEU E  1 239 ? -34.874 -46.219  -66.715 1.00 48.61  ? 239 LEU E CG  1 
ATOM   9462  C CD1 . LEU E  1 239 ? -35.294 -46.427  -65.268 1.00 60.02  ? 239 LEU E CD1 1 
ATOM   9463  C CD2 . LEU E  1 239 ? -35.538 -47.244  -67.624 1.00 50.95  ? 239 LEU E CD2 1 
ATOM   9464  N N   . VAL E  1 240 ? -35.904 -43.119  -70.232 1.00 63.50  ? 240 VAL E N   1 
ATOM   9465  C CA  . VAL E  1 240 ? -36.544 -41.936  -70.793 1.00 64.66  ? 240 VAL E CA  1 
ATOM   9466  C C   . VAL E  1 240 ? -37.939 -41.748  -70.202 1.00 52.54  ? 240 VAL E C   1 
ATOM   9467  O O   . VAL E  1 240 ? -38.797 -42.624  -70.320 1.00 54.13  ? 240 VAL E O   1 
ATOM   9468  C CB  . VAL E  1 240 ? -36.654 -42.033  -72.326 1.00 65.23  ? 240 VAL E CB  1 
ATOM   9469  C CG1 . VAL E  1 240 ? -37.154 -40.714  -72.907 1.00 61.89  ? 240 VAL E CG1 1 
ATOM   9470  C CG2 . VAL E  1 240 ? -35.313 -42.428  -72.931 1.00 53.71  ? 240 VAL E CG2 1 
ATOM   9471  N N   . GLU E  1 241 ? -38.155 -40.607  -69.556 1.00 65.07  ? 241 GLU E N   1 
ATOM   9472  C CA  . GLU E  1 241 ? -39.450 -40.292  -68.965 1.00 68.62  ? 241 GLU E CA  1 
ATOM   9473  C C   . GLU E  1 241 ? -40.512 -40.157  -70.048 1.00 76.42  ? 241 GLU E C   1 
ATOM   9474  O O   . GLU E  1 241 ? -40.199 -39.812  -71.187 1.00 76.59  ? 241 GLU E O   1 
ATOM   9475  C CB  . GLU E  1 241 ? -39.366 -38.995  -68.156 1.00 75.60  ? 241 GLU E CB  1 
ATOM   9476  C CG  . GLU E  1 241 ? -38.386 -39.046  -66.995 1.00 96.36  ? 241 GLU E CG  1 
ATOM   9477  C CD  . GLU E  1 241 ? -38.852 -39.955  -65.872 1.00 120.30 ? 241 GLU E CD  1 
ATOM   9478  O OE1 . GLU E  1 241 ? -37.990 -40.523  -65.169 1.00 116.59 ? 241 GLU E OE1 1 
ATOM   9479  O OE2 . GLU E  1 241 ? -40.079 -40.102  -65.693 1.00 128.20 ? 241 GLU E OE2 1 
ATOM   9480  N N   . PRO E  1 242 ? -41.775 -40.443  -69.700 1.00 81.23  ? 242 PRO E N   1 
ATOM   9481  C CA  . PRO E  1 242 ? -42.884 -40.244  -70.637 1.00 79.28  ? 242 PRO E CA  1 
ATOM   9482  C C   . PRO E  1 242 ? -42.957 -38.790  -71.090 1.00 80.97  ? 242 PRO E C   1 
ATOM   9483  O O   . PRO E  1 242 ? -42.940 -37.887  -70.254 1.00 73.94  ? 242 PRO E O   1 
ATOM   9484  C CB  . PRO E  1 242 ? -44.115 -40.595  -69.798 1.00 68.38  ? 242 PRO E CB  1 
ATOM   9485  C CG  . PRO E  1 242 ? -43.604 -41.521  -68.748 1.00 73.74  ? 242 PRO E CG  1 
ATOM   9486  C CD  . PRO E  1 242 ? -42.218 -41.046  -68.431 1.00 66.81  ? 242 PRO E CD  1 
ATOM   9487  N N   . GLY E  1 243 ? -43.031 -38.571  -72.399 1.00 75.96  ? 243 GLY E N   1 
ATOM   9488  C CA  . GLY E  1 243 ? -43.087 -37.226  -72.942 1.00 70.53  ? 243 GLY E CA  1 
ATOM   9489  C C   . GLY E  1 243 ? -41.709 -36.629  -73.150 1.00 76.89  ? 243 GLY E C   1 
ATOM   9490  O O   . GLY E  1 243 ? -41.571 -35.519  -73.662 1.00 87.04  ? 243 GLY E O   1 
ATOM   9491  N N   . ASP E  1 244 ? -40.686 -37.374  -72.745 1.00 78.36  ? 244 ASP E N   1 
ATOM   9492  C CA  . ASP E  1 244 ? -39.302 -36.949  -72.912 1.00 66.01  ? 244 ASP E CA  1 
ATOM   9493  C C   . ASP E  1 244 ? -38.726 -37.599  -74.165 1.00 68.11  ? 244 ASP E C   1 
ATOM   9494  O O   . ASP E  1 244 ? -39.225 -38.627  -74.619 1.00 77.76  ? 244 ASP E O   1 
ATOM   9495  C CB  . ASP E  1 244 ? -38.485 -37.347  -71.680 1.00 66.94  ? 244 ASP E CB  1 
ATOM   9496  C CG  . ASP E  1 244 ? -37.099 -36.732  -71.668 1.00 88.79  ? 244 ASP E CG  1 
ATOM   9497  O OD1 . ASP E  1 244 ? -36.342 -36.995  -70.709 1.00 93.53  ? 244 ASP E OD1 1 
ATOM   9498  O OD2 . ASP E  1 244 ? -36.764 -35.984  -72.610 1.00 83.25  ? 244 ASP E OD2 1 
ATOM   9499  N N   . LYS E  1 245 ? -37.686 -36.995  -74.731 1.00 60.85  ? 245 LYS E N   1 
ATOM   9500  C CA  . LYS E  1 245 ? -37.028 -37.570  -75.899 1.00 70.27  ? 245 LYS E CA  1 
ATOM   9501  C C   . LYS E  1 245 ? -35.527 -37.736  -75.675 1.00 67.86  ? 245 LYS E C   1 
ATOM   9502  O O   . LYS E  1 245 ? -34.917 -37.001  -74.897 1.00 69.60  ? 245 LYS E O   1 
ATOM   9503  C CB  . LYS E  1 245 ? -37.294 -36.727  -77.151 1.00 76.04  ? 245 LYS E CB  1 
ATOM   9504  C CG  . LYS E  1 245 ? -36.491 -35.441  -77.233 1.00 79.62  ? 245 LYS E CG  1 
ATOM   9505  C CD  . LYS E  1 245 ? -36.792 -34.682  -78.520 1.00 89.44  ? 245 LYS E CD  1 
ATOM   9506  C CE  . LYS E  1 245 ? -35.949 -33.420  -78.633 1.00 101.77 ? 245 LYS E CE  1 
ATOM   9507  N NZ  . LYS E  1 245 ? -36.311 -32.606  -79.827 1.00 80.72  ? 245 LYS E NZ  1 
ATOM   9508  N N   . ILE E  1 246 ? -34.943 -38.716  -76.356 1.00 58.17  ? 246 ILE E N   1 
ATOM   9509  C CA  . ILE E  1 246 ? -33.513 -38.978  -76.264 1.00 61.37  ? 246 ILE E CA  1 
ATOM   9510  C C   . ILE E  1 246 ? -32.875 -38.885  -77.648 1.00 65.88  ? 246 ILE E C   1 
ATOM   9511  O O   . ILE E  1 246 ? -33.387 -39.449  -78.615 1.00 64.04  ? 246 ILE E O   1 
ATOM   9512  C CB  . ILE E  1 246 ? -33.234 -40.364  -75.652 1.00 55.82  ? 246 ILE E CB  1 
ATOM   9513  C CG1 . ILE E  1 246 ? -31.729 -40.620  -75.559 1.00 60.00  ? 246 ILE E CG1 1 
ATOM   9514  C CG2 . ILE E  1 246 ? -33.917 -41.456  -76.462 1.00 50.39  ? 246 ILE E CG2 1 
ATOM   9515  C CD1 . ILE E  1 246 ? -31.381 -42.003  -75.051 1.00 55.55  ? 246 ILE E CD1 1 
ATOM   9516  N N   . THR E  1 247 ? -31.761 -38.167  -77.739 1.00 82.34  ? 247 THR E N   1 
ATOM   9517  C CA  . THR E  1 247 ? -31.118 -37.923  -79.025 1.00 83.82  ? 247 THR E CA  1 
ATOM   9518  C C   . THR E  1 247 ? -29.769 -38.622  -79.151 1.00 79.99  ? 247 THR E C   1 
ATOM   9519  O O   . THR E  1 247 ? -28.960 -38.609  -78.223 1.00 86.72  ? 247 THR E O   1 
ATOM   9520  C CB  . THR E  1 247 ? -30.924 -36.417  -79.278 1.00 71.88  ? 247 THR E CB  1 
ATOM   9521  O OG1 . THR E  1 247 ? -32.196 -35.757  -79.253 1.00 80.68  ? 247 THR E OG1 1 
ATOM   9522  C CG2 . THR E  1 247 ? -30.262 -36.183  -80.629 1.00 54.91  ? 247 THR E CG2 1 
ATOM   9523  N N   . PHE E  1 248 ? -29.539 -39.230  -80.311 1.00 71.10  ? 248 PHE E N   1 
ATOM   9524  C CA  . PHE E  1 248 ? -28.261 -39.858  -80.616 1.00 75.23  ? 248 PHE E CA  1 
ATOM   9525  C C   . PHE E  1 248 ? -27.542 -39.090  -81.718 1.00 71.92  ? 248 PHE E C   1 
ATOM   9526  O O   . PHE E  1 248 ? -28.150 -38.693  -82.712 1.00 77.82  ? 248 PHE E O   1 
ATOM   9527  C CB  . PHE E  1 248 ? -28.459 -41.318  -81.027 1.00 57.61  ? 248 PHE E CB  1 
ATOM   9528  C CG  . PHE E  1 248 ? -28.886 -42.211  -79.898 1.00 60.77  ? 248 PHE E CG  1 
ATOM   9529  C CD1 . PHE E  1 248 ? -30.213 -42.270  -79.508 1.00 63.61  ? 248 PHE E CD1 1 
ATOM   9530  C CD2 . PHE E  1 248 ? -27.959 -42.989  -79.226 1.00 60.08  ? 248 PHE E CD2 1 
ATOM   9531  C CE1 . PHE E  1 248 ? -30.609 -43.090  -78.469 1.00 60.89  ? 248 PHE E CE1 1 
ATOM   9532  C CE2 . PHE E  1 248 ? -28.349 -43.811  -78.185 1.00 58.51  ? 248 PHE E CE2 1 
ATOM   9533  C CZ  . PHE E  1 248 ? -29.675 -43.861  -77.807 1.00 54.93  ? 248 PHE E CZ  1 
ATOM   9534  N N   . GLU E  1 249 ? -26.244 -38.882  -81.529 1.00 65.48  ? 249 GLU E N   1 
ATOM   9535  C CA  . GLU E  1 249 ? -25.435 -38.120  -82.471 1.00 70.06  ? 249 GLU E CA  1 
ATOM   9536  C C   . GLU E  1 249 ? -24.034 -38.712  -82.526 1.00 67.45  ? 249 GLU E C   1 
ATOM   9537  O O   . GLU E  1 249 ? -23.308 -38.694  -81.534 1.00 77.50  ? 249 GLU E O   1 
ATOM   9538  C CB  . GLU E  1 249 ? -25.377 -36.654  -82.041 1.00 78.48  ? 249 GLU E CB  1 
ATOM   9539  C CG  . GLU E  1 249 ? -24.576 -35.750  -82.959 1.00 95.49  ? 249 GLU E CG  1 
ATOM   9540  C CD  . GLU E  1 249 ? -24.620 -34.299  -82.518 1.00 111.37 ? 249 GLU E CD  1 
ATOM   9541  O OE1 . GLU E  1 249 ? -23.694 -33.538  -82.868 1.00 113.88 ? 249 GLU E OE1 1 
ATOM   9542  O OE2 . GLU E  1 249 ? -25.581 -33.921  -81.814 1.00 100.88 ? 249 GLU E OE2 1 
ATOM   9543  N N   . ALA E  1 250 ? -23.654 -39.240  -83.685 1.00 67.03  ? 250 ALA E N   1 
ATOM   9544  C CA  . ALA E  1 250 ? -22.386 -39.951  -83.801 1.00 73.99  ? 250 ALA E CA  1 
ATOM   9545  C C   . ALA E  1 250 ? -21.696 -39.763  -85.149 1.00 75.83  ? 250 ALA E C   1 
ATOM   9546  O O   . ALA E  1 250 ? -22.347 -39.671  -86.189 1.00 75.29  ? 250 ALA E O   1 
ATOM   9547  C CB  . ALA E  1 250 ? -22.590 -41.433  -83.517 1.00 76.29  ? 250 ALA E CB  1 
ATOM   9548  N N   . THR E  1 251 ? -20.369 -39.707  -85.111 1.00 74.74  ? 251 THR E N   1 
ATOM   9549  C CA  . THR E  1 251 ? -19.559 -39.712  -86.320 1.00 77.14  ? 251 THR E CA  1 
ATOM   9550  C C   . THR E  1 251 ? -18.907 -41.082  -86.450 1.00 78.41  ? 251 THR E C   1 
ATOM   9551  O O   . THR E  1 251 ? -17.957 -41.266  -87.212 1.00 82.16  ? 251 THR E O   1 
ATOM   9552  C CB  . THR E  1 251 ? -18.468 -38.629  -86.278 1.00 72.06  ? 251 THR E CB  1 
ATOM   9553  O OG1 . THR E  1 251 ? -17.823 -38.644  -84.999 1.00 77.87  ? 251 THR E OG1 1 
ATOM   9554  N N   . GLY E  1 252 ? -19.430 -42.039  -85.689 1.00 72.73  ? 252 GLY E N   1 
ATOM   9555  C CA  . GLY E  1 252 ? -18.923 -43.397  -85.697 1.00 73.07  ? 252 GLY E CA  1 
ATOM   9556  C C   . GLY E  1 252 ? -18.891 -44.018  -84.313 1.00 74.71  ? 252 GLY E C   1 
ATOM   9557  O O   . GLY E  1 252 ? -19.127 -43.342  -83.311 1.00 75.36  ? 252 GLY E O   1 
ATOM   9558  N N   . ASN E  1 253 ? -18.607 -45.316  -84.269 1.00 69.64  ? 253 ASN E N   1 
ATOM   9559  C CA  . ASN E  1 253 ? -18.406 -46.039  -83.015 1.00 65.12  ? 253 ASN E CA  1 
ATOM   9560  C C   . ASN E  1 253 ? -19.672 -46.241  -82.187 1.00 65.17  ? 253 ASN E C   1 
ATOM   9561  O O   . ASN E  1 253 ? -19.606 -46.674  -81.037 1.00 65.11  ? 253 ASN E O   1 
ATOM   9562  C CB  . ASN E  1 253 ? -17.316 -45.366  -82.175 1.00 69.16  ? 253 ASN E CB  1 
ATOM   9563  C CG  . ASN E  1 253 ? -16.008 -45.217  -82.929 1.00 70.16  ? 253 ASN E CG  1 
ATOM   9564  O OD1 . ASN E  1 253 ? -15.021 -45.883  -82.619 1.00 75.89  ? 253 ASN E OD1 1 
ATOM   9565  N ND2 . ASN E  1 253 ? -15.998 -44.345  -83.930 1.00 61.01  ? 253 ASN E ND2 1 
ATOM   9566  N N   . LEU E  1 254 ? -20.824 -45.943  -82.779 1.00 69.98  ? 254 LEU E N   1 
ATOM   9567  C CA  . LEU E  1 254 ? -22.088 -46.033  -82.057 1.00 63.46  ? 254 LEU E CA  1 
ATOM   9568  C C   . LEU E  1 254 ? -22.899 -47.280  -82.403 1.00 58.58  ? 254 LEU E C   1 
ATOM   9569  O O   . LEU E  1 254 ? -23.447 -47.394  -83.500 1.00 68.09  ? 254 LEU E O   1 
ATOM   9570  C CB  . LEU E  1 254 ? -22.936 -44.783  -82.302 1.00 63.18  ? 254 LEU E CB  1 
ATOM   9571  C CG  . LEU E  1 254 ? -24.329 -44.797  -81.669 1.00 60.22  ? 254 LEU E CG  1 
ATOM   9572  C CD1 . LEU E  1 254 ? -24.234 -44.972  -80.161 1.00 61.82  ? 254 LEU E CD1 1 
ATOM   9573  C CD2 . LEU E  1 254 ? -25.092 -43.530  -82.018 1.00 59.25  ? 254 LEU E CD2 1 
ATOM   9574  N N   . VAL E  1 255 ? -22.969 -48.212  -81.458 1.00 58.53  ? 255 VAL E N   1 
ATOM   9575  C CA  . VAL E  1 255 ? -23.874 -49.346  -81.573 1.00 54.05  ? 255 VAL E CA  1 
ATOM   9576  C C   . VAL E  1 255 ? -25.270 -48.873  -81.185 1.00 57.67  ? 255 VAL E C   1 
ATOM   9577  O O   . VAL E  1 255 ? -25.618 -48.836  -80.005 1.00 64.08  ? 255 VAL E O   1 
ATOM   9578  C CB  . VAL E  1 255 ? -23.450 -50.507  -80.658 1.00 56.62  ? 255 VAL E CB  1 
ATOM   9579  C CG1 . VAL E  1 255 ? -24.417 -51.674  -80.796 1.00 58.79  ? 255 VAL E CG1 1 
ATOM   9580  C CG2 . VAL E  1 255 ? -22.028 -50.944  -80.980 1.00 49.11  ? 255 VAL E CG2 1 
ATOM   9581  N N   . VAL E  1 256 ? -26.060 -48.504  -82.187 1.00 60.88  ? 256 VAL E N   1 
ATOM   9582  C CA  . VAL E  1 256 ? -27.355 -47.871  -81.957 1.00 57.73  ? 256 VAL E CA  1 
ATOM   9583  C C   . VAL E  1 256 ? -28.414 -48.841  -81.445 1.00 65.63  ? 256 VAL E C   1 
ATOM   9584  O O   . VAL E  1 256 ? -28.356 -50.040  -81.721 1.00 63.86  ? 256 VAL E O   1 
ATOM   9585  C CB  . VAL E  1 256 ? -27.883 -47.193  -83.237 1.00 69.72  ? 256 VAL E CB  1 
ATOM   9586  C CG1 . VAL E  1 256 ? -26.870 -46.186  -83.758 1.00 73.29  ? 256 VAL E CG1 1 
ATOM   9587  C CG2 . VAL E  1 256 ? -28.200 -48.236  -84.297 1.00 76.14  ? 256 VAL E CG2 1 
ATOM   9588  N N   . PRO E  1 257 ? -29.389 -48.317  -80.689 1.00 70.92  ? 257 PRO E N   1 
ATOM   9589  C CA  . PRO E  1 257 ? -30.525 -49.108  -80.207 1.00 56.45  ? 257 PRO E CA  1 
ATOM   9590  C C   . PRO E  1 257 ? -31.420 -49.533  -81.364 1.00 68.58  ? 257 PRO E C   1 
ATOM   9591  O O   . PRO E  1 257 ? -31.608 -48.764  -82.306 1.00 74.09  ? 257 PRO E O   1 
ATOM   9592  C CB  . PRO E  1 257 ? -31.283 -48.123  -79.309 1.00 56.48  ? 257 PRO E CB  1 
ATOM   9593  C CG  . PRO E  1 257 ? -30.298 -47.054  -78.973 1.00 64.36  ? 257 PRO E CG  1 
ATOM   9594  C CD  . PRO E  1 257 ? -29.415 -46.940  -80.169 1.00 59.85  ? 257 PRO E CD  1 
ATOM   9595  N N   . ARG E  1 258 ? -31.955 -50.747  -81.295 1.00 74.51  ? 258 ARG E N   1 
ATOM   9596  C CA  . ARG E  1 258 ? -32.942 -51.203  -82.265 1.00 73.08  ? 258 ARG E CA  1 
ATOM   9597  C C   . ARG E  1 258 ? -34.271 -51.414  -81.552 1.00 62.95  ? 258 ARG E C   1 
ATOM   9598  O O   . ARG E  1 258 ? -35.312 -50.930  -81.996 1.00 67.72  ? 258 ARG E O   1 
ATOM   9599  C CB  . ARG E  1 258 ? -32.485 -52.497  -82.945 1.00 70.81  ? 258 ARG E CB  1 
ATOM   9600  C CG  . ARG E  1 258 ? -33.489 -53.072  -83.937 1.00 73.17  ? 258 ARG E CG  1 
ATOM   9601  C CD  . ARG E  1 258 ? -32.977 -54.367  -84.558 1.00 74.52  ? 258 ARG E CD  1 
ATOM   9602  N NE  . ARG E  1 258 ? -34.068 -55.240  -84.986 1.00 88.93  ? 258 ARG E NE  1 
ATOM   9603  C CZ  . ARG E  1 258 ? -34.634 -55.207  -86.188 1.00 96.09  ? 258 ARG E CZ  1 
ATOM   9604  N NH1 . ARG E  1 258 ? -34.218 -54.342  -87.098 1.00 99.80  ? 258 ARG E NH1 1 
ATOM   9605  N NH2 . ARG E  1 258 ? -35.623 -56.038  -86.481 1.00 97.64  ? 258 ARG E NH2 1 
ATOM   9606  N N   . TYR E  1 259 ? -34.222 -52.133  -80.436 1.00 66.35  ? 259 TYR E N   1 
ATOM   9607  C CA  . TYR E  1 259 ? -35.397 -52.338  -79.601 1.00 64.05  ? 259 TYR E CA  1 
ATOM   9608  C C   . TYR E  1 259 ? -35.234 -51.656  -78.248 1.00 62.66  ? 259 TYR E C   1 
ATOM   9609  O O   . TYR E  1 259 ? -34.171 -51.724  -77.631 1.00 61.04  ? 259 TYR E O   1 
ATOM   9610  C CB  . TYR E  1 259 ? -35.660 -53.830  -79.392 1.00 68.07  ? 259 TYR E CB  1 
ATOM   9611  C CG  . TYR E  1 259 ? -36.174 -54.546  -80.618 1.00 82.32  ? 259 TYR E CG  1 
ATOM   9612  C CD1 . TYR E  1 259 ? -35.298 -55.093  -81.545 1.00 80.92  ? 259 TYR E CD1 1 
ATOM   9613  C CD2 . TYR E  1 259 ? -37.537 -54.679  -80.847 1.00 88.32  ? 259 TYR E CD2 1 
ATOM   9614  C CE1 . TYR E  1 259 ? -35.764 -55.751  -82.666 1.00 91.62  ? 259 TYR E CE1 1 
ATOM   9615  C CE2 . TYR E  1 259 ? -38.013 -55.335  -81.966 1.00 89.22  ? 259 TYR E CE2 1 
ATOM   9616  C CZ  . TYR E  1 259 ? -37.122 -55.868  -82.873 1.00 90.67  ? 259 TYR E CZ  1 
ATOM   9617  O OH  . TYR E  1 259 ? -37.590 -56.523  -83.989 1.00 98.20  ? 259 TYR E OH  1 
ATOM   9618  N N   . ALA E  1 260 ? -36.293 -50.992  -77.798 1.00 61.50  ? 260 ALA E N   1 
ATOM   9619  C CA  . ALA E  1 260 ? -36.328 -50.418  -76.461 1.00 58.38  ? 260 ALA E CA  1 
ATOM   9620  C C   . ALA E  1 260 ? -37.370 -51.163  -75.639 1.00 64.66  ? 260 ALA E C   1 
ATOM   9621  O O   . ALA E  1 260 ? -37.950 -52.143  -76.106 1.00 62.03  ? 260 ALA E O   1 
ATOM   9622  C CB  . ALA E  1 260 ? -36.651 -48.939  -76.523 1.00 57.99  ? 260 ALA E CB  1 
ATOM   9623  N N   . PHE E  1 261 ? -37.614 -50.700  -74.418 1.00 63.08  ? 261 PHE E N   1 
ATOM   9624  C CA  . PHE E  1 261 ? -38.550 -51.388  -73.539 1.00 53.97  ? 261 PHE E CA  1 
ATOM   9625  C C   . PHE E  1 261 ? -39.477 -50.436  -72.787 1.00 58.34  ? 261 PHE E C   1 
ATOM   9626  O O   . PHE E  1 261 ? -39.052 -49.738  -71.866 1.00 59.71  ? 261 PHE E O   1 
ATOM   9627  C CB  . PHE E  1 261 ? -37.795 -52.280  -72.546 1.00 42.41  ? 261 PHE E CB  1 
ATOM   9628  C CG  . PHE E  1 261 ? -36.932 -53.323  -73.201 1.00 48.68  ? 261 PHE E CG  1 
ATOM   9629  C CD1 . PHE E  1 261 ? -35.598 -53.070  -73.467 1.00 58.44  ? 261 PHE E CD1 1 
ATOM   9630  C CD2 . PHE E  1 261 ? -37.454 -54.557  -73.551 1.00 55.47  ? 261 PHE E CD2 1 
ATOM   9631  C CE1 . PHE E  1 261 ? -34.802 -54.027  -74.068 1.00 57.99  ? 261 PHE E CE1 1 
ATOM   9632  C CE2 . PHE E  1 261 ? -36.665 -55.519  -74.152 1.00 50.36  ? 261 PHE E CE2 1 
ATOM   9633  C CZ  . PHE E  1 261 ? -35.337 -55.254  -74.411 1.00 53.95  ? 261 PHE E CZ  1 
ATOM   9634  N N   . ALA E  1 262 ? -40.744 -50.409  -73.191 1.00 66.52  ? 262 ALA E N   1 
ATOM   9635  C CA  . ALA E  1 262 ? -41.767 -49.711  -72.424 1.00 55.80  ? 262 ALA E CA  1 
ATOM   9636  C C   . ALA E  1 262 ? -41.914 -50.451  -71.105 1.00 66.05  ? 262 ALA E C   1 
ATOM   9637  O O   . ALA E  1 262 ? -42.162 -51.658  -71.088 1.00 70.26  ? 262 ALA E O   1 
ATOM   9638  C CB  . ALA E  1 262 ? -43.081 -49.689  -73.178 1.00 75.06  ? 262 ALA E CB  1 
ATOM   9639  N N   . MET E  1 263 ? -41.754 -49.734  -69.999 1.00 63.44  ? 263 MET E N   1 
ATOM   9640  C CA  . MET E  1 263 ? -41.582 -50.391  -68.712 1.00 63.74  ? 263 MET E CA  1 
ATOM   9641  C C   . MET E  1 263 ? -42.184 -49.625  -67.540 1.00 60.29  ? 263 MET E C   1 
ATOM   9642  O O   . MET E  1 263 ? -41.947 -48.429  -67.372 1.00 70.35  ? 263 MET E O   1 
ATOM   9643  C CB  . MET E  1 263 ? -40.092 -50.626  -68.461 1.00 60.70  ? 263 MET E CB  1 
ATOM   9644  C CG  . MET E  1 263 ? -39.781 -51.444  -67.225 1.00 67.44  ? 263 MET E CG  1 
ATOM   9645  S SD  . MET E  1 263 ? -38.007 -51.531  -66.921 1.00 67.84  ? 263 MET E SD  1 
ATOM   9646  C CE  . MET E  1 263 ? -37.648 -49.825  -66.515 1.00 69.10  ? 263 MET E CE  1 
ATOM   9647  N N   . GLU E  1 264 ? -42.962 -50.335  -66.731 1.00 62.97  ? 264 GLU E N   1 
ATOM   9648  C CA  . GLU E  1 264 ? -43.474 -49.798  -65.480 1.00 69.10  ? 264 GLU E CA  1 
ATOM   9649  C C   . GLU E  1 264 ? -42.986 -50.679  -64.340 1.00 68.81  ? 264 GLU E C   1 
ATOM   9650  O O   . GLU E  1 264 ? -43.369 -51.842  -64.237 1.00 74.19  ? 264 GLU E O   1 
ATOM   9651  C CB  . GLU E  1 264 ? -44.997 -49.745  -65.502 1.00 74.17  ? 264 GLU E CB  1 
ATOM   9652  C CG  . GLU E  1 264 ? -45.557 -48.339  -65.525 1.00 95.14  ? 264 GLU E CG  1 
ATOM   9653  C CD  . GLU E  1 264 ? -46.961 -48.296  -66.067 1.00 114.71 ? 264 GLU E CD  1 
ATOM   9654  O OE1 . GLU E  1 264 ? -47.801 -47.571  -65.492 1.00 112.83 ? 264 GLU E OE1 1 
ATOM   9655  O OE2 . GLU E  1 264 ? -47.225 -48.998  -67.066 1.00 125.83 ? 264 GLU E OE2 1 
ATOM   9656  N N   . ARG E  1 265 ? -42.134 -50.118  -63.490 1.00 69.12  ? 265 ARG E N   1 
ATOM   9657  C CA  . ARG E  1 265 ? -41.471 -50.894  -62.450 1.00 75.49  ? 265 ARG E CA  1 
ATOM   9658  C C   . ARG E  1 265 ? -41.967 -50.566  -61.046 1.00 80.41  ? 265 ARG E C   1 
ATOM   9659  O O   . ARG E  1 265 ? -42.247 -49.411  -60.725 1.00 76.43  ? 265 ARG E O   1 
ATOM   9660  C CB  . ARG E  1 265 ? -39.957 -50.689  -62.531 1.00 64.56  ? 265 ARG E CB  1 
ATOM   9661  C CG  . ARG E  1 265 ? -39.554 -49.302  -63.013 1.00 75.00  ? 265 ARG E CG  1 
ATOM   9662  C CD  . ARG E  1 265 ? -38.043 -49.152  -63.105 1.00 78.88  ? 265 ARG E CD  1 
ATOM   9663  N NE  . ARG E  1 265 ? -37.488 -48.430  -61.965 1.00 74.01  ? 265 ARG E NE  1 
ATOM   9664  C CZ  . ARG E  1 265 ? -37.294 -47.115  -61.936 1.00 74.90  ? 265 ARG E CZ  1 
ATOM   9665  N NH1 . ARG E  1 265 ? -37.611 -46.375  -62.988 1.00 73.62  ? 265 ARG E NH1 1 
ATOM   9666  N NH2 . ARG E  1 265 ? -36.783 -46.539  -60.858 1.00 86.89  ? 265 ARG E NH2 1 
ATOM   9667  N N   . ASN E  1 266 ? -42.076 -51.599  -60.219 1.00 81.20  ? 266 ASN E N   1 
ATOM   9668  C CA  . ASN E  1 266 ? -42.394 -51.435  -58.807 1.00 92.74  ? 266 ASN E CA  1 
ATOM   9669  C C   . ASN E  1 266 ? -41.186 -51.795  -57.953 1.00 88.22  ? 266 ASN E C   1 
ATOM   9670  O O   . ASN E  1 266 ? -40.567 -52.839  -58.148 1.00 90.84  ? 266 ASN E O   1 
ATOM   9671  C CB  . ASN E  1 266 ? -43.605 -52.287  -58.422 1.00 98.96  ? 266 ASN E CB  1 
ATOM   9672  C CG  . ASN E  1 266 ? -43.765 -53.509  -59.307 1.00 87.63  ? 266 ASN E CG  1 
ATOM   9673  O OD1 . ASN E  1 266 ? -44.820 -53.721  -59.905 1.00 80.12  ? 266 ASN E OD1 1 
ATOM   9674  N ND2 . ASN E  1 266 ? -42.714 -54.314  -59.402 1.00 81.78  ? 266 ASN E ND2 1 
ATOM   9675  N N   . ALA E  1 267 ? -40.849 -50.922  -57.012 1.00 85.15  ? 267 ALA E N   1 
ATOM   9676  C CA  . ALA E  1 267 ? -39.642 -51.092  -56.212 1.00 91.01  ? 267 ALA E CA  1 
ATOM   9677  C C   . ALA E  1 267 ? -39.767 -52.221  -55.194 1.00 89.65  ? 267 ALA E C   1 
ATOM   9678  O O   . ALA E  1 267 ? -40.867 -52.557  -54.755 1.00 85.84  ? 267 ALA E O   1 
ATOM   9679  C CB  . ALA E  1 267 ? -39.296 -49.790  -55.507 1.00 96.50  ? 267 ALA E CB  1 
ATOM   9680  N N   . GLY E  1 268 ? -38.630 -52.810  -54.832 1.00 92.59  ? 268 GLY E N   1 
ATOM   9681  C CA  . GLY E  1 268 ? -38.572 -53.703  -53.690 1.00 96.36  ? 268 GLY E CA  1 
ATOM   9682  C C   . GLY E  1 268 ? -38.529 -55.204  -53.925 1.00 93.98  ? 268 GLY E C   1 
ATOM   9683  O O   . GLY E  1 268 ? -39.008 -55.965  -53.086 1.00 93.39  ? 268 GLY E O   1 
ATOM   9684  N N   . SER E  1 269 ? -37.955 -55.643  -55.041 1.00 70.70  ? 269 SER E N   1 
ATOM   9685  C CA  . SER E  1 269 ? -37.767 -57.077  -55.261 1.00 61.75  ? 269 SER E CA  1 
ATOM   9686  C C   . SER E  1 269 ? -36.286 -57.436  -55.308 1.00 62.56  ? 269 SER E C   1 
ATOM   9687  O O   . SER E  1 269 ? -35.446 -56.704  -54.784 1.00 71.47  ? 269 SER E O   1 
ATOM   9688  C CB  . SER E  1 269 ? -38.469 -57.543  -56.537 1.00 65.50  ? 269 SER E CB  1 
ATOM   9689  O OG  . SER E  1 269 ? -38.403 -58.955  -56.662 1.00 50.30  ? 269 SER E OG  1 
ATOM   9690  N N   . GLY E  1 270 ? -35.967 -58.565  -55.932 1.00 50.39  ? 270 GLY E N   1 
ATOM   9691  C CA  . GLY E  1 270 ? -34.592 -59.020  -56.001 1.00 52.26  ? 270 GLY E CA  1 
ATOM   9692  C C   . GLY E  1 270 ? -34.324 -60.021  -57.107 1.00 41.61  ? 270 GLY E C   1 
ATOM   9693  O O   . GLY E  1 270 ? -35.167 -60.259  -57.972 1.00 48.77  ? 270 GLY E O   1 
ATOM   9694  N N   . ILE E  1 271 ? -33.133 -60.609  -57.070 1.00 41.77  ? 271 ILE E N   1 
ATOM   9695  C CA  . ILE E  1 271 ? -32.711 -61.579  -58.070 1.00 39.09  ? 271 ILE E CA  1 
ATOM   9696  C C   . ILE E  1 271 ? -32.128 -62.808  -57.386 1.00 48.19  ? 271 ILE E C   1 
ATOM   9697  O O   . ILE E  1 271 ? -31.129 -62.716  -56.673 1.00 56.92  ? 271 ILE E O   1 
ATOM   9698  C CB  . ILE E  1 271 ? -31.654 -60.976  -59.011 1.00 42.04  ? 271 ILE E CB  1 
ATOM   9699  C CG1 . ILE E  1 271 ? -32.224 -59.749  -59.724 1.00 49.27  ? 271 ILE E CG1 1 
ATOM   9700  C CG2 . ILE E  1 271 ? -31.173 -62.017  -60.013 1.00 53.35  ? 271 ILE E CG2 1 
ATOM   9701  C CD1 . ILE E  1 271 ? -31.170 -58.791  -60.228 1.00 57.32  ? 271 ILE E CD1 1 
ATOM   9702  N N   . ILE E  1 272 ? -32.760 -63.956  -57.600 1.00 50.85  ? 272 ILE E N   1 
ATOM   9703  C CA  . ILE E  1 272 ? -32.307 -65.198  -56.988 1.00 56.32  ? 272 ILE E CA  1 
ATOM   9704  C C   . ILE E  1 272 ? -31.469 -66.022  -57.958 1.00 58.39  ? 272 ILE E C   1 
ATOM   9705  O O   . ILE E  1 272 ? -31.908 -66.329  -59.066 1.00 61.79  ? 272 ILE E O   1 
ATOM   9706  C CB  . ILE E  1 272 ? -33.490 -66.054  -56.496 1.00 51.74  ? 272 ILE E CB  1 
ATOM   9707  C CG1 . ILE E  1 272 ? -34.270 -65.314  -55.409 1.00 52.47  ? 272 ILE E CG1 1 
ATOM   9708  C CG2 . ILE E  1 272 ? -32.997 -67.396  -55.978 1.00 53.61  ? 272 ILE E CG2 1 
ATOM   9709  C CD1 . ILE E  1 272 ? -35.376 -66.137  -54.784 1.00 49.03  ? 272 ILE E CD1 1 
ATOM   9710  N N   . ILE E  1 273 ? -30.259 -66.370  -57.536 1.00 55.07  ? 273 ILE E N   1 
ATOM   9711  C CA  . ILE E  1 273 ? -29.406 -67.258  -58.315 1.00 66.55  ? 273 ILE E CA  1 
ATOM   9712  C C   . ILE E  1 273 ? -29.528 -68.676  -57.769 1.00 71.31  ? 273 ILE E C   1 
ATOM   9713  O O   . ILE E  1 273 ? -28.949 -69.006  -56.734 1.00 69.16  ? 273 ILE E O   1 
ATOM   9714  C CB  . ILE E  1 273 ? -27.929 -66.817  -58.292 1.00 60.21  ? 273 ILE E CB  1 
ATOM   9715  C CG1 . ILE E  1 273 ? -27.773 -65.408  -58.873 1.00 62.05  ? 273 ILE E CG1 1 
ATOM   9716  C CG2 . ILE E  1 273 ? -27.069 -67.803  -59.065 1.00 70.33  ? 273 ILE E CG2 1 
ATOM   9717  C CD1 . ILE E  1 273 ? -28.118 -64.295  -57.905 1.00 83.30  ? 273 ILE E CD1 1 
ATOM   9718  N N   . SER E  1 274 ? -30.290 -69.510  -58.469 1.00 74.47  ? 274 SER E N   1 
ATOM   9719  C CA  . SER E  1 274 ? -30.590 -70.854  -57.991 1.00 67.93  ? 274 SER E CA  1 
ATOM   9720  C C   . SER E  1 274 ? -30.842 -71.835  -59.133 1.00 80.01  ? 274 SER E C   1 
ATOM   9721  O O   . SER E  1 274 ? -31.232 -71.439  -60.232 1.00 80.06  ? 274 SER E O   1 
ATOM   9722  C CB  . SER E  1 274 ? -31.804 -70.819  -57.060 1.00 70.05  ? 274 SER E CB  1 
ATOM   9723  O OG  . SER E  1 274 ? -32.368 -72.109  -56.906 1.00 78.09  ? 274 SER E OG  1 
ATOM   9724  N N   . ASP E  1 275 ? -30.616 -73.116  -58.859 1.00 110.84 ? 275 ASP E N   1 
ATOM   9725  C CA  . ASP E  1 275 ? -30.891 -74.173  -59.824 1.00 110.71 ? 275 ASP E CA  1 
ATOM   9726  C C   . ASP E  1 275 ? -32.322 -74.668  -59.654 1.00 99.70  ? 275 ASP E C   1 
ATOM   9727  O O   . ASP E  1 275 ? -32.907 -75.237  -60.575 1.00 120.65 ? 275 ASP E O   1 
ATOM   9728  C CB  . ASP E  1 275 ? -29.918 -75.338  -59.634 1.00 127.05 ? 275 ASP E CB  1 
ATOM   9729  C CG  . ASP E  1 275 ? -28.469 -74.926  -59.807 1.00 152.95 ? 275 ASP E CG  1 
ATOM   9730  O OD1 . ASP E  1 275 ? -27.769 -74.766  -58.785 1.00 161.57 ? 275 ASP E OD1 1 
ATOM   9731  O OD2 . ASP E  1 275 ? -28.029 -74.766  -60.965 1.00 148.05 ? 275 ASP E OD2 1 
ATOM   9732  N N   . THR E  1 276 ? -32.871 -74.443  -58.464 1.00 69.37  ? 276 THR E N   1 
ATOM   9733  C CA  . THR E  1 276 ? -34.219 -74.886  -58.114 1.00 74.24  ? 276 THR E CA  1 
ATOM   9734  C C   . THR E  1 276 ? -35.223 -74.672  -59.245 1.00 79.69  ? 276 THR E C   1 
ATOM   9735  O O   . THR E  1 276 ? -35.222 -73.627  -59.895 1.00 75.82  ? 276 THR E O   1 
ATOM   9736  C CB  . THR E  1 276 ? -34.723 -74.167  -56.844 1.00 67.57  ? 276 THR E CB  1 
ATOM   9737  O OG1 . THR E  1 276 ? -33.795 -74.378  -55.773 1.00 60.73  ? 276 THR E OG1 1 
ATOM   9738  C CG2 . THR E  1 276 ? -36.095 -74.686  -56.433 1.00 65.24  ? 276 THR E CG2 1 
ATOM   9739  N N   . PRO E  1 277 ? -36.082 -75.675  -59.484 1.00 81.20  ? 277 PRO E N   1 
ATOM   9740  C CA  . PRO E  1 277 ? -37.103 -75.636  -60.537 1.00 82.93  ? 277 PRO E CA  1 
ATOM   9741  C C   . PRO E  1 277 ? -38.141 -74.538  -60.324 1.00 77.93  ? 277 PRO E C   1 
ATOM   9742  O O   . PRO E  1 277 ? -38.614 -74.341  -59.204 1.00 73.95  ? 277 PRO E O   1 
ATOM   9743  C CB  . PRO E  1 277 ? -37.780 -77.006  -60.418 1.00 94.51  ? 277 PRO E CB  1 
ATOM   9744  C CG  . PRO E  1 277 ? -36.781 -77.874  -59.741 1.00 97.49  ? 277 PRO E CG  1 
ATOM   9745  C CD  . PRO E  1 277 ? -36.049 -76.978  -58.797 1.00 79.64  ? 277 PRO E CD  1 
ATOM   9746  N N   . VAL E  1 278 ? -38.488 -73.833  -61.397 1.00 80.79  ? 278 VAL E N   1 
ATOM   9747  C CA  . VAL E  1 278 ? -39.596 -72.888  -61.364 1.00 82.68  ? 278 VAL E CA  1 
ATOM   9748  C C   . VAL E  1 278 ? -40.900 -73.676  -61.386 1.00 79.19  ? 278 VAL E C   1 
ATOM   9749  O O   . VAL E  1 278 ? -40.996 -74.707  -62.051 1.00 82.61  ? 278 VAL E O   1 
ATOM   9750  C CB  . VAL E  1 278 ? -39.550 -71.918  -62.561 1.00 75.60  ? 278 VAL E CB  1 
ATOM   9751  C CG1 . VAL E  1 278 ? -39.474 -72.690  -63.870 1.00 92.21  ? 278 VAL E CG1 1 
ATOM   9752  C CG2 . VAL E  1 278 ? -40.757 -70.990  -62.545 1.00 64.28  ? 278 VAL E CG2 1 
ATOM   9753  N N   . HIS E  1 279 ? -41.902 -73.199  -60.654 1.00 73.75  ? 279 HIS E N   1 
ATOM   9754  C CA  . HIS E  1 279 ? -43.145 -73.948  -60.508 1.00 79.23  ? 279 HIS E CA  1 
ATOM   9755  C C   . HIS E  1 279 ? -44.397 -73.083  -60.582 1.00 86.68  ? 279 HIS E C   1 
ATOM   9756  O O   . HIS E  1 279 ? -44.355 -71.876  -60.339 1.00 97.93  ? 279 HIS E O   1 
ATOM   9757  C CB  . HIS E  1 279 ? -43.140 -74.726  -59.190 1.00 96.96  ? 279 HIS E CB  1 
ATOM   9758  C CG  . HIS E  1 279 ? -42.868 -76.189  -59.351 1.00 109.65 ? 279 HIS E CG  1 
ATOM   9759  N ND1 . HIS E  1 279 ? -43.866 -77.138  -59.313 1.00 103.34 ? 279 HIS E ND1 1 
ATOM   9760  C CD2 . HIS E  1 279 ? -41.713 -76.865  -59.553 1.00 108.31 ? 279 HIS E CD2 1 
ATOM   9761  C CE1 . HIS E  1 279 ? -43.338 -78.337  -59.482 1.00 121.67 ? 279 HIS E CE1 1 
ATOM   9762  N NE2 . HIS E  1 279 ? -42.031 -78.199  -59.630 1.00 114.73 ? 279 HIS E NE2 1 
ATOM   9763  N N   . ASP E  1 280 ? -45.513 -73.721  -60.922 1.00 93.45  ? 280 ASP E N   1 
ATOM   9764  C CA  . ASP E  1 280 ? -46.818 -73.077  -60.890 1.00 109.21 ? 280 ASP E CA  1 
ATOM   9765  C C   . ASP E  1 280 ? -47.438 -73.255  -59.509 1.00 108.31 ? 280 ASP E C   1 
ATOM   9766  O O   . ASP E  1 280 ? -48.294 -74.117  -59.309 1.00 129.12 ? 280 ASP E O   1 
ATOM   9767  C CB  . ASP E  1 280 ? -47.736 -73.666  -61.964 1.00 119.04 ? 280 ASP E CB  1 
ATOM   9768  C CG  . ASP E  1 280 ? -49.147 -73.105  -61.902 1.00 132.26 ? 280 ASP E CG  1 
ATOM   9769  O OD1 . ASP E  1 280 ? -49.339 -72.037  -61.285 1.00 127.24 ? 280 ASP E OD1 1 
ATOM   9770  O OD2 . ASP E  1 280 ? -50.066 -73.732  -62.471 1.00 139.49 ? 280 ASP E OD2 1 
ATOM   9771  N N   . CYS E  1 281 ? -46.986 -72.437  -58.563 1.00 97.18  ? 281 CYS E N   1 
ATOM   9772  C CA  . CYS E  1 281 ? -47.482 -72.463  -57.192 1.00 97.12  ? 281 CYS E CA  1 
ATOM   9773  C C   . CYS E  1 281 ? -47.439 -71.054  -56.586 1.00 78.03  ? 281 CYS E C   1 
ATOM   9774  O O   . CYS E  1 281 ? -46.700 -70.188  -57.052 1.00 78.54  ? 281 CYS E O   1 
ATOM   9775  C CB  . CYS E  1 281 ? -46.661 -73.442  -56.346 1.00 83.36  ? 281 CYS E CB  1 
ATOM   9776  S SG  . CYS E  1 281 ? -44.890 -73.079  -56.302 1.00 119.52 ? 281 CYS E SG  1 
ATOM   9777  N N   . ASN E  1 282 ? -48.152 -70.886  -55.486 1.00 82.71  ? 282 ASN E N   1 
ATOM   9778  C CA  . ASN E  1 282 ? -48.205 -69.628  -54.766 1.00 76.32  ? 282 ASN E CA  1 
ATOM   9779  C C   . ASN E  1 282 ? -47.388 -69.644  -53.522 1.00 75.35  ? 282 ASN E C   1 
ATOM   9780  O O   . ASN E  1 282 ? -47.283 -70.641  -52.837 1.00 80.59  ? 282 ASN E O   1 
ATOM   9781  C CB  . ASN E  1 282 ? -49.623 -69.243  -54.368 1.00 83.52  ? 282 ASN E CB  1 
ATOM   9782  C CG  . ASN E  1 282 ? -49.698 -67.847  -53.786 1.00 98.06  ? 282 ASN E CG  1 
ATOM   9783  O OD1 . ASN E  1 282 ? -48.971 -66.968  -54.192 1.00 93.18  ? 282 ASN E OD1 1 
ATOM   9784  N ND2 . ASN E  1 282 ? -50.587 -67.642  -52.839 1.00 123.72 ? 282 ASN E ND2 1 
ATOM   9785  N N   . THR E  1 283 ? -46.823 -68.501  -53.209 1.00 68.50  ? 283 THR E N   1 
ATOM   9786  C CA  . THR E  1 283 ? -46.050 -68.426  -51.967 1.00 65.07  ? 283 THR E CA  1 
ATOM   9787  C C   . THR E  1 283 ? -46.010 -66.982  -51.477 1.00 56.42  ? 283 THR E C   1 
ATOM   9788  O O   . THR E  1 283 ? -46.231 -66.060  -52.253 1.00 60.23  ? 283 THR E O   1 
ATOM   9789  C CB  . THR E  1 283 ? -44.599 -68.932  -52.155 1.00 63.80  ? 283 THR E CB  1 
ATOM   9790  O OG1 . THR E  1 283 ? -43.948 -69.017  -50.882 1.00 51.91  ? 283 THR E OG1 1 
ATOM   9791  C CG2 . THR E  1 283 ? -43.807 -67.985  -53.049 1.00 52.75  ? 283 THR E CG2 1 
ATOM   9792  N N   . THR E  1 284 ? -45.730 -66.784  -50.194 1.00 61.99  ? 284 THR E N   1 
ATOM   9793  C CA  . THR E  1 284 ? -45.621 -65.436  -49.640 1.00 65.38  ? 284 THR E CA  1 
ATOM   9794  C C   . THR E  1 284 ? -44.167 -65.108  -49.349 1.00 54.82  ? 284 THR E C   1 
ATOM   9795  O O   . THR E  1 284 ? -43.810 -63.957  -49.096 1.00 43.12  ? 284 THR E O   1 
ATOM   9796  C CB  . THR E  1 284 ? -46.400 -65.293  -48.323 1.00 61.34  ? 284 THR E CB  1 
ATOM   9797  O OG1 . THR E  1 284 ? -46.436 -63.914  -47.933 1.00 60.54  ? 284 THR E OG1 1 
ATOM   9798  C CG2 . THR E  1 284 ? -45.745 -66.114  -47.225 1.00 61.15  ? 284 THR E CG2 1 
ATOM   9799  N N   . CYS E  1 285 ? -43.334 -66.138  -49.377 1.00 46.93  ? 285 CYS E N   1 
ATOM   9800  C CA  . CYS E  1 285 ? -41.931 -66.001  -49.034 1.00 39.45  ? 285 CYS E CA  1 
ATOM   9801  C C   . CYS E  1 285 ? -41.121 -66.958  -49.892 1.00 42.73  ? 285 CYS E C   1 
ATOM   9802  O O   . CYS E  1 285 ? -41.402 -68.157  -49.937 1.00 47.77  ? 285 CYS E O   1 
ATOM   9803  C CB  . CYS E  1 285 ? -41.722 -66.305  -47.551 1.00 44.01  ? 285 CYS E CB  1 
ATOM   9804  S SG  . CYS E  1 285 ? -40.007 -66.231  -46.997 1.00 60.54  ? 285 CYS E SG  1 
ATOM   9805  N N   . GLN E  1 286 ? -40.122 -66.420  -50.582 1.00 37.96  ? 286 GLN E N   1 
ATOM   9806  C CA  . GLN E  1 286 ? -39.331 -67.212  -51.510 1.00 43.42  ? 286 GLN E CA  1 
ATOM   9807  C C   . GLN E  1 286 ? -37.853 -67.203  -51.140 1.00 46.39  ? 286 GLN E C   1 
ATOM   9808  O O   . GLN E  1 286 ? -37.273 -66.147  -50.888 1.00 54.51  ? 286 GLN E O   1 
ATOM   9809  C CB  . GLN E  1 286 ? -39.516 -66.691  -52.937 1.00 34.88  ? 286 GLN E CB  1 
ATOM   9810  C CG  . GLN E  1 286 ? -38.858 -67.553  -53.997 1.00 45.35  ? 286 GLN E CG  1 
ATOM   9811  C CD  . GLN E  1 286 ? -39.427 -68.956  -54.031 1.00 57.10  ? 286 GLN E CD  1 
ATOM   9812  O OE1 . GLN E  1 286 ? -40.618 -69.148  -54.271 1.00 54.95  ? 286 GLN E OE1 1 
ATOM   9813  N NE2 . GLN E  1 286 ? -38.576 -69.946  -53.790 1.00 46.49  ? 286 GLN E NE2 1 
ATOM   9814  N N   . THR E  1 287 ? -37.251 -68.387  -51.104 1.00 37.75  ? 287 THR E N   1 
ATOM   9815  C CA  . THR E  1 287 ? -35.819 -68.516  -50.866 1.00 42.89  ? 287 THR E CA  1 
ATOM   9816  C C   . THR E  1 287 ? -35.182 -69.220  -52.056 1.00 49.10  ? 287 THR E C   1 
ATOM   9817  O O   . THR E  1 287 ? -35.877 -69.865  -52.841 1.00 59.23  ? 287 THR E O   1 
ATOM   9818  C CB  . THR E  1 287 ? -35.521 -69.326  -49.590 1.00 49.27  ? 287 THR E CB  1 
ATOM   9819  O OG1 . THR E  1 287 ? -35.398 -70.716  -49.916 1.00 39.66  ? 287 THR E OG1 1 
ATOM   9820  C CG2 . THR E  1 287 ? -36.625 -69.138  -48.564 1.00 36.56  ? 287 THR E CG2 1 
ATOM   9821  N N   . PRO E  1 288 ? -33.855 -69.093  -52.201 1.00 51.97  ? 288 PRO E N   1 
ATOM   9822  C CA  . PRO E  1 288 ? -33.133 -69.759  -53.290 1.00 60.13  ? 288 PRO E CA  1 
ATOM   9823  C C   . PRO E  1 288 ? -33.297 -71.280  -53.277 1.00 55.96  ? 288 PRO E C   1 
ATOM   9824  O O   . PRO E  1 288 ? -33.140 -71.916  -54.319 1.00 57.12  ? 288 PRO E O   1 
ATOM   9825  C CB  . PRO E  1 288 ? -31.674 -69.389  -53.015 1.00 61.02  ? 288 PRO E CB  1 
ATOM   9826  C CG  . PRO E  1 288 ? -31.747 -68.103  -52.271 1.00 46.32  ? 288 PRO E CG  1 
ATOM   9827  C CD  . PRO E  1 288 ? -32.980 -68.199  -51.421 1.00 49.45  ? 288 PRO E CD  1 
ATOM   9828  N N   . LYS E  1 289 ? -33.607 -71.850  -52.116 1.00 52.98  ? 289 LYS E N   1 
ATOM   9829  C CA  . LYS E  1 289 ? -33.711 -73.300  -51.981 1.00 63.36  ? 289 LYS E CA  1 
ATOM   9830  C C   . LYS E  1 289 ? -35.139 -73.783  -52.214 1.00 63.38  ? 289 LYS E C   1 
ATOM   9831  O O   . LYS E  1 289 ? -35.362 -74.948  -52.547 1.00 68.94  ? 289 LYS E O   1 
ATOM   9832  C CB  . LYS E  1 289 ? -33.235 -73.740  -50.593 1.00 55.72  ? 289 LYS E CB  1 
ATOM   9833  C CG  . LYS E  1 289 ? -31.855 -73.224  -50.218 1.00 73.92  ? 289 LYS E CG  1 
ATOM   9834  C CD  . LYS E  1 289 ? -31.517 -73.477  -48.748 1.00 73.14  ? 289 LYS E CD  1 
ATOM   9835  C CE  . LYS E  1 289 ? -31.404 -74.961  -48.435 1.00 75.43  ? 289 LYS E CE  1 
ATOM   9836  N NZ  . LYS E  1 289 ? -30.225 -75.280  -47.580 1.00 84.96  ? 289 LYS E NZ  1 
ATOM   9837  N N   . GLY E  1 290 ? -36.101 -72.884  -52.040 1.00 53.42  ? 290 GLY E N   1 
ATOM   9838  C CA  . GLY E  1 290 ? -37.503 -73.240  -52.163 1.00 58.54  ? 290 GLY E CA  1 
ATOM   9839  C C   . GLY E  1 290 ? -38.399 -72.258  -51.430 1.00 61.09  ? 290 GLY E C   1 
ATOM   9840  O O   . GLY E  1 290 ? -37.921 -71.429  -50.656 1.00 64.30  ? 290 GLY E O   1 
ATOM   9841  N N   . ALA E  1 291 ? -39.703 -72.353  -51.668 1.00 62.74  ? 291 ALA E N   1 
ATOM   9842  C CA  . ALA E  1 291 ? -40.667 -71.428  -51.076 1.00 54.37  ? 291 ALA E CA  1 
ATOM   9843  C C   . ALA E  1 291 ? -41.018 -71.806  -49.638 1.00 59.53  ? 291 ALA E C   1 
ATOM   9844  O O   . ALA E  1 291 ? -40.821 -72.948  -49.221 1.00 59.25  ? 291 ALA E O   1 
ATOM   9845  C CB  . ALA E  1 291 ? -41.928 -71.358  -51.931 1.00 42.95  ? 291 ALA E CB  1 
ATOM   9846  N N   . ILE E  1 292 ? -41.541 -70.836  -48.890 1.00 58.30  ? 292 ILE E N   1 
ATOM   9847  C CA  . ILE E  1 292 ? -41.930 -71.038  -47.495 1.00 56.36  ? 292 ILE E CA  1 
ATOM   9848  C C   . ILE E  1 292 ? -43.419 -70.726  -47.268 1.00 67.60  ? 292 ILE E C   1 
ATOM   9849  O O   . ILE E  1 292 ? -43.819 -69.558  -47.270 1.00 68.62  ? 292 ILE E O   1 
ATOM   9850  C CB  . ILE E  1 292 ? -41.066 -70.161  -46.547 1.00 52.22  ? 292 ILE E CB  1 
ATOM   9851  C CG1 . ILE E  1 292 ? -39.610 -70.637  -46.547 1.00 42.34  ? 292 ILE E CG1 1 
ATOM   9852  C CG2 . ILE E  1 292 ? -41.638 -70.145  -45.134 1.00 63.08  ? 292 ILE E CG2 1 
ATOM   9853  C CD1 . ILE E  1 292 ? -38.965 -70.653  -45.164 1.00 58.55  ? 292 ILE E CD1 1 
ATOM   9854  N N   . ASN E  1 293 ? -44.229 -71.774  -47.094 1.00 85.28  ? 293 ASN E N   1 
ATOM   9855  C CA  . ASN E  1 293 ? -45.636 -71.644  -46.693 1.00 98.20  ? 293 ASN E CA  1 
ATOM   9856  C C   . ASN E  1 293 ? -45.753 -71.789  -45.180 1.00 100.59 ? 293 ASN E C   1 
ATOM   9857  O O   . ASN E  1 293 ? -45.943 -72.894  -44.674 1.00 115.19 ? 293 ASN E O   1 
ATOM   9858  C CB  . ASN E  1 293 ? -46.513 -72.695  -47.411 1.00 110.54 ? 293 ASN E CB  1 
ATOM   9859  C CG  . ASN E  1 293 ? -47.576 -73.320  -46.497 1.00 128.20 ? 293 ASN E CG  1 
ATOM   9860  O OD1 . ASN E  1 293 ? -48.604 -72.706  -46.210 1.00 117.08 ? 293 ASN E OD1 1 
ATOM   9861  N ND2 . ASN E  1 293 ? -47.317 -74.546  -46.028 1.00 128.48 ? 293 ASN E ND2 1 
ATOM   9862  N N   . THR E  1 294 ? -45.618 -70.690  -44.441 1.00 85.11  ? 294 THR E N   1 
ATOM   9863  C CA  . THR E  1 294 ? -45.671 -70.814  -42.984 1.00 101.14 ? 294 THR E CA  1 
ATOM   9864  C C   . THR E  1 294 ? -46.239 -69.627  -42.199 1.00 91.31  ? 294 THR E C   1 
ATOM   9865  O O   . THR E  1 294 ? -46.123 -68.469  -42.604 1.00 76.39  ? 294 THR E O   1 
ATOM   9866  C CB  . THR E  1 294 ? -44.300 -71.221  -42.395 1.00 89.64  ? 294 THR E CB  1 
ATOM   9867  O OG1 . THR E  1 294 ? -44.499 -72.059  -41.250 1.00 78.80  ? 294 THR E OG1 1 
ATOM   9868  C CG2 . THR E  1 294 ? -43.500 -69.997  -41.995 1.00 76.72  ? 294 THR E CG2 1 
ATOM   9869  N N   . SER E  1 295 ? -46.862 -69.954  -41.069 1.00 73.67  ? 295 SER E N   1 
ATOM   9870  C CA  . SER E  1 295 ? -47.396 -68.969  -40.138 1.00 78.58  ? 295 SER E CA  1 
ATOM   9871  C C   . SER E  1 295 ? -46.387 -68.705  -39.029 1.00 71.90  ? 295 SER E C   1 
ATOM   9872  O O   . SER E  1 295 ? -46.481 -67.708  -38.314 1.00 70.70  ? 295 SER E O   1 
ATOM   9873  C CB  . SER E  1 295 ? -48.703 -69.475  -39.519 1.00 78.24  ? 295 SER E CB  1 
ATOM   9874  O OG  . SER E  1 295 ? -49.832 -68.814  -40.063 1.00 109.14 ? 295 SER E OG  1 
ATOM   9875  N N   . LEU E  1 296 ? -45.426 -69.612  -38.887 1.00 52.28  ? 296 LEU E N   1 
ATOM   9876  C CA  . LEU E  1 296 ? -44.426 -69.517  -37.828 1.00 52.44  ? 296 LEU E CA  1 
ATOM   9877  C C   . LEU E  1 296 ? -43.592 -68.244  -37.946 1.00 50.21  ? 296 LEU E C   1 
ATOM   9878  O O   . LEU E  1 296 ? -43.319 -67.774  -39.050 1.00 43.50  ? 296 LEU E O   1 
ATOM   9879  C CB  . LEU E  1 296 ? -43.525 -70.753  -37.826 1.00 52.76  ? 296 LEU E CB  1 
ATOM   9880  C CG  . LEU E  1 296 ? -44.251 -72.093  -37.686 1.00 53.56  ? 296 LEU E CG  1 
ATOM   9881  C CD1 . LEU E  1 296 ? -43.255 -73.240  -37.589 1.00 57.77  ? 296 LEU E CD1 1 
ATOM   9882  C CD2 . LEU E  1 296 ? -45.178 -72.078  -36.480 1.00 50.02  ? 296 LEU E CD2 1 
ATOM   9883  N N   . PRO E  1 297 ? -43.189 -67.682  -36.797 1.00 51.13  ? 297 PRO E N   1 
ATOM   9884  C CA  . PRO E  1 297 ? -42.464 -66.409  -36.721 1.00 40.21  ? 297 PRO E CA  1 
ATOM   9885  C C   . PRO E  1 297 ? -41.017 -66.508  -37.195 1.00 46.99  ? 297 PRO E C   1 
ATOM   9886  O O   . PRO E  1 297 ? -40.436 -65.493  -37.579 1.00 45.70  ? 297 PRO E O   1 
ATOM   9887  C CB  . PRO E  1 297 ? -42.491 -66.077  -35.221 1.00 48.25  ? 297 PRO E CB  1 
ATOM   9888  C CG  . PRO E  1 297 ? -43.541 -66.971  -34.629 1.00 61.46  ? 297 PRO E CG  1 
ATOM   9889  C CD  . PRO E  1 297 ? -43.506 -68.207  -35.460 1.00 55.06  ? 297 PRO E CD  1 
ATOM   9890  N N   . PHE E  1 298 ? -40.443 -67.706  -37.169 1.00 43.70  ? 298 PHE E N   1 
ATOM   9891  C CA  . PHE E  1 298 ? -39.024 -67.860  -37.475 1.00 48.84  ? 298 PHE E CA  1 
ATOM   9892  C C   . PHE E  1 298 ? -38.735 -69.015  -38.430 1.00 49.06  ? 298 PHE E C   1 
ATOM   9893  O O   . PHE E  1 298 ? -39.417 -70.039  -38.412 1.00 52.34  ? 298 PHE E O   1 
ATOM   9894  C CB  . PHE E  1 298 ? -38.222 -68.042  -36.184 1.00 50.39  ? 298 PHE E CB  1 
ATOM   9895  C CG  . PHE E  1 298 ? -38.650 -67.130  -35.070 1.00 42.40  ? 298 PHE E CG  1 
ATOM   9896  C CD1 . PHE E  1 298 ? -38.277 -65.796  -35.065 1.00 41.02  ? 298 PHE E CD1 1 
ATOM   9897  C CD2 . PHE E  1 298 ? -39.422 -67.609  -34.025 1.00 43.36  ? 298 PHE E CD2 1 
ATOM   9898  C CE1 . PHE E  1 298 ? -38.670 -64.956  -34.040 1.00 53.17  ? 298 PHE E CE1 1 
ATOM   9899  C CE2 . PHE E  1 298 ? -39.817 -66.775  -32.997 1.00 44.75  ? 298 PHE E CE2 1 
ATOM   9900  C CZ  . PHE E  1 298 ? -39.441 -65.447  -33.004 1.00 44.09  ? 298 PHE E CZ  1 
ATOM   9901  N N   . GLN E  1 299 ? -37.713 -68.837  -39.259 1.00 48.37  ? 299 GLN E N   1 
ATOM   9902  C CA  . GLN E  1 299 ? -37.270 -69.875  -40.181 1.00 48.32  ? 299 GLN E CA  1 
ATOM   9903  C C   . GLN E  1 299 ? -35.747 -69.964  -40.187 1.00 45.12  ? 299 GLN E C   1 
ATOM   9904  O O   . GLN E  1 299 ? -35.059 -68.954  -40.041 1.00 70.74  ? 299 GLN E O   1 
ATOM   9905  C CB  . GLN E  1 299 ? -37.804 -69.606  -41.592 1.00 42.24  ? 299 GLN E CB  1 
ATOM   9906  C CG  . GLN E  1 299 ? -37.413 -68.253  -42.171 1.00 41.44  ? 299 GLN E CG  1 
ATOM   9907  C CD  . GLN E  1 299 ? -36.053 -68.270  -42.842 1.00 43.52  ? 299 GLN E CD  1 
ATOM   9908  O OE1 . GLN E  1 299 ? -35.476 -69.332  -43.074 1.00 48.17  ? 299 GLN E OE1 1 
ATOM   9909  N NE2 . GLN E  1 299 ? -35.537 -67.090  -43.163 1.00 37.24  ? 299 GLN E NE2 1 
ATOM   9910  N N   . ASN E  1 300 ? -35.225 -71.176  -40.346 1.00 46.46  ? 300 ASN E N   1 
ATOM   9911  C CA  . ASN E  1 300 ? -33.782 -71.388  -40.373 1.00 45.28  ? 300 ASN E CA  1 
ATOM   9912  C C   . ASN E  1 300 ? -33.325 -71.986  -41.696 1.00 37.59  ? 300 ASN E C   1 
ATOM   9913  O O   . ASN E  1 300 ? -32.257 -72.592  -41.783 1.00 44.85  ? 300 ASN E O   1 
ATOM   9914  C CB  . ASN E  1 300 ? -33.346 -72.286  -39.214 1.00 36.80  ? 300 ASN E CB  1 
ATOM   9915  C CG  . ASN E  1 300 ? -33.879 -73.700  -39.337 1.00 47.28  ? 300 ASN E CG  1 
ATOM   9916  O OD1 . ASN E  1 300 ? -34.739 -73.984  -40.171 1.00 62.27  ? 300 ASN E OD1 1 
ATOM   9917  N ND2 . ASN E  1 300 ? -33.368 -74.598  -38.503 1.00 46.39  ? 300 ASN E ND2 1 
ATOM   9918  N N   . ILE E  1 301 ? -34.146 -71.809  -42.725 1.00 39.84  ? 301 ILE E N   1 
ATOM   9919  C CA  . ILE E  1 301 ? -33.867 -72.373  -44.038 1.00 44.05  ? 301 ILE E CA  1 
ATOM   9920  C C   . ILE E  1 301 ? -32.785 -71.596  -44.778 1.00 46.55  ? 301 ILE E C   1 
ATOM   9921  O O   . ILE E  1 301 ? -31.778 -72.166  -45.198 1.00 59.59  ? 301 ILE E O   1 
ATOM   9922  C CB  . ILE E  1 301 ? -35.139 -72.427  -44.902 1.00 54.80  ? 301 ILE E CB  1 
ATOM   9923  C CG1 . ILE E  1 301 ? -36.152 -73.392  -44.281 1.00 48.93  ? 301 ILE E CG1 1 
ATOM   9924  C CG2 . ILE E  1 301 ? -34.800 -72.837  -46.327 1.00 48.27  ? 301 ILE E CG2 1 
ATOM   9925  C CD1 . ILE E  1 301 ? -37.424 -73.554  -45.082 1.00 62.76  ? 301 ILE E CD1 1 
ATOM   9926  N N   . HIS E  1 302 ? -32.993 -70.293  -44.934 1.00 39.57  ? 302 HIS E N   1 
ATOM   9927  C CA  . HIS E  1 302 ? -32.060 -69.465  -45.688 1.00 48.20  ? 302 HIS E CA  1 
ATOM   9928  C C   . HIS E  1 302 ? -32.149 -67.999  -45.272 1.00 46.23  ? 302 HIS E C   1 
ATOM   9929  O O   . HIS E  1 302 ? -33.241 -67.485  -45.026 1.00 46.61  ? 302 HIS E O   1 
ATOM   9930  C CB  . HIS E  1 302 ? -32.333 -69.603  -47.186 1.00 48.45  ? 302 HIS E CB  1 
ATOM   9931  C CG  . HIS E  1 302 ? -31.161 -69.255  -48.049 1.00 54.09  ? 302 HIS E CG  1 
ATOM   9932  N ND1 . HIS E  1 302 ? -30.821 -67.954  -48.356 1.00 46.95  ? 302 HIS E ND1 1 
ATOM   9933  C CD2 . HIS E  1 302 ? -30.252 -70.036  -48.675 1.00 56.18  ? 302 HIS E CD2 1 
ATOM   9934  C CE1 . HIS E  1 302 ? -29.754 -67.950  -49.131 1.00 50.44  ? 302 HIS E CE1 1 
ATOM   9935  N NE2 . HIS E  1 302 ? -29.387 -69.206  -49.341 1.00 47.18  ? 302 HIS E NE2 1 
ATOM   9936  N N   . PRO E  1 303 ? -30.992 -67.325  -45.188 1.00 43.36  ? 303 PRO E N   1 
ATOM   9937  C CA  . PRO E  1 303 ? -30.898 -65.909  -44.813 1.00 37.43  ? 303 PRO E CA  1 
ATOM   9938  C C   . PRO E  1 303 ? -31.448 -64.987  -45.899 1.00 49.21  ? 303 PRO E C   1 
ATOM   9939  O O   . PRO E  1 303 ? -32.196 -64.059  -45.594 1.00 39.41  ? 303 PRO E O   1 
ATOM   9940  C CB  . PRO E  1 303 ? -29.388 -65.685  -44.657 1.00 38.58  ? 303 PRO E CB  1 
ATOM   9941  C CG  . PRO E  1 303 ? -28.799 -67.053  -44.511 1.00 58.63  ? 303 PRO E CG  1 
ATOM   9942  C CD  . PRO E  1 303 ? -29.664 -67.938  -45.342 1.00 52.94  ? 303 PRO E CD  1 
ATOM   9943  N N   . ILE E  1 304 ? -31.071 -65.239  -47.148 1.00 47.47  ? 304 ILE E N   1 
ATOM   9944  C CA  . ILE E  1 304 ? -31.562 -64.441  -48.267 1.00 43.51  ? 304 ILE E CA  1 
ATOM   9945  C C   . ILE E  1 304 ? -32.991 -64.841  -48.613 1.00 38.96  ? 304 ILE E C   1 
ATOM   9946  O O   . ILE E  1 304 ? -33.268 -66.003  -48.912 1.00 55.80  ? 304 ILE E O   1 
ATOM   9947  C CB  . ILE E  1 304 ? -30.661 -64.573  -49.510 1.00 36.48  ? 304 ILE E CB  1 
ATOM   9948  C CG1 . ILE E  1 304 ? -29.378 -63.757  -49.330 1.00 34.75  ? 304 ILE E CG1 1 
ATOM   9949  C CG2 . ILE E  1 304 ? -31.397 -64.098  -50.751 1.00 52.10  ? 304 ILE E CG2 1 
ATOM   9950  C CD1 . ILE E  1 304 ? -28.491 -64.228  -48.197 1.00 51.45  ? 304 ILE E CD1 1 
ATOM   9951  N N   . THR E  1 305 ? -33.894 -63.868  -48.570 1.00 40.83  ? 305 THR E N   1 
ATOM   9952  C CA  . THR E  1 305 ? -35.317 -64.142  -48.706 1.00 35.24  ? 305 THR E CA  1 
ATOM   9953  C C   . THR E  1 305 ? -36.029 -63.024  -49.466 1.00 50.76  ? 305 THR E C   1 
ATOM   9954  O O   . THR E  1 305 ? -35.588 -61.875  -49.454 1.00 53.02  ? 305 THR E O   1 
ATOM   9955  C CB  . THR E  1 305 ? -35.966 -64.309  -47.318 1.00 41.32  ? 305 THR E CB  1 
ATOM   9956  O OG1 . THR E  1 305 ? -36.836 -65.448  -47.320 1.00 62.33  ? 305 THR E OG1 1 
ATOM   9957  C CG2 . THR E  1 305 ? -36.746 -63.057  -46.931 1.00 42.54  ? 305 THR E CG2 1 
ATOM   9958  N N   . ILE E  1 306 ? -37.127 -63.367  -50.134 1.00 47.44  ? 306 ILE E N   1 
ATOM   9959  C CA  . ILE E  1 306 ? -37.938 -62.374  -50.833 1.00 41.40  ? 306 ILE E CA  1 
ATOM   9960  C C   . ILE E  1 306 ? -39.416 -62.524  -50.485 1.00 44.68  ? 306 ILE E C   1 
ATOM   9961  O O   . ILE E  1 306 ? -39.948 -63.634  -50.461 1.00 46.83  ? 306 ILE E O   1 
ATOM   9962  C CB  . ILE E  1 306 ? -37.772 -62.462  -52.363 1.00 35.93  ? 306 ILE E CB  1 
ATOM   9963  C CG1 . ILE E  1 306 ? -36.295 -62.396  -52.750 1.00 42.09  ? 306 ILE E CG1 1 
ATOM   9964  C CG2 . ILE E  1 306 ? -38.541 -61.343  -53.043 1.00 37.03  ? 306 ILE E CG2 1 
ATOM   9965  C CD1 . ILE E  1 306 ? -36.062 -62.320  -54.245 1.00 39.50  ? 306 ILE E CD1 1 
ATOM   9966  N N   . GLY E  1 307 ? -40.071 -61.399  -50.216 1.00 48.31  ? 307 GLY E N   1 
ATOM   9967  C CA  . GLY E  1 307 ? -41.482 -61.396  -49.871 1.00 52.06  ? 307 GLY E CA  1 
ATOM   9968  C C   . GLY E  1 307 ? -41.719 -61.012  -48.423 1.00 47.99  ? 307 GLY E C   1 
ATOM   9969  O O   . GLY E  1 307 ? -40.917 -60.298  -47.822 1.00 56.49  ? 307 GLY E O   1 
ATOM   9970  N N   . LYS E  1 308 ? -42.833 -61.475  -47.866 1.00 44.93  ? 308 LYS E N   1 
ATOM   9971  C CA  . LYS E  1 308 ? -43.114 -61.285  -46.449 1.00 51.19  ? 308 LYS E CA  1 
ATOM   9972  C C   . LYS E  1 308 ? -42.783 -62.574  -45.707 1.00 40.47  ? 308 LYS E C   1 
ATOM   9973  O O   . LYS E  1 308 ? -43.596 -63.496  -45.653 1.00 54.91  ? 308 LYS E O   1 
ATOM   9974  C CB  . LYS E  1 308 ? -44.579 -60.905  -46.232 1.00 55.45  ? 308 LYS E CB  1 
ATOM   9975  C CG  . LYS E  1 308 ? -44.936 -60.665  -44.776 1.00 73.17  ? 308 LYS E CG  1 
ATOM   9976  C CD  . LYS E  1 308 ? -46.401 -60.303  -44.590 1.00 85.04  ? 308 LYS E CD  1 
ATOM   9977  C CE  . LYS E  1 308 ? -46.724 -58.951  -45.200 1.00 86.95  ? 308 LYS E CE  1 
ATOM   9978  N NZ  . LYS E  1 308 ? -47.834 -58.278  -44.468 1.00 95.89  ? 308 LYS E NZ  1 
ATOM   9979  N N   . CYS E  1 309 ? -41.585 -62.635  -45.135 1.00 51.97  ? 309 CYS E N   1 
ATOM   9980  C CA  . CYS E  1 309 ? -41.057 -63.894  -44.624 1.00 54.31  ? 309 CYS E CA  1 
ATOM   9981  C C   . CYS E  1 309 ? -40.848 -63.904  -43.115 1.00 43.52  ? 309 CYS E C   1 
ATOM   9982  O O   . CYS E  1 309 ? -40.716 -62.852  -42.492 1.00 49.81  ? 309 CYS E O   1 
ATOM   9983  C CB  . CYS E  1 309 ? -39.738 -64.220  -45.326 1.00 39.01  ? 309 CYS E CB  1 
ATOM   9984  S SG  . CYS E  1 309 ? -39.848 -64.211  -47.128 1.00 63.98  ? 309 CYS E SG  1 
ATOM   9985  N N   . PRO E  1 310 ? -40.821 -65.107  -42.522 1.00 43.02  ? 310 PRO E N   1 
ATOM   9986  C CA  . PRO E  1 310 ? -40.445 -65.267  -41.115 1.00 49.11  ? 310 PRO E CA  1 
ATOM   9987  C C   . PRO E  1 310 ? -39.005 -64.810  -40.911 1.00 47.66  ? 310 PRO E C   1 
ATOM   9988  O O   . PRO E  1 310 ? -38.244 -64.747  -41.877 1.00 41.13  ? 310 PRO E O   1 
ATOM   9989  C CB  . PRO E  1 310 ? -40.548 -66.780  -40.896 1.00 44.82  ? 310 PRO E CB  1 
ATOM   9990  C CG  . PRO E  1 310 ? -41.471 -67.262  -41.963 1.00 44.94  ? 310 PRO E CG  1 
ATOM   9991  C CD  . PRO E  1 310 ? -41.204 -66.386  -43.143 1.00 39.94  ? 310 PRO E CD  1 
ATOM   9992  N N   . LYS E  1 311 ? -38.630 -64.498  -39.677 1.00 44.53  ? 311 LYS E N   1 
ATOM   9993  C CA  . LYS E  1 311 ? -37.269 -64.046  -39.410 1.00 35.90  ? 311 LYS E CA  1 
ATOM   9994  C C   . LYS E  1 311 ? -36.259 -65.181  -39.496 1.00 47.50  ? 311 LYS E C   1 
ATOM   9995  O O   . LYS E  1 311 ? -36.519 -66.292  -39.032 1.00 47.12  ? 311 LYS E O   1 
ATOM   9996  C CB  . LYS E  1 311 ? -37.184 -63.380  -38.041 1.00 38.01  ? 311 LYS E CB  1 
ATOM   9997  C CG  . LYS E  1 311 ? -37.160 -61.864  -38.097 1.00 41.43  ? 311 LYS E CG  1 
ATOM   9998  C CD  . LYS E  1 311 ? -37.996 -61.327  -39.246 1.00 41.55  ? 311 LYS E CD  1 
ATOM   9999  C CE  . LYS E  1 311 ? -38.618 -59.987  -38.891 1.00 40.98  ? 311 LYS E CE  1 
ATOM   10000 N NZ  . LYS E  1 311 ? -38.346 -58.948  -39.913 1.00 32.92  ? 311 LYS E NZ  1 
ATOM   10001 N N   . TYR E  1 312 ? -35.107 -64.898  -40.097 1.00 37.84  ? 312 TYR E N   1 
ATOM   10002 C CA  . TYR E  1 312 ? -34.048 -65.892  -40.180 1.00 42.04  ? 312 TYR E CA  1 
ATOM   10003 C C   . TYR E  1 312 ? -33.341 -66.045  -38.840 1.00 46.46  ? 312 TYR E C   1 
ATOM   10004 O O   . TYR E  1 312 ? -32.868 -65.069  -38.258 1.00 49.26  ? 312 TYR E O   1 
ATOM   10005 C CB  . TYR E  1 312 ? -33.036 -65.543  -41.271 1.00 34.08  ? 312 TYR E CB  1 
ATOM   10006 C CG  . TYR E  1 312 ? -31.925 -66.560  -41.362 1.00 40.64  ? 312 TYR E CG  1 
ATOM   10007 C CD1 . TYR E  1 312 ? -32.193 -67.869  -41.737 1.00 40.74  ? 312 TYR E CD1 1 
ATOM   10008 C CD2 . TYR E  1 312 ? -30.614 -66.221  -41.056 1.00 44.29  ? 312 TYR E CD2 1 
ATOM   10009 C CE1 . TYR E  1 312 ? -31.190 -68.809  -41.813 1.00 38.05  ? 312 TYR E CE1 1 
ATOM   10010 C CE2 . TYR E  1 312 ? -29.601 -67.156  -41.131 1.00 41.01  ? 312 TYR E CE2 1 
ATOM   10011 C CZ  . TYR E  1 312 ? -29.896 -68.449  -41.510 1.00 41.21  ? 312 TYR E CZ  1 
ATOM   10012 O OH  . TYR E  1 312 ? -28.896 -69.390  -41.587 1.00 57.13  ? 312 TYR E OH  1 
ATOM   10013 N N   . VAL E  1 313 ? -33.281 -67.281  -38.358 1.00 48.65  ? 313 VAL E N   1 
ATOM   10014 C CA  . VAL E  1 313 ? -32.658 -67.584  -37.079 1.00 44.05  ? 313 VAL E CA  1 
ATOM   10015 C C   . VAL E  1 313 ? -31.680 -68.745  -37.231 1.00 43.21  ? 313 VAL E C   1 
ATOM   10016 O O   . VAL E  1 313 ? -31.892 -69.644  -38.045 1.00 50.04  ? 313 VAL E O   1 
ATOM   10017 C CB  . VAL E  1 313 ? -33.715 -67.929  -36.011 1.00 44.85  ? 313 VAL E CB  1 
ATOM   10018 C CG1 . VAL E  1 313 ? -33.047 -68.339  -34.714 1.00 62.04  ? 313 VAL E CG1 1 
ATOM   10019 C CG2 . VAL E  1 313 ? -34.639 -66.746  -35.780 1.00 42.59  ? 313 VAL E CG2 1 
ATOM   10020 N N   . LYS E  1 314 ? -30.609 -68.716  -36.446 1.00 47.83  ? 314 LYS E N   1 
ATOM   10021 C CA  . LYS E  1 314 ? -29.564 -69.729  -36.522 1.00 50.82  ? 314 LYS E CA  1 
ATOM   10022 C C   . LYS E  1 314 ? -29.917 -70.945  -35.672 1.00 46.92  ? 314 LYS E C   1 
ATOM   10023 O O   . LYS E  1 314 ? -29.141 -71.896  -35.574 1.00 63.73  ? 314 LYS E O   1 
ATOM   10024 C CB  . LYS E  1 314 ? -28.236 -69.134  -36.058 1.00 47.19  ? 314 LYS E CB  1 
ATOM   10025 C CG  . LYS E  1 314 ? -27.000 -69.863  -36.549 1.00 72.31  ? 314 LYS E CG  1 
ATOM   10026 C CD  . LYS E  1 314 ? -25.753 -69.113  -36.121 1.00 97.22  ? 314 LYS E CD  1 
ATOM   10027 C CE  . LYS E  1 314 ? -25.850 -67.647  -36.515 1.00 96.46  ? 314 LYS E CE  1 
ATOM   10028 N NZ  . LYS E  1 314 ? -24.885 -66.794  -35.770 1.00 83.63  ? 314 LYS E NZ  1 
ATOM   10029 N N   . SER E  1 315 ? -31.097 -70.908  -35.062 1.00 54.48  ? 315 SER E N   1 
ATOM   10030 C CA  . SER E  1 315 ? -31.547 -71.988  -34.193 1.00 59.74  ? 315 SER E CA  1 
ATOM   10031 C C   . SER E  1 315 ? -31.740 -73.296  -34.950 1.00 51.03  ? 315 SER E C   1 
ATOM   10032 O O   . SER E  1 315 ? -32.051 -73.300  -36.141 1.00 47.27  ? 315 SER E O   1 
ATOM   10033 C CB  . SER E  1 315 ? -32.849 -71.602  -33.487 1.00 52.89  ? 315 SER E CB  1 
ATOM   10034 O OG  . SER E  1 315 ? -32.658 -70.483  -32.640 1.00 67.36  ? 315 SER E OG  1 
ATOM   10035 N N   . THR E  1 316 ? -31.546 -74.404  -34.244 1.00 55.40  ? 316 THR E N   1 
ATOM   10036 C CA  . THR E  1 316 ? -31.818 -75.726  -34.787 1.00 57.72  ? 316 THR E CA  1 
ATOM   10037 C C   . THR E  1 316 ? -33.229 -76.145  -34.396 1.00 59.56  ? 316 THR E C   1 
ATOM   10038 O O   . THR E  1 316 ? -33.924 -76.817  -35.157 1.00 67.15  ? 316 THR E O   1 
ATOM   10039 C CB  . THR E  1 316 ? -30.817 -76.765  -34.257 1.00 69.27  ? 316 THR E CB  1 
ATOM   10040 O OG1 . THR E  1 316 ? -31.316 -78.085  -34.506 1.00 91.58  ? 316 THR E OG1 1 
ATOM   10041 C CG2 . THR E  1 316 ? -30.613 -76.587  -32.760 1.00 76.14  ? 316 THR E CG2 1 
ATOM   10042 N N   . LYS E  1 317 ? -33.644 -75.740  -33.200 1.00 63.78  ? 317 LYS E N   1 
ATOM   10043 C CA  . LYS E  1 317 ? -34.988 -76.026  -32.717 1.00 60.30  ? 317 LYS E CA  1 
ATOM   10044 C C   . LYS E  1 317 ? -35.506 -74.940  -31.781 1.00 59.52  ? 317 LYS E C   1 
ATOM   10045 O O   . LYS E  1 317 ? -34.751 -74.354  -31.002 1.00 75.69  ? 317 LYS E O   1 
ATOM   10046 C CB  . LYS E  1 317 ? -35.050 -77.392  -32.026 1.00 70.97  ? 317 LYS E CB  1 
ATOM   10047 C CG  . LYS E  1 317 ? -34.026 -77.592  -30.919 1.00 77.73  ? 317 LYS E CG  1 
ATOM   10048 C CD  . LYS E  1 317 ? -34.230 -78.928  -30.214 1.00 103.24 ? 317 LYS E CD  1 
ATOM   10049 C CE  . LYS E  1 317 ? -35.557 -78.968  -29.469 1.00 98.44  ? 317 LYS E CE  1 
ATOM   10050 N NZ  . LYS E  1 317 ? -35.728 -80.236  -28.707 1.00 74.48  ? 317 LYS E NZ  1 
ATOM   10051 N N   . LEU E  1 318 ? -36.807 -74.686  -31.873 1.00 56.38  ? 318 LEU E N   1 
ATOM   10052 C CA  . LEU E  1 318 ? -37.483 -73.702  -31.040 1.00 53.63  ? 318 LEU E CA  1 
ATOM   10053 C C   . LEU E  1 318 ? -38.813 -74.270  -30.556 1.00 53.21  ? 318 LEU E C   1 
ATOM   10054 O O   . LEU E  1 318 ? -39.867 -73.662  -30.752 1.00 54.17  ? 318 LEU E O   1 
ATOM   10055 C CB  . LEU E  1 318 ? -37.729 -72.416  -31.829 1.00 50.71  ? 318 LEU E CB  1 
ATOM   10056 C CG  . LEU E  1 318 ? -36.528 -71.518  -32.131 1.00 53.22  ? 318 LEU E CG  1 
ATOM   10057 C CD1 . LEU E  1 318 ? -36.950 -70.370  -33.034 1.00 52.97  ? 318 LEU E CD1 1 
ATOM   10058 C CD2 . LEU E  1 318 ? -35.921 -70.996  -30.839 1.00 41.53  ? 318 LEU E CD2 1 
ATOM   10059 N N   . ARG E  1 319 ? -38.753 -75.442  -29.929 1.00 57.02  ? 319 ARG E N   1 
ATOM   10060 C CA  . ARG E  1 319 ? -39.950 -76.154  -29.488 1.00 58.76  ? 319 ARG E CA  1 
ATOM   10061 C C   . ARG E  1 319 ? -40.583 -75.502  -28.261 1.00 47.93  ? 319 ARG E C   1 
ATOM   10062 O O   . ARG E  1 319 ? -39.947 -75.377  -27.216 1.00 48.18  ? 319 ARG E O   1 
ATOM   10063 C CB  . ARG E  1 319 ? -39.628 -77.630  -29.219 1.00 69.49  ? 319 ARG E CB  1 
ATOM   10064 C CG  . ARG E  1 319 ? -40.835 -78.474  -28.825 1.00 67.75  ? 319 ARG E CG  1 
ATOM   10065 C CD  . ARG E  1 319 ? -40.715 -79.931  -29.287 1.00 69.58  ? 319 ARG E CD  1 
ATOM   10066 N NE  . ARG E  1 319 ? -41.171 -80.127  -30.664 1.00 78.96  ? 319 ARG E NE  1 
ATOM   10067 C CZ  . ARG E  1 319 ? -42.441 -80.321  -31.017 1.00 83.62  ? 319 ARG E CZ  1 
ATOM   10068 N NH1 . ARG E  1 319 ? -43.398 -80.337  -30.100 1.00 82.67  ? 319 ARG E NH1 1 
ATOM   10069 N NH2 . ARG E  1 319 ? -42.757 -80.492  -32.295 1.00 86.41  ? 319 ARG E NH2 1 
ATOM   10070 N N   . LEU E  1 320 ? -41.840 -75.090  -28.402 1.00 48.67  ? 320 LEU E N   1 
ATOM   10071 C CA  . LEU E  1 320 ? -42.547 -74.360  -27.355 1.00 44.70  ? 320 LEU E CA  1 
ATOM   10072 C C   . LEU E  1 320 ? -43.507 -75.272  -26.591 1.00 56.39  ? 320 LEU E C   1 
ATOM   10073 O O   . LEU E  1 320 ? -44.418 -75.859  -27.175 1.00 61.85  ? 320 LEU E O   1 
ATOM   10074 C CB  . LEU E  1 320 ? -43.318 -73.192  -27.976 1.00 46.00  ? 320 LEU E CB  1 
ATOM   10075 C CG  . LEU E  1 320 ? -43.957 -72.149  -27.060 1.00 51.65  ? 320 LEU E CG  1 
ATOM   10076 C CD1 . LEU E  1 320 ? -42.895 -71.287  -26.394 1.00 46.96  ? 320 LEU E CD1 1 
ATOM   10077 C CD2 . LEU E  1 320 ? -44.918 -71.286  -27.858 1.00 36.87  ? 320 LEU E CD2 1 
ATOM   10078 N N   . ALA E  1 321 ? -43.303 -75.381  -25.281 1.00 62.42  ? 321 ALA E N   1 
ATOM   10079 C CA  . ALA E  1 321 ? -44.140 -76.228  -24.436 1.00 55.78  ? 321 ALA E CA  1 
ATOM   10080 C C   . ALA E  1 321 ? -45.571 -75.706  -24.347 1.00 56.07  ? 321 ALA E C   1 
ATOM   10081 O O   . ALA E  1 321 ? -45.800 -74.539  -24.032 1.00 57.45  ? 321 ALA E O   1 
ATOM   10082 C CB  . ALA E  1 321 ? -43.534 -76.353  -23.047 1.00 46.75  ? 321 ALA E CB  1 
ATOM   10083 N N   . THR E  1 322 ? -46.529 -76.583  -24.625 1.00 48.11  ? 322 THR E N   1 
ATOM   10084 C CA  . THR E  1 322 ? -47.940 -76.229  -24.543 1.00 57.62  ? 322 THR E CA  1 
ATOM   10085 C C   . THR E  1 322 ? -48.603 -77.017  -23.424 1.00 59.66  ? 322 THR E C   1 
ATOM   10086 O O   . THR E  1 322 ? -49.471 -76.507  -22.714 1.00 59.11  ? 322 THR E O   1 
ATOM   10087 C CB  . THR E  1 322 ? -48.671 -76.523  -25.864 1.00 57.55  ? 322 THR E CB  1 
ATOM   10088 O OG1 . THR E  1 322 ? -48.549 -77.916  -26.181 1.00 67.86  ? 322 THR E OG1 1 
ATOM   10089 C CG2 . THR E  1 322 ? -48.081 -75.697  -26.993 1.00 62.33  ? 322 THR E CG2 1 
ATOM   10090 N N   . GLY E  1 323 ? -48.185 -78.268  -23.275 1.00 62.55  ? 323 GLY E N   1 
ATOM   10091 C CA  . GLY E  1 323 ? -48.692 -79.117  -22.216 1.00 63.00  ? 323 GLY E CA  1 
ATOM   10092 C C   . GLY E  1 323 ? -47.893 -78.971  -20.936 1.00 63.55  ? 323 GLY E C   1 
ATOM   10093 O O   . GLY E  1 323 ? -47.254 -77.943  -20.702 1.00 66.14  ? 323 GLY E O   1 
ATOM   10094 N N   . LEU E  1 324 ? -47.905 -80.019  -20.119 1.00 68.30  ? 324 LEU E N   1 
ATOM   10095 C CA  . LEU E  1 324 ? -47.223 -80.006  -18.829 1.00 68.53  ? 324 LEU E CA  1 
ATOM   10096 C C   . LEU E  1 324 ? -46.148 -81.082  -18.737 1.00 67.39  ? 324 LEU E C   1 
ATOM   10097 O O   . LEU E  1 324 ? -46.051 -81.952  -19.601 1.00 73.54  ? 324 LEU E O   1 
ATOM   10098 C CB  . LEU E  1 324 ? -48.233 -80.194  -17.698 1.00 65.64  ? 324 LEU E CB  1 
ATOM   10099 C CG  . LEU E  1 324 ? -49.261 -81.308  -17.912 1.00 63.45  ? 324 LEU E CG  1 
ATOM   10100 C CD1 . LEU E  1 324 ? -49.748 -81.872  -16.597 1.00 72.23  ? 324 LEU E CD1 1 
ATOM   10101 C CD2 . LEU E  1 324 ? -50.432 -80.813  -18.735 1.00 54.84  ? 324 LEU E CD2 1 
ATOM   10102 N N   . ARG E  1 325 ? -45.341 -81.012  -17.683 1.00 71.36  ? 325 ARG E N   1 
ATOM   10103 C CA  . ARG E  1 325 ? -44.302 -82.002  -17.437 1.00 66.69  ? 325 ARG E CA  1 
ATOM   10104 C C   . ARG E  1 325 ? -44.906 -83.401  -17.486 1.00 76.42  ? 325 ARG E C   1 
ATOM   10105 O O   . ARG E  1 325 ? -46.057 -83.607  -17.101 1.00 75.71  ? 325 ARG E O   1 
ATOM   10106 C CB  . ARG E  1 325 ? -43.629 -81.750  -16.085 1.00 58.36  ? 325 ARG E CB  1 
ATOM   10107 C CG  . ARG E  1 325 ? -42.243 -82.370  -15.941 1.00 68.99  ? 325 ARG E CG  1 
ATOM   10108 C CD  . ARG E  1 325 ? -41.697 -82.215  -14.520 1.00 87.79  ? 325 ARG E CD  1 
ATOM   10109 N NE  . ARG E  1 325 ? -41.357 -80.833  -14.181 1.00 93.79  ? 325 ARG E NE  1 
ATOM   10110 C CZ  . ARG E  1 325 ? -40.142 -80.306  -14.304 1.00 99.53  ? 325 ARG E CZ  1 
ATOM   10111 N NH1 . ARG E  1 325 ? -39.140 -81.042  -14.764 1.00 85.33  ? 325 ARG E NH1 1 
ATOM   10112 N NH2 . ARG E  1 325 ? -39.926 -79.041  -13.967 1.00 97.87  ? 325 ARG E NH2 1 
ATOM   10113 N N   . ASN E  1 326 ? -44.128 -84.363  -17.962 1.00 85.57  ? 326 ASN E N   1 
ATOM   10114 C CA  . ASN E  1 326 ? -44.661 -85.689  -18.222 1.00 93.04  ? 326 ASN E CA  1 
ATOM   10115 C C   . ASN E  1 326 ? -44.067 -86.749  -17.306 1.00 93.46  ? 326 ASN E C   1 
ATOM   10116 O O   . ASN E  1 326 ? -42.858 -86.787  -17.091 1.00 93.65  ? 326 ASN E O   1 
ATOM   10117 C CB  . ASN E  1 326 ? -44.420 -86.060  -19.681 1.00 101.85 ? 326 ASN E CB  1 
ATOM   10118 C CG  . ASN E  1 326 ? -45.223 -87.261  -20.113 1.00 103.33 ? 326 ASN E CG  1 
ATOM   10119 O OD1 . ASN E  1 326 ? -46.360 -87.451  -19.681 1.00 109.47 ? 326 ASN E OD1 1 
ATOM   10120 N ND2 . ASN E  1 326 ? -44.639 -88.078  -20.978 1.00 99.72  ? 326 ASN E ND2 1 
ATOM   10121 N N   . ILE E  1 327 ? -44.922 -87.614  -16.772 1.00 99.44  ? 327 ILE E N   1 
ATOM   10122 C CA  . ILE E  1 327 ? -44.470 -88.644  -15.849 1.00 98.15  ? 327 ILE E CA  1 
ATOM   10123 C C   . ILE E  1 327 ? -45.049 -90.009  -16.206 1.00 91.19  ? 327 ILE E C   1 
ATOM   10124 O O   . ILE E  1 327 ? -45.973 -90.110  -17.014 1.00 82.94  ? 327 ILE E O   1 
ATOM   10125 C CB  . ILE E  1 327 ? -44.844 -88.295  -14.398 1.00 87.29  ? 327 ILE E CB  1 
ATOM   10126 C CG1 . ILE E  1 327 ? -44.406 -86.868  -14.060 1.00 77.34  ? 327 ILE E CG1 1 
ATOM   10127 C CG2 . ILE E  1 327 ? -44.206 -89.279  -13.435 1.00 92.70  ? 327 ILE E CG2 1 
ATOM   10128 C CD1 . ILE E  1 327 ? -42.905 -86.701  -13.947 1.00 71.35  ? 327 ILE E CD1 1 
ATOM   10129 N N   . LEU F  2 2   ? -42.914 -75.089  -9.011  1.00 67.81  ? 2   LEU F N   1 
ATOM   10130 C CA  . LEU F  2 2   ? -43.017 -73.824  -8.290  1.00 73.97  ? 2   LEU F CA  1 
ATOM   10131 C C   . LEU F  2 2   ? -44.069 -73.890  -7.193  1.00 68.20  ? 2   LEU F C   1 
ATOM   10132 O O   . LEU F  2 2   ? -43.926 -73.263  -6.144  1.00 64.22  ? 2   LEU F O   1 
ATOM   10133 C CB  . LEU F  2 2   ? -43.358 -72.677  -9.242  1.00 65.21  ? 2   LEU F CB  1 
ATOM   10134 C CG  . LEU F  2 2   ? -42.323 -71.555  -9.371  1.00 56.57  ? 2   LEU F CG  1 
ATOM   10135 C CD1 . LEU F  2 2   ? -43.015 -70.211  -9.500  1.00 34.14  ? 2   LEU F CD1 1 
ATOM   10136 C CD2 . LEU F  2 2   ? -41.298 -71.573  -8.244  1.00 68.78  ? 2   LEU F CD2 1 
ATOM   10137 N N   . PHE F  2 3   ? -45.124 -74.660  -7.443  1.00 63.43  ? 3   PHE F N   1 
ATOM   10138 C CA  . PHE F  2 3   ? -46.233 -74.783  -6.504  1.00 72.40  ? 3   PHE F CA  1 
ATOM   10139 C C   . PHE F  2 3   ? -46.202 -76.090  -5.709  1.00 78.34  ? 3   PHE F C   1 
ATOM   10140 O O   . PHE F  2 3   ? -47.104 -76.366  -4.919  1.00 83.50  ? 3   PHE F O   1 
ATOM   10141 C CB  . PHE F  2 3   ? -47.569 -74.624  -7.235  1.00 75.12  ? 3   PHE F CB  1 
ATOM   10142 C CG  . PHE F  2 3   ? -47.802 -73.238  -7.768  1.00 73.20  ? 3   PHE F CG  1 
ATOM   10143 C CD1 . PHE F  2 3   ? -47.328 -72.871  -9.018  1.00 68.02  ? 3   PHE F CD1 1 
ATOM   10144 C CD2 . PHE F  2 3   ? -48.487 -72.301  -7.015  1.00 73.52  ? 3   PHE F CD2 1 
ATOM   10145 C CE1 . PHE F  2 3   ? -47.539 -71.594  -9.506  1.00 66.58  ? 3   PHE F CE1 1 
ATOM   10146 C CE2 . PHE F  2 3   ? -48.701 -71.025  -7.497  1.00 66.06  ? 3   PHE F CE2 1 
ATOM   10147 C CZ  . PHE F  2 3   ? -48.227 -70.671  -8.744  1.00 66.71  ? 3   PHE F CZ  1 
ATOM   10148 N N   . GLY F  2 4   ? -45.159 -76.888  -5.923  1.00 75.13  ? 4   GLY F N   1 
ATOM   10149 C CA  . GLY F  2 4   ? -44.931 -78.089  -5.137  1.00 71.11  ? 4   GLY F CA  1 
ATOM   10150 C C   . GLY F  2 4   ? -45.869 -79.247  -5.424  1.00 78.68  ? 4   GLY F C   1 
ATOM   10151 O O   . GLY F  2 4   ? -45.766 -80.305  -4.802  1.00 82.12  ? 4   GLY F O   1 
ATOM   10152 N N   . ALA F  2 5   ? -46.785 -79.055  -6.367  1.00 75.31  ? 5   ALA F N   1 
ATOM   10153 C CA  . ALA F  2 5   ? -47.755 -80.092  -6.701  1.00 66.67  ? 5   ALA F CA  1 
ATOM   10154 C C   . ALA F  2 5   ? -47.174 -81.130  -7.657  1.00 73.81  ? 5   ALA F C   1 
ATOM   10155 O O   . ALA F  2 5   ? -46.899 -82.264  -7.262  1.00 67.59  ? 5   ALA F O   1 
ATOM   10156 C CB  . ALA F  2 5   ? -49.016 -79.473  -7.287  1.00 69.67  ? 5   ALA F CB  1 
ATOM   10157 N N   . ILE F  2 6   ? -46.990 -80.738  -8.914  1.00 78.57  ? 6   ILE F N   1 
ATOM   10158 C CA  . ILE F  2 6   ? -46.463 -81.644  -9.929  1.00 62.17  ? 6   ILE F CA  1 
ATOM   10159 C C   . ILE F  2 6   ? -45.002 -81.983  -9.662  1.00 75.10  ? 6   ILE F C   1 
ATOM   10160 O O   . ILE F  2 6   ? -44.164 -81.093  -9.516  1.00 79.69  ? 6   ILE F O   1 
ATOM   10161 C CB  . ILE F  2 6   ? -46.613 -81.061  -11.346 1.00 53.63  ? 6   ILE F CB  1 
ATOM   10162 C CG1 . ILE F  2 6   ? -48.086 -80.780  -11.645 1.00 54.37  ? 6   ILE F CG1 1 
ATOM   10163 C CG2 . ILE F  2 6   ? -46.028 -82.013  -12.378 1.00 46.75  ? 6   ILE F CG2 1 
ATOM   10164 C CD1 . ILE F  2 6   ? -48.359 -80.397  -13.082 1.00 58.79  ? 6   ILE F CD1 1 
ATOM   10165 N N   . ALA F  2 7   ? -44.707 -83.277  -9.598  1.00 64.57  ? 7   ALA F N   1 
ATOM   10166 C CA  . ALA F  2 7   ? -43.373 -83.751  -9.247  1.00 65.42  ? 7   ALA F CA  1 
ATOM   10167 C C   . ALA F  2 7   ? -43.008 -83.323  -7.825  1.00 77.64  ? 7   ALA F C   1 
ATOM   10168 O O   . ALA F  2 7   ? -41.831 -83.202  -7.481  1.00 74.29  ? 7   ALA F O   1 
ATOM   10169 C CB  . ALA F  2 7   ? -42.341 -83.255  -10.252 1.00 73.84  ? 7   ALA F CB  1 
ATOM   10170 N N   . GLY F  2 8   ? -44.034 -83.103  -7.006  1.00 81.27  ? 8   GLY F N   1 
ATOM   10171 C CA  . GLY F  2 8   ? -43.856 -82.728  -5.613  1.00 79.84  ? 8   GLY F CA  1 
ATOM   10172 C C   . GLY F  2 8   ? -44.576 -83.669  -4.663  1.00 89.87  ? 8   GLY F C   1 
ATOM   10173 O O   . GLY F  2 8   ? -44.213 -84.839  -4.552  1.00 86.31  ? 8   GLY F O   1 
ATOM   10174 N N   . PHE F  2 9   ? -45.604 -83.165  -3.983  1.00 76.54  ? 9   PHE F N   1 
ATOM   10175 C CA  . PHE F  2 9   ? -46.394 -83.991  -3.071  1.00 69.00  ? 9   PHE F CA  1 
ATOM   10176 C C   . PHE F  2 9   ? -47.357 -84.929  -3.813  1.00 82.30  ? 9   PHE F C   1 
ATOM   10177 O O   . PHE F  2 9   ? -48.047 -85.748  -3.193  1.00 102.53 ? 9   PHE F O   1 
ATOM   10178 C CB  . PHE F  2 9   ? -47.111 -83.133  -2.016  1.00 84.46  ? 9   PHE F CB  1 
ATOM   10179 C CG  . PHE F  2 9   ? -48.285 -82.343  -2.540  1.00 77.26  ? 9   PHE F CG  1 
ATOM   10180 C CD1 . PHE F  2 9   ? -49.344 -82.970  -3.177  1.00 80.75  ? 9   PHE F CD1 1 
ATOM   10181 C CD2 . PHE F  2 9   ? -48.350 -80.974  -2.343  1.00 89.10  ? 9   PHE F CD2 1 
ATOM   10182 C CE1 . PHE F  2 9   ? -50.425 -82.245  -3.636  1.00 80.65  ? 9   PHE F CE1 1 
ATOM   10183 C CE2 . PHE F  2 9   ? -49.431 -80.245  -2.796  1.00 93.15  ? 9   PHE F CE2 1 
ATOM   10184 C CZ  . PHE F  2 9   ? -50.471 -80.883  -3.442  1.00 91.50  ? 9   PHE F CZ  1 
ATOM   10185 N N   . ILE F  2 10  ? -47.392 -84.794  -5.139  1.00 74.09  ? 10  ILE F N   1 
ATOM   10186 C CA  . ILE F  2 10  ? -48.030 -85.775  -6.013  1.00 71.74  ? 10  ILE F CA  1 
ATOM   10187 C C   . ILE F  2 10  ? -46.970 -86.280  -6.987  1.00 72.22  ? 10  ILE F C   1 
ATOM   10188 O O   . ILE F  2 10  ? -46.801 -85.721  -8.066  1.00 81.94  ? 10  ILE F O   1 
ATOM   10189 C CB  . ILE F  2 10  ? -49.204 -85.175  -6.826  1.00 64.92  ? 10  ILE F CB  1 
ATOM   10190 C CG1 . ILE F  2 10  ? -50.017 -84.199  -5.975  1.00 68.33  ? 10  ILE F CG1 1 
ATOM   10191 C CG2 . ILE F  2 10  ? -50.091 -86.287  -7.397  1.00 61.10  ? 10  ILE F CG2 1 
ATOM   10192 C CD1 . ILE F  2 10  ? -51.384 -83.871  -6.541  1.00 61.68  ? 10  ILE F CD1 1 
ATOM   10193 N N   . GLU F  2 11  ? -46.268 -87.344  -6.612  1.00 86.28  ? 11  GLU F N   1 
ATOM   10194 C CA  . GLU F  2 11  ? -45.050 -87.752  -7.311  1.00 93.33  ? 11  GLU F CA  1 
ATOM   10195 C C   . GLU F  2 11  ? -45.216 -88.069  -8.799  1.00 87.58  ? 11  GLU F C   1 
ATOM   10196 O O   . GLU F  2 11  ? -44.323 -87.785  -9.600  1.00 92.74  ? 11  GLU F O   1 
ATOM   10197 C CB  . GLU F  2 11  ? -44.410 -88.933  -6.582  1.00 108.80 ? 11  GLU F CB  1 
ATOM   10198 C CG  . GLU F  2 11  ? -44.277 -88.693  -5.087  1.00 125.35 ? 11  GLU F CG  1 
ATOM   10199 C CD  . GLU F  2 11  ? -43.828 -89.921  -4.331  1.00 158.31 ? 11  GLU F CD  1 
ATOM   10200 O OE1 . GLU F  2 11  ? -43.653 -89.826  -3.098  1.00 163.40 ? 11  GLU F OE1 1 
ATOM   10201 O OE2 . GLU F  2 11  ? -43.651 -90.982  -4.966  1.00 154.78 ? 11  GLU F OE2 1 
ATOM   10202 N N   . GLY F  2 12  ? -46.353 -88.648  -9.173  1.00 79.09  ? 12  GLY F N   1 
ATOM   10203 C CA  . GLY F  2 12  ? -46.531 -89.117  -10.535 1.00 73.22  ? 12  GLY F CA  1 
ATOM   10204 C C   . GLY F  2 12  ? -47.798 -88.691  -11.252 1.00 78.45  ? 12  GLY F C   1 
ATOM   10205 O O   . GLY F  2 12  ? -48.736 -88.169  -10.647 1.00 82.68  ? 12  GLY F O   1 
ATOM   10206 N N   . GLY F  2 13  ? -47.815 -88.923  -12.561 1.00 71.98  ? 13  GLY F N   1 
ATOM   10207 C CA  . GLY F  2 13  ? -48.976 -88.643  -13.384 1.00 73.55  ? 13  GLY F CA  1 
ATOM   10208 C C   . GLY F  2 13  ? -49.755 -89.909  -13.685 1.00 75.02  ? 13  GLY F C   1 
ATOM   10209 O O   . GLY F  2 13  ? -49.314 -91.011  -13.359 1.00 75.95  ? 13  GLY F O   1 
ATOM   10210 N N   . TRP F  2 14  ? -50.918 -89.752  -14.311 1.00 70.64  ? 14  TRP F N   1 
ATOM   10211 C CA  . TRP F  2 14  ? -51.778 -90.891  -14.609 1.00 73.42  ? 14  TRP F CA  1 
ATOM   10212 C C   . TRP F  2 14  ? -51.954 -91.115  -16.106 1.00 83.96  ? 14  TRP F C   1 
ATOM   10213 O O   . TRP F  2 14  ? -52.684 -90.380  -16.770 1.00 87.90  ? 14  TRP F O   1 
ATOM   10214 C CB  . TRP F  2 14  ? -53.151 -90.717  -13.957 1.00 79.09  ? 14  TRP F CB  1 
ATOM   10215 C CG  . TRP F  2 14  ? -53.108 -90.622  -12.466 1.00 85.47  ? 14  TRP F CG  1 
ATOM   10216 C CD1 . TRP F  2 14  ? -52.167 -91.160  -11.637 1.00 77.73  ? 14  TRP F CD1 1 
ATOM   10217 C CD2 . TRP F  2 14  ? -54.058 -89.963  -11.621 1.00 76.43  ? 14  TRP F CD2 1 
ATOM   10218 N NE1 . TRP F  2 14  ? -52.466 -90.868  -10.329 1.00 63.62  ? 14  TRP F NE1 1 
ATOM   10219 C CE2 . TRP F  2 14  ? -53.623 -90.134  -10.291 1.00 76.15  ? 14  TRP F CE2 1 
ATOM   10220 C CE3 . TRP F  2 14  ? -55.230 -89.238  -11.859 1.00 69.93  ? 14  TRP F CE3 1 
ATOM   10221 C CZ2 . TRP F  2 14  ? -54.319 -89.609  -9.205  1.00 79.75  ? 14  TRP F CZ2 1 
ATOM   10222 C CZ3 . TRP F  2 14  ? -55.920 -88.718  -10.779 1.00 83.99  ? 14  TRP F CZ3 1 
ATOM   10223 C CH2 . TRP F  2 14  ? -55.462 -88.906  -9.468  1.00 87.60  ? 14  TRP F CH2 1 
ATOM   10224 N N   . THR F  2 15  ? -51.286 -92.137  -16.630 1.00 91.03  ? 15  THR F N   1 
ATOM   10225 C CA  . THR F  2 15  ? -51.485 -92.542  -18.014 1.00 96.33  ? 15  THR F CA  1 
ATOM   10226 C C   . THR F  2 15  ? -52.946 -92.926  -18.214 1.00 102.41 ? 15  THR F C   1 
ATOM   10227 O O   . THR F  2 15  ? -53.486 -92.822  -19.315 1.00 102.43 ? 15  THR F O   1 
ATOM   10228 C CB  . THR F  2 15  ? -50.601 -93.747  -18.379 1.00 94.79  ? 15  THR F CB  1 
ATOM   10229 O OG1 . THR F  2 15  ? -50.979 -94.877  -17.583 1.00 108.94 ? 15  THR F OG1 1 
ATOM   10230 C CG2 . THR F  2 15  ? -49.134 -93.428  -18.133 1.00 88.38  ? 15  THR F CG2 1 
ATOM   10231 N N   . GLY F  2 16  ? -53.580 -93.362  -17.130 1.00 92.67  ? 16  GLY F N   1 
ATOM   10232 C CA  . GLY F  2 16  ? -54.958 -93.817  -17.168 1.00 96.06  ? 16  GLY F CA  1 
ATOM   10233 C C   . GLY F  2 16  ? -55.962 -92.739  -17.525 1.00 98.57  ? 16  GLY F C   1 
ATOM   10234 O O   . GLY F  2 16  ? -56.925 -92.998  -18.246 1.00 101.76 ? 16  GLY F O   1 
ATOM   10235 N N   . MET F  2 17  ? -55.746 -91.529  -17.018 1.00 98.60  ? 17  MET F N   1 
ATOM   10236 C CA  . MET F  2 17  ? -56.648 -90.416  -17.298 1.00 94.44  ? 17  MET F CA  1 
ATOM   10237 C C   . MET F  2 17  ? -56.308 -89.766  -18.635 1.00 102.29 ? 17  MET F C   1 
ATOM   10238 O O   . MET F  2 17  ? -55.278 -89.107  -18.772 1.00 107.35 ? 17  MET F O   1 
ATOM   10239 C CB  . MET F  2 17  ? -56.595 -89.381  -16.173 1.00 75.30  ? 17  MET F CB  1 
ATOM   10240 C CG  . MET F  2 17  ? -57.546 -88.213  -16.364 1.00 89.65  ? 17  MET F CG  1 
ATOM   10241 S SD  . MET F  2 17  ? -57.509 -87.058  -14.981 1.00 102.05 ? 17  MET F SD  1 
ATOM   10242 C CE  . MET F  2 17  ? -55.766 -86.652  -14.925 1.00 90.85  ? 17  MET F CE  1 
ATOM   10243 N N   . VAL F  2 18  ? -57.185 -89.952  -19.617 1.00 105.68 ? 18  VAL F N   1 
ATOM   10244 C CA  . VAL F  2 18  ? -56.936 -89.473  -20.972 1.00 113.28 ? 18  VAL F CA  1 
ATOM   10245 C C   . VAL F  2 18  ? -58.010 -88.494  -21.439 1.00 110.80 ? 18  VAL F C   1 
ATOM   10246 O O   . VAL F  2 18  ? -58.120 -88.202  -22.630 1.00 111.09 ? 18  VAL F O   1 
ATOM   10247 C CB  . VAL F  2 18  ? -56.871 -90.644  -21.969 1.00 116.73 ? 18  VAL F CB  1 
ATOM   10248 C CG1 . VAL F  2 18  ? -55.767 -91.613  -21.576 1.00 102.55 ? 18  VAL F CG1 1 
ATOM   10249 C CG2 . VAL F  2 18  ? -58.212 -91.358  -22.031 1.00 112.86 ? 18  VAL F CG2 1 
ATOM   10250 N N   . ASP F  2 19  ? -58.797 -87.988  -20.496 1.00 114.63 ? 19  ASP F N   1 
ATOM   10251 C CA  . ASP F  2 19  ? -59.893 -87.083  -20.822 1.00 121.53 ? 19  ASP F CA  1 
ATOM   10252 C C   . ASP F  2 19  ? -59.449 -85.624  -20.766 1.00 115.84 ? 19  ASP F C   1 
ATOM   10253 O O   . ASP F  2 19  ? -59.956 -84.783  -21.509 1.00 113.18 ? 19  ASP F O   1 
ATOM   10254 C CB  . ASP F  2 19  ? -61.069 -87.310  -19.871 1.00 134.18 ? 19  ASP F CB  1 
ATOM   10255 C CG  . ASP F  2 19  ? -61.436 -88.775  -19.738 1.00 144.50 ? 19  ASP F CG  1 
ATOM   10256 O OD1 . ASP F  2 19  ? -61.183 -89.545  -20.688 1.00 147.91 ? 19  ASP F OD1 1 
ATOM   10257 O OD2 . ASP F  2 19  ? -61.978 -89.156  -18.679 1.00 139.92 ? 19  ASP F OD2 1 
ATOM   10258 N N   . GLY F  2 20  ? -58.503 -85.329  -19.880 1.00 106.01 ? 20  GLY F N   1 
ATOM   10259 C CA  . GLY F  2 20  ? -58.007 -83.975  -19.714 1.00 88.13  ? 20  GLY F CA  1 
ATOM   10260 C C   . GLY F  2 20  ? -56.635 -83.919  -19.070 1.00 83.86  ? 20  GLY F C   1 
ATOM   10261 O O   . GLY F  2 20  ? -55.974 -84.944  -18.909 1.00 76.03  ? 20  GLY F O   1 
ATOM   10262 N N   . TRP F  2 21  ? -56.207 -82.715  -18.699 1.00 72.37  ? 21  TRP F N   1 
ATOM   10263 C CA  . TRP F  2 21  ? -54.896 -82.521  -18.085 1.00 76.62  ? 21  TRP F CA  1 
ATOM   10264 C C   . TRP F  2 21  ? -54.916 -82.755  -16.577 1.00 72.76  ? 21  TRP F C   1 
ATOM   10265 O O   . TRP F  2 21  ? -53.975 -83.316  -16.017 1.00 65.55  ? 21  TRP F O   1 
ATOM   10266 C CB  . TRP F  2 21  ? -54.348 -81.125  -18.396 1.00 81.78  ? 21  TRP F CB  1 
ATOM   10267 C CG  . TRP F  2 21  ? -53.706 -81.023  -19.745 1.00 76.26  ? 21  TRP F CG  1 
ATOM   10268 C CD1 . TRP F  2 21  ? -53.128 -82.035  -20.454 1.00 66.56  ? 21  TRP F CD1 1 
ATOM   10269 C CD2 . TRP F  2 21  ? -53.557 -79.840  -20.541 1.00 68.03  ? 21  TRP F CD2 1 
ATOM   10270 N NE1 . TRP F  2 21  ? -52.638 -81.559  -21.645 1.00 67.28  ? 21  TRP F NE1 1 
ATOM   10271 C CE2 . TRP F  2 21  ? -52.887 -80.214  -21.723 1.00 63.01  ? 21  TRP F CE2 1 
ATOM   10272 C CE3 . TRP F  2 21  ? -53.928 -78.503  -20.371 1.00 61.81  ? 21  TRP F CE3 1 
ATOM   10273 C CZ2 . TRP F  2 21  ? -52.581 -79.300  -22.729 1.00 71.81  ? 21  TRP F CZ2 1 
ATOM   10274 C CZ3 . TRP F  2 21  ? -53.623 -77.596  -21.371 1.00 61.34  ? 21  TRP F CZ3 1 
ATOM   10275 C CH2 . TRP F  2 21  ? -52.957 -78.000  -22.535 1.00 68.99  ? 21  TRP F CH2 1 
ATOM   10276 N N   . TYR F  2 22  ? -55.985 -82.316  -15.923 1.00 78.01  ? 22  TYR F N   1 
ATOM   10277 C CA  . TYR F  2 22  ? -56.140 -82.525  -14.489 1.00 76.86  ? 22  TYR F CA  1 
ATOM   10278 C C   . TYR F  2 22  ? -57.475 -83.203  -14.210 1.00 84.68  ? 22  TYR F C   1 
ATOM   10279 O O   . TYR F  2 22  ? -58.456 -82.965  -14.912 1.00 91.84  ? 22  TYR F O   1 
ATOM   10280 C CB  . TYR F  2 22  ? -56.062 -81.196  -13.738 1.00 80.45  ? 22  TYR F CB  1 
ATOM   10281 C CG  . TYR F  2 22  ? -55.351 -80.100  -14.497 1.00 75.96  ? 22  TYR F CG  1 
ATOM   10282 C CD1 . TYR F  2 22  ? -56.066 -79.170  -15.239 1.00 71.72  ? 22  TYR F CD1 1 
ATOM   10283 C CD2 . TYR F  2 22  ? -53.966 -79.994  -14.474 1.00 70.68  ? 22  TYR F CD2 1 
ATOM   10284 C CE1 . TYR F  2 22  ? -55.426 -78.166  -15.935 1.00 68.81  ? 22  TYR F CE1 1 
ATOM   10285 C CE2 . TYR F  2 22  ? -53.316 -78.991  -15.168 1.00 66.32  ? 22  TYR F CE2 1 
ATOM   10286 C CZ  . TYR F  2 22  ? -54.052 -78.081  -15.897 1.00 69.32  ? 22  TYR F CZ  1 
ATOM   10287 O OH  . TYR F  2 22  ? -53.415 -77.079  -16.592 1.00 64.13  ? 22  TYR F OH  1 
ATOM   10288 N N   . GLY F  2 23  ? -57.512 -84.049  -13.185 1.00 108.99 ? 23  GLY F N   1 
ATOM   10289 C CA  . GLY F  2 23  ? -58.730 -84.760  -12.844 1.00 118.34 ? 23  GLY F CA  1 
ATOM   10290 C C   . GLY F  2 23  ? -58.646 -85.524  -11.538 1.00 122.97 ? 23  GLY F C   1 
ATOM   10291 O O   . GLY F  2 23  ? -57.740 -85.306  -10.734 1.00 109.42 ? 23  GLY F O   1 
ATOM   10292 N N   . TYR F  2 24  ? -59.596 -86.429  -11.329 1.00 98.66  ? 24  TYR F N   1 
ATOM   10293 C CA  . TYR F  2 24  ? -59.671 -87.180  -10.083 1.00 91.33  ? 24  TYR F CA  1 
ATOM   10294 C C   . TYR F  2 24  ? -59.637 -88.682  -10.325 1.00 99.02  ? 24  TYR F C   1 
ATOM   10295 O O   . TYR F  2 24  ? -59.744 -89.148  -11.459 1.00 93.70  ? 24  TYR F O   1 
ATOM   10296 C CB  . TYR F  2 24  ? -60.960 -86.840  -9.334  1.00 81.71  ? 24  TYR F CB  1 
ATOM   10297 C CG  . TYR F  2 24  ? -61.325 -85.376  -9.343  1.00 84.32  ? 24  TYR F CG  1 
ATOM   10298 C CD1 . TYR F  2 24  ? -62.009 -84.820  -10.416 1.00 83.69  ? 24  TYR F CD1 1 
ATOM   10299 C CD2 . TYR F  2 24  ? -61.001 -84.552  -8.274  1.00 84.94  ? 24  TYR F CD2 1 
ATOM   10300 C CE1 . TYR F  2 24  ? -62.352 -83.484  -10.429 1.00 84.59  ? 24  TYR F CE1 1 
ATOM   10301 C CE2 . TYR F  2 24  ? -61.340 -83.214  -8.278  1.00 84.72  ? 24  TYR F CE2 1 
ATOM   10302 C CZ  . TYR F  2 24  ? -62.016 -82.686  -9.358  1.00 90.17  ? 24  TYR F CZ  1 
ATOM   10303 O OH  . TYR F  2 24  ? -62.357 -81.353  -9.368  1.00 89.34  ? 24  TYR F OH  1 
ATOM   10304 N N   . HIS F  2 25  ? -59.492 -89.436  -9.243  1.00 100.91 ? 25  HIS F N   1 
ATOM   10305 C CA  . HIS F  2 25  ? -59.660 -90.880  -9.293  1.00 100.31 ? 25  HIS F CA  1 
ATOM   10306 C C   . HIS F  2 25  ? -60.374 -91.363  -8.043  1.00 109.48 ? 25  HIS F C   1 
ATOM   10307 O O   . HIS F  2 25  ? -59.754 -91.581  -7.004  1.00 106.51 ? 25  HIS F O   1 
ATOM   10308 C CB  . HIS F  2 25  ? -58.323 -91.599  -9.430  1.00 107.28 ? 25  HIS F CB  1 
ATOM   10309 C CG  . HIS F  2 25  ? -58.406 -93.067  -9.144  1.00 109.66 ? 25  HIS F CG  1 
ATOM   10310 N ND1 . HIS F  2 25  ? -58.005 -93.612  -7.945  1.00 100.93 ? 25  HIS F ND1 1 
ATOM   10311 C CD2 . HIS F  2 25  ? -58.865 -94.096  -9.892  1.00 104.97 ? 25  HIS F CD2 1 
ATOM   10312 C CE1 . HIS F  2 25  ? -58.201 -94.919  -7.970  1.00 103.81 ? 25  HIS F CE1 1 
ATOM   10313 N NE2 . HIS F  2 25  ? -58.722 -95.238  -9.143  1.00 107.58 ? 25  HIS F NE2 1 
ATOM   10314 N N   . HIS F  2 26  ? -61.685 -91.528  -8.153  1.00 128.79 ? 26  HIS F N   1 
ATOM   10315 C CA  . HIS F  2 26  ? -62.497 -91.949  -7.028  1.00 124.49 ? 26  HIS F CA  1 
ATOM   10316 C C   . HIS F  2 26  ? -62.261 -93.425  -6.742  1.00 128.40 ? 26  HIS F C   1 
ATOM   10317 O O   . HIS F  2 26  ? -61.706 -94.146  -7.569  1.00 129.69 ? 26  HIS F O   1 
ATOM   10318 C CB  . HIS F  2 26  ? -63.965 -91.709  -7.340  1.00 119.64 ? 26  HIS F CB  1 
ATOM   10319 C CG  . HIS F  2 26  ? -64.552 -92.724  -8.263  1.00 122.35 ? 26  HIS F CG  1 
ATOM   10320 N ND1 . HIS F  2 26  ? -64.365 -92.688  -9.631  1.00 122.38 ? 26  HIS F ND1 1 
ATOM   10321 C CD2 . HIS F  2 26  ? -65.327 -93.808  -8.019  1.00 137.44 ? 26  HIS F CD2 1 
ATOM   10322 C CE1 . HIS F  2 26  ? -64.998 -93.705  -10.184 1.00 132.38 ? 26  HIS F CE1 1 
ATOM   10323 N NE2 . HIS F  2 26  ? -65.589 -94.399  -9.233  1.00 144.06 ? 26  HIS F NE2 1 
ATOM   10324 N N   . GLN F  2 27  ? -62.701 -93.867  -5.569  1.00 158.73 ? 27  GLN F N   1 
ATOM   10325 C CA  . GLN F  2 27  ? -62.495 -95.239  -5.125  1.00 164.55 ? 27  GLN F CA  1 
ATOM   10326 C C   . GLN F  2 27  ? -63.525 -95.466  -4.018  1.00 161.31 ? 27  GLN F C   1 
ATOM   10327 O O   . GLN F  2 27  ? -63.211 -95.357  -2.833  1.00 159.14 ? 27  GLN F O   1 
ATOM   10328 C CB  . GLN F  2 27  ? -61.073 -95.404  -4.589  1.00 163.80 ? 27  GLN F CB  1 
ATOM   10329 C CG  . GLN F  2 27  ? -60.800 -96.742  -3.920  1.00 164.61 ? 27  GLN F CG  1 
ATOM   10330 C CD  . GLN F  2 27  ? -60.738 -97.883  -4.910  1.00 172.75 ? 27  GLN F CD  1 
ATOM   10331 O OE1 . GLN F  2 27  ? -59.657 -98.287  -5.332  1.00 169.47 ? 27  GLN F OE1 1 
ATOM   10332 N NE2 . GLN F  2 27  ? -61.899 -98.403  -5.294  1.00 178.62 ? 27  GLN F NE2 1 
ATOM   10333 N N   . ASN F  2 28  ? -64.759 -95.787  -4.393  1.00 150.64 ? 28  ASN F N   1 
ATOM   10334 C CA  . ASN F  2 28  ? -65.805 -95.967  -3.390  1.00 154.55 ? 28  ASN F CA  1 
ATOM   10335 C C   . ASN F  2 28  ? -66.332 -97.395  -3.496  1.00 160.22 ? 28  ASN F C   1 
ATOM   10336 O O   . ASN F  2 28  ? -65.571 -98.327  -3.755  1.00 160.47 ? 28  ASN F O   1 
ATOM   10337 C CB  . ASN F  2 28  ? -66.951 -94.943  -3.403  1.00 136.34 ? 28  ASN F CB  1 
ATOM   10338 C CG  . ASN F  2 28  ? -67.718 -94.925  -4.713  1.00 134.14 ? 28  ASN F CG  1 
ATOM   10339 O OD1 . ASN F  2 28  ? -68.672 -94.162  -4.868  1.00 128.37 ? 28  ASN F OD1 1 
ATOM   10340 N ND2 . ASN F  2 28  ? -67.309 -95.763  -5.660  1.00 135.97 ? 28  ASN F ND2 1 
ATOM   10341 N N   . GLU F  2 29  ? -67.636 -97.557  -3.304  1.00 148.79 ? 29  GLU F N   1 
ATOM   10342 C CA  . GLU F  2 29  ? -68.242 -98.882  -3.271  1.00 152.73 ? 29  GLU F CA  1 
ATOM   10343 C C   . GLU F  2 29  ? -68.888 -99.254  -4.603  1.00 147.52 ? 29  GLU F C   1 
ATOM   10344 O O   . GLU F  2 29  ? -69.270 -100.404 -4.813  1.00 141.03 ? 29  GLU F O   1 
ATOM   10345 C CB  . GLU F  2 29  ? -69.276 -98.958  -2.147  1.00 161.77 ? 29  GLU F CB  1 
ATOM   10346 C CG  . GLU F  2 29  ? -68.721 -98.603  -0.779  1.00 161.68 ? 29  GLU F CG  1 
ATOM   10347 C CD  . GLU F  2 29  ? -69.799 -98.163  0.190   1.00 170.15 ? 29  GLU F CD  1 
ATOM   10348 O OE1 . GLU F  2 29  ? -70.846 -97.663  -0.271  1.00 162.63 ? 29  GLU F OE1 1 
ATOM   10349 O OE2 . GLU F  2 29  ? -69.597 -98.311  1.413   1.00 169.93 ? 29  GLU F OE2 1 
ATOM   10350 N N   . GLN F  2 30  ? -69.009 -98.279  -5.498  1.00 148.94 ? 30  GLN F N   1 
ATOM   10351 C CA  . GLN F  2 30  ? -69.613 -98.518  -6.806  1.00 140.53 ? 30  GLN F CA  1 
ATOM   10352 C C   . GLN F  2 30  ? -68.568 -98.662  -7.910  1.00 148.34 ? 30  GLN F C   1 
ATOM   10353 O O   . GLN F  2 30  ? -68.909 -98.735  -9.091  1.00 146.78 ? 30  GLN F O   1 
ATOM   10354 C CB  . GLN F  2 30  ? -70.600 -97.403  -7.158  1.00 126.22 ? 30  GLN F CB  1 
ATOM   10355 C CG  . GLN F  2 30  ? -71.844 -97.385  -6.288  1.00 121.07 ? 30  GLN F CG  1 
ATOM   10356 C CD  . GLN F  2 30  ? -72.048 -96.054  -5.598  1.00 123.72 ? 30  GLN F CD  1 
ATOM   10357 O OE1 . GLN F  2 30  ? -72.727 -95.168  -6.117  1.00 113.80 ? 30  GLN F OE1 1 
ATOM   10358 N NE2 . GLN F  2 30  ? -71.458 -95.905  -4.418  1.00 135.95 ? 30  GLN F NE2 1 
ATOM   10359 N N   . GLY F  2 31  ? -67.297 -98.701  -7.524  1.00 185.51 ? 31  GLY F N   1 
ATOM   10360 C CA  . GLY F  2 31  ? -66.223 -98.900  -8.480  1.00 181.41 ? 31  GLY F CA  1 
ATOM   10361 C C   . GLY F  2 31  ? -65.119 -97.864  -8.400  1.00 173.49 ? 31  GLY F C   1 
ATOM   10362 O O   . GLY F  2 31  ? -65.088 -97.040  -7.485  1.00 164.73 ? 31  GLY F O   1 
ATOM   10363 N N   . SER F  2 32  ? -64.209 -97.911  -9.368  1.00 151.59 ? 32  SER F N   1 
ATOM   10364 C CA  . SER F  2 32  ? -63.085 -96.984  -9.424  1.00 145.59 ? 32  SER F CA  1 
ATOM   10365 C C   . SER F  2 32  ? -63.031 -96.296  -10.783 1.00 137.92 ? 32  SER F C   1 
ATOM   10366 O O   . SER F  2 32  ? -64.017 -96.282  -11.519 1.00 138.84 ? 32  SER F O   1 
ATOM   10367 C CB  . SER F  2 32  ? -61.773 -97.724  -9.165  1.00 136.18 ? 32  SER F CB  1 
ATOM   10368 O OG  . SER F  2 32  ? -61.835 -98.468  -7.961  1.00 148.97 ? 32  SER F OG  1 
ATOM   10369 N N   . GLY F  2 33  ? -61.875 -95.728  -11.113 1.00 143.66 ? 33  GLY F N   1 
ATOM   10370 C CA  . GLY F  2 33  ? -61.682 -95.094  -12.405 1.00 142.18 ? 33  GLY F CA  1 
ATOM   10371 C C   . GLY F  2 33  ? -61.187 -93.662  -12.320 1.00 121.19 ? 33  GLY F C   1 
ATOM   10372 O O   . GLY F  2 33  ? -61.158 -93.065  -11.245 1.00 112.91 ? 33  GLY F O   1 
ATOM   10373 N N   . TYR F  2 34  ? -60.796 -93.112  -13.466 1.00 109.22 ? 34  TYR F N   1 
ATOM   10374 C CA  . TYR F  2 34  ? -60.323 -91.735  -13.538 1.00 94.34  ? 34  TYR F CA  1 
ATOM   10375 C C   . TYR F  2 34  ? -61.358 -90.841  -14.213 1.00 91.40  ? 34  TYR F C   1 
ATOM   10376 O O   . TYR F  2 34  ? -62.074 -91.277  -15.114 1.00 94.78  ? 34  TYR F O   1 
ATOM   10377 C CB  . TYR F  2 34  ? -59.005 -91.660  -14.311 1.00 84.57  ? 34  TYR F CB  1 
ATOM   10378 C CG  . TYR F  2 34  ? -57.926 -92.592  -13.808 1.00 89.48  ? 34  TYR F CG  1 
ATOM   10379 C CD1 . TYR F  2 34  ? -57.817 -93.887  -14.298 1.00 91.30  ? 34  TYR F CD1 1 
ATOM   10380 C CD2 . TYR F  2 34  ? -57.009 -92.175  -12.852 1.00 87.43  ? 34  TYR F CD2 1 
ATOM   10381 C CE1 . TYR F  2 34  ? -56.829 -94.742  -13.845 1.00 97.91  ? 34  TYR F CE1 1 
ATOM   10382 C CE2 . TYR F  2 34  ? -56.018 -93.023  -12.393 1.00 73.98  ? 34  TYR F CE2 1 
ATOM   10383 C CZ  . TYR F  2 34  ? -55.933 -94.305  -12.893 1.00 80.88  ? 34  TYR F CZ  1 
ATOM   10384 O OH  . TYR F  2 34  ? -54.950 -95.154  -12.441 1.00 70.11  ? 34  TYR F OH  1 
ATOM   10385 N N   . ALA F  2 35  ? -61.431 -89.588  -13.775 1.00 84.45  ? 35  ALA F N   1 
ATOM   10386 C CA  . ALA F  2 35  ? -62.336 -88.615  -14.376 1.00 96.80  ? 35  ALA F CA  1 
ATOM   10387 C C   . ALA F  2 35  ? -61.691 -87.233  -14.415 1.00 100.47 ? 35  ALA F C   1 
ATOM   10388 O O   . ALA F  2 35  ? -61.452 -86.622  -13.375 1.00 101.24 ? 35  ALA F O   1 
ATOM   10389 C CB  . ALA F  2 35  ? -63.652 -88.569  -13.615 1.00 101.79 ? 35  ALA F CB  1 
ATOM   10390 N N   . ALA F  2 36  ? -61.411 -86.747  -15.619 1.00 86.58  ? 36  ALA F N   1 
ATOM   10391 C CA  . ALA F  2 36  ? -60.755 -85.456  -15.790 1.00 93.35  ? 36  ALA F CA  1 
ATOM   10392 C C   . ALA F  2 36  ? -61.685 -84.300  -15.441 1.00 89.95  ? 36  ALA F C   1 
ATOM   10393 O O   . ALA F  2 36  ? -62.869 -84.319  -15.780 1.00 102.31 ? 36  ALA F O   1 
ATOM   10394 C CB  . ALA F  2 36  ? -60.240 -85.310  -17.211 1.00 97.51  ? 36  ALA F CB  1 
ATOM   10395 N N   . ASP F  2 37  ? -61.142 -83.294  -14.763 1.00 81.73  ? 37  ASP F N   1 
ATOM   10396 C CA  . ASP F  2 37  ? -61.915 -82.111  -14.406 1.00 82.63  ? 37  ASP F CA  1 
ATOM   10397 C C   . ASP F  2 37  ? -62.301 -81.323  -15.654 1.00 93.16  ? 37  ASP F C   1 
ATOM   10398 O O   . ASP F  2 37  ? -61.443 -80.871  -16.413 1.00 91.76  ? 37  ASP F O   1 
ATOM   10399 C CB  . ASP F  2 37  ? -61.136 -81.224  -13.435 1.00 74.11  ? 37  ASP F CB  1 
ATOM   10400 C CG  . ASP F  2 37  ? -61.958 -80.054  -12.930 1.00 97.06  ? 37  ASP F CG  1 
ATOM   10401 O OD1 . ASP F  2 37  ? -61.397 -79.200  -12.215 1.00 107.30 ? 37  ASP F OD1 1 
ATOM   10402 O OD2 . ASP F  2 37  ? -63.165 -79.987  -13.247 1.00 108.43 ? 37  ASP F OD2 1 
ATOM   10403 N N   . LEU F  2 38  ? -63.603 -81.164  -15.850 1.00 105.28 ? 38  LEU F N   1 
ATOM   10404 C CA  . LEU F  2 38  ? -64.145 -80.523  -17.041 1.00 116.39 ? 38  LEU F CA  1 
ATOM   10405 C C   . LEU F  2 38  ? -63.747 -79.052  -17.180 1.00 100.62 ? 38  LEU F C   1 
ATOM   10406 O O   . LEU F  2 38  ? -63.109 -78.660  -18.160 1.00 86.26  ? 38  LEU F O   1 
ATOM   10407 C CB  . LEU F  2 38  ? -65.668 -80.663  -17.037 1.00 138.09 ? 38  LEU F CB  1 
ATOM   10408 C CG  . LEU F  2 38  ? -66.475 -80.270  -18.276 1.00 150.14 ? 38  LEU F CG  1 
ATOM   10409 C CD1 . LEU F  2 38  ? -65.629 -80.240  -19.544 1.00 146.51 ? 38  LEU F CD1 1 
ATOM   10410 C CD2 . LEU F  2 38  ? -67.675 -81.199  -18.421 1.00 141.77 ? 38  LEU F CD2 1 
ATOM   10411 N N   . LYS F  2 39  ? -64.131 -78.243  -16.198 1.00 128.54 ? 39  LYS F N   1 
ATOM   10412 C CA  . LYS F  2 39  ? -63.903 -76.803  -16.261 1.00 130.64 ? 39  LYS F CA  1 
ATOM   10413 C C   . LYS F  2 39  ? -62.421 -76.431  -16.256 1.00 124.65 ? 39  LYS F C   1 
ATOM   10414 O O   . LYS F  2 39  ? -62.006 -75.510  -16.959 1.00 111.14 ? 39  LYS F O   1 
ATOM   10415 C CB  . LYS F  2 39  ? -64.628 -76.090  -15.116 1.00 138.16 ? 39  LYS F CB  1 
ATOM   10416 C CG  . LYS F  2 39  ? -64.533 -74.573  -15.178 1.00 157.63 ? 39  LYS F CG  1 
ATOM   10417 C CD  . LYS F  2 39  ? -65.407 -73.918  -14.120 1.00 178.16 ? 39  LYS F CD  1 
ATOM   10418 C CE  . LYS F  2 39  ? -65.413 -72.404  -14.267 1.00 180.23 ? 39  LYS F CE  1 
ATOM   10419 N NZ  . LYS F  2 39  ? -66.337 -71.757  -13.294 1.00 165.67 ? 39  LYS F NZ  1 
ATOM   10420 N N   . SER F  2 40  ? -61.627 -77.145  -15.463 1.00 100.29 ? 40  SER F N   1 
ATOM   10421 C CA  . SER F  2 40  ? -60.208 -76.826  -15.319 1.00 88.38  ? 40  SER F CA  1 
ATOM   10422 C C   . SER F  2 40  ? -59.420 -77.104  -16.595 1.00 85.03  ? 40  SER F C   1 
ATOM   10423 O O   . SER F  2 40  ? -58.709 -76.232  -17.097 1.00 89.49  ? 40  SER F O   1 
ATOM   10424 C CB  . SER F  2 40  ? -59.592 -77.592  -14.145 1.00 83.71  ? 40  SER F CB  1 
ATOM   10425 O OG  . SER F  2 40  ? -58.218 -77.274  -13.997 1.00 93.92  ? 40  SER F OG  1 
ATOM   10426 N N   . THR F  2 41  ? -59.545 -78.321  -17.112 1.00 81.56  ? 41  THR F N   1 
ATOM   10427 C CA  . THR F  2 41  ? -58.827 -78.717  -18.317 1.00 73.59  ? 41  THR F CA  1 
ATOM   10428 C C   . THR F  2 41  ? -59.199 -77.833  -19.503 1.00 83.26  ? 41  THR F C   1 
ATOM   10429 O O   . THR F  2 41  ? -58.350 -77.497  -20.329 1.00 74.19  ? 41  THR F O   1 
ATOM   10430 C CB  . THR F  2 41  ? -59.098 -80.189  -18.678 1.00 65.21  ? 41  THR F CB  1 
ATOM   10431 O OG1 . THR F  2 41  ? -58.567 -81.039  -17.654 1.00 77.61  ? 41  THR F OG1 1 
ATOM   10432 C CG2 . THR F  2 41  ? -58.446 -80.540  -20.007 1.00 67.19  ? 41  THR F CG2 1 
ATOM   10433 N N   . GLN F  2 42  ? -60.470 -77.453  -19.578 1.00 89.98  ? 42  GLN F N   1 
ATOM   10434 C CA  . GLN F  2 42  ? -60.952 -76.628  -20.679 1.00 91.20  ? 42  GLN F CA  1 
ATOM   10435 C C   . GLN F  2 42  ? -60.294 -75.251  -20.683 1.00 84.95  ? 42  GLN F C   1 
ATOM   10436 O O   . GLN F  2 42  ? -59.831 -74.781  -21.722 1.00 84.41  ? 42  GLN F O   1 
ATOM   10437 C CB  . GLN F  2 42  ? -62.475 -76.489  -20.628 1.00 95.75  ? 42  GLN F CB  1 
ATOM   10438 C CG  . GLN F  2 42  ? -63.062 -75.775  -21.834 1.00 101.31 ? 42  GLN F CG  1 
ATOM   10439 C CD  . GLN F  2 42  ? -62.703 -76.456  -23.141 1.00 108.38 ? 42  GLN F CD  1 
ATOM   10440 O OE1 . GLN F  2 42  ? -62.518 -77.672  -23.192 1.00 110.44 ? 42  GLN F OE1 1 
ATOM   10441 N NE2 . GLN F  2 42  ? -62.604 -75.672  -24.209 1.00 109.74 ? 42  GLN F NE2 1 
ATOM   10442 N N   . ASN F  2 43  ? -60.257 -74.608  -19.520 1.00 80.24  ? 43  ASN F N   1 
ATOM   10443 C CA  . ASN F  2 43  ? -59.629 -73.297  -19.392 1.00 78.83  ? 43  ASN F CA  1 
ATOM   10444 C C   . ASN F  2 43  ? -58.145 -73.323  -19.741 1.00 77.44  ? 43  ASN F C   1 
ATOM   10445 O O   . ASN F  2 43  ? -57.653 -72.453  -20.460 1.00 70.58  ? 43  ASN F O   1 
ATOM   10446 C CB  . ASN F  2 43  ? -59.826 -72.734  -17.983 1.00 81.61  ? 43  ASN F CB  1 
ATOM   10447 C CG  . ASN F  2 43  ? -61.024 -71.809  -17.887 1.00 92.40  ? 43  ASN F CG  1 
ATOM   10448 O OD1 . ASN F  2 43  ? -62.169 -72.237  -18.039 1.00 97.81  ? 43  ASN F OD1 1 
ATOM   10449 N ND2 . ASN F  2 43  ? -60.765 -70.532  -17.631 1.00 96.94  ? 43  ASN F ND2 1 
ATOM   10450 N N   . ALA F  2 44  ? -57.436 -74.323  -19.227 1.00 71.17  ? 44  ALA F N   1 
ATOM   10451 C CA  . ALA F  2 44  ? -56.012 -74.468  -19.500 1.00 66.18  ? 44  ALA F CA  1 
ATOM   10452 C C   . ALA F  2 44  ? -55.752 -74.531  -21.000 1.00 69.49  ? 44  ALA F C   1 
ATOM   10453 O O   . ALA F  2 44  ? -54.903 -73.809  -21.522 1.00 71.10  ? 44  ALA F O   1 
ATOM   10454 C CB  . ALA F  2 44  ? -55.462 -75.706  -18.811 1.00 56.68  ? 44  ALA F CB  1 
ATOM   10455 N N   . ILE F  2 45  ? -56.490 -75.397  -21.688 1.00 68.10  ? 45  ILE F N   1 
ATOM   10456 C CA  . ILE F  2 45  ? -56.363 -75.536  -23.134 1.00 72.07  ? 45  ILE F CA  1 
ATOM   10457 C C   . ILE F  2 45  ? -56.565 -74.200  -23.843 1.00 71.67  ? 45  ILE F C   1 
ATOM   10458 O O   . ILE F  2 45  ? -55.767 -73.814  -24.695 1.00 65.62  ? 45  ILE F O   1 
ATOM   10459 C CB  . ILE F  2 45  ? -57.359 -76.569  -23.695 1.00 71.70  ? 45  ILE F CB  1 
ATOM   10460 C CG1 . ILE F  2 45  ? -56.909 -77.988  -23.339 1.00 62.59  ? 45  ILE F CG1 1 
ATOM   10461 C CG2 . ILE F  2 45  ? -57.489 -76.422  -25.203 1.00 76.99  ? 45  ILE F CG2 1 
ATOM   10462 C CD1 . ILE F  2 45  ? -57.786 -79.073  -23.926 1.00 82.99  ? 45  ILE F CD1 1 
ATOM   10463 N N   . ASP F  2 46  ? -57.634 -73.497  -23.482 1.00 71.99  ? 46  ASP F N   1 
ATOM   10464 C CA  . ASP F  2 46  ? -57.930 -72.195  -24.069 1.00 73.44  ? 46  ASP F CA  1 
ATOM   10465 C C   . ASP F  2 46  ? -56.787 -71.206  -23.857 1.00 74.83  ? 46  ASP F C   1 
ATOM   10466 O O   . ASP F  2 46  ? -56.356 -70.532  -24.793 1.00 60.16  ? 46  ASP F O   1 
ATOM   10467 C CB  . ASP F  2 46  ? -59.226 -71.625  -23.487 1.00 68.24  ? 46  ASP F CB  1 
ATOM   10468 C CG  . ASP F  2 46  ? -60.461 -72.341  -23.998 1.00 99.80  ? 46  ASP F CG  1 
ATOM   10469 O OD1 . ASP F  2 46  ? -60.358 -73.049  -25.023 1.00 105.65 ? 46  ASP F OD1 1 
ATOM   10470 O OD2 . ASP F  2 46  ? -61.536 -72.191  -23.380 1.00 105.74 ? 46  ASP F OD2 1 
ATOM   10471 N N   . GLU F  2 47  ? -56.299 -71.125  -22.624 1.00 73.32  ? 47  GLU F N   1 
ATOM   10472 C CA  . GLU F  2 47  ? -55.263 -70.159  -22.276 1.00 59.16  ? 47  GLU F CA  1 
ATOM   10473 C C   . GLU F  2 47  ? -53.892 -70.527  -22.840 1.00 54.73  ? 47  GLU F C   1 
ATOM   10474 O O   . GLU F  2 47  ? -53.136 -69.653  -23.261 1.00 53.68  ? 47  GLU F O   1 
ATOM   10475 C CB  . GLU F  2 47  ? -55.193 -69.958  -20.760 1.00 53.38  ? 47  GLU F CB  1 
ATOM   10476 C CG  . GLU F  2 47  ? -56.445 -69.320  -20.177 1.00 69.22  ? 47  GLU F CG  1 
ATOM   10477 C CD  . GLU F  2 47  ? -56.285 -68.929  -18.721 1.00 79.97  ? 47  GLU F CD  1 
ATOM   10478 O OE1 . GLU F  2 47  ? -55.366 -69.453  -18.058 1.00 70.67  ? 47  GLU F OE1 1 
ATOM   10479 O OE2 . GLU F  2 47  ? -57.082 -68.095  -18.241 1.00 83.78  ? 47  GLU F OE2 1 
ATOM   10480 N N   . ILE F  2 48  ? -53.573 -71.817  -22.848 1.00 54.38  ? 48  ILE F N   1 
ATOM   10481 C CA  . ILE F  2 48  ? -52.331 -72.279  -23.457 1.00 44.98  ? 48  ILE F CA  1 
ATOM   10482 C C   . ILE F  2 48  ? -52.374 -72.050  -24.963 1.00 57.49  ? 48  ILE F C   1 
ATOM   10483 O O   . ILE F  2 48  ? -51.376 -71.666  -25.573 1.00 62.35  ? 48  ILE F O   1 
ATOM   10484 C CB  . ILE F  2 48  ? -52.062 -73.767  -23.161 1.00 48.93  ? 48  ILE F CB  1 
ATOM   10485 C CG1 . ILE F  2 48  ? -51.688 -73.956  -21.689 1.00 59.76  ? 48  ILE F CG1 1 
ATOM   10486 C CG2 . ILE F  2 48  ? -50.950 -74.296  -24.054 1.00 45.80  ? 48  ILE F CG2 1 
ATOM   10487 C CD1 . ILE F  2 48  ? -50.479 -73.153  -21.258 1.00 51.47  ? 48  ILE F CD1 1 
ATOM   10488 N N   . THR F  2 49  ? -53.540 -72.285  -25.556 1.00 54.26  ? 49  THR F N   1 
ATOM   10489 C CA  . THR F  2 49  ? -53.750 -72.008  -26.971 1.00 49.71  ? 49  THR F CA  1 
ATOM   10490 C C   . THR F  2 49  ? -53.494 -70.534  -27.256 1.00 55.89  ? 49  THR F C   1 
ATOM   10491 O O   . THR F  2 49  ? -52.734 -70.188  -28.160 1.00 59.67  ? 49  THR F O   1 
ATOM   10492 C CB  . THR F  2 49  ? -55.182 -72.361  -27.411 1.00 67.12  ? 49  THR F CB  1 
ATOM   10493 O OG1 . THR F  2 49  ? -55.362 -73.782  -27.367 1.00 75.70  ? 49  THR F OG1 1 
ATOM   10494 C CG2 . THR F  2 49  ? -55.443 -71.866  -28.825 1.00 49.87  ? 49  THR F CG2 1 
ATOM   10495 N N   . ASN F  2 50  ? -54.134 -69.670  -26.474 1.00 49.18  ? 50  ASN F N   1 
ATOM   10496 C CA  . ASN F  2 50  ? -53.956 -68.231  -26.612 1.00 54.27  ? 50  ASN F CA  1 
ATOM   10497 C C   . ASN F  2 50  ? -52.487 -67.846  -26.491 1.00 59.43  ? 50  ASN F C   1 
ATOM   10498 O O   . ASN F  2 50  ? -52.002 -66.965  -27.201 1.00 54.38  ? 50  ASN F O   1 
ATOM   10499 C CB  . ASN F  2 50  ? -54.782 -67.493  -25.558 1.00 53.55  ? 50  ASN F CB  1 
ATOM   10500 C CG  . ASN F  2 50  ? -54.863 -66.002  -25.820 1.00 63.50  ? 50  ASN F CG  1 
ATOM   10501 O OD1 . ASN F  2 50  ? -55.770 -65.531  -26.508 1.00 73.70  ? 50  ASN F OD1 1 
ATOM   10502 N ND2 . ASN F  2 50  ? -53.915 -65.250  -25.272 1.00 52.67  ? 50  ASN F ND2 1 
ATOM   10503 N N   . LYS F  2 51  ? -51.786 -68.519  -25.586 1.00 52.56  ? 51  LYS F N   1 
ATOM   10504 C CA  . LYS F  2 51  ? -50.365 -68.285  -25.374 1.00 49.22  ? 51  LYS F CA  1 
ATOM   10505 C C   . LYS F  2 51  ? -49.569 -68.559  -26.644 1.00 53.62  ? 51  LYS F C   1 
ATOM   10506 O O   . LYS F  2 51  ? -48.766 -67.732  -27.077 1.00 52.38  ? 51  LYS F O   1 
ATOM   10507 C CB  . LYS F  2 51  ? -49.855 -69.166  -24.233 1.00 53.56  ? 51  LYS F CB  1 
ATOM   10508 C CG  . LYS F  2 51  ? -48.386 -68.990  -23.905 1.00 48.31  ? 51  LYS F CG  1 
ATOM   10509 C CD  . LYS F  2 51  ? -48.055 -69.673  -22.590 1.00 53.70  ? 51  LYS F CD  1 
ATOM   10510 C CE  . LYS F  2 51  ? -46.625 -69.407  -22.167 1.00 53.91  ? 51  LYS F CE  1 
ATOM   10511 N NZ  . LYS F  2 51  ? -46.417 -69.703  -20.722 1.00 49.11  ? 51  LYS F NZ  1 
ATOM   10512 N N   . VAL F  2 52  ? -49.800 -69.725  -27.239 1.00 46.70  ? 52  VAL F N   1 
ATOM   10513 C CA  . VAL F  2 52  ? -49.109 -70.114  -28.462 1.00 45.06  ? 52  VAL F CA  1 
ATOM   10514 C C   . VAL F  2 52  ? -49.446 -69.168  -29.610 1.00 57.13  ? 52  VAL F C   1 
ATOM   10515 O O   . VAL F  2 52  ? -48.575 -68.799  -30.398 1.00 64.69  ? 52  VAL F O   1 
ATOM   10516 C CB  . VAL F  2 52  ? -49.459 -71.557  -28.872 1.00 41.70  ? 52  VAL F CB  1 
ATOM   10517 C CG1 . VAL F  2 52  ? -48.670 -71.964  -30.107 1.00 41.78  ? 52  VAL F CG1 1 
ATOM   10518 C CG2 . VAL F  2 52  ? -49.186 -72.513  -27.724 1.00 48.55  ? 52  VAL F CG2 1 
ATOM   10519 N N   . ASN F  2 53  ? -50.713 -68.778  -29.700 1.00 48.69  ? 53  ASN F N   1 
ATOM   10520 C CA  . ASN F  2 53  ? -51.156 -67.856  -30.740 1.00 55.74  ? 53  ASN F CA  1 
ATOM   10521 C C   . ASN F  2 53  ? -50.489 -66.489  -30.639 1.00 64.86  ? 53  ASN F C   1 
ATOM   10522 O O   . ASN F  2 53  ? -50.180 -65.869  -31.653 1.00 69.36  ? 53  ASN F O   1 
ATOM   10523 C CB  . ASN F  2 53  ? -52.678 -67.701  -30.717 1.00 63.53  ? 53  ASN F CB  1 
ATOM   10524 C CG  . ASN F  2 53  ? -53.391 -68.825  -31.443 1.00 71.11  ? 53  ASN F CG  1 
ATOM   10525 O OD1 . ASN F  2 53  ? -52.761 -69.650  -32.105 1.00 56.09  ? 53  ASN F OD1 1 
ATOM   10526 N ND2 . ASN F  2 53  ? -54.713 -68.858  -31.329 1.00 75.60  ? 53  ASN F ND2 1 
ATOM   10527 N N   . SER F  2 54  ? -50.269 -66.023  -29.414 1.00 54.66  ? 54  SER F N   1 
ATOM   10528 C CA  . SER F  2 54  ? -49.650 -64.720  -29.193 1.00 50.39  ? 54  SER F CA  1 
ATOM   10529 C C   . SER F  2 54  ? -48.217 -64.679  -29.716 1.00 51.96  ? 54  SER F C   1 
ATOM   10530 O O   . SER F  2 54  ? -47.854 -63.790  -30.487 1.00 52.61  ? 54  SER F O   1 
ATOM   10531 C CB  . SER F  2 54  ? -49.679 -64.354  -27.708 1.00 51.76  ? 54  SER F CB  1 
ATOM   10532 O OG  . SER F  2 54  ? -51.010 -64.224  -27.241 1.00 60.84  ? 54  SER F OG  1 
ATOM   10533 N N   . VAL F  2 55  ? -47.409 -65.644  -29.290 1.00 48.73  ? 55  VAL F N   1 
ATOM   10534 C CA  . VAL F  2 55  ? -46.019 -65.734  -29.724 1.00 47.86  ? 55  VAL F CA  1 
ATOM   10535 C C   . VAL F  2 55  ? -45.921 -65.741  -31.247 1.00 50.14  ? 55  VAL F C   1 
ATOM   10536 O O   . VAL F  2 55  ? -44.944 -65.258  -31.821 1.00 52.04  ? 55  VAL F O   1 
ATOM   10537 C CB  . VAL F  2 55  ? -45.336 -66.997  -29.161 1.00 50.17  ? 55  VAL F CB  1 
ATOM   10538 C CG1 . VAL F  2 55  ? -43.940 -67.157  -29.742 1.00 57.67  ? 55  VAL F CG1 1 
ATOM   10539 C CG2 . VAL F  2 55  ? -45.282 -66.938  -27.642 1.00 40.71  ? 55  VAL F CG2 1 
ATOM   10540 N N   . ILE F  2 56  ? -46.946 -66.284  -31.895 1.00 47.15  ? 56  ILE F N   1 
ATOM   10541 C CA  . ILE F  2 56  ? -46.971 -66.392  -33.349 1.00 45.99  ? 56  ILE F CA  1 
ATOM   10542 C C   . ILE F  2 56  ? -47.600 -65.169  -34.015 1.00 46.77  ? 56  ILE F C   1 
ATOM   10543 O O   . ILE F  2 56  ? -47.019 -64.579  -34.925 1.00 52.44  ? 56  ILE F O   1 
ATOM   10544 C CB  . ILE F  2 56  ? -47.744 -67.648  -33.799 1.00 51.72  ? 56  ILE F CB  1 
ATOM   10545 C CG1 . ILE F  2 56  ? -47.001 -68.917  -33.373 1.00 51.92  ? 56  ILE F CG1 1 
ATOM   10546 C CG2 . ILE F  2 56  ? -47.961 -67.633  -35.303 1.00 48.98  ? 56  ILE F CG2 1 
ATOM   10547 C CD1 . ILE F  2 56  ? -47.731 -70.196  -33.721 1.00 42.50  ? 56  ILE F CD1 1 
ATOM   10548 N N   . GLU F  2 57  ? -48.787 -64.794  -33.553 1.00 43.39  ? 57  GLU F N   1 
ATOM   10549 C CA  . GLU F  2 57  ? -49.578 -63.752  -34.202 1.00 48.23  ? 57  GLU F CA  1 
ATOM   10550 C C   . GLU F  2 57  ? -48.901 -62.383  -34.181 1.00 52.73  ? 57  GLU F C   1 
ATOM   10551 O O   . GLU F  2 57  ? -49.118 -61.564  -35.074 1.00 61.43  ? 57  GLU F O   1 
ATOM   10552 C CB  . GLU F  2 57  ? -50.967 -63.668  -33.562 1.00 65.67  ? 57  GLU F CB  1 
ATOM   10553 C CG  . GLU F  2 57  ? -52.007 -62.952  -34.409 1.00 105.99 ? 57  GLU F CG  1 
ATOM   10554 C CD  . GLU F  2 57  ? -52.279 -61.536  -33.940 1.00 112.37 ? 57  GLU F CD  1 
ATOM   10555 O OE1 . GLU F  2 57  ? -52.120 -61.263  -32.731 1.00 96.93  ? 57  GLU F OE1 1 
ATOM   10556 O OE2 . GLU F  2 57  ? -52.663 -60.697  -34.782 1.00 101.29 ? 57  GLU F OE2 1 
ATOM   10557 N N   . LYS F  2 58  ? -48.079 -62.140  -33.165 1.00 47.34  ? 58  LYS F N   1 
ATOM   10558 C CA  . LYS F  2 58  ? -47.419 -60.847  -33.013 1.00 44.99  ? 58  LYS F CA  1 
ATOM   10559 C C   . LYS F  2 58  ? -46.246 -60.676  -33.973 1.00 53.87  ? 58  LYS F C   1 
ATOM   10560 O O   . LYS F  2 58  ? -45.542 -59.667  -33.931 1.00 53.40  ? 58  LYS F O   1 
ATOM   10561 C CB  . LYS F  2 58  ? -46.948 -60.648  -31.571 1.00 49.63  ? 58  LYS F CB  1 
ATOM   10562 C CG  . LYS F  2 58  ? -48.078 -60.537  -30.561 1.00 49.95  ? 58  LYS F CG  1 
ATOM   10563 C CD  . LYS F  2 58  ? -49.002 -59.378  -30.898 1.00 53.39  ? 58  LYS F CD  1 
ATOM   10564 C CE  . LYS F  2 58  ? -50.137 -59.265  -29.892 1.00 53.39  ? 58  LYS F CE  1 
ATOM   10565 N NZ  . LYS F  2 58  ? -51.047 -58.125  -30.196 1.00 51.99  ? 58  LYS F NZ  1 
ATOM   10566 N N   . MET F  2 59  ? -46.038 -61.663  -34.837 1.00 51.14  ? 59  MET F N   1 
ATOM   10567 C CA  . MET F  2 59  ? -44.940 -61.605  -35.793 1.00 46.02  ? 59  MET F CA  1 
ATOM   10568 C C   . MET F  2 59  ? -45.419 -61.165  -37.173 1.00 58.86  ? 59  MET F C   1 
ATOM   10569 O O   . MET F  2 59  ? -45.585 -61.986  -38.076 1.00 72.25  ? 59  MET F O   1 
ATOM   10570 C CB  . MET F  2 59  ? -44.219 -62.953  -35.879 1.00 55.97  ? 59  MET F CB  1 
ATOM   10571 C CG  . MET F  2 59  ? -42.958 -62.915  -36.727 1.00 55.19  ? 59  MET F CG  1 
ATOM   10572 S SD  . MET F  2 59  ? -41.897 -61.526  -36.280 1.00 60.71  ? 59  MET F SD  1 
ATOM   10573 C CE  . MET F  2 59  ? -40.504 -62.373  -35.541 1.00 50.52  ? 59  MET F CE  1 
ATOM   10574 N N   . ASN F  2 60  ? -45.648 -59.865  -37.330 1.00 50.94  ? 60  ASN F N   1 
ATOM   10575 C CA  . ASN F  2 60  ? -46.025 -59.319  -38.628 1.00 65.93  ? 60  ASN F CA  1 
ATOM   10576 C C   . ASN F  2 60  ? -44.830 -58.654  -39.309 1.00 62.95  ? 60  ASN F C   1 
ATOM   10577 O O   . ASN F  2 60  ? -44.486 -57.510  -39.019 1.00 61.01  ? 60  ASN F O   1 
ATOM   10578 C CB  . ASN F  2 60  ? -47.220 -58.362  -38.511 1.00 90.37  ? 60  ASN F CB  1 
ATOM   10579 C CG  . ASN F  2 60  ? -46.837 -56.999  -37.964 1.00 117.66 ? 60  ASN F CG  1 
ATOM   10580 O OD1 . ASN F  2 60  ? -46.598 -56.062  -38.726 1.00 118.26 ? 60  ASN F OD1 1 
ATOM   10581 N ND2 . ASN F  2 60  ? -46.788 -56.878  -36.641 1.00 110.69 ? 60  ASN F ND2 1 
ATOM   10582 N N   . THR F  2 61  ? -44.191 -59.393  -40.209 1.00 67.65  ? 61  THR F N   1 
ATOM   10583 C CA  . THR F  2 61  ? -42.962 -58.932  -40.844 1.00 64.59  ? 61  THR F CA  1 
ATOM   10584 C C   . THR F  2 61  ? -43.225 -58.033  -42.048 1.00 67.07  ? 61  THR F C   1 
ATOM   10585 O O   . THR F  2 61  ? -44.291 -58.089  -42.660 1.00 58.63  ? 61  THR F O   1 
ATOM   10586 C CB  . THR F  2 61  ? -42.077 -60.117  -41.279 1.00 61.81  ? 61  THR F CB  1 
ATOM   10587 O OG1 . THR F  2 61  ? -42.823 -60.982  -42.145 1.00 65.54  ? 61  THR F OG1 1 
ATOM   10588 C CG2 . THR F  2 61  ? -41.615 -60.907  -40.067 1.00 60.73  ? 61  THR F CG2 1 
ATOM   10589 N N   . GLN F  2 62  ? -42.242 -57.201  -42.374 1.00 66.65  ? 62  GLN F N   1 
ATOM   10590 C CA  . GLN F  2 62  ? -42.321 -56.331  -43.539 1.00 64.31  ? 62  GLN F CA  1 
ATOM   10591 C C   . GLN F  2 62  ? -41.968 -57.112  -44.795 1.00 62.34  ? 62  GLN F C   1 
ATOM   10592 O O   . GLN F  2 62  ? -41.264 -58.120  -44.729 1.00 64.25  ? 62  GLN F O   1 
ATOM   10593 C CB  . GLN F  2 62  ? -41.359 -55.152  -43.386 1.00 57.04  ? 62  GLN F CB  1 
ATOM   10594 C CG  . GLN F  2 62  ? -41.705 -54.201  -42.256 1.00 50.86  ? 62  GLN F CG  1 
ATOM   10595 C CD  . GLN F  2 62  ? -43.002 -53.459  -42.501 1.00 61.83  ? 62  GLN F CD  1 
ATOM   10596 O OE1 . GLN F  2 62  ? -44.089 -53.998  -42.293 1.00 74.65  ? 62  GLN F OE1 1 
ATOM   10597 N NE2 . GLN F  2 62  ? -42.895 -52.213  -42.947 1.00 50.87  ? 62  GLN F NE2 1 
ATOM   10598 N N   . PHE F  2 63  ? -42.458 -56.652  -45.941 1.00 53.33  ? 63  PHE F N   1 
ATOM   10599 C CA  . PHE F  2 63  ? -42.042 -57.236  -47.206 1.00 57.70  ? 63  PHE F CA  1 
ATOM   10600 C C   . PHE F  2 63  ? -40.671 -56.692  -47.570 1.00 53.00  ? 63  PHE F C   1 
ATOM   10601 O O   . PHE F  2 63  ? -40.536 -55.537  -47.975 1.00 64.86  ? 63  PHE F O   1 
ATOM   10602 C CB  . PHE F  2 63  ? -43.039 -56.930  -48.322 1.00 57.42  ? 63  PHE F CB  1 
ATOM   10603 C CG  . PHE F  2 63  ? -42.722 -57.623  -49.619 1.00 60.33  ? 63  PHE F CG  1 
ATOM   10604 C CD1 . PHE F  2 63  ? -43.412 -58.763  -49.996 1.00 50.55  ? 63  PHE F CD1 1 
ATOM   10605 C CD2 . PHE F  2 63  ? -41.726 -57.143  -50.454 1.00 56.51  ? 63  PHE F CD2 1 
ATOM   10606 C CE1 . PHE F  2 63  ? -43.121 -59.405  -51.185 1.00 61.74  ? 63  PHE F CE1 1 
ATOM   10607 C CE2 . PHE F  2 63  ? -41.429 -57.782  -51.643 1.00 60.26  ? 63  PHE F CE2 1 
ATOM   10608 C CZ  . PHE F  2 63  ? -42.128 -58.913  -52.010 1.00 66.29  ? 63  PHE F CZ  1 
ATOM   10609 N N   . THR F  2 64  ? -39.652 -57.527  -47.414 1.00 45.07  ? 64  THR F N   1 
ATOM   10610 C CA  . THR F  2 64  ? -38.289 -57.120  -47.713 1.00 62.22  ? 64  THR F CA  1 
ATOM   10611 C C   . THR F  2 64  ? -37.553 -58.193  -48.494 1.00 45.27  ? 64  THR F C   1 
ATOM   10612 O O   . THR F  2 64  ? -37.786 -59.387  -48.308 1.00 38.09  ? 64  THR F O   1 
ATOM   10613 C CB  . THR F  2 64  ? -37.496 -56.806  -46.431 1.00 71.71  ? 64  THR F CB  1 
ATOM   10614 O OG1 . THR F  2 64  ? -37.751 -57.820  -45.450 1.00 53.64  ? 64  THR F OG1 1 
ATOM   10615 C CG2 . THR F  2 64  ? -37.903 -55.454  -45.869 1.00 66.23  ? 64  THR F CG2 1 
ATOM   10616 N N   . ALA F  2 65  ? -36.666 -57.753  -49.378 1.00 43.05  ? 65  ALA F N   1 
ATOM   10617 C CA  . ALA F  2 65  ? -35.787 -58.662  -50.090 1.00 46.64  ? 65  ALA F CA  1 
ATOM   10618 C C   . ALA F  2 65  ? -34.373 -58.512  -49.554 1.00 49.21  ? 65  ALA F C   1 
ATOM   10619 O O   . ALA F  2 65  ? -33.555 -57.796  -50.130 1.00 47.49  ? 65  ALA F O   1 
ATOM   10620 C CB  . ALA F  2 65  ? -35.824 -58.379  -51.579 1.00 36.76  ? 65  ALA F CB  1 
ATOM   10621 N N   . VAL F  2 66  ? -34.095 -59.170  -48.434 1.00 37.38  ? 66  VAL F N   1 
ATOM   10622 C CA  . VAL F  2 66  ? -32.741 -59.207  -47.905 1.00 44.58  ? 66  VAL F CA  1 
ATOM   10623 C C   . VAL F  2 66  ? -31.824 -59.778  -48.974 1.00 51.82  ? 66  VAL F C   1 
ATOM   10624 O O   . VAL F  2 66  ? -32.265 -60.544  -49.829 1.00 67.50  ? 66  VAL F O   1 
ATOM   10625 C CB  . VAL F  2 66  ? -32.656 -60.047  -46.615 1.00 40.02  ? 66  VAL F CB  1 
ATOM   10626 C CG1 . VAL F  2 66  ? -33.749 -61.103  -46.595 1.00 45.38  ? 66  VAL F CG1 1 
ATOM   10627 C CG2 . VAL F  2 66  ? -31.272 -60.668  -46.459 1.00 39.46  ? 66  VAL F CG2 1 
ATOM   10628 N N   . GLY F  2 67  ? -30.553 -59.398  -48.933 1.00 39.60  ? 67  GLY F N   1 
ATOM   10629 C CA  . GLY F  2 67  ? -29.612 -59.825  -49.947 1.00 60.64  ? 67  GLY F CA  1 
ATOM   10630 C C   . GLY F  2 67  ? -29.445 -58.757  -51.007 1.00 50.42  ? 67  GLY F C   1 
ATOM   10631 O O   . GLY F  2 67  ? -30.405 -58.374  -51.674 1.00 36.81  ? 67  GLY F O   1 
ATOM   10632 N N   . LYS F  2 68  ? -28.219 -58.268  -51.152 1.00 55.85  ? 68  LYS F N   1 
ATOM   10633 C CA  . LYS F  2 68  ? -27.915 -57.228  -52.123 1.00 39.12  ? 68  LYS F CA  1 
ATOM   10634 C C   . LYS F  2 68  ? -26.708 -57.642  -52.956 1.00 48.72  ? 68  LYS F C   1 
ATOM   10635 O O   . LYS F  2 68  ? -26.023 -58.612  -52.629 1.00 49.10  ? 68  LYS F O   1 
ATOM   10636 C CB  . LYS F  2 68  ? -27.642 -55.904  -51.407 1.00 51.31  ? 68  LYS F CB  1 
ATOM   10637 C CG  . LYS F  2 68  ? -28.796 -55.423  -50.535 1.00 42.66  ? 68  LYS F CG  1 
ATOM   10638 C CD  . LYS F  2 68  ? -29.735 -54.508  -51.307 1.00 52.61  ? 68  LYS F CD  1 
ATOM   10639 C CE  . LYS F  2 68  ? -31.075 -54.359  -50.605 1.00 64.44  ? 68  LYS F CE  1 
ATOM   10640 N NZ  . LYS F  2 68  ? -32.025 -55.440  -50.994 1.00 61.96  ? 68  LYS F NZ  1 
ATOM   10641 N N   . GLU F  2 69  ? -26.452 -56.910  -54.034 1.00 59.30  ? 69  GLU F N   1 
ATOM   10642 C CA  . GLU F  2 69  ? -25.327 -57.212  -54.909 1.00 48.91  ? 69  GLU F CA  1 
ATOM   10643 C C   . GLU F  2 69  ? -24.361 -56.037  -54.976 1.00 46.50  ? 69  GLU F C   1 
ATOM   10644 O O   . GLU F  2 69  ? -24.768 -54.905  -55.227 1.00 50.68  ? 69  GLU F O   1 
ATOM   10645 C CB  . GLU F  2 69  ? -25.821 -57.569  -56.312 1.00 50.38  ? 69  GLU F CB  1 
ATOM   10646 C CG  . GLU F  2 69  ? -26.698 -58.810  -56.364 1.00 60.43  ? 69  GLU F CG  1 
ATOM   10647 C CD  . GLU F  2 69  ? -27.283 -59.049  -57.742 1.00 65.01  ? 69  GLU F CD  1 
ATOM   10648 O OE1 . GLU F  2 69  ? -27.409 -58.073  -58.510 1.00 68.13  ? 69  GLU F OE1 1 
ATOM   10649 O OE2 . GLU F  2 69  ? -27.619 -60.211  -58.055 1.00 59.74  ? 69  GLU F OE2 1 
ATOM   10650 N N   . PHE F  2 70  ? -23.082 -56.310  -54.745 1.00 42.61  ? 70  PHE F N   1 
ATOM   10651 C CA  . PHE F  2 70  ? -22.061 -55.271  -54.783 1.00 46.13  ? 70  PHE F CA  1 
ATOM   10652 C C   . PHE F  2 70  ? -20.869 -55.722  -55.618 1.00 47.90  ? 70  PHE F C   1 
ATOM   10653 O O   . PHE F  2 70  ? -20.477 -56.887  -55.571 1.00 48.60  ? 70  PHE F O   1 
ATOM   10654 C CB  . PHE F  2 70  ? -21.600 -54.919  -53.367 1.00 48.69  ? 70  PHE F CB  1 
ATOM   10655 C CG  . PHE F  2 70  ? -22.722 -54.558  -52.432 1.00 49.94  ? 70  PHE F CG  1 
ATOM   10656 C CD1 . PHE F  2 70  ? -23.265 -53.284  -52.436 1.00 41.61  ? 70  PHE F CD1 1 
ATOM   10657 C CD2 . PHE F  2 70  ? -23.228 -55.492  -51.542 1.00 39.25  ? 70  PHE F CD2 1 
ATOM   10658 C CE1 . PHE F  2 70  ? -24.293 -52.949  -51.574 1.00 38.51  ? 70  PHE F CE1 1 
ATOM   10659 C CE2 . PHE F  2 70  ? -24.256 -55.163  -50.677 1.00 35.21  ? 70  PHE F CE2 1 
ATOM   10660 C CZ  . PHE F  2 70  ? -24.789 -53.890  -50.694 1.00 38.15  ? 70  PHE F CZ  1 
ATOM   10661 N N   . ASN F  2 71  ? -20.295 -54.800  -56.384 1.00 48.86  ? 71  ASN F N   1 
ATOM   10662 C CA  . ASN F  2 71  ? -19.120 -55.119  -57.185 1.00 47.92  ? 71  ASN F CA  1 
ATOM   10663 C C   . ASN F  2 71  ? -17.848 -55.121  -56.344 1.00 47.79  ? 71  ASN F C   1 
ATOM   10664 O O   . ASN F  2 71  ? -17.879 -54.807  -55.153 1.00 39.12  ? 71  ASN F O   1 
ATOM   10665 C CB  . ASN F  2 71  ? -18.988 -54.170  -58.381 1.00 47.85  ? 71  ASN F CB  1 
ATOM   10666 C CG  . ASN F  2 71  ? -18.831 -52.722  -57.967 1.00 51.05  ? 71  ASN F CG  1 
ATOM   10667 O OD1 . ASN F  2 71  ? -17.956 -52.381  -57.171 1.00 57.29  ? 71  ASN F OD1 1 
ATOM   10668 N ND2 . ASN F  2 71  ? -19.675 -51.857  -58.515 1.00 65.64  ? 71  ASN F ND2 1 
ATOM   10669 N N   . HIS F  2 72  ? -16.732 -55.476  -56.970 1.00 49.00  ? 72  HIS F N   1 
ATOM   10670 C CA  . HIS F  2 72  ? -15.466 -55.640  -56.264 1.00 54.05  ? 72  HIS F CA  1 
ATOM   10671 C C   . HIS F  2 72  ? -14.996 -54.362  -55.573 1.00 56.01  ? 72  HIS F C   1 
ATOM   10672 O O   . HIS F  2 72  ? -14.195 -54.415  -54.642 1.00 65.45  ? 72  HIS F O   1 
ATOM   10673 C CB  . HIS F  2 72  ? -14.388 -56.143  -57.225 1.00 62.14  ? 72  HIS F CB  1 
ATOM   10674 C CG  . HIS F  2 72  ? -14.164 -55.245  -58.402 1.00 76.75  ? 72  HIS F CG  1 
ATOM   10675 N ND1 . HIS F  2 72  ? -14.956 -55.286  -59.529 1.00 81.83  ? 72  HIS F ND1 1 
ATOM   10676 C CD2 . HIS F  2 72  ? -13.240 -54.283  -58.625 1.00 83.20  ? 72  HIS F CD2 1 
ATOM   10677 C CE1 . HIS F  2 72  ? -14.528 -54.387  -60.397 1.00 90.72  ? 72  HIS F CE1 1 
ATOM   10678 N NE2 . HIS F  2 72  ? -13.487 -53.764  -59.873 1.00 86.97  ? 72  HIS F NE2 1 
ATOM   10679 N N   . LEU F  2 73  ? -15.493 -53.218  -56.031 1.00 40.10  ? 73  LEU F N   1 
ATOM   10680 C CA  . LEU F  2 73  ? -15.108 -51.935  -55.453 1.00 51.57  ? 73  LEU F CA  1 
ATOM   10681 C C   . LEU F  2 73  ? -16.159 -51.407  -54.481 1.00 48.02  ? 73  LEU F C   1 
ATOM   10682 O O   . LEU F  2 73  ? -16.226 -50.207  -54.217 1.00 44.26  ? 73  LEU F O   1 
ATOM   10683 C CB  . LEU F  2 73  ? -14.846 -50.905  -56.553 1.00 53.49  ? 73  LEU F CB  1 
ATOM   10684 C CG  . LEU F  2 73  ? -13.598 -51.133  -57.405 1.00 52.12  ? 73  LEU F CG  1 
ATOM   10685 C CD1 . LEU F  2 73  ? -13.550 -50.144  -58.558 1.00 49.73  ? 73  LEU F CD1 1 
ATOM   10686 C CD2 . LEU F  2 73  ? -12.345 -51.032  -56.550 1.00 47.58  ? 73  LEU F CD2 1 
ATOM   10687 N N   . GLU F  2 74  ? -16.975 -52.312  -53.951 1.00 41.22  ? 74  GLU F N   1 
ATOM   10688 C CA  . GLU F  2 74  ? -17.999 -51.946  -52.980 1.00 39.72  ? 74  GLU F CA  1 
ATOM   10689 C C   . GLU F  2 74  ? -17.989 -52.915  -51.802 1.00 46.63  ? 74  GLU F C   1 
ATOM   10690 O O   . GLU F  2 74  ? -19.032 -53.216  -51.221 1.00 39.49  ? 74  GLU F O   1 
ATOM   10691 C CB  . GLU F  2 74  ? -19.378 -51.918  -53.641 1.00 33.02  ? 74  GLU F CB  1 
ATOM   10692 C CG  . GLU F  2 74  ? -19.545 -50.814  -54.674 1.00 39.36  ? 74  GLU F CG  1 
ATOM   10693 C CD  . GLU F  2 74  ? -20.877 -50.888  -55.395 1.00 64.09  ? 74  GLU F CD  1 
ATOM   10694 O OE1 . GLU F  2 74  ? -21.246 -51.991  -55.851 1.00 58.90  ? 74  GLU F OE1 1 
ATOM   10695 O OE2 . GLU F  2 74  ? -21.550 -49.842  -55.514 1.00 45.30  ? 74  GLU F OE2 1 
ATOM   10696 N N   . LYS F  2 75  ? -16.800 -53.396  -51.453 1.00 41.88  ? 75  LYS F N   1 
ATOM   10697 C CA  . LYS F  2 75  ? -16.645 -54.359  -50.368 1.00 48.79  ? 75  LYS F CA  1 
ATOM   10698 C C   . LYS F  2 75  ? -17.077 -53.775  -49.025 1.00 42.04  ? 75  LYS F C   1 
ATOM   10699 O O   . LYS F  2 75  ? -17.536 -54.499  -48.142 1.00 39.42  ? 75  LYS F O   1 
ATOM   10700 C CB  . LYS F  2 75  ? -15.198 -54.854  -50.294 1.00 47.23  ? 75  LYS F CB  1 
ATOM   10701 C CG  . LYS F  2 75  ? -14.917 -55.790  -49.128 1.00 55.63  ? 75  LYS F CG  1 
ATOM   10702 C CD  . LYS F  2 75  ? -15.780 -57.043  -49.189 1.00 61.01  ? 75  LYS F CD  1 
ATOM   10703 C CE  . LYS F  2 75  ? -15.279 -58.019  -50.242 1.00 82.12  ? 75  LYS F CE  1 
ATOM   10704 N NZ  . LYS F  2 75  ? -16.096 -59.266  -50.271 1.00 98.73  ? 75  LYS F NZ  1 
ATOM   10705 N N   . ARG F  2 76  ? -16.933 -52.462  -48.878 1.00 47.09  ? 76  ARG F N   1 
ATOM   10706 C CA  . ARG F  2 76  ? -17.293 -51.794  -47.632 1.00 38.87  ? 76  ARG F CA  1 
ATOM   10707 C C   . ARG F  2 76  ? -18.793 -51.847  -47.355 1.00 38.84  ? 76  ARG F C   1 
ATOM   10708 O O   . ARG F  2 76  ? -19.213 -52.273  -46.280 1.00 41.03  ? 76  ARG F O   1 
ATOM   10709 C CB  . ARG F  2 76  ? -16.793 -50.349  -47.625 1.00 31.63  ? 76  ARG F CB  1 
ATOM   10710 C CG  . ARG F  2 76  ? -15.292 -50.219  -47.417 1.00 33.87  ? 76  ARG F CG  1 
ATOM   10711 C CD  . ARG F  2 76  ? -14.852 -48.770  -47.522 1.00 38.14  ? 76  ARG F CD  1 
ATOM   10712 N NE  . ARG F  2 76  ? -15.207 -48.196  -48.816 1.00 41.73  ? 76  ARG F NE  1 
ATOM   10713 C CZ  . ARG F  2 76  ? -15.576 -46.932  -48.999 1.00 38.06  ? 76  ARG F CZ  1 
ATOM   10714 N NH1 . ARG F  2 76  ? -15.643 -46.101  -47.969 1.00 43.23  ? 76  ARG F NH1 1 
ATOM   10715 N NH2 . ARG F  2 76  ? -15.882 -46.499  -50.214 1.00 33.25  ? 76  ARG F NH2 1 
ATOM   10716 N N   . ILE F  2 77  ? -19.601 -51.416  -48.320 1.00 41.43  ? 77  ILE F N   1 
ATOM   10717 C CA  . ILE F  2 77  ? -21.050 -51.477  -48.160 1.00 40.47  ? 77  ILE F CA  1 
ATOM   10718 C C   . ILE F  2 77  ? -21.533 -52.924  -48.121 1.00 37.84  ? 77  ILE F C   1 
ATOM   10719 O O   . ILE F  2 77  ? -22.541 -53.231  -47.488 1.00 36.44  ? 77  ILE F O   1 
ATOM   10720 C CB  . ILE F  2 77  ? -21.802 -50.702  -49.263 1.00 32.05  ? 77  ILE F CB  1 
ATOM   10721 C CG1 . ILE F  2 77  ? -21.143 -50.927  -50.624 1.00 52.50  ? 77  ILE F CG1 1 
ATOM   10722 C CG2 . ILE F  2 77  ? -21.846 -49.218  -48.937 1.00 39.76  ? 77  ILE F CG2 1 
ATOM   10723 C CD1 . ILE F  2 77  ? -21.786 -50.139  -51.745 1.00 54.07  ? 77  ILE F CD1 1 
ATOM   10724 N N   . GLU F  2 78  ? -20.806 -53.810  -48.795 1.00 36.00  ? 78  GLU F N   1 
ATOM   10725 C CA  . GLU F  2 78  ? -21.118 -55.233  -48.749 1.00 38.79  ? 78  GLU F CA  1 
ATOM   10726 C C   . GLU F  2 78  ? -20.971 -55.749  -47.323 1.00 40.47  ? 78  GLU F C   1 
ATOM   10727 O O   . GLU F  2 78  ? -21.766 -56.568  -46.860 1.00 40.19  ? 78  GLU F O   1 
ATOM   10728 C CB  . GLU F  2 78  ? -20.204 -56.020  -49.690 1.00 41.65  ? 78  GLU F CB  1 
ATOM   10729 C CG  . GLU F  2 78  ? -20.467 -57.519  -49.692 1.00 45.16  ? 78  GLU F CG  1 
ATOM   10730 C CD  . GLU F  2 78  ? -19.467 -58.291  -50.534 1.00 77.82  ? 78  GLU F CD  1 
ATOM   10731 O OE1 . GLU F  2 78  ? -18.917 -57.712  -51.495 1.00 93.62  ? 78  GLU F OE1 1 
ATOM   10732 O OE2 . GLU F  2 78  ? -19.235 -59.481  -50.234 1.00 85.25  ? 78  GLU F OE2 1 
ATOM   10733 N N   . ASN F  2 79  ? -19.945 -55.262  -46.632 1.00 38.48  ? 79  ASN F N   1 
ATOM   10734 C CA  . ASN F  2 79  ? -19.706 -55.638  -45.244 1.00 37.84  ? 79  ASN F CA  1 
ATOM   10735 C C   . ASN F  2 79  ? -20.656 -54.930  -44.285 1.00 40.47  ? 79  ASN F C   1 
ATOM   10736 O O   . ASN F  2 79  ? -21.050 -55.492  -43.264 1.00 48.58  ? 79  ASN F O   1 
ATOM   10737 C CB  . ASN F  2 79  ? -18.249 -55.378  -44.857 1.00 34.47  ? 79  ASN F CB  1 
ATOM   10738 C CG  . ASN F  2 79  ? -17.306 -56.423  -45.416 1.00 46.54  ? 79  ASN F CG  1 
ATOM   10739 O OD1 . ASN F  2 79  ? -17.684 -57.580  -45.600 1.00 46.44  ? 79  ASN F OD1 1 
ATOM   10740 N ND2 . ASN F  2 79  ? -16.070 -56.024  -45.686 1.00 50.76  ? 79  ASN F ND2 1 
ATOM   10741 N N   . LEU F  2 80  ? -21.020 -53.696  -44.616 1.00 26.13  ? 80  LEU F N   1 
ATOM   10742 C CA  . LEU F  2 80  ? -22.034 -52.983  -43.853 1.00 31.96  ? 80  LEU F CA  1 
ATOM   10743 C C   . LEU F  2 80  ? -23.313 -53.809  -43.901 1.00 41.68  ? 80  LEU F C   1 
ATOM   10744 O O   . LEU F  2 80  ? -23.932 -54.086  -42.872 1.00 37.12  ? 80  LEU F O   1 
ATOM   10745 C CB  . LEU F  2 80  ? -22.284 -51.598  -44.452 1.00 36.49  ? 80  LEU F CB  1 
ATOM   10746 C CG  . LEU F  2 80  ? -22.838 -50.497  -43.541 1.00 40.12  ? 80  LEU F CG  1 
ATOM   10747 C CD1 . LEU F  2 80  ? -23.564 -49.448  -44.369 1.00 24.76  ? 80  LEU F CD1 1 
ATOM   10748 C CD2 . LEU F  2 80  ? -23.754 -51.057  -42.463 1.00 39.41  ? 80  LEU F CD2 1 
ATOM   10749 N N   . ASN F  2 81  ? -23.696 -54.206  -45.111 1.00 39.62  ? 81  ASN F N   1 
ATOM   10750 C CA  . ASN F  2 81  ? -24.866 -55.049  -45.321 1.00 32.27  ? 81  ASN F CA  1 
ATOM   10751 C C   . ASN F  2 81  ? -24.768 -56.363  -44.557 1.00 54.33  ? 81  ASN F C   1 
ATOM   10752 O O   . ASN F  2 81  ? -25.732 -56.802  -43.933 1.00 39.47  ? 81  ASN F O   1 
ATOM   10753 C CB  . ASN F  2 81  ? -25.060 -55.329  -46.812 1.00 36.75  ? 81  ASN F CB  1 
ATOM   10754 C CG  . ASN F  2 81  ? -26.227 -56.258  -47.083 1.00 43.49  ? 81  ASN F CG  1 
ATOM   10755 O OD1 . ASN F  2 81  ? -27.375 -55.930  -46.789 1.00 44.30  ? 81  ASN F OD1 1 
ATOM   10756 N ND2 . ASN F  2 81  ? -25.938 -57.424  -47.649 1.00 42.50  ? 81  ASN F ND2 1 
ATOM   10757 N N   . LYS F  2 82  ? -23.599 -56.994  -44.614 1.00 34.85  ? 82  LYS F N   1 
ATOM   10758 C CA  . LYS F  2 82  ? -23.376 -58.233  -43.879 1.00 40.17  ? 82  LYS F CA  1 
ATOM   10759 C C   . LYS F  2 82  ? -23.515 -58.007  -42.378 1.00 41.44  ? 82  LYS F C   1 
ATOM   10760 O O   . LYS F  2 82  ? -23.987 -58.882  -41.652 1.00 45.45  ? 82  LYS F O   1 
ATOM   10761 C CB  . LYS F  2 82  ? -21.998 -58.817  -44.191 1.00 46.18  ? 82  LYS F CB  1 
ATOM   10762 C CG  . LYS F  2 82  ? -21.609 -59.965  -43.273 1.00 57.36  ? 82  LYS F CG  1 
ATOM   10763 C CD  . LYS F  2 82  ? -20.238 -60.521  -43.609 1.00 68.33  ? 82  LYS F CD  1 
ATOM   10764 C CE  . LYS F  2 82  ? -19.767 -61.492  -42.538 1.00 91.26  ? 82  LYS F CE  1 
ATOM   10765 N NZ  . LYS F  2 82  ? -20.739 -62.600  -42.317 1.00 80.36  ? 82  LYS F NZ  1 
ATOM   10766 N N   . LYS F  2 83  ? -23.104 -56.830  -41.916 1.00 43.03  ? 83  LYS F N   1 
ATOM   10767 C CA  . LYS F  2 83  ? -23.195 -56.505  -40.498 1.00 40.45  ? 83  LYS F CA  1 
ATOM   10768 C C   . LYS F  2 83  ? -24.644 -56.407  -40.031 1.00 38.10  ? 83  LYS F C   1 
ATOM   10769 O O   . LYS F  2 83  ? -24.996 -56.919  -38.969 1.00 46.90  ? 83  LYS F O   1 
ATOM   10770 C CB  . LYS F  2 83  ? -22.447 -55.208  -40.172 1.00 26.32  ? 83  LYS F CB  1 
ATOM   10771 C CG  . LYS F  2 83  ? -22.591 -54.799  -38.711 1.00 31.79  ? 83  LYS F CG  1 
ATOM   10772 C CD  . LYS F  2 83  ? -21.596 -53.727  -38.296 1.00 31.39  ? 83  LYS F CD  1 
ATOM   10773 C CE  . LYS F  2 83  ? -21.969 -52.365  -38.847 1.00 37.65  ? 83  LYS F CE  1 
ATOM   10774 N NZ  . LYS F  2 83  ? -21.149 -51.288  -38.224 1.00 43.61  ? 83  LYS F NZ  1 
ATOM   10775 N N   . VAL F  2 84  ? -25.484 -55.750  -40.826 1.00 40.77  ? 84  VAL F N   1 
ATOM   10776 C CA  . VAL F  2 84  ? -26.886 -55.585  -40.461 1.00 42.44  ? 84  VAL F CA  1 
ATOM   10777 C C   . VAL F  2 84  ? -27.620 -56.922  -40.499 1.00 37.75  ? 84  VAL F C   1 
ATOM   10778 O O   . VAL F  2 84  ? -28.578 -57.135  -39.756 1.00 46.63  ? 84  VAL F O   1 
ATOM   10779 C CB  . VAL F  2 84  ? -27.605 -54.554  -41.357 1.00 32.41  ? 84  VAL F CB  1 
ATOM   10780 C CG1 . VAL F  2 84  ? -27.746 -55.078  -42.778 1.00 49.18  ? 84  VAL F CG1 1 
ATOM   10781 C CG2 . VAL F  2 84  ? -28.966 -54.211  -40.774 1.00 39.46  ? 84  VAL F CG2 1 
ATOM   10782 N N   . ASP F  2 85  ? -27.161 -57.822  -41.363 1.00 36.45  ? 85  ASP F N   1 
ATOM   10783 C CA  . ASP F  2 85  ? -27.721 -59.167  -41.433 1.00 34.84  ? 85  ASP F CA  1 
ATOM   10784 C C   . ASP F  2 85  ? -27.295 -59.997  -40.227 1.00 32.33  ? 85  ASP F C   1 
ATOM   10785 O O   . ASP F  2 85  ? -28.107 -60.702  -39.629 1.00 40.96  ? 85  ASP F O   1 
ATOM   10786 C CB  . ASP F  2 85  ? -27.297 -59.868  -42.725 1.00 29.87  ? 85  ASP F CB  1 
ATOM   10787 C CG  . ASP F  2 85  ? -28.094 -59.408  -43.927 1.00 47.62  ? 85  ASP F CG  1 
ATOM   10788 O OD1 . ASP F  2 85  ? -29.126 -58.731  -43.735 1.00 46.10  ? 85  ASP F OD1 1 
ATOM   10789 O OD2 . ASP F  2 85  ? -27.693 -59.729  -45.065 1.00 63.22  ? 85  ASP F OD2 1 
ATOM   10790 N N   . ASP F  2 86  ? -26.015 -59.910  -39.876 1.00 35.06  ? 86  ASP F N   1 
ATOM   10791 C CA  . ASP F  2 86  ? -25.482 -60.653  -38.740 1.00 32.08  ? 86  ASP F CA  1 
ATOM   10792 C C   . ASP F  2 86  ? -25.998 -60.098  -37.418 1.00 38.27  ? 86  ASP F C   1 
ATOM   10793 O O   . ASP F  2 86  ? -26.055 -60.811  -36.416 1.00 37.69  ? 86  ASP F O   1 
ATOM   10794 C CB  . ASP F  2 86  ? -23.953 -60.643  -38.753 1.00 45.00  ? 86  ASP F CB  1 
ATOM   10795 C CG  . ASP F  2 86  ? -23.374 -61.565  -39.807 1.00 64.60  ? 86  ASP F CG  1 
ATOM   10796 O OD1 . ASP F  2 86  ? -24.129 -62.407  -40.339 1.00 69.76  ? 86  ASP F OD1 1 
ATOM   10797 O OD2 . ASP F  2 86  ? -22.165 -61.452  -40.100 1.00 69.79  ? 86  ASP F OD2 1 
ATOM   10798 N N   . GLY F  2 87  ? -26.369 -58.822  -37.422 1.00 39.60  ? 87  GLY F N   1 
ATOM   10799 C CA  . GLY F  2 87  ? -26.913 -58.186  -36.237 1.00 30.61  ? 87  GLY F CA  1 
ATOM   10800 C C   . GLY F  2 87  ? -28.312 -58.684  -35.938 1.00 37.65  ? 87  GLY F C   1 
ATOM   10801 O O   . GLY F  2 87  ? -28.607 -59.108  -34.820 1.00 36.77  ? 87  GLY F O   1 
ATOM   10802 N N   . PHE F  2 88  ? -29.179 -58.632  -36.944 1.00 31.93  ? 88  PHE F N   1 
ATOM   10803 C CA  . PHE F  2 88  ? -30.539 -59.134  -36.805 1.00 36.42  ? 88  PHE F CA  1 
ATOM   10804 C C   . PHE F  2 88  ? -30.528 -60.623  -36.475 1.00 34.86  ? 88  PHE F C   1 
ATOM   10805 O O   . PHE F  2 88  ? -31.358 -61.104  -35.704 1.00 43.57  ? 88  PHE F O   1 
ATOM   10806 C CB  . PHE F  2 88  ? -31.343 -58.886  -38.083 1.00 35.29  ? 88  PHE F CB  1 
ATOM   10807 C CG  . PHE F  2 88  ? -31.614 -57.433  -38.358 1.00 31.34  ? 88  PHE F CG  1 
ATOM   10808 C CD1 . PHE F  2 88  ? -31.876 -56.995  -39.647 1.00 29.77  ? 88  PHE F CD1 1 
ATOM   10809 C CD2 . PHE F  2 88  ? -31.606 -56.506  -37.330 1.00 37.73  ? 88  PHE F CD2 1 
ATOM   10810 C CE1 . PHE F  2 88  ? -32.128 -55.660  -39.903 1.00 32.18  ? 88  PHE F CE1 1 
ATOM   10811 C CE2 . PHE F  2 88  ? -31.856 -55.169  -37.580 1.00 30.56  ? 88  PHE F CE2 1 
ATOM   10812 C CZ  . PHE F  2 88  ? -32.116 -54.746  -38.868 1.00 30.73  ? 88  PHE F CZ  1 
ATOM   10813 N N   . LEU F  2 89  ? -29.579 -61.345  -37.063 1.00 30.47  ? 89  LEU F N   1 
ATOM   10814 C CA  . LEU F  2 89  ? -29.438 -62.774  -36.815 1.00 33.62  ? 89  LEU F CA  1 
ATOM   10815 C C   . LEU F  2 89  ? -29.150 -63.057  -35.344 1.00 39.38  ? 89  LEU F C   1 
ATOM   10816 O O   . LEU F  2 89  ? -29.721 -63.976  -34.758 1.00 43.08  ? 89  LEU F O   1 
ATOM   10817 C CB  . LEU F  2 89  ? -28.330 -63.366  -37.689 1.00 34.33  ? 89  LEU F CB  1 
ATOM   10818 C CG  . LEU F  2 89  ? -27.989 -64.836  -37.432 1.00 38.82  ? 89  LEU F CG  1 
ATOM   10819 C CD1 . LEU F  2 89  ? -29.239 -65.698  -37.504 1.00 42.09  ? 89  LEU F CD1 1 
ATOM   10820 C CD2 . LEU F  2 89  ? -26.936 -65.327  -38.412 1.00 38.90  ? 89  LEU F CD2 1 
ATOM   10821 N N   . ASP F  2 90  ? -28.264 -62.263  -34.752 1.00 35.76  ? 90  ASP F N   1 
ATOM   10822 C CA  . ASP F  2 90  ? -27.886 -62.449  -33.354 1.00 32.12  ? 90  ASP F CA  1 
ATOM   10823 C C   . ASP F  2 90  ? -29.002 -62.051  -32.391 1.00 31.24  ? 90  ASP F C   1 
ATOM   10824 O O   . ASP F  2 90  ? -29.222 -62.715  -31.378 1.00 39.77  ? 90  ASP F O   1 
ATOM   10825 C CB  . ASP F  2 90  ? -26.602 -61.678  -33.032 1.00 31.42  ? 90  ASP F CB  1 
ATOM   10826 C CG  . ASP F  2 90  ? -25.361 -62.359  -33.579 1.00 62.86  ? 90  ASP F CG  1 
ATOM   10827 O OD1 . ASP F  2 90  ? -25.419 -63.579  -33.844 1.00 68.30  ? 90  ASP F OD1 1 
ATOM   10828 O OD2 . ASP F  2 90  ? -24.326 -61.678  -33.739 1.00 70.41  ? 90  ASP F OD2 1 
ATOM   10829 N N   . ILE F  2 91  ? -29.703 -60.968  -32.710 1.00 31.77  ? 91  ILE F N   1 
ATOM   10830 C CA  . ILE F  2 91  ? -30.809 -60.503  -31.880 1.00 38.66  ? 91  ILE F CA  1 
ATOM   10831 C C   . ILE F  2 91  ? -31.948 -61.514  -31.857 1.00 42.23  ? 91  ILE F C   1 
ATOM   10832 O O   . ILE F  2 91  ? -32.418 -61.914  -30.791 1.00 41.79  ? 91  ILE F O   1 
ATOM   10833 C CB  . ILE F  2 91  ? -31.363 -59.155  -32.374 1.00 35.07  ? 91  ILE F CB  1 
ATOM   10834 C CG1 . ILE F  2 91  ? -30.307 -58.058  -32.236 1.00 29.52  ? 91  ILE F CG1 1 
ATOM   10835 C CG2 . ILE F  2 91  ? -32.618 -58.782  -31.599 1.00 38.80  ? 91  ILE F CG2 1 
ATOM   10836 C CD1 . ILE F  2 91  ? -30.757 -56.711  -32.760 1.00 45.36  ? 91  ILE F CD1 1 
ATOM   10837 N N   . TRP F  2 92  ? -32.389 -61.925  -33.041 1.00 31.85  ? 92  TRP F N   1 
ATOM   10838 C CA  . TRP F  2 92  ? -33.518 -62.840  -33.159 1.00 29.91  ? 92  TRP F CA  1 
ATOM   10839 C C   . TRP F  2 92  ? -33.230 -64.223  -32.585 1.00 37.96  ? 92  TRP F C   1 
ATOM   10840 O O   . TRP F  2 92  ? -34.085 -64.815  -31.926 1.00 41.31  ? 92  TRP F O   1 
ATOM   10841 C CB  . TRP F  2 92  ? -33.985 -62.939  -34.613 1.00 30.18  ? 92  TRP F CB  1 
ATOM   10842 C CG  . TRP F  2 92  ? -34.787 -61.753  -35.035 1.00 36.91  ? 92  TRP F CG  1 
ATOM   10843 C CD1 . TRP F  2 92  ? -34.448 -60.820  -35.972 1.00 31.98  ? 92  TRP F CD1 1 
ATOM   10844 C CD2 . TRP F  2 92  ? -36.059 -61.356  -34.513 1.00 35.62  ? 92  TRP F CD2 1 
ATOM   10845 N NE1 . TRP F  2 92  ? -35.438 -59.873  -36.074 1.00 40.83  ? 92  TRP F NE1 1 
ATOM   10846 C CE2 . TRP F  2 92  ? -36.438 -60.179  -35.188 1.00 34.06  ? 92  TRP F CE2 1 
ATOM   10847 C CE3 . TRP F  2 92  ? -36.917 -61.885  -33.545 1.00 37.01  ? 92  TRP F CE3 1 
ATOM   10848 C CZ2 . TRP F  2 92  ? -37.639 -59.523  -34.927 1.00 33.16  ? 92  TRP F CZ2 1 
ATOM   10849 C CZ3 . TRP F  2 92  ? -38.108 -61.232  -33.286 1.00 44.46  ? 92  TRP F CZ3 1 
ATOM   10850 C CH2 . TRP F  2 92  ? -38.458 -60.063  -33.973 1.00 41.47  ? 92  TRP F CH2 1 
ATOM   10851 N N   . THR F  2 93  ? -32.030 -64.734  -32.833 1.00 38.29  ? 93  THR F N   1 
ATOM   10852 C CA  . THR F  2 93  ? -31.637 -66.025  -32.284 1.00 41.07  ? 93  THR F CA  1 
ATOM   10853 C C   . THR F  2 93  ? -31.672 -65.989  -30.761 1.00 40.36  ? 93  THR F C   1 
ATOM   10854 O O   . THR F  2 93  ? -32.282 -66.847  -30.124 1.00 40.51  ? 93  THR F O   1 
ATOM   10855 C CB  . THR F  2 93  ? -30.230 -66.441  -32.749 1.00 37.68  ? 93  THR F CB  1 
ATOM   10856 O OG1 . THR F  2 93  ? -30.228 -66.632  -34.169 1.00 38.90  ? 93  THR F OG1 1 
ATOM   10857 C CG2 . THR F  2 93  ? -29.813 -67.735  -32.073 1.00 33.80  ? 93  THR F CG2 1 
ATOM   10858 N N   . TYR F  2 94  ? -31.021 -64.985  -30.182 1.00 40.47  ? 94  TYR F N   1 
ATOM   10859 C CA  . TYR F  2 94  ? -30.950 -64.855  -28.731 1.00 37.59  ? 94  TYR F CA  1 
ATOM   10860 C C   . TYR F  2 94  ? -32.332 -64.678  -28.110 1.00 38.43  ? 94  TYR F C   1 
ATOM   10861 O O   . TYR F  2 94  ? -32.677 -65.360  -27.145 1.00 40.71  ? 94  TYR F O   1 
ATOM   10862 C CB  . TYR F  2 94  ? -30.039 -63.690  -28.337 1.00 34.86  ? 94  TYR F CB  1 
ATOM   10863 C CG  . TYR F  2 94  ? -29.742 -63.619  -26.855 1.00 38.90  ? 94  TYR F CG  1 
ATOM   10864 C CD1 . TYR F  2 94  ? -28.841 -64.496  -26.267 1.00 38.75  ? 94  TYR F CD1 1 
ATOM   10865 C CD2 . TYR F  2 94  ? -30.358 -62.674  -26.046 1.00 33.77  ? 94  TYR F CD2 1 
ATOM   10866 C CE1 . TYR F  2 94  ? -28.563 -64.437  -24.916 1.00 41.06  ? 94  TYR F CE1 1 
ATOM   10867 C CE2 . TYR F  2 94  ? -30.087 -62.607  -24.693 1.00 35.38  ? 94  TYR F CE2 1 
ATOM   10868 C CZ  . TYR F  2 94  ? -29.189 -63.491  -24.134 1.00 46.11  ? 94  TYR F CZ  1 
ATOM   10869 O OH  . TYR F  2 94  ? -28.914 -63.429  -22.787 1.00 55.47  ? 94  TYR F OH  1 
ATOM   10870 N N   . ASN F  2 95  ? -33.119 -63.762  -28.664 1.00 36.61  ? 95  ASN F N   1 
ATOM   10871 C CA  . ASN F  2 95  ? -34.455 -63.495  -28.140 1.00 37.76  ? 95  ASN F CA  1 
ATOM   10872 C C   . ASN F  2 95  ? -35.383 -64.700  -28.244 1.00 39.88  ? 95  ASN F C   1 
ATOM   10873 O O   . ASN F  2 95  ? -36.106 -65.018  -27.301 1.00 38.91  ? 95  ASN F O   1 
ATOM   10874 C CB  . ASN F  2 95  ? -35.080 -62.280  -28.830 1.00 42.07  ? 95  ASN F CB  1 
ATOM   10875 C CG  . ASN F  2 95  ? -34.421 -60.977  -28.425 1.00 54.90  ? 95  ASN F CG  1 
ATOM   10876 O OD1 . ASN F  2 95  ? -33.328 -60.970  -27.858 1.00 47.36  ? 95  ASN F OD1 1 
ATOM   10877 N ND2 . ASN F  2 95  ? -35.085 -59.863  -28.713 1.00 52.41  ? 95  ASN F ND2 1 
ATOM   10878 N N   . ALA F  2 96  ? -35.359 -65.368  -29.393 1.00 38.79  ? 96  ALA F N   1 
ATOM   10879 C CA  . ALA F  2 96  ? -36.200 -66.538  -29.613 1.00 43.46  ? 96  ALA F CA  1 
ATOM   10880 C C   . ALA F  2 96  ? -35.843 -67.668  -28.651 1.00 46.99  ? 96  ALA F C   1 
ATOM   10881 O O   . ALA F  2 96  ? -36.724 -68.303  -28.069 1.00 46.48  ? 96  ALA F O   1 
ATOM   10882 C CB  . ALA F  2 96  ? -36.091 -67.010  -31.056 1.00 40.55  ? 96  ALA F CB  1 
ATOM   10883 N N   . GLU F  2 97  ? -34.546 -67.912  -28.487 1.00 39.80  ? 97  GLU F N   1 
ATOM   10884 C CA  . GLU F  2 97  ? -34.065 -68.948  -27.580 1.00 43.34  ? 97  GLU F CA  1 
ATOM   10885 C C   . GLU F  2 97  ? -34.498 -68.665  -26.144 1.00 43.81  ? 97  GLU F C   1 
ATOM   10886 O O   . GLU F  2 97  ? -35.010 -69.547  -25.455 1.00 50.25  ? 97  GLU F O   1 
ATOM   10887 C CB  . GLU F  2 97  ? -32.541 -69.064  -27.658 1.00 51.93  ? 97  GLU F CB  1 
ATOM   10888 C CG  . GLU F  2 97  ? -32.012 -69.602  -28.982 1.00 43.83  ? 97  GLU F CG  1 
ATOM   10889 C CD  . GLU F  2 97  ? -32.164 -71.106  -29.111 1.00 57.71  ? 97  GLU F CD  1 
ATOM   10890 O OE1 . GLU F  2 97  ? -31.477 -71.701  -29.968 1.00 59.92  ? 97  GLU F OE1 1 
ATOM   10891 O OE2 . GLU F  2 97  ? -32.961 -71.696  -28.353 1.00 79.29  ? 97  GLU F OE2 1 
ATOM   10892 N N   . LEU F  2 98  ? -34.291 -67.429  -25.701 1.00 34.78  ? 98  LEU F N   1 
ATOM   10893 C CA  . LEU F  2 98  ? -34.668 -67.019  -24.351 1.00 36.95  ? 98  LEU F CA  1 
ATOM   10894 C C   . LEU F  2 98  ? -36.181 -67.006  -24.153 1.00 45.63  ? 98  LEU F C   1 
ATOM   10895 O O   . LEU F  2 98  ? -36.677 -67.361  -23.084 1.00 40.41  ? 98  LEU F O   1 
ATOM   10896 C CB  . LEU F  2 98  ? -34.089 -65.640  -24.028 1.00 36.52  ? 98  LEU F CB  1 
ATOM   10897 C CG  . LEU F  2 98  ? -32.742 -65.584  -23.301 1.00 45.39  ? 98  LEU F CG  1 
ATOM   10898 C CD1 . LEU F  2 98  ? -32.906 -65.831  -21.807 1.00 61.22  ? 98  LEU F CD1 1 
ATOM   10899 C CD2 . LEU F  2 98  ? -31.738 -66.555  -23.909 1.00 50.79  ? 98  LEU F CD2 1 
ATOM   10900 N N   . LEU F  2 99  ? -36.910 -66.590  -25.185 1.00 40.74  ? 99  LEU F N   1 
ATOM   10901 C CA  . LEU F  2 99  ? -38.365 -66.526  -25.113 1.00 46.59  ? 99  LEU F CA  1 
ATOM   10902 C C   . LEU F  2 99  ? -38.958 -67.899  -24.825 1.00 42.42  ? 99  LEU F C   1 
ATOM   10903 O O   . LEU F  2 99  ? -39.837 -68.039  -23.975 1.00 45.77  ? 99  LEU F O   1 
ATOM   10904 C CB  . LEU F  2 99  ? -38.950 -65.970  -26.413 1.00 49.10  ? 99  LEU F CB  1 
ATOM   10905 C CG  . LEU F  2 99  ? -40.477 -65.865  -26.446 1.00 45.62  ? 99  LEU F CG  1 
ATOM   10906 C CD1 . LEU F  2 99  ? -40.963 -64.884  -25.389 1.00 47.83  ? 99  LEU F CD1 1 
ATOM   10907 C CD2 . LEU F  2 99  ? -40.973 -65.461  -27.826 1.00 49.54  ? 99  LEU F CD2 1 
ATOM   10908 N N   . VAL F  2 100 ? -38.475 -68.908  -25.540 1.00 35.22  ? 100 VAL F N   1 
ATOM   10909 C CA  . VAL F  2 100 ? -38.948 -70.274  -25.352 1.00 43.51  ? 100 VAL F CA  1 
ATOM   10910 C C   . VAL F  2 100 ? -38.619 -70.784  -23.953 1.00 47.24  ? 100 VAL F C   1 
ATOM   10911 O O   . VAL F  2 100 ? -39.483 -71.326  -23.264 1.00 52.34  ? 100 VAL F O   1 
ATOM   10912 C CB  . VAL F  2 100 ? -38.352 -71.230  -26.401 1.00 45.22  ? 100 VAL F CB  1 
ATOM   10913 C CG1 . VAL F  2 100 ? -38.644 -72.675  -26.030 1.00 49.09  ? 100 VAL F CG1 1 
ATOM   10914 C CG2 . VAL F  2 100 ? -38.898 -70.906  -27.784 1.00 40.41  ? 100 VAL F CG2 1 
ATOM   10915 N N   . LEU F  2 101 ? -37.368 -70.607  -23.536 1.00 45.66  ? 101 LEU F N   1 
ATOM   10916 C CA  . LEU F  2 101 ? -36.945 -71.025  -22.204 1.00 47.00  ? 101 LEU F CA  1 
ATOM   10917 C C   . LEU F  2 101 ? -37.820 -70.387  -21.134 1.00 46.64  ? 101 LEU F C   1 
ATOM   10918 O O   . LEU F  2 101 ? -38.402 -71.079  -20.300 1.00 53.45  ? 101 LEU F O   1 
ATOM   10919 C CB  . LEU F  2 101 ? -35.481 -70.658  -21.951 1.00 42.56  ? 101 LEU F CB  1 
ATOM   10920 C CG  . LEU F  2 101 ? -34.426 -71.327  -22.832 1.00 44.43  ? 101 LEU F CG  1 
ATOM   10921 C CD1 . LEU F  2 101 ? -33.033 -71.008  -22.317 1.00 46.68  ? 101 LEU F CD1 1 
ATOM   10922 C CD2 . LEU F  2 101 ? -34.645 -72.825  -22.879 1.00 41.22  ? 101 LEU F CD2 1 
ATOM   10923 N N   . LEU F  2 102 ? -37.904 -69.062  -21.163 1.00 44.31  ? 102 LEU F N   1 
ATOM   10924 C CA  . LEU F  2 102 ? -38.713 -68.325  -20.201 1.00 48.44  ? 102 LEU F CA  1 
ATOM   10925 C C   . LEU F  2 102 ? -40.159 -68.808  -20.185 1.00 49.42  ? 102 LEU F C   1 
ATOM   10926 O O   . LEU F  2 102 ? -40.712 -69.092  -19.124 1.00 47.69  ? 102 LEU F O   1 
ATOM   10927 C CB  . LEU F  2 102 ? -38.663 -66.827  -20.500 1.00 44.55  ? 102 LEU F CB  1 
ATOM   10928 C CG  . LEU F  2 102 ? -37.681 -65.985  -19.679 1.00 62.19  ? 102 LEU F CG  1 
ATOM   10929 C CD1 . LEU F  2 102 ? -36.365 -66.712  -19.436 1.00 57.20  ? 102 LEU F CD1 1 
ATOM   10930 C CD2 . LEU F  2 102 ? -37.453 -64.629  -20.334 1.00 88.83  ? 102 LEU F CD2 1 
ATOM   10931 N N   . GLU F  2 103 ? -40.765 -68.908  -21.363 1.00 41.46  ? 103 GLU F N   1 
ATOM   10932 C CA  . GLU F  2 103 ? -42.169 -69.298  -21.468 1.00 46.34  ? 103 GLU F CA  1 
ATOM   10933 C C   . GLU F  2 103 ? -42.431 -70.739  -21.041 1.00 47.66  ? 103 GLU F C   1 
ATOM   10934 O O   . GLU F  2 103 ? -43.457 -71.028  -20.428 1.00 57.68  ? 103 GLU F O   1 
ATOM   10935 C CB  . GLU F  2 103 ? -42.702 -69.055  -22.882 1.00 41.94  ? 103 GLU F CB  1 
ATOM   10936 C CG  . GLU F  2 103 ? -42.928 -67.588  -23.201 1.00 60.80  ? 103 GLU F CG  1 
ATOM   10937 C CD  . GLU F  2 103 ? -43.702 -66.870  -22.111 1.00 74.10  ? 103 GLU F CD  1 
ATOM   10938 O OE1 . GLU F  2 103 ? -44.939 -67.025  -22.053 1.00 72.78  ? 103 GLU F OE1 1 
ATOM   10939 O OE2 . GLU F  2 103 ? -43.071 -66.147  -21.312 1.00 79.02  ? 103 GLU F OE2 1 
ATOM   10940 N N   . ASN F  2 104 ? -41.513 -71.642  -21.371 1.00 38.50  ? 104 ASN F N   1 
ATOM   10941 C CA  . ASN F  2 104 ? -41.639 -73.034  -20.953 1.00 46.40  ? 104 ASN F CA  1 
ATOM   10942 C C   . ASN F  2 104 ? -41.677 -73.159  -19.434 1.00 54.06  ? 104 ASN F C   1 
ATOM   10943 O O   . ASN F  2 104 ? -42.472 -73.918  -18.882 1.00 56.98  ? 104 ASN F O   1 
ATOM   10944 C CB  . ASN F  2 104 ? -40.504 -73.882  -21.529 1.00 36.90  ? 104 ASN F CB  1 
ATOM   10945 C CG  . ASN F  2 104 ? -40.702 -74.201  -22.996 1.00 44.71  ? 104 ASN F CG  1 
ATOM   10946 O OD1 . ASN F  2 104 ? -41.759 -73.930  -23.564 1.00 39.48  ? 104 ASN F OD1 1 
ATOM   10947 N ND2 . ASN F  2 104 ? -39.685 -74.785  -23.619 1.00 52.51  ? 104 ASN F ND2 1 
ATOM   10948 N N   . GLU F  2 105 ? -40.812 -72.406  -18.763 1.00 48.51  ? 105 GLU F N   1 
ATOM   10949 C CA  . GLU F  2 105 ? -40.783 -72.385  -17.308 1.00 45.77  ? 105 GLU F CA  1 
ATOM   10950 C C   . GLU F  2 105 ? -42.132 -71.931  -16.767 1.00 48.90  ? 105 GLU F C   1 
ATOM   10951 O O   . GLU F  2 105 ? -42.634 -72.469  -15.778 1.00 67.80  ? 105 GLU F O   1 
ATOM   10952 C CB  . GLU F  2 105 ? -39.683 -71.447  -16.814 1.00 50.92  ? 105 GLU F CB  1 
ATOM   10953 C CG  . GLU F  2 105 ? -39.592 -71.364  -15.305 1.00 61.80  ? 105 GLU F CG  1 
ATOM   10954 C CD  . GLU F  2 105 ? -39.466 -72.730  -14.665 1.00 106.30 ? 105 GLU F CD  1 
ATOM   10955 O OE1 . GLU F  2 105 ? -38.784 -73.599  -15.249 1.00 100.44 ? 105 GLU F OE1 1 
ATOM   10956 O OE2 . GLU F  2 105 ? -40.053 -72.938  -13.582 1.00 112.85 ? 105 GLU F OE2 1 
ATOM   10957 N N   . ARG F  2 106 ? -42.710 -70.937  -17.435 1.00 49.57  ? 106 ARG F N   1 
ATOM   10958 C CA  . ARG F  2 106 ? -43.999 -70.373  -17.051 1.00 48.22  ? 106 ARG F CA  1 
ATOM   10959 C C   . ARG F  2 106 ? -45.128 -71.368  -17.275 1.00 53.19  ? 106 ARG F C   1 
ATOM   10960 O O   . ARG F  2 106 ? -46.024 -71.496  -16.443 1.00 58.64  ? 106 ARG F O   1 
ATOM   10961 C CB  . ARG F  2 106 ? -44.283 -69.109  -17.864 1.00 49.06  ? 106 ARG F CB  1 
ATOM   10962 C CG  . ARG F  2 106 ? -43.107 -68.146  -17.977 1.00 59.04  ? 106 ARG F CG  1 
ATOM   10963 C CD  . ARG F  2 106 ? -43.386 -66.845  -17.239 1.00 74.32  ? 106 ARG F CD  1 
ATOM   10964 N NE  . ARG F  2 106 ? -44.731 -66.835  -16.670 1.00 75.39  ? 106 ARG F NE  1 
ATOM   10965 C CZ  . ARG F  2 106 ? -45.029 -66.430  -15.439 1.00 84.11  ? 106 ARG F CZ  1 
ATOM   10966 N NH1 . ARG F  2 106 ? -44.070 -65.982  -14.635 1.00 88.35  ? 106 ARG F NH1 1 
ATOM   10967 N NH2 . ARG F  2 106 ? -46.290 -66.465  -15.018 1.00 82.79  ? 106 ARG F NH2 1 
ATOM   10968 N N   . THR F  2 107 ? -45.081 -72.061  -18.409 1.00 52.10  ? 107 THR F N   1 
ATOM   10969 C CA  . THR F  2 107 ? -46.122 -73.015  -18.781 1.00 57.01  ? 107 THR F CA  1 
ATOM   10970 C C   . THR F  2 107 ? -46.210 -74.171  -17.788 1.00 62.29  ? 107 THR F C   1 
ATOM   10971 O O   . THR F  2 107 ? -47.303 -74.599  -17.412 1.00 58.69  ? 107 THR F O   1 
ATOM   10972 C CB  . THR F  2 107 ? -45.891 -73.574  -20.202 1.00 57.24  ? 107 THR F CB  1 
ATOM   10973 O OG1 . THR F  2 107 ? -45.916 -72.500  -21.150 1.00 51.07  ? 107 THR F OG1 1 
ATOM   10974 C CG2 . THR F  2 107 ? -46.964 -74.590  -20.565 1.00 53.63  ? 107 THR F CG2 1 
ATOM   10975 N N   . LEU F  2 108 ? -45.055 -74.676  -17.369 1.00 50.64  ? 108 LEU F N   1 
ATOM   10976 C CA  . LEU F  2 108 ? -45.007 -75.753  -16.390 1.00 48.80  ? 108 LEU F CA  1 
ATOM   10977 C C   . LEU F  2 108 ? -45.515 -75.279  -15.032 1.00 54.39  ? 108 LEU F C   1 
ATOM   10978 O O   . LEU F  2 108 ? -46.256 -75.991  -14.356 1.00 57.14  ? 108 LEU F O   1 
ATOM   10979 C CB  . LEU F  2 108 ? -43.587 -76.310  -16.272 1.00 48.86  ? 108 LEU F CB  1 
ATOM   10980 C CG  . LEU F  2 108 ? -43.032 -76.961  -17.540 1.00 48.61  ? 108 LEU F CG  1 
ATOM   10981 C CD1 . LEU F  2 108 ? -41.683 -77.609  -17.270 1.00 44.48  ? 108 LEU F CD1 1 
ATOM   10982 C CD2 . LEU F  2 108 ? -44.017 -77.981  -18.091 1.00 52.37  ? 108 LEU F CD2 1 
ATOM   10983 N N   . ASP F  2 109 ? -45.114 -74.074  -14.638 1.00 50.10  ? 109 ASP F N   1 
ATOM   10984 C CA  . ASP F  2 109 ? -45.584 -73.486  -13.389 1.00 52.61  ? 109 ASP F CA  1 
ATOM   10985 C C   . ASP F  2 109 ? -47.087 -73.227  -13.442 1.00 56.49  ? 109 ASP F C   1 
ATOM   10986 O O   . ASP F  2 109 ? -47.776 -73.302  -12.425 1.00 60.17  ? 109 ASP F O   1 
ATOM   10987 C CB  . ASP F  2 109 ? -44.833 -72.188  -13.085 1.00 60.15  ? 109 ASP F CB  1 
ATOM   10988 C CG  . ASP F  2 109 ? -43.412 -72.433  -12.619 1.00 79.34  ? 109 ASP F CG  1 
ATOM   10989 O OD1 . ASP F  2 109 ? -43.079 -73.595  -12.305 1.00 75.34  ? 109 ASP F OD1 1 
ATOM   10990 O OD2 . ASP F  2 109 ? -42.628 -71.462  -12.561 1.00 82.75  ? 109 ASP F OD2 1 
ATOM   10991 N N   . TYR F  2 110 ? -47.586 -72.923  -14.636 1.00 51.13  ? 110 TYR F N   1 
ATOM   10992 C CA  . TYR F  2 110 ? -49.012 -72.701  -14.840 1.00 48.74  ? 110 TYR F CA  1 
ATOM   10993 C C   . TYR F  2 110 ? -49.802 -73.980  -14.581 1.00 58.13  ? 110 TYR F C   1 
ATOM   10994 O O   . TYR F  2 110 ? -50.807 -73.966  -13.870 1.00 47.57  ? 110 TYR F O   1 
ATOM   10995 C CB  . TYR F  2 110 ? -49.278 -72.189  -16.257 1.00 43.38  ? 110 TYR F CB  1 
ATOM   10996 C CG  . TYR F  2 110 ? -50.743 -72.141  -16.631 1.00 41.25  ? 110 TYR F CG  1 
ATOM   10997 C CD1 . TYR F  2 110 ? -51.531 -71.046  -16.299 1.00 38.98  ? 110 TYR F CD1 1 
ATOM   10998 C CD2 . TYR F  2 110 ? -51.337 -73.192  -17.318 1.00 47.34  ? 110 TYR F CD2 1 
ATOM   10999 C CE1 . TYR F  2 110 ? -52.870 -71.001  -16.640 1.00 46.71  ? 110 TYR F CE1 1 
ATOM   11000 C CE2 . TYR F  2 110 ? -52.674 -73.155  -17.662 1.00 55.37  ? 110 TYR F CE2 1 
ATOM   11001 C CZ  . TYR F  2 110 ? -53.435 -72.058  -17.321 1.00 56.10  ? 110 TYR F CZ  1 
ATOM   11002 O OH  . TYR F  2 110 ? -54.767 -72.020  -17.664 1.00 63.69  ? 110 TYR F OH  1 
ATOM   11003 N N   . HIS F  2 111 ? -49.343 -75.083  -15.163 1.00 48.65  ? 111 HIS F N   1 
ATOM   11004 C CA  . HIS F  2 111 ? -49.982 -76.377  -14.953 1.00 52.63  ? 111 HIS F CA  1 
ATOM   11005 C C   . HIS F  2 111 ? -49.855 -76.815  -13.500 1.00 61.49  ? 111 HIS F C   1 
ATOM   11006 O O   . HIS F  2 111 ? -50.827 -77.256  -12.888 1.00 54.00  ? 111 HIS F O   1 
ATOM   11007 C CB  . HIS F  2 111 ? -49.378 -77.437  -15.876 1.00 48.05  ? 111 HIS F CB  1 
ATOM   11008 C CG  . HIS F  2 111 ? -49.752 -77.269  -17.315 1.00 57.65  ? 111 HIS F CG  1 
ATOM   11009 N ND1 . HIS F  2 111 ? -51.039 -77.446  -17.773 1.00 62.95  ? 111 HIS F ND1 1 
ATOM   11010 C CD2 . HIS F  2 111 ? -49.007 -76.951  -18.400 1.00 65.37  ? 111 HIS F CD2 1 
ATOM   11011 C CE1 . HIS F  2 111 ? -51.073 -77.237  -19.077 1.00 68.01  ? 111 HIS F CE1 1 
ATOM   11012 N NE2 . HIS F  2 111 ? -49.853 -76.937  -19.482 1.00 65.42  ? 111 HIS F NE2 1 
ATOM   11013 N N   . ASP F  2 112 ? -48.649 -76.693  -12.957 1.00 54.63  ? 112 ASP F N   1 
ATOM   11014 C CA  . ASP F  2 112 ? -48.398 -77.021  -11.560 1.00 46.45  ? 112 ASP F CA  1 
ATOM   11015 C C   . ASP F  2 112 ? -49.391 -76.284  -10.670 1.00 51.18  ? 112 ASP F C   1 
ATOM   11016 O O   . ASP F  2 112 ? -49.912 -76.841  -9.704  1.00 58.14  ? 112 ASP F O   1 
ATOM   11017 C CB  . ASP F  2 112 ? -46.968 -76.639  -11.176 1.00 63.28  ? 112 ASP F CB  1 
ATOM   11018 C CG  . ASP F  2 112 ? -46.574 -77.153  -9.806  1.00 71.73  ? 112 ASP F CG  1 
ATOM   11019 O OD1 . ASP F  2 112 ? -45.596 -76.631  -9.232  1.00 75.71  ? 112 ASP F OD1 1 
ATOM   11020 O OD2 . ASP F  2 112 ? -47.242 -78.079  -9.304  1.00 73.11  ? 112 ASP F OD2 1 
ATOM   11021 N N   . SER F  2 113 ? -49.649 -75.027  -11.014 1.00 58.27  ? 113 SER F N   1 
ATOM   11022 C CA  . SER F  2 113 ? -50.569 -74.186  -10.258 1.00 52.02  ? 113 SER F CA  1 
ATOM   11023 C C   . SER F  2 113 ? -51.992 -74.735  -10.262 1.00 60.02  ? 113 SER F C   1 
ATOM   11024 O O   . SER F  2 113 ? -52.629 -74.835  -9.214  1.00 63.97  ? 113 SER F O   1 
ATOM   11025 C CB  . SER F  2 113 ? -50.562 -72.763  -10.817 1.00 47.57  ? 113 SER F CB  1 
ATOM   11026 O OG  . SER F  2 113 ? -51.626 -72.001  -10.278 1.00 67.05  ? 113 SER F OG  1 
ATOM   11027 N N   . ASN F  2 114 ? -52.486 -75.085  -11.444 1.00 56.00  ? 114 ASN F N   1 
ATOM   11028 C CA  . ASN F  2 114 ? -53.849 -75.587  -11.582 1.00 67.28  ? 114 ASN F CA  1 
ATOM   11029 C C   . ASN F  2 114 ? -54.100 -76.847  -10.758 1.00 66.86  ? 114 ASN F C   1 
ATOM   11030 O O   . ASN F  2 114 ? -55.183 -77.030  -10.203 1.00 58.39  ? 114 ASN F O   1 
ATOM   11031 C CB  . ASN F  2 114 ? -54.184 -75.831  -13.055 1.00 59.52  ? 114 ASN F CB  1 
ATOM   11032 C CG  . ASN F  2 114 ? -54.189 -74.551  -13.868 1.00 65.54  ? 114 ASN F CG  1 
ATOM   11033 O OD1 . ASN F  2 114 ? -54.320 -73.456  -13.322 1.00 77.75  ? 114 ASN F OD1 1 
ATOM   11034 N ND2 . ASN F  2 114 ? -54.046 -74.684  -15.181 1.00 65.86  ? 114 ASN F ND2 1 
ATOM   11035 N N   . VAL F  2 115 ? -53.094 -77.712  -10.684 1.00 60.92  ? 115 VAL F N   1 
ATOM   11036 C CA  . VAL F  2 115 ? -53.180 -78.911  -9.859  1.00 62.48  ? 115 VAL F CA  1 
ATOM   11037 C C   . VAL F  2 115 ? -53.315 -78.526  -8.390  1.00 60.87  ? 115 VAL F C   1 
ATOM   11038 O O   . VAL F  2 115 ? -54.260 -78.934  -7.715  1.00 61.92  ? 115 VAL F O   1 
ATOM   11039 C CB  . VAL F  2 115 ? -51.942 -79.808  -10.036 1.00 57.50  ? 115 VAL F CB  1 
ATOM   11040 C CG1 . VAL F  2 115 ? -51.961 -80.945  -9.027  1.00 67.03  ? 115 VAL F CG1 1 
ATOM   11041 C CG2 . VAL F  2 115 ? -51.878 -80.347  -11.456 1.00 51.45  ? 115 VAL F CG2 1 
ATOM   11042 N N   . LYS F  2 116 ? -52.362 -77.736  -7.906  1.00 60.69  ? 116 LYS F N   1 
ATOM   11043 C CA  . LYS F  2 116 ? -52.380 -77.233  -6.537  1.00 65.80  ? 116 LYS F CA  1 
ATOM   11044 C C   . LYS F  2 116 ? -53.732 -76.618  -6.190  1.00 62.09  ? 116 LYS F C   1 
ATOM   11045 O O   . LYS F  2 116 ? -54.272 -76.849  -5.108  1.00 72.42  ? 116 LYS F O   1 
ATOM   11046 C CB  . LYS F  2 116 ? -51.274 -76.192  -6.348  1.00 63.50  ? 116 LYS F CB  1 
ATOM   11047 C CG  . LYS F  2 116 ? -51.379 -75.375  -5.068  1.00 59.66  ? 116 LYS F CG  1 
ATOM   11048 C CD  . LYS F  2 116 ? -50.542 -75.968  -3.948  1.00 76.76  ? 116 LYS F CD  1 
ATOM   11049 C CE  . LYS F  2 116 ? -50.440 -75.001  -2.777  1.00 86.21  ? 116 LYS F CE  1 
ATOM   11050 N NZ  . LYS F  2 116 ? -49.471 -75.463  -1.746  1.00 101.85 ? 116 LYS F NZ  1 
ATOM   11051 N N   . ASN F  2 117 ? -54.271 -75.832  -7.116  1.00 48.66  ? 117 ASN F N   1 
ATOM   11052 C CA  . ASN F  2 117 ? -55.562 -75.185  -6.917  1.00 61.97  ? 117 ASN F CA  1 
ATOM   11053 C C   . ASN F  2 117 ? -56.708 -76.184  -6.845  1.00 70.68  ? 117 ASN F C   1 
ATOM   11054 O O   . ASN F  2 117 ? -57.632 -76.025  -6.049  1.00 74.92  ? 117 ASN F O   1 
ATOM   11055 C CB  . ASN F  2 117 ? -55.829 -74.159  -8.020  1.00 60.81  ? 117 ASN F CB  1 
ATOM   11056 C CG  . ASN F  2 117 ? -55.029 -72.887  -7.836  1.00 65.35  ? 117 ASN F CG  1 
ATOM   11057 O OD1 . ASN F  2 117 ? -54.430 -72.664  -6.784  1.00 66.78  ? 117 ASN F OD1 1 
ATOM   11058 N ND2 . ASN F  2 117 ? -55.019 -72.040  -8.859  1.00 80.25  ? 117 ASN F ND2 1 
ATOM   11059 N N   . LEU F  2 118 ? -56.646 -77.213  -7.683  1.00 65.96  ? 118 LEU F N   1 
ATOM   11060 C CA  . LEU F  2 118 ? -57.667 -78.249  -7.677  1.00 66.11  ? 118 LEU F CA  1 
ATOM   11061 C C   . LEU F  2 118 ? -57.631 -78.973  -6.339  1.00 70.66  ? 118 LEU F C   1 
ATOM   11062 O O   . LEU F  2 118 ? -58.668 -79.244  -5.737  1.00 85.12  ? 118 LEU F O   1 
ATOM   11063 C CB  . LEU F  2 118 ? -57.439 -79.235  -8.823  1.00 69.68  ? 118 LEU F CB  1 
ATOM   11064 C CG  . LEU F  2 118 ? -58.704 -79.847  -9.425  1.00 77.65  ? 118 LEU F CG  1 
ATOM   11065 C CD1 . LEU F  2 118 ? -59.692 -78.748  -9.783  1.00 68.58  ? 118 LEU F CD1 1 
ATOM   11066 C CD2 . LEU F  2 118 ? -58.370 -80.695  -10.643 1.00 81.70  ? 118 LEU F CD2 1 
ATOM   11067 N N   . TYR F  2 119 ? -56.422 -79.274  -5.879  1.00 68.63  ? 119 TYR F N   1 
ATOM   11068 C CA  . TYR F  2 119 ? -56.221 -79.929  -4.594  1.00 68.52  ? 119 TYR F CA  1 
ATOM   11069 C C   . TYR F  2 119 ? -56.773 -79.081  -3.458  1.00 70.15  ? 119 TYR F C   1 
ATOM   11070 O O   . TYR F  2 119 ? -57.540 -79.562  -2.624  1.00 78.12  ? 119 TYR F O   1 
ATOM   11071 C CB  . TYR F  2 119 ? -54.734 -80.193  -4.367  1.00 74.21  ? 119 TYR F CB  1 
ATOM   11072 C CG  . TYR F  2 119 ? -54.420 -80.786  -3.017  1.00 81.45  ? 119 TYR F CG  1 
ATOM   11073 C CD1 . TYR F  2 119 ? -54.361 -82.160  -2.840  1.00 81.35  ? 119 TYR F CD1 1 
ATOM   11074 C CD2 . TYR F  2 119 ? -54.179 -79.972  -1.918  1.00 79.14  ? 119 TYR F CD2 1 
ATOM   11075 C CE1 . TYR F  2 119 ? -54.072 -82.708  -1.611  1.00 90.07  ? 119 TYR F CE1 1 
ATOM   11076 C CE2 . TYR F  2 119 ? -53.891 -80.510  -0.683  1.00 99.63  ? 119 TYR F CE2 1 
ATOM   11077 C CZ  . TYR F  2 119 ? -53.838 -81.878  -0.536  1.00 102.55 ? 119 TYR F CZ  1 
ATOM   11078 O OH  . TYR F  2 119 ? -53.553 -82.420  0.692   1.00 110.41 ? 119 TYR F OH  1 
ATOM   11079 N N   . GLU F  2 120 ? -56.369 -77.817  -3.426  1.00 72.99  ? 120 GLU F N   1 
ATOM   11080 C CA  . GLU F  2 120 ? -56.846 -76.896  -2.405  1.00 77.54  ? 120 GLU F CA  1 
ATOM   11081 C C   . GLU F  2 120 ? -58.369 -76.787  -2.406  1.00 75.82  ? 120 GLU F C   1 
ATOM   11082 O O   . GLU F  2 120 ? -58.995 -76.816  -1.347  1.00 89.57  ? 120 GLU F O   1 
ATOM   11083 C CB  . GLU F  2 120 ? -56.209 -75.515  -2.581  1.00 92.58  ? 120 GLU F CB  1 
ATOM   11084 C CG  . GLU F  2 120 ? -54.840 -75.378  -1.931  1.00 106.77 ? 120 GLU F CG  1 
ATOM   11085 C CD  . GLU F  2 120 ? -54.913 -75.417  -0.417  1.00 128.33 ? 120 GLU F CD  1 
ATOM   11086 O OE1 . GLU F  2 120 ? -55.982 -75.079  0.134   1.00 122.79 ? 120 GLU F OE1 1 
ATOM   11087 O OE2 . GLU F  2 120 ? -53.904 -75.782  0.222   1.00 126.27 ? 120 GLU F OE2 1 
ATOM   11088 N N   . LYS F  2 121 ? -58.961 -76.674  -3.592  1.00 77.40  ? 121 LYS F N   1 
ATOM   11089 C CA  . LYS F  2 121 ? -60.402 -76.475  -3.701  1.00 89.63  ? 121 LYS F CA  1 
ATOM   11090 C C   . LYS F  2 121 ? -61.169 -77.593  -3.004  1.00 99.01  ? 121 LYS F C   1 
ATOM   11091 O O   . LYS F  2 121 ? -62.153 -77.343  -2.304  1.00 105.71 ? 121 LYS F O   1 
ATOM   11092 C CB  . LYS F  2 121 ? -60.834 -76.381  -5.166  1.00 84.87  ? 121 LYS F CB  1 
ATOM   11093 C CG  . LYS F  2 121 ? -62.149 -75.633  -5.369  1.00 100.83 ? 121 LYS F CG  1 
ATOM   11094 C CD  . LYS F  2 121 ? -62.625 -75.703  -6.817  1.00 111.56 ? 121 LYS F CD  1 
ATOM   11095 C CE  . LYS F  2 121 ? -64.089 -75.287  -6.947  1.00 113.42 ? 121 LYS F CE  1 
ATOM   11096 N NZ  . LYS F  2 121 ? -64.561 -75.176  -8.360  1.00 113.74 ? 121 LYS F NZ  1 
ATOM   11097 N N   . VAL F  2 122 ? -60.709 -78.825  -3.200  1.00 93.14  ? 122 VAL F N   1 
ATOM   11098 C CA  . VAL F  2 122 ? -61.369 -80.002  -2.638  1.00 87.50  ? 122 VAL F CA  1 
ATOM   11099 C C   . VAL F  2 122 ? -61.145 -80.136  -1.135  1.00 94.82  ? 122 VAL F C   1 
ATOM   11100 O O   . VAL F  2 122 ? -62.038 -80.572  -0.410  1.00 115.41 ? 122 VAL F O   1 
ATOM   11101 C CB  . VAL F  2 122 ? -60.914 -81.302  -3.348  1.00 80.08  ? 122 VAL F CB  1 
ATOM   11102 C CG1 . VAL F  2 122 ? -60.710 -81.052  -4.826  1.00 81.25  ? 122 VAL F CG1 1 
ATOM   11103 C CG2 . VAL F  2 122 ? -59.647 -81.862  -2.716  1.00 86.60  ? 122 VAL F CG2 1 
ATOM   11104 N N   . ARG F  2 123 ? -59.958 -79.753  -0.673  1.00 85.96  ? 123 ARG F N   1 
ATOM   11105 C CA  . ARG F  2 123 ? -59.653 -79.784  0.749   1.00 96.60  ? 123 ARG F CA  1 
ATOM   11106 C C   . ARG F  2 123 ? -60.486 -78.769  1.524   1.00 95.52  ? 123 ARG F C   1 
ATOM   11107 O O   . ARG F  2 123 ? -61.136 -79.113  2.508   1.00 114.31 ? 123 ARG F O   1 
ATOM   11108 C CB  . ARG F  2 123 ? -58.180 -79.486  0.985   1.00 94.33  ? 123 ARG F CB  1 
ATOM   11109 C CG  . ARG F  2 123 ? -57.957 -78.181  1.730   1.00 98.26  ? 123 ARG F CG  1 
ATOM   11110 C CD  . ARG F  2 123 ? -56.513 -78.013  2.110   1.00 104.30 ? 123 ARG F CD  1 
ATOM   11111 N NE  . ARG F  2 123 ? -56.043 -79.122  2.931   1.00 117.62 ? 123 ARG F NE  1 
ATOM   11112 C CZ  . ARG F  2 123 ? -54.762 -79.407  3.129   1.00 124.67 ? 123 ARG F CZ  1 
ATOM   11113 N NH1 . ARG F  2 123 ? -53.819 -78.669  2.558   1.00 117.78 ? 123 ARG F NH1 1 
ATOM   11114 N NH2 . ARG F  2 123 ? -54.423 -80.434  3.891   1.00 132.46 ? 123 ARG F NH2 1 
ATOM   11115 N N   . SER F  2 124 ? -60.453 -77.513  1.081   1.00 97.48  ? 124 SER F N   1 
ATOM   11116 C CA  . SER F  2 124 ? -61.096 -76.427  1.807   1.00 115.20 ? 124 SER F CA  1 
ATOM   11117 C C   . SER F  2 124 ? -62.524 -76.858  2.028   1.00 122.90 ? 124 SER F C   1 
ATOM   11118 O O   . SER F  2 124 ? -63.200 -76.421  2.956   1.00 132.77 ? 124 SER F O   1 
ATOM   11119 C CB  . SER F  2 124 ? -61.075 -75.141  0.975   1.00 122.63 ? 124 SER F CB  1 
ATOM   11120 O OG  . SER F  2 124 ? -62.301 -74.944  0.280   1.00 119.06 ? 124 SER F OG  1 
ATOM   11121 N N   . GLN F  2 125 ? -62.959 -77.759  1.163   1.00 105.17 ? 125 GLN F N   1 
ATOM   11122 C CA  . GLN F  2 125 ? -64.363 -78.049  1.007   1.00 103.84 ? 125 GLN F CA  1 
ATOM   11123 C C   . GLN F  2 125 ? -64.686 -79.456  1.545   1.00 112.97 ? 125 GLN F C   1 
ATOM   11124 O O   . GLN F  2 125 ? -65.851 -79.808  1.714   1.00 113.52 ? 125 GLN F O   1 
ATOM   11125 C CB  . GLN F  2 125 ? -64.751 -77.789  -0.455  1.00 93.28  ? 125 GLN F CB  1 
ATOM   11126 C CG  . GLN F  2 125 ? -66.179 -78.029  -0.836  1.00 101.07 ? 125 GLN F CG  1 
ATOM   11127 C CD  . GLN F  2 125 ? -66.349 -79.370  -1.509  1.00 117.18 ? 125 GLN F CD  1 
ATOM   11128 O OE1 . GLN F  2 125 ? -66.326 -79.455  -2.742  1.00 109.01 ? 125 GLN F OE1 1 
ATOM   11129 N NE2 . GLN F  2 125 ? -66.490 -80.440  -0.704  1.00 131.92 ? 125 GLN F NE2 1 
ATOM   11130 N N   . LEU F  2 126 ? -63.645 -80.234  1.856   1.00 116.06 ? 126 LEU F N   1 
ATOM   11131 C CA  . LEU F  2 126 ? -63.720 -81.249  2.920   1.00 98.11  ? 126 LEU F CA  1 
ATOM   11132 C C   . LEU F  2 126 ? -62.751 -80.869  4.029   1.00 117.73 ? 126 LEU F C   1 
ATOM   11133 O O   . LEU F  2 126 ? -61.537 -80.919  3.844   1.00 128.30 ? 126 LEU F O   1 
ATOM   11134 C CB  . LEU F  2 126 ? -63.341 -82.650  2.427   1.00 103.29 ? 126 LEU F CB  1 
ATOM   11135 C CG  . LEU F  2 126 ? -63.399 -83.053  0.939   1.00 99.94  ? 126 LEU F CG  1 
ATOM   11136 C CD1 . LEU F  2 126 ? -62.457 -84.212  0.693   1.00 106.08 ? 126 LEU F CD1 1 
ATOM   11137 C CD2 . LEU F  2 126 ? -64.803 -83.363  0.398   1.00 100.38 ? 126 LEU F CD2 1 
ATOM   11138 N N   . LYS F  2 127 ? -63.281 -80.502  5.187   1.00 113.02 ? 127 LYS F N   1 
ATOM   11139 C CA  . LYS F  2 127 ? -62.418 -80.073  6.284   1.00 112.19 ? 127 LYS F CA  1 
ATOM   11140 C C   . LYS F  2 127 ? -62.184 -81.162  7.341   1.00 135.95 ? 127 LYS F C   1 
ATOM   11141 O O   . LYS F  2 127 ? -61.130 -81.807  7.373   1.00 124.45 ? 127 LYS F O   1 
ATOM   11142 C CB  . LYS F  2 127 ? -62.968 -78.809  6.929   1.00 109.68 ? 127 LYS F CB  1 
ATOM   11143 C CG  . LYS F  2 127 ? -63.287 -77.743  5.883   1.00 111.46 ? 127 LYS F CG  1 
ATOM   11144 C CD  . LYS F  2 127 ? -64.673 -77.148  6.099   1.00 105.26 ? 127 LYS F CD  1 
ATOM   11145 C CE  . LYS F  2 127 ? -64.992 -76.117  5.019   1.00 115.38 ? 127 LYS F CE  1 
ATOM   11146 N NZ  . LYS F  2 127 ? -66.337 -75.486  5.161   1.00 119.50 ? 127 LYS F NZ  1 
ATOM   11147 N N   . ASN F  2 128 ? -63.179 -81.376  8.194   1.00 192.20 ? 128 ASN F N   1 
ATOM   11148 C CA  . ASN F  2 128 ? -63.122 -82.446  9.178   1.00 190.17 ? 128 ASN F CA  1 
ATOM   11149 C C   . ASN F  2 128 ? -63.607 -83.772  8.605   1.00 192.81 ? 128 ASN F C   1 
ATOM   11150 O O   . ASN F  2 128 ? -63.189 -84.831  9.060   1.00 179.85 ? 128 ASN F O   1 
ATOM   11151 C CB  . ASN F  2 128 ? -63.928 -82.065  10.417  1.00 180.09 ? 128 ASN F CB  1 
ATOM   11152 C CG  . ASN F  2 128 ? -63.268 -80.954  11.216  1.00 187.16 ? 128 ASN F CG  1 
ATOM   11153 O OD1 . ASN F  2 128 ? -62.058 -80.977  11.454  1.00 183.36 ? 128 ASN F OD1 1 
ATOM   11154 N ND2 . ASN F  2 128 ? -64.062 -79.982  11.645  1.00 194.04 ? 128 ASN F ND2 1 
ATOM   11155 N N   . ASN F  2 129 ? -64.470 -83.707  7.594   1.00 187.24 ? 129 ASN F N   1 
ATOM   11156 C CA  . ASN F  2 129 ? -65.136 -84.896  7.065   1.00 185.98 ? 129 ASN F CA  1 
ATOM   11157 C C   . ASN F  2 129 ? -64.200 -85.885  6.369   1.00 182.08 ? 129 ASN F C   1 
ATOM   11158 O O   . ASN F  2 129 ? -64.650 -86.878  5.800   1.00 174.06 ? 129 ASN F O   1 
ATOM   11159 C CB  . ASN F  2 129 ? -66.273 -84.489  6.121   1.00 176.98 ? 129 ASN F CB  1 
ATOM   11160 C CG  . ASN F  2 129 ? -67.348 -83.667  6.817   1.00 172.88 ? 129 ASN F CG  1 
ATOM   11161 O OD1 . ASN F  2 129 ? -68.377 -83.343  6.225   1.00 170.24 ? 129 ASN F OD1 1 
ATOM   11162 N ND2 . ASN F  2 129 ? -67.114 -83.331  8.082   1.00 178.37 ? 129 ASN F ND2 1 
ATOM   11163 N N   . ALA F  2 130 ? -62.900 -85.614  6.429   1.00 155.39 ? 130 ALA F N   1 
ATOM   11164 C CA  . ALA F  2 130 ? -61.901 -86.435  5.752   1.00 145.24 ? 130 ALA F CA  1 
ATOM   11165 C C   . ALA F  2 130 ? -60.504 -85.975  6.154   1.00 133.30 ? 130 ALA F C   1 
ATOM   11166 O O   . ALA F  2 130 ? -60.350 -84.910  6.747   1.00 130.38 ? 130 ALA F O   1 
ATOM   11167 C CB  . ALA F  2 130 ? -62.077 -86.343  4.246   1.00 143.83 ? 130 ALA F CB  1 
ATOM   11168 N N   . LYS F  2 131 ? -59.488 -86.770  5.831   1.00 165.04 ? 131 LYS F N   1 
ATOM   11169 C CA  . LYS F  2 131 ? -58.117 -86.423  6.195   1.00 175.59 ? 131 LYS F CA  1 
ATOM   11170 C C   . LYS F  2 131 ? -57.164 -86.495  5.006   1.00 183.93 ? 131 LYS F C   1 
ATOM   11171 O O   . LYS F  2 131 ? -57.362 -87.286  4.085   1.00 178.67 ? 131 LYS F O   1 
ATOM   11172 C CB  . LYS F  2 131 ? -57.607 -87.336  7.310   1.00 172.48 ? 131 LYS F CB  1 
ATOM   11173 C CG  . LYS F  2 131 ? -57.351 -88.765  6.863   1.00 181.42 ? 131 LYS F CG  1 
ATOM   11174 C CD  . LYS F  2 131 ? -56.491 -89.512  7.867   1.00 180.79 ? 131 LYS F CD  1 
ATOM   11175 C CE  . LYS F  2 131 ? -56.089 -90.876  7.335   1.00 173.37 ? 131 LYS F CE  1 
ATOM   11176 N NZ  . LYS F  2 131 ? -55.126 -91.558  8.241   1.00 166.77 ? 131 LYS F NZ  1 
ATOM   11177 N N   . GLU F  2 132 ? -56.124 -85.670  5.038   1.00 161.33 ? 132 GLU F N   1 
ATOM   11178 C CA  . GLU F  2 132 ? -55.104 -85.687  3.999   1.00 148.13 ? 132 GLU F CA  1 
ATOM   11179 C C   . GLU F  2 132 ? -54.158 -86.863  4.210   1.00 150.21 ? 132 GLU F C   1 
ATOM   11180 O O   . GLU F  2 132 ? -53.781 -87.169  5.341   1.00 157.66 ? 132 GLU F O   1 
ATOM   11181 C CB  . GLU F  2 132 ? -54.320 -84.373  4.002   1.00 156.57 ? 132 GLU F CB  1 
ATOM   11182 C CG  . GLU F  2 132 ? -53.190 -84.318  2.988   1.00 157.85 ? 132 GLU F CG  1 
ATOM   11183 C CD  . GLU F  2 132 ? -52.403 -83.022  3.060   1.00 162.47 ? 132 GLU F CD  1 
ATOM   11184 O OE1 . GLU F  2 132 ? -52.658 -82.219  3.981   1.00 152.28 ? 132 GLU F OE1 1 
ATOM   11185 O OE2 . GLU F  2 132 ? -51.528 -82.806  2.196   1.00 163.04 ? 132 GLU F OE2 1 
ATOM   11186 N N   . ILE F  2 133 ? -53.786 -87.526  3.121   1.00 138.26 ? 133 ILE F N   1 
ATOM   11187 C CA  . ILE F  2 133 ? -52.822 -88.618  3.183   1.00 144.48 ? 133 ILE F CA  1 
ATOM   11188 C C   . ILE F  2 133 ? -51.414 -88.068  2.990   1.00 143.53 ? 133 ILE F C   1 
ATOM   11189 O O   . ILE F  2 133 ? -50.454 -88.556  3.587   1.00 145.61 ? 133 ILE F O   1 
ATOM   11190 C CB  . ILE F  2 133 ? -53.100 -89.688  2.108   1.00 145.49 ? 133 ILE F CB  1 
ATOM   11191 C CG1 . ILE F  2 133 ? -54.478 -90.318  2.318   1.00 146.64 ? 133 ILE F CG1 1 
ATOM   11192 C CG2 . ILE F  2 133 ? -52.028 -90.764  2.138   1.00 135.00 ? 133 ILE F CG2 1 
ATOM   11193 C CD1 . ILE F  2 133 ? -54.576 -91.174  3.562   1.00 152.87 ? 133 ILE F CD1 1 
ATOM   11194 N N   . GLY F  2 134 ? -51.303 -87.040  2.155   1.00 145.53 ? 134 GLY F N   1 
ATOM   11195 C CA  . GLY F  2 134 ? -50.023 -86.426  1.861   1.00 143.49 ? 134 GLY F CA  1 
ATOM   11196 C C   . GLY F  2 134 ? -49.619 -86.655  0.419   1.00 124.73 ? 134 GLY F C   1 
ATOM   11197 O O   . GLY F  2 134 ? -48.761 -85.952  -0.117  1.00 108.73 ? 134 GLY F O   1 
ATOM   11198 N N   . ASN F  2 135 ? -50.243 -87.646  -0.211  1.00 116.68 ? 135 ASN F N   1 
ATOM   11199 C CA  . ASN F  2 135 ? -49.938 -87.988  -1.596  1.00 101.48 ? 135 ASN F CA  1 
ATOM   11200 C C   . ASN F  2 135 ? -50.965 -87.377  -2.544  1.00 101.21 ? 135 ASN F C   1 
ATOM   11201 O O   . ASN F  2 135 ? -51.205 -87.878  -3.646  1.00 87.95  ? 135 ASN F O   1 
ATOM   11202 C CB  . ASN F  2 135 ? -49.882 -89.505  -1.774  1.00 107.12 ? 135 ASN F CB  1 
ATOM   11203 C CG  . ASN F  2 135 ? -49.263 -89.912  -3.094  1.00 119.49 ? 135 ASN F CG  1 
ATOM   11204 O OD1 . ASN F  2 135 ? -48.727 -89.079  -3.827  1.00 113.33 ? 135 ASN F OD1 1 
ATOM   11205 N ND2 . ASN F  2 135 ? -49.331 -91.199  -3.405  1.00 136.96 ? 135 ASN F ND2 1 
ATOM   11206 N N   . GLY F  2 136 ? -51.570 -86.283  -2.100  1.00 100.30 ? 136 GLY F N   1 
ATOM   11207 C CA  . GLY F  2 136 ? -52.605 -85.625  -2.870  1.00 90.25  ? 136 GLY F CA  1 
ATOM   11208 C C   . GLY F  2 136 ? -53.975 -86.212  -2.610  1.00 104.01 ? 136 GLY F C   1 
ATOM   11209 O O   . GLY F  2 136 ? -54.990 -85.687  -3.090  1.00 104.71 ? 136 GLY F O   1 
ATOM   11210 N N   . CYS F  2 137 ? -54.011 -87.297  -1.839  1.00 125.21 ? 137 CYS F N   1 
ATOM   11211 C CA  . CYS F  2 137 ? -55.259 -88.036  -1.646  1.00 129.12 ? 137 CYS F CA  1 
ATOM   11212 C C   . CYS F  2 137 ? -55.824 -87.825  -0.240  1.00 129.91 ? 137 CYS F C   1 
ATOM   11213 O O   . CYS F  2 137 ? -55.075 -87.671  0.729   1.00 131.56 ? 137 CYS F O   1 
ATOM   11214 C CB  . CYS F  2 137 ? -55.071 -89.548  -1.933  1.00 112.19 ? 137 CYS F CB  1 
ATOM   11215 S SG  . CYS F  2 137 ? -56.015 -90.260  -3.351  1.00 150.97 ? 137 CYS F SG  1 
ATOM   11216 N N   . PHE F  2 138 ? -57.151 -87.842  -0.149  1.00 122.24 ? 138 PHE F N   1 
ATOM   11217 C CA  . PHE F  2 138 ? -57.879 -87.613  1.093   1.00 129.88 ? 138 PHE F CA  1 
ATOM   11218 C C   . PHE F  2 138 ? -58.731 -88.828  1.399   1.00 147.86 ? 138 PHE F C   1 
ATOM   11219 O O   . PHE F  2 138 ? -59.315 -89.424  0.495   1.00 154.96 ? 138 PHE F O   1 
ATOM   11220 C CB  . PHE F  2 138 ? -58.790 -86.396  0.953   1.00 123.99 ? 138 PHE F CB  1 
ATOM   11221 C CG  . PHE F  2 138 ? -58.061 -85.138  0.611   1.00 114.72 ? 138 PHE F CG  1 
ATOM   11222 C CD1 . PHE F  2 138 ? -58.619 -84.197  -0.234  1.00 102.59 ? 138 PHE F CD1 1 
ATOM   11223 C CD2 . PHE F  2 138 ? -56.801 -84.904  1.127   1.00 113.63 ? 138 PHE F CD2 1 
ATOM   11224 C CE1 . PHE F  2 138 ? -57.935 -83.045  -0.545  1.00 103.88 ? 138 PHE F CE1 1 
ATOM   11225 C CE2 . PHE F  2 138 ? -56.116 -83.755  0.815   1.00 108.51 ? 138 PHE F CE2 1 
ATOM   11226 C CZ  . PHE F  2 138 ? -56.686 -82.823  -0.023  1.00 109.93 ? 138 PHE F CZ  1 
ATOM   11227 N N   . GLU F  2 139 ? -58.802 -89.189  2.674   1.00 155.67 ? 139 GLU F N   1 
ATOM   11228 C CA  . GLU F  2 139 ? -59.586 -90.335  3.096   1.00 144.45 ? 139 GLU F CA  1 
ATOM   11229 C C   . GLU F  2 139 ? -60.848 -89.886  3.819   1.00 137.25 ? 139 GLU F C   1 
ATOM   11230 O O   . GLU F  2 139 ? -60.783 -89.151  4.803   1.00 135.09 ? 139 GLU F O   1 
ATOM   11231 C CB  . GLU F  2 139 ? -58.749 -91.241  3.993   1.00 142.92 ? 139 GLU F CB  1 
ATOM   11232 C CG  . GLU F  2 139 ? -59.496 -92.455  4.490   1.00 164.18 ? 139 GLU F CG  1 
ATOM   11233 C CD  . GLU F  2 139 ? -58.578 -93.476  5.116   1.00 173.80 ? 139 GLU F CD  1 
ATOM   11234 O OE1 . GLU F  2 139 ? -57.350 -93.246  5.125   1.00 159.31 ? 139 GLU F OE1 1 
ATOM   11235 O OE2 . GLU F  2 139 ? -59.083 -94.510  5.596   1.00 176.82 ? 139 GLU F OE2 1 
ATOM   11236 N N   . PHE F  2 140 ? -61.996 -90.332  3.320   1.00 154.18 ? 140 PHE F N   1 
ATOM   11237 C CA  . PHE F  2 140 ? -63.284 -89.956  3.891   1.00 161.94 ? 140 PHE F CA  1 
ATOM   11238 C C   . PHE F  2 140 ? -63.578 -90.685  5.196   1.00 170.13 ? 140 PHE F C   1 
ATOM   11239 O O   . PHE F  2 140 ? -63.354 -91.891  5.313   1.00 166.70 ? 140 PHE F O   1 
ATOM   11240 C CB  . PHE F  2 140 ? -64.417 -90.236  2.900   1.00 161.00 ? 140 PHE F CB  1 
ATOM   11241 C CG  . PHE F  2 140 ? -64.406 -89.347  1.691   1.00 154.76 ? 140 PHE F CG  1 
ATOM   11242 C CD1 . PHE F  2 140 ? -63.835 -89.775  0.509   1.00 162.62 ? 140 PHE F CD1 1 
ATOM   11243 C CD2 . PHE F  2 140 ? -64.977 -88.087  1.733   1.00 150.16 ? 140 PHE F CD2 1 
ATOM   11244 C CE1 . PHE F  2 140 ? -63.825 -88.969  -0.610  1.00 160.98 ? 140 PHE F CE1 1 
ATOM   11245 C CE2 . PHE F  2 140 ? -64.970 -87.272  0.615   1.00 143.84 ? 140 PHE F CE2 1 
ATOM   11246 C CZ  . PHE F  2 140 ? -64.393 -87.715  -0.558  1.00 149.23 ? 140 PHE F CZ  1 
ATOM   11247 N N   . TYR F  2 141 ? -64.084 -89.944  6.176   1.00 156.76 ? 141 TYR F N   1 
ATOM   11248 C CA  . TYR F  2 141 ? -64.613 -90.548  7.388   1.00 146.12 ? 141 TYR F CA  1 
ATOM   11249 C C   . TYR F  2 141 ? -66.094 -90.833  7.182   1.00 139.42 ? 141 TYR F C   1 
ATOM   11250 O O   . TYR F  2 141 ? -66.697 -91.615  7.917   1.00 144.78 ? 141 TYR F O   1 
ATOM   11251 C CB  . TYR F  2 141 ? -64.437 -89.618  8.589   1.00 147.82 ? 141 TYR F CB  1 
ATOM   11252 C CG  . TYR F  2 141 ? -63.003 -89.325  8.962   1.00 139.04 ? 141 TYR F CG  1 
ATOM   11253 C CD1 . TYR F  2 141 ? -62.575 -88.021  9.169   1.00 132.04 ? 141 TYR F CD1 1 
ATOM   11254 C CD2 . TYR F  2 141 ? -62.079 -90.350  9.111   1.00 131.73 ? 141 TYR F CD2 1 
ATOM   11255 C CE1 . TYR F  2 141 ? -61.267 -87.745  9.514   1.00 135.09 ? 141 TYR F CE1 1 
ATOM   11256 C CE2 . TYR F  2 141 ? -60.768 -90.084  9.454   1.00 133.36 ? 141 TYR F CE2 1 
ATOM   11257 C CZ  . TYR F  2 141 ? -60.367 -88.779  9.655   1.00 137.44 ? 141 TYR F CZ  1 
ATOM   11258 O OH  . TYR F  2 141 ? -59.062 -88.509  9.997   1.00 124.15 ? 141 TYR F OH  1 
ATOM   11259 N N   . HIS F  2 142 ? -66.674 -90.187  6.176   1.00 147.83 ? 142 HIS F N   1 
ATOM   11260 C CA  . HIS F  2 142 ? -68.095 -90.333  5.885   1.00 146.51 ? 142 HIS F CA  1 
ATOM   11261 C C   . HIS F  2 142 ? -68.312 -90.992  4.524   1.00 150.41 ? 142 HIS F C   1 
ATOM   11262 O O   . HIS F  2 142 ? -67.865 -90.482  3.496   1.00 160.94 ? 142 HIS F O   1 
ATOM   11263 C CB  . HIS F  2 142 ? -68.803 -88.973  5.978   1.00 146.39 ? 142 HIS F CB  1 
ATOM   11264 C CG  . HIS F  2 142 ? -69.311 -88.452  4.670   1.00 150.84 ? 142 HIS F CG  1 
ATOM   11265 N ND1 . HIS F  2 142 ? -70.622 -88.602  4.267   1.00 149.50 ? 142 HIS F ND1 1 
ATOM   11266 C CD2 . HIS F  2 142 ? -68.691 -87.767  3.678   1.00 148.71 ? 142 HIS F CD2 1 
ATOM   11267 C CE1 . HIS F  2 142 ? -70.783 -88.041  3.083   1.00 145.58 ? 142 HIS F CE1 1 
ATOM   11268 N NE2 . HIS F  2 142 ? -69.629 -87.528  2.703   1.00 153.18 ? 142 HIS F NE2 1 
ATOM   11269 N N   . LYS F  2 143 ? -68.983 -92.141  4.535   1.00 137.90 ? 143 LYS F N   1 
ATOM   11270 C CA  . LYS F  2 143 ? -69.228 -92.912  3.320   1.00 140.34 ? 143 LYS F CA  1 
ATOM   11271 C C   . LYS F  2 143 ? -69.621 -92.015  2.153   1.00 139.97 ? 143 LYS F C   1 
ATOM   11272 O O   . LYS F  2 143 ? -70.687 -91.400  2.162   1.00 133.41 ? 143 LYS F O   1 
ATOM   11273 C CB  . LYS F  2 143 ? -70.312 -93.966  3.559   1.00 139.37 ? 143 LYS F CB  1 
ATOM   11274 C CG  . LYS F  2 143 ? -69.880 -95.138  4.431   1.00 140.69 ? 143 LYS F CG  1 
ATOM   11275 C CD  . LYS F  2 143 ? -69.140 -96.207  3.632   1.00 145.60 ? 143 LYS F CD  1 
ATOM   11276 C CE  . LYS F  2 143 ? -67.676 -95.854  3.413   1.00 147.83 ? 143 LYS F CE  1 
ATOM   11277 N NZ  . LYS F  2 143 ? -66.953 -96.936  2.688   1.00 139.09 ? 143 LYS F NZ  1 
ATOM   11278 N N   . CYS F  2 144 ? -68.752 -91.946  1.150   1.00 177.76 ? 144 CYS F N   1 
ATOM   11279 C CA  . CYS F  2 144 ? -68.989 -91.085  0.000   1.00 182.91 ? 144 CYS F CA  1 
ATOM   11280 C C   . CYS F  2 144 ? -69.142 -91.891  -1.285  1.00 169.27 ? 144 CYS F C   1 
ATOM   11281 O O   . CYS F  2 144 ? -68.155 -92.300  -1.897  1.00 159.98 ? 144 CYS F O   1 
ATOM   11282 C CB  . CYS F  2 144 ? -67.858 -90.066  -0.148  1.00 183.22 ? 144 CYS F CB  1 
ATOM   11283 S SG  . CYS F  2 144 ? -68.185 -88.768  -1.362  1.00 191.61 ? 144 CYS F SG  1 
ATOM   11284 N N   . ASP F  2 145 ? -70.388 -92.114  -1.686  1.00 174.21 ? 145 ASP F N   1 
ATOM   11285 C CA  . ASP F  2 145 ? -70.684 -92.823  -2.925  1.00 179.08 ? 145 ASP F CA  1 
ATOM   11286 C C   . ASP F  2 145 ? -70.494 -91.929  -4.151  1.00 173.72 ? 145 ASP F C   1 
ATOM   11287 O O   . ASP F  2 145 ? -69.875 -90.868  -4.064  1.00 172.94 ? 145 ASP F O   1 
ATOM   11288 C CB  . ASP F  2 145 ? -72.096 -93.421  -2.892  1.00 191.74 ? 145 ASP F CB  1 
ATOM   11289 C CG  . ASP F  2 145 ? -73.132 -92.465  -2.325  1.00 193.92 ? 145 ASP F CG  1 
ATOM   11290 O OD1 . ASP F  2 145 ? -74.338 -92.707  -2.540  1.00 188.46 ? 145 ASP F OD1 1 
ATOM   11291 O OD2 . ASP F  2 145 ? -72.750 -91.477  -1.663  1.00 190.55 ? 145 ASP F OD2 1 
ATOM   11292 N N   . ASN F  2 146 ? -71.025 -92.365  -5.290  1.00 146.07 ? 146 ASN F N   1 
ATOM   11293 C CA  . ASN F  2 146 ? -70.823 -91.664  -6.558  1.00 137.39 ? 146 ASN F CA  1 
ATOM   11294 C C   . ASN F  2 146 ? -71.379 -90.245  -6.591  1.00 145.00 ? 146 ASN F C   1 
ATOM   11295 O O   . ASN F  2 146 ? -70.736 -89.330  -7.107  1.00 159.45 ? 146 ASN F O   1 
ATOM   11296 C CB  . ASN F  2 146 ? -71.407 -92.474  -7.718  1.00 119.99 ? 146 ASN F CB  1 
ATOM   11297 C CG  . ASN F  2 146 ? -70.595 -93.714  -8.029  1.00 120.27 ? 146 ASN F CG  1 
ATOM   11298 O OD1 . ASN F  2 146 ? -71.000 -94.548  -8.839  1.00 121.39 ? 146 ASN F OD1 1 
ATOM   11299 N ND2 . ASN F  2 146 ? -69.440 -93.842  -7.387  1.00 118.39 ? 146 ASN F ND2 1 
ATOM   11300 N N   . THR F  2 147 ? -72.580 -90.064  -6.053  1.00 160.56 ? 147 THR F N   1 
ATOM   11301 C CA  . THR F  2 147 ? -73.219 -88.754  -6.066  1.00 166.51 ? 147 THR F CA  1 
ATOM   11302 C C   . THR F  2 147 ? -72.689 -87.874  -4.938  1.00 170.79 ? 147 THR F C   1 
ATOM   11303 O O   . THR F  2 147 ? -72.953 -86.673  -4.898  1.00 169.03 ? 147 THR F O   1 
ATOM   11304 C CB  . THR F  2 147 ? -74.752 -88.863  -5.981  1.00 162.96 ? 147 THR F CB  1 
ATOM   11305 O OG1 . THR F  2 147 ? -75.129 -89.384  -4.702  1.00 176.43 ? 147 THR F OG1 1 
ATOM   11306 C CG2 . THR F  2 147 ? -75.279 -89.779  -7.079  1.00 115.37 ? 147 THR F CG2 1 
ATOM   11307 N N   . CYS F  2 148 ? -71.946 -88.481  -4.019  1.00 163.84 ? 148 CYS F N   1 
ATOM   11308 C CA  . CYS F  2 148 ? -71.220 -87.722  -3.012  1.00 167.65 ? 148 CYS F CA  1 
ATOM   11309 C C   . CYS F  2 148 ? -69.959 -87.183  -3.668  1.00 175.49 ? 148 CYS F C   1 
ATOM   11310 O O   . CYS F  2 148 ? -69.637 -86.001  -3.556  1.00 176.79 ? 148 CYS F O   1 
ATOM   11311 C CB  . CYS F  2 148 ? -70.855 -88.611  -1.823  1.00 164.50 ? 148 CYS F CB  1 
ATOM   11312 S SG  . CYS F  2 148 ? -69.802 -87.811  -0.589  1.00 161.55 ? 148 CYS F SG  1 
ATOM   11313 N N   . MET F  2 149 ? -69.260 -88.069  -4.368  1.00 160.06 ? 149 MET F N   1 
ATOM   11314 C CA  . MET F  2 149 ? -68.058 -87.712  -5.109  1.00 148.15 ? 149 MET F CA  1 
ATOM   11315 C C   . MET F  2 149 ? -68.302 -86.549  -6.065  1.00 141.41 ? 149 MET F C   1 
ATOM   11316 O O   . MET F  2 149 ? -67.379 -85.805  -6.396  1.00 135.28 ? 149 MET F O   1 
ATOM   11317 C CB  . MET F  2 149 ? -67.549 -88.921  -5.896  1.00 140.18 ? 149 MET F CB  1 
ATOM   11318 C CG  . MET F  2 149 ? -66.973 -90.038  -5.046  1.00 138.45 ? 149 MET F CG  1 
ATOM   11319 S SD  . MET F  2 149 ? -65.441 -89.566  -4.223  1.00 134.91 ? 149 MET F SD  1 
ATOM   11320 C CE  . MET F  2 149 ? -64.903 -91.149  -3.580  1.00 137.84 ? 149 MET F CE  1 
ATOM   11321 N N   . GLU F  2 150 ? -69.545 -86.399  -6.512  1.00 190.06 ? 150 GLU F N   1 
ATOM   11322 C CA  . GLU F  2 150 ? -69.891 -85.376  -7.493  1.00 192.63 ? 150 GLU F CA  1 
ATOM   11323 C C   . GLU F  2 150 ? -69.983 -83.990  -6.855  1.00 196.80 ? 150 GLU F C   1 
ATOM   11324 O O   . GLU F  2 150 ? -69.514 -83.003  -7.423  1.00 195.73 ? 150 GLU F O   1 
ATOM   11325 C CB  . GLU F  2 150 ? -71.212 -85.728  -8.181  1.00 198.22 ? 150 GLU F CB  1 
ATOM   11326 C CG  . GLU F  2 150 ? -71.193 -85.600  -9.700  1.00 200.53 ? 150 GLU F CG  1 
ATOM   11327 C CD  . GLU F  2 150 ? -70.793 -86.890  -10.397 1.00 203.89 ? 150 GLU F CD  1 
ATOM   11328 O OE1 . GLU F  2 150 ? -71.121 -87.050  -11.591 1.00 208.89 ? 150 GLU F OE1 1 
ATOM   11329 O OE2 . GLU F  2 150 ? -70.160 -87.749  -9.752  1.00 193.86 ? 150 GLU F OE2 1 
ATOM   11330 N N   . SER F  2 151 ? -70.595 -83.925  -5.676  1.00 169.95 ? 151 SER F N   1 
ATOM   11331 C CA  . SER F  2 151 ? -70.727 -82.671  -4.941  1.00 162.93 ? 151 SER F CA  1 
ATOM   11332 C C   . SER F  2 151 ? -69.368 -82.003  -4.764  1.00 158.83 ? 151 SER F C   1 
ATOM   11333 O O   . SER F  2 151 ? -69.274 -80.782  -4.637  1.00 161.02 ? 151 SER F O   1 
ATOM   11334 C CB  . SER F  2 151 ? -71.371 -82.917  -3.575  1.00 157.33 ? 151 SER F CB  1 
ATOM   11335 O OG  . SER F  2 151 ? -70.533 -83.707  -2.750  1.00 155.14 ? 151 SER F OG  1 
ATOM   11336 N N   . VAL F  2 152 ? -68.316 -82.815  -4.756  1.00 133.72 ? 152 VAL F N   1 
ATOM   11337 C CA  . VAL F  2 152 ? -66.958 -82.305  -4.625  1.00 122.83 ? 152 VAL F CA  1 
ATOM   11338 C C   . VAL F  2 152 ? -66.469 -81.729  -5.951  1.00 127.95 ? 152 VAL F C   1 
ATOM   11339 O O   . VAL F  2 152 ? -65.917 -80.629  -5.993  1.00 123.52 ? 152 VAL F O   1 
ATOM   11340 C CB  . VAL F  2 152 ? -65.984 -83.401  -4.155  1.00 106.49 ? 152 VAL F CB  1 
ATOM   11341 C CG1 . VAL F  2 152 ? -64.660 -82.783  -3.731  1.00 93.78  ? 152 VAL F CG1 1 
ATOM   11342 C CG2 . VAL F  2 152 ? -66.591 -84.191  -3.007  1.00 118.26 ? 152 VAL F CG2 1 
ATOM   11343 N N   . LYS F  2 153 ? -66.677 -82.476  -7.032  1.00 120.44 ? 153 LYS F N   1 
ATOM   11344 C CA  . LYS F  2 153 ? -66.285 -82.022  -8.363  1.00 117.05 ? 153 LYS F CA  1 
ATOM   11345 C C   . LYS F  2 153 ? -67.056 -80.769  -8.772  1.00 137.73 ? 153 LYS F C   1 
ATOM   11346 O O   . LYS F  2 153 ? -66.459 -79.746  -9.103  1.00 148.99 ? 153 LYS F O   1 
ATOM   11347 C CB  . LYS F  2 153 ? -66.483 -83.130  -9.400  1.00 108.50 ? 153 LYS F CB  1 
ATOM   11348 C CG  . LYS F  2 153 ? -65.570 -84.334  -9.216  1.00 91.55  ? 153 LYS F CG  1 
ATOM   11349 C CD  . LYS F  2 153 ? -65.641 -85.264  -10.419 1.00 100.87 ? 153 LYS F CD  1 
ATOM   11350 C CE  . LYS F  2 153 ? -64.802 -86.515  -10.214 1.00 95.69  ? 153 LYS F CE  1 
ATOM   11351 N NZ  . LYS F  2 153 ? -65.293 -87.336  -9.075  1.00 111.86 ? 153 LYS F NZ  1 
ATOM   11352 N N   . ASN F  2 154 ? -68.384 -80.853  -8.747  1.00 183.51 ? 154 ASN F N   1 
ATOM   11353 C CA  . ASN F  2 154 ? -69.227 -79.702  -9.053  1.00 189.54 ? 154 ASN F CA  1 
ATOM   11354 C C   . ASN F  2 154 ? -68.918 -78.513  -8.148  1.00 193.71 ? 154 ASN F C   1 
ATOM   11355 O O   . ASN F  2 154 ? -69.349 -77.391  -8.410  1.00 198.48 ? 154 ASN F O   1 
ATOM   11356 C CB  . ASN F  2 154 ? -70.710 -80.068  -8.942  1.00 199.39 ? 154 ASN F CB  1 
ATOM   11357 C CG  . ASN F  2 154 ? -71.221 -80.822  -10.157 1.00 199.69 ? 154 ASN F CG  1 
ATOM   11358 O OD1 . ASN F  2 154 ? -71.221 -82.054  -10.184 1.00 200.76 ? 154 ASN F OD1 1 
ATOM   11359 N ND2 . ASN F  2 154 ? -71.658 -80.080  -11.174 1.00 200.24 ? 154 ASN F ND2 1 
ATOM   11360 N N   . GLY F  2 155 ? -68.169 -78.769  -7.081  1.00 182.42 ? 155 GLY F N   1 
ATOM   11361 C CA  . GLY F  2 155 ? -67.843 -77.734  -6.119  1.00 179.70 ? 155 GLY F CA  1 
ATOM   11362 C C   . GLY F  2 155 ? -69.023 -77.435  -5.216  1.00 185.87 ? 155 GLY F C   1 
ATOM   11363 O O   . GLY F  2 155 ? -68.955 -76.543  -4.370  1.00 177.91 ? 155 GLY F O   1 
ATOM   11364 N N   . THR F  2 156 ? -70.108 -78.188  -5.398  1.00 179.90 ? 156 THR F N   1 
ATOM   11365 C CA  . THR F  2 156 ? -71.325 -78.019  -4.600  1.00 182.18 ? 156 THR F CA  1 
ATOM   11366 C C   . THR F  2 156 ? -71.512 -79.130  -3.570  1.00 167.69 ? 156 THR F C   1 
ATOM   11367 O O   . THR F  2 156 ? -72.277 -80.074  -3.778  1.00 161.98 ? 156 THR F O   1 
ATOM   11368 C CB  . THR F  2 156 ? -72.581 -77.995  -5.477  1.00 188.85 ? 156 THR F CB  1 
ATOM   11369 O OG1 . THR F  2 156 ? -72.617 -79.180  -6.283  1.00 181.89 ? 156 THR F OG1 1 
ATOM   11370 C CG2 . THR F  2 156 ? -72.587 -76.770  -6.375  1.00 189.57 ? 156 THR F CG2 1 
ATOM   11371 N N   . TYR F  2 157 ? -70.805 -78.977  -2.458  1.00 153.13 ? 157 TYR F N   1 
ATOM   11372 C CA  . TYR F  2 157 ? -70.788 -79.888  -1.328  1.00 145.09 ? 157 TYR F CA  1 
ATOM   11373 C C   . TYR F  2 157 ? -71.110 -78.850  -0.253  1.00 158.62 ? 157 TYR F C   1 
ATOM   11374 O O   . TYR F  2 157 ? -70.517 -78.825  0.825   1.00 151.30 ? 157 TYR F O   1 
ATOM   11375 C CB  . TYR F  2 157 ? -69.369 -80.473  -1.211  1.00 137.55 ? 157 TYR F CB  1 
ATOM   11376 C CG  . TYR F  2 157 ? -69.069 -81.511  -0.132  1.00 125.54 ? 157 TYR F CG  1 
ATOM   11377 C CD1 . TYR F  2 157 ? -68.797 -82.839  -0.463  1.00 124.93 ? 157 TYR F CD1 1 
ATOM   11378 C CD2 . TYR F  2 157 ? -68.995 -81.150  1.206   1.00 124.03 ? 157 TYR F CD2 1 
ATOM   11379 C CE1 . TYR F  2 157 ? -68.490 -83.777  0.517   1.00 117.81 ? 157 TYR F CE1 1 
ATOM   11380 C CE2 . TYR F  2 157 ? -68.691 -82.082  2.189   1.00 130.24 ? 157 TYR F CE2 1 
ATOM   11381 C CZ  . TYR F  2 157 ? -68.440 -83.392  1.839   1.00 118.57 ? 157 TYR F CZ  1 
ATOM   11382 O OH  . TYR F  2 157 ? -68.136 -84.324  2.808   1.00 110.30 ? 157 TYR F OH  1 
ATOM   11383 N N   . ASP F  2 158 ? -72.027 -77.945  -0.613  1.00 189.11 ? 158 ASP F N   1 
ATOM   11384 C CA  . ASP F  2 158 ? -72.370 -76.765  0.186   1.00 199.35 ? 158 ASP F CA  1 
ATOM   11385 C C   . ASP F  2 158 ? -73.337 -77.111  1.302   1.00 218.00 ? 158 ASP F C   1 
ATOM   11386 O O   . ASP F  2 158 ? -73.380 -76.439  2.332   1.00 222.22 ? 158 ASP F O   1 
ATOM   11387 C CB  . ASP F  2 158 ? -73.021 -75.691  -0.693  1.00 176.30 ? 158 ASP F CB  1 
ATOM   11388 C CG  . ASP F  2 158 ? -72.032 -74.650  -1.190  1.00 165.89 ? 158 ASP F CG  1 
ATOM   11389 O OD1 . ASP F  2 158 ? -72.384 -73.450  -1.194  1.00 146.88 ? 158 ASP F OD1 1 
ATOM   11390 O OD2 . ASP F  2 158 ? -70.905 -75.025  -1.574  1.00 170.54 ? 158 ASP F OD2 1 
ATOM   11391 N N   . TYR F  2 159 ? -74.132 -78.150  1.077   1.00 224.91 ? 159 TYR F N   1 
ATOM   11392 C CA  . TYR F  2 159 ? -75.088 -78.613  2.070   1.00 233.02 ? 159 TYR F CA  1 
ATOM   11393 C C   . TYR F  2 159 ? -74.719 -80.031  2.490   1.00 223.83 ? 159 TYR F C   1 
ATOM   11394 O O   . TYR F  2 159 ? -75.414 -80.988  2.147   1.00 217.39 ? 159 TYR F O   1 
ATOM   11395 C CB  . TYR F  2 159 ? -76.505 -78.573  1.497   1.00 246.38 ? 159 TYR F CB  1 
ATOM   11396 C CG  . TYR F  2 159 ? -77.595 -78.631  2.541   1.00 254.62 ? 159 TYR F CG  1 
ATOM   11397 C CD1 . TYR F  2 159 ? -78.154 -79.842  2.922   1.00 255.32 ? 159 TYR F CD1 1 
ATOM   11398 C CD2 . TYR F  2 159 ? -78.069 -77.472  3.144   1.00 248.06 ? 159 TYR F CD2 1 
ATOM   11399 C CE1 . TYR F  2 159 ? -79.153 -79.900  3.876   1.00 245.47 ? 159 TYR F CE1 1 
ATOM   11400 C CE2 . TYR F  2 159 ? -79.067 -77.520  4.099   1.00 255.64 ? 159 TYR F CE2 1 
ATOM   11401 C CZ  . TYR F  2 159 ? -79.606 -78.736  4.461   1.00 251.06 ? 159 TYR F CZ  1 
ATOM   11402 O OH  . TYR F  2 159 ? -80.601 -78.789  5.412   1.00 235.77 ? 159 TYR F OH  1 
ATOM   11403 N N   . PRO F  2 160 ? -73.612 -80.168  3.237   1.00 222.01 ? 160 PRO F N   1 
ATOM   11404 C CA  . PRO F  2 160 ? -73.047 -81.471  3.604   1.00 210.03 ? 160 PRO F CA  1 
ATOM   11405 C C   . PRO F  2 160 ? -73.937 -82.269  4.550   1.00 203.63 ? 160 PRO F C   1 
ATOM   11406 O O   . PRO F  2 160 ? -74.687 -81.696  5.342   1.00 192.92 ? 160 PRO F O   1 
ATOM   11407 C CB  . PRO F  2 160 ? -71.738 -81.100  4.315   1.00 175.28 ? 160 PRO F CB  1 
ATOM   11408 C CG  . PRO F  2 160 ? -71.461 -79.681  3.926   1.00 192.47 ? 160 PRO F CG  1 
ATOM   11409 C CD  . PRO F  2 160 ? -72.807 -79.059  3.773   1.00 220.62 ? 160 PRO F CD  1 
ATOM   11410 N N   . LYS F  2 161 ? -73.843 -83.591  4.456   1.00 185.23 ? 161 LYS F N   1 
ATOM   11411 C CA  . LYS F  2 161 ? -74.536 -84.493  5.366   1.00 149.90 ? 161 LYS F CA  1 
ATOM   11412 C C   . LYS F  2 161 ? -73.667 -85.714  5.636   1.00 151.91 ? 161 LYS F C   1 
ATOM   11413 O O   . LYS F  2 161 ? -73.634 -86.655  4.843   1.00 142.00 ? 161 LYS F O   1 
ATOM   11414 C CB  . LYS F  2 161 ? -75.893 -84.909  4.796   1.00 130.30 ? 161 LYS F CB  1 
ATOM   11415 C CG  . LYS F  2 161 ? -76.969 -83.847  4.940   1.00 150.60 ? 161 LYS F CG  1 
ATOM   11416 C CD  . LYS F  2 161 ? -77.175 -83.486  6.403   1.00 150.69 ? 161 LYS F CD  1 
ATOM   11417 C CE  . LYS F  2 161 ? -78.191 -82.368  6.567   1.00 142.83 ? 161 LYS F CE  1 
ATOM   11418 N NZ  . LYS F  2 161 ? -78.389 -82.012  7.999   1.00 114.98 ? 161 LYS F NZ  1 
ATOM   11419 N N   . TYR F  2 162 ? -72.960 -85.686  6.761   1.00 153.67 ? 162 TYR F N   1 
ATOM   11420 C CA  . TYR F  2 162 ? -72.002 -86.732  7.099   1.00 150.47 ? 162 TYR F CA  1 
ATOM   11421 C C   . TYR F  2 162 ? -72.625 -87.843  7.941   1.00 150.50 ? 162 TYR F C   1 
ATOM   11422 O O   . TYR F  2 162 ? -73.638 -87.639  8.608   1.00 140.22 ? 162 TYR F O   1 
ATOM   11423 C CB  . TYR F  2 162 ? -70.795 -86.129  7.824   1.00 129.69 ? 162 TYR F CB  1 
ATOM   11424 C CG  . TYR F  2 162 ? -71.150 -85.342  9.067   1.00 146.62 ? 162 TYR F CG  1 
ATOM   11425 C CD1 . TYR F  2 162 ? -71.708 -84.072  8.976   1.00 130.38 ? 162 TYR F CD1 1 
ATOM   11426 C CD2 . TYR F  2 162 ? -70.919 -85.865  10.333  1.00 150.08 ? 162 TYR F CD2 1 
ATOM   11427 C CE1 . TYR F  2 162 ? -72.033 -83.349  10.109  1.00 124.65 ? 162 TYR F CE1 1 
ATOM   11428 C CE2 . TYR F  2 162 ? -71.239 -85.148  11.472  1.00 150.10 ? 162 TYR F CE2 1 
ATOM   11429 C CZ  . TYR F  2 162 ? -71.795 -83.892  11.355  1.00 154.19 ? 162 TYR F CZ  1 
ATOM   11430 O OH  . TYR F  2 162 ? -72.114 -83.176  12.486  1.00 156.66 ? 162 TYR F OH  1 
ATOM   11431 N N   . ASP G  1 7   ? -34.687 -17.193  30.997  1.00 119.95 ? 7   ASP G N   1 
ATOM   11432 C CA  . ASP G  1 7   ? -35.656 -18.028  30.298  1.00 123.61 ? 7   ASP G CA  1 
ATOM   11433 C C   . ASP G  1 7   ? -35.361 -18.071  28.802  1.00 126.04 ? 7   ASP G C   1 
ATOM   11434 O O   . ASP G  1 7   ? -35.116 -19.137  28.242  1.00 143.12 ? 7   ASP G O   1 
ATOM   11435 C CB  . ASP G  1 7   ? -37.079 -17.519  30.543  1.00 116.24 ? 7   ASP G CB  1 
ATOM   11436 C CG  . ASP G  1 7   ? -38.058 -18.639  30.846  1.00 135.91 ? 7   ASP G CG  1 
ATOM   11437 O OD1 . ASP G  1 7   ? -37.618 -19.708  31.320  1.00 122.06 ? 7   ASP G OD1 1 
ATOM   11438 O OD2 . ASP G  1 7   ? -39.271 -18.445  30.621  1.00 113.57 ? 7   ASP G OD2 1 
ATOM   11439 N N   . THR G  1 8   ? -35.369 -16.904  28.165  1.00 118.66 ? 8   THR G N   1 
ATOM   11440 C CA  . THR G  1 8   ? -35.203 -16.830  26.717  1.00 122.24 ? 8   THR G CA  1 
ATOM   11441 C C   . THR G  1 8   ? -33.776 -16.484  26.295  1.00 114.52 ? 8   THR G C   1 
ATOM   11442 O O   . THR G  1 8   ? -33.073 -15.746  26.984  1.00 121.59 ? 8   THR G O   1 
ATOM   11443 C CB  . THR G  1 8   ? -36.166 -15.806  26.088  1.00 107.46 ? 8   THR G CB  1 
ATOM   11444 O OG1 . THR G  1 8   ? -35.599 -14.492  26.171  1.00 121.05 ? 8   THR G OG1 1 
ATOM   11445 C CG2 . THR G  1 8   ? -37.503 -15.829  26.805  1.00 117.56 ? 8   THR G CG2 1 
ATOM   11446 N N   . LEU G  1 9   ? -33.351 -17.032  25.162  1.00 124.87 ? 9   LEU G N   1 
ATOM   11447 C CA  . LEU G  1 9   ? -32.089 -16.637  24.556  1.00 108.83 ? 9   LEU G CA  1 
ATOM   11448 C C   . LEU G  1 9   ? -32.416 -15.968  23.238  1.00 120.90 ? 9   LEU G C   1 
ATOM   11449 O O   . LEU G  1 9   ? -33.557 -16.023  22.791  1.00 120.56 ? 9   LEU G O   1 
ATOM   11450 C CB  . LEU G  1 9   ? -31.187 -17.849  24.326  1.00 96.68  ? 9   LEU G CB  1 
ATOM   11451 C CG  . LEU G  1 9   ? -29.687 -17.588  24.482  1.00 94.12  ? 9   LEU G CG  1 
ATOM   11452 C CD1 . LEU G  1 9   ? -28.896 -18.185  23.331  1.00 84.03  ? 9   LEU G CD1 1 
ATOM   11453 C CD2 . LEU G  1 9   ? -29.406 -16.100  24.610  1.00 84.53  ? 9   LEU G CD2 1 
ATOM   11454 N N   . CYS G  1 10  ? -31.431 -15.337  22.611  1.00 117.81 ? 10  CYS G N   1 
ATOM   11455 C CA  . CYS G  1 10  ? -31.684 -14.669  21.342  1.00 101.92 ? 10  CYS G CA  1 
ATOM   11456 C C   . CYS G  1 10  ? -30.429 -14.442  20.512  1.00 100.64 ? 10  CYS G C   1 
ATOM   11457 O O   . CYS G  1 10  ? -29.325 -14.879  20.861  1.00 102.24 ? 10  CYS G O   1 
ATOM   11458 C CB  . CYS G  1 10  ? -32.404 -13.338  21.561  1.00 110.22 ? 10  CYS G CB  1 
ATOM   11459 S SG  . CYS G  1 10  ? -34.138 -13.509  22.064  1.00 132.87 ? 10  CYS G SG  1 
ATOM   11460 N N   . ILE G  1 11  ? -30.621 -13.740  19.402  1.00 109.99 ? 11  ILE G N   1 
ATOM   11461 C CA  . ILE G  1 11  ? -29.636 -13.675  18.335  1.00 96.61  ? 11  ILE G CA  1 
ATOM   11462 C C   . ILE G  1 11  ? -29.990 -12.522  17.395  1.00 100.98 ? 11  ILE G C   1 
ATOM   11463 O O   . ILE G  1 11  ? -31.135 -12.399  16.955  1.00 105.64 ? 11  ILE G O   1 
ATOM   11464 C CB  . ILE G  1 11  ? -29.580 -15.016  17.536  1.00 96.59  ? 11  ILE G CB  1 
ATOM   11465 C CG1 . ILE G  1 11  ? -30.939 -15.371  16.901  1.00 103.81 ? 11  ILE G CG1 1 
ATOM   11466 C CG2 . ILE G  1 11  ? -29.068 -16.172  18.409  1.00 90.24  ? 11  ILE G CG2 1 
ATOM   11467 C CD1 . ILE G  1 11  ? -32.173 -14.770  17.553  1.00 93.53  ? 11  ILE G CD1 1 
ATOM   11468 N N   . GLY G  1 12  ? -29.013 -11.677  17.088  1.00 133.40 ? 12  GLY G N   1 
ATOM   11469 C CA  . GLY G  1 12  ? -29.270 -10.538  16.228  1.00 121.34 ? 12  GLY G CA  1 
ATOM   11470 C C   . GLY G  1 12  ? -28.051 -9.902   15.593  1.00 110.18 ? 12  GLY G C   1 
ATOM   11471 O O   . GLY G  1 12  ? -26.975 -10.496  15.527  1.00 109.12 ? 12  GLY G O   1 
ATOM   11472 N N   . TYR G  1 13  ? -28.230 -8.673   15.127  1.00 88.72  ? 13  TYR G N   1 
ATOM   11473 C CA  . TYR G  1 13  ? -27.227 -7.998   14.322  1.00 94.60  ? 13  TYR G CA  1 
ATOM   11474 C C   . TYR G  1 13  ? -27.286 -6.497   14.527  1.00 87.98  ? 13  TYR G C   1 
ATOM   11475 O O   . TYR G  1 13  ? -28.195 -5.985   15.176  1.00 85.49  ? 13  TYR G O   1 
ATOM   11476 C CB  . TYR G  1 13  ? -27.409 -8.346   12.844  1.00 78.27  ? 13  TYR G CB  1 
ATOM   11477 C CG  . TYR G  1 13  ? -28.835 -8.647   12.443  1.00 78.00  ? 13  TYR G CG  1 
ATOM   11478 C CD1 . TYR G  1 13  ? -29.639 -7.665   11.887  1.00 72.66  ? 13  TYR G CD1 1 
ATOM   11479 C CD2 . TYR G  1 13  ? -29.370 -9.917   12.609  1.00 60.03  ? 13  TYR G CD2 1 
ATOM   11480 C CE1 . TYR G  1 13  ? -30.934 -7.935   11.516  1.00 60.37  ? 13  TYR G CE1 1 
ATOM   11481 C CE2 . TYR G  1 13  ? -30.665 -10.195  12.239  1.00 62.49  ? 13  TYR G CE2 1 
ATOM   11482 C CZ  . TYR G  1 13  ? -31.443 -9.199   11.694  1.00 64.90  ? 13  TYR G CZ  1 
ATOM   11483 O OH  . TYR G  1 13  ? -32.737 -9.467   11.321  1.00 63.01  ? 13  TYR G OH  1 
ATOM   11484 N N   . HIS G  1 14  ? -26.307 -5.800   13.966  1.00 103.79 ? 14  HIS G N   1 
ATOM   11485 C CA  . HIS G  1 14  ? -26.156 -4.373   14.190  1.00 97.66  ? 14  HIS G CA  1 
ATOM   11486 C C   . HIS G  1 14  ? -27.207 -3.547   13.448  1.00 111.96 ? 14  HIS G C   1 
ATOM   11487 O O   . HIS G  1 14  ? -27.909 -4.060   12.576  1.00 119.85 ? 14  HIS G O   1 
ATOM   11488 C CB  . HIS G  1 14  ? -24.755 -3.925   13.780  1.00 108.40 ? 14  HIS G CB  1 
ATOM   11489 C CG  . HIS G  1 14  ? -24.471 -2.494   14.102  1.00 126.22 ? 14  HIS G CG  1 
ATOM   11490 N ND1 . HIS G  1 14  ? -23.971 -2.094   15.322  1.00 135.26 ? 14  HIS G ND1 1 
ATOM   11491 C CD2 . HIS G  1 14  ? -24.646 -1.365   13.377  1.00 136.05 ? 14  HIS G CD2 1 
ATOM   11492 C CE1 . HIS G  1 14  ? -23.838 -0.780   15.331  1.00 147.29 ? 14  HIS G CE1 1 
ATOM   11493 N NE2 . HIS G  1 14  ? -24.241 -0.313   14.161  1.00 145.14 ? 14  HIS G NE2 1 
ATOM   11494 N N   . ALA G  1 15  ? -27.301 -2.269   13.815  1.00 87.66  ? 15  ALA G N   1 
ATOM   11495 C CA  . ALA G  1 15  ? -28.211 -1.307   13.195  1.00 94.20  ? 15  ALA G CA  1 
ATOM   11496 C C   . ALA G  1 15  ? -27.804 0.096    13.613  1.00 90.77  ? 15  ALA G C   1 
ATOM   11497 O O   . ALA G  1 15  ? -27.201 0.279    14.668  1.00 98.97  ? 15  ALA G O   1 
ATOM   11498 C CB  . ALA G  1 15  ? -29.631 -1.571   13.619  1.00 72.31  ? 15  ALA G CB  1 
ATOM   11499 N N   . ASN G  1 16  ? -28.150 1.085    12.796  1.00 100.47 ? 16  ASN G N   1 
ATOM   11500 C CA  . ASN G  1 16  ? -27.739 2.458    13.058  1.00 111.22 ? 16  ASN G CA  1 
ATOM   11501 C C   . ASN G  1 16  ? -28.550 3.509    12.303  1.00 114.95 ? 16  ASN G C   1 
ATOM   11502 O O   . ASN G  1 16  ? -29.581 3.206    11.698  1.00 113.26 ? 16  ASN G O   1 
ATOM   11503 C CB  . ASN G  1 16  ? -26.249 2.623    12.749  1.00 118.19 ? 16  ASN G CB  1 
ATOM   11504 C CG  . ASN G  1 16  ? -25.891 2.203    11.329  1.00 121.41 ? 16  ASN G CG  1 
ATOM   11505 O OD1 . ASN G  1 16  ? -26.763 2.032    10.476  1.00 105.63 ? 16  ASN G OD1 1 
ATOM   11506 N ND2 . ASN G  1 16  ? -24.598 2.038    11.073  1.00 113.46 ? 16  ASN G ND2 1 
ATOM   11507 N N   . ASN G  1 17  ? -28.067 4.748    12.343  1.00 100.05 ? 17  ASN G N   1 
ATOM   11508 C CA  . ASN G  1 17  ? -28.723 5.862    11.670  1.00 110.53 ? 17  ASN G CA  1 
ATOM   11509 C C   . ASN G  1 17  ? -28.284 6.010    10.218  1.00 125.85 ? 17  ASN G C   1 
ATOM   11510 O O   . ASN G  1 17  ? -28.432 7.077    9.623   1.00 131.94 ? 17  ASN G O   1 
ATOM   11511 C CB  . ASN G  1 17  ? -28.470 7.171    12.426  1.00 131.32 ? 17  ASN G CB  1 
ATOM   11512 C CG  . ASN G  1 17  ? -26.995 7.535    12.501  1.00 140.96 ? 17  ASN G CG  1 
ATOM   11513 O OD1 . ASN G  1 17  ? -26.186 7.098    11.681  1.00 147.68 ? 17  ASN G OD1 1 
ATOM   11514 N ND2 . ASN G  1 17  ? -26.642 8.349    13.487  1.00 147.94 ? 17  ASN G ND2 1 
ATOM   11515 N N   . SER G  1 18  ? -27.749 4.934    9.652   1.00 112.31 ? 18  SER G N   1 
ATOM   11516 C CA  . SER G  1 18  ? -27.230 4.966    8.292   1.00 106.41 ? 18  SER G CA  1 
ATOM   11517 C C   . SER G  1 18  ? -28.348 5.050    7.258   1.00 100.60 ? 18  SER G C   1 
ATOM   11518 O O   . SER G  1 18  ? -29.357 4.352    7.357   1.00 88.23  ? 18  SER G O   1 
ATOM   11519 C CB  . SER G  1 18  ? -26.360 3.736    8.027   1.00 96.52  ? 18  SER G CB  1 
ATOM   11520 O OG  . SER G  1 18  ? -25.718 3.826    6.768   1.00 98.69  ? 18  SER G OG  1 
ATOM   11521 N N   . THR G  1 19  ? -28.160 5.918    6.270   1.00 104.98 ? 19  THR G N   1 
ATOM   11522 C CA  . THR G  1 19  ? -29.113 6.062    5.179   1.00 94.21  ? 19  THR G CA  1 
ATOM   11523 C C   . THR G  1 19  ? -28.509 5.526    3.888   1.00 89.44  ? 19  THR G C   1 
ATOM   11524 O O   . THR G  1 19  ? -29.149 5.541    2.837   1.00 92.17  ? 19  THR G O   1 
ATOM   11525 C CB  . THR G  1 19  ? -29.530 7.530    4.984   1.00 103.45 ? 19  THR G CB  1 
ATOM   11526 O OG1 . THR G  1 19  ? -28.362 8.344    4.828   1.00 115.31 ? 19  THR G OG1 1 
ATOM   11527 C CG2 . THR G  1 19  ? -30.321 8.021    6.186   1.00 105.97 ? 19  THR G CG2 1 
ATOM   11528 N N   . ASP G  1 20  ? -27.270 5.054    3.978   1.00 87.13  ? 20  ASP G N   1 
ATOM   11529 C CA  . ASP G  1 20  ? -26.584 4.473    2.832   1.00 86.54  ? 20  ASP G CA  1 
ATOM   11530 C C   . ASP G  1 20  ? -27.443 3.406    2.164   1.00 86.25  ? 20  ASP G C   1 
ATOM   11531 O O   . ASP G  1 20  ? -27.991 2.531    2.834   1.00 72.75  ? 20  ASP G O   1 
ATOM   11532 C CB  . ASP G  1 20  ? -25.246 3.867    3.261   1.00 77.64  ? 20  ASP G CB  1 
ATOM   11533 C CG  . ASP G  1 20  ? -24.233 4.919    3.666   1.00 91.44  ? 20  ASP G CG  1 
ATOM   11534 O OD1 . ASP G  1 20  ? -23.152 4.545    4.169   1.00 92.38  ? 20  ASP G OD1 1 
ATOM   11535 O OD2 . ASP G  1 20  ? -24.516 6.121    3.480   1.00 95.18  ? 20  ASP G OD2 1 
ATOM   11536 N N   . THR G  1 21  ? -27.560 3.485    0.843   1.00 89.17  ? 21  THR G N   1 
ATOM   11537 C CA  . THR G  1 21  ? -28.306 2.492    0.082   1.00 80.00  ? 21  THR G CA  1 
ATOM   11538 C C   . THR G  1 21  ? -27.458 1.921    -1.046  1.00 74.98  ? 21  THR G C   1 
ATOM   11539 O O   . THR G  1 21  ? -26.802 2.663    -1.779  1.00 86.39  ? 21  THR G O   1 
ATOM   11540 C CB  . THR G  1 21  ? -29.600 3.082    -0.505  1.00 75.04  ? 21  THR G CB  1 
ATOM   11541 O OG1 . THR G  1 21  ? -29.607 4.503    -0.321  1.00 92.77  ? 21  THR G OG1 1 
ATOM   11542 C CG2 . THR G  1 21  ? -30.810 2.491    0.186   1.00 73.25  ? 21  THR G CG2 1 
ATOM   11543 N N   . VAL G  1 22  ? -27.463 0.598    -1.170  1.00 67.71  ? 22  VAL G N   1 
ATOM   11544 C CA  . VAL G  1 22  ? -26.751 -0.072   -2.248  1.00 64.16  ? 22  VAL G CA  1 
ATOM   11545 C C   . VAL G  1 22  ? -27.727 -0.913   -3.058  1.00 68.60  ? 22  VAL G C   1 
ATOM   11546 O O   . VAL G  1 22  ? -28.865 -1.132   -2.642  1.00 65.52  ? 22  VAL G O   1 
ATOM   11547 C CB  . VAL G  1 22  ? -25.636 -0.986   -1.711  1.00 54.99  ? 22  VAL G CB  1 
ATOM   11548 C CG1 . VAL G  1 22  ? -24.794 -0.247   -0.686  1.00 60.65  ? 22  VAL G CG1 1 
ATOM   11549 C CG2 . VAL G  1 22  ? -26.232 -2.247   -1.103  1.00 50.05  ? 22  VAL G CG2 1 
ATOM   11550 N N   . ASP G  1 23  ? -27.279 -1.379   -4.218  1.00 59.96  ? 23  ASP G N   1 
ATOM   11551 C CA  . ASP G  1 23  ? -28.085 -2.265   -5.044  1.00 60.71  ? 23  ASP G CA  1 
ATOM   11552 C C   . ASP G  1 23  ? -27.465 -3.654   -5.090  1.00 56.25  ? 23  ASP G C   1 
ATOM   11553 O O   . ASP G  1 23  ? -26.246 -3.803   -5.012  1.00 58.83  ? 23  ASP G O   1 
ATOM   11554 C CB  . ASP G  1 23  ? -28.222 -1.710   -6.462  1.00 71.61  ? 23  ASP G CB  1 
ATOM   11555 C CG  . ASP G  1 23  ? -29.138 -0.505   -6.532  1.00 73.33  ? 23  ASP G CG  1 
ATOM   11556 O OD1 . ASP G  1 23  ? -29.615 -0.054   -5.470  1.00 82.96  ? 23  ASP G OD1 1 
ATOM   11557 O OD2 . ASP G  1 23  ? -29.384 -0.011   -7.653  1.00 83.00  ? 23  ASP G OD2 1 
ATOM   11558 N N   . THR G  1 24  ? -28.314 -4.668   -5.206  1.00 47.58  ? 24  THR G N   1 
ATOM   11559 C CA  . THR G  1 24  ? -27.854 -6.036   -5.392  1.00 52.63  ? 24  THR G CA  1 
ATOM   11560 C C   . THR G  1 24  ? -28.435 -6.579   -6.690  1.00 54.68  ? 24  THR G C   1 
ATOM   11561 O O   . THR G  1 24  ? -29.144 -5.870   -7.405  1.00 47.68  ? 24  THR G O   1 
ATOM   11562 C CB  . THR G  1 24  ? -28.281 -6.947   -4.225  1.00 63.80  ? 24  THR G CB  1 
ATOM   11563 O OG1 . THR G  1 24  ? -29.698 -7.152   -4.269  1.00 70.46  ? 24  THR G OG1 1 
ATOM   11564 C CG2 . THR G  1 24  ? -27.900 -6.323   -2.890  1.00 51.63  ? 24  THR G CG2 1 
ATOM   11565 N N   . VAL G  1 25  ? -28.133 -7.835   -6.994  1.00 58.58  ? 25  VAL G N   1 
ATOM   11566 C CA  . VAL G  1 25  ? -28.666 -8.465   -8.191  1.00 57.69  ? 25  VAL G CA  1 
ATOM   11567 C C   . VAL G  1 25  ? -30.158 -8.699   -8.021  1.00 60.26  ? 25  VAL G C   1 
ATOM   11568 O O   . VAL G  1 25  ? -30.923 -8.639   -8.983  1.00 48.18  ? 25  VAL G O   1 
ATOM   11569 C CB  . VAL G  1 25  ? -28.002 -9.823   -8.455  1.00 56.62  ? 25  VAL G CB  1 
ATOM   11570 C CG1 . VAL G  1 25  ? -28.100 -10.183  -9.928  1.00 58.74  ? 25  VAL G CG1 1 
ATOM   11571 C CG2 . VAL G  1 25  ? -26.556 -9.796   -8.010  1.00 62.16  ? 25  VAL G CG2 1 
ATOM   11572 N N   . LEU G  1 26  ? -30.564 -8.958   -6.782  1.00 61.25  ? 26  LEU G N   1 
ATOM   11573 C CA  . LEU G  1 26  ? -31.931 -9.371   -6.495  1.00 57.46  ? 26  LEU G CA  1 
ATOM   11574 C C   . LEU G  1 26  ? -32.809 -8.238   -5.976  1.00 63.08  ? 26  LEU G C   1 
ATOM   11575 O O   . LEU G  1 26  ? -34.035 -8.339   -6.009  1.00 60.95  ? 26  LEU G O   1 
ATOM   11576 C CB  . LEU G  1 26  ? -31.934 -10.518  -5.483  1.00 53.78  ? 26  LEU G CB  1 
ATOM   11577 C CG  . LEU G  1 26  ? -30.962 -11.667  -5.758  1.00 63.50  ? 26  LEU G CG  1 
ATOM   11578 C CD1 . LEU G  1 26  ? -31.114 -12.759  -4.706  1.00 44.92  ? 26  LEU G CD1 1 
ATOM   11579 C CD2 . LEU G  1 26  ? -31.134 -12.227  -7.166  1.00 62.67  ? 26  LEU G CD2 1 
ATOM   11580 N N   . GLU G  1 27  ? -32.189 -7.164   -5.498  1.00 71.59  ? 27  GLU G N   1 
ATOM   11581 C CA  . GLU G  1 27  ? -32.941 -6.093   -4.851  1.00 63.14  ? 27  GLU G CA  1 
ATOM   11582 C C   . GLU G  1 27  ? -32.326 -4.709   -5.073  1.00 65.72  ? 27  GLU G C   1 
ATOM   11583 O O   . GLU G  1 27  ? -31.106 -4.564   -5.146  1.00 68.90  ? 27  GLU G O   1 
ATOM   11584 C CB  . GLU G  1 27  ? -33.069 -6.387   -3.354  1.00 75.50  ? 27  GLU G CB  1 
ATOM   11585 C CG  . GLU G  1 27  ? -34.228 -5.688   -2.666  1.00 87.36  ? 27  GLU G CG  1 
ATOM   11586 C CD  . GLU G  1 27  ? -34.507 -6.258   -1.288  1.00 102.45 ? 27  GLU G CD  1 
ATOM   11587 O OE1 . GLU G  1 27  ? -35.212 -5.594   -0.499  1.00 98.18  ? 27  GLU G OE1 1 
ATOM   11588 O OE2 . GLU G  1 27  ? -34.020 -7.370   -0.994  1.00 103.73 ? 27  GLU G OE2 1 
ATOM   11589 N N   . LYS G  1 28  ? -33.185 -3.697   -5.179  1.00 62.13  ? 28  LYS G N   1 
ATOM   11590 C CA  . LYS G  1 28  ? -32.746 -2.316   -5.380  1.00 69.18  ? 28  LYS G CA  1 
ATOM   11591 C C   . LYS G  1 28  ? -33.024 -1.317   -4.254  1.00 69.17  ? 28  LYS G C   1 
ATOM   11592 O O   . LYS G  1 28  ? -34.088 -1.348   -3.635  1.00 68.37  ? 28  LYS G O   1 
ATOM   11593 C CB  . LYS G  1 28  ? -33.516 -1.668   -6.535  1.00 68.11  ? 28  LYS G CB  1 
ATOM   11594 C CG  . LYS G  1 28  ? -32.906 -1.902   -7.909  1.00 73.24  ? 28  LYS G CG  1 
ATOM   11595 C CD  . LYS G  1 28  ? -33.710 -1.197   -8.993  1.00 94.84  ? 28  LYS G CD  1 
ATOM   11596 C CE  . LYS G  1 28  ? -32.898 -1.026   -10.269 1.00 104.42 ? 28  LYS G CE  1 
ATOM   11597 N NZ  . LYS G  1 28  ? -32.358 -2.317   -10.773 1.00 99.27  ? 28  LYS G NZ  1 
ATOM   11598 N N   . ASN G  1 29  ? -32.063 -0.428   -4.010  1.00 88.62  ? 29  ASN G N   1 
ATOM   11599 C CA  . ASN G  1 29  ? -32.134 0.548    -2.919  1.00 81.99  ? 29  ASN G CA  1 
ATOM   11600 C C   . ASN G  1 29  ? -32.294 -0.173   -1.577  1.00 81.37  ? 29  ASN G C   1 
ATOM   11601 O O   . ASN G  1 29  ? -33.299 -0.002   -0.886  1.00 86.05  ? 29  ASN G O   1 
ATOM   11602 C CB  . ASN G  1 29  ? -33.159 1.688    -3.046  1.00 79.38  ? 29  ASN G CB  1 
ATOM   11603 C CG  . ASN G  1 29  ? -32.792 2.698    -4.133  1.00 114.40 ? 29  ASN G CG  1 
ATOM   11604 O OD1 . ASN G  1 29  ? -32.018 3.627    -3.904  1.00 120.91 ? 29  ASN G OD1 1 
ATOM   11605 N ND2 . ASN G  1 29  ? -33.345 2.503    -5.323  1.00 113.67 ? 29  ASN G ND2 1 
ATOM   11606 N N   . VAL G  1 30  ? -31.300 -0.981   -1.220  1.00 70.85  ? 30  VAL G N   1 
ATOM   11607 C CA  . VAL G  1 30  ? -31.277 -1.648   0.078   1.00 55.58  ? 30  VAL G CA  1 
ATOM   11608 C C   . VAL G  1 30  ? -30.411 -0.864   1.057   1.00 66.47  ? 30  VAL G C   1 
ATOM   11609 O O   . VAL G  1 30  ? -29.226 -0.642   0.808   1.00 71.29  ? 30  VAL G O   1 
ATOM   11610 C CB  . VAL G  1 30  ? -30.734 -3.087   -0.025  1.00 63.41  ? 30  VAL G CB  1 
ATOM   11611 C CG1 . VAL G  1 30  ? -30.577 -3.697   1.362   1.00 49.31  ? 30  VAL G CG1 1 
ATOM   11612 C CG2 . VAL G  1 30  ? -31.645 -3.941   -0.889  1.00 63.30  ? 30  VAL G CG2 1 
ATOM   11613 N N   . THR G  1 31  ? -31.006 -0.443   2.168   1.00 66.58  ? 31  THR G N   1 
ATOM   11614 C CA  . THR G  1 31  ? -30.286 0.329    3.174   1.00 72.76  ? 31  THR G CA  1 
ATOM   11615 C C   . THR G  1 31  ? -29.325 -0.552   3.963   1.00 69.29  ? 31  THR G C   1 
ATOM   11616 O O   . THR G  1 31  ? -29.725 -1.564   4.537   1.00 73.16  ? 31  THR G O   1 
ATOM   11617 C CB  . THR G  1 31  ? -31.250 1.027    4.151   1.00 77.76  ? 31  THR G CB  1 
ATOM   11618 O OG1 . THR G  1 31  ? -32.142 1.878    3.421   1.00 73.84  ? 31  THR G OG1 1 
ATOM   11619 C CG2 . THR G  1 31  ? -30.474 1.860    5.161   1.00 80.64  ? 31  THR G CG2 1 
ATOM   11620 N N   . VAL G  1 32  ? -28.056 -0.160   3.989   1.00 76.95  ? 32  VAL G N   1 
ATOM   11621 C CA  . VAL G  1 32  ? -27.037 -0.916   4.707   1.00 66.62  ? 32  VAL G CA  1 
ATOM   11622 C C   . VAL G  1 32  ? -26.409 -0.089   5.824   1.00 70.18  ? 32  VAL G C   1 
ATOM   11623 O O   . VAL G  1 32  ? -26.464 1.141    5.807   1.00 80.67  ? 32  VAL G O   1 
ATOM   11624 C CB  . VAL G  1 32  ? -25.929 -1.416   3.760   1.00 69.14  ? 32  VAL G CB  1 
ATOM   11625 C CG1 . VAL G  1 32  ? -26.470 -2.493   2.832   1.00 66.43  ? 32  VAL G CG1 1 
ATOM   11626 C CG2 . VAL G  1 32  ? -25.341 -0.255   2.967   1.00 64.83  ? 32  VAL G CG2 1 
ATOM   11627 N N   . THR G  1 33  ? -25.812 -0.775   6.793   1.00 79.28  ? 33  THR G N   1 
ATOM   11628 C CA  . THR G  1 33  ? -25.189 -0.117   7.936   1.00 77.73  ? 33  THR G CA  1 
ATOM   11629 C C   . THR G  1 33  ? -23.911 0.617    7.540   1.00 85.68  ? 33  THR G C   1 
ATOM   11630 O O   . THR G  1 33  ? -23.639 1.714    8.029   1.00 93.21  ? 33  THR G O   1 
ATOM   11631 C CB  . THR G  1 33  ? -24.859 -1.125   9.055   1.00 75.17  ? 33  THR G CB  1 
ATOM   11632 O OG1 . THR G  1 33  ? -23.958 -2.122   8.555   1.00 77.29  ? 33  THR G OG1 1 
ATOM   11633 C CG2 . THR G  1 33  ? -26.125 -1.800   9.557   1.00 74.11  ? 33  THR G CG2 1 
ATOM   11634 N N   . HIS G  1 34  ? -23.129 0.006    6.656   1.00 75.18  ? 34  HIS G N   1 
ATOM   11635 C CA  . HIS G  1 34  ? -21.863 0.586    6.227   1.00 80.94  ? 34  HIS G CA  1 
ATOM   11636 C C   . HIS G  1 34  ? -21.595 0.301    4.753   1.00 81.54  ? 34  HIS G C   1 
ATOM   11637 O O   . HIS G  1 34  ? -22.065 -0.699   4.211   1.00 79.02  ? 34  HIS G O   1 
ATOM   11638 C CB  . HIS G  1 34  ? -20.716 0.042    7.079   1.00 74.13  ? 34  HIS G CB  1 
ATOM   11639 C CG  . HIS G  1 34  ? -20.900 0.258    8.548   1.00 87.83  ? 34  HIS G CG  1 
ATOM   11640 N ND1 . HIS G  1 34  ? -21.775 -0.489   9.307   1.00 77.86  ? 34  HIS G ND1 1 
ATOM   11641 C CD2 . HIS G  1 34  ? -20.317 1.134    9.402   1.00 101.00 ? 34  HIS G CD2 1 
ATOM   11642 C CE1 . HIS G  1 34  ? -21.727 -0.080   10.562  1.00 86.83  ? 34  HIS G CE1 1 
ATOM   11643 N NE2 . HIS G  1 34  ? -20.850 0.903    10.647  1.00 109.54 ? 34  HIS G NE2 1 
ATOM   11644 N N   . SER G  1 35  ? -20.835 1.182    4.110   1.00 74.15  ? 35  SER G N   1 
ATOM   11645 C CA  . SER G  1 35  ? -20.497 1.013    2.701   1.00 72.57  ? 35  SER G CA  1 
ATOM   11646 C C   . SER G  1 35  ? -19.348 1.922    2.276   1.00 70.79  ? 35  SER G C   1 
ATOM   11647 O O   . SER G  1 35  ? -18.967 2.841    3.000   1.00 82.84  ? 35  SER G O   1 
ATOM   11648 C CB  . SER G  1 35  ? -21.722 1.271    1.820   1.00 70.81  ? 35  SER G CB  1 
ATOM   11649 O OG  . SER G  1 35  ? -22.221 2.584    2.011   1.00 76.70  ? 35  SER G OG  1 
ATOM   11650 N N   . VAL G  1 36  ? -18.801 1.651    1.096   1.00 66.20  ? 36  VAL G N   1 
ATOM   11651 C CA  . VAL G  1 36  ? -17.734 2.465    0.531   1.00 72.43  ? 36  VAL G CA  1 
ATOM   11652 C C   . VAL G  1 36  ? -18.032 2.750    -0.934  1.00 74.62  ? 36  VAL G C   1 
ATOM   11653 O O   . VAL G  1 36  ? -18.740 1.987    -1.588  1.00 67.40  ? 36  VAL G O   1 
ATOM   11654 C CB  . VAL G  1 36  ? -16.369 1.759    0.628   1.00 63.55  ? 36  VAL G CB  1 
ATOM   11655 C CG1 . VAL G  1 36  ? -16.037 1.442    2.076   1.00 69.54  ? 36  VAL G CG1 1 
ATOM   11656 C CG2 . VAL G  1 36  ? -16.366 0.492    -0.216  1.00 58.56  ? 36  VAL G CG2 1 
ATOM   11657 N N   . ASN G  1 37  ? -17.497 3.851    -1.447  1.00 79.53  ? 37  ASN G N   1 
ATOM   11658 C CA  . ASN G  1 37  ? -17.679 4.185    -2.854  1.00 76.60  ? 37  ASN G CA  1 
ATOM   11659 C C   . ASN G  1 37  ? -16.460 3.782    -3.677  1.00 75.38  ? 37  ASN G C   1 
ATOM   11660 O O   . ASN G  1 37  ? -15.334 4.163    -3.358  1.00 82.74  ? 37  ASN G O   1 
ATOM   11661 C CB  . ASN G  1 37  ? -17.974 5.676    -3.026  1.00 70.73  ? 37  ASN G CB  1 
ATOM   11662 C CG  . ASN G  1 37  ? -18.605 5.993    -4.369  1.00 88.60  ? 37  ASN G CG  1 
ATOM   11663 O OD1 . ASN G  1 37  ? -18.770 7.157    -4.733  1.00 101.64 ? 37  ASN G OD1 1 
ATOM   11664 N ND2 . ASN G  1 37  ? -18.966 4.952    -5.112  1.00 75.91  ? 37  ASN G ND2 1 
ATOM   11665 N N   . LEU G  1 38  ? -16.687 3.000    -4.727  1.00 65.86  ? 38  LEU G N   1 
ATOM   11666 C CA  . LEU G  1 38  ? -15.603 2.543    -5.590  1.00 59.04  ? 38  LEU G CA  1 
ATOM   11667 C C   . LEU G  1 38  ? -15.408 3.509    -6.751  1.00 57.12  ? 38  LEU G C   1 
ATOM   11668 O O   . LEU G  1 38  ? -14.466 3.382    -7.536  1.00 56.84  ? 38  LEU G O   1 
ATOM   11669 C CB  . LEU G  1 38  ? -15.893 1.135    -6.118  1.00 46.97  ? 38  LEU G CB  1 
ATOM   11670 C CG  . LEU G  1 38  ? -15.870 -0.008   -5.099  1.00 47.06  ? 38  LEU G CG  1 
ATOM   11671 C CD1 . LEU G  1 38  ? -16.488 -1.267   -5.686  1.00 60.99  ? 38  LEU G CD1 1 
ATOM   11672 C CD2 . LEU G  1 38  ? -14.451 -0.276   -4.618  1.00 54.59  ? 38  LEU G CD2 1 
ATOM   11673 N N   . LEU G  1 39  ? -16.305 4.482    -6.847  1.00 54.92  ? 39  LEU G N   1 
ATOM   11674 C CA  . LEU G  1 39  ? -16.291 5.426    -7.952  1.00 58.56  ? 39  LEU G CA  1 
ATOM   11675 C C   . LEU G  1 39  ? -15.727 6.773    -7.506  1.00 65.58  ? 39  LEU G C   1 
ATOM   11676 O O   . LEU G  1 39  ? -16.272 7.408    -6.605  1.00 70.74  ? 39  LEU G O   1 
ATOM   11677 C CB  . LEU G  1 39  ? -17.712 5.612    -8.484  1.00 54.79  ? 39  LEU G CB  1 
ATOM   11678 C CG  . LEU G  1 39  ? -17.911 6.004    -9.948  1.00 53.10  ? 39  LEU G CG  1 
ATOM   11679 C CD1 . LEU G  1 39  ? -19.105 6.934    -10.082 1.00 56.43  ? 39  LEU G CD1 1 
ATOM   11680 C CD2 . LEU G  1 39  ? -16.647 6.575    -10.566 1.00 52.49  ? 39  LEU G CD2 1 
ATOM   11681 N N   . GLU G  1 40  ? -14.630 7.201    -8.125  1.00 64.66  ? 40  GLU G N   1 
ATOM   11682 C CA  . GLU G  1 40  ? -14.076 8.526    -7.858  1.00 62.87  ? 40  GLU G CA  1 
ATOM   11683 C C   . GLU G  1 40  ? -14.748 9.552    -8.759  1.00 62.15  ? 40  GLU G C   1 
ATOM   11684 O O   . GLU G  1 40  ? -14.783 9.393    -9.979  1.00 60.75  ? 40  GLU G O   1 
ATOM   11685 C CB  . GLU G  1 40  ? -12.558 8.551    -8.060  1.00 57.06  ? 40  GLU G CB  1 
ATOM   11686 C CG  . GLU G  1 40  ? -11.905 9.910    -7.795  1.00 71.08  ? 40  GLU G CG  1 
ATOM   11687 C CD  . GLU G  1 40  ? -12.120 10.409   -6.373  1.00 81.97  ? 40  GLU G CD  1 
ATOM   11688 O OE1 . GLU G  1 40  ? -11.120 10.602   -5.650  1.00 90.14  ? 40  GLU G OE1 1 
ATOM   11689 O OE2 . GLU G  1 40  ? -13.287 10.611   -5.978  1.00 76.81  ? 40  GLU G OE2 1 
ATOM   11690 N N   . ASP G  1 41  ? -15.291 10.598   -8.149  1.00 60.06  ? 41  ASP G N   1 
ATOM   11691 C CA  . ASP G  1 41  ? -16.017 11.623   -8.884  1.00 70.68  ? 41  ASP G CA  1 
ATOM   11692 C C   . ASP G  1 41  ? -15.620 13.011   -8.404  1.00 74.71  ? 41  ASP G C   1 
ATOM   11693 O O   . ASP G  1 41  ? -16.450 13.918   -8.347  1.00 92.17  ? 41  ASP G O   1 
ATOM   11694 C CB  . ASP G  1 41  ? -17.525 11.421   -8.722  1.00 75.11  ? 41  ASP G CB  1 
ATOM   11695 C CG  . ASP G  1 41  ? -17.958 11.389   -7.267  1.00 105.03 ? 41  ASP G CG  1 
ATOM   11696 O OD1 . ASP G  1 41  ? -17.095 11.558   -6.379  1.00 101.65 ? 41  ASP G OD1 1 
ATOM   11697 O OD2 . ASP G  1 41  ? -19.165 11.193   -7.010  1.00 108.23 ? 41  ASP G OD2 1 
ATOM   11698 N N   . LYS G  1 42  ? -14.346 13.174   -8.064  1.00 76.40  ? 42  LYS G N   1 
ATOM   11699 C CA  . LYS G  1 42  ? -13.873 14.425   -7.489  1.00 79.91  ? 42  LYS G CA  1 
ATOM   11700 C C   . LYS G  1 42  ? -12.438 14.744   -7.902  1.00 78.95  ? 42  LYS G C   1 
ATOM   11701 O O   . LYS G  1 42  ? -11.501 14.035   -7.533  1.00 73.27  ? 42  LYS G O   1 
ATOM   11702 C CB  . LYS G  1 42  ? -13.983 14.371   -5.965  1.00 84.11  ? 42  LYS G CB  1 
ATOM   11703 C CG  . LYS G  1 42  ? -14.553 15.627   -5.335  1.00 107.88 ? 42  LYS G CG  1 
ATOM   11704 C CD  . LYS G  1 42  ? -15.114 15.322   -3.958  1.00 126.63 ? 42  LYS G CD  1 
ATOM   11705 C CE  . LYS G  1 42  ? -16.170 14.230   -4.038  1.00 115.53 ? 42  LYS G CE  1 
ATOM   11706 N NZ  . LYS G  1 42  ? -16.656 13.814   -2.694  1.00 121.18 ? 42  LYS G NZ  1 
ATOM   11707 N N   . HIS G  1 43  ? -12.280 15.817   -8.669  1.00 58.53  ? 43  HIS G N   1 
ATOM   11708 C CA  . HIS G  1 43  ? -10.967 16.279   -9.099  1.00 68.51  ? 43  HIS G CA  1 
ATOM   11709 C C   . HIS G  1 43  ? -10.623 17.581   -8.384  1.00 73.72  ? 43  HIS G C   1 
ATOM   11710 O O   . HIS G  1 43  ? -11.513 18.285   -7.908  1.00 71.09  ? 43  HIS G O   1 
ATOM   11711 C CB  . HIS G  1 43  ? -10.951 16.494   -10.613 1.00 67.65  ? 43  HIS G CB  1 
ATOM   11712 C CG  . HIS G  1 43  ? -11.953 17.496   -11.088 1.00 64.69  ? 43  HIS G CG  1 
ATOM   11713 N ND1 . HIS G  1 43  ? -11.621 18.806   -11.375 1.00 65.62  ? 43  HIS G ND1 1 
ATOM   11714 C CD2 . HIS G  1 43  ? -13.283 17.391   -11.322 1.00 64.90  ? 43  HIS G CD2 1 
ATOM   11715 C CE1 . HIS G  1 43  ? -12.699 19.456   -11.767 1.00 72.56  ? 43  HIS G CE1 1 
ATOM   11716 N NE2 . HIS G  1 43  ? -13.723 18.621   -11.745 1.00 71.37  ? 43  HIS G NE2 1 
ATOM   11717 N N   . ASN G  1 44  ? -9.335  17.902   -8.309  1.00 67.55  ? 44  ASN G N   1 
ATOM   11718 C CA  . ASN G  1 44  ? -8.899  19.116   -7.623  1.00 68.30  ? 44  ASN G CA  1 
ATOM   11719 C C   . ASN G  1 44  ? -8.988  20.368   -8.495  1.00 74.02  ? 44  ASN G C   1 
ATOM   11720 O O   . ASN G  1 44  ? -8.688  21.472   -8.042  1.00 71.75  ? 44  ASN G O   1 
ATOM   11721 C CB  . ASN G  1 44  ? -7.485  18.949   -7.055  1.00 58.16  ? 44  ASN G CB  1 
ATOM   11722 C CG  . ASN G  1 44  ? -6.441  18.714   -8.131  1.00 71.45  ? 44  ASN G CG  1 
ATOM   11723 O OD1 . ASN G  1 44  ? -5.267  18.497   -7.832  1.00 83.71  ? 44  ASN G OD1 1 
ATOM   11724 N ND2 . ASN G  1 44  ? -6.861  18.758   -9.390  1.00 77.60  ? 44  ASN G ND2 1 
ATOM   11725 N N   . GLY G  1 45  ? -9.400  20.187   -9.746  1.00 68.68  ? 45  GLY G N   1 
ATOM   11726 C CA  . GLY G  1 45  ? -9.566  21.299   -10.664 1.00 76.42  ? 45  GLY G CA  1 
ATOM   11727 C C   . GLY G  1 45  ? -8.273  22.034   -10.961 1.00 76.07  ? 45  GLY G C   1 
ATOM   11728 O O   . GLY G  1 45  ? -8.282  23.223   -11.282 1.00 68.17  ? 45  GLY G O   1 
ATOM   11729 N N   . LYS G  1 46  ? -7.156  21.323   -10.850 1.00 74.66  ? 46  LYS G N   1 
ATOM   11730 C CA  . LYS G  1 46  ? -5.849  21.894   -11.142 1.00 69.27  ? 46  LYS G CA  1 
ATOM   11731 C C   . LYS G  1 46  ? -5.135  21.058   -12.190 1.00 66.03  ? 46  LYS G C   1 
ATOM   11732 O O   . LYS G  1 46  ? -5.203  19.829   -12.166 1.00 74.72  ? 46  LYS G O   1 
ATOM   11733 C CB  . LYS G  1 46  ? -4.984  21.929   -9.882  1.00 81.29  ? 46  LYS G CB  1 
ATOM   11734 C CG  . LYS G  1 46  ? -5.537  22.751   -8.733  1.00 82.14  ? 46  LYS G CG  1 
ATOM   11735 C CD  . LYS G  1 46  ? -4.740  22.472   -7.466  1.00 108.54 ? 46  LYS G CD  1 
ATOM   11736 C CE  . LYS G  1 46  ? -5.154  23.381   -6.321  1.00 123.22 ? 46  LYS G CE  1 
ATOM   11737 N NZ  . LYS G  1 46  ? -4.455  23.013   -5.056  1.00 115.03 ? 46  LYS G NZ  1 
ATOM   11738 N N   . LEU G  1 47  ? -4.449  21.723   -13.111 1.00 73.05  ? 47  LEU G N   1 
ATOM   11739 C CA  . LEU G  1 47  ? -3.545  21.028   -14.015 1.00 77.12  ? 47  LEU G CA  1 
ATOM   11740 C C   . LEU G  1 47  ? -2.196  20.884   -13.320 1.00 68.88  ? 47  LEU G C   1 
ATOM   11741 O O   . LEU G  1 47  ? -1.359  21.786   -13.371 1.00 68.89  ? 47  LEU G O   1 
ATOM   11742 C CB  . LEU G  1 47  ? -3.399  21.783   -15.335 1.00 61.07  ? 47  LEU G CB  1 
ATOM   11743 C CG  . LEU G  1 47  ? -4.690  21.950   -16.141 1.00 59.48  ? 47  LEU G CG  1 
ATOM   11744 C CD1 . LEU G  1 47  ? -4.388  22.435   -17.551 1.00 57.59  ? 47  LEU G CD1 1 
ATOM   11745 C CD2 . LEU G  1 47  ? -5.502  20.660   -16.168 1.00 58.82  ? 47  LEU G CD2 1 
ATOM   11746 N N   . CYS G  1 48  ? -2.003  19.742   -12.664 1.00 74.49  ? 48  CYS G N   1 
ATOM   11747 C CA  . CYS G  1 48  ? -0.834  19.500   -11.821 1.00 84.65  ? 48  CYS G CA  1 
ATOM   11748 C C   . CYS G  1 48  ? 0.293   18.799   -12.572 1.00 81.57  ? 48  CYS G C   1 
ATOM   11749 O O   . CYS G  1 48  ? 0.111   18.334   -13.694 1.00 80.83  ? 48  CYS G O   1 
ATOM   11750 C CB  . CYS G  1 48  ? -1.225  18.645   -10.613 1.00 79.08  ? 48  CYS G CB  1 
ATOM   11751 S SG  . CYS G  1 48  ? -2.692  19.199   -9.715  1.00 118.98 ? 48  CYS G SG  1 
ATOM   11752 N N   . LYS G  1 49  ? 1.458   18.708   -11.939 1.00 65.25  ? 49  LYS G N   1 
ATOM   11753 C CA  . LYS G  1 49  ? 2.578   18.002   -12.542 1.00 70.93  ? 49  LYS G CA  1 
ATOM   11754 C C   . LYS G  1 49  ? 2.279   16.512   -12.551 1.00 68.68  ? 49  LYS G C   1 
ATOM   11755 O O   . LYS G  1 49  ? 1.492   16.021   -11.741 1.00 84.05  ? 49  LYS G O   1 
ATOM   11756 C CB  . LYS G  1 49  ? 3.881   18.299   -11.800 1.00 76.47  ? 49  LYS G CB  1 
ATOM   11757 C CG  . LYS G  1 49  ? 4.048   19.761   -11.422 1.00 83.66  ? 49  LYS G CG  1 
ATOM   11758 C CD  . LYS G  1 49  ? 5.380   20.017   -10.727 1.00 92.78  ? 49  LYS G CD  1 
ATOM   11759 C CE  . LYS G  1 49  ? 5.198   20.821   -9.448  1.00 96.64  ? 49  LYS G CE  1 
ATOM   11760 N NZ  . LYS G  1 49  ? 6.453   20.863   -8.648  1.00 96.96  ? 49  LYS G NZ  1 
ATOM   11761 N N   . LEU G  1 50  ? 2.900   15.789   -13.473 1.00 83.84  ? 50  LEU G N   1 
ATOM   11762 C CA  . LEU G  1 50  ? 2.500   14.405   -13.714 1.00 90.26  ? 50  LEU G CA  1 
ATOM   11763 C C   . LEU G  1 50  ? 3.364   13.337   -13.033 1.00 98.18  ? 50  LEU G C   1 
ATOM   11764 O O   . LEU G  1 50  ? 2.836   12.418   -12.420 1.00 110.01 ? 50  LEU G O   1 
ATOM   11765 C CB  . LEU G  1 50  ? 2.424   14.123   -15.220 1.00 84.77  ? 50  LEU G CB  1 
ATOM   11766 C CG  . LEU G  1 50  ? 1.322   13.192   -15.750 1.00 75.54  ? 50  LEU G CG  1 
ATOM   11767 C CD1 . LEU G  1 50  ? 1.583   12.766   -17.198 1.00 67.17  ? 50  LEU G CD1 1 
ATOM   11768 C CD2 . LEU G  1 50  ? 1.171   11.982   -14.858 1.00 76.46  ? 50  LEU G CD2 1 
ATOM   11769 N N   . ARG G  1 51  ? 4.682   13.465   -13.129 1.00 84.59  ? 51  ARG G N   1 
ATOM   11770 C CA  . ARG G  1 51  ? 5.588   12.637   -12.332 1.00 98.75  ? 51  ARG G CA  1 
ATOM   11771 C C   . ARG G  1 51  ? 6.030   13.504   -11.160 1.00 104.14 ? 51  ARG G C   1 
ATOM   11772 O O   . ARG G  1 51  ? 5.475   13.433   -10.063 1.00 119.05 ? 51  ARG G O   1 
ATOM   11773 C CB  . ARG G  1 51  ? 6.821   12.184   -13.118 1.00 109.78 ? 51  ARG G CB  1 
ATOM   11774 C CG  . ARG G  1 51  ? 6.500   11.664   -14.490 1.00 121.96 ? 51  ARG G CG  1 
ATOM   11775 C CD  . ARG G  1 51  ? 7.580   10.732   -14.981 1.00 151.02 ? 51  ARG G CD  1 
ATOM   11776 N NE  . ARG G  1 51  ? 7.612   9.491    -14.212 1.00 165.57 ? 51  ARG G NE  1 
ATOM   11777 C CZ  . ARG G  1 51  ? 8.687   9.026    -13.584 1.00 155.93 ? 51  ARG G CZ  1 
ATOM   11778 N NH1 . ARG G  1 51  ? 9.831   9.695    -13.631 1.00 141.94 ? 51  ARG G NH1 1 
ATOM   11779 N NH2 . ARG G  1 51  ? 8.620   7.885    -12.911 1.00 141.44 ? 51  ARG G NH2 1 
ATOM   11780 N N   . GLY G  1 52  ? 7.050   14.316   -11.415 1.00 92.17  ? 52  GLY G N   1 
ATOM   11781 C CA  . GLY G  1 52  ? 7.443   15.416   -10.553 1.00 100.89 ? 52  GLY G CA  1 
ATOM   11782 C C   . GLY G  1 52  ? 7.737   16.561   -11.501 1.00 105.91 ? 52  GLY G C   1 
ATOM   11783 O O   . GLY G  1 52  ? 8.174   17.643   -11.105 1.00 105.36 ? 52  GLY G O   1 
ATOM   11784 N N   . VAL G  1 53  ? 7.487   16.298   -12.780 1.00 96.04  ? 53  VAL G N   1 
ATOM   11785 C CA  . VAL G  1 53  ? 7.754   17.258   -13.842 1.00 74.21  ? 53  VAL G CA  1 
ATOM   11786 C C   . VAL G  1 53  ? 6.506   18.075   -14.169 1.00 72.75  ? 53  VAL G C   1 
ATOM   11787 O O   . VAL G  1 53  ? 5.393   17.548   -14.192 1.00 71.66  ? 53  VAL G O   1 
ATOM   11788 C CB  . VAL G  1 53  ? 8.245   16.557   -15.123 1.00 70.40  ? 53  VAL G CB  1 
ATOM   11789 C CG1 . VAL G  1 53  ? 8.651   17.589   -16.168 1.00 66.99  ? 53  VAL G CG1 1 
ATOM   11790 C CG2 . VAL G  1 53  ? 9.396   15.605   -14.808 1.00 54.24  ? 53  VAL G CG2 1 
ATOM   11791 N N   . ALA G  1 54  ? 6.699   19.365   -14.418 1.00 70.51  ? 54  ALA G N   1 
ATOM   11792 C CA  . ALA G  1 54  ? 5.588   20.260   -14.717 1.00 66.67  ? 54  ALA G CA  1 
ATOM   11793 C C   . ALA G  1 54  ? 5.205   20.204   -16.190 1.00 68.34  ? 54  ALA G C   1 
ATOM   11794 O O   . ALA G  1 54  ? 6.032   19.877   -17.041 1.00 68.74  ? 54  ALA G O   1 
ATOM   11795 C CB  . ALA G  1 54  ? 5.933   21.685   -14.313 1.00 74.17  ? 54  ALA G CB  1 
ATOM   11796 N N   . PRO G  1 55  ? 3.938   20.514   -16.492 1.00 60.29  ? 55  PRO G N   1 
ATOM   11797 C CA  . PRO G  1 55  ? 3.461   20.599   -17.873 1.00 52.66  ? 55  PRO G CA  1 
ATOM   11798 C C   . PRO G  1 55  ? 3.987   21.852   -18.566 1.00 65.40  ? 55  PRO G C   1 
ATOM   11799 O O   . PRO G  1 55  ? 4.325   22.829   -17.897 1.00 75.00  ? 55  PRO G O   1 
ATOM   11800 C CB  . PRO G  1 55  ? 1.946   20.700   -17.700 1.00 55.45  ? 55  PRO G CB  1 
ATOM   11801 C CG  . PRO G  1 55  ? 1.761   21.301   -16.361 1.00 55.82  ? 55  PRO G CG  1 
ATOM   11802 C CD  . PRO G  1 55  ? 2.842   20.696   -15.525 1.00 55.22  ? 55  PRO G CD  1 
ATOM   11803 N N   . LEU G  1 56  ? 4.062   21.816   -19.892 1.00 68.79  ? 56  LEU G N   1 
ATOM   11804 C CA  . LEU G  1 56  ? 4.447   22.987   -20.667 1.00 54.19  ? 56  LEU G CA  1 
ATOM   11805 C C   . LEU G  1 56  ? 3.199   23.765   -21.063 1.00 60.30  ? 56  LEU G C   1 
ATOM   11806 O O   . LEU G  1 56  ? 2.451   23.344   -21.945 1.00 70.20  ? 56  LEU G O   1 
ATOM   11807 C CB  . LEU G  1 56  ? 5.225   22.569   -21.916 1.00 57.54  ? 56  LEU G CB  1 
ATOM   11808 C CG  . LEU G  1 56  ? 5.693   23.686   -22.850 1.00 57.21  ? 56  LEU G CG  1 
ATOM   11809 C CD1 . LEU G  1 56  ? 6.673   24.602   -22.137 1.00 65.62  ? 56  LEU G CD1 1 
ATOM   11810 C CD2 . LEU G  1 56  ? 6.319   23.104   -24.108 1.00 66.47  ? 56  LEU G CD2 1 
ATOM   11811 N N   . HIS G  1 57  ? 2.970   24.897   -20.405 1.00 62.23  ? 57  HIS G N   1 
ATOM   11812 C CA  . HIS G  1 57  ? 1.785   25.700   -20.683 1.00 63.25  ? 57  HIS G CA  1 
ATOM   11813 C C   . HIS G  1 57  ? 2.080   26.785   -21.715 1.00 72.61  ? 57  HIS G C   1 
ATOM   11814 O O   . HIS G  1 57  ? 2.937   27.640   -21.499 1.00 77.18  ? 57  HIS G O   1 
ATOM   11815 C CB  . HIS G  1 57  ? 1.239   26.324   -19.398 1.00 64.65  ? 57  HIS G CB  1 
ATOM   11816 C CG  . HIS G  1 57  ? -0.172  26.808   -19.519 1.00 72.76  ? 57  HIS G CG  1 
ATOM   11817 N ND1 . HIS G  1 57  ? -0.494  28.034   -20.061 1.00 74.82  ? 57  HIS G ND1 1 
ATOM   11818 C CD2 . HIS G  1 57  ? -1.345  26.228   -19.177 1.00 76.01  ? 57  HIS G CD2 1 
ATOM   11819 C CE1 . HIS G  1 57  ? -1.805  28.188   -20.044 1.00 81.50  ? 57  HIS G CE1 1 
ATOM   11820 N NE2 . HIS G  1 57  ? -2.347  27.107   -19.512 1.00 85.28  ? 57  HIS G NE2 1 
ATOM   11821 N N   . LEU G  1 58  ? 1.362   26.747   -22.834 1.00 83.74  ? 58  LEU G N   1 
ATOM   11822 C CA  . LEU G  1 58  ? 1.611   27.669   -23.940 1.00 77.06  ? 58  LEU G CA  1 
ATOM   11823 C C   . LEU G  1 58  ? 0.841   28.981   -23.850 1.00 81.47  ? 58  LEU G C   1 
ATOM   11824 O O   . LEU G  1 58  ? 1.171   29.949   -24.535 1.00 84.32  ? 58  LEU G O   1 
ATOM   11825 C CB  . LEU G  1 58  ? 1.315   26.991   -25.273 1.00 64.67  ? 58  LEU G CB  1 
ATOM   11826 C CG  . LEU G  1 58  ? 2.483   26.287   -25.966 1.00 56.69  ? 58  LEU G CG  1 
ATOM   11827 C CD1 . LEU G  1 58  ? 3.533   25.804   -24.975 1.00 68.85  ? 58  LEU G CD1 1 
ATOM   11828 C CD2 . LEU G  1 58  ? 1.969   25.154   -26.834 1.00 65.87  ? 58  LEU G CD2 1 
ATOM   11829 N N   . GLY G  1 59  ? -0.189  29.010   -23.015 1.00 78.87  ? 59  GLY G N   1 
ATOM   11830 C CA  . GLY G  1 59  ? -0.977  30.213   -22.837 1.00 76.05  ? 59  GLY G CA  1 
ATOM   11831 C C   . GLY G  1 59  ? -1.731  30.624   -24.087 1.00 84.22  ? 59  GLY G C   1 
ATOM   11832 O O   . GLY G  1 59  ? -2.581  29.885   -24.582 1.00 87.46  ? 59  GLY G O   1 
ATOM   11833 N N   . LYS G  1 60  ? -1.412  31.807   -24.603 1.00 98.10  ? 60  LYS G N   1 
ATOM   11834 C CA  . LYS G  1 60  ? -2.125  32.369   -25.746 1.00 102.46 ? 60  LYS G CA  1 
ATOM   11835 C C   . LYS G  1 60  ? -1.662  31.775   -27.076 1.00 89.86  ? 60  LYS G C   1 
ATOM   11836 O O   . LYS G  1 60  ? -2.223  32.085   -28.127 1.00 98.83  ? 60  LYS G O   1 
ATOM   11837 C CB  . LYS G  1 60  ? -1.954  33.891   -25.778 1.00 107.22 ? 60  LYS G CB  1 
ATOM   11838 C CG  . LYS G  1 60  ? -2.876  34.602   -26.755 1.00 138.95 ? 60  LYS G CG  1 
ATOM   11839 C CD  . LYS G  1 60  ? -4.331  34.444   -26.351 1.00 149.70 ? 60  LYS G CD  1 
ATOM   11840 C CE  . LYS G  1 60  ? -4.599  35.087   -24.999 1.00 157.39 ? 60  LYS G CE  1 
ATOM   11841 N NZ  . LYS G  1 60  ? -6.025  34.950   -24.592 1.00 148.50 ? 60  LYS G NZ  1 
ATOM   11842 N N   . CYS G  1 61  ? -0.644  30.922   -27.029 1.00 86.96  ? 61  CYS G N   1 
ATOM   11843 C CA  . CYS G  1 61  ? -0.058  30.379   -28.248 1.00 76.27  ? 61  CYS G CA  1 
ATOM   11844 C C   . CYS G  1 61  ? -0.197  28.863   -28.334 1.00 75.92  ? 61  CYS G C   1 
ATOM   11845 O O   . CYS G  1 61  ? -0.309  28.185   -27.316 1.00 87.09  ? 61  CYS G O   1 
ATOM   11846 C CB  . CYS G  1 61  ? 1.418   30.776   -28.350 1.00 75.24  ? 61  CYS G CB  1 
ATOM   11847 S SG  . CYS G  1 61  ? 1.744   32.545   -28.204 1.00 117.76 ? 61  CYS G SG  1 
ATOM   11848 N N   . ASN G  1 62  ? -0.181  28.341   -29.556 1.00 63.00  ? 62  ASN G N   1 
ATOM   11849 C CA  . ASN G  1 62  ? -0.227  26.901   -29.774 1.00 72.15  ? 62  ASN G CA  1 
ATOM   11850 C C   . ASN G  1 62  ? 1.148   26.352   -30.146 1.00 68.77  ? 62  ASN G C   1 
ATOM   11851 O O   . ASN G  1 62  ? 2.094   27.115   -30.345 1.00 66.52  ? 62  ASN G O   1 
ATOM   11852 C CB  . ASN G  1 62  ? -1.259  26.549   -30.847 1.00 74.60  ? 62  ASN G CB  1 
ATOM   11853 C CG  . ASN G  1 62  ? -0.998  27.254   -32.162 1.00 69.52  ? 62  ASN G CG  1 
ATOM   11854 O OD1 . ASN G  1 62  ? 0.133   27.630   -32.465 1.00 71.81  ? 62  ASN G OD1 1 
ATOM   11855 N ND2 . ASN G  1 62  ? -2.048  27.437   -32.954 1.00 69.79  ? 62  ASN G ND2 1 
ATOM   11856 N N   . ILE G  1 63  ? 1.254   25.030   -30.240 1.00 58.80  ? 63  ILE G N   1 
ATOM   11857 C CA  . ILE G  1 63  ? 2.525   24.383   -30.554 1.00 55.26  ? 63  ILE G CA  1 
ATOM   11858 C C   . ILE G  1 63  ? 3.218   25.046   -31.742 1.00 56.16  ? 63  ILE G C   1 
ATOM   11859 O O   . ILE G  1 63  ? 4.401   25.379   -31.673 1.00 57.10  ? 63  ILE G O   1 
ATOM   11860 C CB  . ILE G  1 63  ? 2.337   22.882   -30.844 1.00 55.28  ? 63  ILE G CB  1 
ATOM   11861 C CG1 . ILE G  1 63  ? 1.744   22.174   -29.625 1.00 55.28  ? 63  ILE G CG1 1 
ATOM   11862 C CG2 . ILE G  1 63  ? 3.661   22.244   -31.215 1.00 51.99  ? 63  ILE G CG2 1 
ATOM   11863 C CD1 . ILE G  1 63  ? 2.668   22.147   -28.430 1.00 63.43  ? 63  ILE G CD1 1 
ATOM   11864 N N   . ALA G  1 64  ? 2.474   25.242   -32.826 1.00 56.38  ? 64  ALA G N   1 
ATOM   11865 C CA  . ALA G  1 64  ? 3.017   25.857   -34.032 1.00 62.65  ? 64  ALA G CA  1 
ATOM   11866 C C   . ALA G  1 64  ? 3.709   27.185   -33.732 1.00 62.62  ? 64  ALA G C   1 
ATOM   11867 O O   . ALA G  1 64  ? 4.880   27.372   -34.060 1.00 65.60  ? 64  ALA G O   1 
ATOM   11868 C CB  . ALA G  1 64  ? 1.919   26.051   -35.069 1.00 56.95  ? 64  ALA G CB  1 
ATOM   11869 N N   . GLY G  1 65  ? 2.978   28.102   -33.107 1.00 66.34  ? 65  GLY G N   1 
ATOM   11870 C CA  . GLY G  1 65  ? 3.515   29.410   -32.780 1.00 63.53  ? 65  GLY G CA  1 
ATOM   11871 C C   . GLY G  1 65  ? 4.729   29.342   -31.875 1.00 65.74  ? 65  GLY G C   1 
ATOM   11872 O O   . GLY G  1 65  ? 5.699   30.075   -32.066 1.00 74.94  ? 65  GLY G O   1 
ATOM   11873 N N   . TRP G  1 66  ? 4.678   28.452   -30.889 1.00 53.06  ? 66  TRP G N   1 
ATOM   11874 C CA  . TRP G  1 66  ? 5.750   28.330   -29.907 1.00 68.23  ? 66  TRP G CA  1 
ATOM   11875 C C   . TRP G  1 66  ? 7.079   27.873   -30.510 1.00 66.31  ? 66  TRP G C   1 
ATOM   11876 O O   . TRP G  1 66  ? 8.133   28.418   -30.181 1.00 74.81  ? 66  TRP G O   1 
ATOM   11877 C CB  . TRP G  1 66  ? 5.332   27.392   -28.771 1.00 67.48  ? 66  TRP G CB  1 
ATOM   11878 C CG  . TRP G  1 66  ? 6.483   26.891   -27.952 1.00 69.52  ? 66  TRP G CG  1 
ATOM   11879 C CD1 . TRP G  1 66  ? 7.325   27.636   -27.179 1.00 70.77  ? 66  TRP G CD1 1 
ATOM   11880 C CD2 . TRP G  1 66  ? 6.912   25.531   -27.817 1.00 71.33  ? 66  TRP G CD2 1 
ATOM   11881 N NE1 . TRP G  1 66  ? 8.256   26.826   -26.576 1.00 74.86  ? 66  TRP G NE1 1 
ATOM   11882 C CE2 . TRP G  1 66  ? 8.024   25.528   -26.950 1.00 66.47  ? 66  TRP G CE2 1 
ATOM   11883 C CE3 . TRP G  1 66  ? 6.466   24.315   -28.344 1.00 71.27  ? 66  TRP G CE3 1 
ATOM   11884 C CZ2 . TRP G  1 66  ? 8.695   24.358   -26.601 1.00 61.01  ? 66  TRP G CZ2 1 
ATOM   11885 C CZ3 . TRP G  1 66  ? 7.135   23.155   -27.996 1.00 70.98  ? 66  TRP G CZ3 1 
ATOM   11886 C CH2 . TRP G  1 66  ? 8.236   23.185   -27.133 1.00 65.42  ? 66  TRP G CH2 1 
ATOM   11887 N N   . ILE G  1 67  ? 7.029   26.876   -31.388 1.00 66.67  ? 67  ILE G N   1 
ATOM   11888 C CA  . ILE G  1 67  ? 8.249   26.326   -31.970 1.00 66.80  ? 67  ILE G CA  1 
ATOM   11889 C C   . ILE G  1 67  ? 8.790   27.197   -33.098 1.00 72.13  ? 67  ILE G C   1 
ATOM   11890 O O   . ILE G  1 67  ? 10.000  27.370   -33.229 1.00 68.98  ? 67  ILE G O   1 
ATOM   11891 C CB  . ILE G  1 67  ? 8.035   24.908   -32.517 1.00 60.05  ? 67  ILE G CB  1 
ATOM   11892 C CG1 . ILE G  1 67  ? 7.099   24.117   -31.609 1.00 82.32  ? 67  ILE G CG1 1 
ATOM   11893 C CG2 . ILE G  1 67  ? 9.368   24.191   -32.664 1.00 56.89  ? 67  ILE G CG2 1 
ATOM   11894 C CD1 . ILE G  1 67  ? 6.785   22.750   -32.140 1.00 93.53  ? 67  ILE G CD1 1 
ATOM   11895 N N   . LEU G  1 68  ? 7.893   27.732   -33.920 1.00 64.70  ? 68  LEU G N   1 
ATOM   11896 C CA  . LEU G  1 68  ? 8.307   28.594   -35.021 1.00 63.57  ? 68  LEU G CA  1 
ATOM   11897 C C   . LEU G  1 68  ? 8.912   29.890   -34.501 1.00 70.96  ? 68  LEU G C   1 
ATOM   11898 O O   . LEU G  1 68  ? 9.798   30.469   -35.130 1.00 75.40  ? 68  LEU G O   1 
ATOM   11899 C CB  . LEU G  1 68  ? 7.134   28.896   -35.955 1.00 56.64  ? 68  LEU G CB  1 
ATOM   11900 C CG  . LEU G  1 68  ? 6.723   27.767   -36.900 1.00 60.77  ? 68  LEU G CG  1 
ATOM   11901 C CD1 . LEU G  1 68  ? 5.672   28.253   -37.882 1.00 58.61  ? 68  LEU G CD1 1 
ATOM   11902 C CD2 . LEU G  1 68  ? 7.937   27.232   -37.640 1.00 44.68  ? 68  LEU G CD2 1 
ATOM   11903 N N   . GLY G  1 69  ? 8.429   30.341   -33.349 1.00 69.67  ? 69  GLY G N   1 
ATOM   11904 C CA  . GLY G  1 69  ? 8.933   31.556   -32.739 1.00 70.35  ? 69  GLY G CA  1 
ATOM   11905 C C   . GLY G  1 69  ? 8.103   32.777   -33.083 1.00 78.29  ? 69  GLY G C   1 
ATOM   11906 O O   . GLY G  1 69  ? 8.643   33.849   -33.356 1.00 78.88  ? 69  GLY G O   1 
ATOM   11907 N N   . ASN G  1 70  ? 6.785   32.613   -33.077 1.00 82.24  ? 70  ASN G N   1 
ATOM   11908 C CA  . ASN G  1 70  ? 5.876   33.730   -33.294 1.00 86.81  ? 70  ASN G CA  1 
ATOM   11909 C C   . ASN G  1 70  ? 6.209   34.868   -32.336 1.00 97.09  ? 70  ASN G C   1 
ATOM   11910 O O   . ASN G  1 70  ? 6.411   34.640   -31.144 1.00 99.20  ? 70  ASN G O   1 
ATOM   11911 C CB  . ASN G  1 70  ? 4.426   33.273   -33.107 1.00 84.69  ? 70  ASN G CB  1 
ATOM   11912 C CG  . ASN G  1 70  ? 3.416   34.310   -33.567 1.00 89.42  ? 70  ASN G CG  1 
ATOM   11913 O OD1 . ASN G  1 70  ? 3.519   35.490   -33.233 1.00 95.09  ? 70  ASN G OD1 1 
ATOM   11914 N ND2 . ASN G  1 70  ? 2.422   33.867   -34.327 1.00 77.01  ? 70  ASN G ND2 1 
ATOM   11915 N N   . PRO G  1 71  ? 6.283   36.098   -32.862 1.00 106.19 ? 71  PRO G N   1 
ATOM   11916 C CA  . PRO G  1 71  ? 6.607   37.280   -32.056 1.00 100.65 ? 71  PRO G CA  1 
ATOM   11917 C C   . PRO G  1 71  ? 5.751   37.379   -30.791 1.00 100.81 ? 71  PRO G C   1 
ATOM   11918 O O   . PRO G  1 71  ? 6.246   37.798   -29.746 1.00 118.50 ? 71  PRO G O   1 
ATOM   11919 C CB  . PRO G  1 71  ? 6.301   38.440   -33.007 1.00 98.92  ? 71  PRO G CB  1 
ATOM   11920 C CG  . PRO G  1 71  ? 6.492   37.865   -34.370 1.00 96.62  ? 71  PRO G CG  1 
ATOM   11921 C CD  . PRO G  1 71  ? 6.064   36.430   -34.281 1.00 98.84  ? 71  PRO G CD  1 
ATOM   11922 N N   . GLU G  1 72  ? 4.483   36.993   -30.891 1.00 100.94 ? 72  GLU G N   1 
ATOM   11923 C CA  . GLU G  1 72  ? 3.570   37.054   -29.756 1.00 108.41 ? 72  GLU G CA  1 
ATOM   11924 C C   . GLU G  1 72  ? 3.621   35.778   -28.924 1.00 96.29  ? 72  GLU G C   1 
ATOM   11925 O O   . GLU G  1 72  ? 2.784   35.559   -28.040 1.00 100.10 ? 72  GLU G O   1 
ATOM   11926 C CB  . GLU G  1 72  ? 2.148   37.352   -30.232 1.00 101.07 ? 72  GLU G CB  1 
ATOM   11927 C CG  . GLU G  1 72  ? 1.990   38.763   -30.778 1.00 117.53 ? 72  GLU G CG  1 
ATOM   11928 C CD  . GLU G  1 72  ? 2.340   39.816   -29.744 1.00 136.38 ? 72  GLU G CD  1 
ATOM   11929 O OE1 . GLU G  1 72  ? 1.732   39.803   -28.654 1.00 129.00 ? 72  GLU G OE1 1 
ATOM   11930 O OE2 . GLU G  1 72  ? 3.219   40.660   -30.017 1.00 131.56 ? 72  GLU G OE2 1 
ATOM   11931 N N   . CYS G  1 73  ? 4.621   34.947   -29.208 1.00 114.92 ? 73  CYS G N   1 
ATOM   11932 C CA  . CYS G  1 73  ? 4.848   33.728   -28.439 1.00 117.30 ? 73  CYS G CA  1 
ATOM   11933 C C   . CYS G  1 73  ? 6.247   33.717   -27.807 1.00 134.52 ? 73  CYS G C   1 
ATOM   11934 O O   . CYS G  1 73  ? 6.817   32.654   -27.538 1.00 134.00 ? 73  CYS G O   1 
ATOM   11935 C CB  . CYS G  1 73  ? 4.625   32.476   -29.293 1.00 101.56 ? 73  CYS G CB  1 
ATOM   11936 S SG  . CYS G  1 73  ? 2.900   32.240   -29.819 1.00 105.55 ? 73  CYS G SG  1 
ATOM   11937 N N   . GLU G  1 74  ? 6.789   34.908   -27.565 1.00 139.02 ? 74  GLU G N   1 
ATOM   11938 C CA  . GLU G  1 74  ? 7.942   35.072   -26.693 1.00 152.19 ? 74  GLU G CA  1 
ATOM   11939 C C   . GLU G  1 74  ? 7.417   34.835   -25.283 1.00 163.18 ? 74  GLU G C   1 
ATOM   11940 O O   . GLU G  1 74  ? 6.208   34.646   -25.089 1.00 162.60 ? 74  GLU G O   1 
ATOM   11941 C CB  . GLU G  1 74  ? 8.581   36.455   -26.905 1.00 152.33 ? 74  GLU G CB  1 
ATOM   11942 C CG  . GLU G  1 74  ? 10.016  36.575   -26.404 1.00 161.76 ? 74  GLU G CG  1 
ATOM   11943 C CD  . GLU G  1 74  ? 10.710  37.823   -26.922 1.00 172.70 ? 74  GLU G CD  1 
ATOM   11944 O OE1 . GLU G  1 74  ? 10.111  38.519   -27.769 1.00 168.89 ? 74  GLU G OE1 1 
ATOM   11945 O OE2 . GLU G  1 74  ? 11.850  38.109   -26.492 1.00 164.58 ? 74  GLU G OE2 1 
ATOM   11946 N N   . SER G  1 75  ? 8.328   34.796   -24.316 1.00 176.11 ? 75  SER G N   1 
ATOM   11947 C CA  . SER G  1 75  ? 7.962   34.699   -22.906 1.00 188.89 ? 75  SER G CA  1 
ATOM   11948 C C   . SER G  1 75  ? 7.724   33.288   -22.329 1.00 194.48 ? 75  SER G C   1 
ATOM   11949 O O   . SER G  1 75  ? 7.560   33.121   -21.118 1.00 189.52 ? 75  SER G O   1 
ATOM   11950 C CB  . SER G  1 75  ? 6.855   35.716   -22.624 1.00 184.23 ? 75  SER G CB  1 
ATOM   11951 O OG  . SER G  1 75  ? 6.614   35.853   -21.239 1.00 170.90 ? 75  SER G OG  1 
ATOM   11952 N N   . LEU G  1 76  ? 7.736   32.272   -23.190 1.00 214.08 ? 76  LEU G N   1 
ATOM   11953 C CA  . LEU G  1 76  ? 7.521   30.893   -22.753 1.00 209.93 ? 76  LEU G CA  1 
ATOM   11954 C C   . LEU G  1 76  ? 8.460   29.818   -23.267 1.00 210.58 ? 76  LEU G C   1 
ATOM   11955 O O   . LEU G  1 76  ? 8.100   29.032   -24.151 1.00 205.50 ? 76  LEU G O   1 
ATOM   11956 C CB  . LEU G  1 76  ? 6.105   30.541   -23.189 1.00 202.22 ? 76  LEU G CB  1 
ATOM   11957 C CG  . LEU G  1 76  ? 5.346   29.319   -22.674 1.00 190.22 ? 76  LEU G CG  1 
ATOM   11958 C CD1 . LEU G  1 76  ? 4.412   28.915   -23.791 1.00 152.90 ? 76  LEU G CD1 1 
ATOM   11959 C CD2 . LEU G  1 76  ? 6.236   28.145   -22.268 1.00 190.40 ? 76  LEU G CD2 1 
ATOM   11960 N N   . SER G  1 77  ? 9.664   29.783   -22.706 1.00 190.49 ? 77  SER G N   1 
ATOM   11961 C CA  . SER G  1 77  ? 10.709  28.912   -23.219 1.00 190.11 ? 77  SER G CA  1 
ATOM   11962 C C   . SER G  1 77  ? 11.618  28.341   -22.138 1.00 191.16 ? 77  SER G C   1 
ATOM   11963 O O   . SER G  1 77  ? 12.328  27.378   -22.392 1.00 179.02 ? 77  SER G O   1 
ATOM   11964 C CB  . SER G  1 77  ? 11.507  29.749   -24.226 1.00 188.02 ? 77  SER G CB  1 
ATOM   11965 O OG  . SER G  1 77  ? 12.385  30.657   -23.581 1.00 174.94 ? 77  SER G OG  1 
ATOM   11966 N N   . THR G  1 78  ? 11.586  28.932   -20.942 1.00 265.58 ? 78  THR G N   1 
ATOM   11967 C CA  . THR G  1 78  ? 12.443  28.515   -19.823 1.00 268.03 ? 78  THR G CA  1 
ATOM   11968 C C   . THR G  1 78  ? 11.993  27.124   -19.392 1.00 247.65 ? 78  THR G C   1 
ATOM   11969 O O   . THR G  1 78  ? 11.486  26.928   -18.285 1.00 234.44 ? 78  THR G O   1 
ATOM   11970 C CB  . THR G  1 78  ? 12.361  29.488   -18.612 1.00 231.04 ? 78  THR G CB  1 
ATOM   11971 O OG1 . THR G  1 78  ? 11.005  29.602   -18.160 1.00 228.80 ? 78  THR G OG1 1 
ATOM   11972 C CG2 . THR G  1 78  ? 12.873  30.867   -18.999 1.00 146.03 ? 78  THR G CG2 1 
ATOM   11973 N N   . ALA G  1 79  ? 12.188  26.164   -20.288 1.00 178.76 ? 79  ALA G N   1 
ATOM   11974 C CA  . ALA G  1 79  ? 11.704  24.806   -20.108 1.00 151.91 ? 79  ALA G CA  1 
ATOM   11975 C C   . ALA G  1 79  ? 12.794  23.855   -20.572 1.00 134.53 ? 79  ALA G C   1 
ATOM   11976 O O   . ALA G  1 79  ? 13.215  23.895   -21.727 1.00 129.88 ? 79  ALA G O   1 
ATOM   11977 C CB  . ALA G  1 79  ? 10.411  24.520   -20.851 1.00 144.04 ? 79  ALA G CB  1 
ATOM   11978 N N   . SER G  1 80  ? 13.244  22.998   -19.663 1.00 98.14  ? 80  SER G N   1 
ATOM   11979 C CA  . SER G  1 80  ? 14.239  21.989   -19.986 1.00 89.75  ? 80  SER G CA  1 
ATOM   11980 C C   . SER G  1 80  ? 13.539  20.662   -20.246 1.00 83.12  ? 80  SER G C   1 
ATOM   11981 O O   . SER G  1 80  ? 14.078  19.784   -20.917 1.00 81.13  ? 80  SER G O   1 
ATOM   11982 C CB  . SER G  1 80  ? 15.234  21.836   -18.835 1.00 107.32 ? 80  SER G CB  1 
ATOM   11983 O OG  . SER G  1 80  ? 15.707  23.099   -18.397 1.00 114.90 ? 80  SER G OG  1 
ATOM   11984 N N   . SER G  1 81  ? 12.328  20.531   -19.710 1.00 80.05  ? 81  SER G N   1 
ATOM   11985 C CA  . SER G  1 81  ? 11.547  19.305   -19.837 1.00 77.27  ? 81  SER G CA  1 
ATOM   11986 C C   . SER G  1 81  ? 10.096  19.529   -19.421 1.00 71.26  ? 81  SER G C   1 
ATOM   11987 O O   . SER G  1 81  ? 9.781   20.509   -18.746 1.00 64.89  ? 81  SER G O   1 
ATOM   11988 C CB  . SER G  1 81  ? 12.159  18.196   -18.981 1.00 75.78  ? 81  SER G CB  1 
ATOM   11989 O OG  . SER G  1 81  ? 12.239  18.588   -17.622 1.00 74.48  ? 81  SER G OG  1 
ATOM   11990 N N   . TRP G  1 82  ? 9.217   18.616   -19.825 1.00 63.19  ? 82  TRP G N   1 
ATOM   11991 C CA  . TRP G  1 82  ? 7.807   18.686   -19.447 1.00 58.42  ? 82  TRP G CA  1 
ATOM   11992 C C   . TRP G  1 82  ? 7.086   17.357   -19.646 1.00 55.06  ? 82  TRP G C   1 
ATOM   11993 O O   . TRP G  1 82  ? 7.244   16.694   -20.673 1.00 58.73  ? 82  TRP G O   1 
ATOM   11994 C CB  . TRP G  1 82  ? 7.082   19.792   -20.217 1.00 56.51  ? 82  TRP G CB  1 
ATOM   11995 C CG  . TRP G  1 82  ? 7.180   19.653   -21.699 1.00 57.87  ? 82  TRP G CG  1 
ATOM   11996 C CD1 . TRP G  1 82  ? 6.408   18.869   -22.505 1.00 63.42  ? 82  TRP G CD1 1 
ATOM   11997 C CD2 . TRP G  1 82  ? 8.104   20.325   -22.558 1.00 59.48  ? 82  TRP G CD2 1 
ATOM   11998 N NE1 . TRP G  1 82  ? 6.799   19.008   -23.815 1.00 62.49  ? 82  TRP G NE1 1 
ATOM   11999 C CE2 . TRP G  1 82  ? 7.839   19.899   -23.873 1.00 62.51  ? 82  TRP G CE2 1 
ATOM   12000 C CE3 . TRP G  1 82  ? 9.133   21.247   -22.342 1.00 62.46  ? 82  TRP G CE3 1 
ATOM   12001 C CZ2 . TRP G  1 82  ? 8.564   20.362   -24.968 1.00 60.74  ? 82  TRP G CZ2 1 
ATOM   12002 C CZ3 . TRP G  1 82  ? 9.851   21.705   -23.428 1.00 62.70  ? 82  TRP G CZ3 1 
ATOM   12003 C CH2 . TRP G  1 82  ? 9.564   21.263   -24.724 1.00 46.37  ? 82  TRP G CH2 1 
ATOM   12004 N N   . SER G  1 83  ? 6.284   16.986   -18.653 1.00 61.99  ? 83  SER G N   1 
ATOM   12005 C CA  . SER G  1 83  ? 5.530   15.738   -18.687 1.00 61.38  ? 83  SER G CA  1 
ATOM   12006 C C   . SER G  1 83  ? 4.440   15.744   -19.754 1.00 53.70  ? 83  SER G C   1 
ATOM   12007 O O   . SER G  1 83  ? 4.195   14.726   -20.397 1.00 65.03  ? 83  SER G O   1 
ATOM   12008 C CB  . SER G  1 83  ? 4.924   15.438   -17.313 1.00 61.20  ? 83  SER G CB  1 
ATOM   12009 O OG  . SER G  1 83  ? 4.190   16.546   -16.821 1.00 61.35  ? 83  SER G OG  1 
ATOM   12010 N N   . TYR G  1 84  ? 3.790   16.888   -19.940 1.00 43.73  ? 84  TYR G N   1 
ATOM   12011 C CA  . TYR G  1 84  ? 2.728   17.010   -20.936 1.00 55.40  ? 84  TYR G CA  1 
ATOM   12012 C C   . TYR G  1 84  ? 2.589   18.455   -21.400 1.00 60.57  ? 84  TYR G C   1 
ATOM   12013 O O   . TYR G  1 84  ? 3.182   19.352   -20.808 1.00 61.01  ? 84  TYR G O   1 
ATOM   12014 C CB  . TYR G  1 84  ? 1.405   16.473   -20.383 1.00 50.38  ? 84  TYR G CB  1 
ATOM   12015 C CG  . TYR G  1 84  ? 0.919   17.156   -19.131 1.00 49.51  ? 84  TYR G CG  1 
ATOM   12016 C CD1 . TYR G  1 84  ? -0.118  18.068   -19.186 1.00 51.48  ? 84  TYR G CD1 1 
ATOM   12017 C CD2 . TYR G  1 84  ? 1.489   16.880   -17.897 1.00 55.02  ? 84  TYR G CD2 1 
ATOM   12018 C CE1 . TYR G  1 84  ? -0.572  18.689   -18.058 1.00 49.67  ? 84  TYR G CE1 1 
ATOM   12019 C CE2 . TYR G  1 84  ? 1.039   17.500   -16.758 1.00 51.47  ? 84  TYR G CE2 1 
ATOM   12020 C CZ  . TYR G  1 84  ? 0.006   18.404   -16.849 1.00 54.61  ? 84  TYR G CZ  1 
ATOM   12021 O OH  . TYR G  1 84  ? -0.464  19.040   -15.733 1.00 56.50  ? 84  TYR G OH  1 
ATOM   12022 N N   . ILE G  1 85  ? 1.827   18.682   -22.466 1.00 47.96  ? 85  ILE G N   1 
ATOM   12023 C CA  . ILE G  1 85  ? 1.652   20.033   -22.997 1.00 55.26  ? 85  ILE G CA  1 
ATOM   12024 C C   . ILE G  1 85  ? 0.222   20.530   -22.788 1.00 64.20  ? 85  ILE G C   1 
ATOM   12025 O O   . ILE G  1 85  ? -0.738  19.809   -23.052 1.00 65.60  ? 85  ILE G O   1 
ATOM   12026 C CB  . ILE G  1 85  ? 2.035   20.116   -24.496 1.00 52.70  ? 85  ILE G CB  1 
ATOM   12027 C CG1 . ILE G  1 85  ? 3.513   19.764   -24.686 1.00 50.06  ? 85  ILE G CG1 1 
ATOM   12028 C CG2 . ILE G  1 85  ? 1.746   21.503   -25.056 1.00 50.32  ? 85  ILE G CG2 1 
ATOM   12029 C CD1 . ILE G  1 85  ? 3.972   19.796   -26.127 1.00 52.42  ? 85  ILE G CD1 1 
ATOM   12030 N N   . VAL G  1 86  ? 0.089   21.759   -22.297 1.00 57.18  ? 86  VAL G N   1 
ATOM   12031 C CA  . VAL G  1 86  ? -1.221  22.371   -22.101 1.00 58.79  ? 86  VAL G CA  1 
ATOM   12032 C C   . VAL G  1 86  ? -1.473  23.516   -23.076 1.00 58.69  ? 86  VAL G C   1 
ATOM   12033 O O   . VAL G  1 86  ? -0.680  24.451   -23.175 1.00 60.18  ? 86  VAL G O   1 
ATOM   12034 C CB  . VAL G  1 86  ? -1.387  22.904   -20.672 1.00 53.80  ? 86  VAL G CB  1 
ATOM   12035 C CG1 . VAL G  1 86  ? -2.733  23.606   -20.521 1.00 45.70  ? 86  VAL G CG1 1 
ATOM   12036 C CG2 . VAL G  1 86  ? -1.253  21.771   -19.677 1.00 64.11  ? 86  VAL G CG2 1 
ATOM   12037 N N   . GLU G  1 87  ? -2.588  23.434   -23.793 1.00 67.03  ? 87  GLU G N   1 
ATOM   12038 C CA  . GLU G  1 87  ? -2.985  24.479   -24.721 1.00 55.83  ? 87  GLU G CA  1 
ATOM   12039 C C   . GLU G  1 87  ? -4.331  25.025   -24.276 1.00 68.40  ? 87  GLU G C   1 
ATOM   12040 O O   . GLU G  1 87  ? -5.212  24.263   -23.885 1.00 77.20  ? 87  GLU G O   1 
ATOM   12041 C CB  . GLU G  1 87  ? -3.104  23.906   -26.132 1.00 63.34  ? 87  GLU G CB  1 
ATOM   12042 C CG  . GLU G  1 87  ? -2.312  24.650   -27.189 1.00 66.89  ? 87  GLU G CG  1 
ATOM   12043 C CD  . GLU G  1 87  ? -2.366  23.956   -28.535 1.00 78.53  ? 87  GLU G CD  1 
ATOM   12044 O OE1 . GLU G  1 87  ? -1.353  23.988   -29.263 1.00 77.78  ? 87  GLU G OE1 1 
ATOM   12045 O OE2 . GLU G  1 87  ? -3.419  23.366   -28.859 1.00 72.59  ? 87  GLU G OE2 1 
ATOM   12046 N N   . THR G  1 88  ? -4.491  26.343   -24.322 1.00 77.21  ? 88  THR G N   1 
ATOM   12047 C CA  . THR G  1 88  ? -5.767  26.949   -23.972 1.00 83.43  ? 88  THR G CA  1 
ATOM   12048 C C   . THR G  1 88  ? -6.662  26.997   -25.203 1.00 90.04  ? 88  THR G C   1 
ATOM   12049 O O   . THR G  1 88  ? -6.184  27.240   -26.311 1.00 90.37  ? 88  THR G O   1 
ATOM   12050 C CB  . THR G  1 88  ? -5.593  28.369   -23.404 1.00 90.25  ? 88  THR G CB  1 
ATOM   12051 O OG1 . THR G  1 88  ? -5.118  29.245   -24.433 1.00 101.56 ? 88  THR G OG1 1 
ATOM   12052 C CG2 . THR G  1 88  ? -4.607  28.361   -22.245 1.00 70.22  ? 88  THR G CG2 1 
ATOM   12053 N N   . PRO G  1 89  ? -7.967  26.756   -25.014 1.00 121.46 ? 89  PRO G N   1 
ATOM   12054 C CA  . PRO G  1 89  ? -8.926  26.760   -26.123 1.00 119.30 ? 89  PRO G CA  1 
ATOM   12055 C C   . PRO G  1 89  ? -8.939  28.102   -26.845 1.00 131.55 ? 89  PRO G C   1 
ATOM   12056 O O   . PRO G  1 89  ? -9.502  28.208   -27.934 1.00 133.37 ? 89  PRO G O   1 
ATOM   12057 C CB  . PRO G  1 89  ? -10.270 26.532   -25.423 1.00 107.47 ? 89  PRO G CB  1 
ATOM   12058 C CG  . PRO G  1 89  ? -9.924  25.864   -24.137 1.00 115.20 ? 89  PRO G CG  1 
ATOM   12059 C CD  . PRO G  1 89  ? -8.610  26.449   -23.725 1.00 118.90 ? 89  PRO G CD  1 
ATOM   12060 N N   . SER G  1 90  ? -8.319  29.111   -26.241 1.00 114.98 ? 90  SER G N   1 
ATOM   12061 C CA  . SER G  1 90  ? -8.322  30.459   -26.797 1.00 118.83 ? 90  SER G CA  1 
ATOM   12062 C C   . SER G  1 90  ? -6.951  30.854   -27.340 1.00 130.47 ? 90  SER G C   1 
ATOM   12063 O O   . SER G  1 90  ? -6.630  32.039   -27.437 1.00 141.01 ? 90  SER G O   1 
ATOM   12064 C CB  . SER G  1 90  ? -8.778  31.465   -25.738 1.00 124.17 ? 90  SER G CB  1 
ATOM   12065 O OG  . SER G  1 90  ? -8.920  32.762   -26.290 1.00 147.65 ? 90  SER G OG  1 
ATOM   12066 N N   . SER G  1 91  ? -6.145  29.858   -27.694 1.00 124.99 ? 91  SER G N   1 
ATOM   12067 C CA  . SER G  1 91  ? -4.813  30.108   -28.235 1.00 113.20 ? 91  SER G CA  1 
ATOM   12068 C C   . SER G  1 91  ? -4.822  30.049   -29.761 1.00 113.85 ? 91  SER G C   1 
ATOM   12069 O O   . SER G  1 91  ? -5.095  29.002   -30.347 1.00 113.01 ? 91  SER G O   1 
ATOM   12070 C CB  . SER G  1 91  ? -3.807  29.101   -27.673 1.00 101.93 ? 91  SER G CB  1 
ATOM   12071 O OG  . SER G  1 91  ? -4.170  27.774   -28.011 1.00 100.68 ? 91  SER G OG  1 
ATOM   12072 N N   . ASP G  1 92  ? -4.517  31.176   -30.399 1.00 134.45 ? 92  ASP G N   1 
ATOM   12073 C CA  . ASP G  1 92  ? -4.582  31.269   -31.856 1.00 137.50 ? 92  ASP G CA  1 
ATOM   12074 C C   . ASP G  1 92  ? -3.320  31.847   -32.486 1.00 132.66 ? 92  ASP G C   1 
ATOM   12075 O O   . ASP G  1 92  ? -3.217  31.940   -33.711 1.00 135.23 ? 92  ASP G O   1 
ATOM   12076 C CB  . ASP G  1 92  ? -5.796  32.096   -32.281 1.00 160.29 ? 92  ASP G CB  1 
ATOM   12077 C CG  . ASP G  1 92  ? -7.104  31.403   -31.972 1.00 165.37 ? 92  ASP G CG  1 
ATOM   12078 O OD1 . ASP G  1 92  ? -7.099  30.162   -31.847 1.00 162.79 ? 92  ASP G OD1 1 
ATOM   12079 O OD2 . ASP G  1 92  ? -8.135  32.097   -31.858 1.00 170.99 ? 92  ASP G OD2 1 
ATOM   12080 N N   . ASN G  1 93  ? -2.366  32.244   -31.652 1.00 125.73 ? 93  ASN G N   1 
ATOM   12081 C CA  . ASN G  1 93  ? -1.094  32.746   -32.155 1.00 124.20 ? 93  ASN G CA  1 
ATOM   12082 C C   . ASN G  1 93  ? -0.194  31.616   -32.641 1.00 109.35 ? 93  ASN G C   1 
ATOM   12083 O O   . ASN G  1 93  ? 0.734   31.207   -31.945 1.00 95.19  ? 93  ASN G O   1 
ATOM   12084 C CB  . ASN G  1 93  ? -0.375  33.579   -31.094 1.00 119.92 ? 93  ASN G CB  1 
ATOM   12085 C CG  . ASN G  1 93  ? -0.987  34.956   -30.919 1.00 137.79 ? 93  ASN G CG  1 
ATOM   12086 O OD1 . ASN G  1 93  ? -1.330  35.358   -29.807 1.00 135.59 ? 93  ASN G OD1 1 
ATOM   12087 N ND2 . ASN G  1 93  ? -1.131  35.685   -32.021 1.00 131.66 ? 93  ASN G ND2 1 
ATOM   12088 N N   . GLY G  1 94  ? -0.481  31.114   -33.837 1.00 107.64 ? 94  GLY G N   1 
ATOM   12089 C CA  . GLY G  1 94  ? 0.314   30.058   -34.435 1.00 95.02  ? 94  GLY G CA  1 
ATOM   12090 C C   . GLY G  1 94  ? 1.077   30.556   -35.645 1.00 95.30  ? 94  GLY G C   1 
ATOM   12091 O O   . GLY G  1 94  ? 1.964   31.400   -35.524 1.00 91.01  ? 94  GLY G O   1 
ATOM   12092 N N   . THR G  1 95  ? 0.732   30.034   -36.817 1.00 77.26  ? 95  THR G N   1 
ATOM   12093 C CA  . THR G  1 95  ? 1.367   30.464   -38.057 1.00 79.75  ? 95  THR G CA  1 
ATOM   12094 C C   . THR G  1 95  ? 0.761   31.768   -38.567 1.00 77.94  ? 95  THR G C   1 
ATOM   12095 O O   . THR G  1 95  ? -0.272  31.767   -39.237 1.00 75.39  ? 95  THR G O   1 
ATOM   12096 C CB  . THR G  1 95  ? 1.275   29.383   -39.151 1.00 68.90  ? 95  THR G CB  1 
ATOM   12097 O OG1 . THR G  1 95  ? -0.057  28.857   -39.195 1.00 67.18  ? 95  THR G OG1 1 
ATOM   12098 C CG2 . THR G  1 95  ? 2.248   28.252   -38.861 1.00 65.79  ? 95  THR G CG2 1 
ATOM   12099 N N   . CYS G  1 96  ? 1.415   32.878   -38.241 1.00 80.90  ? 96  CYS G N   1 
ATOM   12100 C CA  . CYS G  1 96  ? 0.949   34.199   -38.646 1.00 74.68  ? 96  CYS G CA  1 
ATOM   12101 C C   . CYS G  1 96  ? 0.973   34.385   -40.162 1.00 75.28  ? 96  CYS G C   1 
ATOM   12102 O O   . CYS G  1 96  ? 0.141   35.101   -40.717 1.00 72.57  ? 96  CYS G O   1 
ATOM   12103 C CB  . CYS G  1 96  ? 1.769   35.291   -37.955 1.00 70.64  ? 96  CYS G CB  1 
ATOM   12104 S SG  . CYS G  1 96  ? 3.538   34.946   -37.857 1.00 84.56  ? 96  CYS G SG  1 
ATOM   12105 N N   . TYR G  1 97  ? 1.926   33.747   -40.831 1.00 66.39  ? 97  TYR G N   1 
ATOM   12106 C CA  . TYR G  1 97  ? 1.934   33.750   -42.288 1.00 59.96  ? 97  TYR G CA  1 
ATOM   12107 C C   . TYR G  1 97  ? 1.225   32.497   -42.786 1.00 62.02  ? 97  TYR G C   1 
ATOM   12108 O O   . TYR G  1 97  ? 1.594   31.383   -42.416 1.00 77.71  ? 97  TYR G O   1 
ATOM   12109 C CB  . TYR G  1 97  ? 3.360   33.822   -42.840 1.00 69.86  ? 97  TYR G CB  1 
ATOM   12110 C CG  . TYR G  1 97  ? 3.425   34.264   -44.287 1.00 61.21  ? 97  TYR G CG  1 
ATOM   12111 C CD1 . TYR G  1 97  ? 3.836   35.547   -44.625 1.00 68.74  ? 97  TYR G CD1 1 
ATOM   12112 C CD2 . TYR G  1 97  ? 3.063   33.402   -45.314 1.00 65.47  ? 97  TYR G CD2 1 
ATOM   12113 C CE1 . TYR G  1 97  ? 3.892   35.956   -45.945 1.00 83.05  ? 97  TYR G CE1 1 
ATOM   12114 C CE2 . TYR G  1 97  ? 3.116   33.802   -46.636 1.00 65.64  ? 97  TYR G CE2 1 
ATOM   12115 C CZ  . TYR G  1 97  ? 3.530   35.079   -46.946 1.00 72.62  ? 97  TYR G CZ  1 
ATOM   12116 O OH  . TYR G  1 97  ? 3.583   35.479   -48.262 1.00 64.26  ? 97  TYR G OH  1 
ATOM   12117 N N   . PRO G  1 98  ? 0.194   32.679   -43.622 1.00 58.24  ? 98  PRO G N   1 
ATOM   12118 C CA  . PRO G  1 98  ? -0.637  31.574   -44.113 1.00 58.06  ? 98  PRO G CA  1 
ATOM   12119 C C   . PRO G  1 98  ? 0.197   30.482   -44.766 1.00 70.14  ? 98  PRO G C   1 
ATOM   12120 O O   . PRO G  1 98  ? 1.163   30.781   -45.468 1.00 63.60  ? 98  PRO G O   1 
ATOM   12121 C CB  . PRO G  1 98  ? -1.525  32.245   -45.163 1.00 55.46  ? 98  PRO G CB  1 
ATOM   12122 C CG  . PRO G  1 98  ? -1.568  33.667   -44.766 1.00 72.74  ? 98  PRO G CG  1 
ATOM   12123 C CD  . PRO G  1 98  ? -0.228  33.975   -44.177 1.00 79.01  ? 98  PRO G CD  1 
ATOM   12124 N N   . GLY G  1 99  ? -0.179  29.229   -44.536 1.00 74.01  ? 99  GLY G N   1 
ATOM   12125 C CA  . GLY G  1 99  ? 0.536   28.107   -45.111 1.00 67.71  ? 99  GLY G CA  1 
ATOM   12126 C C   . GLY G  1 99  ? 0.202   26.795   -44.433 1.00 72.97  ? 99  GLY G C   1 
ATOM   12127 O O   . GLY G  1 99  ? -0.573  26.756   -43.478 1.00 62.60  ? 99  GLY G O   1 
ATOM   12128 N N   . ASP G  1 100 ? 0.798   25.717   -44.930 1.00 75.02  ? 100 ASP G N   1 
ATOM   12129 C CA  . ASP G  1 100 ? 0.541   24.387   -44.399 1.00 58.66  ? 100 ASP G CA  1 
ATOM   12130 C C   . ASP G  1 100 ? 1.695   23.917   -43.520 1.00 51.30  ? 100 ASP G C   1 
ATOM   12131 O O   . ASP G  1 100 ? 2.861   24.046   -43.891 1.00 56.74  ? 100 ASP G O   1 
ATOM   12132 C CB  . ASP G  1 100 ? 0.319   23.396   -45.544 1.00 61.59  ? 100 ASP G CB  1 
ATOM   12133 C CG  . ASP G  1 100 ? -0.304  22.095   -45.078 1.00 94.89  ? 100 ASP G CG  1 
ATOM   12134 O OD1 . ASP G  1 100 ? -0.879  22.074   -43.970 1.00 107.77 ? 100 ASP G OD1 1 
ATOM   12135 O OD2 . ASP G  1 100 ? -0.223  21.095   -45.823 1.00 86.88  ? 100 ASP G OD2 1 
ATOM   12136 N N   . PHE G  1 101 ? 1.363   23.381   -42.349 1.00 46.40  ? 101 PHE G N   1 
ATOM   12137 C CA  . PHE G  1 101 ? 2.365   22.802   -41.463 1.00 51.25  ? 101 PHE G CA  1 
ATOM   12138 C C   . PHE G  1 101 ? 2.381   21.292   -41.669 1.00 47.84  ? 101 PHE G C   1 
ATOM   12139 O O   . PHE G  1 101 ? 1.537   20.575   -41.133 1.00 48.34  ? 101 PHE G O   1 
ATOM   12140 C CB  . PHE G  1 101 ? 2.051   23.133   -40.003 1.00 45.35  ? 101 PHE G CB  1 
ATOM   12141 C CG  . PHE G  1 101 ? 3.257   23.129   -39.104 1.00 42.33  ? 101 PHE G CG  1 
ATOM   12142 C CD1 . PHE G  1 101 ? 3.604   24.261   -38.385 1.00 52.48  ? 101 PHE G CD1 1 
ATOM   12143 C CD2 . PHE G  1 101 ? 4.047   21.998   -38.984 1.00 51.25  ? 101 PHE G CD2 1 
ATOM   12144 C CE1 . PHE G  1 101 ? 4.712   24.264   -37.558 1.00 44.91  ? 101 PHE G CE1 1 
ATOM   12145 C CE2 . PHE G  1 101 ? 5.158   21.995   -38.159 1.00 44.13  ? 101 PHE G CE2 1 
ATOM   12146 C CZ  . PHE G  1 101 ? 5.490   23.130   -37.446 1.00 33.83  ? 101 PHE G CZ  1 
ATOM   12147 N N   . ILE G  1 102 ? 3.341   20.817   -42.456 1.00 43.50  ? 102 ILE G N   1 
ATOM   12148 C CA  . ILE G  1 102 ? 3.406   19.407   -42.826 1.00 46.37  ? 102 ILE G CA  1 
ATOM   12149 C C   . ILE G  1 102 ? 3.642   18.502   -41.620 1.00 49.53  ? 102 ILE G C   1 
ATOM   12150 O O   . ILE G  1 102 ? 4.540   18.748   -40.814 1.00 47.32  ? 102 ILE G O   1 
ATOM   12151 C CB  . ILE G  1 102 ? 4.509   19.155   -43.869 1.00 61.70  ? 102 ILE G CB  1 
ATOM   12152 C CG1 . ILE G  1 102 ? 4.414   20.181   -44.999 1.00 57.79  ? 102 ILE G CG1 1 
ATOM   12153 C CG2 . ILE G  1 102 ? 4.420   17.734   -44.407 1.00 48.27  ? 102 ILE G CG2 1 
ATOM   12154 C CD1 . ILE G  1 102 ? 3.092   20.163   -45.733 1.00 49.38  ? 102 ILE G CD1 1 
ATOM   12155 N N   . ASP G  1 103 ? 2.831   17.454   -41.508 1.00 51.24  ? 103 ASP G N   1 
ATOM   12156 C CA  . ASP G  1 103 ? 2.938   16.511   -40.401 1.00 38.50  ? 103 ASP G CA  1 
ATOM   12157 C C   . ASP G  1 103 ? 2.917   17.240   -39.061 1.00 44.95  ? 103 ASP G C   1 
ATOM   12158 O O   . ASP G  1 103 ? 3.721   16.956   -38.174 1.00 44.65  ? 103 ASP G O   1 
ATOM   12159 C CB  . ASP G  1 103 ? 4.213   15.674   -40.530 1.00 48.76  ? 103 ASP G CB  1 
ATOM   12160 C CG  . ASP G  1 103 ? 4.223   14.817   -41.781 1.00 56.03  ? 103 ASP G CG  1 
ATOM   12161 O OD1 . ASP G  1 103 ? 3.135   14.390   -42.221 1.00 63.11  ? 103 ASP G OD1 1 
ATOM   12162 O OD2 . ASP G  1 103 ? 5.321   14.567   -42.322 1.00 52.28  ? 103 ASP G OD2 1 
ATOM   12163 N N   . TYR G  1 104 ? 1.987   18.179   -38.925 1.00 50.17  ? 104 TYR G N   1 
ATOM   12164 C CA  . TYR G  1 104 ? 1.883   18.999   -37.723 1.00 44.17  ? 104 TYR G CA  1 
ATOM   12165 C C   . TYR G  1 104 ? 1.451   18.189   -36.503 1.00 47.61  ? 104 TYR G C   1 
ATOM   12166 O O   . TYR G  1 104 ? 2.089   18.254   -35.452 1.00 42.02  ? 104 TYR G O   1 
ATOM   12167 C CB  . TYR G  1 104 ? 0.923   20.168   -37.960 1.00 43.55  ? 104 TYR G CB  1 
ATOM   12168 C CG  . TYR G  1 104 ? 0.714   21.055   -36.754 1.00 47.28  ? 104 TYR G CG  1 
ATOM   12169 C CD1 . TYR G  1 104 ? 1.794   21.610   -36.080 1.00 43.11  ? 104 TYR G CD1 1 
ATOM   12170 C CD2 . TYR G  1 104 ? -0.564  21.350   -36.299 1.00 42.73  ? 104 TYR G CD2 1 
ATOM   12171 C CE1 . TYR G  1 104 ? 1.607   22.423   -34.979 1.00 44.30  ? 104 TYR G CE1 1 
ATOM   12172 C CE2 . TYR G  1 104 ? -0.760  22.164   -35.201 1.00 53.60  ? 104 TYR G CE2 1 
ATOM   12173 C CZ  . TYR G  1 104 ? 0.328   22.697   -34.544 1.00 46.13  ? 104 TYR G CZ  1 
ATOM   12174 O OH  . TYR G  1 104 ? 0.136   23.508   -33.450 1.00 53.56  ? 104 TYR G OH  1 
ATOM   12175 N N   . GLU G  1 105 ? 0.370   17.429   -36.646 1.00 54.05  ? 105 GLU G N   1 
ATOM   12176 C CA  . GLU G  1 105 ? -0.141  16.615   -35.549 1.00 40.90  ? 105 GLU G CA  1 
ATOM   12177 C C   . GLU G  1 105 ? 0.932   15.652   -35.060 1.00 41.60  ? 105 GLU G C   1 
ATOM   12178 O O   . GLU G  1 105 ? 1.023   15.364   -33.868 1.00 44.50  ? 105 GLU G O   1 
ATOM   12179 C CB  . GLU G  1 105 ? -1.393  15.843   -35.974 1.00 45.90  ? 105 GLU G CB  1 
ATOM   12180 C CG  . GLU G  1 105 ? -2.512  16.718   -36.508 1.00 43.55  ? 105 GLU G CG  1 
ATOM   12181 C CD  . GLU G  1 105 ? -2.168  17.340   -37.845 1.00 57.25  ? 105 GLU G CD  1 
ATOM   12182 O OE1 . GLU G  1 105 ? -1.440  16.696   -38.628 1.00 60.71  ? 105 GLU G OE1 1 
ATOM   12183 O OE2 . GLU G  1 105 ? -2.624  18.472   -38.113 1.00 58.39  ? 105 GLU G OE2 1 
ATOM   12184 N N   . GLU G  1 106 ? 1.746   15.158   -35.988 1.00 41.93  ? 106 GLU G N   1 
ATOM   12185 C CA  . GLU G  1 106 ? 2.852   14.276   -35.638 1.00 47.40  ? 106 GLU G CA  1 
ATOM   12186 C C   . GLU G  1 106 ? 3.881   15.009   -34.791 1.00 44.82  ? 106 GLU G C   1 
ATOM   12187 O O   . GLU G  1 106 ? 4.327   14.505   -33.761 1.00 39.73  ? 106 GLU G O   1 
ATOM   12188 C CB  . GLU G  1 106 ? 3.503   13.703   -36.897 1.00 44.08  ? 106 GLU G CB  1 
ATOM   12189 C CG  . GLU G  1 106 ? 2.807   12.462   -37.425 1.00 66.35  ? 106 GLU G CG  1 
ATOM   12190 C CD  . GLU G  1 106 ? 2.987   11.266   -36.507 1.00 55.53  ? 106 GLU G CD  1 
ATOM   12191 O OE1 . GLU G  1 106 ? 4.083   11.124   -35.925 1.00 54.46  ? 106 GLU G OE1 1 
ATOM   12192 O OE2 . GLU G  1 106 ? 2.038   10.464   -36.374 1.00 48.31  ? 106 GLU G OE2 1 
ATOM   12193 N N   . LEU G  1 107 ? 4.248   16.207   -35.231 1.00 52.25  ? 107 LEU G N   1 
ATOM   12194 C CA  . LEU G  1 107 ? 5.187   17.038   -34.492 1.00 49.99  ? 107 LEU G CA  1 
ATOM   12195 C C   . LEU G  1 107 ? 4.718   17.218   -33.049 1.00 45.23  ? 107 LEU G C   1 
ATOM   12196 O O   . LEU G  1 107 ? 5.484   17.021   -32.105 1.00 39.43  ? 107 LEU G O   1 
ATOM   12197 C CB  . LEU G  1 107 ? 5.312   18.403   -35.165 1.00 49.16  ? 107 LEU G CB  1 
ATOM   12198 C CG  . LEU G  1 107 ? 6.692   19.063   -35.195 1.00 52.61  ? 107 LEU G CG  1 
ATOM   12199 C CD1 . LEU G  1 107 ? 6.557   20.571   -35.053 1.00 46.28  ? 107 LEU G CD1 1 
ATOM   12200 C CD2 . LEU G  1 107 ? 7.643   18.468   -34.165 1.00 43.14  ? 107 LEU G CD2 1 
ATOM   12201 N N   . ARG G  1 108 ? 3.450   17.589   -32.891 1.00 39.27  ? 108 ARG G N   1 
ATOM   12202 C CA  . ARG G  1 108 ? 2.852   17.796   -31.576 1.00 50.65  ? 108 ARG G CA  1 
ATOM   12203 C C   . ARG G  1 108 ? 2.954   16.549   -30.701 1.00 53.23  ? 108 ARG G C   1 
ATOM   12204 O O   . ARG G  1 108 ? 3.294   16.634   -29.521 1.00 44.25  ? 108 ARG G O   1 
ATOM   12205 C CB  . ARG G  1 108 ? 1.386   18.205   -31.726 1.00 42.48  ? 108 ARG G CB  1 
ATOM   12206 C CG  . ARG G  1 108 ? 1.176   19.480   -32.528 1.00 45.24  ? 108 ARG G CG  1 
ATOM   12207 C CD  . ARG G  1 108 ? -0.291  19.678   -32.875 1.00 52.63  ? 108 ARG G CD  1 
ATOM   12208 N NE  . ARG G  1 108 ? -1.138  19.707   -31.687 1.00 53.81  ? 108 ARG G NE  1 
ATOM   12209 C CZ  . ARG G  1 108 ? -1.544  20.818   -31.082 1.00 54.47  ? 108 ARG G CZ  1 
ATOM   12210 N NH1 . ARG G  1 108 ? -1.184  22.004   -31.553 1.00 44.59  ? 108 ARG G NH1 1 
ATOM   12211 N NH2 . ARG G  1 108 ? -2.314  20.745   -30.005 1.00 49.87  ? 108 ARG G NH2 1 
ATOM   12212 N N   . GLU G  1 109 ? 2.651   15.395   -31.286 1.00 49.28  ? 109 GLU G N   1 
ATOM   12213 C CA  . GLU G  1 109 ? 2.713   14.131   -30.563 1.00 47.43  ? 109 GLU G CA  1 
ATOM   12214 C C   . GLU G  1 109 ? 4.123   13.851   -30.057 1.00 50.10  ? 109 GLU G C   1 
ATOM   12215 O O   . GLU G  1 109 ? 4.308   13.363   -28.942 1.00 49.21  ? 109 GLU G O   1 
ATOM   12216 C CB  . GLU G  1 109 ? 2.244   12.983   -31.460 1.00 47.63  ? 109 GLU G CB  1 
ATOM   12217 C CG  . GLU G  1 109 ? 2.210   11.625   -30.775 1.00 61.16  ? 109 GLU G CG  1 
ATOM   12218 C CD  . GLU G  1 109 ? 1.129   11.531   -29.714 1.00 75.87  ? 109 GLU G CD  1 
ATOM   12219 O OE1 . GLU G  1 109 ? 0.523   12.570   -29.381 1.00 75.94  ? 109 GLU G OE1 1 
ATOM   12220 O OE2 . GLU G  1 109 ? 0.882   10.415   -29.214 1.00 83.86  ? 109 GLU G OE2 1 
ATOM   12221 N N   . GLN G  1 110 ? 5.116   14.164   -30.882 1.00 42.91  ? 110 GLN G N   1 
ATOM   12222 C CA  . GLN G  1 110 ? 6.507   13.898   -30.537 1.00 50.49  ? 110 GLN G CA  1 
ATOM   12223 C C   . GLN G  1 110 ? 6.992   14.855   -29.460 1.00 60.53  ? 110 GLN G C   1 
ATOM   12224 O O   . GLN G  1 110 ? 7.858   14.515   -28.655 1.00 65.04  ? 110 GLN G O   1 
ATOM   12225 C CB  . GLN G  1 110 ? 7.396   14.028   -31.772 1.00 51.71  ? 110 GLN G CB  1 
ATOM   12226 C CG  . GLN G  1 110 ? 6.824   13.366   -33.006 1.00 52.78  ? 110 GLN G CG  1 
ATOM   12227 C CD  . GLN G  1 110 ? 7.687   12.239   -33.523 1.00 65.85  ? 110 GLN G CD  1 
ATOM   12228 O OE1 . GLN G  1 110 ? 8.693   11.875   -32.913 1.00 74.06  ? 110 GLN G OE1 1 
ATOM   12229 N NE2 . GLN G  1 110 ? 7.297   11.676   -34.657 1.00 60.12  ? 110 GLN G NE2 1 
ATOM   12230 N N   . LEU G  1 111 ? 6.429   16.057   -29.452 1.00 65.68  ? 111 LEU G N   1 
ATOM   12231 C CA  . LEU G  1 111 ? 6.852   17.081   -28.507 1.00 54.82  ? 111 LEU G CA  1 
ATOM   12232 C C   . LEU G  1 111 ? 6.018   17.060   -27.239 1.00 59.42  ? 111 LEU G C   1 
ATOM   12233 O O   . LEU G  1 111 ? 6.325   17.763   -26.278 1.00 57.15  ? 111 LEU G O   1 
ATOM   12234 C CB  . LEU G  1 111 ? 6.794   18.467   -29.148 1.00 51.37  ? 111 LEU G CB  1 
ATOM   12235 C CG  . LEU G  1 111 ? 7.974   18.759   -30.076 1.00 56.00  ? 111 LEU G CG  1 
ATOM   12236 C CD1 . LEU G  1 111 ? 7.697   19.956   -30.953 1.00 49.27  ? 111 LEU G CD1 1 
ATOM   12237 C CD2 . LEU G  1 111 ? 9.266   18.925   -29.295 1.00 66.09  ? 111 LEU G CD2 1 
ATOM   12238 N N   . SER G  1 112 ? 4.969   16.244   -27.239 1.00 53.37  ? 112 SER G N   1 
ATOM   12239 C CA  . SER G  1 112 ? 4.067   16.143   -26.096 1.00 49.39  ? 112 SER G CA  1 
ATOM   12240 C C   . SER G  1 112 ? 4.821   15.981   -24.774 1.00 55.23  ? 112 SER G C   1 
ATOM   12241 O O   . SER G  1 112 ? 4.365   16.456   -23.736 1.00 61.77  ? 112 SER G O   1 
ATOM   12242 C CB  . SER G  1 112 ? 3.075   14.989   -26.293 1.00 54.61  ? 112 SER G CB  1 
ATOM   12243 O OG  . SER G  1 112 ? 3.726   13.729   -26.286 1.00 51.37  ? 112 SER G OG  1 
ATOM   12244 N N   . SER G  1 113 ? 5.974   15.315   -24.821 1.00 55.84  ? 113 SER G N   1 
ATOM   12245 C CA  . SER G  1 113 ? 6.795   15.094   -23.631 1.00 54.39  ? 113 SER G CA  1 
ATOM   12246 C C   . SER G  1 113 ? 8.275   14.980   -23.978 1.00 64.06  ? 113 SER G C   1 
ATOM   12247 O O   . SER G  1 113 ? 8.682   14.084   -24.713 1.00 68.43  ? 113 SER G O   1 
ATOM   12248 C CB  . SER G  1 113 ? 6.346   13.833   -22.890 1.00 66.22  ? 113 SER G CB  1 
ATOM   12249 O OG  . SER G  1 113 ? 6.991   13.722   -21.633 1.00 62.45  ? 113 SER G OG  1 
ATOM   12250 N N   . VAL G  1 114 ? 9.081   15.887   -23.438 1.00 57.43  ? 114 VAL G N   1 
ATOM   12251 C CA  . VAL G  1 114 ? 10.520  15.851   -23.676 1.00 69.07  ? 114 VAL G CA  1 
ATOM   12252 C C   . VAL G  1 114 ? 11.309  15.728   -22.372 1.00 69.17  ? 114 VAL G C   1 
ATOM   12253 O O   . VAL G  1 114 ? 10.956  16.337   -21.362 1.00 65.33  ? 114 VAL G O   1 
ATOM   12254 C CB  . VAL G  1 114 ? 11.011  17.105   -24.433 1.00 71.24  ? 114 VAL G CB  1 
ATOM   12255 C CG1 . VAL G  1 114 ? 10.230  17.297   -25.729 1.00 62.77  ? 114 VAL G CG1 1 
ATOM   12256 C CG2 . VAL G  1 114 ? 10.930  18.338   -23.535 1.00 67.34  ? 114 VAL G CG2 1 
ATOM   12257 N N   . SER G  1 115 ? 12.380  14.938   -22.405 1.00 75.32  ? 115 SER G N   1 
ATOM   12258 C CA  . SER G  1 115 ? 13.260  14.760   -21.252 1.00 91.68  ? 115 SER G CA  1 
ATOM   12259 C C   . SER G  1 115 ? 14.180  15.968   -21.098 1.00 94.84  ? 115 SER G C   1 
ATOM   12260 O O   . SER G  1 115 ? 14.282  16.544   -20.017 1.00 100.12 ? 115 SER G O   1 
ATOM   12261 C CB  . SER G  1 115 ? 14.087  13.479   -21.400 1.00 91.66  ? 115 SER G CB  1 
ATOM   12262 O OG  . SER G  1 115 ? 14.538  13.002   -20.143 1.00 100.78 ? 115 SER G OG  1 
ATOM   12263 N N   . SER G  1 116 ? 14.850  16.342   -22.184 1.00 84.40  ? 116 SER G N   1 
ATOM   12264 C CA  . SER G  1 116 ? 15.674  17.548   -22.209 1.00 88.17  ? 116 SER G CA  1 
ATOM   12265 C C   . SER G  1 116 ? 15.417  18.327   -23.496 1.00 90.41  ? 116 SER G C   1 
ATOM   12266 O O   . SER G  1 116 ? 15.236  17.738   -24.563 1.00 88.93  ? 116 SER G O   1 
ATOM   12267 C CB  . SER G  1 116 ? 17.160  17.208   -22.070 1.00 92.68  ? 116 SER G CB  1 
ATOM   12268 O OG  . SER G  1 116 ? 17.674  16.643   -23.262 1.00 106.49 ? 116 SER G OG  1 
ATOM   12269 N N   . PHE G  1 117 ? 15.406  19.652   -23.390 1.00 76.55  ? 117 PHE G N   1 
ATOM   12270 C CA  . PHE G  1 117 ? 14.990  20.504   -24.497 1.00 72.47  ? 117 PHE G CA  1 
ATOM   12271 C C   . PHE G  1 117 ? 15.701  21.852   -24.476 1.00 70.11  ? 117 PHE G C   1 
ATOM   12272 O O   . PHE G  1 117 ? 15.277  22.771   -23.774 1.00 80.27  ? 117 PHE G O   1 
ATOM   12273 C CB  . PHE G  1 117 ? 13.478  20.729   -24.427 1.00 68.60  ? 117 PHE G CB  1 
ATOM   12274 C CG  . PHE G  1 117 ? 12.893  21.341   -25.668 1.00 68.03  ? 117 PHE G CG  1 
ATOM   12275 C CD1 . PHE G  1 117 ? 12.852  22.716   -25.831 1.00 62.45  ? 117 PHE G CD1 1 
ATOM   12276 C CD2 . PHE G  1 117 ? 12.372  20.538   -26.667 1.00 67.21  ? 117 PHE G CD2 1 
ATOM   12277 C CE1 . PHE G  1 117 ? 12.309  23.275   -26.971 1.00 55.51  ? 117 PHE G CE1 1 
ATOM   12278 C CE2 . PHE G  1 117 ? 11.828  21.091   -27.808 1.00 66.91  ? 117 PHE G CE2 1 
ATOM   12279 C CZ  . PHE G  1 117 ? 11.797  22.461   -27.961 1.00 61.80  ? 117 PHE G CZ  1 
ATOM   12280 N N   . GLU G  1 118 ? 16.776  21.979   -25.248 1.00 66.67  ? 118 GLU G N   1 
ATOM   12281 C CA  . GLU G  1 118 ? 17.483  23.252   -25.325 1.00 80.51  ? 118 GLU G CA  1 
ATOM   12282 C C   . GLU G  1 118 ? 17.436  23.858   -26.726 1.00 75.47  ? 118 GLU G C   1 
ATOM   12283 O O   . GLU G  1 118 ? 17.547  23.154   -27.731 1.00 72.66  ? 118 GLU G O   1 
ATOM   12284 C CB  . GLU G  1 118 ? 18.930  23.116   -24.849 1.00 87.98  ? 118 GLU G CB  1 
ATOM   12285 C CG  . GLU G  1 118 ? 19.881  22.574   -25.894 1.00 99.17  ? 118 GLU G CG  1 
ATOM   12286 C CD  . GLU G  1 118 ? 21.305  23.038   -25.671 1.00 127.58 ? 118 GLU G CD  1 
ATOM   12287 O OE1 . GLU G  1 118 ? 21.555  23.729   -24.661 1.00 136.41 ? 118 GLU G OE1 1 
ATOM   12288 O OE2 . GLU G  1 118 ? 22.174  22.716   -26.508 1.00 122.71 ? 118 GLU G OE2 1 
ATOM   12289 N N   . ARG G  1 119 ? 17.272  25.175   -26.775 1.00 69.15  ? 119 ARG G N   1 
ATOM   12290 C CA  . ARG G  1 119 ? 17.152  25.906   -28.030 1.00 72.48  ? 119 ARG G CA  1 
ATOM   12291 C C   . ARG G  1 119 ? 18.447  26.644   -28.355 1.00 70.86  ? 119 ARG G C   1 
ATOM   12292 O O   . ARG G  1 119 ? 18.826  27.587   -27.661 1.00 90.42  ? 119 ARG G O   1 
ATOM   12293 C CB  . ARG G  1 119 ? 15.984  26.890   -27.942 1.00 72.31  ? 119 ARG G CB  1 
ATOM   12294 C CG  . ARG G  1 119 ? 15.976  27.983   -28.996 1.00 73.45  ? 119 ARG G CG  1 
ATOM   12295 C CD  . ARG G  1 119 ? 14.868  28.990   -28.709 1.00 83.78  ? 119 ARG G CD  1 
ATOM   12296 N NE  . ARG G  1 119 ? 15.018  30.216   -29.489 1.00 84.51  ? 119 ARG G NE  1 
ATOM   12297 C CZ  . ARG G  1 119 ? 15.701  31.287   -29.092 1.00 100.47 ? 119 ARG G CZ  1 
ATOM   12298 N NH1 . ARG G  1 119 ? 16.312  31.303   -27.913 1.00 111.62 ? 119 ARG G NH1 1 
ATOM   12299 N NH2 . ARG G  1 119 ? 15.773  32.348   -29.881 1.00 84.61  ? 119 ARG G NH2 1 
ATOM   12300 N N   . PHE G  1 120 ? 19.123  26.207   -29.412 1.00 68.66  ? 120 PHE G N   1 
ATOM   12301 C CA  . PHE G  1 120 ? 20.397  26.799   -29.798 1.00 72.26  ? 120 PHE G CA  1 
ATOM   12302 C C   . PHE G  1 120 ? 20.348  27.363   -31.212 1.00 70.73  ? 120 PHE G C   1 
ATOM   12303 O O   . PHE G  1 120 ? 19.556  26.919   -32.042 1.00 72.89  ? 120 PHE G O   1 
ATOM   12304 C CB  . PHE G  1 120 ? 21.521  25.768   -29.691 1.00 72.95  ? 120 PHE G CB  1 
ATOM   12305 C CG  . PHE G  1 120 ? 21.427  24.660   -30.702 1.00 74.56  ? 120 PHE G CG  1 
ATOM   12306 C CD1 . PHE G  1 120 ? 22.169  24.705   -31.872 1.00 76.47  ? 120 PHE G CD1 1 
ATOM   12307 C CD2 . PHE G  1 120 ? 20.598  23.573   -30.483 1.00 78.75  ? 120 PHE G CD2 1 
ATOM   12308 C CE1 . PHE G  1 120 ? 22.084  23.687   -32.803 1.00 70.74  ? 120 PHE G CE1 1 
ATOM   12309 C CE2 . PHE G  1 120 ? 20.509  22.552   -31.410 1.00 74.47  ? 120 PHE G CE2 1 
ATOM   12310 C CZ  . PHE G  1 120 ? 21.253  22.609   -32.572 1.00 74.30  ? 120 PHE G CZ  1 
ATOM   12311 N N   . GLU G  1 121 ? 21.205  28.342   -31.480 1.00 79.25  ? 121 GLU G N   1 
ATOM   12312 C CA  . GLU G  1 121 ? 21.285  28.940   -32.804 1.00 78.96  ? 121 GLU G CA  1 
ATOM   12313 C C   . GLU G  1 121 ? 22.081  28.034   -33.736 1.00 80.75  ? 121 GLU G C   1 
ATOM   12314 O O   . GLU G  1 121 ? 23.305  27.950   -33.641 1.00 89.26  ? 121 GLU G O   1 
ATOM   12315 C CB  . GLU G  1 121 ? 21.928  30.325   -32.728 1.00 81.14  ? 121 GLU G CB  1 
ATOM   12316 C CG  . GLU G  1 121 ? 21.682  31.194   -33.949 1.00 91.45  ? 121 GLU G CG  1 
ATOM   12317 C CD  . GLU G  1 121 ? 22.251  32.590   -33.791 1.00 97.89  ? 121 GLU G CD  1 
ATOM   12318 O OE1 . GLU G  1 121 ? 23.045  32.808   -32.851 1.00 99.58  ? 121 GLU G OE1 1 
ATOM   12319 O OE2 . GLU G  1 121 ? 21.907  33.470   -34.608 1.00 99.91  ? 121 GLU G OE2 1 
ATOM   12320 N N   . ILE G  1 122 ? 21.375  27.349   -34.631 1.00 78.88  ? 122 ILE G N   1 
ATOM   12321 C CA  . ILE G  1 122 ? 22.010  26.426   -35.564 1.00 78.22  ? 122 ILE G CA  1 
ATOM   12322 C C   . ILE G  1 122 ? 22.723  27.177   -36.686 1.00 81.05  ? 122 ILE G C   1 
ATOM   12323 O O   . ILE G  1 122 ? 23.827  26.808   -37.087 1.00 83.01  ? 122 ILE G O   1 
ATOM   12324 C CB  . ILE G  1 122 ? 20.991  25.430   -36.155 1.00 75.91  ? 122 ILE G CB  1 
ATOM   12325 C CG1 . ILE G  1 122 ? 21.656  24.540   -37.206 1.00 70.02  ? 122 ILE G CG1 1 
ATOM   12326 C CG2 . ILE G  1 122 ? 19.800  26.169   -36.749 1.00 73.29  ? 122 ILE G CG2 1 
ATOM   12327 C CD1 . ILE G  1 122 ? 20.722  23.518   -37.813 1.00 63.74  ? 122 ILE G CD1 1 
ATOM   12328 N N   . PHE G  1 123 ? 22.088  28.231   -37.185 1.00 92.92  ? 123 PHE G N   1 
ATOM   12329 C CA  . PHE G  1 123 ? 22.705  29.090   -38.188 1.00 85.83  ? 123 PHE G CA  1 
ATOM   12330 C C   . PHE G  1 123 ? 22.655  30.549   -37.746 1.00 91.72  ? 123 PHE G C   1 
ATOM   12331 O O   . PHE G  1 123 ? 21.650  31.227   -37.953 1.00 87.76  ? 123 PHE G O   1 
ATOM   12332 C CB  . PHE G  1 123 ? 22.011  28.936   -39.545 1.00 79.12  ? 123 PHE G CB  1 
ATOM   12333 C CG  . PHE G  1 123 ? 22.123  27.559   -40.134 1.00 81.87  ? 123 PHE G CG  1 
ATOM   12334 C CD1 . PHE G  1 123 ? 20.987  26.824   -40.428 1.00 79.60  ? 123 PHE G CD1 1 
ATOM   12335 C CD2 . PHE G  1 123 ? 23.363  26.999   -40.391 1.00 85.45  ? 123 PHE G CD2 1 
ATOM   12336 C CE1 . PHE G  1 123 ? 21.085  25.557   -40.970 1.00 75.27  ? 123 PHE G CE1 1 
ATOM   12337 C CE2 . PHE G  1 123 ? 23.468  25.732   -40.932 1.00 79.88  ? 123 PHE G CE2 1 
ATOM   12338 C CZ  . PHE G  1 123 ? 22.327  25.010   -41.222 1.00 74.86  ? 123 PHE G CZ  1 
ATOM   12339 N N   . PRO G  1 124 ? 23.743  31.035   -37.129 1.00 102.83 ? 124 PRO G N   1 
ATOM   12340 C CA  . PRO G  1 124 ? 23.828  32.436   -36.696 1.00 100.87 ? 124 PRO G CA  1 
ATOM   12341 C C   . PRO G  1 124 ? 23.547  33.392   -37.852 1.00 102.78 ? 124 PRO G C   1 
ATOM   12342 O O   . PRO G  1 124 ? 24.097  33.198   -38.933 1.00 100.48 ? 124 PRO G O   1 
ATOM   12343 C CB  . PRO G  1 124 ? 25.283  32.573   -36.245 1.00 105.43 ? 124 PRO G CB  1 
ATOM   12344 C CG  . PRO G  1 124 ? 25.692  31.193   -35.865 1.00 101.96 ? 124 PRO G CG  1 
ATOM   12345 C CD  . PRO G  1 124 ? 24.963  30.277   -36.801 1.00 94.58  ? 124 PRO G CD  1 
ATOM   12346 N N   . LYS G  1 125 ? 22.717  34.407   -37.620 1.00 100.45 ? 125 LYS G N   1 
ATOM   12347 C CA  . LYS G  1 125 ? 22.267  35.299   -38.684 1.00 108.05 ? 125 LYS G CA  1 
ATOM   12348 C C   . LYS G  1 125 ? 23.402  36.055   -39.365 1.00 123.82 ? 125 LYS G C   1 
ATOM   12349 O O   . LYS G  1 125 ? 23.322  36.363   -40.556 1.00 114.61 ? 125 LYS G O   1 
ATOM   12350 C CB  . LYS G  1 125 ? 21.239  36.299   -38.145 1.00 105.35 ? 125 LYS G CB  1 
ATOM   12351 C CG  . LYS G  1 125 ? 20.666  37.218   -39.210 1.00 97.32  ? 125 LYS G CG  1 
ATOM   12352 C CD  . LYS G  1 125 ? 19.401  37.918   -38.746 1.00 89.32  ? 125 LYS G CD  1 
ATOM   12353 C CE  . LYS G  1 125 ? 19.683  38.930   -37.649 1.00 103.72 ? 125 LYS G CE  1 
ATOM   12354 N NZ  . LYS G  1 125 ? 18.460  39.697   -37.269 1.00 102.22 ? 125 LYS G NZ  1 
ATOM   12355 N N   . THR G  1 126 ? 24.463  36.347   -38.622 1.00 176.66 ? 126 THR G N   1 
ATOM   12356 C CA  . THR G  1 126 ? 25.474  37.293   -39.099 1.00 177.66 ? 126 THR G CA  1 
ATOM   12357 C C   . THR G  1 126 ? 26.776  36.693   -39.640 1.00 173.36 ? 126 THR G C   1 
ATOM   12358 O O   . THR G  1 126 ? 27.755  37.417   -39.818 1.00 187.43 ? 126 THR G O   1 
ATOM   12359 C CB  . THR G  1 126 ? 25.874  38.263   -37.962 1.00 140.64 ? 126 THR G CB  1 
ATOM   12360 O OG1 . THR G  1 126 ? 25.916  37.549   -36.716 1.00 135.49 ? 126 THR G OG1 1 
ATOM   12361 N N   . SER G  1 127 ? 26.794  35.392   -39.901 1.00 112.07 ? 127 SER G N   1 
ATOM   12362 C CA  . SER G  1 127 ? 27.988  34.756   -40.426 1.00 107.39 ? 127 SER G CA  1 
ATOM   12363 C C   . SER G  1 127 ? 27.636  33.653   -41.433 1.00 104.26 ? 127 SER G C   1 
ATOM   12364 O O   . SER G  1 127 ? 28.487  33.192   -42.195 1.00 114.85 ? 127 SER G O   1 
ATOM   12365 C CB  . SER G  1 127 ? 28.837  34.213   -39.279 1.00 114.57 ? 127 SER G CB  1 
ATOM   12366 O OG  . SER G  1 127 ? 28.088  33.302   -38.491 1.00 104.79 ? 127 SER G OG  1 
ATOM   12367 N N   . SER G  1 128 ? 26.364  33.272   -41.468 1.00 101.27 ? 128 SER G N   1 
ATOM   12368 C CA  . SER G  1 128 ? 25.918  32.145   -42.276 1.00 90.64  ? 128 SER G CA  1 
ATOM   12369 C C   . SER G  1 128 ? 25.442  32.588   -43.653 1.00 96.66  ? 128 SER G C   1 
ATOM   12370 O O   . SER G  1 128 ? 25.514  31.832   -44.624 1.00 97.09  ? 128 SER G O   1 
ATOM   12371 C CB  . SER G  1 128 ? 24.803  31.393   -41.547 1.00 96.99  ? 128 SER G CB  1 
ATOM   12372 O OG  . SER G  1 128 ? 25.217  31.030   -40.239 1.00 95.00  ? 128 SER G OG  1 
ATOM   12373 N N   . TRP G  1 129 ? 24.970  33.826   -43.734 1.00 104.23 ? 129 TRP G N   1 
ATOM   12374 C CA  . TRP G  1 129 ? 24.384  34.331   -44.968 1.00 100.63 ? 129 TRP G CA  1 
ATOM   12375 C C   . TRP G  1 129 ? 25.030  35.640   -45.411 1.00 110.79 ? 129 TRP G C   1 
ATOM   12376 O O   . TRP G  1 129 ? 24.466  36.716   -45.214 1.00 105.54 ? 129 TRP G O   1 
ATOM   12377 C CB  . TRP G  1 129 ? 22.875  34.494   -44.793 1.00 107.36 ? 129 TRP G CB  1 
ATOM   12378 C CG  . TRP G  1 129 ? 22.278  33.402   -43.957 1.00 91.31  ? 129 TRP G CG  1 
ATOM   12379 C CD1 . TRP G  1 129 ? 21.726  33.527   -42.716 1.00 88.73  ? 129 TRP G CD1 1 
ATOM   12380 C CD2 . TRP G  1 129 ? 22.201  32.011   -44.292 1.00 87.74  ? 129 TRP G CD2 1 
ATOM   12381 N NE1 . TRP G  1 129 ? 21.298  32.303   -42.262 1.00 94.66  ? 129 TRP G NE1 1 
ATOM   12382 C CE2 . TRP G  1 129 ? 21.579  31.356   -43.211 1.00 86.01  ? 129 TRP G CE2 1 
ATOM   12383 C CE3 . TRP G  1 129 ? 22.591  31.258   -45.403 1.00 89.04  ? 129 TRP G CE3 1 
ATOM   12384 C CZ2 . TRP G  1 129 ? 21.338  29.983   -43.209 1.00 85.60  ? 129 TRP G CZ2 1 
ATOM   12385 C CZ3 . TRP G  1 129 ? 22.353  29.896   -45.399 1.00 76.54  ? 129 TRP G CZ3 1 
ATOM   12386 C CH2 . TRP G  1 129 ? 21.732  29.273   -44.310 1.00 77.93  ? 129 TRP G CH2 1 
ATOM   12387 N N   . PRO G  1 130 ? 26.223  35.541   -46.018 1.00 120.11 ? 130 PRO G N   1 
ATOM   12388 C CA  . PRO G  1 130 ? 27.037  36.672   -46.473 1.00 108.89 ? 130 PRO G CA  1 
ATOM   12389 C C   . PRO G  1 130 ? 26.698  37.090   -47.899 1.00 117.12 ? 130 PRO G C   1 
ATOM   12390 O O   . PRO G  1 130 ? 27.133  38.151   -48.346 1.00 126.95 ? 130 PRO G O   1 
ATOM   12391 C CB  . PRO G  1 130 ? 28.467  36.108   -46.441 1.00 117.04 ? 130 PRO G CB  1 
ATOM   12392 C CG  . PRO G  1 130 ? 28.350  34.687   -45.906 1.00 112.99 ? 130 PRO G CG  1 
ATOM   12393 C CD  . PRO G  1 130 ? 26.947  34.272   -46.172 1.00 121.51 ? 130 PRO G CD  1 
ATOM   12394 N N   . ASN G  1 131 ? 25.943  36.256   -48.606 1.00 114.38 ? 131 ASN G N   1 
ATOM   12395 C CA  . ASN G  1 131 ? 25.577  36.540   -49.988 1.00 116.78 ? 131 ASN G CA  1 
ATOM   12396 C C   . ASN G  1 131 ? 24.086  36.814   -50.136 1.00 108.36 ? 131 ASN G C   1 
ATOM   12397 O O   . ASN G  1 131 ? 23.574  36.940   -51.249 1.00 99.73  ? 131 ASN G O   1 
ATOM   12398 C CB  . ASN G  1 131 ? 25.988  35.381   -50.899 1.00 121.29 ? 131 ASN G CB  1 
ATOM   12399 C CG  . ASN G  1 131 ? 27.489  35.166   -50.926 1.00 131.71 ? 131 ASN G CG  1 
ATOM   12400 O OD1 . ASN G  1 131 ? 28.262  36.059   -50.582 1.00 136.11 ? 131 ASN G OD1 1 
ATOM   12401 N ND2 . ASN G  1 131 ? 27.908  33.976   -51.340 1.00 137.85 ? 131 ASN G ND2 1 
ATOM   12402 N N   . HIS G  1 132 ? 23.396  36.904   -49.004 1.00 107.19 ? 132 HIS G N   1 
ATOM   12403 C CA  . HIS G  1 132 ? 21.957  37.130   -48.997 1.00 90.39  ? 132 HIS G CA  1 
ATOM   12404 C C   . HIS G  1 132 ? 21.573  38.085   -47.875 1.00 93.45  ? 132 HIS G C   1 
ATOM   12405 O O   . HIS G  1 132 ? 22.280  38.196   -46.873 1.00 105.11 ? 132 HIS G O   1 
ATOM   12406 C CB  . HIS G  1 132 ? 21.217  35.803   -48.825 1.00 86.67  ? 132 HIS G CB  1 
ATOM   12407 C CG  . HIS G  1 132 ? 21.688  34.725   -49.749 1.00 81.89  ? 132 HIS G CG  1 
ATOM   12408 N ND1 . HIS G  1 132 ? 21.008  34.375   -50.896 1.00 81.22  ? 132 HIS G ND1 1 
ATOM   12409 C CD2 . HIS G  1 132 ? 22.778  33.920   -49.698 1.00 79.46  ? 132 HIS G CD2 1 
ATOM   12410 C CE1 . HIS G  1 132 ? 21.656  33.400   -51.508 1.00 83.00  ? 132 HIS G CE1 1 
ATOM   12411 N NE2 . HIS G  1 132 ? 22.731  33.106   -50.805 1.00 78.45  ? 132 HIS G NE2 1 
ATOM   12412 N N   . ASP G  1 133 ? 20.451  38.775   -48.045 1.00 77.72  ? 133 ASP G N   1 
ATOM   12413 C CA  . ASP G  1 133 ? 19.974  39.704   -47.029 1.00 93.96  ? 133 ASP G CA  1 
ATOM   12414 C C   . ASP G  1 133 ? 19.170  38.963   -45.967 1.00 94.73  ? 133 ASP G C   1 
ATOM   12415 O O   . ASP G  1 133 ? 18.154  38.335   -46.266 1.00 84.75  ? 133 ASP G O   1 
ATOM   12416 C CB  . ASP G  1 133 ? 19.131  40.810   -47.666 1.00 91.64  ? 133 ASP G CB  1 
ATOM   12417 C CG  . ASP G  1 133 ? 18.891  41.977   -46.727 1.00 111.83 ? 133 ASP G CG  1 
ATOM   12418 O OD1 . ASP G  1 133 ? 18.563  41.740   -45.546 1.00 111.14 ? 133 ASP G OD1 1 
ATOM   12419 O OD2 . ASP G  1 133 ? 19.029  43.135   -47.174 1.00 122.43 ? 133 ASP G OD2 1 
ATOM   12420 N N   . SER G  1 134 ? 19.634  39.037   -44.725 1.00 87.60  ? 134 SER G N   1 
ATOM   12421 C CA  . SER G  1 134 ? 18.976  38.354   -43.620 1.00 82.45  ? 134 SER G CA  1 
ATOM   12422 C C   . SER G  1 134 ? 18.289  39.347   -42.689 1.00 86.58  ? 134 SER G C   1 
ATOM   12423 O O   . SER G  1 134 ? 18.144  39.094   -41.494 1.00 100.08 ? 134 SER G O   1 
ATOM   12424 C CB  . SER G  1 134 ? 19.990  37.513   -42.841 1.00 93.08  ? 134 SER G CB  1 
ATOM   12425 O OG  . SER G  1 134 ? 21.107  38.293   -42.453 1.00 95.61  ? 134 SER G OG  1 
ATOM   12426 N N   . ASN G  1 135 ? 17.859  40.476   -43.247 1.00 93.22  ? 135 ASN G N   1 
ATOM   12427 C CA  . ASN G  1 135 ? 17.251  41.540   -42.455 1.00 97.62  ? 135 ASN G CA  1 
ATOM   12428 C C   . ASN G  1 135 ? 15.914  42.022   -43.013 1.00 98.65  ? 135 ASN G C   1 
ATOM   12429 O O   . ASN G  1 135 ? 15.061  42.506   -42.270 1.00 114.03 ? 135 ASN G O   1 
ATOM   12430 C CB  . ASN G  1 135 ? 18.216  42.721   -42.328 1.00 107.63 ? 135 ASN G CB  1 
ATOM   12431 C CG  . ASN G  1 135 ? 19.466  42.369   -41.548 1.00 107.84 ? 135 ASN G CG  1 
ATOM   12432 O OD1 . ASN G  1 135 ? 19.395  41.753   -40.484 1.00 90.74  ? 135 ASN G OD1 1 
ATOM   12433 N ND2 . ASN G  1 135 ? 20.622  42.765   -42.070 1.00 104.11 ? 135 ASN G ND2 1 
ATOM   12434 N N   . LYS G  1 136 ? 15.736  41.886   -44.322 1.00 94.09  ? 136 LYS G N   1 
ATOM   12435 C CA  . LYS G  1 136 ? 14.525  42.358   -44.984 1.00 102.82 ? 136 LYS G CA  1 
ATOM   12436 C C   . LYS G  1 136 ? 13.385  41.358   -44.872 1.00 108.62 ? 136 LYS G C   1 
ATOM   12437 O O   . LYS G  1 136 ? 12.308  41.571   -45.429 1.00 106.13 ? 136 LYS G O   1 
ATOM   12438 C CB  . LYS G  1 136 ? 14.802  42.626   -46.459 1.00 115.63 ? 136 LYS G CB  1 
ATOM   12439 C CG  . LYS G  1 136 ? 15.938  43.578   -46.688 1.00 124.20 ? 136 LYS G CG  1 
ATOM   12440 C CD  . LYS G  1 136 ? 15.484  44.773   -47.480 1.00 130.84 ? 136 LYS G CD  1 
ATOM   12441 C CE  . LYS G  1 136 ? 16.287  45.966   -47.058 1.00 144.19 ? 136 LYS G CE  1 
ATOM   12442 N NZ  . LYS G  1 136 ? 16.326  46.073   -45.575 1.00 142.00 ? 136 LYS G NZ  1 
ATOM   12443 N N   . GLY G  1 137 ? 13.628  40.268   -44.154 1.00 98.10  ? 137 GLY G N   1 
ATOM   12444 C CA  . GLY G  1 137 ? 12.662  39.190   -44.064 1.00 92.55  ? 137 GLY G CA  1 
ATOM   12445 C C   . GLY G  1 137 ? 11.574  39.410   -43.030 1.00 88.38  ? 137 GLY G C   1 
ATOM   12446 O O   . GLY G  1 137 ? 11.500  38.687   -42.038 1.00 84.66  ? 137 GLY G O   1 
ATOM   12447 N N   . VAL G  1 138 ? 10.725  40.408   -43.258 1.00 85.89  ? 138 VAL G N   1 
ATOM   12448 C CA  . VAL G  1 138 ? 9.611   40.671   -42.354 1.00 84.28  ? 138 VAL G CA  1 
ATOM   12449 C C   . VAL G  1 138 ? 8.304   40.782   -43.131 1.00 79.25  ? 138 VAL G C   1 
ATOM   12450 O O   . VAL G  1 138 ? 8.310   40.835   -44.361 1.00 73.49  ? 138 VAL G O   1 
ATOM   12451 C CB  . VAL G  1 138 ? 9.822   41.959   -41.524 1.00 91.05  ? 138 VAL G CB  1 
ATOM   12452 C CG1 . VAL G  1 138 ? 11.115  41.887   -40.714 1.00 92.84  ? 138 VAL G CG1 1 
ATOM   12453 C CG2 . VAL G  1 138 ? 9.794   43.197   -42.414 1.00 86.93  ? 138 VAL G CG2 1 
ATOM   12454 N N   . THR G  1 139 ? 7.189   40.822   -42.406 1.00 76.18  ? 139 THR G N   1 
ATOM   12455 C CA  . THR G  1 139 ? 5.866   40.886   -43.023 1.00 88.28  ? 139 THR G CA  1 
ATOM   12456 C C   . THR G  1 139 ? 4.801   41.445   -42.078 1.00 95.89  ? 139 THR G C   1 
ATOM   12457 O O   . THR G  1 139 ? 4.927   41.350   -40.856 1.00 95.18  ? 139 THR G O   1 
ATOM   12458 C CB  . THR G  1 139 ? 5.410   39.499   -43.517 1.00 86.50  ? 139 THR G CB  1 
ATOM   12459 O OG1 . THR G  1 139 ? 4.045   39.568   -43.947 1.00 82.48  ? 139 THR G OG1 1 
ATOM   12460 C CG2 . THR G  1 139 ? 5.527   38.471   -42.401 1.00 87.07  ? 139 THR G CG2 1 
ATOM   12461 N N   . ALA G  1 140 ? 3.750   42.026   -42.652 1.00 101.86 ? 140 ALA G N   1 
ATOM   12462 C CA  . ALA G  1 140 ? 2.641   42.559   -41.868 1.00 106.06 ? 140 ALA G CA  1 
ATOM   12463 C C   . ALA G  1 140 ? 1.837   41.424   -41.250 1.00 107.91 ? 140 ALA G C   1 
ATOM   12464 O O   . ALA G  1 140 ? 1.014   41.639   -40.361 1.00 104.13 ? 140 ALA G O   1 
ATOM   12465 C CB  . ALA G  1 140 ? 1.748   43.437   -42.731 1.00 109.38 ? 140 ALA G CB  1 
ATOM   12466 N N   . ALA G  1 141 ? 2.084   40.211   -41.730 1.00 107.71 ? 141 ALA G N   1 
ATOM   12467 C CA  . ALA G  1 141 ? 1.433   39.030   -41.183 1.00 96.35  ? 141 ALA G CA  1 
ATOM   12468 C C   . ALA G  1 141 ? 1.967   38.679   -39.796 1.00 94.03  ? 141 ALA G C   1 
ATOM   12469 O O   . ALA G  1 141 ? 1.215   38.252   -38.928 1.00 92.23  ? 141 ALA G O   1 
ATOM   12470 C CB  . ALA G  1 141 ? 1.584   37.853   -42.126 1.00 87.47  ? 141 ALA G CB  1 
ATOM   12471 N N   . CYS G  1 142 ? 3.263   38.858   -39.575 1.00 87.11  ? 142 CYS G N   1 
ATOM   12472 C CA  . CYS G  1 142 ? 3.817   38.579   -38.253 1.00 82.69  ? 142 CYS G CA  1 
ATOM   12473 C C   . CYS G  1 142 ? 4.190   39.865   -37.513 1.00 83.25  ? 142 CYS G C   1 
ATOM   12474 O O   . CYS G  1 142 ? 5.364   40.189   -37.356 1.00 91.01  ? 142 CYS G O   1 
ATOM   12475 C CB  . CYS G  1 142 ? 4.987   37.597   -38.354 1.00 99.35  ? 142 CYS G CB  1 
ATOM   12476 S SG  . CYS G  1 142 ? 4.536   36.069   -39.224 1.00 102.30 ? 142 CYS G SG  1 
ATOM   12477 N N   . PRO G  1 143 ? 3.172   40.602   -37.042 1.00 89.20  ? 143 PRO G N   1 
ATOM   12478 C CA  . PRO G  1 143 ? 3.411   41.921   -36.457 1.00 97.57  ? 143 PRO G CA  1 
ATOM   12479 C C   . PRO G  1 143 ? 3.912   41.841   -35.025 1.00 110.51 ? 143 PRO G C   1 
ATOM   12480 O O   . PRO G  1 143 ? 3.347   41.119   -34.201 1.00 120.04 ? 143 PRO G O   1 
ATOM   12481 C CB  . PRO G  1 143 ? 2.018   42.571   -36.468 1.00 107.24 ? 143 PRO G CB  1 
ATOM   12482 C CG  . PRO G  1 143 ? 1.114   41.613   -37.212 1.00 101.11 ? 143 PRO G CG  1 
ATOM   12483 C CD  . PRO G  1 143 ? 1.740   40.273   -37.056 1.00 101.11 ? 143 PRO G CD  1 
ATOM   12484 N N   . HIS G  1 144 ? 4.972   42.584   -34.739 1.00 115.64 ? 144 HIS G N   1 
ATOM   12485 C CA  . HIS G  1 144 ? 5.403   42.782   -33.368 1.00 126.08 ? 144 HIS G CA  1 
ATOM   12486 C C   . HIS G  1 144 ? 5.152   44.237   -33.000 1.00 136.90 ? 144 HIS G C   1 
ATOM   12487 O O   . HIS G  1 144 ? 5.956   45.117   -33.310 1.00 134.08 ? 144 HIS G O   1 
ATOM   12488 C CB  . HIS G  1 144 ? 6.878   42.420   -33.196 1.00 114.92 ? 144 HIS G CB  1 
ATOM   12489 C CG  . HIS G  1 144 ? 7.241   42.029   -31.797 1.00 124.82 ? 144 HIS G CG  1 
ATOM   12490 N ND1 . HIS G  1 144 ? 8.425   42.404   -31.200 1.00 136.32 ? 144 HIS G ND1 1 
ATOM   12491 C CD2 . HIS G  1 144 ? 6.570   41.300   -30.875 1.00 132.84 ? 144 HIS G CD2 1 
ATOM   12492 C CE1 . HIS G  1 144 ? 8.471   41.918   -29.973 1.00 136.97 ? 144 HIS G CE1 1 
ATOM   12493 N NE2 . HIS G  1 144 ? 7.356   41.244   -29.750 1.00 135.94 ? 144 HIS G NE2 1 
ATOM   12494 N N   . ALA G  1 145 ? 4.013   44.483   -32.361 1.00 136.29 ? 145 ALA G N   1 
ATOM   12495 C CA  . ALA G  1 145 ? 3.643   45.828   -31.944 1.00 133.71 ? 145 ALA G CA  1 
ATOM   12496 C C   . ALA G  1 145 ? 3.601   46.785   -33.136 1.00 134.46 ? 145 ALA G C   1 
ATOM   12497 O O   . ALA G  1 145 ? 4.443   47.677   -33.261 1.00 127.36 ? 145 ALA G O   1 
ATOM   12498 C CB  . ALA G  1 145 ? 4.603   46.324   -30.882 1.00 115.13 ? 145 ALA G CB  1 
ATOM   12499 N N   . GLY G  1 146 ? 2.615   46.581   -34.008 1.00 151.84 ? 146 GLY G N   1 
ATOM   12500 C CA  . GLY G  1 146 ? 2.424   47.405   -35.191 1.00 153.94 ? 146 GLY G CA  1 
ATOM   12501 C C   . GLY G  1 146 ? 3.436   47.113   -36.282 1.00 153.88 ? 146 GLY G C   1 
ATOM   12502 O O   . GLY G  1 146 ? 3.092   46.945   -37.453 1.00 144.67 ? 146 GLY G O   1 
ATOM   12503 N N   . ALA G  1 147 ? 4.694   47.049   -35.869 1.00 131.49 ? 147 ALA G N   1 
ATOM   12504 C CA  . ALA G  1 147 ? 5.835   46.824   -36.743 1.00 129.32 ? 147 ALA G CA  1 
ATOM   12505 C C   . ALA G  1 147 ? 5.803   45.450   -37.441 1.00 122.00 ? 147 ALA G C   1 
ATOM   12506 O O   . ALA G  1 147 ? 5.342   44.470   -36.861 1.00 128.18 ? 147 ALA G O   1 
ATOM   12507 C CB  . ALA G  1 147 ? 7.091   46.979   -35.917 1.00 131.33 ? 147 ALA G CB  1 
ATOM   12508 N N   . LYS G  1 148 ? 6.300   45.386   -38.680 1.00 110.74 ? 148 LYS G N   1 
ATOM   12509 C CA  . LYS G  1 148 ? 6.257   44.159   -39.494 1.00 100.31 ? 148 LYS G CA  1 
ATOM   12510 C C   . LYS G  1 148 ? 7.371   43.171   -39.152 1.00 110.65 ? 148 LYS G C   1 
ATOM   12511 O O   . LYS G  1 148 ? 8.497   43.341   -39.608 1.00 106.59 ? 148 LYS G O   1 
ATOM   12512 C CB  . LYS G  1 148 ? 6.391   44.493   -40.984 1.00 98.70  ? 148 LYS G CB  1 
ATOM   12513 C CG  . LYS G  1 148 ? 5.245   45.258   -41.616 1.00 119.71 ? 148 LYS G CG  1 
ATOM   12514 C CD  . LYS G  1 148 ? 5.464   45.371   -43.124 1.00 120.06 ? 148 LYS G CD  1 
ATOM   12515 C CE  . LYS G  1 148 ? 6.846   45.935   -43.447 1.00 120.56 ? 148 LYS G CE  1 
ATOM   12516 N NZ  . LYS G  1 148 ? 7.105   46.017   -44.914 1.00 112.59 ? 148 LYS G NZ  1 
ATOM   12517 N N   . SER G  1 149 ? 7.064   42.129   -38.384 1.00 113.12 ? 149 SER G N   1 
ATOM   12518 C CA  . SER G  1 149 ? 8.105   41.208   -37.918 1.00 99.84  ? 149 SER G CA  1 
ATOM   12519 C C   . SER G  1 149 ? 8.086   39.835   -38.602 1.00 96.59  ? 149 SER G C   1 
ATOM   12520 O O   . SER G  1 149 ? 7.605   39.692   -39.726 1.00 80.48  ? 149 SER G O   1 
ATOM   12521 C CB  . SER G  1 149 ? 8.023   41.042   -36.397 1.00 103.97 ? 149 SER G CB  1 
ATOM   12522 O OG  . SER G  1 149 ? 9.210   40.469   -35.877 1.00 115.65 ? 149 SER G OG  1 
ATOM   12523 N N   . PHE G  1 150 ? 8.627   38.833   -37.913 1.00 99.93  ? 150 PHE G N   1 
ATOM   12524 C CA  . PHE G  1 150 ? 8.683   37.469   -38.431 1.00 81.28  ? 150 PHE G CA  1 
ATOM   12525 C C   . PHE G  1 150 ? 8.963   36.479   -37.303 1.00 85.44  ? 150 PHE G C   1 
ATOM   12526 O O   . PHE G  1 150 ? 9.177   36.878   -36.158 1.00 91.97  ? 150 PHE G O   1 
ATOM   12527 C CB  . PHE G  1 150 ? 9.760   37.351   -39.515 1.00 72.73  ? 150 PHE G CB  1 
ATOM   12528 C CG  . PHE G  1 150 ? 9.655   36.101   -40.343 1.00 70.24  ? 150 PHE G CG  1 
ATOM   12529 C CD1 . PHE G  1 150 ? 8.549   35.880   -41.146 1.00 66.48  ? 150 PHE G CD1 1 
ATOM   12530 C CD2 . PHE G  1 150 ? 10.666  35.153   -40.328 1.00 70.51  ? 150 PHE G CD2 1 
ATOM   12531 C CE1 . PHE G  1 150 ? 8.447   34.736   -41.912 1.00 60.80  ? 150 PHE G CE1 1 
ATOM   12532 C CE2 . PHE G  1 150 ? 10.570  34.005   -41.095 1.00 71.05  ? 150 PHE G CE2 1 
ATOM   12533 C CZ  . PHE G  1 150 ? 9.459   33.797   -41.888 1.00 61.28  ? 150 PHE G CZ  1 
ATOM   12534 N N   . TYR G  1 151 ? 8.953   35.189   -37.627 1.00 83.06  ? 151 TYR G N   1 
ATOM   12535 C CA  . TYR G  1 151 ? 9.271   34.157   -36.647 1.00 68.62  ? 151 TYR G CA  1 
ATOM   12536 C C   . TYR G  1 151 ? 10.701  34.340   -36.152 1.00 68.37  ? 151 TYR G C   1 
ATOM   12537 O O   . TYR G  1 151 ? 11.597  34.659   -36.932 1.00 74.16  ? 151 TYR G O   1 
ATOM   12538 C CB  . TYR G  1 151 ? 9.103   32.762   -37.254 1.00 70.89  ? 151 TYR G CB  1 
ATOM   12539 C CG  . TYR G  1 151 ? 7.744   32.515   -37.870 1.00 62.74  ? 151 TYR G CG  1 
ATOM   12540 C CD1 . TYR G  1 151 ? 6.644   32.214   -37.078 1.00 67.53  ? 151 TYR G CD1 1 
ATOM   12541 C CD2 . TYR G  1 151 ? 7.564   32.577   -39.245 1.00 55.50  ? 151 TYR G CD2 1 
ATOM   12542 C CE1 . TYR G  1 151 ? 5.401   31.986   -37.638 1.00 65.50  ? 151 TYR G CE1 1 
ATOM   12543 C CE2 . TYR G  1 151 ? 6.325   32.350   -39.815 1.00 51.93  ? 151 TYR G CE2 1 
ATOM   12544 C CZ  . TYR G  1 151 ? 5.247   32.055   -39.007 1.00 60.54  ? 151 TYR G CZ  1 
ATOM   12545 O OH  . TYR G  1 151 ? 4.011   31.829   -39.567 1.00 61.01  ? 151 TYR G OH  1 
ATOM   12546 N N   . LYS G  1 152 ? 10.912  34.140   -34.855 1.00 65.18  ? 152 LYS G N   1 
ATOM   12547 C CA  . LYS G  1 152 ? 12.229  34.328   -34.254 1.00 75.51  ? 152 LYS G CA  1 
ATOM   12548 C C   . LYS G  1 152 ? 13.190  33.206   -34.627 1.00 76.41  ? 152 LYS G C   1 
ATOM   12549 O O   . LYS G  1 152 ? 14.367  33.445   -34.898 1.00 86.11  ? 152 LYS G O   1 
ATOM   12550 C CB  . LYS G  1 152 ? 12.113  34.416   -32.730 1.00 81.71  ? 152 LYS G CB  1 
ATOM   12551 C CG  . LYS G  1 152 ? 11.256  35.567   -32.233 1.00 108.25 ? 152 LYS G CG  1 
ATOM   12552 C CD  . LYS G  1 152 ? 11.829  36.907   -32.659 1.00 125.24 ? 152 LYS G CD  1 
ATOM   12553 C CE  . LYS G  1 152 ? 10.986  38.057   -32.130 1.00 138.78 ? 152 LYS G CE  1 
ATOM   12554 N NZ  . LYS G  1 152 ? 11.510  39.380   -32.566 1.00 137.92 ? 152 LYS G NZ  1 
ATOM   12555 N N   . ASN G  1 153 ? 12.681  31.980   -34.636 1.00 73.67  ? 153 ASN G N   1 
ATOM   12556 C CA  . ASN G  1 153 ? 13.509  30.804   -34.865 1.00 66.22  ? 153 ASN G CA  1 
ATOM   12557 C C   . ASN G  1 153 ? 13.781  30.540   -36.342 1.00 64.66  ? 153 ASN G C   1 
ATOM   12558 O O   . ASN G  1 153 ? 14.387  29.530   -36.697 1.00 60.90  ? 153 ASN G O   1 
ATOM   12559 C CB  . ASN G  1 153 ? 12.861  29.578   -34.223 1.00 56.51  ? 153 ASN G CB  1 
ATOM   12560 C CG  . ASN G  1 153 ? 12.695  29.728   -32.726 1.00 72.44  ? 153 ASN G CG  1 
ATOM   12561 O OD1 . ASN G  1 153 ? 13.397  30.514   -32.090 1.00 86.29  ? 153 ASN G OD1 1 
ATOM   12562 N ND2 . ASN G  1 153 ? 11.766  28.973   -32.153 1.00 77.98  ? 153 ASN G ND2 1 
ATOM   12563 N N   . LEU G  1 154 ? 13.332  31.455   -37.194 1.00 65.31  ? 154 LEU G N   1 
ATOM   12564 C CA  . LEU G  1 154 ? 13.488  31.316   -38.638 1.00 71.85  ? 154 LEU G CA  1 
ATOM   12565 C C   . LEU G  1 154 ? 13.885  32.651   -39.270 1.00 76.53  ? 154 LEU G C   1 
ATOM   12566 O O   . LEU G  1 154 ? 13.474  33.710   -38.799 1.00 87.10  ? 154 LEU G O   1 
ATOM   12567 C CB  . LEU G  1 154 ? 12.182  30.810   -39.268 1.00 71.54  ? 154 LEU G CB  1 
ATOM   12568 C CG  . LEU G  1 154 ? 11.713  29.385   -38.950 1.00 63.95  ? 154 LEU G CG  1 
ATOM   12569 C CD1 . LEU G  1 154 ? 10.370  29.074   -39.609 1.00 65.86  ? 154 LEU G CD1 1 
ATOM   12570 C CD2 . LEU G  1 154 ? 12.758  28.364   -39.374 1.00 68.55  ? 154 LEU G CD2 1 
ATOM   12571 N N   . ILE G  1 155 ? 14.694  32.598   -40.325 1.00 73.94  ? 155 ILE G N   1 
ATOM   12572 C CA  . ILE G  1 155 ? 15.048  33.797   -41.084 1.00 82.62  ? 155 ILE G CA  1 
ATOM   12573 C C   . ILE G  1 155 ? 14.562  33.709   -42.523 1.00 72.26  ? 155 ILE G C   1 
ATOM   12574 O O   . ILE G  1 155 ? 14.909  32.776   -43.248 1.00 62.16  ? 155 ILE G O   1 
ATOM   12575 C CB  . ILE G  1 155 ? 16.566  34.029   -41.166 1.00 81.85  ? 155 ILE G CB  1 
ATOM   12576 C CG1 . ILE G  1 155 ? 17.167  34.332   -39.797 1.00 81.64  ? 155 ILE G CG1 1 
ATOM   12577 C CG2 . ILE G  1 155 ? 16.862  35.183   -42.113 1.00 69.93  ? 155 ILE G CG2 1 
ATOM   12578 C CD1 . ILE G  1 155 ? 18.666  34.640   -39.853 1.00 104.55 ? 155 ILE G CD1 1 
ATOM   12579 N N   . TRP G  1 156 ? 13.784  34.701   -42.939 1.00 62.33  ? 156 TRP G N   1 
ATOM   12580 C CA  . TRP G  1 156 ? 13.305  34.766   -44.312 1.00 63.98  ? 156 TRP G CA  1 
ATOM   12581 C C   . TRP G  1 156 ? 14.328  35.464   -45.208 1.00 77.40  ? 156 TRP G C   1 
ATOM   12582 O O   . TRP G  1 156 ? 14.325  36.689   -45.337 1.00 90.07  ? 156 TRP G O   1 
ATOM   12583 C CB  . TRP G  1 156 ? 11.956  35.486   -44.370 1.00 67.68  ? 156 TRP G CB  1 
ATOM   12584 C CG  . TRP G  1 156 ? 11.290  35.436   -45.717 1.00 66.24  ? 156 TRP G CG  1 
ATOM   12585 C CD1 . TRP G  1 156 ? 11.800  34.908   -46.870 1.00 66.41  ? 156 TRP G CD1 1 
ATOM   12586 C CD2 . TRP G  1 156 ? 9.988   35.937   -46.049 1.00 74.28  ? 156 TRP G CD2 1 
ATOM   12587 N NE1 . TRP G  1 156 ? 10.896  35.050   -47.896 1.00 67.70  ? 156 TRP G NE1 1 
ATOM   12588 C CE2 . TRP G  1 156 ? 9.776   35.679   -47.418 1.00 74.22  ? 156 TRP G CE2 1 
ATOM   12589 C CE3 . TRP G  1 156 ? 8.978   36.569   -45.319 1.00 75.95  ? 156 TRP G CE3 1 
ATOM   12590 C CZ2 . TRP G  1 156 ? 8.600   36.040   -48.072 1.00 79.19  ? 156 TRP G CZ2 1 
ATOM   12591 C CZ3 . TRP G  1 156 ? 7.815   36.936   -45.971 1.00 82.38  ? 156 TRP G CZ3 1 
ATOM   12592 C CH2 . TRP G  1 156 ? 7.634   36.666   -47.333 1.00 79.16  ? 156 TRP G CH2 1 
ATOM   12593 N N   . LEU G  1 157 ? 15.201  34.675   -45.825 1.00 70.13  ? 157 LEU G N   1 
ATOM   12594 C CA  . LEU G  1 157 ? 16.248  35.214   -46.688 1.00 67.45  ? 157 LEU G CA  1 
ATOM   12595 C C   . LEU G  1 157 ? 15.691  35.781   -47.988 1.00 75.51  ? 157 LEU G C   1 
ATOM   12596 O O   . LEU G  1 157 ? 14.894  35.136   -48.668 1.00 71.61  ? 157 LEU G O   1 
ATOM   12597 C CB  . LEU G  1 157 ? 17.295  34.146   -47.005 1.00 64.50  ? 157 LEU G CB  1 
ATOM   12598 C CG  . LEU G  1 157 ? 18.209  33.713   -45.859 1.00 72.85  ? 157 LEU G CG  1 
ATOM   12599 C CD1 . LEU G  1 157 ? 19.321  32.816   -46.381 1.00 71.65  ? 157 LEU G CD1 1 
ATOM   12600 C CD2 . LEU G  1 157 ? 18.780  34.917   -45.119 1.00 73.95  ? 157 LEU G CD2 1 
ATOM   12601 N N   . VAL G  1 158 ? 16.123  36.992   -48.325 1.00 82.43  ? 158 VAL G N   1 
ATOM   12602 C CA  . VAL G  1 158 ? 15.746  37.625   -49.582 1.00 76.58  ? 158 VAL G CA  1 
ATOM   12603 C C   . VAL G  1 158 ? 16.998  38.002   -50.366 1.00 80.83  ? 158 VAL G C   1 
ATOM   12604 O O   . VAL G  1 158 ? 18.108  37.947   -49.836 1.00 82.82  ? 158 VAL G O   1 
ATOM   12605 C CB  . VAL G  1 158 ? 14.888  38.885   -49.354 1.00 74.76  ? 158 VAL G CB  1 
ATOM   12606 C CG1 . VAL G  1 158 ? 13.575  38.522   -48.676 1.00 86.46  ? 158 VAL G CG1 1 
ATOM   12607 C CG2 . VAL G  1 158 ? 15.654  39.908   -48.531 1.00 87.00  ? 158 VAL G CG2 1 
ATOM   12608 N N   . LYS G  1 159 ? 16.819  38.385   -51.626 1.00 94.83  ? 159 LYS G N   1 
ATOM   12609 C CA  . LYS G  1 159 ? 17.949  38.726   -52.483 1.00 99.16  ? 159 LYS G CA  1 
ATOM   12610 C C   . LYS G  1 159 ? 18.692  39.952   -51.961 1.00 98.26  ? 159 LYS G C   1 
ATOM   12611 O O   . LYS G  1 159 ? 18.076  40.912   -51.496 1.00 83.62  ? 159 LYS G O   1 
ATOM   12612 C CB  . LYS G  1 159 ? 17.483  38.970   -53.920 1.00 102.72 ? 159 LYS G CB  1 
ATOM   12613 C CG  . LYS G  1 159 ? 16.624  40.211   -54.092 1.00 102.12 ? 159 LYS G CG  1 
ATOM   12614 C CD  . LYS G  1 159 ? 16.302  40.465   -55.554 1.00 110.45 ? 159 LYS G CD  1 
ATOM   12615 C CE  . LYS G  1 159 ? 15.580  41.789   -55.733 1.00 111.08 ? 159 LYS G CE  1 
ATOM   12616 N NZ  . LYS G  1 159 ? 15.245  42.047   -57.160 1.00 111.79 ? 159 LYS G NZ  1 
ATOM   12617 N N   . LYS G  1 160 ? 20.018  39.915   -52.040 1.00 117.19 ? 160 LYS G N   1 
ATOM   12618 C CA  . LYS G  1 160 ? 20.837  41.037   -51.596 1.00 124.32 ? 160 LYS G CA  1 
ATOM   12619 C C   . LYS G  1 160 ? 21.145  41.986   -52.745 1.00 130.07 ? 160 LYS G C   1 
ATOM   12620 O O   . LYS G  1 160 ? 22.121  41.799   -53.471 1.00 117.26 ? 160 LYS G O   1 
ATOM   12621 C CB  . LYS G  1 160 ? 22.143  40.546   -50.976 1.00 114.48 ? 160 LYS G CB  1 
ATOM   12622 C CG  . LYS G  1 160 ? 23.120  41.663   -50.650 1.00 122.61 ? 160 LYS G CG  1 
ATOM   12623 C CD  . LYS G  1 160 ? 24.401  41.118   -50.048 1.00 124.48 ? 160 LYS G CD  1 
ATOM   12624 C CE  . LYS G  1 160 ? 24.113  40.283   -48.813 1.00 125.70 ? 160 LYS G CE  1 
ATOM   12625 N NZ  . LYS G  1 160 ? 25.353  39.986   -48.047 1.00 132.16 ? 160 LYS G NZ  1 
ATOM   12626 N N   . GLY G  1 161 ? 20.308  43.006   -52.901 1.00 133.41 ? 161 GLY G N   1 
ATOM   12627 C CA  . GLY G  1 161 ? 20.496  43.982   -53.954 1.00 119.38 ? 161 GLY G CA  1 
ATOM   12628 C C   . GLY G  1 161 ? 20.642  43.328   -55.312 1.00 126.84 ? 161 GLY G C   1 
ATOM   12629 O O   . GLY G  1 161 ? 21.707  43.387   -55.927 1.00 136.93 ? 161 GLY G O   1 
ATOM   12630 N N   . ASN G  1 162 ? 19.571  42.687   -55.769 1.00 118.60 ? 162 ASN G N   1 
ATOM   12631 C CA  . ASN G  1 162 ? 19.524  42.112   -57.109 1.00 127.44 ? 162 ASN G CA  1 
ATOM   12632 C C   . ASN G  1 162 ? 20.389  40.875   -57.301 1.00 129.55 ? 162 ASN G C   1 
ATOM   12633 O O   . ASN G  1 162 ? 20.825  40.582   -58.414 1.00 131.23 ? 162 ASN G O   1 
ATOM   12634 C CB  . ASN G  1 162 ? 19.898  43.162   -58.152 1.00 146.68 ? 162 ASN G CB  1 
ATOM   12635 C CG  . ASN G  1 162 ? 18.759  43.469   -59.087 1.00 157.48 ? 162 ASN G CG  1 
ATOM   12636 O OD1 . ASN G  1 162 ? 18.913  44.218   -60.046 1.00 174.97 ? 162 ASN G OD1 1 
ATOM   12637 N ND2 . ASN G  1 162 ? 17.602  42.881   -58.818 1.00 150.50 ? 162 ASN G ND2 1 
ATOM   12638 N N   . SER G  1 163 ? 20.631  40.145   -56.221 1.00 128.63 ? 163 SER G N   1 
ATOM   12639 C CA  . SER G  1 163 ? 21.457  38.953   -56.314 1.00 127.96 ? 163 SER G CA  1 
ATOM   12640 C C   . SER G  1 163 ? 21.018  37.883   -55.328 1.00 120.66 ? 163 SER G C   1 
ATOM   12641 O O   . SER G  1 163 ? 20.990  38.108   -54.118 1.00 116.64 ? 163 SER G O   1 
ATOM   12642 C CB  . SER G  1 163 ? 22.929  39.304   -56.093 1.00 123.38 ? 163 SER G CB  1 
ATOM   12643 O OG  . SER G  1 163 ? 23.767  38.211   -56.426 1.00 108.23 ? 163 SER G OG  1 
ATOM   12644 N N   . TYR G  1 164 ? 20.666  36.719   -55.859 1.00 100.63 ? 164 TYR G N   1 
ATOM   12645 C CA  . TYR G  1 164 ? 20.378  35.561   -55.030 1.00 94.01  ? 164 TYR G CA  1 
ATOM   12646 C C   . TYR G  1 164 ? 21.118  34.358   -55.588 1.00 88.88  ? 164 TYR G C   1 
ATOM   12647 O O   . TYR G  1 164 ? 20.561  33.580   -56.363 1.00 80.59  ? 164 TYR G O   1 
ATOM   12648 C CB  . TYR G  1 164 ? 18.880  35.281   -54.980 1.00 96.98  ? 164 TYR G CB  1 
ATOM   12649 C CG  . TYR G  1 164 ? 18.469  34.370   -53.849 1.00 95.32  ? 164 TYR G CG  1 
ATOM   12650 C CD1 . TYR G  1 164 ? 17.623  34.821   -52.845 1.00 93.21  ? 164 TYR G CD1 1 
ATOM   12651 C CD2 . TYR G  1 164 ? 18.936  33.065   -53.775 1.00 82.88  ? 164 TYR G CD2 1 
ATOM   12652 C CE1 . TYR G  1 164 ? 17.246  33.994   -51.806 1.00 89.15  ? 164 TYR G CE1 1 
ATOM   12653 C CE2 . TYR G  1 164 ? 18.568  32.232   -52.739 1.00 74.21  ? 164 TYR G CE2 1 
ATOM   12654 C CZ  . TYR G  1 164 ? 17.722  32.702   -51.757 1.00 83.47  ? 164 TYR G CZ  1 
ATOM   12655 O OH  . TYR G  1 164 ? 17.350  31.875   -50.723 1.00 77.97  ? 164 TYR G OH  1 
ATOM   12656 N N   . PRO G  1 165 ? 22.390  34.212   -55.199 1.00 74.58  ? 165 PRO G N   1 
ATOM   12657 C CA  . PRO G  1 165 ? 23.250  33.109   -55.632 1.00 87.60  ? 165 PRO G CA  1 
ATOM   12658 C C   . PRO G  1 165 ? 22.849  31.823   -54.927 1.00 89.03  ? 165 PRO G C   1 
ATOM   12659 O O   . PRO G  1 165 ? 22.345  31.880   -53.806 1.00 77.19  ? 165 PRO G O   1 
ATOM   12660 C CB  . PRO G  1 165 ? 24.644  33.543   -55.157 1.00 83.65  ? 165 PRO G CB  1 
ATOM   12661 C CG  . PRO G  1 165 ? 24.512  34.994   -54.766 1.00 96.20  ? 165 PRO G CG  1 
ATOM   12662 C CD  . PRO G  1 165 ? 23.103  35.149   -54.318 1.00 81.01  ? 165 PRO G CD  1 
ATOM   12663 N N   . LYS G  1 166 ? 23.065  30.682   -55.571 1.00 70.52  ? 166 LYS G N   1 
ATOM   12664 C CA  . LYS G  1 166 ? 22.804  29.401   -54.930 1.00 80.49  ? 166 LYS G CA  1 
ATOM   12665 C C   . LYS G  1 166 ? 23.490  29.344   -53.573 1.00 90.81  ? 166 LYS G C   1 
ATOM   12666 O O   . LYS G  1 166 ? 24.715  29.429   -53.485 1.00 87.76  ? 166 LYS G O   1 
ATOM   12667 C CB  . LYS G  1 166 ? 23.303  28.244   -55.797 1.00 76.94  ? 166 LYS G CB  1 
ATOM   12668 C CG  . LYS G  1 166 ? 23.473  26.945   -55.020 1.00 87.47  ? 166 LYS G CG  1 
ATOM   12669 C CD  . LYS G  1 166 ? 24.200  25.882   -55.828 1.00 103.53 ? 166 LYS G CD  1 
ATOM   12670 C CE  . LYS G  1 166 ? 23.307  25.286   -56.903 1.00 105.34 ? 166 LYS G CE  1 
ATOM   12671 N NZ  . LYS G  1 166 ? 23.959  24.128   -57.576 1.00 120.01 ? 166 LYS G NZ  1 
ATOM   12672 N N   . LEU G  1 167 ? 22.702  29.209   -52.512 1.00 82.05  ? 167 LEU G N   1 
ATOM   12673 C CA  . LEU G  1 167 ? 23.277  29.040   -51.184 1.00 85.64  ? 167 LEU G CA  1 
ATOM   12674 C C   . LEU G  1 167 ? 23.425  27.559   -50.862 1.00 90.73  ? 167 LEU G C   1 
ATOM   12675 O O   . LEU G  1 167 ? 22.697  26.723   -51.398 1.00 81.12  ? 167 LEU G O   1 
ATOM   12676 C CB  . LEU G  1 167 ? 22.452  29.766   -50.114 1.00 70.94  ? 167 LEU G CB  1 
ATOM   12677 C CG  . LEU G  1 167 ? 21.003  29.375   -49.799 1.00 76.25  ? 167 LEU G CG  1 
ATOM   12678 C CD1 . LEU G  1 167 ? 20.868  27.935   -49.315 1.00 73.51  ? 167 LEU G CD1 1 
ATOM   12679 C CD2 . LEU G  1 167 ? 20.430  30.339   -48.769 1.00 79.55  ? 167 LEU G CD2 1 
ATOM   12680 N N   . SER G  1 168 ? 24.376  27.237   -49.992 1.00 84.70  ? 168 SER G N   1 
ATOM   12681 C CA  . SER G  1 168 ? 24.630  25.848   -49.636 1.00 74.63  ? 168 SER G CA  1 
ATOM   12682 C C   . SER G  1 168 ? 25.232  25.726   -48.238 1.00 84.74  ? 168 SER G C   1 
ATOM   12683 O O   . SER G  1 168 ? 26.447  25.603   -48.080 1.00 109.63 ? 168 SER G O   1 
ATOM   12684 C CB  . SER G  1 168 ? 25.544  25.191   -50.673 1.00 88.24  ? 168 SER G CB  1 
ATOM   12685 O OG  . SER G  1 168 ? 25.420  23.780   -50.643 1.00 97.27  ? 168 SER G OG  1 
ATOM   12686 N N   . LYS G  1 169 ? 24.368  25.768   -47.230 1.00 79.49  ? 169 LYS G N   1 
ATOM   12687 C CA  . LYS G  1 169 ? 24.782  25.587   -45.845 1.00 81.39  ? 169 LYS G CA  1 
ATOM   12688 C C   . LYS G  1 169 ? 24.415  24.184   -45.380 1.00 80.73  ? 169 LYS G C   1 
ATOM   12689 O O   . LYS G  1 169 ? 23.453  23.594   -45.870 1.00 72.68  ? 169 LYS G O   1 
ATOM   12690 C CB  . LYS G  1 169 ? 24.106  26.625   -44.946 1.00 74.15  ? 169 LYS G CB  1 
ATOM   12691 C CG  . LYS G  1 169 ? 25.023  27.731   -44.446 1.00 90.51  ? 169 LYS G CG  1 
ATOM   12692 C CD  . LYS G  1 169 ? 25.999  27.215   -43.399 1.00 98.42  ? 169 LYS G CD  1 
ATOM   12693 C CE  . LYS G  1 169 ? 26.696  28.360   -42.680 1.00 102.30 ? 169 LYS G CE  1 
ATOM   12694 N NZ  . LYS G  1 169 ? 27.448  29.239   -43.618 1.00 108.16 ? 169 LYS G NZ  1 
ATOM   12695 N N   . SER G  1 170 ? 25.184  23.651   -44.438 1.00 87.27  ? 170 SER G N   1 
ATOM   12696 C CA  . SER G  1 170 ? 24.897  22.336   -43.877 1.00 77.61  ? 170 SER G CA  1 
ATOM   12697 C C   . SER G  1 170 ? 25.440  22.206   -42.458 1.00 74.10  ? 170 SER G C   1 
ATOM   12698 O O   . SER G  1 170 ? 26.620  22.451   -42.206 1.00 82.45  ? 170 SER G O   1 
ATOM   12699 C CB  . SER G  1 170 ? 25.456  21.227   -44.773 1.00 76.33  ? 170 SER G CB  1 
ATOM   12700 O OG  . SER G  1 170 ? 26.847  21.392   -44.987 1.00 115.63 ? 170 SER G OG  1 
ATOM   12701 N N   . TYR G  1 171 ? 24.563  21.824   -41.536 1.00 74.44  ? 171 TYR G N   1 
ATOM   12702 C CA  . TYR G  1 171 ? 24.928  21.676   -40.133 1.00 74.08  ? 171 TYR G CA  1 
ATOM   12703 C C   . TYR G  1 171 ? 25.027  20.206   -39.743 1.00 72.66  ? 171 TYR G C   1 
ATOM   12704 O O   . TYR G  1 171 ? 24.242  19.379   -40.204 1.00 61.90  ? 171 TYR G O   1 
ATOM   12705 C CB  . TYR G  1 171 ? 23.906  22.392   -39.246 1.00 75.26  ? 171 TYR G CB  1 
ATOM   12706 C CG  . TYR G  1 171 ? 23.869  21.898   -37.817 1.00 73.92  ? 171 TYR G CG  1 
ATOM   12707 C CD1 . TYR G  1 171 ? 24.685  22.460   -36.843 1.00 70.11  ? 171 TYR G CD1 1 
ATOM   12708 C CD2 . TYR G  1 171 ? 23.011  20.872   -37.439 1.00 79.03  ? 171 TYR G CD2 1 
ATOM   12709 C CE1 . TYR G  1 171 ? 24.651  22.010   -35.535 1.00 76.84  ? 171 TYR G CE1 1 
ATOM   12710 C CE2 . TYR G  1 171 ? 22.971  20.416   -36.136 1.00 81.33  ? 171 TYR G CE2 1 
ATOM   12711 C CZ  . TYR G  1 171 ? 23.792  20.989   -35.187 1.00 82.17  ? 171 TYR G CZ  1 
ATOM   12712 O OH  . TYR G  1 171 ? 23.754  20.538   -33.887 1.00 84.93  ? 171 TYR G OH  1 
ATOM   12713 N N   . ILE G  1 172 ? 25.997  19.886   -38.893 1.00 72.16  ? 172 ILE G N   1 
ATOM   12714 C CA  . ILE G  1 172 ? 26.168  18.520   -38.412 1.00 75.72  ? 172 ILE G CA  1 
ATOM   12715 C C   . ILE G  1 172 ? 25.857  18.421   -36.920 1.00 77.41  ? 172 ILE G C   1 
ATOM   12716 O O   . ILE G  1 172 ? 26.339  19.222   -36.119 1.00 80.63  ? 172 ILE G O   1 
ATOM   12717 C CB  . ILE G  1 172 ? 27.587  17.985   -38.703 1.00 72.15  ? 172 ILE G CB  1 
ATOM   12718 C CG1 . ILE G  1 172 ? 27.698  16.514   -38.298 1.00 74.89  ? 172 ILE G CG1 1 
ATOM   12719 C CG2 . ILE G  1 172 ? 28.637  18.829   -37.996 1.00 90.19  ? 172 ILE G CG2 1 
ATOM   12720 C CD1 . ILE G  1 172 ? 28.303  15.633   -39.369 1.00 84.64  ? 172 ILE G CD1 1 
ATOM   12721 N N   . ASN G  1 173 ? 25.040  17.438   -36.557 1.00 77.32  ? 173 ASN G N   1 
ATOM   12722 C CA  . ASN G  1 173 ? 24.598  17.271   -35.178 1.00 75.45  ? 173 ASN G CA  1 
ATOM   12723 C C   . ASN G  1 173 ? 25.725  16.836   -34.246 1.00 85.06  ? 173 ASN G C   1 
ATOM   12724 O O   . ASN G  1 173 ? 26.039  15.650   -34.145 1.00 77.31  ? 173 ASN G O   1 
ATOM   12725 C CB  . ASN G  1 173 ? 23.439  16.273   -35.107 1.00 70.36  ? 173 ASN G CB  1 
ATOM   12726 C CG  . ASN G  1 173 ? 22.766  16.254   -33.749 1.00 79.73  ? 173 ASN G CG  1 
ATOM   12727 O OD1 . ASN G  1 173 ? 23.184  16.953   -32.827 1.00 83.30  ? 173 ASN G OD1 1 
ATOM   12728 N ND2 . ASN G  1 173 ? 21.715  15.454   -33.621 1.00 77.56  ? 173 ASN G ND2 1 
ATOM   12729 N N   . ASP G  1 174 ? 26.328  17.806   -33.566 1.00 94.78  ? 174 ASP G N   1 
ATOM   12730 C CA  . ASP G  1 174 ? 27.412  17.528   -32.632 1.00 91.88  ? 174 ASP G CA  1 
ATOM   12731 C C   . ASP G  1 174 ? 26.877  17.277   -31.226 1.00 95.26  ? 174 ASP G C   1 
ATOM   12732 O O   . ASP G  1 174 ? 27.638  16.986   -30.304 1.00 111.48 ? 174 ASP G O   1 
ATOM   12733 C CB  . ASP G  1 174 ? 28.417  18.681   -32.617 1.00 102.53 ? 174 ASP G CB  1 
ATOM   12734 C CG  . ASP G  1 174 ? 27.770  20.013   -32.296 1.00 116.35 ? 174 ASP G CG  1 
ATOM   12735 O OD1 . ASP G  1 174 ? 27.837  20.443   -31.125 1.00 124.98 ? 174 ASP G OD1 1 
ATOM   12736 O OD2 . ASP G  1 174 ? 27.193  20.631   -33.215 1.00 111.67 ? 174 ASP G OD2 1 
ATOM   12737 N N   . LYS G  1 175 ? 25.562  17.393   -31.071 1.00 83.82  ? 175 LYS G N   1 
ATOM   12738 C CA  . LYS G  1 175 ? 24.913  17.128   -29.793 1.00 84.97  ? 175 LYS G CA  1 
ATOM   12739 C C   . LYS G  1 175 ? 24.871  15.625   -29.529 1.00 89.28  ? 175 LYS G C   1 
ATOM   12740 O O   . LYS G  1 175 ? 25.202  14.824   -30.403 1.00 91.46  ? 175 LYS G O   1 
ATOM   12741 C CB  . LYS G  1 175 ? 23.493  17.700   -29.787 1.00 84.35  ? 175 LYS G CB  1 
ATOM   12742 C CG  . LYS G  1 175 ? 23.394  19.167   -30.194 1.00 84.89  ? 175 LYS G CG  1 
ATOM   12743 C CD  . LYS G  1 175 ? 23.957  20.095   -29.128 1.00 78.03  ? 175 LYS G CD  1 
ATOM   12744 C CE  . LYS G  1 175 ? 23.722  21.555   -29.493 1.00 76.06  ? 175 LYS G CE  1 
ATOM   12745 N NZ  . LYS G  1 175 ? 24.187  22.489   -28.430 1.00 97.34  ? 175 LYS G NZ  1 
ATOM   12746 N N   . GLY G  1 176 ? 24.469  15.246   -28.320 1.00 71.94  ? 176 GLY G N   1 
ATOM   12747 C CA  . GLY G  1 176 ? 24.328  13.843   -27.972 1.00 95.51  ? 176 GLY G CA  1 
ATOM   12748 C C   . GLY G  1 176 ? 22.869  13.436   -27.975 1.00 90.20  ? 176 GLY G C   1 
ATOM   12749 O O   . GLY G  1 176 ? 22.483  12.433   -27.375 1.00 94.52  ? 176 GLY G O   1 
ATOM   12750 N N   . LYS G  1 177 ? 22.059  14.229   -28.666 1.00 88.47  ? 177 LYS G N   1 
ATOM   12751 C CA  . LYS G  1 177 ? 20.620  14.029   -28.707 1.00 79.58  ? 177 LYS G CA  1 
ATOM   12752 C C   . LYS G  1 177 ? 20.088  14.510   -30.051 1.00 71.69  ? 177 LYS G C   1 
ATOM   12753 O O   . LYS G  1 177 ? 20.741  15.300   -30.732 1.00 75.06  ? 177 LYS G O   1 
ATOM   12754 C CB  . LYS G  1 177 ? 19.960  14.805   -27.567 1.00 79.85  ? 177 LYS G CB  1 
ATOM   12755 C CG  . LYS G  1 177 ? 20.309  16.287   -27.552 1.00 71.93  ? 177 LYS G CG  1 
ATOM   12756 C CD  . LYS G  1 177 ? 19.757  16.987   -26.319 1.00 76.88  ? 177 LYS G CD  1 
ATOM   12757 C CE  . LYS G  1 177 ? 20.429  16.491   -25.048 1.00 90.07  ? 177 LYS G CE  1 
ATOM   12758 N NZ  . LYS G  1 177 ? 21.893  16.763   -25.042 1.00 93.91  ? 177 LYS G NZ  1 
ATOM   12759 N N   . GLU G  1 178 ? 18.909  14.032   -30.436 1.00 69.59  ? 178 GLU G N   1 
ATOM   12760 C CA  . GLU G  1 178 ? 18.300  14.454   -31.691 1.00 68.38  ? 178 GLU G CA  1 
ATOM   12761 C C   . GLU G  1 178 ? 18.149  15.969   -31.733 1.00 72.72  ? 178 GLU G C   1 
ATOM   12762 O O   . GLU G  1 178 ? 18.041  16.625   -30.697 1.00 71.65  ? 178 GLU G O   1 
ATOM   12763 C CB  . GLU G  1 178 ? 16.934  13.798   -31.881 1.00 69.48  ? 178 GLU G CB  1 
ATOM   12764 C CG  . GLU G  1 178 ? 16.965  12.284   -31.946 1.00 86.78  ? 178 GLU G CG  1 
ATOM   12765 C CD  . GLU G  1 178 ? 15.573  11.689   -31.943 1.00 94.93  ? 178 GLU G CD  1 
ATOM   12766 O OE1 . GLU G  1 178 ? 14.742  12.139   -31.127 1.00 86.54  ? 178 GLU G OE1 1 
ATOM   12767 O OE2 . GLU G  1 178 ? 15.310  10.776   -32.753 1.00 106.93 ? 178 GLU G OE2 1 
ATOM   12768 N N   . VAL G  1 179 ? 18.136  16.514   -32.942 1.00 59.16  ? 179 VAL G N   1 
ATOM   12769 C CA  . VAL G  1 179 ? 18.011  17.949   -33.144 1.00 62.49  ? 179 VAL G CA  1 
ATOM   12770 C C   . VAL G  1 179 ? 16.817  18.240   -34.059 1.00 60.13  ? 179 VAL G C   1 
ATOM   12771 O O   . VAL G  1 179 ? 16.800  17.830   -35.219 1.00 53.06  ? 179 VAL G O   1 
ATOM   12772 C CB  . VAL G  1 179 ? 19.336  18.536   -33.710 1.00 60.25  ? 179 VAL G CB  1 
ATOM   12773 C CG1 . VAL G  1 179 ? 19.105  19.837   -34.469 1.00 62.82  ? 179 VAL G CG1 1 
ATOM   12774 C CG2 . VAL G  1 179 ? 20.359  18.724   -32.589 1.00 58.99  ? 179 VAL G CG2 1 
ATOM   12775 N N   . LEU G  1 180 ? 15.804  18.916   -33.519 1.00 56.88  ? 180 LEU G N   1 
ATOM   12776 C CA  . LEU G  1 180 ? 14.630  19.306   -34.299 1.00 52.97  ? 180 LEU G CA  1 
ATOM   12777 C C   . LEU G  1 180 ? 14.946  20.530   -35.147 1.00 50.84  ? 180 LEU G C   1 
ATOM   12778 O O   . LEU G  1 180 ? 15.140  21.626   -34.619 1.00 61.71  ? 180 LEU G O   1 
ATOM   12779 C CB  . LEU G  1 180 ? 13.440  19.611   -33.381 1.00 55.00  ? 180 LEU G CB  1 
ATOM   12780 C CG  . LEU G  1 180 ? 12.117  20.048   -34.024 1.00 52.09  ? 180 LEU G CG  1 
ATOM   12781 C CD1 . LEU G  1 180 ? 11.352  18.852   -34.584 1.00 52.63  ? 180 LEU G CD1 1 
ATOM   12782 C CD2 . LEU G  1 180 ? 11.254  20.808   -33.023 1.00 47.55  ? 180 LEU G CD2 1 
ATOM   12783 N N   . VAL G  1 181 ? 15.000  20.343   -36.460 1.00 53.72  ? 181 VAL G N   1 
ATOM   12784 C CA  . VAL G  1 181 ? 15.252  21.452   -37.370 1.00 53.07  ? 181 VAL G CA  1 
ATOM   12785 C C   . VAL G  1 181 ? 13.986  21.812   -38.137 1.00 57.16  ? 181 VAL G C   1 
ATOM   12786 O O   . VAL G  1 181 ? 13.364  20.955   -38.764 1.00 57.23  ? 181 VAL G O   1 
ATOM   12787 C CB  . VAL G  1 181 ? 16.370  21.121   -38.373 1.00 49.32  ? 181 VAL G CB  1 
ATOM   12788 C CG1 . VAL G  1 181 ? 16.733  22.358   -39.182 1.00 57.61  ? 181 VAL G CG1 1 
ATOM   12789 C CG2 . VAL G  1 181 ? 17.589  20.582   -37.646 1.00 53.82  ? 181 VAL G CG2 1 
ATOM   12790 N N   . LEU G  1 182 ? 13.604  23.082   -38.080 1.00 61.72  ? 182 LEU G N   1 
ATOM   12791 C CA  . LEU G  1 182 ? 12.443  23.557   -38.820 1.00 59.09  ? 182 LEU G CA  1 
ATOM   12792 C C   . LEU G  1 182 ? 12.860  24.535   -39.903 1.00 52.01  ? 182 LEU G C   1 
ATOM   12793 O O   . LEU G  1 182 ? 13.824  25.282   -39.742 1.00 52.94  ? 182 LEU G O   1 
ATOM   12794 C CB  . LEU G  1 182 ? 11.431  24.220   -37.886 1.00 45.58  ? 182 LEU G CB  1 
ATOM   12795 C CG  . LEU G  1 182 ? 10.766  23.314   -36.852 1.00 54.55  ? 182 LEU G CG  1 
ATOM   12796 C CD1 . LEU G  1 182 ? 11.267  23.652   -35.459 1.00 62.98  ? 182 LEU G CD1 1 
ATOM   12797 C CD2 . LEU G  1 182 ? 9.252   23.439   -36.928 1.00 51.32  ? 182 LEU G CD2 1 
ATOM   12798 N N   . TRP G  1 183 ? 12.125  24.528   -41.007 1.00 50.73  ? 183 TRP G N   1 
ATOM   12799 C CA  . TRP G  1 183 ? 12.404  25.433   -42.108 1.00 49.28  ? 183 TRP G CA  1 
ATOM   12800 C C   . TRP G  1 183 ? 11.127  25.667   -42.906 1.00 55.67  ? 183 TRP G C   1 
ATOM   12801 O O   . TRP G  1 183 ? 10.133  24.967   -42.715 1.00 56.44  ? 183 TRP G O   1 
ATOM   12802 C CB  . TRP G  1 183 ? 13.509  24.862   -42.996 1.00 58.96  ? 183 TRP G CB  1 
ATOM   12803 C CG  . TRP G  1 183 ? 13.076  23.689   -43.808 1.00 49.48  ? 183 TRP G CG  1 
ATOM   12804 C CD1 . TRP G  1 183 ? 12.518  23.722   -45.049 1.00 53.28  ? 183 TRP G CD1 1 
ATOM   12805 C CD2 . TRP G  1 183 ? 13.163  22.304   -43.443 1.00 57.49  ? 183 TRP G CD2 1 
ATOM   12806 N NE1 . TRP G  1 183 ? 12.249  22.449   -45.482 1.00 49.78  ? 183 TRP G NE1 1 
ATOM   12807 C CE2 . TRP G  1 183 ? 12.637  21.559   -44.516 1.00 55.87  ? 183 TRP G CE2 1 
ATOM   12808 C CE3 . TRP G  1 183 ? 13.633  21.623   -42.316 1.00 59.90  ? 183 TRP G CE3 1 
ATOM   12809 C CZ2 . TRP G  1 183 ? 12.567  20.171   -44.498 1.00 56.46  ? 183 TRP G CZ2 1 
ATOM   12810 C CZ3 . TRP G  1 183 ? 13.562  20.241   -42.301 1.00 54.86  ? 183 TRP G CZ3 1 
ATOM   12811 C CH2 . TRP G  1 183 ? 13.033  19.530   -43.385 1.00 53.03  ? 183 TRP G CH2 1 
ATOM   12812 N N   . GLY G  1 184 ? 11.148  26.656   -43.793 1.00 53.36  ? 184 GLY G N   1 
ATOM   12813 C CA  . GLY G  1 184 ? 9.962   27.002   -44.552 1.00 40.06  ? 184 GLY G CA  1 
ATOM   12814 C C   . GLY G  1 184 ? 10.211  27.203   -46.033 1.00 50.93  ? 184 GLY G C   1 
ATOM   12815 O O   . GLY G  1 184 ? 11.296  27.613   -46.444 1.00 56.41  ? 184 GLY G O   1 
ATOM   12816 N N   . ILE G  1 185 ? 9.195   26.903   -46.836 1.00 43.51  ? 185 ILE G N   1 
ATOM   12817 C CA  . ILE G  1 185 ? 9.242   27.153   -48.270 1.00 45.07  ? 185 ILE G CA  1 
ATOM   12818 C C   . ILE G  1 185 ? 8.205   28.195   -48.638 1.00 57.74  ? 185 ILE G C   1 
ATOM   12819 O O   . ILE G  1 185 ? 7.004   27.954   -48.522 1.00 56.69  ? 185 ILE G O   1 
ATOM   12820 C CB  . ILE G  1 185 ? 8.968   25.883   -49.079 1.00 49.34  ? 185 ILE G CB  1 
ATOM   12821 C CG1 . ILE G  1 185 ? 10.007  24.832   -48.739 1.00 54.33  ? 185 ILE G CG1 1 
ATOM   12822 C CG2 . ILE G  1 185 ? 9.066   26.176   -50.564 1.00 44.74  ? 185 ILE G CG2 1 
ATOM   12823 C CD1 . ILE G  1 185 ? 11.400  25.297   -49.073 1.00 50.84  ? 185 ILE G CD1 1 
ATOM   12824 N N   . HIS G  1 186 ? 8.669   29.358   -49.076 1.00 62.50  ? 186 HIS G N   1 
ATOM   12825 C CA  . HIS G  1 186 ? 7.759   30.438   -49.417 1.00 60.32  ? 186 HIS G CA  1 
ATOM   12826 C C   . HIS G  1 186 ? 7.273   30.336   -50.858 1.00 51.21  ? 186 HIS G C   1 
ATOM   12827 O O   . HIS G  1 186 ? 8.064   30.148   -51.782 1.00 55.77  ? 186 HIS G O   1 
ATOM   12828 C CB  . HIS G  1 186 ? 8.406   31.799   -49.166 1.00 64.28  ? 186 HIS G CB  1 
ATOM   12829 C CG  . HIS G  1 186 ? 7.544   32.953   -49.570 1.00 70.05  ? 186 HIS G CG  1 
ATOM   12830 N ND1 . HIS G  1 186 ? 7.841   33.763   -50.644 1.00 67.68  ? 186 HIS G ND1 1 
ATOM   12831 C CD2 . HIS G  1 186 ? 6.382   33.418   -49.057 1.00 71.19  ? 186 HIS G CD2 1 
ATOM   12832 C CE1 . HIS G  1 186 ? 6.904   34.686   -50.768 1.00 70.12  ? 186 HIS G CE1 1 
ATOM   12833 N NE2 . HIS G  1 186 ? 6.005   34.498   -49.817 1.00 65.39  ? 186 HIS G NE2 1 
ATOM   12834 N N   . HIS G  1 187 ? 5.962   30.453   -51.035 1.00 61.52  ? 187 HIS G N   1 
ATOM   12835 C CA  . HIS G  1 187 ? 5.360   30.444   -52.360 1.00 60.76  ? 187 HIS G CA  1 
ATOM   12836 C C   . HIS G  1 187 ? 4.717   31.798   -52.637 1.00 71.20  ? 187 HIS G C   1 
ATOM   12837 O O   . HIS G  1 187 ? 3.596   32.057   -52.201 1.00 73.01  ? 187 HIS G O   1 
ATOM   12838 C CB  . HIS G  1 187 ? 4.316   29.331   -52.466 1.00 58.75  ? 187 HIS G CB  1 
ATOM   12839 C CG  . HIS G  1 187 ? 4.843   27.973   -52.127 1.00 66.51  ? 187 HIS G CG  1 
ATOM   12840 N ND1 . HIS G  1 187 ? 5.447   27.153   -53.056 1.00 64.86  ? 187 HIS G ND1 1 
ATOM   12841 C CD2 . HIS G  1 187 ? 4.858   27.287   -50.958 1.00 65.04  ? 187 HIS G CD2 1 
ATOM   12842 C CE1 . HIS G  1 187 ? 5.810   26.024   -52.476 1.00 69.16  ? 187 HIS G CE1 1 
ATOM   12843 N NE2 . HIS G  1 187 ? 5.464   26.079   -51.203 1.00 69.97  ? 187 HIS G NE2 1 
ATOM   12844 N N   . PRO G  1 188 ? 5.435   32.671   -53.358 1.00 65.44  ? 188 PRO G N   1 
ATOM   12845 C CA  . PRO G  1 188 ? 4.952   34.020   -53.671 1.00 70.84  ? 188 PRO G CA  1 
ATOM   12846 C C   . PRO G  1 188 ? 3.622   33.994   -54.413 1.00 74.43  ? 188 PRO G C   1 
ATOM   12847 O O   . PRO G  1 188 ? 3.264   32.978   -55.009 1.00 64.98  ? 188 PRO G O   1 
ATOM   12848 C CB  . PRO G  1 188 ? 6.051   34.581   -54.577 1.00 73.64  ? 188 PRO G CB  1 
ATOM   12849 C CG  . PRO G  1 188 ? 7.273   33.820   -54.194 1.00 69.79  ? 188 PRO G CG  1 
ATOM   12850 C CD  . PRO G  1 188 ? 6.790   32.436   -53.884 1.00 63.97  ? 188 PRO G CD  1 
ATOM   12851 N N   . SER G  1 189 ? 2.902   35.110   -54.375 1.00 82.92  ? 189 SER G N   1 
ATOM   12852 C CA  . SER G  1 189 ? 1.592   35.200   -55.007 1.00 78.19  ? 189 SER G CA  1 
ATOM   12853 C C   . SER G  1 189 ? 1.708   35.448   -56.510 1.00 69.42  ? 189 SER G C   1 
ATOM   12854 O O   . SER G  1 189 ? 0.950   34.887   -57.301 1.00 66.65  ? 189 SER G O   1 
ATOM   12855 C CB  . SER G  1 189 ? 0.756   36.297   -54.343 1.00 74.80  ? 189 SER G CB  1 
ATOM   12856 O OG  . SER G  1 189 ? 1.415   37.550   -54.408 1.00 90.33  ? 189 SER G OG  1 
ATOM   12857 N N   . THR G  1 190 ? 2.667   36.282   -56.899 1.00 84.24  ? 190 THR G N   1 
ATOM   12858 C CA  . THR G  1 190 ? 2.847   36.640   -58.303 1.00 86.22  ? 190 THR G CA  1 
ATOM   12859 C C   . THR G  1 190 ? 4.293   36.474   -58.770 1.00 84.51  ? 190 THR G C   1 
ATOM   12860 O O   . THR G  1 190 ? 5.225   36.549   -57.970 1.00 83.29  ? 190 THR G O   1 
ATOM   12861 C CB  . THR G  1 190 ? 2.378   38.085   -58.577 1.00 85.08  ? 190 THR G CB  1 
ATOM   12862 O OG1 . THR G  1 190 ? 3.151   38.644   -59.646 1.00 109.89 ? 190 THR G OG1 1 
ATOM   12863 C CG2 . THR G  1 190 ? 2.548   38.947   -57.333 1.00 80.52  ? 190 THR G CG2 1 
ATOM   12864 N N   . SER G  1 191 ? 4.472   36.247   -60.070 1.00 96.35  ? 191 SER G N   1 
ATOM   12865 C CA  . SER G  1 191 ? 5.805   36.097   -60.646 1.00 97.21  ? 191 SER G CA  1 
ATOM   12866 C C   . SER G  1 191 ? 6.621   37.373   -60.468 1.00 88.02  ? 191 SER G C   1 
ATOM   12867 O O   . SER G  1 191 ? 7.851   37.341   -60.463 1.00 87.24  ? 191 SER G O   1 
ATOM   12868 C CB  . SER G  1 191 ? 5.722   35.721   -62.129 1.00 83.87  ? 191 SER G CB  1 
ATOM   12869 O OG  . SER G  1 191 ? 5.096   36.742   -62.888 1.00 97.92  ? 191 SER G OG  1 
ATOM   12870 N N   . ALA G  1 192 ? 5.923   38.496   -60.325 1.00 97.17  ? 192 ALA G N   1 
ATOM   12871 C CA  . ALA G  1 192 ? 6.571   39.771   -60.049 1.00 98.49  ? 192 ALA G CA  1 
ATOM   12872 C C   . ALA G  1 192 ? 7.109   39.781   -58.623 1.00 99.12  ? 192 ALA G C   1 
ATOM   12873 O O   . ALA G  1 192 ? 8.198   40.290   -58.364 1.00 90.77  ? 192 ALA G O   1 
ATOM   12874 C CB  . ALA G  1 192 ? 5.598   40.919   -60.261 1.00 102.04 ? 192 ALA G CB  1 
ATOM   12875 N N   . ASP G  1 193 ? 6.336   39.213   -57.702 1.00 98.64  ? 193 ASP G N   1 
ATOM   12876 C CA  . ASP G  1 193 ? 6.769   39.077   -56.316 1.00 97.83  ? 193 ASP G CA  1 
ATOM   12877 C C   . ASP G  1 193 ? 7.937   38.107   -56.211 1.00 87.73  ? 193 ASP G C   1 
ATOM   12878 O O   . ASP G  1 193 ? 8.798   38.247   -55.342 1.00 72.85  ? 193 ASP G O   1 
ATOM   12879 C CB  . ASP G  1 193 ? 5.617   38.600   -55.430 1.00 91.69  ? 193 ASP G CB  1 
ATOM   12880 C CG  . ASP G  1 193 ? 4.935   39.737   -54.695 1.00 116.35 ? 193 ASP G CG  1 
ATOM   12881 O OD1 . ASP G  1 193 ? 4.687   40.790   -55.320 1.00 125.78 ? 193 ASP G OD1 1 
ATOM   12882 O OD2 . ASP G  1 193 ? 4.645   39.577   -53.491 1.00 134.06 ? 193 ASP G OD2 1 
ATOM   12883 N N   . GLN G  1 194 ? 7.959   37.120   -57.100 1.00 81.90  ? 194 GLN G N   1 
ATOM   12884 C CA  . GLN G  1 194 ? 9.029   36.131   -57.119 1.00 77.13  ? 194 GLN G CA  1 
ATOM   12885 C C   . GLN G  1 194 ? 10.380  36.784   -57.387 1.00 90.74  ? 194 GLN G C   1 
ATOM   12886 O O   . GLN G  1 194 ? 11.294  36.696   -56.567 1.00 89.64  ? 194 GLN G O   1 
ATOM   12887 C CB  . GLN G  1 194 ? 8.743   35.053   -58.167 1.00 82.30  ? 194 GLN G CB  1 
ATOM   12888 C CG  . GLN G  1 194 ? 9.904   34.104   -58.431 1.00 81.77  ? 194 GLN G CG  1 
ATOM   12889 C CD  . GLN G  1 194 ? 10.192  33.175   -57.266 1.00 81.00  ? 194 GLN G CD  1 
ATOM   12890 O OE1 . GLN G  1 194 ? 11.245  32.540   -57.212 1.00 90.05  ? 194 GLN G OE1 1 
ATOM   12891 N NE2 . GLN G  1 194 ? 9.256   33.088   -56.329 1.00 73.41  ? 194 GLN G NE2 1 
ATOM   12892 N N   . GLN G  1 195 ? 10.500  37.441   -58.536 1.00 109.34 ? 195 GLN G N   1 
ATOM   12893 C CA  . GLN G  1 195 ? 11.749  38.093   -58.916 1.00 120.80 ? 195 GLN G CA  1 
ATOM   12894 C C   . GLN G  1 195 ? 12.074  39.274   -58.002 1.00 112.53 ? 195 GLN G C   1 
ATOM   12895 O O   . GLN G  1 195 ? 13.232  39.666   -57.870 1.00 111.18 ? 195 GLN G O   1 
ATOM   12896 C CB  . GLN G  1 195 ? 11.707  38.533   -60.383 1.00 118.37 ? 195 GLN G CB  1 
ATOM   12897 C CG  . GLN G  1 195 ? 10.525  39.416   -60.743 1.00 143.86 ? 195 GLN G CG  1 
ATOM   12898 C CD  . GLN G  1 195 ? 10.421  39.664   -62.236 1.00 162.62 ? 195 GLN G CD  1 
ATOM   12899 O OE1 . GLN G  1 195 ? 9.520   40.362   -62.701 1.00 158.87 ? 195 GLN G OE1 1 
ATOM   12900 N NE2 . GLN G  1 195 ? 11.345  39.087   -62.996 1.00 165.53 ? 195 GLN G NE2 1 
ATOM   12901 N N   . SER G  1 196 ? 11.047  39.829   -57.366 1.00 91.57  ? 196 SER G N   1 
ATOM   12902 C CA  . SER G  1 196 ? 11.224  40.943   -56.437 1.00 82.22  ? 196 SER G CA  1 
ATOM   12903 C C   . SER G  1 196 ? 11.928  40.516   -55.149 1.00 97.14  ? 196 SER G C   1 
ATOM   12904 O O   . SER G  1 196 ? 12.716  41.269   -54.574 1.00 95.46  ? 196 SER G O   1 
ATOM   12905 C CB  . SER G  1 196 ? 9.868   41.558   -56.092 1.00 84.26  ? 196 SER G CB  1 
ATOM   12906 O OG  . SER G  1 196 ? 9.995   42.523   -55.064 1.00 104.85 ? 196 SER G OG  1 
ATOM   12907 N N   . LEU G  1 197 ? 11.618  39.303   -54.705 1.00 103.06 ? 197 LEU G N   1 
ATOM   12908 C CA  . LEU G  1 197 ? 12.119  38.753   -53.453 1.00 90.49  ? 197 LEU G CA  1 
ATOM   12909 C C   . LEU G  1 197 ? 13.370  37.947   -53.719 1.00 83.20  ? 197 LEU G C   1 
ATOM   12910 O O   . LEU G  1 197 ? 14.417  38.168   -53.123 1.00 80.13  ? 197 LEU G O   1 
ATOM   12911 C CB  . LEU G  1 197 ? 11.062  37.836   -52.856 1.00 85.48  ? 197 LEU G CB  1 
ATOM   12912 C CG  . LEU G  1 197 ? 9.958   38.515   -52.065 1.00 71.48  ? 197 LEU G CG  1 
ATOM   12913 C CD1 . LEU G  1 197 ? 8.891   37.497   -51.743 1.00 78.25  ? 197 LEU G CD1 1 
ATOM   12914 C CD2 . LEU G  1 197 ? 10.568  39.095   -50.809 1.00 75.56  ? 197 LEU G CD2 1 
ATOM   12915 N N   . TYR G  1 198 ? 13.227  36.989   -54.623 1.00 80.82  ? 198 TYR G N   1 
ATOM   12916 C CA  . TYR G  1 198 ? 14.345  36.223   -55.148 1.00 91.25  ? 198 TYR G CA  1 
ATOM   12917 C C   . TYR G  1 198 ? 14.308  36.495   -56.650 1.00 100.77 ? 198 TYR G C   1 
ATOM   12918 O O   . TYR G  1 198 ? 13.398  36.086   -57.373 1.00 108.17 ? 198 TYR G O   1 
ATOM   12919 C CB  . TYR G  1 198 ? 14.228  34.757   -54.744 1.00 95.40  ? 198 TYR G CB  1 
ATOM   12920 C CG  . TYR G  1 198 ? 13.259  34.577   -53.616 1.00 82.76  ? 198 TYR G CG  1 
ATOM   12921 C CD1 . TYR G  1 198 ? 11.921  34.345   -53.875 1.00 74.96  ? 198 TYR G CD1 1 
ATOM   12922 C CD2 . TYR G  1 198 ? 13.665  34.698   -52.296 1.00 84.61  ? 198 TYR G CD2 1 
ATOM   12923 C CE1 . TYR G  1 198 ? 11.013  34.202   -52.857 1.00 75.05  ? 198 TYR G CE1 1 
ATOM   12924 C CE2 . TYR G  1 198 ? 12.762  34.555   -51.260 1.00 78.67  ? 198 TYR G CE2 1 
ATOM   12925 C CZ  . TYR G  1 198 ? 11.432  34.307   -51.548 1.00 74.20  ? 198 TYR G CZ  1 
ATOM   12926 O OH  . TYR G  1 198 ? 10.517  34.162   -50.528 1.00 64.97  ? 198 TYR G OH  1 
ATOM   12927 N N   . GLN G  1 199 ? 15.323  37.218   -57.096 1.00 100.52 ? 199 GLN G N   1 
ATOM   12928 C CA  . GLN G  1 199 ? 15.503  37.569   -58.495 1.00 108.36 ? 199 GLN G CA  1 
ATOM   12929 C C   . GLN G  1 199 ? 15.043  36.450   -59.445 1.00 102.70 ? 199 GLN G C   1 
ATOM   12930 O O   . GLN G  1 199 ? 14.110  36.625   -60.232 1.00 96.30  ? 199 GLN G O   1 
ATOM   12931 C CB  . GLN G  1 199 ? 16.992  37.843   -58.710 1.00 117.98 ? 199 GLN G CB  1 
ATOM   12932 C CG  . GLN G  1 199 ? 17.368  39.300   -58.993 1.00 133.00 ? 199 GLN G CG  1 
ATOM   12933 C CD  . GLN G  1 199 ? 16.826  39.782   -60.318 1.00 135.66 ? 199 GLN G CD  1 
ATOM   12934 O OE1 . GLN G  1 199 ? 17.025  39.147   -61.355 1.00 134.41 ? 199 GLN G OE1 1 
ATOM   12935 N NE2 . GLN G  1 199 ? 16.143  40.915   -60.295 1.00 120.33 ? 199 GLN G NE2 1 
ATOM   12936 N N   . ASN G  1 200 ? 15.698  35.298   -59.361 1.00 113.04 ? 200 ASN G N   1 
ATOM   12937 C CA  . ASN G  1 200 ? 15.459  34.203   -60.296 1.00 108.59 ? 200 ASN G CA  1 
ATOM   12938 C C   . ASN G  1 200 ? 13.983  33.813   -60.410 1.00 105.74 ? 200 ASN G C   1 
ATOM   12939 O O   . ASN G  1 200 ? 13.230  33.883   -59.436 1.00 107.23 ? 200 ASN G O   1 
ATOM   12940 C CB  . ASN G  1 200 ? 16.310  32.996   -59.910 1.00 105.83 ? 200 ASN G CB  1 
ATOM   12941 C CG  . ASN G  1 200 ? 17.678  33.396   -59.384 1.00 103.39 ? 200 ASN G CG  1 
ATOM   12942 O OD1 . ASN G  1 200 ? 18.132  34.523   -59.588 1.00 118.89 ? 200 ASN G OD1 1 
ATOM   12943 N ND2 . ASN G  1 200 ? 18.340  32.472   -58.700 1.00 104.01 ? 200 ASN G ND2 1 
ATOM   12944 N N   . ALA G  1 201 ? 13.576  33.404   -61.607 1.00 91.33  ? 201 ALA G N   1 
ATOM   12945 C CA  . ALA G  1 201 ? 12.186  33.035   -61.860 1.00 90.41  ? 201 ALA G CA  1 
ATOM   12946 C C   . ALA G  1 201 ? 11.945  31.549   -61.618 1.00 106.69 ? 201 ALA G C   1 
ATOM   12947 O O   . ALA G  1 201 ? 10.932  31.163   -61.035 1.00 106.56 ? 201 ALA G O   1 
ATOM   12948 C CB  . ALA G  1 201 ? 11.783  33.419   -63.278 1.00 96.05  ? 201 ALA G CB  1 
ATOM   12949 N N   . ASP G  1 202 ? 12.880  30.720   -62.069 1.00 110.88 ? 202 ASP G N   1 
ATOM   12950 C CA  . ASP G  1 202 ? 12.773  29.278   -61.892 1.00 103.14 ? 202 ASP G CA  1 
ATOM   12951 C C   . ASP G  1 202 ? 13.752  28.815   -60.820 1.00 99.82  ? 202 ASP G C   1 
ATOM   12952 O O   . ASP G  1 202 ? 14.931  28.592   -61.096 1.00 104.21 ? 202 ASP G O   1 
ATOM   12953 C CB  . ASP G  1 202 ? 13.050  28.556   -63.211 1.00 114.78 ? 202 ASP G CB  1 
ATOM   12954 C CG  . ASP G  1 202 ? 12.498  27.144   -63.230 1.00 120.84 ? 202 ASP G CG  1 
ATOM   12955 O OD1 . ASP G  1 202 ? 11.349  26.949   -62.782 1.00 119.90 ? 202 ASP G OD1 1 
ATOM   12956 O OD2 . ASP G  1 202 ? 13.210  26.233   -63.701 1.00 123.85 ? 202 ASP G OD2 1 
ATOM   12957 N N   . THR G  1 203 ? 13.258  28.675   -59.594 1.00 87.78  ? 203 THR G N   1 
ATOM   12958 C CA  . THR G  1 203 ? 14.113  28.343   -58.461 1.00 80.07  ? 203 THR G CA  1 
ATOM   12959 C C   . THR G  1 203 ? 13.769  26.990   -57.853 1.00 73.57  ? 203 THR G C   1 
ATOM   12960 O O   . THR G  1 203 ? 12.773  26.366   -58.217 1.00 80.82  ? 203 THR G O   1 
ATOM   12961 C CB  . THR G  1 203 ? 14.007  29.407   -57.357 1.00 82.87  ? 203 THR G CB  1 
ATOM   12962 O OG1 . THR G  1 203 ? 12.662  29.451   -56.865 1.00 68.94  ? 203 THR G OG1 1 
ATOM   12963 C CG2 . THR G  1 203 ? 14.391  30.775   -57.897 1.00 80.11  ? 203 THR G CG2 1 
ATOM   12964 N N   . TYR G  1 204 ? 14.601  26.543   -56.918 1.00 75.36  ? 204 TYR G N   1 
ATOM   12965 C CA  . TYR G  1 204 ? 14.355  25.290   -56.220 1.00 66.32  ? 204 TYR G CA  1 
ATOM   12966 C C   . TYR G  1 204 ? 14.971  25.301   -54.827 1.00 70.46  ? 204 TYR G C   1 
ATOM   12967 O O   . TYR G  1 204 ? 15.954  25.998   -54.576 1.00 71.76  ? 204 TYR G O   1 
ATOM   12968 C CB  . TYR G  1 204 ? 14.907  24.108   -57.020 1.00 65.11  ? 204 TYR G CB  1 
ATOM   12969 C CG  . TYR G  1 204 ? 16.415  23.982   -56.979 1.00 75.76  ? 204 TYR G CG  1 
ATOM   12970 C CD1 . TYR G  1 204 ? 17.041  23.193   -56.022 1.00 77.05  ? 204 TYR G CD1 1 
ATOM   12971 C CD2 . TYR G  1 204 ? 17.213  24.649   -57.900 1.00 82.73  ? 204 TYR G CD2 1 
ATOM   12972 C CE1 . TYR G  1 204 ? 18.417  23.073   -55.982 1.00 85.06  ? 204 TYR G CE1 1 
ATOM   12973 C CE2 . TYR G  1 204 ? 18.591  24.535   -57.867 1.00 85.42  ? 204 TYR G CE2 1 
ATOM   12974 C CZ  . TYR G  1 204 ? 19.187  23.746   -56.906 1.00 88.98  ? 204 TYR G CZ  1 
ATOM   12975 O OH  . TYR G  1 204 ? 20.557  23.628   -56.869 1.00 95.72  ? 204 TYR G OH  1 
ATOM   12976 N N   . VAL G  1 205 ? 14.383  24.525   -53.925 1.00 69.06  ? 205 VAL G N   1 
ATOM   12977 C CA  . VAL G  1 205 ? 14.948  24.333   -52.596 1.00 66.17  ? 205 VAL G CA  1 
ATOM   12978 C C   . VAL G  1 205 ? 15.157  22.839   -52.352 1.00 67.53  ? 205 VAL G C   1 
ATOM   12979 O O   . VAL G  1 205 ? 14.340  22.022   -52.769 1.00 65.97  ? 205 VAL G O   1 
ATOM   12980 C CB  . VAL G  1 205 ? 14.030  24.915   -51.506 1.00 56.56  ? 205 VAL G CB  1 
ATOM   12981 C CG1 . VAL G  1 205 ? 14.678  24.774   -50.139 1.00 52.78  ? 205 VAL G CG1 1 
ATOM   12982 C CG2 . VAL G  1 205 ? 13.701  26.377   -51.810 1.00 65.18  ? 205 VAL G CG2 1 
ATOM   12983 N N   . PHE G  1 206 ? 16.255  22.476   -51.696 1.00 68.59  ? 206 PHE G N   1 
ATOM   12984 C CA  . PHE G  1 206 ? 16.517  21.069   -51.402 1.00 56.53  ? 206 PHE G CA  1 
ATOM   12985 C C   . PHE G  1 206 ? 17.073  20.869   -49.996 1.00 64.19  ? 206 PHE G C   1 
ATOM   12986 O O   . PHE G  1 206 ? 18.079  21.476   -49.624 1.00 73.51  ? 206 PHE G O   1 
ATOM   12987 C CB  . PHE G  1 206 ? 17.466  20.472   -52.439 1.00 62.18  ? 206 PHE G CB  1 
ATOM   12988 C CG  . PHE G  1 206 ? 17.737  19.012   -52.242 1.00 63.27  ? 206 PHE G CG  1 
ATOM   12989 C CD1 . PHE G  1 206 ? 18.773  18.590   -51.425 1.00 70.41  ? 206 PHE G CD1 1 
ATOM   12990 C CD2 . PHE G  1 206 ? 16.967  18.060   -52.890 1.00 70.98  ? 206 PHE G CD2 1 
ATOM   12991 C CE1 . PHE G  1 206 ? 19.031  17.248   -51.249 1.00 76.50  ? 206 PHE G CE1 1 
ATOM   12992 C CE2 . PHE G  1 206 ? 17.217  16.715   -52.718 1.00 59.92  ? 206 PHE G CE2 1 
ATOM   12993 C CZ  . PHE G  1 206 ? 18.252  16.307   -51.897 1.00 78.92  ? 206 PHE G CZ  1 
ATOM   12994 N N   . VAL G  1 207 ? 16.407  20.014   -49.226 1.00 67.65  ? 207 VAL G N   1 
ATOM   12995 C CA  . VAL G  1 207 ? 16.823  19.706   -47.865 1.00 60.74  ? 207 VAL G CA  1 
ATOM   12996 C C   . VAL G  1 207 ? 17.072  18.211   -47.714 1.00 65.02  ? 207 VAL G C   1 
ATOM   12997 O O   . VAL G  1 207 ? 16.190  17.394   -47.988 1.00 67.31  ? 207 VAL G O   1 
ATOM   12998 C CB  . VAL G  1 207 ? 15.761  20.142   -46.846 1.00 51.05  ? 207 VAL G CB  1 
ATOM   12999 C CG1 . VAL G  1 207 ? 16.214  19.807   -45.435 1.00 48.57  ? 207 VAL G CG1 1 
ATOM   13000 C CG2 . VAL G  1 207 ? 15.482  21.628   -46.980 1.00 57.97  ? 207 VAL G CG2 1 
ATOM   13001 N N   . GLY G  1 208 ? 18.272  17.855   -47.270 1.00 65.35  ? 208 GLY G N   1 
ATOM   13002 C CA  . GLY G  1 208 ? 18.639  16.458   -47.145 1.00 55.96  ? 208 GLY G CA  1 
ATOM   13003 C C   . GLY G  1 208 ? 19.493  16.130   -45.938 1.00 69.27  ? 208 GLY G C   1 
ATOM   13004 O O   . GLY G  1 208 ? 20.344  16.916   -45.522 1.00 77.49  ? 208 GLY G O   1 
ATOM   13005 N N   . SER G  1 209 ? 19.250  14.953   -45.371 1.00 63.92  ? 209 SER G N   1 
ATOM   13006 C CA  . SER G  1 209 ? 20.088  14.409   -44.312 1.00 63.85  ? 209 SER G CA  1 
ATOM   13007 C C   . SER G  1 209 ? 20.417  12.964   -44.666 1.00 69.81  ? 209 SER G C   1 
ATOM   13008 O O   . SER G  1 209 ? 20.293  12.562   -45.822 1.00 67.43  ? 209 SER G O   1 
ATOM   13009 C CB  . SER G  1 209 ? 19.373  14.477   -42.962 1.00 66.50  ? 209 SER G CB  1 
ATOM   13010 O OG  . SER G  1 209 ? 18.293  13.563   -42.907 1.00 58.95  ? 209 SER G OG  1 
ATOM   13011 N N   . SER G  1 210 ? 20.834  12.182   -43.676 1.00 83.22  ? 210 SER G N   1 
ATOM   13012 C CA  . SER G  1 210 ? 21.118  10.772   -43.910 1.00 80.77  ? 210 SER G CA  1 
ATOM   13013 C C   . SER G  1 210 ? 19.836  10.016   -44.239 1.00 87.56  ? 210 SER G C   1 
ATOM   13014 O O   . SER G  1 210 ? 19.868  8.979    -44.903 1.00 70.05  ? 210 SER G O   1 
ATOM   13015 C CB  . SER G  1 210 ? 21.799  10.142   -42.693 1.00 91.35  ? 210 SER G CB  1 
ATOM   13016 O OG  . SER G  1 210 ? 23.100  10.670   -42.503 1.00 108.54 ? 210 SER G OG  1 
ATOM   13017 N N   . ARG G  1 211 ? 18.709  10.549   -43.779 1.00 86.66  ? 211 ARG G N   1 
ATOM   13018 C CA  . ARG G  1 211 ? 17.424  9.879    -43.937 1.00 90.37  ? 211 ARG G CA  1 
ATOM   13019 C C   . ARG G  1 211 ? 16.423  10.726   -44.721 1.00 89.40  ? 211 ARG G C   1 
ATOM   13020 O O   . ARG G  1 211 ? 15.598  10.195   -45.463 1.00 103.69 ? 211 ARG G O   1 
ATOM   13021 C CB  . ARG G  1 211 ? 16.848  9.532    -42.564 1.00 97.59  ? 211 ARG G CB  1 
ATOM   13022 C CG  . ARG G  1 211 ? 16.466  10.748   -41.738 1.00 108.06 ? 211 ARG G CG  1 
ATOM   13023 C CD  . ARG G  1 211 ? 16.357  10.413   -40.263 1.00 123.54 ? 211 ARG G CD  1 
ATOM   13024 N NE  . ARG G  1 211 ? 15.616  9.179    -40.029 1.00 137.95 ? 211 ARG G NE  1 
ATOM   13025 C CZ  . ARG G  1 211 ? 15.137  8.813    -38.845 1.00 127.39 ? 211 ARG G CZ  1 
ATOM   13026 N NH1 . ARG G  1 211 ? 15.312  9.594    -37.789 1.00 117.63 ? 211 ARG G NH1 1 
ATOM   13027 N NH2 . ARG G  1 211 ? 14.475  7.671    -38.719 1.00 115.24 ? 211 ARG G NH2 1 
ATOM   13028 N N   . TYR G  1 212 ? 16.496  12.041   -44.548 1.00 91.64  ? 212 TYR G N   1 
ATOM   13029 C CA  . TYR G  1 212 ? 15.565  12.958   -45.207 1.00 62.45  ? 212 TYR G CA  1 
ATOM   13030 C C   . TYR G  1 212 ? 16.086  13.589   -46.497 1.00 62.77  ? 212 TYR G C   1 
ATOM   13031 O O   . TYR G  1 212 ? 17.184  14.144   -46.527 1.00 69.71  ? 212 TYR G O   1 
ATOM   13032 C CB  . TYR G  1 212 ? 15.270  14.155   -44.309 1.00 55.84  ? 212 TYR G CB  1 
ATOM   13033 C CG  . TYR G  1 212 ? 14.126  15.021   -44.789 1.00 72.13  ? 212 TYR G CG  1 
ATOM   13034 C CD1 . TYR G  1 212 ? 12.842  14.849   -44.288 1.00 63.79  ? 212 TYR G CD1 1 
ATOM   13035 C CD2 . TYR G  1 212 ? 14.331  16.012   -45.739 1.00 73.85  ? 212 TYR G CD2 1 
ATOM   13036 C CE1 . TYR G  1 212 ? 11.794  15.639   -44.723 1.00 68.38  ? 212 TYR G CE1 1 
ATOM   13037 C CE2 . TYR G  1 212 ? 13.289  16.806   -46.180 1.00 61.85  ? 212 TYR G CE2 1 
ATOM   13038 C CZ  . TYR G  1 212 ? 12.023  16.615   -45.669 1.00 66.06  ? 212 TYR G CZ  1 
ATOM   13039 O OH  . TYR G  1 212 ? 10.983  17.402   -46.104 1.00 61.48  ? 212 TYR G OH  1 
ATOM   13040 N N   . SER G  1 213 ? 15.292  13.502   -47.560 1.00 56.00  ? 213 SER G N   1 
ATOM   13041 C CA  . SER G  1 213 ? 15.667  14.090   -48.839 1.00 63.48  ? 213 SER G CA  1 
ATOM   13042 C C   . SER G  1 213 ? 14.482  14.495   -49.705 1.00 62.94  ? 213 SER G C   1 
ATOM   13043 O O   . SER G  1 213 ? 13.695  13.650   -50.130 1.00 70.37  ? 213 SER G O   1 
ATOM   13044 C CB  . SER G  1 213 ? 16.479  12.999   -49.556 1.00 61.95  ? 213 SER G CB  1 
ATOM   13045 O OG  . SER G  1 213 ? 16.946  13.456   -50.813 1.00 59.48  ? 213 SER G OG  1 
ATOM   13046 N N   . LYS G  1 214 ? 14.354  15.793   -49.964 1.00 65.59  ? 214 LYS G N   1 
ATOM   13047 C CA  . LYS G  1 214 ? 13.289  16.282   -50.834 1.00 67.03  ? 214 LYS G CA  1 
ATOM   13048 C C   . LYS G  1 214 ? 13.639  17.599   -51.519 1.00 71.69  ? 214 LYS G C   1 
ATOM   13049 O O   . LYS G  1 214 ? 14.262  18.480   -50.925 1.00 64.38  ? 214 LYS G O   1 
ATOM   13050 C CB  . LYS G  1 214 ? 11.970  16.416   -50.067 1.00 64.69  ? 214 LYS G CB  1 
ATOM   13051 C CG  . LYS G  1 214 ? 10.784  16.765   -50.956 1.00 68.39  ? 214 LYS G CG  1 
ATOM   13052 C CD  . LYS G  1 214 ? 9.537   16.000   -50.545 1.00 88.07  ? 214 LYS G CD  1 
ATOM   13053 C CE  . LYS G  1 214 ? 8.595   16.858   -49.718 1.00 83.92  ? 214 LYS G CE  1 
ATOM   13054 N NZ  . LYS G  1 214 ? 7.943   17.913   -50.543 1.00 97.18  ? 214 LYS G NZ  1 
ATOM   13055 N N   . LYS G  1 215 ? 13.228  17.716   -52.777 1.00 64.97  ? 215 LYS G N   1 
ATOM   13056 C CA  . LYS G  1 215 ? 13.451  18.922   -53.562 1.00 60.94  ? 215 LYS G CA  1 
ATOM   13057 C C   . LYS G  1 215 ? 12.135  19.673   -53.718 1.00 66.16  ? 215 LYS G C   1 
ATOM   13058 O O   . LYS G  1 215 ? 11.118  19.087   -54.090 1.00 73.61  ? 215 LYS G O   1 
ATOM   13059 C CB  . LYS G  1 215 ? 14.018  18.555   -54.933 1.00 78.32  ? 215 LYS G CB  1 
ATOM   13060 C CG  . LYS G  1 215 ? 14.440  19.740   -55.785 1.00 79.93  ? 215 LYS G CG  1 
ATOM   13061 C CD  . LYS G  1 215 ? 15.084  19.263   -57.077 1.00 87.49  ? 215 LYS G CD  1 
ATOM   13062 C CE  . LYS G  1 215 ? 15.776  20.398   -57.812 1.00 94.91  ? 215 LYS G CE  1 
ATOM   13063 N NZ  . LYS G  1 215 ? 16.568  19.897   -58.969 1.00 88.73  ? 215 LYS G NZ  1 
ATOM   13064 N N   . PHE G  1 216 ? 12.157  20.970   -53.431 1.00 68.21  ? 216 PHE G N   1 
ATOM   13065 C CA  . PHE G  1 216 ? 10.945  21.779   -53.455 1.00 63.23  ? 216 PHE G CA  1 
ATOM   13066 C C   . PHE G  1 216 ? 10.902  22.729   -54.646 1.00 58.56  ? 216 PHE G C   1 
ATOM   13067 O O   . PHE G  1 216 ? 11.883  23.405   -54.955 1.00 63.44  ? 216 PHE G O   1 
ATOM   13068 C CB  . PHE G  1 216 ? 10.810  22.575   -52.155 1.00 72.91  ? 216 PHE G CB  1 
ATOM   13069 C CG  . PHE G  1 216 ? 10.826  21.723   -50.919 1.00 66.14  ? 216 PHE G CG  1 
ATOM   13070 C CD1 . PHE G  1 216 ? 12.017  21.442   -50.271 1.00 58.61  ? 216 PHE G CD1 1 
ATOM   13071 C CD2 . PHE G  1 216 ? 9.650   21.202   -50.406 1.00 57.43  ? 216 PHE G CD2 1 
ATOM   13072 C CE1 . PHE G  1 216 ? 12.035  20.658   -49.135 1.00 66.20  ? 216 PHE G CE1 1 
ATOM   13073 C CE2 . PHE G  1 216 ? 9.662   20.418   -49.268 1.00 69.38  ? 216 PHE G CE2 1 
ATOM   13074 C CZ  . PHE G  1 216 ? 10.856  20.145   -48.632 1.00 63.02  ? 216 PHE G CZ  1 
ATOM   13075 N N   . LYS G  1 217 ? 9.752   22.771   -55.310 1.00 67.76  ? 217 LYS G N   1 
ATOM   13076 C CA  . LYS G  1 217 ? 9.518   23.720   -56.389 1.00 73.19  ? 217 LYS G CA  1 
ATOM   13077 C C   . LYS G  1 217 ? 8.444   24.719   -55.976 1.00 71.17  ? 217 LYS G C   1 
ATOM   13078 O O   . LYS G  1 217 ? 7.310   24.333   -55.693 1.00 73.12  ? 217 LYS G O   1 
ATOM   13079 C CB  . LYS G  1 217 ? 9.099   22.994   -57.668 1.00 77.40  ? 217 LYS G CB  1 
ATOM   13080 C CG  . LYS G  1 217 ? 10.230  22.773   -58.658 1.00 82.66  ? 217 LYS G CG  1 
ATOM   13081 C CD  . LYS G  1 217 ? 10.754  24.098   -59.192 1.00 91.21  ? 217 LYS G CD  1 
ATOM   13082 C CE  . LYS G  1 217 ? 11.861  23.888   -60.212 1.00 105.36 ? 217 LYS G CE  1 
ATOM   13083 N NZ  . LYS G  1 217 ? 12.354  25.177   -60.771 1.00 112.09 ? 217 LYS G NZ  1 
ATOM   13084 N N   . PRO G  1 218 ? 8.804   26.010   -55.932 1.00 75.88  ? 218 PRO G N   1 
ATOM   13085 C CA  . PRO G  1 218 ? 7.868   27.072   -55.549 1.00 69.23  ? 218 PRO G CA  1 
ATOM   13086 C C   . PRO G  1 218 ? 6.626   27.085   -56.434 1.00 70.34  ? 218 PRO G C   1 
ATOM   13087 O O   . PRO G  1 218 ? 6.738   27.128   -57.659 1.00 66.27  ? 218 PRO G O   1 
ATOM   13088 C CB  . PRO G  1 218 ? 8.684   28.350   -55.767 1.00 69.95  ? 218 PRO G CB  1 
ATOM   13089 C CG  . PRO G  1 218 ? 10.102  27.918   -55.636 1.00 76.93  ? 218 PRO G CG  1 
ATOM   13090 C CD  . PRO G  1 218 ? 10.152  26.534   -56.210 1.00 77.40  ? 218 PRO G CD  1 
ATOM   13091 N N   . GLU G  1 219 ? 5.454   27.043   -55.809 1.00 76.16  ? 219 GLU G N   1 
ATOM   13092 C CA  . GLU G  1 219 ? 4.192   27.081   -56.536 1.00 71.50  ? 219 GLU G CA  1 
ATOM   13093 C C   . GLU G  1 219 ? 3.618   28.493   -56.523 1.00 72.72  ? 219 GLU G C   1 
ATOM   13094 O O   . GLU G  1 219 ? 2.952   28.896   -55.570 1.00 65.49  ? 219 GLU G O   1 
ATOM   13095 C CB  . GLU G  1 219 ? 3.195   26.094   -55.924 1.00 71.66  ? 219 GLU G CB  1 
ATOM   13096 C CG  . GLU G  1 219 ? 3.709   24.664   -55.857 1.00 82.47  ? 219 GLU G CG  1 
ATOM   13097 C CD  . GLU G  1 219 ? 2.704   23.710   -55.238 1.00 92.53  ? 219 GLU G CD  1 
ATOM   13098 O OE1 . GLU G  1 219 ? 1.659   24.182   -54.743 1.00 83.21  ? 219 GLU G OE1 1 
ATOM   13099 O OE2 . GLU G  1 219 ? 2.959   22.487   -55.248 1.00 85.56  ? 219 GLU G OE2 1 
ATOM   13100 N N   . ILE G  1 220 ? 3.883   29.241   -57.589 1.00 79.31  ? 220 ILE G N   1 
ATOM   13101 C CA  . ILE G  1 220 ? 3.492   30.645   -57.667 1.00 73.56  ? 220 ILE G CA  1 
ATOM   13102 C C   . ILE G  1 220 ? 2.070   30.827   -58.192 1.00 68.70  ? 220 ILE G C   1 
ATOM   13103 O O   . ILE G  1 220 ? 1.763   30.453   -59.324 1.00 72.78  ? 220 ILE G O   1 
ATOM   13104 C CB  . ILE G  1 220 ? 4.467   31.436   -58.558 1.00 71.08  ? 220 ILE G CB  1 
ATOM   13105 C CG1 . ILE G  1 220 ? 5.893   31.318   -58.014 1.00 64.44  ? 220 ILE G CG1 1 
ATOM   13106 C CG2 . ILE G  1 220 ? 4.039   32.893   -58.656 1.00 74.95  ? 220 ILE G CG2 1 
ATOM   13107 C CD1 . ILE G  1 220 ? 6.957   31.813   -58.969 1.00 86.93  ? 220 ILE G CD1 1 
ATOM   13108 N N   . ALA G  1 221 ? 1.209   31.408   -57.362 1.00 65.34  ? 221 ALA G N   1 
ATOM   13109 C CA  . ALA G  1 221 ? -0.180  31.656   -57.737 1.00 61.45  ? 221 ALA G CA  1 
ATOM   13110 C C   . ALA G  1 221 ? -0.884  32.541   -56.711 1.00 73.36  ? 221 ALA G C   1 
ATOM   13111 O O   . ALA G  1 221 ? -0.329  32.847   -55.656 1.00 66.74  ? 221 ALA G O   1 
ATOM   13112 C CB  . ALA G  1 221 ? -0.927  30.341   -57.909 1.00 50.68  ? 221 ALA G CB  1 
ATOM   13113 N N   . ILE G  1 222 ? -2.109  32.948   -57.027 1.00 77.39  ? 222 ILE G N   1 
ATOM   13114 C CA  . ILE G  1 222 ? -2.884  33.809   -56.140 1.00 86.26  ? 222 ILE G CA  1 
ATOM   13115 C C   . ILE G  1 222 ? -3.862  33.014   -55.280 1.00 78.98  ? 222 ILE G C   1 
ATOM   13116 O O   . ILE G  1 222 ? -4.836  32.455   -55.786 1.00 74.49  ? 222 ILE G O   1 
ATOM   13117 C CB  . ILE G  1 222 ? -3.670  34.874   -56.929 1.00 92.80  ? 222 ILE G CB  1 
ATOM   13118 C CG1 . ILE G  1 222 ? -2.718  35.740   -57.756 1.00 87.27  ? 222 ILE G CG1 1 
ATOM   13119 C CG2 . ILE G  1 222 ? -4.496  35.735   -55.985 1.00 77.90  ? 222 ILE G CG2 1 
ATOM   13120 C CD1 . ILE G  1 222 ? -1.716  36.511   -56.924 1.00 96.84  ? 222 ILE G CD1 1 
ATOM   13121 N N   . ARG G  1 223 ? -3.596  32.968   -53.978 1.00 74.69  ? 223 ARG G N   1 
ATOM   13122 C CA  . ARG G  1 223 ? -4.499  32.319   -53.036 1.00 80.23  ? 223 ARG G CA  1 
ATOM   13123 C C   . ARG G  1 223 ? -5.400  33.354   -52.372 1.00 82.69  ? 223 ARG G C   1 
ATOM   13124 O O   . ARG G  1 223 ? -5.006  34.509   -52.210 1.00 81.12  ? 223 ARG G O   1 
ATOM   13125 C CB  . ARG G  1 223 ? -3.716  31.559   -51.962 1.00 78.39  ? 223 ARG G CB  1 
ATOM   13126 C CG  . ARG G  1 223 ? -2.977  30.324   -52.453 1.00 66.44  ? 223 ARG G CG  1 
ATOM   13127 C CD  . ARG G  1 223 ? -1.610  30.667   -53.023 1.00 61.69  ? 223 ARG G CD  1 
ATOM   13128 N NE  . ARG G  1 223 ? -0.763  29.482   -53.122 1.00 63.95  ? 223 ARG G NE  1 
ATOM   13129 C CZ  . ARG G  1 223 ? 0.480   29.485   -53.593 1.00 66.55  ? 223 ARG G CZ  1 
ATOM   13130 N NH1 . ARG G  1 223 ? 1.029   30.614   -54.017 1.00 76.62  ? 223 ARG G NH1 1 
ATOM   13131 N NH2 . ARG G  1 223 ? 1.172   28.355   -53.640 1.00 72.76  ? 223 ARG G NH2 1 
ATOM   13132 N N   . PRO G  1 224 ? -6.617  32.941   -51.987 1.00 78.16  ? 224 PRO G N   1 
ATOM   13133 C CA  . PRO G  1 224 ? -7.538  33.823   -51.264 1.00 71.43  ? 224 PRO G CA  1 
ATOM   13134 C C   . PRO G  1 224 ? -6.862  34.429   -50.041 1.00 81.58  ? 224 PRO G C   1 
ATOM   13135 O O   . PRO G  1 224 ? -6.278  33.703   -49.238 1.00 88.28  ? 224 PRO G O   1 
ATOM   13136 C CB  . PRO G  1 224 ? -8.659  32.875   -50.835 1.00 63.26  ? 224 PRO G CB  1 
ATOM   13137 C CG  . PRO G  1 224 ? -8.650  31.805   -51.868 1.00 76.51  ? 224 PRO G CG  1 
ATOM   13138 C CD  . PRO G  1 224 ? -7.208  31.617   -52.248 1.00 79.31  ? 224 PRO G CD  1 
ATOM   13139 N N   . LYS G  1 225 ? -6.946  35.748   -49.908 1.00 90.79  ? 225 LYS G N   1 
ATOM   13140 C CA  . LYS G  1 225 ? -6.247  36.457   -48.844 1.00 84.81  ? 225 LYS G CA  1 
ATOM   13141 C C   . LYS G  1 225 ? -6.560  35.931   -47.449 1.00 76.69  ? 225 LYS G C   1 
ATOM   13142 O O   . LYS G  1 225 ? -7.714  35.920   -47.015 1.00 86.32  ? 225 LYS G O   1 
ATOM   13143 C CB  . LYS G  1 225 ? -6.543  37.956   -48.910 1.00 104.45 ? 225 LYS G CB  1 
ATOM   13144 C CG  . LYS G  1 225 ? -5.897  38.664   -50.087 1.00 122.05 ? 225 LYS G CG  1 
ATOM   13145 C CD  . LYS G  1 225 ? -6.190  40.154   -50.062 1.00 136.30 ? 225 LYS G CD  1 
ATOM   13146 C CE  . LYS G  1 225 ? -5.526  40.862   -51.231 1.00 153.44 ? 225 LYS G CE  1 
ATOM   13147 N NZ  . LYS G  1 225 ? -4.049  40.670   -51.226 1.00 158.35 ? 225 LYS G NZ  1 
ATOM   13148 N N   . VAL G  1 226 ? -5.514  35.490   -46.759 1.00 76.89  ? 226 VAL G N   1 
ATOM   13149 C CA  . VAL G  1 226 ? -5.587  35.171   -45.341 1.00 78.29  ? 226 VAL G CA  1 
ATOM   13150 C C   . VAL G  1 226 ? -4.530  36.010   -44.633 1.00 78.12  ? 226 VAL G C   1 
ATOM   13151 O O   . VAL G  1 226 ? -3.335  35.771   -44.796 1.00 77.20  ? 226 VAL G O   1 
ATOM   13152 C CB  . VAL G  1 226 ? -5.309  33.678   -45.074 1.00 72.88  ? 226 VAL G CB  1 
ATOM   13153 C CG1 . VAL G  1 226 ? -5.371  33.386   -43.581 1.00 76.92  ? 226 VAL G CG1 1 
ATOM   13154 C CG2 . VAL G  1 226 ? -6.293  32.805   -45.839 1.00 66.33  ? 226 VAL G CG2 1 
ATOM   13155 N N   . ARG G  1 227 ? -4.970  37.010   -43.875 1.00 82.67  ? 227 ARG G N   1 
ATOM   13156 C CA  . ARG G  1 227 ? -4.051  37.931   -43.206 1.00 80.63  ? 227 ARG G CA  1 
ATOM   13157 C C   . ARG G  1 227 ? -3.331  38.865   -44.187 1.00 87.43  ? 227 ARG G C   1 
ATOM   13158 O O   . ARG G  1 227 ? -2.201  39.286   -43.933 1.00 93.98  ? 227 ARG G O   1 
ATOM   13159 C CB  . ARG G  1 227 ? -3.042  37.163   -42.338 1.00 74.65  ? 227 ARG G CB  1 
ATOM   13160 C CG  . ARG G  1 227 ? -3.610  36.692   -40.996 1.00 76.14  ? 227 ARG G CG  1 
ATOM   13161 C CD  . ARG G  1 227 ? -2.645  35.767   -40.255 1.00 81.53  ? 227 ARG G CD  1 
ATOM   13162 N NE  . ARG G  1 227 ? -2.388  36.245   -38.901 1.00 70.36  ? 227 ARG G NE  1 
ATOM   13163 C CZ  . ARG G  1 227 ? -1.558  37.240   -38.596 1.00 85.87  ? 227 ARG G CZ  1 
ATOM   13164 N NH1 . ARG G  1 227 ? -0.889  37.883   -39.546 1.00 98.16  ? 227 ARG G NH1 1 
ATOM   13165 N NH2 . ARG G  1 227 ? -1.403  37.595   -37.330 1.00 85.31  ? 227 ARG G NH2 1 
ATOM   13166 N N   . ASP G  1 228 ? -3.997  39.191   -45.294 1.00 94.12  ? 228 ASP G N   1 
ATOM   13167 C CA  . ASP G  1 228 ? -3.457  40.121   -46.293 1.00 112.92 ? 228 ASP G CA  1 
ATOM   13168 C C   . ASP G  1 228 ? -2.489  39.465   -47.276 1.00 111.31 ? 228 ASP G C   1 
ATOM   13169 O O   . ASP G  1 228 ? -2.057  40.094   -48.242 1.00 124.29 ? 228 ASP G O   1 
ATOM   13170 C CB  . ASP G  1 228 ? -2.781  41.324   -45.622 1.00 137.73 ? 228 ASP G CB  1 
ATOM   13171 C CG  . ASP G  1 228 ? -3.701  42.519   -45.502 1.00 160.59 ? 228 ASP G CG  1 
ATOM   13172 O OD1 . ASP G  1 228 ? -4.088  43.076   -46.551 1.00 160.38 ? 228 ASP G OD1 1 
ATOM   13173 O OD2 . ASP G  1 228 ? -4.027  42.910   -44.362 1.00 175.12 ? 228 ASP G OD2 1 
ATOM   13174 N N   . GLN G  1 229 ? -2.152  38.204   -47.028 1.00 97.24  ? 229 GLN G N   1 
ATOM   13175 C CA  . GLN G  1 229 ? -1.203  37.493   -47.875 1.00 90.02  ? 229 GLN G CA  1 
ATOM   13176 C C   . GLN G  1 229 ? -1.912  36.615   -48.900 1.00 79.64  ? 229 GLN G C   1 
ATOM   13177 O O   . GLN G  1 229 ? -2.709  35.749   -48.542 1.00 82.35  ? 229 GLN G O   1 
ATOM   13178 C CB  . GLN G  1 229 ? -0.262  36.641   -47.021 1.00 80.56  ? 229 GLN G CB  1 
ATOM   13179 C CG  . GLN G  1 229 ? 0.310   37.372   -45.818 1.00 75.78  ? 229 GLN G CG  1 
ATOM   13180 C CD  . GLN G  1 229 ? 1.049   38.638   -46.201 1.00 87.60  ? 229 GLN G CD  1 
ATOM   13181 O OE1 . GLN G  1 229 ? 1.639   38.724   -47.278 1.00 91.63  ? 229 GLN G OE1 1 
ATOM   13182 N NE2 . GLN G  1 229 ? 1.023   39.630   -45.317 1.00 101.29 ? 229 GLN G NE2 1 
ATOM   13183 N N   . GLU G  1 230 ? -1.622  36.847   -50.177 1.00 81.33  ? 230 GLU G N   1 
ATOM   13184 C CA  . GLU G  1 230 ? -2.156  36.013   -51.247 1.00 75.14  ? 230 GLU G CA  1 
ATOM   13185 C C   . GLU G  1 230 ? -1.180  34.883   -51.544 1.00 77.64  ? 230 GLU G C   1 
ATOM   13186 O O   . GLU G  1 230 ? -1.489  33.957   -52.292 1.00 72.68  ? 230 GLU G O   1 
ATOM   13187 C CB  . GLU G  1 230 ? -2.407  36.842   -52.507 1.00 97.16  ? 230 GLU G CB  1 
ATOM   13188 N N   . GLY G  1 231 ? 0.007   34.974   -50.954 1.00 67.80  ? 231 GLY G N   1 
ATOM   13189 C CA  . GLY G  1 231 ? 1.000   33.925   -51.071 1.00 70.79  ? 231 GLY G CA  1 
ATOM   13190 C C   . GLY G  1 231 ? 0.909   32.976   -49.894 1.00 73.44  ? 231 GLY G C   1 
ATOM   13191 O O   . GLY G  1 231 ? 0.227   33.260   -48.909 1.00 72.35  ? 231 GLY G O   1 
ATOM   13192 N N   . ARG G  1 232 ? 1.595   31.844   -49.993 1.00 70.07  ? 232 ARG G N   1 
ATOM   13193 C CA  . ARG G  1 232 ? 1.578   30.852   -48.926 1.00 60.32  ? 232 ARG G CA  1 
ATOM   13194 C C   . ARG G  1 232 ? 2.988   30.522   -48.454 1.00 59.50  ? 232 ARG G C   1 
ATOM   13195 O O   . ARG G  1 232 ? 3.967   30.824   -49.135 1.00 58.44  ? 232 ARG G O   1 
ATOM   13196 C CB  . ARG G  1 232 ? 0.859   29.582   -49.387 1.00 62.61  ? 232 ARG G CB  1 
ATOM   13197 C CG  . ARG G  1 232 ? -0.649  29.735   -49.490 1.00 63.88  ? 232 ARG G CG  1 
ATOM   13198 C CD  . ARG G  1 232 ? -1.239  30.118   -48.143 1.00 64.67  ? 232 ARG G CD  1 
ATOM   13199 N NE  . ARG G  1 232 ? -2.674  30.364   -48.211 1.00 74.97  ? 232 ARG G NE  1 
ATOM   13200 C CZ  . ARG G  1 232 ? -3.216  31.521   -48.572 1.00 74.93  ? 232 ARG G CZ  1 
ATOM   13201 N NH1 . ARG G  1 232 ? -2.440  32.543   -48.907 1.00 63.84  ? 232 ARG G NH1 1 
ATOM   13202 N NH2 . ARG G  1 232 ? -4.534  31.656   -48.602 1.00 68.12  ? 232 ARG G NH2 1 
ATOM   13203 N N   . MET G  1 233 ? 3.085   29.910   -47.279 1.00 60.10  ? 233 MET G N   1 
ATOM   13204 C CA  . MET G  1 233 ? 4.370   29.483   -46.742 1.00 61.42  ? 233 MET G CA  1 
ATOM   13205 C C   . MET G  1 233 ? 4.225   28.148   -46.023 1.00 67.71  ? 233 MET G C   1 
ATOM   13206 O O   . MET G  1 233 ? 3.633   28.072   -44.946 1.00 60.94  ? 233 MET G O   1 
ATOM   13207 C CB  . MET G  1 233 ? 4.946   30.541   -45.796 1.00 58.13  ? 233 MET G CB  1 
ATOM   13208 C CG  . MET G  1 233 ? 6.360   30.240   -45.318 1.00 60.96  ? 233 MET G CG  1 
ATOM   13209 S SD  . MET G  1 233 ? 7.061   31.554   -44.300 1.00 74.78  ? 233 MET G SD  1 
ATOM   13210 C CE  . MET G  1 233 ? 7.111   32.905   -45.475 1.00 73.45  ? 233 MET G CE  1 
ATOM   13211 N N   . ASN G  1 234 ? 4.760   27.094   -46.629 1.00 63.95  ? 234 ASN G N   1 
ATOM   13212 C CA  . ASN G  1 234 ? 4.699   25.764   -46.038 1.00 56.19  ? 234 ASN G CA  1 
ATOM   13213 C C   . ASN G  1 234 ? 5.837   25.527   -45.053 1.00 52.62  ? 234 ASN G C   1 
ATOM   13214 O O   . ASN G  1 234 ? 6.984   25.891   -45.314 1.00 57.31  ? 234 ASN G O   1 
ATOM   13215 C CB  . ASN G  1 234 ? 4.701   24.689   -47.126 1.00 51.77  ? 234 ASN G CB  1 
ATOM   13216 C CG  . ASN G  1 234 ? 3.439   24.711   -47.966 1.00 60.21  ? 234 ASN G CG  1 
ATOM   13217 O OD1 . ASN G  1 234 ? 2.516   25.481   -47.701 1.00 58.05  ? 234 ASN G OD1 1 
ATOM   13218 N ND2 . ASN G  1 234 ? 3.392   23.860   -48.985 1.00 65.20  ? 234 ASN G ND2 1 
ATOM   13219 N N   . TYR G  1 235 ? 5.511   24.916   -43.920 1.00 47.86  ? 235 TYR G N   1 
ATOM   13220 C CA  . TYR G  1 235 ? 6.491   24.683   -42.868 1.00 43.58  ? 235 TYR G CA  1 
ATOM   13221 C C   . TYR G  1 235 ? 6.854   23.207   -42.764 1.00 54.21  ? 235 TYR G C   1 
ATOM   13222 O O   . TYR G  1 235 ? 5.980   22.342   -42.698 1.00 51.18  ? 235 TYR G O   1 
ATOM   13223 C CB  . TYR G  1 235 ? 5.965   25.205   -41.530 1.00 41.55  ? 235 TYR G CB  1 
ATOM   13224 C CG  . TYR G  1 235 ? 5.483   26.634   -41.605 1.00 61.26  ? 235 TYR G CG  1 
ATOM   13225 C CD1 . TYR G  1 235 ? 4.149   26.924   -41.856 1.00 62.80  ? 235 TYR G CD1 1 
ATOM   13226 C CD2 . TYR G  1 235 ? 6.365   27.694   -41.443 1.00 58.95  ? 235 TYR G CD2 1 
ATOM   13227 C CE1 . TYR G  1 235 ? 3.705   28.229   -41.935 1.00 59.75  ? 235 TYR G CE1 1 
ATOM   13228 C CE2 . TYR G  1 235 ? 5.930   29.002   -41.520 1.00 63.55  ? 235 TYR G CE2 1 
ATOM   13229 C CZ  . TYR G  1 235 ? 4.600   29.264   -41.766 1.00 58.99  ? 235 TYR G CZ  1 
ATOM   13230 O OH  . TYR G  1 235 ? 4.162   30.566   -41.844 1.00 62.87  ? 235 TYR G OH  1 
ATOM   13231 N N   . TYR G  1 236 ? 8.153   22.929   -42.753 1.00 52.23  ? 236 TYR G N   1 
ATOM   13232 C CA  . TYR G  1 236 ? 8.644   21.560   -42.690 1.00 45.55  ? 236 TYR G CA  1 
ATOM   13233 C C   . TYR G  1 236 ? 9.566   21.359   -41.493 1.00 49.68  ? 236 TYR G C   1 
ATOM   13234 O O   . TYR G  1 236 ? 10.123  22.318   -40.958 1.00 58.69  ? 236 TYR G O   1 
ATOM   13235 C CB  . TYR G  1 236 ? 9.376   21.199   -43.983 1.00 39.37  ? 236 TYR G CB  1 
ATOM   13236 C CG  . TYR G  1 236 ? 8.498   21.229   -45.213 1.00 56.65  ? 236 TYR G CG  1 
ATOM   13237 C CD1 . TYR G  1 236 ? 8.252   22.418   -45.888 1.00 56.66  ? 236 TYR G CD1 1 
ATOM   13238 C CD2 . TYR G  1 236 ? 7.915   20.068   -45.700 1.00 52.11  ? 236 TYR G CD2 1 
ATOM   13239 C CE1 . TYR G  1 236 ? 7.450   22.449   -47.014 1.00 55.86  ? 236 TYR G CE1 1 
ATOM   13240 C CE2 . TYR G  1 236 ? 7.113   20.088   -46.825 1.00 60.29  ? 236 TYR G CE2 1 
ATOM   13241 C CZ  . TYR G  1 236 ? 6.882   21.280   -47.477 1.00 63.10  ? 236 TYR G CZ  1 
ATOM   13242 O OH  . TYR G  1 236 ? 6.082   21.300   -48.597 1.00 54.14  ? 236 TYR G OH  1 
ATOM   13243 N N   . TRP G  1 237 ? 9.721   20.106   -41.077 1.00 52.88  ? 237 TRP G N   1 
ATOM   13244 C CA  . TRP G  1 237 ? 10.579  19.773   -39.946 1.00 47.89  ? 237 TRP G CA  1 
ATOM   13245 C C   . TRP G  1 237 ? 11.138  18.358   -40.078 1.00 46.17  ? 237 TRP G C   1 
ATOM   13246 O O   . TRP G  1 237 ? 10.623  17.545   -40.844 1.00 54.65  ? 237 TRP G O   1 
ATOM   13247 C CB  . TRP G  1 237 ? 9.809   19.914   -38.630 1.00 40.87  ? 237 TRP G CB  1 
ATOM   13248 C CG  . TRP G  1 237 ? 8.668   18.950   -38.495 1.00 54.38  ? 237 TRP G CG  1 
ATOM   13249 C CD1 . TRP G  1 237 ? 7.375   19.148   -38.885 1.00 51.29  ? 237 TRP G CD1 1 
ATOM   13250 C CD2 . TRP G  1 237 ? 8.720   17.634   -37.931 1.00 50.65  ? 237 TRP G CD2 1 
ATOM   13251 N NE1 . TRP G  1 237 ? 6.619   18.038   -38.598 1.00 53.44  ? 237 TRP G NE1 1 
ATOM   13252 C CE2 . TRP G  1 237 ? 7.421   17.094   -38.013 1.00 53.33  ? 237 TRP G CE2 1 
ATOM   13253 C CE3 . TRP G  1 237 ? 9.738   16.860   -37.366 1.00 46.84  ? 237 TRP G CE3 1 
ATOM   13254 C CZ2 . TRP G  1 237 ? 7.114   15.816   -37.549 1.00 57.53  ? 237 TRP G CZ2 1 
ATOM   13255 C CZ3 . TRP G  1 237 ? 9.432   15.592   -36.907 1.00 56.62  ? 237 TRP G CZ3 1 
ATOM   13256 C CH2 . TRP G  1 237 ? 8.131   15.083   -37.001 1.00 51.58  ? 237 TRP G CH2 1 
ATOM   13257 N N   . THR G  1 238 ? 12.198  18.075   -39.327 1.00 47.34  ? 238 THR G N   1 
ATOM   13258 C CA  . THR G  1 238 ? 12.824  16.757   -39.330 1.00 53.64  ? 238 THR G CA  1 
ATOM   13259 C C   . THR G  1 238 ? 13.773  16.608   -38.146 1.00 57.38  ? 238 THR G C   1 
ATOM   13260 O O   . THR G  1 238 ? 14.355  17.586   -37.676 1.00 59.18  ? 238 THR G O   1 
ATOM   13261 C CB  . THR G  1 238 ? 13.630  16.516   -40.615 1.00 49.36  ? 238 THR G CB  1 
ATOM   13262 O OG1 . THR G  1 238 ? 14.124  15.171   -40.626 1.00 57.25  ? 238 THR G OG1 1 
ATOM   13263 C CG2 . THR G  1 238 ? 14.805  17.474   -40.683 1.00 52.09  ? 238 THR G CG2 1 
ATOM   13264 N N   . LEU G  1 239 ? 13.934  15.375   -37.677 1.00 55.61  ? 239 LEU G N   1 
ATOM   13265 C CA  . LEU G  1 239 ? 14.835  15.087   -36.567 1.00 55.22  ? 239 LEU G CA  1 
ATOM   13266 C C   . LEU G  1 239 ? 16.146  14.490   -37.061 1.00 66.61  ? 239 LEU G C   1 
ATOM   13267 O O   . LEU G  1 239 ? 16.196  13.326   -37.452 1.00 80.96  ? 239 LEU G O   1 
ATOM   13268 C CB  . LEU G  1 239 ? 14.168  14.133   -35.573 1.00 60.83  ? 239 LEU G CB  1 
ATOM   13269 C CG  . LEU G  1 239 ? 12.910  14.668   -34.888 1.00 48.58  ? 239 LEU G CG  1 
ATOM   13270 C CD1 . LEU G  1 239 ? 12.212  13.570   -34.104 1.00 72.12  ? 239 LEU G CD1 1 
ATOM   13271 C CD2 . LEU G  1 239 ? 13.257  15.839   -33.987 1.00 54.54  ? 239 LEU G CD2 1 
ATOM   13272 N N   . VAL G  1 240 ? 17.208  15.289   -37.044 1.00 62.34  ? 240 VAL G N   1 
ATOM   13273 C CA  . VAL G  1 240 ? 18.517  14.798   -37.455 1.00 64.01  ? 240 VAL G CA  1 
ATOM   13274 C C   . VAL G  1 240 ? 19.238  14.098   -36.313 1.00 66.28  ? 240 VAL G C   1 
ATOM   13275 O O   . VAL G  1 240 ? 19.442  14.672   -35.246 1.00 67.32  ? 240 VAL G O   1 
ATOM   13276 C CB  . VAL G  1 240 ? 19.402  15.905   -38.065 1.00 66.73  ? 240 VAL G CB  1 
ATOM   13277 C CG1 . VAL G  1 240 ? 18.797  17.280   -37.810 1.00 57.32  ? 240 VAL G CG1 1 
ATOM   13278 C CG2 . VAL G  1 240 ? 20.826  15.800   -37.536 1.00 73.81  ? 240 VAL G CG2 1 
ATOM   13279 N N   . GLU G  1 241 ? 19.623  12.852   -36.564 1.00 74.49  ? 241 GLU G N   1 
ATOM   13280 C CA  . GLU G  1 241 ? 20.245  11.998   -35.561 1.00 65.58  ? 241 GLU G CA  1 
ATOM   13281 C C   . GLU G  1 241 ? 21.595  12.533   -35.093 1.00 72.78  ? 241 GLU G C   1 
ATOM   13282 O O   . GLU G  1 241 ? 22.261  13.270   -35.820 1.00 72.58  ? 241 GLU G O   1 
ATOM   13283 C CB  . GLU G  1 241 ? 20.426  10.591   -36.130 1.00 82.79  ? 241 GLU G CB  1 
ATOM   13284 C CG  . GLU G  1 241 ? 19.136  9.941    -36.599 1.00 98.41  ? 241 GLU G CG  1 
ATOM   13285 C CD  . GLU G  1 241 ? 18.270  9.478    -35.447 1.00 122.66 ? 241 GLU G CD  1 
ATOM   13286 O OE1 . GLU G  1 241 ? 17.033  9.442    -35.607 1.00 128.32 ? 241 GLU G OE1 1 
ATOM   13287 O OE2 . GLU G  1 241 ? 18.830  9.152    -34.379 1.00 135.50 ? 241 GLU G OE2 1 
ATOM   13288 N N   . PRO G  1 242 ? 22.005  12.157   -33.871 1.00 84.64  ? 242 PRO G N   1 
ATOM   13289 C CA  . PRO G  1 242 ? 23.337  12.526   -33.384 1.00 82.76  ? 242 PRO G CA  1 
ATOM   13290 C C   . PRO G  1 242 ? 24.417  12.007   -34.325 1.00 81.26  ? 242 PRO G C   1 
ATOM   13291 O O   . PRO G  1 242 ? 24.411  10.826   -34.674 1.00 74.19  ? 242 PRO G O   1 
ATOM   13292 C CB  . PRO G  1 242 ? 23.426  11.808   -32.035 1.00 63.86  ? 242 PRO G CB  1 
ATOM   13293 C CG  . PRO G  1 242 ? 22.013  11.644   -31.599 1.00 65.12  ? 242 PRO G CG  1 
ATOM   13294 C CD  . PRO G  1 242 ? 21.230  11.419   -32.859 1.00 69.31  ? 242 PRO G CD  1 
ATOM   13295 N N   . GLY G  1 243 ? 25.328  12.882   -34.735 1.00 74.42  ? 243 GLY G N   1 
ATOM   13296 C CA  . GLY G  1 243 ? 26.395  12.497   -35.640 1.00 77.12  ? 243 GLY G CA  1 
ATOM   13297 C C   . GLY G  1 243 ? 25.982  12.593   -37.095 1.00 73.34  ? 243 GLY G C   1 
ATOM   13298 O O   . GLY G  1 243 ? 26.786  12.358   -37.997 1.00 88.83  ? 243 GLY G O   1 
ATOM   13299 N N   . ASP G  1 244 ? 24.719  12.936   -37.322 1.00 73.88  ? 244 ASP G N   1 
ATOM   13300 C CA  . ASP G  1 244 ? 24.204  13.114   -38.674 1.00 69.32  ? 244 ASP G CA  1 
ATOM   13301 C C   . ASP G  1 244 ? 24.211  14.595   -39.035 1.00 71.93  ? 244 ASP G C   1 
ATOM   13302 O O   . ASP G  1 244 ? 24.226  15.453   -38.154 1.00 83.48  ? 244 ASP G O   1 
ATOM   13303 C CB  . ASP G  1 244 ? 22.786  12.548   -38.779 1.00 74.94  ? 244 ASP G CB  1 
ATOM   13304 C CG  . ASP G  1 244 ? 22.299  12.450   -40.213 1.00 90.89  ? 244 ASP G CG  1 
ATOM   13305 O OD1 . ASP G  1 244 ? 21.175  11.951   -40.423 1.00 92.82  ? 244 ASP G OD1 1 
ATOM   13306 O OD2 . ASP G  1 244 ? 23.037  12.864   -41.130 1.00 81.22  ? 244 ASP G OD2 1 
ATOM   13307 N N   . LYS G  1 245 ? 24.210  14.894   -40.329 1.00 65.25  ? 245 LYS G N   1 
ATOM   13308 C CA  . LYS G  1 245 ? 24.173  16.277   -40.785 1.00 75.40  ? 245 LYS G CA  1 
ATOM   13309 C C   . LYS G  1 245 ? 23.035  16.515   -41.772 1.00 75.67  ? 245 LYS G C   1 
ATOM   13310 O O   . LYS G  1 245 ? 22.625  15.608   -42.497 1.00 74.17  ? 245 LYS G O   1 
ATOM   13311 C CB  . LYS G  1 245 ? 25.509  16.683   -41.411 1.00 86.05  ? 245 LYS G CB  1 
ATOM   13312 C CG  . LYS G  1 245 ? 25.738  16.149   -42.815 1.00 84.49  ? 245 LYS G CG  1 
ATOM   13313 C CD  . LYS G  1 245 ? 27.068  16.635   -43.369 1.00 84.97  ? 245 LYS G CD  1 
ATOM   13314 C CE  . LYS G  1 245 ? 27.290  16.154   -44.793 1.00 96.72  ? 245 LYS G CE  1 
ATOM   13315 N NZ  . LYS G  1 245 ? 28.636  16.536   -45.303 1.00 95.10  ? 245 LYS G NZ  1 
ATOM   13316 N N   . ILE G  1 246 ? 22.530  17.743   -41.787 1.00 69.37  ? 246 ILE G N   1 
ATOM   13317 C CA  . ILE G  1 246 ? 21.457  18.126   -42.694 1.00 65.77  ? 246 ILE G CA  1 
ATOM   13318 C C   . ILE G  1 246 ? 21.905  19.277   -43.591 1.00 71.16  ? 246 ILE G C   1 
ATOM   13319 O O   . ILE G  1 246 ? 22.477  20.259   -43.119 1.00 72.08  ? 246 ILE G O   1 
ATOM   13320 C CB  . ILE G  1 246 ? 20.184  18.527   -41.922 1.00 63.55  ? 246 ILE G CB  1 
ATOM   13321 C CG1 . ILE G  1 246 ? 19.068  18.919   -42.892 1.00 58.01  ? 246 ILE G CG1 1 
ATOM   13322 C CG2 . ILE G  1 246 ? 20.479  19.662   -40.952 1.00 61.65  ? 246 ILE G CG2 1 
ATOM   13323 C CD1 . ILE G  1 246 ? 17.805  19.390   -42.204 1.00 54.76  ? 246 ILE G CD1 1 
ATOM   13324 N N   . THR G  1 247 ? 21.647  19.145   -44.887 1.00 73.95  ? 247 THR G N   1 
ATOM   13325 C CA  . THR G  1 247 ? 22.093  20.131   -45.864 1.00 78.44  ? 247 THR G CA  1 
ATOM   13326 C C   . THR G  1 247 ? 20.942  20.945   -46.445 1.00 67.88  ? 247 THR G C   1 
ATOM   13327 O O   . THR G  1 247 ? 19.879  20.408   -46.757 1.00 64.77  ? 247 THR G O   1 
ATOM   13328 C CB  . THR G  1 247 ? 22.864  19.465   -47.022 1.00 77.72  ? 247 THR G CB  1 
ATOM   13329 O OG1 . THR G  1 247 ? 24.142  19.016   -46.555 1.00 89.85  ? 247 THR G OG1 1 
ATOM   13330 C CG2 . THR G  1 247 ? 23.067  20.447   -48.166 1.00 73.80  ? 247 THR G CG2 1 
ATOM   13331 N N   . PHE G  1 248 ? 21.165  22.248   -46.582 1.00 76.41  ? 248 PHE G N   1 
ATOM   13332 C CA  . PHE G  1 248 ? 20.214  23.131   -47.244 1.00 74.89  ? 248 PHE G CA  1 
ATOM   13333 C C   . PHE G  1 248 ? 20.825  23.687   -48.525 1.00 70.42  ? 248 PHE G C   1 
ATOM   13334 O O   . PHE G  1 248 ? 21.987  24.091   -48.547 1.00 79.83  ? 248 PHE G O   1 
ATOM   13335 C CB  . PHE G  1 248 ? 19.791  24.269   -46.316 1.00 59.59  ? 248 PHE G CB  1 
ATOM   13336 C CG  . PHE G  1 248 ? 18.928  23.826   -45.171 1.00 56.62  ? 248 PHE G CG  1 
ATOM   13337 C CD1 . PHE G  1 248 ? 19.494  23.277   -44.032 1.00 63.46  ? 248 PHE G CD1 1 
ATOM   13338 C CD2 . PHE G  1 248 ? 17.551  23.957   -45.233 1.00 60.19  ? 248 PHE G CD2 1 
ATOM   13339 C CE1 . PHE G  1 248 ? 18.702  22.866   -42.977 1.00 64.11  ? 248 PHE G CE1 1 
ATOM   13340 C CE2 . PHE G  1 248 ? 16.754  23.549   -44.181 1.00 62.04  ? 248 PHE G CE2 1 
ATOM   13341 C CZ  . PHE G  1 248 ? 17.330  23.002   -43.052 1.00 47.88  ? 248 PHE G CZ  1 
ATOM   13342 N N   . GLU G  1 249 ? 20.032  23.700   -49.590 1.00 61.43  ? 249 GLU G N   1 
ATOM   13343 C CA  . GLU G  1 249 ? 20.495  24.156   -50.893 1.00 70.10  ? 249 GLU G CA  1 
ATOM   13344 C C   . GLU G  1 249 ? 19.349  24.841   -51.624 1.00 74.47  ? 249 GLU G C   1 
ATOM   13345 O O   . GLU G  1 249 ? 18.350  24.205   -51.956 1.00 82.83  ? 249 GLU G O   1 
ATOM   13346 C CB  . GLU G  1 249 ? 21.013  22.969   -51.705 1.00 78.76  ? 249 GLU G CB  1 
ATOM   13347 C CG  . GLU G  1 249 ? 21.523  23.318   -53.091 1.00 94.48  ? 249 GLU G CG  1 
ATOM   13348 C CD  . GLU G  1 249 ? 22.086  22.111   -53.817 1.00 105.72 ? 249 GLU G CD  1 
ATOM   13349 O OE1 . GLU G  1 249 ? 22.124  22.129   -55.065 1.00 112.99 ? 249 GLU G OE1 1 
ATOM   13350 O OE2 . GLU G  1 249 ? 22.486  21.141   -53.138 1.00 92.00  ? 249 GLU G OE2 1 
ATOM   13351 N N   . ALA G  1 250 ? 19.490  26.139   -51.872 1.00 71.20  ? 250 ALA G N   1 
ATOM   13352 C CA  . ALA G  1 250 ? 18.391  26.909   -52.443 1.00 67.17  ? 250 ALA G CA  1 
ATOM   13353 C C   . ALA G  1 250 ? 18.839  27.994   -53.416 1.00 78.48  ? 250 ALA G C   1 
ATOM   13354 O O   . ALA G  1 250 ? 19.881  28.624   -53.234 1.00 77.27  ? 250 ALA G O   1 
ATOM   13355 C CB  . ALA G  1 250 ? 17.546  27.517   -51.331 1.00 70.02  ? 250 ALA G CB  1 
ATOM   13356 N N   . THR G  1 251 ? 18.035  28.198   -54.454 1.00 69.32  ? 251 THR G N   1 
ATOM   13357 C CA  . THR G  1 251 ? 18.213  29.318   -55.366 1.00 74.45  ? 251 THR G CA  1 
ATOM   13358 C C   . THR G  1 251 ? 17.145  30.364   -55.071 1.00 81.26  ? 251 THR G C   1 
ATOM   13359 O O   . THR G  1 251 ? 16.902  31.269   -55.871 1.00 71.63  ? 251 THR G O   1 
ATOM   13360 C CB  . THR G  1 251 ? 18.113  28.875   -56.836 1.00 71.14  ? 251 THR G CB  1 
ATOM   13361 O OG1 . THR G  1 251 ? 16.944  28.067   -57.014 1.00 70.39  ? 251 THR G OG1 1 
ATOM   13362 C CG2 . THR G  1 251 ? 19.338  28.068   -57.231 1.00 71.83  ? 251 THR G CG2 1 
ATOM   13363 N N   . GLY G  1 252 ? 16.507  30.226   -53.911 1.00 82.63  ? 252 GLY G N   1 
ATOM   13364 C CA  . GLY G  1 252 ? 15.478  31.153   -53.480 1.00 76.93  ? 252 GLY G CA  1 
ATOM   13365 C C   . GLY G  1 252 ? 14.319  30.469   -52.780 1.00 72.30  ? 252 GLY G C   1 
ATOM   13366 O O   . GLY G  1 252 ? 14.233  29.241   -52.758 1.00 74.57  ? 252 GLY G O   1 
ATOM   13367 N N   . ASN G  1 253 ? 13.433  31.272   -52.197 1.00 74.63  ? 253 ASN G N   1 
ATOM   13368 C CA  . ASN G  1 253 ? 12.198  30.773   -51.596 1.00 67.48  ? 253 ASN G CA  1 
ATOM   13369 C C   . ASN G  1 253 ? 12.403  29.958   -50.320 1.00 61.63  ? 253 ASN G C   1 
ATOM   13370 O O   . ASN G  1 253 ? 11.473  29.311   -49.838 1.00 68.41  ? 253 ASN G O   1 
ATOM   13371 C CB  . ASN G  1 253 ? 11.400  29.951   -52.613 1.00 66.77  ? 253 ASN G CB  1 
ATOM   13372 C CG  . ASN G  1 253 ? 11.122  30.715   -53.894 1.00 61.54  ? 253 ASN G CG  1 
ATOM   13373 O OD1 . ASN G  1 253 ? 9.982   31.080   -54.176 1.00 66.80  ? 253 ASN G OD1 1 
ATOM   13374 N ND2 . ASN G  1 253 ? 12.166  30.960   -54.676 1.00 68.81  ? 253 ASN G ND2 1 
ATOM   13375 N N   . LEU G  1 254 ? 13.613  29.994   -49.772 1.00 63.90  ? 254 LEU G N   1 
ATOM   13376 C CA  . LEU G  1 254 ? 13.926  29.205   -48.585 1.00 61.64  ? 254 LEU G CA  1 
ATOM   13377 C C   . LEU G  1 254 ? 13.949  30.031   -47.302 1.00 58.86  ? 254 LEU G C   1 
ATOM   13378 O O   . LEU G  1 254 ? 14.837  30.858   -47.095 1.00 76.48  ? 254 LEU G O   1 
ATOM   13379 C CB  . LEU G  1 254 ? 15.258  28.470   -48.753 1.00 65.04  ? 254 LEU G CB  1 
ATOM   13380 C CG  . LEU G  1 254 ? 15.756  27.697   -47.529 1.00 57.63  ? 254 LEU G CG  1 
ATOM   13381 C CD1 . LEU G  1 254 ? 14.749  26.640   -47.106 1.00 63.25  ? 254 LEU G CD1 1 
ATOM   13382 C CD2 . LEU G  1 254 ? 17.108  27.064   -47.804 1.00 56.26  ? 254 LEU G CD2 1 
ATOM   13383 N N   . VAL G  1 255 ? 12.960  29.794   -46.448 1.00 51.76  ? 255 VAL G N   1 
ATOM   13384 C CA  . VAL G  1 255 ? 12.924  30.368   -45.112 1.00 53.21  ? 255 VAL G CA  1 
ATOM   13385 C C   . VAL G  1 255 ? 13.830  29.512   -44.223 1.00 54.68  ? 255 VAL G C   1 
ATOM   13386 O O   . VAL G  1 255 ? 13.398  28.500   -43.670 1.00 63.30  ? 255 VAL G O   1 
ATOM   13387 C CB  . VAL G  1 255 ? 11.467  30.401   -44.584 1.00 49.73  ? 255 VAL G CB  1 
ATOM   13388 C CG1 . VAL G  1 255 ? 11.383  31.003   -43.202 1.00 60.62  ? 255 VAL G CG1 1 
ATOM   13389 C CG2 . VAL G  1 255 ? 10.589  31.195   -45.535 1.00 48.24  ? 255 VAL G CG2 1 
ATOM   13390 N N   . VAL G  1 256 ? 15.096  29.912   -44.110 1.00 58.93  ? 256 VAL G N   1 
ATOM   13391 C CA  . VAL G  1 256 ? 16.116  29.093   -43.454 1.00 59.98  ? 256 VAL G CA  1 
ATOM   13392 C C   . VAL G  1 256 ? 15.969  29.034   -41.937 1.00 58.32  ? 256 VAL G C   1 
ATOM   13393 O O   . VAL G  1 256 ? 15.464  29.968   -41.318 1.00 69.65  ? 256 VAL G O   1 
ATOM   13394 C CB  . VAL G  1 256 ? 17.542  29.587   -43.783 1.00 69.22  ? 256 VAL G CB  1 
ATOM   13395 C CG1 . VAL G  1 256 ? 17.765  29.607   -45.286 1.00 66.38  ? 256 VAL G CG1 1 
ATOM   13396 C CG2 . VAL G  1 256 ? 17.783  30.963   -43.179 1.00 78.95  ? 256 VAL G CG2 1 
ATOM   13397 N N   . PRO G  1 257 ? 16.416  27.923   -41.333 1.00 60.10  ? 257 PRO G N   1 
ATOM   13398 C CA  . PRO G  1 257 ? 16.402  27.761   -39.877 1.00 61.37  ? 257 PRO G CA  1 
ATOM   13399 C C   . PRO G  1 257 ? 17.362  28.731   -39.202 1.00 65.55  ? 257 PRO G C   1 
ATOM   13400 O O   . PRO G  1 257 ? 18.422  29.025   -39.749 1.00 71.72  ? 257 PRO G O   1 
ATOM   13401 C CB  . PRO G  1 257 ? 16.907  26.328   -39.678 1.00 55.86  ? 257 PRO G CB  1 
ATOM   13402 C CG  . PRO G  1 257 ? 16.673  25.647   -40.978 1.00 61.77  ? 257 PRO G CG  1 
ATOM   13403 C CD  . PRO G  1 257 ? 16.863  26.700   -42.020 1.00 56.34  ? 257 PRO G CD  1 
ATOM   13404 N N   . ARG G  1 258 ? 16.993  29.222   -38.027 1.00 76.79  ? 258 ARG G N   1 
ATOM   13405 C CA  . ARG G  1 258 ? 17.896  30.052   -37.246 1.00 73.00  ? 258 ARG G CA  1 
ATOM   13406 C C   . ARG G  1 258 ? 18.229  29.334   -35.955 1.00 64.06  ? 258 ARG G C   1 
ATOM   13407 O O   . ARG G  1 258 ? 19.396  29.151   -35.607 1.00 70.15  ? 258 ARG G O   1 
ATOM   13408 C CB  . ARG G  1 258 ? 17.248  31.392   -36.924 1.00 75.35  ? 258 ARG G CB  1 
ATOM   13409 C CG  . ARG G  1 258 ? 18.036  32.578   -37.416 1.00 75.60  ? 258 ARG G CG  1 
ATOM   13410 C CD  . ARG G  1 258 ? 17.804  33.792   -36.543 1.00 86.63  ? 258 ARG G CD  1 
ATOM   13411 N NE  . ARG G  1 258 ? 18.647  33.776   -35.353 1.00 92.41  ? 258 ARG G NE  1 
ATOM   13412 C CZ  . ARG G  1 258 ? 19.102  34.872   -34.757 1.00 96.58  ? 258 ARG G CZ  1 
ATOM   13413 N NH1 . ARG G  1 258 ? 18.796  36.063   -35.247 1.00 89.56  ? 258 ARG G NH1 1 
ATOM   13414 N NH2 . ARG G  1 258 ? 19.865  34.781   -33.677 1.00 95.14  ? 258 ARG G NH2 1 
ATOM   13415 N N   . TYR G  1 259 ? 17.183  28.937   -35.244 1.00 68.31  ? 259 TYR G N   1 
ATOM   13416 C CA  . TYR G  1 259 ? 17.336  28.181   -34.016 1.00 62.17  ? 259 TYR G CA  1 
ATOM   13417 C C   . TYR G  1 259 ? 16.824  26.767   -34.228 1.00 63.86  ? 259 TYR G C   1 
ATOM   13418 O O   . TYR G  1 259 ? 15.789  26.560   -34.862 1.00 67.63  ? 259 TYR G O   1 
ATOM   13419 C CB  . TYR G  1 259 ? 16.566  28.852   -32.877 1.00 67.20  ? 259 TYR G CB  1 
ATOM   13420 C CG  . TYR G  1 259 ? 17.195  30.136   -32.385 1.00 89.62  ? 259 TYR G CG  1 
ATOM   13421 C CD1 . TYR G  1 259 ? 16.888  31.356   -32.974 1.00 82.06  ? 259 TYR G CD1 1 
ATOM   13422 C CD2 . TYR G  1 259 ? 18.096  30.127   -31.329 1.00 89.09  ? 259 TYR G CD2 1 
ATOM   13423 C CE1 . TYR G  1 259 ? 17.463  32.530   -32.525 1.00 86.03  ? 259 TYR G CE1 1 
ATOM   13424 C CE2 . TYR G  1 259 ? 18.676  31.295   -30.874 1.00 87.63  ? 259 TYR G CE2 1 
ATOM   13425 C CZ  . TYR G  1 259 ? 18.357  32.493   -31.475 1.00 87.76  ? 259 TYR G CZ  1 
ATOM   13426 O OH  . TYR G  1 259 ? 18.935  33.655   -31.019 1.00 103.97 ? 259 TYR G OH  1 
ATOM   13427 N N   . ALA G  1 260 ? 17.568  25.796   -33.712 1.00 64.21  ? 260 ALA G N   1 
ATOM   13428 C CA  . ALA G  1 260 ? 17.115  24.414   -33.682 1.00 61.33  ? 260 ALA G CA  1 
ATOM   13429 C C   . ALA G  1 260 ? 16.887  24.034   -32.226 1.00 63.86  ? 260 ALA G C   1 
ATOM   13430 O O   . ALA G  1 260 ? 16.995  24.880   -31.341 1.00 61.33  ? 260 ALA G O   1 
ATOM   13431 C CB  . ALA G  1 260 ? 18.143  23.499   -34.325 1.00 57.49  ? 260 ALA G CB  1 
ATOM   13432 N N   . PHE G  1 261 ? 16.580  22.767   -31.975 1.00 73.50  ? 261 PHE G N   1 
ATOM   13433 C CA  . PHE G  1 261 ? 16.272  22.307   -30.625 1.00 57.63  ? 261 PHE G CA  1 
ATOM   13434 C C   . PHE G  1 261 ? 16.917  20.966   -30.280 1.00 62.65  ? 261 PHE G C   1 
ATOM   13435 O O   . PHE G  1 261 ? 16.419  19.912   -30.673 1.00 70.89  ? 261 PHE G O   1 
ATOM   13436 C CB  . PHE G  1 261 ? 14.759  22.203   -30.447 1.00 49.52  ? 261 PHE G CB  1 
ATOM   13437 C CG  . PHE G  1 261 ? 14.040  23.498   -30.665 1.00 57.09  ? 261 PHE G CG  1 
ATOM   13438 C CD1 . PHE G  1 261 ? 13.519  23.817   -31.907 1.00 60.56  ? 261 PHE G CD1 1 
ATOM   13439 C CD2 . PHE G  1 261 ? 13.899  24.405   -29.630 1.00 59.48  ? 261 PHE G CD2 1 
ATOM   13440 C CE1 . PHE G  1 261 ? 12.862  25.014   -32.109 1.00 63.98  ? 261 PHE G CE1 1 
ATOM   13441 C CE2 . PHE G  1 261 ? 13.244  25.602   -29.824 1.00 51.36  ? 261 PHE G CE2 1 
ATOM   13442 C CZ  . PHE G  1 261 ? 12.725  25.908   -31.065 1.00 59.36  ? 261 PHE G CZ  1 
ATOM   13443 N N   . ALA G  1 262 ? 18.025  21.008   -29.546 1.00 68.99  ? 262 ALA G N   1 
ATOM   13444 C CA  . ALA G  1 262 ? 18.617  19.790   -29.008 1.00 58.68  ? 262 ALA G CA  1 
ATOM   13445 C C   . ALA G  1 262 ? 17.592  19.141   -28.085 1.00 66.91  ? 262 ALA G C   1 
ATOM   13446 O O   . ALA G  1 262 ? 17.026  19.803   -27.213 1.00 72.84  ? 262 ALA G O   1 
ATOM   13447 C CB  . ALA G  1 262 ? 19.899  20.103   -28.257 1.00 81.91  ? 262 ALA G CB  1 
ATOM   13448 N N   . MET G  1 263 ? 17.349  17.849   -28.276 1.00 66.43  ? 263 MET G N   1 
ATOM   13449 C CA  . MET G  1 263 ? 16.190  17.214   -27.660 1.00 72.08  ? 263 MET G CA  1 
ATOM   13450 C C   . MET G  1 263 ? 16.405  15.760   -27.264 1.00 71.32  ? 263 MET G C   1 
ATOM   13451 O O   . MET G  1 263 ? 17.169  15.034   -27.898 1.00 79.26  ? 263 MET G O   1 
ATOM   13452 C CB  . MET G  1 263 ? 15.010  17.275   -28.627 1.00 64.55  ? 263 MET G CB  1 
ATOM   13453 C CG  . MET G  1 263 ? 13.770  17.941   -28.079 1.00 68.23  ? 263 MET G CG  1 
ATOM   13454 S SD  . MET G  1 263 ? 12.423  17.806   -29.270 1.00 88.94  ? 263 MET G SD  1 
ATOM   13455 C CE  . MET G  1 263 ? 13.353  17.410   -30.752 1.00 70.49  ? 263 MET G CE  1 
ATOM   13456 N N   . GLU G  1 264 ? 15.712  15.344   -26.212 1.00 70.57  ? 264 GLU G N   1 
ATOM   13457 C CA  . GLU G  1 264 ? 15.595  13.938   -25.864 1.00 73.32  ? 264 GLU G CA  1 
ATOM   13458 C C   . GLU G  1 264 ? 14.157  13.704   -25.449 1.00 75.45  ? 264 GLU G C   1 
ATOM   13459 O O   . GLU G  1 264 ? 13.712  14.201   -24.419 1.00 77.75  ? 264 GLU G O   1 
ATOM   13460 C CB  . GLU G  1 264 ? 16.548  13.569   -24.729 1.00 77.00  ? 264 GLU G CB  1 
ATOM   13461 C CG  . GLU G  1 264 ? 17.723  12.717   -25.170 1.00 98.61  ? 264 GLU G CG  1 
ATOM   13462 C CD  . GLU G  1 264 ? 18.909  12.834   -24.236 1.00 112.13 ? 264 GLU G CD  1 
ATOM   13463 O OE1 . GLU G  1 264 ? 19.504  11.792   -23.891 1.00 114.41 ? 264 GLU G OE1 1 
ATOM   13464 O OE2 . GLU G  1 264 ? 19.247  13.970   -23.845 1.00 115.95 ? 264 GLU G OE2 1 
ATOM   13465 N N   . ARG G  1 265 ? 13.425  12.964   -26.270 1.00 73.77  ? 265 ARG G N   1 
ATOM   13466 C CA  . ARG G  1 265 ? 12.015  12.725   -26.022 1.00 81.36  ? 265 ARG G CA  1 
ATOM   13467 C C   . ARG G  1 265 ? 11.774  11.308   -25.520 1.00 82.30  ? 265 ARG G C   1 
ATOM   13468 O O   . ARG G  1 265 ? 12.377  10.351   -26.011 1.00 73.28  ? 265 ARG G O   1 
ATOM   13469 C CB  . ARG G  1 265 ? 11.209  12.982   -27.297 1.00 69.25  ? 265 ARG G CB  1 
ATOM   13470 C CG  . ARG G  1 265 ? 11.939  12.579   -28.573 1.00 73.43  ? 265 ARG G CG  1 
ATOM   13471 C CD  . ARG G  1 265 ? 11.104  12.862   -29.810 1.00 79.26  ? 265 ARG G CD  1 
ATOM   13472 N NE  . ARG G  1 265 ? 10.526  11.644   -30.371 1.00 84.50  ? 265 ARG G NE  1 
ATOM   13473 C CZ  . ARG G  1 265 ? 11.116  10.903   -31.303 1.00 81.10  ? 265 ARG G CZ  1 
ATOM   13474 N NH1 . ARG G  1 265 ? 12.302  11.256   -31.779 1.00 78.63  ? 265 ARG G NH1 1 
ATOM   13475 N NH2 . ARG G  1 265 ? 10.523  9.809    -31.761 1.00 80.58  ? 265 ARG G NH2 1 
ATOM   13476 N N   . ASN G  1 266 ? 10.914  11.189   -24.513 1.00 85.12  ? 266 ASN G N   1 
ATOM   13477 C CA  . ASN G  1 266 ? 10.343  9.906    -24.120 1.00 95.29  ? 266 ASN G CA  1 
ATOM   13478 C C   . ASN G  1 266 ? 9.099   9.695    -24.956 1.00 94.91  ? 266 ASN G C   1 
ATOM   13479 O O   . ASN G  1 266 ? 8.601   10.630   -25.578 1.00 97.61  ? 266 ASN G O   1 
ATOM   13480 C CB  . ASN G  1 266 ? 9.949   9.918    -22.641 1.00 99.86  ? 266 ASN G CB  1 
ATOM   13481 C CG  . ASN G  1 266 ? 10.116  11.283   -22.009 1.00 89.24  ? 266 ASN G CG  1 
ATOM   13482 O OD1 . ASN G  1 266 ? 11.084  11.525   -21.293 1.00 78.63  ? 266 ASN G OD1 1 
ATOM   13483 N ND2 . ASN G  1 266 ? 9.174   12.184   -22.273 1.00 82.87  ? 266 ASN G ND2 1 
ATOM   13484 N N   . ALA G  1 267 ? 8.525   8.496    -24.890 1.00 84.01  ? 267 ALA G N   1 
ATOM   13485 C CA  . ALA G  1 267 ? 7.320   8.204    -25.667 1.00 97.72  ? 267 ALA G CA  1 
ATOM   13486 C C   . ALA G  1 267 ? 6.070   7.761    -24.885 1.00 93.63  ? 267 ALA G C   1 
ATOM   13487 O O   . ALA G  1 267 ? 5.787   6.566    -24.791 1.00 89.41  ? 267 ALA G O   1 
ATOM   13488 C CB  . ALA G  1 267 ? 7.639   7.190    -26.765 1.00 97.10  ? 267 ALA G CB  1 
ATOM   13489 N N   . GLY G  1 268 ? 5.317   8.723    -24.353 1.00 116.26 ? 268 GLY G N   1 
ATOM   13490 C CA  . GLY G  1 268 ? 3.949   8.496    -23.959 1.00 118.33 ? 268 GLY G CA  1 
ATOM   13491 C C   . GLY G  1 268 ? 2.983   9.628    -24.210 1.00 124.69 ? 268 GLY G C   1 
ATOM   13492 O O   . GLY G  1 268 ? 2.165   9.572    -25.115 1.00 126.56 ? 268 GLY G O   1 
ATOM   13493 N N   . SER G  1 269 ? 3.124   10.668   -23.400 1.00 81.82  ? 269 SER G N   1 
ATOM   13494 C CA  . SER G  1 269 ? 2.093   11.649   -23.117 1.00 68.80  ? 269 SER G CA  1 
ATOM   13495 C C   . SER G  1 269 ? 1.536   12.363   -24.310 1.00 71.51  ? 269 SER G C   1 
ATOM   13496 O O   . SER G  1 269 ? 1.961   12.214   -25.436 1.00 77.50  ? 269 SER G O   1 
ATOM   13497 C CB  . SER G  1 269 ? 2.679   12.860   -22.500 1.00 66.87  ? 269 SER G CB  1 
ATOM   13498 O OG  . SER G  1 269 ? 1.757   13.894   -22.702 1.00 66.45  ? 269 SER G OG  1 
ATOM   13499 N N   . GLY G  1 270 ? 0.526   13.151   -24.007 1.00 55.07  ? 270 GLY G N   1 
ATOM   13500 C CA  . GLY G  1 270 ? -0.019  14.144   -24.918 1.00 61.26  ? 270 GLY G CA  1 
ATOM   13501 C C   . GLY G  1 270 ? -0.362  15.538   -24.488 1.00 55.97  ? 270 GLY G C   1 
ATOM   13502 O O   . GLY G  1 270 ? 0.106   15.987   -23.444 1.00 54.37  ? 270 GLY G O   1 
ATOM   13503 N N   . ILE G  1 271 ? -1.180  16.226   -25.278 1.00 50.73  ? 271 ILE G N   1 
ATOM   13504 C CA  . ILE G  1 271 ? -1.484  17.634   -25.046 1.00 42.49  ? 271 ILE G CA  1 
ATOM   13505 C C   . ILE G  1 271 ? -2.938  17.840   -24.611 1.00 55.04  ? 271 ILE G C   1 
ATOM   13506 O O   . ILE G  1 271 ? -3.863  17.380   -25.284 1.00 67.58  ? 271 ILE G O   1 
ATOM   13507 C CB  . ILE G  1 271 ? -1.209  18.458   -26.323 1.00 44.29  ? 271 ILE G CB  1 
ATOM   13508 C CG1 . ILE G  1 271 ? 0.155   18.086   -26.907 1.00 43.34  ? 271 ILE G CG1 1 
ATOM   13509 C CG2 . ILE G  1 271 ? -1.279  19.946   -26.032 1.00 56.50  ? 271 ILE G CG2 1 
ATOM   13510 C CD1 . ILE G  1 271 ? 0.120   17.710   -28.374 1.00 53.88  ? 271 ILE G CD1 1 
ATOM   13511 N N   . ILE G  1 272 ? -3.133  18.527   -23.487 1.00 54.26  ? 272 ILE G N   1 
ATOM   13512 C CA  . ILE G  1 272 ? -4.476  18.811   -22.985 1.00 62.75  ? 272 ILE G CA  1 
ATOM   13513 C C   . ILE G  1 272 ? -4.912  20.220   -23.374 1.00 60.39  ? 272 ILE G C   1 
ATOM   13514 O O   . ILE G  1 272 ? -4.197  21.189   -23.120 1.00 57.58  ? 272 ILE G O   1 
ATOM   13515 C CB  . ILE G  1 272 ? -4.551  18.671   -21.451 1.00 58.31  ? 272 ILE G CB  1 
ATOM   13516 C CG1 . ILE G  1 272 ? -4.280  17.225   -21.033 1.00 62.65  ? 272 ILE G CG1 1 
ATOM   13517 C CG2 . ILE G  1 272 ? -5.910  19.128   -20.930 1.00 61.04  ? 272 ILE G CG2 1 
ATOM   13518 C CD1 . ILE G  1 272 ? -4.356  16.989   -19.541 1.00 63.13  ? 272 ILE G CD1 1 
ATOM   13519 N N   . ILE G  1 273 ? -6.080  20.333   -23.998 1.00 60.08  ? 273 ILE G N   1 
ATOM   13520 C CA  . ILE G  1 273 ? -6.634  21.643   -24.317 1.00 66.37  ? 273 ILE G CA  1 
ATOM   13521 C C   . ILE G  1 273 ? -7.636  22.037   -23.238 1.00 73.22  ? 273 ILE G C   1 
ATOM   13522 O O   . ILE G  1 273 ? -8.769  21.558   -23.226 1.00 72.57  ? 273 ILE G O   1 
ATOM   13523 C CB  . ILE G  1 273 ? -7.316  21.677   -25.700 1.00 67.32  ? 273 ILE G CB  1 
ATOM   13524 C CG1 . ILE G  1 273 ? -6.316  21.339   -26.811 1.00 65.76  ? 273 ILE G CG1 1 
ATOM   13525 C CG2 . ILE G  1 273 ? -7.933  23.045   -25.952 1.00 69.69  ? 273 ILE G CG2 1 
ATOM   13526 C CD1 . ILE G  1 273 ? -6.051  19.858   -26.980 1.00 84.99  ? 273 ILE G CD1 1 
ATOM   13527 N N   . SER G  1 274 ? -7.207  22.910   -22.331 1.00 75.33  ? 274 SER G N   1 
ATOM   13528 C CA  . SER G  1 274 ? -8.019  23.270   -21.173 1.00 74.69  ? 274 SER G CA  1 
ATOM   13529 C C   . SER G  1 274 ? -7.749  24.689   -20.672 1.00 78.78  ? 274 SER G C   1 
ATOM   13530 O O   . SER G  1 274 ? -6.668  25.238   -20.882 1.00 77.23  ? 274 SER G O   1 
ATOM   13531 C CB  . SER G  1 274 ? -7.784  22.268   -20.041 1.00 67.98  ? 274 SER G CB  1 
ATOM   13532 O OG  . SER G  1 274 ? -8.223  22.789   -18.799 1.00 74.53  ? 274 SER G OG  1 
ATOM   13533 N N   . ASP G  1 275 ? -8.744  25.271   -20.006 1.00 101.99 ? 275 ASP G N   1 
ATOM   13534 C CA  . ASP G  1 275 ? -8.609  26.590   -19.396 1.00 98.07  ? 275 ASP G CA  1 
ATOM   13535 C C   . ASP G  1 275 ? -8.119  26.460   -17.955 1.00 85.11  ? 275 ASP G C   1 
ATOM   13536 O O   . ASP G  1 275 ? -7.637  27.425   -17.361 1.00 92.72  ? 275 ASP G O   1 
ATOM   13537 C CB  . ASP G  1 275 ? -9.950  27.330   -19.410 1.00 116.04 ? 275 ASP G CB  1 
ATOM   13538 C CG  . ASP G  1 275 ? -10.498 27.530   -20.810 1.00 131.01 ? 275 ASP G CG  1 
ATOM   13539 O OD1 . ASP G  1 275 ? -11.425 26.786   -21.198 1.00 145.25 ? 275 ASP G OD1 1 
ATOM   13540 O OD2 . ASP G  1 275 ? -10.009 28.433   -21.521 1.00 121.93 ? 275 ASP G OD2 1 
ATOM   13541 N N   . THR G  1 276 ? -8.254  25.257   -17.406 1.00 82.48  ? 276 THR G N   1 
ATOM   13542 C CA  . THR G  1 276 ? -7.891  24.962   -16.020 1.00 78.41  ? 276 THR G CA  1 
ATOM   13543 C C   . THR G  1 276 ? -6.513  25.505   -15.639 1.00 85.08  ? 276 THR G C   1 
ATOM   13544 O O   . THR G  1 276 ? -5.571  25.424   -16.428 1.00 80.54  ? 276 THR G O   1 
ATOM   13545 C CB  . THR G  1 276 ? -7.927  23.437   -15.765 1.00 66.58  ? 276 THR G CB  1 
ATOM   13546 O OG1 . THR G  1 276 ? -9.229  22.929   -16.081 1.00 69.29  ? 276 THR G OG1 1 
ATOM   13547 C CG2 . THR G  1 276 ? -7.594  23.109   -14.316 1.00 68.93  ? 276 THR G CG2 1 
ATOM   13548 N N   . PRO G  1 277 ? -6.395  26.060   -14.420 1.00 87.52  ? 277 PRO G N   1 
ATOM   13549 C CA  . PRO G  1 277 ? -5.143  26.637   -13.914 1.00 76.65  ? 277 PRO G CA  1 
ATOM   13550 C C   . PRO G  1 277 ? -4.013  25.618   -13.778 1.00 76.78  ? 277 PRO G C   1 
ATOM   13551 O O   . PRO G  1 277 ? -4.234  24.520   -13.267 1.00 83.61  ? 277 PRO G O   1 
ATOM   13552 C CB  . PRO G  1 277 ? -5.528  27.137   -12.516 1.00 90.23  ? 277 PRO G CB  1 
ATOM   13553 C CG  . PRO G  1 277 ? -7.012  27.282   -12.545 1.00 103.69 ? 277 PRO G CG  1 
ATOM   13554 C CD  . PRO G  1 277 ? -7.495  26.198   -13.448 1.00 86.44  ? 277 PRO G CD  1 
ATOM   13555 N N   . VAL G  1 278 ? -2.814  25.988   -14.219 1.00 78.70  ? 278 VAL G N   1 
ATOM   13556 C CA  . VAL G  1 278 ? -1.626  25.181   -13.961 1.00 84.40  ? 278 VAL G CA  1 
ATOM   13557 C C   . VAL G  1 278 ? -1.237  25.378   -12.502 1.00 82.57  ? 278 VAL G C   1 
ATOM   13558 O O   . VAL G  1 278 ? -1.345  26.479   -11.970 1.00 92.15  ? 278 VAL G O   1 
ATOM   13559 C CB  . VAL G  1 278 ? -0.448  25.573   -14.881 1.00 75.03  ? 278 VAL G CB  1 
ATOM   13560 C CG1 . VAL G  1 278 ? -0.168  27.066   -14.787 1.00 92.84  ? 278 VAL G CG1 1 
ATOM   13561 C CG2 . VAL G  1 278 ? 0.798   24.764   -14.537 1.00 67.78  ? 278 VAL G CG2 1 
ATOM   13562 N N   . HIS G  1 279 ? -0.799  24.312   -11.845 1.00 81.80  ? 279 HIS G N   1 
ATOM   13563 C CA  . HIS G  1 279 ? -0.526  24.392   -10.415 1.00 84.36  ? 279 HIS G CA  1 
ATOM   13564 C C   . HIS G  1 279 ? 0.762   23.692   -10.004 1.00 89.47  ? 279 HIS G C   1 
ATOM   13565 O O   . HIS G  1 279 ? 1.258   22.809   -10.703 1.00 99.34  ? 279 HIS G O   1 
ATOM   13566 C CB  . HIS G  1 279 ? -1.708  23.833   -9.616  1.00 101.55 ? 279 HIS G CB  1 
ATOM   13567 C CG  . HIS G  1 279 ? -2.574  24.886   -8.998  1.00 106.79 ? 279 HIS G CG  1 
ATOM   13568 N ND1 . HIS G  1 279 ? -2.509  25.212   -7.660  1.00 107.75 ? 279 HIS G ND1 1 
ATOM   13569 C CD2 . HIS G  1 279 ? -3.525  25.690   -9.534  1.00 106.56 ? 279 HIS G CD2 1 
ATOM   13570 C CE1 . HIS G  1 279 ? -3.382  26.168   -7.398  1.00 117.77 ? 279 HIS G CE1 1 
ATOM   13571 N NE2 . HIS G  1 279 ? -4.010  26.476   -8.518  1.00 113.57 ? 279 HIS G NE2 1 
ATOM   13572 N N   . ASP G  1 280 ? 1.301   24.107   -8.864  1.00 95.51  ? 280 ASP G N   1 
ATOM   13573 C CA  . ASP G  1 280 ? 2.442   23.436   -8.262  1.00 101.64 ? 280 ASP G CA  1 
ATOM   13574 C C   . ASP G  1 280 ? 1.938   22.324   -7.351  1.00 106.35 ? 280 ASP G C   1 
ATOM   13575 O O   . ASP G  1 280 ? 1.874   22.488   -6.133  1.00 122.58 ? 280 ASP G O   1 
ATOM   13576 C CB  . ASP G  1 280 ? 3.290   24.428   -7.465  1.00 110.18 ? 280 ASP G CB  1 
ATOM   13577 C CG  . ASP G  1 280 ? 4.428   23.757   -6.719  1.00 134.55 ? 280 ASP G CG  1 
ATOM   13578 O OD1 . ASP G  1 280 ? 4.767   22.605   -7.059  1.00 138.77 ? 280 ASP G OD1 1 
ATOM   13579 O OD2 . ASP G  1 280 ? 4.983   24.382   -5.791  1.00 136.87 ? 280 ASP G OD2 1 
ATOM   13580 N N   . CYS G  1 281 ? 1.568   21.196   -7.951  1.00 104.51 ? 281 CYS G N   1 
ATOM   13581 C CA  . CYS G  1 281 ? 1.055   20.057   -7.196  1.00 102.97 ? 281 CYS G CA  1 
ATOM   13582 C C   . CYS G  1 281 ? 1.437   18.726   -7.846  1.00 98.88  ? 281 CYS G C   1 
ATOM   13583 O O   . CYS G  1 281 ? 1.773   18.677   -9.029  1.00 100.62 ? 281 CYS G O   1 
ATOM   13584 C CB  . CYS G  1 281 ? -0.466  20.158   -7.041  1.00 90.40  ? 281 CYS G CB  1 
ATOM   13585 S SG  . CYS G  1 281 ? -1.377  20.271   -8.599  1.00 126.72 ? 281 CYS G SG  1 
ATOM   13586 N N   . ASN G  1 282 ? 1.390   17.654   -7.058  1.00 89.14  ? 282 ASN G N   1 
ATOM   13587 C CA  . ASN G  1 282 ? 1.689   16.309   -7.544  1.00 81.89  ? 282 ASN G CA  1 
ATOM   13588 C C   . ASN G  1 282 ? 0.409   15.540   -7.889  1.00 86.22  ? 282 ASN G C   1 
ATOM   13589 O O   . ASN G  1 282 ? -0.583  15.620   -7.166  1.00 86.07  ? 282 ASN G O   1 
ATOM   13590 C CB  . ASN G  1 282 ? 2.506   15.530   -6.499  1.00 88.07  ? 282 ASN G CB  1 
ATOM   13591 C CG  . ASN G  1 282 ? 3.982   15.403   -6.871  1.00 109.54 ? 282 ASN G CG  1 
ATOM   13592 O OD1 . ASN G  1 282 ? 4.327   15.291   -8.045  1.00 109.21 ? 282 ASN G OD1 1 
ATOM   13593 N ND2 . ASN G  1 282 ? 4.858   15.417   -5.864  1.00 137.65 ? 282 ASN G ND2 1 
ATOM   13594 N N   . THR G  1 283 ? 0.433   14.806   -8.999  1.00 80.38  ? 283 THR G N   1 
ATOM   13595 C CA  . THR G  1 283 ? -0.675  13.934   -9.384  1.00 71.00  ? 283 THR G CA  1 
ATOM   13596 C C   . THR G  1 283 ? -0.156  12.731   -10.163 1.00 64.06  ? 283 THR G C   1 
ATOM   13597 O O   . THR G  1 283 ? 0.915   12.788   -10.760 1.00 74.67  ? 283 THR G O   1 
ATOM   13598 C CB  . THR G  1 283 ? -1.724  14.669   -10.248 1.00 64.36  ? 283 THR G CB  1 
ATOM   13599 O OG1 . THR G  1 283 ? -2.902  13.861   -10.366 1.00 59.02  ? 283 THR G OG1 1 
ATOM   13600 C CG2 . THR G  1 283 ? -1.178  14.950   -11.637 1.00 63.49  ? 283 THR G CG2 1 
ATOM   13601 N N   . THR G  1 284 ? -0.916  11.641   -10.153 1.00 60.14  ? 284 THR G N   1 
ATOM   13602 C CA  . THR G  1 284 ? -0.555  10.449   -10.911 1.00 64.62  ? 284 THR G CA  1 
ATOM   13603 C C   . THR G  1 284 ? -1.490  10.284   -12.104 1.00 68.22  ? 284 THR G C   1 
ATOM   13604 O O   . THR G  1 284 ? -1.262  9.451    -12.983 1.00 61.30  ? 284 THR G O   1 
ATOM   13605 C CB  . THR G  1 284 ? -0.618  9.184    -10.036 1.00 61.87  ? 284 THR G CB  1 
ATOM   13606 O OG1 . THR G  1 284 ? -0.021  8.084    -10.735 1.00 69.48  ? 284 THR G OG1 1 
ATOM   13607 N N   . CYS G  1 285 ? -2.545  11.092   -12.125 1.00 54.49  ? 285 CYS G N   1 
ATOM   13608 C CA  . CYS G  1 285 ? -3.537  11.049   -13.191 1.00 55.75  ? 285 CYS G CA  1 
ATOM   13609 C C   . CYS G  1 285 ? -4.070  12.451   -13.472 1.00 53.45  ? 285 CYS G C   1 
ATOM   13610 O O   . CYS G  1 285 ? -4.529  13.142   -12.562 1.00 54.91  ? 285 CYS G O   1 
ATOM   13611 C CB  . CYS G  1 285 ? -4.684  10.110   -12.811 1.00 50.40  ? 285 CYS G CB  1 
ATOM   13612 S SG  . CYS G  1 285 ? -6.014  10.018   -14.028 1.00 71.33  ? 285 CYS G SG  1 
ATOM   13613 N N   . GLN G  1 286 ? -4.008  12.865   -14.734 1.00 53.39  ? 286 GLN G N   1 
ATOM   13614 C CA  . GLN G  1 286 ? -4.398  14.219   -15.112 1.00 53.73  ? 286 GLN G CA  1 
ATOM   13615 C C   . GLN G  1 286 ? -5.521  14.246   -16.148 1.00 54.97  ? 286 GLN G C   1 
ATOM   13616 O O   . GLN G  1 286 ? -5.462  13.550   -17.162 1.00 61.96  ? 286 GLN G O   1 
ATOM   13617 C CB  . GLN G  1 286 ? -3.187  14.992   -15.639 1.00 48.74  ? 286 GLN G CB  1 
ATOM   13618 C CG  . GLN G  1 286 ? -3.458  16.463   -15.892 1.00 53.42  ? 286 GLN G CG  1 
ATOM   13619 C CD  . GLN G  1 286 ? -3.845  17.201   -14.627 1.00 64.58  ? 286 GLN G CD  1 
ATOM   13620 O OE1 . GLN G  1 286 ? -3.075  17.258   -13.668 1.00 62.42  ? 286 GLN G OE1 1 
ATOM   13621 N NE2 . GLN G  1 286 ? -5.044  17.770   -14.618 1.00 42.71  ? 286 GLN G NE2 1 
ATOM   13622 N N   . THR G  1 287 ? -6.541  15.056   -15.883 1.00 45.15  ? 287 THR G N   1 
ATOM   13623 C CA  . THR G  1 287 ? -7.633  15.257   -16.827 1.00 50.53  ? 287 THR G CA  1 
ATOM   13624 C C   . THR G  1 287 ? -7.724  16.736   -17.191 1.00 50.64  ? 287 THR G C   1 
ATOM   13625 O O   . THR G  1 287 ? -7.208  17.587   -16.468 1.00 60.90  ? 287 THR G O   1 
ATOM   13626 C CB  . THR G  1 287 ? -8.986  14.805   -16.243 1.00 57.91  ? 287 THR G CB  1 
ATOM   13627 O OG1 . THR G  1 287 ? -9.617  15.906   -15.576 1.00 41.53  ? 287 THR G OG1 1 
ATOM   13628 C CG2 . THR G  1 287 ? -8.796  13.652   -15.267 1.00 49.17  ? 287 THR G CG2 1 
ATOM   13629 N N   . PRO G  1 288 ? -8.377  17.046   -18.321 1.00 49.77  ? 288 PRO G N   1 
ATOM   13630 C CA  . PRO G  1 288 ? -8.564  18.437   -18.747 1.00 52.23  ? 288 PRO G CA  1 
ATOM   13631 C C   . PRO G  1 288 ? -9.293  19.282   -17.703 1.00 60.69  ? 288 PRO G C   1 
ATOM   13632 O O   . PRO G  1 288 ? -9.098  20.496   -17.654 1.00 59.14  ? 288 PRO G O   1 
ATOM   13633 C CB  . PRO G  1 288 ? -9.426  18.300   -20.004 1.00 63.72  ? 288 PRO G CB  1 
ATOM   13634 C CG  . PRO G  1 288 ? -9.102  16.947   -20.532 1.00 56.35  ? 288 PRO G CG  1 
ATOM   13635 C CD  . PRO G  1 288 ? -8.875  16.089   -19.324 1.00 54.62  ? 288 PRO G CD  1 
ATOM   13636 N N   . LYS G  1 289 ? -10.121 18.644   -16.882 1.00 65.87  ? 289 LYS G N   1 
ATOM   13637 C CA  . LYS G  1 289 ? -10.910 19.356   -15.881 1.00 63.61  ? 289 LYS G CA  1 
ATOM   13638 C C   . LYS G  1 289 ? -10.141 19.536   -14.574 1.00 59.85  ? 289 LYS G C   1 
ATOM   13639 O O   . LYS G  1 289 ? -10.371 20.492   -13.833 1.00 58.69  ? 289 LYS G O   1 
ATOM   13640 C CB  . LYS G  1 289 ? -12.228 18.621   -15.622 1.00 62.86  ? 289 LYS G CB  1 
ATOM   13641 C CG  . LYS G  1 289 ? -13.080 18.440   -16.870 1.00 77.09  ? 289 LYS G CG  1 
ATOM   13642 C CD  . LYS G  1 289 ? -14.244 17.486   -16.638 1.00 76.29  ? 289 LYS G CD  1 
ATOM   13643 C CE  . LYS G  1 289 ? -15.317 18.103   -15.757 1.00 85.11  ? 289 LYS G CE  1 
ATOM   13644 N NZ  . LYS G  1 289 ? -16.522 17.230   -15.675 1.00 90.31  ? 289 LYS G NZ  1 
ATOM   13645 N N   . GLY G  1 290 ? -9.226  18.612   -14.301 1.00 55.48  ? 290 GLY G N   1 
ATOM   13646 C CA  . GLY G  1 290 ? -8.439  18.648   -13.082 1.00 56.68  ? 290 GLY G CA  1 
ATOM   13647 C C   . GLY G  1 290 ? -7.767  17.315   -12.815 1.00 63.66  ? 290 GLY G C   1 
ATOM   13648 O O   . GLY G  1 290 ? -8.036  16.328   -13.499 1.00 74.27  ? 290 GLY G O   1 
ATOM   13649 N N   . ALA G  1 291 ? -6.890  17.284   -11.817 1.00 59.34  ? 291 ALA G N   1 
ATOM   13650 C CA  . ALA G  1 291 ? -6.158  16.069   -11.478 1.00 53.67  ? 291 ALA G CA  1 
ATOM   13651 C C   . ALA G  1 291 ? -6.971  15.153   -10.570 1.00 67.53  ? 291 ALA G C   1 
ATOM   13652 O O   . ALA G  1 291 ? -7.904  15.595   -9.900  1.00 61.16  ? 291 ALA G O   1 
ATOM   13653 C CB  . ALA G  1 291 ? -4.829  16.419   -10.825 1.00 47.13  ? 291 ALA G CB  1 
ATOM   13654 N N   . ILE G  1 292 ? -6.611  13.874   -10.557 1.00 67.35  ? 292 ILE G N   1 
ATOM   13655 C CA  . ILE G  1 292 ? -7.281  12.897   -9.710  1.00 62.84  ? 292 ILE G CA  1 
ATOM   13656 C C   . ILE G  1 292 ? -6.302  12.252   -8.734  1.00 73.58  ? 292 ILE G C   1 
ATOM   13657 O O   . ILE G  1 292 ? -5.401  11.516   -9.139  1.00 81.65  ? 292 ILE G O   1 
ATOM   13658 C CB  . ILE G  1 292 ? -7.963  11.789   -10.545 1.00 56.66  ? 292 ILE G CB  1 
ATOM   13659 C CG1 . ILE G  1 292 ? -9.032  12.387   -11.462 1.00 50.74  ? 292 ILE G CG1 1 
ATOM   13660 C CG2 . ILE G  1 292 ? -8.572  10.731   -9.637  1.00 68.87  ? 292 ILE G CG2 1 
ATOM   13661 C CD1 . ILE G  1 292 ? -9.778  11.357   -12.291 1.00 62.10  ? 292 ILE G CD1 1 
ATOM   13662 N N   . ASN G  1 293 ? -6.473  12.550   -7.450  1.00 90.42  ? 293 ASN G N   1 
ATOM   13663 C CA  . ASN G  1 293 ? -5.756  11.846   -6.395  1.00 110.44 ? 293 ASN G CA  1 
ATOM   13664 C C   . ASN G  1 293 ? -6.669  10.770   -5.826  1.00 109.43 ? 293 ASN G C   1 
ATOM   13665 O O   . ASN G  1 293 ? -7.461  11.034   -4.920  1.00 110.13 ? 293 ASN G O   1 
ATOM   13666 C CB  . ASN G  1 293 ? -5.302  12.821   -5.300  1.00 123.14 ? 293 ASN G CB  1 
ATOM   13667 C CG  . ASN G  1 293 ? -4.902  12.120   -4.007  1.00 127.93 ? 293 ASN G CG  1 
ATOM   13668 O OD1 . ASN G  1 293 ? -4.929  10.893   -3.911  1.00 125.17 ? 293 ASN G OD1 1 
ATOM   13669 N ND2 . ASN G  1 293 ? -4.534  12.907   -3.001  1.00 119.80 ? 293 ASN G ND2 1 
ATOM   13670 N N   . THR G  1 294 ? -6.586  9.561    -6.368  1.00 95.61  ? 294 THR G N   1 
ATOM   13671 C CA  . THR G  1 294 ? -7.440  8.492    -5.866  1.00 105.55 ? 294 THR G CA  1 
ATOM   13672 C C   . THR G  1 294 ? -6.770  7.127    -5.732  1.00 95.97  ? 294 THR G C   1 
ATOM   13673 O O   . THR G  1 294 ? -5.609  6.931    -6.101  1.00 85.57  ? 294 THR G O   1 
ATOM   13674 C CB  . THR G  1 294 ? -8.757  8.364    -6.669  1.00 94.19  ? 294 THR G CB  1 
ATOM   13675 O OG1 . THR G  1 294 ? -9.871  8.471    -5.772  1.00 73.26  ? 294 THR G OG1 1 
ATOM   13676 N N   . SER G  1 295 ? -7.538  6.194    -5.183  1.00 85.12  ? 295 SER G N   1 
ATOM   13677 C CA  . SER G  1 295 ? -7.063  4.871    -4.829  1.00 82.19  ? 295 SER G CA  1 
ATOM   13678 C C   . SER G  1 295 ? -8.061  3.893    -5.405  1.00 72.46  ? 295 SER G C   1 
ATOM   13679 O O   . SER G  1 295 ? -7.830  2.684    -5.454  1.00 73.47  ? 295 SER G O   1 
ATOM   13680 C CB  . SER G  1 295 ? -7.055  4.744    -3.312  1.00 81.93  ? 295 SER G CB  1 
ATOM   13681 O OG  . SER G  1 295 ? -7.254  6.012    -2.710  1.00 97.80  ? 295 SER G OG  1 
ATOM   13682 N N   . LEU G  1 296 ? -9.184  4.453    -5.837  1.00 62.95  ? 296 LEU G N   1 
ATOM   13683 C CA  . LEU G  1 296 ? -10.299 3.683    -6.349  1.00 55.37  ? 296 LEU G CA  1 
ATOM   13684 C C   . LEU G  1 296 ? -10.019 3.232    -7.777  1.00 62.26  ? 296 LEU G C   1 
ATOM   13685 O O   . LEU G  1 296 ? -9.174  3.806    -8.466  1.00 62.19  ? 296 LEU G O   1 
ATOM   13686 C CB  . LEU G  1 296 ? -11.582 4.515    -6.272  1.00 56.95  ? 296 LEU G CB  1 
ATOM   13687 C CG  . LEU G  1 296 ? -11.836 5.161    -4.907  1.00 59.12  ? 296 LEU G CG  1 
ATOM   13688 C CD1 . LEU G  1 296 ? -13.210 5.791    -4.846  1.00 59.26  ? 296 LEU G CD1 1 
ATOM   13689 C CD2 . LEU G  1 296 ? -11.683 4.149    -3.795  1.00 55.48  ? 296 LEU G CD2 1 
ATOM   13690 N N   . PRO G  1 297 ? -10.713 2.175    -8.214  1.00 51.87  ? 297 PRO G N   1 
ATOM   13691 C CA  . PRO G  1 297 ? -10.514 1.549    -9.523  1.00 51.63  ? 297 PRO G CA  1 
ATOM   13692 C C   . PRO G  1 297 ? -11.186 2.304    -10.669 1.00 60.14  ? 297 PRO G C   1 
ATOM   13693 O O   . PRO G  1 297 ? -10.764 2.154    -11.815 1.00 60.30  ? 297 PRO G O   1 
ATOM   13694 C CB  . PRO G  1 297 ? -11.173 0.172    -9.356  1.00 54.21  ? 297 PRO G CB  1 
ATOM   13695 C CG  . PRO G  1 297 ? -11.407 0.007    -7.878  1.00 64.89  ? 297 PRO G CG  1 
ATOM   13696 C CD  . PRO G  1 297 ? -11.614 1.385    -7.363  1.00 52.01  ? 297 PRO G CD  1 
ATOM   13697 N N   . PHE G  1 298 ? -12.211 3.097    -10.371 1.00 50.96  ? 298 PHE G N   1 
ATOM   13698 C CA  . PHE G  1 298 ? -12.990 3.734    -11.430 1.00 56.56  ? 298 PHE G CA  1 
ATOM   13699 C C   . PHE G  1 298 ? -13.247 5.221    -11.194 1.00 58.14  ? 298 PHE G C   1 
ATOM   13700 O O   . PHE G  1 298 ? -13.392 5.669    -10.058 1.00 61.68  ? 298 PHE G O   1 
ATOM   13701 C CB  . PHE G  1 298 ? -14.320 3.000    -11.620 1.00 47.37  ? 298 PHE G CB  1 
ATOM   13702 C CG  . PHE G  1 298 ? -14.201 1.504    -11.563 1.00 52.75  ? 298 PHE G CG  1 
ATOM   13703 C CD1 . PHE G  1 298 ? -13.721 0.790    -12.649 1.00 45.47  ? 298 PHE G CD1 1 
ATOM   13704 C CD2 . PHE G  1 298 ? -14.571 0.811    -10.423 1.00 46.96  ? 298 PHE G CD2 1 
ATOM   13705 C CE1 . PHE G  1 298 ? -13.611 -0.587   -12.597 1.00 55.23  ? 298 PHE G CE1 1 
ATOM   13706 C CE2 . PHE G  1 298 ? -14.465 -0.565   -10.365 1.00 50.97  ? 298 PHE G CE2 1 
ATOM   13707 C CZ  . PHE G  1 298 ? -13.984 -1.265   -11.453 1.00 50.94  ? 298 PHE G CZ  1 
ATOM   13708 N N   . GLN G  1 299 ? -13.308 5.977    -12.286 1.00 49.28  ? 299 GLN G N   1 
ATOM   13709 C CA  . GLN G  1 299 ? -13.608 7.401    -12.228 1.00 40.89  ? 299 GLN G CA  1 
ATOM   13710 C C   . GLN G  1 299 ? -14.591 7.781    -13.332 1.00 49.79  ? 299 GLN G C   1 
ATOM   13711 O O   . GLN G  1 299 ? -14.551 7.220    -14.426 1.00 76.52  ? 299 GLN G O   1 
ATOM   13712 C CB  . GLN G  1 299 ? -12.323 8.227    -12.340 1.00 50.87  ? 299 GLN G CB  1 
ATOM   13713 C CG  . GLN G  1 299 ? -11.502 7.960    -13.594 1.00 50.52  ? 299 GLN G CG  1 
ATOM   13714 C CD  . GLN G  1 299 ? -11.942 8.799    -14.778 1.00 50.75  ? 299 GLN G CD  1 
ATOM   13715 O OE1 . GLN G  1 299 ? -12.749 9.718    -14.639 1.00 53.97  ? 299 GLN G OE1 1 
ATOM   13716 N NE2 . GLN G  1 299 ? -11.406 8.490    -15.953 1.00 49.41  ? 299 GLN G NE2 1 
ATOM   13717 N N   . ASN G  1 300 ? -15.479 8.724    -13.037 1.00 50.67  ? 300 ASN G N   1 
ATOM   13718 C CA  . ASN G  1 300 ? -16.464 9.174    -14.014 1.00 55.90  ? 300 ASN G CA  1 
ATOM   13719 C C   . ASN G  1 300 ? -16.308 10.656   -14.331 1.00 52.39  ? 300 ASN G C   1 
ATOM   13720 O O   . ASN G  1 300 ? -17.247 11.307   -14.790 1.00 55.48  ? 300 ASN G O   1 
ATOM   13721 C CB  . ASN G  1 300 ? -17.886 8.889    -13.525 1.00 46.83  ? 300 ASN G CB  1 
ATOM   13722 C CG  . ASN G  1 300 ? -18.255 9.698    -12.296 1.00 54.08  ? 300 ASN G CG  1 
ATOM   13723 O OD1 . ASN G  1 300 ? -17.400 10.326   -11.671 1.00 61.14  ? 300 ASN G OD1 1 
ATOM   13724 N ND2 . ASN G  1 300 ? -19.535 9.686    -11.943 1.00 50.63  ? 300 ASN G ND2 1 
ATOM   13725 N N   . ILE G  1 301 ? -15.113 11.180   -14.080 1.00 52.20  ? 301 ILE G N   1 
ATOM   13726 C CA  . ILE G  1 301 ? -14.829 12.594   -14.288 1.00 53.35  ? 301 ILE G CA  1 
ATOM   13727 C C   . ILE G  1 301 ? -14.655 12.939   -15.764 1.00 52.26  ? 301 ILE G C   1 
ATOM   13728 O O   . ILE G  1 301 ? -15.348 13.810   -16.290 1.00 61.02  ? 301 ILE G O   1 
ATOM   13729 C CB  . ILE G  1 301 ? -13.568 13.032   -13.519 1.00 59.87  ? 301 ILE G CB  1 
ATOM   13730 C CG1 . ILE G  1 301 ? -13.794 12.901   -12.012 1.00 47.94  ? 301 ILE G CG1 1 
ATOM   13731 C CG2 . ILE G  1 301 ? -13.193 14.460   -13.881 1.00 55.76  ? 301 ILE G CG2 1 
ATOM   13732 C CD1 . ILE G  1 301 ? -12.571 13.214   -11.182 1.00 56.25  ? 301 ILE G CD1 1 
ATOM   13733 N N   . HIS G  1 302 ? -13.728 12.255   -16.427 1.00 50.21  ? 302 HIS G N   1 
ATOM   13734 C CA  . HIS G  1 302 ? -13.425 12.554   -17.821 1.00 53.02  ? 302 HIS G CA  1 
ATOM   13735 C C   . HIS G  1 302 ? -12.811 11.353   -18.538 1.00 52.38  ? 302 HIS G C   1 
ATOM   13736 O O   . HIS G  1 302 ? -11.977 10.646   -17.971 1.00 46.73  ? 302 HIS G O   1 
ATOM   13737 C CB  . HIS G  1 302 ? -12.479 13.753   -17.904 1.00 47.57  ? 302 HIS G CB  1 
ATOM   13738 C CG  . HIS G  1 302 ? -12.515 14.463   -19.221 1.00 56.37  ? 302 HIS G CG  1 
ATOM   13739 N ND1 . HIS G  1 302 ? -11.824 14.016   -20.326 1.00 56.12  ? 302 HIS G ND1 1 
ATOM   13740 C CD2 . HIS G  1 302 ? -13.154 15.591   -19.608 1.00 62.12  ? 302 HIS G CD2 1 
ATOM   13741 C CE1 . HIS G  1 302 ? -12.038 14.837   -21.339 1.00 57.90  ? 302 HIS G CE1 1 
ATOM   13742 N NE2 . HIS G  1 302 ? -12.843 15.803   -20.928 1.00 55.83  ? 302 HIS G NE2 1 
ATOM   13743 N N   . PRO G  1 303 ? -13.230 11.120   -19.791 1.00 51.25  ? 303 PRO G N   1 
ATOM   13744 C CA  . PRO G  1 303 ? -12.738 10.017   -20.626 1.00 40.93  ? 303 PRO G CA  1 
ATOM   13745 C C   . PRO G  1 303 ? -11.278 10.206   -21.025 1.00 50.71  ? 303 PRO G C   1 
ATOM   13746 O O   . PRO G  1 303 ? -10.489 9.266    -20.930 1.00 49.48  ? 303 PRO G O   1 
ATOM   13747 C CB  . PRO G  1 303 ? -13.630 10.093   -21.872 1.00 46.09  ? 303 PRO G CB  1 
ATOM   13748 C CG  . PRO G  1 303 ? -14.818 10.900   -21.459 1.00 67.79  ? 303 PRO G CG  1 
ATOM   13749 C CD  . PRO G  1 303 ? -14.298 11.879   -20.461 1.00 56.78  ? 303 PRO G CD  1 
ATOM   13750 N N   . ILE G  1 304 ? -10.929 11.408   -21.474 1.00 44.73  ? 304 ILE G N   1 
ATOM   13751 C CA  . ILE G  1 304 ? -9.555  11.708   -21.859 1.00 50.37  ? 304 ILE G CA  1 
ATOM   13752 C C   . ILE G  1 304 ? -8.700  11.925   -20.618 1.00 50.52  ? 304 ILE G C   1 
ATOM   13753 O O   . ILE G  1 304 ? -8.998  12.783   -19.788 1.00 53.93  ? 304 ILE G O   1 
ATOM   13754 C CB  . ILE G  1 304 ? -9.466  12.945   -22.774 1.00 45.16  ? 304 ILE G CB  1 
ATOM   13755 C CG1 . ILE G  1 304 ? -9.935  12.600   -24.190 1.00 44.79  ? 304 ILE G CG1 1 
ATOM   13756 C CG2 . ILE G  1 304 ? -8.040  13.471   -22.817 1.00 53.31  ? 304 ILE G CG2 1 
ATOM   13757 C CD1 . ILE G  1 304 ? -11.394 12.205   -24.285 1.00 55.66  ? 304 ILE G CD1 1 
ATOM   13758 N N   . THR G  1 305 ? -7.633  11.144   -20.498 1.00 45.11  ? 305 THR G N   1 
ATOM   13759 C CA  . THR G  1 305 ? -6.838  11.139   -19.281 1.00 44.67  ? 305 THR G CA  1 
ATOM   13760 C C   . THR G  1 305 ? -5.362  10.900   -19.594 1.00 55.77  ? 305 THR G C   1 
ATOM   13761 O O   . THR G  1 305 ? -5.028  10.315   -20.621 1.00 60.62  ? 305 THR G O   1 
ATOM   13762 C CB  . THR G  1 305 ? -7.361  10.060   -18.306 1.00 54.37  ? 305 THR G CB  1 
ATOM   13763 O OG1 . THR G  1 305 ? -7.435  10.596   -16.980 1.00 54.10  ? 305 THR G OG1 1 
ATOM   13764 C CG2 . THR G  1 305 ? -6.467  8.835    -18.318 1.00 44.69  ? 305 THR G CG2 1 
ATOM   13765 N N   . ILE G  1 306 ? -4.481  11.370   -18.716 1.00 47.65  ? 306 ILE G N   1 
ATOM   13766 C CA  . ILE G  1 306 ? -3.044  11.167   -18.887 1.00 56.10  ? 306 ILE G CA  1 
ATOM   13767 C C   . ILE G  1 306 ? -2.404  10.663   -17.596 1.00 56.12  ? 306 ILE G C   1 
ATOM   13768 O O   . ILE G  1 306 ? -2.689  11.172   -16.513 1.00 51.14  ? 306 ILE G O   1 
ATOM   13769 C CB  . ILE G  1 306 ? -2.326  12.458   -19.334 1.00 42.98  ? 306 ILE G CB  1 
ATOM   13770 C CG1 . ILE G  1 306 ? -2.972  13.025   -20.600 1.00 49.66  ? 306 ILE G CG1 1 
ATOM   13771 C CG2 . ILE G  1 306 ? -0.847  12.192   -19.571 1.00 40.03  ? 306 ILE G CG2 1 
ATOM   13772 C CD1 . ILE G  1 306 ? -2.225  14.205   -21.189 1.00 52.34  ? 306 ILE G CD1 1 
ATOM   13773 N N   . GLY G  1 307 ? -1.540  9.661    -17.719 1.00 48.69  ? 307 GLY G N   1 
ATOM   13774 C CA  . GLY G  1 307 ? -0.870  9.082    -16.568 1.00 50.97  ? 307 GLY G CA  1 
ATOM   13775 C C   . GLY G  1 307 ? -1.367  7.684    -16.255 1.00 57.27  ? 307 GLY G C   1 
ATOM   13776 O O   . GLY G  1 307 ? -1.846  6.974    -17.139 1.00 66.79  ? 307 GLY G O   1 
ATOM   13777 N N   . LYS G  1 308 ? -1.240  7.282    -14.995 1.00 54.28  ? 308 LYS G N   1 
ATOM   13778 C CA  . LYS G  1 308 ? -1.784  6.009    -14.538 1.00 52.25  ? 308 LYS G CA  1 
ATOM   13779 C C   . LYS G  1 308 ? -3.101  6.268    -13.817 1.00 52.67  ? 308 LYS G C   1 
ATOM   13780 O O   . LYS G  1 308 ? -3.118  6.614    -12.636 1.00 59.36  ? 308 LYS G O   1 
ATOM   13781 C CB  . LYS G  1 308 ? -0.796  5.292    -13.616 1.00 59.16  ? 308 LYS G CB  1 
ATOM   13782 C CG  . LYS G  1 308 ? -1.283  3.934    -13.139 1.00 82.13  ? 308 LYS G CG  1 
ATOM   13783 C CD  . LYS G  1 308 ? -0.298  3.270    -12.188 1.00 90.66  ? 308 LYS G CD  1 
ATOM   13784 C CE  . LYS G  1 308 ? 0.992   2.892    -12.895 1.00 92.10  ? 308 LYS G CE  1 
ATOM   13785 N NZ  . LYS G  1 308 ? 1.613   1.687    -12.278 1.00 102.25 ? 308 LYS G NZ  1 
ATOM   13786 N N   . CYS G  1 309 ? -4.204  6.099    -14.536 1.00 60.57  ? 309 CYS G N   1 
ATOM   13787 C CA  . CYS G  1 309 ? -5.501  6.547    -14.048 1.00 58.37  ? 309 CYS G CA  1 
ATOM   13788 C C   . CYS G  1 309 ? -6.504  5.422    -13.840 1.00 51.86  ? 309 CYS G C   1 
ATOM   13789 O O   . CYS G  1 309 ? -6.380  4.348    -14.432 1.00 54.92  ? 309 CYS G O   1 
ATOM   13790 C CB  . CYS G  1 309 ? -6.087  7.579    -15.013 1.00 48.36  ? 309 CYS G CB  1 
ATOM   13791 S SG  . CYS G  1 309 ? -4.966  8.942    -15.393 1.00 86.29  ? 309 CYS G SG  1 
ATOM   13792 N N   . PRO G  1 310 ? -7.509  5.674    -12.989 1.00 51.58  ? 310 PRO G N   1 
ATOM   13793 C CA  . PRO G  1 310 ? -8.639  4.760    -12.834 1.00 52.19  ? 310 PRO G CA  1 
ATOM   13794 C C   . PRO G  1 310 ? -9.392  4.670    -14.150 1.00 53.95  ? 310 PRO G C   1 
ATOM   13795 O O   . PRO G  1 310 ? -9.252  5.545    -15.006 1.00 49.76  ? 310 PRO G O   1 
ATOM   13796 C CB  . PRO G  1 310 ? -9.510  5.455    -11.781 1.00 46.03  ? 310 PRO G CB  1 
ATOM   13797 C CG  . PRO G  1 310 ? -8.586  6.376    -11.064 1.00 46.51  ? 310 PRO G CG  1 
ATOM   13798 C CD  . PRO G  1 310 ? -7.626  6.845    -12.106 1.00 42.38  ? 310 PRO G CD  1 
ATOM   13799 N N   . LYS G  1 311 ? -10.190 3.624    -14.312 1.00 46.11  ? 311 LYS G N   1 
ATOM   13800 C CA  . LYS G  1 311 ? -10.916 3.432    -15.558 1.00 46.35  ? 311 LYS G CA  1 
ATOM   13801 C C   . LYS G  1 311 ? -12.077 4.421    -15.648 1.00 49.56  ? 311 LYS G C   1 
ATOM   13802 O O   . LYS G  1 311 ? -12.727 4.710    -14.643 1.00 50.41  ? 311 LYS G O   1 
ATOM   13803 C CB  . LYS G  1 311 ? -11.430 1.994    -15.656 1.00 41.84  ? 311 LYS G CB  1 
ATOM   13804 C CG  . LYS G  1 311 ? -10.550 0.959    -14.967 1.00 49.84  ? 311 LYS G CG  1 
ATOM   13805 C CD  . LYS G  1 311 ? -9.102  1.039    -15.424 1.00 43.68  ? 311 LYS G CD  1 
ATOM   13806 C CE  . LYS G  1 311 ? -8.947  0.588    -16.864 1.00 41.50  ? 311 LYS G CE  1 
ATOM   13807 N NZ  . LYS G  1 311 ? -7.671  1.049    -17.472 1.00 42.20  ? 311 LYS G NZ  1 
ATOM   13808 N N   . TYR G  1 312 ? -12.327 4.959    -16.837 1.00 46.97  ? 312 TYR G N   1 
ATOM   13809 C CA  . TYR G  1 312 ? -13.482 5.825    -17.006 1.00 50.04  ? 312 TYR G CA  1 
ATOM   13810 C C   . TYR G  1 312 ? -14.749 4.996    -17.145 1.00 52.11  ? 312 TYR G C   1 
ATOM   13811 O O   . TYR G  1 312 ? -14.818 4.079    -17.966 1.00 61.97  ? 312 TYR G O   1 
ATOM   13812 C CB  . TYR G  1 312 ? -13.332 6.770    -18.198 1.00 41.48  ? 312 TYR G CB  1 
ATOM   13813 C CG  . TYR G  1 312 ? -14.471 7.757    -18.274 1.00 52.43  ? 312 TYR G CG  1 
ATOM   13814 C CD1 . TYR G  1 312 ? -14.703 8.646    -17.235 1.00 50.15  ? 312 TYR G CD1 1 
ATOM   13815 C CD2 . TYR G  1 312 ? -15.324 7.791    -19.367 1.00 51.69  ? 312 TYR G CD2 1 
ATOM   13816 C CE1 . TYR G  1 312 ? -15.738 9.541    -17.284 1.00 44.94  ? 312 TYR G CE1 1 
ATOM   13817 C CE2 . TYR G  1 312 ? -16.368 8.687    -19.421 1.00 40.24  ? 312 TYR G CE2 1 
ATOM   13818 C CZ  . TYR G  1 312 ? -16.567 9.560    -18.374 1.00 51.55  ? 312 TYR G CZ  1 
ATOM   13819 O OH  . TYR G  1 312 ? -17.598 10.464   -18.405 1.00 57.17  ? 312 TYR G OH  1 
ATOM   13820 N N   . VAL G  1 313 ? -15.744 5.324    -16.327 1.00 45.20  ? 313 VAL G N   1 
ATOM   13821 C CA  . VAL G  1 313 ? -17.007 4.605    -16.319 1.00 50.06  ? 313 VAL G CA  1 
ATOM   13822 C C   . VAL G  1 313 ? -18.160 5.600    -16.409 1.00 52.26  ? 313 VAL G C   1 
ATOM   13823 O O   . VAL G  1 313 ? -18.072 6.713    -15.892 1.00 54.09  ? 313 VAL G O   1 
ATOM   13824 C CB  . VAL G  1 313 ? -17.150 3.745    -15.046 1.00 48.32  ? 313 VAL G CB  1 
ATOM   13825 C CG1 . VAL G  1 313 ? -18.530 3.118    -14.976 1.00 62.87  ? 313 VAL G CG1 1 
ATOM   13826 C CG2 . VAL G  1 313 ? -16.074 2.671    -15.004 1.00 48.87  ? 313 VAL G CG2 1 
ATOM   13827 N N   . LYS G  1 314 ? -19.238 5.199    -17.073 1.00 50.83  ? 314 LYS G N   1 
ATOM   13828 C CA  . LYS G  1 314 ? -20.380 6.079    -17.279 1.00 48.69  ? 314 LYS G CA  1 
ATOM   13829 C C   . LYS G  1 314 ? -21.299 6.061    -16.064 1.00 53.02  ? 314 LYS G C   1 
ATOM   13830 O O   . LYS G  1 314 ? -22.355 6.693    -16.058 1.00 63.36  ? 314 LYS G O   1 
ATOM   13831 C CB  . LYS G  1 314 ? -21.148 5.648    -18.527 1.00 39.22  ? 314 LYS G CB  1 
ATOM   13832 C CG  . LYS G  1 314 ? -22.017 6.726    -19.142 1.00 71.75  ? 314 LYS G CG  1 
ATOM   13833 C CD  . LYS G  1 314 ? -22.649 6.207    -20.416 1.00 99.80  ? 314 LYS G CD  1 
ATOM   13834 C CE  . LYS G  1 314 ? -21.590 5.615    -21.332 1.00 96.48  ? 314 LYS G CE  1 
ATOM   13835 N NZ  . LYS G  1 314 ? -22.163 4.609    -22.264 1.00 76.97  ? 314 LYS G NZ  1 
ATOM   13836 N N   . SER G  1 315 ? -20.885 5.333    -15.032 1.00 57.15  ? 315 SER G N   1 
ATOM   13837 C CA  . SER G  1 315 ? -21.682 5.190    -13.821 1.00 60.98  ? 315 SER G CA  1 
ATOM   13838 C C   . SER G  1 315 ? -21.830 6.507    -13.066 1.00 60.61  ? 315 SER G C   1 
ATOM   13839 O O   . SER G  1 315 ? -20.955 7.372    -13.119 1.00 49.11  ? 315 SER G O   1 
ATOM   13840 C CB  . SER G  1 315 ? -21.070 4.132    -12.900 1.00 51.17  ? 315 SER G CB  1 
ATOM   13841 O OG  . SER G  1 315 ? -21.136 2.844    -13.487 1.00 75.46  ? 315 SER G OG  1 
ATOM   13842 N N   . THR G  1 316 ? -22.951 6.644    -12.366 1.00 66.24  ? 316 THR G N   1 
ATOM   13843 C CA  . THR G  1 316 ? -23.197 7.790    -11.500 1.00 68.28  ? 316 THR G CA  1 
ATOM   13844 C C   . THR G  1 316 ? -22.773 7.467    -10.071 1.00 62.78  ? 316 THR G C   1 
ATOM   13845 O O   . THR G  1 316 ? -22.296 8.336    -9.341  1.00 63.02  ? 316 THR G O   1 
ATOM   13846 C CB  . THR G  1 316 ? -24.683 8.198    -11.509 1.00 62.80  ? 316 THR G CB  1 
ATOM   13847 O OG1 . THR G  1 316 ? -24.952 9.052    -10.391 1.00 84.09  ? 316 THR G OG1 1 
ATOM   13848 C CG2 . THR G  1 316 ? -25.575 6.969    -11.421 1.00 70.49  ? 316 THR G CG2 1 
ATOM   13849 N N   . LYS G  1 317 ? -22.951 6.208    -9.683  1.00 69.07  ? 317 LYS G N   1 
ATOM   13850 C CA  . LYS G  1 317 ? -22.555 5.741    -8.360  1.00 69.36  ? 317 LYS G CA  1 
ATOM   13851 C C   . LYS G  1 317 ? -22.191 4.258    -8.380  1.00 64.03  ? 317 LYS G C   1 
ATOM   13852 O O   . LYS G  1 317 ? -22.808 3.465    -9.092  1.00 72.55  ? 317 LYS G O   1 
ATOM   13853 C CB  . LYS G  1 317 ? -23.670 5.994    -7.342  1.00 69.44  ? 317 LYS G CB  1 
ATOM   13854 C CG  . LYS G  1 317 ? -25.016 5.408    -7.739  1.00 84.68  ? 317 LYS G CG  1 
ATOM   13855 C CD  . LYS G  1 317 ? -26.051 5.584    -6.637  1.00 100.01 ? 317 LYS G CD  1 
ATOM   13856 C CE  . LYS G  1 317 ? -25.704 4.752    -5.411  1.00 94.85  ? 317 LYS G CE  1 
ATOM   13857 N NZ  . LYS G  1 317 ? -26.731 4.884    -4.340  1.00 75.94  ? 317 LYS G NZ  1 
ATOM   13858 N N   . LEU G  1 318 ? -21.181 3.895    -7.598  1.00 59.71  ? 318 LEU G N   1 
ATOM   13859 C CA  . LEU G  1 318 ? -20.771 2.503    -7.461  1.00 60.67  ? 318 LEU G CA  1 
ATOM   13860 C C   . LEU G  1 318 ? -20.589 2.166    -5.987  1.00 59.52  ? 318 LEU G C   1 
ATOM   13861 O O   . LEU G  1 318 ? -19.512 1.746    -5.566  1.00 56.86  ? 318 LEU G O   1 
ATOM   13862 C CB  . LEU G  1 318 ? -19.470 2.244    -8.224  1.00 43.89  ? 318 LEU G CB  1 
ATOM   13863 C CG  . LEU G  1 318 ? -19.555 2.226    -9.751  1.00 50.74  ? 318 LEU G CG  1 
ATOM   13864 C CD1 . LEU G  1 318 ? -18.166 2.181    -10.368 1.00 49.80  ? 318 LEU G CD1 1 
ATOM   13865 C CD2 . LEU G  1 318 ? -20.399 1.051    -10.230 1.00 52.59  ? 318 LEU G CD2 1 
ATOM   13866 N N   . ARG G  1 319 ? -21.646 2.358    -5.205  1.00 61.19  ? 319 ARG G N   1 
ATOM   13867 C CA  . ARG G  1 319 ? -21.569 2.152    -3.764  1.00 61.27  ? 319 ARG G CA  1 
ATOM   13868 C C   . ARG G  1 319 ? -21.504 0.669    -3.399  1.00 56.21  ? 319 ARG G C   1 
ATOM   13869 O O   . ARG G  1 319 ? -22.409 -0.103   -3.716  1.00 56.38  ? 319 ARG G O   1 
ATOM   13870 C CB  . ARG G  1 319 ? -22.737 2.840    -3.054  1.00 71.44  ? 319 ARG G CB  1 
ATOM   13871 C CG  . ARG G  1 319 ? -22.648 2.790    -1.539  1.00 70.49  ? 319 ARG G CG  1 
ATOM   13872 C CD  . ARG G  1 319 ? -23.226 4.045    -0.903  1.00 73.84  ? 319 ARG G CD  1 
ATOM   13873 N NE  . ARG G  1 319 ? -22.369 5.210    -1.111  1.00 81.97  ? 319 ARG G NE  1 
ATOM   13874 C CZ  . ARG G  1 319 ? -21.370 5.554    -0.305  1.00 85.08  ? 319 ARG G CZ  1 
ATOM   13875 N NH1 . ARG G  1 319 ? -21.097 4.821    0.766   1.00 87.47  ? 319 ARG G NH1 1 
ATOM   13876 N NH2 . ARG G  1 319 ? -20.642 6.631    -0.569  1.00 88.52  ? 319 ARG G NH2 1 
ATOM   13877 N N   . LEU G  1 320 ? -20.422 0.290    -2.724  1.00 57.51  ? 320 LEU G N   1 
ATOM   13878 C CA  . LEU G  1 320 ? -20.154 -1.099   -2.364  1.00 48.08  ? 320 LEU G CA  1 
ATOM   13879 C C   . LEU G  1 320 ? -20.489 -1.353   -0.892  1.00 57.11  ? 320 LEU G C   1 
ATOM   13880 O O   . LEU G  1 320 ? -19.936 -0.706   -0.002  1.00 73.60  ? 320 LEU G O   1 
ATOM   13881 C CB  . LEU G  1 320 ? -18.681 -1.420   -2.641  1.00 51.02  ? 320 LEU G CB  1 
ATOM   13882 C CG  . LEU G  1 320 ? -18.188 -2.870   -2.654  1.00 59.58  ? 320 LEU G CG  1 
ATOM   13883 C CD1 . LEU G  1 320 ? -18.760 -3.643   -3.833  1.00 52.00  ? 320 LEU G CD1 1 
ATOM   13884 C CD2 . LEU G  1 320 ? -16.665 -2.935   -2.656  1.00 54.38  ? 320 LEU G CD2 1 
ATOM   13885 N N   . ALA G  1 321 ? -21.395 -2.297   -0.647  1.00 57.49  ? 321 ALA G N   1 
ATOM   13886 C CA  . ALA G  1 321 ? -21.866 -2.613   0.704   1.00 53.38  ? 321 ALA G CA  1 
ATOM   13887 C C   . ALA G  1 321 ? -20.812 -3.312   1.560   1.00 57.96  ? 321 ALA G C   1 
ATOM   13888 O O   . ALA G  1 321 ? -20.349 -4.400   1.222   1.00 63.88  ? 321 ALA G O   1 
ATOM   13889 C CB  . ALA G  1 321 ? -23.124 -3.469   0.632   1.00 47.93  ? 321 ALA G CB  1 
ATOM   13890 N N   . THR G  1 322 ? -20.454 -2.699   2.683   1.00 69.41  ? 322 THR G N   1 
ATOM   13891 C CA  . THR G  1 322 ? -19.471 -3.286   3.586   1.00 62.95  ? 322 THR G CA  1 
ATOM   13892 C C   . THR G  1 322 ? -20.133 -3.861   4.835   1.00 66.85  ? 322 THR G C   1 
ATOM   13893 O O   . THR G  1 322 ? -19.732 -4.913   5.335   1.00 65.83  ? 322 THR G O   1 
ATOM   13894 C CB  . THR G  1 322 ? -18.406 -2.259   4.000   1.00 69.05  ? 322 THR G CB  1 
ATOM   13895 O OG1 . THR G  1 322 ? -19.037 -1.156   4.661   1.00 73.31  ? 322 THR G OG1 1 
ATOM   13896 C CG2 . THR G  1 322 ? -17.660 -1.750   2.778   1.00 73.69  ? 322 THR G CG2 1 
ATOM   13897 N N   . GLY G  1 323 ? -21.147 -3.162   5.336   1.00 71.18  ? 323 GLY G N   1 
ATOM   13898 C CA  . GLY G  1 323 ? -21.900 -3.623   6.489   1.00 74.83  ? 323 GLY G CA  1 
ATOM   13899 C C   . GLY G  1 323 ? -23.017 -4.566   6.087   1.00 73.93  ? 323 GLY G C   1 
ATOM   13900 O O   . GLY G  1 323 ? -22.978 -5.148   5.003   1.00 71.98  ? 323 GLY G O   1 
ATOM   13901 N N   . LEU G  1 324 ? -24.014 -4.713   6.957   1.00 71.68  ? 324 LEU G N   1 
ATOM   13902 C CA  . LEU G  1 324 ? -25.166 -5.569   6.672   1.00 67.86  ? 324 LEU G CA  1 
ATOM   13903 C C   . LEU G  1 324 ? -26.477 -4.784   6.685   1.00 75.10  ? 324 LEU G C   1 
ATOM   13904 O O   . LEU G  1 324 ? -26.521 -3.655   7.175   1.00 88.13  ? 324 LEU G O   1 
ATOM   13905 C CB  . LEU G  1 324 ? -25.227 -6.748   7.650   1.00 75.34  ? 324 LEU G CB  1 
ATOM   13906 C CG  . LEU G  1 324 ? -25.273 -6.484   9.157   1.00 68.06  ? 324 LEU G CG  1 
ATOM   13907 C CD1 . LEU G  1 324 ? -26.632 -5.966   9.573   1.00 73.35  ? 324 LEU G CD1 1 
ATOM   13908 C CD2 . LEU G  1 324 ? -24.948 -7.749   9.924   1.00 60.65  ? 324 LEU G CD2 1 
ATOM   13909 N N   . ARG G  1 325 ? -27.534 -5.388   6.145   1.00 68.49  ? 325 ARG G N   1 
ATOM   13910 C CA  . ARG G  1 325 ? -28.840 -4.738   6.043   1.00 74.45  ? 325 ARG G CA  1 
ATOM   13911 C C   . ARG G  1 325 ? -29.171 -3.942   7.300   1.00 82.61  ? 325 ARG G C   1 
ATOM   13912 O O   . ARG G  1 325 ? -28.805 -4.335   8.406   1.00 85.21  ? 325 ARG G O   1 
ATOM   13913 C CB  . ARG G  1 325 ? -29.934 -5.774   5.767   1.00 66.27  ? 325 ARG G CB  1 
ATOM   13914 C CG  . ARG G  1 325 ? -31.172 -5.194   5.094   1.00 75.84  ? 325 ARG G CG  1 
ATOM   13915 C CD  . ARG G  1 325 ? -32.275 -6.232   4.923   1.00 88.71  ? 325 ARG G CD  1 
ATOM   13916 N NE  . ARG G  1 325 ? -31.947 -7.257   3.934   1.00 92.55  ? 325 ARG G NE  1 
ATOM   13917 C CZ  . ARG G  1 325 ? -32.340 -7.230   2.663   1.00 98.06  ? 325 ARG G CZ  1 
ATOM   13918 N NH1 . ARG G  1 325 ? -33.076 -6.223   2.212   1.00 85.19  ? 325 ARG G NH1 1 
ATOM   13919 N NH2 . ARG G  1 325 ? -31.997 -8.212   1.840   1.00 88.43  ? 325 ARG G NH2 1 
ATOM   13920 N N   . ASN G  1 326 ? -29.857 -2.818   7.135   1.00 103.98 ? 326 ASN G N   1 
ATOM   13921 C CA  . ASN G  1 326 ? -30.111 -1.945   8.273   1.00 113.76 ? 326 ASN G CA  1 
ATOM   13922 C C   . ASN G  1 326 ? -31.564 -1.949   8.704   1.00 119.76 ? 326 ASN G C   1 
ATOM   13923 O O   . ASN G  1 326 ? -32.465 -1.788   7.882   1.00 125.71 ? 326 ASN G O   1 
ATOM   13924 C CB  . ASN G  1 326 ? -29.668 -0.513   7.979   1.00 126.73 ? 326 ASN G CB  1 
ATOM   13925 C CG  . ASN G  1 326 ? -29.582 0.333    9.235   1.00 133.32 ? 326 ASN G CG  1 
ATOM   13926 O OD1 . ASN G  1 326 ? -29.238 -0.163   10.307  1.00 130.91 ? 326 ASN G OD1 1 
ATOM   13927 N ND2 . ASN G  1 326 ? -29.893 1.617    9.108   1.00 132.53 ? 326 ASN G ND2 1 
ATOM   13928 N N   . ILE G  1 327 ? -31.792 -2.123   9.999   1.00 104.95 ? 327 ILE G N   1 
ATOM   13929 C CA  . ILE G  1 327 ? -33.149 -2.052   10.515  1.00 99.96  ? 327 ILE G CA  1 
ATOM   13930 C C   . ILE G  1 327 ? -33.283 -1.144   11.730  1.00 96.63  ? 327 ILE G C   1 
ATOM   13931 O O   . ILE G  1 327 ? -32.300 -0.625   12.254  1.00 95.17  ? 327 ILE G O   1 
ATOM   13932 C CB  . ILE G  1 327 ? -33.693 -3.424   10.895  1.00 87.07  ? 327 ILE G CB  1 
ATOM   13933 C CG1 . ILE G  1 327 ? -33.370 -4.458   9.828   1.00 81.17  ? 327 ILE G CG1 1 
ATOM   13934 C CG2 . ILE G  1 327 ? -35.189 -3.348   11.011  1.00 83.86  ? 327 ILE G CG2 1 
ATOM   13935 C CD1 . ILE G  1 327 ? -34.282 -4.390   8.633   1.00 75.01  ? 327 ILE G CD1 1 
ATOM   13936 N N   . GLY H  2 1   ? -30.812 -13.206  2.914   1.00 57.93  ? 1   GLY H N   1 
ATOM   13937 C CA  . GLY H  2 1   ? -32.080 -13.913  2.898   1.00 92.70  ? 1   GLY H CA  1 
ATOM   13938 C C   . GLY H  2 1   ? -31.956 -15.319  2.344   1.00 69.43  ? 1   GLY H C   1 
ATOM   13939 O O   . GLY H  2 1   ? -32.944 -16.048  2.247   1.00 78.59  ? 1   GLY H O   1 
ATOM   13940 N N   . LEU H  2 2   ? -30.736 -15.704  1.987   1.00 66.04  ? 2   LEU H N   1 
ATOM   13941 C CA  . LEU H  2 2   ? -30.489 -17.013  1.394   1.00 68.26  ? 2   LEU H CA  1 
ATOM   13942 C C   . LEU H  2 2   ? -30.423 -18.118  2.447   1.00 65.74  ? 2   LEU H C   1 
ATOM   13943 O O   . LEU H  2 2   ? -30.629 -19.288  2.142   1.00 60.74  ? 2   LEU H O   1 
ATOM   13944 C CB  . LEU H  2 2   ? -29.196 -16.991  0.577   1.00 62.42  ? 2   LEU H CB  1 
ATOM   13945 C CG  . LEU H  2 2   ? -29.100 -18.031  -0.541  1.00 65.25  ? 2   LEU H CG  1 
ATOM   13946 C CD1 . LEU H  2 2   ? -30.191 -17.802  -1.582  1.00 66.05  ? 2   LEU H CD1 1 
ATOM   13947 C CD2 . LEU H  2 2   ? -27.719 -18.012  -1.182  1.00 35.44  ? 2   LEU H CD2 1 
ATOM   13948 N N   . PHE H  2 3   ? -30.128 -17.750  3.686   1.00 66.93  ? 3   PHE H N   1 
ATOM   13949 C CA  . PHE H  2 3   ? -30.050 -18.740  4.754   1.00 67.44  ? 3   PHE H CA  1 
ATOM   13950 C C   . PHE H  2 3   ? -31.253 -18.654  5.690   1.00 75.50  ? 3   PHE H C   1 
ATOM   13951 O O   . PHE H  2 3   ? -31.328 -19.371  6.686   1.00 77.53  ? 3   PHE H O   1 
ATOM   13952 C CB  . PHE H  2 3   ? -28.731 -18.614  5.520   1.00 70.65  ? 3   PHE H CB  1 
ATOM   13953 C CG  . PHE H  2 3   ? -27.527 -19.032  4.720   1.00 70.82  ? 3   PHE H CG  1 
ATOM   13954 C CD1 . PHE H  2 3   ? -26.896 -18.136  3.872   1.00 64.07  ? 3   PHE H CD1 1 
ATOM   13955 C CD2 . PHE H  2 3   ? -27.032 -20.323  4.809   1.00 79.20  ? 3   PHE H CD2 1 
ATOM   13956 C CE1 . PHE H  2 3   ? -25.792 -18.518  3.131   1.00 60.19  ? 3   PHE H CE1 1 
ATOM   13957 C CE2 . PHE H  2 3   ? -25.928 -20.711  4.071   1.00 73.32  ? 3   PHE H CE2 1 
ATOM   13958 C CZ  . PHE H  2 3   ? -25.307 -19.807  3.232   1.00 62.86  ? 3   PHE H CZ  1 
ATOM   13959 N N   . GLY H  2 4   ? -32.193 -17.775  5.355   1.00 80.30  ? 4   GLY H N   1 
ATOM   13960 C CA  . GLY H  2 4   ? -33.448 -17.675  6.078   1.00 74.28  ? 4   GLY H CA  1 
ATOM   13961 C C   . GLY H  2 4   ? -33.352 -17.034  7.450   1.00 80.04  ? 4   GLY H C   1 
ATOM   13962 O O   . GLY H  2 4   ? -34.355 -16.907  8.153   1.00 82.12  ? 4   GLY H O   1 
ATOM   13963 N N   . ALA H  2 5   ? -32.149 -16.624  7.834   1.00 82.09  ? 5   ALA H N   1 
ATOM   13964 C CA  . ALA H  2 5   ? -31.937 -16.026  9.148   1.00 68.66  ? 5   ALA H CA  1 
ATOM   13965 C C   . ALA H  2 5   ? -32.296 -14.541  9.170   1.00 74.97  ? 5   ALA H C   1 
ATOM   13966 O O   . ALA H  2 5   ? -33.312 -14.149  9.745   1.00 70.55  ? 5   ALA H O   1 
ATOM   13967 C CB  . ALA H  2 5   ? -30.501 -16.236  9.602   1.00 65.92  ? 5   ALA H CB  1 
ATOM   13968 N N   . ILE H  2 6   ? -31.458 -13.720  8.545   1.00 78.29  ? 6   ILE H N   1 
ATOM   13969 C CA  . ILE H  2 6   ? -31.683 -12.279  8.510   1.00 66.90  ? 6   ILE H CA  1 
ATOM   13970 C C   . ILE H  2 6   ? -32.903 -11.934  7.664   1.00 71.33  ? 6   ILE H C   1 
ATOM   13971 O O   . ILE H  2 6   ? -32.999 -12.334  6.503   1.00 66.94  ? 6   ILE H O   1 
ATOM   13972 C CB  . ILE H  2 6   ? -30.451 -11.524  7.977   1.00 61.33  ? 6   ILE H CB  1 
ATOM   13973 C CG1 . ILE H  2 6   ? -29.236 -11.805  8.864   1.00 59.60  ? 6   ILE H CG1 1 
ATOM   13974 C CG2 . ILE H  2 6   ? -30.727 -10.032  7.913   1.00 47.21  ? 6   ILE H CG2 1 
ATOM   13975 C CD1 . ILE H  2 6   ? -28.023 -10.968  8.522   1.00 61.78  ? 6   ILE H CD1 1 
ATOM   13976 N N   . ALA H  2 7   ? -33.830 -11.187  8.257   1.00 68.17  ? 7   ALA H N   1 
ATOM   13977 C CA  . ALA H  2 7   ? -35.105 -10.884  7.617   1.00 64.12  ? 7   ALA H CA  1 
ATOM   13978 C C   . ALA H  2 7   ? -35.892 -12.169  7.380   1.00 74.79  ? 7   ALA H C   1 
ATOM   13979 O O   . ALA H  2 7   ? -36.739 -12.237  6.490   1.00 79.78  ? 7   ALA H O   1 
ATOM   13980 C CB  . ALA H  2 7   ? -34.889 -10.132  6.311   1.00 66.68  ? 7   ALA H CB  1 
ATOM   13981 N N   . GLY H  2 8   ? -35.600 -13.186  8.187   1.00 77.98  ? 8   GLY H N   1 
ATOM   13982 C CA  . GLY H  2 8   ? -36.280 -14.466  8.099   1.00 77.43  ? 8   GLY H CA  1 
ATOM   13983 C C   . GLY H  2 8   ? -36.996 -14.808  9.392   1.00 85.27  ? 8   GLY H C   1 
ATOM   13984 O O   . GLY H  2 8   ? -37.913 -14.096  9.801   1.00 87.41  ? 8   GLY H O   1 
ATOM   13985 N N   . PHE H  2 9   ? -36.582 -15.894  10.040  1.00 69.54  ? 9   PHE H N   1 
ATOM   13986 C CA  . PHE H  2 9   ? -37.175 -16.270  11.322  1.00 71.69  ? 9   PHE H CA  1 
ATOM   13987 C C   . PHE H  2 9   ? -36.703 -15.340  12.438  1.00 82.41  ? 9   PHE H C   1 
ATOM   13988 O O   . PHE H  2 9   ? -37.312 -15.273  13.506  1.00 101.66 ? 9   PHE H O   1 
ATOM   13989 C CB  . PHE H  2 9   ? -36.917 -17.744  11.666  1.00 80.11  ? 9   PHE H CB  1 
ATOM   13990 C CG  . PHE H  2 9   ? -35.464 -18.127  11.698  1.00 78.16  ? 9   PHE H CG  1 
ATOM   13991 C CD1 . PHE H  2 9   ? -34.663 -17.777  12.771  1.00 87.77  ? 9   PHE H CD1 1 
ATOM   13992 C CD2 . PHE H  2 9   ? -34.908 -18.867  10.668  1.00 88.70  ? 9   PHE H CD2 1 
ATOM   13993 C CE1 . PHE H  2 9   ? -33.329 -18.139  12.806  1.00 88.41  ? 9   PHE H CE1 1 
ATOM   13994 C CE2 . PHE H  2 9   ? -33.575 -19.233  10.698  1.00 91.61  ? 9   PHE H CE2 1 
ATOM   13995 C CZ  . PHE H  2 9   ? -32.784 -18.867  11.768  1.00 91.34  ? 9   PHE H CZ  1 
ATOM   13996 N N   . ILE H  2 10  ? -35.611 -14.628  12.179  1.00 75.43  ? 10  ILE H N   1 
ATOM   13997 C CA  . ILE H  2 10  ? -35.199 -13.519  13.027  1.00 74.79  ? 10  ILE H CA  1 
ATOM   13998 C C   . ILE H  2 10  ? -35.548 -12.241  12.281  1.00 74.00  ? 10  ILE H C   1 
ATOM   13999 O O   . ILE H  2 10  ? -34.750 -11.723  11.498  1.00 75.22  ? 10  ILE H O   1 
ATOM   14000 C CB  . ILE H  2 10  ? -33.697 -13.546  13.325  1.00 60.41  ? 10  ILE H CB  1 
ATOM   14001 C CG1 . ILE H  2 10  ? -33.278 -14.932  13.812  1.00 72.70  ? 10  ILE H CG1 1 
ATOM   14002 C CG2 . ILE H  2 10  ? -33.346 -12.493  14.365  1.00 59.24  ? 10  ILE H CG2 1 
ATOM   14003 C CD1 . ILE H  2 10  ? -31.784 -15.114  13.887  1.00 65.99  ? 10  ILE H CD1 1 
ATOM   14004 N N   . GLU H  2 11  ? -36.757 -11.751  12.524  1.00 85.29  ? 11  GLU H N   1 
ATOM   14005 C CA  . GLU H  2 11  ? -37.336 -10.670  11.738  1.00 96.05  ? 11  GLU H CA  1 
ATOM   14006 C C   . GLU H  2 11  ? -36.544 -9.375   11.836  1.00 92.56  ? 11  GLU H C   1 
ATOM   14007 O O   . GLU H  2 11  ? -36.483 -8.603   10.879  1.00 85.82  ? 11  GLU H O   1 
ATOM   14008 C CB  . GLU H  2 11  ? -38.775 -10.420  12.190  1.00 102.79 ? 11  GLU H CB  1 
ATOM   14009 C CG  . GLU H  2 11  ? -39.637 -11.668  12.210  1.00 121.19 ? 11  GLU H CG  1 
ATOM   14010 C CD  . GLU H  2 11  ? -41.010 -11.416  12.796  1.00 152.20 ? 11  GLU H CD  1 
ATOM   14011 O OE1 . GLU H  2 11  ? -41.814 -12.369  12.862  1.00 156.73 ? 11  GLU H OE1 1 
ATOM   14012 O OE2 . GLU H  2 11  ? -41.285 -10.264  13.192  1.00 151.25 ? 11  GLU H OE2 1 
ATOM   14013 N N   . GLY H  2 12  ? -35.936 -9.141   12.993  1.00 89.37  ? 12  GLY H N   1 
ATOM   14014 C CA  . GLY H  2 12  ? -35.379 -7.837   13.280  1.00 76.93  ? 12  GLY H CA  1 
ATOM   14015 C C   . GLY H  2 12  ? -33.938 -7.740   13.739  1.00 79.05  ? 12  GLY H C   1 
ATOM   14016 O O   . GLY H  2 12  ? -33.329 -8.719   14.170  1.00 79.96  ? 12  GLY H O   1 
ATOM   14017 N N   . GLY H  2 13  ? -33.409 -6.524   13.646  1.00 79.38  ? 13  GLY H N   1 
ATOM   14018 C CA  . GLY H  2 13  ? -32.071 -6.198   14.091  1.00 81.57  ? 13  GLY H CA  1 
ATOM   14019 C C   . GLY H  2 13  ? -32.076 -5.484   15.428  1.00 79.83  ? 13  GLY H C   1 
ATOM   14020 O O   . GLY H  2 13  ? -33.122 -5.035   15.896  1.00 81.08  ? 13  GLY H O   1 
ATOM   14021 N N   . TRP H  2 14  ? -30.903 -5.375   16.045  1.00 80.47  ? 14  TRP H N   1 
ATOM   14022 C CA  . TRP H  2 14  ? -30.787 -4.743   17.353  1.00 82.33  ? 14  TRP H CA  1 
ATOM   14023 C C   . TRP H  2 14  ? -29.921 -3.491   17.323  1.00 94.38  ? 14  TRP H C   1 
ATOM   14024 O O   . TRP H  2 14  ? -28.692 -3.574   17.292  1.00 95.90  ? 14  TRP H O   1 
ATOM   14025 C CB  . TRP H  2 14  ? -30.223 -5.723   18.382  1.00 84.08  ? 14  TRP H CB  1 
ATOM   14026 C CG  . TRP H  2 14  ? -31.069 -6.934   18.597  1.00 84.89  ? 14  TRP H CG  1 
ATOM   14027 C CD1 . TRP H  2 14  ? -32.410 -7.048   18.375  1.00 80.96  ? 14  TRP H CD1 1 
ATOM   14028 C CD2 . TRP H  2 14  ? -30.634 -8.203   19.094  1.00 66.20  ? 14  TRP H CD2 1 
ATOM   14029 N NE1 . TRP H  2 14  ? -32.835 -8.315   18.695  1.00 79.91  ? 14  TRP H NE1 1 
ATOM   14030 C CE2 . TRP H  2 14  ? -31.763 -9.043   19.140  1.00 76.41  ? 14  TRP H CE2 1 
ATOM   14031 C CE3 . TRP H  2 14  ? -29.397 -8.712   19.502  1.00 75.45  ? 14  TRP H CE3 1 
ATOM   14032 C CZ2 . TRP H  2 14  ? -31.694 -10.364  19.577  1.00 78.87  ? 14  TRP H CZ2 1 
ATOM   14033 C CZ3 . TRP H  2 14  ? -29.329 -10.023  19.936  1.00 92.80  ? 14  TRP H CZ3 1 
ATOM   14034 C CH2 . TRP H  2 14  ? -30.471 -10.832  19.973  1.00 96.40  ? 14  TRP H CH2 1 
ATOM   14035 N N   . THR H  2 15  ? -30.569 -2.333   17.338  1.00 95.73  ? 15  THR H N   1 
ATOM   14036 C CA  . THR H  2 15  ? -29.863 -1.068   17.467  1.00 101.99 ? 15  THR H CA  1 
ATOM   14037 C C   . THR H  2 15  ? -29.069 -1.077   18.768  1.00 119.27 ? 15  THR H C   1 
ATOM   14038 O O   . THR H  2 15  ? -28.039 -0.413   18.890  1.00 123.68 ? 15  THR H O   1 
ATOM   14039 C CB  . THR H  2 15  ? -30.846 0.112    17.493  1.00 106.20 ? 15  THR H CB  1 
ATOM   14040 O OG1 . THR H  2 15  ? -31.672 0.018    18.659  1.00 125.87 ? 15  THR H OG1 1 
ATOM   14041 C CG2 . THR H  2 15  ? -31.731 0.089    16.263  1.00 103.58 ? 15  THR H CG2 1 
ATOM   14042 N N   . GLY H  2 16  ? -29.558 -1.849   19.734  1.00 100.69 ? 16  GLY H N   1 
ATOM   14043 C CA  . GLY H  2 16  ? -28.953 -1.923   21.051  1.00 98.04  ? 16  GLY H CA  1 
ATOM   14044 C C   . GLY H  2 16  ? -27.551 -2.501   21.069  1.00 98.26  ? 16  GLY H C   1 
ATOM   14045 O O   . GLY H  2 16  ? -26.692 -2.032   21.815  1.00 106.88 ? 16  GLY H O   1 
ATOM   14046 N N   . MET H  2 17  ? -27.316 -3.524   20.254  1.00 99.16  ? 17  MET H N   1 
ATOM   14047 C CA  . MET H  2 17  ? -26.002 -4.154   20.184  1.00 102.24 ? 17  MET H CA  1 
ATOM   14048 C C   . MET H  2 17  ? -25.076 -3.376   19.254  1.00 113.49 ? 17  MET H C   1 
ATOM   14049 O O   . MET H  2 17  ? -25.265 -3.368   18.038  1.00 118.40 ? 17  MET H O   1 
ATOM   14050 C CB  . MET H  2 17  ? -26.122 -5.608   19.724  1.00 87.27  ? 17  MET H CB  1 
ATOM   14051 C CG  . MET H  2 17  ? -24.797 -6.352   19.676  1.00 104.22 ? 17  MET H CG  1 
ATOM   14052 S SD  . MET H  2 17  ? -24.986 -8.078   19.194  1.00 113.72 ? 17  MET H SD  1 
ATOM   14053 C CE  . MET H  2 17  ? -25.854 -7.898   17.639  1.00 93.64  ? 17  MET H CE  1 
ATOM   14054 N N   . VAL H  2 18  ? -24.074 -2.725   19.836  1.00 113.54 ? 18  VAL H N   1 
ATOM   14055 C CA  . VAL H  2 18  ? -23.175 -1.861   19.078  1.00 119.00 ? 18  VAL H CA  1 
ATOM   14056 C C   . VAL H  2 18  ? -21.722 -2.313   19.187  1.00 112.11 ? 18  VAL H C   1 
ATOM   14057 O O   . VAL H  2 18  ? -20.803 -1.561   18.863  1.00 124.66 ? 18  VAL H O   1 
ATOM   14058 C CB  . VAL H  2 18  ? -23.274 -0.403   19.560  1.00 123.20 ? 18  VAL H CB  1 
ATOM   14059 C CG1 . VAL H  2 18  ? -24.697 0.110    19.407  1.00 108.65 ? 18  VAL H CG1 1 
ATOM   14060 C CG2 . VAL H  2 18  ? -22.818 -0.295   21.007  1.00 120.71 ? 18  VAL H CG2 1 
ATOM   14061 N N   . ASP H  2 19  ? -21.520 -3.545   19.641  1.00 129.26 ? 19  ASP H N   1 
ATOM   14062 C CA  . ASP H  2 19  ? -20.176 -4.075   19.838  1.00 140.40 ? 19  ASP H CA  1 
ATOM   14063 C C   . ASP H  2 19  ? -19.682 -4.830   18.608  1.00 134.54 ? 19  ASP H C   1 
ATOM   14064 O O   . ASP H  2 19  ? -18.485 -4.846   18.316  1.00 132.02 ? 19  ASP H O   1 
ATOM   14065 C CB  . ASP H  2 19  ? -20.142 -4.991   21.062  1.00 155.83 ? 19  ASP H CB  1 
ATOM   14066 C CG  . ASP H  2 19  ? -20.797 -4.365   22.277  1.00 166.69 ? 19  ASP H CG  1 
ATOM   14067 O OD1 . ASP H  2 19  ? -20.817 -3.119   22.370  1.00 169.66 ? 19  ASP H OD1 1 
ATOM   14068 O OD2 . ASP H  2 19  ? -21.291 -5.120   23.140  1.00 157.67 ? 19  ASP H OD2 1 
ATOM   14069 N N   . GLY H  2 20  ? -20.610 -5.456   17.890  1.00 117.46 ? 20  GLY H N   1 
ATOM   14070 C CA  . GLY H  2 20  ? -20.270 -6.228   16.709  1.00 96.25  ? 20  GLY H CA  1 
ATOM   14071 C C   . GLY H  2 20  ? -21.443 -6.417   15.767  1.00 92.30  ? 20  GLY H C   1 
ATOM   14072 O O   . GLY H  2 20  ? -22.499 -5.809   15.944  1.00 80.10  ? 20  GLY H O   1 
ATOM   14073 N N   . TRP H  2 21  ? -21.256 -7.266   14.760  1.00 76.08  ? 21  TRP H N   1 
ATOM   14074 C CA  . TRP H  2 21  ? -22.297 -7.522   13.768  1.00 78.03  ? 21  TRP H CA  1 
ATOM   14075 C C   . TRP H  2 21  ? -23.286 -8.589   14.221  1.00 77.13  ? 21  TRP H C   1 
ATOM   14076 O O   . TRP H  2 21  ? -24.478 -8.489   13.948  1.00 74.06  ? 21  TRP H O   1 
ATOM   14077 C CB  . TRP H  2 21  ? -21.685 -7.916   12.422  1.00 84.23  ? 21  TRP H CB  1 
ATOM   14078 C CG  . TRP H  2 21  ? -21.236 -6.747   11.608  1.00 84.68  ? 21  TRP H CG  1 
ATOM   14079 C CD1 . TRP H  2 21  ? -21.718 -5.472   11.672  1.00 67.52  ? 21  TRP H CD1 1 
ATOM   14080 C CD2 . TRP H  2 21  ? -20.226 -6.743   10.593  1.00 71.08  ? 21  TRP H CD2 1 
ATOM   14081 N NE1 . TRP H  2 21  ? -21.065 -4.673   10.767  1.00 75.21  ? 21  TRP H NE1 1 
ATOM   14082 C CE2 . TRP H  2 21  ? -20.144 -5.429   10.090  1.00 72.85  ? 21  TRP H CE2 1 
ATOM   14083 C CE3 . TRP H  2 21  ? -19.380 -7.722   10.063  1.00 67.43  ? 21  TRP H CE3 1 
ATOM   14084 C CZ2 . TRP H  2 21  ? -19.251 -5.069   9.084   1.00 75.45  ? 21  TRP H CZ2 1 
ATOM   14085 C CZ3 . TRP H  2 21  ? -18.494 -7.362   9.063   1.00 65.95  ? 21  TRP H CZ3 1 
ATOM   14086 C CH2 . TRP H  2 21  ? -18.436 -6.048   8.585   1.00 73.27  ? 21  TRP H CH2 1 
ATOM   14087 N N   . TYR H  2 22  ? -22.787 -9.614   14.903  1.00 85.15  ? 22  TYR H N   1 
ATOM   14088 C CA  . TYR H  2 22  ? -23.647 -10.664  15.435  1.00 78.17  ? 22  TYR H CA  1 
ATOM   14089 C C   . TYR H  2 22  ? -23.370 -10.844  16.922  1.00 91.52  ? 22  TYR H C   1 
ATOM   14090 O O   . TYR H  2 22  ? -22.237 -10.672  17.371  1.00 106.16 ? 22  TYR H O   1 
ATOM   14091 C CB  . TYR H  2 22  ? -23.412 -11.982  14.693  1.00 86.55  ? 22  TYR H CB  1 
ATOM   14092 C CG  . TYR H  2 22  ? -22.804 -11.815  13.318  1.00 80.99  ? 22  TYR H CG  1 
ATOM   14093 C CD1 . TYR H  2 22  ? -21.435 -11.936  13.126  1.00 73.66  ? 22  TYR H CD1 1 
ATOM   14094 C CD2 . TYR H  2 22  ? -23.598 -11.534  12.213  1.00 79.26  ? 22  TYR H CD2 1 
ATOM   14095 C CE1 . TYR H  2 22  ? -20.871 -11.785  11.875  1.00 76.72  ? 22  TYR H CE1 1 
ATOM   14096 C CE2 . TYR H  2 22  ? -23.043 -11.380  10.956  1.00 73.91  ? 22  TYR H CE2 1 
ATOM   14097 C CZ  . TYR H  2 22  ? -21.679 -11.507  10.793  1.00 78.79  ? 22  TYR H CZ  1 
ATOM   14098 O OH  . TYR H  2 22  ? -21.118 -11.355  9.546   1.00 52.33  ? 22  TYR H OH  1 
ATOM   14099 N N   . GLY H  2 23  ? -24.404 -11.184  17.686  1.00 103.22 ? 23  GLY H N   1 
ATOM   14100 C CA  . GLY H  2 23  ? -24.256 -11.363  19.119  1.00 111.95 ? 23  GLY H CA  1 
ATOM   14101 C C   . GLY H  2 23  ? -25.486 -11.936  19.796  1.00 117.73 ? 23  GLY H C   1 
ATOM   14102 O O   . GLY H  2 23  ? -26.383 -12.460  19.136  1.00 102.97 ? 23  GLY H O   1 
ATOM   14103 N N   . TYR H  2 24  ? -25.528 -11.828  21.122  1.00 106.77 ? 24  TYR H N   1 
ATOM   14104 C CA  . TYR H  2 24  ? -26.613 -12.408  21.907  1.00 90.72  ? 24  TYR H CA  1 
ATOM   14105 C C   . TYR H  2 24  ? -27.308 -11.373  22.788  1.00 101.61 ? 24  TYR H C   1 
ATOM   14106 O O   . TYR H  2 24  ? -26.853 -10.237  22.916  1.00 107.09 ? 24  TYR H O   1 
ATOM   14107 C CB  . TYR H  2 24  ? -26.081 -13.530  22.802  1.00 90.73  ? 24  TYR H CB  1 
ATOM   14108 C CG  . TYR H  2 24  ? -25.063 -14.435  22.148  1.00 91.09  ? 24  TYR H CG  1 
ATOM   14109 C CD1 . TYR H  2 24  ? -23.723 -14.076  22.088  1.00 92.69  ? 24  TYR H CD1 1 
ATOM   14110 C CD2 . TYR H  2 24  ? -25.437 -15.657  21.608  1.00 90.62  ? 24  TYR H CD2 1 
ATOM   14111 C CE1 . TYR H  2 24  ? -22.787 -14.903  21.503  1.00 96.77  ? 24  TYR H CE1 1 
ATOM   14112 C CE2 . TYR H  2 24  ? -24.508 -16.491  21.018  1.00 78.46  ? 24  TYR H CE2 1 
ATOM   14113 C CZ  . TYR H  2 24  ? -23.184 -16.109  20.969  1.00 94.77  ? 24  TYR H CZ  1 
ATOM   14114 O OH  . TYR H  2 24  ? -22.253 -16.935  20.383  1.00 88.03  ? 24  TYR H OH  1 
ATOM   14115 N N   . HIS H  2 25  ? -28.414 -11.783  23.399  1.00 96.82  ? 25  HIS H N   1 
ATOM   14116 C CA  . HIS H  2 25  ? -29.099 -10.965  24.394  1.00 107.26 ? 25  HIS H CA  1 
ATOM   14117 C C   . HIS H  2 25  ? -29.680 -11.857  25.486  1.00 121.34 ? 25  HIS H C   1 
ATOM   14118 O O   . HIS H  2 25  ? -30.770 -12.409  25.341  1.00 102.83 ? 25  HIS H O   1 
ATOM   14119 C CB  . HIS H  2 25  ? -30.199 -10.113  23.756  1.00 106.67 ? 25  HIS H CB  1 
ATOM   14120 C CG  . HIS H  2 25  ? -31.137 -9.499   24.747  1.00 116.64 ? 25  HIS H CG  1 
ATOM   14121 N ND1 . HIS H  2 25  ? -32.364 -10.049  25.049  1.00 109.81 ? 25  HIS H ND1 1 
ATOM   14122 C CD2 . HIS H  2 25  ? -31.026 -8.385   25.512  1.00 116.50 ? 25  HIS H CD2 1 
ATOM   14123 C CE1 . HIS H  2 25  ? -32.969 -9.300   25.954  1.00 115.65 ? 25  HIS H CE1 1 
ATOM   14124 N NE2 . HIS H  2 25  ? -32.180 -8.286   26.251  1.00 130.10 ? 25  HIS H NE2 1 
ATOM   14125 N N   . HIS H  2 26  ? -28.937 -11.996  26.577  1.00 140.81 ? 26  HIS H N   1 
ATOM   14126 C CA  . HIS H  2 26  ? -29.327 -12.865  27.677  1.00 128.66 ? 26  HIS H CA  1 
ATOM   14127 C C   . HIS H  2 26  ? -30.435 -12.223  28.502  1.00 137.57 ? 26  HIS H C   1 
ATOM   14128 O O   . HIS H  2 26  ? -30.648 -11.015  28.429  1.00 146.60 ? 26  HIS H O   1 
ATOM   14129 C CB  . HIS H  2 26  ? -28.119 -13.138  28.557  1.00 128.30 ? 26  HIS H CB  1 
ATOM   14130 C CG  . HIS H  2 26  ? -27.746 -11.988  29.434  1.00 132.72 ? 26  HIS H CG  1 
ATOM   14131 N ND1 . HIS H  2 26  ? -27.033 -10.899  28.979  1.00 134.01 ? 26  HIS H ND1 1 
ATOM   14132 C CD2 . HIS H  2 26  ? -27.982 -11.759  30.749  1.00 147.38 ? 26  HIS H CD2 1 
ATOM   14133 C CE1 . HIS H  2 26  ? -26.851 -10.048  29.973  1.00 146.90 ? 26  HIS H CE1 1 
ATOM   14134 N NE2 . HIS H  2 26  ? -27.415 -10.546  31.056  1.00 155.65 ? 26  HIS H NE2 1 
ATOM   14135 N N   . GLN H  2 27  ? -31.129 -13.031  29.295  1.00 164.87 ? 27  GLN H N   1 
ATOM   14136 C CA  . GLN H  2 27  ? -32.261 -12.547  30.076  1.00 173.42 ? 27  GLN H CA  1 
ATOM   14137 C C   . GLN H  2 27  ? -32.455 -13.401  31.329  1.00 163.51 ? 27  GLN H C   1 
ATOM   14138 O O   . GLN H  2 27  ? -33.530 -13.958  31.553  1.00 154.93 ? 27  GLN H O   1 
ATOM   14139 C CB  . GLN H  2 27  ? -33.530 -12.546  29.211  1.00 165.85 ? 27  GLN H CB  1 
ATOM   14140 C CG  . GLN H  2 27  ? -34.829 -12.164  29.919  1.00 167.78 ? 27  GLN H CG  1 
ATOM   14141 C CD  . GLN H  2 27  ? -34.840 -10.730  30.411  1.00 178.83 ? 27  GLN H CD  1 
ATOM   14142 O OE1 . GLN H  2 27  ? -35.443 -9.854   29.792  1.00 169.26 ? 27  GLN H OE1 1 
ATOM   14143 N NE2 . GLN H  2 27  ? -34.173 -10.484  31.532  1.00 187.89 ? 27  GLN H NE2 1 
ATOM   14144 N N   . ASN H  2 28  ? -31.404 -13.508  32.141  1.00 155.86 ? 28  ASN H N   1 
ATOM   14145 C CA  . ASN H  2 28  ? -31.467 -14.297  33.366  1.00 148.64 ? 28  ASN H CA  1 
ATOM   14146 C C   . ASN H  2 28  ? -31.657 -13.435  34.608  1.00 155.97 ? 28  ASN H C   1 
ATOM   14147 O O   . ASN H  2 28  ? -31.931 -12.239  34.511  1.00 154.48 ? 28  ASN H O   1 
ATOM   14148 C CB  . ASN H  2 28  ? -30.239 -15.202  33.512  1.00 132.25 ? 28  ASN H CB  1 
ATOM   14149 C CG  . ASN H  2 28  ? -28.965 -14.433  33.849  1.00 141.88 ? 28  ASN H CG  1 
ATOM   14150 O OD1 . ASN H  2 28  ? -27.924 -15.034  34.115  1.00 140.34 ? 28  ASN H OD1 1 
ATOM   14151 N ND2 . ASN H  2 28  ? -29.042 -13.105  33.839  1.00 147.53 ? 28  ASN H ND2 1 
ATOM   14152 N N   . GLU H  2 29  ? -31.493 -14.052  35.771  1.00 154.58 ? 29  GLU H N   1 
ATOM   14153 C CA  . GLU H  2 29  ? -31.817 -13.419  37.044  1.00 161.15 ? 29  GLU H CA  1 
ATOM   14154 C C   . GLU H  2 29  ? -30.829 -12.331  37.467  1.00 159.73 ? 29  GLU H C   1 
ATOM   14155 O O   . GLU H  2 29  ? -31.083 -11.600  38.423  1.00 154.53 ? 29  GLU H O   1 
ATOM   14156 C CB  . GLU H  2 29  ? -31.917 -14.487  38.132  1.00 171.83 ? 29  GLU H CB  1 
ATOM   14157 C CG  . GLU H  2 29  ? -32.828 -15.656  37.765  1.00 169.95 ? 29  GLU H CG  1 
ATOM   14158 C CD  . GLU H  2 29  ? -32.454 -16.942  38.483  1.00 180.18 ? 29  GLU H CD  1 
ATOM   14159 O OE1 . GLU H  2 29  ? -31.271 -17.097  38.848  1.00 176.62 ? 29  GLU H OE1 1 
ATOM   14160 O OE2 . GLU H  2 29  ? -33.342 -17.799  38.676  1.00 177.43 ? 29  GLU H OE2 1 
ATOM   14161 N N   . GLN H  2 30  ? -29.708 -12.221  36.762  1.00 164.77 ? 30  GLN H N   1 
ATOM   14162 C CA  . GLN H  2 30  ? -28.714 -11.208  37.104  1.00 167.04 ? 30  GLN H CA  1 
ATOM   14163 C C   . GLN H  2 30  ? -28.766 -10.001  36.179  1.00 171.98 ? 30  GLN H C   1 
ATOM   14164 O O   . GLN H  2 30  ? -27.901 -9.128   36.242  1.00 172.78 ? 30  GLN H O   1 
ATOM   14165 C CB  . GLN H  2 30  ? -27.307 -11.799  37.110  1.00 154.48 ? 30  GLN H CB  1 
ATOM   14166 C CG  . GLN H  2 30  ? -27.074 -12.796  38.217  1.00 143.91 ? 30  GLN H CG  1 
ATOM   14167 C CD  . GLN H  2 30  ? -26.625 -14.131  37.684  1.00 146.17 ? 30  GLN H CD  1 
ATOM   14168 O OE1 . GLN H  2 30  ? -25.432 -14.379  37.528  1.00 140.23 ? 30  GLN H OE1 1 
ATOM   14169 N NE2 . GLN H  2 30  ? -27.582 -15.002  37.389  1.00 150.28 ? 30  GLN H NE2 1 
ATOM   14170 N N   . GLY H  2 31  ? -29.775 -9.951   35.318  1.00 215.66 ? 31  GLY H N   1 
ATOM   14171 C CA  . GLY H  2 31  ? -29.953 -8.808   34.444  1.00 214.78 ? 31  GLY H CA  1 
ATOM   14172 C C   . GLY H  2 31  ? -30.105 -9.163   32.981  1.00 210.32 ? 31  GLY H C   1 
ATOM   14173 O O   . GLY H  2 31  ? -30.203 -10.335  32.624  1.00 207.62 ? 31  GLY H O   1 
ATOM   14174 N N   . SER H  2 32  ? -30.127 -8.140   32.135  1.00 176.11 ? 32  SER H N   1 
ATOM   14175 C CA  . SER H  2 32  ? -30.272 -8.331   30.698  1.00 162.98 ? 32  SER H CA  1 
ATOM   14176 C C   . SER H  2 32  ? -29.137 -7.630   29.962  1.00 156.64 ? 32  SER H C   1 
ATOM   14177 O O   . SER H  2 32  ? -28.101 -7.325   30.552  1.00 155.65 ? 32  SER H O   1 
ATOM   14178 C CB  . SER H  2 32  ? -31.618 -7.785   30.224  1.00 150.13 ? 32  SER H CB  1 
ATOM   14179 O OG  . SER H  2 32  ? -32.682 -8.310   30.997  1.00 156.55 ? 32  SER H OG  1 
ATOM   14180 N N   . GLY H  2 33  ? -29.338 -7.375   28.673  1.00 163.88 ? 33  GLY H N   1 
ATOM   14181 C CA  . GLY H  2 33  ? -28.353 -6.665   27.879  1.00 156.20 ? 33  GLY H CA  1 
ATOM   14182 C C   . GLY H  2 33  ? -27.921 -7.414   26.634  1.00 142.89 ? 33  GLY H C   1 
ATOM   14183 O O   . GLY H  2 33  ? -28.240 -8.590   26.459  1.00 137.41 ? 33  GLY H O   1 
ATOM   14184 N N   . TYR H  2 34  ? -27.189 -6.724   25.765  1.00 114.65 ? 34  TYR H N   1 
ATOM   14185 C CA  . TYR H  2 34  ? -26.685 -7.323   24.536  1.00 96.83  ? 34  TYR H CA  1 
ATOM   14186 C C   . TYR H  2 34  ? -25.180 -7.553   24.628  1.00 98.14  ? 34  TYR H C   1 
ATOM   14187 O O   . TYR H  2 34  ? -24.463 -6.785   25.270  1.00 106.99 ? 34  TYR H O   1 
ATOM   14188 C CB  . TYR H  2 34  ? -26.991 -6.423   23.337  1.00 91.99  ? 34  TYR H CB  1 
ATOM   14189 C CG  . TYR H  2 34  ? -28.444 -6.023   23.208  1.00 92.31  ? 34  TYR H CG  1 
ATOM   14190 C CD1 . TYR H  2 34  ? -28.929 -4.884   23.836  1.00 92.00  ? 34  TYR H CD1 1 
ATOM   14191 C CD2 . TYR H  2 34  ? -29.328 -6.778   22.449  1.00 89.27  ? 34  TYR H CD2 1 
ATOM   14192 C CE1 . TYR H  2 34  ? -30.255 -4.510   23.718  1.00 95.92  ? 34  TYR H CE1 1 
ATOM   14193 C CE2 . TYR H  2 34  ? -30.656 -6.413   22.324  1.00 81.54  ? 34  TYR H CE2 1 
ATOM   14194 C CZ  . TYR H  2 34  ? -31.114 -5.278   22.961  1.00 90.84  ? 34  TYR H CZ  1 
ATOM   14195 O OH  . TYR H  2 34  ? -32.435 -4.910   22.840  1.00 78.61  ? 34  TYR H OH  1 
ATOM   14196 N N   . ALA H  2 35  ? -24.706 -8.612   23.979  1.00 97.82  ? 35  ALA H N   1 
ATOM   14197 C CA  . ALA H  2 35  ? -23.279 -8.912   23.938  1.00 102.08 ? 35  ALA H CA  1 
ATOM   14198 C C   . ALA H  2 35  ? -22.891 -9.492   22.582  1.00 108.68 ? 35  ALA H C   1 
ATOM   14199 O O   . ALA H  2 35  ? -23.305 -10.595  22.228  1.00 111.31 ? 35  ALA H O   1 
ATOM   14200 C CB  . ALA H  2 35  ? -22.905 -9.871   25.056  1.00 113.17 ? 35  ALA H CB  1 
ATOM   14201 N N   . ALA H  2 36  ? -22.094 -8.743   21.827  1.00 102.27 ? 36  ALA H N   1 
ATOM   14202 C CA  . ALA H  2 36  ? -21.689 -9.165   20.491  1.00 105.05 ? 36  ALA H CA  1 
ATOM   14203 C C   . ALA H  2 36  ? -20.702 -10.325  20.539  1.00 94.10  ? 36  ALA H C   1 
ATOM   14204 O O   . ALA H  2 36  ? -19.798 -10.349  21.375  1.00 109.69 ? 36  ALA H O   1 
ATOM   14205 C CB  . ALA H  2 36  ? -21.095 -7.996   19.724  1.00 103.31 ? 36  ALA H CB  1 
ATOM   14206 N N   . ASP H  2 37  ? -20.882 -11.284  19.637  1.00 87.73  ? 37  ASP H N   1 
ATOM   14207 C CA  . ASP H  2 37  ? -19.991 -12.434  19.559  1.00 96.89  ? 37  ASP H CA  1 
ATOM   14208 C C   . ASP H  2 37  ? -18.606 -12.003  19.106  1.00 107.13 ? 37  ASP H C   1 
ATOM   14209 O O   . ASP H  2 37  ? -18.437 -11.428  18.030  1.00 104.95 ? 37  ASP H O   1 
ATOM   14210 C CB  . ASP H  2 37  ? -20.545 -13.498  18.612  1.00 87.69  ? 37  ASP H CB  1 
ATOM   14211 C CG  . ASP H  2 37  ? -19.697 -14.756  18.593  1.00 99.23  ? 37  ASP H CG  1 
ATOM   14212 O OD1 . ASP H  2 37  ? -19.988 -15.657  17.782  1.00 117.28 ? 37  ASP H OD1 1 
ATOM   14213 O OD2 . ASP H  2 37  ? -18.738 -14.846  19.390  1.00 115.02 ? 37  ASP H OD2 1 
ATOM   14214 N N   . LEU H  2 38  ? -17.616 -12.297  19.937  1.00 112.20 ? 38  LEU H N   1 
ATOM   14215 C CA  . LEU H  2 38  ? -16.257 -11.840  19.705  1.00 122.58 ? 38  LEU H CA  1 
ATOM   14216 C C   . LEU H  2 38  ? -15.638 -12.445  18.444  1.00 111.43 ? 38  LEU H C   1 
ATOM   14217 O O   . LEU H  2 38  ? -15.287 -11.725  17.510  1.00 106.05 ? 38  LEU H O   1 
ATOM   14218 C CB  . LEU H  2 38  ? -15.391 -12.152  20.925  1.00 147.44 ? 38  LEU H CB  1 
ATOM   14219 C CG  . LEU H  2 38  ? -14.315 -11.117  21.246  1.00 158.15 ? 38  LEU H CG  1 
ATOM   14220 C CD1 . LEU H  2 38  ? -13.597 -11.468  22.542  1.00 149.51 ? 38  LEU H CD1 1 
ATOM   14221 C CD2 . LEU H  2 38  ? -13.338 -10.971  20.088  1.00 155.66 ? 38  LEU H CD2 1 
ATOM   14222 N N   . LYS H  2 39  ? -15.510 -13.768  18.422  1.00 132.26 ? 39  LYS H N   1 
ATOM   14223 C CA  . LYS H  2 39  ? -14.829 -14.459  17.329  1.00 136.75 ? 39  LYS H CA  1 
ATOM   14224 C C   . LYS H  2 39  ? -15.529 -14.305  15.979  1.00 131.89 ? 39  LYS H C   1 
ATOM   14225 O O   . LYS H  2 39  ? -14.872 -14.179  14.945  1.00 125.19 ? 39  LYS H O   1 
ATOM   14226 C CB  . LYS H  2 39  ? -14.659 -15.943  17.663  1.00 154.72 ? 39  LYS H CB  1 
ATOM   14227 C CG  . LYS H  2 39  ? -13.841 -16.717  16.644  1.00 168.85 ? 39  LYS H CG  1 
ATOM   14228 C CD  . LYS H  2 39  ? -13.572 -18.135  17.119  1.00 184.29 ? 39  LYS H CD  1 
ATOM   14229 C CE  . LYS H  2 39  ? -12.659 -18.873  16.155  1.00 188.53 ? 39  LYS H CE  1 
ATOM   14230 N NZ  . LYS H  2 39  ? -12.314 -20.235  16.648  1.00 178.06 ? 39  LYS H NZ  1 
ATOM   14231 N N   . SER H  2 40  ? -16.857 -14.319  15.990  1.00 113.00 ? 40  SER H N   1 
ATOM   14232 C CA  . SER H  2 40  ? -17.630 -14.247  14.754  1.00 97.08  ? 40  SER H CA  1 
ATOM   14233 C C   . SER H  2 40  ? -17.510 -12.880  14.082  1.00 86.70  ? 40  SER H C   1 
ATOM   14234 O O   . SER H  2 40  ? -17.173 -12.788  12.902  1.00 90.58  ? 40  SER H O   1 
ATOM   14235 C CB  . SER H  2 40  ? -19.100 -14.579  15.020  1.00 95.03  ? 40  SER H CB  1 
ATOM   14236 O OG  . SER H  2 40  ? -19.815 -14.741  13.808  1.00 101.57 ? 40  SER H OG  1 
ATOM   14237 N N   . THR H  2 41  ? -17.788 -11.823  14.839  1.00 86.22  ? 41  THR H N   1 
ATOM   14238 C CA  . THR H  2 41  ? -17.726 -10.465  14.308  1.00 85.24  ? 41  THR H CA  1 
ATOM   14239 C C   . THR H  2 41  ? -16.328 -10.122  13.801  1.00 86.02  ? 41  THR H C   1 
ATOM   14240 O O   . THR H  2 41  ? -16.176 -9.445   12.784  1.00 74.25  ? 41  THR H O   1 
ATOM   14241 C CB  . THR H  2 41  ? -18.150 -9.424   15.363  1.00 78.04  ? 41  THR H CB  1 
ATOM   14242 O OG1 . THR H  2 41  ? -19.525 -9.626   15.711  1.00 84.85  ? 41  THR H OG1 1 
ATOM   14243 C CG2 . THR H  2 41  ? -17.975 -8.016   14.819  1.00 77.80  ? 41  THR H CG2 1 
ATOM   14244 N N   . GLN H  2 42  ? -15.312 -10.598  14.513  1.00 103.67 ? 42  GLN H N   1 
ATOM   14245 C CA  . GLN H  2 42  ? -13.928 -10.323  14.144  1.00 106.57 ? 42  GLN H CA  1 
ATOM   14246 C C   . GLN H  2 42  ? -13.581 -10.915  12.783  1.00 99.27  ? 42  GLN H C   1 
ATOM   14247 O O   . GLN H  2 42  ? -13.002 -10.239  11.932  1.00 100.95 ? 42  GLN H O   1 
ATOM   14248 C CB  . GLN H  2 42  ? -12.967 -10.857  15.207  1.00 108.51 ? 42  GLN H CB  1 
ATOM   14249 C CG  . GLN H  2 42  ? -11.520 -10.477  14.958  1.00 117.56 ? 42  GLN H CG  1 
ATOM   14250 C CD  . GLN H  2 42  ? -11.331 -8.977   14.885  1.00 133.60 ? 42  GLN H CD  1 
ATOM   14251 O OE1 . GLN H  2 42  ? -12.067 -8.221   15.517  1.00 135.97 ? 42  GLN H OE1 1 
ATOM   14252 N NE2 . GLN H  2 42  ? -10.344 -8.538   14.111  1.00 128.20 ? 42  GLN H NE2 1 
ATOM   14253 N N   . ASN H  2 43  ? -13.934 -12.181  12.584  1.00 85.22  ? 43  ASN H N   1 
ATOM   14254 C CA  . ASN H  2 43  ? -13.673 -12.855  11.316  1.00 90.04  ? 43  ASN H CA  1 
ATOM   14255 C C   . ASN H  2 43  ? -14.383 -12.191  10.142  1.00 89.97  ? 43  ASN H C   1 
ATOM   14256 O O   . ASN H  2 43  ? -13.791 -11.993  9.080   1.00 77.66  ? 43  ASN H O   1 
ATOM   14257 C CB  . ASN H  2 43  ? -14.057 -14.334  11.397  1.00 88.60  ? 43  ASN H CB  1 
ATOM   14258 C CG  . ASN H  2 43  ? -12.887 -15.220  11.775  1.00 104.04 ? 43  ASN H CG  1 
ATOM   14259 O OD1 . ASN H  2 43  ? -12.352 -15.129  12.879  1.00 116.16 ? 43  ASN H OD1 1 
ATOM   14260 N ND2 . ASN H  2 43  ? -12.484 -16.088  10.857  1.00 101.98 ? 43  ASN H ND2 1 
ATOM   14261 N N   . ALA H  2 44  ? -15.653 -11.851  10.337  1.00 79.37  ? 44  ALA H N   1 
ATOM   14262 C CA  . ALA H  2 44  ? -16.434 -11.194  9.296   1.00 72.97  ? 44  ALA H CA  1 
ATOM   14263 C C   . ALA H  2 44  ? -15.752 -9.910   8.840   1.00 74.12  ? 44  ALA H C   1 
ATOM   14264 O O   . ALA H  2 44  ? -15.570 -9.684   7.644   1.00 78.96  ? 44  ALA H O   1 
ATOM   14265 C CB  . ALA H  2 44  ? -17.841 -10.905  9.792   1.00 66.10  ? 44  ALA H CB  1 
ATOM   14266 N N   . ILE H  2 45  ? -15.374 -9.073   9.801   1.00 78.11  ? 45  ILE H N   1 
ATOM   14267 C CA  . ILE H  2 45  ? -14.685 -7.822   9.503   1.00 78.24  ? 45  ILE H CA  1 
ATOM   14268 C C   . ILE H  2 45  ? -13.423 -8.060   8.679   1.00 76.90  ? 45  ILE H C   1 
ATOM   14269 O O   . ILE H  2 45  ? -13.205 -7.408   7.659   1.00 73.41  ? 45  ILE H O   1 
ATOM   14270 C CB  . ILE H  2 45  ? -14.320 -7.057   10.790  1.00 81.83  ? 45  ILE H CB  1 
ATOM   14271 C CG1 . ILE H  2 45  ? -15.571 -6.433   11.411  1.00 76.22  ? 45  ILE H CG1 1 
ATOM   14272 C CG2 . ILE H  2 45  ? -13.287 -5.981   10.496  1.00 83.30  ? 45  ILE H CG2 1 
ATOM   14273 C CD1 . ILE H  2 45  ? -15.291 -5.585   12.633  1.00 92.49  ? 45  ILE H CD1 1 
ATOM   14274 N N   . ASP H  2 46  ? -12.595 -8.999   9.127   1.00 75.65  ? 46  ASP H N   1 
ATOM   14275 C CA  . ASP H  2 46  ? -11.364 -9.335   8.421   1.00 73.87  ? 46  ASP H CA  1 
ATOM   14276 C C   . ASP H  2 46  ? -11.643 -9.768   6.987   1.00 73.44  ? 46  ASP H C   1 
ATOM   14277 O O   . ASP H  2 46  ? -10.997 -9.300   6.050   1.00 76.31  ? 46  ASP H O   1 
ATOM   14278 C CB  . ASP H  2 46  ? -10.608 -10.443  9.157   1.00 83.77  ? 46  ASP H CB  1 
ATOM   14279 C CG  . ASP H  2 46  ? -9.958  -9.956   10.436  1.00 108.40 ? 46  ASP H CG  1 
ATOM   14280 O OD1 . ASP H  2 46  ? -9.805  -8.727   10.596  1.00 103.18 ? 46  ASP H OD1 1 
ATOM   14281 O OD2 . ASP H  2 46  ? -9.594  -10.804  11.278  1.00 119.76 ? 46  ASP H OD2 1 
ATOM   14282 N N   . GLU H  2 47  ? -12.611 -10.663  6.824   1.00 77.97  ? 47  GLU H N   1 
ATOM   14283 C CA  . GLU H  2 47  ? -12.926 -11.218  5.513   1.00 68.57  ? 47  GLU H CA  1 
ATOM   14284 C C   . GLU H  2 47  ? -13.606 -10.208  4.591   1.00 67.70  ? 47  GLU H C   1 
ATOM   14285 O O   . GLU H  2 47  ? -13.302 -10.144  3.401   1.00 67.05  ? 47  GLU H O   1 
ATOM   14286 C CB  . GLU H  2 47  ? -13.772 -12.484  5.654   1.00 59.70  ? 47  GLU H CB  1 
ATOM   14287 C CG  . GLU H  2 47  ? -13.024 -13.645  6.288   1.00 75.13  ? 47  GLU H CG  1 
ATOM   14288 C CD  . GLU H  2 47  ? -13.742 -14.966  6.112   1.00 79.59  ? 47  GLU H CD  1 
ATOM   14289 O OE1 . GLU H  2 47  ? -14.986 -14.957  6.011   1.00 67.45  ? 47  GLU H OE1 1 
ATOM   14290 O OE2 . GLU H  2 47  ? -13.062 -16.013  6.074   1.00 86.89  ? 47  GLU H OE2 1 
ATOM   14291 N N   . ILE H  2 48  ? -14.524 -9.420   5.141   1.00 62.43  ? 48  ILE H N   1 
ATOM   14292 C CA  . ILE H  2 48  ? -15.168 -8.365   4.367   1.00 49.69  ? 48  ILE H CA  1 
ATOM   14293 C C   . ILE H  2 48  ? -14.139 -7.319   3.954   1.00 58.25  ? 48  ILE H C   1 
ATOM   14294 O O   . ILE H  2 48  ? -14.181 -6.799   2.840   1.00 64.72  ? 48  ILE H O   1 
ATOM   14295 C CB  . ILE H  2 48  ? -16.314 -7.695   5.149   1.00 56.34  ? 48  ILE H CB  1 
ATOM   14296 C CG1 . ILE H  2 48  ? -17.501 -8.651   5.272   1.00 65.79  ? 48  ILE H CG1 1 
ATOM   14297 C CG2 . ILE H  2 48  ? -16.748 -6.411   4.462   1.00 48.10  ? 48  ILE H CG2 1 
ATOM   14298 C CD1 . ILE H  2 48  ? -18.037 -9.131   3.939   1.00 68.04  ? 48  ILE H CD1 1 
ATOM   14299 N N   . THR H  2 49  ? -13.212 -7.020   4.859   1.00 62.76  ? 49  THR H N   1 
ATOM   14300 C CA  . THR H  2 49  ? -12.121 -6.099   4.563   1.00 65.55  ? 49  THR H CA  1 
ATOM   14301 C C   . THR H  2 49  ? -11.306 -6.607   3.381   1.00 67.85  ? 49  THR H C   1 
ATOM   14302 O O   . THR H  2 49  ? -11.075 -5.882   2.414   1.00 69.69  ? 49  THR H O   1 
ATOM   14303 C CB  . THR H  2 49  ? -11.185 -5.922   5.773   1.00 74.83  ? 49  THR H CB  1 
ATOM   14304 O OG1 . THR H  2 49  ? -11.866 -5.196   6.804   1.00 79.10  ? 49  THR H OG1 1 
ATOM   14305 C CG2 . THR H  2 49  ? -9.930  -5.161   5.370   1.00 61.85  ? 49  THR H CG2 1 
ATOM   14306 N N   . ASN H  2 50  ? -10.873 -7.860   3.470   1.00 51.36  ? 50  ASN H N   1 
ATOM   14307 C CA  . ASN H  2 50  ? -10.117 -8.489   2.396   1.00 63.92  ? 50  ASN H CA  1 
ATOM   14308 C C   . ASN H  2 50  ? -10.895 -8.442   1.086   1.00 68.63  ? 50  ASN H C   1 
ATOM   14309 O O   . ASN H  2 50  ? -10.316 -8.261   0.015   1.00 58.97  ? 50  ASN H O   1 
ATOM   14310 C CB  . ASN H  2 50  ? -9.778  -9.934   2.768   1.00 58.80  ? 50  ASN H CB  1 
ATOM   14311 C CG  . ASN H  2 50  ? -8.728  -10.545  1.858   1.00 64.81  ? 50  ASN H CG  1 
ATOM   14312 O OD1 . ASN H  2 50  ? -7.534  -10.491  2.148   1.00 83.32  ? 50  ASN H OD1 1 
ATOM   14313 N ND2 . ASN H  2 50  ? -9.169  -11.139  0.756   1.00 58.97  ? 50  ASN H ND2 1 
ATOM   14314 N N   . LYS H  2 51  ? -12.212 -8.601   1.183   1.00 60.19  ? 51  LYS H N   1 
ATOM   14315 C CA  . LYS H  2 51  ? -13.086 -8.549   0.015   1.00 56.99  ? 51  LYS H CA  1 
ATOM   14316 C C   . LYS H  2 51  ? -12.961 -7.205   -0.685  1.00 59.99  ? 51  LYS H C   1 
ATOM   14317 O O   . LYS H  2 51  ? -12.733 -7.138   -1.892  1.00 64.44  ? 51  LYS H O   1 
ATOM   14318 C CB  . LYS H  2 51  ? -14.539 -8.798   0.423   1.00 69.31  ? 51  LYS H CB  1 
ATOM   14319 C CG  . LYS H  2 51  ? -15.529 -8.798   -0.731  1.00 50.91  ? 51  LYS H CG  1 
ATOM   14320 C CD  . LYS H  2 51  ? -16.852 -9.414   -0.307  1.00 61.95  ? 51  LYS H CD  1 
ATOM   14321 C CE  . LYS H  2 51  ? -17.806 -9.541   -1.480  1.00 61.54  ? 51  LYS H CE  1 
ATOM   14322 N NZ  . LYS H  2 51  ? -18.890 -10.526  -1.206  1.00 64.04  ? 51  LYS H NZ  1 
ATOM   14323 N N   . VAL H  2 52  ? -13.109 -6.138   0.091   1.00 53.35  ? 52  VAL H N   1 
ATOM   14324 C CA  . VAL H  2 52  ? -13.022 -4.784   -0.435  1.00 54.51  ? 52  VAL H CA  1 
ATOM   14325 C C   . VAL H  2 52  ? -11.633 -4.504   -1.000  1.00 66.32  ? 52  VAL H C   1 
ATOM   14326 O O   . VAL H  2 52  ? -11.495 -3.877   -2.050  1.00 74.42  ? 52  VAL H O   1 
ATOM   14327 C CB  . VAL H  2 52  ? -13.352 -3.747   0.652   1.00 47.99  ? 52  VAL H CB  1 
ATOM   14328 C CG1 . VAL H  2 52  ? -13.327 -2.345   0.072   1.00 50.53  ? 52  VAL H CG1 1 
ATOM   14329 C CG2 . VAL H  2 52  ? -14.709 -4.046   1.270   1.00 55.78  ? 52  VAL H CG2 1 
ATOM   14330 N N   . ASN H  2 53  ? -10.606 -4.975   -0.300  1.00 54.89  ? 53  ASN H N   1 
ATOM   14331 C CA  . ASN H  2 53  ? -9.230  -4.790   -0.748  1.00 64.44  ? 53  ASN H CA  1 
ATOM   14332 C C   . ASN H  2 53  ? -8.949  -5.465   -2.087  1.00 70.69  ? 53  ASN H C   1 
ATOM   14333 O O   . ASN H  2 53  ? -8.222  -4.926   -2.917  1.00 69.13  ? 53  ASN H O   1 
ATOM   14334 C CB  . ASN H  2 53  ? -8.242  -5.287   0.309   1.00 73.25  ? 53  ASN H CB  1 
ATOM   14335 C CG  . ASN H  2 53  ? -8.007  -4.271   1.411   1.00 78.52  ? 53  ASN H CG  1 
ATOM   14336 O OD1 . ASN H  2 53  ? -8.458  -3.129   1.326   1.00 60.57  ? 53  ASN H OD1 1 
ATOM   14337 N ND2 . ASN H  2 53  ? -7.290  -4.683   2.450   1.00 81.10  ? 53  ASN H ND2 1 
ATOM   14338 N N   . SER H  2 54  ? -9.528  -6.644   -2.290  1.00 59.80  ? 54  SER H N   1 
ATOM   14339 C CA  . SER H  2 54  ? -9.325  -7.391   -3.527  1.00 54.53  ? 54  SER H CA  1 
ATOM   14340 C C   . SER H  2 54  ? -9.864  -6.630   -4.735  1.00 55.13  ? 54  SER H C   1 
ATOM   14341 O O   . SER H  2 54  ? -9.147  -6.411   -5.712  1.00 56.13  ? 54  SER H O   1 
ATOM   14342 C CB  . SER H  2 54  ? -9.979  -8.771   -3.437  1.00 55.30  ? 54  SER H CB  1 
ATOM   14343 O OG  . SER H  2 54  ? -9.372  -9.557   -2.427  1.00 67.30  ? 54  SER H OG  1 
ATOM   14344 N N   . VAL H  2 55  ? -11.129 -6.229   -4.661  1.00 53.43  ? 55  VAL H N   1 
ATOM   14345 C CA  . VAL H  2 55  ? -11.765 -5.482   -5.740  1.00 54.20  ? 55  VAL H CA  1 
ATOM   14346 C C   . VAL H  2 55  ? -10.944 -4.251   -6.117  1.00 60.69  ? 55  VAL H C   1 
ATOM   14347 O O   . VAL H  2 55  ? -10.938 -3.823   -7.271  1.00 64.81  ? 55  VAL H O   1 
ATOM   14348 C CB  . VAL H  2 55  ? -13.195 -5.047   -5.356  1.00 50.62  ? 55  VAL H CB  1 
ATOM   14349 C CG1 . VAL H  2 55  ? -13.793 -4.156   -6.436  1.00 54.85  ? 55  VAL H CG1 1 
ATOM   14350 C CG2 . VAL H  2 55  ? -14.075 -6.265   -5.113  1.00 43.68  ? 55  VAL H CG2 1 
ATOM   14351 N N   . ILE H  2 56  ? -10.244 -3.691   -5.137  1.00 59.62  ? 56  ILE H N   1 
ATOM   14352 C CA  . ILE H  2 56  ? -9.440  -2.493   -5.351  1.00 58.49  ? 56  ILE H CA  1 
ATOM   14353 C C   . ILE H  2 56  ? -8.004  -2.816   -5.766  1.00 60.05  ? 56  ILE H C   1 
ATOM   14354 O O   . ILE H  2 56  ? -7.498  -2.280   -6.751  1.00 47.37  ? 56  ILE H O   1 
ATOM   14355 C CB  . ILE H  2 56  ? -9.397  -1.616   -4.084  1.00 59.13  ? 56  ILE H CB  1 
ATOM   14356 C CG1 . ILE H  2 56  ? -10.785 -1.053   -3.770  1.00 56.23  ? 56  ILE H CG1 1 
ATOM   14357 C CG2 . ILE H  2 56  ? -8.389  -0.491   -4.248  1.00 45.90  ? 56  ILE H CG2 1 
ATOM   14358 C CD1 . ILE H  2 56  ? -10.838 -0.244   -2.490  1.00 53.90  ? 56  ILE H CD1 1 
ATOM   14359 N N   . GLU H  2 57  ? -7.357  -3.698   -5.010  1.00 53.56  ? 57  GLU H N   1 
ATOM   14360 C CA  . GLU H  2 57  ? -5.929  -3.965   -5.173  1.00 56.98  ? 57  GLU H CA  1 
ATOM   14361 C C   . GLU H  2 57  ? -5.571  -4.569   -6.530  1.00 59.81  ? 57  GLU H C   1 
ATOM   14362 O O   . GLU H  2 57  ? -4.478  -4.341   -7.051  1.00 65.21  ? 57  GLU H O   1 
ATOM   14363 C CB  . GLU H  2 57  ? -5.424  -4.859   -4.035  1.00 74.40  ? 57  GLU H CB  1 
ATOM   14364 C CG  . GLU H  2 57  ? -3.912  -4.883   -3.873  1.00 108.37 ? 57  GLU H CG  1 
ATOM   14365 C CD  . GLU H  2 57  ? -3.272  -6.111   -4.492  1.00 112.65 ? 57  GLU H CD  1 
ATOM   14366 O OE1 . GLU H  2 57  ? -3.936  -7.167   -4.549  1.00 101.22 ? 57  GLU H OE1 1 
ATOM   14367 O OE2 . GLU H  2 57  ? -2.099  -6.021   -4.913  1.00 102.01 ? 57  GLU H OE2 1 
ATOM   14368 N N   . LYS H  2 58  ? -6.496  -5.330   -7.102  1.00 53.56  ? 58  LYS H N   1 
ATOM   14369 C CA  . LYS H  2 58  ? -6.262  -5.983   -8.385  1.00 55.06  ? 58  LYS H CA  1 
ATOM   14370 C C   . LYS H  2 58  ? -6.231  -5.001   -9.549  1.00 61.16  ? 58  LYS H C   1 
ATOM   14371 O O   . LYS H  2 58  ? -5.819  -5.349   -10.656 1.00 57.88  ? 58  LYS H O   1 
ATOM   14372 C CB  . LYS H  2 58  ? -7.316  -7.061   -8.632  1.00 56.16  ? 58  LYS H CB  1 
ATOM   14373 C CG  . LYS H  2 58  ? -6.997  -8.384   -7.962  1.00 63.13  ? 58  LYS H CG  1 
ATOM   14374 C CD  . LYS H  2 58  ? -5.709  -8.287   -7.162  1.00 62.29  ? 58  LYS H CD  1 
ATOM   14375 C CE  . LYS H  2 58  ? -5.056  -9.644   -6.998  1.00 56.20  ? 58  LYS H CE  1 
ATOM   14376 N NZ  . LYS H  2 58  ? -3.711  -9.524   -6.376  1.00 53.43  ? 58  LYS H NZ  1 
ATOM   14377 N N   . MET H  2 59  ? -6.658  -3.771   -9.294  1.00 52.16  ? 59  MET H N   1 
ATOM   14378 C CA  . MET H  2 59  ? -6.702  -2.764   -10.344 1.00 51.64  ? 59  MET H CA  1 
ATOM   14379 C C   . MET H  2 59  ? -5.374  -2.024   -10.503 1.00 60.20  ? 59  MET H C   1 
ATOM   14380 O O   . MET H  2 59  ? -5.220  -0.901   -10.025 1.00 63.12  ? 59  MET H O   1 
ATOM   14381 C CB  . MET H  2 59  ? -7.841  -1.774   -10.090 1.00 68.07  ? 59  MET H CB  1 
ATOM   14382 C CG  . MET H  2 59  ? -8.010  -0.759   -11.202 1.00 60.61  ? 59  MET H CG  1 
ATOM   14383 S SD  . MET H  2 59  ? -8.123  -1.571   -12.807 1.00 75.45  ? 59  MET H SD  1 
ATOM   14384 C CE  . MET H  2 59  ? -9.894  -1.555   -13.069 1.00 53.51  ? 59  MET H CE  1 
ATOM   14385 N N   . ASN H  2 60  ? -4.415  -2.654   -11.177 1.00 66.25  ? 60  ASN H N   1 
ATOM   14386 C CA  . ASN H  2 60  ? -3.157  -1.982   -11.482 1.00 76.19  ? 60  ASN H CA  1 
ATOM   14387 C C   . ASN H  2 60  ? -3.086  -1.585   -12.950 1.00 73.63  ? 60  ASN H C   1 
ATOM   14388 O O   . ASN H  2 60  ? -2.815  -2.413   -13.823 1.00 77.51  ? 60  ASN H O   1 
ATOM   14389 C CB  . ASN H  2 60  ? -1.953  -2.837   -11.092 1.00 88.78  ? 60  ASN H CB  1 
ATOM   14390 C CG  . ASN H  2 60  ? -0.757  -1.998   -10.688 1.00 105.42 ? 60  ASN H CG  1 
ATOM   14391 O OD1 . ASN H  2 60  ? -0.826  -0.768   -10.675 1.00 116.72 ? 60  ASN H OD1 1 
ATOM   14392 N ND2 . ASN H  2 60  ? 0.343   -2.656   -10.352 1.00 101.41 ? 60  ASN H ND2 1 
ATOM   14393 N N   . THR H  2 61  ? -3.332  -0.304   -13.202 1.00 66.33  ? 61  THR H N   1 
ATOM   14394 C CA  . THR H  2 61  ? -3.448  0.229    -14.550 1.00 68.29  ? 61  THR H CA  1 
ATOM   14395 C C   . THR H  2 61  ? -2.100  0.615    -15.152 1.00 69.41  ? 61  THR H C   1 
ATOM   14396 O O   . THR H  2 61  ? -1.130  0.867    -14.436 1.00 66.95  ? 61  THR H O   1 
ATOM   14397 C CB  . THR H  2 61  ? -4.368  1.463    -14.566 1.00 77.87  ? 61  THR H CB  1 
ATOM   14398 O OG1 . THR H  2 61  ? -3.878  2.438    -13.636 1.00 71.56  ? 61  THR H OG1 1 
ATOM   14399 C CG2 . THR H  2 61  ? -5.784  1.075    -14.173 1.00 64.41  ? 61  THR H CG2 1 
ATOM   14400 N N   . GLN H  2 62  ? -2.054  0.656    -16.479 1.00 69.84  ? 62  GLN H N   1 
ATOM   14401 C CA  . GLN H  2 62  ? -0.859  1.068    -17.200 1.00 72.93  ? 62  GLN H CA  1 
ATOM   14402 C C   . GLN H  2 62  ? -0.765  2.585    -17.222 1.00 73.49  ? 62  GLN H C   1 
ATOM   14403 O O   . GLN H  2 62  ? -1.779  3.276    -17.123 1.00 62.39  ? 62  GLN H O   1 
ATOM   14404 C CB  . GLN H  2 62  ? -0.901  0.538    -18.634 1.00 63.67  ? 62  GLN H CB  1 
ATOM   14405 C CG  . GLN H  2 62  ? -0.796  -0.970   -18.743 1.00 58.13  ? 62  GLN H CG  1 
ATOM   14406 C CD  . GLN H  2 62  ? 0.553   -1.486   -18.289 1.00 68.43  ? 62  GLN H CD  1 
ATOM   14407 O OE1 . GLN H  2 62  ? 0.843   -1.535   -17.094 1.00 87.04  ? 62  GLN H OE1 1 
ATOM   14408 N NE2 . GLN H  2 62  ? 1.389   -1.872   -19.245 1.00 60.43  ? 62  GLN H NE2 1 
ATOM   14409 N N   . PHE H  2 63  ? 0.452   3.106    -17.343 1.00 66.48  ? 63  PHE H N   1 
ATOM   14410 C CA  . PHE H  2 63  ? 0.626   4.539    -17.535 1.00 62.21  ? 63  PHE H CA  1 
ATOM   14411 C C   . PHE H  2 63  ? 0.330   4.869    -18.984 1.00 60.50  ? 63  PHE H C   1 
ATOM   14412 O O   . PHE H  2 63  ? 1.093   4.512    -19.880 1.00 73.15  ? 63  PHE H O   1 
ATOM   14413 C CB  . PHE H  2 63  ? 2.045   4.989    -17.195 1.00 62.99  ? 63  PHE H CB  1 
ATOM   14414 C CG  . PHE H  2 63  ? 2.237   6.479    -17.281 1.00 68.94  ? 63  PHE H CG  1 
ATOM   14415 C CD1 . PHE H  2 63  ? 2.249   7.252    -16.134 1.00 54.79  ? 63  PHE H CD1 1 
ATOM   14416 C CD2 . PHE H  2 63  ? 2.383   7.108    -18.509 1.00 65.29  ? 63  PHE H CD2 1 
ATOM   14417 C CE1 . PHE H  2 63  ? 2.417   8.620    -16.204 1.00 62.01  ? 63  PHE H CE1 1 
ATOM   14418 C CE2 . PHE H  2 63  ? 2.550   8.480    -18.586 1.00 61.56  ? 63  PHE H CE2 1 
ATOM   14419 C CZ  . PHE H  2 63  ? 2.567   9.236    -17.431 1.00 69.09  ? 63  PHE H CZ  1 
ATOM   14420 N N   . THR H  2 64  ? -0.780  5.554    -19.215 1.00 49.62  ? 64  THR H N   1 
ATOM   14421 C CA  . THR H  2 64  ? -1.211  5.830    -20.573 1.00 67.73  ? 64  THR H CA  1 
ATOM   14422 C C   . THR H  2 64  ? -1.816  7.220    -20.659 1.00 53.83  ? 64  THR H C   1 
ATOM   14423 O O   . THR H  2 64  ? -2.388  7.722    -19.694 1.00 50.71  ? 64  THR H O   1 
ATOM   14424 C CB  . THR H  2 64  ? -2.226  4.771    -21.060 1.00 69.79  ? 64  THR H CB  1 
ATOM   14425 O OG1 . THR H  2 64  ? -2.521  4.982    -22.445 1.00 68.04  ? 64  THR H OG1 1 
ATOM   14426 C CG2 . THR H  2 64  ? -3.507  4.846    -20.256 1.00 54.50  ? 64  THR H CG2 1 
ATOM   14427 N N   . ALA H  2 65  ? -1.666  7.856    -21.812 1.00 50.67  ? 65  ALA H N   1 
ATOM   14428 C CA  . ALA H  2 65  ? -2.262  9.166    -22.014 1.00 53.37  ? 65  ALA H CA  1 
ATOM   14429 C C   . ALA H  2 65  ? -3.417  9.083    -22.998 1.00 52.86  ? 65  ALA H C   1 
ATOM   14430 O O   . ALA H  2 65  ? -3.232  9.272    -24.199 1.00 47.02  ? 65  ALA H O   1 
ATOM   14431 C CB  . ALA H  2 65  ? -1.221  10.161   -22.494 1.00 50.17  ? 65  ALA H CB  1 
ATOM   14432 N N   . VAL H  2 66  ? -4.609  8.792    -22.486 1.00 50.18  ? 66  VAL H N   1 
ATOM   14433 C CA  . VAL H  2 66  ? -5.806  8.783    -23.314 1.00 46.15  ? 66  VAL H CA  1 
ATOM   14434 C C   . VAL H  2 66  ? -5.880  10.123   -24.053 1.00 55.84  ? 66  VAL H C   1 
ATOM   14435 O O   . VAL H  2 66  ? -5.255  11.106   -23.643 1.00 67.68  ? 66  VAL H O   1 
ATOM   14436 C CB  . VAL H  2 66  ? -7.080  8.566    -22.469 1.00 40.79  ? 66  VAL H CB  1 
ATOM   14437 C CG1 . VAL H  2 66  ? -8.262  8.189    -23.361 1.00 48.26  ? 66  VAL H CG1 1 
ATOM   14438 C CG2 . VAL H  2 66  ? -6.829  7.512    -21.385 1.00 42.81  ? 66  VAL H CG2 1 
ATOM   14439 N N   . GLY H  2 67  ? -6.606  10.153   -25.164 1.00 50.09  ? 67  GLY H N   1 
ATOM   14440 C CA  . GLY H  2 67  ? -6.769  11.376   -25.928 1.00 68.09  ? 67  GLY H CA  1 
ATOM   14441 C C   . GLY H  2 67  ? -5.646  11.592   -26.921 1.00 53.17  ? 67  GLY H C   1 
ATOM   14442 O O   . GLY H  2 67  ? -4.473  11.626   -26.552 1.00 33.09  ? 67  GLY H O   1 
ATOM   14443 N N   . LYS H  2 68  ? -6.015  11.729   -28.190 1.00 54.88  ? 68  LYS H N   1 
ATOM   14444 C CA  . LYS H  2 68  ? -5.056  11.980   -29.257 1.00 44.60  ? 68  LYS H CA  1 
ATOM   14445 C C   . LYS H  2 68  ? -5.532  13.164   -30.089 1.00 54.71  ? 68  LYS H C   1 
ATOM   14446 O O   . LYS H  2 68  ? -6.677  13.598   -29.963 1.00 48.83  ? 68  LYS H O   1 
ATOM   14447 C CB  . LYS H  2 68  ? -4.907  10.738   -30.136 1.00 50.91  ? 68  LYS H CB  1 
ATOM   14448 C CG  . LYS H  2 68  ? -4.451  9.501    -29.381 1.00 47.21  ? 68  LYS H CG  1 
ATOM   14449 C CD  . LYS H  2 68  ? -2.937  9.371    -29.396 1.00 55.56  ? 68  LYS H CD  1 
ATOM   14450 C CE  . LYS H  2 68  ? -2.445  8.383    -28.350 1.00 65.77  ? 68  LYS H CE  1 
ATOM   14451 N NZ  . LYS H  2 68  ? -2.190  9.046    -27.041 1.00 64.55  ? 68  LYS H NZ  1 
ATOM   14452 N N   . GLU H  2 69  ? -4.653  13.684   -30.938 1.00 54.28  ? 69  GLU H N   1 
ATOM   14453 C CA  . GLU H  2 69  ? -4.993  14.824   -31.780 1.00 52.06  ? 69  GLU H CA  1 
ATOM   14454 C C   . GLU H  2 69  ? -4.879  14.472   -33.257 1.00 45.98  ? 69  GLU H C   1 
ATOM   14455 O O   . GLU H  2 69  ? -3.856  13.950   -33.704 1.00 51.41  ? 69  GLU H O   1 
ATOM   14456 C CB  . GLU H  2 69  ? -4.096  16.017   -31.456 1.00 51.41  ? 69  GLU H CB  1 
ATOM   14457 C CG  . GLU H  2 69  ? -4.230  16.526   -30.031 1.00 68.72  ? 69  GLU H CG  1 
ATOM   14458 C CD  . GLU H  2 69  ? -3.198  17.582   -29.703 1.00 78.95  ? 69  GLU H CD  1 
ATOM   14459 O OE1 . GLU H  2 69  ? -2.143  17.602   -30.370 1.00 77.35  ? 69  GLU H OE1 1 
ATOM   14460 O OE2 . GLU H  2 69  ? -3.439  18.388   -28.779 1.00 72.59  ? 69  GLU H OE2 1 
ATOM   14461 N N   . PHE H  2 70  ? -5.936  14.757   -34.008 1.00 41.32  ? 70  PHE H N   1 
ATOM   14462 C CA  . PHE H  2 70  ? -5.946  14.487   -35.439 1.00 45.39  ? 70  PHE H CA  1 
ATOM   14463 C C   . PHE H  2 70  ? -6.406  15.720   -36.208 1.00 51.13  ? 70  PHE H C   1 
ATOM   14464 O O   . PHE H  2 70  ? -7.222  16.498   -35.710 1.00 58.21  ? 70  PHE H O   1 
ATOM   14465 C CB  . PHE H  2 70  ? -6.861  13.302   -35.757 1.00 39.89  ? 70  PHE H CB  1 
ATOM   14466 C CG  . PHE H  2 70  ? -6.546  12.055   -34.972 1.00 51.75  ? 70  PHE H CG  1 
ATOM   14467 C CD1 . PHE H  2 70  ? -5.526  11.202   -35.369 1.00 42.79  ? 70  PHE H CD1 1 
ATOM   14468 C CD2 . PHE H  2 70  ? -7.285  11.728   -33.847 1.00 45.58  ? 70  PHE H CD2 1 
ATOM   14469 C CE1 . PHE H  2 70  ? -5.244  10.053   -34.651 1.00 43.63  ? 70  PHE H CE1 1 
ATOM   14470 C CE2 . PHE H  2 70  ? -7.009  10.581   -33.127 1.00 36.79  ? 70  PHE H CE2 1 
ATOM   14471 C CZ  . PHE H  2 70  ? -5.988  9.742    -33.530 1.00 43.50  ? 70  PHE H CZ  1 
ATOM   14472 N N   . ASN H  2 71  ? -5.875  15.901   -37.415 1.00 37.96  ? 71  ASN H N   1 
ATOM   14473 C CA  . ASN H  2 71  ? -6.299  17.009   -38.263 1.00 57.18  ? 71  ASN H CA  1 
ATOM   14474 C C   . ASN H  2 71  ? -7.562  16.670   -39.045 1.00 51.55  ? 71  ASN H C   1 
ATOM   14475 O O   . ASN H  2 71  ? -8.047  15.540   -39.000 1.00 46.48  ? 71  ASN H O   1 
ATOM   14476 C CB  . ASN H  2 71  ? -5.177  17.444   -39.210 1.00 61.25  ? 71  ASN H CB  1 
ATOM   14477 C CG  . ASN H  2 71  ? -4.754  16.344   -40.164 1.00 58.14  ? 71  ASN H CG  1 
ATOM   14478 O OD1 . ASN H  2 71  ? -5.583  15.738   -40.841 1.00 51.79  ? 71  ASN H OD1 1 
ATOM   14479 N ND2 . ASN H  2 71  ? -3.455  16.086   -40.227 1.00 66.67  ? 71  ASN H ND2 1 
ATOM   14480 N N   . HIS H  2 72  ? -8.085  17.657   -39.764 1.00 51.39  ? 72  HIS H N   1 
ATOM   14481 C CA  . HIS H  2 72  ? -9.352  17.517   -40.474 1.00 59.70  ? 72  HIS H CA  1 
ATOM   14482 C C   . HIS H  2 72  ? -9.340  16.374   -41.488 1.00 54.73  ? 72  HIS H C   1 
ATOM   14483 O O   . HIS H  2 72  ? -10.393 15.870   -41.882 1.00 60.79  ? 72  HIS H O   1 
ATOM   14484 C CB  . HIS H  2 72  ? -9.711  18.832   -41.166 1.00 66.17  ? 72  HIS H CB  1 
ATOM   14485 C CG  . HIS H  2 72  ? -8.666  19.314   -42.122 1.00 85.40  ? 72  HIS H CG  1 
ATOM   14486 N ND1 . HIS H  2 72  ? -7.553  20.017   -41.717 1.00 90.42  ? 72  HIS H ND1 1 
ATOM   14487 C CD2 . HIS H  2 72  ? -8.563  19.191   -43.467 1.00 74.36  ? 72  HIS H CD2 1 
ATOM   14488 C CE1 . HIS H  2 72  ? -6.809  20.308   -42.769 1.00 100.46 ? 72  HIS H CE1 1 
ATOM   14489 N NE2 . HIS H  2 72  ? -7.402  19.817   -43.844 1.00 88.37  ? 72  HIS H NE2 1 
ATOM   14490 N N   . LEU H  2 73  ? -8.147  15.969   -41.908 1.00 53.24  ? 73  LEU H N   1 
ATOM   14491 C CA  . LEU H  2 73  ? -8.008  14.884   -42.871 1.00 52.81  ? 73  LEU H CA  1 
ATOM   14492 C C   . LEU H  2 73  ? -7.670  13.560   -42.188 1.00 62.32  ? 73  LEU H C   1 
ATOM   14493 O O   . LEU H  2 73  ? -7.182  12.628   -42.828 1.00 56.78  ? 73  LEU H O   1 
ATOM   14494 C CB  . LEU H  2 73  ? -6.956  15.229   -43.929 1.00 56.78  ? 73  LEU H CB  1 
ATOM   14495 C CG  . LEU H  2 73  ? -7.339  16.327   -44.926 1.00 65.39  ? 73  LEU H CG  1 
ATOM   14496 C CD1 . LEU H  2 73  ? -6.155  16.708   -45.803 1.00 55.94  ? 73  LEU H CD1 1 
ATOM   14497 C CD2 . LEU H  2 73  ? -8.523  15.891   -45.776 1.00 43.78  ? 73  LEU H CD2 1 
ATOM   14498 N N   . GLU H  2 74  ? -7.939  13.479   -40.889 1.00 53.87  ? 74  GLU H N   1 
ATOM   14499 C CA  . GLU H  2 74  ? -7.695  12.252   -40.135 1.00 43.56  ? 74  GLU H CA  1 
ATOM   14500 C C   . GLU H  2 74  ? -8.904  11.852   -39.297 1.00 52.64  ? 74  GLU H C   1 
ATOM   14501 O O   . GLU H  2 74  ? -8.765  11.265   -38.225 1.00 50.62  ? 74  GLU H O   1 
ATOM   14502 C CB  . GLU H  2 74  ? -6.451  12.391   -39.267 1.00 45.81  ? 74  GLU H CB  1 
ATOM   14503 C CG  . GLU H  2 74  ? -5.187  12.525   -40.082 1.00 40.02  ? 74  GLU H CG  1 
ATOM   14504 C CD  . GLU H  2 74  ? -3.974  12.800   -39.234 1.00 58.43  ? 74  GLU H CD  1 
ATOM   14505 O OE1 . GLU H  2 74  ? -4.040  13.701   -38.372 1.00 56.76  ? 74  GLU H OE1 1 
ATOM   14506 O OE2 . GLU H  2 74  ? -2.951  12.119   -39.443 1.00 45.02  ? 74  GLU H OE2 1 
ATOM   14507 N N   . LYS H  2 75  ? -10.088 12.167   -39.809 1.00 46.43  ? 75  LYS H N   1 
ATOM   14508 C CA  . LYS H  2 75  ? -11.342 11.842   -39.141 1.00 51.19  ? 75  LYS H CA  1 
ATOM   14509 C C   . LYS H  2 75  ? -11.547 10.335   -38.943 1.00 50.85  ? 75  LYS H C   1 
ATOM   14510 O O   . LYS H  2 75  ? -12.185 9.917    -37.976 1.00 51.88  ? 75  LYS H O   1 
ATOM   14511 C CB  . LYS H  2 75  ? -12.519 12.442   -39.916 1.00 46.74  ? 75  LYS H CB  1 
ATOM   14512 C CG  . LYS H  2 75  ? -13.881 12.120   -39.330 1.00 54.98  ? 75  LYS H CG  1 
ATOM   14513 C CD  . LYS H  2 75  ? -14.022 12.655   -37.913 1.00 64.59  ? 75  LYS H CD  1 
ATOM   14514 C CE  . LYS H  2 75  ? -14.244 14.159   -37.898 1.00 81.93  ? 75  LYS H CE  1 
ATOM   14515 N NZ  . LYS H  2 75  ? -14.421 14.675   -36.511 1.00 93.12  ? 75  LYS H NZ  1 
ATOM   14516 N N   . ARG H  2 76  ? -11.014 9.523    -39.853 1.00 50.91  ? 76  ARG H N   1 
ATOM   14517 C CA  . ARG H  2 76  ? -11.160 8.070    -39.747 1.00 41.00  ? 76  ARG H CA  1 
ATOM   14518 C C   . ARG H  2 76  ? -10.445 7.508    -38.521 1.00 46.95  ? 76  ARG H C   1 
ATOM   14519 O O   . ARG H  2 76  ? -11.047 6.789    -37.723 1.00 41.81  ? 76  ARG H O   1 
ATOM   14520 C CB  . ARG H  2 76  ? -10.669 7.361    -41.015 1.00 37.16  ? 76  ARG H CB  1 
ATOM   14521 C CG  . ARG H  2 76  ? -11.698 7.280    -42.139 1.00 35.62  ? 76  ARG H CG  1 
ATOM   14522 C CD  . ARG H  2 76  ? -11.080 6.681    -43.394 1.00 42.48  ? 76  ARG H CD  1 
ATOM   14523 N NE  . ARG H  2 76  ? -9.829  7.352    -43.734 1.00 45.47  ? 76  ARG H NE  1 
ATOM   14524 C CZ  . ARG H  2 76  ? -8.803  6.770    -44.343 1.00 41.62  ? 76  ARG H CZ  1 
ATOM   14525 N NH1 . ARG H  2 76  ? -8.869  5.492    -44.688 1.00 48.00  ? 76  ARG H NH1 1 
ATOM   14526 N NH2 . ARG H  2 76  ? -7.705  7.467    -44.604 1.00 43.43  ? 76  ARG H NH2 1 
ATOM   14527 N N   . ILE H  2 77  ? -9.163  7.829    -38.373 1.00 47.77  ? 77  ILE H N   1 
ATOM   14528 C CA  . ILE H  2 77  ? -8.411  7.376    -37.208 1.00 37.86  ? 77  ILE H CA  1 
ATOM   14529 C C   . ILE H  2 77  ? -8.926  8.032    -35.932 1.00 35.91  ? 77  ILE H C   1 
ATOM   14530 O O   . ILE H  2 77  ? -8.837  7.453    -34.850 1.00 36.01  ? 77  ILE H O   1 
ATOM   14531 C CB  . ILE H  2 77  ? -6.892  7.621    -37.350 1.00 37.72  ? 77  ILE H CB  1 
ATOM   14532 C CG1 . ILE H  2 77  ? -6.620  8.987    -37.981 1.00 58.56  ? 77  ILE H CG1 1 
ATOM   14533 C CG2 . ILE H  2 77  ? -6.249  6.520    -38.179 1.00 40.34  ? 77  ILE H CG2 1 
ATOM   14534 C CD1 . ILE H  2 77  ? -5.148  9.268    -38.208 1.00 59.93  ? 77  ILE H CD1 1 
ATOM   14535 N N   . GLU H  2 78  ? -9.468  9.240    -36.060 1.00 34.43  ? 78  GLU H N   1 
ATOM   14536 C CA  . GLU H  2 78  ? -10.072 9.913    -34.919 1.00 42.51  ? 78  GLU H CA  1 
ATOM   14537 C C   . GLU H  2 78  ? -11.275 9.115    -34.434 1.00 44.48  ? 78  GLU H C   1 
ATOM   14538 O O   . GLU H  2 78  ? -11.510 8.993    -33.232 1.00 45.54  ? 78  GLU H O   1 
ATOM   14539 C CB  . GLU H  2 78  ? -10.502 11.333   -35.284 1.00 45.01  ? 78  GLU H CB  1 
ATOM   14540 C CG  . GLU H  2 78  ? -11.189 12.063   -34.143 1.00 47.49  ? 78  GLU H CG  1 
ATOM   14541 C CD  . GLU H  2 78  ? -11.713 13.427   -34.545 1.00 80.77  ? 78  GLU H CD  1 
ATOM   14542 O OE1 . GLU H  2 78  ? -11.167 14.019   -35.498 1.00 91.07  ? 78  GLU H OE1 1 
ATOM   14543 O OE2 . GLU H  2 78  ? -12.671 13.908   -33.903 1.00 85.93  ? 78  GLU H OE2 1 
ATOM   14544 N N   . ASN H  2 79  ? -12.035 8.572    -35.380 1.00 36.31  ? 79  ASN H N   1 
ATOM   14545 C CA  . ASN H  2 79  ? -13.193 7.747    -35.054 1.00 36.84  ? 79  ASN H CA  1 
ATOM   14546 C C   . ASN H  2 79  ? -12.797 6.353    -34.570 1.00 41.06  ? 79  ASN H C   1 
ATOM   14547 O O   . ASN H  2 79  ? -13.448 5.784    -33.696 1.00 43.16  ? 79  ASN H O   1 
ATOM   14548 C CB  . ASN H  2 79  ? -14.151 7.660    -36.245 1.00 44.86  ? 79  ASN H CB  1 
ATOM   14549 C CG  . ASN H  2 79  ? -14.984 8.917    -36.413 1.00 61.38  ? 79  ASN H CG  1 
ATOM   14550 O OD1 . ASN H  2 79  ? -15.281 9.611    -35.442 1.00 59.96  ? 79  ASN H OD1 1 
ATOM   14551 N ND2 . ASN H  2 79  ? -15.366 9.214    -37.650 1.00 48.19  ? 79  ASN H ND2 1 
ATOM   14552 N N   . LEU H  2 80  ? -11.727 5.807    -35.138 1.00 39.77  ? 80  LEU H N   1 
ATOM   14553 C CA  . LEU H  2 80  ? -11.170 4.558    -34.640 1.00 33.46  ? 80  LEU H CA  1 
ATOM   14554 C C   . LEU H  2 80  ? -10.778 4.737    -33.181 1.00 35.17  ? 80  LEU H C   1 
ATOM   14555 O O   . LEU H  2 80  ? -11.092 3.904    -32.330 1.00 37.13  ? 80  LEU H O   1 
ATOM   14556 C CB  . LEU H  2 80  ? -9.954  4.146    -35.470 1.00 31.32  ? 80  LEU H CB  1 
ATOM   14557 C CG  . LEU H  2 80  ? -9.137  2.965    -34.937 1.00 33.90  ? 80  LEU H CG  1 
ATOM   14558 C CD1 . LEU H  2 80  ? -10.017 1.786    -34.539 1.00 29.65  ? 80  LEU H CD1 1 
ATOM   14559 C CD2 . LEU H  2 80  ? -8.071  2.560    -35.943 1.00 27.54  ? 80  LEU H CD2 1 
ATOM   14560 N N   . ASN H  2 81  ? -10.090 5.840    -32.907 1.00 31.92  ? 81  ASN H N   1 
ATOM   14561 C CA  . ASN H  2 81  ? -9.692  6.183    -31.553 1.00 33.40  ? 81  ASN H CA  1 
ATOM   14562 C C   . ASN H  2 81  ? -10.899 6.346    -30.642 1.00 43.99  ? 81  ASN H C   1 
ATOM   14563 O O   . ASN H  2 81  ? -10.913 5.846    -29.518 1.00 51.43  ? 81  ASN H O   1 
ATOM   14564 C CB  . ASN H  2 81  ? -8.864  7.465    -31.548 1.00 33.80  ? 81  ASN H CB  1 
ATOM   14565 C CG  . ASN H  2 81  ? -8.478  7.896    -30.151 1.00 48.33  ? 81  ASN H CG  1 
ATOM   14566 O OD1 . ASN H  2 81  ? -7.733  7.202    -29.461 1.00 55.03  ? 81  ASN H OD1 1 
ATOM   14567 N ND2 . ASN H  2 81  ? -8.987  9.045    -29.723 1.00 49.62  ? 81  ASN H ND2 1 
ATOM   14568 N N   . LYS H  2 82  ? -11.911 7.054    -31.129 1.00 38.90  ? 82  LYS H N   1 
ATOM   14569 C CA  . LYS H  2 82  ? -13.143 7.214    -30.373 1.00 40.86  ? 82  LYS H CA  1 
ATOM   14570 C C   . LYS H  2 82  ? -13.774 5.853    -30.093 1.00 43.83  ? 82  LYS H C   1 
ATOM   14571 O O   . LYS H  2 82  ? -14.436 5.667    -29.074 1.00 35.65  ? 82  LYS H O   1 
ATOM   14572 C CB  . LYS H  2 82  ? -14.128 8.122    -31.114 1.00 48.10  ? 82  LYS H CB  1 
ATOM   14573 C CG  . LYS H  2 82  ? -15.525 8.146    -30.508 1.00 58.45  ? 82  LYS H CG  1 
ATOM   14574 C CD  . LYS H  2 82  ? -16.448 9.090    -31.261 1.00 64.34  ? 82  LYS H CD  1 
ATOM   14575 C CE  . LYS H  2 82  ? -17.889 8.941    -30.796 1.00 88.73  ? 82  LYS H CE  1 
ATOM   14576 N NZ  . LYS H  2 82  ? -18.028 9.109    -29.323 1.00 79.77  ? 82  LYS H NZ  1 
ATOM   14577 N N   . LYS H  2 83  ? -13.556 4.899    -30.995 1.00 50.14  ? 83  LYS H N   1 
ATOM   14578 C CA  . LYS H  2 83  ? -14.131 3.566    -30.833 1.00 39.24  ? 83  LYS H CA  1 
ATOM   14579 C C   . LYS H  2 83  ? -13.498 2.775    -29.693 1.00 37.65  ? 83  LYS H C   1 
ATOM   14580 O O   . LYS H  2 83  ? -14.197 2.119    -28.925 1.00 36.98  ? 83  LYS H O   1 
ATOM   14581 C CB  . LYS H  2 83  ? -14.087 2.768    -32.141 1.00 28.47  ? 83  LYS H CB  1 
ATOM   14582 C CG  . LYS H  2 83  ? -14.778 1.413    -32.035 1.00 28.56  ? 83  LYS H CG  1 
ATOM   14583 C CD  . LYS H  2 83  ? -15.038 0.765    -33.388 1.00 29.50  ? 83  LYS H CD  1 
ATOM   14584 C CE  . LYS H  2 83  ? -13.756 0.297    -34.052 1.00 36.38  ? 83  LYS H CE  1 
ATOM   14585 N NZ  . LYS H  2 83  ? -14.044 -0.629   -35.185 1.00 44.95  ? 83  LYS H NZ  1 
ATOM   14586 N N   . VAL H  2 84  ? -12.176 2.832    -29.587 1.00 26.35  ? 84  VAL H N   1 
ATOM   14587 C CA  . VAL H  2 84  ? -11.488 2.157    -28.491 1.00 39.37  ? 84  VAL H CA  1 
ATOM   14588 C C   . VAL H  2 84  ? -11.965 2.742    -27.157 1.00 37.00  ? 84  VAL H C   1 
ATOM   14589 O O   . VAL H  2 84  ? -12.251 2.009    -26.203 1.00 44.03  ? 84  VAL H O   1 
ATOM   14590 C CB  . VAL H  2 84  ? -9.958  2.306    -28.595 1.00 32.75  ? 84  VAL H CB  1 
ATOM   14591 C CG1 . VAL H  2 84  ? -9.308  0.944    -28.779 1.00 44.68  ? 84  VAL H CG1 1 
ATOM   14592 C CG2 . VAL H  2 84  ? -9.598  3.234    -29.738 1.00 48.71  ? 84  VAL H CG2 1 
ATOM   14593 N N   . ASP H  2 85  ? -12.096 4.066    -27.118 1.00 32.80  ? 85  ASP H N   1 
ATOM   14594 C CA  . ASP H  2 85  ? -12.521 4.770    -25.915 1.00 34.79  ? 85  ASP H CA  1 
ATOM   14595 C C   . ASP H  2 85  ? -13.941 4.394    -25.504 1.00 40.11  ? 85  ASP H C   1 
ATOM   14596 O O   . ASP H  2 85  ? -14.206 4.130    -24.331 1.00 40.71  ? 85  ASP H O   1 
ATOM   14597 C CB  . ASP H  2 85  ? -12.381 6.280    -26.118 1.00 35.21  ? 85  ASP H CB  1 
ATOM   14598 C CG  . ASP H  2 85  ? -10.932 6.731    -26.090 1.00 54.36  ? 85  ASP H CG  1 
ATOM   14599 O OD1 . ASP H  2 85  ? -10.074 5.909    -25.701 1.00 48.53  ? 85  ASP H OD1 1 
ATOM   14600 O OD2 . ASP H  2 85  ? -10.647 7.895    -26.446 1.00 65.67  ? 85  ASP H OD2 1 
ATOM   14601 N N   . ASP H  2 86  ? -14.848 4.364    -26.473 1.00 34.23  ? 86  ASP H N   1 
ATOM   14602 C CA  . ASP H  2 86  ? -16.229 3.987    -26.209 1.00 31.66  ? 86  ASP H CA  1 
ATOM   14603 C C   . ASP H  2 86  ? -16.363 2.494    -25.919 1.00 47.44  ? 86  ASP H C   1 
ATOM   14604 O O   . ASP H  2 86  ? -17.292 2.070    -25.232 1.00 43.48  ? 86  ASP H O   1 
ATOM   14605 C CB  . ASP H  2 86  ? -17.124 4.397    -27.376 1.00 52.31  ? 86  ASP H CB  1 
ATOM   14606 C CG  . ASP H  2 86  ? -17.354 5.893    -27.426 1.00 72.25  ? 86  ASP H CG  1 
ATOM   14607 O OD1 . ASP H  2 86  ? -17.026 6.576    -26.432 1.00 72.34  ? 86  ASP H OD1 1 
ATOM   14608 O OD2 . ASP H  2 86  ? -17.865 6.387    -28.451 1.00 77.61  ? 86  ASP H OD2 1 
ATOM   14609 N N   . GLY H  2 87  ? -15.431 1.703    -26.440 1.00 44.15  ? 87  GLY H N   1 
ATOM   14610 C CA  . GLY H  2 87  ? -15.420 0.275    -26.180 1.00 32.88  ? 87  GLY H CA  1 
ATOM   14611 C C   . GLY H  2 87  ? -15.031 -0.023   -24.746 1.00 35.33  ? 87  GLY H C   1 
ATOM   14612 O O   . GLY H  2 87  ? -15.752 -0.716   -24.026 1.00 40.48  ? 87  GLY H O   1 
ATOM   14613 N N   . PHE H  2 88  ? -13.885 0.506    -24.330 1.00 35.08  ? 88  PHE H N   1 
ATOM   14614 C CA  . PHE H  2 88  ? -13.415 0.334    -22.961 1.00 38.59  ? 88  PHE H CA  1 
ATOM   14615 C C   . PHE H  2 88  ? -14.413 0.918    -21.970 1.00 39.85  ? 88  PHE H C   1 
ATOM   14616 O O   . PHE H  2 88  ? -14.580 0.404    -20.865 1.00 35.55  ? 88  PHE H O   1 
ATOM   14617 C CB  . PHE H  2 88  ? -12.046 0.990    -22.771 1.00 31.29  ? 88  PHE H CB  1 
ATOM   14618 C CG  . PHE H  2 88  ? -10.938 0.314    -23.526 1.00 34.22  ? 88  PHE H CG  1 
ATOM   14619 C CD1 . PHE H  2 88  ? -9.783  1.005    -23.854 1.00 33.88  ? 88  PHE H CD1 1 
ATOM   14620 C CD2 . PHE H  2 88  ? -11.050 -1.013   -23.908 1.00 35.15  ? 88  PHE H CD2 1 
ATOM   14621 C CE1 . PHE H  2 88  ? -8.760  0.385    -24.547 1.00 35.20  ? 88  PHE H CE1 1 
ATOM   14622 C CE2 . PHE H  2 88  ? -10.031 -1.638   -24.602 1.00 35.47  ? 88  PHE H CE2 1 
ATOM   14623 C CZ  . PHE H  2 88  ? -8.886  -0.938   -24.923 1.00 34.58  ? 88  PHE H CZ  1 
ATOM   14624 N N   . LEU H  2 89  ? -15.074 1.998    -22.375 1.00 38.86  ? 89  LEU H N   1 
ATOM   14625 C CA  . LEU H  2 89  ? -16.070 2.646    -21.531 1.00 37.07  ? 89  LEU H CA  1 
ATOM   14626 C C   . LEU H  2 89  ? -17.252 1.719    -21.267 1.00 42.74  ? 89  LEU H C   1 
ATOM   14627 O O   . LEU H  2 89  ? -17.734 1.619    -20.139 1.00 43.50  ? 89  LEU H O   1 
ATOM   14628 C CB  . LEU H  2 89  ? -16.552 3.948    -22.174 1.00 33.20  ? 89  LEU H CB  1 
ATOM   14629 C CG  . LEU H  2 89  ? -17.692 4.674    -21.457 1.00 40.88  ? 89  LEU H CG  1 
ATOM   14630 C CD1 . LEU H  2 89  ? -17.354 4.895    -19.993 1.00 43.98  ? 89  LEU H CD1 1 
ATOM   14631 C CD2 . LEU H  2 89  ? -18.007 5.993    -22.143 1.00 38.30  ? 89  LEU H CD2 1 
ATOM   14632 N N   . ASP H  2 90  ? -17.710 1.039    -22.313 1.00 38.71  ? 90  ASP H N   1 
ATOM   14633 C CA  . ASP H  2 90  ? -18.849 0.133    -22.203 1.00 34.87  ? 90  ASP H CA  1 
ATOM   14634 C C   . ASP H  2 90  ? -18.510 -1.131   -21.417 1.00 35.86  ? 90  ASP H C   1 
ATOM   14635 O O   . ASP H  2 90  ? -19.323 -1.618   -20.631 1.00 39.33  ? 90  ASP H O   1 
ATOM   14636 C CB  . ASP H  2 90  ? -19.388 -0.226   -23.591 1.00 35.49  ? 90  ASP H CB  1 
ATOM   14637 C CG  . ASP H  2 90  ? -20.176 0.907    -24.221 1.00 57.99  ? 90  ASP H CG  1 
ATOM   14638 O OD1 . ASP H  2 90  ? -20.650 1.789    -23.473 1.00 69.28  ? 90  ASP H OD1 1 
ATOM   14639 O OD2 . ASP H  2 90  ? -20.328 0.913    -25.461 1.00 63.01  ? 90  ASP H OD2 1 
ATOM   14640 N N   . ILE H  2 91  ? -17.309 -1.659   -21.633 1.00 35.65  ? 91  ILE H N   1 
ATOM   14641 C CA  . ILE H  2 91  ? -16.861 -2.851   -20.920 1.00 36.34  ? 91  ILE H CA  1 
ATOM   14642 C C   . ILE H  2 91  ? -16.745 -2.589   -19.424 1.00 42.49  ? 91  ILE H C   1 
ATOM   14643 O O   . ILE H  2 91  ? -17.317 -3.313   -18.609 1.00 42.52  ? 91  ILE H O   1 
ATOM   14644 C CB  . ILE H  2 91  ? -15.496 -3.341   -21.437 1.00 31.99  ? 91  ILE H CB  1 
ATOM   14645 C CG1 . ILE H  2 91  ? -15.607 -3.803   -22.890 1.00 38.49  ? 91  ILE H CG1 1 
ATOM   14646 C CG2 . ILE H  2 91  ? -14.972 -4.469   -20.562 1.00 39.64  ? 91  ILE H CG2 1 
ATOM   14647 C CD1 . ILE H  2 91  ? -14.295 -4.266   -23.484 1.00 49.94  ? 91  ILE H CD1 1 
ATOM   14648 N N   . TRP H  2 92  ? -16.002 -1.545   -19.070 1.00 34.76  ? 92  TRP H N   1 
ATOM   14649 C CA  . TRP H  2 92  ? -15.749 -1.222   -17.671 1.00 28.60  ? 92  TRP H CA  1 
ATOM   14650 C C   . TRP H  2 92  ? -17.008 -0.823   -16.907 1.00 36.63  ? 92  TRP H C   1 
ATOM   14651 O O   . TRP H  2 92  ? -17.184 -1.206   -15.752 1.00 42.72  ? 92  TRP H O   1 
ATOM   14652 C CB  . TRP H  2 92  ? -14.681 -0.134   -17.553 1.00 29.70  ? 92  TRP H CB  1 
ATOM   14653 C CG  . TRP H  2 92  ? -13.304 -0.661   -17.768 1.00 39.29  ? 92  TRP H CG  1 
ATOM   14654 C CD1 . TRP H  2 92  ? -12.450 -0.344   -18.783 1.00 34.45  ? 92  TRP H CD1 1 
ATOM   14655 C CD2 . TRP H  2 92  ? -12.624 -1.622   -16.956 1.00 39.52  ? 92  TRP H CD2 1 
ATOM   14656 N NE1 . TRP H  2 92  ? -11.274 -1.042   -18.646 1.00 42.17  ? 92  TRP H NE1 1 
ATOM   14657 C CE2 . TRP H  2 92  ? -11.356 -1.834   -17.532 1.00 33.87  ? 92  TRP H CE2 1 
ATOM   14658 C CE3 . TRP H  2 92  ? -12.962 -2.321   -15.793 1.00 40.24  ? 92  TRP H CE3 1 
ATOM   14659 C CZ2 . TRP H  2 92  ? -10.427 -2.715   -16.985 1.00 37.24  ? 92  TRP H CZ2 1 
ATOM   14660 C CZ3 . TRP H  2 92  ? -12.040 -3.195   -15.252 1.00 45.22  ? 92  TRP H CZ3 1 
ATOM   14661 C CH2 . TRP H  2 92  ? -10.786 -3.385   -15.848 1.00 49.77  ? 92  TRP H CH2 1 
ATOM   14662 N N   . THR H  2 93  ? -17.878 -0.054   -17.552 1.00 43.90  ? 93  THR H N   1 
ATOM   14663 C CA  . THR H  2 93  ? -19.135 0.339    -16.930 1.00 40.44  ? 93  THR H CA  1 
ATOM   14664 C C   . THR H  2 93  ? -19.979 -0.889   -16.613 1.00 39.47  ? 93  THR H C   1 
ATOM   14665 O O   . THR H  2 93  ? -20.433 -1.068   -15.484 1.00 42.72  ? 93  THR H O   1 
ATOM   14666 C CB  . THR H  2 93  ? -19.944 1.291    -17.829 1.00 38.35  ? 93  THR H CB  1 
ATOM   14667 O OG1 . THR H  2 93  ? -19.211 2.507    -18.022 1.00 34.86  ? 93  THR H OG1 1 
ATOM   14668 C CG2 . THR H  2 93  ? -21.287 1.612    -17.189 1.00 34.89  ? 93  THR H CG2 1 
ATOM   14669 N N   . TYR H  2 94  ? -20.175 -1.739   -17.616 1.00 43.81  ? 94  TYR H N   1 
ATOM   14670 C CA  . TYR H  2 94  ? -20.994 -2.933   -17.455 1.00 37.07  ? 94  TYR H CA  1 
ATOM   14671 C C   . TYR H  2 94  ? -20.416 -3.875   -16.403 1.00 37.63  ? 94  TYR H C   1 
ATOM   14672 O O   . TYR H  2 94  ? -21.133 -4.342   -15.519 1.00 33.29  ? 94  TYR H O   1 
ATOM   14673 C CB  . TYR H  2 94  ? -21.150 -3.664   -18.790 1.00 31.35  ? 94  TYR H CB  1 
ATOM   14674 C CG  . TYR H  2 94  ? -22.145 -4.801   -18.748 1.00 37.13  ? 94  TYR H CG  1 
ATOM   14675 C CD1 . TYR H  2 94  ? -23.511 -4.551   -18.753 1.00 38.08  ? 94  TYR H CD1 1 
ATOM   14676 C CD2 . TYR H  2 94  ? -21.721 -6.122   -18.707 1.00 41.21  ? 94  TYR H CD2 1 
ATOM   14677 C CE1 . TYR H  2 94  ? -24.426 -5.585   -18.715 1.00 48.06  ? 94  TYR H CE1 1 
ATOM   14678 C CE2 . TYR H  2 94  ? -22.630 -7.163   -18.669 1.00 42.84  ? 94  TYR H CE2 1 
ATOM   14679 C CZ  . TYR H  2 94  ? -23.981 -6.889   -18.674 1.00 52.35  ? 94  TYR H CZ  1 
ATOM   14680 O OH  . TYR H  2 94  ? -24.890 -7.920   -18.637 1.00 54.72  ? 94  TYR H OH  1 
ATOM   14681 N N   . ASN H  2 95  ? -19.119 -4.150   -16.499 1.00 42.75  ? 95  ASN H N   1 
ATOM   14682 C CA  . ASN H  2 95  ? -18.463 -5.049   -15.555 1.00 41.96  ? 95  ASN H CA  1 
ATOM   14683 C C   . ASN H  2 95  ? -18.486 -4.523   -14.123 1.00 46.63  ? 95  ASN H C   1 
ATOM   14684 O O   . ASN H  2 95  ? -18.746 -5.273   -13.183 1.00 45.63  ? 95  ASN H O   1 
ATOM   14685 C CB  . ASN H  2 95  ? -17.025 -5.341   -15.990 1.00 35.68  ? 95  ASN H CB  1 
ATOM   14686 C CG  . ASN H  2 95  ? -16.956 -6.229   -17.218 1.00 54.98  ? 95  ASN H CG  1 
ATOM   14687 O OD1 . ASN H  2 95  ? -17.948 -6.409   -17.926 1.00 54.59  ? 95  ASN H OD1 1 
ATOM   14688 N ND2 . ASN H  2 95  ? -15.781 -6.790   -17.477 1.00 57.47  ? 95  ASN H ND2 1 
ATOM   14689 N N   . ALA H  2 96  ? -18.215 -3.232   -13.962 1.00 41.44  ? 96  ALA H N   1 
ATOM   14690 C CA  . ALA H  2 96  ? -18.209 -2.613   -12.642 1.00 40.03  ? 96  ALA H CA  1 
ATOM   14691 C C   . ALA H  2 96  ? -19.597 -2.643   -12.007 1.00 49.27  ? 96  ALA H C   1 
ATOM   14692 O O   . ALA H  2 96  ? -19.741 -2.958   -10.826 1.00 49.48  ? 96  ALA H O   1 
ATOM   14693 C CB  . ALA H  2 96  ? -17.693 -1.187   -12.727 1.00 41.97  ? 96  ALA H CB  1 
ATOM   14694 N N   . GLU H  2 97  ? -20.613 -2.311   -12.797 1.00 37.26  ? 97  GLU H N   1 
ATOM   14695 C CA  . GLU H  2 97  ? -21.994 -2.328   -12.324 1.00 42.44  ? 97  GLU H CA  1 
ATOM   14696 C C   . GLU H  2 97  ? -22.409 -3.729   -11.880 1.00 42.73  ? 97  GLU H C   1 
ATOM   14697 O O   . GLU H  2 97  ? -22.974 -3.906   -10.800 1.00 40.99  ? 97  GLU H O   1 
ATOM   14698 C CB  . GLU H  2 97  ? -22.942 -1.820   -13.414 1.00 52.81  ? 97  GLU H CB  1 
ATOM   14699 C CG  . GLU H  2 97  ? -22.789 -0.342   -13.756 1.00 46.20  ? 97  GLU H CG  1 
ATOM   14700 C CD  . GLU H  2 97  ? -23.416 0.574    -12.721 1.00 60.12  ? 97  GLU H CD  1 
ATOM   14701 O OE1 . GLU H  2 97  ? -23.636 1.763    -13.034 1.00 63.32  ? 97  GLU H OE1 1 
ATOM   14702 O OE2 . GLU H  2 97  ? -23.696 0.107    -11.597 1.00 77.36  ? 97  GLU H OE2 1 
ATOM   14703 N N   . LEU H  2 98  ? -22.125 -4.719   -12.722 1.00 41.89  ? 98  LEU H N   1 
ATOM   14704 C CA  . LEU H  2 98  ? -22.458 -6.109   -12.425 1.00 40.19  ? 98  LEU H CA  1 
ATOM   14705 C C   . LEU H  2 98  ? -21.653 -6.655   -11.249 1.00 46.35  ? 98  LEU H C   1 
ATOM   14706 O O   . LEU H  2 98  ? -22.174 -7.418   -10.435 1.00 44.81  ? 98  LEU H O   1 
ATOM   14707 C CB  . LEU H  2 98  ? -22.241 -6.990   -13.658 1.00 38.19  ? 98  LEU H CB  1 
ATOM   14708 C CG  . LEU H  2 98  ? -23.446 -7.256   -14.566 1.00 44.40  ? 98  LEU H CG  1 
ATOM   14709 C CD1 . LEU H  2 98  ? -24.359 -8.325   -13.977 1.00 60.12  ? 98  LEU H CD1 1 
ATOM   14710 C CD2 . LEU H  2 98  ? -24.216 -5.975   -14.856 1.00 49.58  ? 98  LEU H CD2 1 
ATOM   14711 N N   . LEU H  2 99  ? -20.384 -6.267   -11.167 1.00 47.70  ? 99  LEU H N   1 
ATOM   14712 C CA  . LEU H  2 99  ? -19.513 -6.731   -10.091 1.00 55.94  ? 99  LEU H CA  1 
ATOM   14713 C C   . LEU H  2 99  ? -20.069 -6.337   -8.730  1.00 45.83  ? 99  LEU H C   1 
ATOM   14714 O O   . LEU H  2 99  ? -20.116 -7.151   -7.808  1.00 52.88  ? 99  LEU H O   1 
ATOM   14715 C CB  . LEU H  2 99  ? -18.099 -6.169   -10.253 1.00 49.88  ? 99  LEU H CB  1 
ATOM   14716 C CG  . LEU H  2 99  ? -17.097 -6.598   -9.177  1.00 51.07  ? 99  LEU H CG  1 
ATOM   14717 C CD1 . LEU H  2 99  ? -16.888 -8.105   -9.212  1.00 51.40  ? 99  LEU H CD1 1 
ATOM   14718 C CD2 . LEU H  2 99  ? -15.773 -5.867   -9.339  1.00 48.48  ? 99  LEU H CD2 1 
ATOM   14719 N N   . VAL H  2 100 ? -20.485 -5.081   -8.610  1.00 36.92  ? 100 VAL H N   1 
ATOM   14720 C CA  . VAL H  2 100 ? -21.055 -4.585   -7.365  1.00 47.38  ? 100 VAL H CA  1 
ATOM   14721 C C   . VAL H  2 100 ? -22.343 -5.324   -7.021  1.00 48.62  ? 100 VAL H C   1 
ATOM   14722 O O   . VAL H  2 100 ? -22.528 -5.768   -5.888  1.00 64.25  ? 100 VAL H O   1 
ATOM   14723 C CB  . VAL H  2 100 ? -21.331 -3.071   -7.432  1.00 48.22  ? 100 VAL H CB  1 
ATOM   14724 C CG1 . VAL H  2 100 ? -22.164 -2.631   -6.241  1.00 42.29  ? 100 VAL H CG1 1 
ATOM   14725 C CG2 . VAL H  2 100 ? -20.024 -2.298   -7.490  1.00 47.97  ? 100 VAL H CG2 1 
ATOM   14726 N N   . LEU H  2 101 ? -23.230 -5.456   -8.003  1.00 46.78  ? 101 LEU H N   1 
ATOM   14727 C CA  . LEU H  2 101 ? -24.491 -6.157   -7.792  1.00 48.07  ? 101 LEU H CA  1 
ATOM   14728 C C   . LEU H  2 101 ? -24.241 -7.574   -7.290  1.00 49.27  ? 101 LEU H C   1 
ATOM   14729 O O   . LEU H  2 101 ? -24.752 -7.968   -6.241  1.00 51.68  ? 101 LEU H O   1 
ATOM   14730 C CB  . LEU H  2 101 ? -25.322 -6.195   -9.076  1.00 40.25  ? 101 LEU H CB  1 
ATOM   14731 C CG  . LEU H  2 101 ? -25.839 -4.860   -9.614  1.00 43.23  ? 101 LEU H CG  1 
ATOM   14732 C CD1 . LEU H  2 101 ? -26.814 -5.092   -10.758 1.00 44.81  ? 101 LEU H CD1 1 
ATOM   14733 C CD2 . LEU H  2 101 ? -26.497 -4.055   -8.509  1.00 39.65  ? 101 LEU H CD2 1 
ATOM   14734 N N   . LEU H  2 102 ? -23.451 -8.333   -8.043  1.00 46.85  ? 102 LEU H N   1 
ATOM   14735 C CA  . LEU H  2 102 ? -23.151 -9.716   -7.684  1.00 46.40  ? 102 LEU H CA  1 
ATOM   14736 C C   . LEU H  2 102 ? -22.527 -9.826   -6.299  1.00 49.52  ? 102 LEU H C   1 
ATOM   14737 O O   . LEU H  2 102 ? -22.939 -10.658  -5.493  1.00 48.46  ? 102 LEU H O   1 
ATOM   14738 C CB  . LEU H  2 102 ? -22.227 -10.366  -8.713  1.00 49.95  ? 102 LEU H CB  1 
ATOM   14739 C CG  . LEU H  2 102 ? -22.747 -10.500  -10.146 1.00 62.10  ? 102 LEU H CG  1 
ATOM   14740 C CD1 . LEU H  2 102 ? -21.852 -11.430  -10.949 1.00 84.21  ? 102 LEU H CD1 1 
ATOM   14741 C CD2 . LEU H  2 102 ? -24.212 -10.924  -10.215 1.00 60.71  ? 102 LEU H CD2 1 
ATOM   14742 N N   . GLU H  2 103 ? -21.535 -8.984   -6.027  1.00 47.47  ? 103 GLU H N   1 
ATOM   14743 C CA  . GLU H  2 103 ? -20.829 -9.025   -4.749  1.00 51.78  ? 103 GLU H CA  1 
ATOM   14744 C C   . GLU H  2 103 ? -21.704 -8.618   -3.569  1.00 42.45  ? 103 GLU H C   1 
ATOM   14745 O O   . GLU H  2 103 ? -21.608 -9.206   -2.493  1.00 58.39  ? 103 GLU H O   1 
ATOM   14746 C CB  . GLU H  2 103 ? -19.563 -8.168   -4.794  1.00 45.03  ? 103 GLU H CB  1 
ATOM   14747 C CG  . GLU H  2 103 ? -18.442 -8.792   -5.603  1.00 69.73  ? 103 GLU H CG  1 
ATOM   14748 C CD  . GLU H  2 103 ? -18.226 -10.252  -5.256  1.00 78.03  ? 103 GLU H CD  1 
ATOM   14749 O OE1 . GLU H  2 103 ? -17.586 -10.534  -4.222  1.00 76.87  ? 103 GLU H OE1 1 
ATOM   14750 O OE2 . GLU H  2 103 ? -18.697 -11.121  -6.020  1.00 78.98  ? 103 GLU H OE2 1 
ATOM   14751 N N   . ASN H  2 104 ? -22.550 -7.612   -3.764  1.00 36.03  ? 104 ASN H N   1 
ATOM   14752 C CA  . ASN H  2 104 ? -23.477 -7.199   -2.717  1.00 47.07  ? 104 ASN H CA  1 
ATOM   14753 C C   . ASN H  2 104 ? -24.416 -8.335   -2.325  1.00 55.00  ? 104 ASN H C   1 
ATOM   14754 O O   . ASN H  2 104 ? -24.702 -8.539   -1.145  1.00 55.82  ? 104 ASN H O   1 
ATOM   14755 C CB  . ASN H  2 104 ? -24.274 -5.967   -3.148  1.00 38.69  ? 104 ASN H CB  1 
ATOM   14756 C CG  . ASN H  2 104 ? -23.462 -4.689   -3.059  1.00 48.80  ? 104 ASN H CG  1 
ATOM   14757 O OD1 . ASN H  2 104 ? -22.358 -4.678   -2.514  1.00 54.77  ? 104 ASN H OD1 1 
ATOM   14758 N ND2 . ASN H  2 104 ? -24.010 -3.602   -3.588  1.00 49.77  ? 104 ASN H ND2 1 
ATOM   14759 N N   . GLU H  2 105 ? -24.888 -9.076   -3.322  1.00 47.53  ? 105 GLU H N   1 
ATOM   14760 C CA  . GLU H  2 105 ? -25.734 -10.234  -3.069  1.00 51.15  ? 105 GLU H CA  1 
ATOM   14761 C C   . GLU H  2 105 ? -24.983 -11.260  -2.229  1.00 53.57  ? 105 GLU H C   1 
ATOM   14762 O O   . GLU H  2 105 ? -25.541 -11.845  -1.301  1.00 62.00  ? 105 GLU H O   1 
ATOM   14763 C CB  . GLU H  2 105 ? -26.198 -10.864  -4.384  1.00 57.55  ? 105 GLU H CB  1 
ATOM   14764 C CG  . GLU H  2 105 ? -27.096 -12.073  -4.195  1.00 63.11  ? 105 GLU H CG  1 
ATOM   14765 C CD  . GLU H  2 105 ? -28.287 -11.772  -3.307  1.00 104.38 ? 105 GLU H CD  1 
ATOM   14766 O OE1 . GLU H  2 105 ? -28.832 -10.652  -3.401  1.00 99.17  ? 105 GLU H OE1 1 
ATOM   14767 O OE2 . GLU H  2 105 ? -28.680 -12.656  -2.515  1.00 105.17 ? 105 GLU H OE2 1 
ATOM   14768 N N   . ARG H  2 106 ? -23.711 -11.466  -2.556  1.00 45.91  ? 106 ARG H N   1 
ATOM   14769 C CA  . ARG H  2 106 ? -22.877 -12.419  -1.832  1.00 53.25  ? 106 ARG H CA  1 
ATOM   14770 C C   . ARG H  2 106 ? -22.559 -11.946  -0.417  1.00 61.25  ? 106 ARG H C   1 
ATOM   14771 O O   . ARG H  2 106 ? -22.490 -12.750  0.512   1.00 66.95  ? 106 ARG H O   1 
ATOM   14772 C CB  . ARG H  2 106 ? -21.579 -12.694  -2.594  1.00 48.63  ? 106 ARG H CB  1 
ATOM   14773 C CG  . ARG H  2 106 ? -21.774 -13.429  -3.908  1.00 62.34  ? 106 ARG H CG  1 
ATOM   14774 C CD  . ARG H  2 106 ? -20.466 -14.016  -4.412  1.00 72.95  ? 106 ARG H CD  1 
ATOM   14775 N NE  . ARG H  2 106 ? -19.841 -14.881  -3.415  1.00 79.71  ? 106 ARG H NE  1 
ATOM   14776 C CZ  . ARG H  2 106 ? -20.241 -16.120  -3.146  1.00 84.24  ? 106 ARG H CZ  1 
ATOM   14777 N NH1 . ARG H  2 106 ? -21.271 -16.642  -3.795  1.00 80.74  ? 106 ARG H NH1 1 
ATOM   14778 N NH2 . ARG H  2 106 ? -19.614 -16.837  -2.223  1.00 85.38  ? 106 ARG H NH2 1 
ATOM   14779 N N   . THR H  2 107 ? -22.363 -10.641  -0.258  1.00 53.55  ? 107 THR H N   1 
ATOM   14780 C CA  . THR H  2 107 ? -22.025 -10.075  1.044   1.00 48.12  ? 107 THR H CA  1 
ATOM   14781 C C   . THR H  2 107 ? -23.176 -10.233  2.030   1.00 54.23  ? 107 THR H C   1 
ATOM   14782 O O   . THR H  2 107 ? -22.964 -10.577  3.192   1.00 58.57  ? 107 THR H O   1 
ATOM   14783 C CB  . THR H  2 107 ? -21.645 -8.587   0.938   1.00 55.21  ? 107 THR H CB  1 
ATOM   14784 O OG1 . THR H  2 107 ? -20.490 -8.446   0.102   1.00 63.74  ? 107 THR H OG1 1 
ATOM   14785 C CG2 . THR H  2 107 ? -21.341 -8.015   2.315   1.00 44.84  ? 107 THR H CG2 1 
ATOM   14786 N N   . LEU H  2 108 ? -24.394 -9.980   1.562   1.00 58.65  ? 108 LEU H N   1 
ATOM   14787 C CA  . LEU H  2 108 ? -25.576 -10.136  2.401   1.00 57.26  ? 108 LEU H CA  1 
ATOM   14788 C C   . LEU H  2 108 ? -25.798 -11.601  2.765   1.00 58.62  ? 108 LEU H C   1 
ATOM   14789 O O   . LEU H  2 108 ? -26.118 -11.922  3.908   1.00 56.88  ? 108 LEU H O   1 
ATOM   14790 C CB  . LEU H  2 108 ? -26.813 -9.561   1.708   1.00 49.77  ? 108 LEU H CB  1 
ATOM   14791 C CG  . LEU H  2 108 ? -26.778 -8.054   1.447   1.00 50.57  ? 108 LEU H CG  1 
ATOM   14792 C CD1 . LEU H  2 108 ? -28.116 -7.567   0.906   1.00 42.25  ? 108 LEU H CD1 1 
ATOM   14793 C CD2 . LEU H  2 108 ? -26.404 -7.303   2.717   1.00 54.98  ? 108 LEU H CD2 1 
ATOM   14794 N N   . ASP H  2 109 ? -25.625 -12.485  1.787   1.00 52.58  ? 109 ASP H N   1 
ATOM   14795 C CA  . ASP H  2 109 ? -25.745 -13.918  2.026   1.00 54.12  ? 109 ASP H CA  1 
ATOM   14796 C C   . ASP H  2 109 ? -24.663 -14.394  2.987   1.00 54.92  ? 109 ASP H C   1 
ATOM   14797 O O   . ASP H  2 109 ? -24.870 -15.334  3.754   1.00 54.70  ? 109 ASP H O   1 
ATOM   14798 C CB  . ASP H  2 109 ? -25.671 -14.695  0.710   1.00 63.11  ? 109 ASP H CB  1 
ATOM   14799 C CG  . ASP H  2 109 ? -26.937 -14.568  -0.113  1.00 81.66  ? 109 ASP H CG  1 
ATOM   14800 O OD1 . ASP H  2 109 ? -27.952 -14.080  0.428   1.00 82.78  ? 109 ASP H OD1 1 
ATOM   14801 O OD2 . ASP H  2 109 ? -26.920 -14.961  -1.299  1.00 81.88  ? 109 ASP H OD2 1 
ATOM   14802 N N   . TYR H  2 110 ? -23.508 -13.738  2.940   1.00 55.86  ? 110 TYR H N   1 
ATOM   14803 C CA  . TYR H  2 110 ? -22.412 -14.052  3.849   1.00 56.38  ? 110 TYR H CA  1 
ATOM   14804 C C   . TYR H  2 110 ? -22.788 -13.721  5.291   1.00 63.42  ? 110 TYR H C   1 
ATOM   14805 O O   . TYR H  2 110 ? -22.584 -14.529  6.194   1.00 57.04  ? 110 TYR H O   1 
ATOM   14806 C CB  . TYR H  2 110 ? -21.140 -13.304  3.441   1.00 48.77  ? 110 TYR H CB  1 
ATOM   14807 C CG  . TYR H  2 110 ? -20.015 -13.409  4.447   1.00 50.46  ? 110 TYR H CG  1 
ATOM   14808 C CD1 . TYR H  2 110 ? -19.126 -14.477  4.419   1.00 46.58  ? 110 TYR H CD1 1 
ATOM   14809 C CD2 . TYR H  2 110 ? -19.841 -12.438  5.424   1.00 53.34  ? 110 TYR H CD2 1 
ATOM   14810 C CE1 . TYR H  2 110 ? -18.097 -14.574  5.339   1.00 51.37  ? 110 TYR H CE1 1 
ATOM   14811 C CE2 . TYR H  2 110 ? -18.816 -12.527  6.347   1.00 54.53  ? 110 TYR H CE2 1 
ATOM   14812 C CZ  . TYR H  2 110 ? -17.947 -13.596  6.301   1.00 56.98  ? 110 TYR H CZ  1 
ATOM   14813 O OH  . TYR H  2 110 ? -16.927 -13.685  7.220   1.00 61.20  ? 110 TYR H OH  1 
ATOM   14814 N N   . HIS H  2 111 ? -23.339 -12.532  5.507   1.00 49.93  ? 111 HIS H N   1 
ATOM   14815 C CA  . HIS H  2 111 ? -23.770 -12.143  6.845   1.00 50.63  ? 111 HIS H CA  1 
ATOM   14816 C C   . HIS H  2 111 ? -24.920 -13.023  7.313   1.00 61.41  ? 111 HIS H C   1 
ATOM   14817 O O   . HIS H  2 111 ? -24.918 -13.514  8.442   1.00 58.19  ? 111 HIS H O   1 
ATOM   14818 C CB  . HIS H  2 111 ? -24.171 -10.667  6.888   1.00 49.02  ? 111 HIS H CB  1 
ATOM   14819 C CG  . HIS H  2 111 ? -23.015 -9.728   6.771   1.00 58.70  ? 111 HIS H CG  1 
ATOM   14820 N ND1 . HIS H  2 111 ? -22.057 -9.601   7.755   1.00 72.12  ? 111 HIS H ND1 1 
ATOM   14821 C CD2 . HIS H  2 111 ? -22.658 -8.867   5.787   1.00 63.15  ? 111 HIS H CD2 1 
ATOM   14822 C CE1 . HIS H  2 111 ? -21.160 -8.707   7.380   1.00 68.07  ? 111 HIS H CE1 1 
ATOM   14823 N NE2 . HIS H  2 111 ? -21.501 -8.246   6.194   1.00 67.11  ? 111 HIS H NE2 1 
ATOM   14824 N N   . ASP H  2 112 ? -25.896 -13.223  6.434   1.00 61.30  ? 112 ASP H N   1 
ATOM   14825 C CA  . ASP H  2 112 ? -27.039 -14.074  6.733   1.00 54.21  ? 112 ASP H CA  1 
ATOM   14826 C C   . ASP H  2 112 ? -26.570 -15.438  7.222   1.00 53.82  ? 112 ASP H C   1 
ATOM   14827 O O   . ASP H  2 112 ? -27.123 -15.998  8.169   1.00 64.28  ? 112 ASP H O   1 
ATOM   14828 C CB  . ASP H  2 112 ? -27.913 -14.239  5.488   1.00 64.79  ? 112 ASP H CB  1 
ATOM   14829 C CG  . ASP H  2 112 ? -29.229 -14.924  5.787   1.00 63.78  ? 112 ASP H CG  1 
ATOM   14830 O OD1 . ASP H  2 112 ? -29.872 -15.419  4.840   1.00 72.40  ? 112 ASP H OD1 1 
ATOM   14831 O OD2 . ASP H  2 112 ? -29.621 -14.965  6.971   1.00 72.86  ? 112 ASP H OD2 1 
ATOM   14832 N N   . SER H  2 113 ? -25.540 -15.964  6.569   1.00 57.47  ? 113 SER H N   1 
ATOM   14833 C CA  . SER H  2 113 ? -25.010 -17.280  6.900   1.00 52.08  ? 113 SER H CA  1 
ATOM   14834 C C   . SER H  2 113 ? -24.385 -17.328  8.294   1.00 62.82  ? 113 SER H C   1 
ATOM   14835 O O   . SER H  2 113 ? -24.626 -18.266  9.052   1.00 63.54  ? 113 SER H O   1 
ATOM   14836 C CB  . SER H  2 113 ? -24.000 -17.723  5.843   1.00 48.94  ? 113 SER H CB  1 
ATOM   14837 O OG  . SER H  2 113 ? -23.181 -18.769  6.329   1.00 65.45  ? 113 SER H OG  1 
ATOM   14838 N N   . ASN H  2 114 ? -23.584 -16.321  8.630   1.00 63.86  ? 114 ASN H N   1 
ATOM   14839 C CA  . ASN H  2 114 ? -22.947 -16.268  9.944   1.00 66.30  ? 114 ASN H CA  1 
ATOM   14840 C C   . ASN H  2 114 ? -23.957 -16.273  11.089  1.00 68.59  ? 114 ASN H C   1 
ATOM   14841 O O   . ASN H  2 114 ? -23.717 -16.876  12.135  1.00 62.32  ? 114 ASN H O   1 
ATOM   14842 C CB  . ASN H  2 114 ? -22.028 -15.051  10.055  1.00 60.19  ? 114 ASN H CB  1 
ATOM   14843 C CG  . ASN H  2 114 ? -20.846 -15.126  9.110   1.00 70.17  ? 114 ASN H CG  1 
ATOM   14844 O OD1 . ASN H  2 114 ? -20.479 -16.202  8.640   1.00 79.98  ? 114 ASN H OD1 1 
ATOM   14845 N ND2 . ASN H  2 114 ? -20.240 -13.979  8.830   1.00 74.43  ? 114 ASN H ND2 1 
ATOM   14846 N N   . VAL H  2 115 ? -25.082 -15.595  10.888  1.00 61.06  ? 115 VAL H N   1 
ATOM   14847 C CA  . VAL H  2 115 ? -26.159 -15.595  11.872  1.00 62.45  ? 115 VAL H CA  1 
ATOM   14848 C C   . VAL H  2 115 ? -26.727 -17.000  12.029  1.00 63.14  ? 115 VAL H C   1 
ATOM   14849 O O   . VAL H  2 115 ? -26.772 -17.543  13.133  1.00 67.76  ? 115 VAL H O   1 
ATOM   14850 C CB  . VAL H  2 115 ? -27.291 -14.630  11.473  1.00 57.04  ? 115 VAL H CB  1 
ATOM   14851 C CG1 . VAL H  2 115 ? -28.487 -14.803  12.397  1.00 69.18  ? 115 VAL H CG1 1 
ATOM   14852 C CG2 . VAL H  2 115 ? -26.795 -13.193  11.493  1.00 51.03  ? 115 VAL H CG2 1 
ATOM   14853 N N   . LYS H  2 116 ? -27.156 -17.582  10.913  1.00 60.10  ? 116 LYS H N   1 
ATOM   14854 C CA  . LYS H  2 116 ? -27.668 -18.948  10.889  1.00 65.25  ? 116 LYS H CA  1 
ATOM   14855 C C   . LYS H  2 116 ? -26.715 -19.904  11.599  1.00 67.95  ? 116 LYS H C   1 
ATOM   14856 O O   . LYS H  2 116 ? -27.142 -20.762  12.372  1.00 72.38  ? 116 LYS H O   1 
ATOM   14857 C CB  . LYS H  2 116 ? -27.881 -19.402  9.444   1.00 65.74  ? 116 LYS H CB  1 
ATOM   14858 C CG  . LYS H  2 116 ? -28.126 -20.895  9.275   1.00 58.05  ? 116 LYS H CG  1 
ATOM   14859 C CD  . LYS H  2 116 ? -29.608 -21.225  9.245   1.00 66.88  ? 116 LYS H CD  1 
ATOM   14860 C CE  . LYS H  2 116 ? -29.834 -22.660  8.793   1.00 88.84  ? 116 LYS H CE  1 
ATOM   14861 N NZ  . LYS H  2 116 ? -31.272 -22.957  8.544   1.00 106.97 ? 116 LYS H NZ  1 
ATOM   14862 N N   . ASN H  2 117 ? -25.423 -19.750  11.328  1.00 59.00  ? 117 ASN H N   1 
ATOM   14863 C CA  . ASN H  2 117 ? -24.404 -20.594  11.942  1.00 73.97  ? 117 ASN H CA  1 
ATOM   14864 C C   . ASN H  2 117 ? -24.306 -20.392  13.448  1.00 78.48  ? 117 ASN H C   1 
ATOM   14865 O O   . ASN H  2 117 ? -24.124 -21.349  14.201  1.00 71.66  ? 117 ASN H O   1 
ATOM   14866 C CB  . ASN H  2 117 ? -23.042 -20.350  11.291  1.00 62.33  ? 117 ASN H CB  1 
ATOM   14867 C CG  . ASN H  2 117 ? -22.914 -21.027  9.943   1.00 65.98  ? 117 ASN H CG  1 
ATOM   14868 O OD1 . ASN H  2 117 ? -23.714 -21.894  9.595   1.00 72.04  ? 117 ASN H OD1 1 
ATOM   14869 N ND2 . ASN H  2 117 ? -21.899 -20.639  9.179   1.00 76.40  ? 117 ASN H ND2 1 
ATOM   14870 N N   . LEU H  2 118 ? -24.422 -19.142  13.881  1.00 76.55  ? 118 LEU H N   1 
ATOM   14871 C CA  . LEU H  2 118 ? -24.380 -18.823  15.301  1.00 71.07  ? 118 LEU H CA  1 
ATOM   14872 C C   . LEU H  2 118 ? -25.579 -19.452  16.000  1.00 73.53  ? 118 LEU H C   1 
ATOM   14873 O O   . LEU H  2 118 ? -25.454 -20.022  17.084  1.00 85.91  ? 118 LEU H O   1 
ATOM   14874 C CB  . LEU H  2 118 ? -24.377 -17.308  15.506  1.00 73.19  ? 118 LEU H CB  1 
ATOM   14875 C CG  . LEU H  2 118 ? -23.592 -16.810  16.717  1.00 76.36  ? 118 LEU H CG  1 
ATOM   14876 C CD1 . LEU H  2 118 ? -22.192 -17.401  16.704  1.00 74.83  ? 118 LEU H CD1 1 
ATOM   14877 C CD2 . LEU H  2 118 ? -23.540 -15.290  16.740  1.00 85.70  ? 118 LEU H CD2 1 
ATOM   14878 N N   . TYR H  2 119 ? -26.740 -19.349  15.364  1.00 68.84  ? 119 TYR H N   1 
ATOM   14879 C CA  . TYR H  2 119 ? -27.961 -19.952  15.879  1.00 71.62  ? 119 TYR H CA  1 
ATOM   14880 C C   . TYR H  2 119 ? -27.811 -21.466  15.992  1.00 76.10  ? 119 TYR H C   1 
ATOM   14881 O O   . TYR H  2 119 ? -28.110 -22.053  17.031  1.00 87.80  ? 119 TYR H O   1 
ATOM   14882 C CB  . TYR H  2 119 ? -29.144 -19.611  14.971  1.00 65.01  ? 119 TYR H CB  1 
ATOM   14883 C CG  . TYR H  2 119 ? -30.443 -20.268  15.377  1.00 83.00  ? 119 TYR H CG  1 
ATOM   14884 C CD1 . TYR H  2 119 ? -31.312 -19.645  16.262  1.00 90.93  ? 119 TYR H CD1 1 
ATOM   14885 C CD2 . TYR H  2 119 ? -30.801 -21.511  14.872  1.00 82.76  ? 119 TYR H CD2 1 
ATOM   14886 C CE1 . TYR H  2 119 ? -32.500 -20.242  16.635  1.00 96.27  ? 119 TYR H CE1 1 
ATOM   14887 C CE2 . TYR H  2 119 ? -31.987 -22.116  15.240  1.00 97.64  ? 119 TYR H CE2 1 
ATOM   14888 C CZ  . TYR H  2 119 ? -32.833 -21.478  16.121  1.00 101.19 ? 119 TYR H CZ  1 
ATOM   14889 O OH  . TYR H  2 119 ? -34.016 -22.077  16.489  1.00 105.58 ? 119 TYR H OH  1 
ATOM   14890 N N   . GLU H  2 120 ? -27.346 -22.089  14.914  1.00 81.61  ? 120 GLU H N   1 
ATOM   14891 C CA  . GLU H  2 120 ? -27.166 -23.536  14.877  1.00 81.32  ? 120 GLU H CA  1 
ATOM   14892 C C   . GLU H  2 120 ? -26.167 -24.028  15.920  1.00 79.42  ? 120 GLU H C   1 
ATOM   14893 O O   . GLU H  2 120 ? -26.397 -25.044  16.576  1.00 88.80  ? 120 GLU H O   1 
ATOM   14894 C CB  . GLU H  2 120 ? -26.730 -23.988  13.481  1.00 99.56  ? 120 GLU H CB  1 
ATOM   14895 C CG  . GLU H  2 120 ? -27.881 -24.223  12.517  1.00 105.07 ? 120 GLU H CG  1 
ATOM   14896 C CD  . GLU H  2 120 ? -28.717 -25.430  12.899  1.00 131.28 ? 120 GLU H CD  1 
ATOM   14897 O OE1 . GLU H  2 120 ? -28.192 -26.321  13.600  1.00 122.98 ? 120 GLU H OE1 1 
ATOM   14898 O OE2 . GLU H  2 120 ? -29.897 -25.490  12.494  1.00 139.33 ? 120 GLU H OE2 1 
ATOM   14899 N N   . LYS H  2 121 ? -25.060 -23.308  16.069  1.00 84.50  ? 121 LYS H N   1 
ATOM   14900 C CA  . LYS H  2 121 ? -24.020 -23.700  17.015  1.00 92.62  ? 121 LYS H CA  1 
ATOM   14901 C C   . LYS H  2 121 ? -24.554 -23.743  18.443  1.00 96.25  ? 121 LYS H C   1 
ATOM   14902 O O   . LYS H  2 121 ? -24.138 -24.577  19.247  1.00 104.31 ? 121 LYS H O   1 
ATOM   14903 C CB  . LYS H  2 121 ? -22.819 -22.756  16.926  1.00 87.41  ? 121 LYS H CB  1 
ATOM   14904 C CG  . LYS H  2 121 ? -21.642 -23.184  17.785  1.00 104.94 ? 121 LYS H CG  1 
ATOM   14905 C CD  . LYS H  2 121 ? -20.468 -22.231  17.646  1.00 117.06 ? 121 LYS H CD  1 
ATOM   14906 C CE  . LYS H  2 121 ? -19.291 -22.695  18.488  1.00 121.24 ? 121 LYS H CE  1 
ATOM   14907 N NZ  . LYS H  2 121 ? -18.136 -21.763  18.397  1.00 134.43 ? 121 LYS H NZ  1 
ATOM   14908 N N   . VAL H  2 122 ? -25.476 -22.837  18.753  1.00 91.35  ? 122 VAL H N   1 
ATOM   14909 C CA  . VAL H  2 122 ? -26.121 -22.813  20.060  1.00 94.96  ? 122 VAL H CA  1 
ATOM   14910 C C   . VAL H  2 122 ? -27.130 -23.946  20.171  1.00 100.57 ? 122 VAL H C   1 
ATOM   14911 O O   . VAL H  2 122 ? -27.199 -24.638  21.187  1.00 121.80 ? 122 VAL H O   1 
ATOM   14912 C CB  . VAL H  2 122 ? -26.850 -21.477  20.304  1.00 83.83  ? 122 VAL H CB  1 
ATOM   14913 C CG1 . VAL H  2 122 ? -27.858 -21.616  21.435  1.00 90.19  ? 122 VAL H CG1 1 
ATOM   14914 C CG2 . VAL H  2 122 ? -25.850 -20.369  20.597  1.00 96.63  ? 122 VAL H CG2 1 
ATOM   14915 N N   . ARG H  2 123 ? -27.905 -24.134  19.109  1.00 90.32  ? 123 ARG H N   1 
ATOM   14916 C CA  . ARG H  2 123 ? -28.985 -25.112  19.106  1.00 94.99  ? 123 ARG H CA  1 
ATOM   14917 C C   . ARG H  2 123 ? -28.491 -26.558  19.172  1.00 97.97  ? 123 ARG H C   1 
ATOM   14918 O O   . ARG H  2 123 ? -29.075 -27.381  19.868  1.00 107.08 ? 123 ARG H O   1 
ATOM   14919 C CB  . ARG H  2 123 ? -29.873 -24.919  17.878  1.00 93.80  ? 123 ARG H CB  1 
ATOM   14920 C CG  . ARG H  2 123 ? -31.180 -25.678  17.955  1.00 101.23 ? 123 ARG H CG  1 
ATOM   14921 C CD  . ARG H  2 123 ? -31.600 -26.173  16.590  1.00 112.20 ? 123 ARG H CD  1 
ATOM   14922 N NE  . ARG H  2 123 ? -30.638 -27.123  16.043  1.00 132.66 ? 123 ARG H NE  1 
ATOM   14923 C CZ  . ARG H  2 123 ? -30.930 -28.022  15.111  1.00 142.69 ? 123 ARG H CZ  1 
ATOM   14924 N NH1 . ARG H  2 123 ? -32.159 -28.101  14.629  1.00 131.65 ? 123 ARG H NH1 1 
ATOM   14925 N NH2 . ARG H  2 123 ? -29.995 -28.846  14.668  1.00 144.88 ? 123 ARG H NH2 1 
ATOM   14926 N N   . SER H  2 124 ? -27.427 -26.875  18.442  1.00 106.34 ? 124 SER H N   1 
ATOM   14927 C CA  . SER H  2 124 ? -26.872 -28.227  18.476  1.00 116.42 ? 124 SER H CA  1 
ATOM   14928 C C   . SER H  2 124 ? -26.005 -28.413  19.710  1.00 123.93 ? 124 SER H C   1 
ATOM   14929 O O   . SER H  2 124 ? -25.179 -29.326  19.779  1.00 132.94 ? 124 SER H O   1 
ATOM   14930 C CB  . SER H  2 124 ? -26.047 -28.509  17.224  1.00 124.95 ? 124 SER H CB  1 
ATOM   14931 O OG  . SER H  2 124 ? -24.968 -27.600  17.110  1.00 128.69 ? 124 SER H OG  1 
ATOM   14932 N N   . GLN H  2 125 ? -26.195 -27.537  20.686  1.00 113.12 ? 125 GLN H N   1 
ATOM   14933 C CA  . GLN H  2 125 ? -25.390 -27.568  21.892  1.00 109.45 ? 125 GLN H CA  1 
ATOM   14934 C C   . GLN H  2 125 ? -26.314 -27.634  23.108  1.00 121.58 ? 125 GLN H C   1 
ATOM   14935 O O   . GLN H  2 125 ? -26.115 -28.453  24.012  1.00 122.25 ? 125 GLN H O   1 
ATOM   14936 C CB  . GLN H  2 125 ? -24.476 -26.352  21.939  1.00 101.18 ? 125 GLN H CB  1 
ATOM   14937 C CG  . GLN H  2 125 ? -23.465 -26.386  23.052  1.00 112.16 ? 125 GLN H CG  1 
ATOM   14938 C CD  . GLN H  2 125 ? -22.578 -25.166  23.046  1.00 128.95 ? 125 GLN H CD  1 
ATOM   14939 O OE1 . GLN H  2 125 ? -22.999 -24.082  22.643  1.00 122.27 ? 125 GLN H OE1 1 
ATOM   14940 N NE2 . GLN H  2 125 ? -21.341 -25.333  23.492  1.00 132.84 ? 125 GLN H NE2 1 
ATOM   14941 N N   . LEU H  2 126 ? -27.336 -26.783  23.127  1.00 122.08 ? 126 LEU H N   1 
ATOM   14942 C CA  . LEU H  2 126 ? -28.499 -27.062  23.953  1.00 108.67 ? 126 LEU H CA  1 
ATOM   14943 C C   . LEU H  2 126 ? -29.386 -27.915  23.086  1.00 117.26 ? 126 LEU H C   1 
ATOM   14944 O O   . LEU H  2 126 ? -29.743 -27.512  21.984  1.00 134.04 ? 126 LEU H O   1 
ATOM   14945 C CB  . LEU H  2 126 ? -29.264 -25.786  24.306  1.00 102.68 ? 126 LEU H CB  1 
ATOM   14946 C CG  . LEU H  2 126 ? -28.570 -24.411  24.308  1.00 104.91 ? 126 LEU H CG  1 
ATOM   14947 C CD1 . LEU H  2 126 ? -29.619 -23.318  24.285  1.00 108.17 ? 126 LEU H CD1 1 
ATOM   14948 C CD2 . LEU H  2 126 ? -27.587 -24.202  25.461  1.00 110.42 ? 126 LEU H CD2 1 
ATOM   14949 N N   . LYS H  2 127 ? -29.745 -29.089  23.577  1.00 118.14 ? 127 LYS H N   1 
ATOM   14950 C CA  . LYS H  2 127 ? -30.643 -29.953  22.832  1.00 119.29 ? 127 LYS H CA  1 
ATOM   14951 C C   . LYS H  2 127 ? -31.979 -30.098  23.564  1.00 139.18 ? 127 LYS H C   1 
ATOM   14952 O O   . LYS H  2 127 ? -32.945 -29.393  23.266  1.00 120.58 ? 127 LYS H O   1 
ATOM   14953 C CB  . LYS H  2 127 ? -29.993 -31.308  22.585  1.00 115.12 ? 127 LYS H CB  1 
ATOM   14954 C CG  . LYS H  2 127 ? -28.605 -31.153  21.954  1.00 124.43 ? 127 LYS H CG  1 
ATOM   14955 C CD  . LYS H  2 127 ? -27.561 -32.042  22.625  1.00 122.21 ? 127 LYS H CD  1 
ATOM   14956 C CE  . LYS H  2 127 ? -26.176 -31.809  22.018  1.00 127.82 ? 127 LYS H CE  1 
ATOM   14957 N NZ  . LYS H  2 127 ? -25.105 -32.648  22.638  1.00 119.96 ? 127 LYS H NZ  1 
ATOM   14958 N N   . ASN H  2 128 ? -32.025 -30.992  24.545  1.00 170.77 ? 128 ASN H N   1 
ATOM   14959 C CA  . ASN H  2 128 ? -33.200 -31.133  25.392  1.00 166.86 ? 128 ASN H CA  1 
ATOM   14960 C C   . ASN H  2 128 ? -33.261 -30.060  26.471  1.00 166.60 ? 128 ASN H C   1 
ATOM   14961 O O   . ASN H  2 128 ? -34.344 -29.688  26.909  1.00 156.96 ? 128 ASN H O   1 
ATOM   14962 C CB  . ASN H  2 128 ? -33.234 -32.525  26.014  1.00 162.76 ? 128 ASN H CB  1 
ATOM   14963 C CG  . ASN H  2 128 ? -33.474 -33.611  24.982  1.00 170.31 ? 128 ASN H CG  1 
ATOM   14964 O OD1 . ASN H  2 128 ? -34.348 -33.483  24.121  1.00 163.42 ? 128 ASN H OD1 1 
ATOM   14965 N ND2 . ASN H  2 128 ? -32.707 -34.690  25.068  1.00 183.49 ? 128 ASN H ND2 1 
ATOM   14966 N N   . ASN H  2 129 ? -32.104 -29.551  26.884  1.00 166.92 ? 129 ASN H N   1 
ATOM   14967 C CA  . ASN H  2 129 ? -32.034 -28.615  28.005  1.00 174.26 ? 129 ASN H CA  1 
ATOM   14968 C C   . ASN H  2 129 ? -32.727 -27.278  27.749  1.00 172.04 ? 129 ASN H C   1 
ATOM   14969 O O   . ASN H  2 129 ? -32.737 -26.404  28.614  1.00 176.45 ? 129 ASN H O   1 
ATOM   14970 C CB  . ASN H  2 129 ? -30.579 -28.386  28.419  1.00 168.61 ? 129 ASN H CB  1 
ATOM   14971 C CG  . ASN H  2 129 ? -29.929 -29.639  28.974  1.00 166.44 ? 129 ASN H CG  1 
ATOM   14972 O OD1 . ASN H  2 129 ? -28.770 -29.618  29.386  1.00 169.19 ? 129 ASN H OD1 1 
ATOM   14973 N ND2 . ASN H  2 129 ? -30.675 -30.740  28.988  1.00 165.14 ? 129 ASN H ND2 1 
ATOM   14974 N N   . ALA H  2 130 ? -33.306 -27.126  26.563  1.00 156.22 ? 130 ALA H N   1 
ATOM   14975 C CA  . ALA H  2 130 ? -34.021 -25.905  26.207  1.00 147.04 ? 130 ALA H CA  1 
ATOM   14976 C C   . ALA H  2 130 ? -34.861 -26.128  24.957  1.00 134.80 ? 130 ALA H C   1 
ATOM   14977 O O   . ALA H  2 130 ? -34.712 -27.143  24.276  1.00 135.98 ? 130 ALA H O   1 
ATOM   14978 C CB  . ALA H  2 130 ? -33.045 -24.759  25.996  1.00 148.19 ? 130 ALA H CB  1 
ATOM   14979 N N   . LYS H  2 131 ? -35.743 -25.181  24.654  1.00 135.29 ? 131 LYS H N   1 
ATOM   14980 C CA  . LYS H  2 131 ? -36.612 -25.302  23.490  1.00 144.01 ? 131 LYS H CA  1 
ATOM   14981 C C   . LYS H  2 131 ? -36.535 -24.076  22.588  1.00 153.03 ? 131 LYS H C   1 
ATOM   14982 O O   . LYS H  2 131 ? -36.311 -22.960  23.056  1.00 152.93 ? 131 LYS H O   1 
ATOM   14983 C CB  . LYS H  2 131 ? -38.062 -25.531  23.921  1.00 144.71 ? 131 LYS H CB  1 
ATOM   14984 C CG  . LYS H  2 131 ? -38.730 -24.304  24.521  1.00 153.55 ? 131 LYS H CG  1 
ATOM   14985 C CD  . LYS H  2 131 ? -40.243 -24.455  24.539  1.00 149.22 ? 131 LYS H CD  1 
ATOM   14986 C CE  . LYS H  2 131 ? -40.922 -23.170  24.988  1.00 148.73 ? 131 LYS H CE  1 
ATOM   14987 N NZ  . LYS H  2 131 ? -42.405 -23.250  24.872  1.00 147.26 ? 131 LYS H NZ  1 
ATOM   14988 N N   . GLU H  2 132 ? -36.726 -24.292  21.291  1.00 158.91 ? 132 GLU H N   1 
ATOM   14989 C CA  . GLU H  2 132 ? -36.761 -23.200  20.329  1.00 154.32 ? 132 GLU H CA  1 
ATOM   14990 C C   . GLU H  2 132 ? -38.089 -22.461  20.419  1.00 152.10 ? 132 GLU H C   1 
ATOM   14991 O O   . GLU H  2 132 ? -39.141 -23.079  20.572  1.00 155.51 ? 132 GLU H O   1 
ATOM   14992 C CB  . GLU H  2 132 ? -36.581 -23.730  18.906  1.00 153.47 ? 132 GLU H CB  1 
ATOM   14993 C CG  . GLU H  2 132 ? -35.297 -24.497  18.667  1.00 155.30 ? 132 GLU H CG  1 
ATOM   14994 C CD  . GLU H  2 132 ? -35.227 -25.061  17.263  1.00 156.34 ? 132 GLU H CD  1 
ATOM   14995 O OE1 . GLU H  2 132 ? -34.353 -25.912  17.002  1.00 152.36 ? 132 GLU H OE1 1 
ATOM   14996 O OE2 . GLU H  2 132 ? -36.055 -24.658  16.420  1.00 153.62 ? 132 GLU H OE2 1 
ATOM   14997 N N   . ILE H  2 133 ? -38.038 -21.138  20.322  1.00 145.25 ? 133 ILE H N   1 
ATOM   14998 C CA  . ILE H  2 133 ? -39.250 -20.331  20.282  1.00 149.29 ? 133 ILE H CA  1 
ATOM   14999 C C   . ILE H  2 133 ? -39.687 -20.133  18.835  1.00 150.30 ? 133 ILE H C   1 
ATOM   15000 O O   . ILE H  2 133 ? -40.879 -20.092  18.533  1.00 149.89 ? 133 ILE H O   1 
ATOM   15001 C CB  . ILE H  2 133 ? -39.041 -18.955  20.942  1.00 149.52 ? 133 ILE H CB  1 
ATOM   15002 C CG1 . ILE H  2 133 ? -38.672 -19.116  22.418  1.00 150.36 ? 133 ILE H CG1 1 
ATOM   15003 C CG2 . ILE H  2 133 ? -40.294 -18.106  20.810  1.00 139.40 ? 133 ILE H CG2 1 
ATOM   15004 C CD1 . ILE H  2 133 ? -39.800 -19.646  23.275  1.00 154.00 ? 133 ILE H CD1 1 
ATOM   15005 N N   . GLY H  2 134 ? -38.708 -20.020  17.943  1.00 153.34 ? 134 GLY H N   1 
ATOM   15006 C CA  . GLY H  2 134 ? -38.979 -19.810  16.533  1.00 145.96 ? 134 GLY H CA  1 
ATOM   15007 C C   . GLY H  2 134 ? -38.517 -18.442  16.072  1.00 128.80 ? 134 GLY H C   1 
ATOM   15008 O O   . GLY H  2 134 ? -38.341 -18.202  14.878  1.00 111.89 ? 134 GLY H O   1 
ATOM   15009 N N   . ASN H  2 135 ? -38.318 -17.542  17.030  1.00 113.73 ? 135 ASN H N   1 
ATOM   15010 C CA  . ASN H  2 135 ? -37.866 -16.188  16.735  1.00 93.73  ? 135 ASN H CA  1 
ATOM   15011 C C   . ASN H  2 135 ? -36.356 -16.058  16.922  1.00 95.51  ? 135 ASN H C   1 
ATOM   15012 O O   . ASN H  2 135 ? -35.846 -14.984  17.246  1.00 82.12  ? 135 ASN H O   1 
ATOM   15013 C CB  . ASN H  2 135 ? -38.606 -15.182  17.621  1.00 101.62 ? 135 ASN H CB  1 
ATOM   15014 C CG  . ASN H  2 135 ? -38.454 -13.753  17.137  1.00 120.38 ? 135 ASN H CG  1 
ATOM   15015 O OD1 . ASN H  2 135 ? -37.912 -13.503  16.061  1.00 111.12 ? 135 ASN H OD1 1 
ATOM   15016 N ND2 . ASN H  2 135 ? -38.937 -12.804  17.932  1.00 134.15 ? 135 ASN H ND2 1 
ATOM   15017 N N   . GLY H  2 136 ? -35.649 -17.165  16.707  1.00 101.82 ? 136 GLY H N   1 
ATOM   15018 C CA  . GLY H  2 136 ? -34.214 -17.224  16.908  1.00 95.45  ? 136 GLY H CA  1 
ATOM   15019 C C   . GLY H  2 136 ? -33.867 -17.272  18.380  1.00 97.78  ? 136 GLY H C   1 
ATOM   15020 O O   . GLY H  2 136 ? -32.713 -17.103  18.773  1.00 103.49 ? 136 GLY H O   1 
ATOM   15021 N N   . CYS H  2 137 ? -34.878 -17.525  19.198  1.00 131.84 ? 137 CYS H N   1 
ATOM   15022 C CA  . CYS H  2 137 ? -34.729 -17.413  20.637  1.00 131.18 ? 137 CYS H CA  1 
ATOM   15023 C C   . CYS H  2 137 ? -35.021 -18.743  21.341  1.00 132.62 ? 137 CYS H C   1 
ATOM   15024 O O   . CYS H  2 137 ? -35.961 -19.449  20.979  1.00 135.37 ? 137 CYS H O   1 
ATOM   15025 C CB  . CYS H  2 137 ? -35.652 -16.302  21.159  1.00 122.12 ? 137 CYS H CB  1 
ATOM   15026 S SG  . CYS H  2 137 ? -35.098 -14.618  20.717  1.00 151.85 ? 137 CYS H SG  1 
ATOM   15027 N N   . PHE H  2 138 ? -34.208 -19.090  22.336  1.00 129.09 ? 138 PHE H N   1 
ATOM   15028 C CA  . PHE H  2 138 ? -34.370 -20.353  23.061  1.00 137.68 ? 138 PHE H CA  1 
ATOM   15029 C C   . PHE H  2 138 ? -34.919 -20.125  24.464  1.00 151.64 ? 138 PHE H C   1 
ATOM   15030 O O   . PHE H  2 138 ? -34.731 -19.059  25.041  1.00 154.61 ? 138 PHE H O   1 
ATOM   15031 C CB  . PHE H  2 138 ? -33.033 -21.090  23.167  1.00 134.25 ? 138 PHE H CB  1 
ATOM   15032 C CG  . PHE H  2 138 ? -32.443 -21.476  21.844  1.00 121.81 ? 138 PHE H CG  1 
ATOM   15033 C CD1 . PHE H  2 138 ? -31.672 -20.577  21.131  1.00 114.07 ? 138 PHE H CD1 1 
ATOM   15034 C CD2 . PHE H  2 138 ? -32.650 -22.742  21.318  1.00 123.44 ? 138 PHE H CD2 1 
ATOM   15035 C CE1 . PHE H  2 138 ? -31.124 -20.925  19.916  1.00 116.14 ? 138 PHE H CE1 1 
ATOM   15036 C CE2 . PHE H  2 138 ? -32.102 -23.097  20.099  1.00 115.51 ? 138 PHE H CE2 1 
ATOM   15037 C CZ  . PHE H  2 138 ? -31.338 -22.185  19.398  1.00 112.76 ? 138 PHE H CZ  1 
ATOM   15038 N N   . GLU H  2 139 ? -35.596 -21.127  25.015  1.00 161.20 ? 139 GLU H N   1 
ATOM   15039 C CA  . GLU H  2 139 ? -36.039 -21.050  26.403  1.00 153.38 ? 139 GLU H CA  1 
ATOM   15040 C C   . GLU H  2 139 ? -35.462 -22.184  27.243  1.00 144.25 ? 139 GLU H C   1 
ATOM   15041 O O   . GLU H  2 139 ? -35.677 -23.358  26.948  1.00 144.81 ? 139 GLU H O   1 
ATOM   15042 C CB  . GLU H  2 139 ? -37.566 -21.024  26.509  1.00 152.94 ? 139 GLU H CB  1 
ATOM   15043 C CG  . GLU H  2 139 ? -38.068 -20.912  27.945  1.00 172.25 ? 139 GLU H CG  1 
ATOM   15044 C CD  . GLU H  2 139 ? -39.550 -20.610  28.031  1.00 181.06 ? 139 GLU H CD  1 
ATOM   15045 O OE1 . GLU H  2 139 ? -40.185 -20.423  26.971  1.00 167.55 ? 139 GLU H OE1 1 
ATOM   15046 O OE2 . GLU H  2 139 ? -40.080 -20.555  29.161  1.00 185.48 ? 139 GLU H OE2 1 
ATOM   15047 N N   . PHE H  2 140 ? -34.731 -21.822  28.293  1.00 148.30 ? 140 PHE H N   1 
ATOM   15048 C CA  . PHE H  2 140 ? -34.075 -22.800  29.153  1.00 162.72 ? 140 PHE H CA  1 
ATOM   15049 C C   . PHE H  2 140 ? -35.052 -23.498  30.092  1.00 168.94 ? 140 PHE H C   1 
ATOM   15050 O O   . PHE H  2 140 ? -35.915 -22.859  30.695  1.00 163.77 ? 140 PHE H O   1 
ATOM   15051 C CB  . PHE H  2 140 ? -32.974 -22.133  29.984  1.00 164.92 ? 140 PHE H CB  1 
ATOM   15052 C CG  . PHE H  2 140 ? -31.798 -21.665  29.177  1.00 157.21 ? 140 PHE H CG  1 
ATOM   15053 C CD1 . PHE H  2 140 ? -31.690 -20.340  28.788  1.00 158.40 ? 140 PHE H CD1 1 
ATOM   15054 C CD2 . PHE H  2 140 ? -30.794 -22.547  28.816  1.00 153.11 ? 140 PHE H CD2 1 
ATOM   15055 C CE1 . PHE H  2 140 ? -30.605 -19.906  28.050  1.00 158.31 ? 140 PHE H CE1 1 
ATOM   15056 C CE2 . PHE H  2 140 ? -29.707 -22.120  28.077  1.00 151.02 ? 140 PHE H CE2 1 
ATOM   15057 C CZ  . PHE H  2 140 ? -29.612 -20.797  27.694  1.00 154.17 ? 140 PHE H CZ  1 
ATOM   15058 N N   . TYR H  2 141 ? -34.911 -24.814  30.210  1.00 167.81 ? 141 TYR H N   1 
ATOM   15059 C CA  . TYR H  2 141 ? -35.626 -25.568  31.230  1.00 158.81 ? 141 TYR H CA  1 
ATOM   15060 C C   . TYR H  2 141 ? -34.766 -25.620  32.484  1.00 152.31 ? 141 TYR H C   1 
ATOM   15061 O O   . TYR H  2 141 ? -35.251 -25.917  33.575  1.00 157.80 ? 141 TYR H O   1 
ATOM   15062 C CB  . TYR H  2 141 ? -35.923 -26.992  30.759  1.00 158.41 ? 141 TYR H CB  1 
ATOM   15063 C CG  . TYR H  2 141 ? -36.848 -27.083  29.568  1.00 153.02 ? 141 TYR H CG  1 
ATOM   15064 C CD1 . TYR H  2 141 ? -36.520 -27.868  28.471  1.00 150.90 ? 141 TYR H CD1 1 
ATOM   15065 C CD2 . TYR H  2 141 ? -38.050 -26.387  29.540  1.00 144.30 ? 141 TYR H CD2 1 
ATOM   15066 C CE1 . TYR H  2 141 ? -37.363 -27.961  27.380  1.00 146.31 ? 141 TYR H CE1 1 
ATOM   15067 C CE2 . TYR H  2 141 ? -38.899 -26.472  28.452  1.00 147.42 ? 141 TYR H CE2 1 
ATOM   15068 C CZ  . TYR H  2 141 ? -38.550 -27.260  27.375  1.00 145.19 ? 141 TYR H CZ  1 
ATOM   15069 O OH  . TYR H  2 141 ? -39.391 -27.348  26.289  1.00 128.04 ? 141 TYR H OH  1 
ATOM   15070 N N   . HIS H  2 142 ? -33.480 -25.331  32.314  1.00 146.63 ? 142 HIS H N   1 
ATOM   15071 C CA  . HIS H  2 142 ? -32.531 -25.377  33.418  1.00 147.05 ? 142 HIS H CA  1 
ATOM   15072 C C   . HIS H  2 142 ? -31.974 -23.985  33.715  1.00 147.43 ? 142 HIS H C   1 
ATOM   15073 O O   . HIS H  2 142 ? -31.353 -23.356  32.857  1.00 162.19 ? 142 HIS H O   1 
ATOM   15074 C CB  . HIS H  2 142 ? -31.418 -26.395  33.124  1.00 149.23 ? 142 HIS H CB  1 
ATOM   15075 C CG  . HIS H  2 142 ? -30.065 -25.788  32.914  1.00 155.28 ? 142 HIS H CG  1 
ATOM   15076 N ND1 . HIS H  2 142 ? -29.117 -25.724  33.912  1.00 154.42 ? 142 HIS H ND1 1 
ATOM   15077 C CD2 . HIS H  2 142 ? -29.493 -25.236  31.817  1.00 158.03 ? 142 HIS H CD2 1 
ATOM   15078 C CE1 . HIS H  2 142 ? -28.023 -25.150  33.442  1.00 156.08 ? 142 HIS H CE1 1 
ATOM   15079 N NE2 . HIS H  2 142 ? -28.226 -24.844  32.174  1.00 162.04 ? 142 HIS H NE2 1 
ATOM   15080 N N   . LYS H  2 143 ? -32.230 -23.506  34.930  1.00 142.97 ? 143 LYS H N   1 
ATOM   15081 C CA  . LYS H  2 143 ? -31.796 -22.178  35.357  1.00 147.33 ? 143 LYS H CA  1 
ATOM   15082 C C   . LYS H  2 143 ? -30.395 -21.857  34.859  1.00 151.46 ? 143 LYS H C   1 
ATOM   15083 O O   . LYS H  2 143 ? -29.420 -22.464  35.296  1.00 144.77 ? 143 LYS H O   1 
ATOM   15084 C CB  . LYS H  2 143 ? -31.841 -22.063  36.882  1.00 152.24 ? 143 LYS H CB  1 
ATOM   15085 C CG  . LYS H  2 143 ? -33.239 -21.990  37.480  1.00 151.40 ? 143 LYS H CG  1 
ATOM   15086 C CD  . LYS H  2 143 ? -33.807 -20.577  37.435  1.00 158.39 ? 143 LYS H CD  1 
ATOM   15087 C CE  . LYS H  2 143 ? -34.355 -20.229  36.062  1.00 155.56 ? 143 LYS H CE  1 
ATOM   15088 N NZ  . LYS H  2 143 ? -34.938 -18.860  36.033  1.00 148.09 ? 143 LYS H NZ  1 
ATOM   15089 N N   . CYS H  2 144 ? -30.299 -20.898  33.946  1.00 162.10 ? 144 CYS H N   1 
ATOM   15090 C CA  . CYS H  2 144 ? -29.016 -20.539  33.356  1.00 171.32 ? 144 CYS H CA  1 
ATOM   15091 C C   . CYS H  2 144 ? -28.602 -19.114  33.710  1.00 161.61 ? 144 CYS H C   1 
ATOM   15092 O O   . CYS H  2 144 ? -29.061 -18.151  33.096  1.00 162.77 ? 144 CYS H O   1 
ATOM   15093 C CB  . CYS H  2 144 ? -29.056 -20.719  31.838  1.00 167.68 ? 144 CYS H CB  1 
ATOM   15094 S SG  . CYS H  2 144 ? -27.473 -20.440  31.017  1.00 171.19 ? 144 CYS H SG  1 
ATOM   15095 N N   . ASP H  2 145 ? -27.731 -18.991  34.705  1.00 168.76 ? 145 ASP H N   1 
ATOM   15096 C CA  . ASP H  2 145 ? -27.215 -17.694  35.129  1.00 176.70 ? 145 ASP H CA  1 
ATOM   15097 C C   . ASP H  2 145 ? -26.117 -17.187  34.187  1.00 168.95 ? 145 ASP H C   1 
ATOM   15098 O O   . ASP H  2 145 ? -25.958 -17.705  33.083  1.00 166.71 ? 145 ASP H O   1 
ATOM   15099 C CB  . ASP H  2 145 ? -26.704 -17.765  36.569  1.00 191.91 ? 145 ASP H CB  1 
ATOM   15100 C CG  . ASP H  2 145 ? -25.873 -19.002  36.834  1.00 193.88 ? 145 ASP H CG  1 
ATOM   15101 O OD1 . ASP H  2 145 ? -24.971 -18.937  37.695  1.00 185.81 ? 145 ASP H OD1 1 
ATOM   15102 O OD2 . ASP H  2 145 ? -26.110 -20.039  36.176  1.00 192.12 ? 145 ASP H OD2 1 
ATOM   15103 N N   . ASN H  2 146 ? -25.370 -16.175  34.625  1.00 151.13 ? 146 ASN H N   1 
ATOM   15104 C CA  . ASN H  2 146 ? -24.360 -15.525  33.787  1.00 140.74 ? 146 ASN H CA  1 
ATOM   15105 C C   . ASN H  2 146 ? -23.216 -16.442  33.359  1.00 148.08 ? 146 ASN H C   1 
ATOM   15106 O O   . ASN H  2 146 ? -22.773 -16.392  32.205  1.00 168.23 ? 146 ASN H O   1 
ATOM   15107 C CB  . ASN H  2 146 ? -23.773 -14.303  34.497  1.00 131.71 ? 146 ASN H CB  1 
ATOM   15108 C CG  . ASN H  2 146 ? -24.759 -13.162  34.612  1.00 131.22 ? 146 ASN H CG  1 
ATOM   15109 O OD1 . ASN H  2 146 ? -24.499 -12.168  35.295  1.00 132.99 ? 146 ASN H OD1 1 
ATOM   15110 N ND2 . ASN H  2 146 ? -25.900 -13.295  33.943  1.00 120.39 ? 146 ASN H ND2 1 
ATOM   15111 N N   . THR H  2 147 ? -22.709 -17.252  34.288  1.00 172.68 ? 147 THR H N   1 
ATOM   15112 C CA  . THR H  2 147 ? -21.626 -18.177  33.949  1.00 181.68 ? 147 THR H CA  1 
ATOM   15113 C C   . THR H  2 147 ? -22.179 -19.481  33.394  1.00 178.84 ? 147 THR H C   1 
ATOM   15114 O O   . THR H  2 147 ? -21.461 -20.461  33.256  1.00 173.84 ? 147 THR H O   1 
ATOM   15115 C CB  . THR H  2 147 ? -20.667 -18.449  35.134  1.00 176.77 ? 147 THR H CB  1 
ATOM   15116 O OG1 . THR H  2 147 ? -21.298 -19.311  36.087  1.00 182.97 ? 147 THR H OG1 1 
ATOM   15117 N N   . CYS H  2 148 ? -23.468 -19.473  33.084  1.00 169.67 ? 148 CYS H N   1 
ATOM   15118 C CA  . CYS H  2 148 ? -24.105 -20.558  32.364  1.00 174.97 ? 148 CYS H CA  1 
ATOM   15119 C C   . CYS H  2 148 ? -24.183 -20.085  30.917  1.00 184.26 ? 148 CYS H C   1 
ATOM   15120 O O   . CYS H  2 148 ? -23.781 -20.772  29.973  1.00 179.19 ? 148 CYS H O   1 
ATOM   15121 C CB  . CYS H  2 148 ? -25.497 -20.748  32.957  1.00 170.25 ? 148 CYS H CB  1 
ATOM   15122 S SG  . CYS H  2 148 ? -26.619 -21.904  32.141  1.00 167.70 ? 148 CYS H SG  1 
ATOM   15123 N N   . MET H  2 149 ? -24.672 -18.860  30.786  1.00 181.19 ? 149 MET H N   1 
ATOM   15124 C CA  . MET H  2 149 ? -24.738 -18.139  29.531  1.00 166.19 ? 149 MET H CA  1 
ATOM   15125 C C   . MET H  2 149 ? -23.386 -18.104  28.820  1.00 166.48 ? 149 MET H C   1 
ATOM   15126 O O   . MET H  2 149 ? -23.328 -18.020  27.594  1.00 159.58 ? 149 MET H O   1 
ATOM   15127 C CB  . MET H  2 149 ? -25.221 -16.712  29.795  1.00 161.17 ? 149 MET H CB  1 
ATOM   15128 C CG  . MET H  2 149 ? -26.688 -16.613  30.196  1.00 155.60 ? 149 MET H CG  1 
ATOM   15129 S SD  . MET H  2 149 ? -27.824 -17.205  28.928  1.00 135.81 ? 149 MET H SD  1 
ATOM   15130 C CE  . MET H  2 149 ? -29.393 -16.669  29.608  1.00 134.73 ? 149 MET H CE  1 
ATOM   15131 N N   . GLU H  2 150 ? -22.300 -18.170  29.587  1.00 284.41 ? 150 GLU H N   1 
ATOM   15132 C CA  . GLU H  2 150 ? -20.956 -18.081  29.021  1.00 285.14 ? 150 GLU H CA  1 
ATOM   15133 C C   . GLU H  2 150 ? -20.553 -19.370  28.324  1.00 283.32 ? 150 GLU H C   1 
ATOM   15134 O O   . GLU H  2 150 ? -19.982 -19.348  27.233  1.00 281.54 ? 150 GLU H O   1 
ATOM   15135 C CB  . GLU H  2 150 ? -19.933 -17.768  30.111  1.00 289.32 ? 150 GLU H CB  1 
ATOM   15136 C CG  . GLU H  2 150 ? -18.983 -16.640  29.767  1.00 294.68 ? 150 GLU H CG  1 
ATOM   15137 C CD  . GLU H  2 150 ? -19.564 -15.284  30.089  1.00 297.73 ? 150 GLU H CD  1 
ATOM   15138 O OE1 . GLU H  2 150 ? -18.772 -14.352  30.313  1.00 297.53 ? 150 GLU H OE1 1 
ATOM   15139 O OE2 . GLU H  2 150 ? -20.806 -15.153  30.126  1.00 291.43 ? 150 GLU H OE2 1 
ATOM   15140 N N   . SER H  2 151 ? -20.835 -20.491  28.979  1.00 179.31 ? 151 SER H N   1 
ATOM   15141 C CA  . SER H  2 151 ? -20.487 -21.802  28.451  1.00 175.08 ? 151 SER H CA  1 
ATOM   15142 C C   . SER H  2 151 ? -21.041 -21.979  27.044  1.00 165.89 ? 151 SER H C   1 
ATOM   15143 O O   . SER H  2 151 ? -20.505 -22.748  26.248  1.00 168.91 ? 151 SER H O   1 
ATOM   15144 C CB  . SER H  2 151 ? -21.020 -22.901  29.372  1.00 167.51 ? 151 SER H CB  1 
ATOM   15145 O OG  . SER H  2 151 ? -22.436 -22.912  29.388  1.00 158.82 ? 151 SER H OG  1 
ATOM   15146 N N   . VAL H  2 152 ? -22.117 -21.259  26.744  1.00 150.04 ? 152 VAL H N   1 
ATOM   15147 C CA  . VAL H  2 152 ? -22.737 -21.319  25.428  1.00 138.83 ? 152 VAL H CA  1 
ATOM   15148 C C   . VAL H  2 152 ? -21.959 -20.474  24.422  1.00 139.56 ? 152 VAL H C   1 
ATOM   15149 O O   . VAL H  2 152 ? -21.671 -20.924  23.313  1.00 123.12 ? 152 VAL H O   1 
ATOM   15150 C CB  . VAL H  2 152 ? -24.196 -20.834  25.471  1.00 120.22 ? 152 VAL H CB  1 
ATOM   15151 C CG1 . VAL H  2 152 ? -24.904 -21.175  24.170  1.00 105.18 ? 152 VAL H CG1 1 
ATOM   15152 C CG2 . VAL H  2 152 ? -24.924 -21.453  26.652  1.00 129.27 ? 152 VAL H CG2 1 
ATOM   15153 N N   . LYS H  2 153 ? -21.621 -19.249  24.813  1.00 139.63 ? 153 LYS H N   1 
ATOM   15154 C CA  . LYS H  2 153 ? -20.875 -18.356  23.933  1.00 130.98 ? 153 LYS H CA  1 
ATOM   15155 C C   . LYS H  2 153 ? -19.485 -18.918  23.657  1.00 158.42 ? 153 LYS H C   1 
ATOM   15156 O O   . LYS H  2 153 ? -19.078 -19.058  22.503  1.00 157.87 ? 153 LYS H O   1 
ATOM   15157 C CB  . LYS H  2 153 ? -20.777 -16.948  24.528  1.00 123.59 ? 153 LYS H CB  1 
ATOM   15158 C CG  . LYS H  2 153 ? -22.119 -16.236  24.677  1.00 101.54 ? 153 LYS H CG  1 
ATOM   15159 C CD  . LYS H  2 153 ? -21.944 -14.720  24.722  1.00 108.84 ? 153 LYS H CD  1 
ATOM   15160 C CE  . LYS H  2 153 ? -23.212 -14.022  25.196  1.00 105.70 ? 153 LYS H CE  1 
ATOM   15161 N NZ  . LYS H  2 153 ? -23.783 -14.648  26.421  1.00 104.89 ? 153 LYS H NZ  1 
ATOM   15162 N N   . ASN H  2 154 ? -18.767 -19.247  24.725  1.00 261.93 ? 154 ASN H N   1 
ATOM   15163 C CA  . ASN H  2 154 ? -17.453 -19.867  24.617  1.00 263.30 ? 154 ASN H CA  1 
ATOM   15164 C C   . ASN H  2 154 ? -17.484 -21.172  23.834  1.00 261.01 ? 154 ASN H C   1 
ATOM   15165 O O   . ASN H  2 154 ? -16.444 -21.683  23.418  1.00 264.47 ? 154 ASN H O   1 
ATOM   15166 C CB  . ASN H  2 154 ? -16.879 -20.117  26.009  1.00 267.23 ? 154 ASN H CB  1 
ATOM   15167 C CG  . ASN H  2 154 ? -15.461 -20.624  25.964  1.00 273.75 ? 154 ASN H CG  1 
ATOM   15168 O OD1 . ASN H  2 154 ? -14.999 -21.140  24.947  1.00 276.77 ? 154 ASN H OD1 1 
ATOM   15169 N ND2 . ASN H  2 154 ? -14.761 -20.490  27.073  1.00 272.36 ? 154 ASN H ND2 1 
ATOM   15170 N N   . GLY H  2 155 ? -18.684 -21.707  23.641  1.00 182.74 ? 155 GLY H N   1 
ATOM   15171 C CA  . GLY H  2 155 ? -18.854 -22.962  22.935  1.00 172.38 ? 155 GLY H CA  1 
ATOM   15172 C C   . GLY H  2 155 ? -18.499 -24.150  23.806  1.00 181.96 ? 155 GLY H C   1 
ATOM   15173 O O   . GLY H  2 155 ? -18.551 -25.296  23.361  1.00 169.33 ? 155 GLY H O   1 
ATOM   15174 N N   . THR H  2 156 ? -18.131 -23.873  25.052  1.00 220.52 ? 156 THR H N   1 
ATOM   15175 C CA  . THR H  2 156 ? -17.789 -24.923  26.004  1.00 224.70 ? 156 THR H CA  1 
ATOM   15176 C C   . THR H  2 156 ? -18.951 -25.174  26.948  1.00 206.34 ? 156 THR H C   1 
ATOM   15177 O O   . THR H  2 156 ? -18.970 -24.683  28.077  1.00 206.24 ? 156 THR H O   1 
ATOM   15178 C CB  . THR H  2 156 ? -16.554 -24.554  26.832  1.00 232.86 ? 156 THR H CB  1 
ATOM   15179 O OG1 . THR H  2 156 ? -16.771 -23.291  27.472  1.00 227.24 ? 156 THR H OG1 1 
ATOM   15180 C CG2 . THR H  2 156 ? -15.331 -24.462  25.941  1.00 234.79 ? 156 THR H CG2 1 
ATOM   15181 N N   . TYR H  2 157 ? -19.917 -25.949  26.474  1.00 159.23 ? 157 TYR H N   1 
ATOM   15182 C CA  . TYR H  2 157 ? -21.130 -26.216  27.226  1.00 158.25 ? 157 TYR H CA  1 
ATOM   15183 C C   . TYR H  2 157 ? -21.312 -27.708  27.432  1.00 171.12 ? 157 TYR H C   1 
ATOM   15184 O O   . TYR H  2 157 ? -21.743 -28.408  26.514  1.00 155.43 ? 157 TYR H O   1 
ATOM   15185 C CB  . TYR H  2 157 ? -22.330 -25.662  26.454  1.00 145.35 ? 157 TYR H CB  1 
ATOM   15186 C CG  . TYR H  2 157 ? -23.671 -25.842  27.129  1.00 130.24 ? 157 TYR H CG  1 
ATOM   15187 C CD1 . TYR H  2 157 ? -24.321 -24.763  27.705  1.00 135.22 ? 157 TYR H CD1 1 
ATOM   15188 C CD2 . TYR H  2 157 ? -24.294 -27.084  27.181  1.00 119.23 ? 157 TYR H CD2 1 
ATOM   15189 C CE1 . TYR H  2 157 ? -25.546 -24.912  28.309  1.00 132.39 ? 157 TYR H CE1 1 
ATOM   15190 C CE2 . TYR H  2 157 ? -25.523 -27.243  27.797  1.00 129.35 ? 157 TYR H CE2 1 
ATOM   15191 C CZ  . TYR H  2 157 ? -26.142 -26.149  28.363  1.00 128.87 ? 157 TYR H CZ  1 
ATOM   15192 O OH  . TYR H  2 157 ? -27.366 -26.280  28.981  1.00 120.63 ? 157 TYR H OH  1 
ATOM   15193 N N   . ASP H  2 158 ? -20.978 -28.212  28.617  1.00 271.44 ? 158 ASP H N   1 
ATOM   15194 C CA  . ASP H  2 158 ? -21.385 -29.578  28.928  1.00 280.38 ? 158 ASP H CA  1 
ATOM   15195 C C   . ASP H  2 158 ? -22.889 -29.579  29.192  1.00 259.77 ? 158 ASP H C   1 
ATOM   15196 O O   . ASP H  2 158 ? -23.428 -28.634  29.777  1.00 262.60 ? 158 ASP H O   1 
ATOM   15197 C CB  . ASP H  2 158 ? -20.582 -30.238  30.074  1.00 293.73 ? 158 ASP H CB  1 
ATOM   15198 C CG  . ASP H  2 158 ? -20.433 -29.357  31.296  1.00 308.69 ? 158 ASP H CG  1 
ATOM   15199 O OD1 . ASP H  2 158 ? -21.285 -29.432  32.208  1.00 300.47 ? 158 ASP H OD1 1 
ATOM   15200 O OD2 . ASP H  2 158 ? -19.431 -28.615  31.365  1.00 330.34 ? 158 ASP H OD2 1 
ATOM   15201 N N   . TYR H  2 159 ? -23.555 -30.643  28.754  1.00 205.56 ? 159 TYR H N   1 
ATOM   15202 C CA  . TYR H  2 159 ? -25.009 -30.737  28.774  1.00 181.36 ? 159 TYR H CA  1 
ATOM   15203 C C   . TYR H  2 159 ? -25.466 -31.746  29.864  1.00 184.32 ? 159 TYR H C   1 
ATOM   15204 O O   . TYR H  2 159 ? -26.013 -32.798  29.557  1.00 167.80 ? 159 TYR H O   1 
ATOM   15205 C CB  . TYR H  2 159 ? -25.475 -31.088  27.338  1.00 172.83 ? 159 TYR H CB  1 
ATOM   15206 C CG  . TYR H  2 159 ? -26.832 -31.736  27.169  1.00 163.72 ? 159 TYR H CG  1 
ATOM   15207 C CD1 . TYR H  2 159 ? -27.959 -30.983  26.862  1.00 155.76 ? 159 TYR H CD1 1 
ATOM   15208 C CD2 . TYR H  2 159 ? -26.973 -33.114  27.253  1.00 156.73 ? 159 TYR H CD2 1 
ATOM   15209 C CE1 . TYR H  2 159 ? -29.194 -31.588  26.689  1.00 134.93 ? 159 TYR H CE1 1 
ATOM   15210 C CE2 . TYR H  2 159 ? -28.196 -33.718  27.089  1.00 142.53 ? 159 TYR H CE2 1 
ATOM   15211 C CZ  . TYR H  2 159 ? -29.300 -32.956  26.805  1.00 131.23 ? 159 TYR H CZ  1 
ATOM   15212 O OH  . TYR H  2 159 ? -30.513 -33.578  26.639  1.00 140.65 ? 159 TYR H OH  1 
ATOM   15213 N N   . PRO H  2 160 ? -25.232 -31.424  31.156  1.00 202.16 ? 160 PRO H N   1 
ATOM   15214 C CA  . PRO H  2 160 ? -25.545 -32.406  32.210  1.00 177.18 ? 160 PRO H CA  1 
ATOM   15215 C C   . PRO H  2 160 ? -26.790 -32.144  33.080  1.00 141.71 ? 160 PRO H C   1 
ATOM   15216 O O   . PRO H  2 160 ? -26.872 -32.783  34.145  1.00 150.73 ? 160 PRO H O   1 
ATOM   15217 C CB  . PRO H  2 160 ? -24.317 -32.336  33.136  1.00 172.05 ? 160 PRO H CB  1 
ATOM   15218 C CG  . PRO H  2 160 ? -23.387 -31.306  32.556  1.00 193.77 ? 160 PRO H CG  1 
ATOM   15219 C CD  . PRO H  2 160 ? -24.213 -30.465  31.608  1.00 206.73 ? 160 PRO H CD  1 
ATOM   15220 N N   . LYS H  2 161 ? -27.744 -31.306  32.677  1.00 121.67 ? 161 LYS H N   1 
ATOM   15221 C CA  . LYS H  2 161 ? -28.689 -30.811  33.683  1.00 125.14 ? 161 LYS H CA  1 
ATOM   15222 C C   . LYS H  2 161 ? -30.082 -30.417  33.153  1.00 126.91 ? 161 LYS H C   1 
ATOM   15223 O O   . LYS H  2 161 ? -30.249 -29.341  32.565  1.00 134.32 ? 161 LYS H O   1 
ATOM   15224 C CB  . LYS H  2 161 ? -28.061 -29.622  34.411  1.00 151.92 ? 161 LYS H CB  1 
ATOM   15225 C CG  . LYS H  2 161 ? -28.936 -28.945  35.454  1.00 162.73 ? 161 LYS H CG  1 
ATOM   15226 C CD  . LYS H  2 161 ? -28.139 -27.806  36.058  1.00 168.36 ? 161 LYS H CD  1 
ATOM   15227 C CE  . LYS H  2 161 ? -28.880 -27.002  37.084  1.00 142.02 ? 161 LYS H CE  1 
ATOM   15228 N NZ  . LYS H  2 161 ? -28.016 -25.899  37.616  1.00 117.55 ? 161 LYS H NZ  1 
ATOM   15229 N N   . TYR H  2 162 ? -31.077 -31.273  33.402  1.00 130.07 ? 162 TYR H N   1 
ATOM   15230 C CA  . TYR H  2 162 ? -32.483 -31.050  33.007  1.00 124.66 ? 162 TYR H CA  1 
ATOM   15231 C C   . TYR H  2 162 ? -32.734 -29.701  32.331  1.00 132.69 ? 162 TYR H C   1 
ATOM   15232 O O   . TYR H  2 162 ? -33.706 -29.527  31.590  1.00 131.54 ? 162 TYR H O   1 
ATOM   15233 C CB  . TYR H  2 162 ? -33.406 -31.192  34.227  1.00 123.67 ? 162 TYR H CB  1 
ATOM   15234 C CG  . TYR H  2 162 ? -34.868 -31.455  33.908  1.00 125.49 ? 162 TYR H CG  1 
ATOM   15235 C CD1 . TYR H  2 162 ? -35.419 -32.716  34.094  1.00 107.78 ? 162 TYR H CD1 1 
ATOM   15236 C CD2 . TYR H  2 162 ? -35.698 -30.444  33.439  1.00 114.73 ? 162 TYR H CD2 1 
ATOM   15237 C CE1 . TYR H  2 162 ? -36.744 -32.967  33.813  1.00 119.40 ? 162 TYR H CE1 1 
ATOM   15238 C CE2 . TYR H  2 162 ? -37.027 -30.687  33.153  1.00 108.21 ? 162 TYR H CE2 1 
ATOM   15239 C CZ  . TYR H  2 162 ? -37.544 -31.948  33.343  1.00 124.38 ? 162 TYR H CZ  1 
ATOM   15240 O OH  . TYR H  2 162 ? -38.867 -32.184  33.058  1.00 81.56  ? 162 TYR H OH  1 
ATOM   15241 N N   . ASP I  1 7   ? -52.701 -37.683  8.653   1.00 85.82  ? 7   ASP I N   1 
ATOM   15242 C CA  . ASP I  1 7   ? -51.452 -38.184  9.209   1.00 97.27  ? 7   ASP I CA  1 
ATOM   15243 C C   . ASP I  1 7   ? -50.300 -37.184  9.091   1.00 103.01 ? 7   ASP I C   1 
ATOM   15244 O O   . ASP I  1 7   ? -49.472 -37.085  9.996   1.00 113.73 ? 7   ASP I O   1 
ATOM   15245 C CB  . ASP I  1 7   ? -51.059 -39.510  8.548   1.00 99.27  ? 7   ASP I CB  1 
ATOM   15246 C CG  . ASP I  1 7   ? -51.612 -40.712  9.283   1.00 105.28 ? 7   ASP I CG  1 
ATOM   15247 O OD1 . ASP I  1 7   ? -50.815 -41.587  9.681   1.00 77.31  ? 7   ASP I OD1 1 
ATOM   15248 O OD2 . ASP I  1 7   ? -52.843 -40.777  9.476   1.00 107.93 ? 7   ASP I OD2 1 
ATOM   15249 N N   . THR I  1 8   ? -50.241 -36.434  7.995   1.00 96.89  ? 8   THR I N   1 
ATOM   15250 C CA  . THR I  1 8   ? -49.019 -35.692  7.693   1.00 113.43 ? 8   THR I CA  1 
ATOM   15251 C C   . THR I  1 8   ? -49.263 -34.354  6.990   1.00 90.82  ? 8   THR I C   1 
ATOM   15252 O O   . THR I  1 8   ? -50.386 -33.875  6.896   1.00 115.25 ? 8   THR I O   1 
ATOM   15253 C CB  . THR I  1 8   ? -48.056 -36.536  6.810   1.00 104.56 ? 8   THR I CB  1 
ATOM   15254 O OG1 . THR I  1 8   ? -48.808 -37.201  5.791   1.00 74.75  ? 8   THR I OG1 1 
ATOM   15255 C CG2 . THR I  1 8   ? -47.291 -37.591  7.630   1.00 120.00 ? 8   THR I CG2 1 
ATOM   15256 N N   . LEU I  1 9   ? -48.185 -33.773  6.481   1.00 59.36  ? 9   LEU I N   1 
ATOM   15257 C CA  . LEU I  1 9   ? -48.202 -32.494  5.779   1.00 77.53  ? 9   LEU I CA  1 
ATOM   15258 C C   . LEU I  1 9   ? -46.823 -32.439  5.144   1.00 87.11  ? 9   LEU I C   1 
ATOM   15259 O O   . LEU I  1 9   ? -45.868 -32.853  5.781   1.00 75.21  ? 9   LEU I O   1 
ATOM   15260 C CB  . LEU I  1 9   ? -48.319 -31.347  6.778   1.00 73.80  ? 9   LEU I CB  1 
ATOM   15261 C CG  . LEU I  1 9   ? -47.777 -30.026  6.220   1.00 72.91  ? 9   LEU I CG  1 
ATOM   15262 C CD1 . LEU I  1 9   ? -48.787 -29.397  5.286   1.00 68.82  ? 9   LEU I CD1 1 
ATOM   15263 C CD2 . LEU I  1 9   ? -47.396 -29.055  7.318   1.00 83.95  ? 9   LEU I CD2 1 
ATOM   15264 N N   . CYS I  1 10  ? -46.684 -31.945  3.919   1.00 108.61 ? 10  CYS I N   1 
ATOM   15265 C CA  . CYS I  1 10  ? -45.378 -32.036  3.274   1.00 96.76  ? 10  CYS I CA  1 
ATOM   15266 C C   . CYS I  1 10  ? -44.971 -30.805  2.455   1.00 91.68  ? 10  CYS I C   1 
ATOM   15267 O O   . CYS I  1 10  ? -45.815 -30.168  1.825   1.00 99.40  ? 10  CYS I O   1 
ATOM   15268 C CB  . CYS I  1 10  ? -45.274 -33.298  2.416   1.00 89.90  ? 10  CYS I CB  1 
ATOM   15269 S SG  . CYS I  1 10  ? -45.779 -34.824  3.216   1.00 115.54 ? 10  CYS I SG  1 
ATOM   15270 N N   . ILE I  1 11  ? -43.668 -30.508  2.436   1.00 93.23  ? 11  ILE I N   1 
ATOM   15271 C CA  . ILE I  1 11  ? -43.118 -29.348  1.734   1.00 103.67 ? 11  ILE I CA  1 
ATOM   15272 C C   . ILE I  1 11  ? -42.385 -29.817  0.479   1.00 92.05  ? 11  ILE I C   1 
ATOM   15273 O O   . ILE I  1 11  ? -41.547 -30.723  0.549   1.00 85.95  ? 11  ILE I O   1 
ATOM   15274 C CB  . ILE I  1 11  ? -42.103 -28.615  2.638   1.00 97.54  ? 11  ILE I CB  1 
ATOM   15275 C CG1 . ILE I  1 11  ? -42.443 -28.891  4.100   1.00 101.85 ? 11  ILE I CG1 1 
ATOM   15276 C CG2 . ILE I  1 11  ? -42.006 -27.127  2.292   1.00 89.01  ? 11  ILE I CG2 1 
ATOM   15277 C CD1 . ILE I  1 11  ? -42.428 -27.679  5.003   1.00 83.80  ? 11  ILE I CD1 1 
ATOM   15278 N N   . GLY I  1 12  ? -42.716 -29.226  -0.667  1.00 126.80 ? 12  GLY I N   1 
ATOM   15279 C CA  . GLY I  1 12  ? -42.107 -29.617  -1.928  1.00 118.83 ? 12  GLY I CA  1 
ATOM   15280 C C   . GLY I  1 12  ? -41.737 -28.437  -2.807  1.00 108.40 ? 12  GLY I C   1 
ATOM   15281 O O   . GLY I  1 12  ? -42.028 -27.277  -2.490  1.00 94.05  ? 12  GLY I O   1 
ATOM   15282 N N   . TYR I  1 13  ? -41.077 -28.732  -3.918  1.00 81.48  ? 13  TYR I N   1 
ATOM   15283 C CA  . TYR I  1 13  ? -40.838 -27.712  -4.916  1.00 79.26  ? 13  TYR I CA  1 
ATOM   15284 C C   . TYR I  1 13  ? -41.644 -28.009  -6.173  1.00 77.47  ? 13  TYR I C   1 
ATOM   15285 O O   . TYR I  1 13  ? -42.274 -29.061  -6.299  1.00 76.59  ? 13  TYR I O   1 
ATOM   15286 C CB  . TYR I  1 13  ? -39.344 -27.555  -5.208  1.00 52.09  ? 13  TYR I CB  1 
ATOM   15287 C CG  . TYR I  1 13  ? -38.560 -28.837  -5.136  1.00 57.98  ? 13  TYR I CG  1 
ATOM   15288 C CD1 . TYR I  1 13  ? -38.200 -29.508  -6.290  1.00 52.81  ? 13  TYR I CD1 1 
ATOM   15289 C CD2 . TYR I  1 13  ? -38.171 -29.371  -3.916  1.00 55.43  ? 13  TYR I CD2 1 
ATOM   15290 C CE1 . TYR I  1 13  ? -37.485 -30.670  -6.237  1.00 50.88  ? 13  TYR I CE1 1 
ATOM   15291 C CE2 . TYR I  1 13  ? -37.451 -30.538  -3.854  1.00 46.74  ? 13  TYR I CE2 1 
ATOM   15292 C CZ  . TYR I  1 13  ? -37.112 -31.183  -5.021  1.00 56.42  ? 13  TYR I CZ  1 
ATOM   15293 O OH  . TYR I  1 13  ? -36.394 -32.350  -4.987  1.00 59.99  ? 13  TYR I OH  1 
ATOM   15294 N N   . HIS I  1 14  ? -41.633 -27.056  -7.089  1.00 82.11  ? 14  HIS I N   1 
ATOM   15295 C CA  . HIS I  1 14  ? -42.418 -27.143  -8.302  1.00 64.08  ? 14  HIS I CA  1 
ATOM   15296 C C   . HIS I  1 14  ? -41.767 -28.064  -9.320  1.00 75.34  ? 14  HIS I C   1 
ATOM   15297 O O   . HIS I  1 14  ? -40.551 -28.256  -9.314  1.00 74.01  ? 14  HIS I O   1 
ATOM   15298 C CB  . HIS I  1 14  ? -42.564 -25.749  -8.903  1.00 79.78  ? 14  HIS I CB  1 
ATOM   15299 C CG  . HIS I  1 14  ? -43.358 -25.713  -10.166 1.00 90.48  ? 14  HIS I CG  1 
ATOM   15300 N ND1 . HIS I  1 14  ? -44.694 -25.377  -10.199 1.00 99.04  ? 14  HIS I ND1 1 
ATOM   15301 C CD2 . HIS I  1 14  ? -43.003 -25.963  -11.453 1.00 92.40  ? 14  HIS I CD2 1 
ATOM   15302 C CE1 . HIS I  1 14  ? -45.129 -25.426  -11.445 1.00 104.68 ? 14  HIS I CE1 1 
ATOM   15303 N NE2 . HIS I  1 14  ? -44.124 -25.778  -12.223 1.00 90.79  ? 14  HIS I NE2 1 
ATOM   15304 N N   . ALA I  1 15  ? -42.596 -28.636  -10.184 1.00 66.89  ? 15  ALA I N   1 
ATOM   15305 C CA  . ALA I  1 15  ? -42.125 -29.355  -11.356 1.00 70.88  ? 15  ALA I CA  1 
ATOM   15306 C C   . ALA I  1 15  ? -43.096 -29.035  -12.476 1.00 67.99  ? 15  ALA I C   1 
ATOM   15307 O O   . ALA I  1 15  ? -44.235 -28.648  -12.217 1.00 79.04  ? 15  ALA I O   1 
ATOM   15308 C CB  . ALA I  1 15  ? -42.086 -30.841  -11.096 1.00 65.23  ? 15  ALA I CB  1 
ATOM   15309 N N   . ASN I  1 16  ? -42.652 -29.183  -13.718 1.00 74.52  ? 16  ASN I N   1 
ATOM   15310 C CA  . ASN I  1 16  ? -43.525 -28.927  -14.855 1.00 92.44  ? 16  ASN I CA  1 
ATOM   15311 C C   . ASN I  1 16  ? -43.042 -29.642  -16.111 1.00 93.52  ? 16  ASN I C   1 
ATOM   15312 O O   . ASN I  1 16  ? -42.111 -30.444  -16.062 1.00 90.16  ? 16  ASN I O   1 
ATOM   15313 C CB  . ASN I  1 16  ? -43.669 -27.423  -15.102 1.00 98.88  ? 16  ASN I CB  1 
ATOM   15314 C CG  . ASN I  1 16  ? -42.335 -26.739  -15.328 1.00 92.29  ? 16  ASN I CG  1 
ATOM   15315 O OD1 . ASN I  1 16  ? -41.308 -27.395  -15.504 1.00 78.37  ? 16  ASN I OD1 1 
ATOM   15316 N ND2 . ASN I  1 16  ? -42.345 -25.413  -15.328 1.00 89.41  ? 16  ASN I ND2 1 
ATOM   15317 N N   . ASN I  1 17  ? -43.680 -29.351  -17.237 1.00 93.05  ? 17  ASN I N   1 
ATOM   15318 C CA  . ASN I  1 17  ? -43.324 -29.996  -18.492 1.00 93.36  ? 17  ASN I CA  1 
ATOM   15319 C C   . ASN I  1 17  ? -42.189 -29.272  -19.202 1.00 103.41 ? 17  ASN I C   1 
ATOM   15320 O O   . ASN I  1 17  ? -42.006 -29.425  -20.408 1.00 107.47 ? 17  ASN I O   1 
ATOM   15321 C CB  . ASN I  1 17  ? -44.543 -30.075  -19.409 1.00 115.14 ? 17  ASN I CB  1 
ATOM   15322 C CG  . ASN I  1 17  ? -45.127 -28.713  -19.714 1.00 127.45 ? 17  ASN I CG  1 
ATOM   15323 O OD1 . ASN I  1 17  ? -44.443 -27.693  -19.611 1.00 129.98 ? 17  ASN I OD1 1 
ATOM   15324 N ND2 . ASN I  1 17  ? -46.397 -28.687  -20.095 1.00 137.45 ? 17  ASN I ND2 1 
ATOM   15325 N N   . SER I  1 18  ? -41.425 -28.485  -18.451 1.00 103.44 ? 18  SER I N   1 
ATOM   15326 C CA  . SER I  1 18  ? -40.349 -27.693  -19.034 1.00 97.65  ? 18  SER I CA  1 
ATOM   15327 C C   . SER I  1 18  ? -39.187 -28.569  -19.490 1.00 83.25  ? 18  SER I C   1 
ATOM   15328 O O   . SER I  1 18  ? -38.766 -29.483  -18.781 1.00 73.55  ? 18  SER I O   1 
ATOM   15329 C CB  . SER I  1 18  ? -39.856 -26.636  -18.043 1.00 96.85  ? 18  SER I CB  1 
ATOM   15330 O OG  . SER I  1 18  ? -38.935 -25.752  -18.659 1.00 82.84  ? 18  SER I OG  1 
ATOM   15331 N N   . THR I  1 19  ? -38.681 -28.284  -20.685 1.00 95.05  ? 19  THR I N   1 
ATOM   15332 C CA  . THR I  1 19  ? -37.527 -28.992  -21.222 1.00 91.48  ? 19  THR I CA  1 
ATOM   15333 C C   . THR I  1 19  ? -36.326 -28.057  -21.291 1.00 87.98  ? 19  THR I C   1 
ATOM   15334 O O   . THR I  1 19  ? -35.241 -28.451  -21.721 1.00 80.12  ? 19  THR I O   1 
ATOM   15335 C CB  . THR I  1 19  ? -37.814 -29.561  -22.621 1.00 84.54  ? 19  THR I CB  1 
ATOM   15336 O OG1 . THR I  1 19  ? -38.281 -28.511  -23.478 1.00 105.25 ? 19  THR I OG1 1 
ATOM   15337 C CG2 . THR I  1 19  ? -38.873 -30.648  -22.544 1.00 93.64  ? 19  THR I CG2 1 
ATOM   15338 N N   . ASP I  1 20  ? -36.531 -26.815  -20.863 1.00 79.71  ? 20  ASP I N   1 
ATOM   15339 C CA  . ASP I  1 20  ? -35.461 -25.827  -20.825 1.00 70.21  ? 20  ASP I CA  1 
ATOM   15340 C C   . ASP I  1 20  ? -34.250 -26.372  -20.085 1.00 70.06  ? 20  ASP I C   1 
ATOM   15341 O O   . ASP I  1 20  ? -34.377 -26.929  -18.995 1.00 77.13  ? 20  ASP I O   1 
ATOM   15342 C CB  . ASP I  1 20  ? -35.938 -24.544  -20.143 1.00 78.37  ? 20  ASP I CB  1 
ATOM   15343 C CG  . ASP I  1 20  ? -36.959 -23.790  -20.967 1.00 86.18  ? 20  ASP I CG  1 
ATOM   15344 O OD1 . ASP I  1 20  ? -37.528 -22.807  -20.448 1.00 75.71  ? 20  ASP I OD1 1 
ATOM   15345 O OD2 . ASP I  1 20  ? -37.193 -24.177  -22.131 1.00 78.57  ? 20  ASP I OD2 1 
ATOM   15346 N N   . THR I  1 21  ? -33.077 -26.210  -20.683 1.00 69.45  ? 21  THR I N   1 
ATOM   15347 C CA  . THR I  1 21  ? -31.835 -26.619  -20.043 1.00 66.06  ? 21  THR I CA  1 
ATOM   15348 C C   . THR I  1 21  ? -30.833 -25.473  -20.009 1.00 57.49  ? 21  THR I C   1 
ATOM   15349 O O   . THR I  1 21  ? -30.662 -24.752  -20.992 1.00 67.41  ? 21  THR I O   1 
ATOM   15350 C CB  . THR I  1 21  ? -31.200 -27.827  -20.750 1.00 59.36  ? 21  THR I CB  1 
ATOM   15351 O OG1 . THR I  1 21  ? -31.144 -27.580  -22.160 1.00 80.08  ? 21  THR I OG1 1 
ATOM   15352 C CG2 . THR I  1 21  ? -32.019 -29.082  -20.495 1.00 64.97  ? 21  THR I CG2 1 
ATOM   15353 N N   . VAL I  1 22  ? -30.182 -25.305  -18.864 1.00 65.36  ? 22  VAL I N   1 
ATOM   15354 C CA  . VAL I  1 22  ? -29.155 -24.289  -18.708 1.00 52.89  ? 22  VAL I CA  1 
ATOM   15355 C C   . VAL I  1 22  ? -27.870 -24.946  -18.231 1.00 56.39  ? 22  VAL I C   1 
ATOM   15356 O O   . VAL I  1 22  ? -27.865 -26.116  -17.844 1.00 59.80  ? 22  VAL I O   1 
ATOM   15357 C CB  . VAL I  1 22  ? -29.567 -23.219  -17.683 1.00 44.69  ? 22  VAL I CB  1 
ATOM   15358 C CG1 . VAL I  1 22  ? -30.975 -22.724  -17.970 1.00 44.62  ? 22  VAL I CG1 1 
ATOM   15359 C CG2 . VAL I  1 22  ? -29.474 -23.777  -16.272 1.00 43.94  ? 22  VAL I CG2 1 
ATOM   15360 N N   . ASP I  1 23  ? -26.781 -24.190  -18.266 1.00 48.84  ? 23  ASP I N   1 
ATOM   15361 C CA  . ASP I  1 23  ? -25.512 -24.662  -17.739 1.00 51.04  ? 23  ASP I CA  1 
ATOM   15362 C C   . ASP I  1 23  ? -25.115 -23.858  -16.518 1.00 50.89  ? 23  ASP I C   1 
ATOM   15363 O O   . ASP I  1 23  ? -25.417 -22.670  -16.415 1.00 50.27  ? 23  ASP I O   1 
ATOM   15364 C CB  . ASP I  1 23  ? -24.411 -24.552  -18.788 1.00 60.97  ? 23  ASP I CB  1 
ATOM   15365 C CG  . ASP I  1 23  ? -24.557 -25.565  -19.890 1.00 72.75  ? 23  ASP I CG  1 
ATOM   15366 O OD1 . ASP I  1 23  ? -25.546 -26.329  -19.867 1.00 87.36  ? 23  ASP I OD1 1 
ATOM   15367 O OD2 . ASP I  1 23  ? -23.677 -25.595  -20.776 1.00 68.89  ? 23  ASP I OD2 1 
ATOM   15368 N N   . THR I  1 24  ? -24.435 -24.520  -15.593 1.00 43.77  ? 24  THR I N   1 
ATOM   15369 C CA  . THR I  1 24  ? -23.865 -23.854  -14.438 1.00 47.51  ? 24  THR I CA  1 
ATOM   15370 C C   . THR I  1 24  ? -22.356 -24.051  -14.488 1.00 49.82  ? 24  THR I C   1 
ATOM   15371 O O   . THR I  1 24  ? -21.835 -24.627  -15.442 1.00 40.16  ? 24  THR I O   1 
ATOM   15372 C CB  . THR I  1 24  ? -24.415 -24.437  -13.129 1.00 59.63  ? 24  THR I CB  1 
ATOM   15373 O OG1 . THR I  1 24  ? -23.920 -25.769  -12.952 1.00 65.75  ? 24  THR I OG1 1 
ATOM   15374 C CG2 . THR I  1 24  ? -25.939 -24.462  -13.155 1.00 46.99  ? 24  THR I CG2 1 
ATOM   15375 N N   . VAL I  1 25  ? -21.659 -23.571  -13.465 1.00 60.81  ? 25  VAL I N   1 
ATOM   15376 C CA  . VAL I  1 25  ? -20.218 -23.757  -13.369 1.00 53.37  ? 25  VAL I CA  1 
ATOM   15377 C C   . VAL I  1 25  ? -19.909 -25.204  -13.015 1.00 54.22  ? 25  VAL I C   1 
ATOM   15378 O O   . VAL I  1 25  ? -18.903 -25.763  -13.452 1.00 48.58  ? 25  VAL I O   1 
ATOM   15379 C CB  . VAL I  1 25  ? -19.617 -22.872  -12.272 1.00 50.43  ? 25  VAL I CB  1 
ATOM   15380 C CG1 . VAL I  1 25  ? -18.149 -22.594  -12.561 1.00 51.99  ? 25  VAL I CG1 1 
ATOM   15381 C CG2 . VAL I  1 25  ? -20.401 -21.580  -12.157 1.00 57.03  ? 25  VAL I CG2 1 
ATOM   15382 N N   . LEU I  1 26  ? -20.789 -25.804  -12.220 1.00 56.38  ? 26  LEU I N   1 
ATOM   15383 C CA  . LEU I  1 26  ? -20.566 -27.144  -11.690 1.00 50.56  ? 26  LEU I CA  1 
ATOM   15384 C C   . LEU I  1 26  ? -21.196 -28.249  -12.531 1.00 53.98  ? 26  LEU I C   1 
ATOM   15385 O O   . LEU I  1 26  ? -20.770 -29.401  -12.464 1.00 57.79  ? 26  LEU I O   1 
ATOM   15386 C CB  . LEU I  1 26  ? -21.112 -27.239  -10.266 1.00 43.70  ? 26  LEU I CB  1 
ATOM   15387 C CG  . LEU I  1 26  ? -20.262 -26.674  -9.127  1.00 51.89  ? 26  LEU I CG  1 
ATOM   15388 C CD1 . LEU I  1 26  ? -19.235 -25.663  -9.618  1.00 60.82  ? 26  LEU I CD1 1 
ATOM   15389 C CD2 . LEU I  1 26  ? -21.152 -26.091  -8.038  1.00 43.77  ? 26  LEU I CD2 1 
ATOM   15390 N N   . GLU I  1 27  ? -22.210 -27.904  -13.316 1.00 62.45  ? 27  GLU I N   1 
ATOM   15391 C CA  . GLU I  1 27  ? -22.992 -28.921  -14.012 1.00 58.86  ? 27  GLU I CA  1 
ATOM   15392 C C   . GLU I  1 27  ? -23.477 -28.464  -15.389 1.00 65.19  ? 27  GLU I C   1 
ATOM   15393 O O   . GLU I  1 27  ? -23.776 -27.288  -15.596 1.00 65.96  ? 27  GLU I O   1 
ATOM   15394 C CB  . GLU I  1 27  ? -24.179 -29.341  -13.139 1.00 70.88  ? 27  GLU I CB  1 
ATOM   15395 C CG  . GLU I  1 27  ? -24.762 -30.705  -13.462 1.00 84.68  ? 27  GLU I CG  1 
ATOM   15396 C CD  . GLU I  1 27  ? -25.703 -31.194  -12.378 1.00 98.25  ? 27  GLU I CD  1 
ATOM   15397 O OE1 . GLU I  1 27  ? -26.492 -32.125  -12.642 1.00 84.94  ? 27  GLU I OE1 1 
ATOM   15398 O OE2 . GLU I  1 27  ? -25.655 -30.641  -11.258 1.00 98.89  ? 27  GLU I OE2 1 
ATOM   15399 N N   . LYS I  1 28  ? -23.550 -29.406  -16.327 1.00 64.91  ? 28  LYS I N   1 
ATOM   15400 C CA  . LYS I  1 28  ? -24.007 -29.114  -17.685 1.00 61.64  ? 28  LYS I CA  1 
ATOM   15401 C C   . LYS I  1 28  ? -25.420 -29.632  -17.954 1.00 71.95  ? 28  LYS I C   1 
ATOM   15402 O O   . LYS I  1 28  ? -25.902 -30.532  -17.266 1.00 78.72  ? 28  LYS I O   1 
ATOM   15403 C CB  . LYS I  1 28  ? -23.042 -29.701  -18.719 1.00 62.60  ? 28  LYS I CB  1 
ATOM   15404 C CG  . LYS I  1 28  ? -21.881 -28.793  -19.086 1.00 62.28  ? 28  LYS I CG  1 
ATOM   15405 C CD  . LYS I  1 28  ? -21.007 -29.432  -20.155 1.00 76.71  ? 28  LYS I CD  1 
ATOM   15406 C CE  . LYS I  1 28  ? -20.136 -28.398  -20.851 1.00 89.54  ? 28  LYS I CE  1 
ATOM   15407 N NZ  . LYS I  1 28  ? -19.335 -27.598  -19.886 1.00 97.42  ? 28  LYS I NZ  1 
ATOM   15408 N N   . ASN I  1 29  ? -26.068 -29.059  -18.965 1.00 73.18  ? 29  ASN I N   1 
ATOM   15409 C CA  . ASN I  1 29  ? -27.419 -29.453  -19.359 1.00 59.64  ? 29  ASN I CA  1 
ATOM   15410 C C   . ASN I  1 29  ? -28.330 -29.804  -18.177 1.00 59.41  ? 29  ASN I C   1 
ATOM   15411 O O   . ASN I  1 29  ? -28.779 -30.942  -18.039 1.00 68.54  ? 29  ASN I O   1 
ATOM   15412 C CB  . ASN I  1 29  ? -27.373 -30.596  -20.385 1.00 66.26  ? 29  ASN I CB  1 
ATOM   15413 C CG  . ASN I  1 29  ? -27.007 -30.114  -21.789 1.00 99.61  ? 29  ASN I CG  1 
ATOM   15414 O OD1 . ASN I  1 29  ? -27.814 -29.473  -22.462 1.00 100.12 ? 29  ASN I OD1 1 
ATOM   15415 N ND2 . ASN I  1 29  ? -25.784 -30.424  -22.232 1.00 101.60 ? 29  ASN I ND2 1 
ATOM   15416 N N   . VAL I  1 30  ? -28.590 -28.814  -17.327 1.00 53.31  ? 30  VAL I N   1 
ATOM   15417 C CA  . VAL I  1 30  ? -29.495 -28.978  -16.194 1.00 46.20  ? 30  VAL I CA  1 
ATOM   15418 C C   . VAL I  1 30  ? -30.883 -28.456  -16.547 1.00 53.67  ? 30  VAL I C   1 
ATOM   15419 O O   . VAL I  1 30  ? -31.042 -27.290  -16.910 1.00 57.91  ? 30  VAL I O   1 
ATOM   15420 C CB  . VAL I  1 30  ? -28.989 -28.229  -14.943 1.00 47.88  ? 30  VAL I CB  1 
ATOM   15421 C CG1 . VAL I  1 30  ? -30.031 -28.281  -13.832 1.00 37.21  ? 30  VAL I CG1 1 
ATOM   15422 C CG2 . VAL I  1 30  ? -27.660 -28.806  -14.474 1.00 49.61  ? 30  VAL I CG2 1 
ATOM   15423 N N   . THR I  1 31  ? -31.887 -29.321  -16.441 1.00 47.48  ? 31  THR I N   1 
ATOM   15424 C CA  . THR I  1 31  ? -33.256 -28.938  -16.765 1.00 58.22  ? 31  THR I CA  1 
ATOM   15425 C C   . THR I  1 31  ? -33.861 -28.063  -15.675 1.00 53.66  ? 31  THR I C   1 
ATOM   15426 O O   . THR I  1 31  ? -33.899 -28.446  -14.507 1.00 63.49  ? 31  THR I O   1 
ATOM   15427 C CB  . THR I  1 31  ? -34.157 -30.167  -16.980 1.00 58.26  ? 31  THR I CB  1 
ATOM   15428 O OG1 . THR I  1 31  ? -33.624 -30.975  -18.035 1.00 50.10  ? 31  THR I OG1 1 
ATOM   15429 C CG2 . THR I  1 31  ? -35.567 -29.731  -17.346 1.00 62.83  ? 31  THR I CG2 1 
ATOM   15430 N N   . VAL I  1 32  ? -34.334 -26.886  -16.066 1.00 50.19  ? 32  VAL I N   1 
ATOM   15431 C CA  . VAL I  1 32  ? -34.936 -25.960  -15.120 1.00 58.18  ? 32  VAL I CA  1 
ATOM   15432 C C   . VAL I  1 32  ? -36.404 -25.722  -15.453 1.00 61.75  ? 32  VAL I C   1 
ATOM   15433 O O   . VAL I  1 32  ? -36.832 -25.911  -16.593 1.00 68.17  ? 32  VAL I O   1 
ATOM   15434 C CB  . VAL I  1 32  ? -34.185 -24.617  -15.095 1.00 52.21  ? 32  VAL I CB  1 
ATOM   15435 C CG1 . VAL I  1 32  ? -32.815 -24.788  -14.457 1.00 51.90  ? 32  VAL I CG1 1 
ATOM   15436 C CG2 . VAL I  1 32  ? -34.062 -24.056  -16.503 1.00 52.91  ? 32  VAL I CG2 1 
ATOM   15437 N N   . THR I  1 33  ? -37.170 -25.314  -14.448 1.00 60.81  ? 33  THR I N   1 
ATOM   15438 C CA  . THR I  1 33  ? -38.592 -25.052  -14.624 1.00 51.30  ? 33  THR I CA  1 
ATOM   15439 C C   . THR I  1 33  ? -38.816 -23.861  -15.549 1.00 65.97  ? 33  THR I C   1 
ATOM   15440 O O   . THR I  1 33  ? -39.784 -23.830  -16.313 1.00 76.51  ? 33  THR I O   1 
ATOM   15441 C CB  . THR I  1 33  ? -39.282 -24.779  -13.275 1.00 63.00  ? 33  THR I CB  1 
ATOM   15442 O OG1 . THR I  1 33  ? -38.681 -23.636  -12.652 1.00 60.63  ? 33  THR I OG1 1 
ATOM   15443 C CG2 . THR I  1 33  ? -39.153 -25.980  -12.354 1.00 70.84  ? 33  THR I CG2 1 
ATOM   15444 N N   . HIS I  1 34  ? -37.915 -22.883  -15.484 1.00 74.27  ? 34  HIS I N   1 
ATOM   15445 C CA  . HIS I  1 34  ? -38.045 -21.679  -16.300 1.00 62.90  ? 34  HIS I CA  1 
ATOM   15446 C C   . HIS I  1 34  ? -36.687 -21.088  -16.671 1.00 64.74  ? 34  HIS I C   1 
ATOM   15447 O O   . HIS I  1 34  ? -35.658 -21.494  -16.128 1.00 70.03  ? 34  HIS I O   1 
ATOM   15448 C CB  . HIS I  1 34  ? -38.887 -20.640  -15.565 1.00 63.37  ? 34  HIS I CB  1 
ATOM   15449 C CG  . HIS I  1 34  ? -40.230 -21.141  -15.143 1.00 70.61  ? 34  HIS I CG  1 
ATOM   15450 N ND1 . HIS I  1 34  ? -40.397 -22.077  -14.142 1.00 74.55  ? 34  HIS I ND1 1 
ATOM   15451 C CD2 . HIS I  1 34  ? -41.477 -20.826  -15.573 1.00 79.28  ? 34  HIS I CD2 1 
ATOM   15452 C CE1 . HIS I  1 34  ? -41.685 -22.322  -13.983 1.00 81.98  ? 34  HIS I CE1 1 
ATOM   15453 N NE2 . HIS I  1 34  ? -42.360 -21.579  -14.835 1.00 86.85  ? 34  HIS I NE2 1 
ATOM   15454 N N   . SER I  1 35  ? -36.691 -20.117  -17.581 1.00 65.03  ? 35  SER I N   1 
ATOM   15455 C CA  . SER I  1 35  ? -35.451 -19.588  -18.143 1.00 61.18  ? 35  SER I CA  1 
ATOM   15456 C C   . SER I  1 35  ? -35.725 -18.453  -19.119 1.00 56.25  ? 35  SER I C   1 
ATOM   15457 O O   . SER I  1 35  ? -36.783 -18.407  -19.745 1.00 61.91  ? 35  SER I O   1 
ATOM   15458 C CB  . SER I  1 35  ? -34.699 -20.698  -18.879 1.00 51.98  ? 35  SER I CB  1 
ATOM   15459 O OG  . SER I  1 35  ? -35.490 -21.216  -19.935 1.00 61.44  ? 35  SER I OG  1 
ATOM   15460 N N   . VAL I  1 36  ? -34.768 -17.540  -19.245 1.00 59.12  ? 36  VAL I N   1 
ATOM   15461 C CA  . VAL I  1 36  ? -34.851 -16.480  -20.237 1.00 55.32  ? 36  VAL I CA  1 
ATOM   15462 C C   . VAL I  1 36  ? -33.582 -16.499  -21.071 1.00 52.00  ? 36  VAL I C   1 
ATOM   15463 O O   . VAL I  1 36  ? -32.537 -16.958  -20.610 1.00 46.78  ? 36  VAL I O   1 
ATOM   15464 C CB  . VAL I  1 36  ? -35.013 -15.096  -19.583 1.00 54.90  ? 36  VAL I CB  1 
ATOM   15465 C CG1 . VAL I  1 36  ? -36.259 -15.069  -18.714 1.00 60.42  ? 36  VAL I CG1 1 
ATOM   15466 C CG2 . VAL I  1 36  ? -33.778 -14.745  -18.764 1.00 51.63  ? 36  VAL I CG2 1 
ATOM   15467 N N   . ASN I  1 37  ? -33.674 -16.015  -22.302 1.00 71.55  ? 37  ASN I N   1 
ATOM   15468 C CA  . ASN I  1 37  ? -32.506 -15.946  -23.163 1.00 62.63  ? 37  ASN I CA  1 
ATOM   15469 C C   . ASN I  1 37  ? -31.923 -14.540  -23.161 1.00 43.33  ? 37  ASN I C   1 
ATOM   15470 O O   . ASN I  1 37  ? -32.627 -13.568  -23.434 1.00 53.00  ? 37  ASN I O   1 
ATOM   15471 C CB  . ASN I  1 37  ? -32.856 -16.381  -24.585 1.00 55.10  ? 37  ASN I CB  1 
ATOM   15472 C CG  . ASN I  1 37  ? -31.633 -16.750  -25.396 1.00 62.61  ? 37  ASN I CG  1 
ATOM   15473 O OD1 . ASN I  1 37  ? -31.723 -17.002  -26.597 1.00 73.77  ? 37  ASN I OD1 1 
ATOM   15474 N ND2 . ASN I  1 37  ? -30.478 -16.786  -24.741 1.00 56.51  ? 37  ASN I ND2 1 
ATOM   15475 N N   . LEU I  1 38  ? -30.640 -14.438  -22.835 1.00 39.32  ? 38  LEU I N   1 
ATOM   15476 C CA  . LEU I  1 38  ? -29.957 -13.151  -22.798 1.00 44.97  ? 38  LEU I CA  1 
ATOM   15477 C C   . LEU I  1 38  ? -29.341 -12.830  -24.154 1.00 42.06  ? 38  LEU I C   1 
ATOM   15478 O O   . LEU I  1 38  ? -28.840 -11.728  -24.376 1.00 43.96  ? 38  LEU I O   1 
ATOM   15479 C CB  . LEU I  1 38  ? -28.874 -13.151  -21.716 1.00 36.87  ? 38  LEU I CB  1 
ATOM   15480 C CG  . LEU I  1 38  ? -29.342 -13.172  -20.260 1.00 36.59  ? 38  LEU I CG  1 
ATOM   15481 C CD1 . LEU I  1 38  ? -28.181 -13.478  -19.326 1.00 59.89  ? 38  LEU I CD1 1 
ATOM   15482 C CD2 . LEU I  1 38  ? -30.005 -11.854  -19.889 1.00 41.64  ? 38  LEU I CD2 1 
ATOM   15483 N N   . LEU I  1 39  ? -29.387 -13.802  -25.059 1.00 48.07  ? 39  LEU I N   1 
ATOM   15484 C CA  . LEU I  1 39  ? -28.796 -13.644  -26.382 1.00 44.45  ? 39  LEU I CA  1 
ATOM   15485 C C   . LEU I  1 39  ? -29.847 -13.407  -27.460 1.00 50.08  ? 39  LEU I C   1 
ATOM   15486 O O   . LEU I  1 39  ? -30.734 -14.234  -27.671 1.00 57.47  ? 39  LEU I O   1 
ATOM   15487 C CB  . LEU I  1 39  ? -27.959 -14.873  -26.739 1.00 40.09  ? 39  LEU I CB  1 
ATOM   15488 C CG  . LEU I  1 39  ? -27.370 -14.873  -28.150 1.00 41.12  ? 39  LEU I CG  1 
ATOM   15489 C CD1 . LEU I  1 39  ? -26.465 -13.667  -28.357 1.00 42.47  ? 39  LEU I CD1 1 
ATOM   15490 C CD2 . LEU I  1 39  ? -26.625 -16.170  -28.418 1.00 43.48  ? 39  LEU I CD2 1 
ATOM   15491 N N   . GLU I  1 40  ? -29.740 -12.271  -28.141 1.00 52.29  ? 40  GLU I N   1 
ATOM   15492 C CA  . GLU I  1 40  ? -30.618 -11.972  -29.263 1.00 49.96  ? 40  GLU I CA  1 
ATOM   15493 C C   . GLU I  1 40  ? -30.043 -12.566  -30.543 1.00 49.13  ? 40  GLU I C   1 
ATOM   15494 O O   . GLU I  1 40  ? -28.894 -12.306  -30.896 1.00 46.34  ? 40  GLU I O   1 
ATOM   15495 C CB  . GLU I  1 40  ? -30.806 -10.463  -29.418 1.00 40.40  ? 40  GLU I CB  1 
ATOM   15496 C CG  . GLU I  1 40  ? -31.715 -10.065  -30.572 1.00 52.39  ? 40  GLU I CG  1 
ATOM   15497 C CD  . GLU I  1 40  ? -33.132 -10.588  -30.415 1.00 62.95  ? 40  GLU I CD  1 
ATOM   15498 O OE1 . GLU I  1 40  ? -34.051 -9.763   -30.232 1.00 76.72  ? 40  GLU I OE1 1 
ATOM   15499 O OE2 . GLU I  1 40  ? -33.329 -11.820  -30.476 1.00 67.27  ? 40  GLU I OE2 1 
ATOM   15500 N N   . ASP I  1 41  ? -30.849 -13.366  -31.232 1.00 55.35  ? 41  ASP I N   1 
ATOM   15501 C CA  . ASP I  1 41  ? -30.406 -14.044  -32.443 1.00 59.01  ? 41  ASP I CA  1 
ATOM   15502 C C   . ASP I  1 41  ? -31.458 -13.945  -33.539 1.00 64.56  ? 41  ASP I C   1 
ATOM   15503 O O   . ASP I  1 41  ? -31.642 -14.878  -34.321 1.00 87.08  ? 41  ASP I O   1 
ATOM   15504 C CB  . ASP I  1 41  ? -30.104 -15.514  -32.145 1.00 70.51  ? 41  ASP I CB  1 
ATOM   15505 C CG  . ASP I  1 41  ? -31.277 -16.234  -31.502 1.00 90.00  ? 41  ASP I CG  1 
ATOM   15506 O OD1 . ASP I  1 41  ? -32.344 -15.607  -31.328 1.00 92.10  ? 41  ASP I OD1 1 
ATOM   15507 O OD2 . ASP I  1 41  ? -31.131 -17.428  -31.167 1.00 88.74  ? 41  ASP I OD2 1 
ATOM   15508 N N   . LYS I  1 42  ? -32.145 -12.809  -33.596 1.00 63.18  ? 42  LYS I N   1 
ATOM   15509 C CA  . LYS I  1 42  ? -33.252 -12.643  -34.527 1.00 71.39  ? 42  LYS I CA  1 
ATOM   15510 C C   . LYS I  1 42  ? -33.364 -11.209  -35.031 1.00 66.25  ? 42  LYS I C   1 
ATOM   15511 O O   . LYS I  1 42  ? -33.668 -10.294  -34.269 1.00 63.39  ? 42  LYS I O   1 
ATOM   15512 C CB  . LYS I  1 42  ? -34.559 -13.064  -33.854 1.00 71.68  ? 42  LYS I CB  1 
ATOM   15513 C CG  . LYS I  1 42  ? -35.465 -13.920  -34.717 1.00 100.69 ? 42  LYS I CG  1 
ATOM   15514 C CD  . LYS I  1 42  ? -36.433 -14.700  -33.848 1.00 119.87 ? 42  LYS I CD  1 
ATOM   15515 C CE  . LYS I  1 42  ? -35.679 -15.563  -32.847 1.00 112.59 ? 42  LYS I CE  1 
ATOM   15516 N NZ  . LYS I  1 42  ? -36.597 -16.263  -31.908 1.00 106.11 ? 42  LYS I NZ  1 
ATOM   15517 N N   . HIS I  1 43  ? -33.120 -11.022  -36.323 1.00 56.32  ? 43  HIS I N   1 
ATOM   15518 C CA  . HIS I  1 43  ? -33.253 -9.714   -36.950 1.00 46.49  ? 43  HIS I CA  1 
ATOM   15519 C C   . HIS I  1 43  ? -34.472 -9.704   -37.866 1.00 58.15  ? 43  HIS I C   1 
ATOM   15520 O O   . HIS I  1 43  ? -34.940 -10.759  -38.295 1.00 70.55  ? 43  HIS I O   1 
ATOM   15521 C CB  . HIS I  1 43  ? -31.997 -9.389   -37.755 1.00 39.84  ? 43  HIS I CB  1 
ATOM   15522 C CG  . HIS I  1 43  ? -31.706 -10.383  -38.834 1.00 43.93  ? 43  HIS I CG  1 
ATOM   15523 N ND1 . HIS I  1 43  ? -32.050 -10.174  -40.150 1.00 56.80  ? 43  HIS I ND1 1 
ATOM   15524 C CD2 . HIS I  1 43  ? -31.116 -11.604  -38.785 1.00 59.34  ? 43  HIS I CD2 1 
ATOM   15525 C CE1 . HIS I  1 43  ? -31.677 -11.220  -40.871 1.00 69.05  ? 43  HIS I CE1 1 
ATOM   15526 N NE2 . HIS I  1 43  ? -31.111 -12.097  -40.068 1.00 67.08  ? 43  HIS I NE2 1 
ATOM   15527 N N   . ASN I  1 44  ? -34.986 -8.516   -38.166 1.00 58.90  ? 44  ASN I N   1 
ATOM   15528 C CA  . ASN I  1 44  ? -36.168 -8.399   -39.015 1.00 51.31  ? 44  ASN I CA  1 
ATOM   15529 C C   . ASN I  1 44  ? -35.854 -8.463   -40.510 1.00 50.52  ? 44  ASN I C   1 
ATOM   15530 O O   . ASN I  1 44  ? -36.758 -8.417   -41.344 1.00 59.68  ? 44  ASN I O   1 
ATOM   15531 C CB  . ASN I  1 44  ? -36.959 -7.129   -38.684 1.00 45.49  ? 44  ASN I CB  1 
ATOM   15532 C CG  . ASN I  1 44  ? -36.167 -5.859   -38.935 1.00 47.59  ? 44  ASN I CG  1 
ATOM   15533 O OD1 . ASN I  1 44  ? -36.638 -4.757   -38.655 1.00 56.00  ? 44  ASN I OD1 1 
ATOM   15534 N ND2 . ASN I  1 44  ? -34.959 -6.005   -39.467 1.00 46.41  ? 44  ASN I ND2 1 
ATOM   15535 N N   . GLY I  1 45  ? -34.571 -8.571   -40.840 1.00 57.91  ? 45  GLY I N   1 
ATOM   15536 C CA  . GLY I  1 45  ? -34.147 -8.681   -42.224 1.00 67.92  ? 45  GLY I CA  1 
ATOM   15537 C C   . GLY I  1 45  ? -34.488 -7.459   -43.055 1.00 60.58  ? 45  GLY I C   1 
ATOM   15538 O O   . GLY I  1 45  ? -34.664 -7.551   -44.270 1.00 60.85  ? 45  GLY I O   1 
ATOM   15539 N N   . LYS I  1 46  ? -34.582 -6.310   -42.396 1.00 57.41  ? 46  LYS I N   1 
ATOM   15540 C CA  . LYS I  1 46  ? -34.872 -5.057   -43.079 1.00 59.64  ? 46  LYS I CA  1 
ATOM   15541 C C   . LYS I  1 46  ? -33.803 -4.024   -42.766 1.00 54.72  ? 46  LYS I C   1 
ATOM   15542 O O   . LYS I  1 46  ? -33.353 -3.914   -41.627 1.00 45.69  ? 46  LYS I O   1 
ATOM   15543 C CB  . LYS I  1 46  ? -36.219 -4.503   -42.625 1.00 59.79  ? 46  LYS I CB  1 
ATOM   15544 C CG  . LYS I  1 46  ? -37.409 -5.392   -42.904 1.00 76.15  ? 46  LYS I CG  1 
ATOM   15545 C CD  . LYS I  1 46  ? -38.615 -4.861   -42.158 1.00 89.13  ? 46  LYS I CD  1 
ATOM   15546 C CE  . LYS I  1 46  ? -39.878 -5.614   -42.510 1.00 114.64 ? 46  LYS I CE  1 
ATOM   15547 N NZ  . LYS I  1 46  ? -40.991 -5.165   -41.636 1.00 113.32 ? 46  LYS I NZ  1 
ATOM   15548 N N   . LEU I  1 47  ? -33.401 -3.262   -43.775 1.00 62.65  ? 47  LEU I N   1 
ATOM   15549 C CA  . LEU I  1 47  ? -32.543 -2.111   -43.541 1.00 54.75  ? 47  LEU I CA  1 
ATOM   15550 C C   . LEU I  1 47  ? -33.427 -0.933   -43.152 1.00 53.18  ? 47  LEU I C   1 
ATOM   15551 O O   . LEU I  1 47  ? -33.965 -0.242   -44.018 1.00 68.99  ? 47  LEU I O   1 
ATOM   15552 C CB  . LEU I  1 47  ? -31.727 -1.782   -44.790 1.00 38.13  ? 47  LEU I CB  1 
ATOM   15553 C CG  . LEU I  1 47  ? -30.749 -2.876   -45.220 1.00 50.48  ? 47  LEU I CG  1 
ATOM   15554 C CD1 . LEU I  1 47  ? -29.750 -2.335   -46.229 1.00 52.70  ? 47  LEU I CD1 1 
ATOM   15555 C CD2 . LEU I  1 47  ? -30.037 -3.480   -44.015 1.00 50.67  ? 47  LEU I CD2 1 
ATOM   15556 N N   . CYS I  1 48  ? -33.589 -0.717   -41.848 1.00 48.00  ? 48  CYS I N   1 
ATOM   15557 C CA  . CYS I  1 48  ? -34.543 0.277    -41.351 1.00 57.98  ? 48  CYS I CA  1 
ATOM   15558 C C   . CYS I  1 48  ? -33.906 1.612    -40.957 1.00 49.40  ? 48  CYS I C   1 
ATOM   15559 O O   . CYS I  1 48  ? -32.682 1.775    -41.013 1.00 46.03  ? 48  CYS I O   1 
ATOM   15560 C CB  . CYS I  1 48  ? -35.342 -0.280   -40.161 1.00 52.16  ? 48  CYS I CB  1 
ATOM   15561 S SG  . CYS I  1 48  ? -36.728 -1.362   -40.604 1.00 89.10  ? 48  CYS I SG  1 
ATOM   15562 N N   . LYS I  1 49  ? -34.752 2.556    -40.541 1.00 57.43  ? 49  LYS I N   1 
ATOM   15563 C CA  . LYS I  1 49  ? -34.296 3.908    -40.225 1.00 62.37  ? 49  LYS I CA  1 
ATOM   15564 C C   . LYS I  1 49  ? -33.716 3.986    -38.817 1.00 55.48  ? 49  LYS I C   1 
ATOM   15565 O O   . LYS I  1 49  ? -34.295 3.475    -37.853 1.00 64.21  ? 49  LYS I O   1 
ATOM   15566 C CB  . LYS I  1 49  ? -35.419 4.931    -40.395 1.00 66.80  ? 49  LYS I CB  1 
ATOM   15567 C CG  . LYS I  1 49  ? -36.216 4.786    -41.686 1.00 65.60  ? 49  LYS I CG  1 
ATOM   15568 C CD  . LYS I  1 49  ? -37.341 5.810    -41.731 1.00 80.21  ? 49  LYS I CD  1 
ATOM   15569 C CE  . LYS I  1 49  ? -37.522 6.420    -40.354 1.00 84.27  ? 49  LYS I CE  1 
ATOM   15570 N NZ  . LYS I  1 49  ? -38.906 6.863    -40.040 1.00 88.75  ? 49  LYS I NZ  1 
ATOM   15571 N N   . LEU I  1 50  ? -32.574 4.652    -38.710 1.00 60.89  ? 50  LEU I N   1 
ATOM   15572 C CA  . LEU I  1 50  ? -31.738 4.570    -37.520 1.00 67.40  ? 50  LEU I CA  1 
ATOM   15573 C C   . LEU I  1 50  ? -32.169 5.369    -36.287 1.00 84.98  ? 50  LEU I C   1 
ATOM   15574 O O   . LEU I  1 50  ? -32.180 4.850    -35.173 1.00 105.38 ? 50  LEU I O   1 
ATOM   15575 C CB  . LEU I  1 50  ? -30.308 4.977    -37.883 1.00 56.28  ? 50  LEU I CB  1 
ATOM   15576 C CG  . LEU I  1 50  ? -29.214 4.680    -36.845 1.00 57.07  ? 50  LEU I CG  1 
ATOM   15577 C CD1 . LEU I  1 50  ? -29.626 3.540    -35.931 1.00 60.36  ? 50  LEU I CD1 1 
ATOM   15578 C CD2 . LEU I  1 50  ? -27.848 4.404    -37.487 1.00 47.09  ? 50  LEU I CD2 1 
ATOM   15579 N N   . ARG I  1 51  ? -32.508 6.635    -36.487 1.00 72.19  ? 51  ARG I N   1 
ATOM   15580 C CA  . ARG I  1 51  ? -33.133 7.422    -35.434 1.00 90.03  ? 51  ARG I CA  1 
ATOM   15581 C C   . ARG I  1 51  ? -34.605 7.515    -35.809 1.00 96.01  ? 51  ARG I C   1 
ATOM   15582 O O   . ARG I  1 51  ? -35.439 6.751    -35.320 1.00 110.44 ? 51  ARG I O   1 
ATOM   15583 C CB  . ARG I  1 51  ? -32.552 8.831    -35.322 1.00 100.84 ? 51  ARG I CB  1 
ATOM   15584 C CG  . ARG I  1 51  ? -31.063 8.889    -35.423 1.00 113.62 ? 51  ARG I CG  1 
ATOM   15585 C CD  . ARG I  1 51  ? -30.557 10.194   -34.841 1.00 150.13 ? 51  ARG I CD  1 
ATOM   15586 N NE  . ARG I  1 51  ? -30.754 10.290   -33.394 1.00 162.86 ? 51  ARG I NE  1 
ATOM   15587 C CZ  . ARG I  1 51  ? -31.414 11.271   -32.780 1.00 152.72 ? 51  ARG I CZ  1 
ATOM   15588 N NH1 . ARG I  1 51  ? -31.963 12.260   -33.477 1.00 138.04 ? 51  ARG I NH1 1 
ATOM   15589 N NH2 . ARG I  1 51  ? -31.525 11.263   -31.458 1.00 134.88 ? 51  ARG I NH2 1 
ATOM   15590 N N   . GLY I  1 52  ? -34.903 8.474    -36.681 1.00 79.25  ? 52  GLY I N   1 
ATOM   15591 C CA  . GLY I  1 52  ? -36.195 8.601    -37.333 1.00 92.51  ? 52  GLY I CA  1 
ATOM   15592 C C   . GLY I  1 52  ? -35.955 8.960    -38.788 1.00 89.90  ? 52  GLY I C   1 
ATOM   15593 O O   . GLY I  1 52  ? -36.891 9.144    -39.563 1.00 87.45  ? 52  GLY I O   1 
ATOM   15594 N N   . VAL I  1 53  ? -34.681 9.058    -39.156 1.00 91.07  ? 53  VAL I N   1 
ATOM   15595 C CA  . VAL I  1 53  ? -34.297 9.394    -40.525 1.00 73.54  ? 53  VAL I CA  1 
ATOM   15596 C C   . VAL I  1 53  ? -33.800 8.181    -41.301 1.00 53.26  ? 53  VAL I C   1 
ATOM   15597 O O   . VAL I  1 53  ? -33.129 7.314    -40.748 1.00 50.89  ? 53  VAL I O   1 
ATOM   15598 C CB  . VAL I  1 53  ? -33.237 10.518   -40.567 1.00 55.54  ? 53  VAL I CB  1 
ATOM   15599 C CG1 . VAL I  1 53  ? -32.722 10.822   -39.161 1.00 43.26  ? 53  VAL I CG1 1 
ATOM   15600 C CG2 . VAL I  1 53  ? -32.110 10.151   -41.517 1.00 61.33  ? 53  VAL I CG2 1 
ATOM   15601 N N   . ALA I  1 54  ? -34.119 8.149    -42.592 1.00 52.48  ? 54  ALA I N   1 
ATOM   15602 C CA  . ALA I  1 54  ? -33.856 6.988    -43.433 1.00 56.20  ? 54  ALA I CA  1 
ATOM   15603 C C   . ALA I  1 54  ? -32.419 6.922    -43.950 1.00 58.21  ? 54  ALA I C   1 
ATOM   15604 O O   . ALA I  1 54  ? -31.730 7.940    -44.025 1.00 54.76  ? 54  ALA I O   1 
ATOM   15605 C CB  . ALA I  1 54  ? -34.838 6.960    -44.599 1.00 66.16  ? 54  ALA I CB  1 
ATOM   15606 N N   . PRO I  1 55  ? -31.965 5.711    -44.308 1.00 41.36  ? 55  PRO I N   1 
ATOM   15607 C CA  . PRO I  1 55  ? -30.656 5.542    -44.944 1.00 40.40  ? 55  PRO I CA  1 
ATOM   15608 C C   . PRO I  1 55  ? -30.671 6.041    -46.385 1.00 56.19  ? 55  PRO I C   1 
ATOM   15609 O O   . PRO I  1 55  ? -31.732 6.101    -47.008 1.00 66.29  ? 55  PRO I O   1 
ATOM   15610 C CB  . PRO I  1 55  ? -30.457 4.024    -44.925 1.00 38.33  ? 55  PRO I CB  1 
ATOM   15611 C CG  . PRO I  1 55  ? -31.839 3.470    -44.922 1.00 41.82  ? 55  PRO I CG  1 
ATOM   15612 C CD  . PRO I  1 55  ? -32.633 4.418    -44.072 1.00 33.40  ? 55  PRO I CD  1 
ATOM   15613 N N   . LEU I  1 56  ? -29.502 6.400    -46.902 1.00 47.38  ? 56  LEU I N   1 
ATOM   15614 C CA  . LEU I  1 56  ? -29.369 6.782    -48.300 1.00 40.23  ? 56  LEU I CA  1 
ATOM   15615 C C   . LEU I  1 56  ? -28.985 5.554    -49.117 1.00 47.25  ? 56  LEU I C   1 
ATOM   15616 O O   . LEU I  1 56  ? -27.856 5.073    -49.033 1.00 55.09  ? 56  LEU I O   1 
ATOM   15617 C CB  . LEU I  1 56  ? -28.313 7.877    -48.457 1.00 46.10  ? 56  LEU I CB  1 
ATOM   15618 C CG  . LEU I  1 56  ? -28.021 8.370    -49.875 1.00 49.86  ? 56  LEU I CG  1 
ATOM   15619 C CD1 . LEU I  1 56  ? -29.245 9.043    -50.470 1.00 59.19  ? 56  LEU I CD1 1 
ATOM   15620 C CD2 . LEU I  1 56  ? -26.833 9.318    -49.870 1.00 45.21  ? 56  LEU I CD2 1 
ATOM   15621 N N   . HIS I  1 57  ? -29.933 5.042    -49.894 1.00 46.21  ? 57  HIS I N   1 
ATOM   15622 C CA  . HIS I  1 57  ? -29.701 3.843    -50.690 1.00 46.92  ? 57  HIS I CA  1 
ATOM   15623 C C   . HIS I  1 57  ? -29.329 4.223    -52.114 1.00 63.49  ? 57  HIS I C   1 
ATOM   15624 O O   . HIS I  1 57  ? -30.097 4.892    -52.794 1.00 64.88  ? 57  HIS I O   1 
ATOM   15625 C CB  . HIS I  1 57  ? -30.951 2.963    -50.699 1.00 50.09  ? 57  HIS I CB  1 
ATOM   15626 C CG  . HIS I  1 57  ? -30.698 1.562    -51.163 1.00 51.50  ? 57  HIS I CG  1 
ATOM   15627 N ND1 . HIS I  1 57  ? -30.638 1.218    -52.495 1.00 65.60  ? 57  HIS I ND1 1 
ATOM   15628 C CD2 . HIS I  1 57  ? -30.489 0.421    -50.468 1.00 62.74  ? 57  HIS I CD2 1 
ATOM   15629 C CE1 . HIS I  1 57  ? -30.401 -0.078   -52.602 1.00 71.85  ? 57  HIS I CE1 1 
ATOM   15630 N NE2 . HIS I  1 57  ? -30.307 -0.586   -51.386 1.00 74.48  ? 57  HIS I NE2 1 
ATOM   15631 N N   . LEU I  1 58  ? -28.156 3.783    -52.562 1.00 55.71  ? 58  LEU I N   1 
ATOM   15632 C CA  . LEU I  1 58  ? -27.631 4.189    -53.864 1.00 61.44  ? 58  LEU I CA  1 
ATOM   15633 C C   . LEU I  1 58  ? -27.988 3.223    -54.988 1.00 72.82  ? 58  LEU I C   1 
ATOM   15634 O O   . LEU I  1 58  ? -27.808 3.538    -56.164 1.00 80.56  ? 58  LEU I O   1 
ATOM   15635 C CB  . LEU I  1 58  ? -26.115 4.362    -53.797 1.00 60.73  ? 58  LEU I CB  1 
ATOM   15636 C CG  . LEU I  1 58  ? -25.613 5.329    -52.725 1.00 44.55  ? 58  LEU I CG  1 
ATOM   15637 C CD1 . LEU I  1 58  ? -24.105 5.478    -52.815 1.00 56.76  ? 58  LEU I CD1 1 
ATOM   15638 C CD2 . LEU I  1 58  ? -26.306 6.680    -52.827 1.00 56.56  ? 58  LEU I CD2 1 
ATOM   15639 N N   . GLY I  1 59  ? -28.484 2.046    -54.624 1.00 61.65  ? 59  GLY I N   1 
ATOM   15640 C CA  . GLY I  1 59  ? -28.888 1.058    -55.608 1.00 61.85  ? 59  GLY I CA  1 
ATOM   15641 C C   . GLY I  1 59  ? -27.744 0.543    -56.460 1.00 70.10  ? 59  GLY I C   1 
ATOM   15642 O O   . GLY I  1 59  ? -26.810 -0.078   -55.953 1.00 85.69  ? 59  GLY I O   1 
ATOM   15643 N N   . LYS I  1 60  ? -27.817 0.808    -57.760 1.00 76.80  ? 60  LYS I N   1 
ATOM   15644 C CA  . LYS I  1 60  ? -26.831 0.302    -58.709 1.00 94.35  ? 60  LYS I CA  1 
ATOM   15645 C C   . LYS I  1 60  ? -25.547 1.131    -58.712 1.00 84.45  ? 60  LYS I C   1 
ATOM   15646 O O   . LYS I  1 60  ? -24.578 0.784    -59.387 1.00 95.68  ? 60  LYS I O   1 
ATOM   15647 C CB  . LYS I  1 60  ? -27.430 0.255    -60.118 1.00 102.48 ? 60  LYS I CB  1 
ATOM   15648 C CG  . LYS I  1 60  ? -26.601 -0.522   -61.130 1.00 132.83 ? 60  LYS I CG  1 
ATOM   15649 C CD  . LYS I  1 60  ? -26.537 -1.999   -60.773 1.00 140.71 ? 60  LYS I CD  1 
ATOM   15650 C CE  . LYS I  1 60  ? -27.918 -2.635   -60.804 1.00 151.07 ? 60  LYS I CE  1 
ATOM   15651 N NZ  . LYS I  1 60  ? -27.868 -4.085   -60.468 1.00 138.59 ? 60  LYS I NZ  1 
ATOM   15652 N N   . CYS I  1 61  ? -25.543 2.223    -57.955 1.00 72.20  ? 61  CYS I N   1 
ATOM   15653 C CA  . CYS I  1 61  ? -24.395 3.123    -57.924 1.00 69.22  ? 61  CYS I CA  1 
ATOM   15654 C C   . CYS I  1 61  ? -23.653 3.077    -56.595 1.00 65.66  ? 61  CYS I C   1 
ATOM   15655 O O   . CYS I  1 61  ? -24.195 2.640    -55.578 1.00 72.19  ? 61  CYS I O   1 
ATOM   15656 C CB  . CYS I  1 61  ? -24.834 4.561    -58.209 1.00 65.38  ? 61  CYS I CB  1 
ATOM   15657 S SG  . CYS I  1 61  ? -25.581 4.820    -59.834 1.00 108.87 ? 61  CYS I SG  1 
ATOM   15658 N N   . ASN I  1 62  ? -22.404 3.529    -56.617 1.00 52.59  ? 62  ASN I N   1 
ATOM   15659 C CA  . ASN I  1 62  ? -21.623 3.676    -55.399 1.00 53.08  ? 62  ASN I CA  1 
ATOM   15660 C C   . ASN I  1 62  ? -21.400 5.145    -55.073 1.00 54.50  ? 62  ASN I C   1 
ATOM   15661 O O   . ASN I  1 62  ? -21.752 6.029    -55.855 1.00 65.56  ? 62  ASN I O   1 
ATOM   15662 C CB  . ASN I  1 62  ? -20.283 2.938    -55.505 1.00 64.68  ? 62  ASN I CB  1 
ATOM   15663 C CG  . ASN I  1 62  ? -19.434 3.426    -56.663 1.00 64.80  ? 62  ASN I CG  1 
ATOM   15664 O OD1 . ASN I  1 62  ? -19.593 4.550    -57.133 1.00 65.40  ? 62  ASN I OD1 1 
ATOM   15665 N ND2 . ASN I  1 62  ? -18.526 2.575    -57.132 1.00 69.80  ? 62  ASN I ND2 1 
ATOM   15666 N N   . ILE I  1 63  ? -20.814 5.399    -53.912 1.00 44.27  ? 63  ILE I N   1 
ATOM   15667 C CA  . ILE I  1 63  ? -20.543 6.761    -53.486 1.00 45.28  ? 63  ILE I CA  1 
ATOM   15668 C C   . ILE I  1 63  ? -19.935 7.606    -54.615 1.00 44.35  ? 63  ILE I C   1 
ATOM   15669 O O   . ILE I  1 63  ? -20.485 8.643    -54.969 1.00 55.28  ? 63  ILE I O   1 
ATOM   15670 C CB  . ILE I  1 63  ? -19.660 6.780    -52.227 1.00 58.16  ? 63  ILE I CB  1 
ATOM   15671 C CG1 . ILE I  1 63  ? -20.408 6.141    -51.051 1.00 51.20  ? 63  ILE I CG1 1 
ATOM   15672 C CG2 . ILE I  1 63  ? -19.246 8.197    -51.883 1.00 47.56  ? 63  ILE I CG2 1 
ATOM   15673 C CD1 . ILE I  1 63  ? -21.688 6.866    -50.670 1.00 56.80  ? 63  ILE I CD1 1 
ATOM   15674 N N   . ALA I  1 64  ? -18.822 7.152    -55.191 1.00 43.80  ? 64  ALA I N   1 
ATOM   15675 C CA  . ALA I  1 64  ? -18.181 7.860    -56.307 1.00 48.46  ? 64  ALA I CA  1 
ATOM   15676 C C   . ALA I  1 64  ? -19.169 8.297    -57.392 1.00 53.23  ? 64  ALA I C   1 
ATOM   15677 O O   . ALA I  1 64  ? -19.271 9.483    -57.708 1.00 51.87  ? 64  ALA I O   1 
ATOM   15678 C CB  . ALA I  1 64  ? -17.060 7.013    -56.916 1.00 44.04  ? 64  ALA I CB  1 
ATOM   15679 N N   . GLY I  1 65  ? -19.887 7.336    -57.964 1.00 53.28  ? 65  GLY I N   1 
ATOM   15680 C CA  . GLY I  1 65  ? -20.838 7.623    -59.023 1.00 52.74  ? 65  GLY I CA  1 
ATOM   15681 C C   . GLY I  1 65  ? -21.916 8.616    -58.627 1.00 51.58  ? 65  GLY I C   1 
ATOM   15682 O O   . GLY I  1 65  ? -22.291 9.481    -59.419 1.00 63.21  ? 65  GLY I O   1 
ATOM   15683 N N   . TRP I  1 66  ? -22.408 8.498    -57.396 1.00 46.53  ? 66  TRP I N   1 
ATOM   15684 C CA  . TRP I  1 66  ? -23.528 9.316    -56.929 1.00 59.70  ? 66  TRP I CA  1 
ATOM   15685 C C   . TRP I  1 66  ? -23.213 10.815   -56.838 1.00 46.03  ? 66  TRP I C   1 
ATOM   15686 O O   . TRP I  1 66  ? -24.004 11.641   -57.296 1.00 64.88  ? 66  TRP I O   1 
ATOM   15687 C CB  . TRP I  1 66  ? -24.076 8.792    -55.593 1.00 53.94  ? 66  TRP I CB  1 
ATOM   15688 C CG  . TRP I  1 66  ? -24.920 9.802    -54.866 1.00 60.13  ? 66  TRP I CG  1 
ATOM   15689 C CD1 . TRP I  1 66  ? -26.098 10.343   -55.290 1.00 71.90  ? 66  TRP I CD1 1 
ATOM   15690 C CD2 . TRP I  1 66  ? -24.647 10.393   -53.590 1.00 52.49  ? 66  TRP I CD2 1 
ATOM   15691 N NE1 . TRP I  1 66  ? -26.572 11.236   -54.359 1.00 73.96  ? 66  TRP I NE1 1 
ATOM   15692 C CE2 . TRP I  1 66  ? -25.697 11.282   -53.304 1.00 54.43  ? 66  TRP I CE2 1 
ATOM   15693 C CE3 . TRP I  1 66  ? -23.620 10.252   -52.659 1.00 61.20  ? 66  TRP I CE3 1 
ATOM   15694 C CZ2 . TRP I  1 66  ? -25.741 12.030   -52.129 1.00 50.80  ? 66  TRP I CZ2 1 
ATOM   15695 C CZ3 . TRP I  1 66  ? -23.660 10.994   -51.500 1.00 57.39  ? 66  TRP I CZ3 1 
ATOM   15696 C CH2 . TRP I  1 66  ? -24.712 11.869   -51.241 1.00 59.55  ? 66  TRP I CH2 1 
ATOM   15697 N N   . ILE I  1 67  ? -22.070 11.163   -56.250 1.00 39.39  ? 67  ILE I N   1 
ATOM   15698 C CA  . ILE I  1 67  ? -21.672 12.567   -56.125 1.00 59.79  ? 67  ILE I CA  1 
ATOM   15699 C C   . ILE I  1 67  ? -21.116 13.124   -57.433 1.00 69.20  ? 67  ILE I C   1 
ATOM   15700 O O   . ILE I  1 67  ? -21.383 14.269   -57.787 1.00 62.33  ? 67  ILE I O   1 
ATOM   15701 C CB  . ILE I  1 67  ? -20.613 12.795   -55.021 1.00 47.86  ? 67  ILE I CB  1 
ATOM   15702 C CG1 . ILE I  1 67  ? -20.044 11.468   -54.528 1.00 71.06  ? 67  ILE I CG1 1 
ATOM   15703 C CG2 . ILE I  1 67  ? -21.195 13.594   -53.867 1.00 46.84  ? 67  ILE I CG2 1 
ATOM   15704 C CD1 . ILE I  1 67  ? -18.596 11.547   -54.121 1.00 82.35  ? 67  ILE I CD1 1 
ATOM   15705 N N   . LEU I  1 68  ? -20.332 12.323   -58.146 1.00 56.93  ? 68  LEU I N   1 
ATOM   15706 C CA  . LEU I  1 68  ? -19.753 12.788   -59.402 1.00 53.58  ? 68  LEU I CA  1 
ATOM   15707 C C   . LEU I  1 68  ? -20.819 12.962   -60.482 1.00 62.24  ? 68  LEU I C   1 
ATOM   15708 O O   . LEU I  1 68  ? -20.580 13.616   -61.497 1.00 65.58  ? 68  LEU I O   1 
ATOM   15709 C CB  . LEU I  1 68  ? -18.620 11.870   -59.876 1.00 53.26  ? 68  LEU I CB  1 
ATOM   15710 C CG  . LEU I  1 68  ? -17.308 12.068   -59.115 1.00 53.36  ? 68  LEU I CG  1 
ATOM   15711 C CD1 . LEU I  1 68  ? -16.109 11.547   -59.892 1.00 50.75  ? 68  LEU I CD1 1 
ATOM   15712 C CD2 . LEU I  1 68  ? -17.134 13.536   -58.805 1.00 35.99  ? 68  LEU I CD2 1 
ATOM   15713 N N   . GLY I  1 69  ? -22.000 12.397   -60.246 1.00 60.27  ? 69  GLY I N   1 
ATOM   15714 C CA  . GLY I  1 69  ? -23.113 12.560   -61.162 1.00 64.01  ? 69  GLY I CA  1 
ATOM   15715 C C   . GLY I  1 69  ? -23.023 11.669   -62.382 1.00 72.20  ? 69  GLY I C   1 
ATOM   15716 O O   . GLY I  1 69  ? -23.291 12.107   -63.500 1.00 81.22  ? 69  GLY I O   1 
ATOM   15717 N N   . ASN I  1 70  ? -22.635 10.415   -62.170 1.00 62.56  ? 70  ASN I N   1 
ATOM   15718 C CA  . ASN I  1 70  ? -22.621 9.434    -63.245 1.00 73.78  ? 70  ASN I CA  1 
ATOM   15719 C C   . ASN I  1 70  ? -23.991 9.401    -63.911 1.00 82.71  ? 70  ASN I C   1 
ATOM   15720 O O   . ASN I  1 70  ? -25.013 9.377    -63.225 1.00 75.71  ? 70  ASN I O   1 
ATOM   15721 C CB  . ASN I  1 70  ? -22.255 8.051    -62.700 1.00 73.70  ? 70  ASN I CB  1 
ATOM   15722 C CG  . ASN I  1 70  ? -22.011 7.031    -63.800 1.00 82.00  ? 70  ASN I CG  1 
ATOM   15723 O OD1 . ASN I  1 70  ? -22.797 6.910    -64.739 1.00 87.83  ? 70  ASN I OD1 1 
ATOM   15724 N ND2 . ASN I  1 70  ? -20.920 6.283    -63.679 1.00 73.29  ? 70  ASN I ND2 1 
ATOM   15725 N N   . PRO I  1 71  ? -24.019 9.419    -65.252 1.00 97.33  ? 71  PRO I N   1 
ATOM   15726 C CA  . PRO I  1 71  ? -25.279 9.420    -66.002 1.00 91.29  ? 71  PRO I CA  1 
ATOM   15727 C C   . PRO I  1 71  ? -26.266 8.357    -65.519 1.00 91.03  ? 71  PRO I C   1 
ATOM   15728 O O   . PRO I  1 71  ? -27.476 8.547    -65.639 1.00 110.75 ? 71  PRO I O   1 
ATOM   15729 C CB  . PRO I  1 71  ? -24.828 9.109    -67.430 1.00 86.38  ? 71  PRO I CB  1 
ATOM   15730 C CG  . PRO I  1 71  ? -23.453 9.671    -67.508 1.00 98.86  ? 71  PRO I CG  1 
ATOM   15731 C CD  . PRO I  1 71  ? -22.845 9.483    -66.142 1.00 91.63  ? 71  PRO I CD  1 
ATOM   15732 N N   . GLU I  1 72  ? -25.754 7.259    -64.974 1.00 92.92  ? 72  GLU I N   1 
ATOM   15733 C CA  . GLU I  1 72  ? -26.604 6.151    -64.547 1.00 97.77  ? 72  GLU I CA  1 
ATOM   15734 C C   . GLU I  1 72  ? -27.046 6.259    -63.087 1.00 86.35  ? 72  GLU I C   1 
ATOM   15735 O O   . GLU I  1 72  ? -27.849 5.456    -62.615 1.00 83.99  ? 72  GLU I O   1 
ATOM   15736 C CB  . GLU I  1 72  ? -25.899 4.812    -64.789 1.00 88.63  ? 72  GLU I CB  1 
ATOM   15737 C CG  . GLU I  1 72  ? -25.512 4.562    -66.242 1.00 109.44 ? 72  GLU I CG  1 
ATOM   15738 C CD  . GLU I  1 72  ? -26.714 4.363    -67.147 1.00 125.66 ? 72  GLU I CD  1 
ATOM   15739 O OE1 . GLU I  1 72  ? -27.783 3.965    -66.639 1.00 124.02 ? 72  GLU I OE1 1 
ATOM   15740 O OE2 . GLU I  1 72  ? -26.587 4.600    -68.368 1.00 119.33 ? 72  GLU I OE2 1 
ATOM   15741 N N   . CYS I  1 73  ? -26.527 7.253    -62.374 1.00 102.03 ? 73  CYS I N   1 
ATOM   15742 C CA  . CYS I  1 73  ? -26.910 7.471    -60.982 1.00 102.93 ? 73  CYS I CA  1 
ATOM   15743 C C   . CYS I  1 73  ? -27.936 8.602    -60.861 1.00 123.68 ? 73  CYS I C   1 
ATOM   15744 O O   . CYS I  1 73  ? -27.805 9.477    -60.008 1.00 129.17 ? 73  CYS I O   1 
ATOM   15745 C CB  . CYS I  1 73  ? -25.670 7.796    -60.146 1.00 92.81  ? 73  CYS I CB  1 
ATOM   15746 S SG  . CYS I  1 73  ? -24.428 6.472    -60.095 1.00 87.47  ? 73  CYS I SG  1 
ATOM   15747 N N   . GLU I  1 74  ? -28.965 8.555    -61.705 1.00 145.68 ? 74  GLU I N   1 
ATOM   15748 C CA  . GLU I  1 74  ? -29.857 9.691    -61.937 1.00 155.04 ? 74  GLU I CA  1 
ATOM   15749 C C   . GLU I  1 74  ? -30.948 9.802    -60.903 1.00 164.05 ? 74  GLU I C   1 
ATOM   15750 O O   . GLU I  1 74  ? -31.227 10.882   -60.381 1.00 161.11 ? 74  GLU I O   1 
ATOM   15751 C CB  . GLU I  1 74  ? -30.519 9.551    -63.309 1.00 146.36 ? 74  GLU I CB  1 
ATOM   15752 C CG  . GLU I  1 74  ? -30.783 10.858   -64.045 1.00 162.08 ? 74  GLU I CG  1 
ATOM   15753 C CD  . GLU I  1 74  ? -30.438 10.777   -65.525 1.00 166.86 ? 74  GLU I CD  1 
ATOM   15754 O OE1 . GLU I  1 74  ? -29.805 9.787    -65.957 1.00 164.47 ? 74  GLU I OE1 1 
ATOM   15755 O OE2 . GLU I  1 74  ? -30.797 11.720   -66.257 1.00 153.47 ? 74  GLU I OE2 1 
ATOM   15756 N N   . SER I  1 75  ? -31.566 8.672    -60.600 1.00 164.23 ? 75  SER I N   1 
ATOM   15757 C CA  . SER I  1 75  ? -32.873 8.680    -59.939 1.00 176.27 ? 75  SER I CA  1 
ATOM   15758 C C   . SER I  1 75  ? -32.926 9.156    -58.483 1.00 182.65 ? 75  SER I C   1 
ATOM   15759 O O   . SER I  1 75  ? -33.942 9.710    -58.055 1.00 188.67 ? 75  SER I O   1 
ATOM   15760 C CB  . SER I  1 75  ? -33.480 7.284    -60.039 1.00 175.26 ? 75  SER I CB  1 
ATOM   15761 O OG  . SER I  1 75  ? -32.575 6.425    -60.751 1.00 159.05 ? 75  SER I OG  1 
ATOM   15762 N N   . LEU I  1 76  ? -31.846 8.954    -57.736 1.00 187.61 ? 76  LEU I N   1 
ATOM   15763 C CA  . LEU I  1 76  ? -31.851 9.263    -56.313 1.00 192.83 ? 76  LEU I CA  1 
ATOM   15764 C C   . LEU I  1 76  ? -31.533 10.720   -55.891 1.00 194.40 ? 76  LEU I C   1 
ATOM   15765 O O   . LEU I  1 76  ? -31.302 10.972   -54.694 1.00 194.59 ? 76  LEU I O   1 
ATOM   15766 C CB  . LEU I  1 76  ? -30.901 8.321    -55.578 1.00 184.42 ? 76  LEU I CB  1 
ATOM   15767 C CG  . LEU I  1 76  ? -31.368 6.919    -55.168 1.00 175.01 ? 76  LEU I CG  1 
ATOM   15768 C CD1 . LEU I  1 76  ? -30.096 6.136    -55.055 1.00 144.54 ? 76  LEU I CD1 1 
ATOM   15769 C CD2 . LEU I  1 76  ? -32.150 6.960    -53.857 1.00 172.61 ? 76  LEU I CD2 1 
ATOM   15770 N N   . SER I  1 77  ? -31.549 11.675   -56.826 1.00 164.66 ? 77  SER I N   1 
ATOM   15771 C CA  . SER I  1 77  ? -31.423 13.078   -56.452 1.00 171.97 ? 77  SER I CA  1 
ATOM   15772 C C   . SER I  1 77  ? -32.509 13.332   -55.451 1.00 194.34 ? 77  SER I C   1 
ATOM   15773 O O   . SER I  1 77  ? -33.390 12.484   -55.277 1.00 191.38 ? 77  SER I O   1 
ATOM   15774 C CB  . SER I  1 77  ? -31.635 14.020   -57.649 1.00 157.94 ? 77  SER I CB  1 
ATOM   15775 O OG  . SER I  1 77  ? -30.733 13.740   -58.696 1.00 115.51 ? 77  SER I OG  1 
ATOM   15776 N N   . THR I  1 78  ? -32.447 14.504   -54.819 1.00 240.71 ? 78  THR I N   1 
ATOM   15777 C CA  . THR I  1 78  ? -33.403 14.925   -53.797 1.00 234.45 ? 78  THR I CA  1 
ATOM   15778 C C   . THR I  1 78  ? -33.324 14.056   -52.554 1.00 219.64 ? 78  THR I C   1 
ATOM   15779 O O   . THR I  1 78  ? -34.185 13.224   -52.344 1.00 218.90 ? 78  THR I O   1 
ATOM   15780 C CB  . THR I  1 78  ? -34.867 14.904   -54.312 1.00 233.42 ? 78  THR I CB  1 
ATOM   15781 O OG1 . THR I  1 78  ? -35.188 13.587   -54.777 1.00 231.50 ? 78  THR I OG1 1 
ATOM   15782 C CG2 . THR I  1 78  ? -35.078 15.932   -55.427 1.00 215.68 ? 78  THR I CG2 1 
ATOM   15783 N N   . ALA I  1 79  ? -32.272 14.218   -51.761 1.00 177.10 ? 79  ALA I N   1 
ATOM   15784 C CA  . ALA I  1 79  ? -32.300 13.746   -50.384 1.00 146.58 ? 79  ALA I CA  1 
ATOM   15785 C C   . ALA I  1 79  ? -31.777 14.849   -49.474 1.00 127.31 ? 79  ALA I C   1 
ATOM   15786 O O   . ALA I  1 79  ? -30.772 15.483   -49.783 1.00 121.49 ? 79  ALA I O   1 
ATOM   15787 C CB  . ALA I  1 79  ? -31.498 12.453   -50.210 1.00 139.39 ? 79  ALA I CB  1 
ATOM   15788 N N   . SER I  1 80  ? -32.465 15.089   -48.362 1.00 96.71  ? 80  SER I N   1 
ATOM   15789 C CA  . SER I  1 80  ? -32.098 16.192   -47.473 1.00 90.29  ? 80  SER I CA  1 
ATOM   15790 C C   . SER I  1 80  ? -31.171 15.757   -46.341 1.00 67.91  ? 80  SER I C   1 
ATOM   15791 O O   . SER I  1 80  ? -30.378 16.551   -45.840 1.00 62.22  ? 80  SER I O   1 
ATOM   15792 C CB  . SER I  1 80  ? -33.347 16.863   -46.899 1.00 103.67 ? 80  SER I CB  1 
ATOM   15793 O OG  . SER I  1 80  ? -34.269 17.176   -47.927 1.00 111.91 ? 80  SER I OG  1 
ATOM   15794 N N   . SER I  1 81  ? -31.280 14.496   -45.942 1.00 70.17  ? 81  SER I N   1 
ATOM   15795 C CA  . SER I  1 81  ? -30.479 13.968   -44.845 1.00 68.28  ? 81  SER I CA  1 
ATOM   15796 C C   . SER I  1 81  ? -30.576 12.453   -44.818 1.00 61.68  ? 81  SER I C   1 
ATOM   15797 O O   . SER I  1 81  ? -31.494 11.872   -45.397 1.00 53.21  ? 81  SER I O   1 
ATOM   15798 C CB  . SER I  1 81  ? -30.961 14.535   -43.510 1.00 55.10  ? 81  SER I CB  1 
ATOM   15799 O OG  . SER I  1 81  ? -32.336 14.261   -43.313 1.00 59.95  ? 81  SER I OG  1 
ATOM   15800 N N   . TRP I  1 82  ? -29.625 11.814   -44.148 1.00 49.27  ? 82  TRP I N   1 
ATOM   15801 C CA  . TRP I  1 82  ? -29.655 10.369   -43.976 1.00 50.80  ? 82  TRP I CA  1 
ATOM   15802 C C   . TRP I  1 82  ? -28.824 9.948    -42.772 1.00 50.14  ? 82  TRP I C   1 
ATOM   15803 O O   . TRP I  1 82  ? -27.814 10.574   -42.450 1.00 46.28  ? 82  TRP I O   1 
ATOM   15804 C CB  . TRP I  1 82  ? -29.182 9.651    -45.243 1.00 52.81  ? 82  TRP I CB  1 
ATOM   15805 C CG  . TRP I  1 82  ? -27.841 10.096   -45.737 1.00 48.28  ? 82  TRP I CG  1 
ATOM   15806 C CD1 . TRP I  1 82  ? -26.624 9.633    -45.332 1.00 52.07  ? 82  TRP I CD1 1 
ATOM   15807 C CD2 . TRP I  1 82  ? -27.581 11.085   -46.740 1.00 52.74  ? 82  TRP I CD2 1 
ATOM   15808 N NE1 . TRP I  1 82  ? -25.621 10.276   -46.016 1.00 44.95  ? 82  TRP I NE1 1 
ATOM   15809 C CE2 . TRP I  1 82  ? -26.182 11.172   -46.886 1.00 49.49  ? 82  TRP I CE2 1 
ATOM   15810 C CE3 . TRP I  1 82  ? -28.394 11.907   -47.525 1.00 55.99  ? 82  TRP I CE3 1 
ATOM   15811 C CZ2 . TRP I  1 82  ? -25.579 12.048   -47.787 1.00 52.28  ? 82  TRP I CZ2 1 
ATOM   15812 C CZ3 . TRP I  1 82  ? -27.793 12.777   -48.418 1.00 55.94  ? 82  TRP I CZ3 1 
ATOM   15813 C CH2 . TRP I  1 82  ? -26.400 12.840   -48.541 1.00 43.95  ? 82  TRP I CH2 1 
ATOM   15814 N N   . SER I  1 83  ? -29.265 8.888    -42.105 1.00 57.25  ? 83  SER I N   1 
ATOM   15815 C CA  . SER I  1 83  ? -28.589 8.389    -40.918 1.00 46.70  ? 83  SER I CA  1 
ATOM   15816 C C   . SER I  1 83  ? -27.357 7.576    -41.275 1.00 45.66  ? 83  SER I C   1 
ATOM   15817 O O   . SER I  1 83  ? -26.357 7.602    -40.560 1.00 42.20  ? 83  SER I O   1 
ATOM   15818 C CB  . SER I  1 83  ? -29.540 7.533    -40.095 1.00 44.60  ? 83  SER I CB  1 
ATOM   15819 O OG  . SER I  1 83  ? -30.207 6.576    -40.898 1.00 49.75  ? 83  SER I OG  1 
ATOM   15820 N N   . TYR I  1 84  ? -27.444 6.841    -42.377 1.00 41.95  ? 84  TYR I N   1 
ATOM   15821 C CA  . TYR I  1 84  ? -26.315 6.070    -42.876 1.00 41.34  ? 84  TYR I CA  1 
ATOM   15822 C C   . TYR I  1 84  ? -26.482 5.812    -44.367 1.00 42.80  ? 84  TYR I C   1 
ATOM   15823 O O   . TYR I  1 84  ? -27.520 6.131    -44.946 1.00 58.06  ? 84  TYR I O   1 
ATOM   15824 C CB  . TYR I  1 84  ? -26.169 4.753    -42.109 1.00 41.23  ? 84  TYR I CB  1 
ATOM   15825 C CG  . TYR I  1 84  ? -27.334 3.801    -42.262 1.00 42.27  ? 84  TYR I CG  1 
ATOM   15826 C CD1 . TYR I  1 84  ? -27.278 2.744    -43.161 1.00 43.28  ? 84  TYR I CD1 1 
ATOM   15827 C CD2 . TYR I  1 84  ? -28.486 3.953    -41.502 1.00 34.79  ? 84  TYR I CD2 1 
ATOM   15828 C CE1 . TYR I  1 84  ? -28.336 1.868    -43.301 1.00 38.68  ? 84  TYR I CE1 1 
ATOM   15829 C CE2 . TYR I  1 84  ? -29.551 3.081    -41.636 1.00 29.46  ? 84  TYR I CE2 1 
ATOM   15830 C CZ  . TYR I  1 84  ? -29.470 2.041    -42.538 1.00 36.13  ? 84  TYR I CZ  1 
ATOM   15831 O OH  . TYR I  1 84  ? -30.526 1.169    -42.680 1.00 43.12  ? 84  TYR I OH  1 
ATOM   15832 N N   . ILE I  1 85  ? -25.457 5.240    -44.987 1.00 32.91  ? 85  ILE I N   1 
ATOM   15833 C CA  . ILE I  1 85  ? -25.488 4.992    -46.421 1.00 48.33  ? 85  ILE I CA  1 
ATOM   15834 C C   . ILE I  1 85  ? -25.509 3.502    -46.733 1.00 42.66  ? 85  ILE I C   1 
ATOM   15835 O O   . ILE I  1 85  ? -24.762 2.721    -46.145 1.00 43.82  ? 85  ILE I O   1 
ATOM   15836 C CB  . ILE I  1 85  ? -24.294 5.654    -47.133 1.00 43.92  ? 85  ILE I CB  1 
ATOM   15837 C CG1 . ILE I  1 85  ? -24.347 7.171    -46.944 1.00 37.65  ? 85  ILE I CG1 1 
ATOM   15838 C CG2 . ILE I  1 85  ? -24.290 5.301    -48.613 1.00 41.63  ? 85  ILE I CG2 1 
ATOM   15839 C CD1 . ILE I  1 85  ? -23.181 7.907    -47.559 1.00 35.03  ? 85  ILE I CD1 1 
ATOM   15840 N N   . VAL I  1 86  ? -26.376 3.112    -47.659 1.00 42.29  ? 86  VAL I N   1 
ATOM   15841 C CA  . VAL I  1 86  ? -26.464 1.722    -48.073 1.00 42.28  ? 86  VAL I CA  1 
ATOM   15842 C C   . VAL I  1 86  ? -25.965 1.561    -49.498 1.00 43.89  ? 86  VAL I C   1 
ATOM   15843 O O   . VAL I  1 86  ? -26.438 2.227    -50.417 1.00 50.92  ? 86  VAL I O   1 
ATOM   15844 C CB  . VAL I  1 86  ? -27.903 1.195    -47.986 1.00 37.91  ? 86  VAL I CB  1 
ATOM   15845 C CG1 . VAL I  1 86  ? -27.952 -0.272   -48.384 1.00 37.64  ? 86  VAL I CG1 1 
ATOM   15846 C CG2 . VAL I  1 86  ? -28.447 1.387    -46.586 1.00 34.25  ? 86  VAL I CG2 1 
ATOM   15847 N N   . GLU I  1 87  ? -24.999 0.672    -49.673 1.00 39.68  ? 87  GLU I N   1 
ATOM   15848 C CA  . GLU I  1 87  ? -24.481 0.368    -50.990 1.00 41.73  ? 87  GLU I CA  1 
ATOM   15849 C C   . GLU I  1 87  ? -24.774 -1.093   -51.261 1.00 51.19  ? 87  GLU I C   1 
ATOM   15850 O O   . GLU I  1 87  ? -24.569 -1.938   -50.397 1.00 60.12  ? 87  GLU I O   1 
ATOM   15851 C CB  . GLU I  1 87  ? -22.978 0.610    -51.024 1.00 54.02  ? 87  GLU I CB  1 
ATOM   15852 C CG  . GLU I  1 87  ? -22.513 1.420    -52.205 1.00 60.74  ? 87  GLU I CG  1 
ATOM   15853 C CD  . GLU I  1 87  ? -21.041 1.750    -52.125 1.00 66.87  ? 87  GLU I CD  1 
ATOM   15854 O OE1 . GLU I  1 87  ? -20.671 2.885    -52.487 1.00 65.20  ? 87  GLU I OE1 1 
ATOM   15855 O OE2 . GLU I  1 87  ? -20.255 0.880    -51.689 1.00 65.86  ? 87  GLU I OE2 1 
ATOM   15856 N N   . THR I  1 88  ? -25.274 -1.402   -52.447 1.00 64.16  ? 88  THR I N   1 
ATOM   15857 C CA  . THR I  1 88  ? -25.505 -2.794   -52.779 1.00 72.26  ? 88  THR I CA  1 
ATOM   15858 C C   . THR I  1 88  ? -24.204 -3.427   -53.224 1.00 81.16  ? 88  THR I C   1 
ATOM   15859 O O   . THR I  1 88  ? -23.405 -2.787   -53.908 1.00 92.21  ? 88  THR I O   1 
ATOM   15860 C CB  . THR I  1 88  ? -26.544 -2.957   -53.908 1.00 72.82  ? 88  THR I CB  1 
ATOM   15861 O OG1 . THR I  1 88  ? -26.019 -2.433   -55.135 1.00 85.93  ? 88  THR I OG1 1 
ATOM   15862 C CG2 . THR I  1 88  ? -27.839 -2.240   -53.560 1.00 56.22  ? 88  THR I CG2 1 
ATOM   15863 N N   . PRO I  1 89  ? -23.966 -4.680   -52.811 1.00 91.00  ? 89  PRO I N   1 
ATOM   15864 C CA  . PRO I  1 89  ? -23.051 -5.372   -53.703 1.00 98.78  ? 89  PRO I CA  1 
ATOM   15865 C C   . PRO I  1 89  ? -23.799 -5.134   -54.988 1.00 103.10 ? 89  PRO I C   1 
ATOM   15866 O O   . PRO I  1 89  ? -25.015 -4.902   -54.917 1.00 115.25 ? 89  PRO I O   1 
ATOM   15867 C CB  . PRO I  1 89  ? -23.108 -6.834   -53.242 1.00 95.03  ? 89  PRO I CB  1 
ATOM   15868 C CG  . PRO I  1 89  ? -23.885 -6.867   -52.003 1.00 95.63  ? 89  PRO I CG  1 
ATOM   15869 C CD  . PRO I  1 89  ? -24.602 -5.567   -51.827 1.00 90.00  ? 89  PRO I CD  1 
ATOM   15870 N N   . SER I  1 90  ? -23.106 -5.183   -56.119 1.00 105.60 ? 90  SER I N   1 
ATOM   15871 C CA  . SER I  1 90  ? -23.663 -4.796   -57.420 1.00 118.26 ? 90  SER I CA  1 
ATOM   15872 C C   . SER I  1 90  ? -23.825 -3.281   -57.623 1.00 125.85 ? 90  SER I C   1 
ATOM   15873 O O   . SER I  1 90  ? -24.748 -2.853   -58.319 1.00 126.53 ? 90  SER I O   1 
ATOM   15874 C CB  . SER I  1 90  ? -25.021 -5.488   -57.670 1.00 122.41 ? 90  SER I CB  1 
ATOM   15875 O OG  . SER I  1 90  ? -25.336 -6.467   -56.689 1.00 143.06 ? 90  SER I OG  1 
ATOM   15876 N N   . SER I  1 91  ? -22.943 -2.478   -57.026 1.00 122.78 ? 91  SER I N   1 
ATOM   15877 C CA  . SER I  1 91  ? -22.871 -1.051   -57.349 1.00 104.61 ? 91  SER I CA  1 
ATOM   15878 C C   . SER I  1 91  ? -21.528 -0.709   -57.983 1.00 112.32 ? 91  SER I C   1 
ATOM   15879 O O   . SER I  1 91  ? -20.568 -0.393   -57.285 1.00 112.53 ? 91  SER I O   1 
ATOM   15880 C CB  . SER I  1 91  ? -23.076 -0.171   -56.113 1.00 90.14  ? 91  SER I CB  1 
ATOM   15881 O OG  . SER I  1 91  ? -23.866 -0.801   -55.127 1.00 92.63  ? 91  SER I OG  1 
ATOM   15882 N N   . ASP I  1 92  ? -21.478 -0.735   -59.309 1.00 124.71 ? 92  ASP I N   1 
ATOM   15883 C CA  . ASP I  1 92  ? -20.228 -0.544   -60.033 1.00 136.16 ? 92  ASP I CA  1 
ATOM   15884 C C   . ASP I  1 92  ? -20.251 0.706    -60.902 1.00 126.38 ? 92  ASP I C   1 
ATOM   15885 O O   . ASP I  1 92  ? -19.244 1.074    -61.509 1.00 136.87 ? 92  ASP I O   1 
ATOM   15886 C CB  . ASP I  1 92  ? -19.949 -1.766   -60.896 1.00 160.98 ? 92  ASP I CB  1 
ATOM   15887 C CG  . ASP I  1 92  ? -19.995 -3.056   -60.103 1.00 162.99 ? 92  ASP I CG  1 
ATOM   15888 O OD1 . ASP I  1 92  ? -19.909 -3.004   -58.854 1.00 162.56 ? 92  ASP I OD1 1 
ATOM   15889 O OD2 . ASP I  1 92  ? -20.100 -4.128   -60.735 1.00 157.65 ? 92  ASP I OD2 1 
ATOM   15890 N N   . ASN I  1 93  ? -21.411 1.346    -60.971 1.00 113.50 ? 93  ASN I N   1 
ATOM   15891 C CA  . ASN I  1 93  ? -21.519 2.629    -61.645 1.00 112.00 ? 93  ASN I CA  1 
ATOM   15892 C C   . ASN I  1 93  ? -20.886 3.744    -60.815 1.00 94.20  ? 93  ASN I C   1 
ATOM   15893 O O   . ASN I  1 93  ? -21.592 4.528    -60.182 1.00 78.80  ? 93  ASN I O   1 
ATOM   15894 C CB  . ASN I  1 93  ? -22.984 2.968    -61.932 1.00 105.91 ? 93  ASN I CB  1 
ATOM   15895 C CG  . ASN I  1 93  ? -23.558 2.167    -63.086 1.00 114.77 ? 93  ASN I CG  1 
ATOM   15896 O OD1 . ASN I  1 93  ? -24.632 1.575    -62.967 1.00 115.27 ? 93  ASN I OD1 1 
ATOM   15897 N ND2 . ASN I  1 93  ? -22.852 2.152    -64.212 1.00 114.54 ? 93  ASN I ND2 1 
ATOM   15898 N N   . GLY I  1 94  ? -19.556 3.798    -60.810 1.00 95.85  ? 94  GLY I N   1 
ATOM   15899 C CA  . GLY I  1 94  ? -18.825 4.849    -60.122 1.00 84.04  ? 94  GLY I CA  1 
ATOM   15900 C C   . GLY I  1 94  ? -18.076 5.708    -61.120 1.00 88.43  ? 94  GLY I C   1 
ATOM   15901 O O   . GLY I  1 94  ? -18.684 6.438    -61.902 1.00 90.23  ? 94  GLY I O   1 
ATOM   15902 N N   . THR I  1 95  ? -16.752 5.615    -61.104 1.00 69.48  ? 95  THR I N   1 
ATOM   15903 C CA  . THR I  1 95  ? -15.938 6.319    -62.084 1.00 77.67  ? 95  THR I CA  1 
ATOM   15904 C C   . THR I  1 95  ? -16.039 5.640    -63.446 1.00 70.76  ? 95  THR I C   1 
ATOM   15905 O O   . THR I  1 95  ? -15.487 4.558    -63.648 1.00 72.87  ? 95  THR I O   1 
ATOM   15906 C CB  . THR I  1 95  ? -14.467 6.374    -61.651 1.00 57.51  ? 95  THR I CB  1 
ATOM   15907 O OG1 . THR I  1 95  ? -14.362 7.089    -60.413 1.00 40.19  ? 95  THR I OG1 1 
ATOM   15908 N N   . CYS I  1 96  ? -16.755 6.271    -64.372 1.00 66.15  ? 96  CYS I N   1 
ATOM   15909 C CA  . CYS I  1 96  ? -16.847 5.759    -65.734 1.00 66.96  ? 96  CYS I CA  1 
ATOM   15910 C C   . CYS I  1 96  ? -15.575 6.070    -66.519 1.00 71.78  ? 96  CYS I C   1 
ATOM   15911 O O   . CYS I  1 96  ? -15.149 5.280    -67.361 1.00 80.46  ? 96  CYS I O   1 
ATOM   15912 C CB  . CYS I  1 96  ? -18.091 6.298    -66.447 1.00 65.79  ? 96  CYS I CB  1 
ATOM   15913 S SG  . CYS I  1 96  ? -18.489 8.033    -66.131 1.00 93.19  ? 96  CYS I SG  1 
ATOM   15914 N N   . TYR I  1 97  ? -14.966 7.217    -66.235 1.00 63.47  ? 97  TYR I N   1 
ATOM   15915 C CA  . TYR I  1 97  ? -13.664 7.541    -66.805 1.00 62.54  ? 97  TYR I CA  1 
ATOM   15916 C C   . TYR I  1 97  ? -12.570 7.137    -65.820 1.00 55.43  ? 97  TYR I C   1 
ATOM   15917 O O   . TYR I  1 97  ? -12.562 7.590    -64.676 1.00 55.93  ? 97  TYR I O   1 
ATOM   15918 C CB  . TYR I  1 97  ? -13.558 9.031    -67.137 1.00 64.50  ? 97  TYR I CB  1 
ATOM   15919 C CG  . TYR I  1 97  ? -12.452 9.351    -68.120 1.00 61.01  ? 97  TYR I CG  1 
ATOM   15920 C CD1 . TYR I  1 97  ? -12.739 9.650    -69.446 1.00 72.80  ? 97  TYR I CD1 1 
ATOM   15921 C CD2 . TYR I  1 97  ? -11.120 9.339    -67.727 1.00 56.92  ? 97  TYR I CD2 1 
ATOM   15922 C CE1 . TYR I  1 97  ? -11.731 9.938    -70.349 1.00 77.82  ? 97  TYR I CE1 1 
ATOM   15923 C CE2 . TYR I  1 97  ? -10.106 9.624    -68.623 1.00 62.08  ? 97  TYR I CE2 1 
ATOM   15924 C CZ  . TYR I  1 97  ? -10.417 9.923    -69.932 1.00 64.47  ? 97  TYR I CZ  1 
ATOM   15925 O OH  . TYR I  1 97  ? -9.410  10.207   -70.825 1.00 55.96  ? 97  TYR I OH  1 
ATOM   15926 N N   . PRO I  1 98  ? -11.644 6.276    -66.267 1.00 58.80  ? 98  PRO I N   1 
ATOM   15927 C CA  . PRO I  1 98  ? -10.573 5.733    -65.425 1.00 49.08  ? 98  PRO I CA  1 
ATOM   15928 C C   . PRO I  1 98  ? -9.780  6.829    -64.726 1.00 54.70  ? 98  PRO I C   1 
ATOM   15929 O O   . PRO I  1 98  ? -9.515  7.874    -65.319 1.00 68.65  ? 98  PRO I O   1 
ATOM   15930 C CB  . PRO I  1 98  ? -9.675  5.007    -66.428 1.00 50.45  ? 98  PRO I CB  1 
ATOM   15931 C CG  . PRO I  1 98  ? -10.565 4.682    -67.562 1.00 62.44  ? 98  PRO I CG  1 
ATOM   15932 C CD  . PRO I  1 98  ? -11.542 5.808    -67.658 1.00 70.83  ? 98  PRO I CD  1 
ATOM   15933 N N   . GLY I  1 99  ? -9.403  6.585    -63.476 1.00 62.90  ? 99  GLY I N   1 
ATOM   15934 C CA  . GLY I  1 99  ? -8.644  7.555    -62.713 1.00 59.82  ? 99  GLY I CA  1 
ATOM   15935 C C   . GLY I  1 99  ? -8.648  7.258    -61.228 1.00 58.04  ? 99  GLY I C   1 
ATOM   15936 O O   . GLY I  1 99  ? -9.266  6.294    -60.776 1.00 46.97  ? 99  GLY I O   1 
ATOM   15937 N N   . ASP I  1 100 ? -7.956  8.096    -60.465 1.00 59.51  ? 100 ASP I N   1 
ATOM   15938 C CA  . ASP I  1 100 ? -7.846  7.906    -59.026 1.00 55.00  ? 100 ASP I CA  1 
ATOM   15939 C C   . ASP I  1 100 ? -8.733  8.893    -58.277 1.00 50.53  ? 100 ASP I C   1 
ATOM   15940 O O   . ASP I  1 100 ? -8.742  10.085   -58.580 1.00 57.02  ? 100 ASP I O   1 
ATOM   15941 C CB  . ASP I  1 100 ? -6.391  8.069    -58.582 1.00 61.83  ? 100 ASP I CB  1 
ATOM   15942 C CG  . ASP I  1 100 ? -6.141  7.521    -57.192 1.00 87.50  ? 100 ASP I CG  1 
ATOM   15943 O OD1 . ASP I  1 100 ? -6.971  6.724    -56.707 1.00 102.58 ? 100 ASP I OD1 1 
ATOM   15944 O OD2 . ASP I  1 100 ? -5.110  7.883    -56.586 1.00 84.86  ? 100 ASP I OD2 1 
ATOM   15945 N N   . PHE I  1 101 ? -9.484  8.388    -57.303 1.00 42.52  ? 101 PHE I N   1 
ATOM   15946 C CA  . PHE I  1 101 ? -10.305 9.242    -56.454 1.00 39.51  ? 101 PHE I CA  1 
ATOM   15947 C C   . PHE I  1 101 ? -9.554  9.512    -55.155 1.00 42.68  ? 101 PHE I C   1 
ATOM   15948 O O   . PHE I  1 101 ? -9.567  8.690    -54.239 1.00 48.52  ? 101 PHE I O   1 
ATOM   15949 C CB  . PHE I  1 101 ? -11.651 8.579    -56.158 1.00 37.26  ? 101 PHE I CB  1 
ATOM   15950 C CG  . PHE I  1 101 ? -12.750 9.553    -55.832 1.00 43.96  ? 101 PHE I CG  1 
ATOM   15951 C CD1 . PHE I  1 101 ? -13.904 9.597    -56.597 1.00 47.78  ? 101 PHE I CD1 1 
ATOM   15952 C CD2 . PHE I  1 101 ? -12.623 10.433   -54.770 1.00 45.17  ? 101 PHE I CD2 1 
ATOM   15953 C CE1 . PHE I  1 101 ? -14.916 10.492   -56.303 1.00 37.21  ? 101 PHE I CE1 1 
ATOM   15954 C CE2 . PHE I  1 101 ? -13.631 11.332   -54.472 1.00 35.81  ? 101 PHE I CE2 1 
ATOM   15955 C CZ  . PHE I  1 101 ? -14.778 11.361   -55.240 1.00 31.58  ? 101 PHE I CZ  1 
ATOM   15956 N N   . ILE I  1 102 ? -8.896  10.664   -55.086 1.00 36.62  ? 102 ILE I N   1 
ATOM   15957 C CA  . ILE I  1 102 ? -8.046  11.000   -53.949 1.00 35.81  ? 102 ILE I CA  1 
ATOM   15958 C C   . ILE I  1 102 ? -8.833  11.077   -52.644 1.00 39.51  ? 102 ILE I C   1 
ATOM   15959 O O   . ILE I  1 102 ? -9.874  11.730   -52.575 1.00 49.79  ? 102 ILE I O   1 
ATOM   15960 C CB  . ILE I  1 102 ? -7.310  12.334   -54.178 1.00 48.22  ? 102 ILE I CB  1 
ATOM   15961 C CG1 . ILE I  1 102 ? -6.665  12.351   -55.565 1.00 49.77  ? 102 ILE I CG1 1 
ATOM   15962 C CG2 . ILE I  1 102 ? -6.274  12.570   -53.087 1.00 36.31  ? 102 ILE I CG2 1 
ATOM   15963 C CD1 . ILE I  1 102 ? -5.689  11.221   -55.799 1.00 52.90  ? 102 ILE I CD1 1 
ATOM   15964 N N   . ASP I  1 103 ? -8.325  10.407   -51.614 1.00 46.14  ? 103 ASP I N   1 
ATOM   15965 C CA  . ASP I  1 103 ? -8.970  10.396   -50.305 1.00 44.86  ? 103 ASP I CA  1 
ATOM   15966 C C   . ASP I  1 103 ? -10.434 9.988    -50.420 1.00 40.77  ? 103 ASP I C   1 
ATOM   15967 O O   . ASP I  1 103 ? -11.310 10.592   -49.801 1.00 42.81  ? 103 ASP I O   1 
ATOM   15968 C CB  . ASP I  1 103 ? -8.854  11.767   -49.638 1.00 42.82  ? 103 ASP I CB  1 
ATOM   15969 C CG  . ASP I  1 103 ? -7.416  12.161   -49.362 1.00 52.03  ? 103 ASP I CG  1 
ATOM   15970 O OD1 . ASP I  1 103 ? -6.582  11.259   -49.138 1.00 63.51  ? 103 ASP I OD1 1 
ATOM   15971 O OD2 . ASP I  1 103 ? -7.122  13.375   -49.365 1.00 60.65  ? 103 ASP I OD2 1 
ATOM   15972 N N   . TYR I  1 104 ? -10.689 8.957    -51.218 1.00 45.29  ? 104 TYR I N   1 
ATOM   15973 C CA  . TYR I  1 104 ? -12.047 8.486    -51.464 1.00 39.20  ? 104 TYR I CA  1 
ATOM   15974 C C   . TYR I  1 104 ? -12.704 7.936    -50.199 1.00 39.82  ? 104 TYR I C   1 
ATOM   15975 O O   . TYR I  1 104 ? -13.836 8.296    -49.876 1.00 36.89  ? 104 TYR I O   1 
ATOM   15976 C CB  . TYR I  1 104 ? -12.047 7.433    -52.576 1.00 38.71  ? 104 TYR I CB  1 
ATOM   15977 C CG  . TYR I  1 104 ? -13.409 6.856    -52.887 1.00 42.49  ? 104 TYR I CG  1 
ATOM   15978 C CD1 . TYR I  1 104 ? -14.492 7.684    -53.152 1.00 40.23  ? 104 TYR I CD1 1 
ATOM   15979 C CD2 . TYR I  1 104 ? -13.608 5.482    -52.932 1.00 31.01  ? 104 TYR I CD2 1 
ATOM   15980 C CE1 . TYR I  1 104 ? -15.738 7.159    -53.440 1.00 40.63  ? 104 TYR I CE1 1 
ATOM   15981 C CE2 . TYR I  1 104 ? -14.848 4.949    -53.222 1.00 41.24  ? 104 TYR I CE2 1 
ATOM   15982 C CZ  . TYR I  1 104 ? -15.909 5.791    -53.474 1.00 39.54  ? 104 TYR I CZ  1 
ATOM   15983 O OH  . TYR I  1 104 ? -17.145 5.262    -53.763 1.00 44.28  ? 104 TYR I OH  1 
ATOM   15984 N N   . GLU I  1 105 ? -11.988 7.069    -49.489 1.00 46.73  ? 105 GLU I N   1 
ATOM   15985 C CA  . GLU I  1 105 ? -12.508 6.442    -48.277 1.00 40.86  ? 105 GLU I CA  1 
ATOM   15986 C C   . GLU I  1 105 ? -12.818 7.494    -47.222 1.00 37.55  ? 105 GLU I C   1 
ATOM   15987 O O   . GLU I  1 105 ? -13.792 7.383    -46.479 1.00 42.58  ? 105 GLU I O   1 
ATOM   15988 C CB  . GLU I  1 105 ? -11.507 5.424    -47.727 1.00 42.51  ? 105 GLU I CB  1 
ATOM   15989 C CG  . GLU I  1 105 ? -11.158 4.307    -48.697 1.00 42.57  ? 105 GLU I CG  1 
ATOM   15990 C CD  . GLU I  1 105 ? -10.229 4.761    -49.809 1.00 62.01  ? 105 GLU I CD  1 
ATOM   15991 O OE1 . GLU I  1 105 ? -9.416  5.678    -49.568 1.00 61.16  ? 105 GLU I OE1 1 
ATOM   15992 O OE2 . GLU I  1 105 ? -10.307 4.196    -50.920 1.00 57.97  ? 105 GLU I OE2 1 
ATOM   15993 N N   . GLU I  1 106 ? -11.981 8.520    -47.167 1.00 39.94  ? 106 GLU I N   1 
ATOM   15994 C CA  . GLU I  1 106 ? -12.189 9.621    -46.242 1.00 35.32  ? 106 GLU I CA  1 
ATOM   15995 C C   . GLU I  1 106 ? -13.474 10.391   -46.533 1.00 42.49  ? 106 GLU I C   1 
ATOM   15996 O O   . GLU I  1 106 ? -14.176 10.800   -45.610 1.00 43.86  ? 106 GLU I O   1 
ATOM   15997 C CB  . GLU I  1 106 ? -10.980 10.547   -46.265 1.00 36.63  ? 106 GLU I CB  1 
ATOM   15998 C CG  . GLU I  1 106 ? -9.969  10.186   -45.214 1.00 64.92  ? 106 GLU I CG  1 
ATOM   15999 C CD  . GLU I  1 106 ? -10.498 10.484   -43.835 1.00 57.07  ? 106 GLU I CD  1 
ATOM   16000 O OE1 . GLU I  1 106 ? -11.108 11.562   -43.664 1.00 59.73  ? 106 GLU I OE1 1 
ATOM   16001 O OE2 . GLU I  1 106 ? -10.299 9.659    -42.919 1.00 49.67  ? 106 GLU I OE2 1 
ATOM   16002 N N   . LEU I  1 107 ? -13.784 10.573   -47.815 1.00 47.86  ? 107 LEU I N   1 
ATOM   16003 C CA  . LEU I  1 107 ? -15.003 11.269   -48.224 1.00 42.56  ? 107 LEU I CA  1 
ATOM   16004 C C   . LEU I  1 107 ? -16.235 10.461   -47.839 1.00 45.42  ? 107 LEU I C   1 
ATOM   16005 O O   . LEU I  1 107 ? -17.150 10.970   -47.188 1.00 45.75  ? 107 LEU I O   1 
ATOM   16006 C CB  . LEU I  1 107 ? -14.994 11.513   -49.734 1.00 43.99  ? 107 LEU I CB  1 
ATOM   16007 C CG  . LEU I  1 107 ? -16.185 12.269   -50.325 1.00 48.09  ? 107 LEU I CG  1 
ATOM   16008 C CD1 . LEU I  1 107 ? -16.188 13.702   -49.856 1.00 43.85  ? 107 LEU I CD1 1 
ATOM   16009 C CD2 . LEU I  1 107 ? -16.147 12.225   -51.832 1.00 42.41  ? 107 LEU I CD2 1 
ATOM   16010 N N   . ARG I  1 108 ? -16.246 9.200    -48.258 1.00 36.68  ? 108 ARG I N   1 
ATOM   16011 C CA  . ARG I  1 108 ? -17.302 8.264    -47.899 1.00 43.36  ? 108 ARG I CA  1 
ATOM   16012 C C   . ARG I  1 108 ? -17.630 8.346    -46.410 1.00 43.35  ? 108 ARG I C   1 
ATOM   16013 O O   . ARG I  1 108 ? -18.797 8.414    -46.021 1.00 38.63  ? 108 ARG I O   1 
ATOM   16014 C CB  . ARG I  1 108 ? -16.875 6.839    -48.259 1.00 42.34  ? 108 ARG I CB  1 
ATOM   16015 C CG  . ARG I  1 108 ? -16.648 6.605    -49.751 1.00 41.30  ? 108 ARG I CG  1 
ATOM   16016 C CD  . ARG I  1 108 ? -16.056 5.224    -50.022 1.00 41.52  ? 108 ARG I CD  1 
ATOM   16017 N NE  . ARG I  1 108 ? -16.913 4.145    -49.538 1.00 36.55  ? 108 ARG I NE  1 
ATOM   16018 C CZ  . ARG I  1 108 ? -17.796 3.493    -50.289 1.00 50.19  ? 108 ARG I CZ  1 
ATOM   16019 N NH1 . ARG I  1 108 ? -17.943 3.806    -51.569 1.00 48.63  ? 108 ARG I NH1 1 
ATOM   16020 N NH2 . ARG I  1 108 ? -18.532 2.525    -49.760 1.00 36.58  ? 108 ARG I NH2 1 
ATOM   16021 N N   . GLU I  1 109 ? -16.589 8.336    -45.584 1.00 41.06  ? 109 GLU I N   1 
ATOM   16022 C CA  . GLU I  1 109 ? -16.748 8.414    -44.139 1.00 44.97  ? 109 GLU I CA  1 
ATOM   16023 C C   . GLU I  1 109 ? -17.420 9.717    -43.718 1.00 38.14  ? 109 GLU I C   1 
ATOM   16024 O O   . GLU I  1 109 ? -18.240 9.728    -42.803 1.00 37.91  ? 109 GLU I O   1 
ATOM   16025 C CB  . GLU I  1 109 ? -15.392 8.275    -43.444 1.00 46.05  ? 109 GLU I CB  1 
ATOM   16026 C CG  . GLU I  1 109 ? -15.463 8.314    -41.925 1.00 55.33  ? 109 GLU I CG  1 
ATOM   16027 C CD  . GLU I  1 109 ? -16.123 7.081    -41.333 1.00 66.55  ? 109 GLU I CD  1 
ATOM   16028 O OE1 . GLU I  1 109 ? -16.686 6.272    -42.101 1.00 75.47  ? 109 GLU I OE1 1 
ATOM   16029 O OE2 . GLU I  1 109 ? -16.076 6.919    -40.096 1.00 74.39  ? 109 GLU I OE2 1 
ATOM   16030 N N   . GLN I  1 110 ? -17.073 10.814   -44.386 1.00 36.09  ? 110 GLN I N   1 
ATOM   16031 C CA  . GLN I  1 110 ? -17.643 12.121   -44.058 1.00 51.13  ? 110 GLN I CA  1 
ATOM   16032 C C   . GLN I  1 110 ? -19.095 12.231   -44.528 1.00 55.89  ? 110 GLN I C   1 
ATOM   16033 O O   . GLN I  1 110 ? -19.912 12.913   -43.910 1.00 54.38  ? 110 GLN I O   1 
ATOM   16034 C CB  . GLN I  1 110 ? -16.805 13.247   -44.674 1.00 56.84  ? 110 GLN I CB  1 
ATOM   16035 C CG  . GLN I  1 110 ? -15.300 13.048   -44.555 1.00 54.57  ? 110 GLN I CG  1 
ATOM   16036 C CD  . GLN I  1 110 ? -14.612 14.128   -43.743 1.00 60.01  ? 110 GLN I CD  1 
ATOM   16037 O OE1 . GLN I  1 110 ? -15.260 15.020   -43.197 1.00 68.06  ? 110 GLN I OE1 1 
ATOM   16038 N NE2 . GLN I  1 110 ? -13.288 14.051   -43.658 1.00 46.65  ? 110 GLN I NE2 1 
ATOM   16039 N N   . LEU I  1 111 ? -19.406 11.557   -45.630 1.00 58.35  ? 111 LEU I N   1 
ATOM   16040 C CA  . LEU I  1 111 ? -20.747 11.572   -46.201 1.00 43.13  ? 111 LEU I CA  1 
ATOM   16041 C C   . LEU I  1 111 ? -21.669 10.585   -45.488 1.00 47.49  ? 111 LEU I C   1 
ATOM   16042 O O   . LEU I  1 111 ? -22.892 10.710   -45.557 1.00 49.37  ? 111 LEU I O   1 
ATOM   16043 C CB  . LEU I  1 111 ? -20.679 11.218   -47.689 1.00 42.13  ? 111 LEU I CB  1 
ATOM   16044 C CG  . LEU I  1 111 ? -20.646 12.334   -48.738 1.00 48.33  ? 111 LEU I CG  1 
ATOM   16045 C CD1 . LEU I  1 111 ? -20.110 13.623   -48.157 1.00 61.15  ? 111 LEU I CD1 1 
ATOM   16046 C CD2 . LEU I  1 111 ? -19.845 11.920   -49.961 1.00 45.05  ? 111 LEU I CD2 1 
ATOM   16047 N N   . SER I  1 112 ? -21.074 9.610    -44.803 1.00 47.61  ? 112 SER I N   1 
ATOM   16048 C CA  . SER I  1 112 ? -21.818 8.507    -44.195 1.00 44.41  ? 112 SER I CA  1 
ATOM   16049 C C   . SER I  1 112 ? -23.101 8.955    -43.502 1.00 44.89  ? 112 SER I C   1 
ATOM   16050 O O   . SER I  1 112 ? -24.122 8.272    -43.573 1.00 52.40  ? 112 SER I O   1 
ATOM   16051 C CB  . SER I  1 112 ? -20.932 7.731    -43.217 1.00 50.47  ? 112 SER I CB  1 
ATOM   16052 O OG  . SER I  1 112 ? -20.649 8.494    -42.058 1.00 47.62  ? 112 SER I OG  1 
ATOM   16053 N N   . SER I  1 113 ? -23.047 10.100   -42.833 1.00 44.82  ? 113 SER I N   1 
ATOM   16054 C CA  . SER I  1 113 ? -24.236 10.660   -42.202 1.00 46.73  ? 113 SER I CA  1 
ATOM   16055 C C   . SER I  1 113 ? -24.291 12.171   -42.387 1.00 57.11  ? 113 SER I C   1 
ATOM   16056 O O   . SER I  1 113 ? -23.344 12.885   -42.051 1.00 52.65  ? 113 SER I O   1 
ATOM   16057 C CB  . SER I  1 113 ? -24.284 10.298   -40.719 1.00 61.23  ? 113 SER I CB  1 
ATOM   16058 O OG  . SER I  1 113 ? -25.537 10.631   -40.149 1.00 61.76  ? 113 SER I OG  1 
ATOM   16059 N N   . VAL I  1 114 ? -25.411 12.647   -42.921 1.00 63.68  ? 114 VAL I N   1 
ATOM   16060 C CA  . VAL I  1 114 ? -25.569 14.054   -43.261 1.00 62.49  ? 114 VAL I CA  1 
ATOM   16061 C C   . VAL I  1 114 ? -26.844 14.640   -42.662 1.00 64.97  ? 114 VAL I C   1 
ATOM   16062 O O   . VAL I  1 114 ? -27.912 14.032   -42.730 1.00 64.19  ? 114 VAL I O   1 
ATOM   16063 C CB  . VAL I  1 114 ? -25.580 14.243   -44.788 1.00 57.61  ? 114 VAL I CB  1 
ATOM   16064 C CG1 . VAL I  1 114 ? -26.821 15.008   -45.230 1.00 62.89  ? 114 VAL I CG1 1 
ATOM   16065 C CG2 . VAL I  1 114 ? -24.295 14.927   -45.249 1.00 55.98  ? 114 VAL I CG2 1 
ATOM   16066 N N   . SER I  1 115 ? -26.724 15.823   -42.068 1.00 64.50  ? 115 SER I N   1 
ATOM   16067 C CA  . SER I  1 115 ? -27.859 16.470   -41.421 1.00 82.94  ? 115 SER I CA  1 
ATOM   16068 C C   . SER I  1 115 ? -28.712 17.222   -42.439 1.00 75.74  ? 115 SER I C   1 
ATOM   16069 O O   . SER I  1 115 ? -29.926 17.033   -42.507 1.00 86.45  ? 115 SER I O   1 
ATOM   16070 C CB  . SER I  1 115 ? -27.379 17.417   -40.322 1.00 85.41  ? 115 SER I CB  1 
ATOM   16071 O OG  . SER I  1 115 ? -28.438 17.740   -39.440 1.00 85.97  ? 115 SER I OG  1 
ATOM   16072 N N   . SER I  1 116 ? -28.074 18.086   -43.220 1.00 78.48  ? 116 SER I N   1 
ATOM   16073 C CA  . SER I  1 116 ? -28.738 18.724   -44.349 1.00 82.13  ? 116 SER I CA  1 
ATOM   16074 C C   . SER I  1 116 ? -27.834 18.626   -45.569 1.00 79.03  ? 116 SER I C   1 
ATOM   16075 O O   . SER I  1 116 ? -26.618 18.787   -45.465 1.00 79.02  ? 116 SER I O   1 
ATOM   16076 C CB  . SER I  1 116 ? -29.086 20.183   -44.046 1.00 91.81  ? 116 SER I CB  1 
ATOM   16077 O OG  . SER I  1 116 ? -27.927 20.995   -44.027 1.00 101.48 ? 116 SER I OG  1 
ATOM   16078 N N   . PHE I  1 117 ? -28.432 18.356   -46.723 1.00 74.76  ? 117 PHE I N   1 
ATOM   16079 C CA  . PHE I  1 117 ? -27.668 18.103   -47.934 1.00 68.90  ? 117 PHE I CA  1 
ATOM   16080 C C   . PHE I  1 117 ? -28.409 18.654   -49.142 1.00 64.98  ? 117 PHE I C   1 
ATOM   16081 O O   . PHE I  1 117 ? -29.408 18.083   -49.580 1.00 73.36  ? 117 PHE I O   1 
ATOM   16082 C CB  . PHE I  1 117 ? -27.451 16.597   -48.095 1.00 62.81  ? 117 PHE I CB  1 
ATOM   16083 C CG  . PHE I  1 117 ? -26.421 16.231   -49.124 1.00 60.62  ? 117 PHE I CG  1 
ATOM   16084 C CD1 . PHE I  1 117 ? -26.782 16.035   -50.446 1.00 50.71  ? 117 PHE I CD1 1 
ATOM   16085 C CD2 . PHE I  1 117 ? -25.093 16.065   -48.766 1.00 58.38  ? 117 PHE I CD2 1 
ATOM   16086 C CE1 . PHE I  1 117 ? -25.837 15.691   -51.393 1.00 44.38  ? 117 PHE I CE1 1 
ATOM   16087 C CE2 . PHE I  1 117 ? -24.144 15.722   -49.708 1.00 60.14  ? 117 PHE I CE2 1 
ATOM   16088 C CZ  . PHE I  1 117 ? -24.516 15.534   -51.023 1.00 54.25  ? 117 PHE I CZ  1 
ATOM   16089 N N   . GLU I  1 118 ? -27.925 19.768   -49.679 1.00 71.64  ? 118 GLU I N   1 
ATOM   16090 C CA  . GLU I  1 118 ? -28.515 20.328   -50.888 1.00 71.52  ? 118 GLU I CA  1 
ATOM   16091 C C   . GLU I  1 118 ? -27.484 20.405   -52.007 1.00 60.78  ? 118 GLU I C   1 
ATOM   16092 O O   . GLU I  1 118 ? -26.289 20.583   -51.758 1.00 69.90  ? 118 GLU I O   1 
ATOM   16093 C CB  . GLU I  1 118 ? -29.123 21.708   -50.627 1.00 85.32  ? 118 GLU I CB  1 
ATOM   16094 C CG  . GLU I  1 118 ? -28.125 22.850   -50.716 1.00 98.75  ? 118 GLU I CG  1 
ATOM   16095 C CD  . GLU I  1 118 ? -28.577 23.957   -51.649 1.00 121.31 ? 118 GLU I CD  1 
ATOM   16096 O OE1 . GLU I  1 118 ? -29.389 23.683   -52.557 1.00 122.78 ? 118 GLU I OE1 1 
ATOM   16097 O OE2 . GLU I  1 118 ? -28.109 25.103   -51.479 1.00 117.24 ? 118 GLU I OE2 1 
ATOM   16098 N N   . ARG I  1 119 ? -27.958 20.256   -53.238 1.00 63.15  ? 119 ARG I N   1 
ATOM   16099 C CA  . ARG I  1 119 ? -27.095 20.275   -54.409 1.00 65.09  ? 119 ARG I CA  1 
ATOM   16100 C C   . ARG I  1 119 ? -27.420 21.491   -55.270 1.00 64.94  ? 119 ARG I C   1 
ATOM   16101 O O   . ARG I  1 119 ? -28.500 21.577   -55.858 1.00 75.88  ? 119 ARG I O   1 
ATOM   16102 C CB  . ARG I  1 119 ? -27.276 18.979   -55.202 1.00 64.38  ? 119 ARG I CB  1 
ATOM   16103 C CG  . ARG I  1 119 ? -26.589 18.947   -56.554 1.00 61.91  ? 119 ARG I CG  1 
ATOM   16104 C CD  . ARG I  1 119 ? -27.613 18.910   -57.675 1.00 75.76  ? 119 ARG I CD  1 
ATOM   16105 N NE  . ARG I  1 119 ? -27.347 17.824   -58.614 1.00 80.79  ? 119 ARG I NE  1 
ATOM   16106 C CZ  . ARG I  1 119 ? -28.051 17.592   -59.718 1.00 98.51  ? 119 ARG I CZ  1 
ATOM   16107 N NH1 . ARG I  1 119 ? -29.075 18.369   -60.042 1.00 102.46 ? 119 ARG I NH1 1 
ATOM   16108 N NH2 . ARG I  1 119 ? -27.726 16.577   -60.504 1.00 91.39  ? 119 ARG I NH2 1 
ATOM   16109 N N   . PHE I  1 120 ? -26.484 22.434   -55.329 1.00 67.80  ? 120 PHE I N   1 
ATOM   16110 C CA  . PHE I  1 120 ? -26.694 23.675   -56.061 1.00 69.08  ? 120 PHE I CA  1 
ATOM   16111 C C   . PHE I  1 120 ? -25.640 23.861   -57.142 1.00 62.40  ? 120 PHE I C   1 
ATOM   16112 O O   . PHE I  1 120 ? -24.529 23.342   -57.036 1.00 60.65  ? 120 PHE I O   1 
ATOM   16113 C CB  . PHE I  1 120 ? -26.675 24.869   -55.104 1.00 68.26  ? 120 PHE I CB  1 
ATOM   16114 C CG  . PHE I  1 120 ? -25.326 25.141   -54.494 1.00 66.39  ? 120 PHE I CG  1 
ATOM   16115 C CD1 . PHE I  1 120 ? -24.487 26.100   -55.037 1.00 74.93  ? 120 PHE I CD1 1 
ATOM   16116 C CD2 . PHE I  1 120 ? -24.902 24.445   -53.374 1.00 75.22  ? 120 PHE I CD2 1 
ATOM   16117 C CE1 . PHE I  1 120 ? -23.249 26.356   -54.479 1.00 72.03  ? 120 PHE I CE1 1 
ATOM   16118 C CE2 . PHE I  1 120 ? -23.663 24.697   -52.810 1.00 69.05  ? 120 PHE I CE2 1 
ATOM   16119 C CZ  . PHE I  1 120 ? -22.836 25.655   -53.364 1.00 62.39  ? 120 PHE I CZ  1 
ATOM   16120 N N   . GLU I  1 121 ? -25.994 24.607   -58.182 1.00 69.69  ? 121 GLU I N   1 
ATOM   16121 C CA  . GLU I  1 121 ? -25.063 24.893   -59.262 1.00 65.32  ? 121 GLU I CA  1 
ATOM   16122 C C   . GLU I  1 121 ? -24.088 25.984   -58.832 1.00 69.81  ? 121 GLU I C   1 
ATOM   16123 O O   . GLU I  1 121 ? -24.446 27.160   -58.764 1.00 86.42  ? 121 GLU I O   1 
ATOM   16124 C CB  . GLU I  1 121 ? -25.820 25.313   -60.523 1.00 69.12  ? 121 GLU I CB  1 
ATOM   16125 C CG  . GLU I  1 121 ? -25.002 25.223   -61.799 1.00 85.19  ? 121 GLU I CG  1 
ATOM   16126 C CD  . GLU I  1 121 ? -25.830 25.498   -63.039 1.00 100.49 ? 121 GLU I CD  1 
ATOM   16127 O OE1 . GLU I  1 121 ? -26.914 26.104   -62.908 1.00 112.74 ? 121 GLU I OE1 1 
ATOM   16128 O OE2 . GLU I  1 121 ? -25.397 25.110   -64.145 1.00 93.72  ? 121 GLU I OE2 1 
ATOM   16129 N N   . ILE I  1 122 ? -22.858 25.584   -58.530 1.00 72.43  ? 122 ILE I N   1 
ATOM   16130 C CA  . ILE I  1 122 ? -21.831 26.520   -58.089 1.00 67.10  ? 122 ILE I CA  1 
ATOM   16131 C C   . ILE I  1 122 ? -21.303 27.348   -59.257 1.00 79.78  ? 122 ILE I C   1 
ATOM   16132 O O   . ILE I  1 122 ? -21.084 28.552   -59.127 1.00 86.06  ? 122 ILE I O   1 
ATOM   16133 C CB  . ILE I  1 122 ? -20.666 25.792   -57.387 1.00 72.55  ? 122 ILE I CB  1 
ATOM   16134 C CG1 . ILE I  1 122 ? -19.555 26.779   -57.024 1.00 63.99  ? 122 ILE I CG1 1 
ATOM   16135 C CG2 . ILE I  1 122 ? -20.126 24.671   -58.263 1.00 67.89  ? 122 ILE I CG2 1 
ATOM   16136 C CD1 . ILE I  1 122 ? -18.392 26.141   -56.300 1.00 54.77  ? 122 ILE I CD1 1 
ATOM   16137 N N   . PHE I  1 123 ? -21.102 26.696   -60.398 1.00 78.53  ? 123 PHE I N   1 
ATOM   16138 C CA  . PHE I  1 123 ? -20.697 27.390   -61.614 1.00 67.56  ? 123 PHE I CA  1 
ATOM   16139 C C   . PHE I  1 123 ? -21.642 27.052   -62.762 1.00 81.37  ? 123 PHE I C   1 
ATOM   16140 O O   . PHE I  1 123 ? -21.471 26.030   -63.426 1.00 76.28  ? 123 PHE I O   1 
ATOM   16141 C CB  . PHE I  1 123 ? -19.259 27.033   -62.001 1.00 68.32  ? 123 PHE I CB  1 
ATOM   16142 C CG  . PHE I  1 123 ? -18.232 27.459   -60.990 1.00 75.01  ? 123 PHE I CG  1 
ATOM   16143 C CD1 . PHE I  1 123 ? -17.395 26.527   -60.400 1.00 71.31  ? 123 PHE I CD1 1 
ATOM   16144 C CD2 . PHE I  1 123 ? -18.108 28.789   -60.625 1.00 79.67  ? 123 PHE I CD2 1 
ATOM   16145 C CE1 . PHE I  1 123 ? -16.450 26.914   -59.469 1.00 72.52  ? 123 PHE I CE1 1 
ATOM   16146 C CE2 . PHE I  1 123 ? -17.166 29.182   -59.694 1.00 75.60  ? 123 PHE I CE2 1 
ATOM   16147 C CZ  . PHE I  1 123 ? -16.336 28.243   -59.115 1.00 75.24  ? 123 PHE I CZ  1 
ATOM   16148 N N   . PRO I  1 124 ? -22.646 27.910   -62.996 1.00 101.03 ? 124 PRO I N   1 
ATOM   16149 C CA  . PRO I  1 124 ? -23.586 27.720   -64.108 1.00 98.22  ? 124 PRO I CA  1 
ATOM   16150 C C   . PRO I  1 124 ? -22.850 27.568   -65.437 1.00 97.35  ? 124 PRO I C   1 
ATOM   16151 O O   . PRO I  1 124 ? -21.943 28.350   -65.709 1.00 92.07  ? 124 PRO I O   1 
ATOM   16152 C CB  . PRO I  1 124 ? -24.393 29.020   -64.106 1.00 103.28 ? 124 PRO I CB  1 
ATOM   16153 C CG  . PRO I  1 124 ? -24.308 29.516   -62.705 1.00 105.71 ? 124 PRO I CG  1 
ATOM   16154 C CD  . PRO I  1 124 ? -22.947 29.121   -62.213 1.00 95.83  ? 124 PRO I CD  1 
ATOM   16155 N N   . LYS I  1 125 ? -23.243 26.589   -66.248 1.00 90.40  ? 125 LYS I N   1 
ATOM   16156 C CA  . LYS I  1 125 ? -22.524 26.263   -67.476 1.00 102.35 ? 125 LYS I CA  1 
ATOM   16157 C C   . LYS I  1 125 ? -22.488 27.405   -68.484 1.00 127.81 ? 125 LYS I C   1 
ATOM   16158 O O   . LYS I  1 125 ? -21.531 27.533   -69.248 1.00 124.77 ? 125 LYS I O   1 
ATOM   16159 C CB  . LYS I  1 125 ? -23.130 25.024   -68.140 1.00 95.55  ? 125 LYS I CB  1 
ATOM   16160 C CG  . LYS I  1 125 ? -22.382 24.566   -69.379 1.00 101.51 ? 125 LYS I CG  1 
ATOM   16161 C CD  . LYS I  1 125 ? -22.750 23.148   -69.782 1.00 93.97  ? 125 LYS I CD  1 
ATOM   16162 C CE  . LYS I  1 125 ? -24.187 23.047   -70.267 1.00 102.48 ? 125 LYS I CE  1 
ATOM   16163 N NZ  . LYS I  1 125 ? -24.513 21.678   -70.767 1.00 98.68  ? 125 LYS I NZ  1 
ATOM   16164 N N   . THR I  1 126 ? -23.520 28.240   -68.487 1.00 178.94 ? 126 THR I N   1 
ATOM   16165 C CA  . THR I  1 126 ? -23.707 29.192   -69.581 1.00 168.99 ? 126 THR I CA  1 
ATOM   16166 C C   . THR I  1 126 ? -23.306 30.645   -69.303 1.00 170.02 ? 126 THR I C   1 
ATOM   16167 O O   . THR I  1 126 ? -23.619 31.529   -70.101 1.00 193.18 ? 126 THR I O   1 
ATOM   16168 C CB  . THR I  1 126 ? -25.193 29.216   -70.017 1.00 133.59 ? 126 THR I CB  1 
ATOM   16169 O OG1 . THR I  1 126 ? -26.033 29.045   -68.863 1.00 132.66 ? 126 THR I OG1 1 
ATOM   16170 N N   . SER I  1 127 ? -22.622 30.896   -68.193 1.00 111.19 ? 127 SER I N   1 
ATOM   16171 C CA  . SER I  1 127 ? -22.195 32.245   -67.870 1.00 114.35 ? 127 SER I CA  1 
ATOM   16172 C C   . SER I  1 127 ? -20.780 32.270   -67.270 1.00 109.72 ? 127 SER I C   1 
ATOM   16173 O O   . SER I  1 127 ? -20.133 33.316   -67.214 1.00 112.80 ? 127 SER I O   1 
ATOM   16174 C CB  . SER I  1 127 ? -23.211 32.904   -66.939 1.00 120.62 ? 127 SER I CB  1 
ATOM   16175 O OG  . SER I  1 127 ? -23.395 32.125   -65.768 1.00 99.91  ? 127 SER I OG  1 
ATOM   16176 N N   . SER I  1 128 ? -20.283 31.101   -66.879 1.00 109.39 ? 128 SER I N   1 
ATOM   16177 C CA  . SER I  1 128 ? -19.014 30.997   -66.166 1.00 101.66 ? 128 SER I CA  1 
ATOM   16178 C C   . SER I  1 128 ? -17.831 30.777   -67.105 1.00 98.07  ? 128 SER I C   1 
ATOM   16179 O O   . SER I  1 128 ? -16.698 31.153   -66.798 1.00 92.10  ? 128 SER I O   1 
ATOM   16180 C CB  . SER I  1 128 ? -19.090 29.864   -65.138 1.00 90.82  ? 128 SER I CB  1 
ATOM   16181 O OG  . SER I  1 128 ? -20.246 29.999   -64.327 1.00 72.03  ? 128 SER I OG  1 
ATOM   16182 N N   . TRP I  1 129 ? -18.103 30.179   -68.258 1.00 98.64  ? 129 TRP I N   1 
ATOM   16183 C CA  . TRP I  1 129 ? -17.046 29.802   -69.187 1.00 100.21 ? 129 TRP I CA  1 
ATOM   16184 C C   . TRP I  1 129 ? -17.278 30.369   -70.586 1.00 104.90 ? 129 TRP I C   1 
ATOM   16185 O O   . TRP I  1 129 ? -17.649 29.638   -71.502 1.00 96.21  ? 129 TRP I O   1 
ATOM   16186 C CB  . TRP I  1 129 ? -16.925 28.277   -69.234 1.00 105.90 ? 129 TRP I CB  1 
ATOM   16187 C CG  . TRP I  1 129 ? -17.100 27.655   -67.884 1.00 97.46  ? 129 TRP I CG  1 
ATOM   16188 C CD1 . TRP I  1 129 ? -18.110 26.829   -67.484 1.00 88.29  ? 129 TRP I CD1 1 
ATOM   16189 C CD2 . TRP I  1 129 ? -16.256 27.839   -66.743 1.00 88.89  ? 129 TRP I CD2 1 
ATOM   16190 N NE1 . TRP I  1 129 ? -17.937 26.474   -66.167 1.00 77.95  ? 129 TRP I NE1 1 
ATOM   16191 C CE2 . TRP I  1 129 ? -16.807 27.083   -65.689 1.00 79.91  ? 129 TRP I CE2 1 
ATOM   16192 C CE3 . TRP I  1 129 ? -15.083 28.564   -66.511 1.00 83.23  ? 129 TRP I CE3 1 
ATOM   16193 C CZ2 . TRP I  1 129 ? -16.225 27.032   -64.425 1.00 87.59  ? 129 TRP I CZ2 1 
ATOM   16194 C CZ3 . TRP I  1 129 ? -14.507 28.512   -65.255 1.00 74.84  ? 129 TRP I CZ3 1 
ATOM   16195 C CH2 . TRP I  1 129 ? -15.079 27.751   -64.228 1.00 78.97  ? 129 TRP I CH2 1 
ATOM   16196 N N   . PRO I  1 130 ? -17.046 31.681   -70.754 1.00 116.11 ? 130 PRO I N   1 
ATOM   16197 C CA  . PRO I  1 130 ? -17.298 32.388   -72.014 1.00 109.38 ? 130 PRO I CA  1 
ATOM   16198 C C   . PRO I  1 130 ? -16.126 32.282   -72.984 1.00 122.43 ? 130 PRO I C   1 
ATOM   16199 O O   . PRO I  1 130 ? -16.272 32.608   -74.162 1.00 123.19 ? 130 PRO I O   1 
ATOM   16200 C CB  . PRO I  1 130 ? -17.459 33.850   -71.569 1.00 106.62 ? 130 PRO I CB  1 
ATOM   16201 C CG  . PRO I  1 130 ? -17.393 33.836   -70.049 1.00 103.93 ? 130 PRO I CG  1 
ATOM   16202 C CD  . PRO I  1 130 ? -16.629 32.612   -69.696 1.00 119.36 ? 130 PRO I CD  1 
ATOM   16203 N N   . ASN I  1 131 ? -14.976 31.838   -72.487 1.00 138.52 ? 131 ASN I N   1 
ATOM   16204 C CA  . ASN I  1 131 ? -13.771 31.739   -73.303 1.00 132.04 ? 131 ASN I CA  1 
ATOM   16205 C C   . ASN I  1 131 ? -13.380 30.291   -73.563 1.00 125.74 ? 131 ASN I C   1 
ATOM   16206 O O   . ASN I  1 131 ? -12.310 30.011   -74.104 1.00 123.64 ? 131 ASN I O   1 
ATOM   16207 C CB  . ASN I  1 131 ? -12.615 32.478   -72.628 1.00 130.39 ? 131 ASN I CB  1 
ATOM   16208 C CG  . ASN I  1 131 ? -12.877 33.963   -72.484 1.00 138.50 ? 131 ASN I CG  1 
ATOM   16209 O OD1 . ASN I  1 131 ? -13.721 34.525   -73.182 1.00 148.30 ? 131 ASN I OD1 1 
ATOM   16210 N ND2 . ASN I  1 131 ? -12.152 34.607   -71.578 1.00 136.50 ? 131 ASN I ND2 1 
ATOM   16211 N N   . HIS I  1 132 ? -14.261 29.376   -73.174 1.00 101.52 ? 132 HIS I N   1 
ATOM   16212 C CA  . HIS I  1 132 ? -13.987 27.950   -73.271 1.00 86.80  ? 132 HIS I CA  1 
ATOM   16213 C C   . HIS I  1 132 ? -15.247 27.202   -73.694 1.00 85.02  ? 132 HIS I C   1 
ATOM   16214 O O   . HIS I  1 132 ? -16.361 27.656   -73.434 1.00 95.09  ? 132 HIS I O   1 
ATOM   16215 C CB  . HIS I  1 132 ? -13.489 27.426   -71.922 1.00 81.28  ? 132 HIS I CB  1 
ATOM   16216 C CG  . HIS I  1 132 ? -12.355 28.220   -71.346 1.00 79.41  ? 132 HIS I CG  1 
ATOM   16217 N ND1 . HIS I  1 132 ? -11.038 27.837   -71.473 1.00 73.28  ? 132 HIS I ND1 1 
ATOM   16218 C CD2 . HIS I  1 132 ? -12.344 29.378   -70.645 1.00 85.20  ? 132 HIS I CD2 1 
ATOM   16219 C CE1 . HIS I  1 132 ? -10.263 28.724   -70.873 1.00 84.07  ? 132 HIS I CE1 1 
ATOM   16220 N NE2 . HIS I  1 132 ? -11.032 29.669   -70.363 1.00 86.17  ? 132 HIS I NE2 1 
ATOM   16221 N N   . ASP I  1 133 ? -15.073 26.060   -74.353 1.00 72.77  ? 133 ASP I N   1 
ATOM   16222 C CA  . ASP I  1 133 ? -16.211 25.255   -74.786 1.00 84.16  ? 133 ASP I CA  1 
ATOM   16223 C C   . ASP I  1 133 ? -16.679 24.338   -73.661 1.00 91.24  ? 133 ASP I C   1 
ATOM   16224 O O   . ASP I  1 133 ? -15.926 23.488   -73.185 1.00 85.08  ? 133 ASP I O   1 
ATOM   16225 C CB  . ASP I  1 133 ? -15.858 24.439   -76.033 1.00 84.73  ? 133 ASP I CB  1 
ATOM   16226 C CG  . ASP I  1 133 ? -17.082 23.834   -76.703 1.00 104.78 ? 133 ASP I CG  1 
ATOM   16227 O OD1 . ASP I  1 133 ? -17.958 23.303   -75.990 1.00 103.11 ? 133 ASP I OD1 1 
ATOM   16228 O OD2 . ASP I  1 133 ? -17.165 23.887   -77.948 1.00 121.47 ? 133 ASP I OD2 1 
ATOM   16229 N N   . SER I  1 134 ? -17.926 24.517   -73.240 1.00 86.92  ? 134 SER I N   1 
ATOM   16230 C CA  . SER I  1 134 ? -18.489 23.730   -72.150 1.00 81.73  ? 134 SER I CA  1 
ATOM   16231 C C   . SER I  1 134 ? -19.529 22.738   -72.661 1.00 79.37  ? 134 SER I C   1 
ATOM   16232 O O   . SER I  1 134 ? -20.468 22.388   -71.946 1.00 91.77  ? 134 SER I O   1 
ATOM   16233 C CB  . SER I  1 134 ? -19.116 24.653   -71.104 1.00 85.74  ? 134 SER I CB  1 
ATOM   16234 O OG  . SER I  1 134 ? -20.070 25.514   -71.700 1.00 100.06 ? 134 SER I OG  1 
ATOM   16235 N N   . ASN I  1 135 ? -19.353 22.284   -73.898 1.00 77.68  ? 135 ASN I N   1 
ATOM   16236 C CA  . ASN I  1 135 ? -20.314 21.385   -74.527 1.00 91.73  ? 135 ASN I CA  1 
ATOM   16237 C C   . ASN I  1 135 ? -19.671 20.144   -75.145 1.00 88.34  ? 135 ASN I C   1 
ATOM   16238 O O   . ASN I  1 135 ? -20.314 19.103   -75.272 1.00 101.57 ? 135 ASN I O   1 
ATOM   16239 C CB  . ASN I  1 135 ? -21.123 22.134   -75.589 1.00 111.71 ? 135 ASN I CB  1 
ATOM   16240 C CG  . ASN I  1 135 ? -21.984 23.234   -75.000 1.00 108.05 ? 135 ASN I CG  1 
ATOM   16241 O OD1 . ASN I  1 135 ? -22.688 23.025   -74.012 1.00 90.71  ? 135 ASN I OD1 1 
ATOM   16242 N ND2 . ASN I  1 135 ? -21.937 24.414   -75.609 1.00 101.88 ? 135 ASN I ND2 1 
ATOM   16243 N N   . LYS I  1 136 ? -18.402 20.260   -75.526 1.00 86.87  ? 136 LYS I N   1 
ATOM   16244 C CA  . LYS I  1 136 ? -17.702 19.171   -76.202 1.00 99.69  ? 136 LYS I CA  1 
ATOM   16245 C C   . LYS I  1 136 ? -17.088 18.172   -75.227 1.00 103.01 ? 136 LYS I C   1 
ATOM   16246 O O   . LYS I  1 136 ? -16.430 17.217   -75.641 1.00 97.85  ? 136 LYS I O   1 
ATOM   16247 C CB  . LYS I  1 136 ? -16.617 19.730   -77.126 1.00 110.05 ? 136 LYS I CB  1 
ATOM   16248 C CG  . LYS I  1 136 ? -17.139 20.712   -78.161 1.00 115.17 ? 136 LYS I CG  1 
ATOM   16249 C CD  . LYS I  1 136 ? -16.701 20.322   -79.564 1.00 118.66 ? 136 LYS I CD  1 
ATOM   16250 C CE  . LYS I  1 136 ? -17.651 20.896   -80.601 1.00 138.89 ? 136 LYS I CE  1 
ATOM   16251 N NZ  . LYS I  1 136 ? -19.065 20.515   -80.315 1.00 142.50 ? 136 LYS I NZ  1 
ATOM   16252 N N   . GLY I  1 137 ? -17.314 18.388   -73.936 1.00 93.44  ? 137 GLY I N   1 
ATOM   16253 C CA  . GLY I  1 137 ? -16.719 17.553   -72.909 1.00 82.76  ? 137 GLY I CA  1 
ATOM   16254 C C   . GLY I  1 137 ? -17.483 16.274   -72.623 1.00 83.30  ? 137 GLY I C   1 
ATOM   16255 O O   . GLY I  1 137 ? -18.061 16.115   -71.549 1.00 78.34  ? 137 GLY I O   1 
ATOM   16256 N N   . VAL I  1 138 ? -17.485 15.358   -73.586 1.00 78.74  ? 138 VAL I N   1 
ATOM   16257 C CA  . VAL I  1 138 ? -18.124 14.059   -73.400 1.00 72.43  ? 138 VAL I CA  1 
ATOM   16258 C C   . VAL I  1 138 ? -17.169 12.930   -73.773 1.00 75.85  ? 138 VAL I C   1 
ATOM   16259 O O   . VAL I  1 138 ? -16.089 13.174   -74.309 1.00 87.32  ? 138 VAL I O   1 
ATOM   16260 C CB  . VAL I  1 138 ? -19.416 13.930   -74.228 1.00 77.25  ? 138 VAL I CB  1 
ATOM   16261 C CG1 . VAL I  1 138 ? -20.383 15.049   -73.878 1.00 90.49  ? 138 VAL I CG1 1 
ATOM   16262 C CG2 . VAL I  1 138 ? -19.099 13.935   -75.715 1.00 87.20  ? 138 VAL I CG2 1 
ATOM   16263 N N   . THR I  1 139 ? -17.572 11.696   -73.491 1.00 60.24  ? 139 THR I N   1 
ATOM   16264 C CA  . THR I  1 139 ? -16.715 10.542   -73.741 1.00 83.23  ? 139 THR I CA  1 
ATOM   16265 C C   . THR I  1 139 ? -17.510 9.244    -73.824 1.00 88.87  ? 139 THR I C   1 
ATOM   16266 O O   . THR I  1 139 ? -18.585 9.122    -73.239 1.00 83.11  ? 139 THR I O   1 
ATOM   16267 C CB  . THR I  1 139 ? -15.638 10.397   -72.648 1.00 86.83  ? 139 THR I CB  1 
ATOM   16268 O OG1 . THR I  1 139 ? -14.951 9.150    -72.811 1.00 70.49  ? 139 THR I OG1 1 
ATOM   16269 C CG2 . THR I  1 139 ? -16.273 10.435   -71.269 1.00 80.39  ? 139 THR I CG2 1 
ATOM   16270 N N   . ALA I  1 140 ? -16.971 8.276    -74.556 1.00 96.46  ? 140 ALA I N   1 
ATOM   16271 C CA  . ALA I  1 140 ? -17.592 6.965    -74.662 1.00 93.45  ? 140 ALA I CA  1 
ATOM   16272 C C   . ALA I  1 140 ? -17.484 6.212    -73.338 1.00 96.20  ? 140 ALA I C   1 
ATOM   16273 O O   . ALA I  1 140 ? -18.122 5.179    -73.148 1.00 96.58  ? 140 ALA I O   1 
ATOM   16274 C CB  . ALA I  1 140 ? -16.949 6.164    -75.790 1.00 98.13  ? 140 ALA I CB  1 
ATOM   16275 N N   . ALA I  1 141 ? -16.671 6.745    -72.429 1.00 92.56  ? 141 ALA I N   1 
ATOM   16276 C CA  . ALA I  1 141 ? -16.414 6.117    -71.141 1.00 93.38  ? 141 ALA I CA  1 
ATOM   16277 C C   . ALA I  1 141 ? -17.559 6.388    -70.181 1.00 87.60  ? 141 ALA I C   1 
ATOM   16278 O O   . ALA I  1 141 ? -17.839 5.587    -69.295 1.00 81.16  ? 141 ALA I O   1 
ATOM   16279 C CB  . ALA I  1 141 ? -15.101 6.621    -70.561 1.00 86.42  ? 141 ALA I CB  1 
ATOM   16280 N N   . CYS I  1 142 ? -18.221 7.525    -70.351 1.00 80.06  ? 142 CYS I N   1 
ATOM   16281 C CA  . CYS I  1 142 ? -19.419 7.798    -69.574 1.00 73.17  ? 142 CYS I CA  1 
ATOM   16282 C C   . CYS I  1 142 ? -20.670 7.735    -70.463 1.00 85.30  ? 142 CYS I C   1 
ATOM   16283 O O   . CYS I  1 142 ? -21.308 8.754    -70.731 1.00 88.77  ? 142 CYS I O   1 
ATOM   16284 C CB  . CYS I  1 142 ? -19.297 9.129    -68.825 1.00 90.36  ? 142 CYS I CB  1 
ATOM   16285 S SG  . CYS I  1 142 ? -17.889 9.218    -67.669 1.00 97.97  ? 142 CYS I SG  1 
ATOM   16286 N N   . PRO I  1 143 ? -21.037 6.513    -70.888 1.00 86.31  ? 143 PRO I N   1 
ATOM   16287 C CA  . PRO I  1 143 ? -22.108 6.183    -71.843 1.00 94.63  ? 143 PRO I CA  1 
ATOM   16288 C C   . PRO I  1 143 ? -23.509 6.257    -71.250 1.00 99.65  ? 143 PRO I C   1 
ATOM   16289 O O   . PRO I  1 143 ? -23.680 5.963    -70.069 1.00 106.23 ? 143 PRO I O   1 
ATOM   16290 C CB  . PRO I  1 143 ? -21.821 4.727    -72.217 1.00 92.55  ? 143 PRO I CB  1 
ATOM   16291 C CG  . PRO I  1 143 ? -20.872 4.211    -71.174 1.00 87.92  ? 143 PRO I CG  1 
ATOM   16292 C CD  . PRO I  1 143 ? -20.491 5.313    -70.238 1.00 87.25  ? 143 PRO I CD  1 
ATOM   16293 N N   . HIS I  1 144 ? -24.490 6.620    -72.073 1.00 112.22 ? 144 HIS I N   1 
ATOM   16294 C CA  . HIS I  1 144 ? -25.880 6.728    -71.644 1.00 116.41 ? 144 HIS I CA  1 
ATOM   16295 C C   . HIS I  1 144 ? -26.818 6.503    -72.832 1.00 134.22 ? 144 HIS I C   1 
ATOM   16296 O O   . HIS I  1 144 ? -27.026 7.406    -73.646 1.00 130.46 ? 144 HIS I O   1 
ATOM   16297 C CB  . HIS I  1 144 ? -26.128 8.112    -71.043 1.00 106.25 ? 144 HIS I CB  1 
ATOM   16298 C CG  . HIS I  1 144 ? -27.305 8.177    -70.120 1.00 114.69 ? 144 HIS I CG  1 
ATOM   16299 N ND1 . HIS I  1 144 ? -28.121 9.285    -70.029 1.00 124.84 ? 144 HIS I ND1 1 
ATOM   16300 C CD2 . HIS I  1 144 ? -27.801 7.275    -69.238 1.00 122.13 ? 144 HIS I CD2 1 
ATOM   16301 C CE1 . HIS I  1 144 ? -29.065 9.063    -69.134 1.00 127.00 ? 144 HIS I CE1 1 
ATOM   16302 N NE2 . HIS I  1 144 ? -28.896 7.851    -68.639 1.00 125.75 ? 144 HIS I NE2 1 
ATOM   16303 N N   . ALA I  1 145 ? -27.380 5.300    -72.926 1.00 120.05 ? 145 ALA I N   1 
ATOM   16304 C CA  . ALA I  1 145 ? -28.259 4.931    -74.037 1.00 120.60 ? 145 ALA I CA  1 
ATOM   16305 C C   . ALA I  1 145 ? -27.512 4.936    -75.367 1.00 127.07 ? 145 ALA I C   1 
ATOM   16306 O O   . ALA I  1 145 ? -28.121 4.987    -76.435 1.00 123.12 ? 145 ALA I O   1 
ATOM   16307 C CB  . ALA I  1 145 ? -29.477 5.849    -74.099 1.00 109.60 ? 145 ALA I CB  1 
ATOM   16308 N N   . GLY I  1 146 ? -26.186 4.880    -75.293 1.00 145.48 ? 146 GLY I N   1 
ATOM   16309 C CA  . GLY I  1 146 ? -25.354 4.852    -76.481 1.00 140.78 ? 146 GLY I CA  1 
ATOM   16310 C C   . GLY I  1 146 ? -24.536 6.115    -76.669 1.00 143.78 ? 146 GLY I C   1 
ATOM   16311 O O   . GLY I  1 146 ? -23.346 6.055    -76.978 1.00 150.10 ? 146 GLY I O   1 
ATOM   16312 N N   . ALA I  1 147 ? -25.178 7.262    -76.477 1.00 122.48 ? 147 ALA I N   1 
ATOM   16313 C CA  . ALA I  1 147 ? -24.531 8.554    -76.680 1.00 132.59 ? 147 ALA I CA  1 
ATOM   16314 C C   . ALA I  1 147 ? -23.385 8.783    -75.698 1.00 120.27 ? 147 ALA I C   1 
ATOM   16315 O O   . ALA I  1 147 ? -23.430 8.321    -74.558 1.00 107.73 ? 147 ALA I O   1 
ATOM   16316 C CB  . ALA I  1 147 ? -25.553 9.675    -76.573 1.00 127.34 ? 147 ALA I CB  1 
ATOM   16317 N N   . LYS I  1 148 ? -22.359 9.497    -76.152 1.00 110.72 ? 148 LYS I N   1 
ATOM   16318 C CA  . LYS I  1 148 ? -21.223 9.837    -75.303 1.00 94.17  ? 148 LYS I CA  1 
ATOM   16319 C C   . LYS I  1 148 ? -21.594 10.966   -74.350 1.00 96.67  ? 148 LYS I C   1 
ATOM   16320 O O   . LYS I  1 148 ? -21.877 12.084   -74.782 1.00 96.41  ? 148 LYS I O   1 
ATOM   16321 C CB  . LYS I  1 148 ? -20.021 10.257   -76.153 1.00 95.71  ? 148 LYS I CB  1 
ATOM   16322 C CG  . LYS I  1 148 ? -19.517 9.189    -77.110 1.00 107.61 ? 148 LYS I CG  1 
ATOM   16323 C CD  . LYS I  1 148 ? -18.267 9.661    -77.839 1.00 106.55 ? 148 LYS I CD  1 
ATOM   16324 C CE  . LYS I  1 148 ? -18.519 10.966   -78.579 1.00 107.31 ? 148 LYS I CE  1 
ATOM   16325 N NZ  . LYS I  1 148 ? -17.288 11.483   -79.241 1.00 101.63 ? 148 LYS I NZ  1 
ATOM   16326 N N   . SER I  1 149 ? -21.590 10.675   -73.054 1.00 96.78  ? 149 SER I N   1 
ATOM   16327 C CA  . SER I  1 149 ? -21.965 11.670   -72.056 1.00 98.03  ? 149 SER I CA  1 
ATOM   16328 C C   . SER I  1 149 ? -20.830 11.935   -71.069 1.00 92.21  ? 149 SER I C   1 
ATOM   16329 O O   . SER I  1 149 ? -19.661 11.697   -71.372 1.00 83.43  ? 149 SER I O   1 
ATOM   16330 C CB  . SER I  1 149 ? -23.228 11.231   -71.312 1.00 87.60  ? 149 SER I CB  1 
ATOM   16331 O OG  . SER I  1 149 ? -23.788 12.304   -70.573 1.00 94.95  ? 149 SER I OG  1 
ATOM   16332 N N   . PHE I  1 150 ? -21.186 12.431   -69.889 1.00 92.62  ? 150 PHE I N   1 
ATOM   16333 C CA  . PHE I  1 150 ? -20.205 12.754   -68.861 1.00 73.18  ? 150 PHE I CA  1 
ATOM   16334 C C   . PHE I  1 150 ? -20.896 12.910   -67.513 1.00 70.41  ? 150 PHE I C   1 
ATOM   16335 O O   . PHE I  1 150 ? -22.119 12.806   -67.417 1.00 87.23  ? 150 PHE I O   1 
ATOM   16336 C CB  . PHE I  1 150 ? -19.459 14.040   -69.227 1.00 65.29  ? 150 PHE I CB  1 
ATOM   16337 C CG  . PHE I  1 150 ? -18.221 14.280   -68.409 1.00 64.20  ? 150 PHE I CG  1 
ATOM   16338 C CD1 . PHE I  1 150 ? -17.148 13.409   -68.485 1.00 57.60  ? 150 PHE I CD1 1 
ATOM   16339 C CD2 . PHE I  1 150 ? -18.124 15.384   -67.577 1.00 67.06  ? 150 PHE I CD2 1 
ATOM   16340 C CE1 . PHE I  1 150 ? -16.005 13.626   -67.739 1.00 37.82  ? 150 PHE I CE1 1 
ATOM   16341 C CE2 . PHE I  1 150 ? -16.982 15.608   -66.829 1.00 62.18  ? 150 PHE I CE2 1 
ATOM   16342 C CZ  . PHE I  1 150 ? -15.922 14.727   -66.911 1.00 48.53  ? 150 PHE I CZ  1 
ATOM   16343 N N   . TYR I  1 151 ? -20.108 13.152   -66.471 1.00 68.98  ? 151 TYR I N   1 
ATOM   16344 C CA  . TYR I  1 151 ? -20.656 13.391   -65.144 1.00 58.20  ? 151 TYR I CA  1 
ATOM   16345 C C   . TYR I  1 151 ? -21.529 14.640   -65.166 1.00 64.08  ? 151 TYR I C   1 
ATOM   16346 O O   . TYR I  1 151 ? -21.176 15.640   -65.789 1.00 78.43  ? 151 TYR I O   1 
ATOM   16347 C CB  . TYR I  1 151 ? -19.530 13.554   -64.123 1.00 68.76  ? 151 TYR I CB  1 
ATOM   16348 C CG  . TYR I  1 151 ? -18.554 12.400   -64.089 1.00 56.95  ? 151 TYR I CG  1 
ATOM   16349 C CD1 . TYR I  1 151 ? -18.879 11.206   -63.457 1.00 52.84  ? 151 TYR I CD1 1 
ATOM   16350 C CD2 . TYR I  1 151 ? -17.303 12.507   -64.682 1.00 56.99  ? 151 TYR I CD2 1 
ATOM   16351 C CE1 . TYR I  1 151 ? -17.987 10.150   -63.424 1.00 58.08  ? 151 TYR I CE1 1 
ATOM   16352 C CE2 . TYR I  1 151 ? -16.405 11.457   -64.653 1.00 50.73  ? 151 TYR I CE2 1 
ATOM   16353 C CZ  . TYR I  1 151 ? -16.751 10.281   -64.023 1.00 56.69  ? 151 TYR I CZ  1 
ATOM   16354 O OH  . TYR I  1 151 ? -15.862 9.232    -63.991 1.00 53.67  ? 151 TYR I OH  1 
ATOM   16355 N N   . LYS I  1 152 ? -22.672 14.577   -64.491 1.00 60.07  ? 152 LYS I N   1 
ATOM   16356 C CA  . LYS I  1 152 ? -23.595 15.704   -64.452 1.00 71.83  ? 152 LYS I CA  1 
ATOM   16357 C C   . LYS I  1 152 ? -23.042 16.834   -63.596 1.00 68.42  ? 152 LYS I C   1 
ATOM   16358 O O   . LYS I  1 152 ? -23.202 18.011   -63.920 1.00 84.91  ? 152 LYS I O   1 
ATOM   16359 C CB  . LYS I  1 152 ? -24.954 15.265   -63.906 1.00 71.00  ? 152 LYS I CB  1 
ATOM   16360 C CG  . LYS I  1 152 ? -25.633 14.182   -64.722 1.00 95.56  ? 152 LYS I CG  1 
ATOM   16361 C CD  . LYS I  1 152 ? -25.902 14.650   -66.142 1.00 125.72 ? 152 LYS I CD  1 
ATOM   16362 C CE  . LYS I  1 152 ? -26.607 13.575   -66.950 1.00 132.82 ? 152 LYS I CE  1 
ATOM   16363 N NZ  . LYS I  1 152 ? -26.851 14.010   -68.352 1.00 131.21 ? 152 LYS I NZ  1 
ATOM   16364 N N   . ASN I  1 153 ? -22.385 16.466   -62.501 1.00 56.93  ? 153 ASN I N   1 
ATOM   16365 C CA  . ASN I  1 153 ? -21.910 17.444   -61.533 1.00 60.57  ? 153 ASN I CA  1 
ATOM   16366 C C   . ASN I  1 153 ? -20.564 18.079   -61.881 1.00 59.37  ? 153 ASN I C   1 
ATOM   16367 O O   . ASN I  1 153 ? -20.046 18.907   -61.131 1.00 59.49  ? 153 ASN I O   1 
ATOM   16368 C CB  . ASN I  1 153 ? -21.895 16.845   -60.127 1.00 55.84  ? 153 ASN I CB  1 
ATOM   16369 C CG  . ASN I  1 153 ? -23.280 16.444   -59.657 1.00 67.45  ? 153 ASN I CG  1 
ATOM   16370 O OD1 . ASN I  1 153 ? -24.287 16.929   -60.174 1.00 85.16  ? 153 ASN I OD1 1 
ATOM   16371 N ND2 . ASN I  1 153 ? -23.339 15.556   -58.675 1.00 66.48  ? 153 ASN I ND2 1 
ATOM   16372 N N   . LEU I  1 154 ? -20.014 17.704   -63.030 1.00 59.71  ? 154 LEU I N   1 
ATOM   16373 C CA  . LEU I  1 154 ? -18.758 18.276   -63.496 1.00 71.55  ? 154 LEU I CA  1 
ATOM   16374 C C   . LEU I  1 154 ? -18.842 18.639   -64.974 1.00 66.04  ? 154 LEU I C   1 
ATOM   16375 O O   . LEU I  1 154 ? -19.622 18.050   -65.722 1.00 65.48  ? 154 LEU I O   1 
ATOM   16376 C CB  . LEU I  1 154 ? -17.605 17.298   -63.261 1.00 69.21  ? 154 LEU I CB  1 
ATOM   16377 C CG  . LEU I  1 154 ? -17.338 16.900   -61.808 1.00 49.77  ? 154 LEU I CG  1 
ATOM   16378 C CD1 . LEU I  1 154 ? -16.344 15.752   -61.737 1.00 59.44  ? 154 LEU I CD1 1 
ATOM   16379 C CD2 . LEU I  1 154 ? -16.844 18.093   -61.007 1.00 60.26  ? 154 LEU I CD2 1 
ATOM   16380 N N   . ILE I  1 155 ? -18.043 19.615   -65.388 1.00 69.61  ? 155 ILE I N   1 
ATOM   16381 C CA  . ILE I  1 155 ? -17.980 20.000   -66.792 1.00 85.28  ? 155 ILE I CA  1 
ATOM   16382 C C   . ILE I  1 155 ? -16.557 19.875   -67.319 1.00 70.55  ? 155 ILE I C   1 
ATOM   16383 O O   . ILE I  1 155 ? -15.636 20.506   -66.801 1.00 64.23  ? 155 ILE I O   1 
ATOM   16384 C CB  . ILE I  1 155 ? -18.471 21.440   -67.016 1.00 87.18  ? 155 ILE I CB  1 
ATOM   16385 C CG1 . ILE I  1 155 ? -19.937 21.574   -66.601 1.00 85.31  ? 155 ILE I CG1 1 
ATOM   16386 C CG2 . ILE I  1 155 ? -18.292 21.840   -68.473 1.00 67.98  ? 155 ILE I CG2 1 
ATOM   16387 C CD1 . ILE I  1 155 ? -20.490 22.970   -66.768 1.00 93.04  ? 155 ILE I CD1 1 
ATOM   16388 N N   . TRP I  1 156 ? -16.385 19.054   -68.348 1.00 52.62  ? 156 TRP I N   1 
ATOM   16389 C CA  . TRP I  1 156 ? -15.075 18.859   -68.955 1.00 58.04  ? 156 TRP I CA  1 
ATOM   16390 C C   . TRP I  1 156 ? -14.799 19.948   -69.985 1.00 71.05  ? 156 TRP I C   1 
ATOM   16391 O O   . TRP I  1 156 ? -15.143 19.810   -71.159 1.00 80.31  ? 156 TRP I O   1 
ATOM   16392 C CB  . TRP I  1 156 ? -14.988 17.481   -69.609 1.00 55.99  ? 156 TRP I CB  1 
ATOM   16393 C CG  . TRP I  1 156 ? -13.606 17.113   -70.050 1.00 64.42  ? 156 TRP I CG  1 
ATOM   16394 C CD1 . TRP I  1 156 ? -12.488 17.893   -69.986 1.00 71.46  ? 156 TRP I CD1 1 
ATOM   16395 C CD2 . TRP I  1 156 ? -13.194 15.867   -70.622 1.00 59.80  ? 156 TRP I CD2 1 
ATOM   16396 N NE1 . TRP I  1 156 ? -11.405 17.210   -70.484 1.00 68.38  ? 156 TRP I NE1 1 
ATOM   16397 C CE2 . TRP I  1 156 ? -11.812 15.963   -70.881 1.00 62.13  ? 156 TRP I CE2 1 
ATOM   16398 C CE3 . TRP I  1 156 ? -13.859 14.679   -70.942 1.00 63.13  ? 156 TRP I CE3 1 
ATOM   16399 C CZ2 . TRP I  1 156 ? -11.084 14.918   -71.444 1.00 68.64  ? 156 TRP I CZ2 1 
ATOM   16400 C CZ3 . TRP I  1 156 ? -13.135 13.643   -71.500 1.00 69.41  ? 156 TRP I CZ3 1 
ATOM   16401 C CH2 . TRP I  1 156 ? -11.761 13.769   -71.745 1.00 77.32  ? 156 TRP I CH2 1 
ATOM   16402 N N   . LEU I  1 157 ? -14.177 21.032   -69.535 1.00 58.54  ? 157 LEU I N   1 
ATOM   16403 C CA  . LEU I  1 157 ? -13.881 22.158   -70.411 1.00 63.60  ? 157 LEU I CA  1 
ATOM   16404 C C   . LEU I  1 157 ? -12.808 21.815   -71.436 1.00 70.82  ? 157 LEU I C   1 
ATOM   16405 O O   . LEU I  1 157 ? -11.759 21.268   -71.096 1.00 79.37  ? 157 LEU I O   1 
ATOM   16406 C CB  . LEU I  1 157 ? -13.444 23.376   -69.597 1.00 64.39  ? 157 LEU I CB  1 
ATOM   16407 C CG  . LEU I  1 157 ? -14.523 24.069   -68.764 1.00 71.57  ? 157 LEU I CG  1 
ATOM   16408 C CD1 . LEU I  1 157 ? -13.978 25.363   -68.182 1.00 68.36  ? 157 LEU I CD1 1 
ATOM   16409 C CD2 . LEU I  1 157 ? -15.782 24.325   -69.585 1.00 73.75  ? 157 LEU I CD2 1 
ATOM   16410 N N   . VAL I  1 158 ? -13.083 22.141   -72.695 1.00 77.36  ? 158 VAL I N   1 
ATOM   16411 C CA  . VAL I  1 158 ? -12.113 21.961   -73.767 1.00 76.39  ? 158 VAL I CA  1 
ATOM   16412 C C   . VAL I  1 158 ? -11.886 23.282   -74.490 1.00 82.41  ? 158 VAL I C   1 
ATOM   16413 O O   . VAL I  1 158 ? -12.611 24.251   -74.269 1.00 82.84  ? 158 VAL I O   1 
ATOM   16414 C CB  . VAL I  1 158 ? -12.580 20.911   -74.789 1.00 71.66  ? 158 VAL I CB  1 
ATOM   16415 C CG1 . VAL I  1 158 ? -12.720 19.548   -74.129 1.00 76.13  ? 158 VAL I CG1 1 
ATOM   16416 C CG2 . VAL I  1 158 ? -13.889 21.344   -75.429 1.00 87.43  ? 158 VAL I CG2 1 
ATOM   16417 N N   . LYS I  1 159 ? -10.887 23.312   -75.365 1.00 93.30  ? 159 LYS I N   1 
ATOM   16418 C CA  . LYS I  1 159 ? -10.518 24.539   -76.062 1.00 105.65 ? 159 LYS I CA  1 
ATOM   16419 C C   . LYS I  1 159 ? -11.631 25.027   -76.990 1.00 103.37 ? 159 LYS I C   1 
ATOM   16420 O O   . LYS I  1 159 ? -12.294 24.223   -77.647 1.00 83.27  ? 159 LYS I O   1 
ATOM   16421 C CB  . LYS I  1 159 ? -9.217  24.340   -76.844 1.00 103.70 ? 159 LYS I CB  1 
ATOM   16422 C CG  . LYS I  1 159 ? -9.328  23.397   -78.026 1.00 92.91  ? 159 LYS I CG  1 
ATOM   16423 C CD  . LYS I  1 159 ? -8.038  23.380   -78.826 1.00 106.88 ? 159 LYS I CD  1 
ATOM   16424 C CE  . LYS I  1 159 ? -8.187  22.553   -80.088 1.00 107.14 ? 159 LYS I CE  1 
ATOM   16425 N NZ  . LYS I  1 159 ? -6.931  22.532   -80.883 1.00 106.18 ? 159 LYS I NZ  1 
ATOM   16426 N N   . LYS I  1 160 ? -11.840 26.341   -77.042 1.00 113.97 ? 160 LYS I N   1 
ATOM   16427 C CA  . LYS I  1 160 ? -12.916 26.902   -77.863 1.00 122.11 ? 160 LYS I CA  1 
ATOM   16428 C C   . LYS I  1 160 ? -12.508 26.980   -79.336 1.00 128.54 ? 160 LYS I C   1 
ATOM   16429 O O   . LYS I  1 160 ? -11.794 27.891   -79.750 1.00 124.93 ? 160 LYS I O   1 
ATOM   16430 C CB  . LYS I  1 160 ? -13.386 28.269   -77.328 1.00 108.79 ? 160 LYS I CB  1 
ATOM   16431 C CG  . LYS I  1 160 ? -12.836 29.492   -78.065 1.00 117.36 ? 160 LYS I CG  1 
ATOM   16432 C CD  . LYS I  1 160 ? -13.877 30.604   -78.222 1.00 125.38 ? 160 LYS I CD  1 
ATOM   16433 C CE  . LYS I  1 160 ? -15.303 30.069   -78.196 1.00 122.89 ? 160 LYS I CE  1 
ATOM   16434 N NZ  . LYS I  1 160 ? -15.939 30.254   -76.860 1.00 119.05 ? 160 LYS I NZ  1 
ATOM   16435 N N   . GLY I  1 161 ? -12.955 26.002   -80.118 1.00 117.99 ? 161 GLY I N   1 
ATOM   16436 C CA  . GLY I  1 161 ? -12.602 25.915   -81.524 1.00 112.95 ? 161 GLY I CA  1 
ATOM   16437 C C   . GLY I  1 161 ? -11.131 25.564   -81.683 1.00 125.75 ? 161 GLY I C   1 
ATOM   16438 O O   . GLY I  1 161 ? -10.800 24.521   -82.260 1.00 126.61 ? 161 GLY I O   1 
ATOM   16439 N N   . ASN I  1 162 ? -10.258 26.438   -81.174 1.00 123.81 ? 162 ASN I N   1 
ATOM   16440 C CA  . ASN I  1 162 ? -8.801  26.303   -81.305 1.00 126.51 ? 162 ASN I CA  1 
ATOM   16441 C C   . ASN I  1 162 ? -8.018  26.958   -80.152 1.00 128.33 ? 162 ASN I C   1 
ATOM   16442 O O   . ASN I  1 162 ? -6.782  26.993   -80.147 1.00 127.55 ? 162 ASN I O   1 
ATOM   16443 C CB  . ASN I  1 162 ? -8.349  26.947   -82.628 1.00 144.71 ? 162 ASN I CB  1 
ATOM   16444 C CG  . ASN I  1 162 ? -7.013  26.399   -83.117 1.00 154.82 ? 162 ASN I CG  1 
ATOM   16445 O OD1 . ASN I  1 162 ? -5.945  26.877   -82.732 1.00 172.28 ? 162 ASN I OD1 1 
ATOM   16446 N ND2 . ASN I  1 162 ? -7.073  25.369   -83.952 1.00 141.43 ? 162 ASN I ND2 1 
ATOM   16447 N N   . SER I  1 163 ? -8.727  27.455   -79.154 1.00 126.91 ? 163 SER I N   1 
ATOM   16448 C CA  . SER I  1 163 ? -8.052  28.249   -78.151 1.00 133.25 ? 163 SER I CA  1 
ATOM   16449 C C   . SER I  1 163 ? -8.277  27.780   -76.698 1.00 119.51 ? 163 SER I C   1 
ATOM   16450 O O   . SER I  1 163 ? -9.235  27.066   -76.422 1.00 110.00 ? 163 SER I O   1 
ATOM   16451 C CB  . SER I  1 163 ? -8.518  29.674   -78.308 1.00 118.24 ? 163 SER I CB  1 
ATOM   16452 O OG  . SER I  1 163 ? -7.629  30.573   -77.689 1.00 99.65  ? 163 SER I OG  1 
ATOM   16453 N N   . TYR I  1 164 ? -7.387  28.161   -75.776 1.00 93.99  ? 164 TYR I N   1 
ATOM   16454 C CA  . TYR I  1 164 ? -7.590  27.889   -74.348 1.00 86.07  ? 164 TYR I CA  1 
ATOM   16455 C C   . TYR I  1 164 ? -6.832  28.894   -73.475 1.00 90.70  ? 164 TYR I C   1 
ATOM   16456 O O   . TYR I  1 164 ? -5.706  28.632   -73.051 1.00 84.41  ? 164 TYR I O   1 
ATOM   16457 C CB  . TYR I  1 164 ? -7.165  26.460   -73.994 1.00 98.88  ? 164 TYR I CB  1 
ATOM   16458 C CG  . TYR I  1 164 ? -7.729  25.956   -72.680 1.00 94.76  ? 164 TYR I CG  1 
ATOM   16459 C CD1 . TYR I  1 164 ? -8.577  24.857   -72.645 1.00 79.27  ? 164 TYR I CD1 1 
ATOM   16460 C CD2 . TYR I  1 164 ? -7.417  26.578   -71.479 1.00 90.12  ? 164 TYR I CD2 1 
ATOM   16461 C CE1 . TYR I  1 164 ? -9.097  24.391   -71.452 1.00 75.05  ? 164 TYR I CE1 1 
ATOM   16462 C CE2 . TYR I  1 164 ? -7.934  26.120   -70.280 1.00 81.04  ? 164 TYR I CE2 1 
ATOM   16463 C CZ  . TYR I  1 164 ? -8.774  25.026   -70.273 1.00 81.42  ? 164 TYR I CZ  1 
ATOM   16464 O OH  . TYR I  1 164 ? -9.293  24.561   -69.087 1.00 75.11  ? 164 TYR I OH  1 
ATOM   16465 N N   . PRO I  1 165 ? -7.456  30.048   -73.198 1.00 76.87  ? 165 PRO I N   1 
ATOM   16466 C CA  . PRO I  1 165 ? -6.863  31.107   -72.372 1.00 80.66  ? 165 PRO I CA  1 
ATOM   16467 C C   . PRO I  1 165 ? -6.903  30.748   -70.890 1.00 83.30  ? 165 PRO I C   1 
ATOM   16468 O O   . PRO I  1 165 ? -7.807  30.031   -70.461 1.00 78.89  ? 165 PRO I O   1 
ATOM   16469 C CB  . PRO I  1 165 ? -7.784  32.311   -72.626 1.00 82.98  ? 165 PRO I CB  1 
ATOM   16470 C CG  . PRO I  1 165 ? -8.689  31.908   -73.770 1.00 100.37 ? 165 PRO I CG  1 
ATOM   16471 C CD  . PRO I  1 165 ? -8.784  30.426   -73.700 1.00 76.84  ? 165 PRO I CD  1 
ATOM   16472 N N   . LYS I  1 166 ? -5.939  31.244   -70.120 1.00 74.01  ? 166 LYS I N   1 
ATOM   16473 C CA  . LYS I  1 166 ? -5.951  31.044   -68.675 1.00 81.46  ? 166 LYS I CA  1 
ATOM   16474 C C   . LYS I  1 166 ? -7.309  31.422   -68.101 1.00 95.70  ? 166 LYS I C   1 
ATOM   16475 O O   . LYS I  1 166 ? -7.730  32.575   -68.195 1.00 90.49  ? 166 LYS I O   1 
ATOM   16476 C CB  . LYS I  1 166 ? -4.866  31.880   -67.990 1.00 65.74  ? 166 LYS I CB  1 
ATOM   16477 C CG  . LYS I  1 166 ? -5.099  32.061   -66.491 1.00 87.05  ? 166 LYS I CG  1 
ATOM   16478 C CD  . LYS I  1 166 ? -4.147  33.073   -65.871 1.00 95.21  ? 166 LYS I CD  1 
ATOM   16479 C CE  . LYS I  1 166 ? -2.747  32.505   -65.716 1.00 109.90 ? 166 LYS I CE  1 
ATOM   16480 N NZ  . LYS I  1 166 ? -1.858  33.430   -64.959 1.00 115.67 ? 166 LYS I NZ  1 
ATOM   16481 N N   . LEU I  1 167 ? -7.998  30.451   -67.514 1.00 94.31  ? 167 LEU I N   1 
ATOM   16482 C CA  . LEU I  1 167 ? -9.259  30.743   -66.846 1.00 84.05  ? 167 LEU I CA  1 
ATOM   16483 C C   . LEU I  1 167 ? -9.018  31.014   -65.367 1.00 81.11  ? 167 LEU I C   1 
ATOM   16484 O O   . LEU I  1 167 ? -8.036  30.541   -64.794 1.00 81.56  ? 167 LEU I O   1 
ATOM   16485 C CB  . LEU I  1 167 ? -10.282 29.618   -67.050 1.00 63.46  ? 167 LEU I CB  1 
ATOM   16486 C CG  . LEU I  1 167 ? -10.067 28.204   -66.499 1.00 75.49  ? 167 LEU I CG  1 
ATOM   16487 C CD1 . LEU I  1 167 ? -9.925  28.168   -64.982 1.00 79.17  ? 167 LEU I CD1 1 
ATOM   16488 C CD2 . LEU I  1 167 ? -11.215 27.310   -66.947 1.00 70.83  ? 167 LEU I CD2 1 
ATOM   16489 N N   . SER I  1 168 ? -9.908  31.787   -64.755 1.00 76.07  ? 168 SER I N   1 
ATOM   16490 C CA  . SER I  1 168 ? -9.753  32.144   -63.351 1.00 84.26  ? 168 SER I CA  1 
ATOM   16491 C C   . SER I  1 168 ? -11.098 32.442   -62.696 1.00 87.83  ? 168 SER I C   1 
ATOM   16492 O O   . SER I  1 168 ? -11.496 33.600   -62.565 1.00 106.10 ? 168 SER I O   1 
ATOM   16493 C CB  . SER I  1 168 ? -8.809  33.340   -63.207 1.00 92.86  ? 168 SER I CB  1 
ATOM   16494 O OG  . SER I  1 168 ? -8.261  33.406   -61.902 1.00 96.25  ? 168 SER I OG  1 
ATOM   16495 N N   . LYS I  1 169 ? -11.794 31.384   -62.294 1.00 74.47  ? 169 LYS I N   1 
ATOM   16496 C CA  . LYS I  1 169 ? -13.061 31.513   -61.587 1.00 77.53  ? 169 LYS I CA  1 
ATOM   16497 C C   . LYS I  1 169 ? -12.848 31.246   -60.103 1.00 76.43  ? 169 LYS I C   1 
ATOM   16498 O O   . LYS I  1 169 ? -11.952 30.493   -59.724 1.00 87.13  ? 169 LYS I O   1 
ATOM   16499 C CB  . LYS I  1 169 ? -14.087 30.528   -62.149 1.00 69.56  ? 169 LYS I CB  1 
ATOM   16500 C CG  . LYS I  1 169 ? -15.189 31.160   -62.987 1.00 89.04  ? 169 LYS I CG  1 
ATOM   16501 C CD  . LYS I  1 169 ? -16.166 31.942   -62.124 1.00 96.76  ? 169 LYS I CD  1 
ATOM   16502 C CE  . LYS I  1 169 ? -17.413 32.324   -62.906 1.00 96.48  ? 169 LYS I CE  1 
ATOM   16503 N NZ  . LYS I  1 169 ? -17.094 33.130   -64.117 1.00 105.50 ? 169 LYS I NZ  1 
ATOM   16504 N N   . SER I  1 170 ? -13.669 31.867   -59.265 1.00 81.85  ? 170 SER I N   1 
ATOM   16505 C CA  . SER I  1 170 ? -13.594 31.642   -57.827 1.00 83.18  ? 170 SER I CA  1 
ATOM   16506 C C   . SER I  1 170 ? -14.944 31.876   -57.158 1.00 76.92  ? 170 SER I C   1 
ATOM   16507 O O   . SER I  1 170 ? -15.557 32.931   -57.319 1.00 83.31  ? 170 SER I O   1 
ATOM   16508 C CB  . SER I  1 170 ? -12.516 32.523   -57.190 1.00 78.66  ? 170 SER I CB  1 
ATOM   16509 O OG  . SER I  1 170 ? -12.728 33.891   -57.487 1.00 106.20 ? 170 SER I OG  1 
ATOM   16510 N N   . TYR I  1 171 ? -15.401 30.875   -56.414 1.00 71.52  ? 171 TYR I N   1 
ATOM   16511 C CA  . TYR I  1 171 ? -16.678 30.946   -55.719 1.00 71.68  ? 171 TYR I CA  1 
ATOM   16512 C C   . TYR I  1 171 ? -16.467 31.132   -54.225 1.00 69.37  ? 171 TYR I C   1 
ATOM   16513 O O   . TYR I  1 171 ? -15.519 30.600   -53.651 1.00 68.07  ? 171 TYR I O   1 
ATOM   16514 C CB  . TYR I  1 171 ? -17.494 29.679   -55.977 1.00 75.10  ? 171 TYR I CB  1 
ATOM   16515 C CG  . TYR I  1 171 ? -18.560 29.404   -54.939 1.00 76.06  ? 171 TYR I CG  1 
ATOM   16516 C CD1 . TYR I  1 171 ? -19.845 29.911   -55.081 1.00 71.58  ? 171 TYR I CD1 1 
ATOM   16517 C CD2 . TYR I  1 171 ? -18.282 28.630   -53.819 1.00 72.54  ? 171 TYR I CD2 1 
ATOM   16518 C CE1 . TYR I  1 171 ? -20.822 29.658   -54.134 1.00 78.94  ? 171 TYR I CE1 1 
ATOM   16519 C CE2 . TYR I  1 171 ? -19.251 28.373   -52.868 1.00 75.17  ? 171 TYR I CE2 1 
ATOM   16520 C CZ  . TYR I  1 171 ? -20.519 28.889   -53.030 1.00 80.79  ? 171 TYR I CZ  1 
ATOM   16521 O OH  . TYR I  1 171 ? -21.487 28.635   -52.086 1.00 85.62  ? 171 TYR I OH  1 
ATOM   16522 N N   . ILE I  1 172 ? -17.360 31.886   -53.597 1.00 71.69  ? 172 ILE I N   1 
ATOM   16523 C CA  . ILE I  1 172 ? -17.271 32.126   -52.166 1.00 78.51  ? 172 ILE I CA  1 
ATOM   16524 C C   . ILE I  1 172 ? -18.499 31.564   -51.458 1.00 82.32  ? 172 ILE I C   1 
ATOM   16525 O O   . ILE I  1 172 ? -19.634 31.779   -51.886 1.00 71.48  ? 172 ILE I O   1 
ATOM   16526 C CB  . ILE I  1 172 ? -17.124 33.621   -51.863 1.00 69.91  ? 172 ILE I CB  1 
ATOM   16527 C CG1 . ILE I  1 172 ? -16.935 33.850   -50.362 1.00 83.10  ? 172 ILE I CG1 1 
ATOM   16528 C CG2 . ILE I  1 172 ? -18.320 34.369   -52.386 1.00 83.40  ? 172 ILE I CG2 1 
ATOM   16529 C CD1 . ILE I  1 172 ? -15.634 34.546   -50.014 1.00 89.85  ? 172 ILE I CD1 1 
ATOM   16530 N N   . ASN I  1 173 ? -18.258 30.835   -50.375 1.00 79.99  ? 173 ASN I N   1 
ATOM   16531 C CA  . ASN I  1 173 ? -19.318 30.142   -49.655 1.00 69.28  ? 173 ASN I CA  1 
ATOM   16532 C C   . ASN I  1 173 ? -20.260 31.095   -48.926 1.00 81.10  ? 173 ASN I C   1 
ATOM   16533 O O   . ASN I  1 173 ? -19.973 31.537   -47.813 1.00 75.54  ? 173 ASN I O   1 
ATOM   16534 C CB  . ASN I  1 173 ? -18.713 29.138   -48.672 1.00 72.07  ? 173 ASN I CB  1 
ATOM   16535 C CG  . ASN I  1 173 ? -19.747 28.200   -48.088 1.00 77.96  ? 173 ASN I CG  1 
ATOM   16536 O OD1 . ASN I  1 173 ? -20.938 28.313   -48.376 1.00 79.87  ? 173 ASN I OD1 1 
ATOM   16537 N ND2 . ASN I  1 173 ? -19.296 27.263   -47.263 1.00 74.25  ? 173 ASN I ND2 1 
ATOM   16538 N N   . ASP I  1 174 ? -21.387 31.402   -49.559 1.00 91.10  ? 174 ASP I N   1 
ATOM   16539 C CA  . ASP I  1 174 ? -22.381 32.291   -48.968 1.00 92.32  ? 174 ASP I CA  1 
ATOM   16540 C C   . ASP I  1 174 ? -23.400 31.509   -48.147 1.00 94.45  ? 174 ASP I C   1 
ATOM   16541 O O   . ASP I  1 174 ? -24.292 32.090   -47.531 1.00 106.97 ? 174 ASP I O   1 
ATOM   16542 C CB  . ASP I  1 174 ? -23.089 33.102   -50.054 1.00 99.76  ? 174 ASP I CB  1 
ATOM   16543 C CG  . ASP I  1 174 ? -23.713 32.228   -51.122 1.00 113.43 ? 174 ASP I CG  1 
ATOM   16544 O OD1 . ASP I  1 174 ? -24.932 31.968   -51.043 1.00 120.45 ? 174 ASP I OD1 1 
ATOM   16545 O OD2 . ASP I  1 174 ? -22.984 31.799   -52.040 1.00 110.12 ? 174 ASP I OD2 1 
ATOM   16546 N N   . LYS I  1 175 ? -23.261 30.187   -48.147 1.00 90.66  ? 175 LYS I N   1 
ATOM   16547 C CA  . LYS I  1 175 ? -24.134 29.323   -47.362 1.00 80.89  ? 175 LYS I CA  1 
ATOM   16548 C C   . LYS I  1 175 ? -23.780 29.429   -45.881 1.00 85.11  ? 175 LYS I C   1 
ATOM   16549 O O   . LYS I  1 175 ? -22.781 30.050   -45.517 1.00 89.30  ? 175 LYS I O   1 
ATOM   16550 C CB  . LYS I  1 175 ? -24.003 27.869   -47.825 1.00 75.63  ? 175 LYS I CB  1 
ATOM   16551 C CG  . LYS I  1 175 ? -24.173 27.658   -49.326 1.00 72.41  ? 175 LYS I CG  1 
ATOM   16552 C CD  . LYS I  1 175 ? -25.613 27.865   -49.770 1.00 67.32  ? 175 LYS I CD  1 
ATOM   16553 C CE  . LYS I  1 175 ? -25.788 27.516   -51.243 1.00 65.86  ? 175 LYS I CE  1 
ATOM   16554 N NZ  . LYS I  1 175 ? -27.202 27.650   -51.694 1.00 94.42  ? 175 LYS I NZ  1 
ATOM   16555 N N   . GLY I  1 176 ? -24.603 28.826   -45.029 1.00 68.60  ? 176 GLY I N   1 
ATOM   16556 C CA  . GLY I  1 176 ? -24.338 28.803   -43.601 1.00 90.80  ? 176 GLY I CA  1 
ATOM   16557 C C   . GLY I  1 176 ? -23.815 27.446   -43.182 1.00 94.66  ? 176 GLY I C   1 
ATOM   16558 O O   . GLY I  1 176 ? -23.842 27.081   -42.006 1.00 100.75 ? 176 GLY I O   1 
ATOM   16559 N N   . LYS I  1 177 ? -23.337 26.694   -44.165 1.00 88.91  ? 177 LYS I N   1 
ATOM   16560 C CA  . LYS I  1 177 ? -22.846 25.346   -43.942 1.00 77.17  ? 177 LYS I CA  1 
ATOM   16561 C C   . LYS I  1 177 ? -21.712 25.090   -44.915 1.00 65.82  ? 177 LYS I C   1 
ATOM   16562 O O   . LYS I  1 177 ? -21.595 25.773   -45.930 1.00 67.37  ? 177 LYS I O   1 
ATOM   16563 C CB  . LYS I  1 177 ? -23.969 24.339   -44.177 1.00 81.01  ? 177 LYS I CB  1 
ATOM   16564 C CG  . LYS I  1 177 ? -24.648 24.494   -45.530 1.00 69.70  ? 177 LYS I CG  1 
ATOM   16565 C CD  . LYS I  1 177 ? -25.874 23.604   -45.650 1.00 77.05  ? 177 LYS I CD  1 
ATOM   16566 C CE  . LYS I  1 177 ? -26.985 24.052   -44.713 1.00 86.25  ? 177 LYS I CE  1 
ATOM   16567 N NZ  . LYS I  1 177 ? -27.464 25.427   -45.021 1.00 85.12  ? 177 LYS I NZ  1 
ATOM   16568 N N   . GLU I  1 178 ? -20.871 24.110   -44.611 1.00 61.03  ? 178 GLU I N   1 
ATOM   16569 C CA  . GLU I  1 178 ? -19.770 23.793   -45.505 1.00 65.79  ? 178 GLU I CA  1 
ATOM   16570 C C   . GLU I  1 178 ? -20.286 23.398   -46.870 1.00 67.79  ? 178 GLU I C   1 
ATOM   16571 O O   . GLU I  1 178 ? -21.410 22.920   -47.010 1.00 65.52  ? 178 GLU I O   1 
ATOM   16572 C CB  . GLU I  1 178 ? -18.946 22.641   -44.964 1.00 69.60  ? 178 GLU I CB  1 
ATOM   16573 C CG  . GLU I  1 178 ? -18.249 22.925   -43.673 1.00 86.78  ? 178 GLU I CG  1 
ATOM   16574 C CD  . GLU I  1 178 ? -17.887 21.647   -42.977 1.00 94.17  ? 178 GLU I CD  1 
ATOM   16575 O OE1 . GLU I  1 178 ? -18.714 20.711   -43.030 1.00 87.38  ? 178 GLU I OE1 1 
ATOM   16576 O OE2 . GLU I  1 178 ? -16.786 21.571   -42.392 1.00 96.60  ? 178 GLU I OE2 1 
ATOM   16577 N N   . VAL I  1 179 ? -19.439 23.577   -47.874 1.00 53.17  ? 179 VAL I N   1 
ATOM   16578 C CA  . VAL I  1 179 ? -19.785 23.202   -49.232 1.00 59.52  ? 179 VAL I CA  1 
ATOM   16579 C C   . VAL I  1 179 ? -18.764 22.230   -49.805 1.00 53.02  ? 179 VAL I C   1 
ATOM   16580 O O   . VAL I  1 179 ? -17.575 22.537   -49.889 1.00 47.92  ? 179 VAL I O   1 
ATOM   16581 C CB  . VAL I  1 179 ? -19.883 24.434   -50.144 1.00 63.57  ? 179 VAL I CB  1 
ATOM   16582 C CG1 . VAL I  1 179 ? -19.953 24.009   -51.599 1.00 56.11  ? 179 VAL I CG1 1 
ATOM   16583 C CG2 . VAL I  1 179 ? -21.092 25.274   -49.766 1.00 55.96  ? 179 VAL I CG2 1 
ATOM   16584 N N   . LEU I  1 180 ? -19.238 21.052   -50.191 1.00 47.92  ? 180 LEU I N   1 
ATOM   16585 C CA  . LEU I  1 180 ? -18.381 20.054   -50.811 1.00 48.41  ? 180 LEU I CA  1 
ATOM   16586 C C   . LEU I  1 180 ? -18.184 20.381   -52.284 1.00 47.58  ? 180 LEU I C   1 
ATOM   16587 O O   . LEU I  1 180 ? -19.128 20.326   -53.071 1.00 54.53  ? 180 LEU I O   1 
ATOM   16588 C CB  . LEU I  1 180 ? -18.992 18.661   -50.669 1.00 46.87  ? 180 LEU I CB  1 
ATOM   16589 C CG  . LEU I  1 180 ? -18.232 17.532   -51.367 1.00 40.19  ? 180 LEU I CG  1 
ATOM   16590 C CD1 . LEU I  1 180 ? -16.947 17.220   -50.623 1.00 44.79  ? 180 LEU I CD1 1 
ATOM   16591 C CD2 . LEU I  1 180 ? -19.100 16.291   -51.480 1.00 38.97  ? 180 LEU I CD2 1 
ATOM   16592 N N   . VAL I  1 181 ? -16.956 20.728   -52.651 1.00 43.92  ? 181 VAL I N   1 
ATOM   16593 C CA  . VAL I  1 181 ? -16.637 21.019   -54.041 1.00 46.59  ? 181 VAL I CA  1 
ATOM   16594 C C   . VAL I  1 181 ? -15.773 19.912   -54.631 1.00 53.13  ? 181 VAL I C   1 
ATOM   16595 O O   . VAL I  1 181 ? -14.739 19.552   -54.068 1.00 46.30  ? 181 VAL I O   1 
ATOM   16596 C CB  . VAL I  1 181 ? -15.903 22.362   -54.185 1.00 47.60  ? 181 VAL I CB  1 
ATOM   16597 C CG1 . VAL I  1 181 ? -15.745 22.722   -55.653 1.00 50.47  ? 181 VAL I CG1 1 
ATOM   16598 C CG2 . VAL I  1 181 ? -16.653 23.455   -53.443 1.00 50.70  ? 181 VAL I CG2 1 
ATOM   16599 N N   . LEU I  1 182 ? -16.207 19.368   -55.763 1.00 56.32  ? 182 LEU I N   1 
ATOM   16600 C CA  . LEU I  1 182 ? -15.443 18.337   -56.452 1.00 49.28  ? 182 LEU I CA  1 
ATOM   16601 C C   . LEU I  1 182 ? -14.953 18.844   -57.800 1.00 44.42  ? 182 LEU I C   1 
ATOM   16602 O O   . LEU I  1 182 ? -15.635 19.620   -58.469 1.00 52.93  ? 182 LEU I O   1 
ATOM   16603 C CB  . LEU I  1 182 ? -16.281 17.071   -56.639 1.00 40.51  ? 182 LEU I CB  1 
ATOM   16604 C CG  . LEU I  1 182 ? -16.689 16.320   -55.371 1.00 46.02  ? 182 LEU I CG  1 
ATOM   16605 C CD1 . LEU I  1 182 ? -18.182 16.451   -55.128 1.00 62.10  ? 182 LEU I CD1 1 
ATOM   16606 C CD2 . LEU I  1 182 ? -16.291 14.858   -55.468 1.00 50.02  ? 182 LEU I CD2 1 
ATOM   16607 N N   . TRP I  1 183 ? -13.761 18.408   -58.190 1.00 52.71  ? 183 TRP I N   1 
ATOM   16608 C CA  . TRP I  1 183 ? -13.207 18.761   -59.489 1.00 56.61  ? 183 TRP I CA  1 
ATOM   16609 C C   . TRP I  1 183 ? -12.297 17.647   -59.987 1.00 54.99  ? 183 TRP I C   1 
ATOM   16610 O O   . TRP I  1 183 ? -11.961 16.730   -59.240 1.00 48.37  ? 183 TRP I O   1 
ATOM   16611 C CB  . TRP I  1 183 ? -12.445 20.085   -59.414 1.00 53.79  ? 183 TRP I CB  1 
ATOM   16612 C CG  . TRP I  1 183 ? -11.154 20.010   -58.659 1.00 40.84  ? 183 TRP I CG  1 
ATOM   16613 C CD1 . TRP I  1 183 ? -9.917  19.764   -59.177 1.00 45.08  ? 183 TRP I CD1 1 
ATOM   16614 C CD2 . TRP I  1 183 ? -10.970 20.195   -57.250 1.00 48.03  ? 183 TRP I CD2 1 
ATOM   16615 N NE1 . TRP I  1 183 ? -8.973  19.781   -58.179 1.00 47.73  ? 183 TRP I NE1 1 
ATOM   16616 C CE2 . TRP I  1 183 ? -9.594  20.044   -56.986 1.00 51.24  ? 183 TRP I CE2 1 
ATOM   16617 C CE3 . TRP I  1 183 ? -11.834 20.473   -56.186 1.00 53.80  ? 183 TRP I CE3 1 
ATOM   16618 C CZ2 . TRP I  1 183 ? -9.063  20.160   -55.703 1.00 46.14  ? 183 TRP I CZ2 1 
ATOM   16619 C CZ3 . TRP I  1 183 ? -11.304 20.587   -54.914 1.00 51.13  ? 183 TRP I CZ3 1 
ATOM   16620 C CH2 . TRP I  1 183 ? -9.933  20.431   -54.683 1.00 47.89  ? 183 TRP I CH2 1 
ATOM   16621 N N   . GLY I  1 184 ? -11.904 17.728   -61.253 1.00 57.53  ? 184 GLY I N   1 
ATOM   16622 C CA  . GLY I  1 184 ? -11.072 16.699   -61.846 1.00 46.68  ? 184 GLY I CA  1 
ATOM   16623 C C   . GLY I  1 184 ? -9.892  17.250   -62.618 1.00 52.18  ? 184 GLY I C   1 
ATOM   16624 O O   . GLY I  1 184 ? -9.957  18.341   -63.184 1.00 58.46  ? 184 GLY I O   1 
ATOM   16625 N N   . ILE I  1 185 ? -8.802  16.491   -62.629 1.00 55.24  ? 185 ILE I N   1 
ATOM   16626 C CA  . ILE I  1 185 ? -7.636  16.829   -63.431 1.00 45.20  ? 185 ILE I CA  1 
ATOM   16627 C C   . ILE I  1 185 ? -7.443  15.753   -64.489 1.00 51.79  ? 185 ILE I C   1 
ATOM   16628 O O   . ILE I  1 185 ? -7.152  14.602   -64.166 1.00 51.10  ? 185 ILE I O   1 
ATOM   16629 C CB  . ILE I  1 185 ? -6.363  16.920   -62.573 1.00 47.86  ? 185 ILE I CB  1 
ATOM   16630 C CG1 . ILE I  1 185 ? -6.580  17.869   -61.393 1.00 45.92  ? 185 ILE I CG1 1 
ATOM   16631 C CG2 . ILE I  1 185 ? -5.180  17.367   -63.421 1.00 45.00  ? 185 ILE I CG2 1 
ATOM   16632 C CD1 . ILE I  1 185 ? -6.943  19.278   -61.802 1.00 48.29  ? 185 ILE I CD1 1 
ATOM   16633 N N   . HIS I  1 186 ? -7.616  16.125   -65.753 1.00 61.69  ? 186 HIS I N   1 
ATOM   16634 C CA  . HIS I  1 186 ? -7.499  15.161   -66.841 1.00 56.54  ? 186 HIS I CA  1 
ATOM   16635 C C   . HIS I  1 186 ? -6.062  15.010   -67.325 1.00 54.17  ? 186 HIS I C   1 
ATOM   16636 O O   . HIS I  1 186 ? -5.371  15.997   -67.575 1.00 60.90  ? 186 HIS I O   1 
ATOM   16637 C CB  . HIS I  1 186 ? -8.412  15.537   -68.009 1.00 56.28  ? 186 HIS I CB  1 
ATOM   16638 C CG  . HIS I  1 186 ? -8.270  14.633   -69.195 1.00 58.23  ? 186 HIS I CG  1 
ATOM   16639 N ND1 . HIS I  1 186 ? -7.703  15.046   -70.382 1.00 69.75  ? 186 HIS I ND1 1 
ATOM   16640 C CD2 . HIS I  1 186 ? -8.604  13.334   -69.370 1.00 51.64  ? 186 HIS I CD2 1 
ATOM   16641 C CE1 . HIS I  1 186 ? -7.704  14.043   -71.240 1.00 70.25  ? 186 HIS I CE1 1 
ATOM   16642 N NE2 . HIS I  1 186 ? -8.245  12.991   -70.651 1.00 48.18  ? 186 HIS I NE2 1 
ATOM   16643 N N   . HIS I  1 187 ? -5.622  13.763   -67.450 1.00 59.81  ? 187 HIS I N   1 
ATOM   16644 C CA  . HIS I  1 187 ? -4.294  13.461   -67.963 1.00 50.58  ? 187 HIS I CA  1 
ATOM   16645 C C   . HIS I  1 187 ? -4.410  12.715   -69.287 1.00 65.18  ? 187 HIS I C   1 
ATOM   16646 O O   . HIS I  1 187 ? -4.625  11.503   -69.303 1.00 63.96  ? 187 HIS I O   1 
ATOM   16647 C CB  . HIS I  1 187 ? -3.507  12.623   -66.953 1.00 49.43  ? 187 HIS I CB  1 
ATOM   16648 C CG  . HIS I  1 187 ? -3.419  13.240   -65.593 1.00 57.73  ? 187 HIS I CG  1 
ATOM   16649 N ND1 . HIS I  1 187 ? -2.434  14.141   -65.244 1.00 58.68  ? 187 HIS I ND1 1 
ATOM   16650 C CD2 . HIS I  1 187 ? -4.190  13.084   -64.490 1.00 63.30  ? 187 HIS I CD2 1 
ATOM   16651 C CE1 . HIS I  1 187 ? -2.604  14.513   -63.989 1.00 67.18  ? 187 HIS I CE1 1 
ATOM   16652 N NE2 . HIS I  1 187 ? -3.663  13.886   -63.508 1.00 60.69  ? 187 HIS I NE2 1 
ATOM   16653 N N   . PRO I  1 188 ? -4.277  13.444   -70.404 1.00 63.93  ? 188 PRO I N   1 
ATOM   16654 C CA  . PRO I  1 188 ? -4.384  12.865   -71.748 1.00 61.37  ? 188 PRO I CA  1 
ATOM   16655 C C   . PRO I  1 188 ? -3.372  11.748   -71.974 1.00 69.08  ? 188 PRO I C   1 
ATOM   16656 O O   . PRO I  1 188 ? -2.363  11.673   -71.272 1.00 61.89  ? 188 PRO I O   1 
ATOM   16657 C CB  . PRO I  1 188 ? -4.074  14.053   -72.663 1.00 65.88  ? 188 PRO I CB  1 
ATOM   16658 C CG  . PRO I  1 188 ? -4.432  15.250   -71.855 1.00 69.34  ? 188 PRO I CG  1 
ATOM   16659 C CD  . PRO I  1 188 ? -4.060  14.900   -70.449 1.00 59.25  ? 188 PRO I CD  1 
ATOM   16660 N N   . SER I  1 189 ? -3.644  10.891   -72.952 1.00 76.56  ? 189 SER I N   1 
ATOM   16661 C CA  . SER I  1 189 ? -2.779  9.753    -73.234 1.00 64.00  ? 189 SER I CA  1 
ATOM   16662 C C   . SER I  1 189 ? -1.562  10.153   -74.060 1.00 71.65  ? 189 SER I C   1 
ATOM   16663 O O   . SER I  1 189 ? -0.465  9.634    -73.854 1.00 69.58  ? 189 SER I O   1 
ATOM   16664 C CB  . SER I  1 189 ? -3.564  8.650    -73.949 1.00 65.49  ? 189 SER I CB  1 
ATOM   16665 O OG  . SER I  1 189 ? -4.184  9.144    -75.124 1.00 86.94  ? 189 SER I OG  1 
ATOM   16666 N N   . THR I  1 190 ? -1.758  11.079   -74.991 1.00 77.95  ? 190 THR I N   1 
ATOM   16667 C CA  . THR I  1 190 ? -0.676  11.507   -75.868 1.00 74.79  ? 190 THR I CA  1 
ATOM   16668 C C   . THR I  1 190 ? -0.586  13.023   -75.977 1.00 77.84  ? 190 THR I C   1 
ATOM   16669 O O   . THR I  1 190 ? -1.565  13.733   -75.747 1.00 79.78  ? 190 THR I O   1 
ATOM   16670 C CB  . THR I  1 190 ? -0.843  10.931   -77.276 1.00 77.35  ? 190 THR I CB  1 
ATOM   16671 O OG1 . THR I  1 190 ? -0.444  11.911   -78.242 1.00 111.14 ? 190 THR I OG1 1 
ATOM   16672 N N   . SER I  1 191 ? 0.597   13.511   -76.336 1.00 87.09  ? 191 SER I N   1 
ATOM   16673 C CA  . SER I  1 191 ? 0.819   14.942   -76.499 1.00 92.76  ? 191 SER I CA  1 
ATOM   16674 C C   . SER I  1 191 ? -0.037  15.505   -77.629 1.00 90.93  ? 191 SER I C   1 
ATOM   16675 O O   . SER I  1 191 ? -0.326  16.701   -77.662 1.00 91.10  ? 191 SER I O   1 
ATOM   16676 C CB  . SER I  1 191 ? 2.300   15.232   -76.756 1.00 80.01  ? 191 SER I CB  1 
ATOM   16677 O OG  . SER I  1 191 ? 2.739   14.625   -77.958 1.00 88.10  ? 191 SER I OG  1 
ATOM   16678 N N   . ALA I  1 192 ? -0.437  14.639   -78.554 1.00 86.98  ? 192 ALA I N   1 
ATOM   16679 C CA  . ALA I  1 192 ? -1.335  15.034   -79.633 1.00 98.11  ? 192 ALA I CA  1 
ATOM   16680 C C   . ALA I  1 192 ? -2.738  15.263   -79.084 1.00 103.98 ? 192 ALA I C   1 
ATOM   16681 O O   . ALA I  1 192 ? -3.427  16.202   -79.483 1.00 92.54  ? 192 ALA I O   1 
ATOM   16682 C CB  . ALA I  1 192 ? -1.353  13.979   -80.727 1.00 97.56  ? 192 ALA I CB  1 
ATOM   16683 N N   . ASP I  1 193 ? -3.154  14.397   -78.165 1.00 100.43 ? 193 ASP I N   1 
ATOM   16684 C CA  . ASP I  1 193 ? -4.441  14.544   -77.496 1.00 89.26  ? 193 ASP I CA  1 
ATOM   16685 C C   . ASP I  1 193 ? -4.454  15.788   -76.616 1.00 82.32  ? 193 ASP I C   1 
ATOM   16686 O O   . ASP I  1 193 ? -5.498  16.411   -76.420 1.00 77.47  ? 193 ASP I O   1 
ATOM   16687 C CB  . ASP I  1 193 ? -4.754  13.309   -76.647 1.00 81.67  ? 193 ASP I CB  1 
ATOM   16688 C CG  . ASP I  1 193 ? -5.662  12.326   -77.358 1.00 107.71 ? 193 ASP I CG  1 
ATOM   16689 O OD1 . ASP I  1 193 ? -5.471  12.101   -78.571 1.00 113.69 ? 193 ASP I OD1 1 
ATOM   16690 O OD2 . ASP I  1 193 ? -6.569  11.775   -76.699 1.00 128.83 ? 193 ASP I OD2 1 
ATOM   16691 N N   . GLN I  1 194 ? -3.287  16.141   -76.086 1.00 80.11  ? 194 GLN I N   1 
ATOM   16692 C CA  . GLN I  1 194 ? -3.155  17.302   -75.213 1.00 79.52  ? 194 GLN I CA  1 
ATOM   16693 C C   . GLN I  1 194 ? -3.478  18.599   -75.948 1.00 88.36  ? 194 GLN I C   1 
ATOM   16694 O O   . GLN I  1 194 ? -4.352  19.356   -75.530 1.00 88.26  ? 194 GLN I O   1 
ATOM   16695 C CB  . GLN I  1 194 ? -1.743  17.370   -74.623 1.00 83.98  ? 194 GLN I CB  1 
ATOM   16696 C CG  . GLN I  1 194 ? -1.423  18.674   -73.906 1.00 81.35  ? 194 GLN I CG  1 
ATOM   16697 C CD  . GLN I  1 194 ? -2.178  18.832   -72.601 1.00 75.22  ? 194 GLN I CD  1 
ATOM   16698 O OE1 . GLN I  1 194 ? -2.235  19.922   -72.032 1.00 84.75  ? 194 GLN I OE1 1 
ATOM   16699 N NE2 . GLN I  1 194 ? -2.759  17.742   -72.118 1.00 62.55  ? 194 GLN I NE2 1 
ATOM   16700 N N   . GLN I  1 195 ? -2.767  18.850   -77.043 1.00 137.08 ? 195 GLN I N   1 
ATOM   16701 C CA  . GLN I  1 195 ? -2.984  20.058   -77.832 1.00 149.58 ? 195 GLN I CA  1 
ATOM   16702 C C   . GLN I  1 195 ? -4.323  20.007   -78.561 1.00 138.11 ? 195 GLN I C   1 
ATOM   16703 O O   . GLN I  1 195 ? -4.899  21.042   -78.895 1.00 131.27 ? 195 GLN I O   1 
ATOM   16704 C CB  . GLN I  1 195 ? -1.836  20.274   -78.821 1.00 143.43 ? 195 GLN I CB  1 
ATOM   16705 C CG  . GLN I  1 195 ? -1.559  19.090   -79.731 1.00 165.69 ? 195 GLN I CG  1 
ATOM   16706 C CD  . GLN I  1 195 ? -0.302  19.275   -80.559 1.00 189.20 ? 195 GLN I CD  1 
ATOM   16707 O OE1 . GLN I  1 195 ? 0.064   18.411   -81.355 1.00 186.86 ? 195 GLN I OE1 1 
ATOM   16708 N NE2 . GLN I  1 195 ? 0.369   20.406   -80.371 1.00 193.77 ? 195 GLN I NE2 1 
ATOM   16709 N N   . SER I  1 196 ? -4.815  18.796   -78.803 1.00 87.70  ? 196 SER I N   1 
ATOM   16710 C CA  . SER I  1 196 ? -6.117  18.611   -79.429 1.00 81.83  ? 196 SER I CA  1 
ATOM   16711 C C   . SER I  1 196 ? -7.230  19.093   -78.507 1.00 101.12 ? 196 SER I C   1 
ATOM   16712 O O   . SER I  1 196 ? -8.251  19.609   -78.962 1.00 109.88 ? 196 SER I O   1 
ATOM   16713 C CB  . SER I  1 196 ? -6.337  17.138   -79.778 1.00 76.29  ? 196 SER I CB  1 
ATOM   16714 O OG  . SER I  1 196 ? -7.660  16.914   -80.233 1.00 89.69  ? 196 SER I OG  1 
ATOM   16715 N N   . LEU I  1 197 ? -7.020  18.923   -77.206 1.00 89.55  ? 197 LEU I N   1 
ATOM   16716 C CA  . LEU I  1 197 ? -8.034  19.252   -76.211 1.00 75.79  ? 197 LEU I CA  1 
ATOM   16717 C C   . LEU I  1 197 ? -7.876  20.653   -75.625 1.00 83.99  ? 197 LEU I C   1 
ATOM   16718 O O   . LEU I  1 197 ? -8.861  21.369   -75.449 1.00 85.82  ? 197 LEU I O   1 
ATOM   16719 C CB  . LEU I  1 197 ? -8.033  18.215   -75.085 1.00 87.15  ? 197 LEU I CB  1 
ATOM   16720 C CG  . LEU I  1 197 ? -8.745  16.889   -75.363 1.00 79.54  ? 197 LEU I CG  1 
ATOM   16721 C CD1 . LEU I  1 197 ? -8.387  15.851   -74.310 1.00 73.35  ? 197 LEU I CD1 1 
ATOM   16722 C CD2 . LEU I  1 197 ? -10.249 17.098   -75.425 1.00 68.71  ? 197 LEU I CD2 1 
ATOM   16723 N N   . TYR I  1 198 ? -6.643  21.044   -75.319 1.00 85.40  ? 198 TYR I N   1 
ATOM   16724 C CA  . TYR I  1 198 ? -6.413  22.307   -74.626 1.00 90.59  ? 198 TYR I CA  1 
ATOM   16725 C C   . TYR I  1 198 ? -5.382  23.186   -75.331 1.00 91.99  ? 198 TYR I C   1 
ATOM   16726 O O   . TYR I  1 198 ? -5.027  24.256   -74.835 1.00 96.90  ? 198 TYR I O   1 
ATOM   16727 C CB  . TYR I  1 198 ? -5.998  22.046   -73.176 1.00 102.76 ? 198 TYR I CB  1 
ATOM   16728 C CG  . TYR I  1 198 ? -6.703  20.864   -72.548 1.00 77.50  ? 198 TYR I CG  1 
ATOM   16729 C CD1 . TYR I  1 198 ? -6.053  19.646   -72.400 1.00 67.32  ? 198 TYR I CD1 1 
ATOM   16730 C CD2 . TYR I  1 198 ? -8.019  20.960   -72.116 1.00 77.11  ? 198 TYR I CD2 1 
ATOM   16731 C CE1 . TYR I  1 198 ? -6.690  18.560   -71.832 1.00 77.54  ? 198 TYR I CE1 1 
ATOM   16732 C CE2 . TYR I  1 198 ? -8.666  19.878   -71.546 1.00 75.91  ? 198 TYR I CE2 1 
ATOM   16733 C CZ  . TYR I  1 198 ? -7.996  18.681   -71.407 1.00 80.02  ? 198 TYR I CZ  1 
ATOM   16734 O OH  . TYR I  1 198 ? -8.631  17.601   -70.841 1.00 67.85  ? 198 TYR I OH  1 
ATOM   16735 N N   . GLN I  1 199 ? -4.916  22.740   -76.492 1.00 92.37  ? 199 GLN I N   1 
ATOM   16736 C CA  . GLN I  1 199 ? -4.012  23.530   -77.327 1.00 106.62 ? 199 GLN I CA  1 
ATOM   16737 C C   . GLN I  1 199 ? -3.009  24.398   -76.559 1.00 103.61 ? 199 GLN I C   1 
ATOM   16738 O O   . GLN I  1 199 ? -2.894  25.597   -76.814 1.00 105.32 ? 199 GLN I O   1 
ATOM   16739 C CB  . GLN I  1 199 ? -4.815  24.403   -78.296 1.00 120.75 ? 199 GLN I CB  1 
ATOM   16740 C CG  . GLN I  1 199 ? -4.647  24.024   -79.758 1.00 125.49 ? 199 GLN I CG  1 
ATOM   16741 C CD  . GLN I  1 199 ? -3.349  24.538   -80.348 1.00 128.08 ? 199 GLN I CD  1 
ATOM   16742 O OE1 . GLN I  1 199 ? -2.730  25.456   -79.810 1.00 131.73 ? 199 GLN I OE1 1 
ATOM   16743 N NE2 . GLN I  1 199 ? -2.930  23.947   -81.461 1.00 112.58 ? 199 GLN I NE2 1 
ATOM   16744 N N   . ASN I  1 200 ? -2.278  23.785   -75.634 1.00 116.49 ? 200 ASN I N   1 
ATOM   16745 C CA  . ASN I  1 200 ? -1.163  24.439   -74.964 1.00 114.04 ? 200 ASN I CA  1 
ATOM   16746 C C   . ASN I  1 200 ? -0.536  23.095   -74.598 1.00 115.12 ? 200 ASN I C   1 
ATOM   16747 O O   . ASN I  1 200 ? -1.242  22.151   -74.241 1.00 113.65 ? 200 ASN I O   1 
ATOM   16748 C CB  . ASN I  1 200 ? -1.309  25.316   -73.720 1.00 110.70 ? 200 ASN I CB  1 
ATOM   16749 C CG  . ASN I  1 200 ? -2.246  26.489   -73.943 1.00 113.22 ? 200 ASN I CG  1 
ATOM   16750 O OD1 . ASN I  1 200 ? -2.602  26.805   -75.078 1.00 121.67 ? 200 ASN I OD1 1 
ATOM   16751 N ND2 . ASN I  1 200 ? -2.653  27.137   -72.859 1.00 109.04 ? 200 ASN I ND2 1 
ATOM   16752 N N   . ALA I  1 201 ? 0.787   23.010   -74.693 1.00 96.33  ? 201 ALA I N   1 
ATOM   16753 C CA  . ALA I  1 201 ? 1.495   21.765   -74.409 1.00 91.56  ? 201 ALA I CA  1 
ATOM   16754 C C   . ALA I  1 201 ? 1.899   21.675   -72.942 1.00 106.24 ? 201 ALA I C   1 
ATOM   16755 O O   . ALA I  1 201 ? 1.778   20.621   -72.317 1.00 100.11 ? 201 ALA I O   1 
ATOM   16756 C CB  . ALA I  1 201 ? 2.715   21.630   -75.309 1.00 99.69  ? 201 ALA I CB  1 
ATOM   16757 N N   . ASP I  1 202 ? 2.382   22.787   -72.398 1.00 106.11 ? 202 ASP I N   1 
ATOM   16758 C CA  . ASP I  1 202 ? 2.795   22.839   -71.002 1.00 107.23 ? 202 ASP I CA  1 
ATOM   16759 C C   . ASP I  1 202 ? 1.772   23.620   -70.185 1.00 102.10 ? 202 ASP I C   1 
ATOM   16760 O O   . ASP I  1 202 ? 1.808   24.850   -70.140 1.00 103.63 ? 202 ASP I O   1 
ATOM   16761 C CB  . ASP I  1 202 ? 4.177   23.483   -70.880 1.00 120.05 ? 202 ASP I CB  1 
ATOM   16762 C CG  . ASP I  1 202 ? 4.868   23.136   -69.577 1.00 127.88 ? 202 ASP I CG  1 
ATOM   16763 O OD1 . ASP I  1 202 ? 4.828   21.953   -69.179 1.00 123.05 ? 202 ASP I OD1 1 
ATOM   16764 O OD2 . ASP I  1 202 ? 5.458   24.044   -68.955 1.00 129.37 ? 202 ASP I OD2 1 
ATOM   16765 N N   . THR I  1 203 ? 0.859   22.900   -69.542 1.00 93.31  ? 203 THR I N   1 
ATOM   16766 C CA  . THR I  1 203 ? -0.238  23.528   -68.813 1.00 77.15  ? 203 THR I CA  1 
ATOM   16767 C C   . THR I  1 203 ? -0.178  23.247   -67.317 1.00 66.18  ? 203 THR I C   1 
ATOM   16768 O O   . THR I  1 203 ? 0.642   22.455   -66.856 1.00 78.88  ? 203 THR I O   1 
ATOM   16769 C CB  . THR I  1 203 ? -1.601  23.049   -69.338 1.00 75.68  ? 203 THR I CB  1 
ATOM   16770 O OG1 . THR I  1 203 ? -1.719  21.635   -69.141 1.00 60.99  ? 203 THR I OG1 1 
ATOM   16771 C CG2 . THR I  1 203 ? -1.741  23.363   -70.817 1.00 86.61  ? 203 THR I CG2 1 
ATOM   16772 N N   . TYR I  1 204 ? -1.058  23.901   -66.566 1.00 67.82  ? 204 TYR I N   1 
ATOM   16773 C CA  . TYR I  1 204 ? -1.136  23.691   -65.127 1.00 77.05  ? 204 TYR I CA  1 
ATOM   16774 C C   . TYR I  1 204 ? -2.528  24.006   -64.593 1.00 72.61  ? 204 TYR I C   1 
ATOM   16775 O O   . TYR I  1 204 ? -3.277  24.780   -65.189 1.00 63.11  ? 204 TYR I O   1 
ATOM   16776 C CB  . TYR I  1 204 ? -0.101  24.550   -64.397 1.00 66.12  ? 204 TYR I CB  1 
ATOM   16777 C CG  . TYR I  1 204 ? -0.464  26.017   -64.318 1.00 74.19  ? 204 TYR I CG  1 
ATOM   16778 C CD1 . TYR I  1 204 ? -1.164  26.523   -63.230 1.00 78.79  ? 204 TYR I CD1 1 
ATOM   16779 C CD2 . TYR I  1 204 ? -0.105  26.897   -65.331 1.00 79.25  ? 204 TYR I CD2 1 
ATOM   16780 C CE1 . TYR I  1 204 ? -1.498  27.864   -63.154 1.00 89.57  ? 204 TYR I CE1 1 
ATOM   16781 C CE2 . TYR I  1 204 ? -0.434  28.239   -65.264 1.00 85.57  ? 204 TYR I CE2 1 
ATOM   16782 C CZ  . TYR I  1 204 ? -1.130  28.716   -64.174 1.00 93.59  ? 204 TYR I CZ  1 
ATOM   16783 O OH  . TYR I  1 204 ? -1.459  30.051   -64.103 1.00 97.21  ? 204 TYR I OH  1 
ATOM   16784 N N   . VAL I  1 205 ? -2.865  23.398   -63.462 1.00 65.24  ? 205 VAL I N   1 
ATOM   16785 C CA  . VAL I  1 205 ? -4.121  23.681   -62.781 1.00 59.25  ? 205 VAL I CA  1 
ATOM   16786 C C   . VAL I  1 205 ? -3.827  24.016   -61.324 1.00 61.17  ? 205 VAL I C   1 
ATOM   16787 O O   . VAL I  1 205 ? -2.980  23.384   -60.698 1.00 66.59  ? 205 VAL I O   1 
ATOM   16788 C CB  . VAL I  1 205 ? -5.077  22.477   -62.839 1.00 58.37  ? 205 VAL I CB  1 
ATOM   16789 C CG1 . VAL I  1 205 ? -6.416  22.831   -62.200 1.00 56.67  ? 205 VAL I CG1 1 
ATOM   16790 C CG2 . VAL I  1 205 ? -5.259  22.008   -64.278 1.00 58.47  ? 205 VAL I CG2 1 
ATOM   16791 N N   . PHE I  1 206 ? -4.507  25.023   -60.788 1.00 59.78  ? 206 PHE I N   1 
ATOM   16792 C CA  . PHE I  1 206 ? -4.317  25.390   -59.390 1.00 65.83  ? 206 PHE I CA  1 
ATOM   16793 C C   . PHE I  1 206 ? -5.640  25.623   -58.668 1.00 68.83  ? 206 PHE I C   1 
ATOM   16794 O O   . PHE I  1 206 ? -6.460  26.434   -59.095 1.00 70.33  ? 206 PHE I O   1 
ATOM   16795 C CB  . PHE I  1 206 ? -3.419  26.623   -59.260 1.00 53.16  ? 206 PHE I CB  1 
ATOM   16796 C CG  . PHE I  1 206 ? -3.359  27.179   -57.866 1.00 67.83  ? 206 PHE I CG  1 
ATOM   16797 C CD1 . PHE I  1 206 ? -4.183  28.228   -57.492 1.00 66.46  ? 206 PHE I CD1 1 
ATOM   16798 C CD2 . PHE I  1 206 ? -2.490  26.649   -56.928 1.00 75.59  ? 206 PHE I CD2 1 
ATOM   16799 C CE1 . PHE I  1 206 ? -4.137  28.741   -56.211 1.00 71.18  ? 206 PHE I CE1 1 
ATOM   16800 C CE2 . PHE I  1 206 ? -2.439  27.158   -55.644 1.00 72.89  ? 206 PHE I CE2 1 
ATOM   16801 C CZ  . PHE I  1 206 ? -3.264  28.206   -55.286 1.00 82.85  ? 206 PHE I CZ  1 
ATOM   16802 N N   . VAL I  1 207 ? -5.833  24.901   -57.569 1.00 58.60  ? 207 VAL I N   1 
ATOM   16803 C CA  . VAL I  1 207 ? -7.031  25.040   -56.752 1.00 51.72  ? 207 VAL I CA  1 
ATOM   16804 C C   . VAL I  1 207 ? -6.652  25.448   -55.335 1.00 66.47  ? 207 VAL I C   1 
ATOM   16805 O O   . VAL I  1 207 ? -5.859  24.772   -54.678 1.00 75.86  ? 207 VAL I O   1 
ATOM   16806 C CB  . VAL I  1 207 ? -7.826  23.727   -56.698 1.00 53.63  ? 207 VAL I CB  1 
ATOM   16807 C CG1 . VAL I  1 207 ? -9.067  23.898   -55.840 1.00 51.08  ? 207 VAL I CG1 1 
ATOM   16808 C CG2 . VAL I  1 207 ? -8.200  23.280   -58.100 1.00 53.30  ? 207 VAL I CG2 1 
ATOM   16809 N N   . GLY I  1 208 ? -7.219  26.553   -54.864 1.00 67.21  ? 208 GLY I N   1 
ATOM   16810 C CA  . GLY I  1 208 ? -6.886  27.059   -53.547 1.00 69.28  ? 208 GLY I CA  1 
ATOM   16811 C C   . GLY I  1 208 ? -8.042  27.683   -52.790 1.00 71.89  ? 208 GLY I C   1 
ATOM   16812 O O   . GLY I  1 208 ? -8.926  28.306   -53.377 1.00 71.77  ? 208 GLY I O   1 
ATOM   16813 N N   . SER I  1 209 ? -8.031  27.500   -51.474 1.00 66.48  ? 209 SER I N   1 
ATOM   16814 C CA  . SER I  1 209 ? -8.976  28.158   -50.583 1.00 60.35  ? 209 SER I CA  1 
ATOM   16815 C C   . SER I  1 209 ? -8.192  28.739   -49.416 1.00 63.74  ? 209 SER I C   1 
ATOM   16816 O O   . SER I  1 209 ? -6.983  28.932   -49.515 1.00 70.88  ? 209 SER I O   1 
ATOM   16817 C CB  . SER I  1 209 ? -10.025 27.167   -50.075 1.00 70.41  ? 209 SER I CB  1 
ATOM   16818 O OG  . SER I  1 209 ? -9.446  26.209   -49.206 1.00 65.63  ? 209 SER I OG  1 
ATOM   16819 N N   . SER I  1 210 ? -8.872  29.014   -48.309 1.00 75.86  ? 210 SER I N   1 
ATOM   16820 C CA  . SER I  1 210 ? -8.194  29.520   -47.122 1.00 86.94  ? 210 SER I CA  1 
ATOM   16821 C C   . SER I  1 210 ? -7.288  28.452   -46.518 1.00 88.72  ? 210 SER I C   1 
ATOM   16822 O O   . SER I  1 210 ? -6.311  28.764   -45.838 1.00 71.24  ? 210 SER I O   1 
ATOM   16823 C CB  . SER I  1 210 ? -9.205  30.003   -46.081 1.00 91.28  ? 210 SER I CB  1 
ATOM   16824 O OG  . SER I  1 210 ? -9.892  31.157   -46.533 1.00 105.11 ? 210 SER I OG  1 
ATOM   16825 N N   . ARG I  1 211 ? -7.615  27.190   -46.781 1.00 80.41  ? 211 ARG I N   1 
ATOM   16826 C CA  . ARG I  1 211 ? -6.885  26.072   -46.197 1.00 97.79  ? 211 ARG I CA  1 
ATOM   16827 C C   . ARG I  1 211 ? -6.253  25.178   -47.264 1.00 89.71  ? 211 ARG I C   1 
ATOM   16828 O O   . ARG I  1 211 ? -5.150  24.664   -47.081 1.00 107.79 ? 211 ARG I O   1 
ATOM   16829 C CB  . ARG I  1 211 ? -7.816  25.249   -45.303 1.00 106.07 ? 211 ARG I CB  1 
ATOM   16830 C CG  . ARG I  1 211 ? -8.925  24.541   -46.060 1.00 111.20 ? 211 ARG I CG  1 
ATOM   16831 C CD  . ARG I  1 211 ? -10.082 24.172   -45.151 1.00 123.60 ? 211 ARG I CD  1 
ATOM   16832 N NE  . ARG I  1 211 ? -9.643  23.571   -43.896 1.00 140.02 ? 211 ARG I NE  1 
ATOM   16833 C CZ  . ARG I  1 211 ? -10.446 22.911   -43.068 1.00 129.51 ? 211 ARG I CZ  1 
ATOM   16834 N NH1 . ARG I  1 211 ? -11.728 22.756   -43.370 1.00 113.51 ? 211 ARG I NH1 1 
ATOM   16835 N NH2 . ARG I  1 211 ? -9.966  22.398   -41.944 1.00 124.16 ? 211 ARG I NH2 1 
ATOM   16836 N N   . TYR I  1 212 ? -6.955  25.000   -48.379 1.00 81.42  ? 212 TYR I N   1 
ATOM   16837 C CA  . TYR I  1 212 ? -6.484  24.134   -49.454 1.00 63.16  ? 212 TYR I CA  1 
ATOM   16838 C C   . TYR I  1 212 ? -5.622  24.910   -50.445 1.00 70.35  ? 212 TYR I C   1 
ATOM   16839 O O   . TYR I  1 212 ? -5.862  26.090   -50.696 1.00 75.24  ? 212 TYR I O   1 
ATOM   16840 C CB  . TYR I  1 212 ? -7.671  23.496   -50.180 1.00 59.85  ? 212 TYR I CB  1 
ATOM   16841 C CG  . TYR I  1 212 ? -7.290  22.376   -51.122 1.00 68.87  ? 212 TYR I CG  1 
ATOM   16842 C CD1 . TYR I  1 212 ? -7.354  21.050   -50.714 1.00 65.84  ? 212 TYR I CD1 1 
ATOM   16843 C CD2 . TYR I  1 212 ? -6.868  22.642   -52.417 1.00 70.78  ? 212 TYR I CD2 1 
ATOM   16844 C CE1 . TYR I  1 212 ? -7.008  20.022   -51.569 1.00 63.24  ? 212 TYR I CE1 1 
ATOM   16845 C CE2 . TYR I  1 212 ? -6.518  21.620   -53.279 1.00 66.62  ? 212 TYR I CE2 1 
ATOM   16846 C CZ  . TYR I  1 212 ? -6.590  20.312   -52.850 1.00 64.12  ? 212 TYR I CZ  1 
ATOM   16847 O OH  . TYR I  1 212 ? -6.244  19.289   -53.703 1.00 56.67  ? 212 TYR I OH  1 
ATOM   16848 N N   . SER I  1 213 ? -4.619  24.241   -51.006 1.00 66.17  ? 213 SER I N   1 
ATOM   16849 C CA  . SER I  1 213 ? -3.734  24.869   -51.981 1.00 67.87  ? 213 SER I CA  1 
ATOM   16850 C C   . SER I  1 213 ? -2.900  23.774   -52.638 1.00 68.29  ? 213 SER I C   1 
ATOM   16851 O O   . SER I  1 213 ? -2.172  23.047   -51.962 1.00 83.83  ? 213 SER I O   1 
ATOM   16852 C CB  . SER I  1 213 ? -2.888  25.957   -51.315 1.00 63.87  ? 213 SER I CB  1 
ATOM   16853 O OG  . SER I  1 213 ? -2.080  26.630   -52.266 1.00 53.16  ? 213 SER I OG  1 
ATOM   16854 N N   . LYS I  1 214 ? -3.008  23.656   -53.957 1.00 59.26  ? 214 LYS I N   1 
ATOM   16855 C CA  . LYS I  1 214 ? -2.203  22.689   -54.695 1.00 65.22  ? 214 LYS I CA  1 
ATOM   16856 C C   . LYS I  1 214 ? -2.178  23.012   -56.186 1.00 73.56  ? 214 LYS I C   1 
ATOM   16857 O O   . LYS I  1 214 ? -3.193  23.388   -56.773 1.00 58.55  ? 214 LYS I O   1 
ATOM   16858 C CB  . LYS I  1 214 ? -2.615  21.230   -54.475 1.00 59.33  ? 214 LYS I CB  1 
ATOM   16859 C CG  . LYS I  1 214 ? -1.654  20.227   -55.101 1.00 71.06  ? 214 LYS I CG  1 
ATOM   16860 C CD  . LYS I  1 214 ? -1.407  19.041   -54.180 1.00 90.73  ? 214 LYS I CD  1 
ATOM   16861 C CE  . LYS I  1 214 ? -2.223  17.828   -54.593 1.00 92.46  ? 214 LYS I CE  1 
ATOM   16862 N NZ  . LYS I  1 214 ? -1.713  17.221   -55.854 1.00 89.19  ? 214 LYS I NZ  1 
ATOM   16863 N N   . LYS I  1 215 ? -1.002  22.860   -56.785 1.00 74.69  ? 215 LYS I N   1 
ATOM   16864 C CA  . LYS I  1 215 ? -0.820  23.085   -58.211 1.00 67.21  ? 215 LYS I CA  1 
ATOM   16865 C C   . LYS I  1 215 ? -0.643  21.745   -58.913 1.00 61.26  ? 215 LYS I C   1 
ATOM   16866 O O   . LYS I  1 215 ? 0.159   20.914   -58.486 1.00 75.92  ? 215 LYS I O   1 
ATOM   16867 C CB  . LYS I  1 215 ? 0.400   23.974   -58.448 1.00 74.95  ? 215 LYS I CB  1 
ATOM   16868 C CG  . LYS I  1 215 ? 0.604   24.399   -59.890 1.00 73.66  ? 215 LYS I CG  1 
ATOM   16869 C CD  . LYS I  1 215 ? 1.770   25.368   -59.998 1.00 93.09  ? 215 LYS I CD  1 
ATOM   16870 C CE  . LYS I  1 215 ? 1.818   26.036   -61.361 1.00 96.34  ? 215 LYS I CE  1 
ATOM   16871 N NZ  . LYS I  1 215 ? 2.844   27.113   -61.406 1.00 86.44  ? 215 LYS I NZ  1 
ATOM   16872 N N   . PHE I  1 216 ? -1.396  21.536   -59.987 1.00 59.02  ? 216 PHE I N   1 
ATOM   16873 C CA  . PHE I  1 216 ? -1.385  20.259   -60.690 1.00 52.37  ? 216 PHE I CA  1 
ATOM   16874 C C   . PHE I  1 216 ? -0.677  20.344   -62.037 1.00 57.67  ? 216 PHE I C   1 
ATOM   16875 O O   . PHE I  1 216 ? -0.907  21.268   -62.817 1.00 66.38  ? 216 PHE I O   1 
ATOM   16876 C CB  . PHE I  1 216 ? -2.813  19.747   -60.890 1.00 61.12  ? 216 PHE I CB  1 
ATOM   16877 C CG  . PHE I  1 216 ? -3.593  19.611   -59.614 1.00 72.86  ? 216 PHE I CG  1 
ATOM   16878 C CD1 . PHE I  1 216 ? -4.350  20.666   -59.133 1.00 65.05  ? 216 PHE I CD1 1 
ATOM   16879 C CD2 . PHE I  1 216 ? -3.571  18.427   -58.895 1.00 62.89  ? 216 PHE I CD2 1 
ATOM   16880 C CE1 . PHE I  1 216 ? -5.069  20.545   -57.960 1.00 61.33  ? 216 PHE I CE1 1 
ATOM   16881 C CE2 . PHE I  1 216 ? -4.288  18.299   -57.720 1.00 65.02  ? 216 PHE I CE2 1 
ATOM   16882 C CZ  . PHE I  1 216 ? -5.038  19.360   -57.252 1.00 63.26  ? 216 PHE I CZ  1 
ATOM   16883 N N   . LYS I  1 217 ? 0.186   19.370   -62.300 1.00 69.47  ? 217 LYS I N   1 
ATOM   16884 C CA  . LYS I  1 217 ? 0.837   19.248   -63.596 1.00 65.04  ? 217 LYS I CA  1 
ATOM   16885 C C   . LYS I  1 217 ? 0.354   17.988   -64.300 1.00 66.17  ? 217 LYS I C   1 
ATOM   16886 O O   . LYS I  1 217 ? 0.530   16.882   -63.791 1.00 76.16  ? 217 LYS I O   1 
ATOM   16887 C CB  . LYS I  1 217 ? 2.358   19.213   -63.438 1.00 76.71  ? 217 LYS I CB  1 
ATOM   16888 C CG  . LYS I  1 217 ? 3.040   20.551   -63.669 1.00 85.20  ? 217 LYS I CG  1 
ATOM   16889 C CD  . LYS I  1 217 ? 2.876   21.005   -65.113 1.00 93.35  ? 217 LYS I CD  1 
ATOM   16890 C CE  . LYS I  1 217 ? 3.592   22.324   -65.369 1.00 100.09 ? 217 LYS I CE  1 
ATOM   16891 N NZ  . LYS I  1 217 ? 3.477   22.753   -66.790 1.00 109.57 ? 217 LYS I NZ  1 
ATOM   16892 N N   . PRO I  1 218 ? -0.270  18.154   -65.474 1.00 67.46  ? 218 PRO I N   1 
ATOM   16893 C CA  . PRO I  1 218 ? -0.780  17.024   -66.258 1.00 70.55  ? 218 PRO I CA  1 
ATOM   16894 C C   . PRO I  1 218 ? 0.313   16.009   -66.579 1.00 67.59  ? 218 PRO I C   1 
ATOM   16895 O O   . PRO I  1 218 ? 1.366   16.375   -67.101 1.00 66.90  ? 218 PRO I O   1 
ATOM   16896 C CB  . PRO I  1 218 ? -1.275  17.689   -67.545 1.00 62.60  ? 218 PRO I CB  1 
ATOM   16897 C CG  . PRO I  1 218 ? -1.592  19.088   -67.147 1.00 71.37  ? 218 PRO I CG  1 
ATOM   16898 C CD  . PRO I  1 218 ? -0.570  19.448   -66.109 1.00 75.22  ? 218 PRO I CD  1 
ATOM   16899 N N   . GLU I  1 219 ? 0.057   14.744   -66.265 1.00 79.23  ? 219 GLU I N   1 
ATOM   16900 C CA  . GLU I  1 219 ? 1.007   13.675   -66.542 1.00 73.07  ? 219 GLU I CA  1 
ATOM   16901 C C   . GLU I  1 219 ? 0.604   12.922   -67.801 1.00 66.47  ? 219 GLU I C   1 
ATOM   16902 O O   . GLU I  1 219 ? -0.208  12.000   -67.755 1.00 61.41  ? 219 GLU I O   1 
ATOM   16903 C CB  . GLU I  1 219 ? 1.088   12.719   -65.354 1.00 63.66  ? 219 GLU I CB  1 
ATOM   16904 C CG  . GLU I  1 219 ? 1.442   13.416   -64.059 1.00 74.32  ? 219 GLU I CG  1 
ATOM   16905 C CD  . GLU I  1 219 ? 1.493   12.474   -62.880 1.00 85.78  ? 219 GLU I CD  1 
ATOM   16906 O OE1 . GLU I  1 219 ? 1.194   11.274   -63.055 1.00 86.86  ? 219 GLU I OE1 1 
ATOM   16907 O OE2 . GLU I  1 219 ? 1.835   12.943   -61.775 1.00 78.80  ? 219 GLU I OE2 1 
ATOM   16908 N N   . ILE I  1 220 ? 1.182   13.325   -68.926 1.00 72.22  ? 220 ILE I N   1 
ATOM   16909 C CA  . ILE I  1 220 ? 0.814   12.769   -70.221 1.00 75.37  ? 220 ILE I CA  1 
ATOM   16910 C C   . ILE I  1 220 ? 1.568   11.480   -70.533 1.00 68.97  ? 220 ILE I C   1 
ATOM   16911 O O   . ILE I  1 220 ? 2.796   11.473   -70.623 1.00 71.66  ? 220 ILE I O   1 
ATOM   16912 C CB  . ILE I  1 220 ? 1.058   13.791   -71.343 1.00 67.69  ? 220 ILE I CB  1 
ATOM   16913 C CG1 . ILE I  1 220 ? 0.268   15.072   -71.067 1.00 61.26  ? 220 ILE I CG1 1 
ATOM   16914 C CG2 . ILE I  1 220 ? 0.684   13.200   -72.692 1.00 67.16  ? 220 ILE I CG2 1 
ATOM   16915 C CD1 . ILE I  1 220 ? 0.662   16.238   -71.945 1.00 80.82  ? 220 ILE I CD1 1 
ATOM   16916 N N   . ALA I  1 221 ? 0.821   10.393   -70.700 1.00 60.98  ? 221 ALA I N   1 
ATOM   16917 C CA  . ALA I  1 221 ? 1.404   9.094    -71.022 1.00 58.98  ? 221 ALA I CA  1 
ATOM   16918 C C   . ALA I  1 221 ? 0.326   8.078    -71.388 1.00 66.67  ? 221 ALA I C   1 
ATOM   16919 O O   . ALA I  1 221 ? -0.866  8.347    -71.246 1.00 77.13  ? 221 ALA I O   1 
ATOM   16920 C CB  . ALA I  1 221 ? 2.238   8.585    -69.860 1.00 57.92  ? 221 ALA I CB  1 
ATOM   16921 N N   . ILE I  1 222 ? 0.754   6.909    -71.853 1.00 67.30  ? 222 ILE I N   1 
ATOM   16922 C CA  . ILE I  1 222 ? -0.173  5.859    -72.259 1.00 76.49  ? 222 ILE I CA  1 
ATOM   16923 C C   . ILE I  1 222 ? -0.386  4.830    -71.153 1.00 74.17  ? 222 ILE I C   1 
ATOM   16924 O O   . ILE I  1 222 ? 0.520   4.066    -70.819 1.00 70.86  ? 222 ILE I O   1 
ATOM   16925 C CB  . ILE I  1 222 ? 0.320   5.128    -73.524 1.00 89.22  ? 222 ILE I CB  1 
ATOM   16926 C CG1 . ILE I  1 222 ? 0.496   6.115    -74.679 1.00 90.96  ? 222 ILE I CG1 1 
ATOM   16927 C CG2 . ILE I  1 222 ? -0.648  4.017    -73.910 1.00 69.61  ? 222 ILE I CG2 1 
ATOM   16928 C CD1 . ILE I  1 222 ? -0.784  6.809    -75.086 1.00 96.01  ? 222 ILE I CD1 1 
ATOM   16929 N N   . ARG I  1 223 ? -1.588  4.818    -70.587 1.00 70.47  ? 223 ARG I N   1 
ATOM   16930 C CA  . ARG I  1 223 ? -1.952  3.827    -69.582 1.00 68.85  ? 223 ARG I CA  1 
ATOM   16931 C C   . ARG I  1 223 ? -2.715  2.677    -70.228 1.00 70.86  ? 223 ARG I C   1 
ATOM   16932 O O   . ARG I  1 223 ? -3.404  2.872    -71.229 1.00 85.98  ? 223 ARG I O   1 
ATOM   16933 C CB  . ARG I  1 223 ? -2.810  4.454    -68.481 1.00 65.30  ? 223 ARG I CB  1 
ATOM   16934 C CG  . ARG I  1 223 ? -2.087  5.439    -67.576 1.00 59.23  ? 223 ARG I CG  1 
ATOM   16935 C CD  . ARG I  1 223 ? -2.048  6.837    -68.170 1.00 56.62  ? 223 ARG I CD  1 
ATOM   16936 N NE  . ARG I  1 223 ? -1.734  7.839    -67.154 1.00 55.60  ? 223 ARG I NE  1 
ATOM   16937 C CZ  . ARG I  1 223 ? -1.615  9.140    -67.396 1.00 62.42  ? 223 ARG I CZ  1 
ATOM   16938 N NH1 . ARG I  1 223 ? -1.781  9.608    -68.625 1.00 68.24  ? 223 ARG I NH1 1 
ATOM   16939 N NH2 . ARG I  1 223 ? -1.329  9.974    -66.405 1.00 66.75  ? 223 ARG I NH2 1 
ATOM   16940 N N   . PRO I  1 224 ? -2.594  1.470    -69.656 1.00 65.21  ? 224 PRO I N   1 
ATOM   16941 C CA  . PRO I  1 224 ? -3.346  0.310    -70.143 1.00 73.93  ? 224 PRO I CA  1 
ATOM   16942 C C   . PRO I  1 224 ? -4.837  0.620    -70.219 1.00 72.29  ? 224 PRO I C   1 
ATOM   16943 O O   . PRO I  1 224 ? -5.414  1.111    -69.249 1.00 74.30  ? 224 PRO I O   1 
ATOM   16944 C CB  . PRO I  1 224 ? -3.079  -0.751   -69.075 1.00 65.37  ? 224 PRO I CB  1 
ATOM   16945 C CG  . PRO I  1 224 ? -1.756  -0.377   -68.506 1.00 69.69  ? 224 PRO I CG  1 
ATOM   16946 C CD  . PRO I  1 224 ? -1.714  1.126    -68.526 1.00 69.71  ? 224 PRO I CD  1 
ATOM   16947 N N   . LYS I  1 225 ? -5.446  0.331    -71.363 1.00 76.33  ? 225 LYS I N   1 
ATOM   16948 C CA  . LYS I  1 225 ? -6.843  0.680    -71.602 1.00 84.72  ? 225 LYS I CA  1 
ATOM   16949 C C   . LYS I  1 225 ? -7.802  0.153    -70.540 1.00 77.66  ? 225 LYS I C   1 
ATOM   16950 O O   . LYS I  1 225 ? -7.884  -1.050   -70.293 1.00 68.60  ? 225 LYS I O   1 
ATOM   16951 C CB  . LYS I  1 225 ? -7.290  0.206    -72.986 1.00 99.94  ? 225 LYS I CB  1 
ATOM   16952 C CG  . LYS I  1 225 ? -6.680  0.992    -74.127 1.00 116.11 ? 225 LYS I CG  1 
ATOM   16953 C CD  . LYS I  1 225 ? -7.183  0.510    -75.473 1.00 130.60 ? 225 LYS I CD  1 
ATOM   16954 C CE  . LYS I  1 225 ? -6.552  1.308    -76.598 1.00 149.05 ? 225 LYS I CE  1 
ATOM   16955 N NZ  . LYS I  1 225 ? -6.892  2.757    -76.511 1.00 147.13 ? 225 LYS I NZ  1 
ATOM   16956 N N   . VAL I  1 226 ? -8.521  1.077    -69.915 1.00 72.45  ? 226 VAL I N   1 
ATOM   16957 C CA  . VAL I  1 226 ? -9.635  0.738    -69.044 1.00 70.03  ? 226 VAL I CA  1 
ATOM   16958 C C   . VAL I  1 226 ? -10.853 1.486    -69.565 1.00 75.51  ? 226 VAL I C   1 
ATOM   16959 O O   . VAL I  1 226 ? -10.922 2.709    -69.472 1.00 74.26  ? 226 VAL I O   1 
ATOM   16960 C CB  . VAL I  1 226 ? -9.365  1.145    -67.585 1.00 70.48  ? 226 VAL I CB  1 
ATOM   16961 C CG1 . VAL I  1 226 ? -10.556 0.793    -66.708 1.00 67.01  ? 226 VAL I CG1 1 
ATOM   16962 C CG2 . VAL I  1 226 ? -8.104  0.468    -67.072 1.00 63.20  ? 226 VAL I CG2 1 
ATOM   16963 N N   . ARG I  1 227 ? -11.801 0.752    -70.137 1.00 75.27  ? 227 ARG I N   1 
ATOM   16964 C CA  . ARG I  1 227 ? -12.966 1.370    -70.760 1.00 73.23  ? 227 ARG I CA  1 
ATOM   16965 C C   . ARG I  1 227 ? -12.559 2.230    -71.956 1.00 87.92  ? 227 ARG I C   1 
ATOM   16966 O O   . ARG I  1 227 ? -13.059 3.342    -72.131 1.00 96.40  ? 227 ARG I O   1 
ATOM   16967 C CB  . ARG I  1 227 ? -13.744 2.208    -69.743 1.00 69.53  ? 227 ARG I CB  1 
ATOM   16968 C CG  . ARG I  1 227 ? -14.364 1.398    -68.615 1.00 72.55  ? 227 ARG I CG  1 
ATOM   16969 C CD  . ARG I  1 227 ? -14.934 2.308    -67.542 1.00 70.03  ? 227 ARG I CD  1 
ATOM   16970 N NE  . ARG I  1 227 ? -16.304 1.951    -67.191 1.00 69.29  ? 227 ARG I NE  1 
ATOM   16971 C CZ  . ARG I  1 227 ? -17.373 2.333    -67.882 1.00 84.53  ? 227 ARG I CZ  1 
ATOM   16972 N NH1 . ARG I  1 227 ? -17.231 3.078    -68.969 1.00 91.06  ? 227 ARG I NH1 1 
ATOM   16973 N NH2 . ARG I  1 227 ? -18.584 1.962    -67.492 1.00 75.13  ? 227 ARG I NH2 1 
ATOM   16974 N N   . ASP I  1 228 ? -11.639 1.708    -72.763 1.00 91.04  ? 228 ASP I N   1 
ATOM   16975 C CA  . ASP I  1 228 ? -11.227 2.349    -74.013 1.00 100.08 ? 228 ASP I CA  1 
ATOM   16976 C C   . ASP I  1 228 ? -10.335 3.577    -73.840 1.00 93.53  ? 228 ASP I C   1 
ATOM   16977 O O   . ASP I  1 228 ? -9.808  4.106    -74.819 1.00 108.05 ? 228 ASP I O   1 
ATOM   16978 C CB  . ASP I  1 228 ? -12.446 2.705    -74.869 1.00 131.38 ? 228 ASP I CB  1 
ATOM   16979 C CG  . ASP I  1 228 ? -12.766 1.642    -75.898 1.00 152.69 ? 228 ASP I CG  1 
ATOM   16980 O OD1 . ASP I  1 228 ? -11.939 1.433    -76.811 1.00 150.32 ? 228 ASP I OD1 1 
ATOM   16981 O OD2 . ASP I  1 228 ? -13.844 1.020    -75.799 1.00 162.73 ? 228 ASP I OD2 1 
ATOM   16982 N N   . GLN I  1 229 ? -10.163 4.028    -72.603 1.00 82.11  ? 229 GLN I N   1 
ATOM   16983 C CA  . GLN I  1 229 ? -9.363  5.220    -72.344 1.00 87.94  ? 229 GLN I CA  1 
ATOM   16984 C C   . GLN I  1 229 ? -7.941  4.862    -71.925 1.00 78.52  ? 229 GLN I C   1 
ATOM   16985 O O   . GLN I  1 229 ? -7.737  4.125    -70.962 1.00 73.56  ? 229 GLN I O   1 
ATOM   16986 C CB  . GLN I  1 229 ? -10.021 6.084    -71.266 1.00 69.66  ? 229 GLN I CB  1 
ATOM   16987 C CG  . GLN I  1 229 ? -11.515 6.290    -71.459 1.00 72.97  ? 229 GLN I CG  1 
ATOM   16988 C CD  . GLN I  1 229 ? -11.853 6.911    -72.800 1.00 82.48  ? 229 GLN I CD  1 
ATOM   16989 O OE1 . GLN I  1 229 ? -11.097 7.728    -73.327 1.00 90.55  ? 229 GLN I OE1 1 
ATOM   16990 N NE2 . GLN I  1 229 ? -12.996 6.529    -73.357 1.00 89.67  ? 229 GLN I NE2 1 
ATOM   16991 N N   . GLU I  1 230 ? -6.961  5.383    -72.656 1.00 78.13  ? 230 GLU I N   1 
ATOM   16992 C CA  . GLU I  1 230 ? -5.562  5.203    -72.285 1.00 73.29  ? 230 GLU I CA  1 
ATOM   16993 C C   . GLU I  1 230 ? -5.077  6.390    -71.460 1.00 72.85  ? 230 GLU I C   1 
ATOM   16994 O O   . GLU I  1 230 ? -3.963  6.388    -70.938 1.00 78.58  ? 230 GLU I O   1 
ATOM   16995 C CB  . GLU I  1 230 ? -4.687  4.988    -73.523 1.00 95.19  ? 230 GLU I CB  1 
ATOM   16996 C CG  . GLU I  1 230 ? -4.589  3.529    -73.943 1.00 96.63  ? 230 GLU I CG  1 
ATOM   16997 C CD  . GLU I  1 230 ? -4.081  3.349    -75.358 1.00 129.29 ? 230 GLU I CD  1 
ATOM   16998 O OE1 . GLU I  1 230 ? -3.562  2.256    -75.670 1.00 113.99 ? 230 GLU I OE1 1 
ATOM   16999 O OE2 . GLU I  1 230 ? -4.202  4.298    -76.161 1.00 143.18 ? 230 GLU I OE2 1 
ATOM   17000 N N   . GLY I  1 231 ? -5.932  7.401    -71.345 1.00 59.81  ? 231 GLY I N   1 
ATOM   17001 C CA  . GLY I  1 231 ? -5.670  8.527    -70.470 1.00 63.23  ? 231 GLY I CA  1 
ATOM   17002 C C   . GLY I  1 231 ? -6.325  8.300    -69.122 1.00 66.97  ? 231 GLY I C   1 
ATOM   17003 O O   . GLY I  1 231 ? -7.124  7.378    -68.961 1.00 62.65  ? 231 GLY I O   1 
ATOM   17004 N N   . ARG I  1 232 ? -5.985  9.137    -68.149 1.00 60.47  ? 232 ARG I N   1 
ATOM   17005 C CA  . ARG I  1 232 ? -6.558  9.023    -66.813 1.00 56.97  ? 232 ARG I CA  1 
ATOM   17006 C C   . ARG I  1 232 ? -7.202  10.331   -66.376 1.00 59.65  ? 232 ARG I C   1 
ATOM   17007 O O   . ARG I  1 232 ? -6.959  11.383   -66.965 1.00 52.54  ? 232 ARG I O   1 
ATOM   17008 C CB  . ARG I  1 232 ? -5.490  8.603    -65.801 1.00 58.96  ? 232 ARG I CB  1 
ATOM   17009 C CG  . ARG I  1 232 ? -5.032  7.162    -65.939 1.00 53.12  ? 232 ARG I CG  1 
ATOM   17010 C CD  . ARG I  1 232 ? -6.170  6.196    -65.658 1.00 55.59  ? 232 ARG I CD  1 
ATOM   17011 N NE  . ARG I  1 232 ? -5.761  4.808    -65.841 1.00 59.82  ? 232 ARG I NE  1 
ATOM   17012 C CZ  . ARG I  1 232 ? -5.761  4.179    -67.012 1.00 68.40  ? 232 ARG I CZ  1 
ATOM   17013 N NH1 . ARG I  1 232 ? -6.147  4.816    -68.109 1.00 65.77  ? 232 ARG I NH1 1 
ATOM   17014 N NH2 . ARG I  1 232 ? -5.372  2.914    -67.086 1.00 66.11  ? 232 ARG I NH2 1 
ATOM   17015 N N   . MET I  1 233 ? -8.028  10.255   -65.338 1.00 64.94  ? 233 MET I N   1 
ATOM   17016 C CA  . MET I  1 233 ? -8.668  11.436   -64.779 1.00 56.58  ? 233 MET I CA  1 
ATOM   17017 C C   . MET I  1 233 ? -8.754  11.316   -63.262 1.00 53.23  ? 233 MET I C   1 
ATOM   17018 O O   . MET I  1 233 ? -9.520  10.510   -62.736 1.00 45.65  ? 233 MET I O   1 
ATOM   17019 C CB  . MET I  1 233 ? -10.062 11.631   -65.382 1.00 49.81  ? 233 MET I CB  1 
ATOM   17020 C CG  . MET I  1 233 ? -10.746 12.922   -64.963 1.00 54.30  ? 233 MET I CG  1 
ATOM   17021 S SD  . MET I  1 233 ? -12.325 13.178   -65.796 1.00 61.45  ? 233 MET I SD  1 
ATOM   17022 C CE  . MET I  1 233 ? -11.791 13.326   -67.500 1.00 64.75  ? 233 MET I CE  1 
ATOM   17023 N N   . ASN I  1 234 ? -7.953  12.114   -62.564 1.00 48.33  ? 234 ASN I N   1 
ATOM   17024 C CA  . ASN I  1 234 ? -7.952  12.102   -61.107 1.00 49.51  ? 234 ASN I CA  1 
ATOM   17025 C C   . ASN I  1 234 ? -9.022  13.019   -60.531 1.00 51.42  ? 234 ASN I C   1 
ATOM   17026 O O   . ASN I  1 234 ? -9.224  14.133   -61.014 1.00 48.14  ? 234 ASN I O   1 
ATOM   17027 C CB  . ASN I  1 234 ? -6.575  12.485   -60.564 1.00 48.59  ? 234 ASN I CB  1 
ATOM   17028 C CG  . ASN I  1 234 ? -5.522  11.436   -60.858 1.00 55.64  ? 234 ASN I CG  1 
ATOM   17029 O OD1 . ASN I  1 234 ? -5.821  10.378   -61.412 1.00 54.90  ? 234 ASN I OD1 1 
ATOM   17030 N ND2 . ASN I  1 234 ? -4.281  11.724   -60.486 1.00 65.73  ? 234 ASN I ND2 1 
ATOM   17031 N N   . TYR I  1 235 ? -9.704  12.543   -59.496 1.00 48.72  ? 235 TYR I N   1 
ATOM   17032 C CA  . TYR I  1 235 ? -10.796 13.294   -58.891 1.00 43.34  ? 235 TYR I CA  1 
ATOM   17033 C C   . TYR I  1 235 ? -10.415 13.818   -57.513 1.00 47.08  ? 235 TYR I C   1 
ATOM   17034 O O   . TYR I  1 235 ? -9.935  13.071   -56.661 1.00 45.57  ? 235 TYR I O   1 
ATOM   17035 C CB  . TYR I  1 235 ? -12.052 12.426   -58.810 1.00 38.24  ? 235 TYR I CB  1 
ATOM   17036 C CG  . TYR I  1 235 ? -12.412 11.787   -60.130 1.00 52.23  ? 235 TYR I CG  1 
ATOM   17037 C CD1 . TYR I  1 235 ? -11.988 10.501   -60.438 1.00 51.03  ? 235 TYR I CD1 1 
ATOM   17038 C CD2 . TYR I  1 235 ? -13.159 12.475   -61.076 1.00 49.32  ? 235 TYR I CD2 1 
ATOM   17039 C CE1 . TYR I  1 235 ? -12.308 9.915    -61.646 1.00 50.11  ? 235 TYR I CE1 1 
ATOM   17040 C CE2 . TYR I  1 235 ? -13.485 11.896   -62.287 1.00 50.18  ? 235 TYR I CE2 1 
ATOM   17041 C CZ  . TYR I  1 235 ? -13.056 10.616   -62.566 1.00 45.17  ? 235 TYR I CZ  1 
ATOM   17042 O OH  . TYR I  1 235 ? -13.375 10.034   -63.770 1.00 54.60  ? 235 TYR I OH  1 
ATOM   17043 N N   . TYR I  1 236 ? -10.630 15.112   -57.306 1.00 45.92  ? 236 TYR I N   1 
ATOM   17044 C CA  . TYR I  1 236 ? -10.287 15.755   -56.047 1.00 43.44  ? 236 TYR I CA  1 
ATOM   17045 C C   . TYR I  1 236 ? -11.506 16.418   -55.420 1.00 47.95  ? 236 TYR I C   1 
ATOM   17046 O O   . TYR I  1 236 ? -12.485 16.715   -56.103 1.00 57.23  ? 236 TYR I O   1 
ATOM   17047 C CB  . TYR I  1 236 ? -9.183  16.790   -56.263 1.00 36.96  ? 236 TYR I CB  1 
ATOM   17048 C CG  . TYR I  1 236 ? -7.885  16.200   -56.761 1.00 45.80  ? 236 TYR I CG  1 
ATOM   17049 C CD1 . TYR I  1 236 ? -7.688  15.943   -58.111 1.00 46.96  ? 236 TYR I CD1 1 
ATOM   17050 C CD2 . TYR I  1 236 ? -6.855  15.902   -55.880 1.00 53.19  ? 236 TYR I CD2 1 
ATOM   17051 C CE1 . TYR I  1 236 ? -6.501  15.404   -58.570 1.00 51.54  ? 236 TYR I CE1 1 
ATOM   17052 C CE2 . TYR I  1 236 ? -5.665  15.363   -56.330 1.00 57.89  ? 236 TYR I CE2 1 
ATOM   17053 C CZ  . TYR I  1 236 ? -5.493  15.115   -57.675 1.00 60.92  ? 236 TYR I CZ  1 
ATOM   17054 O OH  . TYR I  1 236 ? -4.309  14.578   -58.126 1.00 52.05  ? 236 TYR I OH  1 
ATOM   17055 N N   . TRP I  1 237 ? -11.437 16.647   -54.113 1.00 46.42  ? 237 TRP I N   1 
ATOM   17056 C CA  . TRP I  1 237 ? -12.531 17.278   -53.391 1.00 39.05  ? 237 TRP I CA  1 
ATOM   17057 C C   . TRP I  1 237 ? -12.007 18.043   -52.183 1.00 39.50  ? 237 TRP I C   1 
ATOM   17058 O O   . TRP I  1 237 ? -10.872 17.841   -51.752 1.00 51.51  ? 237 TRP I O   1 
ATOM   17059 C CB  . TRP I  1 237 ? -13.553 16.231   -52.944 1.00 43.75  ? 237 TRP I CB  1 
ATOM   17060 C CG  . TRP I  1 237 ? -13.005 15.236   -51.966 1.00 44.54  ? 237 TRP I CG  1 
ATOM   17061 C CD1 . TRP I  1 237 ? -12.402 14.046   -52.257 1.00 45.09  ? 237 TRP I CD1 1 
ATOM   17062 C CD2 . TRP I  1 237 ? -13.009 15.344   -50.537 1.00 48.69  ? 237 TRP I CD2 1 
ATOM   17063 N NE1 . TRP I  1 237 ? -12.031 13.407   -51.099 1.00 46.67  ? 237 TRP I NE1 1 
ATOM   17064 C CE2 . TRP I  1 237 ? -12.392 14.183   -50.028 1.00 53.39  ? 237 TRP I CE2 1 
ATOM   17065 C CE3 . TRP I  1 237 ? -13.474 16.309   -49.638 1.00 46.39  ? 237 TRP I CE3 1 
ATOM   17066 C CZ2 . TRP I  1 237 ? -12.229 13.962   -48.662 1.00 50.70  ? 237 TRP I CZ2 1 
ATOM   17067 C CZ3 . TRP I  1 237 ? -13.311 16.088   -48.283 1.00 52.43  ? 237 TRP I CZ3 1 
ATOM   17068 C CH2 . TRP I  1 237 ? -12.694 14.924   -47.808 1.00 46.99  ? 237 TRP I CH2 1 
ATOM   17069 N N   . THR I  1 238 ? -12.842 18.924   -51.644 1.00 42.30  ? 238 THR I N   1 
ATOM   17070 C CA  . THR I  1 238 ? -12.494 19.689   -50.455 1.00 47.73  ? 238 THR I CA  1 
ATOM   17071 C C   . THR I  1 238 ? -13.745 20.320   -49.855 1.00 49.65  ? 238 THR I C   1 
ATOM   17072 O O   . THR I  1 238 ? -14.761 20.471   -50.534 1.00 49.89  ? 238 THR I O   1 
ATOM   17073 C CB  . THR I  1 238 ? -11.469 20.794   -50.768 1.00 51.28  ? 238 THR I CB  1 
ATOM   17074 O OG1 . THR I  1 238 ? -11.084 21.451   -49.554 1.00 50.81  ? 238 THR I OG1 1 
ATOM   17075 C CG2 . THR I  1 238 ? -12.063 21.815   -51.725 1.00 52.57  ? 238 THR I CG2 1 
ATOM   17076 N N   . LEU I  1 239 ? -13.667 20.685   -48.581 1.00 52.11  ? 239 LEU I N   1 
ATOM   17077 C CA  . LEU I  1 239 ? -14.798 21.296   -47.896 1.00 62.24  ? 239 LEU I CA  1 
ATOM   17078 C C   . LEU I  1 239 ? -14.542 22.773   -47.619 1.00 69.05  ? 239 LEU I C   1 
ATOM   17079 O O   . LEU I  1 239 ? -13.726 23.119   -46.769 1.00 76.78  ? 239 LEU I O   1 
ATOM   17080 C CB  . LEU I  1 239 ? -15.098 20.557   -46.592 1.00 62.46  ? 239 LEU I CB  1 
ATOM   17081 C CG  . LEU I  1 239 ? -15.635 19.134   -46.749 1.00 46.59  ? 239 LEU I CG  1 
ATOM   17082 C CD1 . LEU I  1 239 ? -15.764 18.451   -45.397 1.00 63.55  ? 239 LEU I CD1 1 
ATOM   17083 C CD2 . LEU I  1 239 ? -16.970 19.151   -47.476 1.00 51.36  ? 239 LEU I CD2 1 
ATOM   17084 N N   . VAL I  1 240 ? -15.247 23.637   -48.343 1.00 62.99  ? 240 VAL I N   1 
ATOM   17085 C CA  . VAL I  1 240 ? -15.099 25.079   -48.180 1.00 65.22  ? 240 VAL I CA  1 
ATOM   17086 C C   . VAL I  1 240 ? -15.891 25.567   -46.969 1.00 58.44  ? 240 VAL I C   1 
ATOM   17087 O O   . VAL I  1 240 ? -17.106 25.380   -46.897 1.00 56.33  ? 240 VAL I O   1 
ATOM   17088 C CB  . VAL I  1 240 ? -15.579 25.835   -49.433 1.00 64.67  ? 240 VAL I CB  1 
ATOM   17089 C CG1 . VAL I  1 240 ? -15.254 27.320   -49.315 1.00 67.38  ? 240 VAL I CG1 1 
ATOM   17090 C CG2 . VAL I  1 240 ? -14.959 25.232   -50.687 1.00 55.82  ? 240 VAL I CG2 1 
ATOM   17091 N N   . GLU I  1 241 ? -15.197 26.182   -46.015 1.00 59.87  ? 241 GLU I N   1 
ATOM   17092 C CA  . GLU I  1 241 ? -15.840 26.707   -44.814 1.00 69.97  ? 241 GLU I CA  1 
ATOM   17093 C C   . GLU I  1 241 ? -16.791 27.841   -45.175 1.00 75.49  ? 241 GLU I C   1 
ATOM   17094 O O   . GLU I  1 241 ? -16.592 28.522   -46.180 1.00 78.83  ? 241 GLU I O   1 
ATOM   17095 C CB  . GLU I  1 241 ? -14.793 27.209   -43.816 1.00 83.06  ? 241 GLU I CB  1 
ATOM   17096 C CG  . GLU I  1 241 ? -13.835 26.141   -43.310 1.00 104.44 ? 241 GLU I CG  1 
ATOM   17097 C CD  . GLU I  1 241 ? -14.510 25.121   -42.413 1.00 124.93 ? 241 GLU I CD  1 
ATOM   17098 O OE1 . GLU I  1 241 ? -14.061 23.955   -42.395 1.00 128.96 ? 241 GLU I OE1 1 
ATOM   17099 O OE2 . GLU I  1 241 ? -15.488 25.483   -41.726 1.00 131.62 ? 241 GLU I OE2 1 
ATOM   17100 N N   . PRO I  1 242 ? -17.837 28.039   -44.360 1.00 85.47  ? 242 PRO I N   1 
ATOM   17101 C CA  . PRO I  1 242 ? -18.748 29.171   -44.555 1.00 84.57  ? 242 PRO I CA  1 
ATOM   17102 C C   . PRO I  1 242 ? -17.989 30.492   -44.498 1.00 85.32  ? 242 PRO I C   1 
ATOM   17103 O O   . PRO I  1 242 ? -17.224 30.719   -43.561 1.00 76.20  ? 242 PRO I O   1 
ATOM   17104 C CB  . PRO I  1 242 ? -19.701 29.059   -43.363 1.00 63.08  ? 242 PRO I CB  1 
ATOM   17105 C CG  . PRO I  1 242 ? -19.670 27.616   -42.991 1.00 74.89  ? 242 PRO I CG  1 
ATOM   17106 C CD  . PRO I  1 242 ? -18.267 27.161   -43.258 1.00 72.72  ? 242 PRO I CD  1 
ATOM   17107 N N   . GLY I  1 243 ? -18.194 31.346   -45.495 1.00 71.04  ? 243 GLY I N   1 
ATOM   17108 C CA  . GLY I  1 243 ? -17.515 32.628   -45.549 1.00 76.06  ? 243 GLY I CA  1 
ATOM   17109 C C   . GLY I  1 243 ? -16.156 32.530   -46.214 1.00 79.87  ? 243 GLY I C   1 
ATOM   17110 O O   . GLY I  1 243 ? -15.467 33.534   -46.398 1.00 93.62  ? 243 GLY I O   1 
ATOM   17111 N N   . ASP I  1 244 ? -15.770 31.310   -46.572 1.00 86.63  ? 244 ASP I N   1 
ATOM   17112 C CA  . ASP I  1 244 ? -14.506 31.064   -47.253 1.00 81.44  ? 244 ASP I CA  1 
ATOM   17113 C C   . ASP I  1 244 ? -14.753 30.964   -48.754 1.00 77.91  ? 244 ASP I C   1 
ATOM   17114 O O   . ASP I  1 244 ? -15.872 30.688   -49.184 1.00 86.75  ? 244 ASP I O   1 
ATOM   17115 C CB  . ASP I  1 244 ? -13.877 29.770   -46.730 1.00 75.20  ? 244 ASP I CB  1 
ATOM   17116 C CG  . ASP I  1 244 ? -12.446 29.579   -47.196 1.00 89.97  ? 244 ASP I CG  1 
ATOM   17117 O OD1 . ASP I  1 244 ? -11.832 28.560   -46.817 1.00 92.20  ? 244 ASP I OD1 1 
ATOM   17118 O OD2 . ASP I  1 244 ? -11.932 30.444   -47.934 1.00 82.29  ? 244 ASP I OD2 1 
ATOM   17119 N N   . LYS I  1 245 ? -13.715 31.199   -49.552 1.00 66.16  ? 245 LYS I N   1 
ATOM   17120 C CA  . LYS I  1 245 ? -13.835 31.072   -51.000 1.00 71.83  ? 245 LYS I CA  1 
ATOM   17121 C C   . LYS I  1 245 ? -12.769 30.148   -51.579 1.00 69.29  ? 245 LYS I C   1 
ATOM   17122 O O   . LYS I  1 245 ? -11.672 30.025   -51.033 1.00 70.11  ? 245 LYS I O   1 
ATOM   17123 C CB  . LYS I  1 245 ? -13.765 32.441   -51.682 1.00 81.26  ? 245 LYS I CB  1 
ATOM   17124 C CG  . LYS I  1 245 ? -12.371 33.039   -51.763 1.00 85.55  ? 245 LYS I CG  1 
ATOM   17125 C CD  . LYS I  1 245 ? -12.398 34.384   -52.476 1.00 89.00  ? 245 LYS I CD  1 
ATOM   17126 C CE  . LYS I  1 245 ? -11.003 34.970   -52.615 1.00 94.88  ? 245 LYS I CE  1 
ATOM   17127 N NZ  . LYS I  1 245 ? -11.032 36.332   -53.219 1.00 88.19  ? 245 LYS I NZ  1 
ATOM   17128 N N   . ILE I  1 246 ? -13.105 29.502   -52.690 1.00 56.08  ? 246 ILE I N   1 
ATOM   17129 C CA  . ILE I  1 246 ? -12.180 28.607   -53.371 1.00 60.61  ? 246 ILE I CA  1 
ATOM   17130 C C   . ILE I  1 246 ? -11.936 29.081   -54.802 1.00 70.68  ? 246 ILE I C   1 
ATOM   17131 O O   . ILE I  1 246 ? -12.876 29.390   -55.534 1.00 69.38  ? 246 ILE I O   1 
ATOM   17132 C CB  . ILE I  1 246 ? -12.704 27.159   -53.383 1.00 61.17  ? 246 ILE I CB  1 
ATOM   17133 C CG1 . ILE I  1 246 ? -11.714 26.237   -54.097 1.00 64.07  ? 246 ILE I CG1 1 
ATOM   17134 C CG2 . ILE I  1 246 ? -14.073 27.089   -54.038 1.00 50.37  ? 246 ILE I CG2 1 
ATOM   17135 C CD1 . ILE I  1 246 ? -12.204 24.813   -54.240 1.00 47.58  ? 246 ILE I CD1 1 
ATOM   17136 N N   . THR I  1 247 ? -10.667 29.138   -55.193 1.00 79.05  ? 247 THR I N   1 
ATOM   17137 C CA  . THR I  1 247 ? -10.292 29.648   -56.507 1.00 71.22  ? 247 THR I CA  1 
ATOM   17138 C C   . THR I  1 247 ? -9.807  28.548   -57.444 1.00 64.45  ? 247 THR I C   1 
ATOM   17139 O O   . THR I  1 247 ? -9.068  27.651   -57.038 1.00 75.08  ? 247 THR I O   1 
ATOM   17140 C CB  . THR I  1 247 ? -9.195  30.728   -56.397 1.00 79.42  ? 247 THR I CB  1 
ATOM   17141 O OG1 . THR I  1 247 ? -9.748  31.917   -55.819 1.00 92.86  ? 247 THR I OG1 1 
ATOM   17142 C CG2 . THR I  1 247 ? -8.627  31.059   -57.769 1.00 69.78  ? 247 THR I CG2 1 
ATOM   17143 N N   . PHE I  1 248 ? -10.239 28.626   -58.699 1.00 66.41  ? 248 PHE I N   1 
ATOM   17144 C CA  . PHE I  1 248 ? -9.758  27.731   -59.743 1.00 73.92  ? 248 PHE I CA  1 
ATOM   17145 C C   . PHE I  1 248 ? -8.981  28.518   -60.793 1.00 73.60  ? 248 PHE I C   1 
ATOM   17146 O O   . PHE I  1 248 ? -9.405  29.592   -61.219 1.00 76.18  ? 248 PHE I O   1 
ATOM   17147 C CB  . PHE I  1 248 ? -10.921 26.979   -60.393 1.00 57.71  ? 248 PHE I CB  1 
ATOM   17148 C CG  . PHE I  1 248 ? -11.551 25.951   -59.499 1.00 61.59  ? 248 PHE I CG  1 
ATOM   17149 C CD1 . PHE I  1 248 ? -12.488 26.321   -58.549 1.00 61.15  ? 248 PHE I CD1 1 
ATOM   17150 C CD2 . PHE I  1 248 ? -11.207 24.613   -59.608 1.00 63.33  ? 248 PHE I CD2 1 
ATOM   17151 C CE1 . PHE I  1 248 ? -13.069 25.378   -57.724 1.00 54.65  ? 248 PHE I CE1 1 
ATOM   17152 C CE2 . PHE I  1 248 ? -11.786 23.665   -58.787 1.00 61.23  ? 248 PHE I CE2 1 
ATOM   17153 C CZ  . PHE I  1 248 ? -12.717 24.048   -57.842 1.00 53.64  ? 248 PHE I CZ  1 
ATOM   17154 N N   . GLU I  1 249 ? -7.839  27.977   -61.200 1.00 71.11  ? 249 GLU I N   1 
ATOM   17155 C CA  . GLU I  1 249 ? -6.967  28.643   -62.159 1.00 69.79  ? 249 GLU I CA  1 
ATOM   17156 C C   . GLU I  1 249 ? -6.290  27.600   -63.037 1.00 65.40  ? 249 GLU I C   1 
ATOM   17157 O O   . GLU I  1 249 ? -5.497  26.794   -62.554 1.00 82.40  ? 249 GLU I O   1 
ATOM   17158 C CB  . GLU I  1 249 ? -5.921  29.478   -61.420 1.00 75.85  ? 249 GLU I CB  1 
ATOM   17159 C CG  . GLU I  1 249 ? -4.937  30.208   -62.317 1.00 92.99  ? 249 GLU I CG  1 
ATOM   17160 C CD  . GLU I  1 249 ? -3.968  31.069   -61.528 1.00 109.63 ? 249 GLU I CD  1 
ATOM   17161 O OE1 . GLU I  1 249 ? -2.872  31.367   -62.048 1.00 111.18 ? 249 GLU I OE1 1 
ATOM   17162 O OE2 . GLU I  1 249 ? -4.302  31.443   -60.383 1.00 100.56 ? 249 GLU I OE2 1 
ATOM   17163 N N   . ALA I  1 250 ? -6.605  27.612   -64.328 1.00 64.66  ? 250 ALA I N   1 
ATOM   17164 C CA  . ALA I  1 250 ? -6.111  26.573   -65.224 1.00 65.11  ? 250 ALA I CA  1 
ATOM   17165 C C   . ALA I  1 250 ? -5.773  27.074   -66.625 1.00 84.12  ? 250 ALA I C   1 
ATOM   17166 O O   . ALA I  1 250 ? -6.429  27.970   -67.158 1.00 81.61  ? 250 ALA I O   1 
ATOM   17167 C CB  . ALA I  1 250 ? -7.114  25.429   -65.302 1.00 62.66  ? 250 ALA I CB  1 
ATOM   17168 N N   . THR I  1 251 ? -4.738  26.482   -67.210 1.00 79.92  ? 251 THR I N   1 
ATOM   17169 C CA  . THR I  1 251 ? -4.403  26.707   -68.608 1.00 69.44  ? 251 THR I CA  1 
ATOM   17170 C C   . THR I  1 251 ? -4.794  25.472   -69.409 1.00 72.11  ? 251 THR I C   1 
ATOM   17171 O O   . THR I  1 251 ? -4.372  25.295   -70.552 1.00 75.14  ? 251 THR I O   1 
ATOM   17172 C CB  . THR I  1 251 ? -2.903  26.993   -68.796 1.00 65.22  ? 251 THR I CB  1 
ATOM   17173 O OG1 . THR I  1 251 ? -2.136  26.001   -68.102 1.00 84.26  ? 251 THR I OG1 1 
ATOM   17174 C CG2 . THR I  1 251 ? -2.551  28.366   -68.250 1.00 70.87  ? 251 THR I CG2 1 
ATOM   17175 N N   . GLY I  1 252 ? -5.604  24.617   -68.790 1.00 72.95  ? 252 GLY I N   1 
ATOM   17176 C CA  . GLY I  1 252 ? -6.083  23.406   -69.429 1.00 69.67  ? 252 GLY I CA  1 
ATOM   17177 C C   . GLY I  1 252 ? -6.162  22.225   -68.480 1.00 69.85  ? 252 GLY I C   1 
ATOM   17178 O O   . GLY I  1 252 ? -5.688  22.294   -67.346 1.00 71.86  ? 252 GLY I O   1 
ATOM   17179 N N   . ASN I  1 253 ? -6.775  21.141   -68.949 1.00 64.86  ? 253 ASN I N   1 
ATOM   17180 C CA  . ASN I  1 253 ? -6.818  19.881   -68.209 1.00 63.50  ? 253 ASN I CA  1 
ATOM   17181 C C   . ASN I  1 253 ? -7.698  19.906   -66.959 1.00 68.57  ? 253 ASN I C   1 
ATOM   17182 O O   . ASN I  1 253 ? -7.659  18.977   -66.152 1.00 64.08  ? 253 ASN I O   1 
ATOM   17183 C CB  . ASN I  1 253 ? -5.401  19.430   -67.836 1.00 66.68  ? 253 ASN I CB  1 
ATOM   17184 C CG  . ASN I  1 253 ? -4.483  19.330   -69.040 1.00 62.37  ? 253 ASN I CG  1 
ATOM   17185 O OD1 . ASN I  1 253 ? -4.090  18.237   -69.446 1.00 66.73  ? 253 ASN I OD1 1 
ATOM   17186 N ND2 . ASN I  1 253 ? -4.134  20.474   -69.616 1.00 63.23  ? 253 ASN I ND2 1 
ATOM   17187 N N   . LEU I  1 254 ? -8.495  20.958   -66.803 1.00 72.24  ? 254 LEU I N   1 
ATOM   17188 C CA  . LEU I  1 254 ? -9.320  21.109   -65.607 1.00 63.70  ? 254 LEU I CA  1 
ATOM   17189 C C   . LEU I  1 254 ? -10.788 20.758   -65.833 1.00 48.21  ? 254 LEU I C   1 
ATOM   17190 O O   . LEU I  1 254 ? -11.519 21.501   -66.487 1.00 64.25  ? 254 LEU I O   1 
ATOM   17191 C CB  . LEU I  1 254 ? -9.212  22.532   -65.053 1.00 62.23  ? 254 LEU I CB  1 
ATOM   17192 C CG  . LEU I  1 254 ? -10.129 22.854   -63.869 1.00 57.50  ? 254 LEU I CG  1 
ATOM   17193 C CD1 . LEU I  1 254 ? -9.858  21.920   -62.700 1.00 64.38  ? 254 LEU I CD1 1 
ATOM   17194 C CD2 . LEU I  1 254 ? -9.977  24.305   -63.440 1.00 55.93  ? 254 LEU I CD2 1 
ATOM   17195 N N   . VAL I  1 255 ? -11.212 19.623   -65.286 1.00 52.76  ? 255 VAL I N   1 
ATOM   17196 C CA  . VAL I  1 255 ? -12.626 19.271   -65.260 1.00 44.00  ? 255 VAL I CA  1 
ATOM   17197 C C   . VAL I  1 255 ? -13.293 20.062   -64.141 1.00 55.73  ? 255 VAL I C   1 
ATOM   17198 O O   . VAL I  1 255 ? -13.276 19.651   -62.981 1.00 53.91  ? 255 VAL I O   1 
ATOM   17199 C CB  . VAL I  1 255 ? -12.835 17.766   -65.018 1.00 46.85  ? 255 VAL I CB  1 
ATOM   17200 C CG1 . VAL I  1 255 ? -14.319 17.435   -64.979 1.00 50.62  ? 255 VAL I CG1 1 
ATOM   17201 C CG2 . VAL I  1 255 ? -12.134 16.953   -66.095 1.00 45.89  ? 255 VAL I CG2 1 
ATOM   17202 N N   . VAL I  1 256 ? -13.872 21.204   -64.498 1.00 56.90  ? 256 VAL I N   1 
ATOM   17203 C CA  . VAL I  1 256 ? -14.391 22.146   -63.513 1.00 50.84  ? 256 VAL I CA  1 
ATOM   17204 C C   . VAL I  1 256 ? -15.673 21.667   -62.840 1.00 58.69  ? 256 VAL I C   1 
ATOM   17205 O O   . VAL I  1 256 ? -16.441 20.902   -63.423 1.00 59.78  ? 256 VAL I O   1 
ATOM   17206 C CB  . VAL I  1 256 ? -14.649 23.529   -64.143 1.00 63.52  ? 256 VAL I CB  1 
ATOM   17207 C CG1 . VAL I  1 256 ? -13.375 24.070   -64.771 1.00 72.98  ? 256 VAL I CG1 1 
ATOM   17208 C CG2 . VAL I  1 256 ? -15.763 23.442   -65.174 1.00 70.80  ? 256 VAL I CG2 1 
ATOM   17209 N N   . PRO I  1 257 ? -15.902 22.119   -61.599 1.00 52.90  ? 257 PRO I N   1 
ATOM   17210 C CA  . PRO I  1 257 ? -17.142 21.830   -60.875 1.00 51.16  ? 257 PRO I CA  1 
ATOM   17211 C C   . PRO I  1 257 ? -18.318 22.538   -61.530 1.00 67.01  ? 257 PRO I C   1 
ATOM   17212 O O   . PRO I  1 257 ? -18.162 23.656   -62.018 1.00 72.31  ? 257 PRO I O   1 
ATOM   17213 C CB  . PRO I  1 257 ? -16.893 22.442   -59.491 1.00 48.16  ? 257 PRO I CB  1 
ATOM   17214 C CG  . PRO I  1 257 ? -15.416 22.605   -59.388 1.00 55.37  ? 257 PRO I CG  1 
ATOM   17215 C CD  . PRO I  1 257 ? -14.947 22.880   -60.776 1.00 56.75  ? 257 PRO I CD  1 
ATOM   17216 N N   . ARG I  1 258 ? -19.477 21.891   -61.544 1.00 71.02  ? 258 ARG I N   1 
ATOM   17217 C CA  . ARG I  1 258 ? -20.697 22.534   -62.012 1.00 64.37  ? 258 ARG I CA  1 
ATOM   17218 C C   . ARG I  1 258 ? -21.695 22.607   -60.858 1.00 60.84  ? 258 ARG I C   1 
ATOM   17219 O O   . ARG I  1 258 ? -22.305 23.648   -60.617 1.00 65.25  ? 258 ARG I O   1 
ATOM   17220 C CB  . ARG I  1 258 ? -21.279 21.785   -63.216 1.00 60.24  ? 258 ARG I CB  1 
ATOM   17221 C CG  . ARG I  1 258 ? -22.652 22.268   -63.668 1.00 67.62  ? 258 ARG I CG  1 
ATOM   17222 C CD  . ARG I  1 258 ? -23.209 21.379   -64.774 1.00 68.73  ? 258 ARG I CD  1 
ATOM   17223 N NE  . ARG I  1 258 ? -24.663 21.473   -64.877 1.00 81.43  ? 258 ARG I NE  1 
ATOM   17224 C CZ  . ARG I  1 258 ? -25.307 22.255   -65.737 1.00 92.64  ? 258 ARG I CZ  1 
ATOM   17225 N NH1 . ARG I  1 258 ? -24.628 23.016   -66.582 1.00 96.61  ? 258 ARG I NH1 1 
ATOM   17226 N NH2 . ARG I  1 258 ? -26.633 22.274   -65.755 1.00 89.41  ? 258 ARG I NH2 1 
ATOM   17227 N N   . TYR I  1 259 ? -21.837 21.500   -60.135 1.00 67.78  ? 259 TYR I N   1 
ATOM   17228 C CA  . TYR I  1 259 ? -22.681 21.453   -58.945 1.00 57.87  ? 259 TYR I CA  1 
ATOM   17229 C C   . TYR I  1 259 ? -21.848 21.168   -57.698 1.00 57.71  ? 259 TYR I C   1 
ATOM   17230 O O   . TYR I  1 259 ? -20.989 20.288   -57.702 1.00 50.77  ? 259 TYR I O   1 
ATOM   17231 C CB  . TYR I  1 259 ? -23.764 20.377   -59.080 1.00 60.91  ? 259 TYR I CB  1 
ATOM   17232 C CG  . TYR I  1 259 ? -24.886 20.706   -60.044 1.00 74.15  ? 259 TYR I CG  1 
ATOM   17233 C CD1 . TYR I  1 259 ? -24.811 20.339   -61.379 1.00 77.41  ? 259 TYR I CD1 1 
ATOM   17234 C CD2 . TYR I  1 259 ? -26.030 21.362   -59.612 1.00 76.81  ? 259 TYR I CD2 1 
ATOM   17235 C CE1 . TYR I  1 259 ? -25.827 20.626   -62.262 1.00 90.04  ? 259 TYR I CE1 1 
ATOM   17236 C CE2 . TYR I  1 259 ? -27.060 21.653   -60.492 1.00 85.90  ? 259 TYR I CE2 1 
ATOM   17237 C CZ  . TYR I  1 259 ? -26.950 21.282   -61.817 1.00 90.02  ? 259 TYR I CZ  1 
ATOM   17238 O OH  . TYR I  1 259 ? -27.963 21.563   -62.704 1.00 97.10  ? 259 TYR I OH  1 
ATOM   17239 N N   . ALA I  1 260 ? -22.107 21.919   -56.633 1.00 65.85  ? 260 ALA I N   1 
ATOM   17240 C CA  . ALA I  1 260 ? -21.479 21.661   -55.345 1.00 52.67  ? 260 ALA I CA  1 
ATOM   17241 C C   . ALA I  1 260 ? -22.547 21.181   -54.375 1.00 58.72  ? 260 ALA I C   1 
ATOM   17242 O O   . ALA I  1 260 ? -23.694 20.970   -54.768 1.00 56.31  ? 260 ALA I O   1 
ATOM   17243 C CB  . ALA I  1 260 ? -20.800 22.912   -54.820 1.00 50.99  ? 260 ALA I CB  1 
ATOM   17244 N N   . PHE I  1 261 ? -22.181 21.011   -53.111 1.00 66.51  ? 261 PHE I N   1 
ATOM   17245 C CA  . PHE I  1 261 ? -23.130 20.509   -52.127 1.00 51.85  ? 261 PHE I CA  1 
ATOM   17246 C C   . PHE I  1 261 ? -23.055 21.258   -50.802 1.00 51.80  ? 261 PHE I C   1 
ATOM   17247 O O   . PHE I  1 261 ? -22.087 21.117   -50.055 1.00 58.06  ? 261 PHE I O   1 
ATOM   17248 C CB  . PHE I  1 261 ? -22.915 19.011   -51.894 1.00 42.82  ? 261 PHE I CB  1 
ATOM   17249 C CG  . PHE I  1 261 ? -23.057 18.177   -53.136 1.00 46.87  ? 261 PHE I CG  1 
ATOM   17250 C CD1 . PHE I  1 261 ? -21.954 17.881   -53.920 1.00 51.11  ? 261 PHE I CD1 1 
ATOM   17251 C CD2 . PHE I  1 261 ? -24.294 17.687   -53.519 1.00 45.39  ? 261 PHE I CD2 1 
ATOM   17252 C CE1 . PHE I  1 261 ? -22.083 17.112   -55.062 1.00 50.32  ? 261 PHE I CE1 1 
ATOM   17253 C CE2 . PHE I  1 261 ? -24.429 16.917   -54.659 1.00 46.08  ? 261 PHE I CE2 1 
ATOM   17254 C CZ  . PHE I  1 261 ? -23.322 16.630   -55.431 1.00 54.08  ? 261 PHE I CZ  1 
ATOM   17255 N N   . ALA I  1 262 ? -24.076 22.060   -50.518 1.00 65.05  ? 262 ALA I N   1 
ATOM   17256 C CA  . ALA I  1 262 ? -24.218 22.656   -49.198 1.00 64.18  ? 262 ALA I CA  1 
ATOM   17257 C C   . ALA I  1 262 ? -24.515 21.519   -48.234 1.00 63.22  ? 262 ALA I C   1 
ATOM   17258 O O   . ALA I  1 262 ? -25.453 20.748   -48.440 1.00 62.92  ? 262 ALA I O   1 
ATOM   17259 C CB  . ALA I  1 262 ? -25.331 23.681   -49.185 1.00 68.99  ? 262 ALA I CB  1 
ATOM   17260 N N   . MET I  1 263 ? -23.710 21.409   -47.185 1.00 52.80  ? 263 MET I N   1 
ATOM   17261 C CA  . MET I  1 263 ? -23.706 20.197   -46.380 1.00 65.49  ? 263 MET I CA  1 
ATOM   17262 C C   . MET I  1 263 ? -23.441 20.455   -44.903 1.00 65.90  ? 263 MET I C   1 
ATOM   17263 O O   . MET I  1 263 ? -22.489 21.144   -44.540 1.00 75.52  ? 263 MET I O   1 
ATOM   17264 C CB  . MET I  1 263 ? -22.658 19.228   -46.930 1.00 61.79  ? 263 MET I CB  1 
ATOM   17265 C CG  . MET I  1 263 ? -22.681 17.848   -46.306 1.00 62.70  ? 263 MET I CG  1 
ATOM   17266 S SD  . MET I  1 263 ? -21.343 16.810   -46.923 1.00 86.10  ? 263 MET I SD  1 
ATOM   17267 C CE  . MET I  1 263 ? -19.915 17.674   -46.274 1.00 69.79  ? 263 MET I CE  1 
ATOM   17268 N N   . GLU I  1 264 ? -24.295 19.889   -44.059 1.00 65.64  ? 264 GLU I N   1 
ATOM   17269 C CA  . GLU I  1 264 ? -24.085 19.906   -42.621 1.00 73.52  ? 264 GLU I CA  1 
ATOM   17270 C C   . GLU I  1 264 ? -24.008 18.471   -42.130 1.00 65.20  ? 264 GLU I C   1 
ATOM   17271 O O   . GLU I  1 264 ? -24.967 17.709   -42.251 1.00 74.80  ? 264 GLU I O   1 
ATOM   17272 C CB  . GLU I  1 264 ? -25.215 20.652   -41.916 1.00 75.49  ? 264 GLU I CB  1 
ATOM   17273 C CG  . GLU I  1 264 ? -24.771 21.939   -41.241 1.00 99.28  ? 264 GLU I CG  1 
ATOM   17274 C CD  . GLU I  1 264 ? -25.920 22.894   -41.000 1.00 115.41 ? 264 GLU I CD  1 
ATOM   17275 O OE1 . GLU I  1 264 ? -25.954 23.529   -39.927 1.00 112.27 ? 264 GLU I OE1 1 
ATOM   17276 O OE2 . GLU I  1 264 ? -26.796 23.004   -41.882 1.00 113.97 ? 264 GLU I OE2 1 
ATOM   17277 N N   . ARG I  1 265 ? -22.859 18.107   -41.575 1.00 71.59  ? 265 ARG I N   1 
ATOM   17278 C CA  . ARG I  1 265 ? -22.599 16.720   -41.217 1.00 80.43  ? 265 ARG I CA  1 
ATOM   17279 C C   . ARG I  1 265 ? -22.570 16.470   -39.711 1.00 77.65  ? 265 ARG I C   1 
ATOM   17280 O O   . ARG I  1 265 ? -22.241 17.357   -38.922 1.00 67.06  ? 265 ARG I O   1 
ATOM   17281 C CB  . ARG I  1 265 ? -21.298 16.244   -41.874 1.00 58.51  ? 265 ARG I CB  1 
ATOM   17282 C CG  . ARG I  1 265 ? -20.169 17.264   -41.833 1.00 62.17  ? 265 ARG I CG  1 
ATOM   17283 C CD  . ARG I  1 265 ? -19.081 16.954   -42.856 1.00 75.54  ? 265 ARG I CD  1 
ATOM   17284 N NE  . ARG I  1 265 ? -17.765 16.814   -42.237 1.00 77.08  ? 265 ARG I NE  1 
ATOM   17285 C CZ  . ARG I  1 265 ? -16.966 17.827   -41.910 1.00 79.13  ? 265 ARG I CZ  1 
ATOM   17286 N NH1 . ARG I  1 265 ? -17.337 19.077   -42.130 1.00 82.91  ? 265 ARG I NH1 1 
ATOM   17287 N NH2 . ARG I  1 265 ? -15.789 17.583   -41.352 1.00 87.70  ? 265 ARG I NH2 1 
ATOM   17288 N N   . ASN I  1 266 ? -22.950 15.257   -39.325 1.00 71.67  ? 266 ASN I N   1 
ATOM   17289 C CA  . ASN I  1 266 ? -22.806 14.799   -37.952 1.00 86.31  ? 266 ASN I CA  1 
ATOM   17290 C C   . ASN I  1 266 ? -21.923 13.561   -37.924 1.00 93.54  ? 266 ASN I C   1 
ATOM   17291 O O   . ASN I  1 266 ? -22.161 12.604   -38.658 1.00 100.46 ? 266 ASN I O   1 
ATOM   17292 C CB  . ASN I  1 266 ? -24.170 14.507   -37.323 1.00 92.95  ? 266 ASN I CB  1 
ATOM   17293 C CG  . ASN I  1 266 ? -25.230 14.173   -38.355 1.00 88.36  ? 266 ASN I CG  1 
ATOM   17294 O OD1 . ASN I  1 266 ? -26.267 14.831   -38.427 1.00 80.14  ? 266 ASN I OD1 1 
ATOM   17295 N ND2 . ASN I  1 266 ? -24.973 13.150   -39.163 1.00 84.50  ? 266 ASN I ND2 1 
ATOM   17296 N N   . ALA I  1 267 ? -20.895 13.588   -37.085 1.00 83.80  ? 267 ALA I N   1 
ATOM   17297 C CA  . ALA I  1 267 ? -19.920 12.505   -37.048 1.00 97.98  ? 267 ALA I CA  1 
ATOM   17298 C C   . ALA I  1 267 ? -20.513 11.230   -36.464 1.00 90.71  ? 267 ALA I C   1 
ATOM   17299 O O   . ALA I  1 267 ? -21.469 11.279   -35.691 1.00 81.46  ? 267 ALA I O   1 
ATOM   17300 C CB  . ALA I  1 267 ? -18.697 12.927   -36.251 1.00 101.59 ? 267 ALA I CB  1 
ATOM   17301 N N   . GLY I  1 268 ? -19.948 10.089   -36.845 1.00 93.62  ? 268 GLY I N   1 
ATOM   17302 C CA  . GLY I  1 268 ? -20.286 8.831    -36.206 1.00 99.12  ? 268 GLY I CA  1 
ATOM   17303 C C   . GLY I  1 268 ? -21.365 7.978    -36.850 1.00 97.43  ? 268 GLY I C   1 
ATOM   17304 O O   . GLY I  1 268 ? -22.306 7.558    -36.179 1.00 96.46  ? 268 GLY I O   1 
ATOM   17305 N N   . SER I  1 269 ? -21.233 7.714    -38.145 1.00 71.85  ? 269 SER I N   1 
ATOM   17306 C CA  . SER I  1 269 ? -22.082 6.727    -38.805 1.00 62.52  ? 269 SER I CA  1 
ATOM   17307 C C   . SER I  1 269 ? -21.221 5.812    -39.664 1.00 63.02  ? 269 SER I C   1 
ATOM   17308 O O   . SER I  1 269 ? -20.020 5.686    -39.430 1.00 74.11  ? 269 SER I O   1 
ATOM   17309 C CB  . SER I  1 269 ? -23.164 7.394    -39.652 1.00 59.05  ? 269 SER I CB  1 
ATOM   17310 O OG  . SER I  1 269 ? -24.057 6.428    -40.182 1.00 58.91  ? 269 SER I OG  1 
ATOM   17311 N N   . GLY I  1 270 ? -21.829 5.176    -40.658 1.00 41.88  ? 270 GLY I N   1 
ATOM   17312 C CA  . GLY I  1 270 ? -21.091 4.267    -41.512 1.00 51.83  ? 270 GLY I CA  1 
ATOM   17313 C C   . GLY I  1 270 ? -21.770 3.958    -42.829 1.00 36.95  ? 270 GLY I C   1 
ATOM   17314 O O   . GLY I  1 270 ? -22.757 4.591    -43.204 1.00 41.25  ? 270 GLY I O   1 
ATOM   17315 N N   . ILE I  1 271 ? -21.227 2.970    -43.530 1.00 45.09  ? 271 ILE I N   1 
ATOM   17316 C CA  . ILE I  1 271 ? -21.739 2.570    -44.830 1.00 34.63  ? 271 ILE I CA  1 
ATOM   17317 C C   . ILE I  1 271 ? -21.920 1.059    -44.869 1.00 41.37  ? 271 ILE I C   1 
ATOM   17318 O O   . ILE I  1 271 ? -20.959 0.305    -44.715 1.00 61.59  ? 271 ILE I O   1 
ATOM   17319 C CB  . ILE I  1 271 ? -20.780 2.999    -45.951 1.00 36.56  ? 271 ILE I CB  1 
ATOM   17320 C CG1 . ILE I  1 271 ? -20.594 4.517    -45.928 1.00 37.58  ? 271 ILE I CG1 1 
ATOM   17321 C CG2 . ILE I  1 271 ? -21.296 2.532    -47.304 1.00 49.89  ? 271 ILE I CG2 1 
ATOM   17322 C CD1 . ILE I  1 271 ? -19.307 4.986    -46.561 1.00 51.16  ? 271 ILE I CD1 1 
ATOM   17323 N N   . ILE I  1 272 ? -23.158 0.623    -45.069 1.00 43.80  ? 272 ILE I N   1 
ATOM   17324 C CA  . ILE I  1 272 ? -23.467 -0.799   -45.107 1.00 48.39  ? 272 ILE I CA  1 
ATOM   17325 C C   . ILE I  1 272 ? -23.572 -1.308   -46.539 1.00 48.54  ? 272 ILE I C   1 
ATOM   17326 O O   . ILE I  1 272 ? -24.352 -0.788   -47.336 1.00 52.01  ? 272 ILE I O   1 
ATOM   17327 C CB  . ILE I  1 272 ? -24.782 -1.109   -44.370 1.00 41.29  ? 272 ILE I CB  1 
ATOM   17328 C CG1 . ILE I  1 272 ? -24.658 -0.760   -42.885 1.00 39.85  ? 272 ILE I CG1 1 
ATOM   17329 C CG2 . ILE I  1 272 ? -25.151 -2.570   -44.539 1.00 58.18  ? 272 ILE I CG2 1 
ATOM   17330 C CD1 . ILE I  1 272 ? -25.860 -1.169   -42.062 1.00 55.58  ? 272 ILE I CD1 1 
ATOM   17331 N N   . ILE I  1 273 ? -22.778 -2.323   -46.862 1.00 43.35  ? 273 ILE I N   1 
ATOM   17332 C CA  . ILE I  1 273 ? -22.866 -2.973   -48.163 1.00 52.22  ? 273 ILE I CA  1 
ATOM   17333 C C   . ILE I  1 273 ? -23.730 -4.222   -48.042 1.00 58.45  ? 273 ILE I C   1 
ATOM   17334 O O   . ILE I  1 273 ? -23.275 -5.259   -47.559 1.00 77.68  ? 273 ILE I O   1 
ATOM   17335 C CB  . ILE I  1 273 ? -21.480 -3.352   -48.720 1.00 49.72  ? 273 ILE I CB  1 
ATOM   17336 C CG1 . ILE I  1 273 ? -20.607 -2.106   -48.897 1.00 56.54  ? 273 ILE I CG1 1 
ATOM   17337 C CG2 . ILE I  1 273 ? -21.624 -4.083   -50.046 1.00 62.35  ? 273 ILE I CG2 1 
ATOM   17338 C CD1 . ILE I  1 273 ? -19.963 -1.610   -47.618 1.00 76.59  ? 273 ILE I CD1 1 
ATOM   17339 N N   . SER I  1 274 ? -24.980 -4.114   -48.479 1.00 62.37  ? 274 SER I N   1 
ATOM   17340 C CA  . SER I  1 274 ? -25.943 -5.194   -48.313 1.00 63.59  ? 274 SER I CA  1 
ATOM   17341 C C   . SER I  1 274 ? -26.993 -5.216   -49.420 1.00 73.98  ? 274 SER I C   1 
ATOM   17342 O O   . SER I  1 274 ? -27.288 -4.191   -50.034 1.00 66.22  ? 274 SER I O   1 
ATOM   17343 C CB  . SER I  1 274 ? -26.630 -5.076   -46.951 1.00 57.75  ? 274 SER I CB  1 
ATOM   17344 O OG  . SER I  1 274 ? -27.825 -5.834   -46.916 1.00 68.36  ? 274 SER I OG  1 
ATOM   17345 N N   . ASP I  1 275 ? -27.552 -6.397   -49.667 1.00 90.55  ? 275 ASP I N   1 
ATOM   17346 C CA  . ASP I  1 275 ? -28.632 -6.556   -50.632 1.00 83.69  ? 275 ASP I CA  1 
ATOM   17347 C C   . ASP I  1 275 ? -29.970 -6.339   -49.939 1.00 73.70  ? 275 ASP I C   1 
ATOM   17348 O O   . ASP I  1 275 ? -30.976 -6.038   -50.582 1.00 99.07  ? 275 ASP I O   1 
ATOM   17349 C CB  . ASP I  1 275 ? -28.596 -7.956   -51.250 1.00 108.37 ? 275 ASP I CB  1 
ATOM   17350 C CG  . ASP I  1 275 ? -27.298 -8.240   -51.982 1.00 125.74 ? 275 ASP I CG  1 
ATOM   17351 O OD1 . ASP I  1 275 ? -26.446 -8.965   -51.425 1.00 136.07 ? 275 ASP I OD1 1 
ATOM   17352 O OD2 . ASP I  1 275 ? -27.131 -7.742   -53.115 1.00 114.27 ? 275 ASP I OD2 1 
ATOM   17353 N N   . THR I  1 276 ? -29.965 -6.494   -48.618 1.00 61.71  ? 276 THR I N   1 
ATOM   17354 C CA  . THR I  1 276 ? -31.171 -6.391   -47.799 1.00 65.79  ? 276 THR I CA  1 
ATOM   17355 C C   . THR I  1 276 ? -32.059 -5.212   -48.186 1.00 66.75  ? 276 THR I C   1 
ATOM   17356 O O   . THR I  1 276 ? -31.567 -4.113   -48.443 1.00 64.23  ? 276 THR I O   1 
ATOM   17357 C CB  . THR I  1 276 ? -30.819 -6.281   -46.301 1.00 57.90  ? 276 THR I CB  1 
ATOM   17358 O OG1 . THR I  1 276 ? -30.051 -7.424   -45.902 1.00 59.02  ? 276 THR I OG1 1 
ATOM   17359 C CG2 . THR I  1 276 ? -32.081 -6.199   -45.452 1.00 58.05  ? 276 THR I CG2 1 
ATOM   17360 N N   . PRO I  1 277 ? -33.379 -5.447   -48.232 1.00 77.89  ? 277 PRO I N   1 
ATOM   17361 C CA  . PRO I  1 277 ? -34.389 -4.436   -48.566 1.00 74.28  ? 277 PRO I CA  1 
ATOM   17362 C C   . PRO I  1 277 ? -34.406 -3.242   -47.616 1.00 67.05  ? 277 PRO I C   1 
ATOM   17363 O O   . PRO I  1 277 ? -34.385 -3.418   -46.397 1.00 69.29  ? 277 PRO I O   1 
ATOM   17364 C CB  . PRO I  1 277 ? -35.705 -5.210   -48.438 1.00 74.07  ? 277 PRO I CB  1 
ATOM   17365 C CG  . PRO I  1 277 ? -35.336 -6.623   -48.692 1.00 88.12  ? 277 PRO I CG  1 
ATOM   17366 C CD  . PRO I  1 277 ? -33.970 -6.790   -48.099 1.00 73.44  ? 277 PRO I CD  1 
ATOM   17367 N N   . VAL I  1 278 ? -34.444 -2.036   -48.176 1.00 70.68  ? 278 VAL I N   1 
ATOM   17368 C CA  . VAL I  1 278 ? -34.677 -0.840   -47.376 1.00 67.05  ? 278 VAL I CA  1 
ATOM   17369 C C   . VAL I  1 278 ? -36.154 -0.800   -47.000 1.00 70.28  ? 278 VAL I C   1 
ATOM   17370 O O   . VAL I  1 278 ? -37.013 -1.174   -47.799 1.00 82.07  ? 278 VAL I O   1 
ATOM   17371 C CB  . VAL I  1 278 ? -34.289 0.449    -48.129 1.00 68.23  ? 278 VAL I CB  1 
ATOM   17372 C CG1 . VAL I  1 278 ? -34.993 0.519    -49.475 1.00 88.01  ? 278 VAL I CG1 1 
ATOM   17373 C CG2 . VAL I  1 278 ? -34.611 1.673    -47.284 1.00 52.41  ? 278 VAL I CG2 1 
ATOM   17374 N N   . HIS I  1 279 ? -36.448 -0.361   -45.780 1.00 74.94  ? 279 HIS I N   1 
ATOM   17375 C CA  . HIS I  1 279 ? -37.816 -0.403   -45.270 1.00 75.71  ? 279 HIS I CA  1 
ATOM   17376 C C   . HIS I  1 279 ? -38.232 0.871    -44.534 1.00 77.51  ? 279 HIS I C   1 
ATOM   17377 O O   . HIS I  1 279 ? -37.391 1.626    -44.049 1.00 89.03  ? 279 HIS I O   1 
ATOM   17378 C CB  . HIS I  1 279 ? -38.007 -1.623   -44.363 1.00 85.00  ? 279 HIS I CB  1 
ATOM   17379 C CG  . HIS I  1 279 ? -38.726 -2.758   -45.019 1.00 91.30  ? 279 HIS I CG  1 
ATOM   17380 N ND1 . HIS I  1 279 ? -40.054 -3.039   -44.775 1.00 89.73  ? 279 HIS I ND1 1 
ATOM   17381 C CD2 . HIS I  1 279 ? -38.308 -3.681   -45.920 1.00 97.47  ? 279 HIS I CD2 1 
ATOM   17382 C CE1 . HIS I  1 279 ? -40.420 -4.085   -45.493 1.00 110.26 ? 279 HIS I CE1 1 
ATOM   17383 N NE2 . HIS I  1 279 ? -39.382 -4.493   -46.196 1.00 100.56 ? 279 HIS I NE2 1 
ATOM   17384 N N   . ASP I  1 280 ? -39.540 1.097    -44.461 1.00 84.06  ? 280 ASP I N   1 
ATOM   17385 C CA  . ASP I  1 280 ? -40.099 2.233    -43.741 1.00 98.26  ? 280 ASP I CA  1 
ATOM   17386 C C   . ASP I  1 280 ? -40.529 1.798    -42.343 1.00 92.10  ? 280 ASP I C   1 
ATOM   17387 O O   . ASP I  1 280 ? -41.707 1.549    -42.087 1.00 113.64 ? 280 ASP I O   1 
ATOM   17388 C CB  . ASP I  1 280 ? -41.269 2.840    -44.530 1.00 118.21 ? 280 ASP I CB  1 
ATOM   17389 C CG  . ASP I  1 280 ? -42.249 3.605    -43.656 1.00 126.11 ? 280 ASP I CG  1 
ATOM   17390 O OD1 . ASP I  1 280 ? -41.814 4.318    -42.727 1.00 114.46 ? 280 ASP I OD1 1 
ATOM   17391 O OD2 . ASP I  1 280 ? -43.466 3.503    -43.919 1.00 127.82 ? 280 ASP I OD2 1 
ATOM   17392 N N   . CYS I  1 281 ? -39.552 1.681    -41.449 1.00 83.83  ? 281 CYS I N   1 
ATOM   17393 C CA  . CYS I  1 281 ? -39.822 1.349    -40.054 1.00 84.88  ? 281 CYS I CA  1 
ATOM   17394 C C   . CYS I  1 281 ? -38.760 1.979    -39.158 1.00 75.00  ? 281 CYS I C   1 
ATOM   17395 O O   . CYS I  1 281 ? -37.973 2.811    -39.603 1.00 83.88  ? 281 CYS I O   1 
ATOM   17396 C CB  . CYS I  1 281 ? -39.897 -0.181   -39.854 1.00 75.64  ? 281 CYS I CB  1 
ATOM   17397 S SG  . CYS I  1 281 ? -38.320 -1.024   -39.422 1.00 115.16 ? 281 CYS I SG  1 
ATOM   17398 N N   . ASN I  1 282 ? -38.732 1.570    -37.898 1.00 73.03  ? 282 ASN I N   1 
ATOM   17399 C CA  . ASN I  1 282 ? -37.777 2.131    -36.953 1.00 64.74  ? 282 ASN I CA  1 
ATOM   17400 C C   . ASN I  1 282 ? -36.849 1.085    -36.337 1.00 75.22  ? 282 ASN I C   1 
ATOM   17401 O O   . ASN I  1 282 ? -37.223 -0.077   -36.181 1.00 81.02  ? 282 ASN I O   1 
ATOM   17402 C CB  . ASN I  1 282 ? -38.504 2.891    -35.852 1.00 75.33  ? 282 ASN I CB  1 
ATOM   17403 C CG  . ASN I  1 282 ? -38.097 4.349    -35.782 1.00 91.99  ? 282 ASN I CG  1 
ATOM   17404 O OD1 . ASN I  1 282 ? -37.078 4.756    -36.345 1.00 94.77  ? 282 ASN I OD1 1 
ATOM   17405 N ND2 . ASN I  1 282 ? -38.896 5.146    -35.084 1.00 110.18 ? 282 ASN I ND2 1 
ATOM   17406 N N   . THR I  1 283 ? -35.631 1.503    -36.004 1.00 66.17  ? 283 THR I N   1 
ATOM   17407 C CA  . THR I  1 283 ? -34.685 0.641    -35.307 1.00 60.19  ? 283 THR I CA  1 
ATOM   17408 C C   . THR I  1 283 ? -33.669 1.479    -34.544 1.00 52.59  ? 283 THR I C   1 
ATOM   17409 O O   . THR I  1 283 ? -33.436 2.640    -34.873 1.00 55.76  ? 283 THR I O   1 
ATOM   17410 C CB  . THR I  1 283 ? -33.933 -0.292   -36.273 1.00 58.64  ? 283 THR I CB  1 
ATOM   17411 O OG1 . THR I  1 283 ? -33.234 -1.296   -35.525 1.00 46.95  ? 283 THR I OG1 1 
ATOM   17412 C CG2 . THR I  1 283 ? -32.942 0.495    -37.116 1.00 55.38  ? 283 THR I CG2 1 
ATOM   17413 N N   . THR I  1 284 ? -33.068 0.879    -33.522 1.00 51.56  ? 284 THR I N   1 
ATOM   17414 C CA  . THR I  1 284 ? -32.033 1.544    -32.738 1.00 57.72  ? 284 THR I CA  1 
ATOM   17415 C C   . THR I  1 284 ? -30.680 0.899    -32.998 1.00 49.34  ? 284 THR I C   1 
ATOM   17416 O O   . THR I  1 284 ? -29.640 1.420    -32.594 1.00 37.89  ? 284 THR I O   1 
ATOM   17417 C CB  . THR I  1 284 ? -32.322 1.461    -31.232 1.00 51.40  ? 284 THR I CB  1 
ATOM   17418 O OG1 . THR I  1 284 ? -31.397 2.296    -30.523 1.00 48.86  ? 284 THR I OG1 1 
ATOM   17419 C CG2 . THR I  1 284 ? -32.180 0.024    -30.743 1.00 58.05  ? 284 THR I CG2 1 
ATOM   17420 N N   . CYS I  1 285 ? -30.701 -0.248   -33.666 1.00 44.59  ? 285 CYS I N   1 
ATOM   17421 C CA  . CYS I  1 285 ? -29.474 -0.939   -34.024 1.00 33.74  ? 285 CYS I CA  1 
ATOM   17422 C C   . CYS I  1 285 ? -29.603 -1.533   -35.418 1.00 36.29  ? 285 CYS I C   1 
ATOM   17423 O O   . CYS I  1 285 ? -30.531 -2.293   -35.694 1.00 43.95  ? 285 CYS I O   1 
ATOM   17424 C CB  . CYS I  1 285 ? -29.163 -2.039   -33.008 1.00 36.84  ? 285 CYS I CB  1 
ATOM   17425 S SG  . CYS I  1 285 ? -27.693 -3.021   -33.393 1.00 62.17  ? 285 CYS I SG  1 
ATOM   17426 N N   . GLN I  1 286 ? -28.669 -1.187   -36.296 1.00 36.55  ? 286 GLN I N   1 
ATOM   17427 C CA  . GLN I  1 286 ? -28.703 -1.682   -37.665 1.00 38.16  ? 286 GLN I CA  1 
ATOM   17428 C C   . GLN I  1 286 ? -27.519 -2.604   -37.995 1.00 39.51  ? 286 GLN I C   1 
ATOM   17429 O O   . GLN I  1 286 ? -26.371 -2.295   -37.674 1.00 38.68  ? 286 GLN I O   1 
ATOM   17430 C CB  . GLN I  1 286 ? -28.739 -0.497   -38.630 1.00 32.64  ? 286 GLN I CB  1 
ATOM   17431 C CG  . GLN I  1 286 ? -29.203 -0.847   -40.021 1.00 30.22  ? 286 GLN I CG  1 
ATOM   17432 C CD  . GLN I  1 286 ? -30.585 -1.441   -40.015 1.00 45.05  ? 286 GLN I CD  1 
ATOM   17433 O OE1 . GLN I  1 286 ? -31.534 -0.815   -39.555 1.00 46.54  ? 286 GLN I OE1 1 
ATOM   17434 N NE2 . GLN I  1 286 ? -30.708 -2.657   -40.522 1.00 40.73  ? 286 GLN I NE2 1 
ATOM   17435 N N   . THR I  1 287 ? -27.816 -3.751   -38.606 1.00 38.29  ? 287 THR I N   1 
ATOM   17436 C CA  . THR I  1 287 ? -26.796 -4.619   -39.194 1.00 34.59  ? 287 THR I CA  1 
ATOM   17437 C C   . THR I  1 287 ? -27.027 -4.685   -40.704 1.00 34.89  ? 287 THR I C   1 
ATOM   17438 O O   . THR I  1 287 ? -28.066 -4.244   -41.194 1.00 50.97  ? 287 THR I O   1 
ATOM   17439 C CB  . THR I  1 287 ? -26.832 -6.054   -38.602 1.00 42.26  ? 287 THR I CB  1 
ATOM   17440 O OG1 . THR I  1 287 ? -27.771 -6.863   -39.323 1.00 39.39  ? 287 THR I OG1 1 
ATOM   17441 C CG2 . THR I  1 287 ? -27.216 -6.023   -37.132 1.00 33.81  ? 287 THR I CG2 1 
ATOM   17442 N N   . PRO I  1 288 ? -26.039 -5.200   -41.451 1.00 40.80  ? 288 PRO I N   1 
ATOM   17443 C CA  . PRO I  1 288 ? -26.183 -5.439   -42.890 1.00 46.50  ? 288 PRO I CA  1 
ATOM   17444 C C   . PRO I  1 288 ? -27.155 -6.573   -43.209 1.00 49.94  ? 288 PRO I C   1 
ATOM   17445 O O   . PRO I  1 288 ? -27.592 -6.661   -44.355 1.00 52.19  ? 288 PRO I O   1 
ATOM   17446 C CB  . PRO I  1 288 ? -24.768 -5.836   -43.323 1.00 49.93  ? 288 PRO I CB  1 
ATOM   17447 C CG  . PRO I  1 288 ? -23.871 -5.238   -42.295 1.00 39.34  ? 288 PRO I CG  1 
ATOM   17448 C CD  . PRO I  1 288 ? -24.638 -5.316   -41.013 1.00 41.00  ? 288 PRO I CD  1 
ATOM   17449 N N   . LYS I  1 289 ? -27.486 -7.424   -42.238 1.00 40.73  ? 289 LYS I N   1 
ATOM   17450 C CA  . LYS I  1 289 ? -28.435 -8.511   -42.489 1.00 44.65  ? 289 LYS I CA  1 
ATOM   17451 C C   . LYS I  1 289 ? -29.867 -8.089   -42.179 1.00 48.31  ? 289 LYS I C   1 
ATOM   17452 O O   . LYS I  1 289 ? -30.821 -8.643   -42.731 1.00 55.06  ? 289 LYS I O   1 
ATOM   17453 C CB  . LYS I  1 289 ? -28.094 -9.751   -41.662 1.00 51.56  ? 289 LYS I CB  1 
ATOM   17454 C CG  . LYS I  1 289 ? -26.611 -10.006  -41.476 1.00 67.15  ? 289 LYS I CG  1 
ATOM   17455 C CD  . LYS I  1 289 ? -26.368 -11.390  -40.895 1.00 59.20  ? 289 LYS I CD  1 
ATOM   17456 C CE  . LYS I  1 289 ? -27.543 -11.838  -40.044 1.00 75.56  ? 289 LYS I CE  1 
ATOM   17457 N NZ  . LYS I  1 289 ? -27.381 -13.217  -39.502 1.00 84.85  ? 289 LYS I NZ  1 
ATOM   17458 N N   . GLY I  1 290 ? -30.011 -7.113   -41.288 1.00 38.10  ? 290 GLY I N   1 
ATOM   17459 C CA  . GLY I  1 290 ? -31.317 -6.667   -40.842 1.00 44.19  ? 290 GLY I CA  1 
ATOM   17460 C C   . GLY I  1 290 ? -31.196 -5.907   -39.534 1.00 46.19  ? 290 GLY I C   1 
ATOM   17461 O O   . GLY I  1 290 ? -30.132 -5.889   -38.917 1.00 45.85  ? 290 GLY I O   1 
ATOM   17462 N N   . ALA I  1 291 ? -32.286 -5.277   -39.108 1.00 52.18  ? 291 ALA I N   1 
ATOM   17463 C CA  . ALA I  1 291 ? -32.282 -4.482   -37.882 1.00 42.96  ? 291 ALA I CA  1 
ATOM   17464 C C   . ALA I  1 291 ? -32.503 -5.347   -36.649 1.00 47.70  ? 291 ALA I C   1 
ATOM   17465 O O   . ALA I  1 291 ? -33.027 -6.457   -36.745 1.00 48.56  ? 291 ALA I O   1 
ATOM   17466 C CB  . ALA I  1 291 ? -33.341 -3.393   -37.956 1.00 32.78  ? 291 ALA I CB  1 
ATOM   17467 N N   . ILE I  1 292 ? -32.105 -4.832   -35.491 1.00 41.56  ? 292 ILE I N   1 
ATOM   17468 C CA  . ILE I  1 292 ? -32.308 -5.542   -34.237 1.00 51.09  ? 292 ILE I CA  1 
ATOM   17469 C C   . ILE I  1 292 ? -33.176 -4.732   -33.284 1.00 58.74  ? 292 ILE I C   1 
ATOM   17470 O O   . ILE I  1 292 ? -32.791 -3.650   -32.842 1.00 51.81  ? 292 ILE I O   1 
ATOM   17471 C CB  . ILE I  1 292 ? -30.973 -5.882   -33.547 1.00 46.52  ? 292 ILE I CB  1 
ATOM   17472 C CG1 . ILE I  1 292 ? -30.134 -6.804   -34.432 1.00 37.06  ? 292 ILE I CG1 1 
ATOM   17473 C CG2 . ILE I  1 292 ? -31.223 -6.541   -32.205 1.00 52.13  ? 292 ILE I CG2 1 
ATOM   17474 C CD1 . ILE I  1 292 ? -28.819 -7.217   -33.806 1.00 50.61  ? 292 ILE I CD1 1 
ATOM   17475 N N   . ASN I  1 293 ? -34.356 -5.264   -32.985 1.00 83.82  ? 293 ASN I N   1 
ATOM   17476 C CA  . ASN I  1 293 ? -35.263 -4.663   -32.018 1.00 99.65  ? 293 ASN I CA  1 
ATOM   17477 C C   . ASN I  1 293 ? -35.164 -5.437   -30.711 1.00 99.58  ? 293 ASN I C   1 
ATOM   17478 O O   . ASN I  1 293 ? -35.879 -6.418   -30.511 1.00 102.45 ? 293 ASN I O   1 
ATOM   17479 C CB  . ASN I  1 293 ? -36.696 -4.704   -32.552 1.00 117.65 ? 293 ASN I CB  1 
ATOM   17480 C CG  . ASN I  1 293 ? -37.698 -4.083   -31.597 1.00 124.71 ? 293 ASN I CG  1 
ATOM   17481 O OD1 . ASN I  1 293 ? -37.324 -3.454   -30.608 1.00 113.00 ? 293 ASN I OD1 1 
ATOM   17482 N ND2 . ASN I  1 293 ? -38.981 -4.256   -31.893 1.00 118.80 ? 293 ASN I ND2 1 
ATOM   17483 N N   . THR I  1 294 ? -34.274 -5.007   -29.823 1.00 88.17  ? 294 THR I N   1 
ATOM   17484 C CA  . THR I  1 294 ? -33.960 -5.817   -28.651 1.00 95.82  ? 294 THR I CA  1 
ATOM   17485 C C   . THR I  1 294 ? -33.657 -5.027   -27.383 1.00 83.10  ? 294 THR I C   1 
ATOM   17486 O O   . THR I  1 294 ? -33.258 -3.862   -27.429 1.00 82.85  ? 294 THR I O   1 
ATOM   17487 C CB  . THR I  1 294 ? -32.756 -6.733   -28.927 1.00 89.06  ? 294 THR I CB  1 
ATOM   17488 O OG1 . THR I  1 294 ? -32.652 -7.719   -27.893 1.00 61.80  ? 294 THR I OG1 1 
ATOM   17489 C CG2 . THR I  1 294 ? -31.478 -5.917   -28.973 1.00 69.23  ? 294 THR I CG2 1 
ATOM   17490 N N   . SER I  1 295 ? -33.848 -5.691   -26.248 1.00 69.27  ? 295 SER I N   1 
ATOM   17491 C CA  . SER I  1 295 ? -33.459 -5.156   -24.953 1.00 72.99  ? 295 SER I CA  1 
ATOM   17492 C C   . SER I  1 295 ? -32.289 -5.964   -24.407 1.00 59.64  ? 295 SER I C   1 
ATOM   17493 O O   . SER I  1 295 ? -31.605 -5.536   -23.482 1.00 60.17  ? 295 SER I O   1 
ATOM   17494 C CB  . SER I  1 295 ? -34.633 -5.216   -23.974 1.00 66.32  ? 295 SER I CB  1 
ATOM   17495 O OG  . SER I  1 295 ? -35.079 -3.916   -23.631 1.00 103.52 ? 295 SER I OG  1 
ATOM   17496 N N   . LEU I  1 296 ? -32.064 -7.136   -24.994 1.00 47.06  ? 296 LEU I N   1 
ATOM   17497 C CA  . LEU I  1 296 ? -31.019 -8.046   -24.536 1.00 44.21  ? 296 LEU I CA  1 
ATOM   17498 C C   . LEU I  1 296 ? -29.624 -7.439   -24.678 1.00 51.29  ? 296 LEU I C   1 
ATOM   17499 O O   . LEU I  1 296 ? -29.371 -6.658   -25.596 1.00 49.61  ? 296 LEU I O   1 
ATOM   17500 C CB  . LEU I  1 296 ? -31.104 -9.376   -25.288 1.00 47.79  ? 296 LEU I CB  1 
ATOM   17501 C CG  . LEU I  1 296 ? -32.457 -10.087  -25.216 1.00 50.89  ? 296 LEU I CG  1 
ATOM   17502 C CD1 . LEU I  1 296 ? -32.403 -11.433  -25.927 1.00 49.04  ? 296 LEU I CD1 1 
ATOM   17503 C CD2 . LEU I  1 296 ? -32.900 -10.254  -23.769 1.00 41.56  ? 296 LEU I CD2 1 
ATOM   17504 N N   . PRO I  1 297 ? -28.716 -7.801   -23.760 1.00 49.78  ? 297 PRO I N   1 
ATOM   17505 C CA  . PRO I  1 297 ? -27.360 -7.244   -23.692 1.00 39.09  ? 297 PRO I CA  1 
ATOM   17506 C C   . PRO I  1 297 ? -26.436 -7.750   -24.797 1.00 45.49  ? 297 PRO I C   1 
ATOM   17507 O O   . PRO I  1 297 ? -25.440 -7.092   -25.096 1.00 36.59  ? 297 PRO I O   1 
ATOM   17508 C CB  . PRO I  1 297 ? -26.846 -7.735   -22.330 1.00 42.29  ? 297 PRO I CB  1 
ATOM   17509 C CG  . PRO I  1 297 ? -28.058 -8.213   -21.588 1.00 51.03  ? 297 PRO I CG  1 
ATOM   17510 C CD  . PRO I  1 297 ? -28.986 -8.713   -22.638 1.00 48.35  ? 297 PRO I CD  1 
ATOM   17511 N N   . PHE I  1 298 ? -26.753 -8.897   -25.390 1.00 43.72  ? 298 PHE I N   1 
ATOM   17512 C CA  . PHE I  1 298 ? -25.855 -9.507   -26.366 1.00 46.07  ? 298 PHE I CA  1 
ATOM   17513 C C   . PHE I  1 298 ? -26.567 -10.007  -27.620 1.00 45.10  ? 298 PHE I C   1 
ATOM   17514 O O   . PHE I  1 298 ? -27.712 -10.454  -27.564 1.00 47.77  ? 298 PHE I O   1 
ATOM   17515 C CB  . PHE I  1 298 ? -25.077 -10.658  -25.723 1.00 39.75  ? 298 PHE I CB  1 
ATOM   17516 C CG  . PHE I  1 298 ? -24.586 -10.358  -24.335 1.00 47.08  ? 298 PHE I CG  1 
ATOM   17517 C CD1 . PHE I  1 298 ? -23.471 -9.562   -24.136 1.00 37.05  ? 298 PHE I CD1 1 
ATOM   17518 C CD2 . PHE I  1 298 ? -25.236 -10.880  -23.229 1.00 44.15  ? 298 PHE I CD2 1 
ATOM   17519 C CE1 . PHE I  1 298 ? -23.017 -9.287   -22.859 1.00 43.75  ? 298 PHE I CE1 1 
ATOM   17520 C CE2 . PHE I  1 298 ? -24.787 -10.610  -21.950 1.00 41.07  ? 298 PHE I CE2 1 
ATOM   17521 C CZ  . PHE I  1 298 ? -23.675 -9.812   -21.765 1.00 39.00  ? 298 PHE I CZ  1 
ATOM   17522 N N   . GLN I  1 299 ? -25.870 -9.932   -28.750 1.00 42.03  ? 299 GLN I N   1 
ATOM   17523 C CA  . GLN I  1 299 ? -26.388 -10.430  -30.018 1.00 41.03  ? 299 GLN I CA  1 
ATOM   17524 C C   . GLN I  1 299 ? -25.301 -11.188  -30.777 1.00 36.81  ? 299 GLN I C   1 
ATOM   17525 O O   . GLN I  1 299 ? -24.124 -10.833  -30.709 1.00 217.99 ? 299 GLN I O   1 
ATOM   17526 C CB  . GLN I  1 299 ? -26.936 -9.277   -30.865 1.00 37.84  ? 299 GLN I CB  1 
ATOM   17527 C CG  . GLN I  1 299 ? -25.932 -8.172   -31.155 1.00 35.54  ? 299 GLN I CG  1 
ATOM   17528 C CD  . GLN I  1 299 ? -25.122 -8.429   -32.411 1.00 46.65  ? 299 GLN I CD  1 
ATOM   17529 O OE1 . GLN I  1 299 ? -25.417 -9.345   -33.179 1.00 50.91  ? 299 GLN I OE1 1 
ATOM   17530 N NE2 . GLN I  1 299 ? -24.096 -7.614   -32.630 1.00 46.74  ? 299 GLN I NE2 1 
ATOM   17531 N N   . ASN I  1 300 ? -25.697 -12.235  -31.492 1.00 40.66  ? 300 ASN I N   1 
ATOM   17532 C CA  . ASN I  1 300 ? -24.753 -13.037  -32.263 1.00 38.48  ? 300 ASN I CA  1 
ATOM   17533 C C   . ASN I  1 300 ? -25.089 -13.011  -33.748 1.00 38.84  ? 300 ASN I C   1 
ATOM   17534 O O   . ASN I  1 300 ? -24.697 -13.901  -34.506 1.00 48.32  ? 300 ASN I O   1 
ATOM   17535 C CB  . ASN I  1 300 ? -24.736 -14.479  -31.756 1.00 27.97  ? 300 ASN I CB  1 
ATOM   17536 C CG  . ASN I  1 300 ? -26.049 -15.198  -31.999 1.00 36.55  ? 300 ASN I CG  1 
ATOM   17537 O OD1 . ASN I  1 300 ? -27.058 -14.578  -32.335 1.00 49.29  ? 300 ASN I OD1 1 
ATOM   17538 N ND2 . ASN I  1 300 ? -26.041 -16.514  -31.830 1.00 41.49  ? 300 ASN I ND2 1 
ATOM   17539 N N   . ILE I  1 301 ? -25.821 -11.980  -34.152 1.00 31.54  ? 301 ILE I N   1 
ATOM   17540 C CA  . ILE I  1 301 ? -26.269 -11.837  -35.530 1.00 43.99  ? 301 ILE I CA  1 
ATOM   17541 C C   . ILE I  1 301 ? -25.139 -11.401  -36.456 1.00 40.32  ? 301 ILE I C   1 
ATOM   17542 O O   . ILE I  1 301 ? -24.834 -12.081  -37.436 1.00 52.09  ? 301 ILE I O   1 
ATOM   17543 C CB  . ILE I  1 301 ? -27.428 -10.826  -35.630 1.00 44.78  ? 301 ILE I CB  1 
ATOM   17544 C CG1 . ILE I  1 301 ? -28.674 -11.382  -34.939 1.00 35.31  ? 301 ILE I CG1 1 
ATOM   17545 C CG2 . ILE I  1 301 ? -27.726 -10.496  -37.080 1.00 41.76  ? 301 ILE I CG2 1 
ATOM   17546 C CD1 . ILE I  1 301 ? -29.847 -10.430  -34.934 1.00 53.95  ? 301 ILE I CD1 1 
ATOM   17547 N N   . HIS I  1 302 ? -24.518 -10.269  -36.140 1.00 32.48  ? 302 HIS I N   1 
ATOM   17548 C CA  . HIS I  1 302 ? -23.468 -9.721   -36.990 1.00 41.99  ? 302 HIS I CA  1 
ATOM   17549 C C   . HIS I  1 302 ? -22.520 -8.821   -36.202 1.00 44.27  ? 302 HIS I C   1 
ATOM   17550 O O   . HIS I  1 302 ? -22.956 -8.048   -35.347 1.00 42.21  ? 302 HIS I O   1 
ATOM   17551 C CB  . HIS I  1 302 ? -24.090 -8.941   -38.150 1.00 39.84  ? 302 HIS I CB  1 
ATOM   17552 C CG  . HIS I  1 302 ? -23.182 -8.781   -39.329 1.00 47.46  ? 302 HIS I CG  1 
ATOM   17553 N ND1 . HIS I  1 302 ? -22.214 -7.803   -39.399 1.00 32.07  ? 302 HIS I ND1 1 
ATOM   17554 C CD2 . HIS I  1 302 ? -23.101 -9.473   -40.491 1.00 54.85  ? 302 HIS I CD2 1 
ATOM   17555 C CE1 . HIS I  1 302 ? -21.572 -7.901   -40.549 1.00 39.38  ? 302 HIS I CE1 1 
ATOM   17556 N NE2 . HIS I  1 302 ? -22.093 -8.907   -41.231 1.00 47.68  ? 302 HIS I NE2 1 
ATOM   17557 N N   . PRO I  1 303 ? -21.212 -8.925   -36.489 1.00 37.58  ? 303 PRO I N   1 
ATOM   17558 C CA  . PRO I  1 303 ? -20.167 -8.129   -35.835 1.00 29.97  ? 303 PRO I CA  1 
ATOM   17559 C C   . PRO I  1 303 ? -20.245 -6.655   -36.219 1.00 40.33  ? 303 PRO I C   1 
ATOM   17560 O O   . PRO I  1 303 ? -20.158 -5.789   -35.349 1.00 33.11  ? 303 PRO I O   1 
ATOM   17561 C CB  . PRO I  1 303 ? -18.868 -8.740   -36.377 1.00 28.71  ? 303 PRO I CB  1 
ATOM   17562 C CG  . PRO I  1 303 ? -19.255 -10.085  -36.902 1.00 53.18  ? 303 PRO I CG  1 
ATOM   17563 C CD  . PRO I  1 303 ? -20.645 -9.916   -37.417 1.00 41.04  ? 303 PRO I CD  1 
ATOM   17564 N N   . ILE I  1 304 ? -20.398 -6.378   -37.510 1.00 43.83  ? 304 ILE I N   1 
ATOM   17565 C CA  . ILE I  1 304 ? -20.512 -5.004   -37.987 1.00 37.75  ? 304 ILE I CA  1 
ATOM   17566 C C   . ILE I  1 304 ? -21.906 -4.460   -37.700 1.00 42.14  ? 304 ILE I C   1 
ATOM   17567 O O   . ILE I  1 304 ? -22.908 -5.027   -38.136 1.00 54.10  ? 304 ILE I O   1 
ATOM   17568 C CB  . ILE I  1 304 ? -20.199 -4.889   -39.490 1.00 30.27  ? 304 ILE I CB  1 
ATOM   17569 C CG1 . ILE I  1 304 ? -18.690 -4.985   -39.732 1.00 32.36  ? 304 ILE I CG1 1 
ATOM   17570 C CG2 . ILE I  1 304 ? -20.722 -3.574   -40.042 1.00 52.47  ? 304 ILE I CG2 1 
ATOM   17571 C CD1 . ILE I  1 304 ? -18.080 -6.322   -39.360 1.00 58.27  ? 304 ILE I CD1 1 
ATOM   17572 N N   . THR I  1 305 ? -21.959 -3.355   -36.964 1.00 34.45  ? 305 THR I N   1 
ATOM   17573 C CA  . THR I  1 305 ? -23.225 -2.824   -36.479 1.00 30.66  ? 305 THR I CA  1 
ATOM   17574 C C   . THR I  1 305 ? -23.225 -1.296   -36.468 1.00 49.96  ? 305 THR I C   1 
ATOM   17575 O O   . THR I  1 305 ? -22.173 -0.665   -36.363 1.00 39.43  ? 305 THR I O   1 
ATOM   17576 C CB  . THR I  1 305 ? -23.514 -3.343   -35.056 1.00 41.82  ? 305 THR I CB  1 
ATOM   17577 O OG1 . THR I  1 305 ? -24.879 -3.767   -34.960 1.00 65.57  ? 305 THR I OG1 1 
ATOM   17578 C CG2 . THR I  1 305 ? -23.232 -2.262   -34.020 1.00 41.68  ? 305 THR I CG2 1 
ATOM   17579 N N   . ILE I  1 306 ? -24.411 -0.704   -36.584 1.00 48.80  ? 306 ILE I N   1 
ATOM   17580 C CA  . ILE I  1 306 ? -24.549 0.746    -36.508 1.00 46.44  ? 306 ILE I CA  1 
ATOM   17581 C C   . ILE I  1 306 ? -25.664 1.143    -35.544 1.00 39.72  ? 306 ILE I C   1 
ATOM   17582 O O   . ILE I  1 306 ? -26.764 0.593    -35.591 1.00 38.61  ? 306 ILE I O   1 
ATOM   17583 C CB  . ILE I  1 306 ? -24.826 1.375    -37.889 1.00 34.06  ? 306 ILE I CB  1 
ATOM   17584 C CG1 . ILE I  1 306 ? -23.781 0.918    -38.908 1.00 43.03  ? 306 ILE I CG1 1 
ATOM   17585 C CG2 . ILE I  1 306 ? -24.833 2.889    -37.788 1.00 25.77  ? 306 ILE I CG2 1 
ATOM   17586 C CD1 . ILE I  1 306 ? -23.885 1.619    -40.246 1.00 42.47  ? 306 ILE I CD1 1 
ATOM   17587 N N   . GLY I  1 307 ? -25.370 2.098    -34.667 1.00 44.13  ? 307 GLY I N   1 
ATOM   17588 C CA  . GLY I  1 307 ? -26.348 2.589    -33.711 1.00 42.49  ? 307 GLY I CA  1 
ATOM   17589 C C   . GLY I  1 307 ? -26.022 2.236    -32.271 1.00 44.85  ? 307 GLY I C   1 
ATOM   17590 O O   . GLY I  1 307 ? -24.853 2.112    -31.899 1.00 55.22  ? 307 GLY I O   1 
ATOM   17591 N N   . LYS I  1 308 ? -27.064 2.080    -31.457 1.00 46.70  ? 308 LYS I N   1 
ATOM   17592 C CA  . LYS I  1 308 ? -26.914 1.644    -30.072 1.00 45.14  ? 308 LYS I CA  1 
ATOM   17593 C C   . LYS I  1 308 ? -27.225 0.156    -29.984 1.00 43.81  ? 308 LYS I C   1 
ATOM   17594 O O   . LYS I  1 308 ? -28.377 -0.229   -29.773 1.00 56.58  ? 308 LYS I O   1 
ATOM   17595 C CB  . LYS I  1 308 ? -27.873 2.410    -29.159 1.00 45.55  ? 308 LYS I CB  1 
ATOM   17596 C CG  . LYS I  1 308 ? -27.215 3.454    -28.264 1.00 59.12  ? 308 LYS I CG  1 
ATOM   17597 C CD  . LYS I  1 308 ? -27.620 4.862    -28.675 1.00 67.63  ? 308 LYS I CD  1 
ATOM   17598 C CE  . LYS I  1 308 ? -27.242 5.887    -27.614 1.00 77.99  ? 308 LYS I CE  1 
ATOM   17599 N NZ  . LYS I  1 308 ? -27.382 7.278    -28.129 1.00 97.47  ? 308 LYS I NZ  1 
ATOM   17600 N N   . CYS I  1 309 ? -26.206 -0.682   -30.135 1.00 41.07  ? 309 CYS I N   1 
ATOM   17601 C CA  . CYS I  1 309 ? -26.442 -2.109   -30.295 1.00 49.71  ? 309 CYS I CA  1 
ATOM   17602 C C   . CYS I  1 309 ? -25.969 -2.959   -29.121 1.00 45.83  ? 309 CYS I C   1 
ATOM   17603 O O   . CYS I  1 309 ? -25.076 -2.561   -28.372 1.00 50.05  ? 309 CYS I O   1 
ATOM   17604 C CB  . CYS I  1 309 ? -25.798 -2.593   -31.593 1.00 40.17  ? 309 CYS I CB  1 
ATOM   17605 S SG  . CYS I  1 309 ? -26.277 -1.612   -33.030 1.00 68.01  ? 309 CYS I SG  1 
ATOM   17606 N N   . PRO I  1 310 ? -26.586 -4.138   -28.958 1.00 40.87  ? 310 PRO I N   1 
ATOM   17607 C CA  . PRO I  1 310 ? -26.112 -5.135   -28.000 1.00 48.15  ? 310 PRO I CA  1 
ATOM   17608 C C   . PRO I  1 310 ? -24.714 -5.554   -28.406 1.00 46.95  ? 310 PRO I C   1 
ATOM   17609 O O   . PRO I  1 310 ? -24.330 -5.366   -29.561 1.00 46.39  ? 310 PRO I O   1 
ATOM   17610 C CB  . PRO I  1 310 ? -27.079 -6.304   -28.200 1.00 37.80  ? 310 PRO I CB  1 
ATOM   17611 C CG  . PRO I  1 310 ? -28.286 -5.703   -28.811 1.00 42.04  ? 310 PRO I CG  1 
ATOM   17612 C CD  . PRO I  1 310 ? -27.793 -4.587   -29.669 1.00 40.83  ? 310 PRO I CD  1 
ATOM   17613 N N   . LYS I  1 311 ? -23.961 -6.116   -27.474 1.00 35.01  ? 311 LYS I N   1 
ATOM   17614 C CA  . LYS I  1 311 ? -22.589 -6.492   -27.761 1.00 36.69  ? 311 LYS I CA  1 
ATOM   17615 C C   . LYS I  1 311 ? -22.524 -7.781   -28.573 1.00 39.40  ? 311 LYS I C   1 
ATOM   17616 O O   . LYS I  1 311 ? -23.261 -8.730   -28.306 1.00 41.58  ? 311 LYS I O   1 
ATOM   17617 C CB  . LYS I  1 311 ? -21.802 -6.623   -26.462 1.00 30.75  ? 311 LYS I CB  1 
ATOM   17618 C CG  . LYS I  1 311 ? -20.531 -5.815   -26.461 1.00 39.99  ? 311 LYS I CG  1 
ATOM   17619 C CD  . LYS I  1 311 ? -20.764 -4.375   -26.889 1.00 34.20  ? 311 LYS I CD  1 
ATOM   17620 C CE  . LYS I  1 311 ? -21.017 -3.468   -25.698 1.00 40.11  ? 311 LYS I CE  1 
ATOM   17621 N NZ  . LYS I  1 311 ? -20.840 -2.034   -26.064 1.00 36.70  ? 311 LYS I NZ  1 
ATOM   17622 N N   . TYR I  1 312 ? -21.647 -7.808   -29.572 1.00 32.43  ? 312 TYR I N   1 
ATOM   17623 C CA  . TYR I  1 312 ? -21.505 -8.988   -30.416 1.00 34.38  ? 312 TYR I CA  1 
ATOM   17624 C C   . TYR I  1 312 ? -20.775 -10.110  -29.687 1.00 44.45  ? 312 TYR I C   1 
ATOM   17625 O O   . TYR I  1 312 ? -19.681 -9.915   -29.156 1.00 48.52  ? 312 TYR I O   1 
ATOM   17626 C CB  . TYR I  1 312 ? -20.791 -8.654   -31.727 1.00 27.69  ? 312 TYR I CB  1 
ATOM   17627 C CG  . TYR I  1 312 ? -20.603 -9.862   -32.616 1.00 34.05  ? 312 TYR I CG  1 
ATOM   17628 C CD1 . TYR I  1 312 ? -21.696 -10.509  -33.176 1.00 31.46  ? 312 TYR I CD1 1 
ATOM   17629 C CD2 . TYR I  1 312 ? -19.335 -10.360  -32.888 1.00 35.25  ? 312 TYR I CD2 1 
ATOM   17630 C CE1 . TYR I  1 312 ? -21.533 -11.618  -33.985 1.00 33.67  ? 312 TYR I CE1 1 
ATOM   17631 C CE2 . TYR I  1 312 ? -19.162 -11.469  -33.697 1.00 30.06  ? 312 TYR I CE2 1 
ATOM   17632 C CZ  . TYR I  1 312 ? -20.264 -12.093  -34.242 1.00 38.87  ? 312 TYR I CZ  1 
ATOM   17633 O OH  . TYR I  1 312 ? -20.099 -13.196  -35.048 1.00 49.17  ? 312 TYR I OH  1 
ATOM   17634 N N   . VAL I  1 313 ? -21.395 -11.285  -29.670 1.00 46.81  ? 313 VAL I N   1 
ATOM   17635 C CA  . VAL I  1 313 ? -20.836 -12.445  -28.992 1.00 33.65  ? 313 VAL I CA  1 
ATOM   17636 C C   . VAL I  1 313 ? -20.861 -13.663  -29.911 1.00 37.04  ? 313 VAL I C   1 
ATOM   17637 O O   . VAL I  1 313 ? -21.759 -13.807  -30.741 1.00 45.05  ? 313 VAL I O   1 
ATOM   17638 C CB  . VAL I  1 313 ? -21.607 -12.753  -27.694 1.00 35.33  ? 313 VAL I CB  1 
ATOM   17639 C CG1 . VAL I  1 313 ? -21.077 -14.015  -27.043 1.00 57.73  ? 313 VAL I CG1 1 
ATOM   17640 C CG2 . VAL I  1 313 ? -21.509 -11.579  -26.733 1.00 42.78  ? 313 VAL I CG2 1 
ATOM   17641 N N   . LYS I  1 314 ? -19.868 -14.532  -29.760 1.00 41.66  ? 314 LYS I N   1 
ATOM   17642 C CA  . LYS I  1 314 ? -19.741 -15.717  -30.599 1.00 36.53  ? 314 LYS I CA  1 
ATOM   17643 C C   . LYS I  1 314 ? -20.587 -16.866  -30.062 1.00 36.69  ? 314 LYS I C   1 
ATOM   17644 O O   . LYS I  1 314 ? -20.585 -17.965  -30.616 1.00 54.74  ? 314 LYS I O   1 
ATOM   17645 C CB  . LYS I  1 314 ? -18.274 -16.138  -30.674 1.00 37.13  ? 314 LYS I CB  1 
ATOM   17646 C CG  . LYS I  1 314 ? -17.914 -17.005  -31.867 1.00 60.38  ? 314 LYS I CG  1 
ATOM   17647 C CD  . LYS I  1 314 ? -16.414 -17.237  -31.903 1.00 90.06  ? 314 LYS I CD  1 
ATOM   17648 C CE  . LYS I  1 314 ? -15.667 -15.915  -31.792 1.00 92.24  ? 314 LYS I CE  1 
ATOM   17649 N NZ  . LYS I  1 314 ? -14.237 -16.096  -31.419 1.00 78.12  ? 314 LYS I NZ  1 
ATOM   17650 N N   . SER I  1 315 ? -21.314 -16.605  -28.982 1.00 41.61  ? 315 SER I N   1 
ATOM   17651 C CA  . SER I  1 315 ? -22.134 -17.628  -28.344 1.00 49.22  ? 315 SER I CA  1 
ATOM   17652 C C   . SER I  1 315 ? -23.266 -18.113  -29.249 1.00 45.20  ? 315 SER I C   1 
ATOM   17653 O O   . SER I  1 315 ? -23.771 -17.364  -30.084 1.00 32.44  ? 315 SER I O   1 
ATOM   17654 C CB  . SER I  1 315 ? -22.709 -17.101  -27.026 1.00 49.23  ? 315 SER I CB  1 
ATOM   17655 O OG  . SER I  1 315 ? -21.677 -16.810  -26.100 1.00 64.80  ? 315 SER I OG  1 
ATOM   17656 N N   . THR I  1 316 ? -23.651 -19.375  -29.082 1.00 57.12  ? 316 THR I N   1 
ATOM   17657 C CA  . THR I  1 316 ? -24.817 -19.923  -29.768 1.00 50.45  ? 316 THR I CA  1 
ATOM   17658 C C   . THR I  1 316 ? -26.063 -19.758  -28.902 1.00 46.93  ? 316 THR I C   1 
ATOM   17659 O O   . THR I  1 316 ? -27.162 -19.536  -29.411 1.00 54.67  ? 316 THR I O   1 
ATOM   17660 C CB  . THR I  1 316 ? -24.630 -21.415  -30.113 1.00 59.36  ? 316 THR I CB  1 
ATOM   17661 O OG1 . THR I  1 316 ? -25.894 -21.986  -30.475 1.00 80.63  ? 316 THR I OG1 1 
ATOM   17662 C CG2 . THR I  1 316 ? -24.067 -22.175  -28.921 1.00 65.48  ? 316 THR I CG2 1 
ATOM   17663 N N   . LYS I  1 317 ? -25.880 -19.868  -27.589 1.00 50.86  ? 317 LYS I N   1 
ATOM   17664 C CA  . LYS I  1 317 ? -26.978 -19.693  -26.644 1.00 48.85  ? 317 LYS I CA  1 
ATOM   17665 C C   . LYS I  1 317 ? -26.501 -19.115  -25.312 1.00 52.37  ? 317 LYS I C   1 
ATOM   17666 O O   . LYS I  1 317 ? -25.421 -19.452  -24.824 1.00 66.57  ? 317 LYS I O   1 
ATOM   17667 C CB  . LYS I  1 317 ? -27.708 -21.020  -26.413 1.00 58.14  ? 317 LYS I CB  1 
ATOM   17668 C CG  . LYS I  1 317 ? -26.802 -22.165  -25.986 1.00 72.71  ? 317 LYS I CG  1 
ATOM   17669 C CD  . LYS I  1 317 ? -27.599 -23.418  -25.659 1.00 95.97  ? 317 LYS I CD  1 
ATOM   17670 C CE  . LYS I  1 317 ? -28.453 -23.224  -24.416 1.00 92.11  ? 317 LYS I CE  1 
ATOM   17671 N NZ  . LYS I  1 317 ? -29.189 -24.467  -24.054 1.00 70.26  ? 317 LYS I NZ  1 
ATOM   17672 N N   . LEU I  1 318 ? -27.312 -18.231  -24.741 1.00 48.00  ? 318 LEU I N   1 
ATOM   17673 C CA  . LEU I  1 318 ? -27.056 -17.686  -23.414 1.00 42.21  ? 318 LEU I CA  1 
ATOM   17674 C C   . LEU I  1 318 ? -28.322 -17.826  -22.576 1.00 43.80  ? 318 LEU I C   1 
ATOM   17675 O O   . LEU I  1 318 ? -28.991 -16.836  -22.275 1.00 54.96  ? 318 LEU I O   1 
ATOM   17676 C CB  . LEU I  1 318 ? -26.632 -16.215  -23.493 1.00 32.31  ? 318 LEU I CB  1 
ATOM   17677 C CG  . LEU I  1 318 ? -25.310 -15.881  -24.194 1.00 41.53  ? 318 LEU I CG  1 
ATOM   17678 C CD1 . LEU I  1 318 ? -25.081 -14.381  -24.245 1.00 46.74  ? 318 LEU I CD1 1 
ATOM   17679 C CD2 . LEU I  1 318 ? -24.132 -16.559  -23.530 1.00 39.78  ? 318 LEU I CD2 1 
ATOM   17680 N N   . ARG I  1 319 ? -28.648 -19.060  -22.204 1.00 43.47  ? 319 ARG I N   1 
ATOM   17681 C CA  . ARG I  1 319 ? -29.875 -19.340  -21.466 1.00 52.51  ? 319 ARG I CA  1 
ATOM   17682 C C   . ARG I  1 319 ? -29.709 -19.109  -19.966 1.00 46.76  ? 319 ARG I C   1 
ATOM   17683 O O   . ARG I  1 319 ? -28.957 -19.822  -19.299 1.00 41.57  ? 319 ARG I O   1 
ATOM   17684 C CB  . ARG I  1 319 ? -30.328 -20.777  -21.722 1.00 57.37  ? 319 ARG I CB  1 
ATOM   17685 C CG  . ARG I  1 319 ? -31.792 -20.902  -22.107 1.00 59.20  ? 319 ARG I CG  1 
ATOM   17686 C CD  . ARG I  1 319 ? -31.965 -20.905  -23.621 1.00 62.72  ? 319 ARG I CD  1 
ATOM   17687 N NE  . ARG I  1 319 ? -33.233 -20.330  -24.068 1.00 67.81  ? 319 ARG I NE  1 
ATOM   17688 C CZ  . ARG I  1 319 ? -34.361 -20.347  -23.367 1.00 67.79  ? 319 ARG I CZ  1 
ATOM   17689 N NH1 . ARG I  1 319 ? -34.405 -20.920  -22.176 1.00 78.38  ? 319 ARG I NH1 1 
ATOM   17690 N NH2 . ARG I  1 319 ? -35.451 -19.793  -23.864 1.00 75.05  ? 319 ARG I NH2 1 
ATOM   17691 N N   . LEU I  1 320 ? -30.425 -18.119  -19.443 1.00 41.97  ? 320 LEU I N   1 
ATOM   17692 C CA  . LEU I  1 320 ? -30.308 -17.742  -18.041 1.00 34.83  ? 320 LEU I CA  1 
ATOM   17693 C C   . LEU I  1 320 ? -31.435 -18.356  -17.217 1.00 51.97  ? 320 LEU I C   1 
ATOM   17694 O O   . LEU I  1 320 ? -32.613 -18.092  -17.460 1.00 65.03  ? 320 LEU I O   1 
ATOM   17695 C CB  . LEU I  1 320 ? -30.323 -16.218  -17.901 1.00 39.30  ? 320 LEU I CB  1 
ATOM   17696 C CG  . LEU I  1 320 ? -29.957 -15.631  -16.538 1.00 44.61  ? 320 LEU I CG  1 
ATOM   17697 C CD1 . LEU I  1 320 ? -28.477 -15.835  -16.248 1.00 46.19  ? 320 LEU I CD1 1 
ATOM   17698 C CD2 . LEU I  1 320 ? -30.309 -14.154  -16.490 1.00 42.85  ? 320 LEU I CD2 1 
ATOM   17699 N N   . ALA I  1 321 ? -31.061 -19.173  -16.237 1.00 53.43  ? 321 ALA I N   1 
ATOM   17700 C CA  . ALA I  1 321 ? -32.026 -19.838  -15.370 1.00 39.42  ? 321 ALA I CA  1 
ATOM   17701 C C   . ALA I  1 321 ? -32.742 -18.852  -14.455 1.00 40.57  ? 321 ALA I C   1 
ATOM   17702 O O   . ALA I  1 321 ? -32.112 -18.029  -13.787 1.00 52.70  ? 321 ALA I O   1 
ATOM   17703 C CB  . ALA I  1 321 ? -31.343 -20.921  -14.551 1.00 41.75  ? 321 ALA I CB  1 
ATOM   17704 N N   . THR I  1 322 ? -34.067 -18.951  -14.436 1.00 41.21  ? 322 THR I N   1 
ATOM   17705 C CA  . THR I  1 322 ? -34.914 -18.095  -13.618 1.00 60.18  ? 322 THR I CA  1 
ATOM   17706 C C   . THR I  1 322 ? -35.686 -18.954  -12.637 1.00 54.61  ? 322 THR I C   1 
ATOM   17707 O O   . THR I  1 322 ? -35.829 -18.611  -11.462 1.00 50.93  ? 322 THR I O   1 
ATOM   17708 C CB  . THR I  1 322 ? -35.922 -17.334  -14.484 1.00 52.95  ? 322 THR I CB  1 
ATOM   17709 O OG1 . THR I  1 322 ? -36.692 -18.268  -15.251 1.00 49.52  ? 322 THR I OG1 1 
ATOM   17710 C CG2 . THR I  1 322 ? -35.194 -16.403  -15.428 1.00 63.12  ? 322 THR I CG2 1 
ATOM   17711 N N   . GLY I  1 323 ? -36.193 -20.073  -13.142 1.00 48.31  ? 323 GLY I N   1 
ATOM   17712 C CA  . GLY I  1 323 ? -36.863 -21.057  -12.316 1.00 59.35  ? 323 GLY I CA  1 
ATOM   17713 C C   . GLY I  1 323 ? -35.861 -21.998  -11.680 1.00 58.15  ? 323 GLY I C   1 
ATOM   17714 O O   . GLY I  1 323 ? -34.653 -21.776  -11.774 1.00 66.58  ? 323 GLY I O   1 
ATOM   17715 N N   . LEU I  1 324 ? -36.364 -23.051  -11.041 1.00 52.24  ? 324 LEU I N   1 
ATOM   17716 C CA  . LEU I  1 324 ? -35.513 -23.990  -10.316 1.00 64.26  ? 324 LEU I CA  1 
ATOM   17717 C C   . LEU I  1 324 ? -35.329 -25.321  -11.032 1.00 55.65  ? 324 LEU I C   1 
ATOM   17718 O O   . LEU I  1 324 ? -35.971 -25.591  -12.046 1.00 63.45  ? 324 LEU I O   1 
ATOM   17719 C CB  . LEU I  1 324 ? -36.074 -24.255  -8.919  1.00 64.66  ? 324 LEU I CB  1 
ATOM   17720 C CG  . LEU I  1 324 ? -37.492 -24.819  -8.796  1.00 54.69  ? 324 LEU I CG  1 
ATOM   17721 C CD1 . LEU I  1 324 ? -37.589 -25.814  -7.658  1.00 67.90  ? 324 LEU I CD1 1 
ATOM   17722 C CD2 . LEU I  1 324 ? -38.491 -23.703  -8.605  1.00 52.46  ? 324 LEU I CD2 1 
ATOM   17723 N N   . ARG I  1 325 ? -34.450 -26.156  -10.484 1.00 62.49  ? 325 ARG I N   1 
ATOM   17724 C CA  . ARG I  1 325 ? -34.226 -27.487  -11.029 1.00 68.65  ? 325 ARG I CA  1 
ATOM   17725 C C   . ARG I  1 325 ? -35.560 -28.201  -11.155 1.00 68.82  ? 325 ARG I C   1 
ATOM   17726 O O   . ARG I  1 325 ? -36.429 -28.084  -10.289 1.00 64.90  ? 325 ARG I O   1 
ATOM   17727 C CB  . ARG I  1 325 ? -33.275 -28.303  -10.147 1.00 64.66  ? 325 ARG I CB  1 
ATOM   17728 C CG  . ARG I  1 325 ? -32.618 -29.483  -10.870 1.00 64.37  ? 325 ARG I CG  1 
ATOM   17729 C CD  . ARG I  1 325 ? -31.794 -30.367  -9.929  1.00 76.35  ? 325 ARG I CD  1 
ATOM   17730 N NE  . ARG I  1 325 ? -30.595 -29.702  -9.420  1.00 88.06  ? 325 ARG I NE  1 
ATOM   17731 C CZ  . ARG I  1 325 ? -29.383 -29.808  -9.961  1.00 87.51  ? 325 ARG I CZ  1 
ATOM   17732 N NH1 . ARG I  1 325 ? -29.191 -30.555  -11.040 1.00 66.51  ? 325 ARG I NH1 1 
ATOM   17733 N NH2 . ARG I  1 325 ? -28.357 -29.163  -9.420  1.00 84.25  ? 325 ARG I NH2 1 
ATOM   17734 N N   . ASN I  1 326 ? -35.709 -28.951  -12.238 1.00 73.71  ? 326 ASN I N   1 
ATOM   17735 C CA  . ASN I  1 326 ? -36.980 -29.573  -12.563 1.00 85.82  ? 326 ASN I CA  1 
ATOM   17736 C C   . ASN I  1 326 ? -36.947 -31.106  -12.511 1.00 87.23  ? 326 ASN I C   1 
ATOM   17737 O O   . ASN I  1 326 ? -36.085 -31.738  -13.119 1.00 83.83  ? 326 ASN I O   1 
ATOM   17738 C CB  . ASN I  1 326 ? -37.427 -29.087  -13.940 1.00 95.31  ? 326 ASN I CB  1 
ATOM   17739 C CG  . ASN I  1 326 ? -38.829 -29.517  -14.281 1.00 93.24  ? 326 ASN I CG  1 
ATOM   17740 O OD1 . ASN I  1 326 ? -39.743 -29.410  -13.464 1.00 98.59  ? 326 ASN I OD1 1 
ATOM   17741 N ND2 . ASN I  1 326 ? -39.013 -30.003  -15.501 1.00 91.37  ? 326 ASN I ND2 1 
ATOM   17742 N N   . ILE I  1 327 ? -37.892 -31.694  -11.781 1.00 88.83  ? 327 ILE I N   1 
ATOM   17743 C CA  . ILE I  1 327 ? -38.008 -33.148  -11.684 1.00 82.95  ? 327 ILE I CA  1 
ATOM   17744 C C   . ILE I  1 327 ? -39.426 -33.645  -11.978 1.00 88.09  ? 327 ILE I C   1 
ATOM   17745 O O   . ILE I  1 327 ? -40.387 -33.147  -11.395 1.00 87.17  ? 327 ILE I O   1 
ATOM   17746 C CB  . ILE I  1 327 ? -37.645 -33.645  -10.270 1.00 74.44  ? 327 ILE I CB  1 
ATOM   17747 C CG1 . ILE I  1 327 ? -36.179 -33.345  -9.938  1.00 60.83  ? 327 ILE I CG1 1 
ATOM   17748 C CG2 . ILE I  1 327 ? -37.966 -35.122  -10.139 1.00 90.32  ? 327 ILE I CG2 1 
ATOM   17749 C CD1 . ILE I  1 327 ? -35.208 -33.730  -11.037 1.00 61.05  ? 327 ILE I CD1 1 
ATOM   17750 N N   . GLY J  2 1   ? -29.380 -28.918  -4.258  1.00 104.73 ? 1   GLY J N   1 
ATOM   17751 C CA  . GLY J  2 1   ? -27.959 -28.851  -4.541  1.00 99.87  ? 1   GLY J CA  1 
ATOM   17752 C C   . GLY J  2 1   ? -27.124 -28.420  -3.349  1.00 76.71  ? 1   GLY J C   1 
ATOM   17753 O O   . GLY J  2 1   ? -26.741 -29.240  -2.515  1.00 100.41 ? 1   GLY J O   1 
ATOM   17754 N N   . LEU J  2 2   ? -26.847 -27.123  -3.267  1.00 65.44  ? 2   LEU J N   1 
ATOM   17755 C CA  . LEU J  2 2   ? -25.949 -26.591  -2.247  1.00 72.06  ? 2   LEU J CA  1 
ATOM   17756 C C   . LEU J  2 2   ? -26.538 -26.668  -0.838  1.00 60.84  ? 2   LEU J C   1 
ATOM   17757 O O   . LEU J  2 2   ? -25.802 -26.731  0.147   1.00 55.18  ? 2   LEU J O   1 
ATOM   17758 C CB  . LEU J  2 2   ? -25.567 -25.147  -2.579  1.00 63.29  ? 2   LEU J CB  1 
ATOM   17759 C CG  . LEU J  2 2   ? -24.228 -24.668  -2.017  1.00 63.21  ? 2   LEU J CG  1 
ATOM   17760 C CD1 . LEU J  2 2   ? -23.077 -25.495  -2.577  1.00 58.16  ? 2   LEU J CD1 1 
ATOM   17761 C CD2 . LEU J  2 2   ? -24.022 -23.191  -2.305  1.00 36.67  ? 2   LEU J CD2 1 
ATOM   17762 N N   . PHE J  2 3   ? -27.863 -26.663  -0.747  1.00 58.21  ? 3   PHE J N   1 
ATOM   17763 C CA  . PHE J  2 3   ? -28.537 -26.715  0.546   1.00 62.39  ? 3   PHE J CA  1 
ATOM   17764 C C   . PHE J  2 3   ? -29.121 -28.097  0.833   1.00 70.12  ? 3   PHE J C   1 
ATOM   17765 O O   . PHE J  2 3   ? -29.788 -28.300  1.847   1.00 69.57  ? 3   PHE J O   1 
ATOM   17766 C CB  . PHE J  2 3   ? -29.619 -25.637  0.633   1.00 70.55  ? 3   PHE J CB  1 
ATOM   17767 C CG  . PHE J  2 3   ? -29.074 -24.237  0.689   1.00 64.16  ? 3   PHE J CG  1 
ATOM   17768 C CD1 . PHE J  2 3   ? -28.772 -23.549  -0.474  1.00 67.05  ? 3   PHE J CD1 1 
ATOM   17769 C CD2 . PHE J  2 3   ? -28.860 -23.612  1.906   1.00 71.92  ? 3   PHE J CD2 1 
ATOM   17770 C CE1 . PHE J  2 3   ? -28.269 -22.262  -0.425  1.00 67.78  ? 3   PHE J CE1 1 
ATOM   17771 C CE2 . PHE J  2 3   ? -28.357 -22.325  1.962   1.00 70.03  ? 3   PHE J CE2 1 
ATOM   17772 C CZ  . PHE J  2 3   ? -28.061 -21.649  0.795   1.00 70.39  ? 3   PHE J CZ  1 
ATOM   17773 N N   . GLY J  2 4   ? -28.866 -29.041  -0.068  1.00 71.92  ? 4   GLY J N   1 
ATOM   17774 C CA  . GLY J  2 4   ? -29.239 -30.429  0.141   1.00 71.52  ? 4   GLY J CA  1 
ATOM   17775 C C   . GLY J  2 4   ? -30.719 -30.736  0.018   1.00 78.36  ? 4   GLY J C   1 
ATOM   17776 O O   . GLY J  2 4   ? -31.134 -31.882  0.194   1.00 80.10  ? 4   GLY J O   1 
ATOM   17777 N N   . ALA J  2 5   ? -31.519 -29.719  -0.286  1.00 71.58  ? 5   ALA J N   1 
ATOM   17778 C CA  . ALA J  2 5   ? -32.965 -29.897  -0.385  1.00 57.05  ? 5   ALA J CA  1 
ATOM   17779 C C   . ALA J  2 5   ? -33.385 -30.438  -1.750  1.00 65.64  ? 5   ALA J C   1 
ATOM   17780 O O   . ALA J  2 5   ? -33.791 -31.594  -1.871  1.00 59.61  ? 5   ALA J O   1 
ATOM   17781 C CB  . ALA J  2 5   ? -33.686 -28.591  -0.080  1.00 54.94  ? 5   ALA J CB  1 
ATOM   17782 N N   . ILE J  2 6   ? -33.287 -29.596  -2.774  1.00 66.95  ? 6   ILE J N   1 
ATOM   17783 C CA  . ILE J  2 6   ? -33.671 -29.990  -4.124  1.00 46.35  ? 6   ILE J CA  1 
ATOM   17784 C C   . ILE J  2 6   ? -32.697 -31.017  -4.689  1.00 56.51  ? 6   ILE J C   1 
ATOM   17785 O O   . ILE J  2 6   ? -31.486 -30.791  -4.710  1.00 70.60  ? 6   ILE J O   1 
ATOM   17786 C CB  . ILE J  2 6   ? -33.757 -28.777  -5.067  1.00 54.97  ? 6   ILE J CB  1 
ATOM   17787 C CG1 . ILE J  2 6   ? -34.779 -27.770  -4.538  1.00 49.00  ? 6   ILE J CG1 1 
ATOM   17788 C CG2 . ILE J  2 6   ? -34.126 -29.220  -6.474  1.00 47.99  ? 6   ILE J CG2 1 
ATOM   17789 C CD1 . ILE J  2 6   ? -35.036 -26.612  -5.474  1.00 49.49  ? 6   ILE J CD1 1 
ATOM   17790 N N   . ALA J  2 7   ? -33.236 -32.144  -5.144  1.00 53.86  ? 7   ALA J N   1 
ATOM   17791 C CA  . ALA J  2 7   ? -32.419 -33.263  -5.597  1.00 57.47  ? 7   ALA J CA  1 
ATOM   17792 C C   . ALA J  2 7   ? -31.575 -33.797  -4.444  1.00 71.68  ? 7   ALA J C   1 
ATOM   17793 O O   . ALA J  2 7   ? -30.517 -34.392  -4.656  1.00 77.30  ? 7   ALA J O   1 
ATOM   17794 C CB  . ALA J  2 7   ? -31.540 -32.851  -6.768  1.00 58.87  ? 7   ALA J CB  1 
ATOM   17795 N N   . GLY J  2 8   ? -32.055 -33.574  -3.224  1.00 76.59  ? 8   GLY J N   1 
ATOM   17796 C CA  . GLY J  2 8   ? -31.384 -34.046  -2.025  1.00 67.99  ? 8   GLY J CA  1 
ATOM   17797 C C   . GLY J  2 8   ? -32.271 -34.983  -1.227  1.00 82.83  ? 8   GLY J C   1 
ATOM   17798 O O   . GLY J  2 8   ? -32.653 -36.045  -1.717  1.00 83.80  ? 8   GLY J O   1 
ATOM   17799 N N   . PHE J  2 9   ? -32.604 -34.596  0.003   1.00 62.54  ? 9   PHE J N   1 
ATOM   17800 C CA  . PHE J  2 9   ? -33.487 -35.413  0.833   1.00 61.08  ? 9   PHE J CA  1 
ATOM   17801 C C   . PHE J  2 9   ? -34.932 -35.346  0.345   1.00 75.57  ? 9   PHE J C   1 
ATOM   17802 O O   . PHE J  2 9   ? -35.751 -36.203  0.677   1.00 95.93  ? 9   PHE J O   1 
ATOM   17803 C CB  . PHE J  2 9   ? -33.380 -35.045  2.318   1.00 80.36  ? 9   PHE J CB  1 
ATOM   17804 C CG  . PHE J  2 9   ? -33.669 -33.602  2.620   1.00 71.60  ? 9   PHE J CG  1 
ATOM   17805 C CD1 . PHE J  2 9   ? -34.969 -33.125  2.626   1.00 77.21  ? 9   PHE J CD1 1 
ATOM   17806 C CD2 . PHE J  2 9   ? -32.641 -32.730  2.932   1.00 91.57  ? 9   PHE J CD2 1 
ATOM   17807 C CE1 . PHE J  2 9   ? -35.235 -31.799  2.916   1.00 77.86  ? 9   PHE J CE1 1 
ATOM   17808 C CE2 . PHE J  2 9   ? -32.900 -31.405  3.224   1.00 92.25  ? 9   PHE J CE2 1 
ATOM   17809 C CZ  . PHE J  2 9   ? -34.199 -30.939  3.216   1.00 83.94  ? 9   PHE J CZ  1 
ATOM   17810 N N   . ILE J  2 10  ? -35.236 -34.316  -0.436  1.00 72.50  ? 10  ILE J N   1 
ATOM   17811 C CA  . ILE J  2 10  ? -36.470 -34.279  -1.204  1.00 63.66  ? 10  ILE J CA  1 
ATOM   17812 C C   . ILE J  2 10  ? -36.078 -34.620  -2.635  1.00 62.68  ? 10  ILE J C   1 
ATOM   17813 O O   . ILE J  2 10  ? -35.577 -33.771  -3.366  1.00 69.30  ? 10  ILE J O   1 
ATOM   17814 C CB  . ILE J  2 10  ? -37.141 -32.897  -1.149  1.00 49.26  ? 10  ILE J CB  1 
ATOM   17815 C CG1 . ILE J  2 10  ? -37.234 -32.407  0.297   1.00 52.91  ? 10  ILE J CG1 1 
ATOM   17816 C CG2 . ILE J  2 10  ? -38.523 -32.951  -1.778  1.00 51.14  ? 10  ILE J CG2 1 
ATOM   17817 C CD1 . ILE J  2 10  ? -37.936 -31.075  0.451   1.00 57.80  ? 10  ILE J CD1 1 
ATOM   17818 N N   . GLU J  2 11  ? -36.287 -35.874  -3.019  1.00 78.24  ? 11  GLU J N   1 
ATOM   17819 C CA  . GLU J  2 11  ? -35.721 -36.400  -4.258  1.00 86.77  ? 11  GLU J CA  1 
ATOM   17820 C C   . GLU J  2 11  ? -36.349 -35.837  -5.530  1.00 75.84  ? 11  GLU J C   1 
ATOM   17821 O O   . GLU J  2 11  ? -35.661 -35.651  -6.533  1.00 80.19  ? 11  GLU J O   1 
ATOM   17822 C CB  . GLU J  2 11  ? -35.805 -37.928  -4.273  1.00 102.07 ? 11  GLU J CB  1 
ATOM   17823 C CG  . GLU J  2 11  ? -35.157 -38.594  -3.074  1.00 116.30 ? 11  GLU J CG  1 
ATOM   17824 C CD  . GLU J  2 11  ? -35.403 -40.088  -3.039  1.00 154.75 ? 11  GLU J CD  1 
ATOM   17825 O OE1 . GLU J  2 11  ? -34.937 -40.746  -2.084  1.00 160.74 ? 11  GLU J OE1 1 
ATOM   17826 O OE2 . GLU J  2 11  ? -36.063 -40.604  -3.965  1.00 154.64 ? 11  GLU J OE2 1 
ATOM   17827 N N   . GLY J  2 12  ? -37.650 -35.568  -5.494  1.00 75.04  ? 12  GLY J N   1 
ATOM   17828 C CA  . GLY J  2 12  ? -38.355 -35.171  -6.699  1.00 65.38  ? 12  GLY J CA  1 
ATOM   17829 C C   . GLY J  2 12  ? -39.239 -33.946  -6.581  1.00 67.50  ? 12  GLY J C   1 
ATOM   17830 O O   . GLY J  2 12  ? -39.492 -33.445  -5.485  1.00 65.01  ? 12  GLY J O   1 
ATOM   17831 N N   . GLY J  2 13  ? -39.712 -33.467  -7.728  1.00 67.01  ? 13  GLY J N   1 
ATOM   17832 C CA  . GLY J  2 13  ? -40.613 -32.330  -7.778  1.00 62.40  ? 13  GLY J CA  1 
ATOM   17833 C C   . GLY J  2 13  ? -42.043 -32.769  -8.021  1.00 63.06  ? 13  GLY J C   1 
ATOM   17834 O O   . GLY J  2 13  ? -42.303 -33.946  -8.269  1.00 67.36  ? 13  GLY J O   1 
ATOM   17835 N N   . TRP J  2 14  ? -42.973 -31.821  -7.953  1.00 60.63  ? 14  TRP J N   1 
ATOM   17836 C CA  . TRP J  2 14  ? -44.388 -32.131  -8.117  1.00 64.34  ? 14  TRP J CA  1 
ATOM   17837 C C   . TRP J  2 14  ? -44.995 -31.461  -9.344  1.00 73.35  ? 14  TRP J C   1 
ATOM   17838 O O   . TRP J  2 14  ? -45.256 -30.257  -9.340  1.00 78.67  ? 14  TRP J O   1 
ATOM   17839 C CB  . TRP J  2 14  ? -45.177 -31.721  -6.872  1.00 67.88  ? 14  TRP J CB  1 
ATOM   17840 C CG  . TRP J  2 14  ? -44.748 -32.423  -5.625  1.00 74.04  ? 14  TRP J CG  1 
ATOM   17841 C CD1 . TRP J  2 14  ? -44.168 -33.654  -5.534  1.00 71.64  ? 14  TRP J CD1 1 
ATOM   17842 C CD2 . TRP J  2 14  ? -44.881 -31.942  -4.282  1.00 59.09  ? 14  TRP J CD2 1 
ATOM   17843 N NE1 . TRP J  2 14  ? -43.923 -33.966  -4.219  1.00 62.51  ? 14  TRP J NE1 1 
ATOM   17844 C CE2 . TRP J  2 14  ? -44.353 -32.932  -3.430  1.00 66.54  ? 14  TRP J CE2 1 
ATOM   17845 C CE3 . TRP J  2 14  ? -45.392 -30.769  -3.719  1.00 55.94  ? 14  TRP J CE3 1 
ATOM   17846 C CZ2 . TRP J  2 14  ? -44.322 -32.784  -2.045  1.00 74.57  ? 14  TRP J CZ2 1 
ATOM   17847 C CZ3 . TRP J  2 14  ? -45.360 -30.625  -2.344  1.00 72.43  ? 14  TRP J CZ3 1 
ATOM   17848 C CH2 . TRP J  2 14  ? -44.829 -31.627  -1.523  1.00 81.88  ? 14  TRP J CH2 1 
ATOM   17849 N N   . THR J  2 15  ? -45.222 -32.246  -10.392 1.00 72.74  ? 15  THR J N   1 
ATOM   17850 C CA  . THR J  2 15  ? -45.937 -31.760  -11.563 1.00 78.91  ? 15  THR J CA  1 
ATOM   17851 C C   . THR J  2 15  ? -47.326 -31.297  -11.138 1.00 91.39  ? 15  THR J C   1 
ATOM   17852 O O   . THR J  2 15  ? -47.921 -30.416  -11.759 1.00 97.65  ? 15  THR J O   1 
ATOM   17853 C CB  . THR J  2 15  ? -46.088 -32.860  -12.627 1.00 77.66  ? 15  THR J CB  1 
ATOM   17854 O OG1 . THR J  2 15  ? -46.880 -33.931  -12.099 1.00 109.27 ? 15  THR J OG1 1 
ATOM   17855 C CG2 . THR J  2 15  ? -44.725 -33.397  -13.037 1.00 81.27  ? 15  THR J CG2 1 
ATOM   17856 N N   . GLY J  2 16  ? -47.829 -31.897  -10.063 1.00 81.51  ? 16  GLY J N   1 
ATOM   17857 C CA  . GLY J  2 16  ? -49.163 -31.609  -9.567  1.00 86.68  ? 16  GLY J CA  1 
ATOM   17858 C C   . GLY J  2 16  ? -49.359 -30.189  -9.072  1.00 79.97  ? 16  GLY J C   1 
ATOM   17859 O O   . GLY J  2 16  ? -50.423 -29.601  -9.270  1.00 96.05  ? 16  GLY J O   1 
ATOM   17860 N N   . MET J  2 17  ? -48.340 -29.635  -8.423  1.00 80.19  ? 17  MET J N   1 
ATOM   17861 C CA  . MET J  2 17  ? -48.417 -28.271  -7.910  1.00 85.00  ? 17  MET J CA  1 
ATOM   17862 C C   . MET J  2 17  ? -48.066 -27.263  -9.000  1.00 92.79  ? 17  MET J C   1 
ATOM   17863 O O   . MET J  2 17  ? -46.914 -27.167  -9.423  1.00 98.37  ? 17  MET J O   1 
ATOM   17864 C CB  . MET J  2 17  ? -47.494 -28.098  -6.701  1.00 74.26  ? 17  MET J CB  1 
ATOM   17865 C CG  . MET J  2 17  ? -47.552 -26.720  -6.066  1.00 90.19  ? 17  MET J CG  1 
ATOM   17866 S SD  . MET J  2 17  ? -46.514 -26.587  -4.599  1.00 86.81  ? 17  MET J SD  1 
ATOM   17867 C CE  . MET J  2 17  ? -44.921 -27.056  -5.268  1.00 84.76  ? 17  MET J CE  1 
ATOM   17868 N N   . VAL J  2 18  ? -49.067 -26.511  -9.448  1.00 100.11 ? 18  VAL J N   1 
ATOM   17869 C CA  . VAL J  2 18  ? -48.896 -25.583  -10.560 1.00 104.90 ? 18  VAL J CA  1 
ATOM   17870 C C   . VAL J  2 18  ? -49.231 -24.150  -10.160 1.00 103.18 ? 18  VAL J C   1 
ATOM   17871 O O   . VAL J  2 18  ? -49.413 -23.284  -11.017 1.00 104.62 ? 18  VAL J O   1 
ATOM   17872 C CB  . VAL J  2 18  ? -49.783 -25.981  -11.753 1.00 111.87 ? 18  VAL J CB  1 
ATOM   17873 C CG1 . VAL J  2 18  ? -49.440 -27.387  -12.221 1.00 94.26  ? 18  VAL J CG1 1 
ATOM   17874 C CG2 . VAL J  2 18  ? -51.252 -25.887  -11.372 1.00 111.81 ? 18  VAL J CG2 1 
ATOM   17875 N N   . ASP J  2 19  ? -49.312 -23.905  -8.857  1.00 114.44 ? 19  ASP J N   1 
ATOM   17876 C CA  . ASP J  2 19  ? -49.661 -22.584  -8.344  1.00 118.05 ? 19  ASP J CA  1 
ATOM   17877 C C   . ASP J  2 19  ? -48.427 -21.726  -8.076  1.00 106.64 ? 19  ASP J C   1 
ATOM   17878 O O   . ASP J  2 19  ? -48.476 -20.501  -8.195  1.00 108.92 ? 19  ASP J O   1 
ATOM   17879 C CB  . ASP J  2 19  ? -50.516 -22.691  -7.074  1.00 135.22 ? 19  ASP J CB  1 
ATOM   17880 C CG  . ASP J  2 19  ? -50.795 -24.130  -6.664  1.00 139.72 ? 19  ASP J CG  1 
ATOM   17881 O OD1 . ASP J  2 19  ? -51.928 -24.410  -6.220  1.00 133.92 ? 19  ASP J OD1 1 
ATOM   17882 O OD2 . ASP J  2 19  ? -49.887 -24.980  -6.777  1.00 135.63 ? 19  ASP J OD2 1 
ATOM   17883 N N   . GLY J  2 20  ? -47.323 -22.373  -7.716  1.00 95.41  ? 20  GLY J N   1 
ATOM   17884 C CA  . GLY J  2 20  ? -46.090 -21.669  -7.411  1.00 80.13  ? 20  GLY J CA  1 
ATOM   17885 C C   . GLY J  2 20  ? -44.863 -22.555  -7.505  1.00 73.88  ? 20  GLY J C   1 
ATOM   17886 O O   . GLY J  2 20  ? -44.945 -23.698  -7.955  1.00 72.11  ? 20  GLY J O   1 
ATOM   17887 N N   . TRP J  2 21  ? -43.719 -22.026  -7.078  1.00 69.70  ? 21  TRP J N   1 
ATOM   17888 C CA  . TRP J  2 21  ? -42.461 -22.765  -7.139  1.00 66.66  ? 21  TRP J CA  1 
ATOM   17889 C C   . TRP J  2 21  ? -42.261 -23.685  -5.939  1.00 55.17  ? 21  TRP J C   1 
ATOM   17890 O O   . TRP J  2 21  ? -41.720 -24.779  -6.073  1.00 52.30  ? 21  TRP J O   1 
ATOM   17891 C CB  . TRP J  2 21  ? -41.273 -21.810  -7.271  1.00 74.18  ? 21  TRP J CB  1 
ATOM   17892 C CG  . TRP J  2 21  ? -41.028 -21.348  -8.673  1.00 70.94  ? 21  TRP J CG  1 
ATOM   17893 C CD1 . TRP J  2 21  ? -41.365 -22.003  -9.821  1.00 65.31  ? 21  TRP J CD1 1 
ATOM   17894 C CD2 . TRP J  2 21  ? -40.374 -20.139  -9.078  1.00 58.73  ? 21  TRP J CD2 1 
ATOM   17895 N NE1 . TRP J  2 21  ? -40.970 -21.273  -10.916 1.00 58.15  ? 21  TRP J NE1 1 
ATOM   17896 C CE2 . TRP J  2 21  ? -40.358 -20.125  -10.486 1.00 59.89  ? 21  TRP J CE2 1 
ATOM   17897 C CE3 . TRP J  2 21  ? -39.804 -19.067  -8.386  1.00 55.68  ? 21  TRP J CE3 1 
ATOM   17898 C CZ2 . TRP J  2 21  ? -39.795 -19.080  -11.215 1.00 65.33  ? 21  TRP J CZ2 1 
ATOM   17899 C CZ3 . TRP J  2 21  ? -39.245 -18.030  -9.111  1.00 57.49  ? 21  TRP J CZ3 1 
ATOM   17900 C CH2 . TRP J  2 21  ? -39.245 -18.044  -10.511 1.00 60.00  ? 21  TRP J CH2 1 
ATOM   17901 N N   . TYR J  2 22  ? -42.688 -23.233  -4.765  1.00 64.34  ? 22  TYR J N   1 
ATOM   17902 C CA  . TYR J  2 22  ? -42.594 -24.049  -3.561  1.00 66.95  ? 22  TYR J CA  1 
ATOM   17903 C C   . TYR J  2 22  ? -43.954 -24.100  -2.880  1.00 69.62  ? 22  TYR J C   1 
ATOM   17904 O O   . TYR J  2 22  ? -44.707 -23.129  -2.919  1.00 90.74  ? 22  TYR J O   1 
ATOM   17905 C CB  . TYR J  2 22  ? -41.550 -23.477  -2.600  1.00 80.47  ? 22  TYR J CB  1 
ATOM   17906 C CG  . TYR J  2 22  ? -40.513 -22.601  -3.265  1.00 74.35  ? 22  TYR J CG  1 
ATOM   17907 C CD1 . TYR J  2 22  ? -40.652 -21.219  -3.277  1.00 60.19  ? 22  TYR J CD1 1 
ATOM   17908 C CD2 . TYR J  2 22  ? -39.397 -23.152  -3.881  1.00 63.35  ? 22  TYR J CD2 1 
ATOM   17909 C CE1 . TYR J  2 22  ? -39.710 -20.412  -3.882  1.00 61.24  ? 22  TYR J CE1 1 
ATOM   17910 C CE2 . TYR J  2 22  ? -38.449 -22.352  -4.489  1.00 59.29  ? 22  TYR J CE2 1 
ATOM   17911 C CZ  . TYR J  2 22  ? -38.612 -20.983  -4.486  1.00 63.42  ? 22  TYR J CZ  1 
ATOM   17912 O OH  . TYR J  2 22  ? -37.672 -20.180  -5.090  1.00 57.27  ? 22  TYR J OH  1 
ATOM   17913 N N   . GLY J  2 23  ? -44.270 -25.231  -2.259  1.00 92.18  ? 23  GLY J N   1 
ATOM   17914 C CA  . GLY J  2 23  ? -45.551 -25.385  -1.595  1.00 108.82 ? 23  GLY J CA  1 
ATOM   17915 C C   . GLY J  2 23  ? -45.676 -26.652  -0.771  1.00 107.44 ? 23  GLY J C   1 
ATOM   17916 O O   . GLY J  2 23  ? -44.680 -27.303  -0.456  1.00 90.75  ? 23  GLY J O   1 
ATOM   17917 N N   . TYR J  2 24  ? -46.910 -27.005  -0.425  1.00 96.93  ? 24  TYR J N   1 
ATOM   17918 C CA  . TYR J  2 24  ? -47.160 -28.158  0.432   1.00 79.65  ? 24  TYR J CA  1 
ATOM   17919 C C   . TYR J  2 24  ? -48.101 -29.177  -0.206  1.00 86.79  ? 24  TYR J C   1 
ATOM   17920 O O   . TYR J  2 24  ? -48.707 -28.922  -1.245  1.00 88.28  ? 24  TYR J O   1 
ATOM   17921 C CB  . TYR J  2 24  ? -47.747 -27.712  1.774   1.00 76.55  ? 24  TYR J CB  1 
ATOM   17922 C CG  . TYR J  2 24  ? -47.118 -26.466  2.357   1.00 75.46  ? 24  TYR J CG  1 
ATOM   17923 C CD1 . TYR J  2 24  ? -47.530 -25.204  1.950   1.00 80.27  ? 24  TYR J CD1 1 
ATOM   17924 C CD2 . TYR J  2 24  ? -46.128 -26.549  3.327   1.00 76.51  ? 24  TYR J CD2 1 
ATOM   17925 C CE1 . TYR J  2 24  ? -46.968 -24.061  2.482   1.00 87.04  ? 24  TYR J CE1 1 
ATOM   17926 C CE2 . TYR J  2 24  ? -45.558 -25.409  3.867   1.00 80.74  ? 24  TYR J CE2 1 
ATOM   17927 C CZ  . TYR J  2 24  ? -45.983 -24.168  3.440   1.00 86.60  ? 24  TYR J CZ  1 
ATOM   17928 O OH  . TYR J  2 24  ? -45.423 -23.028  3.971   1.00 74.61  ? 24  TYR J OH  1 
ATOM   17929 N N   . HIS J  2 25  ? -48.212 -30.337  0.432   1.00 90.20  ? 25  HIS J N   1 
ATOM   17930 C CA  . HIS J  2 25  ? -49.198 -31.339  0.048   1.00 99.31  ? 25  HIS J CA  1 
ATOM   17931 C C   . HIS J  2 25  ? -49.742 -32.012  1.297   1.00 106.24 ? 25  HIS J C   1 
ATOM   17932 O O   . HIS J  2 25  ? -49.151 -32.953  1.822   1.00 92.05  ? 25  HIS J O   1 
ATOM   17933 C CB  . HIS J  2 25  ? -48.602 -32.384  -0.895  1.00 99.60  ? 25  HIS J CB  1 
ATOM   17934 C CG  . HIS J  2 25  ? -49.474 -33.586  -1.085  1.00 106.39 ? 25  HIS J CG  1 
ATOM   17935 N ND1 . HIS J  2 25  ? -49.268 -34.768  -0.407  1.00 96.92  ? 25  HIS J ND1 1 
ATOM   17936 C CD2 . HIS J  2 25  ? -50.560 -33.787  -1.870  1.00 99.54  ? 25  HIS J CD2 1 
ATOM   17937 C CE1 . HIS J  2 25  ? -50.185 -35.647  -0.770  1.00 104.45 ? 25  HIS J CE1 1 
ATOM   17938 N NE2 . HIS J  2 25  ? -50.981 -35.077  -1.656  1.00 106.35 ? 25  HIS J NE2 1 
ATOM   17939 N N   . HIS J  2 26  ? -50.874 -31.512  1.773   1.00 125.70 ? 26  HIS J N   1 
ATOM   17940 C CA  . HIS J  2 26  ? -51.475 -32.005  2.998   1.00 118.35 ? 26  HIS J CA  1 
ATOM   17941 C C   . HIS J  2 26  ? -52.137 -33.356  2.756   1.00 117.87 ? 26  HIS J C   1 
ATOM   17942 O O   . HIS J  2 26  ? -52.476 -33.696  1.625   1.00 125.98 ? 26  HIS J O   1 
ATOM   17943 C CB  . HIS J  2 26  ? -52.502 -31.001  3.494   1.00 119.14 ? 26  HIS J CB  1 
ATOM   17944 C CG  . HIS J  2 26  ? -53.778 -31.024  2.724   1.00 118.53 ? 26  HIS J CG  1 
ATOM   17945 N ND1 . HIS J  2 26  ? -53.927 -30.406  1.499   1.00 119.45 ? 26  HIS J ND1 1 
ATOM   17946 C CD2 . HIS J  2 26  ? -54.980 -31.589  3.005   1.00 133.50 ? 26  HIS J CD2 1 
ATOM   17947 C CE1 . HIS J  2 26  ? -55.159 -30.592  1.061   1.00 131.91 ? 26  HIS J CE1 1 
ATOM   17948 N NE2 . HIS J  2 26  ? -55.815 -31.303  1.953   1.00 144.30 ? 26  HIS J NE2 1 
ATOM   17949 N N   . GLN J  2 27  ? -52.322 -34.116  3.828   1.00 142.63 ? 27  GLN J N   1 
ATOM   17950 C CA  . GLN J  2 27  ? -52.942 -35.432  3.753   1.00 149.10 ? 27  GLN J CA  1 
ATOM   17951 C C   . GLN J  2 27  ? -53.611 -35.688  5.102   1.00 144.70 ? 27  GLN J C   1 
ATOM   17952 O O   . GLN J  2 27  ? -53.015 -36.303  5.987   1.00 142.38 ? 27  GLN J O   1 
ATOM   17953 C CB  . GLN J  2 27  ? -51.885 -36.500  3.456   1.00 148.52 ? 27  GLN J CB  1 
ATOM   17954 C CG  . GLN J  2 27  ? -52.394 -37.937  3.461   1.00 149.13 ? 27  GLN J CG  1 
ATOM   17955 C CD  . GLN J  2 27  ? -53.248 -38.264  2.250   1.00 162.87 ? 27  GLN J CD  1 
ATOM   17956 O OE1 . GLN J  2 27  ? -52.760 -38.818  1.265   1.00 160.88 ? 27  GLN J OE1 1 
ATOM   17957 N NE2 . GLN J  2 27  ? -54.528 -37.916  2.315   1.00 169.48 ? 27  GLN J NE2 1 
ATOM   17958 N N   . ASN J  2 28  ? -54.841 -35.203  5.267   1.00 145.37 ? 28  ASN J N   1 
ATOM   17959 C CA  . ASN J  2 28  ? -55.577 -35.401  6.515   1.00 147.57 ? 28  ASN J CA  1 
ATOM   17960 C C   . ASN J  2 28  ? -56.885 -36.141  6.247   1.00 155.89 ? 28  ASN J C   1 
ATOM   17961 O O   . ASN J  2 28  ? -56.941 -37.012  5.379   1.00 153.77 ? 28  ASN J O   1 
ATOM   17962 C CB  . ASN J  2 28  ? -55.816 -34.102  7.308   1.00 130.27 ? 28  ASN J CB  1 
ATOM   17963 C CG  . ASN J  2 28  ? -56.705 -33.108  6.573   1.00 133.84 ? 28  ASN J CG  1 
ATOM   17964 O OD1 . ASN J  2 28  ? -57.029 -32.044  7.105   1.00 131.96 ? 28  ASN J OD1 1 
ATOM   17965 N ND2 . ASN J  2 28  ? -57.100 -33.447  5.351   1.00 140.90 ? 28  ASN J ND2 1 
ATOM   17966 N N   . GLU J  2 29  ? -57.936 -35.782  6.978   1.00 139.81 ? 29  GLU J N   1 
ATOM   17967 C CA  . GLU J  2 29  ? -59.192 -36.529  6.928   1.00 137.21 ? 29  GLU J CA  1 
ATOM   17968 C C   . GLU J  2 29  ? -60.242 -35.884  6.029   1.00 138.98 ? 29  GLU J C   1 
ATOM   17969 O O   . GLU J  2 29  ? -61.198 -36.537  5.609   1.00 133.53 ? 29  GLU J O   1 
ATOM   17970 C CB  . GLU J  2 29  ? -59.751 -36.702  8.338   1.00 148.94 ? 29  GLU J CB  1 
ATOM   17971 C CG  . GLU J  2 29  ? -58.783 -37.354  9.302   1.00 149.91 ? 29  GLU J CG  1 
ATOM   17972 C CD  . GLU J  2 29  ? -59.126 -37.047  10.740  1.00 160.88 ? 29  GLU J CD  1 
ATOM   17973 O OE1 . GLU J  2 29  ? -59.725 -35.981  10.984  1.00 158.40 ? 29  GLU J OE1 1 
ATOM   17974 O OE2 . GLU J  2 29  ? -58.799 -37.866  11.624  1.00 157.30 ? 29  GLU J OE2 1 
ATOM   17975 N N   . GLN J  2 30  ? -60.071 -34.596  5.751   1.00 157.79 ? 30  GLN J N   1 
ATOM   17976 C CA  . GLN J  2 30  ? -60.922 -33.924  4.781   1.00 146.31 ? 30  GLN J CA  1 
ATOM   17977 C C   . GLN J  2 30  ? -60.411 -34.194  3.373   1.00 143.49 ? 30  GLN J C   1 
ATOM   17978 O O   . GLN J  2 30  ? -61.187 -34.302  2.436   1.00 143.90 ? 30  GLN J O   1 
ATOM   17979 C CB  . GLN J  2 30  ? -60.990 -32.418  5.040   1.00 138.63 ? 30  GLN J CB  1 
ATOM   17980 C CG  . GLN J  2 30  ? -61.913 -32.011  6.178   1.00 126.15 ? 30  GLN J CG  1 
ATOM   17981 C CD  . GLN J  2 30  ? -61.157 -31.563  7.408   1.00 123.54 ? 30  GLN J CD  1 
ATOM   17982 O OE1 . GLN J  2 30  ? -61.356 -30.455  7.905   1.00 117.18 ? 30  GLN J OE1 1 
ATOM   17983 N NE2 . GLN J  2 30  ? -60.277 -32.420  7.903   1.00 137.08 ? 30  GLN J NE2 1 
ATOM   17984 N N   . GLY J  2 31  ? -59.101 -34.312  3.211   1.00 157.72 ? 31  GLY J N   1 
ATOM   17985 C CA  . GLY J  2 31  ? -58.592 -34.594  1.886   1.00 161.31 ? 31  GLY J CA  1 
ATOM   17986 C C   . GLY J  2 31  ? -57.121 -34.342  1.664   1.00 159.76 ? 31  GLY J C   1 
ATOM   17987 O O   . GLY J  2 31  ? -56.350 -34.180  2.608   1.00 159.09 ? 31  GLY J O   1 
ATOM   17988 N N   . SER J  2 32  ? -56.741 -34.315  0.393   1.00 152.80 ? 32  SER J N   1 
ATOM   17989 C CA  . SER J  2 32  ? -55.354 -34.144  0.007   1.00 142.86 ? 32  SER J CA  1 
ATOM   17990 C C   . SER J  2 32  ? -55.281 -33.143  -1.128  1.00 135.13 ? 32  SER J C   1 
ATOM   17991 O O   . SER J  2 32  ? -56.289 -32.543  -1.506  1.00 143.17 ? 32  SER J O   1 
ATOM   17992 C CB  . SER J  2 32  ? -54.783 -35.479  -0.455  1.00 133.95 ? 32  SER J CB  1 
ATOM   17993 O OG  . SER J  2 32  ? -55.625 -36.540  -0.047  1.00 137.88 ? 32  SER J OG  1 
ATOM   17994 N N   . GLY J  2 33  ? -54.085 -32.971  -1.677  1.00 135.90 ? 33  GLY J N   1 
ATOM   17995 C CA  . GLY J  2 33  ? -53.891 -32.058  -2.782  1.00 142.33 ? 33  GLY J CA  1 
ATOM   17996 C C   . GLY J  2 33  ? -52.674 -31.197  -2.536  1.00 122.70 ? 33  GLY J C   1 
ATOM   17997 O O   . GLY J  2 33  ? -52.056 -31.269  -1.474  1.00 107.47 ? 33  GLY J O   1 
ATOM   17998 N N   . TYR J  2 34  ? -52.330 -30.375  -3.519  1.00 101.80 ? 34  TYR J N   1 
ATOM   17999 C CA  . TYR J  2 34  ? -51.162 -29.516  -3.405  1.00 80.39  ? 34  TYR J CA  1 
ATOM   18000 C C   . TYR J  2 34  ? -51.566 -28.058  -3.215  1.00 75.03  ? 34  TYR J C   1 
ATOM   18001 O O   . TYR J  2 34  ? -52.592 -27.615  -3.731  1.00 93.70  ? 34  TYR J O   1 
ATOM   18002 C CB  . TYR J  2 34  ? -50.285 -29.649  -4.648  1.00 81.39  ? 34  TYR J CB  1 
ATOM   18003 C CG  . TYR J  2 34  ? -49.920 -31.073  -5.009  1.00 81.56  ? 34  TYR J CG  1 
ATOM   18004 C CD1 . TYR J  2 34  ? -50.735 -31.831  -5.841  1.00 74.44  ? 34  TYR J CD1 1 
ATOM   18005 C CD2 . TYR J  2 34  ? -48.752 -31.654  -4.533  1.00 72.34  ? 34  TYR J CD2 1 
ATOM   18006 C CE1 . TYR J  2 34  ? -50.400 -33.129  -6.182  1.00 80.24  ? 34  TYR J CE1 1 
ATOM   18007 C CE2 . TYR J  2 34  ? -48.409 -32.951  -4.868  1.00 70.23  ? 34  TYR J CE2 1 
ATOM   18008 C CZ  . TYR J  2 34  ? -49.237 -33.684  -5.694  1.00 71.29  ? 34  TYR J CZ  1 
ATOM   18009 O OH  . TYR J  2 34  ? -48.903 -34.976  -6.033  1.00 56.86  ? 34  TYR J OH  1 
ATOM   18010 N N   . ALA J  2 35  ? -50.751 -27.317  -2.472  1.00 84.07  ? 35  ALA J N   1 
ATOM   18011 C CA  . ALA J  2 35  ? -50.982 -25.893  -2.264  1.00 88.77  ? 35  ALA J CA  1 
ATOM   18012 C C   . ALA J  2 35  ? -49.660 -25.134  -2.207  1.00 95.11  ? 35  ALA J C   1 
ATOM   18013 O O   . ALA J  2 35  ? -48.874 -25.308  -1.277  1.00 103.46 ? 35  ALA J O   1 
ATOM   18014 C CB  . ALA J  2 35  ? -51.785 -25.664  -0.994  1.00 99.02  ? 35  ALA J CB  1 
ATOM   18015 N N   . ALA J  2 36  ? -49.422 -24.293  -3.207  1.00 85.93  ? 36  ALA J N   1 
ATOM   18016 C CA  . ALA J  2 36  ? -48.179 -23.534  -3.287  1.00 88.70  ? 36  ALA J CA  1 
ATOM   18017 C C   . ALA J  2 36  ? -48.112 -22.441  -2.225  1.00 83.82  ? 36  ALA J C   1 
ATOM   18018 O O   . ALA J  2 36  ? -49.108 -21.774  -1.942  1.00 97.78  ? 36  ALA J O   1 
ATOM   18019 C CB  . ALA J  2 36  ? -48.014 -22.937  -4.674  1.00 92.90  ? 36  ALA J CB  1 
ATOM   18020 N N   . ASP J  2 37  ? -46.931 -22.265  -1.641  1.00 74.26  ? 37  ASP J N   1 
ATOM   18021 C CA  . ASP J  2 37  ? -46.726 -21.236  -0.631  1.00 83.61  ? 37  ASP J CA  1 
ATOM   18022 C C   . ASP J  2 37  ? -46.817 -19.855  -1.262  1.00 97.89  ? 37  ASP J C   1 
ATOM   18023 O O   . ASP J  2 37  ? -46.067 -19.528  -2.181  1.00 95.36  ? 37  ASP J O   1 
ATOM   18024 C CB  . ASP J  2 37  ? -45.374 -21.411  0.059   1.00 80.12  ? 37  ASP J CB  1 
ATOM   18025 C CG  . ASP J  2 37  ? -45.173 -20.435  1.202   1.00 89.94  ? 37  ASP J CG  1 
ATOM   18026 O OD1 . ASP J  2 37  ? -44.063 -20.409  1.772   1.00 106.71 ? 37  ASP J OD1 1 
ATOM   18027 O OD2 . ASP J  2 37  ? -46.123 -19.694  1.533   1.00 93.79  ? 37  ASP J OD2 1 
ATOM   18028 N N   . LEU J  2 38  ? -47.739 -19.047  -0.756  1.00 106.91 ? 38  LEU J N   1 
ATOM   18029 C CA  . LEU J  2 38  ? -48.019 -17.743  -1.339  1.00 109.49 ? 38  LEU J CA  1 
ATOM   18030 C C   . LEU J  2 38  ? -46.837 -16.779  -1.221  1.00 99.63  ? 38  LEU J C   1 
ATOM   18031 O O   . LEU J  2 38  ? -46.301 -16.318  -2.229  1.00 94.22  ? 38  LEU J O   1 
ATOM   18032 C CB  . LEU J  2 38  ? -49.264 -17.137  -0.689  1.00 140.14 ? 38  LEU J CB  1 
ATOM   18033 C CG  . LEU J  2 38  ? -50.249 -16.432  -1.621  1.00 145.54 ? 38  LEU J CG  1 
ATOM   18034 C CD1 . LEU J  2 38  ? -51.441 -15.906  -0.833  1.00 138.18 ? 38  LEU J CD1 1 
ATOM   18035 C CD2 . LEU J  2 38  ? -49.565 -15.318  -2.400  1.00 146.60 ? 38  LEU J CD2 1 
ATOM   18036 N N   . LYS J  2 39  ? -46.432 -16.481  0.010   1.00 122.14 ? 39  LYS J N   1 
ATOM   18037 C CA  . LYS J  2 39  ? -45.388 -15.489  0.256   1.00 126.74 ? 39  LYS J CA  1 
ATOM   18038 C C   . LYS J  2 39  ? -44.031 -15.875  -0.334  1.00 122.53 ? 39  LYS J C   1 
ATOM   18039 O O   . LYS J  2 39  ? -43.312 -15.024  -0.858  1.00 117.95 ? 39  LYS J O   1 
ATOM   18040 C CB  . LYS J  2 39  ? -45.248 -15.218  1.757   1.00 141.71 ? 39  LYS J CB  1 
ATOM   18041 C CG  . LYS J  2 39  ? -44.289 -14.087  2.094   1.00 159.48 ? 39  LYS J CG  1 
ATOM   18042 C CD  . LYS J  2 39  ? -44.322 -13.755  3.577   1.00 174.95 ? 39  LYS J CD  1 
ATOM   18043 C CE  . LYS J  2 39  ? -43.444 -12.556  3.893   1.00 173.97 ? 39  LYS J CE  1 
ATOM   18044 N NZ  . LYS J  2 39  ? -43.535 -12.166  5.327   1.00 163.54 ? 39  LYS J NZ  1 
ATOM   18045 N N   . SER J  2 40  ? -43.685 -17.155  -0.248  1.00 95.76  ? 40  SER J N   1 
ATOM   18046 C CA  . SER J  2 40  ? -42.384 -17.624  -0.714  1.00 87.13  ? 40  SER J CA  1 
ATOM   18047 C C   . SER J  2 40  ? -42.253 -17.533  -2.232  1.00 82.33  ? 40  SER J C   1 
ATOM   18048 O O   . SER J  2 40  ? -41.298 -16.951  -2.747  1.00 89.95  ? 40  SER J O   1 
ATOM   18049 C CB  . SER J  2 40  ? -42.131 -19.059  -0.247  1.00 82.59  ? 40  SER J CB  1 
ATOM   18050 O OG  . SER J  2 40  ? -40.792 -19.447  -0.500  1.00 90.32  ? 40  SER J OG  1 
ATOM   18051 N N   . THR J  2 41  ? -43.214 -18.112  -2.945  1.00 81.73  ? 41  THR J N   1 
ATOM   18052 C CA  . THR J  2 41  ? -43.191 -18.110  -4.403  1.00 72.90  ? 41  THR J CA  1 
ATOM   18053 C C   . THR J  2 41  ? -43.206 -16.691  -4.963  1.00 76.64  ? 41  THR J C   1 
ATOM   18054 O O   . THR J  2 41  ? -42.542 -16.400  -5.958  1.00 74.89  ? 41  THR J O   1 
ATOM   18055 C CB  . THR J  2 41  ? -44.378 -18.896  -4.992  1.00 63.86  ? 41  THR J CB  1 
ATOM   18056 O OG1 . THR J  2 41  ? -44.272 -20.275  -4.619  1.00 73.84  ? 41  THR J OG1 1 
ATOM   18057 C CG2 . THR J  2 41  ? -44.388 -18.786  -6.508  1.00 65.16  ? 41  THR J CG2 1 
ATOM   18058 N N   . GLN J  2 42  ? -43.963 -15.810  -4.317  1.00 87.39  ? 42  GLN J N   1 
ATOM   18059 C CA  . GLN J  2 42  ? -44.079 -14.431  -4.774  1.00 88.83  ? 42  GLN J CA  1 
ATOM   18060 C C   . GLN J  2 42  ? -42.740 -13.702  -4.703  1.00 84.04  ? 42  GLN J C   1 
ATOM   18061 O O   . GLN J  2 42  ? -42.333 -13.041  -5.658  1.00 88.31  ? 42  GLN J O   1 
ATOM   18062 C CB  . GLN J  2 42  ? -45.137 -13.678  -3.965  1.00 99.89  ? 42  GLN J CB  1 
ATOM   18063 C CG  . GLN J  2 42  ? -45.422 -12.281  -4.487  1.00 108.74 ? 42  GLN J CG  1 
ATOM   18064 C CD  . GLN J  2 42  ? -45.862 -12.284  -5.939  1.00 119.67 ? 42  GLN J CD  1 
ATOM   18065 O OE1 . GLN J  2 42  ? -46.473 -13.242  -6.413  1.00 126.21 ? 42  GLN J OE1 1 
ATOM   18066 N NE2 . GLN J  2 42  ? -45.553 -11.207  -6.653  1.00 111.30 ? 42  GLN J NE2 1 
ATOM   18067 N N   . ASN J  2 43  ? -42.059 -13.825  -3.567  1.00 78.24  ? 43  ASN J N   1 
ATOM   18068 C CA  . ASN J  2 43  ? -40.754 -13.196  -3.387  1.00 78.56  ? 43  ASN J CA  1 
ATOM   18069 C C   . ASN J  2 43  ? -39.719 -13.692  -4.391  1.00 74.92  ? 43  ASN J C   1 
ATOM   18070 O O   . ASN J  2 43  ? -38.984 -12.899  -4.979  1.00 70.88  ? 43  ASN J O   1 
ATOM   18071 C CB  . ASN J  2 43  ? -40.242 -13.404  -1.960  1.00 82.42  ? 43  ASN J CB  1 
ATOM   18072 C CG  . ASN J  2 43  ? -40.569 -12.238  -1.047  1.00 96.58  ? 43  ASN J CG  1 
ATOM   18073 O OD1 . ASN J  2 43  ? -41.734 -11.970  -0.755  1.00 105.05 ? 43  ASN J OD1 1 
ATOM   18074 N ND2 . ASN J  2 43  ? -39.537 -11.539  -0.589  1.00 103.50 ? 43  ASN J ND2 1 
ATOM   18075 N N   . ALA J  2 44  ? -39.664 -15.006  -4.579  1.00 71.23  ? 44  ALA J N   1 
ATOM   18076 C CA  . ALA J  2 44  ? -38.727 -15.603  -5.523  1.00 63.90  ? 44  ALA J CA  1 
ATOM   18077 C C   . ALA J  2 44  ? -38.916 -15.017  -6.918  1.00 68.54  ? 44  ALA J C   1 
ATOM   18078 O O   . ALA J  2 44  ? -37.953 -14.602  -7.563  1.00 69.64  ? 44  ALA J O   1 
ATOM   18079 C CB  . ALA J  2 44  ? -38.891 -17.113  -5.552  1.00 49.25  ? 44  ALA J CB  1 
ATOM   18080 N N   . ILE J  2 45  ? -40.163 -14.984  -7.377  1.00 61.50  ? 45  ILE J N   1 
ATOM   18081 C CA  . ILE J  2 45  ? -40.484 -14.419  -8.682  1.00 63.86  ? 45  ILE J CA  1 
ATOM   18082 C C   . ILE J  2 45  ? -39.987 -12.982  -8.798  1.00 65.78  ? 45  ILE J C   1 
ATOM   18083 O O   . ILE J  2 45  ? -39.335 -12.619  -9.776  1.00 63.14  ? 45  ILE J O   1 
ATOM   18084 C CB  . ILE J  2 45  ? -41.998 -14.461  -8.963  1.00 69.66  ? 45  ILE J CB  1 
ATOM   18085 C CG1 . ILE J  2 45  ? -42.438 -15.891  -9.284  1.00 67.74  ? 45  ILE J CG1 1 
ATOM   18086 C CG2 . ILE J  2 45  ? -42.352 -13.534  -10.114 1.00 71.94  ? 45  ILE J CG2 1 
ATOM   18087 C CD1 . ILE J  2 45  ? -43.898 -16.011  -9.667  1.00 78.69  ? 45  ILE J CD1 1 
ATOM   18088 N N   . ASP J  2 46  ? -40.294 -12.170  -7.792  1.00 66.40  ? 46  ASP J N   1 
ATOM   18089 C CA  . ASP J  2 46  ? -39.861 -10.777  -7.773  1.00 67.28  ? 46  ASP J CA  1 
ATOM   18090 C C   . ASP J  2 46  ? -38.342 -10.654  -7.863  1.00 63.11  ? 46  ASP J C   1 
ATOM   18091 O O   . ASP J  2 46  ? -37.819 -9.882   -8.668  1.00 58.05  ? 46  ASP J O   1 
ATOM   18092 C CB  . ASP J  2 46  ? -40.367 -10.075  -6.511  1.00 70.62  ? 46  ASP J CB  1 
ATOM   18093 C CG  . ASP J  2 46  ? -41.858 -9.799   -6.554  1.00 99.08  ? 46  ASP J CG  1 
ATOM   18094 O OD1 . ASP J  2 46  ? -42.446 -9.864   -7.654  1.00 102.98 ? 46  ASP J OD1 1 
ATOM   18095 O OD2 . ASP J  2 46  ? -42.440 -9.508   -5.487  1.00 110.62 ? 46  ASP J OD2 1 
ATOM   18096 N N   . GLU J  2 47  ? -37.638 -11.421  -7.037  1.00 65.03  ? 47  GLU J N   1 
ATOM   18097 C CA  . GLU J  2 47  ? -36.182 -11.334  -6.966  1.00 56.98  ? 47  GLU J CA  1 
ATOM   18098 C C   . GLU J  2 47  ? -35.492 -11.928  -8.192  1.00 55.04  ? 47  GLU J C   1 
ATOM   18099 O O   . GLU J  2 47  ? -34.480 -11.403  -8.655  1.00 57.39  ? 47  GLU J O   1 
ATOM   18100 C CB  . GLU J  2 47  ? -35.662 -11.983  -5.681  1.00 53.34  ? 47  GLU J CB  1 
ATOM   18101 C CG  . GLU J  2 47  ? -36.085 -11.249  -4.419  1.00 65.93  ? 47  GLU J CG  1 
ATOM   18102 C CD  . GLU J  2 47  ? -35.399 -11.774  -3.173  1.00 74.90  ? 47  GLU J CD  1 
ATOM   18103 O OE1 . GLU J  2 47  ? -34.866 -12.902  -3.213  1.00 67.99  ? 47  GLU J OE1 1 
ATOM   18104 O OE2 . GLU J  2 47  ? -35.395 -11.055  -2.151  1.00 81.86  ? 47  GLU J OE2 1 
ATOM   18105 N N   . ILE J  2 48  ? -36.035 -13.022  -8.714  1.00 50.22  ? 48  ILE J N   1 
ATOM   18106 C CA  . ILE J  2 48  ? -35.508 -13.607  -9.941  1.00 42.25  ? 48  ILE J CA  1 
ATOM   18107 C C   . ILE J  2 48  ? -35.746 -12.659  -11.111 1.00 52.06  ? 48  ILE J C   1 
ATOM   18108 O O   . ILE J  2 48  ? -34.893 -12.509  -11.987 1.00 52.71  ? 48  ILE J O   1 
ATOM   18109 C CB  . ILE J  2 48  ? -36.144 -14.973  -10.245 1.00 51.44  ? 48  ILE J CB  1 
ATOM   18110 C CG1 . ILE J  2 48  ? -35.636 -16.026  -9.257  1.00 55.06  ? 48  ILE J CG1 1 
ATOM   18111 C CG2 . ILE J  2 48  ? -35.829 -15.396  -11.667 1.00 37.73  ? 48  ILE J CG2 1 
ATOM   18112 C CD1 . ILE J  2 48  ? -34.128 -16.178  -9.246  1.00 52.82  ? 48  ILE J CD1 1 
ATOM   18113 N N   . THR J  2 49  ? -36.910 -12.018  -11.115 1.00 51.04  ? 49  THR J N   1 
ATOM   18114 C CA  . THR J  2 49  ? -37.225 -11.010  -12.117 1.00 49.44  ? 49  THR J CA  1 
ATOM   18115 C C   . THR J  2 49  ? -36.196 -9.889   -12.066 1.00 56.11  ? 49  THR J C   1 
ATOM   18116 O O   . THR J  2 49  ? -35.608 -9.525   -13.084 1.00 56.05  ? 49  THR J O   1 
ATOM   18117 C CB  . THR J  2 49  ? -38.627 -10.413  -11.901 1.00 59.20  ? 49  THR J CB  1 
ATOM   18118 O OG1 . THR J  2 49  ? -39.620 -11.409  -12.173 1.00 63.56  ? 49  THR J OG1 1 
ATOM   18119 C CG2 . THR J  2 49  ? -38.847 -9.223   -12.824 1.00 51.91  ? 49  THR J CG2 1 
ATOM   18120 N N   . ASN J  2 50  ? -35.981 -9.350   -10.870 1.00 47.94  ? 50  ASN J N   1 
ATOM   18121 C CA  . ASN J  2 50  ? -35.000 -8.291   -10.669 1.00 58.29  ? 50  ASN J CA  1 
ATOM   18122 C C   . ASN J  2 50  ? -33.620 -8.721   -11.151 1.00 57.43  ? 50  ASN J C   1 
ATOM   18123 O O   . ASN J  2 50  ? -32.873 -7.928   -11.725 1.00 53.65  ? 50  ASN J O   1 
ATOM   18124 C CB  . ASN J  2 50  ? -34.944 -7.895   -9.192  1.00 53.96  ? 50  ASN J CB  1 
ATOM   18125 C CG  . ASN J  2 50  ? -34.165 -6.616   -8.962  1.00 59.62  ? 50  ASN J CG  1 
ATOM   18126 O OD1 . ASN J  2 50  ? -34.730 -5.523   -8.977  1.00 68.90  ? 50  ASN J OD1 1 
ATOM   18127 N ND2 . ASN J  2 50  ? -32.862 -6.745   -8.743  1.00 56.50  ? 50  ASN J ND2 1 
ATOM   18128 N N   . LYS J  2 51  ? -33.292 -9.988   -10.916 1.00 44.74  ? 51  LYS J N   1 
ATOM   18129 C CA  . LYS J  2 51  ? -32.019 -10.552  -11.344 1.00 47.63  ? 51  LYS J CA  1 
ATOM   18130 C C   . LYS J  2 51  ? -31.867 -10.466  -12.859 1.00 47.56  ? 51  LYS J C   1 
ATOM   18131 O O   . LYS J  2 51  ? -30.854 -9.982   -13.364 1.00 53.82  ? 51  LYS J O   1 
ATOM   18132 C CB  . LYS J  2 51  ? -31.910 -12.006  -10.881 1.00 57.58  ? 51  LYS J CB  1 
ATOM   18133 C CG  . LYS J  2 51  ? -30.609 -12.693  -11.254 1.00 43.02  ? 51  LYS J CG  1 
ATOM   18134 C CD  . LYS J  2 51  ? -30.474 -14.014  -10.517 1.00 53.21  ? 51  LYS J CD  1 
ATOM   18135 C CE  . LYS J  2 51  ? -29.125 -14.658  -10.774 1.00 50.99  ? 51  LYS J CE  1 
ATOM   18136 N NZ  . LYS J  2 51  ? -28.776 -15.647  -9.716  1.00 58.72  ? 51  LYS J NZ  1 
ATOM   18137 N N   . VAL J  2 52  ? -32.883 -10.932  -13.577 1.00 42.23  ? 52  VAL J N   1 
ATOM   18138 C CA  . VAL J  2 52  ? -32.871 -10.905  -15.035 1.00 45.25  ? 52  VAL J CA  1 
ATOM   18139 C C   . VAL J  2 52  ? -32.818 -9.474   -15.561 1.00 50.04  ? 52  VAL J C   1 
ATOM   18140 O O   . VAL J  2 52  ? -32.115 -9.187   -16.531 1.00 60.71  ? 52  VAL J O   1 
ATOM   18141 C CB  . VAL J  2 52  ? -34.107 -11.611  -15.622 1.00 40.27  ? 52  VAL J CB  1 
ATOM   18142 C CG1 . VAL J  2 52  ? -34.043 -11.620  -17.144 1.00 29.27  ? 52  VAL J CG1 1 
ATOM   18143 C CG2 . VAL J  2 52  ? -34.213 -13.027  -15.078 1.00 44.45  ? 52  VAL J CG2 1 
ATOM   18144 N N   . ASN J  2 53  ? -33.564 -8.580   -14.919 1.00 42.64  ? 53  ASN J N   1 
ATOM   18145 C CA  . ASN J  2 53  ? -33.582 -7.176   -15.315 1.00 54.64  ? 53  ASN J CA  1 
ATOM   18146 C C   . ASN J  2 53  ? -32.223 -6.502   -15.160 1.00 61.35  ? 53  ASN J C   1 
ATOM   18147 O O   . ASN J  2 53  ? -31.848 -5.662   -15.974 1.00 59.59  ? 53  ASN J O   1 
ATOM   18148 C CB  . ASN J  2 53  ? -34.643 -6.402   -14.530 1.00 60.70  ? 53  ASN J CB  1 
ATOM   18149 C CG  . ASN J  2 53  ? -36.035 -6.571   -15.107 1.00 62.12  ? 53  ASN J CG  1 
ATOM   18150 O OD1 . ASN J  2 53  ? -36.209 -7.146   -16.182 1.00 46.95  ? 53  ASN J OD1 1 
ATOM   18151 N ND2 . ASN J  2 53  ? -37.035 -6.062   -14.397 1.00 66.34  ? 53  ASN J ND2 1 
ATOM   18152 N N   . SER J  2 54  ? -31.492 -6.871   -14.113 1.00 54.56  ? 54  SER J N   1 
ATOM   18153 C CA  . SER J  2 54  ? -30.180 -6.286   -13.856 1.00 49.03  ? 54  SER J CA  1 
ATOM   18154 C C   . SER J  2 54  ? -29.186 -6.628   -14.961 1.00 46.48  ? 54  SER J C   1 
ATOM   18155 O O   . SER J  2 54  ? -28.551 -5.741   -15.531 1.00 52.59  ? 54  SER J O   1 
ATOM   18156 C CB  . SER J  2 54  ? -29.639 -6.748   -12.502 1.00 51.45  ? 54  SER J CB  1 
ATOM   18157 O OG  . SER J  2 54  ? -30.463 -6.292   -11.443 1.00 58.38  ? 54  SER J OG  1 
ATOM   18158 N N   . VAL J  2 55  ? -29.057 -7.917   -15.257 1.00 39.17  ? 55  VAL J N   1 
ATOM   18159 C CA  . VAL J  2 55  ? -28.159 -8.377   -16.309 1.00 46.85  ? 55  VAL J CA  1 
ATOM   18160 C C   . VAL J  2 55  ? -28.440 -7.656   -17.625 1.00 53.54  ? 55  VAL J C   1 
ATOM   18161 O O   . VAL J  2 55  ? -27.535 -7.446   -18.429 1.00 49.28  ? 55  VAL J O   1 
ATOM   18162 C CB  . VAL J  2 55  ? -28.277 -9.900   -16.524 1.00 44.96  ? 55  VAL J CB  1 
ATOM   18163 C CG1 . VAL J  2 55  ? -27.449 -10.340  -17.723 1.00 48.81  ? 55  VAL J CG1 1 
ATOM   18164 C CG2 . VAL J  2 55  ? -27.851 -10.647  -15.268 1.00 40.47  ? 55  VAL J CG2 1 
ATOM   18165 N N   . ILE J  2 56  ? -29.698 -7.274   -17.827 1.00 45.11  ? 56  ILE J N   1 
ATOM   18166 C CA  . ILE J  2 56  ? -30.127 -6.608   -19.054 1.00 44.36  ? 56  ILE J CA  1 
ATOM   18167 C C   . ILE J  2 56  ? -30.054 -5.085   -18.964 1.00 50.02  ? 56  ILE J C   1 
ATOM   18168 O O   . ILE J  2 56  ? -29.565 -4.422   -19.876 1.00 46.89  ? 56  ILE J O   1 
ATOM   18169 C CB  . ILE J  2 56  ? -31.575 -6.990   -19.420 1.00 47.98  ? 56  ILE J CB  1 
ATOM   18170 C CG1 . ILE J  2 56  ? -31.664 -8.466   -19.807 1.00 55.52  ? 56  ILE J CG1 1 
ATOM   18171 C CG2 . ILE J  2 56  ? -32.088 -6.114   -20.551 1.00 40.95  ? 56  ILE J CG2 1 
ATOM   18172 C CD1 . ILE J  2 56  ? -33.074 -8.928   -20.114 1.00 48.59  ? 56  ILE J CD1 1 
ATOM   18173 N N   . GLU J  2 57  ? -30.545 -4.531   -17.864 1.00 42.85  ? 57  GLU J N   1 
ATOM   18174 C CA  . GLU J  2 57  ? -30.665 -3.083   -17.741 1.00 53.02  ? 57  GLU J CA  1 
ATOM   18175 C C   . GLU J  2 57  ? -29.305 -2.387   -17.647 1.00 50.33  ? 57  GLU J C   1 
ATOM   18176 O O   . GLU J  2 57  ? -29.169 -1.227   -18.035 1.00 62.61  ? 57  GLU J O   1 
ATOM   18177 C CB  . GLU J  2 57  ? -31.555 -2.723   -16.548 1.00 69.32  ? 57  GLU J CB  1 
ATOM   18178 C CG  . GLU J  2 57  ? -32.090 -1.303   -16.575 1.00 104.17 ? 57  GLU J CG  1 
ATOM   18179 C CD  . GLU J  2 57  ? -31.317 -0.374   -15.665 1.00 117.16 ? 57  GLU J CD  1 
ATOM   18180 O OE1 . GLU J  2 57  ? -30.747 -0.861   -14.666 1.00 106.48 ? 57  GLU J OE1 1 
ATOM   18181 O OE2 . GLU J  2 57  ? -31.285 0.843    -15.944 1.00 105.00 ? 57  GLU J OE2 1 
ATOM   18182 N N   . LYS J  2 58  ? -28.302 -3.111   -17.154 1.00 46.75  ? 58  LYS J N   1 
ATOM   18183 C CA  . LYS J  2 58  ? -26.975 -2.542   -16.908 1.00 42.01  ? 58  LYS J CA  1 
ATOM   18184 C C   . LYS J  2 58  ? -26.134 -2.355   -18.178 1.00 51.94  ? 58  LYS J C   1 
ATOM   18185 O O   . LYS J  2 58  ? -25.093 -1.683   -18.156 1.00 56.56  ? 58  LYS J O   1 
ATOM   18186 C CB  . LYS J  2 58  ? -26.216 -3.370   -15.867 1.00 45.07  ? 58  LYS J CB  1 
ATOM   18187 C CG  . LYS J  2 58  ? -26.777 -3.219   -14.456 1.00 57.25  ? 58  LYS J CG  1 
ATOM   18188 C CD  . LYS J  2 58  ? -26.832 -1.760   -14.035 1.00 51.25  ? 58  LYS J CD  1 
ATOM   18189 C CE  . LYS J  2 58  ? -27.407 -1.629   -12.635 1.00 56.75  ? 58  LYS J CE  1 
ATOM   18190 N NZ  . LYS J  2 58  ? -27.449 -0.214   -12.182 1.00 42.97  ? 58  LYS J NZ  1 
ATOM   18191 N N   . MET J  2 59  ? -26.586 -2.944   -19.281 1.00 49.20  ? 59  MET J N   1 
ATOM   18192 C CA  . MET J  2 59  ? -26.038 -2.599   -20.576 1.00 48.34  ? 59  MET J CA  1 
ATOM   18193 C C   . MET J  2 59  ? -26.635 -1.260   -20.989 1.00 59.77  ? 59  MET J C   1 
ATOM   18194 O O   . MET J  2 59  ? -27.850 -1.046   -20.943 1.00 77.38  ? 59  MET J O   1 
ATOM   18195 C CB  . MET J  2 59  ? -26.340 -3.678   -21.639 1.00 61.53  ? 59  MET J CB  1 
ATOM   18196 C CG  . MET J  2 59  ? -25.458 -3.578   -22.877 1.00 58.12  ? 59  MET J CG  1 
ATOM   18197 S SD  . MET J  2 59  ? -23.713 -3.710   -22.440 1.00 56.53  ? 59  MET J SD  1 
ATOM   18198 C CE  . MET J  2 59  ? -23.384 -5.436   -22.805 1.00 49.95  ? 59  MET J CE  1 
ATOM   18199 N N   . ASN J  2 60  ? -25.766 -0.336   -21.350 1.00 57.97  ? 60  ASN J N   1 
ATOM   18200 C CA  . ASN J  2 60  ? -26.211 0.888    -21.976 1.00 70.57  ? 60  ASN J CA  1 
ATOM   18201 C C   . ASN J  2 60  ? -25.111 1.293    -22.935 1.00 62.33  ? 60  ASN J C   1 
ATOM   18202 O O   . ASN J  2 60  ? -24.141 1.960    -22.572 1.00 70.02  ? 60  ASN J O   1 
ATOM   18203 C CB  . ASN J  2 60  ? -26.529 1.968    -20.937 1.00 85.43  ? 60  ASN J CB  1 
ATOM   18204 C CG  . ASN J  2 60  ? -25.298 2.558    -20.315 1.00 109.42 ? 60  ASN J CG  1 
ATOM   18205 O OD1 . ASN J  2 60  ? -24.751 3.528    -20.831 1.00 118.67 ? 60  ASN J OD1 1 
ATOM   18206 N ND2 . ASN J  2 60  ? -24.854 1.989    -19.196 1.00 93.24  ? 60  ASN J ND2 1 
ATOM   18207 N N   . THR J  2 61  ? -25.259 0.833    -24.167 1.00 63.81  ? 61  THR J N   1 
ATOM   18208 C CA  . THR J  2 61  ? -24.202 0.946    -25.153 1.00 58.58  ? 61  THR J CA  1 
ATOM   18209 C C   . THR J  2 61  ? -24.124 2.336    -25.767 1.00 59.49  ? 61  THR J C   1 
ATOM   18210 O O   . THR J  2 61  ? -25.105 3.079    -25.793 1.00 64.92  ? 61  THR J O   1 
ATOM   18211 C CB  . THR J  2 61  ? -24.362 -0.106   -26.260 1.00 67.96  ? 61  THR J CB  1 
ATOM   18212 O OG1 . THR J  2 61  ? -25.657 0.018    -26.861 1.00 70.17  ? 61  THR J OG1 1 
ATOM   18213 C CG2 . THR J  2 61  ? -24.209 -1.508   -25.684 1.00 56.93  ? 61  THR J CG2 1 
ATOM   18214 N N   . GLN J  2 62  ? -22.940 2.681    -26.256 1.00 60.01  ? 62  GLN J N   1 
ATOM   18215 C CA  . GLN J  2 62  ? -22.736 3.952    -26.929 1.00 66.72  ? 62  GLN J CA  1 
ATOM   18216 C C   . GLN J  2 62  ? -23.218 3.849    -28.363 1.00 65.88  ? 62  GLN J C   1 
ATOM   18217 O O   . GLN J  2 62  ? -23.234 2.765    -28.937 1.00 65.02  ? 62  GLN J O   1 
ATOM   18218 C CB  . GLN J  2 62  ? -21.255 4.325    -26.918 1.00 57.50  ? 62  GLN J CB  1 
ATOM   18219 C CG  . GLN J  2 62  ? -20.709 4.632    -25.543 1.00 54.10  ? 62  GLN J CG  1 
ATOM   18220 C CD  . GLN J  2 62  ? -21.321 5.882    -24.953 1.00 69.44  ? 62  GLN J CD  1 
ATOM   18221 O OE1 . GLN J  2 62  ? -22.464 5.874    -24.496 1.00 86.65  ? 62  GLN J OE1 1 
ATOM   18222 N NE2 . GLN J  2 62  ? -20.562 6.971    -24.964 1.00 63.91  ? 62  GLN J NE2 1 
ATOM   18223 N N   . PHE J  2 63  ? -23.616 4.975    -28.943 1.00 63.56  ? 63  PHE J N   1 
ATOM   18224 C CA  . PHE J  2 63  ? -23.940 4.998    -30.361 1.00 59.78  ? 63  PHE J CA  1 
ATOM   18225 C C   . PHE J  2 63  ? -22.642 4.972    -31.151 1.00 42.98  ? 63  PHE J C   1 
ATOM   18226 O O   . PHE J  2 63  ? -21.922 5.967    -31.213 1.00 60.17  ? 63  PHE J O   1 
ATOM   18227 C CB  . PHE J  2 63  ? -24.753 6.239    -30.730 1.00 52.78  ? 63  PHE J CB  1 
ATOM   18228 C CG  . PHE J  2 63  ? -25.234 6.240    -32.154 1.00 57.26  ? 63  PHE J CG  1 
ATOM   18229 C CD1 . PHE J  2 63  ? -26.539 5.893    -32.457 1.00 51.68  ? 63  PHE J CD1 1 
ATOM   18230 C CD2 . PHE J  2 63  ? -24.378 6.575    -33.189 1.00 50.97  ? 63  PHE J CD2 1 
ATOM   18231 C CE1 . PHE J  2 63  ? -26.984 5.890    -33.765 1.00 56.50  ? 63  PHE J CE1 1 
ATOM   18232 C CE2 . PHE J  2 63  ? -24.815 6.571    -34.499 1.00 56.50  ? 63  PHE J CE2 1 
ATOM   18233 C CZ  . PHE J  2 63  ? -26.120 6.228    -34.787 1.00 64.37  ? 63  PHE J CZ  1 
ATOM   18234 N N   . THR J  2 64  ? -22.343 3.823    -31.744 1.00 45.06  ? 64  THR J N   1 
ATOM   18235 C CA  . THR J  2 64  ? -21.119 3.659    -32.514 1.00 58.34  ? 64  THR J CA  1 
ATOM   18236 C C   . THR J  2 64  ? -21.392 2.953    -33.830 1.00 43.00  ? 64  THR J C   1 
ATOM   18237 O O   . THR J  2 64  ? -22.266 2.091    -33.918 1.00 41.43  ? 64  THR J O   1 
ATOM   18238 C CB  . THR J  2 64  ? -20.068 2.846    -31.737 1.00 57.48  ? 64  THR J CB  1 
ATOM   18239 O OG1 . THR J  2 64  ? -20.688 1.689    -31.162 1.00 53.92  ? 64  THR J OG1 1 
ATOM   18240 C CG2 . THR J  2 64  ? -19.454 3.682    -30.630 1.00 52.33  ? 64  THR J CG2 1 
ATOM   18241 N N   . ALA J  2 65  ? -20.636 3.329    -34.853 1.00 37.98  ? 65  ALA J N   1 
ATOM   18242 C CA  . ALA J  2 65  ? -20.683 2.633    -36.125 1.00 43.81  ? 65  ALA J CA  1 
ATOM   18243 C C   . ALA J  2 65  ? -19.396 1.844    -36.307 1.00 42.83  ? 65  ALA J C   1 
ATOM   18244 O O   . ALA J  2 65  ? -18.456 2.311    -36.950 1.00 59.05  ? 65  ALA J O   1 
ATOM   18245 C CB  . ALA J  2 65  ? -20.873 3.616    -37.265 1.00 42.98  ? 65  ALA J CB  1 
ATOM   18246 N N   . VAL J  2 66  ? -19.348 0.655    -35.718 1.00 41.05  ? 66  VAL J N   1 
ATOM   18247 C CA  . VAL J  2 66  ? -18.216 -0.235   -35.925 1.00 39.00  ? 66  VAL J CA  1 
ATOM   18248 C C   . VAL J  2 66  ? -18.085 -0.529   -37.411 1.00 46.98  ? 66  VAL J C   1 
ATOM   18249 O O   . VAL J  2 66  ? -19.072 -0.491   -38.144 1.00 57.99  ? 66  VAL J O   1 
ATOM   18250 C CB  . VAL J  2 66  ? -18.363 -1.547   -35.126 1.00 30.08  ? 66  VAL J CB  1 
ATOM   18251 C CG1 . VAL J  2 66  ? -19.829 -1.861   -34.882 1.00 39.92  ? 66  VAL J CG1 1 
ATOM   18252 C CG2 . VAL J  2 66  ? -17.656 -2.698   -35.836 1.00 38.82  ? 66  VAL J CG2 1 
ATOM   18253 N N   . GLY J  2 67  ? -16.868 -0.810   -37.858 1.00 46.36  ? 67  GLY J N   1 
ATOM   18254 C CA  . GLY J  2 67  ? -16.626 -1.038   -39.268 1.00 61.27  ? 67  GLY J CA  1 
ATOM   18255 C C   . GLY J  2 67  ? -16.111 0.218    -39.938 1.00 40.90  ? 67  GLY J C   1 
ATOM   18256 O O   . GLY J  2 67  ? -16.774 1.255    -39.934 1.00 33.30  ? 67  GLY J O   1 
ATOM   18257 N N   . LYS J  2 68  ? -14.915 0.121    -40.507 1.00 49.53  ? 68  LYS J N   1 
ATOM   18258 C CA  . LYS J  2 68  ? -14.288 1.248    -41.182 1.00 36.77  ? 68  LYS J CA  1 
ATOM   18259 C C   . LYS J  2 68  ? -13.894 0.840    -42.597 1.00 46.40  ? 68  LYS J C   1 
ATOM   18260 O O   . LYS J  2 68  ? -14.022 -0.327   -42.968 1.00 44.83  ? 68  LYS J O   1 
ATOM   18261 C CB  . LYS J  2 68  ? -13.050 1.704    -40.407 1.00 47.63  ? 68  LYS J CB  1 
ATOM   18262 C CG  . LYS J  2 68  ? -13.305 2.039    -38.942 1.00 45.46  ? 68  LYS J CG  1 
ATOM   18263 C CD  . LYS J  2 68  ? -13.935 3.413    -38.788 1.00 52.18  ? 68  LYS J CD  1 
ATOM   18264 C CE  . LYS J  2 68  ? -14.636 3.551    -37.449 1.00 65.59  ? 68  LYS J CE  1 
ATOM   18265 N NZ  . LYS J  2 68  ? -15.972 4.186    -37.606 1.00 54.83  ? 68  LYS J NZ  1 
ATOM   18266 N N   . GLU J  2 69  ? -13.425 1.800    -43.386 1.00 44.20  ? 69  GLU J N   1 
ATOM   18267 C CA  . GLU J  2 69  ? -12.956 1.513    -44.737 1.00 43.07  ? 69  GLU J CA  1 
ATOM   18268 C C   . GLU J  2 69  ? -11.521 1.994    -44.911 1.00 39.71  ? 69  GLU J C   1 
ATOM   18269 O O   . GLU J  2 69  ? -11.197 3.140    -44.595 1.00 45.24  ? 69  GLU J O   1 
ATOM   18270 C CB  . GLU J  2 69  ? -13.866 2.169    -45.778 1.00 53.94  ? 69  GLU J CB  1 
ATOM   18271 C CG  . GLU J  2 69  ? -15.297 1.660    -45.751 1.00 64.24  ? 69  GLU J CG  1 
ATOM   18272 C CD  . GLU J  2 69  ? -16.217 2.443    -46.667 1.00 67.84  ? 69  GLU J CD  1 
ATOM   18273 O OE1 . GLU J  2 69  ? -15.918 3.622    -46.951 1.00 67.25  ? 69  GLU J OE1 1 
ATOM   18274 O OE2 . GLU J  2 69  ? -17.245 1.879    -47.098 1.00 60.39  ? 69  GLU J OE2 1 
ATOM   18275 N N   . PHE J  2 70  ? -10.663 1.111    -45.410 1.00 35.26  ? 70  PHE J N   1 
ATOM   18276 C CA  . PHE J  2 70  ? -9.262  1.444    -45.626 1.00 41.42  ? 70  PHE J CA  1 
ATOM   18277 C C   . PHE J  2 70  ? -8.829  1.004    -47.018 1.00 43.41  ? 70  PHE J C   1 
ATOM   18278 O O   . PHE J  2 70  ? -9.249  -0.046   -47.503 1.00 51.14  ? 70  PHE J O   1 
ATOM   18279 C CB  . PHE J  2 70  ? -8.380  0.770    -44.571 1.00 42.80  ? 70  PHE J CB  1 
ATOM   18280 C CG  . PHE J  2 70  ? -8.796  1.057    -43.155 1.00 40.33  ? 70  PHE J CG  1 
ATOM   18281 C CD1 . PHE J  2 70  ? -8.456  2.253    -42.546 1.00 33.51  ? 70  PHE J CD1 1 
ATOM   18282 C CD2 . PHE J  2 70  ? -9.519  0.124    -42.430 1.00 38.10  ? 70  PHE J CD2 1 
ATOM   18283 C CE1 . PHE J  2 70  ? -8.835  2.517    -41.243 1.00 38.56  ? 70  PHE J CE1 1 
ATOM   18284 C CE2 . PHE J  2 70  ? -9.900  0.382    -41.126 1.00 33.35  ? 70  PHE J CE2 1 
ATOM   18285 C CZ  . PHE J  2 70  ? -9.558  1.580    -40.532 1.00 33.76  ? 70  PHE J CZ  1 
ATOM   18286 N N   . ASN J  2 71  ? -7.991  1.810    -47.661 1.00 37.97  ? 71  ASN J N   1 
ATOM   18287 C CA  . ASN J  2 71  ? -7.473  1.460    -48.978 1.00 44.45  ? 71  ASN J CA  1 
ATOM   18288 C C   . ASN J  2 71  ? -6.309  0.477    -48.884 1.00 49.98  ? 71  ASN J C   1 
ATOM   18289 O O   . ASN J  2 71  ? -5.850  0.146    -47.790 1.00 48.92  ? 71  ASN J O   1 
ATOM   18290 C CB  . ASN J  2 71  ? -7.075  2.713    -49.765 1.00 40.69  ? 71  ASN J CB  1 
ATOM   18291 C CG  . ASN J  2 71  ? -5.983  3.511    -49.082 1.00 49.91  ? 71  ASN J CG  1 
ATOM   18292 O OD1 . ASN J  2 71  ? -4.928  2.977    -48.742 1.00 59.98  ? 71  ASN J OD1 1 
ATOM   18293 N ND2 . ASN J  2 71  ? -6.228  4.802    -48.889 1.00 61.99  ? 71  ASN J ND2 1 
ATOM   18294 N N   . HIS J  2 72  ? -5.836  0.016    -50.037 1.00 46.02  ? 72  HIS J N   1 
ATOM   18295 C CA  . HIS J  2 72  ? -4.806  -1.018   -50.095 1.00 49.65  ? 72  HIS J CA  1 
ATOM   18296 C C   . HIS J  2 72  ? -3.512  -0.632   -49.379 1.00 51.76  ? 72  HIS J C   1 
ATOM   18297 O O   . HIS J  2 72  ? -2.722  -1.499   -49.005 1.00 63.67  ? 72  HIS J O   1 
ATOM   18298 C CB  . HIS J  2 72  ? -4.511  -1.384   -51.551 1.00 59.99  ? 72  HIS J CB  1 
ATOM   18299 C CG  . HIS J  2 72  ? -4.067  -0.223   -52.387 1.00 80.64  ? 72  HIS J CG  1 
ATOM   18300 N ND1 . HIS J  2 72  ? -4.953  0.662    -52.961 1.00 81.61  ? 72  HIS J ND1 1 
ATOM   18301 C CD2 . HIS J  2 72  ? -2.830  0.195    -52.744 1.00 76.54  ? 72  HIS J CD2 1 
ATOM   18302 C CE1 . HIS J  2 72  ? -4.281  1.578    -53.637 1.00 85.81  ? 72  HIS J CE1 1 
ATOM   18303 N NE2 . HIS J  2 72  ? -2.991  1.316    -53.521 1.00 79.53  ? 72  HIS J NE2 1 
ATOM   18304 N N   . LEU J  2 73  ? -3.298  0.667    -49.191 1.00 40.91  ? 73  LEU J N   1 
ATOM   18305 C CA  . LEU J  2 73  ? -2.086  1.155    -48.539 1.00 45.25  ? 73  LEU J CA  1 
ATOM   18306 C C   . LEU J  2 73  ? -2.320  1.491    -47.069 1.00 38.40  ? 73  LEU J C   1 
ATOM   18307 O O   . LEU J  2 73  ? -1.532  2.209    -46.452 1.00 40.88  ? 73  LEU J O   1 
ATOM   18308 C CB  . LEU J  2 73  ? -1.531  2.373    -49.281 1.00 53.68  ? 73  LEU J CB  1 
ATOM   18309 C CG  . LEU J  2 73  ? -0.912  2.089    -50.651 1.00 48.69  ? 73  LEU J CG  1 
ATOM   18310 C CD1 . LEU J  2 73  ? -0.538  3.384    -51.356 1.00 61.06  ? 73  LEU J CD1 1 
ATOM   18311 C CD2 . LEU J  2 73  ? 0.300   1.183    -50.503 1.00 46.29  ? 73  LEU J CD2 1 
ATOM   18312 N N   . GLU J  2 74  ? -3.407  0.966    -46.514 1.00 33.39  ? 74  GLU J N   1 
ATOM   18313 C CA  . GLU J  2 74  ? -3.741  1.187    -45.113 1.00 41.08  ? 74  GLU J CA  1 
ATOM   18314 C C   . GLU J  2 74  ? -4.067  -0.137   -44.428 1.00 43.46  ? 74  GLU J C   1 
ATOM   18315 O O   . GLU J  2 74  ? -4.884  -0.190   -43.509 1.00 43.44  ? 74  GLU J O   1 
ATOM   18316 C CB  . GLU J  2 74  ? -4.918  2.157    -44.988 1.00 38.51  ? 74  GLU J CB  1 
ATOM   18317 C CG  . GLU J  2 74  ? -4.614  3.563    -45.477 1.00 33.95  ? 74  GLU J CG  1 
ATOM   18318 C CD  . GLU J  2 74  ? -5.829  4.466    -45.439 1.00 58.13  ? 74  GLU J CD  1 
ATOM   18319 O OE1 . GLU J  2 74  ? -6.886  4.062    -45.966 1.00 51.41  ? 74  GLU J OE1 1 
ATOM   18320 O OE2 . GLU J  2 74  ? -5.725  5.582    -44.887 1.00 39.13  ? 74  GLU J OE2 1 
ATOM   18321 N N   . LYS J  2 75  ? -3.421  -1.204   -44.887 1.00 38.15  ? 75  LYS J N   1 
ATOM   18322 C CA  . LYS J  2 75  ? -3.631  -2.530   -44.321 1.00 40.61  ? 75  LYS J CA  1 
ATOM   18323 C C   . LYS J  2 75  ? -3.271  -2.551   -42.841 1.00 40.32  ? 75  LYS J C   1 
ATOM   18324 O O   . LYS J  2 75  ? -3.795  -3.359   -42.075 1.00 41.03  ? 75  LYS J O   1 
ATOM   18325 C CB  . LYS J  2 75  ? -2.801  -3.572   -45.075 1.00 39.53  ? 75  LYS J CB  1 
ATOM   18326 C CG  . LYS J  2 75  ? -2.868  -4.966   -44.471 1.00 49.36  ? 75  LYS J CG  1 
ATOM   18327 C CD  . LYS J  2 75  ? -4.292  -5.505   -44.453 1.00 50.48  ? 75  LYS J CD  1 
ATOM   18328 C CE  . LYS J  2 75  ? -4.747  -5.918   -45.841 1.00 66.97  ? 75  LYS J CE  1 
ATOM   18329 N NZ  . LYS J  2 75  ? -6.134  -6.460   -45.830 1.00 82.59  ? 75  LYS J NZ  1 
ATOM   18330 N N   . ARG J  2 76  ? -2.372  -1.660   -42.441 1.00 44.26  ? 76  ARG J N   1 
ATOM   18331 C CA  . ARG J  2 76  ? -1.940  -1.610   -41.054 1.00 32.12  ? 76  ARG J CA  1 
ATOM   18332 C C   . ARG J  2 76  ? -3.050  -1.155   -40.112 1.00 37.84  ? 76  ARG J C   1 
ATOM   18333 O O   . ARG J  2 76  ? -3.413  -1.874   -39.183 1.00 36.67  ? 76  ARG J O   1 
ATOM   18334 C CB  . ARG J  2 76  ? -0.678  -0.759   -40.893 1.00 38.26  ? 76  ARG J CB  1 
ATOM   18335 C CG  . ARG J  2 76  ? 0.591   -1.508   -41.280 1.00 32.06  ? 76  ARG J CG  1 
ATOM   18336 C CD  . ARG J  2 76  ? 1.810   -0.616   -41.200 1.00 40.21  ? 76  ARG J CD  1 
ATOM   18337 N NE  . ARG J  2 76  ? 1.606   0.624    -41.937 1.00 33.25  ? 76  ARG J NE  1 
ATOM   18338 C CZ  . ARG J  2 76  ? 2.051   1.811    -41.539 1.00 39.64  ? 76  ARG J CZ  1 
ATOM   18339 N NH1 . ARG J  2 76  ? 2.730   1.924    -40.407 1.00 47.56  ? 76  ARG J NH1 1 
ATOM   18340 N NH2 . ARG J  2 76  ? 1.815   2.886    -42.275 1.00 42.14  ? 76  ARG J NH2 1 
ATOM   18341 N N   . ILE J  2 77  ? -3.599  0.029    -40.357 1.00 41.65  ? 77  ILE J N   1 
ATOM   18342 C CA  . ILE J  2 77  ? -4.700  0.516    -39.537 1.00 40.47  ? 77  ILE J CA  1 
ATOM   18343 C C   . ILE J  2 77  ? -5.928  -0.383   -39.674 1.00 36.11  ? 77  ILE J C   1 
ATOM   18344 O O   . ILE J  2 77  ? -6.737  -0.480   -38.753 1.00 39.28  ? 77  ILE J O   1 
ATOM   18345 C CB  . ILE J  2 77  ? -5.068  1.972    -39.871 1.00 34.00  ? 77  ILE J CB  1 
ATOM   18346 C CG1 . ILE J  2 77  ? -5.014  2.203    -41.380 1.00 54.77  ? 77  ILE J CG1 1 
ATOM   18347 C CG2 . ILE J  2 77  ? -4.130  2.936    -39.158 1.00 35.33  ? 77  ILE J CG2 1 
ATOM   18348 C CD1 . ILE J  2 77  ? -5.242  3.644    -41.783 1.00 57.44  ? 77  ILE J CD1 1 
ATOM   18349 N N   . GLU J  2 78  ? -6.059  -1.041   -40.822 1.00 28.12  ? 78  GLU J N   1 
ATOM   18350 C CA  . GLU J  2 78  ? -7.140  -1.999   -41.031 1.00 33.74  ? 78  GLU J CA  1 
ATOM   18351 C C   . GLU J  2 78  ? -7.019  -3.162   -40.050 1.00 38.87  ? 78  GLU J C   1 
ATOM   18352 O O   . GLU J  2 78  ? -8.017  -3.639   -39.509 1.00 45.71  ? 78  GLU J O   1 
ATOM   18353 C CB  . GLU J  2 78  ? -7.129  -2.526   -42.468 1.00 35.35  ? 78  GLU J CB  1 
ATOM   18354 C CG  . GLU J  2 78  ? -8.248  -3.510   -42.771 1.00 39.54  ? 78  GLU J CG  1 
ATOM   18355 C CD  . GLU J  2 78  ? -8.161  -4.090   -44.170 1.00 68.77  ? 78  GLU J CD  1 
ATOM   18356 O OE1 . GLU J  2 78  ? -7.605  -3.418   -45.065 1.00 85.29  ? 78  GLU J OE1 1 
ATOM   18357 O OE2 . GLU J  2 78  ? -8.654  -5.219   -44.375 1.00 79.96  ? 78  GLU J OE2 1 
ATOM   18358 N N   . ASN J  2 79  ? -5.790  -3.614   -39.825 1.00 38.94  ? 79  ASN J N   1 
ATOM   18359 C CA  . ASN J  2 79  ? -5.534  -4.697   -38.882 1.00 36.23  ? 79  ASN J CA  1 
ATOM   18360 C C   . ASN J  2 79  ? -5.611  -4.234   -37.431 1.00 40.88  ? 79  ASN J C   1 
ATOM   18361 O O   . ASN J  2 79  ? -6.025  -4.990   -36.552 1.00 41.56  ? 79  ASN J O   1 
ATOM   18362 C CB  . ASN J  2 79  ? -4.185  -5.357   -39.169 1.00 34.41  ? 79  ASN J CB  1 
ATOM   18363 C CG  . ASN J  2 79  ? -4.232  -6.269   -40.378 1.00 49.24  ? 79  ASN J CG  1 
ATOM   18364 O OD1 . ASN J  2 79  ? -5.273  -6.844   -40.694 1.00 51.10  ? 79  ASN J OD1 1 
ATOM   18365 N ND2 . ASN J  2 79  ? -3.103  -6.410   -41.058 1.00 42.62  ? 79  ASN J ND2 1 
ATOM   18366 N N   . LEU J  2 80  ? -5.212  -2.991   -37.184 1.00 31.29  ? 80  LEU J N   1 
ATOM   18367 C CA  . LEU J  2 80  ? -5.376  -2.400   -35.865 1.00 29.67  ? 80  LEU J CA  1 
ATOM   18368 C C   . LEU J  2 80  ? -6.863  -2.414   -35.538 1.00 36.60  ? 80  LEU J C   1 
ATOM   18369 O O   . LEU J  2 80  ? -7.276  -2.843   -34.460 1.00 39.82  ? 80  LEU J O   1 
ATOM   18370 C CB  . LEU J  2 80  ? -4.856  -0.962   -35.855 1.00 31.51  ? 80  LEU J CB  1 
ATOM   18371 C CG  . LEU J  2 80  ? -4.399  -0.354   -34.525 1.00 30.94  ? 80  LEU J CG  1 
ATOM   18372 C CD1 . LEU J  2 80  ? -4.484  1.166    -34.587 1.00 27.31  ? 80  LEU J CD1 1 
ATOM   18373 C CD2 . LEU J  2 80  ? -5.199  -0.888   -33.348 1.00 32.73  ? 80  LEU J CD2 1 
ATOM   18374 N N   . ASN J  2 81  ? -7.662  -1.945   -36.491 1.00 34.83  ? 81  ASN J N   1 
ATOM   18375 C CA  . ASN J  2 81  ? -9.112  -1.933   -36.360 1.00 33.33  ? 81  ASN J CA  1 
ATOM   18376 C C   . ASN J  2 81  ? -9.676  -3.332   -36.142 1.00 40.88  ? 81  ASN J C   1 
ATOM   18377 O O   . ASN J  2 81  ? -10.557 -3.534   -35.308 1.00 38.14  ? 81  ASN J O   1 
ATOM   18378 C CB  . ASN J  2 81  ? -9.747  -1.302   -37.600 1.00 31.37  ? 81  ASN J CB  1 
ATOM   18379 C CG  . ASN J  2 81  ? -11.260 -1.287   -37.535 1.00 39.93  ? 81  ASN J CG  1 
ATOM   18380 O OD1 . ASN J  2 81  ? -11.848 -0.647   -36.664 1.00 34.97  ? 81  ASN J OD1 1 
ATOM   18381 N ND2 . ASN J  2 81  ? -11.899 -1.989   -38.463 1.00 42.87  ? 81  ASN J ND2 1 
ATOM   18382 N N   . LYS J  2 82  ? -9.170  -4.297   -36.902 1.00 33.43  ? 82  LYS J N   1 
ATOM   18383 C CA  . LYS J  2 82  ? -9.598  -5.681   -36.747 1.00 37.58  ? 82  LYS J CA  1 
ATOM   18384 C C   . LYS J  2 82  ? -9.235  -6.207   -35.363 1.00 43.31  ? 82  LYS J C   1 
ATOM   18385 O O   . LYS J  2 82  ? -9.974  -6.997   -34.775 1.00 35.07  ? 82  LYS J O   1 
ATOM   18386 C CB  . LYS J  2 82  ? -8.973  -6.568   -37.824 1.00 37.61  ? 82  LYS J CB  1 
ATOM   18387 C CG  . LYS J  2 82  ? -9.168  -8.053   -37.575 1.00 55.32  ? 82  LYS J CG  1 
ATOM   18388 C CD  . LYS J  2 82  ? -8.538  -8.893   -38.671 1.00 67.49  ? 82  LYS J CD  1 
ATOM   18389 C CE  . LYS J  2 82  ? -8.515  -10.363  -38.283 1.00 86.26  ? 82  LYS J CE  1 
ATOM   18390 N NZ  . LYS J  2 82  ? -9.872  -10.875  -37.940 1.00 79.61  ? 82  LYS J NZ  1 
ATOM   18391 N N   . LYS J  2 83  ? -8.094  -5.764   -34.845 1.00 45.46  ? 83  LYS J N   1 
ATOM   18392 C CA  . LYS J  2 83  ? -7.646  -6.201   -33.530 1.00 37.45  ? 83  LYS J CA  1 
ATOM   18393 C C   . LYS J  2 83  ? -8.578  -5.708   -32.430 1.00 36.71  ? 83  LYS J C   1 
ATOM   18394 O O   . LYS J  2 83  ? -8.914  -6.456   -31.513 1.00 44.16  ? 83  LYS J O   1 
ATOM   18395 C CB  . LYS J  2 83  ? -6.213  -5.745   -33.246 1.00 28.84  ? 83  LYS J CB  1 
ATOM   18396 C CG  . LYS J  2 83  ? -5.726  -6.157   -31.864 1.00 37.22  ? 83  LYS J CG  1 
ATOM   18397 C CD  . LYS J  2 83  ? -4.233  -5.941   -31.684 1.00 35.88  ? 83  LYS J CD  1 
ATOM   18398 C CE  . LYS J  2 83  ? -3.894  -4.464   -31.606 1.00 36.08  ? 83  LYS J CE  1 
ATOM   18399 N NZ  . LYS J  2 83  ? -2.543  -4.231   -31.030 1.00 41.24  ? 83  LYS J NZ  1 
ATOM   18400 N N   . VAL J  2 84  ? -8.993  -4.448   -32.520 1.00 30.48  ? 84  VAL J N   1 
ATOM   18401 C CA  . VAL J  2 84  ? -9.872  -3.877   -31.506 1.00 40.58  ? 84  VAL J CA  1 
ATOM   18402 C C   . VAL J  2 84  ? -11.258 -4.515   -31.565 1.00 35.22  ? 84  VAL J C   1 
ATOM   18403 O O   . VAL J  2 84  ? -11.954 -4.602   -30.553 1.00 45.39  ? 84  VAL J O   1 
ATOM   18404 C CB  . VAL J  2 84  ? -9.984  -2.342   -31.629 1.00 32.77  ? 84  VAL J CB  1 
ATOM   18405 C CG1 . VAL J  2 84  ? -10.724 -1.957   -32.894 1.00 45.67  ? 84  VAL J CG1 1 
ATOM   18406 C CG2 . VAL J  2 84  ? -10.684 -1.768   -30.410 1.00 48.40  ? 84  VAL J CG2 1 
ATOM   18407 N N   . ASP J  2 85  ? -11.649 -4.965   -32.754 1.00 31.06  ? 85  ASP J N   1 
ATOM   18408 C CA  . ASP J  2 85  ? -12.910 -5.679   -32.921 1.00 33.91  ? 85  ASP J CA  1 
ATOM   18409 C C   . ASP J  2 85  ? -12.818 -7.092   -32.352 1.00 36.53  ? 85  ASP J C   1 
ATOM   18410 O O   . ASP J  2 85  ? -13.725 -7.552   -31.660 1.00 42.45  ? 85  ASP J O   1 
ATOM   18411 C CB  . ASP J  2 85  ? -13.315 -5.736   -34.396 1.00 32.54  ? 85  ASP J CB  1 
ATOM   18412 C CG  . ASP J  2 85  ? -13.912 -4.432   -34.890 1.00 46.81  ? 85  ASP J CG  1 
ATOM   18413 O OD1 . ASP J  2 85  ? -14.241 -3.569   -34.050 1.00 46.30  ? 85  ASP J OD1 1 
ATOM   18414 O OD2 . ASP J  2 85  ? -14.060 -4.276   -36.120 1.00 58.58  ? 85  ASP J OD2 1 
ATOM   18415 N N   . ASP J  2 86  ? -11.717 -7.775   -32.651 1.00 30.56  ? 86  ASP J N   1 
ATOM   18416 C CA  . ASP J  2 86  ? -11.502 -9.136   -32.167 1.00 30.67  ? 86  ASP J CA  1 
ATOM   18417 C C   . ASP J  2 86  ? -11.258 -9.161   -30.664 1.00 42.77  ? 86  ASP J C   1 
ATOM   18418 O O   . ASP J  2 86  ? -11.510 -10.167  -30.001 1.00 43.82  ? 86  ASP J O   1 
ATOM   18419 C CB  . ASP J  2 86  ? -10.330 -9.791   -32.901 1.00 43.74  ? 86  ASP J CB  1 
ATOM   18420 C CG  . ASP J  2 86  ? -10.690 -10.211  -34.311 1.00 68.52  ? 86  ASP J CG  1 
ATOM   18421 O OD1 . ASP J  2 86  ? -11.897 -10.256  -34.628 1.00 71.62  ? 86  ASP J OD1 1 
ATOM   18422 O OD2 . ASP J  2 86  ? -9.765  -10.503  -35.099 1.00 73.92  ? 86  ASP J OD2 1 
ATOM   18423 N N   . GLY J  2 87  ? -10.758 -8.050   -30.135 1.00 34.97  ? 87  GLY J N   1 
ATOM   18424 C CA  . GLY J  2 87  ? -10.548 -7.919   -28.707 1.00 33.55  ? 87  GLY J CA  1 
ATOM   18425 C C   . GLY J  2 87  ? -11.869 -7.845   -27.969 1.00 36.01  ? 87  GLY J C   1 
ATOM   18426 O O   . GLY J  2 87  ? -12.139 -8.648   -27.077 1.00 38.02  ? 87  GLY J O   1 
ATOM   18427 N N   . PHE J  2 88  ? -12.699 -6.878   -28.345 1.00 34.45  ? 88  PHE J N   1 
ATOM   18428 C CA  . PHE J  2 88  ? -14.009 -6.732   -27.726 1.00 35.13  ? 88  PHE J CA  1 
ATOM   18429 C C   . PHE J  2 88  ? -14.817 -8.013   -27.880 1.00 28.24  ? 88  PHE J C   1 
ATOM   18430 O O   . PHE J  2 88  ? -15.574 -8.391   -26.987 1.00 34.48  ? 88  PHE J O   1 
ATOM   18431 C CB  . PHE J  2 88  ? -14.769 -5.542   -28.317 1.00 36.36  ? 88  PHE J CB  1 
ATOM   18432 C CG  . PHE J  2 88  ? -14.144 -4.214   -28.006 1.00 33.44  ? 88  PHE J CG  1 
ATOM   18433 C CD1 . PHE J  2 88  ? -14.353 -3.121   -28.830 1.00 29.54  ? 88  PHE J CD1 1 
ATOM   18434 C CD2 . PHE J  2 88  ? -13.339 -4.062   -26.891 1.00 40.44  ? 88  PHE J CD2 1 
ATOM   18435 C CE1 . PHE J  2 88  ? -13.774 -1.899   -28.541 1.00 36.09  ? 88  PHE J CE1 1 
ATOM   18436 C CE2 . PHE J  2 88  ? -12.757 -2.847   -26.598 1.00 34.25  ? 88  PHE J CE2 1 
ATOM   18437 C CZ  . PHE J  2 88  ? -12.974 -1.763   -27.424 1.00 39.86  ? 88  PHE J CZ  1 
ATOM   18438 N N   . LEU J  2 89  ? -14.644 -8.685   -29.014 1.00 25.97  ? 89  LEU J N   1 
ATOM   18439 C CA  . LEU J  2 89  ? -15.346 -9.936   -29.276 1.00 27.15  ? 89  LEU J CA  1 
ATOM   18440 C C   . LEU J  2 89  ? -14.976 -11.011  -28.259 1.00 37.76  ? 89  LEU J C   1 
ATOM   18441 O O   . LEU J  2 89  ? -15.845 -11.720  -27.749 1.00 43.90  ? 89  LEU J O   1 
ATOM   18442 C CB  . LEU J  2 89  ? -15.053 -10.431  -30.694 1.00 30.92  ? 89  LEU J CB  1 
ATOM   18443 C CG  . LEU J  2 89  ? -15.652 -11.788  -31.073 1.00 36.78  ? 89  LEU J CG  1 
ATOM   18444 C CD1 . LEU J  2 89  ? -17.141 -11.823  -30.766 1.00 34.56  ? 89  LEU J CD1 1 
ATOM   18445 C CD2 . LEU J  2 89  ? -15.392 -12.107  -32.539 1.00 29.12  ? 89  LEU J CD2 1 
ATOM   18446 N N   . ASP J  2 90  ? -13.685 -11.127  -27.967 1.00 31.70  ? 90  ASP J N   1 
ATOM   18447 C CA  . ASP J  2 90  ? -13.198 -12.135  -27.032 1.00 26.69  ? 90  ASP J CA  1 
ATOM   18448 C C   . ASP J  2 90  ? -13.580 -11.823  -25.586 1.00 31.58  ? 90  ASP J C   1 
ATOM   18449 O O   . ASP J  2 90  ? -13.926 -12.724  -24.822 1.00 39.54  ? 90  ASP J O   1 
ATOM   18450 C CB  . ASP J  2 90  ? -11.681 -12.302  -27.164 1.00 33.11  ? 90  ASP J CB  1 
ATOM   18451 C CG  . ASP J  2 90  ? -11.286 -13.059  -28.418 1.00 53.97  ? 90  ASP J CG  1 
ATOM   18452 O OD1 . ASP J  2 90  ? -12.133 -13.804  -28.956 1.00 64.32  ? 90  ASP J OD1 1 
ATOM   18453 O OD2 . ASP J  2 90  ? -10.129 -12.915  -28.865 1.00 64.32  ? 90  ASP J OD2 1 
ATOM   18454 N N   . ILE J  2 91  ? -13.518 -10.549  -25.215 1.00 25.31  ? 91  ILE J N   1 
ATOM   18455 C CA  . ILE J  2 91  ? -13.889 -10.132  -23.867 1.00 33.57  ? 91  ILE J CA  1 
ATOM   18456 C C   . ILE J  2 91  ? -15.365 -10.399  -23.599 1.00 37.68  ? 91  ILE J C   1 
ATOM   18457 O O   . ILE J  2 91  ? -15.722 -11.047  -22.615 1.00 35.24  ? 91  ILE J O   1 
ATOM   18458 C CB  . ILE J  2 91  ? -13.616 -8.634   -23.635 1.00 37.22  ? 91  ILE J CB  1 
ATOM   18459 C CG1 . ILE J  2 91  ? -12.116 -8.343   -23.701 1.00 30.63  ? 91  ILE J CG1 1 
ATOM   18460 C CG2 . ILE J  2 91  ? -14.180 -8.194   -22.293 1.00 43.22  ? 91  ILE J CG2 1 
ATOM   18461 C CD1 . ILE J  2 91  ? -11.775 -6.877   -23.549 1.00 47.77  ? 91  ILE J CD1 1 
ATOM   18462 N N   . TRP J  2 92  ? -16.220 -9.896   -24.482 1.00 33.33  ? 92  TRP J N   1 
ATOM   18463 C CA  . TRP J  2 92  ? -17.662 -10.016  -24.301 1.00 32.31  ? 92  TRP J CA  1 
ATOM   18464 C C   . TRP J  2 92  ? -18.154 -11.456  -24.347 1.00 35.21  ? 92  TRP J C   1 
ATOM   18465 O O   . TRP J  2 92  ? -19.010 -11.849  -23.555 1.00 36.59  ? 92  TRP J O   1 
ATOM   18466 C CB  . TRP J  2 92  ? -18.407 -9.152   -25.319 1.00 28.98  ? 92  TRP J CB  1 
ATOM   18467 C CG  . TRP J  2 92  ? -18.384 -7.711   -24.950 1.00 27.64  ? 92  TRP J CG  1 
ATOM   18468 C CD1 . TRP J  2 92  ? -17.768 -6.697   -25.624 1.00 29.67  ? 92  TRP J CD1 1 
ATOM   18469 C CD2 . TRP J  2 92  ? -18.985 -7.119   -23.794 1.00 27.56  ? 92  TRP J CD2 1 
ATOM   18470 N NE1 . TRP J  2 92  ? -17.962 -5.506   -24.965 1.00 82.86  ? 92  TRP J NE1 1 
ATOM   18471 C CE2 . TRP J  2 92  ? -18.704 -5.739   -23.837 1.00 30.66  ? 92  TRP J CE2 1 
ATOM   18472 C CE3 . TRP J  2 92  ? -19.740 -7.622   -22.729 1.00 28.37  ? 92  TRP J CE3 1 
ATOM   18473 C CZ2 . TRP J  2 92  ? -19.152 -4.856   -22.858 1.00 30.23  ? 92  TRP J CZ2 1 
ATOM   18474 C CZ3 . TRP J  2 92  ? -20.183 -6.745   -21.758 1.00 35.97  ? 92  TRP J CZ3 1 
ATOM   18475 C CH2 . TRP J  2 92  ? -19.887 -5.377   -21.828 1.00 41.10  ? 92  TRP J CH2 1 
ATOM   18476 N N   . THR J  2 93  ? -17.615 -12.241  -25.273 1.00 30.15  ? 93  THR J N   1 
ATOM   18477 C CA  . THR J  2 93  ? -17.980 -13.648  -25.367 1.00 31.06  ? 93  THR J CA  1 
ATOM   18478 C C   . THR J  2 93  ? -17.635 -14.375  -24.074 1.00 31.92  ? 93  THR J C   1 
ATOM   18479 O O   . THR J  2 93  ? -18.480 -15.050  -23.490 1.00 34.36  ? 93  THR J O   1 
ATOM   18480 C CB  . THR J  2 93  ? -17.278 -14.340  -26.546 1.00 33.24  ? 93  THR J CB  1 
ATOM   18481 O OG1 . THR J  2 93  ? -17.728 -13.757  -27.776 1.00 30.80  ? 93  THR J OG1 1 
ATOM   18482 C CG2 . THR J  2 93  ? -17.589 -15.833  -26.551 1.00 30.14  ? 93  THR J CG2 1 
ATOM   18483 N N   . TYR J  2 94  ? -16.394 -14.223  -23.624 1.00 38.98  ? 94  TYR J N   1 
ATOM   18484 C CA  . TYR J  2 94  ? -15.933 -14.893  -22.413 1.00 32.54  ? 94  TYR J CA  1 
ATOM   18485 C C   . TYR J  2 94  ? -16.727 -14.463  -21.182 1.00 31.90  ? 94  TYR J C   1 
ATOM   18486 O O   . TYR J  2 94  ? -17.184 -15.302  -20.406 1.00 36.25  ? 94  TYR J O   1 
ATOM   18487 C CB  . TYR J  2 94  ? -14.438 -14.644  -22.192 1.00 25.46  ? 94  TYR J CB  1 
ATOM   18488 C CG  . TYR J  2 94  ? -13.839 -15.469  -21.074 1.00 38.84  ? 94  TYR J CG  1 
ATOM   18489 C CD1 . TYR J  2 94  ? -13.545 -16.813  -21.260 1.00 41.14  ? 94  TYR J CD1 1 
ATOM   18490 C CD2 . TYR J  2 94  ? -13.561 -14.903  -19.837 1.00 38.08  ? 94  TYR J CD2 1 
ATOM   18491 C CE1 . TYR J  2 94  ? -12.996 -17.572  -20.245 1.00 44.05  ? 94  TYR J CE1 1 
ATOM   18492 C CE2 . TYR J  2 94  ? -13.011 -15.654  -18.815 1.00 39.13  ? 94  TYR J CE2 1 
ATOM   18493 C CZ  . TYR J  2 94  ? -12.731 -16.988  -19.025 1.00 53.10  ? 94  TYR J CZ  1 
ATOM   18494 O OH  . TYR J  2 94  ? -12.183 -17.741  -18.011 1.00 51.36  ? 94  TYR J OH  1 
ATOM   18495 N N   . ASN J  2 95  ? -16.890 -13.156  -21.007 1.00 30.47  ? 95  ASN J N   1 
ATOM   18496 C CA  . ASN J  2 95  ? -17.628 -12.632  -19.863 1.00 33.87  ? 95  ASN J CA  1 
ATOM   18497 C C   . ASN J  2 95  ? -19.093 -13.059  -19.859 1.00 39.76  ? 95  ASN J C   1 
ATOM   18498 O O   . ASN J  2 95  ? -19.628 -13.456  -18.824 1.00 44.07  ? 95  ASN J O   1 
ATOM   18499 C CB  . ASN J  2 95  ? -17.521 -11.107  -19.801 1.00 36.80  ? 95  ASN J CB  1 
ATOM   18500 C CG  . ASN J  2 95  ? -16.133 -10.637  -19.410 1.00 53.64  ? 95  ASN J CG  1 
ATOM   18501 O OD1 . ASN J  2 95  ? -15.170 -11.402  -19.454 1.00 51.07  ? 95  ASN J OD1 1 
ATOM   18502 N ND2 . ASN J  2 95  ? -16.026 -9.371   -19.025 1.00 59.90  ? 95  ASN J ND2 1 
ATOM   18503 N N   . ALA J  2 96  ? -19.736 -12.977  -21.019 1.00 30.24  ? 96  ALA J N   1 
ATOM   18504 C CA  . ALA J  2 96  ? -21.139 -13.359  -21.144 1.00 37.10  ? 96  ALA J CA  1 
ATOM   18505 C C   . ALA J  2 96  ? -21.347 -14.841  -20.841 1.00 41.95  ? 96  ALA J C   1 
ATOM   18506 O O   . ALA J  2 96  ? -22.286 -15.213  -20.138 1.00 43.36  ? 96  ALA J O   1 
ATOM   18507 C CB  . ALA J  2 96  ? -21.662 -13.018  -22.533 1.00 40.74  ? 96  ALA J CB  1 
ATOM   18508 N N   . GLU J  2 97  ? -20.465 -15.682  -21.374 1.00 28.49  ? 97  GLU J N   1 
ATOM   18509 C CA  . GLU J  2 97  ? -20.534 -17.122  -21.140 1.00 36.67  ? 97  GLU J CA  1 
ATOM   18510 C C   . GLU J  2 97  ? -20.369 -17.448  -19.658 1.00 40.73  ? 97  GLU J C   1 
ATOM   18511 O O   . GLU J  2 97  ? -21.144 -18.221  -19.091 1.00 39.13  ? 97  GLU J O   1 
ATOM   18512 C CB  . GLU J  2 97  ? -19.467 -17.853  -21.961 1.00 45.71  ? 97  GLU J CB  1 
ATOM   18513 C CG  . GLU J  2 97  ? -19.686 -17.816  -23.470 1.00 33.56  ? 97  GLU J CG  1 
ATOM   18514 C CD  . GLU J  2 97  ? -20.757 -18.785  -23.940 1.00 50.68  ? 97  GLU J CD  1 
ATOM   18515 O OE1 . GLU J  2 97  ? -20.798 -19.083  -25.152 1.00 47.84  ? 97  GLU J OE1 1 
ATOM   18516 O OE2 . GLU J  2 97  ? -21.553 -19.256  -23.100 1.00 74.83  ? 97  GLU J OE2 1 
ATOM   18517 N N   . LEU J  2 98  ? -19.355 -16.851  -19.037 1.00 34.29  ? 98  LEU J N   1 
ATOM   18518 C CA  . LEU J  2 98  ? -19.080 -17.064  -17.619 1.00 36.80  ? 98  LEU J CA  1 
ATOM   18519 C C   . LEU J  2 98  ? -20.180 -16.492  -16.728 1.00 48.90  ? 98  LEU J C   1 
ATOM   18520 O O   . LEU J  2 98  ? -20.530 -17.084  -15.707 1.00 41.11  ? 98  LEU J O   1 
ATOM   18521 C CB  . LEU J  2 98  ? -17.729 -16.454  -17.238 1.00 31.97  ? 98  LEU J CB  1 
ATOM   18522 C CG  . LEU J  2 98  ? -16.504 -17.372  -17.254 1.00 34.51  ? 98  LEU J CG  1 
ATOM   18523 C CD1 . LEU J  2 98  ? -16.457 -18.246  -16.008 1.00 59.94  ? 98  LEU J CD1 1 
ATOM   18524 C CD2 . LEU J  2 98  ? -16.461 -18.218  -18.518 1.00 46.90  ? 98  LEU J CD2 1 
ATOM   18525 N N   . LEU J  2 99  ? -20.719 -15.340  -17.117 1.00 41.04  ? 99  LEU J N   1 
ATOM   18526 C CA  . LEU J  2 99  ? -21.772 -14.690  -16.343 1.00 44.94  ? 99  LEU J CA  1 
ATOM   18527 C C   . LEU J  2 99  ? -22.994 -15.590  -16.214 1.00 41.05  ? 99  LEU J C   1 
ATOM   18528 O O   . LEU J  2 99  ? -23.553 -15.741  -15.128 1.00 40.43  ? 99  LEU J O   1 
ATOM   18529 C CB  . LEU J  2 99  ? -22.176 -13.360  -16.982 1.00 37.76  ? 99  LEU J CB  1 
ATOM   18530 C CG  . LEU J  2 99  ? -23.283 -12.595  -16.251 1.00 41.44  ? 99  LEU J CG  1 
ATOM   18531 C CD1 . LEU J  2 99  ? -22.824 -12.198  -14.858 1.00 48.94  ? 99  LEU J CD1 1 
ATOM   18532 C CD2 . LEU J  2 99  ? -23.718 -11.371  -17.043 1.00 52.20  ? 99  LEU J CD2 1 
ATOM   18533 N N   . VAL J  2 100 ? -23.404 -16.183  -17.330 1.00 32.58  ? 100 VAL J N   1 
ATOM   18534 C CA  . VAL J  2 100 ? -24.549 -17.085  -17.341 1.00 43.84  ? 100 VAL J CA  1 
ATOM   18535 C C   . VAL J  2 100 ? -24.290 -18.314  -16.477 1.00 41.37  ? 100 VAL J C   1 
ATOM   18536 O O   . VAL J  2 100 ? -25.122 -18.685  -15.650 1.00 50.09  ? 100 VAL J O   1 
ATOM   18537 C CB  . VAL J  2 100 ? -24.908 -17.528  -18.772 1.00 40.49  ? 100 VAL J CB  1 
ATOM   18538 C CG1 . VAL J  2 100 ? -25.925 -18.657  -18.739 1.00 39.70  ? 100 VAL J CG1 1 
ATOM   18539 C CG2 . VAL J  2 100 ? -25.440 -16.349  -19.570 1.00 35.71  ? 100 VAL J CG2 1 
ATOM   18540 N N   . LEU J  2 101 ? -23.132 -18.940  -16.669 1.00 35.81  ? 101 LEU J N   1 
ATOM   18541 C CA  . LEU J  2 101 ? -22.756 -20.106  -15.877 1.00 43.52  ? 101 LEU J CA  1 
ATOM   18542 C C   . LEU J  2 101 ? -22.803 -19.788  -14.387 1.00 45.06  ? 101 LEU J C   1 
ATOM   18543 O O   . LEU J  2 101 ? -23.507 -20.448  -13.623 1.00 47.81  ? 101 LEU J O   1 
ATOM   18544 C CB  . LEU J  2 101 ? -21.359 -20.598  -16.259 1.00 37.64  ? 101 LEU J CB  1 
ATOM   18545 C CG  . LEU J  2 101 ? -21.162 -21.108  -17.687 1.00 36.66  ? 101 LEU J CG  1 
ATOM   18546 C CD1 . LEU J  2 101 ? -19.791 -21.747  -17.838 1.00 36.41  ? 101 LEU J CD1 1 
ATOM   18547 C CD2 . LEU J  2 101 ? -22.251 -22.095  -18.056 1.00 32.28  ? 101 LEU J CD2 1 
ATOM   18548 N N   . LEU J  2 102 ? -22.051 -18.771  -13.982 1.00 45.98  ? 102 LEU J N   1 
ATOM   18549 C CA  . LEU J  2 102 ? -22.006 -18.350  -12.585 1.00 44.27  ? 102 LEU J CA  1 
ATOM   18550 C C   . LEU J  2 102 ? -23.393 -18.066  -12.018 1.00 41.65  ? 102 LEU J C   1 
ATOM   18551 O O   . LEU J  2 102 ? -23.738 -18.541  -10.935 1.00 44.33  ? 102 LEU J O   1 
ATOM   18552 C CB  . LEU J  2 102 ? -21.120 -17.113  -12.433 1.00 50.45  ? 102 LEU J CB  1 
ATOM   18553 C CG  . LEU J  2 102 ? -19.672 -17.329  -11.984 1.00 57.31  ? 102 LEU J CG  1 
ATOM   18554 C CD1 . LEU J  2 102 ? -19.054 -18.570  -12.613 1.00 58.32  ? 102 LEU J CD1 1 
ATOM   18555 C CD2 . LEU J  2 102 ? -18.834 -16.090  -12.268 1.00 77.06  ? 102 LEU J CD2 1 
ATOM   18556 N N   . GLU J  2 103 ? -24.184 -17.289  -12.750 1.00 34.85  ? 103 GLU J N   1 
ATOM   18557 C CA  . GLU J  2 103 ? -25.508 -16.894  -12.279 1.00 42.29  ? 103 GLU J CA  1 
ATOM   18558 C C   . GLU J  2 103 ? -26.490 -18.058  -12.204 1.00 42.92  ? 103 GLU J C   1 
ATOM   18559 O O   . GLU J  2 103 ? -27.299 -18.130  -11.281 1.00 53.05  ? 103 GLU J O   1 
ATOM   18560 C CB  . GLU J  2 103 ? -26.084 -15.767  -13.139 1.00 44.21  ? 103 GLU J CB  1 
ATOM   18561 C CG  . GLU J  2 103 ? -25.447 -14.418  -12.873 1.00 63.21  ? 103 GLU J CG  1 
ATOM   18562 C CD  . GLU J  2 103 ? -25.345 -14.112  -11.390 1.00 81.59  ? 103 GLU J CD  1 
ATOM   18563 O OE1 . GLU J  2 103 ? -26.364 -13.711  -10.790 1.00 75.26  ? 103 GLU J OE1 1 
ATOM   18564 O OE2 . GLU J  2 103 ? -24.244 -14.275  -10.824 1.00 78.53  ? 103 GLU J OE2 1 
ATOM   18565 N N   . ASN J  2 104 ? -26.425 -18.962  -13.176 1.00 37.36  ? 104 ASN J N   1 
ATOM   18566 C CA  . ASN J  2 104 ? -27.277 -20.145  -13.159 1.00 40.63  ? 104 ASN J CA  1 
ATOM   18567 C C   . ASN J  2 104 ? -27.025 -20.991  -11.918 1.00 44.58  ? 104 ASN J C   1 
ATOM   18568 O O   . ASN J  2 104 ? -27.959 -21.499  -11.298 1.00 46.01  ? 104 ASN J O   1 
ATOM   18569 C CB  . ASN J  2 104 ? -27.075 -20.981  -14.423 1.00 32.79  ? 104 ASN J CB  1 
ATOM   18570 C CG  . ASN J  2 104 ? -27.771 -20.386  -15.630 1.00 37.13  ? 104 ASN J CG  1 
ATOM   18571 O OD1 . ASN J  2 104 ? -28.568 -19.457  -15.504 1.00 42.38  ? 104 ASN J OD1 1 
ATOM   18572 N ND2 . ASN J  2 104 ? -27.478 -20.923  -16.809 1.00 43.16  ? 104 ASN J ND2 1 
ATOM   18573 N N   . GLU J  2 105 ? -25.753 -21.136  -11.560 1.00 37.16  ? 105 GLU J N   1 
ATOM   18574 C CA  . GLU J  2 105 ? -25.382 -21.859  -10.353 1.00 41.72  ? 105 GLU J CA  1 
ATOM   18575 C C   . GLU J  2 105 ? -26.005 -21.195  -9.131  1.00 44.84  ? 105 GLU J C   1 
ATOM   18576 O O   . GLU J  2 105 ? -26.514 -21.871  -8.238  1.00 50.87  ? 105 GLU J O   1 
ATOM   18577 C CB  . GLU J  2 105 ? -23.861 -21.918  -10.204 1.00 46.88  ? 105 GLU J CB  1 
ATOM   18578 C CG  . GLU J  2 105 ? -23.402 -22.661  -8.964  1.00 68.08  ? 105 GLU J CG  1 
ATOM   18579 C CD  . GLU J  2 105 ? -23.989 -24.056  -8.879  1.00 107.04 ? 105 GLU J CD  1 
ATOM   18580 O OE1 . GLU J  2 105 ? -24.130 -24.708  -9.936  1.00 101.15 ? 105 GLU J OE1 1 
ATOM   18581 O OE2 . GLU J  2 105 ? -24.310 -24.501  -7.757  1.00 112.25 ? 105 GLU J OE2 1 
ATOM   18582 N N   . ARG J  2 106 ? -25.968 -19.866  -9.104  1.00 47.25  ? 106 ARG J N   1 
ATOM   18583 C CA  . ARG J  2 106 ? -26.532 -19.105  -7.995  1.00 49.24  ? 106 ARG J CA  1 
ATOM   18584 C C   . ARG J  2 106 ? -28.055 -19.185  -7.959  1.00 54.17  ? 106 ARG J C   1 
ATOM   18585 O O   . ARG J  2 106 ? -28.655 -19.232  -6.885  1.00 61.80  ? 106 ARG J O   1 
ATOM   18586 C CB  . ARG J  2 106 ? -26.087 -17.641  -8.058  1.00 50.36  ? 106 ARG J CB  1 
ATOM   18587 C CG  . ARG J  2 106 ? -24.602 -17.430  -7.816  1.00 52.20  ? 106 ARG J CG  1 
ATOM   18588 C CD  . ARG J  2 106 ? -24.298 -15.974  -7.496  1.00 80.06  ? 106 ARG J CD  1 
ATOM   18589 N NE  . ARG J  2 106 ? -25.088 -15.488  -6.368  1.00 85.54  ? 106 ARG J NE  1 
ATOM   18590 C CZ  . ARG J  2 106 ? -24.832 -15.778  -5.097  1.00 79.74  ? 106 ARG J CZ  1 
ATOM   18591 N NH1 . ARG J  2 106 ? -23.810 -16.563  -4.788  1.00 74.77  ? 106 ARG J NH1 1 
ATOM   18592 N NH2 . ARG J  2 106 ? -25.603 -15.291  -4.134  1.00 82.73  ? 106 ARG J NH2 1 
ATOM   18593 N N   . THR J  2 107 ? -28.677 -19.197  -9.134  1.00 45.85  ? 107 THR J N   1 
ATOM   18594 C CA  . THR J  2 107 ? -30.132 -19.246  -9.225  1.00 47.43  ? 107 THR J CA  1 
ATOM   18595 C C   . THR J  2 107 ? -30.678 -20.561  -8.680  1.00 46.09  ? 107 THR J C   1 
ATOM   18596 O O   . THR J  2 107 ? -31.674 -20.578  -7.958  1.00 45.70  ? 107 THR J O   1 
ATOM   18597 C CB  . THR J  2 107 ? -30.620 -19.052  -10.673 1.00 45.03  ? 107 THR J CB  1 
ATOM   18598 O OG1 . THR J  2 107 ? -30.210 -17.764  -11.148 1.00 50.13  ? 107 THR J OG1 1 
ATOM   18599 C CG2 . THR J  2 107 ? -32.138 -19.151  -10.743 1.00 40.29  ? 107 THR J CG2 1 
ATOM   18600 N N   . LEU J  2 108 ? -30.020 -21.661  -9.029  1.00 44.46  ? 108 LEU J N   1 
ATOM   18601 C CA  . LEU J  2 108 ? -30.427 -22.973  -8.541  1.00 45.92  ? 108 LEU J CA  1 
ATOM   18602 C C   . LEU J  2 108 ? -30.223 -23.084  -7.033  1.00 48.20  ? 108 LEU J C   1 
ATOM   18603 O O   . LEU J  2 108 ? -31.075 -23.618  -6.322  1.00 52.88  ? 108 LEU J O   1 
ATOM   18604 C CB  . LEU J  2 108 ? -29.666 -24.081  -9.271  1.00 45.19  ? 108 LEU J CB  1 
ATOM   18605 C CG  . LEU J  2 108 ? -29.937 -24.169  -10.774 1.00 33.61  ? 108 LEU J CG  1 
ATOM   18606 C CD1 . LEU J  2 108 ? -29.240 -25.374  -11.386 1.00 38.61  ? 108 LEU J CD1 1 
ATOM   18607 C CD2 . LEU J  2 108 ? -31.432 -24.229  -11.037 1.00 32.41  ? 108 LEU J CD2 1 
ATOM   18608 N N   . ASP J  2 109 ? -29.094 -22.574  -6.551  1.00 43.31  ? 109 ASP J N   1 
ATOM   18609 C CA  . ASP J  2 109 ? -28.815 -22.561  -5.119  1.00 42.53  ? 109 ASP J CA  1 
ATOM   18610 C C   . ASP J  2 109 ? -29.811 -21.673  -4.381  1.00 51.27  ? 109 ASP J C   1 
ATOM   18611 O O   . ASP J  2 109 ? -30.151 -21.933  -3.227  1.00 53.71  ? 109 ASP J O   1 
ATOM   18612 C CB  . ASP J  2 109 ? -27.384 -22.091  -4.850  1.00 54.80  ? 109 ASP J CB  1 
ATOM   18613 C CG  . ASP J  2 109 ? -26.349 -23.136  -5.219  1.00 76.38  ? 109 ASP J CG  1 
ATOM   18614 O OD1 . ASP J  2 109 ? -26.736 -24.300  -5.455  1.00 76.17  ? 109 ASP J OD1 1 
ATOM   18615 O OD2 . ASP J  2 109 ? -25.148 -22.795  -5.267  1.00 78.22  ? 109 ASP J OD2 1 
ATOM   18616 N N   . TYR J  2 110 ? -30.274 -20.623  -5.053  1.00 45.46  ? 110 TYR J N   1 
ATOM   18617 C CA  . TYR J  2 110 ? -31.268 -19.723  -4.481  1.00 45.48  ? 110 TYR J CA  1 
ATOM   18618 C C   . TYR J  2 110 ? -32.584 -20.454  -4.243  1.00 58.29  ? 110 TYR J C   1 
ATOM   18619 O O   . TYR J  2 110 ? -33.178 -20.352  -3.169  1.00 50.01  ? 110 TYR J O   1 
ATOM   18620 C CB  . TYR J  2 110 ? -31.490 -18.515  -5.395  1.00 42.78  ? 110 TYR J CB  1 
ATOM   18621 C CG  . TYR J  2 110 ? -32.665 -17.651  -4.994  1.00 41.83  ? 110 TYR J CG  1 
ATOM   18622 C CD1 . TYR J  2 110 ? -32.526 -16.657  -4.034  1.00 40.10  ? 110 TYR J CD1 1 
ATOM   18623 C CD2 . TYR J  2 110 ? -33.912 -17.829  -5.577  1.00 46.29  ? 110 TYR J CD2 1 
ATOM   18624 C CE1 . TYR J  2 110 ? -33.598 -15.866  -3.665  1.00 43.35  ? 110 TYR J CE1 1 
ATOM   18625 C CE2 . TYR J  2 110 ? -34.989 -17.044  -5.215  1.00 50.88  ? 110 TYR J CE2 1 
ATOM   18626 C CZ  . TYR J  2 110 ? -34.827 -16.064  -4.259  1.00 55.04  ? 110 TYR J CZ  1 
ATOM   18627 O OH  . TYR J  2 110 ? -35.898 -15.280  -3.896  1.00 64.08  ? 110 TYR J OH  1 
ATOM   18628 N N   . HIS J  2 111 ? -33.035 -21.191  -5.253  1.00 53.44  ? 111 HIS J N   1 
ATOM   18629 C CA  . HIS J  2 111 ? -34.262 -21.968  -5.143  1.00 48.27  ? 111 HIS J CA  1 
ATOM   18630 C C   . HIS J  2 111 ? -34.107 -23.088  -4.123  1.00 54.73  ? 111 HIS J C   1 
ATOM   18631 O O   . HIS J  2 111 ? -34.972 -23.291  -3.271  1.00 52.31  ? 111 HIS J O   1 
ATOM   18632 C CB  . HIS J  2 111 ? -34.653 -22.554  -6.499  1.00 41.92  ? 111 HIS J CB  1 
ATOM   18633 C CG  . HIS J  2 111 ? -35.168 -21.540  -7.472  1.00 47.40  ? 111 HIS J CG  1 
ATOM   18634 N ND1 . HIS J  2 111 ? -36.365 -20.881  -7.295  1.00 55.22  ? 111 HIS J ND1 1 
ATOM   18635 C CD2 . HIS J  2 111 ? -34.656 -21.086  -8.642  1.00 47.25  ? 111 HIS J CD2 1 
ATOM   18636 C CE1 . HIS J  2 111 ? -36.564 -20.056  -8.309  1.00 60.03  ? 111 HIS J CE1 1 
ATOM   18637 N NE2 . HIS J  2 111 ? -35.545 -20.162  -9.139  1.00 53.45  ? 111 HIS J NE2 1 
ATOM   18638 N N   . ASP J  2 112 ? -32.999 -23.816  -4.222  1.00 42.06  ? 112 ASP J N   1 
ATOM   18639 C CA  . ASP J  2 112 ? -32.695 -24.885  -3.281  1.00 47.30  ? 112 ASP J CA  1 
ATOM   18640 C C   . ASP J  2 112 ? -32.809 -24.357  -1.859  1.00 49.12  ? 112 ASP J C   1 
ATOM   18641 O O   . ASP J  2 112 ? -33.337 -25.026  -0.971  1.00 57.36  ? 112 ASP J O   1 
ATOM   18642 C CB  . ASP J  2 112 ? -31.282 -25.416  -3.525  1.00 62.98  ? 112 ASP J CB  1 
ATOM   18643 C CG  . ASP J  2 112 ? -30.974 -26.650  -2.704  1.00 57.76  ? 112 ASP J CG  1 
ATOM   18644 O OD1 . ASP J  2 112 ? -29.780 -26.959  -2.518  1.00 68.93  ? 112 ASP J OD1 1 
ATOM   18645 O OD2 . ASP J  2 112 ? -31.927 -27.312  -2.245  1.00 69.39  ? 112 ASP J OD2 1 
ATOM   18646 N N   . SER J  2 113 ? -32.314 -23.141  -1.659  1.00 51.84  ? 113 SER J N   1 
ATOM   18647 C CA  . SER J  2 113 ? -32.330 -22.500  -0.353  1.00 50.17  ? 113 SER J CA  1 
ATOM   18648 C C   . SER J  2 113 ? -33.744 -22.266  0.167   1.00 55.66  ? 113 SER J C   1 
ATOM   18649 O O   . SER J  2 113 ? -34.052 -22.589  1.314   1.00 62.84  ? 113 SER J O   1 
ATOM   18650 C CB  . SER J  2 113 ? -31.584 -21.170  -0.414  1.00 43.62  ? 113 SER J CB  1 
ATOM   18651 O OG  . SER J  2 113 ? -31.950 -20.352  0.679   1.00 66.38  ? 113 SER J OG  1 
ATOM   18652 N N   . ASN J  2 114 ? -34.597 -21.696  -0.676  1.00 55.74  ? 114 ASN J N   1 
ATOM   18653 C CA  . ASN J  2 114 ? -35.966 -21.387  -0.278  1.00 61.99  ? 114 ASN J CA  1 
ATOM   18654 C C   . ASN J  2 114 ? -36.735 -22.624  0.174   1.00 63.95  ? 114 ASN J C   1 
ATOM   18655 O O   . ASN J  2 114 ? -37.536 -22.560  1.106   1.00 63.57  ? 114 ASN J O   1 
ATOM   18656 C CB  . ASN J  2 114 ? -36.708 -20.675  -1.410  1.00 52.94  ? 114 ASN J CB  1 
ATOM   18657 C CG  . ASN J  2 114 ? -36.111 -19.319  -1.733  1.00 56.51  ? 114 ASN J CG  1 
ATOM   18658 O OD1 . ASN J  2 114 ? -35.415 -18.722  -0.911  1.00 74.50  ? 114 ASN J OD1 1 
ATOM   18659 N ND2 . ASN J  2 114 ? -36.384 -18.824  -2.933  1.00 62.03  ? 114 ASN J ND2 1 
ATOM   18660 N N   . VAL J  2 115 ? -36.487 -23.749  -0.490  1.00 55.45  ? 115 VAL J N   1 
ATOM   18661 C CA  . VAL J  2 115 ? -37.091 -25.015  -0.095  1.00 51.74  ? 115 VAL J CA  1 
ATOM   18662 C C   . VAL J  2 115 ? -36.621 -25.407  1.302   1.00 52.75  ? 115 VAL J C   1 
ATOM   18663 O O   . VAL J  2 115 ? -37.430 -25.621  2.204   1.00 51.72  ? 115 VAL J O   1 
ATOM   18664 C CB  . VAL J  2 115 ? -36.739 -26.143  -1.081  1.00 52.80  ? 115 VAL J CB  1 
ATOM   18665 C CG1 . VAL J  2 115 ? -37.228 -27.480  -0.552  1.00 56.79  ? 115 VAL J CG1 1 
ATOM   18666 C CG2 . VAL J  2 115 ? -37.337 -25.859  -2.449  1.00 45.15  ? 115 VAL J CG2 1 
ATOM   18667 N N   . LYS J  2 116 ? -35.304 -25.495  1.468   1.00 52.89  ? 116 LYS J N   1 
ATOM   18668 C CA  . LYS J  2 116 ? -34.696 -25.800  2.758   1.00 61.64  ? 116 LYS J CA  1 
ATOM   18669 C C   . LYS J  2 116 ? -35.279 -24.922  3.860   1.00 64.94  ? 116 LYS J C   1 
ATOM   18670 O O   . LYS J  2 116 ? -35.586 -25.401  4.952   1.00 65.25  ? 116 LYS J O   1 
ATOM   18671 C CB  . LYS J  2 116 ? -33.181 -25.600  2.683   1.00 62.88  ? 116 LYS J CB  1 
ATOM   18672 C CG  . LYS J  2 116 ? -32.470 -25.599  4.028   1.00 56.47  ? 116 LYS J CG  1 
ATOM   18673 C CD  . LYS J  2 116 ? -31.942 -26.977  4.392   1.00 74.47  ? 116 LYS J CD  1 
ATOM   18674 C CE  . LYS J  2 116 ? -31.003 -26.902  5.586   1.00 84.25  ? 116 LYS J CE  1 
ATOM   18675 N NZ  . LYS J  2 116 ? -30.317 -28.198  5.847   1.00 103.25 ? 116 LYS J NZ  1 
ATOM   18676 N N   . ASN J  2 117 ? -35.428 -23.635  3.564   1.00 55.15  ? 117 ASN J N   1 
ATOM   18677 C CA  . ASN J  2 117 ? -35.973 -22.682  4.524   1.00 60.90  ? 117 ASN J CA  1 
ATOM   18678 C C   . ASN J  2 117 ? -37.434 -22.955  4.858   1.00 69.62  ? 117 ASN J C   1 
ATOM   18679 O O   . ASN J  2 117 ? -37.851 -22.825  6.009   1.00 75.62  ? 117 ASN J O   1 
ATOM   18680 C CB  . ASN J  2 117 ? -35.805 -21.248  4.018   1.00 56.10  ? 117 ASN J CB  1 
ATOM   18681 C CG  . ASN J  2 117 ? -34.380 -20.752  4.147   1.00 55.94  ? 117 ASN J CG  1 
ATOM   18682 O OD1 . ASN J  2 117 ? -33.560 -21.364  4.831   1.00 64.46  ? 117 ASN J OD1 1 
ATOM   18683 N ND2 . ASN J  2 117 ? -34.078 -19.635  3.495   1.00 66.81  ? 117 ASN J ND2 1 
ATOM   18684 N N   . LEU J  2 118 ? -38.208 -23.333  3.847   1.00 70.27  ? 118 LEU J N   1 
ATOM   18685 C CA  . LEU J  2 118 ? -39.613 -23.657  4.047   1.00 63.54  ? 118 LEU J CA  1 
ATOM   18686 C C   . LEU J  2 118 ? -39.730 -24.887  4.938   1.00 61.56  ? 118 LEU J C   1 
ATOM   18687 O O   . LEU J  2 118 ? -40.557 -24.935  5.849   1.00 82.57  ? 118 LEU J O   1 
ATOM   18688 C CB  . LEU J  2 118 ? -40.301 -23.904  2.704   1.00 65.09  ? 118 LEU J CB  1 
ATOM   18689 C CG  . LEU J  2 118 ? -41.771 -23.493  2.627   1.00 62.82  ? 118 LEU J CG  1 
ATOM   18690 C CD1 . LEU J  2 118 ? -41.931 -22.060  3.104   1.00 71.79  ? 118 LEU J CD1 1 
ATOM   18691 C CD2 . LEU J  2 118 ? -42.302 -23.658  1.212   1.00 76.25  ? 118 LEU J CD2 1 
ATOM   18692 N N   . TYR J  2 119 ? -38.888 -25.879  4.668   1.00 55.44  ? 119 TYR J N   1 
ATOM   18693 C CA  . TYR J  2 119 ? -38.840 -27.096  5.468   1.00 64.36  ? 119 TYR J CA  1 
ATOM   18694 C C   . TYR J  2 119 ? -38.487 -26.779  6.918   1.00 68.00  ? 119 TYR J C   1 
ATOM   18695 O O   . TYR J  2 119 ? -39.163 -27.225  7.845   1.00 78.27  ? 119 TYR J O   1 
ATOM   18696 C CB  . TYR J  2 119 ? -37.819 -28.071  4.880   1.00 64.59  ? 119 TYR J CB  1 
ATOM   18697 C CG  . TYR J  2 119 ? -37.630 -29.336  5.686   1.00 78.70  ? 119 TYR J CG  1 
ATOM   18698 C CD1 . TYR J  2 119 ? -38.364 -30.479  5.402   1.00 84.32  ? 119 TYR J CD1 1 
ATOM   18699 C CD2 . TYR J  2 119 ? -36.714 -29.388  6.729   1.00 84.19  ? 119 TYR J CD2 1 
ATOM   18700 C CE1 . TYR J  2 119 ? -38.192 -31.638  6.133   1.00 93.37  ? 119 TYR J CE1 1 
ATOM   18701 C CE2 . TYR J  2 119 ? -36.537 -30.542  7.467   1.00 99.02  ? 119 TYR J CE2 1 
ATOM   18702 C CZ  . TYR J  2 119 ? -37.278 -31.663  7.166   1.00 98.83  ? 119 TYR J CZ  1 
ATOM   18703 O OH  . TYR J  2 119 ? -37.105 -32.814  7.900   1.00 99.69  ? 119 TYR J OH  1 
ATOM   18704 N N   . GLU J  2 120 ? -37.422 -26.005  7.104   1.00 76.41  ? 120 GLU J N   1 
ATOM   18705 C CA  . GLU J  2 120 ? -36.962 -25.634  8.438   1.00 74.02  ? 120 GLU J CA  1 
ATOM   18706 C C   . GLU J  2 120 ? -38.014 -24.849  9.214   1.00 71.35  ? 120 GLU J C   1 
ATOM   18707 O O   . GLU J  2 120 ? -38.224 -25.090  10.402  1.00 91.42  ? 120 GLU J O   1 
ATOM   18708 C CB  . GLU J  2 120 ? -35.661 -24.831  8.355   1.00 93.40  ? 120 GLU J CB  1 
ATOM   18709 C CG  . GLU J  2 120 ? -34.406 -25.686  8.290   1.00 103.67 ? 120 GLU J CG  1 
ATOM   18710 C CD  . GLU J  2 120 ? -34.140 -26.427  9.586   1.00 132.38 ? 120 GLU J CD  1 
ATOM   18711 O OE1 . GLU J  2 120 ? -34.622 -25.969  10.645  1.00 123.87 ? 120 GLU J OE1 1 
ATOM   18712 O OE2 . GLU J  2 120 ? -33.446 -27.464  9.549   1.00 140.63 ? 120 GLU J OE2 1 
ATOM   18713 N N   . LYS J  2 121 ? -38.671 -23.910  8.541   1.00 74.35  ? 121 LYS J N   1 
ATOM   18714 C CA  . LYS J  2 121 ? -39.674 -23.074  9.192   1.00 84.10  ? 121 LYS J CA  1 
ATOM   18715 C C   . LYS J  2 121 ? -40.815 -23.912  9.761   1.00 93.20  ? 121 LYS J C   1 
ATOM   18716 O O   . LYS J  2 121 ? -41.378 -23.584  10.806  1.00 108.46 ? 121 LYS J O   1 
ATOM   18717 C CB  . LYS J  2 121 ? -40.220 -22.024  8.222   1.00 82.95  ? 121 LYS J CB  1 
ATOM   18718 C CG  . LYS J  2 121 ? -41.166 -21.029  8.874   1.00 105.79 ? 121 LYS J CG  1 
ATOM   18719 C CD  . LYS J  2 121 ? -41.660 -19.987  7.885   1.00 110.10 ? 121 LYS J CD  1 
ATOM   18720 C CE  . LYS J  2 121 ? -42.579 -18.988  8.568   1.00 115.86 ? 121 LYS J CE  1 
ATOM   18721 N NZ  . LYS J  2 121 ? -43.112 -17.975  7.618   1.00 125.65 ? 121 LYS J NZ  1 
ATOM   18722 N N   . VAL J  2 122 ? -41.152 -24.994  9.068   1.00 91.42  ? 122 VAL J N   1 
ATOM   18723 C CA  . VAL J  2 122 ? -42.181 -25.913  9.537   1.00 85.48  ? 122 VAL J CA  1 
ATOM   18724 C C   . VAL J  2 122 ? -41.655 -26.779  10.671  1.00 87.95  ? 122 VAL J C   1 
ATOM   18725 O O   . VAL J  2 122 ? -42.334 -26.983  11.677  1.00 113.14 ? 122 VAL J O   1 
ATOM   18726 C CB  . VAL J  2 122 ? -42.677 -26.827  8.403   1.00 80.77  ? 122 VAL J CB  1 
ATOM   18727 C CG1 . VAL J  2 122 ? -43.369 -28.061  8.971   1.00 93.66  ? 122 VAL J CG1 1 
ATOM   18728 C CG2 . VAL J  2 122 ? -43.604 -26.059  7.474   1.00 82.77  ? 122 VAL J CG2 1 
ATOM   18729 N N   . ARG J  2 123 ? -40.436 -27.277  10.502  1.00 85.47  ? 123 ARG J N   1 
ATOM   18730 C CA  . ARG J  2 123 ? -39.841 -28.203  11.456  1.00 93.83  ? 123 ARG J CA  1 
ATOM   18731 C C   . ARG J  2 123 ? -39.609 -27.554  12.819  1.00 94.85  ? 123 ARG J C   1 
ATOM   18732 O O   . ARG J  2 123 ? -39.946 -28.132  13.850  1.00 104.00 ? 123 ARG J O   1 
ATOM   18733 C CB  . ARG J  2 123 ? -38.526 -28.755  10.909  1.00 90.21  ? 123 ARG J CB  1 
ATOM   18734 C CG  . ARG J  2 123 ? -37.999 -29.950  11.675  1.00 96.31  ? 123 ARG J CG  1 
ATOM   18735 C CD  . ARG J  2 123 ? -36.487 -29.967  11.680  1.00 104.53 ? 123 ARG J CD  1 
ATOM   18736 N NE  . ARG J  2 123 ? -35.945 -28.795  12.354  1.00 118.22 ? 123 ARG J NE  1 
ATOM   18737 C CZ  . ARG J  2 123 ? -34.724 -28.728  12.871  1.00 136.41 ? 123 ARG J CZ  1 
ATOM   18738 N NH1 . ARG J  2 123 ? -33.911 -29.774  12.799  1.00 135.62 ? 123 ARG J NH1 1 
ATOM   18739 N NH2 . ARG J  2 123 ? -34.322 -27.615  13.466  1.00 138.81 ? 123 ARG J NH2 1 
ATOM   18740 N N   . SER J  2 124 ? -39.030 -26.357  12.820  1.00 102.27 ? 124 SER J N   1 
ATOM   18741 C CA  . SER J  2 124 ? -38.753 -25.643  14.062  1.00 116.02 ? 124 SER J CA  1 
ATOM   18742 C C   . SER J  2 124 ? -40.032 -25.032  14.634  1.00 118.97 ? 124 SER J C   1 
ATOM   18743 O O   . SER J  2 124 ? -39.982 -24.066  15.398  1.00 131.25 ? 124 SER J O   1 
ATOM   18744 C CB  . SER J  2 124 ? -37.702 -24.552  13.834  1.00 123.46 ? 124 SER J CB  1 
ATOM   18745 O OG  . SER J  2 124 ? -38.194 -23.547  12.966  1.00 117.22 ? 124 SER J OG  1 
ATOM   18746 N N   . GLN J  2 125 ? -41.178 -25.601  14.265  1.00 112.08 ? 125 GLN J N   1 
ATOM   18747 C CA  . GLN J  2 125 ? -42.471 -25.048  14.668  1.00 110.54 ? 125 GLN J CA  1 
ATOM   18748 C C   . GLN J  2 125 ? -43.528 -26.116  14.984  1.00 114.01 ? 125 GLN J C   1 
ATOM   18749 O O   . GLN J  2 125 ? -44.556 -25.833  15.601  1.00 111.25 ? 125 GLN J O   1 
ATOM   18750 C CB  . GLN J  2 125 ? -42.984 -24.073  13.615  1.00 94.36  ? 125 GLN J CB  1 
ATOM   18751 C CG  . GLN J  2 125 ? -44.336 -24.438  13.051  1.00 102.67 ? 125 GLN J CG  1 
ATOM   18752 C CD  . GLN J  2 125 ? -44.999 -23.273  12.345  1.00 121.89 ? 125 GLN J CD  1 
ATOM   18753 O OE1 . GLN J  2 125 ? -45.013 -23.202  11.117  1.00 118.92 ? 125 GLN J OE1 1 
ATOM   18754 N NE2 . GLN J  2 125 ? -45.561 -22.353  13.122  1.00 127.27 ? 125 GLN J NE2 1 
ATOM   18755 N N   . LEU J  2 126 ? -43.279 -27.337  14.533  1.00 116.26 ? 126 LEU J N   1 
ATOM   18756 C CA  . LEU J  2 126 ? -43.792 -28.508  15.220  1.00 99.79  ? 126 LEU J CA  1 
ATOM   18757 C C   . LEU J  2 126 ? -42.576 -29.310  15.607  1.00 125.32 ? 126 LEU J C   1 
ATOM   18758 O O   . LEU J  2 126 ? -41.887 -29.894  14.771  1.00 143.65 ? 126 LEU J O   1 
ATOM   18759 C CB  . LEU J  2 126 ? -44.766 -29.325  14.369  1.00 100.76 ? 126 LEU J CB  1 
ATOM   18760 C CG  . LEU J  2 126 ? -44.752 -28.980  12.881  1.00 102.63 ? 126 LEU J CG  1 
ATOM   18761 C CD1 . LEU J  2 126 ? -44.759 -30.236  12.057  1.00 102.99 ? 126 LEU J CD1 1 
ATOM   18762 C CD2 . LEU J  2 126 ? -45.882 -28.044  12.443  1.00 102.89 ? 126 LEU J CD2 1 
ATOM   18763 N N   . LYS J  2 127 ? -42.318 -29.317  16.902  1.00 115.15 ? 127 LYS J N   1 
ATOM   18764 C CA  . LYS J  2 127 ? -41.136 -29.969  17.421  1.00 118.02 ? 127 LYS J CA  1 
ATOM   18765 C C   . LYS J  2 127 ? -41.441 -31.410  17.844  1.00 139.46 ? 127 LYS J C   1 
ATOM   18766 O O   . LYS J  2 127 ? -41.196 -32.367  17.103  1.00 128.00 ? 127 LYS J O   1 
ATOM   18767 C CB  . LYS J  2 127 ? -40.573 -29.170  18.585  1.00 119.14 ? 127 LYS J CB  1 
ATOM   18768 C CG  . LYS J  2 127 ? -40.298 -27.693  18.208  1.00 120.42 ? 127 LYS J CG  1 
ATOM   18769 C CD  . LYS J  2 127 ? -40.996 -26.726  19.182  1.00 115.21 ? 127 LYS J CD  1 
ATOM   18770 C CE  . LYS J  2 127 ? -40.640 -25.258  18.849  1.00 127.87 ? 127 LYS J CE  1 
ATOM   18771 N NZ  . LYS J  2 127 ? -41.375 -24.240  19.681  1.00 126.81 ? 127 LYS J NZ  1 
ATOM   18772 N N   . ASN J  2 128 ? -42.020 -31.556  19.027  1.00 165.62 ? 128 ASN J N   1 
ATOM   18773 C CA  . ASN J  2 128 ? -42.455 -32.858  19.493  1.00 163.53 ? 128 ASN J CA  1 
ATOM   18774 C C   . ASN J  2 128 ? -43.762 -33.311  18.862  1.00 167.42 ? 128 ASN J C   1 
ATOM   18775 O O   . ASN J  2 128 ? -43.982 -34.504  18.728  1.00 163.34 ? 128 ASN J O   1 
ATOM   18776 C CB  . ASN J  2 128 ? -42.558 -32.865  21.010  1.00 158.66 ? 128 ASN J CB  1 
ATOM   18777 C CG  . ASN J  2 128 ? -41.205 -32.725  21.676  1.00 168.39 ? 128 ASN J CG  1 
ATOM   18778 O OD1 . ASN J  2 128 ? -40.235 -33.388  21.298  1.00 169.54 ? 128 ASN J OD1 1 
ATOM   18779 N ND2 . ASN J  2 128 ? -41.133 -31.867  22.682  1.00 179.75 ? 128 ASN J ND2 1 
ATOM   18780 N N   . ASN J  2 129 ? -44.615 -32.369  18.465  1.00 178.74 ? 129 ASN J N   1 
ATOM   18781 C CA  . ASN J  2 129 ? -45.958 -32.695  17.983  1.00 177.56 ? 129 ASN J CA  1 
ATOM   18782 C C   . ASN J  2 129 ? -45.977 -33.480  16.673  1.00 172.54 ? 129 ASN J C   1 
ATOM   18783 O O   . ASN J  2 129 ? -47.043 -33.814  16.159  1.00 172.44 ? 129 ASN J O   1 
ATOM   18784 C CB  . ASN J  2 129 ? -46.788 -31.419  17.846  1.00 172.37 ? 129 ASN J CB  1 
ATOM   18785 C CG  . ASN J  2 129 ? -46.966 -30.695  19.168  1.00 166.15 ? 129 ASN J CG  1 
ATOM   18786 O OD1 . ASN J  2 129 ? -47.690 -29.706  19.250  1.00 163.75 ? 129 ASN J OD1 1 
ATOM   18787 N ND2 . ASN J  2 129 ? -46.308 -31.191  20.212  1.00 171.75 ? 129 ASN J ND2 1 
ATOM   18788 N N   . ALA J  2 130 ? -44.796 -33.773  16.137  1.00 152.64 ? 130 ALA J N   1 
ATOM   18789 C CA  . ALA J  2 130 ? -44.681 -34.540  14.901  1.00 141.02 ? 130 ALA J CA  1 
ATOM   18790 C C   . ALA J  2 130 ? -43.253 -35.039  14.710  1.00 124.45 ? 130 ALA J C   1 
ATOM   18791 O O   . ALA J  2 130 ? -42.341 -34.611  15.418  1.00 117.72 ? 130 ALA J O   1 
ATOM   18792 C CB  . ALA J  2 130 ? -45.117 -33.700  13.709  1.00 138.31 ? 130 ALA J CB  1 
ATOM   18793 N N   . LYS J  2 131 ? -43.059 -35.942  13.754  1.00 129.46 ? 131 LYS J N   1 
ATOM   18794 C CA  . LYS J  2 131 ? -41.735 -36.499  13.498  1.00 146.86 ? 131 LYS J CA  1 
ATOM   18795 C C   . LYS J  2 131 ? -41.337 -36.378  12.030  1.00 156.10 ? 131 LYS J C   1 
ATOM   18796 O O   . LYS J  2 131 ? -42.186 -36.420  11.140  1.00 147.45 ? 131 LYS J O   1 
ATOM   18797 C CB  . LYS J  2 131 ? -41.676 -37.967  13.925  1.00 145.86 ? 131 LYS J CB  1 
ATOM   18798 C CG  . LYS J  2 131 ? -42.448 -38.909  13.015  1.00 146.55 ? 131 LYS J CG  1 
ATOM   18799 C CD  . LYS J  2 131 ? -42.018 -40.352  13.226  1.00 145.13 ? 131 LYS J CD  1 
ATOM   18800 C CE  . LYS J  2 131 ? -42.661 -41.277  12.205  1.00 139.65 ? 131 LYS J CE  1 
ATOM   18801 N NZ  . LYS J  2 131 ? -42.134 -42.667  12.304  1.00 143.89 ? 131 LYS J NZ  1 
ATOM   18802 N N   . GLU J  2 132 ? -40.039 -36.231  11.786  1.00 161.87 ? 132 GLU J N   1 
ATOM   18803 C CA  . GLU J  2 132 ? -39.516 -36.187  10.427  1.00 150.02 ? 132 GLU J CA  1 
ATOM   18804 C C   . GLU J  2 132 ? -39.492 -37.585  9.827   1.00 150.40 ? 132 GLU J C   1 
ATOM   18805 O O   . GLU J  2 132 ? -39.157 -38.554  10.509  1.00 167.19 ? 132 GLU J O   1 
ATOM   18806 C CB  . GLU J  2 132 ? -38.098 -35.617  10.415  1.00 156.33 ? 132 GLU J CB  1 
ATOM   18807 C CG  . GLU J  2 132 ? -37.961 -34.231  11.014  1.00 158.02 ? 132 GLU J CG  1 
ATOM   18808 C CD  . GLU J  2 132 ? -36.519 -33.767  11.047  1.00 164.08 ? 132 GLU J CD  1 
ATOM   18809 O OE1 . GLU J  2 132 ? -36.235 -32.748  11.707  1.00 162.00 ? 132 GLU J OE1 1 
ATOM   18810 O OE2 . GLU J  2 132 ? -35.666 -34.427  10.416  1.00 165.42 ? 132 GLU J OE2 1 
ATOM   18811 N N   . ILE J  2 133 ? -39.847 -37.688  8.551   1.00 137.41 ? 133 ILE J N   1 
ATOM   18812 C CA  . ILE J  2 133 ? -39.755 -38.955  7.838   1.00 148.97 ? 133 ILE J CA  1 
ATOM   18813 C C   . ILE J  2 133 ? -38.393 -39.066  7.163   1.00 154.60 ? 133 ILE J C   1 
ATOM   18814 O O   . ILE J  2 133 ? -37.822 -40.153  7.062   1.00 160.41 ? 133 ILE J O   1 
ATOM   18815 C CB  . ILE J  2 133 ? -40.860 -39.092  6.774   1.00 153.96 ? 133 ILE J CB  1 
ATOM   18816 C CG1 . ILE J  2 133 ? -42.242 -39.058  7.430   1.00 153.62 ? 133 ILE J CG1 1 
ATOM   18817 C CG2 . ILE J  2 133 ? -40.681 -40.379  5.982   1.00 139.54 ? 133 ILE J CG2 1 
ATOM   18818 C CD1 . ILE J  2 133 ? -42.549 -40.278  8.275   1.00 157.48 ? 133 ILE J CD1 1 
ATOM   18819 N N   . GLY J  2 134 ? -37.873 -37.930  6.710   1.00 136.03 ? 134 GLY J N   1 
ATOM   18820 C CA  . GLY J  2 134 ? -36.593 -37.890  6.028   1.00 136.08 ? 134 GLY J CA  1 
ATOM   18821 C C   . GLY J  2 134 ? -36.751 -37.514  4.569   1.00 116.11 ? 134 GLY J C   1 
ATOM   18822 O O   . GLY J  2 134 ? -35.796 -37.093  3.916   1.00 102.02 ? 134 GLY J O   1 
ATOM   18823 N N   . ASN J  2 135 ? -37.968 -37.667  4.057   1.00 106.26 ? 135 ASN J N   1 
ATOM   18824 C CA  . ASN J  2 135 ? -38.263 -37.343  2.666   1.00 97.50  ? 135 ASN J CA  1 
ATOM   18825 C C   . ASN J  2 135 ? -38.859 -35.945  2.531   1.00 97.69  ? 135 ASN J C   1 
ATOM   18826 O O   . ASN J  2 135 ? -39.614 -35.662  1.599   1.00 80.50  ? 135 ASN J O   1 
ATOM   18827 C CB  . ASN J  2 135 ? -39.207 -38.386  2.064   1.00 99.64  ? 135 ASN J CB  1 
ATOM   18828 C CG  . ASN J  2 135 ? -39.263 -38.318  0.549   1.00 114.44 ? 135 ASN J CG  1 
ATOM   18829 O OD1 . ASN J  2 135 ? -38.506 -37.577  -0.080  1.00 104.85 ? 135 ASN J OD1 1 
ATOM   18830 N ND2 . ASN J  2 135 ? -40.161 -39.095  -0.044  1.00 131.72 ? 135 ASN J ND2 1 
ATOM   18831 N N   . GLY J  2 136 ? -38.514 -35.071  3.469   1.00 94.78  ? 136 GLY J N   1 
ATOM   18832 C CA  . GLY J  2 136 ? -39.025 -33.715  3.469   1.00 79.56  ? 136 GLY J CA  1 
ATOM   18833 C C   . GLY J  2 136 ? -40.430 -33.611  4.004   1.00 97.08  ? 136 GLY J C   1 
ATOM   18834 O O   . GLY J  2 136 ? -41.058 -32.548  3.936   1.00 105.52 ? 136 GLY J O   1 
ATOM   18835 N N   . CYS J  2 137 ? -40.934 -34.718  4.535   1.00 124.57 ? 137 CYS J N   1 
ATOM   18836 C CA  . CYS J  2 137 ? -42.292 -34.732  5.075   1.00 124.63 ? 137 CYS J CA  1 
ATOM   18837 C C   . CYS J  2 137 ? -42.267 -35.135  6.569   1.00 124.13 ? 137 CYS J C   1 
ATOM   18838 O O   . CYS J  2 137 ? -41.330 -35.803  7.046   1.00 129.29 ? 137 CYS J O   1 
ATOM   18839 C CB  . CYS J  2 137 ? -43.204 -35.696  4.320   1.00 107.58 ? 137 CYS J CB  1 
ATOM   18840 S SG  . CYS J  2 137 ? -43.854 -35.047  2.787   1.00 149.98 ? 137 CYS J SG  1 
ATOM   18841 N N   . PHE J  2 138 ? -43.298 -34.708  7.308   1.00 111.21 ? 138 PHE J N   1 
ATOM   18842 C CA  . PHE J  2 138 ? -43.423 -34.885  8.767   1.00 131.02 ? 138 PHE J CA  1 
ATOM   18843 C C   . PHE J  2 138 ? -44.756 -35.534  9.148   1.00 142.13 ? 138 PHE J C   1 
ATOM   18844 O O   . PHE J  2 138 ? -45.825 -35.135  8.667   1.00 135.66 ? 138 PHE J O   1 
ATOM   18845 C CB  . PHE J  2 138 ? -43.380 -33.526  9.465   1.00 124.31 ? 138 PHE J CB  1 
ATOM   18846 C CG  . PHE J  2 138 ? -42.174 -32.697  9.126   1.00 116.74 ? 138 PHE J CG  1 
ATOM   18847 C CD1 . PHE J  2 138 ? -42.121 -32.000  7.935   1.00 111.11 ? 138 PHE J CD1 1 
ATOM   18848 C CD2 . PHE J  2 138 ? -41.115 -32.575  10.016  1.00 121.57 ? 138 PHE J CD2 1 
ATOM   18849 C CE1 . PHE J  2 138 ? -41.032 -31.227  7.616   1.00 117.10 ? 138 PHE J CE1 1 
ATOM   18850 C CE2 . PHE J  2 138 ? -40.014 -31.795  9.700   1.00 115.12 ? 138 PHE J CE2 1 
ATOM   18851 C CZ  . PHE J  2 138 ? -39.977 -31.120  8.498   1.00 114.21 ? 138 PHE J CZ  1 
ATOM   18852 N N   . GLU J  2 139 ? -44.697 -36.485  10.069  1.00 155.99 ? 139 GLU J N   1 
ATOM   18853 C CA  . GLU J  2 139 ? -45.897 -37.181  10.502  1.00 143.78 ? 139 GLU J CA  1 
ATOM   18854 C C   . GLU J  2 139 ? -46.433 -36.652  11.829  1.00 139.70 ? 139 GLU J C   1 
ATOM   18855 O O   . GLU J  2 139 ? -45.720 -36.624  12.828  1.00 141.93 ? 139 GLU J O   1 
ATOM   18856 C CB  . GLU J  2 139 ? -45.646 -38.686  10.574  1.00 151.16 ? 139 GLU J CB  1 
ATOM   18857 C CG  . GLU J  2 139 ? -46.862 -39.487  10.980  1.00 167.40 ? 139 GLU J CG  1 
ATOM   18858 C CD  . GLU J  2 139 ? -46.652 -40.968  10.795  1.00 175.16 ? 139 GLU J CD  1 
ATOM   18859 O OE1 . GLU J  2 139 ? -45.579 -41.360  10.286  1.00 167.53 ? 139 GLU J OE1 1 
ATOM   18860 O OE2 . GLU J  2 139 ? -47.562 -41.740  11.155  1.00 174.21 ? 139 GLU J OE2 1 
ATOM   18861 N N   . PHE J  2 140 ? -47.696 -36.232  11.824  1.00 160.68 ? 140 PHE J N   1 
ATOM   18862 C CA  . PHE J  2 140 ? -48.348 -35.690  13.016  1.00 172.15 ? 140 PHE J CA  1 
ATOM   18863 C C   . PHE J  2 140 ? -48.727 -36.756  14.042  1.00 172.92 ? 140 PHE J C   1 
ATOM   18864 O O   . PHE J  2 140 ? -49.251 -37.815  13.692  1.00 169.51 ? 140 PHE J O   1 
ATOM   18865 C CB  . PHE J  2 140 ? -49.613 -34.919  12.633  1.00 167.80 ? 140 PHE J CB  1 
ATOM   18866 C CG  . PHE J  2 140 ? -49.352 -33.651  11.879  1.00 160.26 ? 140 PHE J CG  1 
ATOM   18867 C CD1 . PHE J  2 140 ? -49.470 -33.616  10.501  1.00 154.60 ? 140 PHE J CD1 1 
ATOM   18868 C CD2 . PHE J  2 140 ? -48.999 -32.491  12.547  1.00 161.32 ? 140 PHE J CD2 1 
ATOM   18869 C CE1 . PHE J  2 140 ? -49.238 -32.452  9.802   1.00 152.47 ? 140 PHE J CE1 1 
ATOM   18870 C CE2 . PHE J  2 140 ? -48.764 -31.320  11.852  1.00 160.22 ? 140 PHE J CE2 1 
ATOM   18871 C CZ  . PHE J  2 140 ? -48.883 -31.301  10.477  1.00 155.79 ? 140 PHE J CZ  1 
ATOM   18872 N N   . TYR J  2 141 ? -48.472 -36.459  15.312  1.00 148.20 ? 141 TYR J N   1 
ATOM   18873 C CA  . TYR J  2 141 ? -48.966 -37.287  16.406  1.00 148.05 ? 141 TYR J CA  1 
ATOM   18874 C C   . TYR J  2 141 ? -50.320 -36.755  16.869  1.00 143.65 ? 141 TYR J C   1 
ATOM   18875 O O   . TYR J  2 141 ? -51.058 -37.434  17.586  1.00 145.06 ? 141 TYR J O   1 
ATOM   18876 C CB  . TYR J  2 141 ? -47.986 -37.288  17.584  1.00 153.40 ? 141 TYR J CB  1 
ATOM   18877 C CG  . TYR J  2 141 ? -46.627 -37.896  17.296  1.00 148.51 ? 141 TYR J CG  1 
ATOM   18878 C CD1 . TYR J  2 141 ? -45.459 -37.221  17.632  1.00 144.23 ? 141 TYR J CD1 1 
ATOM   18879 C CD2 . TYR J  2 141 ? -46.509 -39.147  16.702  1.00 139.07 ? 141 TYR J CD2 1 
ATOM   18880 C CE1 . TYR J  2 141 ? -44.214 -37.770  17.381  1.00 142.11 ? 141 TYR J CE1 1 
ATOM   18881 C CE2 . TYR J  2 141 ? -45.267 -39.704  16.445  1.00 135.97 ? 141 TYR J CE2 1 
ATOM   18882 C CZ  . TYR J  2 141 ? -44.123 -39.012  16.786  1.00 139.29 ? 141 TYR J CZ  1 
ATOM   18883 O OH  . TYR J  2 141 ? -42.885 -39.560  16.533  1.00 130.46 ? 141 TYR J OH  1 
ATOM   18884 N N   . HIS J  2 142 ? -50.636 -35.533  16.448  1.00 144.75 ? 142 HIS J N   1 
ATOM   18885 C CA  . HIS J  2 142 ? -51.837 -34.840  16.897  1.00 141.56 ? 142 HIS J CA  1 
ATOM   18886 C C   . HIS J  2 142 ? -52.756 -34.539  15.718  1.00 140.54 ? 142 HIS J C   1 
ATOM   18887 O O   . HIS J  2 142 ? -52.364 -33.834  14.790  1.00 146.28 ? 142 HIS J O   1 
ATOM   18888 C CB  . HIS J  2 142 ? -51.448 -33.548  17.628  1.00 141.55 ? 142 HIS J CB  1 
ATOM   18889 C CG  . HIS J  2 142 ? -51.349 -32.338  16.742  1.00 146.97 ? 142 HIS J CG  1 
ATOM   18890 N ND1 . HIS J  2 142 ? -52.137 -31.223  16.931  1.00 145.73 ? 142 HIS J ND1 1 
ATOM   18891 C CD2 . HIS J  2 142 ? -50.554 -32.062  15.683  1.00 149.43 ? 142 HIS J CD2 1 
ATOM   18892 C CE1 . HIS J  2 142 ? -51.835 -30.313  16.022  1.00 148.13 ? 142 HIS J CE1 1 
ATOM   18893 N NE2 . HIS J  2 142 ? -50.878 -30.796  15.250  1.00 152.47 ? 142 HIS J NE2 1 
ATOM   18894 N N   . LYS J  2 143 ? -53.974 -35.077  15.744  1.00 140.52 ? 143 LYS J N   1 
ATOM   18895 C CA  . LYS J  2 143 ? -54.884 -34.929  14.606  1.00 139.55 ? 143 LYS J CA  1 
ATOM   18896 C C   . LYS J  2 143 ? -54.891 -33.506  14.050  1.00 141.01 ? 143 LYS J C   1 
ATOM   18897 O O   . LYS J  2 143 ? -55.335 -32.567  14.713  1.00 135.89 ? 143 LYS J O   1 
ATOM   18898 C CB  . LYS J  2 143 ? -56.305 -35.374  14.965  1.00 142.49 ? 143 LYS J CB  1 
ATOM   18899 C CG  . LYS J  2 143 ? -56.479 -36.883  15.145  1.00 144.67 ? 143 LYS J CG  1 
ATOM   18900 C CD  . LYS J  2 143 ? -56.704 -37.621  13.823  1.00 151.02 ? 143 LYS J CD  1 
ATOM   18901 C CE  . LYS J  2 143 ? -55.407 -37.884  13.071  1.00 150.82 ? 143 LYS J CE  1 
ATOM   18902 N NZ  . LYS J  2 143 ? -55.655 -38.647  11.814  1.00 142.29 ? 143 LYS J NZ  1 
ATOM   18903 N N   . CYS J  2 144 ? -54.392 -33.358  12.826  1.00 155.37 ? 144 CYS J N   1 
ATOM   18904 C CA  . CYS J  2 144 ? -54.292 -32.049  12.192  1.00 159.85 ? 144 CYS J CA  1 
ATOM   18905 C C   . CYS J  2 144 ? -55.181 -31.937  10.958  1.00 147.98 ? 144 CYS J C   1 
ATOM   18906 O O   . CYS J  2 144 ? -54.812 -32.374  9.867   1.00 145.41 ? 144 CYS J O   1 
ATOM   18907 C CB  . CYS J  2 144 ? -52.840 -31.740  11.823  1.00 158.58 ? 144 CYS J CB  1 
ATOM   18908 S SG  . CYS J  2 144 ? -52.562 -30.025  11.333  1.00 162.29 ? 144 CYS J SG  1 
ATOM   18909 N N   . ASP J  2 145 ? -56.353 -31.342  11.144  1.00 159.99 ? 145 ASP J N   1 
ATOM   18910 C CA  . ASP J  2 145 ? -57.287 -31.113  10.050  1.00 164.34 ? 145 ASP J CA  1 
ATOM   18911 C C   . ASP J  2 145 ? -56.878 -29.909  9.199   1.00 156.20 ? 145 ASP J C   1 
ATOM   18912 O O   . ASP J  2 145 ? -55.744 -29.438  9.282   1.00 159.06 ? 145 ASP J O   1 
ATOM   18913 C CB  . ASP J  2 145 ? -58.718 -30.953  10.577  1.00 174.40 ? 145 ASP J CB  1 
ATOM   18914 C CG  . ASP J  2 145 ? -58.798 -30.068  11.812  1.00 178.29 ? 145 ASP J CG  1 
ATOM   18915 O OD1 . ASP J  2 145 ? -59.912 -29.607  12.137  1.00 167.05 ? 145 ASP J OD1 1 
ATOM   18916 O OD2 . ASP J  2 145 ? -57.757 -29.835  12.462  1.00 180.15 ? 145 ASP J OD2 1 
ATOM   18917 N N   . ASN J  2 146 ? -57.808 -29.420  8.384   1.00 143.81 ? 146 ASN J N   1 
ATOM   18918 C CA  . ASN J  2 146 ? -57.522 -28.345  7.435   1.00 133.60 ? 146 ASN J CA  1 
ATOM   18919 C C   . ASN J  2 146 ? -57.097 -27.026  8.077   1.00 140.20 ? 146 ASN J C   1 
ATOM   18920 O O   . ASN J  2 146 ? -56.154 -26.382  7.614   1.00 159.76 ? 146 ASN J O   1 
ATOM   18921 C CB  . ASN J  2 146 ? -58.721 -28.111  6.512   1.00 116.13 ? 146 ASN J CB  1 
ATOM   18922 C CG  . ASN J  2 146 ? -58.924 -29.241  5.521   1.00 116.55 ? 146 ASN J CG  1 
ATOM   18923 O OD1 . ASN J  2 146 ? -59.927 -29.283  4.808   1.00 122.61 ? 146 ASN J OD1 1 
ATOM   18924 N ND2 . ASN J  2 146 ? -57.970 -30.162  5.468   1.00 117.44 ? 146 ASN J ND2 1 
ATOM   18925 N N   . THR J  2 147 ? -57.796 -26.619  9.131   1.00 154.81 ? 147 THR J N   1 
ATOM   18926 C CA  . THR J  2 147 ? -57.469 -25.369  9.811   1.00 168.85 ? 147 THR J CA  1 
ATOM   18927 C C   . THR J  2 147 ? -56.260 -25.532  10.728  1.00 174.09 ? 147 THR J C   1 
ATOM   18928 O O   . THR J  2 147 ? -55.711 -24.550  11.226  1.00 174.14 ? 147 THR J O   1 
ATOM   18929 C CB  . THR J  2 147 ? -58.664 -24.812  10.611  1.00 166.54 ? 147 THR J CB  1 
ATOM   18930 O OG1 . THR J  2 147 ? -58.987 -25.707  11.682  1.00 174.70 ? 147 THR J OG1 1 
ATOM   18931 N N   . CYS J  2 148 ? -55.856 -26.776  10.955  1.00 160.22 ? 148 CYS J N   1 
ATOM   18932 C CA  . CYS J  2 148 ? -54.609 -27.046  11.655  1.00 163.38 ? 148 CYS J CA  1 
ATOM   18933 C C   . CYS J  2 148 ? -53.475 -26.863  10.658  1.00 169.50 ? 148 CYS J C   1 
ATOM   18934 O O   . CYS J  2 148 ? -52.478 -26.197  10.938  1.00 165.31 ? 148 CYS J O   1 
ATOM   18935 C CB  . CYS J  2 148 ? -54.602 -28.469  12.215  1.00 156.59 ? 148 CYS J CB  1 
ATOM   18936 S SG  . CYS J  2 148 ? -53.046 -28.962  12.995  1.00 156.09 ? 148 CYS J SG  1 
ATOM   18937 N N   . MET J  2 149 ? -53.653 -27.453  9.481   1.00 169.23 ? 149 MET J N   1 
ATOM   18938 C CA  . MET J  2 149 ? -52.699 -27.332  8.386   1.00 153.62 ? 149 MET J CA  1 
ATOM   18939 C C   . MET J  2 149 ? -52.390 -25.882  8.051   1.00 148.63 ? 149 MET J C   1 
ATOM   18940 O O   . MET J  2 149 ? -51.308 -25.568  7.554   1.00 147.50 ? 149 MET J O   1 
ATOM   18941 C CB  . MET J  2 149 ? -53.255 -28.010  7.139   1.00 142.51 ? 149 MET J CB  1 
ATOM   18942 C CG  . MET J  2 149 ? -53.377 -29.507  7.254   1.00 140.02 ? 149 MET J CG  1 
ATOM   18943 S SD  . MET J  2 149 ? -51.773 -30.303  7.410   1.00 125.18 ? 149 MET J SD  1 
ATOM   18944 C CE  . MET J  2 149 ? -52.272 -32.013  7.299   1.00 128.29 ? 149 MET J CE  1 
ATOM   18945 N N   . GLU J  2 150 ? -53.353 -25.004  8.305   1.00 194.06 ? 150 GLU J N   1 
ATOM   18946 C CA  . GLU J  2 150 ? -53.212 -23.598  7.958   1.00 195.62 ? 150 GLU J CA  1 
ATOM   18947 C C   . GLU J  2 150 ? -52.279 -22.889  8.931   1.00 196.32 ? 150 GLU J C   1 
ATOM   18948 O O   . GLU J  2 150 ? -51.432 -22.095  8.523   1.00 198.36 ? 150 GLU J O   1 
ATOM   18949 C CB  . GLU J  2 150 ? -54.578 -22.911  7.946   1.00 204.36 ? 150 GLU J CB  1 
ATOM   18950 C CG  . GLU J  2 150 ? -54.863 -22.094  6.694   1.00 206.80 ? 150 GLU J CG  1 
ATOM   18951 C CD  . GLU J  2 150 ? -55.419 -22.934  5.558   1.00 205.09 ? 150 GLU J CD  1 
ATOM   18952 O OE1 . GLU J  2 150 ? -56.078 -22.363  4.664   1.00 204.41 ? 150 GLU J OE1 1 
ATOM   18953 O OE2 . GLU J  2 150 ? -55.208 -24.165  5.563   1.00 197.92 ? 150 GLU J OE2 1 
ATOM   18954 N N   . SER J  2 151 ? -52.439 -23.180  10.218  1.00 162.30 ? 151 SER J N   1 
ATOM   18955 C CA  . SER J  2 151 ? -51.621 -22.558  11.253  1.00 161.64 ? 151 SER J CA  1 
ATOM   18956 C C   . SER J  2 151 ? -50.136 -22.737  10.955  1.00 159.12 ? 151 SER J C   1 
ATOM   18957 O O   . SER J  2 151 ? -49.306 -21.926  11.367  1.00 161.67 ? 151 SER J O   1 
ATOM   18958 C CB  . SER J  2 151 ? -51.959 -23.139  12.628  1.00 159.74 ? 151 SER J CB  1 
ATOM   18959 O OG  . SER J  2 151 ? -51.584 -24.502  12.716  1.00 161.51 ? 151 SER J OG  1 
ATOM   18960 N N   . VAL J  2 152 ? -49.812 -23.804  10.232  1.00 132.96 ? 152 VAL J N   1 
ATOM   18961 C CA  . VAL J  2 152 ? -48.434 -24.084  9.851   1.00 119.19 ? 152 VAL J CA  1 
ATOM   18962 C C   . VAL J  2 152 ? -48.011 -23.209  8.674   1.00 124.84 ? 152 VAL J C   1 
ATOM   18963 O O   . VAL J  2 152 ? -46.936 -22.609  8.692   1.00 124.21 ? 152 VAL J O   1 
ATOM   18964 C CB  . VAL J  2 152 ? -48.246 -25.565  9.475   1.00 103.32 ? 152 VAL J CB  1 
ATOM   18965 C CG1 . VAL J  2 152 ? -46.767 -25.906  9.397   1.00 94.75  ? 152 VAL J CG1 1 
ATOM   18966 C CG2 . VAL J  2 152 ? -48.945 -26.459  10.486  1.00 113.17 ? 152 VAL J CG2 1 
ATOM   18967 N N   . LYS J  2 153 ? -48.861 -23.136  7.653   1.00 126.36 ? 153 LYS J N   1 
ATOM   18968 C CA  . LYS J  2 153 ? -48.574 -22.310  6.485   1.00 119.04 ? 153 LYS J CA  1 
ATOM   18969 C C   . LYS J  2 153 ? -48.497 -20.832  6.861   1.00 138.31 ? 153 LYS J C   1 
ATOM   18970 O O   . LYS J  2 153 ? -47.498 -20.166  6.589   1.00 148.56 ? 153 LYS J O   1 
ATOM   18971 C CB  . LYS J  2 153 ? -49.622 -22.522  5.390   1.00 110.35 ? 153 LYS J CB  1 
ATOM   18972 C CG  . LYS J  2 153 ? -49.652 -23.919  4.793   1.00 89.77  ? 153 LYS J CG  1 
ATOM   18973 C CD  . LYS J  2 153 ? -50.553 -23.960  3.566   1.00 106.36 ? 153 LYS J CD  1 
ATOM   18974 C CE  . LYS J  2 153 ? -50.638 -25.358  2.974   1.00 100.49 ? 153 LYS J CE  1 
ATOM   18975 N NZ  . LYS J  2 153 ? -51.260 -26.325  3.919   1.00 107.69 ? 153 LYS J NZ  1 
ATOM   18976 N N   . ASN J  2 154 ? -49.557 -20.325  7.487   1.00 189.70 ? 154 ASN J N   1 
ATOM   18977 C CA  . ASN J  2 154 ? -49.583 -18.948  7.972   1.00 199.18 ? 154 ASN J CA  1 
ATOM   18978 C C   . ASN J  2 154 ? -48.422 -18.651  8.913   1.00 203.22 ? 154 ASN J C   1 
ATOM   18979 O O   . ASN J  2 154 ? -48.125 -17.491  9.201   1.00 209.08 ? 154 ASN J O   1 
ATOM   18980 C CB  . ASN J  2 154 ? -50.905 -18.651  8.684   1.00 210.90 ? 154 ASN J CB  1 
ATOM   18981 C CG  . ASN J  2 154 ? -52.048 -18.411  7.719   1.00 201.56 ? 154 ASN J CG  1 
ATOM   18982 O OD1 . ASN J  2 154 ? -52.840 -19.310  7.439   1.00 203.09 ? 154 ASN J OD1 1 
ATOM   18983 N ND2 . ASN J  2 154 ? -52.144 -17.188  7.211   1.00 187.11 ? 154 ASN J ND2 1 
ATOM   18984 N N   . GLY J  2 155 ? -47.772 -19.705  9.395   1.00 167.51 ? 155 GLY J N   1 
ATOM   18985 C CA  . GLY J  2 155 ? -46.669 -19.561  10.325  1.00 166.50 ? 155 GLY J CA  1 
ATOM   18986 C C   . GLY J  2 155 ? -47.150 -19.270  11.733  1.00 170.33 ? 155 GLY J C   1 
ATOM   18987 O O   . GLY J  2 155 ? -46.349 -19.069  12.645  1.00 164.05 ? 155 GLY J O   1 
ATOM   18988 N N   . THR J  2 156 ? -48.468 -19.245  11.906  1.00 187.66 ? 156 THR J N   1 
ATOM   18989 C CA  . THR J  2 156 ? -49.073 -19.000  13.210  1.00 193.46 ? 156 THR J CA  1 
ATOM   18990 C C   . THR J  2 156 ? -49.541 -20.309  13.835  1.00 181.65 ? 156 THR J C   1 
ATOM   18991 O O   . THR J  2 156 ? -50.721 -20.651  13.768  1.00 175.57 ? 156 THR J O   1 
ATOM   18992 C CB  . THR J  2 156 ? -50.271 -18.039  13.097  1.00 197.21 ? 156 THR J CB  1 
ATOM   18993 O OG1 . THR J  2 156 ? -51.188 -18.530  12.111  1.00 185.80 ? 156 THR J OG1 1 
ATOM   18994 C CG2 . THR J  2 156 ? -49.803 -16.649  12.694  1.00 199.53 ? 156 THR J CG2 1 
ATOM   18995 N N   . TYR J  2 157 ? -48.611 -21.037  14.446  1.00 155.37 ? 157 TYR J N   1 
ATOM   18996 C CA  . TYR J  2 157 ? -48.904 -22.373  14.958  1.00 149.31 ? 157 TYR J CA  1 
ATOM   18997 C C   . TYR J  2 157 ? -48.791 -22.482  16.474  1.00 157.35 ? 157 TYR J C   1 
ATOM   18998 O O   . TYR J  2 157 ? -47.703 -22.365  17.042  1.00 154.02 ? 157 TYR J O   1 
ATOM   18999 C CB  . TYR J  2 157 ? -47.989 -23.405  14.297  1.00 143.62 ? 157 TYR J CB  1 
ATOM   19000 C CG  . TYR J  2 157 ? -48.234 -24.830  14.737  1.00 131.30 ? 157 TYR J CG  1 
ATOM   19001 C CD1 . TYR J  2 157 ? -48.984 -25.698  13.957  1.00 128.82 ? 157 TYR J CD1 1 
ATOM   19002 C CD2 . TYR J  2 157 ? -47.710 -25.311  15.931  1.00 131.90 ? 157 TYR J CD2 1 
ATOM   19003 C CE1 . TYR J  2 157 ? -49.208 -27.002  14.352  1.00 120.51 ? 157 TYR J CE1 1 
ATOM   19004 C CE2 . TYR J  2 157 ? -47.930 -26.613  16.335  1.00 132.31 ? 157 TYR J CE2 1 
ATOM   19005 C CZ  . TYR J  2 157 ? -48.679 -27.455  15.542  1.00 116.49 ? 157 TYR J CZ  1 
ATOM   19006 O OH  . TYR J  2 157 ? -48.900 -28.753  15.940  1.00 107.29 ? 157 TYR J OH  1 
ATOM   19007 N N   . ASP J  2 158 ? -49.928 -22.724  17.116  1.00 147.77 ? 158 ASP J N   1 
ATOM   19008 C CA  . ASP J  2 158 ? -49.970 -22.965  18.550  1.00 155.09 ? 158 ASP J CA  1 
ATOM   19009 C C   . ASP J  2 158 ? -49.435 -24.362  18.848  1.00 154.61 ? 158 ASP J C   1 
ATOM   19010 O O   . ASP J  2 158 ? -50.040 -25.370  18.479  1.00 144.06 ? 158 ASP J O   1 
ATOM   19011 C CB  . ASP J  2 158 ? -51.399 -22.795  19.070  1.00 157.86 ? 158 ASP J CB  1 
ATOM   19012 C CG  . ASP J  2 158 ? -51.573 -23.299  20.489  1.00 155.44 ? 158 ASP J CG  1 
ATOM   19013 O OD1 . ASP J  2 158 ? -51.244 -22.557  21.439  1.00 141.64 ? 158 ASP J OD1 1 
ATOM   19014 O OD2 . ASP J  2 158 ? -52.059 -24.437  20.650  1.00 150.97 ? 158 ASP J OD2 1 
ATOM   19015 N N   . TYR J  2 159 ? -48.284 -24.413  19.505  1.00 170.59 ? 159 TYR J N   1 
ATOM   19016 C CA  . TYR J  2 159 ? -47.618 -25.681  19.771  1.00 168.11 ? 159 TYR J CA  1 
ATOM   19017 C C   . TYR J  2 159 ? -48.248 -26.534  20.885  1.00 176.65 ? 159 TYR J C   1 
ATOM   19018 O O   . TYR J  2 159 ? -48.178 -27.760  20.827  1.00 176.52 ? 159 TYR J O   1 
ATOM   19019 C CB  . TYR J  2 159 ? -46.142 -25.434  20.073  1.00 173.91 ? 159 TYR J CB  1 
ATOM   19020 C CG  . TYR J  2 159 ? -45.930 -24.663  21.344  1.00 199.62 ? 159 TYR J CG  1 
ATOM   19021 C CD1 . TYR J  2 159 ? -45.776 -25.324  22.552  1.00 201.90 ? 159 TYR J CD1 1 
ATOM   19022 C CD2 . TYR J  2 159 ? -45.915 -23.275  21.345  1.00 200.97 ? 159 TYR J CD2 1 
ATOM   19023 C CE1 . TYR J  2 159 ? -45.594 -24.630  23.723  1.00 206.77 ? 159 TYR J CE1 1 
ATOM   19024 C CE2 . TYR J  2 159 ? -45.734 -22.569  22.517  1.00 206.06 ? 159 TYR J CE2 1 
ATOM   19025 C CZ  . TYR J  2 159 ? -45.574 -23.256  23.703  1.00 204.99 ? 159 TYR J CZ  1 
ATOM   19026 O OH  . TYR J  2 159 ? -45.392 -22.580  24.884  1.00 195.63 ? 159 TYR J OH  1 
ATOM   19027 N N   . PRO J  2 160 ? -48.851 -25.897  21.906  1.00 178.32 ? 160 PRO J N   1 
ATOM   19028 C CA  . PRO J  2 160 ? -49.357 -26.687  23.036  1.00 170.32 ? 160 PRO J CA  1 
ATOM   19029 C C   . PRO J  2 160 ? -50.620 -27.487  22.713  1.00 143.81 ? 160 PRO J C   1 
ATOM   19030 O O   . PRO J  2 160 ? -51.708 -27.126  23.158  1.00 136.07 ? 160 PRO J O   1 
ATOM   19031 C CB  . PRO J  2 160 ? -49.669 -25.626  24.101  1.00 171.45 ? 160 PRO J CB  1 
ATOM   19032 C CG  . PRO J  2 160 ? -48.999 -24.368  23.629  1.00 176.53 ? 160 PRO J CG  1 
ATOM   19033 C CD  . PRO J  2 160 ? -48.986 -24.453  22.149  1.00 175.26 ? 160 PRO J CD  1 
ATOM   19034 N N   . LYS J  2 161 ? -50.470 -28.552  21.934  1.00 139.74 ? 161 LYS J N   1 
ATOM   19035 C CA  . LYS J  2 161 ? -51.558 -29.489  21.676  1.00 107.76 ? 161 LYS J CA  1 
ATOM   19036 C C   . LYS J  2 161 ? -51.003 -30.905  21.734  1.00 103.34 ? 161 LYS J C   1 
ATOM   19037 O O   . LYS J  2 161 ? -51.199 -31.708  20.820  1.00 93.26  ? 161 LYS J O   1 
ATOM   19038 C CB  . LYS J  2 161 ? -52.211 -29.217  20.320  1.00 91.92  ? 161 LYS J CB  1 
ATOM   19039 C CG  . LYS J  2 161 ? -52.842 -27.840  20.210  1.00 103.27 ? 161 LYS J CG  1 
ATOM   19040 C CD  . LYS J  2 161 ? -53.962 -27.664  21.224  1.00 92.46  ? 161 LYS J CD  1 
ATOM   19041 C CE  . LYS J  2 161 ? -54.385 -26.209  21.336  1.00 108.70 ? 161 LYS J CE  1 
ATOM   19042 N NZ  . LYS J  2 161 ? -54.746 -25.628  20.014  1.00 119.57 ? 161 LYS J NZ  1 
ATOM   19043 N N   . TYR J  2 162 ? -50.306 -31.195  22.827  1.00 112.91 ? 162 TYR J N   1 
ATOM   19044 C CA  . TYR J  2 162 ? -49.554 -32.435  22.976  1.00 117.53 ? 162 TYR J CA  1 
ATOM   19045 C C   . TYR J  2 162 ? -50.435 -33.680  22.943  1.00 119.86 ? 162 TYR J C   1 
ATOM   19046 O O   . TYR J  2 162 ? -51.468 -33.747  23.611  1.00 108.56 ? 162 TYR J O   1 
ATOM   19047 C CB  . TYR J  2 162 ? -48.740 -32.397  24.273  1.00 135.48 ? 162 TYR J CB  1 
ATOM   19048 C CG  . TYR J  2 162 ? -47.418 -33.127  24.193  1.00 169.83 ? 162 TYR J CG  1 
ATOM   19049 C CD1 . TYR J  2 162 ? -46.385 -32.643  23.401  1.00 174.79 ? 162 TYR J CD1 1 
ATOM   19050 C CD2 . TYR J  2 162 ? -47.197 -34.289  24.920  1.00 158.71 ? 162 TYR J CD2 1 
ATOM   19051 C CE1 . TYR J  2 162 ? -45.173 -33.302  23.325  1.00 164.99 ? 162 TYR J CE1 1 
ATOM   19052 C CE2 . TYR J  2 162 ? -45.986 -34.955  24.851  1.00 169.88 ? 162 TYR J CE2 1 
ATOM   19053 C CZ  . TYR J  2 162 ? -44.978 -34.457  24.052  1.00 168.76 ? 162 TYR J CZ  1 
ATOM   19054 O OH  . TYR J  2 162 ? -43.771 -35.114  23.979  1.00 125.33 ? 162 TYR J OH  1 
ATOM   19055 N N   . ASP K  1 7   ? -19.032 -47.564  18.180  1.00 126.24 ? 7   ASP K N   1 
ATOM   19056 C CA  . ASP K  1 7   ? -20.086 -46.645  18.601  1.00 114.32 ? 7   ASP K CA  1 
ATOM   19057 C C   . ASP K  1 7   ? -19.703 -45.202  18.318  1.00 101.21 ? 7   ASP K C   1 
ATOM   19058 O O   . ASP K  1 7   ? -20.238 -44.266  18.913  1.00 106.58 ? 7   ASP K O   1 
ATOM   19059 C CB  . ASP K  1 7   ? -20.403 -46.821  20.087  1.00 112.11 ? 7   ASP K CB  1 
ATOM   19060 C CG  . ASP K  1 7   ? -19.188 -46.626  20.984  1.00 99.61  ? 7   ASP K CG  1 
ATOM   19061 O OD1 . ASP K  1 7   ? -19.386 -46.257  22.161  1.00 98.64  ? 7   ASP K OD1 1 
ATOM   19062 O OD2 . ASP K  1 7   ? -18.045 -46.848  20.533  1.00 111.63 ? 7   ASP K OD2 1 
ATOM   19063 N N   . THR K  1 8   ? -18.780 -45.038  17.385  1.00 105.99 ? 8   THR K N   1 
ATOM   19064 C CA  . THR K  1 8   ? -18.156 -43.759  17.140  1.00 102.25 ? 8   THR K CA  1 
ATOM   19065 C C   . THR K  1 8   ? -18.151 -43.542  15.649  1.00 95.02  ? 8   THR K C   1 
ATOM   19066 O O   . THR K  1 8   ? -17.412 -44.208  14.925  1.00 81.95  ? 8   THR K O   1 
ATOM   19067 C CB  . THR K  1 8   ? -16.704 -43.796  17.620  1.00 115.85 ? 8   THR K CB  1 
ATOM   19068 O OG1 . THR K  1 8   ? -16.348 -45.157  17.880  1.00 140.13 ? 8   THR K OG1 1 
ATOM   19069 C CG2 . THR K  1 8   ? -16.534 -43.011  18.900  1.00 114.10 ? 8   THR K CG2 1 
ATOM   19070 N N   . LEU K  1 9   ? -18.988 -42.631  15.175  1.00 103.05 ? 9   LEU K N   1 
ATOM   19071 C CA  . LEU K  1 9   ? -18.954 -42.289  13.764  1.00 80.19  ? 9   LEU K CA  1 
ATOM   19072 C C   . LEU K  1 9   ? -18.633 -40.816  13.593  1.00 77.09  ? 9   LEU K C   1 
ATOM   19073 O O   . LEU K  1 9   ? -19.226 -39.965  14.249  1.00 108.18 ? 9   LEU K O   1 
ATOM   19074 C CB  . LEU K  1 9   ? -20.272 -42.646  13.076  1.00 83.87  ? 9   LEU K CB  1 
ATOM   19075 C CG  . LEU K  1 9   ? -20.115 -42.681  11.554  1.00 61.20  ? 9   LEU K CG  1 
ATOM   19076 C CD1 . LEU K  1 9   ? -18.777 -43.286  11.177  1.00 69.32  ? 9   LEU K CD1 1 
ATOM   19077 C CD2 . LEU K  1 9   ? -21.238 -43.442  10.890  1.00 60.32  ? 9   LEU K CD2 1 
ATOM   19078 N N   . CYS K  1 10  ? -17.682 -40.517  12.720  1.00 107.27 ? 10  CYS K N   1 
ATOM   19079 C CA  . CYS K  1 10  ? -17.291 -39.136  12.504  1.00 108.52 ? 10  CYS K CA  1 
ATOM   19080 C C   . CYS K  1 10  ? -16.925 -38.876  11.038  1.00 105.13 ? 10  CYS K C   1 
ATOM   19081 O O   . CYS K  1 10  ? -16.435 -39.762  10.329  1.00 97.49  ? 10  CYS K O   1 
ATOM   19082 C CB  . CYS K  1 10  ? -16.132 -38.744  13.433  1.00 107.65 ? 10  CYS K CB  1 
ATOM   19083 S SG  . CYS K  1 10  ? -16.452 -38.975  15.196  1.00 122.33 ? 10  CYS K SG  1 
ATOM   19084 N N   . ILE K  1 11  ? -17.183 -37.648  10.597  1.00 110.09 ? 11  ILE K N   1 
ATOM   19085 C CA  . ILE K  1 11  ? -16.922 -37.216  9.233   1.00 104.68 ? 11  ILE K CA  1 
ATOM   19086 C C   . ILE K  1 11  ? -15.978 -36.024  9.268   1.00 97.01  ? 11  ILE K C   1 
ATOM   19087 O O   . ILE K  1 11  ? -16.352 -34.927  9.686   1.00 101.27 ? 11  ILE K O   1 
ATOM   19088 C CB  . ILE K  1 11  ? -18.225 -36.818  8.508   1.00 99.96  ? 11  ILE K CB  1 
ATOM   19089 C CG1 . ILE K  1 11  ? -19.192 -36.142  9.484   1.00 104.90 ? 11  ILE K CG1 1 
ATOM   19090 C CG2 . ILE K  1 11  ? -18.888 -38.038  7.885   1.00 97.87  ? 11  ILE K CG2 1 
ATOM   19091 C CD1 . ILE K  1 11  ? -20.461 -36.938  9.753   1.00 95.09  ? 11  ILE K CD1 1 
ATOM   19092 N N   . GLY K  1 12  ? -14.742 -36.259  8.850   1.00 167.53 ? 12  GLY K N   1 
ATOM   19093 C CA  . GLY K  1 12  ? -13.733 -35.224  8.802   1.00 173.57 ? 12  GLY K CA  1 
ATOM   19094 C C   . GLY K  1 12  ? -13.235 -35.189  7.379   1.00 169.90 ? 12  GLY K C   1 
ATOM   19095 O O   . GLY K  1 12  ? -13.070 -36.225  6.736   1.00 153.94 ? 12  GLY K O   1 
ATOM   19096 N N   . TYR K  1 13  ? -13.009 -33.987  6.875   1.00 99.37  ? 13  TYR K N   1 
ATOM   19097 C CA  . TYR K  1 13  ? -12.617 -33.814  5.490   1.00 89.48  ? 13  TYR K CA  1 
ATOM   19098 C C   . TYR K  1 13  ? -11.169 -34.247  5.296   1.00 81.01  ? 13  TYR K C   1 
ATOM   19099 O O   . TYR K  1 13  ? -10.587 -34.916  6.151   1.00 82.65  ? 13  TYR K O   1 
ATOM   19100 C CB  . TYR K  1 13  ? -12.818 -32.365  5.069   1.00 56.57  ? 13  TYR K CB  1 
ATOM   19101 C CG  . TYR K  1 13  ? -12.584 -31.384  6.192   1.00 56.27  ? 13  TYR K CG  1 
ATOM   19102 C CD1 . TYR K  1 13  ? -11.350 -30.773  6.354   1.00 60.88  ? 13  TYR K CD1 1 
ATOM   19103 C CD2 . TYR K  1 13  ? -13.594 -31.074  7.096   1.00 49.95  ? 13  TYR K CD2 1 
ATOM   19104 C CE1 . TYR K  1 13  ? -11.127 -29.875  7.377   1.00 58.38  ? 13  TYR K CE1 1 
ATOM   19105 C CE2 . TYR K  1 13  ? -13.379 -30.175  8.126   1.00 62.24  ? 13  TYR K CE2 1 
ATOM   19106 C CZ  . TYR K  1 13  ? -12.142 -29.579  8.261   1.00 68.17  ? 13  TYR K CZ  1 
ATOM   19107 O OH  . TYR K  1 13  ? -11.915 -28.683  9.279   1.00 72.16  ? 13  TYR K OH  1 
ATOM   19108 N N   . HIS K  1 14  ? -10.593 -33.855  4.166   1.00 88.25  ? 14  HIS K N   1 
ATOM   19109 C CA  . HIS K  1 14  ? -9.264  -34.312  3.787   1.00 58.81  ? 14  HIS K CA  1 
ATOM   19110 C C   . HIS K  1 14  ? -8.161  -33.356  4.232   1.00 87.69  ? 14  HIS K C   1 
ATOM   19111 O O   . HIS K  1 14  ? -8.412  -32.190  4.538   1.00 94.35  ? 14  HIS K O   1 
ATOM   19112 C CB  . HIS K  1 14  ? -9.198  -34.520  2.272   1.00 83.87  ? 14  HIS K CB  1 
ATOM   19113 C CG  . HIS K  1 14  ? -7.912  -35.119  1.798   1.00 98.22  ? 14  HIS K CG  1 
ATOM   19114 N ND1 . HIS K  1 14  ? -7.716  -36.478  1.698   1.00 110.58 ? 14  HIS K ND1 1 
ATOM   19115 C CD2 . HIS K  1 14  ? -6.756  -34.542  1.390   1.00 100.75 ? 14  HIS K CD2 1 
ATOM   19116 C CE1 . HIS K  1 14  ? -6.495  -36.716  1.252   1.00 112.89 ? 14  HIS K CE1 1 
ATOM   19117 N NE2 . HIS K  1 14  ? -5.892  -35.555  1.058   1.00 103.31 ? 14  HIS K NE2 1 
ATOM   19118 N N   . ALA K  1 15  ? -6.937  -33.873  4.269   1.00 75.45  ? 15  ALA K N   1 
ATOM   19119 C CA  . ALA K  1 15  ? -5.757  -33.080  4.585   1.00 78.97  ? 15  ALA K CA  1 
ATOM   19120 C C   . ALA K  1 15  ? -4.533  -33.776  4.004   1.00 79.61  ? 15  ALA K C   1 
ATOM   19121 O O   . ALA K  1 15  ? -4.565  -34.979  3.745   1.00 78.13  ? 15  ALA K O   1 
ATOM   19122 C CB  . ALA K  1 15  ? -5.614  -32.911  6.085   1.00 77.12  ? 15  ALA K CB  1 
ATOM   19123 N N   . ASN K  1 16  ? -3.457  -33.027  3.794   1.00 89.57  ? 16  ASN K N   1 
ATOM   19124 C CA  . ASN K  1 16  ? -2.262  -33.601  3.187   1.00 97.89  ? 16  ASN K CA  1 
ATOM   19125 C C   . ASN K  1 16  ? -1.016  -32.740  3.329   1.00 102.28 ? 16  ASN K C   1 
ATOM   19126 O O   . ASN K  1 16  ? -1.006  -31.746  4.056   1.00 94.41  ? 16  ASN K O   1 
ATOM   19127 C CB  . ASN K  1 16  ? -2.513  -33.902  1.709   1.00 99.23  ? 16  ASN K CB  1 
ATOM   19128 C CG  . ASN K  1 16  ? -2.939  -32.674  0.931   1.00 105.64 ? 16  ASN K CG  1 
ATOM   19129 O OD1 . ASN K  1 16  ? -2.846  -31.548  1.422   1.00 100.02 ? 16  ASN K OD1 1 
ATOM   19130 N ND2 . ASN K  1 16  ? -3.410  -32.884  -0.292  1.00 93.62  ? 16  ASN K ND2 1 
ATOM   19131 N N   . ASN K  1 17  ? 0.035   -33.131  2.617   1.00 105.95 ? 17  ASN K N   1 
ATOM   19132 C CA  . ASN K  1 17  ? 1.306   -32.424  2.674   1.00 116.07 ? 17  ASN K CA  1 
ATOM   19133 C C   . ASN K  1 17  ? 1.383   -31.262  1.700   1.00 125.61 ? 17  ASN K C   1 
ATOM   19134 O O   . ASN K  1 17  ? 2.469   -30.787  1.369   1.00 133.07 ? 17  ASN K O   1 
ATOM   19135 C CB  . ASN K  1 17  ? 2.459   -33.389  2.416   1.00 139.06 ? 17  ASN K CB  1 
ATOM   19136 C CG  . ASN K  1 17  ? 2.411   -34.021  1.029   1.00 136.87 ? 17  ASN K CG  1 
ATOM   19137 O OD1 . ASN K  1 17  ? 1.774   -33.508  0.109   1.00 139.02 ? 17  ASN K OD1 1 
ATOM   19138 N ND2 . ASN K  1 17  ? 3.098   -35.149  0.883   1.00 148.05 ? 17  ASN K ND2 1 
ATOM   19139 N N   . SER K  1 18  ? 0.224   -30.804  1.244   1.00 113.99 ? 18  SER K N   1 
ATOM   19140 C CA  . SER K  1 18  ? 0.168   -29.756  0.237   1.00 102.34 ? 18  SER K CA  1 
ATOM   19141 C C   . SER K  1 18  ? 0.592   -28.402  0.796   1.00 94.19  ? 18  SER K C   1 
ATOM   19142 O O   . SER K  1 18  ? 0.176   -28.011  1.886   1.00 82.68  ? 18  SER K O   1 
ATOM   19143 C CB  . SER K  1 18  ? -1.239  -29.665  -0.349  1.00 100.20 ? 18  SER K CB  1 
ATOM   19144 O OG  . SER K  1 18  ? -1.278  -28.753  -1.431  1.00 95.00  ? 18  SER K OG  1 
ATOM   19145 N N   . THR K  1 19  ? 1.423   -27.691  0.042   1.00 100.94 ? 19  THR K N   1 
ATOM   19146 C CA  . THR K  1 19  ? 1.821   -26.342  0.419   1.00 105.44 ? 19  THR K CA  1 
ATOM   19147 C C   . THR K  1 19  ? 1.203   -25.312  -0.523  1.00 97.13  ? 19  THR K C   1 
ATOM   19148 O O   . THR K  1 19  ? 1.467   -24.115  -0.407  1.00 95.13  ? 19  THR K O   1 
ATOM   19149 C CB  . THR K  1 19  ? 3.355   -26.178  0.451   1.00 104.80 ? 19  THR K CB  1 
ATOM   19150 O OG1 . THR K  1 19  ? 3.907   -26.530  -0.823  1.00 114.94 ? 19  THR K OG1 1 
ATOM   19151 C CG2 . THR K  1 19  ? 3.963   -27.071  1.520   1.00 110.72 ? 19  THR K CG2 1 
ATOM   19152 N N   . ASP K  1 20  ? 0.379   -25.787  -1.453  1.00 92.69  ? 20  ASP K N   1 
ATOM   19153 C CA  . ASP K  1 20  ? -0.320  -24.906  -2.384  1.00 82.40  ? 20  ASP K CA  1 
ATOM   19154 C C   . ASP K  1 20  ? -1.106  -23.838  -1.634  1.00 77.62  ? 20  ASP K C   1 
ATOM   19155 O O   . ASP K  1 20  ? -1.835  -24.138  -0.688  1.00 87.84  ? 20  ASP K O   1 
ATOM   19156 C CB  . ASP K  1 20  ? -1.266  -25.703  -3.290  1.00 83.37  ? 20  ASP K CB  1 
ATOM   19157 C CG  . ASP K  1 20  ? -0.527  -26.624  -4.241  1.00 92.68  ? 20  ASP K CG  1 
ATOM   19158 O OD1 . ASP K  1 20  ? -1.184  -27.458  -4.902  1.00 78.90  ? 20  ASP K OD1 1 
ATOM   19159 O OD2 . ASP K  1 20  ? 0.713   -26.514  -4.328  1.00 92.97  ? 20  ASP K OD2 1 
ATOM   19160 N N   . THR K  1 21  ? -0.948  -22.590  -2.059  1.00 76.50  ? 21  THR K N   1 
ATOM   19161 C CA  . THR K  1 21  ? -1.703  -21.488  -1.481  1.00 76.63  ? 21  THR K CA  1 
ATOM   19162 C C   . THR K  1 21  ? -2.438  -20.704  -2.561  1.00 67.76  ? 21  THR K C   1 
ATOM   19163 O O   . THR K  1 21  ? -1.883  -20.409  -3.619  1.00 75.07  ? 21  THR K O   1 
ATOM   19164 C CB  . THR K  1 21  ? -0.802  -20.524  -0.684  1.00 76.46  ? 21  THR K CB  1 
ATOM   19165 O OG1 . THR K  1 21  ? 0.341   -20.169  -1.472  1.00 92.09  ? 21  THR K OG1 1 
ATOM   19166 C CG2 . THR K  1 21  ? -0.341  -21.172  0.612   1.00 76.36  ? 21  THR K CG2 1 
ATOM   19167 N N   . VAL K  1 22  ? -3.696  -20.380  -2.287  1.00 59.85  ? 22  VAL K N   1 
ATOM   19168 C CA  . VAL K  1 22  ? -4.491  -19.572  -3.198  1.00 61.02  ? 22  VAL K CA  1 
ATOM   19169 C C   . VAL K  1 22  ? -5.022  -18.356  -2.456  1.00 65.31  ? 22  VAL K C   1 
ATOM   19170 O O   . VAL K  1 22  ? -4.951  -18.286  -1.229  1.00 68.77  ? 22  VAL K O   1 
ATOM   19171 C CB  . VAL K  1 22  ? -5.684  -20.363  -3.766  1.00 54.86  ? 22  VAL K CB  1 
ATOM   19172 C CG1 . VAL K  1 22  ? -5.229  -21.721  -4.274  1.00 52.32  ? 22  VAL K CG1 1 
ATOM   19173 C CG2 . VAL K  1 22  ? -6.763  -20.524  -2.708  1.00 50.15  ? 22  VAL K CG2 1 
ATOM   19174 N N   . ASP K  1 23  ? -5.615  -17.438  -3.182  1.00 53.13  ? 23  ASP K N   1 
ATOM   19175 C CA  . ASP K  1 23  ? -6.240  -16.315  -2.557  1.00 55.01  ? 23  ASP K CA  1 
ATOM   19176 C C   . ASP K  1 23  ? -7.712  -16.341  -2.795  1.00 54.80  ? 23  ASP K C   1 
ATOM   19177 O O   . ASP K  1 23  ? -8.192  -16.929  -3.725  1.00 52.40  ? 23  ASP K O   1 
ATOM   19178 C CB  . ASP K  1 23  ? -5.715  -15.045  -3.155  1.00 64.79  ? 23  ASP K CB  1 
ATOM   19179 C CG  . ASP K  1 23  ? -4.445  -14.619  -2.555  1.00 82.09  ? 23  ASP K CG  1 
ATOM   19180 O OD1 . ASP K  1 23  ? -4.228  -14.874  -1.365  1.00 94.25  ? 23  ASP K OD1 1 
ATOM   19181 O OD2 . ASP K  1 23  ? -3.657  -14.017  -3.283  1.00 89.47  ? 23  ASP K OD2 1 
ATOM   19182 N N   . THR K  1 24  ? -8.427  -15.669  -1.928  1.00 54.21  ? 24  THR K N   1 
ATOM   19183 C CA  . THR K  1 24  ? -9.860  -15.506  -2.107  1.00 55.71  ? 24  THR K CA  1 
ATOM   19184 C C   . THR K  1 24  ? -10.201 -14.033  -1.979  1.00 57.52  ? 24  THR K C   1 
ATOM   19185 O O   . THR K  1 24  ? -9.319  -13.197  -1.777  1.00 50.27  ? 24  THR K O   1 
ATOM   19186 C CB  . THR K  1 24  ? -10.664 -16.299  -1.063  1.00 65.42  ? 24  THR K CB  1 
ATOM   19187 O OG1 . THR K  1 24  ? -10.500 -15.700  0.229   1.00 81.20  ? 24  THR K OG1 1 
ATOM   19188 C CG2 . THR K  1 24  ? -10.200 -17.746  -1.015  1.00 52.61  ? 24  THR K CG2 1 
ATOM   19189 N N   . VAL K  1 25  ? -11.482 -13.715  -2.098  1.00 62.59  ? 25  VAL K N   1 
ATOM   19190 C CA  . VAL K  1 25  ? -11.923 -12.342  -1.941  1.00 61.62  ? 25  VAL K CA  1 
ATOM   19191 C C   . VAL K  1 25  ? -11.777 -11.935  -0.483  1.00 62.14  ? 25  VAL K C   1 
ATOM   19192 O O   . VAL K  1 25  ? -11.490 -10.783  -0.183  1.00 54.60  ? 25  VAL K O   1 
ATOM   19193 C CB  . VAL K  1 25  ? -13.389 -12.169  -2.364  1.00 59.54  ? 25  VAL K CB  1 
ATOM   19194 C CG1 . VAL K  1 25  ? -13.645 -10.737  -2.804  1.00 53.40  ? 25  VAL K CG1 1 
ATOM   19195 C CG2 . VAL K  1 25  ? -13.726 -13.133  -3.485  1.00 69.16  ? 25  VAL K CG2 1 
ATOM   19196 N N   . LEU K  1 26  ? -11.950 -12.898  0.418   1.00 65.57  ? 26  LEU K N   1 
ATOM   19197 C CA  . LEU K  1 26  ? -12.013 -12.612  1.848   1.00 64.54  ? 26  LEU K CA  1 
ATOM   19198 C C   . LEU K  1 26  ? -10.733 -12.943  2.607   1.00 66.16  ? 26  LEU K C   1 
ATOM   19199 O O   . LEU K  1 26  ? -10.574 -12.543  3.762   1.00 63.45  ? 26  LEU K O   1 
ATOM   19200 C CB  . LEU K  1 26  ? -13.167 -13.381  2.488   1.00 58.35  ? 26  LEU K CB  1 
ATOM   19201 C CG  . LEU K  1 26  ? -14.519 -13.341  1.777   1.00 61.70  ? 26  LEU K CG  1 
ATOM   19202 C CD1 . LEU K  1 26  ? -15.547 -14.132  2.568   1.00 44.44  ? 26  LEU K CD1 1 
ATOM   19203 C CD2 . LEU K  1 26  ? -14.990 -11.915  1.536   1.00 70.37  ? 26  LEU K CD2 1 
ATOM   19204 N N   . GLU K  1 27  ? -9.826  -13.676  1.973   1.00 69.17  ? 27  GLU K N   1 
ATOM   19205 C CA  . GLU K  1 27  ? -8.621  -14.120  2.662   1.00 63.45  ? 27  GLU K CA  1 
ATOM   19206 C C   . GLU K  1 27  ? -7.440  -14.314  1.714   1.00 65.06  ? 27  GLU K C   1 
ATOM   19207 O O   . GLU K  1 27  ? -7.610  -14.730  0.568   1.00 66.58  ? 27  GLU K O   1 
ATOM   19208 C CB  . GLU K  1 27  ? -8.908  -15.412  3.433   1.00 74.95  ? 27  GLU K CB  1 
ATOM   19209 C CG  . GLU K  1 27  ? -7.971  -15.670  4.599   1.00 96.37  ? 27  GLU K CG  1 
ATOM   19210 C CD  . GLU K  1 27  ? -8.492  -16.751  5.526   1.00 108.31 ? 27  GLU K CD  1 
ATOM   19211 O OE1 . GLU K  1 27  ? -7.693  -17.300  6.314   1.00 102.45 ? 27  GLU K OE1 1 
ATOM   19212 O OE2 . GLU K  1 27  ? -9.702  -17.054  5.463   1.00 110.95 ? 27  GLU K OE2 1 
ATOM   19213 N N   . LYS K  1 28  ? -6.235  -14.099  2.154   1.00 73.24  ? 28  LYS K N   1 
ATOM   19214 C CA  . LYS K  1 28  ? -5.176  -14.419  1.253   1.00 79.52  ? 28  LYS K CA  1 
ATOM   19215 C C   . LYS K  1 28  ? -4.334  -15.532  1.765   1.00 76.39  ? 28  LYS K C   1 
ATOM   19216 O O   . LYS K  1 28  ? -4.534  -16.078  2.836   1.00 74.35  ? 28  LYS K O   1 
ATOM   19217 C CB  . LYS K  1 28  ? -4.319  -13.208  0.959   1.00 80.38  ? 28  LYS K CB  1 
ATOM   19218 C CG  . LYS K  1 28  ? -5.061  -11.929  1.133   1.00 74.41  ? 28  LYS K CG  1 
ATOM   19219 C CD  . LYS K  1 28  ? -4.179  -10.780  0.834   1.00 96.08  ? 28  LYS K CD  1 
ATOM   19220 C CE  . LYS K  1 28  ? -4.593  -10.143  -0.453  1.00 101.90 ? 28  LYS K CE  1 
ATOM   19221 N NZ  . LYS K  1 28  ? -5.937  -10.626  -0.830  1.00 99.16  ? 28  LYS K NZ  1 
ATOM   19222 N N   . ASN K  1 29  ? -3.368  -15.862  0.955   1.00 84.58  ? 29  ASN K N   1 
ATOM   19223 C CA  . ASN K  1 29  ? -2.512  -17.017  1.221   1.00 82.97  ? 29  ASN K CA  1 
ATOM   19224 C C   . ASN K  1 29  ? -3.179  -18.109  2.053   1.00 75.98  ? 29  ASN K C   1 
ATOM   19225 O O   . ASN K  1 29  ? -2.760  -18.398  3.174   1.00 79.78  ? 29  ASN K O   1 
ATOM   19226 C CB  . ASN K  1 29  ? -1.190  -16.578  1.855   1.00 77.70  ? 29  ASN K CB  1 
ATOM   19227 C CG  . ASN K  1 29  ? -0.224  -15.997  0.840   1.00 107.26 ? 29  ASN K CG  1 
ATOM   19228 O OD1 . ASN K  1 29  ? 0.354   -16.724  0.032   1.00 108.01 ? 29  ASN K OD1 1 
ATOM   19229 N ND2 . ASN K  1 29  ? -0.048  -14.679  0.873   1.00 111.14 ? 29  ASN K ND2 1 
ATOM   19230 N N   . VAL K  1 30  ? -4.221  -18.708  1.487   1.00 69.85  ? 30  VAL K N   1 
ATOM   19231 C CA  . VAL K  1 30  ? -4.913  -19.821  2.121   1.00 60.48  ? 30  VAL K CA  1 
ATOM   19232 C C   . VAL K  1 30  ? -4.415  -21.144  1.552   1.00 63.39  ? 30  VAL K C   1 
ATOM   19233 O O   . VAL K  1 30  ? -4.513  -21.387  0.349   1.00 63.48  ? 30  VAL K O   1 
ATOM   19234 C CB  . VAL K  1 30  ? -6.435  -19.732  1.910   1.00 59.27  ? 30  VAL K CB  1 
ATOM   19235 C CG1 . VAL K  1 30  ? -7.117  -20.983  2.439   1.00 54.41  ? 30  VAL K CG1 1 
ATOM   19236 C CG2 . VAL K  1 30  ? -6.993  -18.486  2.580   1.00 64.28  ? 30  VAL K CG2 1 
ATOM   19237 N N   . THR K  1 31  ? -3.879  -21.995  2.420   1.00 68.55  ? 31  THR K N   1 
ATOM   19238 C CA  . THR K  1 31  ? -3.355  -23.289  1.998   1.00 71.68  ? 31  THR K CA  1 
ATOM   19239 C C   . THR K  1 31  ? -4.479  -24.258  1.647   1.00 59.98  ? 31  THR K C   1 
ATOM   19240 O O   . THR K  1 31  ? -5.370  -24.509  2.457   1.00 76.77  ? 31  THR K O   1 
ATOM   19241 C CB  . THR K  1 31  ? -2.468  -23.920  3.087   1.00 73.56  ? 31  THR K CB  1 
ATOM   19242 O OG1 . THR K  1 31  ? -1.398  -23.024  3.414   1.00 66.39  ? 31  THR K OG1 1 
ATOM   19243 C CG2 . THR K  1 31  ? -1.891  -25.242  2.605   1.00 73.75  ? 31  THR K CG2 1 
ATOM   19244 N N   . VAL K  1 32  ? -4.430  -24.800  0.434   1.00 57.27  ? 32  VAL K N   1 
ATOM   19245 C CA  . VAL K  1 32  ? -5.450  -25.735  -0.025  1.00 64.84  ? 32  VAL K CA  1 
ATOM   19246 C C   . VAL K  1 32  ? -4.853  -27.104  -0.334  1.00 63.48  ? 32  VAL K C   1 
ATOM   19247 O O   . VAL K  1 32  ? -3.655  -27.226  -0.591  1.00 76.47  ? 32  VAL K O   1 
ATOM   19248 C CB  . VAL K  1 32  ? -6.190  -25.208  -1.273  1.00 65.54  ? 32  VAL K CB  1 
ATOM   19249 C CG1 . VAL K  1 32  ? -7.049  -24.003  -0.915  1.00 56.47  ? 32  VAL K CG1 1 
ATOM   19250 C CG2 . VAL K  1 32  ? -5.200  -24.865  -2.377  1.00 61.06  ? 32  VAL K CG2 1 
ATOM   19251 N N   . THR K  1 33  ? -5.699  -28.130  -0.305  1.00 63.32  ? 33  THR K N   1 
ATOM   19252 C CA  . THR K  1 33  ? -5.265  -29.499  -0.557  1.00 71.36  ? 33  THR K CA  1 
ATOM   19253 C C   . THR K  1 33  ? -4.877  -29.711  -2.017  1.00 67.57  ? 33  THR K C   1 
ATOM   19254 O O   . THR K  1 33  ? -3.908  -30.408  -2.316  1.00 81.18  ? 33  THR K O   1 
ATOM   19255 C CB  . THR K  1 33  ? -6.363  -30.515  -0.184  1.00 75.91  ? 33  THR K CB  1 
ATOM   19256 O OG1 . THR K  1 33  ? -7.536  -30.265  -0.970  1.00 66.52  ? 33  THR K OG1 1 
ATOM   19257 C CG2 . THR K  1 33  ? -6.715  -30.408  1.291   1.00 80.41  ? 33  THR K CG2 1 
ATOM   19258 N N   . HIS K  1 34  ? -5.643  -29.112  -2.922  1.00 75.58  ? 34  HIS K N   1 
ATOM   19259 C CA  . HIS K  1 34  ? -5.398  -29.264  -4.352  1.00 77.81  ? 34  HIS K CA  1 
ATOM   19260 C C   . HIS K  1 34  ? -5.692  -27.972  -5.106  1.00 71.47  ? 34  HIS K C   1 
ATOM   19261 O O   . HIS K  1 34  ? -6.511  -27.161  -4.671  1.00 63.79  ? 34  HIS K O   1 
ATOM   19262 C CB  . HIS K  1 34  ? -6.246  -30.404  -4.917  1.00 69.59  ? 34  HIS K CB  1 
ATOM   19263 C CG  . HIS K  1 34  ? -6.036  -31.713  -4.226  1.00 75.89  ? 34  HIS K CG  1 
ATOM   19264 N ND1 . HIS K  1 34  ? -6.551  -31.987  -2.975  1.00 77.65  ? 34  HIS K ND1 1 
ATOM   19265 C CD2 . HIS K  1 34  ? -5.371  -32.830  -4.609  1.00 82.26  ? 34  HIS K CD2 1 
ATOM   19266 C CE1 . HIS K  1 34  ? -6.208  -33.211  -2.619  1.00 94.07  ? 34  HIS K CE1 1 
ATOM   19267 N NE2 . HIS K  1 34  ? -5.493  -33.745  -3.591  1.00 102.02 ? 34  HIS K NE2 1 
ATOM   19268 N N   . SER K  1 35  ? -5.023  -27.786  -6.239  1.00 68.72  ? 35  SER K N   1 
ATOM   19269 C CA  . SER K  1 35  ? -5.222  -26.594  -7.054  1.00 62.45  ? 35  SER K CA  1 
ATOM   19270 C C   . SER K  1 35  ? -4.631  -26.752  -8.452  1.00 57.74  ? 35  SER K C   1 
ATOM   19271 O O   . SER K  1 35  ? -3.873  -27.685  -8.718  1.00 66.30  ? 35  SER K O   1 
ATOM   19272 C CB  . SER K  1 35  ? -4.615  -25.368  -6.368  1.00 69.50  ? 35  SER K CB  1 
ATOM   19273 O OG  . SER K  1 35  ? -3.223  -25.533  -6.165  1.00 71.54  ? 35  SER K OG  1 
ATOM   19274 N N   . VAL K  1 36  ? -4.990  -25.831  -9.340  1.00 60.68  ? 36  VAL K N   1 
ATOM   19275 C CA  . VAL K  1 36  ? -4.459  -25.814  -10.696 1.00 66.71  ? 36  VAL K CA  1 
ATOM   19276 C C   . VAL K  1 36  ? -4.062  -24.394  -11.072 1.00 65.48  ? 36  VAL K C   1 
ATOM   19277 O O   . VAL K  1 36  ? -4.602  -23.429  -10.533 1.00 54.85  ? 36  VAL K O   1 
ATOM   19278 C CB  . VAL K  1 36  ? -5.492  -26.324  -11.719 1.00 57.20  ? 36  VAL K CB  1 
ATOM   19279 C CG1 . VAL K  1 36  ? -5.937  -27.734  -11.367 1.00 75.07  ? 36  VAL K CG1 1 
ATOM   19280 C CG2 . VAL K  1 36  ? -6.685  -25.384  -11.783 1.00 54.77  ? 36  VAL K CG2 1 
ATOM   19281 N N   . ASN K  1 37  ? -3.116  -24.265  -11.994 1.00 72.49  ? 37  ASN K N   1 
ATOM   19282 C CA  . ASN K  1 37  ? -2.702  -22.949  -12.460 1.00 62.78  ? 37  ASN K CA  1 
ATOM   19283 C C   . ASN K  1 37  ? -3.383  -22.597  -13.778 1.00 61.49  ? 37  ASN K C   1 
ATOM   19284 O O   . ASN K  1 37  ? -3.301  -23.350  -14.748 1.00 65.62  ? 37  ASN K O   1 
ATOM   19285 C CB  . ASN K  1 37  ? -1.180  -22.878  -12.605 1.00 62.67  ? 37  ASN K CB  1 
ATOM   19286 C CG  . ASN K  1 37  ? -0.665  -21.451  -12.631 1.00 72.54  ? 37  ASN K CG  1 
ATOM   19287 O OD1 . ASN K  1 37  ? 0.511   -21.208  -12.898 1.00 87.95  ? 37  ASN K OD1 1 
ATOM   19288 N ND2 . ASN K  1 37  ? -1.547  -20.500  -12.349 1.00 59.61  ? 37  ASN K ND2 1 
ATOM   19289 N N   . LEU K  1 38  ? -4.065  -21.457  -13.800 1.00 51.50  ? 38  LEU K N   1 
ATOM   19290 C CA  . LEU K  1 38  ? -4.766  -21.003  -14.996 1.00 46.82  ? 38  LEU K CA  1 
ATOM   19291 C C   . LEU K  1 38  ? -3.857  -20.136  -15.855 1.00 50.42  ? 38  LEU K C   1 
ATOM   19292 O O   . LEU K  1 38  ? -4.190  -19.800  -16.991 1.00 45.26  ? 38  LEU K O   1 
ATOM   19293 C CB  . LEU K  1 38  ? -6.024  -20.221  -14.613 1.00 34.89  ? 38  LEU K CB  1 
ATOM   19294 C CG  . LEU K  1 38  ? -7.171  -21.023  -13.997 1.00 38.55  ? 38  LEU K CG  1 
ATOM   19295 C CD1 . LEU K  1 38  ? -8.202  -20.086  -13.389 1.00 63.67  ? 38  LEU K CD1 1 
ATOM   19296 C CD2 . LEU K  1 38  ? -7.805  -21.935  -15.037 1.00 39.15  ? 38  LEU K CD2 1 
ATOM   19297 N N   . LEU K  1 39  ? -2.705  -19.780  -15.301 1.00 53.34  ? 39  LEU K N   1 
ATOM   19298 C CA  . LEU K  1 39  ? -1.753  -18.926  -15.996 1.00 48.15  ? 39  LEU K CA  1 
ATOM   19299 C C   . LEU K  1 39  ? -0.584  -19.713  -16.580 1.00 54.93  ? 39  LEU K C   1 
ATOM   19300 O O   . LEU K  1 39  ? 0.150   -20.389  -15.855 1.00 68.02  ? 39  LEU K O   1 
ATOM   19301 C CB  . LEU K  1 39  ? -1.224  -17.850  -15.048 1.00 42.08  ? 39  LEU K CB  1 
ATOM   19302 C CG  . LEU K  1 39  ? -0.115  -16.965  -15.615 1.00 48.13  ? 39  LEU K CG  1 
ATOM   19303 C CD1 . LEU K  1 39  ? -0.604  -16.239  -16.861 1.00 52.46  ? 39  LEU K CD1 1 
ATOM   19304 C CD2 . LEU K  1 39  ? 0.382   -15.987  -14.564 1.00 44.41  ? 39  LEU K CD2 1 
ATOM   19305 N N   . GLU K  1 40  ? -0.408  -19.614  -17.894 1.00 51.15  ? 40  GLU K N   1 
ATOM   19306 C CA  . GLU K  1 40  ? 0.759   -20.197  -18.546 1.00 53.32  ? 40  GLU K CA  1 
ATOM   19307 C C   . GLU K  1 40  ? 1.933   -19.232  -18.438 1.00 53.47  ? 40  GLU K C   1 
ATOM   19308 O O   . GLU K  1 40  ? 1.779   -18.027  -18.642 1.00 49.83  ? 40  GLU K O   1 
ATOM   19309 C CB  . GLU K  1 40  ? 0.464   -20.505  -20.015 1.00 49.17  ? 40  GLU K CB  1 
ATOM   19310 C CG  . GLU K  1 40  ? 1.584   -21.224  -20.758 1.00 63.04  ? 40  GLU K CG  1 
ATOM   19311 C CD  . GLU K  1 40  ? 1.840   -22.622  -20.231 1.00 75.62  ? 40  GLU K CD  1 
ATOM   19312 O OE1 . GLU K  1 40  ? 1.283   -23.588  -20.793 1.00 76.75  ? 40  GLU K OE1 1 
ATOM   19313 O OE2 . GLU K  1 40  ? 2.607   -22.760  -19.258 1.00 76.19  ? 40  GLU K OE2 1 
ATOM   19314 N N   . ASP K  1 41  ? 3.101   -19.770  -18.101 1.00 67.96  ? 41  ASP K N   1 
ATOM   19315 C CA  . ASP K  1 41  ? 4.313   -18.971  -17.962 1.00 69.28  ? 41  ASP K CA  1 
ATOM   19316 C C   . ASP K  1 41  ? 5.523   -19.754  -18.460 1.00 58.23  ? 41  ASP K C   1 
ATOM   19317 O O   . ASP K  1 41  ? 6.624   -19.627  -17.921 1.00 80.24  ? 41  ASP K O   1 
ATOM   19318 C CB  . ASP K  1 41  ? 4.514   -18.556  -16.502 1.00 70.40  ? 41  ASP K CB  1 
ATOM   19319 C CG  . ASP K  1 41  ? 4.486   -19.738  -15.547 1.00 99.06  ? 41  ASP K CG  1 
ATOM   19320 O OD1 . ASP K  1 41  ? 4.364   -20.890  -16.017 1.00 101.89 ? 41  ASP K OD1 1 
ATOM   19321 O OD2 . ASP K  1 41  ? 4.582   -19.515  -14.322 1.00 99.15  ? 41  ASP K OD2 1 
ATOM   19322 N N   . LYS K  1 42  ? 5.312   -20.565  -19.492 1.00 63.01  ? 42  LYS K N   1 
ATOM   19323 C CA  . LYS K  1 42  ? 6.358   -21.452  -19.985 1.00 71.60  ? 42  LYS K CA  1 
ATOM   19324 C C   . LYS K  1 42  ? 6.291   -21.644  -21.497 1.00 65.59  ? 42  LYS K C   1 
ATOM   19325 O O   . LYS K  1 42  ? 5.344   -22.231  -22.023 1.00 65.97  ? 42  LYS K O   1 
ATOM   19326 C CB  . LYS K  1 42  ? 6.272   -22.804  -19.277 1.00 82.25  ? 42  LYS K CB  1 
ATOM   19327 C CG  . LYS K  1 42  ? 7.606   -23.336  -18.795 1.00 110.12 ? 42  LYS K CG  1 
ATOM   19328 C CD  . LYS K  1 42  ? 7.409   -24.351  -17.686 1.00 129.74 ? 42  LYS K CD  1 
ATOM   19329 C CE  . LYS K  1 42  ? 6.632   -23.742  -16.528 1.00 116.08 ? 42  LYS K CE  1 
ATOM   19330 N NZ  . LYS K  1 42  ? 6.323   -24.741  -15.470 1.00 114.86 ? 42  LYS K NZ  1 
ATOM   19331 N N   . HIS K  1 43  ? 7.309   -21.139  -22.187 1.00 54.52  ? 43  HIS K N   1 
ATOM   19332 C CA  . HIS K  1 43  ? 7.428   -21.292  -23.630 1.00 57.87  ? 43  HIS K CA  1 
ATOM   19333 C C   . HIS K  1 43  ? 8.575   -22.244  -23.949 1.00 64.57  ? 43  HIS K C   1 
ATOM   19334 O O   . HIS K  1 43  ? 9.479   -22.425  -23.133 1.00 71.10  ? 43  HIS K O   1 
ATOM   19335 C CB  . HIS K  1 43  ? 7.684   -19.934  -24.280 1.00 58.15  ? 43  HIS K CB  1 
ATOM   19336 C CG  . HIS K  1 43  ? 8.930   -19.262  -23.796 1.00 65.79  ? 43  HIS K CG  1 
ATOM   19337 N ND1 . HIS K  1 43  ? 10.119  -19.304  -24.494 1.00 72.42  ? 43  HIS K ND1 1 
ATOM   19338 C CD2 . HIS K  1 43  ? 9.179   -18.538  -22.679 1.00 62.90  ? 43  HIS K CD2 1 
ATOM   19339 C CE1 . HIS K  1 43  ? 11.041  -18.631  -23.832 1.00 69.40  ? 43  HIS K CE1 1 
ATOM   19340 N NE2 . HIS K  1 43  ? 10.497  -18.156  -22.725 1.00 64.77  ? 43  HIS K NE2 1 
ATOM   19341 N N   . ASN K  1 44  ? 8.542   -22.850  -25.131 1.00 59.17  ? 44  ASN K N   1 
ATOM   19342 C CA  . ASN K  1 44  ? 9.582   -23.799  -25.520 1.00 54.78  ? 44  ASN K CA  1 
ATOM   19343 C C   . ASN K  1 44  ? 10.842  -23.125  -26.060 1.00 63.82  ? 44  ASN K C   1 
ATOM   19344 O O   . ASN K  1 44  ? 11.812  -23.796  -26.410 1.00 74.98  ? 44  ASN K O   1 
ATOM   19345 C CB  . ASN K  1 44  ? 9.046   -24.828  -26.523 1.00 48.90  ? 44  ASN K CB  1 
ATOM   19346 C CG  . ASN K  1 44  ? 8.586   -24.200  -27.826 1.00 60.60  ? 44  ASN K CG  1 
ATOM   19347 O OD1 . ASN K  1 44  ? 8.069   -24.886  -28.708 1.00 74.94  ? 44  ASN K OD1 1 
ATOM   19348 N ND2 . ASN K  1 44  ? 8.770   -22.892  -27.955 1.00 64.72  ? 44  ASN K ND2 1 
ATOM   19349 N N   . GLY K  1 45  ? 10.821  -21.798  -26.125 1.00 59.60  ? 45  GLY K N   1 
ATOM   19350 C CA  . GLY K  1 45  ? 11.970  -21.042  -26.587 1.00 66.19  ? 45  GLY K CA  1 
ATOM   19351 C C   . GLY K  1 45  ? 12.346  -21.351  -28.023 1.00 61.75  ? 45  GLY K C   1 
ATOM   19352 O O   . GLY K  1 45  ? 13.500  -21.186  -28.424 1.00 59.89  ? 45  GLY K O   1 
ATOM   19353 N N   . LYS K  1 46  ? 11.367  -21.806  -28.798 1.00 61.84  ? 46  LYS K N   1 
ATOM   19354 C CA  . LYS K  1 46  ? 11.566  -22.088  -30.213 1.00 69.78  ? 46  LYS K CA  1 
ATOM   19355 C C   . LYS K  1 46  ? 10.612  -21.267  -31.065 1.00 62.31  ? 46  LYS K C   1 
ATOM   19356 O O   . LYS K  1 46  ? 9.438   -21.109  -30.727 1.00 65.52  ? 46  LYS K O   1 
ATOM   19357 C CB  . LYS K  1 46  ? 11.330  -23.571  -30.509 1.00 71.03  ? 46  LYS K CB  1 
ATOM   19358 C CG  . LYS K  1 46  ? 12.246  -24.533  -29.777 1.00 70.87  ? 46  LYS K CG  1 
ATOM   19359 C CD  . LYS K  1 46  ? 11.736  -25.959  -29.925 1.00 97.84  ? 46  LYS K CD  1 
ATOM   19360 C CE  . LYS K  1 46  ? 12.690  -26.970  -29.313 1.00 115.04 ? 46  LYS K CE  1 
ATOM   19361 N NZ  . LYS K  1 46  ? 12.119  -28.346  -29.356 1.00 110.45 ? 46  LYS K NZ  1 
ATOM   19362 N N   . LEU K  1 47  ? 11.122  -20.741  -32.172 1.00 53.92  ? 47  LEU K N   1 
ATOM   19363 C CA  . LEU K  1 47  ? 10.260  -20.154  -33.186 1.00 51.52  ? 47  LEU K CA  1 
ATOM   19364 C C   . LEU K  1 47  ? 9.745   -21.281  -34.075 1.00 55.68  ? 47  LEU K C   1 
ATOM   19365 O O   . LEU K  1 47  ? 10.465  -21.785  -34.941 1.00 69.58  ? 47  LEU K O   1 
ATOM   19366 C CB  . LEU K  1 47  ? 11.009  -19.096  -34.001 1.00 57.65  ? 47  LEU K CB  1 
ATOM   19367 C CG  . LEU K  1 47  ? 10.949  -17.658  -33.470 1.00 56.77  ? 47  LEU K CG  1 
ATOM   19368 C CD1 . LEU K  1 47  ? 10.809  -17.634  -31.960 1.00 50.83  ? 47  LEU K CD1 1 
ATOM   19369 C CD2 . LEU K  1 47  ? 12.177  -16.875  -33.892 1.00 48.67  ? 47  LEU K CD2 1 
ATOM   19370 N N   . CYS K  1 48  ? 8.496   -21.673  -33.841 1.00 50.49  ? 48  CYS K N   1 
ATOM   19371 C CA  . CYS K  1 48  ? 7.908   -22.837  -34.491 1.00 62.62  ? 48  CYS K CA  1 
ATOM   19372 C C   . CYS K  1 48  ? 6.971   -22.456  -35.629 1.00 64.80  ? 48  CYS K C   1 
ATOM   19373 O O   . CYS K  1 48  ? 6.616   -21.285  -35.803 1.00 59.29  ? 48  CYS K O   1 
ATOM   19374 C CB  . CYS K  1 48  ? 7.145   -23.678  -33.468 1.00 53.44  ? 48  CYS K CB  1 
ATOM   19375 S SG  . CYS K  1 48  ? 8.129   -24.201  -32.049 1.00 90.30  ? 48  CYS K SG  1 
ATOM   19376 N N   . LYS K  1 49  ? 6.583   -23.462  -36.407 1.00 64.53  ? 49  LYS K N   1 
ATOM   19377 C CA  . LYS K  1 49  ? 5.652   -23.270  -37.507 1.00 58.77  ? 49  LYS K CA  1 
ATOM   19378 C C   . LYS K  1 49  ? 4.258   -23.081  -36.935 1.00 52.31  ? 49  LYS K C   1 
ATOM   19379 O O   . LYS K  1 49  ? 3.920   -23.638  -35.886 1.00 60.79  ? 49  LYS K O   1 
ATOM   19380 C CB  . LYS K  1 49  ? 5.680   -24.471  -38.449 1.00 65.10  ? 49  LYS K CB  1 
ATOM   19381 C CG  . LYS K  1 49  ? 6.900   -25.370  -38.258 1.00 62.93  ? 49  LYS K CG  1 
ATOM   19382 C CD  . LYS K  1 49  ? 6.810   -26.646  -39.100 1.00 78.68  ? 49  LYS K CD  1 
ATOM   19383 C CE  . LYS K  1 49  ? 8.025   -27.548  -38.888 1.00 88.97  ? 49  LYS K CE  1 
ATOM   19384 N NZ  . LYS K  1 49  ? 9.299   -26.943  -39.371 1.00 91.03  ? 49  LYS K NZ  1 
ATOM   19385 N N   . LEU K  1 50  ? 3.448   -22.293  -37.626 1.00 58.86  ? 50  LEU K N   1 
ATOM   19386 C CA  . LEU K  1 50  ? 2.215   -21.793  -37.044 1.00 66.83  ? 50  LEU K CA  1 
ATOM   19387 C C   . LEU K  1 50  ? 0.938   -22.595  -37.289 1.00 81.75  ? 50  LEU K C   1 
ATOM   19388 O O   . LEU K  1 50  ? 0.113   -22.759  -36.394 1.00 95.09  ? 50  LEU K O   1 
ATOM   19389 C CB  . LEU K  1 50  ? 1.958   -20.385  -37.580 1.00 68.83  ? 50  LEU K CB  1 
ATOM   19390 C CG  . LEU K  1 50  ? 0.850   -19.558  -36.919 1.00 68.84  ? 50  LEU K CG  1 
ATOM   19391 C CD1 . LEU K  1 50  ? 0.593   -20.009  -35.490 1.00 60.63  ? 50  LEU K CD1 1 
ATOM   19392 C CD2 . LEU K  1 50  ? 1.143   -18.054  -36.979 1.00 55.84  ? 50  LEU K CD2 1 
ATOM   19393 N N   . ARG K  1 51  ? 0.785   -23.089  -38.508 1.00 74.87  ? 51  ARG K N   1 
ATOM   19394 C CA  . ARG K  1 51  ? -0.279  -24.028  -38.826 1.00 88.46  ? 51  ARG K CA  1 
ATOM   19395 C C   . ARG K  1 51  ? 0.432   -25.368  -38.946 1.00 89.90  ? 51  ARG K C   1 
ATOM   19396 O O   . ARG K  1 51  ? 0.495   -26.146  -37.995 1.00 111.79 ? 51  ARG K O   1 
ATOM   19397 C CB  . ARG K  1 51  ? -0.979  -23.699  -40.144 1.00 102.21 ? 51  ARG K CB  1 
ATOM   19398 C CG  . ARG K  1 51  ? -1.372  -22.254  -40.267 1.00 114.59 ? 51  ARG K CG  1 
ATOM   19399 C CD  . ARG K  1 51  ? -2.532  -22.097  -41.216 1.00 143.64 ? 51  ARG K CD  1 
ATOM   19400 N NE  . ARG K  1 51  ? -3.760  -22.658  -40.662 1.00 157.96 ? 51  ARG K NE  1 
ATOM   19401 C CZ  . ARG K  1 51  ? -4.506  -23.579  -41.265 1.00 150.38 ? 51  ARG K CZ  1 
ATOM   19402 N NH1 . ARG K  1 51  ? -4.155  -24.050  -42.455 1.00 136.00 ? 51  ARG K NH1 1 
ATOM   19403 N NH2 . ARG K  1 51  ? -5.609  -24.024  -40.681 1.00 137.75 ? 51  ARG K NH2 1 
ATOM   19404 N N   . GLY K  1 52  ? 0.954   -25.623  -40.139 1.00 75.41  ? 52  GLY K N   1 
ATOM   19405 C CA  . GLY K  1 52  ? 1.870   -26.717  -40.402 1.00 94.88  ? 52  GLY K CA  1 
ATOM   19406 C C   . GLY K  1 52  ? 2.935   -26.111  -41.293 1.00 91.42  ? 52  GLY K C   1 
ATOM   19407 O O   . GLY K  1 52  ? 3.853   -26.782  -41.767 1.00 91.55  ? 52  GLY K O   1 
ATOM   19408 N N   . VAL K  1 53  ? 2.791   -24.807  -41.511 1.00 88.60  ? 53  VAL K N   1 
ATOM   19409 C CA  . VAL K  1 53  ? 3.682   -24.055  -42.383 1.00 68.13  ? 53  VAL K CA  1 
ATOM   19410 C C   . VAL K  1 53  ? 4.799   -23.384  -41.589 1.00 58.41  ? 53  VAL K C   1 
ATOM   19411 O O   . VAL K  1 53  ? 4.571   -22.851  -40.502 1.00 59.85  ? 53  VAL K O   1 
ATOM   19412 C CB  . VAL K  1 53  ? 2.915   -22.972  -43.166 1.00 56.05  ? 53  VAL K CB  1 
ATOM   19413 C CG1 . VAL K  1 53  ? 3.839   -22.298  -44.173 1.00 62.00  ? 53  VAL K CG1 1 
ATOM   19414 C CG2 . VAL K  1 53  ? 1.689   -23.568  -43.851 1.00 41.51  ? 53  VAL K CG2 1 
ATOM   19415 N N   . ALA K  1 54  ? 6.008   -23.412  -42.139 1.00 53.49  ? 54  ALA K N   1 
ATOM   19416 C CA  . ALA K  1 54  ? 7.166   -22.832  -41.471 1.00 47.03  ? 54  ALA K CA  1 
ATOM   19417 C C   . ALA K  1 54  ? 7.254   -21.325  -41.692 1.00 57.09  ? 54  ALA K C   1 
ATOM   19418 O O   . ALA K  1 54  ? 6.746   -20.806  -42.686 1.00 60.26  ? 54  ALA K O   1 
ATOM   19419 C CB  . ALA K  1 54  ? 8.443   -23.512  -41.945 1.00 60.16  ? 54  ALA K CB  1 
ATOM   19420 N N   . PRO K  1 55  ? 7.895   -20.616  -40.752 1.00 48.53  ? 55  PRO K N   1 
ATOM   19421 C CA  . PRO K  1 55  ? 8.142   -19.179  -40.898 1.00 47.22  ? 55  PRO K CA  1 
ATOM   19422 C C   . PRO K  1 55  ? 9.245   -18.904  -41.913 1.00 42.03  ? 55  PRO K C   1 
ATOM   19423 O O   . PRO K  1 55  ? 10.081  -19.773  -42.165 1.00 53.91  ? 55  PRO K O   1 
ATOM   19424 C CB  . PRO K  1 55  ? 8.613   -18.767  -39.501 1.00 43.73  ? 55  PRO K CB  1 
ATOM   19425 C CG  . PRO K  1 55  ? 9.190   -20.012  -38.920 1.00 40.84  ? 55  PRO K CG  1 
ATOM   19426 C CD  . PRO K  1 55  ? 8.321   -21.118  -39.435 1.00 44.01  ? 55  PRO K CD  1 
ATOM   19427 N N   . LEU K  1 56  ? 9.239   -17.708  -42.491 1.00 45.28  ? 56  LEU K N   1 
ATOM   19428 C CA  . LEU K  1 56  ? 10.295  -17.292  -43.403 1.00 47.28  ? 56  LEU K CA  1 
ATOM   19429 C C   . LEU K  1 56  ? 11.375  -16.549  -42.627 1.00 49.03  ? 56  LEU K C   1 
ATOM   19430 O O   . LEU K  1 56  ? 11.174  -15.411  -42.204 1.00 51.44  ? 56  LEU K O   1 
ATOM   19431 C CB  . LEU K  1 56  ? 9.730   -16.396  -44.507 1.00 49.94  ? 56  LEU K CB  1 
ATOM   19432 C CG  . LEU K  1 56  ? 10.723  -15.850  -45.536 1.00 44.83  ? 56  LEU K CG  1 
ATOM   19433 C CD1 . LEU K  1 56  ? 11.354  -16.983  -46.331 1.00 52.13  ? 56  LEU K CD1 1 
ATOM   19434 C CD2 . LEU K  1 56  ? 10.038  -14.858  -46.464 1.00 56.12  ? 56  LEU K CD2 1 
ATOM   19435 N N   . HIS K  1 57  ? 12.518  -17.200  -42.433 1.00 49.98  ? 57  HIS K N   1 
ATOM   19436 C CA  . HIS K  1 57  ? 13.613  -16.611  -41.671 1.00 48.83  ? 57  HIS K CA  1 
ATOM   19437 C C   . HIS K  1 57  ? 14.624  -15.954  -42.603 1.00 61.32  ? 57  HIS K C   1 
ATOM   19438 O O   . HIS K  1 57  ? 15.194  -16.609  -43.469 1.00 65.97  ? 57  HIS K O   1 
ATOM   19439 C CB  . HIS K  1 57  ? 14.301  -17.676  -40.817 1.00 56.72  ? 57  HIS K CB  1 
ATOM   19440 C CG  . HIS K  1 57  ? 15.141  -17.113  -39.714 1.00 59.83  ? 57  HIS K CG  1 
ATOM   19441 N ND1 . HIS K  1 57  ? 16.428  -16.663  -39.912 1.00 63.34  ? 57  HIS K ND1 1 
ATOM   19442 C CD2 . HIS K  1 57  ? 14.875  -16.926  -38.400 1.00 60.62  ? 57  HIS K CD2 1 
ATOM   19443 C CE1 . HIS K  1 57  ? 16.919  -16.222  -38.768 1.00 70.16  ? 57  HIS K CE1 1 
ATOM   19444 N NE2 . HIS K  1 57  ? 15.997  -16.371  -37.834 1.00 69.52  ? 57  HIS K NE2 1 
ATOM   19445 N N   . LEU K  1 58  ? 14.851  -14.659  -42.415 1.00 65.38  ? 58  LEU K N   1 
ATOM   19446 C CA  . LEU K  1 58  ? 15.705  -13.899  -43.322 1.00 66.42  ? 58  LEU K CA  1 
ATOM   19447 C C   . LEU K  1 58  ? 17.154  -13.832  -42.856 1.00 77.33  ? 58  LEU K C   1 
ATOM   19448 O O   . LEU K  1 58  ? 18.036  -13.420  -43.609 1.00 80.57  ? 58  LEU K O   1 
ATOM   19449 C CB  . LEU K  1 58  ? 15.159  -12.485  -43.511 1.00 66.32  ? 58  LEU K CB  1 
ATOM   19450 C CG  . LEU K  1 58  ? 13.713  -12.402  -44.001 1.00 48.73  ? 58  LEU K CG  1 
ATOM   19451 C CD1 . LEU K  1 58  ? 13.313  -10.956  -44.227 1.00 54.27  ? 58  LEU K CD1 1 
ATOM   19452 C CD2 . LEU K  1 58  ? 13.499  -13.234  -45.260 1.00 51.34  ? 58  LEU K CD2 1 
ATOM   19453 N N   . GLY K  1 59  ? 17.395  -14.229  -41.612 1.00 73.07  ? 59  GLY K N   1 
ATOM   19454 C CA  . GLY K  1 59  ? 18.739  -14.233  -41.064 1.00 63.54  ? 59  GLY K CA  1 
ATOM   19455 C C   . GLY K  1 59  ? 19.368  -12.854  -40.992 1.00 76.00  ? 59  GLY K C   1 
ATOM   19456 O O   . GLY K  1 59  ? 18.885  -11.978  -40.275 1.00 85.11  ? 59  GLY K O   1 
ATOM   19457 N N   . LYS K  1 60  ? 20.447  -12.663  -41.743 1.00 86.05  ? 60  LYS K N   1 
ATOM   19458 C CA  . LYS K  1 60  ? 21.205  -11.416  -41.704 1.00 96.03  ? 60  LYS K CA  1 
ATOM   19459 C C   . LYS K  1 60  ? 20.542  -10.304  -42.516 1.00 94.46  ? 60  LYS K C   1 
ATOM   19460 O O   . LYS K  1 60  ? 20.993  -9.159   -42.496 1.00 95.13  ? 60  LYS K O   1 
ATOM   19461 C CB  . LYS K  1 60  ? 22.634  -11.650  -42.205 1.00 106.26 ? 60  LYS K CB  1 
ATOM   19462 C CG  . LYS K  1 60  ? 23.593  -10.502  -41.927 1.00 144.73 ? 60  LYS K CG  1 
ATOM   19463 C CD  . LYS K  1 60  ? 23.798  -10.304  -40.434 1.00 149.93 ? 60  LYS K CD  1 
ATOM   19464 C CE  . LYS K  1 60  ? 24.439  -11.526  -39.798 1.00 156.08 ? 60  LYS K CE  1 
ATOM   19465 N NZ  . LYS K  1 60  ? 24.659  -11.341  -38.337 1.00 149.32 ? 60  LYS K NZ  1 
ATOM   19466 N N   . CYS K  1 61  ? 19.470  -10.641  -43.226 1.00 85.45  ? 61  CYS K N   1 
ATOM   19467 C CA  . CYS K  1 61  ? 18.796  -9.672   -44.084 1.00 73.17  ? 61  CYS K CA  1 
ATOM   19468 C C   . CYS K  1 61  ? 17.431  -9.260   -43.542 1.00 68.55  ? 61  CYS K C   1 
ATOM   19469 O O   . CYS K  1 61  ? 16.854  -9.938   -42.693 1.00 76.63  ? 61  CYS K O   1 
ATOM   19470 C CB  . CYS K  1 61  ? 18.637  -10.231  -45.500 1.00 69.08  ? 61  CYS K CB  1 
ATOM   19471 S SG  . CYS K  1 61  ? 20.190  -10.592  -46.351 1.00 91.33  ? 61  CYS K SG  1 
ATOM   19472 N N   . ASN K  1 62  ? 16.927  -8.136   -44.041 1.00 57.31  ? 62  ASN K N   1 
ATOM   19473 C CA  . ASN K  1 62  ? 15.570  -7.700   -43.740 1.00 68.12  ? 62  ASN K CA  1 
ATOM   19474 C C   . ASN K  1 62  ? 14.695  -7.783   -44.987 1.00 61.84  ? 62  ASN K C   1 
ATOM   19475 O O   . ASN K  1 62  ? 15.194  -8.036   -46.083 1.00 56.34  ? 62  ASN K O   1 
ATOM   19476 C CB  . ASN K  1 62  ? 15.567  -6.282   -43.163 1.00 67.54  ? 62  ASN K CB  1 
ATOM   19477 C CG  . ASN K  1 62  ? 16.224  -5.273   -44.084 1.00 63.58  ? 62  ASN K CG  1 
ATOM   19478 O OD1 . ASN K  1 62  ? 16.285  -5.468   -45.297 1.00 66.06  ? 62  ASN K OD1 1 
ATOM   19479 N ND2 . ASN K  1 62  ? 16.716  -4.183   -43.509 1.00 66.98  ? 62  ASN K ND2 1 
ATOM   19480 N N   . ILE K  1 63  ? 13.394  -7.577   -44.817 1.00 49.46  ? 63  ILE K N   1 
ATOM   19481 C CA  . ILE K  1 63  ? 12.453  -7.684   -45.927 1.00 46.32  ? 63  ILE K CA  1 
ATOM   19482 C C   . ILE K  1 63  ? 12.952  -6.940   -47.163 1.00 47.66  ? 63  ILE K C   1 
ATOM   19483 O O   . ILE K  1 63  ? 12.961  -7.487   -48.265 1.00 51.67  ? 63  ILE K O   1 
ATOM   19484 C CB  . ILE K  1 63  ? 11.059  -7.156   -45.538 1.00 53.04  ? 63  ILE K CB  1 
ATOM   19485 C CG1 . ILE K  1 63  ? 10.492  -7.959   -44.366 1.00 40.42  ? 63  ILE K CG1 1 
ATOM   19486 C CG2 . ILE K  1 63  ? 10.116  -7.226   -46.723 1.00 43.28  ? 63  ILE K CG2 1 
ATOM   19487 C CD1 . ILE K  1 63  ? 10.193  -9.402   -44.705 1.00 53.41  ? 63  ILE K CD1 1 
ATOM   19488 N N   . ALA K  1 64  ? 13.374  -5.694   -46.970 1.00 50.49  ? 64  ALA K N   1 
ATOM   19489 C CA  . ALA K  1 64  ? 13.863  -4.869   -48.070 1.00 48.45  ? 64  ALA K CA  1 
ATOM   19490 C C   . ALA K  1 64  ? 14.956  -5.572   -48.867 1.00 52.50  ? 64  ALA K C   1 
ATOM   19491 O O   . ALA K  1 64  ? 14.847  -5.728   -50.083 1.00 60.68  ? 64  ALA K O   1 
ATOM   19492 C CB  . ALA K  1 64  ? 14.365  -3.531   -47.547 1.00 44.52  ? 64  ALA K CB  1 
ATOM   19493 N N   . GLY K  1 65  ? 16.010  -5.992   -48.175 1.00 56.00  ? 65  GLY K N   1 
ATOM   19494 C CA  . GLY K  1 65  ? 17.124  -6.660   -48.820 1.00 51.22  ? 65  GLY K CA  1 
ATOM   19495 C C   . GLY K  1 65  ? 16.716  -7.937   -49.529 1.00 51.27  ? 65  GLY K C   1 
ATOM   19496 O O   . GLY K  1 65  ? 17.180  -8.220   -50.633 1.00 52.52  ? 65  GLY K O   1 
ATOM   19497 N N   . TRP K  1 66  ? 15.839  -8.707   -48.893 1.00 48.88  ? 66  TRP K N   1 
ATOM   19498 C CA  . TRP K  1 66  ? 15.409  -9.993   -49.434 1.00 61.39  ? 66  TRP K CA  1 
ATOM   19499 C C   . TRP K  1 66  ? 14.647  -9.866   -50.752 1.00 48.59  ? 66  TRP K C   1 
ATOM   19500 O O   . TRP K  1 66  ? 14.905  -10.614  -51.695 1.00 56.31  ? 66  TRP K O   1 
ATOM   19501 C CB  . TRP K  1 66  ? 14.575  -10.760  -48.402 1.00 55.34  ? 66  TRP K CB  1 
ATOM   19502 C CG  . TRP K  1 66  ? 13.771  -11.881  -48.988 1.00 58.88  ? 66  TRP K CG  1 
ATOM   19503 C CD1 . TRP K  1 66  ? 14.251  -13.004  -49.596 1.00 65.48  ? 66  TRP K CD1 1 
ATOM   19504 C CD2 . TRP K  1 66  ? 12.343  -11.990  -49.011 1.00 57.54  ? 66  TRP K CD2 1 
ATOM   19505 N NE1 . TRP K  1 66  ? 13.210  -13.803  -50.004 1.00 66.78  ? 66  TRP K NE1 1 
ATOM   19506 C CE2 . TRP K  1 66  ? 12.027  -13.203  -49.655 1.00 59.96  ? 66  TRP K CE2 1 
ATOM   19507 C CE3 . TRP K  1 66  ? 11.301  -11.180  -48.551 1.00 52.57  ? 66  TRP K CE3 1 
ATOM   19508 C CZ2 . TRP K  1 66  ? 10.714  -13.624  -49.852 1.00 57.96  ? 66  TRP K CZ2 1 
ATOM   19509 C CZ3 . TRP K  1 66  ? 9.997   -11.599  -48.748 1.00 59.61  ? 66  TRP K CZ3 1 
ATOM   19510 C CH2 . TRP K  1 66  ? 9.715   -12.810  -49.392 1.00 58.43  ? 66  TRP K CH2 1 
ATOM   19511 N N   . ILE K  1 67  ? 13.716  -8.920   -50.819 1.00 53.00  ? 67  ILE K N   1 
ATOM   19512 C CA  . ILE K  1 67  ? 12.886  -8.765   -52.010 1.00 60.43  ? 67  ILE K CA  1 
ATOM   19513 C C   . ILE K  1 67  ? 13.627  -8.053   -53.135 1.00 57.46  ? 67  ILE K C   1 
ATOM   19514 O O   . ILE K  1 67  ? 13.489  -8.416   -54.302 1.00 58.46  ? 67  ILE K O   1 
ATOM   19515 C CB  . ILE K  1 67  ? 11.587  -7.997   -51.715 1.00 41.92  ? 67  ILE K CB  1 
ATOM   19516 C CG1 . ILE K  1 67  ? 11.030  -8.381   -50.347 1.00 70.98  ? 67  ILE K CG1 1 
ATOM   19517 C CG2 . ILE K  1 67  ? 10.558  -8.267   -52.799 1.00 44.56  ? 67  ILE K CG2 1 
ATOM   19518 C CD1 . ILE K  1 67  ? 9.747   -7.669   -50.006 1.00 85.27  ? 67  ILE K CD1 1 
ATOM   19519 N N   . LEU K  1 68  ? 14.404  -7.033   -52.786 1.00 49.18  ? 68  LEU K N   1 
ATOM   19520 C CA  . LEU K  1 68  ? 15.167  -6.295   -53.785 1.00 52.15  ? 68  LEU K CA  1 
ATOM   19521 C C   . LEU K  1 68  ? 16.241  -7.171   -54.418 1.00 56.11  ? 68  LEU K C   1 
ATOM   19522 O O   . LEU K  1 68  ? 16.590  -6.996   -55.585 1.00 53.35  ? 68  LEU K O   1 
ATOM   19523 C CB  . LEU K  1 68  ? 15.795  -5.038   -53.177 1.00 51.37  ? 68  LEU K CB  1 
ATOM   19524 C CG  . LEU K  1 68  ? 14.836  -3.874   -52.928 1.00 54.38  ? 68  LEU K CG  1 
ATOM   19525 C CD1 . LEU K  1 68  ? 15.600  -2.635   -52.489 1.00 44.84  ? 68  LEU K CD1 1 
ATOM   19526 C CD2 . LEU K  1 68  ? 14.025  -3.584   -54.180 1.00 36.31  ? 68  LEU K CD2 1 
ATOM   19527 N N   . GLY K  1 69  ? 16.758  -8.116   -53.641 1.00 61.75  ? 69  GLY K N   1 
ATOM   19528 C CA  . GLY K  1 69  ? 17.771  -9.030   -54.130 1.00 55.76  ? 69  GLY K CA  1 
ATOM   19529 C C   . GLY K  1 69  ? 19.172  -8.565   -53.796 1.00 63.42  ? 69  GLY K C   1 
ATOM   19530 O O   . GLY K  1 69  ? 20.079  -8.656   -54.622 1.00 59.69  ? 69  GLY K O   1 
ATOM   19531 N N   . ASN K  1 70  ? 19.346  -8.056   -52.581 1.00 67.92  ? 70  ASN K N   1 
ATOM   19532 C CA  . ASN K  1 70  ? 20.661  -7.650   -52.108 1.00 74.14  ? 70  ASN K CA  1 
ATOM   19533 C C   . ASN K  1 70  ? 21.646  -8.802   -52.269 1.00 86.27  ? 70  ASN K C   1 
ATOM   19534 O O   . ASN K  1 70  ? 21.331  -9.941   -51.924 1.00 81.28  ? 70  ASN K O   1 
ATOM   19535 C CB  . ASN K  1 70  ? 20.582  -7.208   -50.645 1.00 70.12  ? 70  ASN K CB  1 
ATOM   19536 C CG  . ASN K  1 70  ? 21.871  -6.582   -50.149 1.00 79.27  ? 70  ASN K CG  1 
ATOM   19537 O OD1 . ASN K  1 70  ? 22.956  -7.127   -50.343 1.00 85.31  ? 70  ASN K OD1 1 
ATOM   19538 N ND2 . ASN K  1 70  ? 21.755  -5.433   -49.493 1.00 80.02  ? 70  ASN K ND2 1 
ATOM   19539 N N   . PRO K  1 71  ? 22.838  -8.513   -52.812 1.00 98.07  ? 71  PRO K N   1 
ATOM   19540 C CA  . PRO K  1 71  ? 23.855  -9.541   -53.055 1.00 87.07  ? 71  PRO K CA  1 
ATOM   19541 C C   . PRO K  1 71  ? 24.099  -10.446  -51.848 1.00 88.40  ? 71  PRO K C   1 
ATOM   19542 O O   . PRO K  1 71  ? 24.474  -11.604  -52.023 1.00 112.54 ? 71  PRO K O   1 
ATOM   19543 C CB  . PRO K  1 71  ? 25.108  -8.718   -53.352 1.00 90.63  ? 71  PRO K CB  1 
ATOM   19544 C CG  . PRO K  1 71  ? 24.587  -7.467   -53.959 1.00 94.90  ? 71  PRO K CG  1 
ATOM   19545 C CD  . PRO K  1 71  ? 23.276  -7.183   -53.272 1.00 96.03  ? 71  PRO K CD  1 
ATOM   19546 N N   . GLU K  1 72  ? 23.884  -9.923   -50.645 1.00 89.52  ? 72  GLU K N   1 
ATOM   19547 C CA  . GLU K  1 72  ? 24.163  -10.672  -49.423 1.00 94.73  ? 72  GLU K CA  1 
ATOM   19548 C C   . GLU K  1 72  ? 22.953  -11.455  -48.914 1.00 82.12  ? 72  GLU K C   1 
ATOM   19549 O O   . GLU K  1 72  ? 23.060  -12.223  -47.959 1.00 87.04  ? 72  GLU K O   1 
ATOM   19550 C CB  . GLU K  1 72  ? 24.678  -9.733   -48.330 1.00 92.79  ? 72  GLU K CB  1 
ATOM   19551 C CG  . GLU K  1 72  ? 25.945  -8.978   -48.703 1.00 111.55 ? 72  GLU K CG  1 
ATOM   19552 C CD  . GLU K  1 72  ? 27.157  -9.884   -48.817 1.00 130.61 ? 72  GLU K CD  1 
ATOM   19553 O OE1 . GLU K  1 72  ? 27.152  -10.969  -48.200 1.00 135.26 ? 72  GLU K OE1 1 
ATOM   19554 O OE2 . GLU K  1 72  ? 28.119  -9.507   -49.521 1.00 112.57 ? 72  GLU K OE2 1 
ATOM   19555 N N   . CYS K  1 73  ? 21.804  -11.255  -49.549 1.00 100.62 ? 73  CYS K N   1 
ATOM   19556 C CA  . CYS K  1 73  ? 20.593  -11.978  -49.178 1.00 101.79 ? 73  CYS K CA  1 
ATOM   19557 C C   . CYS K  1 73  ? 20.354  -13.141  -50.137 1.00 122.02 ? 73  CYS K C   1 
ATOM   19558 O O   . CYS K  1 73  ? 19.225  -13.399  -50.552 1.00 130.29 ? 73  CYS K O   1 
ATOM   19559 C CB  . CYS K  1 73  ? 19.394  -11.031  -49.176 1.00 86.94  ? 73  CYS K CB  1 
ATOM   19560 S SG  . CYS K  1 73  ? 19.557  -9.637   -48.028 1.00 83.98  ? 73  CYS K SG  1 
ATOM   19561 N N   . GLU K  1 74  ? 21.430  -13.848  -50.464 1.00 132.45 ? 74  GLU K N   1 
ATOM   19562 C CA  . GLU K  1 74  ? 21.425  -14.854  -51.520 1.00 145.78 ? 74  GLU K CA  1 
ATOM   19563 C C   . GLU K  1 74  ? 20.668  -16.130  -51.161 1.00 157.50 ? 74  GLU K C   1 
ATOM   19564 O O   . GLU K  1 74  ? 19.694  -16.488  -51.818 1.00 154.67 ? 74  GLU K O   1 
ATOM   19565 C CB  . GLU K  1 74  ? 22.869  -15.210  -51.886 1.00 148.07 ? 74  GLU K CB  1 
ATOM   19566 C CG  . GLU K  1 74  ? 23.109  -15.498  -53.355 1.00 158.49 ? 74  GLU K CG  1 
ATOM   19567 C CD  . GLU K  1 74  ? 24.345  -14.793  -53.880 1.00 161.54 ? 74  GLU K CD  1 
ATOM   19568 O OE1 . GLU K  1 74  ? 24.904  -13.939  -53.158 1.00 157.50 ? 74  GLU K OE1 1 
ATOM   19569 O OE2 . GLU K  1 74  ? 24.752  -15.088  -55.021 1.00 155.90 ? 74  GLU K OE2 1 
ATOM   19570 N N   . SER K  1 75  ? 21.101  -16.791  -50.092 1.00 159.99 ? 75  SER K N   1 
ATOM   19571 C CA  . SER K  1 75  ? 20.851  -18.227  -49.898 1.00 173.59 ? 75  SER K CA  1 
ATOM   19572 C C   . SER K  1 75  ? 19.454  -18.765  -49.506 1.00 179.10 ? 75  SER K C   1 
ATOM   19573 O O   . SER K  1 75  ? 19.338  -19.961  -49.213 1.00 183.64 ? 75  SER K O   1 
ATOM   19574 C CB  . SER K  1 75  ? 21.876  -18.771  -48.898 1.00 172.17 ? 75  SER K CB  1 
ATOM   19575 O OG  . SER K  1 75  ? 22.210  -17.772  -47.941 1.00 157.92 ? 75  SER K OG  1 
ATOM   19576 N N   . LEU K  1 76  ? 18.392  -17.965  -49.552 1.00 190.35 ? 76  LEU K N   1 
ATOM   19577 C CA  . LEU K  1 76  ? 17.124  -18.486  -49.037 1.00 190.89 ? 76  LEU K CA  1 
ATOM   19578 C C   . LEU K  1 76  ? 15.889  -18.339  -49.967 1.00 190.88 ? 76  LEU K C   1 
ATOM   19579 O O   . LEU K  1 76  ? 14.754  -18.275  -49.496 1.00 180.26 ? 76  LEU K O   1 
ATOM   19580 C CB  . LEU K  1 76  ? 16.860  -17.902  -47.650 1.00 182.47 ? 76  LEU K CB  1 
ATOM   19581 C CG  . LEU K  1 76  ? 15.783  -18.504  -46.755 1.00 173.38 ? 76  LEU K CG  1 
ATOM   19582 C CD1 . LEU K  1 76  ? 15.497  -19.959  -47.177 1.00 175.67 ? 76  LEU K CD1 1 
ATOM   19583 C CD2 . LEU K  1 76  ? 16.206  -18.395  -45.288 1.00 142.45 ? 76  LEU K CD2 1 
ATOM   19584 N N   . SER K  1 77  ? 16.098  -18.340  -51.284 1.00 172.60 ? 77  SER K N   1 
ATOM   19585 C CA  . SER K  1 77  ? 14.979  -18.261  -52.237 1.00 158.55 ? 77  SER K CA  1 
ATOM   19586 C C   . SER K  1 77  ? 13.961  -19.387  -52.003 1.00 155.65 ? 77  SER K C   1 
ATOM   19587 O O   . SER K  1 77  ? 12.761  -19.234  -52.266 1.00 141.36 ? 77  SER K O   1 
ATOM   19588 C CB  . SER K  1 77  ? 15.485  -18.239  -53.689 1.00 153.27 ? 77  SER K CB  1 
ATOM   19589 O OG  . SER K  1 77  ? 15.210  -19.452  -54.361 1.00 142.16 ? 77  SER K OG  1 
ATOM   19590 N N   . THR K  1 78  ? 14.451  -20.507  -51.477 1.00 211.65 ? 78  THR K N   1 
ATOM   19591 C CA  . THR K  1 78  ? 13.653  -21.735  -51.350 1.00 211.30 ? 78  THR K CA  1 
ATOM   19592 C C   . THR K  1 78  ? 12.459  -21.631  -50.381 1.00 204.87 ? 78  THR K C   1 
ATOM   19593 O O   . THR K  1 78  ? 12.492  -22.115  -49.244 1.00 202.75 ? 78  THR K O   1 
ATOM   19594 C CB  . THR K  1 78  ? 14.559  -22.986  -51.098 1.00 195.22 ? 78  THR K CB  1 
ATOM   19595 O OG1 . THR K  1 78  ? 14.959  -23.532  -52.361 1.00 194.06 ? 78  THR K OG1 1 
ATOM   19596 C CG2 . THR K  1 78  ? 13.843  -24.071  -50.310 1.00 146.78 ? 78  THR K CG2 1 
ATOM   19597 N N   . ALA K  1 79  ? 11.396  -20.998  -50.873 1.00 177.02 ? 79  ALA K N   1 
ATOM   19598 C CA  . ALA K  1 79  ? 10.184  -20.758  -50.097 1.00 144.54 ? 79  ALA K CA  1 
ATOM   19599 C C   . ALA K  1 79  ? 8.977   -20.597  -51.014 1.00 122.61 ? 79  ALA K C   1 
ATOM   19600 O O   . ALA K  1 79  ? 8.942   -19.713  -51.870 1.00 116.33 ? 79  ALA K O   1 
ATOM   19601 C CB  . ALA K  1 79  ? 10.351  -19.528  -49.225 1.00 134.43 ? 79  ALA K CB  1 
ATOM   19602 N N   . SER K  1 80  ? 7.991   -21.465  -50.829 1.00 86.99  ? 80  SER K N   1 
ATOM   19603 C CA  . SER K  1 80  ? 6.782   -21.422  -51.630 1.00 86.87  ? 80  SER K CA  1 
ATOM   19604 C C   . SER K  1 80  ? 5.682   -20.769  -50.818 1.00 73.85  ? 80  SER K C   1 
ATOM   19605 O O   . SER K  1 80  ? 4.710   -20.248  -51.363 1.00 69.17  ? 80  SER K O   1 
ATOM   19606 C CB  . SER K  1 80  ? 6.365   -22.835  -52.028 1.00 102.05 ? 80  SER K CB  1 
ATOM   19607 O OG  . SER K  1 80  ? 7.428   -23.507  -52.676 1.00 112.30 ? 80  SER K OG  1 
ATOM   19608 N N   . SER K  1 81  ? 5.849   -20.799  -49.502 1.00 62.75  ? 81  SER K N   1 
ATOM   19609 C CA  . SER K  1 81  ? 4.867   -20.235  -48.593 1.00 61.85  ? 81  SER K CA  1 
ATOM   19610 C C   . SER K  1 81  ? 5.444   -20.110  -47.193 1.00 54.37  ? 81  SER K C   1 
ATOM   19611 O O   . SER K  1 81  ? 6.437   -20.756  -46.860 1.00 58.06  ? 81  SER K O   1 
ATOM   19612 C CB  . SER K  1 81  ? 3.617   -21.113  -48.557 1.00 62.27  ? 81  SER K CB  1 
ATOM   19613 O OG  . SER K  1 81  ? 3.938   -22.442  -48.186 1.00 63.02  ? 81  SER K OG  1 
ATOM   19614 N N   . TRP K  1 82  ? 4.819   -19.272  -46.377 1.00 41.45  ? 82  TRP K N   1 
ATOM   19615 C CA  . TRP K  1 82  ? 5.220   -19.135  -44.985 1.00 46.91  ? 82  TRP K CA  1 
ATOM   19616 C C   . TRP K  1 82  ? 4.090   -18.572  -44.135 1.00 48.68  ? 82  TRP K C   1 
ATOM   19617 O O   . TRP K  1 82  ? 3.300   -17.744  -44.594 1.00 51.00  ? 82  TRP K O   1 
ATOM   19618 C CB  . TRP K  1 82  ? 6.481   -18.275  -44.853 1.00 47.74  ? 82  TRP K CB  1 
ATOM   19619 C CG  . TRP K  1 82  ? 6.380   -16.933  -45.506 1.00 53.14  ? 82  TRP K CG  1 
ATOM   19620 C CD1 . TRP K  1 82  ? 5.852   -15.796  -44.967 1.00 54.54  ? 82  TRP K CD1 1 
ATOM   19621 C CD2 . TRP K  1 82  ? 6.832   -16.582  -46.819 1.00 48.24  ? 82  TRP K CD2 1 
ATOM   19622 N NE1 . TRP K  1 82  ? 5.942   -14.760  -45.865 1.00 50.59  ? 82  TRP K NE1 1 
ATOM   19623 C CE2 . TRP K  1 82  ? 6.540   -15.217  -47.010 1.00 47.94  ? 82  TRP K CE2 1 
ATOM   19624 C CE3 . TRP K  1 82  ? 7.452   -17.290  -47.853 1.00 43.78  ? 82  TRP K CE3 1 
ATOM   19625 C CZ2 . TRP K  1 82  ? 6.847   -14.547  -48.193 1.00 49.16  ? 82  TRP K CZ2 1 
ATOM   19626 C CZ3 . TRP K  1 82  ? 7.756   -16.623  -49.025 1.00 51.03  ? 82  TRP K CZ3 1 
ATOM   19627 C CH2 . TRP K  1 82  ? 7.453   -15.266  -49.185 1.00 44.69  ? 82  TRP K CH2 1 
ATOM   19628 N N   . SER K  1 83  ? 4.018   -19.039  -42.894 1.00 51.57  ? 83  SER K N   1 
ATOM   19629 C CA  . SER K  1 83  ? 2.968   -18.627  -41.976 1.00 52.10  ? 83  SER K CA  1 
ATOM   19630 C C   . SER K  1 83  ? 3.236   -17.243  -41.401 1.00 45.36  ? 83  SER K C   1 
ATOM   19631 O O   . SER K  1 83  ? 2.302   -16.501  -41.135 1.00 55.52  ? 83  SER K O   1 
ATOM   19632 C CB  . SER K  1 83  ? 2.813   -19.647  -40.849 1.00 52.95  ? 83  SER K CB  1 
ATOM   19633 O OG  . SER K  1 83  ? 4.053   -19.876  -40.204 1.00 52.32  ? 83  SER K OG  1 
ATOM   19634 N N   . TYR K  1 84  ? 4.509   -16.912  -41.204 1.00 36.96  ? 84  TYR K N   1 
ATOM   19635 C CA  . TYR K  1 84  ? 4.910   -15.581  -40.749 1.00 40.64  ? 84  TYR K CA  1 
ATOM   19636 C C   . TYR K  1 84  ? 6.376   -15.327  -41.084 1.00 44.46  ? 84  TYR K C   1 
ATOM   19637 O O   . TYR K  1 84  ? 7.072   -16.224  -41.555 1.00 54.18  ? 84  TYR K O   1 
ATOM   19638 C CB  . TYR K  1 84  ? 4.665   -15.411  -39.246 1.00 40.10  ? 84  TYR K CB  1 
ATOM   19639 C CG  . TYR K  1 84  ? 5.483   -16.333  -38.370 1.00 50.27  ? 84  TYR K CG  1 
ATOM   19640 C CD1 . TYR K  1 84  ? 6.642   -15.885  -37.749 1.00 44.08  ? 84  TYR K CD1 1 
ATOM   19641 C CD2 . TYR K  1 84  ? 5.095   -17.649  -38.162 1.00 48.76  ? 84  TYR K CD2 1 
ATOM   19642 C CE1 . TYR K  1 84  ? 7.390   -16.724  -36.945 1.00 43.75  ? 84  TYR K CE1 1 
ATOM   19643 C CE2 . TYR K  1 84  ? 5.838   -18.495  -37.361 1.00 39.97  ? 84  TYR K CE2 1 
ATOM   19644 C CZ  . TYR K  1 84  ? 6.984   -18.027  -36.755 1.00 43.88  ? 84  TYR K CZ  1 
ATOM   19645 O OH  . TYR K  1 84  ? 7.729   -18.865  -35.957 1.00 53.21  ? 84  TYR K OH  1 
ATOM   19646 N N   . ILE K  1 85  ? 6.843   -14.106  -40.844 1.00 35.68  ? 85  ILE K N   1 
ATOM   19647 C CA  . ILE K  1 85  ? 8.216   -13.742  -41.182 1.00 45.21  ? 85  ILE K CA  1 
ATOM   19648 C C   . ILE K  1 85  ? 9.060   -13.460  -39.944 1.00 49.22  ? 85  ILE K C   1 
ATOM   19649 O O   . ILE K  1 85  ? 8.622   -12.767  -39.025 1.00 43.87  ? 85  ILE K O   1 
ATOM   19650 C CB  . ILE K  1 85  ? 8.262   -12.523  -42.125 1.00 44.26  ? 85  ILE K CB  1 
ATOM   19651 C CG1 . ILE K  1 85  ? 7.564   -12.852  -43.446 1.00 40.13  ? 85  ILE K CG1 1 
ATOM   19652 C CG2 . ILE K  1 85  ? 9.701   -12.094  -42.373 1.00 37.54  ? 85  ILE K CG2 1 
ATOM   19653 C CD1 . ILE K  1 85  ? 7.499   -11.690  -44.411 1.00 45.46  ? 85  ILE K CD1 1 
ATOM   19654 N N   . VAL K  1 86  ? 10.273  -14.003  -39.927 1.00 48.23  ? 86  VAL K N   1 
ATOM   19655 C CA  . VAL K  1 86  ? 11.189  -13.790  -38.814 1.00 44.24  ? 86  VAL K CA  1 
ATOM   19656 C C   . VAL K  1 86  ? 12.397  -12.958  -39.234 1.00 41.48  ? 86  VAL K C   1 
ATOM   19657 O O   . VAL K  1 86  ? 13.080  -13.277  -40.208 1.00 46.14  ? 86  VAL K O   1 
ATOM   19658 C CB  . VAL K  1 86  ? 11.680  -15.120  -38.213 1.00 46.92  ? 86  VAL K CB  1 
ATOM   19659 C CG1 . VAL K  1 86  ? 12.581  -14.856  -37.016 1.00 42.81  ? 86  VAL K CG1 1 
ATOM   19660 C CG2 . VAL K  1 86  ? 10.501  -15.988  -37.811 1.00 47.54  ? 86  VAL K CG2 1 
ATOM   19661 N N   . GLU K  1 87  ? 12.646  -11.888  -38.488 1.00 48.64  ? 87  GLU K N   1 
ATOM   19662 C CA  . GLU K  1 87  ? 13.789  -11.017  -38.723 1.00 51.77  ? 87  GLU K CA  1 
ATOM   19663 C C   . GLU K  1 87  ? 14.640  -10.987  -37.459 1.00 65.17  ? 87  GLU K C   1 
ATOM   19664 O O   . GLU K  1 87  ? 14.107  -10.894  -36.356 1.00 68.72  ? 87  GLU K O   1 
ATOM   19665 C CB  . GLU K  1 87  ? 13.310  -9.603   -39.057 1.00 51.44  ? 87  GLU K CB  1 
ATOM   19666 C CG  . GLU K  1 87  ? 13.866  -9.023   -40.349 1.00 56.66  ? 87  GLU K CG  1 
ATOM   19667 C CD  . GLU K  1 87  ? 13.265  -7.668   -40.678 1.00 67.72  ? 87  GLU K CD  1 
ATOM   19668 O OE1 . GLU K  1 87  ? 13.055  -7.381   -41.875 1.00 68.38  ? 87  GLU K OE1 1 
ATOM   19669 O OE2 . GLU K  1 87  ? 12.991  -6.894   -39.737 1.00 69.48  ? 87  GLU K OE2 1 
ATOM   19670 N N   . THR K  1 88  ? 15.957  -11.072  -37.613 1.00 70.73  ? 88  THR K N   1 
ATOM   19671 C CA  . THR K  1 88  ? 16.862  -11.016  -36.467 1.00 72.84  ? 88  THR K CA  1 
ATOM   19672 C C   . THR K  1 88  ? 17.194  -9.562   -36.137 1.00 78.51  ? 88  THR K C   1 
ATOM   19673 O O   . THR K  1 88  ? 17.345  -8.747   -37.043 1.00 88.79  ? 88  THR K O   1 
ATOM   19674 C CB  . THR K  1 88  ? 18.166  -11.781  -36.752 1.00 79.03  ? 88  THR K CB  1 
ATOM   19675 O OG1 . THR K  1 88  ? 18.911  -11.096  -37.767 1.00 94.03  ? 88  THR K OG1 1 
ATOM   19676 C CG2 . THR K  1 88  ? 17.863  -13.203  -37.214 1.00 67.38  ? 88  THR K CG2 1 
ATOM   19677 N N   . PRO K  1 89  ? 17.304  -9.226   -34.838 1.00 97.95  ? 89  PRO K N   1 
ATOM   19678 C CA  . PRO K  1 89  ? 17.564  -7.836   -34.444 1.00 97.04  ? 89  PRO K CA  1 
ATOM   19679 C C   . PRO K  1 89  ? 18.890  -7.368   -35.016 1.00 108.66 ? 89  PRO K C   1 
ATOM   19680 O O   . PRO K  1 89  ? 19.141  -6.167   -35.106 1.00 107.95 ? 89  PRO K O   1 
ATOM   19681 C CB  . PRO K  1 89  ? 17.648  -7.911   -32.917 1.00 92.33  ? 89  PRO K CB  1 
ATOM   19682 C CG  . PRO K  1 89  ? 16.892  -9.126   -32.558 1.00 97.66  ? 89  PRO K CG  1 
ATOM   19683 C CD  . PRO K  1 89  ? 17.133  -10.101  -33.668 1.00 104.29 ? 89  PRO K CD  1 
ATOM   19684 N N   . SER K  1 90  ? 19.728  -8.323   -35.407 1.00 125.38 ? 90  SER K N   1 
ATOM   19685 C CA  . SER K  1 90  ? 21.000  -8.005   -36.043 1.00 123.35 ? 90  SER K CA  1 
ATOM   19686 C C   . SER K  1 90  ? 20.877  -8.141   -37.576 1.00 130.94 ? 90  SER K C   1 
ATOM   19687 O O   . SER K  1 90  ? 21.815  -8.608   -38.243 1.00 144.53 ? 90  SER K O   1 
ATOM   19688 C CB  . SER K  1 90  ? 22.120  -8.905   -35.503 1.00 131.87 ? 90  SER K CB  1 
ATOM   19689 O OG  . SER K  1 90  ? 23.394  -8.468   -35.942 1.00 153.19 ? 90  SER K OG  1 
ATOM   19690 N N   . SER K  1 91  ? 19.737  -7.708   -38.133 1.00 110.75 ? 91  SER K N   1 
ATOM   19691 C CA  . SER K  1 91  ? 19.617  -7.583   -39.586 1.00 105.24 ? 91  SER K CA  1 
ATOM   19692 C C   . SER K  1 91  ? 20.483  -6.376   -39.879 1.00 113.35 ? 91  SER K C   1 
ATOM   19693 O O   . SER K  1 91  ? 21.250  -5.929   -39.019 1.00 112.24 ? 91  SER K O   1 
ATOM   19694 C CB  . SER K  1 91  ? 18.173  -7.298   -40.049 1.00 98.35  ? 91  SER K CB  1 
ATOM   19695 O OG  . SER K  1 91  ? 17.195  -7.659   -39.088 1.00 99.48  ? 91  SER K OG  1 
ATOM   19696 N N   . ASP K  1 92  ? 20.347  -5.832   -41.082 1.00 129.16 ? 92  ASP K N   1 
ATOM   19697 C CA  . ASP K  1 92  ? 21.307  -4.844   -41.553 1.00 134.74 ? 92  ASP K CA  1 
ATOM   19698 C C   . ASP K  1 92  ? 21.103  -3.420   -42.061 1.00 124.33 ? 92  ASP K C   1 
ATOM   19699 O O   . ASP K  1 92  ? 21.680  -2.999   -43.074 1.00 132.15 ? 92  ASP K O   1 
ATOM   19700 C CB  . ASP K  1 92  ? 22.360  -5.494   -42.460 1.00 149.60 ? 92  ASP K CB  1 
ATOM   19701 C CG  . ASP K  1 92  ? 21.849  -5.797   -43.864 1.00 146.50 ? 92  ASP K CG  1 
ATOM   19702 O OD1 . ASP K  1 92  ? 20.832  -6.515   -43.961 1.00 145.60 ? 92  ASP K OD1 1 
ATOM   19703 O OD2 . ASP K  1 92  ? 22.424  -5.305   -44.860 1.00 148.75 ? 92  ASP K OD2 1 
ATOM   19704 N N   . ASN K  1 93  ? 20.251  -2.705   -41.346 1.00 108.78 ? 93  ASN K N   1 
ATOM   19705 C CA  . ASN K  1 93  ? 19.857  -1.375   -41.723 1.00 104.15 ? 93  ASN K CA  1 
ATOM   19706 C C   . ASN K  1 93  ? 19.239  -1.494   -43.072 1.00 102.46 ? 93  ASN K C   1 
ATOM   19707 O O   . ASN K  1 93  ? 18.491  -2.417   -43.319 1.00 91.63  ? 93  ASN K O   1 
ATOM   19708 C CB  . ASN K  1 93  ? 20.786  -0.175   -41.650 1.00 104.20 ? 93  ASN K CB  1 
ATOM   19709 C CG  . ASN K  1 93  ? 20.297  0.857    -40.666 1.00 111.16 ? 93  ASN K CG  1 
ATOM   19710 O OD1 . ASN K  1 93  ? 20.510  2.051    -40.851 1.00 110.56 ? 93  ASN K OD1 1 
ATOM   19711 N ND2 . ASN K  1 93  ? 19.613  0.398    -39.613 1.00 107.76 ? 93  ASN K ND2 1 
ATOM   19712 N N   . GLY K  1 94  ? 19.527  -0.556   -43.953 1.00 125.08 ? 94  GLY K N   1 
ATOM   19713 C CA  . GLY K  1 94  ? 18.658  -0.404   -45.102 1.00 109.81 ? 94  GLY K CA  1 
ATOM   19714 C C   . GLY K  1 94  ? 19.192  -0.990   -46.394 1.00 117.35 ? 94  GLY K C   1 
ATOM   19715 O O   . GLY K  1 94  ? 20.165  -1.740   -46.391 1.00 105.92 ? 94  GLY K O   1 
ATOM   19716 N N   . THR K  1 95  ? 18.534  -0.655   -47.501 1.00 74.39  ? 95  THR K N   1 
ATOM   19717 C CA  . THR K  1 95  ? 19.026  -0.999   -48.830 1.00 76.39  ? 95  THR K CA  1 
ATOM   19718 C C   . THR K  1 95  ? 20.495  -0.604   -48.924 1.00 68.28  ? 95  THR K C   1 
ATOM   19719 O O   . THR K  1 95  ? 20.939  0.311    -48.229 1.00 66.71  ? 95  THR K O   1 
ATOM   19720 C CB  . THR K  1 95  ? 18.241  -0.252   -49.930 1.00 63.53  ? 95  THR K CB  1 
ATOM   19721 O OG1 . THR K  1 95  ? 18.935  0.950    -50.280 1.00 65.04  ? 95  THR K OG1 1 
ATOM   19722 C CG2 . THR K  1 95  ? 16.841  0.103    -49.445 1.00 61.16  ? 95  THR K CG2 1 
ATOM   19723 N N   . CYS K  1 96  ? 21.252  -1.298   -49.769 1.00 58.67  ? 96  CYS K N   1 
ATOM   19724 C CA  . CYS K  1 96  ? 22.665  -0.978   -49.953 1.00 70.10  ? 96  CYS K CA  1 
ATOM   19725 C C   . CYS K  1 96  ? 22.872  0.387    -50.617 1.00 63.85  ? 96  CYS K C   1 
ATOM   19726 O O   . CYS K  1 96  ? 23.806  1.112    -50.275 1.00 67.96  ? 96  CYS K O   1 
ATOM   19727 C CB  . CYS K  1 96  ? 23.395  -2.089   -50.714 1.00 72.71  ? 96  CYS K CB  1 
ATOM   19728 S SG  . CYS K  1 96  ? 22.582  -2.685   -52.214 1.00 83.60  ? 96  CYS K SG  1 
ATOM   19729 N N   . TYR K  1 97  ? 22.002  0.735    -51.561 1.00 64.89  ? 97  TYR K N   1 
ATOM   19730 C CA  . TYR K  1 97  ? 22.031  2.071    -52.153 1.00 59.67  ? 97  TYR K CA  1 
ATOM   19731 C C   . TYR K  1 97  ? 21.018  2.983    -51.465 1.00 59.32  ? 97  TYR K C   1 
ATOM   19732 O O   . TYR K  1 97  ? 19.819  2.714    -51.491 1.00 60.08  ? 97  TYR K O   1 
ATOM   19733 C CB  . TYR K  1 97  ? 21.756  2.025    -53.658 1.00 58.64  ? 97  TYR K CB  1 
ATOM   19734 C CG  . TYR K  1 97  ? 22.207  3.276    -54.387 1.00 58.72  ? 97  TYR K CG  1 
ATOM   19735 C CD1 . TYR K  1 97  ? 23.344  3.266    -55.183 1.00 69.91  ? 97  TYR K CD1 1 
ATOM   19736 C CD2 . TYR K  1 97  ? 21.507  4.471    -54.264 1.00 61.18  ? 97  TYR K CD2 1 
ATOM   19737 C CE1 . TYR K  1 97  ? 23.767  4.405    -55.845 1.00 71.55  ? 97  TYR K CE1 1 
ATOM   19738 C CE2 . TYR K  1 97  ? 21.924  5.617    -54.923 1.00 62.89  ? 97  TYR K CE2 1 
ATOM   19739 C CZ  . TYR K  1 97  ? 23.054  5.577    -55.712 1.00 62.38  ? 97  TYR K CZ  1 
ATOM   19740 O OH  . TYR K  1 97  ? 23.477  6.710    -56.370 1.00 63.11  ? 97  TYR K OH  1 
ATOM   19741 N N   . PRO K  1 98  ? 21.499  4.080    -50.864 1.00 54.80  ? 98  PRO K N   1 
ATOM   19742 C CA  . PRO K  1 98  ? 20.652  4.985    -50.077 1.00 51.95  ? 98  PRO K CA  1 
ATOM   19743 C C   . PRO K  1 98  ? 19.401  5.418    -50.833 1.00 61.70  ? 98  PRO K C   1 
ATOM   19744 O O   . PRO K  1 98  ? 19.457  5.651    -52.040 1.00 55.06  ? 98  PRO K O   1 
ATOM   19745 C CB  . PRO K  1 98  ? 21.558  6.196    -49.841 1.00 56.51  ? 98  PRO K CB  1 
ATOM   19746 C CG  . PRO K  1 98  ? 22.932  5.671    -49.969 1.00 63.47  ? 98  PRO K CG  1 
ATOM   19747 C CD  . PRO K  1 98  ? 22.872  4.594    -51.003 1.00 64.85  ? 98  PRO K CD  1 
ATOM   19748 N N   . GLY K  1 99  ? 18.285  5.529    -50.122 1.00 59.01  ? 99  GLY K N   1 
ATOM   19749 C CA  . GLY K  1 99  ? 17.036  5.932    -50.738 1.00 55.28  ? 99  GLY K CA  1 
ATOM   19750 C C   . GLY K  1 99  ? 15.832  5.615    -49.875 1.00 59.02  ? 99  GLY K C   1 
ATOM   19751 O O   . GLY K  1 99  ? 15.964  5.052    -48.789 1.00 56.58  ? 99  GLY K O   1 
ATOM   19752 N N   . ASP K  1 100 ? 14.652  5.977    -50.364 1.00 65.25  ? 100 ASP K N   1 
ATOM   19753 C CA  . ASP K  1 100 ? 13.421  5.758    -49.619 1.00 50.95  ? 100 ASP K CA  1 
ATOM   19754 C C   . ASP K  1 100 ? 12.651  4.569    -50.181 1.00 44.92  ? 100 ASP K C   1 
ATOM   19755 O O   . ASP K  1 100 ? 12.477  4.452    -51.393 1.00 49.21  ? 100 ASP K O   1 
ATOM   19756 C CB  . ASP K  1 100 ? 12.547  7.015    -49.664 1.00 54.82  ? 100 ASP K CB  1 
ATOM   19757 C CG  . ASP K  1 100 ? 11.454  7.004    -48.614 1.00 88.20  ? 100 ASP K CG  1 
ATOM   19758 O OD1 . ASP K  1 100 ? 11.556  6.205    -47.659 1.00 102.15 ? 100 ASP K OD1 1 
ATOM   19759 O OD2 . ASP K  1 100 ? 10.497  7.798    -48.738 1.00 93.92  ? 100 ASP K OD2 1 
ATOM   19760 N N   . PHE K  1 101 ? 12.199  3.683    -49.300 1.00 34.82  ? 101 PHE K N   1 
ATOM   19761 C CA  . PHE K  1 101 ? 11.343  2.576    -49.708 1.00 43.03  ? 101 PHE K CA  1 
ATOM   19762 C C   . PHE K  1 101 ? 9.884   2.959    -49.468 1.00 44.44  ? 101 PHE K C   1 
ATOM   19763 O O   . PHE K  1 101 ? 9.396   2.908    -48.340 1.00 44.01  ? 101 PHE K O   1 
ATOM   19764 C CB  . PHE K  1 101 ? 11.701  1.303    -48.938 1.00 39.80  ? 101 PHE K CB  1 
ATOM   19765 C CG  . PHE K  1 101 ? 11.348  0.036    -49.665 1.00 35.28  ? 101 PHE K CG  1 
ATOM   19766 C CD1 . PHE K  1 101 ? 12.322  -0.901   -49.970 1.00 43.34  ? 101 PHE K CD1 1 
ATOM   19767 C CD2 . PHE K  1 101 ? 10.044  -0.211   -50.054 1.00 46.84  ? 101 PHE K CD2 1 
ATOM   19768 C CE1 . PHE K  1 101 ? 11.998  -2.066   -50.640 1.00 36.98  ? 101 PHE K CE1 1 
ATOM   19769 C CE2 . PHE K  1 101 ? 9.713   -1.372   -50.726 1.00 40.90  ? 101 PHE K CE2 1 
ATOM   19770 C CZ  . PHE K  1 101 ? 10.691  -2.301   -51.020 1.00 33.09  ? 101 PHE K CZ  1 
ATOM   19771 N N   . ILE K  1 102 ? 9.194   3.346    -50.536 1.00 34.12  ? 102 ILE K N   1 
ATOM   19772 C CA  . ILE K  1 102 ? 7.835   3.870    -50.433 1.00 36.55  ? 102 ILE K CA  1 
ATOM   19773 C C   . ILE K  1 102 ? 6.861   2.826    -49.894 1.00 41.74  ? 102 ILE K C   1 
ATOM   19774 O O   . ILE K  1 102 ? 6.838   1.690    -50.370 1.00 44.59  ? 102 ILE K O   1 
ATOM   19775 C CB  . ILE K  1 102 ? 7.330   4.387    -51.797 1.00 46.37  ? 102 ILE K CB  1 
ATOM   19776 C CG1 . ILE K  1 102 ? 8.477   5.031    -52.584 1.00 54.24  ? 102 ILE K CG1 1 
ATOM   19777 C CG2 . ILE K  1 102 ? 6.172   5.359    -51.609 1.00 43.62  ? 102 ILE K CG2 1 
ATOM   19778 C CD1 . ILE K  1 102 ? 9.175   6.181    -51.872 1.00 44.19  ? 102 ILE K CD1 1 
ATOM   19779 N N   . ASP K  1 103 ? 6.056   3.220    -48.909 1.00 45.08  ? 103 ASP K N   1 
ATOM   19780 C CA  . ASP K  1 103 ? 5.088   2.316    -48.295 1.00 39.85  ? 103 ASP K CA  1 
ATOM   19781 C C   . ASP K  1 103 ? 5.743   0.975    -47.984 1.00 39.82  ? 103 ASP K C   1 
ATOM   19782 O O   . ASP K  1 103 ? 5.250   -0.080   -48.382 1.00 37.80  ? 103 ASP K O   1 
ATOM   19783 C CB  . ASP K  1 103 ? 3.871   2.132    -49.206 1.00 50.65  ? 103 ASP K CB  1 
ATOM   19784 C CG  . ASP K  1 103 ? 3.103   3.420    -49.415 1.00 53.63  ? 103 ASP K CG  1 
ATOM   19785 O OD1 . ASP K  1 103 ? 3.049   4.237    -48.473 1.00 53.88  ? 103 ASP K OD1 1 
ATOM   19786 O OD2 . ASP K  1 103 ? 2.542   3.608    -50.514 1.00 49.09  ? 103 ASP K OD2 1 
ATOM   19787 N N   . TYR K  1 104 ? 6.866   1.036    -47.274 1.00 45.46  ? 104 TYR K N   1 
ATOM   19788 C CA  . TYR K  1 104 ? 7.651   -0.149   -46.946 1.00 41.76  ? 104 TYR K CA  1 
ATOM   19789 C C   . TYR K  1 104 ? 6.952   -1.008   -45.901 1.00 44.21  ? 104 TYR K C   1 
ATOM   19790 O O   . TYR K  1 104 ? 6.824   -2.221   -46.067 1.00 37.34  ? 104 TYR K O   1 
ATOM   19791 C CB  . TYR K  1 104 ? 9.042   0.265    -46.456 1.00 39.25  ? 104 TYR K CB  1 
ATOM   19792 C CG  . TYR K  1 104 ? 9.917   -0.880   -46.001 1.00 45.60  ? 104 TYR K CG  1 
ATOM   19793 C CD1 . TYR K  1 104 ? 10.143  -1.975   -46.823 1.00 38.74  ? 104 TYR K CD1 1 
ATOM   19794 C CD2 . TYR K  1 104 ? 10.529  -0.858   -44.755 1.00 34.88  ? 104 TYR K CD2 1 
ATOM   19795 C CE1 . TYR K  1 104 ? 10.945  -3.023   -46.411 1.00 44.92  ? 104 TYR K CE1 1 
ATOM   19796 C CE2 . TYR K  1 104 ? 11.334  -1.900   -44.336 1.00 41.12  ? 104 TYR K CE2 1 
ATOM   19797 C CZ  . TYR K  1 104 ? 11.539  -2.979   -45.168 1.00 40.77  ? 104 TYR K CZ  1 
ATOM   19798 O OH  . TYR K  1 104 ? 12.340  -4.017   -44.753 1.00 47.96  ? 104 TYR K OH  1 
ATOM   19799 N N   . GLU K  1 105 ? 6.496   -0.372   -44.828 1.00 38.04  ? 105 GLU K N   1 
ATOM   19800 C CA  . GLU K  1 105 ? 5.802   -1.078   -43.758 1.00 34.52  ? 105 GLU K CA  1 
ATOM   19801 C C   . GLU K  1 105 ? 4.576   -1.800   -44.302 1.00 41.03  ? 105 GLU K C   1 
ATOM   19802 O O   . GLU K  1 105 ? 4.243   -2.899   -43.859 1.00 42.36  ? 105 GLU K O   1 
ATOM   19803 C CB  . GLU K  1 105 ? 5.396   -0.112   -42.643 1.00 40.15  ? 105 GLU K CB  1 
ATOM   19804 C CG  . GLU K  1 105 ? 6.555   0.667    -42.043 1.00 35.09  ? 105 GLU K CG  1 
ATOM   19805 C CD  . GLU K  1 105 ? 7.085   1.739    -42.978 1.00 64.96  ? 105 GLU K CD  1 
ATOM   19806 O OE1 . GLU K  1 105 ? 6.283   2.302    -43.754 1.00 69.55  ? 105 GLU K OE1 1 
ATOM   19807 O OE2 . GLU K  1 105 ? 8.301   2.019    -42.935 1.00 57.41  ? 105 GLU K OE2 1 
ATOM   19808 N N   . GLU K  1 106 ? 3.906   -1.174   -45.264 1.00 44.93  ? 106 GLU K N   1 
ATOM   19809 C CA  . GLU K  1 106 ? 2.759   -1.789   -45.919 1.00 37.97  ? 106 GLU K CA  1 
ATOM   19810 C C   . GLU K  1 106 ? 3.168   -3.053   -46.667 1.00 35.47  ? 106 GLU K C   1 
ATOM   19811 O O   . GLU K  1 106 ? 2.531   -4.094   -46.530 1.00 37.34  ? 106 GLU K O   1 
ATOM   19812 C CB  . GLU K  1 106 ? 2.082   -0.800   -46.870 1.00 32.59  ? 106 GLU K CB  1 
ATOM   19813 C CG  . GLU K  1 106 ? 1.069   0.107    -46.191 1.00 49.85  ? 106 GLU K CG  1 
ATOM   19814 C CD  . GLU K  1 106 ? -0.172  -0.642   -45.738 1.00 49.09  ? 106 GLU K CD  1 
ATOM   19815 O OE1 . GLU K  1 106 ? -0.616  -1.558   -46.463 1.00 46.00  ? 106 GLU K OE1 1 
ATOM   19816 O OE2 . GLU K  1 106 ? -0.707  -0.309   -44.660 1.00 42.90  ? 106 GLU K OE2 1 
ATOM   19817 N N   . LEU K  1 107 ? 4.236   -2.958   -47.451 1.00 41.99  ? 107 LEU K N   1 
ATOM   19818 C CA  . LEU K  1 107 ? 4.738   -4.105   -48.196 1.00 47.03  ? 107 LEU K CA  1 
ATOM   19819 C C   . LEU K  1 107 ? 5.015   -5.282   -47.268 1.00 39.22  ? 107 LEU K C   1 
ATOM   19820 O O   . LEU K  1 107 ? 4.664   -6.423   -47.572 1.00 38.95  ? 107 LEU K O   1 
ATOM   19821 C CB  . LEU K  1 107 ? 6.010   -3.731   -48.955 1.00 30.84  ? 107 LEU K CB  1 
ATOM   19822 C CG  . LEU K  1 107 ? 6.579   -4.832   -49.852 1.00 32.18  ? 107 LEU K CG  1 
ATOM   19823 C CD1 . LEU K  1 107 ? 5.534   -5.326   -50.848 1.00 38.46  ? 107 LEU K CD1 1 
ATOM   19824 C CD2 . LEU K  1 107 ? 7.834   -4.353   -50.561 1.00 37.82  ? 107 LEU K CD2 1 
ATOM   19825 N N   . ARG K  1 108 ? 5.648   -4.996   -46.134 1.00 30.60  ? 108 ARG K N   1 
ATOM   19826 C CA  . ARG K  1 108 ? 6.003   -6.029   -45.168 1.00 43.91  ? 108 ARG K CA  1 
ATOM   19827 C C   . ARG K  1 108 ? 4.746   -6.684   -44.598 1.00 49.00  ? 108 ARG K C   1 
ATOM   19828 O O   . ARG K  1 108 ? 4.690   -7.899   -44.415 1.00 36.17  ? 108 ARG K O   1 
ATOM   19829 C CB  . ARG K  1 108 ? 6.834   -5.425   -44.036 1.00 35.51  ? 108 ARG K CB  1 
ATOM   19830 C CG  . ARG K  1 108 ? 8.046   -4.622   -44.486 1.00 36.82  ? 108 ARG K CG  1 
ATOM   19831 C CD  . ARG K  1 108 ? 8.608   -3.788   -43.338 1.00 40.81  ? 108 ARG K CD  1 
ATOM   19832 N NE  . ARG K  1 108 ? 8.893   -4.602   -42.158 1.00 51.25  ? 108 ARG K NE  1 
ATOM   19833 C CZ  . ARG K  1 108 ? 10.112  -4.976   -41.778 1.00 47.73  ? 108 ARG K CZ  1 
ATOM   19834 N NH1 . ARG K  1 108 ? 11.176  -4.606   -42.473 1.00 38.93  ? 108 ARG K NH1 1 
ATOM   19835 N NH2 . ARG K  1 108 ? 10.273  -5.720   -40.695 1.00 43.11  ? 108 ARG K NH2 1 
ATOM   19836 N N   . GLU K  1 109 ? 3.737   -5.867   -44.315 1.00 44.54  ? 109 GLU K N   1 
ATOM   19837 C CA  . GLU K  1 109 ? 2.464   -6.367   -43.816 1.00 34.79  ? 109 GLU K CA  1 
ATOM   19838 C C   . GLU K  1 109 ? 1.833   -7.344   -44.798 1.00 39.14  ? 109 GLU K C   1 
ATOM   19839 O O   . GLU K  1 109 ? 1.320   -8.389   -44.401 1.00 45.73  ? 109 GLU K O   1 
ATOM   19840 C CB  . GLU K  1 109 ? 1.511   -5.203   -43.559 1.00 41.45  ? 109 GLU K CB  1 
ATOM   19841 C CG  . GLU K  1 109 ? 1.324   -4.878   -42.094 1.00 59.95  ? 109 GLU K CG  1 
ATOM   19842 C CD  . GLU K  1 109 ? 0.485   -5.911   -41.381 1.00 66.38  ? 109 GLU K CD  1 
ATOM   19843 O OE1 . GLU K  1 109 ? 0.976   -6.504   -40.400 1.00 78.36  ? 109 GLU K OE1 1 
ATOM   19844 O OE2 . GLU K  1 109 ? -0.668  -6.130   -41.803 1.00 70.28  ? 109 GLU K OE2 1 
ATOM   19845 N N   . GLN K  1 110 ? 1.885   -6.998   -46.080 1.00 37.08  ? 110 GLN K N   1 
ATOM   19846 C CA  . GLN K  1 110 ? 1.315   -7.828   -47.135 1.00 45.84  ? 110 GLN K CA  1 
ATOM   19847 C C   . GLN K  1 110 ? 2.116   -9.115   -47.356 1.00 44.60  ? 110 GLN K C   1 
ATOM   19848 O O   . GLN K  1 110 ? 1.551   -10.157  -47.685 1.00 62.88  ? 110 GLN K O   1 
ATOM   19849 C CB  . GLN K  1 110 ? 1.233   -7.032   -48.440 1.00 48.83  ? 110 GLN K CB  1 
ATOM   19850 C CG  . GLN K  1 110 ? 0.773   -5.588   -48.260 1.00 49.76  ? 110 GLN K CG  1 
ATOM   19851 C CD  . GLN K  1 110 ? -0.540  -5.293   -48.957 1.00 61.78  ? 110 GLN K CD  1 
ATOM   19852 O OE1 . GLN K  1 110 ? -1.172  -6.185   -49.524 1.00 67.04  ? 110 GLN K OE1 1 
ATOM   19853 N NE2 . GLN K  1 110 ? -0.959  -4.033   -48.917 1.00 57.54  ? 110 GLN K NE2 1 
ATOM   19854 N N   . LEU K  1 111 ? 3.431   -9.034   -47.175 1.00 51.33  ? 111 LEU K N   1 
ATOM   19855 C CA  . LEU K  1 111 ? 4.308   -10.187  -47.351 1.00 41.83  ? 111 LEU K CA  1 
ATOM   19856 C C   . LEU K  1 111 ? 4.365   -11.070  -46.109 1.00 40.78  ? 111 LEU K C   1 
ATOM   19857 O O   . LEU K  1 111 ? 4.880   -12.185  -46.160 1.00 51.26  ? 111 LEU K O   1 
ATOM   19858 C CB  . LEU K  1 111 ? 5.723   -9.726   -47.704 1.00 39.29  ? 111 LEU K CB  1 
ATOM   19859 C CG  . LEU K  1 111 ? 6.169   -9.834   -49.163 1.00 41.53  ? 111 LEU K CG  1 
ATOM   19860 C CD1 . LEU K  1 111 ? 5.122   -10.534  -50.017 1.00 56.06  ? 111 LEU K CD1 1 
ATOM   19861 C CD2 . LEU K  1 111 ? 6.499   -8.464   -49.721 1.00 40.95  ? 111 LEU K CD2 1 
ATOM   19862 N N   . SER K  1 112 ? 3.836   -10.567  -44.998 1.00 39.04  ? 112 SER K N   1 
ATOM   19863 C CA  . SER K  1 112 ? 3.942   -11.253  -43.711 1.00 41.44  ? 112 SER K CA  1 
ATOM   19864 C C   . SER K  1 112 ? 3.518   -12.718  -43.784 1.00 44.80  ? 112 SER K C   1 
ATOM   19865 O O   . SER K  1 112 ? 4.113   -13.578  -43.136 1.00 50.09  ? 112 SER K O   1 
ATOM   19866 C CB  . SER K  1 112 ? 3.124   -10.523  -42.647 1.00 44.00  ? 112 SER K CB  1 
ATOM   19867 O OG  . SER K  1 112 ? 1.740   -10.629  -42.918 1.00 50.48  ? 112 SER K OG  1 
ATOM   19868 N N   . SER K  1 113 ? 2.483   -12.999  -44.568 1.00 46.06  ? 113 SER K N   1 
ATOM   19869 C CA  . SER K  1 113 ? 2.046   -14.374  -44.779 1.00 41.40  ? 113 SER K CA  1 
ATOM   19870 C C   . SER K  1 113 ? 1.671   -14.599  -46.238 1.00 53.19  ? 113 SER K C   1 
ATOM   19871 O O   . SER K  1 113 ? 0.871   -13.856  -46.808 1.00 57.22  ? 113 SER K O   1 
ATOM   19872 C CB  . SER K  1 113 ? 0.872   -14.720  -43.864 1.00 58.21  ? 113 SER K CB  1 
ATOM   19873 O OG  . SER K  1 113 ? 0.596   -16.110  -43.893 1.00 56.45  ? 113 SER K OG  1 
ATOM   19874 N N   . VAL K  1 114 ? 2.257   -15.631  -46.835 1.00 51.57  ? 114 VAL K N   1 
ATOM   19875 C CA  . VAL K  1 114 ? 2.073   -15.910  -48.252 1.00 59.47  ? 114 VAL K CA  1 
ATOM   19876 C C   . VAL K  1 114 ? 1.677   -17.363  -48.489 1.00 58.22  ? 114 VAL K C   1 
ATOM   19877 O O   . VAL K  1 114 ? 2.255   -18.278  -47.904 1.00 53.20  ? 114 VAL K O   1 
ATOM   19878 C CB  . VAL K  1 114 ? 3.355   -15.589  -49.040 1.00 63.32  ? 114 VAL K CB  1 
ATOM   19879 C CG1 . VAL K  1 114 ? 3.791   -16.789  -49.872 1.00 65.20  ? 114 VAL K CG1 1 
ATOM   19880 C CG2 . VAL K  1 114 ? 3.157   -14.340  -49.900 1.00 53.38  ? 114 VAL K CG2 1 
ATOM   19881 N N   . SER K  1 115 ? 0.682   -17.570  -49.346 1.00 66.67  ? 115 SER K N   1 
ATOM   19882 C CA  . SER K  1 115 ? 0.195   -18.914  -49.630 1.00 76.28  ? 115 SER K CA  1 
ATOM   19883 C C   . SER K  1 115 ? 1.057   -19.594  -50.689 1.00 73.18  ? 115 SER K C   1 
ATOM   19884 O O   . SER K  1 115 ? 1.527   -20.714  -50.494 1.00 83.85  ? 115 SER K O   1 
ATOM   19885 C CB  . SER K  1 115 ? -1.265  -18.876  -50.078 1.00 80.65  ? 115 SER K CB  1 
ATOM   19886 O OG  . SER K  1 115 ? -1.837  -20.171  -50.024 1.00 90.90  ? 115 SER K OG  1 
ATOM   19887 N N   . SER K  1 116 ? 1.251   -18.917  -51.815 1.00 82.33  ? 116 SER K N   1 
ATOM   19888 C CA  . SER K  1 116 ? 2.197   -19.377  -52.824 1.00 89.96  ? 116 SER K CA  1 
ATOM   19889 C C   . SER K  1 116 ? 3.058   -18.203  -53.266 1.00 90.72  ? 116 SER K C   1 
ATOM   19890 O O   . SER K  1 116 ? 2.575   -17.078  -53.382 1.00 89.87  ? 116 SER K O   1 
ATOM   19891 C CB  . SER K  1 116 ? 1.482   -20.005  -54.022 1.00 91.33  ? 116 SER K CB  1 
ATOM   19892 O OG  . SER K  1 116 ? 0.838   -19.022  -54.813 1.00 105.92 ? 116 SER K OG  1 
ATOM   19893 N N   . PHE K  1 117 ? 4.334   -18.472  -53.509 1.00 74.77  ? 117 PHE K N   1 
ATOM   19894 C CA  . PHE K  1 117 ? 5.297   -17.416  -53.776 1.00 60.60  ? 117 PHE K CA  1 
ATOM   19895 C C   . PHE K  1 117 ? 6.385   -17.933  -54.702 1.00 62.51  ? 117 PHE K C   1 
ATOM   19896 O O   . PHE K  1 117 ? 7.274   -18.669  -54.274 1.00 71.06  ? 117 PHE K O   1 
ATOM   19897 C CB  . PHE K  1 117 ? 5.918   -16.948  -52.458 1.00 53.57  ? 117 PHE K CB  1 
ATOM   19898 C CG  . PHE K  1 117 ? 6.681   -15.656  -52.560 1.00 56.56  ? 117 PHE K CG  1 
ATOM   19899 C CD1 . PHE K  1 117 ? 8.025   -15.652  -52.893 1.00 55.35  ? 117 PHE K CD1 1 
ATOM   19900 C CD2 . PHE K  1 117 ? 6.057   -14.447  -52.299 1.00 56.33  ? 117 PHE K CD2 1 
ATOM   19901 C CE1 . PHE K  1 117 ? 8.729   -14.465  -52.977 1.00 42.48  ? 117 PHE K CE1 1 
ATOM   19902 C CE2 . PHE K  1 117 ? 6.755   -13.257  -52.382 1.00 61.13  ? 117 PHE K CE2 1 
ATOM   19903 C CZ  . PHE K  1 117 ? 8.093   -13.266  -52.721 1.00 46.64  ? 117 PHE K CZ  1 
ATOM   19904 N N   . GLU K  1 118 ? 6.307   -17.561  -55.976 1.00 64.92  ? 118 GLU K N   1 
ATOM   19905 C CA  . GLU K  1 118 ? 7.346   -17.931  -56.927 1.00 69.19  ? 118 GLU K CA  1 
ATOM   19906 C C   . GLU K  1 118 ? 7.945   -16.696  -57.584 1.00 60.39  ? 118 GLU K C   1 
ATOM   19907 O O   . GLU K  1 118 ? 7.233   -15.754  -57.938 1.00 62.96  ? 118 GLU K O   1 
ATOM   19908 C CB  . GLU K  1 118 ? 6.812   -18.891  -57.992 1.00 82.04  ? 118 GLU K CB  1 
ATOM   19909 C CG  . GLU K  1 118 ? 6.076   -18.213  -59.130 1.00 93.45  ? 118 GLU K CG  1 
ATOM   19910 C CD  . GLU K  1 118 ? 6.137   -19.011  -60.416 1.00 114.07 ? 118 GLU K CD  1 
ATOM   19911 O OE1 . GLU K  1 118 ? 6.703   -20.124  -60.399 1.00 121.83 ? 118 GLU K OE1 1 
ATOM   19912 O OE2 . GLU K  1 118 ? 5.623   -18.524  -61.445 1.00 111.32 ? 118 GLU K OE2 1 
ATOM   19913 N N   . ARG K  1 119 ? 9.264   -16.708  -57.737 1.00 62.40  ? 119 ARG K N   1 
ATOM   19914 C CA  . ARG K  1 119 ? 9.979   -15.593  -58.337 1.00 59.53  ? 119 ARG K CA  1 
ATOM   19915 C C   . ARG K  1 119 ? 10.379  -15.921  -59.770 1.00 57.37  ? 119 ARG K C   1 
ATOM   19916 O O   . ARG K  1 119 ? 11.145  -16.856  -60.009 1.00 74.86  ? 119 ARG K O   1 
ATOM   19917 C CB  . ARG K  1 119 ? 11.207  -15.253  -57.493 1.00 57.04  ? 119 ARG K CB  1 
ATOM   19918 C CG  . ARG K  1 119 ? 12.317  -14.541  -58.236 1.00 57.92  ? 119 ARG K CG  1 
ATOM   19919 C CD  . ARG K  1 119 ? 13.599  -15.363  -58.216 1.00 67.48  ? 119 ARG K CD  1 
ATOM   19920 N NE  . ARG K  1 119 ? 14.771  -14.526  -57.978 1.00 73.29  ? 119 ARG K NE  1 
ATOM   19921 C CZ  . ARG K  1 119 ? 16.003  -14.822  -58.380 1.00 91.07  ? 119 ARG K CZ  1 
ATOM   19922 N NH1 . ARG K  1 119 ? 16.238  -15.938  -59.055 1.00 99.17  ? 119 ARG K NH1 1 
ATOM   19923 N NH2 . ARG K  1 119 ? 17.000  -13.993  -58.113 1.00 83.42  ? 119 ARG K NH2 1 
ATOM   19924 N N   . PHE K  1 120 ? 9.845   -15.157  -60.719 1.00 60.66  ? 120 PHE K N   1 
ATOM   19925 C CA  . PHE K  1 120 ? 10.115  -15.383  -62.132 1.00 63.13  ? 120 PHE K CA  1 
ATOM   19926 C C   . PHE K  1 120 ? 10.721  -14.139  -62.766 1.00 57.46  ? 120 PHE K C   1 
ATOM   19927 O O   . PHE K  1 120 ? 10.509  -13.023  -62.292 1.00 60.80  ? 120 PHE K O   1 
ATOM   19928 C CB  . PHE K  1 120 ? 8.826   -15.756  -62.865 1.00 61.24  ? 120 PHE K CB  1 
ATOM   19929 C CG  . PHE K  1 120 ? 7.813   -14.646  -62.911 1.00 56.21  ? 120 PHE K CG  1 
ATOM   19930 C CD1 . PHE K  1 120 ? 7.699   -13.840  -64.032 1.00 69.53  ? 120 PHE K CD1 1 
ATOM   19931 C CD2 . PHE K  1 120 ? 6.977   -14.407  -61.833 1.00 66.92  ? 120 PHE K CD2 1 
ATOM   19932 C CE1 . PHE K  1 120 ? 6.770   -12.818  -64.078 1.00 67.72  ? 120 PHE K CE1 1 
ATOM   19933 C CE2 . PHE K  1 120 ? 6.045   -13.385  -61.872 1.00 63.91  ? 120 PHE K CE2 1 
ATOM   19934 C CZ  . PHE K  1 120 ? 5.942   -12.590  -62.997 1.00 67.95  ? 120 PHE K CZ  1 
ATOM   19935 N N   . GLU K  1 121 ? 11.472  -14.336  -63.843 1.00 62.31  ? 121 GLU K N   1 
ATOM   19936 C CA  . GLU K  1 121 ? 12.065  -13.221  -64.565 1.00 64.65  ? 121 GLU K CA  1 
ATOM   19937 C C   . GLU K  1 121 ? 11.003  -12.554  -65.430 1.00 62.23  ? 121 GLU K C   1 
ATOM   19938 O O   . GLU K  1 121 ? 10.586  -13.101  -66.451 1.00 74.43  ? 121 GLU K O   1 
ATOM   19939 C CB  . GLU K  1 121 ? 13.233  -13.705  -65.426 1.00 72.22  ? 121 GLU K CB  1 
ATOM   19940 C CG  . GLU K  1 121 ? 14.179  -12.605  -65.869 1.00 80.89  ? 121 GLU K CG  1 
ATOM   19941 C CD  . GLU K  1 121 ? 15.407  -13.147  -66.570 1.00 90.36  ? 121 GLU K CD  1 
ATOM   19942 O OE1 . GLU K  1 121 ? 15.367  -14.308  -67.027 1.00 103.23 ? 121 GLU K OE1 1 
ATOM   19943 O OE2 . GLU K  1 121 ? 16.413  -12.413  -66.663 1.00 92.30  ? 121 GLU K OE2 1 
ATOM   19944 N N   . ILE K  1 122 ? 10.556  -11.377  -65.004 1.00 63.13  ? 122 ILE K N   1 
ATOM   19945 C CA  . ILE K  1 122 ? 9.530   -10.638  -65.729 1.00 64.82  ? 122 ILE K CA  1 
ATOM   19946 C C   . ILE K  1 122 ? 10.109  -9.968   -66.973 1.00 75.46  ? 122 ILE K C   1 
ATOM   19947 O O   . ILE K  1 122 ? 9.483   -9.957   -68.033 1.00 71.66  ? 122 ILE K O   1 
ATOM   19948 C CB  . ILE K  1 122 ? 8.850   -9.588   -64.828 1.00 61.48  ? 122 ILE K CB  1 
ATOM   19949 C CG1 . ILE K  1 122 ? 7.842   -8.762   -65.629 1.00 55.63  ? 122 ILE K CG1 1 
ATOM   19950 C CG2 . ILE K  1 122 ? 9.888   -8.687   -64.175 1.00 67.94  ? 122 ILE K CG2 1 
ATOM   19951 C CD1 . ILE K  1 122 ? 7.112   -7.728   -64.801 1.00 52.83  ? 122 ILE K CD1 1 
ATOM   19952 N N   . PHE K  1 123 ? 11.310  -9.414   -66.839 1.00 78.06  ? 123 PHE K N   1 
ATOM   19953 C CA  . PHE K  1 123 ? 12.015  -8.833   -67.974 1.00 65.60  ? 123 PHE K CA  1 
ATOM   19954 C C   . PHE K  1 123 ? 13.422  -9.411   -68.083 1.00 77.65  ? 123 PHE K C   1 
ATOM   19955 O O   . PHE K  1 123 ? 14.343  -8.930   -67.424 1.00 77.62  ? 123 PHE K O   1 
ATOM   19956 C CB  . PHE K  1 123 ? 12.091  -7.308   -67.851 1.00 71.88  ? 123 PHE K CB  1 
ATOM   19957 C CG  . PHE K  1 123 ? 10.752  -6.628   -67.876 1.00 72.13  ? 123 PHE K CG  1 
ATOM   19958 C CD1 . PHE K  1 123 ? 10.345  -5.832   -66.819 1.00 67.73  ? 123 PHE K CD1 1 
ATOM   19959 C CD2 . PHE K  1 123 ? 9.900   -6.786   -68.956 1.00 74.36  ? 123 PHE K CD2 1 
ATOM   19960 C CE1 . PHE K  1 123 ? 9.115   -5.204   -66.839 1.00 63.36  ? 123 PHE K CE1 1 
ATOM   19961 C CE2 . PHE K  1 123 ? 8.668   -6.161   -68.982 1.00 67.93  ? 123 PHE K CE2 1 
ATOM   19962 C CZ  . PHE K  1 123 ? 8.275   -5.369   -67.922 1.00 64.24  ? 123 PHE K CZ  1 
ATOM   19963 N N   . PRO K  1 124 ? 13.592  -10.450  -68.916 1.00 88.99  ? 124 PRO K N   1 
ATOM   19964 C CA  . PRO K  1 124 ? 14.909  -11.059  -69.143 1.00 93.18  ? 124 PRO K CA  1 
ATOM   19965 C C   . PRO K  1 124 ? 15.941  -10.016  -69.568 1.00 95.00  ? 124 PRO K C   1 
ATOM   19966 O O   . PRO K  1 124 ? 15.645  -9.207   -70.444 1.00 95.09  ? 124 PRO K O   1 
ATOM   19967 C CB  . PRO K  1 124 ? 14.647  -12.032  -70.295 1.00 97.63  ? 124 PRO K CB  1 
ATOM   19968 C CG  . PRO K  1 124 ? 13.197  -12.357  -70.192 1.00 90.53  ? 124 PRO K CG  1 
ATOM   19969 C CD  . PRO K  1 124 ? 12.532  -11.108  -69.699 1.00 87.14  ? 124 PRO K CD  1 
ATOM   19970 N N   . LYS K  1 125 ? 17.127  -10.046  -68.967 1.00 88.76  ? 125 LYS K N   1 
ATOM   19971 C CA  . LYS K  1 125 ? 18.138  -9.017   -69.191 1.00 97.30  ? 125 LYS K CA  1 
ATOM   19972 C C   . LYS K  1 125 ? 18.595  -8.910   -70.640 1.00 109.45 ? 125 LYS K C   1 
ATOM   19973 O O   . LYS K  1 125 ? 18.936  -7.822   -71.110 1.00 107.96 ? 125 LYS K O   1 
ATOM   19974 C CB  . LYS K  1 125 ? 19.354  -9.258   -68.293 1.00 96.77  ? 125 LYS K CB  1 
ATOM   19975 C CG  . LYS K  1 125 ? 20.418  -8.185   -68.407 1.00 97.56  ? 125 LYS K CG  1 
ATOM   19976 C CD  . LYS K  1 125 ? 21.405  -8.231   -67.255 1.00 90.32  ? 125 LYS K CD  1 
ATOM   19977 C CE  . LYS K  1 125 ? 22.262  -9.484   -67.288 1.00 96.28  ? 125 LYS K CE  1 
ATOM   19978 N NZ  . LYS K  1 125 ? 23.288  -9.476   -66.205 1.00 102.33 ? 125 LYS K NZ  1 
ATOM   19979 N N   . THR K  1 126 ? 18.597  -10.027  -71.357 1.00 154.19 ? 126 THR K N   1 
ATOM   19980 C CA  . THR K  1 126 ? 19.264  -10.079  -72.658 1.00 159.44 ? 126 THR K CA  1 
ATOM   19981 C C   . THR K  1 126 ? 18.368  -9.946   -73.894 1.00 164.73 ? 126 THR K C   1 
ATOM   19982 O O   . THR K  1 126 ? 18.841  -10.137  -75.013 1.00 180.83 ? 126 THR K O   1 
ATOM   19983 C CB  . THR K  1 126 ? 20.028  -11.419  -72.809 1.00 123.97 ? 126 THR K CB  1 
ATOM   19984 O OG1 . THR K  1 126 ? 19.291  -12.467  -72.157 1.00 133.95 ? 126 THR K OG1 1 
ATOM   19985 N N   . SER K  1 127 ? 17.093  -9.627   -73.703 1.00 115.70 ? 127 SER K N   1 
ATOM   19986 C CA  . SER K  1 127 ? 16.187  -9.495   -74.829 1.00 101.15 ? 127 SER K CA  1 
ATOM   19987 C C   . SER K  1 127 ? 15.254  -8.287   -74.670 1.00 90.49  ? 127 SER K C   1 
ATOM   19988 O O   . SER K  1 127 ? 14.626  -7.838   -75.629 1.00 106.60 ? 127 SER K O   1 
ATOM   19989 C CB  . SER K  1 127 ? 15.398  -10.789  -75.014 1.00 106.51 ? 127 SER K CB  1 
ATOM   19990 O OG  . SER K  1 127 ? 14.692  -11.119  -73.830 1.00 98.59  ? 127 SER K OG  1 
ATOM   19991 N N   . SER K  1 128 ? 15.214  -7.727   -73.466 1.00 92.19  ? 128 SER K N   1 
ATOM   19992 C CA  . SER K  1 128 ? 14.265  -6.670   -73.141 1.00 87.36  ? 128 SER K CA  1 
ATOM   19993 C C   . SER K  1 128 ? 14.861  -5.286   -73.356 1.00 86.36  ? 128 SER K C   1 
ATOM   19994 O O   . SER K  1 128 ? 14.143  -4.319   -73.624 1.00 90.13  ? 128 SER K O   1 
ATOM   19995 C CB  . SER K  1 128 ? 13.793  -6.825   -71.695 1.00 85.51  ? 128 SER K CB  1 
ATOM   19996 O OG  . SER K  1 128 ? 13.292  -8.133   -71.475 1.00 83.93  ? 128 SER K OG  1 
ATOM   19997 N N   . TRP K  1 129 ? 16.181  -5.202   -73.253 1.00 90.32  ? 129 TRP K N   1 
ATOM   19998 C CA  . TRP K  1 129 ? 16.864  -3.919   -73.333 1.00 94.12  ? 129 TRP K CA  1 
ATOM   19999 C C   . TRP K  1 129 ? 17.973  -3.927   -74.382 1.00 103.32 ? 129 TRP K C   1 
ATOM   20000 O O   . TRP K  1 129 ? 19.153  -4.041   -74.049 1.00 92.17  ? 129 TRP K O   1 
ATOM   20001 C CB  . TRP K  1 129 ? 17.409  -3.540   -71.957 1.00 96.61  ? 129 TRP K CB  1 
ATOM   20002 C CG  . TRP K  1 129 ? 16.480  -3.939   -70.851 1.00 80.21  ? 129 TRP K CG  1 
ATOM   20003 C CD1 . TRP K  1 129 ? 16.700  -4.890   -69.898 1.00 79.90  ? 129 TRP K CD1 1 
ATOM   20004 C CD2 . TRP K  1 129 ? 15.168  -3.421   -70.605 1.00 81.14  ? 129 TRP K CD2 1 
ATOM   20005 N NE1 . TRP K  1 129 ? 15.612  -4.985   -69.063 1.00 86.02  ? 129 TRP K NE1 1 
ATOM   20006 C CE2 . TRP K  1 129 ? 14.657  -4.094   -69.477 1.00 80.97  ? 129 TRP K CE2 1 
ATOM   20007 C CE3 . TRP K  1 129 ? 14.377  -2.448   -71.224 1.00 78.60  ? 129 TRP K CE3 1 
ATOM   20008 C CZ2 . TRP K  1 129 ? 13.393  -3.825   -68.956 1.00 84.50  ? 129 TRP K CZ2 1 
ATOM   20009 C CZ3 . TRP K  1 129 ? 13.123  -2.183   -70.706 1.00 67.94  ? 129 TRP K CZ3 1 
ATOM   20010 C CH2 . TRP K  1 129 ? 12.644  -2.868   -69.583 1.00 73.48  ? 129 TRP K CH2 1 
ATOM   20011 N N   . PRO K  1 130 ? 17.585  -3.800   -75.660 1.00 112.06 ? 130 PRO K N   1 
ATOM   20012 C CA  . PRO K  1 130 ? 18.480  -3.834   -76.820 1.00 102.73 ? 130 PRO K CA  1 
ATOM   20013 C C   . PRO K  1 130 ? 19.019  -2.453   -77.171 1.00 111.04 ? 130 PRO K C   1 
ATOM   20014 O O   . PRO K  1 130 ? 19.948  -2.344   -77.971 1.00 121.84 ? 130 PRO K O   1 
ATOM   20015 C CB  . PRO K  1 130 ? 17.562  -4.319   -77.955 1.00 108.74 ? 130 PRO K CB  1 
ATOM   20016 C CG  . PRO K  1 130 ? 16.201  -4.574   -77.319 1.00 101.44 ? 130 PRO K CG  1 
ATOM   20017 C CD  . PRO K  1 130 ? 16.178  -3.755   -76.078 1.00 108.38 ? 130 PRO K CD  1 
ATOM   20018 N N   . ASN K  1 131 ? 18.430  -1.413   -76.591 1.00 103.01 ? 131 ASN K N   1 
ATOM   20019 C CA  . ASN K  1 131 ? 18.843  -0.043   -76.872 1.00 110.33 ? 131 ASN K CA  1 
ATOM   20020 C C   . ASN K  1 131 ? 19.503  0.612    -75.666 1.00 102.08 ? 131 ASN K C   1 
ATOM   20021 O O   . ASN K  1 131 ? 19.812  1.804    -75.684 1.00 103.63 ? 131 ASN K O   1 
ATOM   20022 C CB  . ASN K  1 131 ? 17.646  0.793    -77.330 1.00 116.37 ? 131 ASN K CB  1 
ATOM   20023 C CG  . ASN K  1 131 ? 17.054  0.296    -78.634 1.00 126.05 ? 131 ASN K CG  1 
ATOM   20024 O OD1 . ASN K  1 131 ? 17.706  -0.423   -79.391 1.00 129.63 ? 131 ASN K OD1 1 
ATOM   20025 N ND2 . ASN K  1 131 ? 15.812  0.681    -78.905 1.00 129.82 ? 131 ASN K ND2 1 
ATOM   20026 N N   . HIS K  1 132 ? 19.717  -0.176   -74.619 1.00 90.46  ? 132 HIS K N   1 
ATOM   20027 C CA  . HIS K  1 132 ? 20.311  0.327    -73.388 1.00 81.71  ? 132 HIS K CA  1 
ATOM   20028 C C   . HIS K  1 132 ? 21.298  -0.685   -72.823 1.00 82.39  ? 132 HIS K C   1 
ATOM   20029 O O   . HIS K  1 132 ? 21.194  -1.882   -73.091 1.00 91.11  ? 132 HIS K O   1 
ATOM   20030 C CB  . HIS K  1 132 ? 19.220  0.622    -72.359 1.00 75.04  ? 132 HIS K CB  1 
ATOM   20031 C CG  . HIS K  1 132 ? 18.086  1.434    -72.899 1.00 83.29  ? 132 HIS K CG  1 
ATOM   20032 N ND1 . HIS K  1 132 ? 17.957  2.788    -72.662 1.00 82.15  ? 132 HIS K ND1 1 
ATOM   20033 C CD2 . HIS K  1 132 ? 17.028  1.088    -73.671 1.00 72.70  ? 132 HIS K CD2 1 
ATOM   20034 C CE1 . HIS K  1 132 ? 16.870  3.235    -73.260 1.00 75.81  ? 132 HIS K CE1 1 
ATOM   20035 N NE2 . HIS K  1 132 ? 16.287  2.226    -73.880 1.00 63.31  ? 132 HIS K NE2 1 
ATOM   20036 N N   . ASP K  1 133 ? 22.257  -0.201   -72.041 1.00 67.05  ? 133 ASP K N   1 
ATOM   20037 C CA  . ASP K  1 133 ? 23.248  -1.077   -71.429 1.00 85.29  ? 133 ASP K CA  1 
ATOM   20038 C C   . ASP K  1 133 ? 22.713  -1.659   -70.124 1.00 82.13  ? 133 ASP K C   1 
ATOM   20039 O O   . ASP K  1 133 ? 22.388  -0.925   -69.191 1.00 75.59  ? 133 ASP K O   1 
ATOM   20040 C CB  . ASP K  1 133 ? 24.557  -0.323   -71.184 1.00 86.54  ? 133 ASP K CB  1 
ATOM   20041 C CG  . ASP K  1 133 ? 25.713  -1.250   -70.859 1.00 97.77  ? 133 ASP K CG  1 
ATOM   20042 O OD1 . ASP K  1 133 ? 25.526  -2.182   -70.050 1.00 92.33  ? 133 ASP K OD1 1 
ATOM   20043 O OD2 . ASP K  1 133 ? 26.813  -1.043   -71.413 1.00 118.12 ? 133 ASP K OD2 1 
ATOM   20044 N N   . SER K  1 134 ? 22.621  -2.983   -70.070 1.00 79.91  ? 134 SER K N   1 
ATOM   20045 C CA  . SER K  1 134 ? 22.100  -3.668   -68.895 1.00 82.20  ? 134 SER K CA  1 
ATOM   20046 C C   . SER K  1 134 ? 23.210  -4.396   -68.143 1.00 76.46  ? 134 SER K C   1 
ATOM   20047 O O   . SER K  1 134 ? 22.969  -5.416   -67.497 1.00 87.70  ? 134 SER K O   1 
ATOM   20048 C CB  . SER K  1 134 ? 21.002  -4.653   -69.301 1.00 82.66  ? 134 SER K CB  1 
ATOM   20049 O OG  . SER K  1 134 ? 21.456  -5.527   -70.320 1.00 91.51  ? 134 SER K OG  1 
ATOM   20050 N N   . ASN K  1 135 ? 24.423  -3.860   -68.223 1.00 82.35  ? 135 ASN K N   1 
ATOM   20051 C CA  . ASN K  1 135 ? 25.583  -4.494   -67.607 1.00 85.43  ? 135 ASN K CA  1 
ATOM   20052 C C   . ASN K  1 135 ? 26.409  -3.548   -66.733 1.00 88.37  ? 135 ASN K C   1 
ATOM   20053 O O   . ASN K  1 135 ? 27.087  -3.986   -65.803 1.00 106.36 ? 135 ASN K O   1 
ATOM   20054 C CB  . ASN K  1 135 ? 26.474  -5.126   -68.682 1.00 95.53  ? 135 ASN K CB  1 
ATOM   20055 C CG  . ASN K  1 135 ? 25.787  -6.262   -69.418 1.00 97.60  ? 135 ASN K CG  1 
ATOM   20056 O OD1 . ASN K  1 135 ? 25.174  -7.135   -68.802 1.00 82.04  ? 135 ASN K OD1 1 
ATOM   20057 N ND2 . ASN K  1 135 ? 25.892  -6.260   -70.743 1.00 93.99  ? 135 ASN K ND2 1 
ATOM   20058 N N   . LYS K  1 136 ? 26.346  -2.253   -67.031 1.00 81.47  ? 136 LYS K N   1 
ATOM   20059 C CA  . LYS K  1 136 ? 27.184  -1.264   -66.354 1.00 95.53  ? 136 LYS K CA  1 
ATOM   20060 C C   . LYS K  1 136 ? 26.552  -0.739   -65.074 1.00 93.48  ? 136 LYS K C   1 
ATOM   20061 O O   . LYS K  1 136 ? 27.095  0.154    -64.424 1.00 94.74  ? 136 LYS K O   1 
ATOM   20062 C CB  . LYS K  1 136 ? 27.485  -0.092   -67.289 1.00 110.64 ? 136 LYS K CB  1 
ATOM   20063 C CG  . LYS K  1 136 ? 28.191  -0.499   -68.563 1.00 110.80 ? 136 LYS K CG  1 
ATOM   20064 C CD  . LYS K  1 136 ? 29.449  0.314    -68.783 1.00 120.40 ? 136 LYS K CD  1 
ATOM   20065 C CE  . LYS K  1 136 ? 30.403  -0.435   -69.690 1.00 142.73 ? 136 LYS K CE  1 
ATOM   20066 N NZ  . LYS K  1 136 ? 30.705  -1.791   -69.147 1.00 137.88 ? 136 LYS K NZ  1 
ATOM   20067 N N   . GLY K  1 137 ? 25.403  -1.301   -64.716 1.00 87.54  ? 137 GLY K N   1 
ATOM   20068 C CA  . GLY K  1 137 ? 24.640  -0.828   -63.576 1.00 79.63  ? 137 GLY K CA  1 
ATOM   20069 C C   . GLY K  1 137 ? 25.040  -1.459   -62.258 1.00 78.65  ? 137 GLY K C   1 
ATOM   20070 O O   . GLY K  1 137 ? 24.280  -2.228   -61.670 1.00 73.11  ? 137 GLY K O   1 
ATOM   20071 N N   . VAL K  1 138 ? 26.236  -1.126   -61.789 1.00 79.20  ? 138 VAL K N   1 
ATOM   20072 C CA  . VAL K  1 138 ? 26.726  -1.630   -60.515 1.00 75.79  ? 138 VAL K CA  1 
ATOM   20073 C C   . VAL K  1 138 ? 27.217  -0.461   -59.679 1.00 77.53  ? 138 VAL K C   1 
ATOM   20074 O O   . VAL K  1 138 ? 27.303  0.664    -60.168 1.00 76.83  ? 138 VAL K O   1 
ATOM   20075 C CB  . VAL K  1 138 ? 27.866  -2.637   -60.713 1.00 84.82  ? 138 VAL K CB  1 
ATOM   20076 C CG1 . VAL K  1 138 ? 27.382  -3.814   -61.545 1.00 80.89  ? 138 VAL K CG1 1 
ATOM   20077 C CG2 . VAL K  1 138 ? 29.056  -1.963   -61.380 1.00 81.06  ? 138 VAL K CG2 1 
ATOM   20078 N N   . THR K  1 139 ? 27.539  -0.719   -58.419 1.00 67.02  ? 139 THR K N   1 
ATOM   20079 C CA  . THR K  1 139 ? 27.950  0.356    -57.527 1.00 75.72  ? 139 THR K CA  1 
ATOM   20080 C C   . THR K  1 139 ? 28.747  -0.161   -56.342 1.00 86.47  ? 139 THR K C   1 
ATOM   20081 O O   . THR K  1 139 ? 28.616  -1.323   -55.951 1.00 78.88  ? 139 THR K O   1 
ATOM   20082 C CB  . THR K  1 139 ? 26.735  1.147    -57.006 1.00 78.74  ? 139 THR K CB  1 
ATOM   20083 O OG1 . THR K  1 139 ? 27.156  2.044    -55.971 1.00 74.20  ? 139 THR K OG1 1 
ATOM   20084 C CG2 . THR K  1 139 ? 25.683  0.198    -56.450 1.00 78.02  ? 139 THR K CG2 1 
ATOM   20085 N N   . ALA K  1 140 ? 29.573  0.709    -55.770 1.00 105.17 ? 140 ALA K N   1 
ATOM   20086 C CA  . ALA K  1 140 ? 30.326  0.356    -54.578 1.00 98.66  ? 140 ALA K CA  1 
ATOM   20087 C C   . ALA K  1 140 ? 29.467  0.480    -53.332 1.00 109.57 ? 140 ALA K C   1 
ATOM   20088 O O   . ALA K  1 140 ? 29.991  0.518    -52.223 1.00 107.49 ? 140 ALA K O   1 
ATOM   20089 C CB  . ALA K  1 140 ? 31.557  1.225    -54.459 1.00 102.39 ? 140 ALA K CB  1 
ATOM   20090 N N   . ALA K  1 141 ? 28.153  0.577    -53.528 1.00 111.92 ? 141 ALA K N   1 
ATOM   20091 C CA  . ALA K  1 141 ? 27.188  0.576    -52.430 1.00 104.45 ? 141 ALA K CA  1 
ATOM   20092 C C   . ALA K  1 141 ? 27.026  -0.838   -51.891 1.00 94.42  ? 141 ALA K C   1 
ATOM   20093 O O   . ALA K  1 141 ? 27.533  -1.172   -50.825 1.00 96.95  ? 141 ALA K O   1 
ATOM   20094 C CB  . ALA K  1 141 ? 25.839  1.118    -52.902 1.00 100.12 ? 141 ALA K CB  1 
ATOM   20095 N N   . CYS K  1 142 ? 26.319  -1.668   -52.648 1.00 74.26  ? 142 CYS K N   1 
ATOM   20096 C CA  . CYS K  1 142 ? 26.182  -3.081   -52.317 1.00 88.63  ? 142 CYS K CA  1 
ATOM   20097 C C   . CYS K  1 142 ? 27.185  -3.923   -53.100 1.00 87.18  ? 142 CYS K C   1 
ATOM   20098 O O   . CYS K  1 142 ? 26.872  -4.409   -54.189 1.00 70.83  ? 142 CYS K O   1 
ATOM   20099 C CB  . CYS K  1 142 ? 24.757  -3.559   -52.609 1.00 105.90 ? 142 CYS K CB  1 
ATOM   20100 S SG  . CYS K  1 142 ? 23.853  -2.534   -53.804 1.00 82.18  ? 142 CYS K SG  1 
ATOM   20101 N N   . PRO K  1 143 ? 28.391  -4.119   -52.534 1.00 96.29  ? 143 PRO K N   1 
ATOM   20102 C CA  . PRO K  1 143 ? 29.450  -4.920   -53.151 1.00 96.46  ? 143 PRO K CA  1 
ATOM   20103 C C   . PRO K  1 143 ? 29.380  -6.396   -52.768 1.00 113.48 ? 143 PRO K C   1 
ATOM   20104 O O   . PRO K  1 143 ? 29.218  -6.704   -51.576 1.00 119.37 ? 143 PRO K O   1 
ATOM   20105 C CB  . PRO K  1 143 ? 30.731  -4.349   -52.529 1.00 102.16 ? 143 PRO K CB  1 
ATOM   20106 C CG  . PRO K  1 143 ? 30.263  -3.429   -51.374 1.00 96.47  ? 143 PRO K CG  1 
ATOM   20107 C CD  . PRO K  1 143 ? 28.786  -3.722   -51.180 1.00 95.82  ? 143 PRO K CD  1 
ATOM   20108 N N   . HIS K  1 144 ? 29.572  -7.244   -53.795 1.00 111.43 ? 144 HIS K N   1 
ATOM   20109 C CA  . HIS K  1 144 ? 29.545  -8.722   -53.817 1.00 121.07 ? 144 HIS K CA  1 
ATOM   20110 C C   . HIS K  1 144 ? 30.851  -9.199   -54.470 1.00 130.26 ? 144 HIS K C   1 
ATOM   20111 O O   . HIS K  1 144 ? 31.231  -8.897   -55.614 1.00 124.36 ? 144 HIS K O   1 
ATOM   20112 C CB  . HIS K  1 144 ? 28.186  -9.109   -54.487 1.00 108.60 ? 144 HIS K CB  1 
ATOM   20113 C CG  . HIS K  1 144 ? 27.937  -10.558  -54.812 1.00 119.20 ? 144 HIS K CG  1 
ATOM   20114 N ND1 . HIS K  1 144 ? 28.369  -11.134  -55.989 1.00 125.31 ? 144 HIS K ND1 1 
ATOM   20115 C CD2 . HIS K  1 144 ? 27.153  -11.497  -54.210 1.00 121.15 ? 144 HIS K CD2 1 
ATOM   20116 C CE1 . HIS K  1 144 ? 27.952  -12.388  -56.052 1.00 128.12 ? 144 HIS K CE1 1 
ATOM   20117 N NE2 . HIS K  1 144 ? 27.214  -12.635  -54.986 1.00 118.62 ? 144 HIS K NE2 1 
ATOM   20118 N N   . ALA K  1 145 ? 31.543  -10.014  -53.681 1.00 127.81 ? 145 ALA K N   1 
ATOM   20119 C CA  . ALA K  1 145 ? 32.829  -10.554  -54.059 1.00 125.96 ? 145 ALA K CA  1 
ATOM   20120 C C   . ALA K  1 145 ? 33.832  -9.431   -54.249 1.00 136.68 ? 145 ALA K C   1 
ATOM   20121 O O   . ALA K  1 145 ? 34.668  -9.484   -55.136 1.00 131.10 ? 145 ALA K O   1 
ATOM   20122 C CB  . ALA K  1 145 ? 32.688  -11.331  -55.308 1.00 115.86 ? 145 ALA K CB  1 
ATOM   20123 N N   . GLY K  1 146 ? 33.751  -8.410   -53.412 1.00 155.10 ? 146 GLY K N   1 
ATOM   20124 C CA  . GLY K  1 146 ? 34.602  -7.252   -53.574 1.00 151.04 ? 146 GLY K CA  1 
ATOM   20125 C C   . GLY K  1 146 ? 34.391  -6.696   -54.954 1.00 149.89 ? 146 GLY K C   1 
ATOM   20126 O O   . GLY K  1 146 ? 35.074  -5.775   -55.383 1.00 143.95 ? 146 GLY K O   1 
ATOM   20127 N N   . ALA K  1 147 ? 33.413  -7.279   -55.637 1.00 134.60 ? 147 ALA K N   1 
ATOM   20128 C CA  . ALA K  1 147 ? 32.997  -6.857   -56.960 1.00 127.63 ? 147 ALA K CA  1 
ATOM   20129 C C   . ALA K  1 147 ? 31.833  -5.901   -56.871 1.00 118.86 ? 147 ALA K C   1 
ATOM   20130 O O   . ALA K  1 147 ? 30.868  -6.177   -56.188 1.00 110.80 ? 147 ALA K O   1 
ATOM   20131 C CB  . ALA K  1 147 ? 32.602  -8.053   -57.763 1.00 118.34 ? 147 ALA K CB  1 
ATOM   20132 N N   . LYS K  1 148 ? 31.945  -4.779   -57.573 1.00 105.44 ? 148 LYS K N   1 
ATOM   20133 C CA  . LYS K  1 148 ? 30.872  -3.801   -57.742 1.00 98.20  ? 148 LYS K CA  1 
ATOM   20134 C C   . LYS K  1 148 ? 29.622  -4.544   -58.185 1.00 96.68  ? 148 LYS K C   1 
ATOM   20135 O O   . LYS K  1 148 ? 29.587  -5.099   -59.282 1.00 80.01  ? 148 LYS K O   1 
ATOM   20136 C CB  . LYS K  1 148 ? 31.246  -2.780   -58.825 1.00 89.21  ? 148 LYS K CB  1 
ATOM   20137 C CG  . LYS K  1 148 ? 32.589  -2.072   -58.648 1.00 110.44 ? 148 LYS K CG  1 
ATOM   20138 C CD  . LYS K  1 148 ? 32.426  -0.550   -58.622 1.00 103.98 ? 148 LYS K CD  1 
ATOM   20139 C CE  . LYS K  1 148 ? 31.589  -0.042   -59.787 1.00 104.75 ? 148 LYS K CE  1 
ATOM   20140 N NZ  . LYS K  1 148 ? 31.215  1.396    -59.630 1.00 111.01 ? 148 LYS K NZ  1 
ATOM   20141 N N   . SER K  1 149 ? 28.598  -4.564   -57.341 1.00 99.68  ? 149 SER K N   1 
ATOM   20142 C CA  . SER K  1 149 ? 27.381  -5.287   -57.683 1.00 92.06  ? 149 SER K CA  1 
ATOM   20143 C C   . SER K  1 149 ? 26.136  -4.424   -57.546 1.00 92.10  ? 149 SER K C   1 
ATOM   20144 O O   . SER K  1 149 ? 26.210  -3.195   -57.486 1.00 85.98  ? 149 SER K O   1 
ATOM   20145 C CB  . SER K  1 149 ? 27.237  -6.549   -56.829 1.00 98.71  ? 149 SER K CB  1 
ATOM   20146 O OG  . SER K  1 149 ? 26.416  -7.509   -57.473 1.00 103.68 ? 149 SER K OG  1 
ATOM   20147 N N   . PHE K  1 150 ? 24.992  -5.093   -57.485 1.00 90.36  ? 150 PHE K N   1 
ATOM   20148 C CA  . PHE K  1 150 ? 23.706  -4.428   -57.427 1.00 73.78  ? 150 PHE K CA  1 
ATOM   20149 C C   . PHE K  1 150 ? 22.646  -5.457   -57.057 1.00 71.74  ? 150 PHE K C   1 
ATOM   20150 O O   . PHE K  1 150 ? 22.947  -6.643   -56.919 1.00 81.19  ? 150 PHE K O   1 
ATOM   20151 C CB  . PHE K  1 150 ? 23.395  -3.795   -58.782 1.00 68.49  ? 150 PHE K CB  1 
ATOM   20152 C CG  . PHE K  1 150 ? 22.228  -2.859   -58.760 1.00 66.53  ? 150 PHE K CG  1 
ATOM   20153 C CD1 . PHE K  1 150 ? 22.296  -1.672   -58.055 1.00 63.99  ? 150 PHE K CD1 1 
ATOM   20154 C CD2 . PHE K  1 150 ? 21.070  -3.155   -59.459 1.00 58.98  ? 150 PHE K CD2 1 
ATOM   20155 C CE1 . PHE K  1 150 ? 21.228  -0.801   -58.034 1.00 51.90  ? 150 PHE K CE1 1 
ATOM   20156 C CE2 . PHE K  1 150 ? 19.997  -2.288   -59.443 1.00 62.84  ? 150 PHE K CE2 1 
ATOM   20157 C CZ  . PHE K  1 150 ? 20.076  -1.108   -58.730 1.00 58.58  ? 150 PHE K CZ  1 
ATOM   20158 N N   . TYR K  1 151 ? 21.408  -5.005   -56.892 1.00 68.67  ? 151 TYR K N   1 
ATOM   20159 C CA  . TYR K  1 151 ? 20.312  -5.900   -56.547 1.00 58.76  ? 151 TYR K CA  1 
ATOM   20160 C C   . TYR K  1 151 ? 20.088  -6.916   -57.660 1.00 55.23  ? 151 TYR K C   1 
ATOM   20161 O O   . TYR K  1 151 ? 20.108  -6.566   -58.838 1.00 70.34  ? 151 TYR K O   1 
ATOM   20162 C CB  . TYR K  1 151 ? 19.030  -5.106   -56.310 1.00 58.58  ? 151 TYR K CB  1 
ATOM   20163 C CG  . TYR K  1 151 ? 19.175  -3.996   -55.297 1.00 51.95  ? 151 TYR K CG  1 
ATOM   20164 C CD1 . TYR K  1 151 ? 19.131  -4.264   -53.936 1.00 44.45  ? 151 TYR K CD1 1 
ATOM   20165 C CD2 . TYR K  1 151 ? 19.351  -2.678   -55.700 1.00 51.95  ? 151 TYR K CD2 1 
ATOM   20166 C CE1 . TYR K  1 151 ? 19.262  -3.253   -53.005 1.00 54.01  ? 151 TYR K CE1 1 
ATOM   20167 C CE2 . TYR K  1 151 ? 19.482  -1.660   -54.777 1.00 45.86  ? 151 TYR K CE2 1 
ATOM   20168 C CZ  . TYR K  1 151 ? 19.436  -1.953   -53.430 1.00 53.79  ? 151 TYR K CZ  1 
ATOM   20169 O OH  . TYR K  1 151 ? 19.566  -0.944   -52.505 1.00 57.72  ? 151 TYR K OH  1 
ATOM   20170 N N   . LYS K  1 152 ? 19.866  -8.170   -57.285 1.00 60.64  ? 152 LYS K N   1 
ATOM   20171 C CA  . LYS K  1 152 ? 19.669  -9.233   -58.264 1.00 67.73  ? 152 LYS K CA  1 
ATOM   20172 C C   . LYS K  1 152 ? 18.348  -9.083   -59.012 1.00 60.15  ? 152 LYS K C   1 
ATOM   20173 O O   . LYS K  1 152 ? 18.277  -9.326   -60.217 1.00 62.13  ? 152 LYS K O   1 
ATOM   20174 C CB  . LYS K  1 152 ? 19.728  -10.603  -57.586 1.00 69.92  ? 152 LYS K CB  1 
ATOM   20175 C CG  . LYS K  1 152 ? 21.044  -10.894  -56.885 1.00 98.96  ? 152 LYS K CG  1 
ATOM   20176 C CD  . LYS K  1 152 ? 22.207  -10.878  -57.864 1.00 124.67 ? 152 LYS K CD  1 
ATOM   20177 C CE  . LYS K  1 152 ? 23.518  -11.203  -57.168 1.00 131.13 ? 152 LYS K CE  1 
ATOM   20178 N NZ  . LYS K  1 152 ? 24.670  -11.178  -58.111 1.00 123.43 ? 152 LYS K NZ  1 
ATOM   20179 N N   . ASN K  1 153 ? 17.308  -8.677   -58.292 1.00 57.47  ? 153 ASN K N   1 
ATOM   20180 C CA  . ASN K  1 153 ? 15.962  -8.609   -58.853 1.00 64.95  ? 153 ASN K CA  1 
ATOM   20181 C C   . ASN K  1 153 ? 15.670  -7.320   -59.619 1.00 61.12  ? 153 ASN K C   1 
ATOM   20182 O O   . ASN K  1 153 ? 14.560  -7.120   -60.113 1.00 52.39  ? 153 ASN K O   1 
ATOM   20183 C CB  . ASN K  1 153 ? 14.921  -8.823   -57.752 1.00 54.63  ? 153 ASN K CB  1 
ATOM   20184 C CG  . ASN K  1 153 ? 15.067  -10.169  -57.071 1.00 62.53  ? 153 ASN K CG  1 
ATOM   20185 O OD1 . ASN K  1 153 ? 15.639  -11.102  -57.635 1.00 73.52  ? 153 ASN K OD1 1 
ATOM   20186 N ND2 . ASN K  1 153 ? 14.551  -10.277  -55.854 1.00 62.53  ? 153 ASN K ND2 1 
ATOM   20187 N N   . LEU K  1 154 ? 16.670  -6.450   -59.717 1.00 62.43  ? 154 LEU K N   1 
ATOM   20188 C CA  . LEU K  1 154 ? 16.527  -5.205   -60.461 1.00 60.70  ? 154 LEU K CA  1 
ATOM   20189 C C   . LEU K  1 154 ? 17.728  -4.982   -61.372 1.00 64.47  ? 154 LEU K C   1 
ATOM   20190 O O   . LEU K  1 154 ? 18.825  -5.467   -61.096 1.00 73.42  ? 154 LEU K O   1 
ATOM   20191 C CB  . LEU K  1 154 ? 16.370  -4.022   -59.503 1.00 62.47  ? 154 LEU K CB  1 
ATOM   20192 C CG  . LEU K  1 154 ? 15.151  -4.034   -58.579 1.00 48.98  ? 154 LEU K CG  1 
ATOM   20193 C CD1 . LEU K  1 154 ? 15.237  -2.907   -57.561 1.00 57.05  ? 154 LEU K CD1 1 
ATOM   20194 C CD2 . LEU K  1 154 ? 13.868  -3.936   -59.382 1.00 54.73  ? 154 LEU K CD2 1 
ATOM   20195 N N   . ILE K  1 155 ? 17.515  -4.250   -62.460 1.00 66.63  ? 155 ILE K N   1 
ATOM   20196 C CA  . ILE K  1 155 ? 18.597  -3.905   -63.374 1.00 75.39  ? 155 ILE K CA  1 
ATOM   20197 C C   . ILE K  1 155 ? 18.720  -2.394   -63.529 1.00 62.50  ? 155 ILE K C   1 
ATOM   20198 O O   . ILE K  1 155 ? 17.769  -1.722   -63.930 1.00 52.70  ? 155 ILE K O   1 
ATOM   20199 C CB  . ILE K  1 155 ? 18.394  -4.534   -64.763 1.00 76.58  ? 155 ILE K CB  1 
ATOM   20200 C CG1 . ILE K  1 155 ? 18.369  -6.060   -64.661 1.00 82.69  ? 155 ILE K CG1 1 
ATOM   20201 C CG2 . ILE K  1 155 ? 19.492  -4.082   -65.713 1.00 64.19  ? 155 ILE K CG2 1 
ATOM   20202 C CD1 . ILE K  1 155 ? 18.155  -6.753   -65.987 1.00 89.82  ? 155 ILE K CD1 1 
ATOM   20203 N N   . TRP K  1 156 ? 19.894  -1.863   -63.206 1.00 55.85  ? 156 TRP K N   1 
ATOM   20204 C CA  . TRP K  1 156 ? 20.139  -0.431   -63.319 1.00 60.30  ? 156 TRP K CA  1 
ATOM   20205 C C   . TRP K  1 156 ? 20.560  -0.083   -64.741 1.00 64.28  ? 156 TRP K C   1 
ATOM   20206 O O   . TRP K  1 156 ? 21.744  -0.122   -65.075 1.00 76.32  ? 156 TRP K O   1 
ATOM   20207 C CB  . TRP K  1 156 ? 21.215  0.011    -62.328 1.00 66.66  ? 156 TRP K CB  1 
ATOM   20208 C CG  . TRP K  1 156 ? 21.371  1.497    -62.230 1.00 62.77  ? 156 TRP K CG  1 
ATOM   20209 C CD1 . TRP K  1 156 ? 20.736  2.441    -62.985 1.00 58.50  ? 156 TRP K CD1 1 
ATOM   20210 C CD2 . TRP K  1 156 ? 22.217  2.212    -61.323 1.00 68.51  ? 156 TRP K CD2 1 
ATOM   20211 N NE1 . TRP K  1 156 ? 21.135  3.698    -62.605 1.00 53.14  ? 156 TRP K NE1 1 
ATOM   20212 C CE2 . TRP K  1 156 ? 22.044  3.586    -61.586 1.00 56.15  ? 156 TRP K CE2 1 
ATOM   20213 C CE3 . TRP K  1 156 ? 23.105  1.824    -60.315 1.00 65.18  ? 156 TRP K CE3 1 
ATOM   20214 C CZ2 . TRP K  1 156 ? 22.724  4.573    -60.877 1.00 61.00  ? 156 TRP K CZ2 1 
ATOM   20215 C CZ3 . TRP K  1 156 ? 23.779  2.805    -59.613 1.00 70.60  ? 156 TRP K CZ3 1 
ATOM   20216 C CH2 . TRP K  1 156 ? 23.585  4.164    -59.896 1.00 73.95  ? 156 TRP K CH2 1 
ATOM   20217 N N   . LEU K  1 157 ? 19.582  0.255    -65.574 1.00 54.54  ? 157 LEU K N   1 
ATOM   20218 C CA  . LEU K  1 157 ? 19.848  0.585    -66.968 1.00 50.49  ? 157 LEU K CA  1 
ATOM   20219 C C   . LEU K  1 157 ? 20.583  1.912    -67.113 1.00 65.88  ? 157 LEU K C   1 
ATOM   20220 O O   . LEU K  1 157 ? 20.185  2.922    -66.531 1.00 67.76  ? 157 LEU K O   1 
ATOM   20221 C CB  . LEU K  1 157 ? 18.550  0.623    -67.775 1.00 51.79  ? 157 LEU K CB  1 
ATOM   20222 C CG  . LEU K  1 157 ? 17.868  -0.720   -68.039 1.00 58.69  ? 157 LEU K CG  1 
ATOM   20223 C CD1 . LEU K  1 157 ? 16.726  -0.545   -69.024 1.00 59.04  ? 157 LEU K CD1 1 
ATOM   20224 C CD2 . LEU K  1 157 ? 18.862  -1.759   -68.540 1.00 70.95  ? 157 LEU K CD2 1 
ATOM   20225 N N   . VAL K  1 158 ? 21.659  1.897    -67.891 1.00 71.75  ? 158 VAL K N   1 
ATOM   20226 C CA  . VAL K  1 158 ? 22.415  3.107    -68.188 1.00 70.09  ? 158 VAL K CA  1 
ATOM   20227 C C   . VAL K  1 158 ? 22.486  3.311    -69.697 1.00 72.36  ? 158 VAL K C   1 
ATOM   20228 O O   . VAL K  1 158 ? 22.141  2.415    -70.468 1.00 68.03  ? 158 VAL K O   1 
ATOM   20229 C CB  . VAL K  1 158 ? 23.843  3.042    -67.615 1.00 74.00  ? 158 VAL K CB  1 
ATOM   20230 C CG1 . VAL K  1 158 ? 23.803  2.939    -66.097 1.00 72.02  ? 158 VAL K CG1 1 
ATOM   20231 C CG2 . VAL K  1 158 ? 24.604  1.871    -68.217 1.00 79.60  ? 158 VAL K CG2 1 
ATOM   20232 N N   . LYS K  1 159 ? 22.934  4.490    -70.116 1.00 84.91  ? 159 LYS K N   1 
ATOM   20233 C CA  . LYS K  1 159 ? 23.008  4.814    -71.537 1.00 94.98  ? 159 LYS K CA  1 
ATOM   20234 C C   . LYS K  1 159 ? 23.981  3.898    -72.272 1.00 92.78  ? 159 LYS K C   1 
ATOM   20235 O O   . LYS K  1 159 ? 25.056  3.580    -71.763 1.00 86.35  ? 159 LYS K O   1 
ATOM   20236 C CB  . LYS K  1 159 ? 23.414  6.276    -71.737 1.00 96.05  ? 159 LYS K CB  1 
ATOM   20237 C CG  . LYS K  1 159 ? 24.846  6.583    -71.332 1.00 94.71  ? 159 LYS K CG  1 
ATOM   20238 C CD  . LYS K  1 159 ? 25.226  8.009    -71.685 1.00 98.31  ? 159 LYS K CD  1 
ATOM   20239 C CE  . LYS K  1 159 ? 26.698  8.267    -71.414 1.00 95.64  ? 159 LYS K CE  1 
ATOM   20240 N NZ  . LYS K  1 159 ? 27.086  9.664    -71.747 1.00 110.51 ? 159 LYS K NZ  1 
ATOM   20241 N N   . LYS K  1 160 ? 23.596  3.473    -73.471 1.00 100.31 ? 160 LYS K N   1 
ATOM   20242 C CA  . LYS K  1 160 ? 24.457  2.634    -74.295 1.00 113.67 ? 160 LYS K CA  1 
ATOM   20243 C C   . LYS K  1 160 ? 25.320  3.483    -75.221 1.00 124.56 ? 160 LYS K C   1 
ATOM   20244 O O   . LYS K  1 160 ? 24.876  3.892    -76.294 1.00 110.44 ? 160 LYS K O   1 
ATOM   20245 C CB  . LYS K  1 160 ? 23.625  1.651    -75.120 1.00 101.78 ? 160 LYS K CB  1 
ATOM   20246 C CG  . LYS K  1 160 ? 24.447  0.837    -76.106 1.00 111.01 ? 160 LYS K CG  1 
ATOM   20247 C CD  . LYS K  1 160 ? 23.580  -0.137   -76.881 1.00 118.35 ? 160 LYS K CD  1 
ATOM   20248 C CE  . LYS K  1 160 ? 22.808  -1.044   -75.942 1.00 117.41 ? 160 LYS K CE  1 
ATOM   20249 N NZ  . LYS K  1 160 ? 22.180  -2.182   -76.663 1.00 123.63 ? 160 LYS K NZ  1 
ATOM   20250 N N   . GLY K  1 161 ? 26.553  3.743    -74.799 1.00 119.33 ? 161 GLY K N   1 
ATOM   20251 C CA  . GLY K  1 161 ? 27.478  4.536    -75.586 1.00 113.73 ? 161 GLY K CA  1 
ATOM   20252 C C   . GLY K  1 161 ? 26.937  5.850    -76.116 1.00 121.71 ? 161 GLY K C   1 
ATOM   20253 O O   . GLY K  1 161 ? 26.865  6.057    -77.327 1.00 121.42 ? 161 GLY K O   1 
ATOM   20254 N N   . ASN K  1 162 ? 26.548  6.736    -75.204 1.00 119.18 ? 162 ASN K N   1 
ATOM   20255 C CA  . ASN K  1 162 ? 26.074  8.069    -75.568 1.00 124.46 ? 162 ASN K CA  1 
ATOM   20256 C C   . ASN K  1 162 ? 24.659  8.048    -76.142 1.00 113.36 ? 162 ASN K C   1 
ATOM   20257 O O   . ASN K  1 162 ? 24.305  8.899    -76.956 1.00 117.81 ? 162 ASN K O   1 
ATOM   20258 C CB  . ASN K  1 162 ? 27.018  8.769    -76.551 1.00 133.67 ? 162 ASN K CB  1 
ATOM   20259 C CG  . ASN K  1 162 ? 27.899  9.801    -75.879 1.00 143.42 ? 162 ASN K CG  1 
ATOM   20260 O OD1 . ASN K  1 162 ? 28.702  10.468   -76.532 1.00 161.38 ? 162 ASN K OD1 1 
ATOM   20261 N ND2 . ASN K  1 162 ? 27.747  9.946    -74.568 1.00 138.44 ? 162 ASN K ND2 1 
ATOM   20262 N N   . SER K  1 163 ? 23.848  7.085    -75.718 1.00 121.46 ? 163 SER K N   1 
ATOM   20263 C CA  . SER K  1 163 ? 22.480  7.002    -76.217 1.00 120.34 ? 163 SER K CA  1 
ATOM   20264 C C   . SER K  1 163 ? 21.514  6.396    -75.204 1.00 111.82 ? 163 SER K C   1 
ATOM   20265 O O   . SER K  1 163 ? 21.691  5.261    -74.761 1.00 109.16 ? 163 SER K O   1 
ATOM   20266 C CB  . SER K  1 163 ? 22.431  6.210    -77.526 1.00 111.21 ? 163 SER K CB  1 
ATOM   20267 O OG  . SER K  1 163 ? 21.160  6.326    -78.143 1.00 97.69  ? 163 SER K OG  1 
ATOM   20268 N N   . TYR K  1 164 ? 20.493  7.166    -74.844 1.00 98.92  ? 164 TYR K N   1 
ATOM   20269 C CA  . TYR K  1 164 ? 19.415  6.669    -74.001 1.00 85.70  ? 164 TYR K CA  1 
ATOM   20270 C C   . TYR K  1 164 ? 18.072  7.047    -74.615 1.00 81.73  ? 164 TYR K C   1 
ATOM   20271 O O   . TYR K  1 164 ? 17.483  8.067    -74.254 1.00 66.80  ? 164 TYR K O   1 
ATOM   20272 C CB  . TYR K  1 164 ? 19.519  7.229    -72.582 1.00 88.59  ? 164 TYR K CB  1 
ATOM   20273 C CG  . TYR K  1 164 ? 18.719  6.444    -71.567 1.00 87.83  ? 164 TYR K CG  1 
ATOM   20274 C CD1 . TYR K  1 164 ? 19.347  5.781    -70.522 1.00 85.43  ? 164 TYR K CD1 1 
ATOM   20275 C CD2 . TYR K  1 164 ? 17.337  6.350    -71.666 1.00 82.17  ? 164 TYR K CD2 1 
ATOM   20276 C CE1 . TYR K  1 164 ? 18.620  5.057    -69.596 1.00 79.95  ? 164 TYR K CE1 1 
ATOM   20277 C CE2 . TYR K  1 164 ? 16.602  5.627    -70.747 1.00 71.96  ? 164 TYR K CE2 1 
ATOM   20278 C CZ  . TYR K  1 164 ? 17.248  4.983    -69.714 1.00 81.30  ? 164 TYR K CZ  1 
ATOM   20279 O OH  . TYR K  1 164 ? 16.520  4.263    -68.794 1.00 69.75  ? 164 TYR K OH  1 
ATOM   20280 N N   . PRO K  1 165 ? 17.591  6.225    -75.558 1.00 72.53  ? 165 PRO K N   1 
ATOM   20281 C CA  . PRO K  1 165 ? 16.321  6.448    -76.256 1.00 81.77  ? 165 PRO K CA  1 
ATOM   20282 C C   . PRO K  1 165 ? 15.147  6.133    -75.344 1.00 84.55  ? 165 PRO K C   1 
ATOM   20283 O O   . PRO K  1 165 ? 15.279  5.287    -74.460 1.00 76.47  ? 165 PRO K O   1 
ATOM   20284 C CB  . PRO K  1 165 ? 16.366  5.428    -77.403 1.00 68.43  ? 165 PRO K CB  1 
ATOM   20285 C CG  . PRO K  1 165 ? 17.786  4.927    -77.450 1.00 84.77  ? 165 PRO K CG  1 
ATOM   20286 C CD  . PRO K  1 165 ? 18.282  5.026    -76.052 1.00 71.68  ? 165 PRO K CD  1 
ATOM   20287 N N   . LYS K  1 166 ? 14.016  6.800    -75.548 1.00 74.54  ? 166 LYS K N   1 
ATOM   20288 C CA  . LYS K  1 166 ? 12.823  6.483    -74.778 1.00 76.75  ? 166 LYS K CA  1 
ATOM   20289 C C   . LYS K  1 166 ? 12.551  4.987    -74.822 1.00 85.63  ? 166 LYS K C   1 
ATOM   20290 O O   . LYS K  1 166 ? 12.353  4.412    -75.895 1.00 76.20  ? 166 LYS K O   1 
ATOM   20291 C CB  . LYS K  1 166 ? 11.602  7.230    -75.310 1.00 69.32  ? 166 LYS K CB  1 
ATOM   20292 C CG  . LYS K  1 166 ? 10.292  6.622    -74.836 1.00 81.74  ? 166 LYS K CG  1 
ATOM   20293 C CD  . LYS K  1 166 ? 9.097   7.209    -75.561 1.00 100.86 ? 166 LYS K CD  1 
ATOM   20294 C CE  . LYS K  1 166 ? 8.769   8.602    -75.060 1.00 105.90 ? 166 LYS K CE  1 
ATOM   20295 N NZ  . LYS K  1 166 ? 7.496   9.084    -75.658 1.00 112.07 ? 166 LYS K NZ  1 
ATOM   20296 N N   . LEU K  1 167 ? 12.543  4.356    -73.655 1.00 88.11  ? 167 LEU K N   1 
ATOM   20297 C CA  . LEU K  1 167 ? 12.252  2.934    -73.578 1.00 81.62  ? 167 LEU K CA  1 
ATOM   20298 C C   . LEU K  1 167 ? 10.784  2.725    -73.219 1.00 74.38  ? 167 LEU K C   1 
ATOM   20299 O O   . LEU K  1 167 ? 10.176  3.568    -72.560 1.00 68.87  ? 167 LEU K O   1 
ATOM   20300 C CB  . LEU K  1 167 ? 13.210  2.246    -72.595 1.00 67.34  ? 167 LEU K CB  1 
ATOM   20301 C CG  . LEU K  1 167 ? 12.841  1.723    -71.197 1.00 69.31  ? 167 LEU K CG  1 
ATOM   20302 C CD1 . LEU K  1 167 ? 14.112  1.534    -70.376 1.00 68.18  ? 167 LEU K CD1 1 
ATOM   20303 C CD2 . LEU K  1 167 ? 11.815  2.554    -70.438 1.00 81.08  ? 167 LEU K CD2 1 
ATOM   20304 N N   . SER K  1 168 ? 10.207  1.617    -73.672 1.00 71.34  ? 168 SER K N   1 
ATOM   20305 C CA  . SER K  1 168 ? 8.786   1.378    -73.454 1.00 78.89  ? 168 SER K CA  1 
ATOM   20306 C C   . SER K  1 168 ? 8.452   -0.110   -73.413 1.00 83.32  ? 168 SER K C   1 
ATOM   20307 O O   . SER K  1 168 ? 8.007   -0.688   -74.404 1.00 102.73 ? 168 SER K O   1 
ATOM   20308 C CB  . SER K  1 168 ? 7.957   2.082    -74.531 1.00 87.73  ? 168 SER K CB  1 
ATOM   20309 O OG  . SER K  1 168 ? 6.616   2.263    -74.110 1.00 102.62 ? 168 SER K OG  1 
ATOM   20310 N N   . LYS K  1 169 ? 8.676   -0.722   -72.256 1.00 64.78  ? 169 LYS K N   1 
ATOM   20311 C CA  . LYS K  1 169 ? 8.342   -2.123   -72.044 1.00 75.35  ? 169 LYS K CA  1 
ATOM   20312 C C   . LYS K  1 169 ? 7.066   -2.231   -71.220 1.00 75.91  ? 169 LYS K C   1 
ATOM   20313 O O   . LYS K  1 169 ? 6.765   -1.353   -70.413 1.00 76.80  ? 169 LYS K O   1 
ATOM   20314 C CB  . LYS K  1 169 ? 9.486   -2.838   -71.324 1.00 69.20  ? 169 LYS K CB  1 
ATOM   20315 C CG  . LYS K  1 169 ? 10.306  -3.772   -72.200 1.00 87.62  ? 169 LYS K CG  1 
ATOM   20316 C CD  . LYS K  1 169 ? 9.530   -5.032   -72.547 1.00 91.69  ? 169 LYS K CD  1 
ATOM   20317 C CE  . LYS K  1 169 ? 10.442  -6.097   -73.139 1.00 101.92 ? 169 LYS K CE  1 
ATOM   20318 N NZ  . LYS K  1 169 ? 11.129  -5.627   -74.373 1.00 102.07 ? 169 LYS K NZ  1 
ATOM   20319 N N   . SER K  1 170 ? 6.315   -3.307   -71.427 1.00 81.84  ? 170 SER K N   1 
ATOM   20320 C CA  . SER K  1 170 ? 5.102   -3.545   -70.654 1.00 80.48  ? 170 SER K CA  1 
ATOM   20321 C C   . SER K  1 170 ? 4.793   -5.035   -70.548 1.00 67.56  ? 170 SER K C   1 
ATOM   20322 O O   . SER K  1 170 ? 4.719   -5.740   -71.555 1.00 71.11  ? 170 SER K O   1 
ATOM   20323 C CB  . SER K  1 170 ? 3.914   -2.790   -71.255 1.00 78.16  ? 170 SER K CB  1 
ATOM   20324 O OG  . SER K  1 170 ? 3.710   -3.146   -72.610 1.00 113.74 ? 170 SER K OG  1 
ATOM   20325 N N   . TYR K  1 171 ? 4.618   -5.504   -69.317 1.00 65.08  ? 171 TYR K N   1 
ATOM   20326 C CA  . TYR K  1 171 ? 4.336   -6.909   -69.054 1.00 70.27  ? 171 TYR K CA  1 
ATOM   20327 C C   . TYR K  1 171 ? 2.878   -7.111   -68.657 1.00 69.37  ? 171 TYR K C   1 
ATOM   20328 O O   . TYR K  1 171 ? 2.297   -6.282   -67.957 1.00 62.22  ? 171 TYR K O   1 
ATOM   20329 C CB  . TYR K  1 171 ? 5.263   -7.435   -67.954 1.00 73.07  ? 171 TYR K CB  1 
ATOM   20330 C CG  . TYR K  1 171 ? 4.753   -8.670   -67.245 1.00 66.60  ? 171 TYR K CG  1 
ATOM   20331 C CD1 . TYR K  1 171 ? 5.066   -9.941   -67.709 1.00 61.32  ? 171 TYR K CD1 1 
ATOM   20332 C CD2 . TYR K  1 171 ? 3.964   -8.564   -66.107 1.00 68.93  ? 171 TYR K CD2 1 
ATOM   20333 C CE1 . TYR K  1 171 ? 4.603   -11.071  -67.061 1.00 63.18  ? 171 TYR K CE1 1 
ATOM   20334 C CE2 . TYR K  1 171 ? 3.497   -9.687   -65.454 1.00 68.86  ? 171 TYR K CE2 1 
ATOM   20335 C CZ  . TYR K  1 171 ? 3.819   -10.938  -65.934 1.00 72.36  ? 171 TYR K CZ  1 
ATOM   20336 O OH  . TYR K  1 171 ? 3.356   -12.060  -65.285 1.00 77.87  ? 171 TYR K OH  1 
ATOM   20337 N N   . ILE K  1 172 ? 2.291   -8.215   -69.108 1.00 66.53  ? 172 ILE K N   1 
ATOM   20338 C CA  . ILE K  1 172 ? 0.912   -8.540   -68.763 1.00 66.91  ? 172 ILE K CA  1 
ATOM   20339 C C   . ILE K  1 172 ? 0.849   -9.782   -67.875 1.00 72.84  ? 172 ILE K C   1 
ATOM   20340 O O   . ILE K  1 172 ? 1.479   -10.799  -68.163 1.00 72.58  ? 172 ILE K O   1 
ATOM   20341 C CB  . ILE K  1 172 ? 0.038   -8.734   -70.022 1.00 71.07  ? 172 ILE K CB  1 
ATOM   20342 C CG1 . ILE K  1 172 ? -1.425  -8.950   -69.630 1.00 75.50  ? 172 ILE K CG1 1 
ATOM   20343 C CG2 . ILE K  1 172 ? 0.557   -9.890   -70.867 1.00 85.71  ? 172 ILE K CG2 1 
ATOM   20344 C CD1 . ILE K  1 172 ? -2.396  -8.075   -70.395 1.00 78.02  ? 172 ILE K CD1 1 
ATOM   20345 N N   . ASN K  1 173 ? 0.088   -9.685   -66.789 1.00 70.81  ? 173 ASN K N   1 
ATOM   20346 C CA  . ASN K  1 173 ? 0.002   -10.761  -65.809 1.00 65.83  ? 173 ASN K CA  1 
ATOM   20347 C C   . ASN K  1 173 ? -0.732  -11.988  -66.341 1.00 76.95  ? 173 ASN K C   1 
ATOM   20348 O O   . ASN K  1 173 ? -1.960  -12.061  -66.289 1.00 66.57  ? 173 ASN K O   1 
ATOM   20349 C CB  . ASN K  1 173 ? -0.665  -10.261  -64.525 1.00 62.16  ? 173 ASN K CB  1 
ATOM   20350 C CG  . ASN K  1 173 ? -0.560  -11.256  -63.386 1.00 74.17  ? 173 ASN K CG  1 
ATOM   20351 O OD1 . ASN K  1 173 ? -0.025  -12.352  -63.550 1.00 69.81  ? 173 ASN K OD1 1 
ATOM   20352 N ND2 . ASN K  1 173 ? -1.068  -10.875  -62.219 1.00 69.74  ? 173 ASN K ND2 1 
ATOM   20353 N N   . ASP K  1 174 ? 0.029   -12.951  -66.851 1.00 88.55  ? 174 ASP K N   1 
ATOM   20354 C CA  . ASP K  1 174 ? -0.544  -14.183  -67.379 1.00 77.52  ? 174 ASP K CA  1 
ATOM   20355 C C   . ASP K  1 174 ? -0.690  -15.233  -66.283 1.00 82.73  ? 174 ASP K C   1 
ATOM   20356 O O   . ASP K  1 174 ? -1.201  -16.327  -66.523 1.00 98.37  ? 174 ASP K O   1 
ATOM   20357 C CB  . ASP K  1 174 ? 0.314   -14.727  -68.523 1.00 86.26  ? 174 ASP K CB  1 
ATOM   20358 C CG  . ASP K  1 174 ? 1.756   -14.952  -68.113 1.00 108.34 ? 174 ASP K CG  1 
ATOM   20359 O OD1 . ASP K  1 174 ? 2.113   -16.107  -67.797 1.00 108.95 ? 174 ASP K OD1 1 
ATOM   20360 O OD2 . ASP K  1 174 ? 2.533   -13.974  -68.107 1.00 109.01 ? 174 ASP K OD2 1 
ATOM   20361 N N   . LYS K  1 175 ? -0.237  -14.892  -65.081 1.00 77.69  ? 175 LYS K N   1 
ATOM   20362 C CA  . LYS K  1 175 ? -0.349  -15.787  -63.936 1.00 80.83  ? 175 LYS K CA  1 
ATOM   20363 C C   . LYS K  1 175 ? -1.789  -15.840  -63.439 1.00 86.61  ? 175 LYS K C   1 
ATOM   20364 O O   . LYS K  1 175 ? -2.649  -15.098  -63.916 1.00 88.52  ? 175 LYS K O   1 
ATOM   20365 C CB  . LYS K  1 175 ? 0.568   -15.325  -62.801 1.00 71.27  ? 175 LYS K CB  1 
ATOM   20366 C CG  . LYS K  1 175 ? 2.021   -15.122  -63.200 1.00 70.50  ? 175 LYS K CG  1 
ATOM   20367 C CD  . LYS K  1 175 ? 2.721   -16.440  -63.485 1.00 63.54  ? 175 LYS K CD  1 
ATOM   20368 C CE  . LYS K  1 175 ? 4.201   -16.218  -63.760 1.00 65.59  ? 175 LYS K CE  1 
ATOM   20369 N NZ  . LYS K  1 175 ? 4.936   -17.494  -63.983 1.00 87.98  ? 175 LYS K NZ  1 
ATOM   20370 N N   . GLY K  1 176 ? -2.045  -16.719  -62.476 1.00 58.86  ? 176 GLY K N   1 
ATOM   20371 C CA  . GLY K  1 176 ? -3.363  -16.842  -61.883 1.00 83.94  ? 176 GLY K CA  1 
ATOM   20372 C C   . GLY K  1 176 ? -3.420  -16.221  -60.507 1.00 86.73  ? 176 GLY K C   1 
ATOM   20373 O O   . GLY K  1 176 ? -4.335  -16.475  -59.723 1.00 85.65  ? 176 GLY K O   1 
ATOM   20374 N N   . LYS K  1 177 ? -2.426  -15.391  -60.226 1.00 80.65  ? 177 LYS K N   1 
ATOM   20375 C CA  . LYS K  1 177 ? -2.273  -14.774  -58.923 1.00 70.30  ? 177 LYS K CA  1 
ATOM   20376 C C   . LYS K  1 177 ? -1.645  -13.405  -59.119 1.00 61.07  ? 177 LYS K C   1 
ATOM   20377 O O   . LYS K  1 177 ? -1.038  -13.140  -60.156 1.00 72.00  ? 177 LYS K O   1 
ATOM   20378 C CB  . LYS K  1 177 ? -1.373  -15.646  -58.050 1.00 66.73  ? 177 LYS K CB  1 
ATOM   20379 C CG  . LYS K  1 177 ? -0.068  -16.031  -58.733 1.00 69.67  ? 177 LYS K CG  1 
ATOM   20380 C CD  . LYS K  1 177 ? 0.716   -17.056  -57.930 1.00 68.55  ? 177 LYS K CD  1 
ATOM   20381 C CE  . LYS K  1 177 ? 0.032   -18.413  -57.932 1.00 78.28  ? 177 LYS K CE  1 
ATOM   20382 N NZ  . LYS K  1 177 ? -0.097  -18.991  -59.298 1.00 79.31  ? 177 LYS K NZ  1 
ATOM   20383 N N   . GLU K  1 178 ? -1.796  -12.533  -58.129 1.00 53.97  ? 178 GLU K N   1 
ATOM   20384 C CA  . GLU K  1 178 ? -1.192  -11.210  -58.197 1.00 58.00  ? 178 GLU K CA  1 
ATOM   20385 C C   . GLU K  1 178 ? 0.310   -11.330  -58.417 1.00 65.11  ? 178 GLU K C   1 
ATOM   20386 O O   . GLU K  1 178 ? 0.926   -12.321  -58.025 1.00 61.46  ? 178 GLU K O   1 
ATOM   20387 C CB  . GLU K  1 178 ? -1.460  -10.435  -56.910 1.00 56.29  ? 178 GLU K CB  1 
ATOM   20388 C CG  . GLU K  1 178 ? -2.929  -10.224  -56.604 1.00 82.29  ? 178 GLU K CG  1 
ATOM   20389 C CD  . GLU K  1 178 ? -3.147  -9.633   -55.228 1.00 90.88  ? 178 GLU K CD  1 
ATOM   20390 O OE1 . GLU K  1 178 ? -2.533  -10.138  -54.265 1.00 86.46  ? 178 GLU K OE1 1 
ATOM   20391 O OE2 . GLU K  1 178 ? -3.930  -8.668   -55.110 1.00 94.57  ? 178 GLU K OE2 1 
ATOM   20392 N N   . VAL K  1 179 ? 0.895   -10.322  -59.052 1.00 52.17  ? 179 VAL K N   1 
ATOM   20393 C CA  . VAL K  1 179 ? 2.338   -10.283  -59.239 1.00 52.92  ? 179 VAL K CA  1 
ATOM   20394 C C   . VAL K  1 179 ? 2.931   -9.025   -58.617 1.00 53.46  ? 179 VAL K C   1 
ATOM   20395 O O   . VAL K  1 179 ? 2.555   -7.908   -58.971 1.00 50.93  ? 179 VAL K O   1 
ATOM   20396 C CB  . VAL K  1 179 ? 2.728   -10.348  -60.727 1.00 53.23  ? 179 VAL K CB  1 
ATOM   20397 C CG1 . VAL K  1 179 ? 4.199   -10.008  -60.901 1.00 52.21  ? 179 VAL K CG1 1 
ATOM   20398 C CG2 . VAL K  1 179 ? 2.424   -11.724  -61.295 1.00 54.20  ? 179 VAL K CG2 1 
ATOM   20399 N N   . LEU K  1 180 ? 3.852   -9.216   -57.679 1.00 41.90  ? 180 LEU K N   1 
ATOM   20400 C CA  . LEU K  1 180 ? 4.538   -8.101   -57.041 1.00 44.17  ? 180 LEU K CA  1 
ATOM   20401 C C   . LEU K  1 180 ? 5.664   -7.602   -57.934 1.00 47.01  ? 180 LEU K C   1 
ATOM   20402 O O   . LEU K  1 180 ? 6.640   -8.314   -58.168 1.00 54.68  ? 180 LEU K O   1 
ATOM   20403 C CB  . LEU K  1 180 ? 5.106   -8.529   -55.688 1.00 43.04  ? 180 LEU K CB  1 
ATOM   20404 C CG  . LEU K  1 180 ? 5.910   -7.471   -54.929 1.00 42.98  ? 180 LEU K CG  1 
ATOM   20405 C CD1 . LEU K  1 180 ? 4.991   -6.391   -54.384 1.00 46.38  ? 180 LEU K CD1 1 
ATOM   20406 C CD2 . LEU K  1 180 ? 6.707   -8.107   -53.804 1.00 37.14  ? 180 LEU K CD2 1 
ATOM   20407 N N   . VAL K  1 181 ? 5.530   -6.378   -58.433 1.00 46.88  ? 181 VAL K N   1 
ATOM   20408 C CA  . VAL K  1 181 ? 6.560   -5.799   -59.288 1.00 52.66  ? 181 VAL K CA  1 
ATOM   20409 C C   . VAL K  1 181 ? 7.319   -4.692   -58.563 1.00 52.41  ? 181 VAL K C   1 
ATOM   20410 O O   . VAL K  1 181 ? 6.717   -3.747   -58.059 1.00 52.52  ? 181 VAL K O   1 
ATOM   20411 C CB  . VAL K  1 181 ? 5.964   -5.239   -60.593 1.00 44.37  ? 181 VAL K CB  1 
ATOM   20412 C CG1 . VAL K  1 181 ? 7.075   -4.779   -61.524 1.00 44.93  ? 181 VAL K CG1 1 
ATOM   20413 C CG2 . VAL K  1 181 ? 5.099   -6.289   -61.271 1.00 42.19  ? 181 VAL K CG2 1 
ATOM   20414 N N   . LEU K  1 182 ? 8.641   -4.817   -58.502 1.00 50.25  ? 182 LEU K N   1 
ATOM   20415 C CA  . LEU K  1 182 ? 9.465   -3.787   -57.877 1.00 47.93  ? 182 LEU K CA  1 
ATOM   20416 C C   . LEU K  1 182 ? 10.327  -3.058   -58.904 1.00 44.94  ? 182 LEU K C   1 
ATOM   20417 O O   . LEU K  1 182 ? 10.812  -3.659   -59.863 1.00 53.24  ? 182 LEU K O   1 
ATOM   20418 C CB  . LEU K  1 182 ? 10.323  -4.365   -56.746 1.00 34.07  ? 182 LEU K CB  1 
ATOM   20419 C CG  . LEU K  1 182 ? 9.530   -4.872   -55.534 1.00 45.20  ? 182 LEU K CG  1 
ATOM   20420 C CD1 . LEU K  1 182 ? 9.571   -6.393   -55.437 1.00 47.22  ? 182 LEU K CD1 1 
ATOM   20421 C CD2 . LEU K  1 182 ? 10.013  -4.232   -54.235 1.00 44.27  ? 182 LEU K CD2 1 
ATOM   20422 N N   . TRP K  1 183 ? 10.498  -1.755   -58.695 1.00 39.88  ? 183 TRP K N   1 
ATOM   20423 C CA  . TRP K  1 183 ? 11.300  -0.917   -59.578 1.00 42.93  ? 183 TRP K CA  1 
ATOM   20424 C C   . TRP K  1 183 ? 11.886  0.256    -58.793 1.00 41.27  ? 183 TRP K C   1 
ATOM   20425 O O   . TRP K  1 183 ? 11.432  0.557    -57.691 1.00 42.63  ? 183 TRP K O   1 
ATOM   20426 C CB  . TRP K  1 183 ? 10.458  -0.411   -60.758 1.00 57.35  ? 183 TRP K CB  1 
ATOM   20427 C CG  . TRP K  1 183 ? 9.478   0.685    -60.411 1.00 45.48  ? 183 TRP K CG  1 
ATOM   20428 C CD1 . TRP K  1 183 ? 9.737   2.025    -60.363 1.00 49.76  ? 183 TRP K CD1 1 
ATOM   20429 C CD2 . TRP K  1 183 ? 8.086   0.536    -60.085 1.00 49.08  ? 183 TRP K CD2 1 
ATOM   20430 N NE1 . TRP K  1 183 ? 8.600   2.716    -60.018 1.00 44.36  ? 183 TRP K NE1 1 
ATOM   20431 C CE2 . TRP K  1 183 ? 7.574   1.827    -59.843 1.00 48.47  ? 183 TRP K CE2 1 
ATOM   20432 C CE3 . TRP K  1 183 ? 7.224   -0.560   -59.979 1.00 51.49  ? 183 TRP K CE3 1 
ATOM   20433 C CZ2 . TRP K  1 183 ? 6.241   2.049    -59.492 1.00 48.78  ? 183 TRP K CZ2 1 
ATOM   20434 C CZ3 . TRP K  1 183 ? 5.901   -0.337   -59.621 1.00 48.02  ? 183 TRP K CZ3 1 
ATOM   20435 C CH2 . TRP K  1 183 ? 5.424   0.958    -59.387 1.00 46.19  ? 183 TRP K CH2 1 
ATOM   20436 N N   . GLY K  1 184 ? 12.892  0.917    -59.356 1.00 40.07  ? 184 GLY K N   1 
ATOM   20437 C CA  . GLY K  1 184 ? 13.527  2.031    -58.673 1.00 42.46  ? 184 GLY K CA  1 
ATOM   20438 C C   . GLY K  1 184 ? 13.687  3.272    -59.528 1.00 41.97  ? 184 GLY K C   1 
ATOM   20439 O O   . GLY K  1 184 ? 13.804  3.187    -60.749 1.00 44.25  ? 184 GLY K O   1 
ATOM   20440 N N   . ILE K  1 185 ? 13.687  4.431    -58.879 1.00 41.64  ? 185 ILE K N   1 
ATOM   20441 C CA  . ILE K  1 185 ? 13.942  5.691    -59.559 1.00 40.35  ? 185 ILE K CA  1 
ATOM   20442 C C   . ILE K  1 185 ? 15.231  6.280    -59.010 1.00 41.45  ? 185 ILE K C   1 
ATOM   20443 O O   . ILE K  1 185 ? 15.301  6.643    -57.837 1.00 49.00  ? 185 ILE K O   1 
ATOM   20444 C CB  . ILE K  1 185 ? 12.797  6.699    -59.341 1.00 49.95  ? 185 ILE K CB  1 
ATOM   20445 C CG1 . ILE K  1 185 ? 11.455  6.076    -59.730 1.00 45.80  ? 185 ILE K CG1 1 
ATOM   20446 C CG2 . ILE K  1 185 ? 13.049  7.976    -60.131 1.00 44.00  ? 185 ILE K CG2 1 
ATOM   20447 C CD1 . ILE K  1 185 ? 11.397  5.606    -61.162 1.00 41.58  ? 185 ILE K CD1 1 
ATOM   20448 N N   . HIS K  1 186 ? 16.254  6.364    -59.853 1.00 46.38  ? 186 HIS K N   1 
ATOM   20449 C CA  . HIS K  1 186 ? 17.547  6.876    -59.414 1.00 54.42  ? 186 HIS K CA  1 
ATOM   20450 C C   . HIS K  1 186 ? 17.630  8.393    -59.518 1.00 46.04  ? 186 HIS K C   1 
ATOM   20451 O O   . HIS K  1 186 ? 17.295  8.976    -60.549 1.00 49.63  ? 186 HIS K O   1 
ATOM   20452 C CB  . HIS K  1 186 ? 18.690  6.229    -60.198 1.00 48.92  ? 186 HIS K CB  1 
ATOM   20453 C CG  . HIS K  1 186 ? 20.041  6.772    -59.845 1.00 58.26  ? 186 HIS K CG  1 
ATOM   20454 N ND1 . HIS K  1 186 ? 20.787  7.533    -60.717 1.00 59.93  ? 186 HIS K ND1 1 
ATOM   20455 C CD2 . HIS K  1 186 ? 20.769  6.679    -58.708 1.00 60.65  ? 186 HIS K CD2 1 
ATOM   20456 C CE1 . HIS K  1 186 ? 21.924  7.877    -60.137 1.00 66.04  ? 186 HIS K CE1 1 
ATOM   20457 N NE2 . HIS K  1 186 ? 21.937  7.372    -58.917 1.00 60.71  ? 186 HIS K NE2 1 
ATOM   20458 N N   . HIS K  1 187 ? 18.076  9.025    -58.438 1.00 48.92  ? 187 HIS K N   1 
ATOM   20459 C CA  . HIS K  1 187 ? 18.277  10.466   -58.416 1.00 50.16  ? 187 HIS K CA  1 
ATOM   20460 C C   . HIS K  1 187 ? 19.761  10.777   -58.250 1.00 59.79  ? 187 HIS K C   1 
ATOM   20461 O O   . HIS K  1 187 ? 20.285  10.747   -57.137 1.00 60.45  ? 187 HIS K O   1 
ATOM   20462 C CB  . HIS K  1 187 ? 17.473  11.104   -57.281 1.00 50.28  ? 187 HIS K CB  1 
ATOM   20463 C CG  . HIS K  1 187 ? 16.013  10.774   -57.315 1.00 56.13  ? 187 HIS K CG  1 
ATOM   20464 N ND1 . HIS K  1 187 ? 15.099  11.506   -58.037 1.00 61.17  ? 187 HIS K ND1 1 
ATOM   20465 C CD2 . HIS K  1 187 ? 15.309  9.784    -56.708 1.00 58.90  ? 187 HIS K CD2 1 
ATOM   20466 C CE1 . HIS K  1 187 ? 13.893  10.984   -57.877 1.00 65.60  ? 187 HIS K CE1 1 
ATOM   20467 N NE2 . HIS K  1 187 ? 13.995  9.943    -57.079 1.00 61.27  ? 187 HIS K NE2 1 
ATOM   20468 N N   . PRO K  1 188 ? 20.446  11.065   -59.366 1.00 51.48  ? 188 PRO K N   1 
ATOM   20469 C CA  . PRO K  1 188 ? 21.879  11.375   -59.362 1.00 60.71  ? 188 PRO K CA  1 
ATOM   20470 C C   . PRO K  1 188 ? 22.211  12.571   -58.476 1.00 64.96  ? 188 PRO K C   1 
ATOM   20471 O O   . PRO K  1 188 ? 21.332  13.374   -58.162 1.00 59.53  ? 188 PRO K O   1 
ATOM   20472 C CB  . PRO K  1 188 ? 22.166  11.710   -60.828 1.00 59.36  ? 188 PRO K CB  1 
ATOM   20473 C CG  . PRO K  1 188 ? 21.114  10.985   -61.590 1.00 61.16  ? 188 PRO K CG  1 
ATOM   20474 C CD  . PRO K  1 188 ? 19.889  11.053   -60.730 1.00 52.49  ? 188 PRO K CD  1 
ATOM   20475 N N   . SER K  1 189 ? 23.475  12.682   -58.083 1.00 69.08  ? 189 SER K N   1 
ATOM   20476 C CA  . SER K  1 189 ? 23.912  13.745   -57.186 1.00 67.83  ? 189 SER K CA  1 
ATOM   20477 C C   . SER K  1 189 ? 24.174  15.049   -57.932 1.00 74.13  ? 189 SER K C   1 
ATOM   20478 O O   . SER K  1 189 ? 23.871  16.133   -57.433 1.00 82.11  ? 189 SER K O   1 
ATOM   20479 C CB  . SER K  1 189 ? 25.168  13.312   -56.427 1.00 71.70  ? 189 SER K CB  1 
ATOM   20480 O OG  . SER K  1 189 ? 26.192  12.913   -57.321 1.00 78.21  ? 189 SER K OG  1 
ATOM   20481 N N   . THR K  1 190 ? 24.737  14.938   -59.130 1.00 85.43  ? 190 THR K N   1 
ATOM   20482 C CA  . THR K  1 190 ? 25.086  16.111   -59.922 1.00 87.17  ? 190 THR K CA  1 
ATOM   20483 C C   . THR K  1 190 ? 24.565  16.008   -61.353 1.00 77.28  ? 190 THR K C   1 
ATOM   20484 O O   . THR K  1 190 ? 24.346  14.911   -61.867 1.00 71.84  ? 190 THR K O   1 
ATOM   20485 C CB  . THR K  1 190 ? 26.611  16.336   -59.942 1.00 79.97  ? 190 THR K CB  1 
ATOM   20486 O OG1 . THR K  1 190 ? 26.993  16.935   -61.187 1.00 105.23 ? 190 THR K OG1 1 
ATOM   20487 C CG2 . THR K  1 190 ? 27.346  15.015   -59.781 1.00 81.26  ? 190 THR K CG2 1 
ATOM   20488 N N   . SER K  1 191 ? 24.364  17.158   -61.989 1.00 90.23  ? 191 SER K N   1 
ATOM   20489 C CA  . SER K  1 191 ? 23.891  17.198   -63.368 1.00 94.67  ? 191 SER K CA  1 
ATOM   20490 C C   . SER K  1 191 ? 24.908  16.556   -64.305 1.00 81.02  ? 191 SER K C   1 
ATOM   20491 O O   . SER K  1 191 ? 24.563  16.099   -65.395 1.00 76.69  ? 191 SER K O   1 
ATOM   20492 C CB  . SER K  1 191 ? 23.601  18.637   -63.799 1.00 82.72  ? 191 SER K CB  1 
ATOM   20493 O OG  . SER K  1 191 ? 24.770  19.435   -63.734 1.00 92.53  ? 191 SER K OG  1 
ATOM   20494 N N   . ALA K  1 192 ? 26.165  16.527   -63.874 1.00 87.45  ? 192 ALA K N   1 
ATOM   20495 C CA  . ALA K  1 192 ? 27.218  15.865   -64.632 1.00 100.27 ? 192 ALA K CA  1 
ATOM   20496 C C   . ALA K  1 192 ? 27.038  14.353   -64.556 1.00 101.32 ? 192 ALA K C   1 
ATOM   20497 O O   . ALA K  1 192 ? 27.239  13.642   -65.540 1.00 89.42  ? 192 ALA K O   1 
ATOM   20498 C CB  . ALA K  1 192 ? 28.586  16.269   -64.108 1.00 101.27 ? 192 ALA K CB  1 
ATOM   20499 N N   . ASP K  1 193 ? 26.658  13.869   -63.377 1.00 99.16  ? 193 ASP K N   1 
ATOM   20500 C CA  . ASP K  1 193 ? 26.369  12.453   -63.184 1.00 87.91  ? 193 ASP K CA  1 
ATOM   20501 C C   . ASP K  1 193 ? 25.133  12.041   -63.975 1.00 77.36  ? 193 ASP K C   1 
ATOM   20502 O O   . ASP K  1 193 ? 25.026  10.902   -64.430 1.00 65.28  ? 193 ASP K O   1 
ATOM   20503 C CB  . ASP K  1 193 ? 26.163  12.141   -61.700 1.00 87.88  ? 193 ASP K CB  1 
ATOM   20504 C CG  . ASP K  1 193 ? 27.405  11.570   -61.044 1.00 110.17 ? 193 ASP K CG  1 
ATOM   20505 O OD1 . ASP K  1 193 ? 28.515  12.071   -61.323 1.00 114.69 ? 193 ASP K OD1 1 
ATOM   20506 O OD2 . ASP K  1 193 ? 27.269  10.619   -60.246 1.00 128.76 ? 193 ASP K OD2 1 
ATOM   20507 N N   . GLN K  1 194 ? 24.202  12.977   -64.133 1.00 77.82  ? 194 GLN K N   1 
ATOM   20508 C CA  . GLN K  1 194 ? 22.963  12.723   -64.859 1.00 69.99  ? 194 GLN K CA  1 
ATOM   20509 C C   . GLN K  1 194 ? 23.225  12.399   -66.326 1.00 79.53  ? 194 GLN K C   1 
ATOM   20510 O O   . GLN K  1 194 ? 22.820  11.347   -66.819 1.00 76.33  ? 194 GLN K O   1 
ATOM   20511 C CB  . GLN K  1 194 ? 22.025  13.927   -64.749 1.00 81.39  ? 194 GLN K CB  1 
ATOM   20512 C CG  . GLN K  1 194 ? 20.821  13.873   -65.680 1.00 81.25  ? 194 GLN K CG  1 
ATOM   20513 C CD  . GLN K  1 194 ? 19.815  12.810   -65.286 1.00 66.74  ? 194 GLN K CD  1 
ATOM   20514 O OE1 . GLN K  1 194 ? 18.946  12.439   -66.074 1.00 70.36  ? 194 GLN K OE1 1 
ATOM   20515 N NE2 . GLN K  1 194 ? 19.926  12.315   -64.060 1.00 62.59  ? 194 GLN K NE2 1 
ATOM   20516 N N   . GLN K  1 195 ? 23.901  13.309   -67.019 1.00 110.34 ? 195 GLN K N   1 
ATOM   20517 C CA  . GLN K  1 195 ? 24.210  13.114   -68.432 1.00 116.08 ? 195 GLN K CA  1 
ATOM   20518 C C   . GLN K  1 195 ? 25.243  12.009   -68.624 1.00 103.33 ? 195 GLN K C   1 
ATOM   20519 O O   . GLN K  1 195 ? 25.304  11.380   -69.680 1.00 99.56  ? 195 GLN K O   1 
ATOM   20520 C CB  . GLN K  1 195 ? 24.687  14.422   -69.069 1.00 127.17 ? 195 GLN K CB  1 
ATOM   20521 C CG  . GLN K  1 195 ? 25.853  15.082   -68.353 1.00 150.17 ? 195 GLN K CG  1 
ATOM   20522 C CD  . GLN K  1 195 ? 26.162  16.463   -68.900 1.00 165.27 ? 195 GLN K CD  1 
ATOM   20523 O OE1 . GLN K  1 195 ? 27.086  17.134   -68.440 1.00 159.82 ? 195 GLN K OE1 1 
ATOM   20524 N NE2 . GLN K  1 195 ? 25.386  16.897   -69.888 1.00 166.02 ? 195 GLN K NE2 1 
ATOM   20525 N N   . SER K  1 196 ? 26.051  11.774   -67.596 1.00 82.81  ? 196 SER K N   1 
ATOM   20526 C CA  . SER K  1 196 ? 27.030  10.696   -67.625 1.00 79.64  ? 196 SER K CA  1 
ATOM   20527 C C   . SER K  1 196 ? 26.335  9.339    -67.656 1.00 92.66  ? 196 SER K C   1 
ATOM   20528 O O   . SER K  1 196 ? 26.821  8.394    -68.278 1.00 99.84  ? 196 SER K O   1 
ATOM   20529 C CB  . SER K  1 196 ? 27.951  10.778   -66.407 1.00 79.28  ? 196 SER K CB  1 
ATOM   20530 O OG  . SER K  1 196 ? 28.823  9.663    -66.350 1.00 91.84  ? 196 SER K OG  1 
ATOM   20531 N N   . LEU K  1 197 ? 25.191  9.255    -66.985 1.00 92.08  ? 197 LEU K N   1 
ATOM   20532 C CA  . LEU K  1 197 ? 24.469  7.995    -66.844 1.00 76.36  ? 197 LEU K CA  1 
ATOM   20533 C C   . LEU K  1 197 ? 23.383  7.798    -67.899 1.00 80.42  ? 197 LEU K C   1 
ATOM   20534 O O   . LEU K  1 197 ? 23.237  6.706    -68.447 1.00 73.11  ? 197 LEU K O   1 
ATOM   20535 C CB  . LEU K  1 197 ? 23.858  7.887    -65.445 1.00 74.04  ? 197 LEU K CB  1 
ATOM   20536 C CG  . LEU K  1 197 ? 24.791  7.457    -64.313 1.00 72.72  ? 197 LEU K CG  1 
ATOM   20537 C CD1 . LEU K  1 197 ? 24.135  7.684    -62.959 1.00 72.67  ? 197 LEU K CD1 1 
ATOM   20538 C CD2 . LEU K  1 197 ? 25.190  6.000    -64.484 1.00 69.39  ? 197 LEU K CD2 1 
ATOM   20539 N N   . TYR K  1 198 ? 22.619  8.848    -68.182 1.00 81.77  ? 198 TYR K N   1 
ATOM   20540 C CA  . TYR K  1 198 ? 21.475  8.718    -69.078 1.00 84.71  ? 198 TYR K CA  1 
ATOM   20541 C C   . TYR K  1 198 ? 21.482  9.761    -70.193 1.00 95.96  ? 198 TYR K C   1 
ATOM   20542 O O   . TYR K  1 198 ? 20.531  9.861    -70.969 1.00 92.16  ? 198 TYR K O   1 
ATOM   20543 C CB  . TYR K  1 198 ? 20.171  8.812    -68.284 1.00 90.54  ? 198 TYR K CB  1 
ATOM   20544 C CG  . TYR K  1 198 ? 20.245  8.160    -66.920 1.00 78.09  ? 198 TYR K CG  1 
ATOM   20545 C CD1 . TYR K  1 198 ? 20.377  8.928    -65.771 1.00 70.88  ? 198 TYR K CD1 1 
ATOM   20546 C CD2 . TYR K  1 198 ? 20.196  6.778    -66.782 1.00 78.52  ? 198 TYR K CD2 1 
ATOM   20547 C CE1 . TYR K  1 198 ? 20.448  8.341    -64.521 1.00 74.46  ? 198 TYR K CE1 1 
ATOM   20548 C CE2 . TYR K  1 198 ? 20.268  6.181    -65.533 1.00 70.38  ? 198 TYR K CE2 1 
ATOM   20549 C CZ  . TYR K  1 198 ? 20.394  6.969    -64.408 1.00 66.55  ? 198 TYR K CZ  1 
ATOM   20550 O OH  . TYR K  1 198 ? 20.465  6.386    -63.165 1.00 64.44  ? 198 TYR K OH  1 
ATOM   20551 N N   . GLN K  1 199 ? 22.562  10.528   -70.282 1.00 98.48  ? 199 GLN K N   1 
ATOM   20552 C CA  . GLN K  1 199 ? 22.762  11.479   -71.378 1.00 101.52 ? 199 GLN K CA  1 
ATOM   20553 C C   . GLN K  1 199 ? 21.496  12.160   -71.916 1.00 98.51  ? 199 GLN K C   1 
ATOM   20554 O O   . GLN K  1 199 ? 21.294  12.234   -73.128 1.00 102.39 ? 199 GLN K O   1 
ATOM   20555 C CB  . GLN K  1 199 ? 23.514  10.805   -72.530 1.00 102.00 ? 199 GLN K CB  1 
ATOM   20556 C CG  . GLN K  1 199 ? 24.904  11.368   -72.777 1.00 111.76 ? 199 GLN K CG  1 
ATOM   20557 C CD  . GLN K  1 199 ? 24.875  12.674   -73.547 1.00 120.56 ? 199 GLN K CD  1 
ATOM   20558 O OE1 . GLN K  1 199 ? 23.881  13.005   -74.194 1.00 121.03 ? 199 GLN K OE1 1 
ATOM   20559 N NE2 . GLN K  1 199 ? 25.969  13.424   -73.482 1.00 105.20 ? 199 GLN K NE2 1 
ATOM   20560 N N   . ASN K  1 200 ? 20.660  12.667   -71.016 1.00 102.47 ? 200 ASN K N   1 
ATOM   20561 C CA  . ASN K  1 200 ? 19.535  13.521   -71.383 1.00 101.49 ? 200 ASN K CA  1 
ATOM   20562 C C   . ASN K  1 200 ? 19.530  14.237   -70.031 1.00 101.01 ? 200 ASN K C   1 
ATOM   20563 O O   . ASN K  1 200 ? 19.738  13.613   -68.990 1.00 97.95  ? 200 ASN K O   1 
ATOM   20564 C CB  . ASN K  1 200 ? 18.148  12.957   -71.690 1.00 100.20 ? 200 ASN K CB  1 
ATOM   20565 C CG  . ASN K  1 200 ? 18.176  11.923   -72.799 1.00 92.57  ? 200 ASN K CG  1 
ATOM   20566 O OD1 . ASN K  1 200 ? 19.162  11.805   -73.528 1.00 110.46 ? 200 ASN K OD1 1 
ATOM   20567 N ND2 . ASN K  1 200 ? 17.096  11.164   -72.930 1.00 93.00  ? 200 ASN K ND2 1 
ATOM   20568 N N   . ALA K  1 201 ? 19.294  15.545   -70.051 1.00 94.55  ? 201 ALA K N   1 
ATOM   20569 C CA  . ALA K  1 201 ? 19.303  16.339   -68.826 1.00 86.52  ? 201 ALA K CA  1 
ATOM   20570 C C   . ALA K  1 201 ? 17.923  16.383   -68.181 1.00 104.14 ? 201 ALA K C   1 
ATOM   20571 O O   . ALA K  1 201 ? 17.788  16.246   -66.965 1.00 99.58  ? 201 ALA K O   1 
ATOM   20572 C CB  . ALA K  1 201 ? 19.805  17.748   -69.107 1.00 104.26 ? 201 ALA K CB  1 
ATOM   20573 N N   . ASP K  1 202 ? 16.899  16.578   -69.003 1.00 113.66 ? 202 ASP K N   1 
ATOM   20574 C CA  . ASP K  1 202 ? 15.529  16.630   -68.515 1.00 110.11 ? 202 ASP K CA  1 
ATOM   20575 C C   . ASP K  1 202 ? 14.804  15.335   -68.865 1.00 101.52 ? 202 ASP K C   1 
ATOM   20576 O O   . ASP K  1 202 ? 14.305  15.175   -69.978 1.00 105.96 ? 202 ASP K O   1 
ATOM   20577 C CB  . ASP K  1 202 ? 14.798  17.830   -69.116 1.00 121.78 ? 202 ASP K CB  1 
ATOM   20578 C CG  . ASP K  1 202 ? 13.582  18.235   -68.309 1.00 129.48 ? 202 ASP K CG  1 
ATOM   20579 O OD1 . ASP K  1 202 ? 13.679  18.273   -67.065 1.00 129.06 ? 202 ASP K OD1 1 
ATOM   20580 O OD2 . ASP K  1 202 ? 12.531  18.522   -68.920 1.00 132.80 ? 202 ASP K OD2 1 
ATOM   20581 N N   . THR K  1 203 ? 14.753  14.414   -67.908 1.00 91.08  ? 203 THR K N   1 
ATOM   20582 C CA  . THR K  1 203 ? 14.166  13.100   -68.142 1.00 71.63  ? 203 THR K CA  1 
ATOM   20583 C C   . THR K  1 203 ? 12.940  12.851   -67.270 1.00 65.76  ? 203 THR K C   1 
ATOM   20584 O O   . THR K  1 203 ? 12.618  13.644   -66.386 1.00 77.28  ? 203 THR K O   1 
ATOM   20585 C CB  . THR K  1 203 ? 15.185  11.978   -67.874 1.00 73.00  ? 203 THR K CB  1 
ATOM   20586 O OG1 . THR K  1 203 ? 15.571  12.007   -66.495 1.00 71.57  ? 203 THR K OG1 1 
ATOM   20587 C CG2 . THR K  1 203 ? 16.417  12.154   -68.745 1.00 84.37  ? 203 THR K CG2 1 
ATOM   20588 N N   . TYR K  1 204 ? 12.265  11.737   -67.532 1.00 64.22  ? 204 TYR K N   1 
ATOM   20589 C CA  . TYR K  1 204 ? 11.094  11.333   -66.768 1.00 68.54  ? 204 TYR K CA  1 
ATOM   20590 C C   . TYR K  1 204 ? 10.915  9.828    -66.878 1.00 67.41  ? 204 TYR K C   1 
ATOM   20591 O O   . TYR K  1 204 ? 11.357  9.215    -67.847 1.00 62.20  ? 204 TYR K O   1 
ATOM   20592 C CB  . TYR K  1 204 ? 9.839   12.025   -67.307 1.00 65.09  ? 204 TYR K CB  1 
ATOM   20593 C CG  . TYR K  1 204 ? 9.325   11.440   -68.610 1.00 70.61  ? 204 TYR K CG  1 
ATOM   20594 C CD1 . TYR K  1 204 ? 8.368   10.430   -68.615 1.00 66.18  ? 204 TYR K CD1 1 
ATOM   20595 C CD2 . TYR K  1 204 ? 9.798   11.896   -69.833 1.00 77.36  ? 204 TYR K CD2 1 
ATOM   20596 C CE1 . TYR K  1 204 ? 7.899   9.892    -69.804 1.00 73.27  ? 204 TYR K CE1 1 
ATOM   20597 C CE2 . TYR K  1 204 ? 9.335   11.366   -71.025 1.00 84.88  ? 204 TYR K CE2 1 
ATOM   20598 C CZ  . TYR K  1 204 ? 8.385   10.364   -71.005 1.00 86.18  ? 204 TYR K CZ  1 
ATOM   20599 O OH  . TYR K  1 204 ? 7.920   9.832    -72.188 1.00 87.49  ? 204 TYR K OH  1 
ATOM   20600 N N   . VAL K  1 205 ? 10.266  9.237    -65.882 1.00 56.34  ? 205 VAL K N   1 
ATOM   20601 C CA  . VAL K  1 205 ? 9.852   7.843    -65.971 1.00 57.23  ? 205 VAL K CA  1 
ATOM   20602 C C   . VAL K  1 205 ? 8.416   7.697    -65.501 1.00 56.79  ? 205 VAL K C   1 
ATOM   20603 O O   . VAL K  1 205 ? 8.000   8.348    -64.546 1.00 55.88  ? 205 VAL K O   1 
ATOM   20604 C CB  . VAL K  1 205 ? 10.776  6.892    -65.180 1.00 56.97  ? 205 VAL K CB  1 
ATOM   20605 C CG1 . VAL K  1 205 ? 11.768  7.682    -64.331 1.00 63.19  ? 205 VAL K CG1 1 
ATOM   20606 C CG2 . VAL K  1 205 ? 9.953   5.925    -64.341 1.00 42.96  ? 205 VAL K CG2 1 
ATOM   20607 N N   . PHE K  1 206 ? 7.671   6.827    -66.172 1.00 51.05  ? 206 PHE K N   1 
ATOM   20608 C CA  . PHE K  1 206 ? 6.254   6.650    -65.895 1.00 53.80  ? 206 PHE K CA  1 
ATOM   20609 C C   . PHE K  1 206 ? 5.881   5.178    -65.775 1.00 61.43  ? 206 PHE K C   1 
ATOM   20610 O O   . PHE K  1 206 ? 6.178   4.378    -66.661 1.00 63.56  ? 206 PHE K O   1 
ATOM   20611 C CB  . PHE K  1 206 ? 5.425   7.309    -66.998 1.00 60.61  ? 206 PHE K CB  1 
ATOM   20612 C CG  . PHE K  1 206 ? 3.969   6.937    -66.972 1.00 70.73  ? 206 PHE K CG  1 
ATOM   20613 C CD1 . PHE K  1 206 ? 3.490   5.900    -67.758 1.00 65.95  ? 206 PHE K CD1 1 
ATOM   20614 C CD2 . PHE K  1 206 ? 3.077   7.628    -66.170 1.00 69.33  ? 206 PHE K CD2 1 
ATOM   20615 C CE1 . PHE K  1 206 ? 2.150   5.557    -67.740 1.00 63.34  ? 206 PHE K CE1 1 
ATOM   20616 C CE2 . PHE K  1 206 ? 1.736   7.290    -66.148 1.00 60.78  ? 206 PHE K CE2 1 
ATOM   20617 C CZ  . PHE K  1 206 ? 1.273   6.253    -66.933 1.00 72.48  ? 206 PHE K CZ  1 
ATOM   20618 N N   . VAL K  1 207 ? 5.223   4.830    -64.674 1.00 53.08  ? 207 VAL K N   1 
ATOM   20619 C CA  . VAL K  1 207 ? 4.790   3.459    -64.439 1.00 57.61  ? 207 VAL K CA  1 
ATOM   20620 C C   . VAL K  1 207 ? 3.279   3.414    -64.262 1.00 65.21  ? 207 VAL K C   1 
ATOM   20621 O O   . VAL K  1 207 ? 2.728   4.100    -63.402 1.00 72.38  ? 207 VAL K O   1 
ATOM   20622 C CB  . VAL K  1 207 ? 5.460   2.864    -63.186 1.00 54.82  ? 207 VAL K CB  1 
ATOM   20623 C CG1 . VAL K  1 207 ? 4.983   1.437    -62.952 1.00 48.76  ? 207 VAL K CG1 1 
ATOM   20624 C CG2 . VAL K  1 207 ? 6.974   2.911    -63.321 1.00 42.84  ? 207 VAL K CG2 1 
ATOM   20625 N N   . GLY K  1 208 ? 2.610   2.606    -65.076 1.00 62.30  ? 208 GLY K N   1 
ATOM   20626 C CA  . GLY K  1 208 ? 1.162   2.536    -65.030 1.00 63.96  ? 208 GLY K CA  1 
ATOM   20627 C C   . GLY K  1 208 ? 0.586   1.150    -65.237 1.00 64.10  ? 208 GLY K C   1 
ATOM   20628 O O   . GLY K  1 208 ? 1.116   0.346    -66.001 1.00 67.70  ? 208 GLY K O   1 
ATOM   20629 N N   . SER K  1 209 ? -0.507  0.874    -64.535 1.00 55.66  ? 209 SER K N   1 
ATOM   20630 C CA  . SER K  1 209 ? -1.280  -0.342   -64.741 1.00 59.07  ? 209 SER K CA  1 
ATOM   20631 C C   . SER K  1 209 ? -2.748  0.053    -64.842 1.00 64.68  ? 209 SER K C   1 
ATOM   20632 O O   . SER K  1 209 ? -3.063  1.216    -65.091 1.00 67.90  ? 209 SER K O   1 
ATOM   20633 C CB  . SER K  1 209 ? -1.071  -1.323   -63.587 1.00 67.78  ? 209 SER K CB  1 
ATOM   20634 O OG  . SER K  1 209 ? -1.662  -0.841   -62.393 1.00 54.23  ? 209 SER K OG  1 
ATOM   20635 N N   . SER K  1 210 ? -3.646  -0.906   -64.647 1.00 73.05  ? 210 SER K N   1 
ATOM   20636 C CA  . SER K  1 210 ? -5.074  -0.608   -64.669 1.00 83.88  ? 210 SER K CA  1 
ATOM   20637 C C   . SER K  1 210 ? -5.463  0.276    -63.490 1.00 83.07  ? 210 SER K C   1 
ATOM   20638 O O   . SER K  1 210 ? -6.454  1.004    -63.547 1.00 66.54  ? 210 SER K O   1 
ATOM   20639 C CB  . SER K  1 210 ? -5.901  -1.894   -64.653 1.00 83.64  ? 210 SER K CB  1 
ATOM   20640 O OG  . SER K  1 210 ? -5.736  -2.624   -65.855 1.00 104.91 ? 210 SER K OG  1 
ATOM   20641 N N   . ARG K  1 211 ? -4.671  0.213    -62.425 1.00 78.01  ? 211 ARG K N   1 
ATOM   20642 C CA  . ARG K  1 211 ? -4.977  0.938    -61.197 1.00 85.99  ? 211 ARG K CA  1 
ATOM   20643 C C   . ARG K  1 211 ? -3.876  1.931    -60.829 1.00 87.07  ? 211 ARG K C   1 
ATOM   20644 O O   . ARG K  1 211 ? -4.153  3.015    -60.318 1.00 96.57  ? 211 ARG K O   1 
ATOM   20645 C CB  . ARG K  1 211 ? -5.197  -0.050   -60.050 1.00 83.66  ? 211 ARG K CB  1 
ATOM   20646 C CG  . ARG K  1 211 ? -3.955  -0.845   -59.679 1.00 103.28 ? 211 ARG K CG  1 
ATOM   20647 C CD  . ARG K  1 211 ? -4.306  -2.119   -58.930 1.00 112.45 ? 211 ARG K CD  1 
ATOM   20648 N NE  . ARG K  1 211 ? -5.314  -1.894   -57.898 1.00 129.28 ? 211 ARG K NE  1 
ATOM   20649 C CZ  . ARG K  1 211 ? -5.585  -2.754   -56.921 1.00 123.02 ? 211 ARG K CZ  1 
ATOM   20650 N NH1 . ARG K  1 211 ? -4.913  -3.894   -56.834 1.00 114.52 ? 211 ARG K NH1 1 
ATOM   20651 N NH2 . ARG K  1 211 ? -6.520  -2.470   -56.026 1.00 109.29 ? 211 ARG K NH2 1 
ATOM   20652 N N   . TYR K  1 212 ? -2.629  1.555    -61.091 1.00 83.61  ? 212 TYR K N   1 
ATOM   20653 C CA  . TYR K  1 212 ? -1.487  2.391    -60.741 1.00 64.86  ? 212 TYR K CA  1 
ATOM   20654 C C   . TYR K  1 212 ? -1.138  3.343    -61.880 1.00 66.92  ? 212 TYR K C   1 
ATOM   20655 O O   . TYR K  1 212 ? -1.290  3.001    -63.052 1.00 75.05  ? 212 TYR K O   1 
ATOM   20656 C CB  . TYR K  1 212 ? -0.279  1.517    -60.392 1.00 52.74  ? 212 TYR K CB  1 
ATOM   20657 C CG  . TYR K  1 212 ? 0.869   2.270    -59.757 1.00 63.79  ? 212 TYR K CG  1 
ATOM   20658 C CD1 . TYR K  1 212 ? 1.016   2.314    -58.376 1.00 60.74  ? 212 TYR K CD1 1 
ATOM   20659 C CD2 . TYR K  1 212 ? 1.807   2.933    -60.537 1.00 69.51  ? 212 TYR K CD2 1 
ATOM   20660 C CE1 . TYR K  1 212 ? 2.064   2.999    -57.791 1.00 63.76  ? 212 TYR K CE1 1 
ATOM   20661 C CE2 . TYR K  1 212 ? 2.858   3.622    -59.960 1.00 61.46  ? 212 TYR K CE2 1 
ATOM   20662 C CZ  . TYR K  1 212 ? 2.982   3.651    -58.587 1.00 65.92  ? 212 TYR K CZ  1 
ATOM   20663 O OH  . TYR K  1 212 ? 4.026   4.335    -58.008 1.00 58.48  ? 212 TYR K OH  1 
ATOM   20664 N N   . SER K  1 213 ? -0.675  4.539    -61.531 1.00 65.45  ? 213 SER K N   1 
ATOM   20665 C CA  . SER K  1 213 ? -0.289  5.531    -62.529 1.00 64.60  ? 213 SER K CA  1 
ATOM   20666 C C   . SER K  1 213 ? 0.483   6.629    -61.804 1.00 58.53  ? 213 SER K C   1 
ATOM   20667 O O   . SER K  1 213 ? -0.012  7.216    -60.842 1.00 65.80  ? 213 SER K O   1 
ATOM   20668 C CB  . SER K  1 213 ? -1.516  6.028    -63.297 1.00 64.28  ? 213 SER K CB  1 
ATOM   20669 O OG  . SER K  1 213 ? -1.145  6.937    -64.318 1.00 61.59  ? 213 SER K OG  1 
ATOM   20670 N N   . LYS K  1 214 ? 1.696   6.905    -62.271 1.00 53.80  ? 214 LYS K N   1 
ATOM   20671 C CA  . LYS K  1 214 ? 2.509   7.959    -61.675 1.00 54.54  ? 214 LYS K CA  1 
ATOM   20672 C C   . LYS K  1 214 ? 3.707   8.290    -62.559 1.00 63.46  ? 214 LYS K C   1 
ATOM   20673 O O   . LYS K  1 214 ? 4.377   7.399    -63.082 1.00 60.00  ? 214 LYS K O   1 
ATOM   20674 C CB  . LYS K  1 214 ? 2.969   7.668    -60.243 1.00 60.69  ? 214 LYS K CB  1 
ATOM   20675 C CG  . LYS K  1 214 ? 3.730   8.811    -59.590 1.00 67.02  ? 214 LYS K CG  1 
ATOM   20676 C CD  . LYS K  1 214 ? 3.219   9.085    -58.184 1.00 88.70  ? 214 LYS K CD  1 
ATOM   20677 C CE  . LYS K  1 214 ? 4.227   8.655    -57.133 1.00 88.05  ? 214 LYS K CE  1 
ATOM   20678 N NZ  . LYS K  1 214 ? 5.457   9.495    -57.175 1.00 95.85  ? 214 LYS K NZ  1 
ATOM   20679 N N   . LYS K  1 215 ? 3.962   9.584    -62.720 1.00 64.36  ? 215 LYS K N   1 
ATOM   20680 C CA  . LYS K  1 215 ? 5.092   10.067   -63.501 1.00 67.76  ? 215 LYS K CA  1 
ATOM   20681 C C   . LYS K  1 215 ? 6.165   10.600   -62.560 1.00 60.21  ? 215 LYS K C   1 
ATOM   20682 O O   . LYS K  1 215 ? 5.876   11.390   -61.662 1.00 62.75  ? 215 LYS K O   1 
ATOM   20683 C CB  . LYS K  1 215 ? 4.634   11.167   -64.460 1.00 77.05  ? 215 LYS K CB  1 
ATOM   20684 C CG  . LYS K  1 215 ? 5.696   11.644   -65.437 1.00 74.20  ? 215 LYS K CG  1 
ATOM   20685 C CD  . LYS K  1 215 ? 5.111   12.648   -66.418 1.00 77.23  ? 215 LYS K CD  1 
ATOM   20686 C CE  . LYS K  1 215 ? 6.065   12.929   -67.566 1.00 93.25  ? 215 LYS K CE  1 
ATOM   20687 N NZ  . LYS K  1 215 ? 5.424   13.762   -68.622 1.00 90.70  ? 215 LYS K NZ  1 
ATOM   20688 N N   . PHE K  1 216 ? 7.403   10.163   -62.765 1.00 59.37  ? 216 PHE K N   1 
ATOM   20689 C CA  . PHE K  1 216 ? 8.498   10.535   -61.877 1.00 59.12  ? 216 PHE K CA  1 
ATOM   20690 C C   . PHE K  1 216 ? 9.469   11.520   -62.519 1.00 58.16  ? 216 PHE K C   1 
ATOM   20691 O O   . PHE K  1 216 ? 9.885   11.346   -63.665 1.00 55.04  ? 216 PHE K O   1 
ATOM   20692 C CB  . PHE K  1 216 ? 9.260   9.289    -61.420 1.00 64.09  ? 216 PHE K CB  1 
ATOM   20693 C CG  . PHE K  1 216 ? 8.395   8.258    -60.756 1.00 66.66  ? 216 PHE K CG  1 
ATOM   20694 C CD1 . PHE K  1 216 ? 7.809   7.246    -61.496 1.00 57.56  ? 216 PHE K CD1 1 
ATOM   20695 C CD2 . PHE K  1 216 ? 8.170   8.300    -59.390 1.00 53.43  ? 216 PHE K CD2 1 
ATOM   20696 C CE1 . PHE K  1 216 ? 7.013   6.294    -60.888 1.00 54.57  ? 216 PHE K CE1 1 
ATOM   20697 C CE2 . PHE K  1 216 ? 7.375   7.351    -58.776 1.00 57.42  ? 216 PHE K CE2 1 
ATOM   20698 C CZ  . PHE K  1 216 ? 6.796   6.347    -59.526 1.00 58.79  ? 216 PHE K CZ  1 
ATOM   20699 N N   . LYS K  1 217 ? 9.826   12.554   -61.766 1.00 68.39  ? 217 LYS K N   1 
ATOM   20700 C CA  . LYS K  1 217 ? 10.838  13.509   -62.196 1.00 63.85  ? 217 LYS K CA  1 
ATOM   20701 C C   . LYS K  1 217 ? 12.067  13.406   -61.302 1.00 60.23  ? 217 LYS K C   1 
ATOM   20702 O O   . LYS K  1 217 ? 11.982  13.639   -60.097 1.00 64.80  ? 217 LYS K O   1 
ATOM   20703 C CB  . LYS K  1 217 ? 10.285  14.935   -62.168 1.00 79.10  ? 217 LYS K CB  1 
ATOM   20704 C CG  . LYS K  1 217 ? 9.810   15.446   -63.518 1.00 77.65  ? 217 LYS K CG  1 
ATOM   20705 C CD  . LYS K  1 217 ? 10.968  15.564   -64.496 1.00 85.89  ? 217 LYS K CD  1 
ATOM   20706 C CE  . LYS K  1 217 ? 10.507  16.114   -65.836 1.00 104.87 ? 217 LYS K CE  1 
ATOM   20707 N NZ  . LYS K  1 217 ? 11.641  16.278   -66.787 1.00 113.52 ? 217 LYS K NZ  1 
ATOM   20708 N N   . PRO K  1 218 ? 13.215  13.048   -61.893 1.00 66.26  ? 218 PRO K N   1 
ATOM   20709 C CA  . PRO K  1 218 ? 14.472  12.907   -61.150 1.00 68.79  ? 218 PRO K CA  1 
ATOM   20710 C C   . PRO K  1 218 ? 14.842  14.182   -60.397 1.00 67.76  ? 218 PRO K C   1 
ATOM   20711 O O   . PRO K  1 218 ? 14.909  15.255   -60.995 1.00 66.57  ? 218 PRO K O   1 
ATOM   20712 C CB  . PRO K  1 218 ? 15.498  12.633   -62.253 1.00 66.09  ? 218 PRO K CB  1 
ATOM   20713 C CG  . PRO K  1 218 ? 14.707  12.035   -63.363 1.00 70.33  ? 218 PRO K CG  1 
ATOM   20714 C CD  . PRO K  1 218 ? 13.376  12.723   -63.320 1.00 71.95  ? 218 PRO K CD  1 
ATOM   20715 N N   . GLU K  1 219 ? 15.077  14.057   -59.095 1.00 73.44  ? 219 GLU K N   1 
ATOM   20716 C CA  . GLU K  1 219 ? 15.462  15.195   -58.270 1.00 64.63  ? 219 GLU K CA  1 
ATOM   20717 C C   . GLU K  1 219 ? 16.974  15.213   -58.073 1.00 63.34  ? 219 GLU K C   1 
ATOM   20718 O O   . GLU K  1 219 ? 17.504  14.533   -57.196 1.00 58.17  ? 219 GLU K O   1 
ATOM   20719 C CB  . GLU K  1 219 ? 14.746  15.141   -56.920 1.00 67.02  ? 219 GLU K CB  1 
ATOM   20720 C CG  . GLU K  1 219 ? 13.229  15.072   -57.032 1.00 75.48  ? 219 GLU K CG  1 
ATOM   20721 C CD  . GLU K  1 219 ? 12.542  15.002   -55.681 1.00 88.87  ? 219 GLU K CD  1 
ATOM   20722 O OE1 . GLU K  1 219 ? 13.247  14.885   -54.657 1.00 80.00  ? 219 GLU K OE1 1 
ATOM   20723 O OE2 . GLU K  1 219 ? 11.294  15.062   -55.645 1.00 89.66  ? 219 GLU K OE2 1 
ATOM   20724 N N   . ILE K  1 220 ? 17.661  15.998   -58.897 1.00 78.98  ? 220 ILE K N   1 
ATOM   20725 C CA  . ILE K  1 220 ? 19.120  16.034   -58.898 1.00 75.33  ? 220 ILE K CA  1 
ATOM   20726 C C   . ILE K  1 220 ? 19.684  17.019   -57.877 1.00 66.05  ? 220 ILE K C   1 
ATOM   20727 O O   . ILE K  1 220 ? 19.445  18.224   -57.964 1.00 64.79  ? 220 ILE K O   1 
ATOM   20728 C CB  . ILE K  1 220 ? 19.660  16.392   -60.295 1.00 60.61  ? 220 ILE K CB  1 
ATOM   20729 C CG1 . ILE K  1 220 ? 19.176  15.370   -61.326 1.00 65.20  ? 220 ILE K CG1 1 
ATOM   20730 C CG2 . ILE K  1 220 ? 21.177  16.467   -60.277 1.00 68.81  ? 220 ILE K CG2 1 
ATOM   20731 C CD1 . ILE K  1 220 ? 19.402  15.791   -62.760 1.00 81.18  ? 220 ILE K CD1 1 
ATOM   20732 N N   . ALA K  1 221 ? 20.439  16.497   -56.915 1.00 55.72  ? 221 ALA K N   1 
ATOM   20733 C CA  . ALA K  1 221 ? 21.051  17.323   -55.879 1.00 54.79  ? 221 ALA K CA  1 
ATOM   20734 C C   . ALA K  1 221 ? 22.047  16.522   -55.045 1.00 68.97  ? 221 ALA K C   1 
ATOM   20735 O O   . ALA K  1 221 ? 22.154  15.305   -55.189 1.00 73.56  ? 221 ALA K O   1 
ATOM   20736 C CB  . ALA K  1 221 ? 19.981  17.934   -54.985 1.00 67.67  ? 221 ALA K CB  1 
ATOM   20737 N N   . ILE K  1 222 ? 22.771  17.214   -54.170 1.00 75.79  ? 222 ILE K N   1 
ATOM   20738 C CA  . ILE K  1 222 ? 23.774  16.572   -53.328 1.00 78.01  ? 222 ILE K CA  1 
ATOM   20739 C C   . ILE K  1 222 ? 23.232  16.248   -51.939 1.00 74.76  ? 222 ILE K C   1 
ATOM   20740 O O   . ILE K  1 222 ? 22.956  17.147   -51.145 1.00 81.79  ? 222 ILE K O   1 
ATOM   20741 C CB  . ILE K  1 222 ? 25.031  17.451   -53.176 1.00 90.89  ? 222 ILE K CB  1 
ATOM   20742 C CG1 . ILE K  1 222 ? 25.642  17.756   -54.545 1.00 84.81  ? 222 ILE K CG1 1 
ATOM   20743 C CG2 . ILE K  1 222 ? 26.049  16.772   -52.272 1.00 78.31  ? 222 ILE K CG2 1 
ATOM   20744 C CD1 . ILE K  1 222 ? 26.097  16.527   -55.297 1.00 88.20  ? 222 ILE K CD1 1 
ATOM   20745 N N   . ARG K  1 223 ? 23.081  14.958   -51.654 1.00 66.07  ? 223 ARG K N   1 
ATOM   20746 C CA  . ARG K  1 223 ? 22.655  14.512   -50.333 1.00 76.50  ? 223 ARG K CA  1 
ATOM   20747 C C   . ARG K  1 223 ? 23.861  14.109   -49.495 1.00 72.82  ? 223 ARG K C   1 
ATOM   20748 O O   . ARG K  1 223 ? 24.871  13.656   -50.035 1.00 79.96  ? 223 ARG K O   1 
ATOM   20749 C CB  . ARG K  1 223 ? 21.690  13.327   -50.439 1.00 71.32  ? 223 ARG K CB  1 
ATOM   20750 C CG  . ARG K  1 223 ? 20.320  13.655   -51.011 1.00 62.52  ? 223 ARG K CG  1 
ATOM   20751 C CD  . ARG K  1 223 ? 20.315  13.619   -52.531 1.00 61.47  ? 223 ARG K CD  1 
ATOM   20752 N NE  . ARG K  1 223 ? 18.956  13.530   -53.058 1.00 57.01  ? 223 ARG K NE  1 
ATOM   20753 C CZ  . ARG K  1 223 ? 18.652  13.525   -54.351 1.00 57.20  ? 223 ARG K CZ  1 
ATOM   20754 N NH1 . ARG K  1 223 ? 19.612  13.609   -55.261 1.00 64.90  ? 223 ARG K NH1 1 
ATOM   20755 N NH2 . ARG K  1 223 ? 17.385  13.439   -54.735 1.00 66.28  ? 223 ARG K NH2 1 
ATOM   20756 N N   . PRO K  1 224 ? 23.761  14.276   -48.167 1.00 66.65  ? 224 PRO K N   1 
ATOM   20757 C CA  . PRO K  1 224 ? 24.826  13.845   -47.259 1.00 68.10  ? 224 PRO K CA  1 
ATOM   20758 C C   . PRO K  1 224 ? 25.167  12.388   -47.508 1.00 80.33  ? 224 PRO K C   1 
ATOM   20759 O O   . PRO K  1 224 ? 24.274  11.544   -47.563 1.00 83.46  ? 224 PRO K O   1 
ATOM   20760 C CB  . PRO K  1 224 ? 24.191  14.002   -45.878 1.00 70.05  ? 224 PRO K CB  1 
ATOM   20761 C CG  . PRO K  1 224 ? 23.183  15.071   -46.055 1.00 78.24  ? 224 PRO K CG  1 
ATOM   20762 C CD  . PRO K  1 224 ? 22.638  14.896   -47.444 1.00 76.16  ? 224 PRO K CD  1 
ATOM   20763 N N   . LYS K  1 225 ? 26.453  12.102   -47.655 1.00 92.35  ? 225 LYS K N   1 
ATOM   20764 C CA  . LYS K  1 225 ? 26.901  10.765   -48.009 1.00 81.53  ? 225 LYS K CA  1 
ATOM   20765 C C   . LYS K  1 225 ? 26.424  9.672    -47.076 1.00 73.38  ? 225 LYS K C   1 
ATOM   20766 O O   . LYS K  1 225 ? 26.681  9.699    -45.872 1.00 78.67  ? 225 LYS K O   1 
ATOM   20767 C CB  . LYS K  1 225 ? 28.416  10.711   -48.050 1.00 99.81  ? 225 LYS K CB  1 
ATOM   20768 C CG  . LYS K  1 225 ? 29.009  11.440   -49.197 1.00 115.80 ? 225 LYS K CG  1 
ATOM   20769 C CD  . LYS K  1 225 ? 30.491  11.218   -49.210 1.00 132.29 ? 225 LYS K CD  1 
ATOM   20770 C CE  . LYS K  1 225 ? 31.061  11.738   -50.487 1.00 148.64 ? 225 LYS K CE  1 
ATOM   20771 N NZ  . LYS K  1 225 ? 30.322  11.173   -51.648 1.00 144.59 ? 225 LYS K NZ  1 
ATOM   20772 N N   . VAL K  1 226 ? 25.747  8.695    -47.658 1.00 65.38  ? 226 VAL K N   1 
ATOM   20773 C CA  . VAL K  1 226 ? 25.425  7.466    -46.965 1.00 75.91  ? 226 VAL K CA  1 
ATOM   20774 C C   . VAL K  1 226 ? 25.961  6.329    -47.821 1.00 82.60  ? 226 VAL K C   1 
ATOM   20775 O O   . VAL K  1 226 ? 25.457  6.079    -48.912 1.00 72.41  ? 226 VAL K O   1 
ATOM   20776 C CB  . VAL K  1 226 ? 23.913  7.322    -46.778 1.00 75.23  ? 226 VAL K CB  1 
ATOM   20777 C CG1 . VAL K  1 226 ? 23.593  6.026    -46.062 1.00 67.45  ? 226 VAL K CG1 1 
ATOM   20778 C CG2 . VAL K  1 226 ? 23.367  8.518    -46.008 1.00 77.02  ? 226 VAL K CG2 1 
ATOM   20779 N N   . ARG K  1 227 ? 27.005  5.663    -47.340 1.00 92.88  ? 227 ARG K N   1 
ATOM   20780 C CA  . ARG K  1 227 ? 27.654  4.607    -48.109 1.00 83.23  ? 227 ARG K CA  1 
ATOM   20781 C C   . ARG K  1 227 ? 28.301  5.154    -49.375 1.00 91.13  ? 227 ARG K C   1 
ATOM   20782 O O   . ARG K  1 227 ? 28.214  4.539    -50.438 1.00 93.20  ? 227 ARG K O   1 
ATOM   20783 C CB  . ARG K  1 227 ? 26.651  3.518    -48.480 1.00 66.99  ? 227 ARG K CB  1 
ATOM   20784 C CG  . ARG K  1 227 ? 26.218  2.665    -47.318 1.00 74.51  ? 227 ARG K CG  1 
ATOM   20785 C CD  . ARG K  1 227 ? 25.026  1.814    -47.694 1.00 76.83  ? 227 ARG K CD  1 
ATOM   20786 N NE  . ARG K  1 227 ? 25.161  0.452    -47.195 1.00 71.47  ? 227 ARG K NE  1 
ATOM   20787 C CZ  . ARG K  1 227 ? 25.906  -0.475   -47.782 1.00 83.57  ? 227 ARG K CZ  1 
ATOM   20788 N NH1 . ARG K  1 227 ? 26.583  -0.175   -48.878 1.00 89.58  ? 227 ARG K NH1 1 
ATOM   20789 N NH2 . ARG K  1 227 ? 25.980  -1.695   -47.274 1.00 82.70  ? 227 ARG K NH2 1 
ATOM   20790 N N   . ASP K  1 228 ? 28.935  6.317    -49.254 1.00 95.69  ? 228 ASP K N   1 
ATOM   20791 C CA  . ASP K  1 228 ? 29.693  6.909    -50.354 1.00 108.76 ? 228 ASP K CA  1 
ATOM   20792 C C   . ASP K  1 228 ? 28.832  7.531    -51.452 1.00 104.74 ? 228 ASP K C   1 
ATOM   20793 O O   . ASP K  1 228 ? 29.355  8.179    -52.359 1.00 116.11 ? 228 ASP K O   1 
ATOM   20794 C CB  . ASP K  1 228 ? 30.654  5.884    -50.962 1.00 136.89 ? 228 ASP K CB  1 
ATOM   20795 C CG  . ASP K  1 228 ? 32.046  5.971    -50.373 1.00 154.94 ? 228 ASP K CG  1 
ATOM   20796 O OD1 . ASP K  1 228 ? 32.707  7.011    -50.573 1.00 152.71 ? 228 ASP K OD1 1 
ATOM   20797 O OD2 . ASP K  1 228 ? 32.480  5.002    -49.716 1.00 156.57 ? 228 ASP K OD2 1 
ATOM   20798 N N   . GLN K  1 229 ? 27.520  7.341    -51.373 1.00 86.82  ? 229 GLN K N   1 
ATOM   20799 C CA  . GLN K  1 229 ? 26.625  7.868    -52.397 1.00 84.54  ? 229 GLN K CA  1 
ATOM   20800 C C   . GLN K  1 229 ? 25.992  9.186    -51.970 1.00 80.45  ? 229 GLN K C   1 
ATOM   20801 O O   . GLN K  1 229 ? 25.367  9.273    -50.914 1.00 87.73  ? 229 GLN K O   1 
ATOM   20802 C CB  . GLN K  1 229 ? 25.530  6.854    -52.734 1.00 73.49  ? 229 GLN K CB  1 
ATOM   20803 C CG  . GLN K  1 229 ? 26.037  5.438    -52.945 1.00 68.35  ? 229 GLN K CG  1 
ATOM   20804 C CD  . GLN K  1 229 ? 27.090  5.346    -54.030 1.00 80.20  ? 229 GLN K CD  1 
ATOM   20805 O OE1 . GLN K  1 229 ? 27.051  6.081    -55.017 1.00 82.08  ? 229 GLN K OE1 1 
ATOM   20806 N NE2 . GLN K  1 229 ? 28.039  4.433    -53.854 1.00 94.15  ? 229 GLN K NE2 1 
ATOM   20807 N N   . GLU K  1 230 ? 26.159  10.212   -52.796 1.00 77.39  ? 230 GLU K N   1 
ATOM   20808 C CA  . GLU K  1 230 ? 25.525  11.497   -52.543 1.00 81.56  ? 230 GLU K CA  1 
ATOM   20809 C C   . GLU K  1 230 ? 24.207  11.577   -53.292 1.00 72.64  ? 230 GLU K C   1 
ATOM   20810 O O   . GLU K  1 230 ? 23.422  12.504   -53.096 1.00 76.17  ? 230 GLU K O   1 
ATOM   20811 C CB  . GLU K  1 230 ? 26.435  12.641   -52.969 1.00 100.85 ? 230 GLU K CB  1 
ATOM   20812 C CG  . GLU K  1 230 ? 27.678  12.774   -52.126 1.00 126.73 ? 230 GLU K CG  1 
ATOM   20813 C CD  . GLU K  1 230 ? 28.559  13.903   -52.598 1.00 144.58 ? 230 GLU K CD  1 
ATOM   20814 O OE1 . GLU K  1 230 ? 28.445  14.277   -53.784 1.00 146.75 ? 230 GLU K OE1 1 
ATOM   20815 O OE2 . GLU K  1 230 ? 29.358  14.415   -51.787 1.00 152.36 ? 230 GLU K OE2 1 
ATOM   20816 N N   . GLY K  1 231 ? 23.980  10.600   -54.162 1.00 57.14  ? 231 GLY K N   1 
ATOM   20817 C CA  . GLY K  1 231 ? 22.712  10.473   -54.850 1.00 58.20  ? 231 GLY K CA  1 
ATOM   20818 C C   . GLY K  1 231 ? 21.796  9.544    -54.081 1.00 62.67  ? 231 GLY K C   1 
ATOM   20819 O O   . GLY K  1 231 ? 22.229  8.854    -53.158 1.00 63.78  ? 231 GLY K O   1 
ATOM   20820 N N   . ARG K  1 232 ? 20.523  9.526    -54.458 1.00 61.52  ? 232 ARG K N   1 
ATOM   20821 C CA  . ARG K  1 232 ? 19.548  8.669    -53.798 1.00 50.41  ? 232 ARG K CA  1 
ATOM   20822 C C   . ARG K  1 232 ? 18.856  7.752    -54.795 1.00 50.96  ? 232 ARG K C   1 
ATOM   20823 O O   . ARG K  1 232 ? 18.928  7.964    -56.005 1.00 48.67  ? 232 ARG K O   1 
ATOM   20824 C CB  . ARG K  1 232 ? 18.510  9.511    -53.056 1.00 53.61  ? 232 ARG K CB  1 
ATOM   20825 C CG  . ARG K  1 232 ? 19.044  10.203   -51.815 1.00 53.93  ? 232 ARG K CG  1 
ATOM   20826 C CD  . ARG K  1 232 ? 19.479  9.189    -50.770 1.00 59.72  ? 232 ARG K CD  1 
ATOM   20827 N NE  . ARG K  1 232 ? 20.028  9.830    -49.579 1.00 70.02  ? 232 ARG K NE  1 
ATOM   20828 C CZ  . ARG K  1 232 ? 21.297  10.203   -49.452 1.00 68.66  ? 232 ARG K CZ  1 
ATOM   20829 N NH1 . ARG K  1 232 ? 22.151  10.003   -50.446 1.00 61.42  ? 232 ARG K NH1 1 
ATOM   20830 N NH2 . ARG K  1 232 ? 21.712  10.779   -48.332 1.00 69.76  ? 232 ARG K NH2 1 
ATOM   20831 N N   . MET K  1 233 ? 18.188  6.729    -54.277 1.00 54.26  ? 233 MET K N   1 
ATOM   20832 C CA  . MET K  1 233 ? 17.426  5.810    -55.110 1.00 50.87  ? 233 MET K CA  1 
ATOM   20833 C C   . MET K  1 233 ? 16.149  5.384    -54.395 1.00 59.47  ? 233 MET K C   1 
ATOM   20834 O O   . MET K  1 233 ? 16.190  4.630    -53.423 1.00 53.41  ? 233 MET K O   1 
ATOM   20835 C CB  . MET K  1 233 ? 18.268  4.585    -55.475 1.00 52.26  ? 233 MET K CB  1 
ATOM   20836 C CG  . MET K  1 233 ? 17.594  3.644    -56.463 1.00 55.33  ? 233 MET K CG  1 
ATOM   20837 S SD  . MET K  1 233 ? 18.647  2.271    -56.970 1.00 64.70  ? 233 MET K SD  1 
ATOM   20838 C CE  . MET K  1 233 ? 19.970  3.146    -57.802 1.00 63.51  ? 233 MET K CE  1 
ATOM   20839 N N   . ASN K  1 234 ? 15.014  5.879    -54.877 1.00 56.63  ? 234 ASN K N   1 
ATOM   20840 C CA  . ASN K  1 234 ? 13.725  5.539    -54.290 1.00 53.48  ? 234 ASN K CA  1 
ATOM   20841 C C   . ASN K  1 234 ? 13.171  4.240    -54.860 1.00 46.85  ? 234 ASN K C   1 
ATOM   20842 O O   . ASN K  1 234 ? 13.243  4.000    -56.065 1.00 45.80  ? 234 ASN K O   1 
ATOM   20843 C CB  . ASN K  1 234 ? 12.724  6.678    -54.488 1.00 48.85  ? 234 ASN K CB  1 
ATOM   20844 C CG  . ASN K  1 234 ? 13.093  7.918    -53.701 1.00 43.28  ? 234 ASN K CG  1 
ATOM   20845 O OD1 . ASN K  1 234 ? 14.073  7.925    -52.958 1.00 49.64  ? 234 ASN K OD1 1 
ATOM   20846 N ND2 . ASN K  1 234 ? 12.305  8.975    -53.859 1.00 54.19  ? 234 ASN K ND2 1 
ATOM   20847 N N   . TYR K  1 235 ? 12.620  3.406    -53.986 1.00 39.82  ? 235 TYR K N   1 
ATOM   20848 C CA  . TYR K  1 235 ? 12.110  2.103    -54.390 1.00 40.20  ? 235 TYR K CA  1 
ATOM   20849 C C   . TYR K  1 235 ? 10.590  2.063    -54.325 1.00 43.42  ? 235 TYR K C   1 
ATOM   20850 O O   . TYR K  1 235 ? 9.988   2.429    -53.315 1.00 39.42  ? 235 TYR K O   1 
ATOM   20851 C CB  . TYR K  1 235 ? 12.715  1.004    -53.516 1.00 44.08  ? 235 TYR K CB  1 
ATOM   20852 C CG  . TYR K  1 235 ? 14.222  1.072    -53.442 1.00 55.18  ? 235 TYR K CG  1 
ATOM   20853 C CD1 . TYR K  1 235 ? 14.855  1.745    -52.405 1.00 54.01  ? 235 TYR K CD1 1 
ATOM   20854 C CD2 . TYR K  1 235 ? 15.012  0.481    -54.418 1.00 51.52  ? 235 TYR K CD2 1 
ATOM   20855 C CE1 . TYR K  1 235 ? 16.232  1.817    -52.338 1.00 46.73  ? 235 TYR K CE1 1 
ATOM   20856 C CE2 . TYR K  1 235 ? 16.390  0.548    -54.358 1.00 46.11  ? 235 TYR K CE2 1 
ATOM   20857 C CZ  . TYR K  1 235 ? 16.994  1.217    -53.316 1.00 45.14  ? 235 TYR K CZ  1 
ATOM   20858 O OH  . TYR K  1 235 ? 18.365  1.287    -53.254 1.00 52.78  ? 235 TYR K OH  1 
ATOM   20859 N N   . TYR K  1 236 ? 9.977   1.620    -55.416 1.00 43.89  ? 236 TYR K N   1 
ATOM   20860 C CA  . TYR K  1 236 ? 8.527   1.557    -55.507 1.00 49.25  ? 236 TYR K CA  1 
ATOM   20861 C C   . TYR K  1 236 ? 8.075   0.128    -55.772 1.00 50.56  ? 236 TYR K C   1 
ATOM   20862 O O   . TYR K  1 236 ? 8.874   -0.714   -56.183 1.00 48.79  ? 236 TYR K O   1 
ATOM   20863 C CB  . TYR K  1 236 ? 8.024   2.497    -56.604 1.00 37.02  ? 236 TYR K CB  1 
ATOM   20864 C CG  . TYR K  1 236 ? 8.321   3.954    -56.324 1.00 49.51  ? 236 TYR K CG  1 
ATOM   20865 C CD1 . TYR K  1 236 ? 9.556   4.506    -56.641 1.00 49.99  ? 236 TYR K CD1 1 
ATOM   20866 C CD2 . TYR K  1 236 ? 7.370   4.774    -55.734 1.00 51.10  ? 236 TYR K CD2 1 
ATOM   20867 C CE1 . TYR K  1 236 ? 9.832   5.836    -56.381 1.00 50.76  ? 236 TYR K CE1 1 
ATOM   20868 C CE2 . TYR K  1 236 ? 7.636   6.104    -55.473 1.00 60.19  ? 236 TYR K CE2 1 
ATOM   20869 C CZ  . TYR K  1 236 ? 8.868   6.630    -55.796 1.00 62.94  ? 236 TYR K CZ  1 
ATOM   20870 O OH  . TYR K  1 236 ? 9.135   7.955    -55.534 1.00 59.88  ? 236 TYR K OH  1 
ATOM   20871 N N   . TRP K  1 237 ? 6.797   -0.143   -55.519 1.00 44.81  ? 237 TRP K N   1 
ATOM   20872 C CA  . TRP K  1 237 ? 6.224   -1.464   -55.752 1.00 42.52  ? 237 TRP K CA  1 
ATOM   20873 C C   . TRP K  1 237 ? 4.720   -1.375   -55.978 1.00 40.42  ? 237 TRP K C   1 
ATOM   20874 O O   . TRP K  1 237 ? 4.086   -0.386   -55.615 1.00 44.21  ? 237 TRP K O   1 
ATOM   20875 C CB  . TRP K  1 237 ? 6.518   -2.397   -54.578 1.00 42.00  ? 237 TRP K CB  1 
ATOM   20876 C CG  . TRP K  1 237 ? 5.870   -1.967   -53.299 1.00 39.83  ? 237 TRP K CG  1 
ATOM   20877 C CD1 . TRP K  1 237 ? 6.399   -1.141   -52.351 1.00 37.77  ? 237 TRP K CD1 1 
ATOM   20878 C CD2 . TRP K  1 237 ? 4.568   -2.338   -52.827 1.00 42.33  ? 237 TRP K CD2 1 
ATOM   20879 N NE1 . TRP K  1 237 ? 5.509   -0.976   -51.317 1.00 34.37  ? 237 TRP K NE1 1 
ATOM   20880 C CE2 . TRP K  1 237 ? 4.378   -1.700   -51.585 1.00 41.35  ? 237 TRP K CE2 1 
ATOM   20881 C CE3 . TRP K  1 237 ? 3.547   -3.148   -53.333 1.00 46.80  ? 237 TRP K CE3 1 
ATOM   20882 C CZ2 . TRP K  1 237 ? 3.208   -1.847   -50.842 1.00 47.45  ? 237 TRP K CZ2 1 
ATOM   20883 C CZ3 . TRP K  1 237 ? 2.385   -3.292   -52.593 1.00 44.27  ? 237 TRP K CZ3 1 
ATOM   20884 C CH2 . TRP K  1 237 ? 2.226   -2.645   -51.361 1.00 42.57  ? 237 TRP K CH2 1 
ATOM   20885 N N   . THR K  1 238 ? 4.156   -2.418   -56.579 1.00 40.14  ? 238 THR K N   1 
ATOM   20886 C CA  . THR K  1 238 ? 2.719   -2.487   -56.815 1.00 41.74  ? 238 THR K CA  1 
ATOM   20887 C C   . THR K  1 238 ? 2.295   -3.925   -57.089 1.00 49.47  ? 238 THR K C   1 
ATOM   20888 O O   . THR K  1 238 ? 3.122   -4.771   -57.428 1.00 53.06  ? 238 THR K O   1 
ATOM   20889 C CB  . THR K  1 238 ? 2.294   -1.599   -58.001 1.00 44.56  ? 238 THR K CB  1 
ATOM   20890 O OG1 . THR K  1 238 ? 0.866   -1.607   -58.120 1.00 48.33  ? 238 THR K OG1 1 
ATOM   20891 C CG2 . THR K  1 238 ? 2.909   -2.106   -59.295 1.00 44.21  ? 238 THR K CG2 1 
ATOM   20892 N N   . LEU K  1 239 ? 1.004   -4.199   -56.938 1.00 53.56  ? 239 LEU K N   1 
ATOM   20893 C CA  . LEU K  1 239 ? 0.480   -5.539   -57.176 1.00 57.78  ? 239 LEU K CA  1 
ATOM   20894 C C   . LEU K  1 239 ? -0.388  -5.585   -58.430 1.00 62.58  ? 239 LEU K C   1 
ATOM   20895 O O   . LEU K  1 239 ? -1.506  -5.070   -58.446 1.00 67.44  ? 239 LEU K O   1 
ATOM   20896 C CB  . LEU K  1 239 ? -0.307  -6.033   -55.961 1.00 59.79  ? 239 LEU K CB  1 
ATOM   20897 C CG  . LEU K  1 239 ? 0.515   -6.302   -54.698 1.00 47.93  ? 239 LEU K CG  1 
ATOM   20898 C CD1 . LEU K  1 239 ? -0.391  -6.628   -53.523 1.00 57.65  ? 239 LEU K CD1 1 
ATOM   20899 C CD2 . LEU K  1 239 ? 1.512   -7.425   -54.937 1.00 56.71  ? 239 LEU K CD2 1 
ATOM   20900 N N   . VAL K  1 240 ? 0.138   -6.205   -59.481 1.00 55.52  ? 240 VAL K N   1 
ATOM   20901 C CA  . VAL K  1 240 ? -0.581  -6.321   -60.744 1.00 56.50  ? 240 VAL K CA  1 
ATOM   20902 C C   . VAL K  1 240 ? -1.606  -7.450   -60.674 1.00 59.95  ? 240 VAL K C   1 
ATOM   20903 O O   . VAL K  1 240 ? -1.255  -8.605   -60.427 1.00 61.65  ? 240 VAL K O   1 
ATOM   20904 C CB  . VAL K  1 240 ? 0.382   -6.582   -61.915 1.00 54.04  ? 240 VAL K CB  1 
ATOM   20905 C CG1 . VAL K  1 240 ? -0.366  -6.524   -63.243 1.00 62.59  ? 240 VAL K CG1 1 
ATOM   20906 C CG2 . VAL K  1 240 ? 1.532   -5.584   -61.887 1.00 49.81  ? 240 VAL K CG2 1 
ATOM   20907 N N   . GLU K  1 241 ? -2.874  -7.107   -60.878 1.00 69.06  ? 241 GLU K N   1 
ATOM   20908 C CA  . GLU K  1 241 ? -3.952  -8.088   -60.860 1.00 66.83  ? 241 GLU K CA  1 
ATOM   20909 C C   . GLU K  1 241 ? -3.787  -9.078   -62.005 1.00 69.31  ? 241 GLU K C   1 
ATOM   20910 O O   . GLU K  1 241 ? -3.203  -8.747   -63.036 1.00 69.46  ? 241 GLU K O   1 
ATOM   20911 C CB  . GLU K  1 241 ? -5.311  -7.390   -60.969 1.00 78.80  ? 241 GLU K CB  1 
ATOM   20912 C CG  . GLU K  1 241 ? -5.613  -6.426   -59.833 1.00 89.97  ? 241 GLU K CG  1 
ATOM   20913 C CD  . GLU K  1 241 ? -5.856  -7.133   -58.514 1.00 112.79 ? 241 GLU K CD  1 
ATOM   20914 O OE1 . GLU K  1 241 ? -5.565  -6.538   -57.455 1.00 118.64 ? 241 GLU K OE1 1 
ATOM   20915 O OE2 . GLU K  1 241 ? -6.336  -8.286   -58.535 1.00 116.37 ? 241 GLU K OE2 1 
ATOM   20916 N N   . PRO K  1 242 ? -4.292  -10.306  -61.821 1.00 79.94  ? 242 PRO K N   1 
ATOM   20917 C CA  . PRO K  1 242 ? -4.288  -11.300  -62.898 1.00 74.50  ? 242 PRO K CA  1 
ATOM   20918 C C   . PRO K  1 242 ? -5.047  -10.780  -64.113 1.00 79.60  ? 242 PRO K C   1 
ATOM   20919 O O   . PRO K  1 242 ? -6.177  -10.310  -63.977 1.00 68.59  ? 242 PRO K O   1 
ATOM   20920 C CB  . PRO K  1 242 ? -5.034  -12.485  -62.280 1.00 61.60  ? 242 PRO K CB  1 
ATOM   20921 C CG  . PRO K  1 242 ? -4.836  -12.330  -60.812 1.00 63.23  ? 242 PRO K CG  1 
ATOM   20922 C CD  . PRO K  1 242 ? -4.824  -10.853  -60.562 1.00 68.66  ? 242 PRO K CD  1 
ATOM   20923 N N   . GLY K  1 243 ? -4.429  -10.859  -65.286 1.00 71.55  ? 243 GLY K N   1 
ATOM   20924 C CA  . GLY K  1 243 ? -5.050  -10.377  -66.505 1.00 64.12  ? 243 GLY K CA  1 
ATOM   20925 C C   . GLY K  1 243 ? -4.796  -8.900   -66.734 1.00 68.07  ? 243 GLY K C   1 
ATOM   20926 O O   . GLY K  1 243 ? -5.186  -8.343   -67.759 1.00 82.40  ? 243 GLY K O   1 
ATOM   20927 N N   . ASP K  1 244 ? -4.140  -8.264   -65.770 1.00 66.52  ? 244 ASP K N   1 
ATOM   20928 C CA  . ASP K  1 244 ? -3.784  -6.856   -65.887 1.00 61.86  ? 244 ASP K CA  1 
ATOM   20929 C C   . ASP K  1 244 ? -2.346  -6.725   -66.377 1.00 60.23  ? 244 ASP K C   1 
ATOM   20930 O O   . ASP K  1 244 ? -1.552  -7.654   -66.241 1.00 67.48  ? 244 ASP K O   1 
ATOM   20931 C CB  . ASP K  1 244 ? -3.950  -6.154   -64.538 1.00 60.44  ? 244 ASP K CB  1 
ATOM   20932 C CG  . ASP K  1 244 ? -3.892  -4.643   -64.653 1.00 84.72  ? 244 ASP K CG  1 
ATOM   20933 O OD1 . ASP K  1 244 ? -4.086  -3.964   -63.624 1.00 94.70  ? 244 ASP K OD1 1 
ATOM   20934 O OD2 . ASP K  1 244 ? -3.658  -4.131   -65.767 1.00 79.65  ? 244 ASP K OD2 1 
ATOM   20935 N N   . LYS K  1 245 ? -2.016  -5.574   -66.954 1.00 63.25  ? 245 LYS K N   1 
ATOM   20936 C CA  . LYS K  1 245 ? -0.657  -5.325   -67.417 1.00 71.36  ? 245 LYS K CA  1 
ATOM   20937 C C   . LYS K  1 245 ? -0.098  -4.025   -66.848 1.00 60.37  ? 245 LYS K C   1 
ATOM   20938 O O   . LYS K  1 245 ? -0.841  -3.083   -66.570 1.00 57.83  ? 245 LYS K O   1 
ATOM   20939 C CB  . LYS K  1 245 ? -0.595  -5.302   -68.947 1.00 79.55  ? 245 LYS K CB  1 
ATOM   20940 C CG  . LYS K  1 245 ? -1.121  -4.027   -69.584 1.00 76.45  ? 245 LYS K CG  1 
ATOM   20941 C CD  . LYS K  1 245 ? -0.976  -4.080   -71.098 1.00 72.44  ? 245 LYS K CD  1 
ATOM   20942 C CE  . LYS K  1 245 ? -1.458  -2.795   -71.751 1.00 96.33  ? 245 LYS K CE  1 
ATOM   20943 N NZ  . LYS K  1 245 ? -1.421  -2.885   -73.238 1.00 91.62  ? 245 LYS K NZ  1 
ATOM   20944 N N   . ILE K  1 246 ? 1.218   -3.988   -66.674 1.00 53.40  ? 246 ILE K N   1 
ATOM   20945 C CA  . ILE K  1 246 ? 1.899   -2.807   -66.162 1.00 55.01  ? 246 ILE K CA  1 
ATOM   20946 C C   . ILE K  1 246 ? 2.919   -2.305   -67.178 1.00 61.54  ? 246 ILE K C   1 
ATOM   20947 O O   . ILE K  1 246 ? 3.697   -3.084   -67.728 1.00 58.73  ? 246 ILE K O   1 
ATOM   20948 C CB  . ILE K  1 246 ? 2.596   -3.097   -64.817 1.00 54.37  ? 246 ILE K CB  1 
ATOM   20949 C CG1 . ILE K  1 246 ? 3.294   -1.841   -64.294 1.00 63.10  ? 246 ILE K CG1 1 
ATOM   20950 C CG2 . ILE K  1 246 ? 3.583   -4.246   -64.959 1.00 46.08  ? 246 ILE K CG2 1 
ATOM   20951 C CD1 . ILE K  1 246 ? 4.043   -2.059   -62.999 1.00 48.67  ? 246 ILE K CD1 1 
ATOM   20952 N N   . THR K  1 247 ? 2.906   -1.000   -67.430 1.00 76.32  ? 247 THR K N   1 
ATOM   20953 C CA  . THR K  1 247 ? 3.778   -0.404   -68.436 1.00 71.26  ? 247 THR K CA  1 
ATOM   20954 C C   . THR K  1 247 ? 4.881   0.451    -67.823 1.00 61.68  ? 247 THR K C   1 
ATOM   20955 O O   . THR K  1 247 ? 4.649   1.198    -66.872 1.00 61.37  ? 247 THR K O   1 
ATOM   20956 C CB  . THR K  1 247 ? 2.977   0.459    -69.433 1.00 65.50  ? 247 THR K CB  1 
ATOM   20957 O OG1 . THR K  1 247 ? 2.184   -0.388   -70.273 1.00 79.29  ? 247 THR K OG1 1 
ATOM   20958 C CG2 . THR K  1 247 ? 3.915   1.284    -70.301 1.00 82.16  ? 247 THR K CG2 1 
ATOM   20959 N N   . PHE K  1 248 ? 6.082   0.329    -68.377 1.00 67.27  ? 248 PHE K N   1 
ATOM   20960 C CA  . PHE K  1 248 ? 7.201   1.178    -67.992 1.00 67.65  ? 248 PHE K CA  1 
ATOM   20961 C C   . PHE K  1 248 ? 7.617   2.058    -69.166 1.00 63.07  ? 248 PHE K C   1 
ATOM   20962 O O   . PHE K  1 248 ? 7.702   1.596    -70.304 1.00 66.55  ? 248 PHE K O   1 
ATOM   20963 C CB  . PHE K  1 248 ? 8.382   0.336    -67.509 1.00 51.36  ? 248 PHE K CB  1 
ATOM   20964 C CG  . PHE K  1 248 ? 8.145   -0.337   -66.188 1.00 58.95  ? 248 PHE K CG  1 
ATOM   20965 C CD1 . PHE K  1 248 ? 7.440   -1.526   -66.117 1.00 56.35  ? 248 PHE K CD1 1 
ATOM   20966 C CD2 . PHE K  1 248 ? 8.627   0.221    -65.015 1.00 62.45  ? 248 PHE K CD2 1 
ATOM   20967 C CE1 . PHE K  1 248 ? 7.218   -2.147   -64.903 1.00 51.07  ? 248 PHE K CE1 1 
ATOM   20968 C CE2 . PHE K  1 248 ? 8.409   -0.396   -63.797 1.00 53.19  ? 248 PHE K CE2 1 
ATOM   20969 C CZ  . PHE K  1 248 ? 7.704   -1.581   -63.742 1.00 44.84  ? 248 PHE K CZ  1 
ATOM   20970 N N   . GLU K  1 249 ? 7.869   3.329    -68.879 1.00 60.18  ? 249 GLU K N   1 
ATOM   20971 C CA  . GLU K  1 249 ? 8.233   4.296    -69.905 1.00 68.19  ? 249 GLU K CA  1 
ATOM   20972 C C   . GLU K  1 249 ? 9.216   5.300    -69.321 1.00 62.18  ? 249 GLU K C   1 
ATOM   20973 O O   . GLU K  1 249 ? 8.876   6.049    -68.407 1.00 69.16  ? 249 GLU K O   1 
ATOM   20974 C CB  . GLU K  1 249 ? 6.981   5.010    -70.416 1.00 78.83  ? 249 GLU K CB  1 
ATOM   20975 C CG  . GLU K  1 249 ? 7.233   6.041    -71.501 1.00 88.54  ? 249 GLU K CG  1 
ATOM   20976 C CD  . GLU K  1 249 ? 5.947   6.661    -72.015 1.00 103.74 ? 249 GLU K CD  1 
ATOM   20977 O OE1 . GLU K  1 249 ? 5.997   7.792    -72.541 1.00 116.24 ? 249 GLU K OE1 1 
ATOM   20978 O OE2 . GLU K  1 249 ? 4.883   6.018    -71.886 1.00 84.60  ? 249 GLU K OE2 1 
ATOM   20979 N N   . ALA K  1 250 ? 10.437  5.313    -69.844 1.00 60.89  ? 250 ALA K N   1 
ATOM   20980 C CA  . ALA K  1 250 ? 11.484  6.145    -69.266 1.00 62.32  ? 250 ALA K CA  1 
ATOM   20981 C C   . ALA K  1 250 ? 12.439  6.737    -70.297 1.00 69.06  ? 250 ALA K C   1 
ATOM   20982 O O   . ALA K  1 250 ? 12.752  6.111    -71.309 1.00 70.19  ? 250 ALA K O   1 
ATOM   20983 C CB  . ALA K  1 250 ? 12.264  5.357    -68.223 1.00 62.20  ? 250 ALA K CB  1 
ATOM   20984 N N   . THR K  1 251 ? 12.893  7.955    -70.021 1.00 66.03  ? 251 THR K N   1 
ATOM   20985 C CA  . THR K  1 251 ? 13.952  8.582    -70.796 1.00 65.49  ? 251 THR K CA  1 
ATOM   20986 C C   . THR K  1 251 ? 15.229  8.578    -69.965 1.00 66.64  ? 251 THR K C   1 
ATOM   20987 O O   . THR K  1 251 ? 16.189  9.285    -70.271 1.00 72.96  ? 251 THR K O   1 
ATOM   20988 C CB  . THR K  1 251 ? 13.592  10.027   -71.185 1.00 70.27  ? 251 THR K CB  1 
ATOM   20989 O OG1 . THR K  1 251 ? 13.118  10.729   -70.029 1.00 75.45  ? 251 THR K OG1 1 
ATOM   20990 C CG2 . THR K  1 251 ? 12.508  10.037   -72.252 1.00 61.56  ? 251 THR K CG2 1 
ATOM   20991 N N   . GLY K  1 252 ? 15.223  7.774    -68.905 1.00 68.18  ? 252 GLY K N   1 
ATOM   20992 C CA  . GLY K  1 252 ? 16.372  7.641    -68.030 1.00 70.01  ? 252 GLY K CA  1 
ATOM   20993 C C   . GLY K  1 252 ? 15.994  7.511    -66.566 1.00 65.21  ? 252 GLY K C   1 
ATOM   20994 O O   . GLY K  1 252 ? 14.831  7.675    -66.198 1.00 67.77  ? 252 GLY K O   1 
ATOM   20995 N N   . ASN K  1 253 ? 16.985  7.202    -65.734 1.00 59.86  ? 253 ASN K N   1 
ATOM   20996 C CA  . ASN K  1 253 ? 16.809  7.168    -64.284 1.00 55.76  ? 253 ASN K CA  1 
ATOM   20997 C C   . ASN K  1 253 ? 15.931  6.024    -63.779 1.00 62.58  ? 253 ASN K C   1 
ATOM   20998 O O   . ASN K  1 253 ? 15.542  6.006    -62.611 1.00 56.40  ? 253 ASN K O   1 
ATOM   20999 C CB  . ASN K  1 253 ? 16.254  8.505    -63.780 1.00 53.84  ? 253 ASN K CB  1 
ATOM   21000 C CG  . ASN K  1 253 ? 17.100  9.689    -64.209 1.00 58.09  ? 253 ASN K CG  1 
ATOM   21001 O OD1 . ASN K  1 253 ? 17.745  10.335   -63.384 1.00 57.51  ? 253 ASN K OD1 1 
ATOM   21002 N ND2 . ASN K  1 253 ? 17.099  9.980    -65.505 1.00 61.38  ? 253 ASN K ND2 1 
ATOM   21003 N N   . LEU K  1 254 ? 15.623  5.070    -64.651 1.00 61.47  ? 254 LEU K N   1 
ATOM   21004 C CA  . LEU K  1 254 ? 14.738  3.971    -64.277 1.00 51.63  ? 254 LEU K CA  1 
ATOM   21005 C C   . LEU K  1 254 ? 15.481  2.673    -63.980 1.00 51.70  ? 254 LEU K C   1 
ATOM   21006 O O   . LEU K  1 254 ? 16.019  2.033    -64.884 1.00 60.32  ? 254 LEU K O   1 
ATOM   21007 C CB  . LEU K  1 254 ? 13.690  3.725    -65.366 1.00 53.77  ? 254 LEU K CB  1 
ATOM   21008 C CG  . LEU K  1 254 ? 12.778  2.514    -65.147 1.00 50.34  ? 254 LEU K CG  1 
ATOM   21009 C CD1 . LEU K  1 254 ? 12.016  2.639    -63.834 1.00 51.74  ? 254 LEU K CD1 1 
ATOM   21010 C CD2 . LEU K  1 254 ? 11.817  2.336    -66.314 1.00 50.86  ? 254 LEU K CD2 1 
ATOM   21011 N N   . VAL K  1 255 ? 15.508  2.291    -62.707 1.00 53.98  ? 255 VAL K N   1 
ATOM   21012 C CA  . VAL K  1 255 ? 16.009  0.982    -62.314 1.00 47.02  ? 255 VAL K CA  1 
ATOM   21013 C C   . VAL K  1 255 ? 14.906  -0.038   -62.571 1.00 50.48  ? 255 VAL K C   1 
ATOM   21014 O O   . VAL K  1 255 ? 14.022  -0.235   -61.737 1.00 51.50  ? 255 VAL K O   1 
ATOM   21015 C CB  . VAL K  1 255 ? 16.408  0.946    -60.827 1.00 45.15  ? 255 VAL K CB  1 
ATOM   21016 C CG1 . VAL K  1 255 ? 16.929  -0.432   -60.450 1.00 51.99  ? 255 VAL K CG1 1 
ATOM   21017 C CG2 . VAL K  1 255 ? 17.452  2.010    -60.533 1.00 41.06  ? 255 VAL K CG2 1 
ATOM   21018 N N   . VAL K  1 256 ? 14.960  -0.675   -63.735 1.00 48.53  ? 256 VAL K N   1 
ATOM   21019 C CA  . VAL K  1 256 ? 13.884  -1.551   -64.188 1.00 51.88  ? 256 VAL K CA  1 
ATOM   21020 C C   . VAL K  1 256 ? 13.831  -2.872   -63.430 1.00 52.67  ? 256 VAL K C   1 
ATOM   21021 O O   . VAL K  1 256 ? 14.848  -3.348   -62.925 1.00 61.75  ? 256 VAL K O   1 
ATOM   21022 C CB  . VAL K  1 256 ? 14.004  -1.851   -65.695 1.00 59.17  ? 256 VAL K CB  1 
ATOM   21023 C CG1 . VAL K  1 256 ? 14.015  -0.558   -66.493 1.00 59.91  ? 256 VAL K CG1 1 
ATOM   21024 C CG2 . VAL K  1 256 ? 15.257  -2.664   -65.975 1.00 69.43  ? 256 VAL K CG2 1 
ATOM   21025 N N   . PRO K  1 257 ? 12.632  -3.465   -63.345 1.00 56.96  ? 257 PRO K N   1 
ATOM   21026 C CA  . PRO K  1 257 ? 12.446  -4.787   -62.741 1.00 49.73  ? 257 PRO K CA  1 
ATOM   21027 C C   . PRO K  1 257 ? 13.098  -5.870   -63.589 1.00 56.65  ? 257 PRO K C   1 
ATOM   21028 O O   . PRO K  1 257 ? 13.071  -5.789   -64.817 1.00 60.81  ? 257 PRO K O   1 
ATOM   21029 C CB  . PRO K  1 257 ? 10.924  -4.972   -62.760 1.00 47.57  ? 257 PRO K CB  1 
ATOM   21030 C CG  . PRO K  1 257 ? 10.361  -3.600   -62.911 1.00 53.56  ? 257 PRO K CG  1 
ATOM   21031 C CD  . PRO K  1 257 ? 11.353  -2.852   -63.738 1.00 55.44  ? 257 PRO K CD  1 
ATOM   21032 N N   . ARG K  1 258 ? 13.684  -6.868   -62.937 1.00 67.58  ? 258 ARG K N   1 
ATOM   21033 C CA  . ARG K  1 258 ? 14.214  -8.030   -63.636 1.00 61.51  ? 258 ARG K CA  1 
ATOM   21034 C C   . ARG K  1 258 ? 13.413  -9.258   -63.223 1.00 53.17  ? 258 ARG K C   1 
ATOM   21035 O O   . ARG K  1 258 ? 12.957  -10.031  -64.066 1.00 53.16  ? 258 ARG K O   1 
ATOM   21036 C CB  . ARG K  1 258 ? 15.697  -8.225   -63.320 1.00 61.63  ? 258 ARG K CB  1 
ATOM   21037 C CG  . ARG K  1 258 ? 16.313  -9.455   -63.971 1.00 61.96  ? 258 ARG K CG  1 
ATOM   21038 C CD  . ARG K  1 258 ? 17.778  -9.607   -63.593 1.00 74.44  ? 258 ARG K CD  1 
ATOM   21039 N NE  . ARG K  1 258 ? 18.216  -10.998  -63.667 1.00 81.26  ? 258 ARG K NE  1 
ATOM   21040 C CZ  . ARG K  1 258 ? 18.860  -11.531  -64.701 1.00 87.63  ? 258 ARG K CZ  1 
ATOM   21041 N NH1 . ARG K  1 258 ? 19.153  -10.787  -65.757 1.00 93.14  ? 258 ARG K NH1 1 
ATOM   21042 N NH2 . ARG K  1 258 ? 19.215  -12.808  -64.676 1.00 85.39  ? 258 ARG K NH2 1 
ATOM   21043 N N   . TYR K  1 259 ? 13.241  -9.422   -61.916 1.00 57.30  ? 259 TYR K N   1 
ATOM   21044 C CA  . TYR K  1 259 ? 12.418  -10.496  -61.377 1.00 53.16  ? 259 TYR K CA  1 
ATOM   21045 C C   . TYR K  1 259 ? 11.185  -9.932   -60.681 1.00 48.09  ? 259 TYR K C   1 
ATOM   21046 O O   . TYR K  1 259 ? 11.265  -8.937   -59.960 1.00 53.96  ? 259 TYR K O   1 
ATOM   21047 C CB  . TYR K  1 259 ? 13.217  -11.349  -60.389 1.00 60.97  ? 259 TYR K CB  1 
ATOM   21048 C CG  . TYR K  1 259 ? 14.267  -12.226  -61.030 1.00 66.26  ? 259 TYR K CG  1 
ATOM   21049 C CD1 . TYR K  1 259 ? 15.552  -11.752  -61.253 1.00 69.90  ? 259 TYR K CD1 1 
ATOM   21050 C CD2 . TYR K  1 259 ? 13.976  -13.531  -61.405 1.00 73.13  ? 259 TYR K CD2 1 
ATOM   21051 C CE1 . TYR K  1 259 ? 16.516  -12.550  -61.834 1.00 83.63  ? 259 TYR K CE1 1 
ATOM   21052 C CE2 . TYR K  1 259 ? 14.934  -14.337  -61.989 1.00 72.67  ? 259 TYR K CE2 1 
ATOM   21053 C CZ  . TYR K  1 259 ? 16.202  -13.841  -62.201 1.00 78.11  ? 259 TYR K CZ  1 
ATOM   21054 O OH  . TYR K  1 259 ? 17.161  -14.639  -62.782 1.00 91.30  ? 259 TYR K OH  1 
ATOM   21055 N N   . ALA K  1 260 ? 10.044  -10.573  -60.911 1.00 52.08  ? 260 ALA K N   1 
ATOM   21056 C CA  . ALA K  1 260 ? 8.820   -10.242  -60.198 1.00 56.58  ? 260 ALA K CA  1 
ATOM   21057 C C   . ALA K  1 260 ? 8.431   -11.426  -59.324 1.00 50.89  ? 260 ALA K C   1 
ATOM   21058 O O   . ALA K  1 260 ? 9.170   -12.407  -59.238 1.00 56.79  ? 260 ALA K O   1 
ATOM   21059 C CB  . ALA K  1 260 ? 7.708   -9.906   -61.172 1.00 55.21  ? 260 ALA K CB  1 
ATOM   21060 N N   . PHE K  1 261 ? 7.274   -11.342  -58.678 1.00 58.70  ? 261 PHE K N   1 
ATOM   21061 C CA  . PHE K  1 261 ? 6.845   -12.408  -57.784 1.00 46.33  ? 261 PHE K CA  1 
ATOM   21062 C C   . PHE K  1 261 ? 5.372   -12.761  -57.943 1.00 49.95  ? 261 PHE K C   1 
ATOM   21063 O O   . PHE K  1 261 ? 4.493   -12.013  -57.515 1.00 55.19  ? 261 PHE K O   1 
ATOM   21064 C CB  . PHE K  1 261 ? 7.137   -12.039  -56.327 1.00 36.45  ? 261 PHE K CB  1 
ATOM   21065 C CG  . PHE K  1 261 ? 8.586   -11.759  -56.050 1.00 46.09  ? 261 PHE K CG  1 
ATOM   21066 C CD1 . PHE K  1 261 ? 9.086   -10.471  -56.139 1.00 55.39  ? 261 PHE K CD1 1 
ATOM   21067 C CD2 . PHE K  1 261 ? 9.449   -12.784  -55.702 1.00 48.19  ? 261 PHE K CD2 1 
ATOM   21068 C CE1 . PHE K  1 261 ? 10.419  -10.210  -55.885 1.00 55.00  ? 261 PHE K CE1 1 
ATOM   21069 C CE2 . PHE K  1 261 ? 10.783  -12.530  -55.446 1.00 43.55  ? 261 PHE K CE2 1 
ATOM   21070 C CZ  . PHE K  1 261 ? 11.269  -11.241  -55.538 1.00 49.47  ? 261 PHE K CZ  1 
ATOM   21071 N N   . ALA K  1 262 ? 5.108   -13.902  -58.570 1.00 54.49  ? 262 ALA K N   1 
ATOM   21072 C CA  . ALA K  1 262 ? 3.770   -14.470  -58.558 1.00 53.46  ? 262 ALA K CA  1 
ATOM   21073 C C   . ALA K  1 262 ? 3.469   -14.866  -57.118 1.00 60.24  ? 262 ALA K C   1 
ATOM   21074 O O   . ALA K  1 262 ? 4.210   -15.649  -56.522 1.00 61.79  ? 262 ALA K O   1 
ATOM   21075 C CB  . ALA K  1 262 ? 3.695   -15.676  -59.482 1.00 65.89  ? 262 ALA K CB  1 
ATOM   21076 N N   . MET K  1 263 ? 2.407   -14.309  -56.544 1.00 54.06  ? 263 MET K N   1 
ATOM   21077 C CA  . MET K  1 263 ? 2.131   -14.548  -55.129 1.00 57.61  ? 263 MET K CA  1 
ATOM   21078 C C   . MET K  1 263 ? 0.656   -14.475  -54.753 1.00 62.20  ? 263 MET K C   1 
ATOM   21079 O O   . MET K  1 263 ? -0.071  -13.572  -55.176 1.00 73.05  ? 263 MET K O   1 
ATOM   21080 C CB  . MET K  1 263 ? 2.951   -13.597  -54.248 1.00 57.91  ? 263 MET K CB  1 
ATOM   21081 C CG  . MET K  1 263 ? 2.148   -12.487  -53.587 1.00 59.00  ? 263 MET K CG  1 
ATOM   21082 S SD  . MET K  1 263 ? 3.210   -11.319  -52.714 1.00 59.35  ? 263 MET K SD  1 
ATOM   21083 C CE  . MET K  1 263 ? 2.063   -9.983   -52.368 1.00 68.88  ? 263 MET K CE  1 
ATOM   21084 N N   . GLU K  1 264 ? 0.230   -15.453  -53.962 1.00 62.22  ? 264 GLU K N   1 
ATOM   21085 C CA  . GLU K  1 264 ? -1.105  -15.468  -53.390 1.00 64.20  ? 264 GLU K CA  1 
ATOM   21086 C C   . GLU K  1 264 ? -0.982  -15.272  -51.897 1.00 61.00  ? 264 GLU K C   1 
ATOM   21087 O O   . GLU K  1 264 ? -0.416  -16.109  -51.197 1.00 69.36  ? 264 GLU K O   1 
ATOM   21088 C CB  . GLU K  1 264 ? -1.791  -16.798  -53.675 1.00 70.40  ? 264 GLU K CB  1 
ATOM   21089 C CG  . GLU K  1 264 ? -2.863  -16.713  -54.733 1.00 86.95  ? 264 GLU K CG  1 
ATOM   21090 C CD  . GLU K  1 264 ? -3.073  -18.033  -55.429 1.00 106.53 ? 264 GLU K CD  1 
ATOM   21091 O OE1 . GLU K  1 264 ? -4.182  -18.593  -55.322 1.00 108.44 ? 264 GLU K OE1 1 
ATOM   21092 O OE2 . GLU K  1 264 ? -2.118  -18.519  -56.068 1.00 110.69 ? 264 GLU K OE2 1 
ATOM   21093 N N   . ARG K  1 265 ? -1.514  -14.161  -51.410 1.00 70.40  ? 265 ARG K N   1 
ATOM   21094 C CA  . ARG K  1 265 ? -1.399  -13.833  -50.002 1.00 70.05  ? 265 ARG K CA  1 
ATOM   21095 C C   . ARG K  1 265 ? -2.732  -13.996  -49.270 1.00 78.21  ? 265 ARG K C   1 
ATOM   21096 O O   . ARG K  1 265 ? -3.805  -13.779  -49.842 1.00 78.22  ? 265 ARG K O   1 
ATOM   21097 C CB  . ARG K  1 265 ? -0.880  -12.403  -49.845 1.00 54.81  ? 265 ARG K CB  1 
ATOM   21098 C CG  . ARG K  1 265 ? -1.436  -11.442  -50.876 1.00 61.74  ? 265 ARG K CG  1 
ATOM   21099 C CD  . ARG K  1 265 ? -0.905  -10.038  -50.672 1.00 71.50  ? 265 ARG K CD  1 
ATOM   21100 N NE  . ARG K  1 265 ? -1.921  -9.155   -50.110 1.00 78.95  ? 265 ARG K NE  1 
ATOM   21101 C CZ  . ARG K  1 265 ? -2.766  -8.434   -50.840 1.00 74.48  ? 265 ARG K CZ  1 
ATOM   21102 N NH1 . ARG K  1 265 ? -2.714  -8.490   -52.163 1.00 76.54  ? 265 ARG K NH1 1 
ATOM   21103 N NH2 . ARG K  1 265 ? -3.662  -7.655   -50.250 1.00 74.13  ? 265 ARG K NH2 1 
ATOM   21104 N N   . ASN K  1 266 ? -2.648  -14.399  -48.005 1.00 82.62  ? 266 ASN K N   1 
ATOM   21105 C CA  . ASN K  1 266 ? -3.794  -14.438  -47.098 1.00 88.01  ? 266 ASN K CA  1 
ATOM   21106 C C   . ASN K  1 266 ? -3.931  -13.141  -46.307 1.00 87.74  ? 266 ASN K C   1 
ATOM   21107 O O   . ASN K  1 266 ? -3.403  -12.104  -46.707 1.00 87.91  ? 266 ASN K O   1 
ATOM   21108 C CB  . ASN K  1 266 ? -3.702  -15.670  -46.178 1.00 91.02  ? 266 ASN K CB  1 
ATOM   21109 C CG  . ASN K  1 266 ? -2.351  -16.377  -46.275 1.00 97.16  ? 266 ASN K CG  1 
ATOM   21110 O OD1 . ASN K  1 266 ? -2.282  -17.594  -46.445 1.00 86.57  ? 266 ASN K OD1 1 
ATOM   21111 N ND2 . ASN K  1 266 ? -1.272  -15.610  -46.163 1.00 93.05  ? 266 ASN K ND2 1 
ATOM   21112 N N   . ALA K  1 267 ? -4.655  -13.197  -45.195 1.00 83.37  ? 267 ALA K N   1 
ATOM   21113 C CA  . ALA K  1 267 ? -4.593  -12.128  -44.217 1.00 85.40  ? 267 ALA K CA  1 
ATOM   21114 C C   . ALA K  1 267 ? -3.442  -12.560  -43.332 1.00 87.17  ? 267 ALA K C   1 
ATOM   21115 O O   . ALA K  1 267 ? -2.333  -12.036  -43.432 1.00 86.06  ? 267 ALA K O   1 
ATOM   21116 C CB  . ALA K  1 267 ? -5.870  -12.044  -43.413 1.00 85.46  ? 267 ALA K CB  1 
ATOM   21117 N N   . GLY K  1 268 ? -3.699  -13.523  -42.461 1.00 84.16  ? 268 GLY K N   1 
ATOM   21118 C CA  . GLY K  1 268 ? -2.629  -14.075  -41.661 1.00 95.10  ? 268 GLY K CA  1 
ATOM   21119 C C   . GLY K  1 268 ? -1.718  -13.071  -40.975 1.00 99.58  ? 268 GLY K C   1 
ATOM   21120 O O   . GLY K  1 268 ? -2.123  -11.951  -40.641 1.00 89.63  ? 268 GLY K O   1 
ATOM   21121 N N   . SER K  1 269 ? -0.459  -13.485  -40.844 1.00 84.44  ? 269 SER K N   1 
ATOM   21122 C CA  . SER K  1 269 ? 0.464   -13.063  -39.788 1.00 71.85  ? 269 SER K CA  1 
ATOM   21123 C C   . SER K  1 269 ? 1.084   -11.687  -39.861 1.00 73.42  ? 269 SER K C   1 
ATOM   21124 O O   . SER K  1 269 ? 0.691   -10.852  -40.673 1.00 83.04  ? 269 SER K O   1 
ATOM   21125 C CB  . SER K  1 269 ? 1.603   -14.070  -39.722 1.00 71.04  ? 269 SER K CB  1 
ATOM   21126 O OG  . SER K  1 269 ? 1.980   -14.435  -41.037 1.00 67.31  ? 269 SER K OG  1 
ATOM   21127 N N   . GLY K  1 270 ? 2.066   -11.489  -38.981 1.00 42.56  ? 270 GLY K N   1 
ATOM   21128 C CA  . GLY K  1 270 ? 2.917   -10.316  -38.969 1.00 49.50  ? 270 GLY K CA  1 
ATOM   21129 C C   . GLY K  1 270 ? 4.368   -10.756  -39.037 1.00 43.27  ? 270 GLY K C   1 
ATOM   21130 O O   . GLY K  1 270 ? 4.668   -11.820  -39.575 1.00 46.46  ? 270 GLY K O   1 
ATOM   21131 N N   . ILE K  1 271 ? 5.278   -9.952   -38.500 1.00 41.88  ? 271 ILE K N   1 
ATOM   21132 C CA  . ILE K  1 271 ? 6.688   -10.311  -38.546 1.00 33.40  ? 271 ILE K CA  1 
ATOM   21133 C C   . ILE K  1 271 ? 7.266   -10.233  -37.135 1.00 52.47  ? 271 ILE K C   1 
ATOM   21134 O O   . ILE K  1 271 ? 6.967   -9.297   -36.391 1.00 60.00  ? 271 ILE K O   1 
ATOM   21135 C CB  . ILE K  1 271 ? 7.465   -9.419   -39.551 1.00 37.63  ? 271 ILE K CB  1 
ATOM   21136 C CG1 . ILE K  1 271 ? 8.222   -8.300   -38.836 1.00 41.57  ? 271 ILE K CG1 1 
ATOM   21137 C CG2 . ILE K  1 271 ? 6.519   -8.846   -40.603 1.00 47.80  ? 271 ILE K CG2 1 
ATOM   21138 C CD1 . ILE K  1 271 ? 9.692   -8.587   -38.671 1.00 53.00  ? 271 ILE K CD1 1 
ATOM   21139 N N   . ILE K  1 272 ? 8.044   -11.243  -36.752 1.00 53.39  ? 272 ILE K N   1 
ATOM   21140 C CA  . ILE K  1 272 ? 8.658   -11.276  -35.429 1.00 52.86  ? 272 ILE K CA  1 
ATOM   21141 C C   . ILE K  1 272 ? 10.140  -10.950  -35.533 1.00 49.23  ? 272 ILE K C   1 
ATOM   21142 O O   . ILE K  1 272 ? 10.868  -11.565  -36.314 1.00 52.94  ? 272 ILE K O   1 
ATOM   21143 C CB  . ILE K  1 272 ? 8.484   -12.650  -34.743 1.00 49.70  ? 272 ILE K CB  1 
ATOM   21144 C CG1 . ILE K  1 272 ? 7.002   -12.939  -34.495 1.00 51.81  ? 272 ILE K CG1 1 
ATOM   21145 C CG2 . ILE K  1 272 ? 9.255   -12.700  -33.429 1.00 53.96  ? 272 ILE K CG2 1 
ATOM   21146 C CD1 . ILE K  1 272 ? 6.736   -14.244  -33.772 1.00 56.34  ? 272 ILE K CD1 1 
ATOM   21147 N N   . ILE K  1 273 ? 10.579  -9.964   -34.759 1.00 48.30  ? 273 ILE K N   1 
ATOM   21148 C CA  . ILE K  1 273 ? 11.994  -9.637   -34.686 1.00 59.80  ? 273 ILE K CA  1 
ATOM   21149 C C   . ILE K  1 273 ? 12.592  -10.304  -33.457 1.00 69.38  ? 273 ILE K C   1 
ATOM   21150 O O   . ILE K  1 273 ? 12.420  -9.828   -32.335 1.00 75.78  ? 273 ILE K O   1 
ATOM   21151 C CB  . ILE K  1 273 ? 12.247  -8.120   -34.620 1.00 58.82  ? 273 ILE K CB  1 
ATOM   21152 C CG1 . ILE K  1 273 ? 11.673  -7.417   -35.853 1.00 53.81  ? 273 ILE K CG1 1 
ATOM   21153 C CG2 . ILE K  1 273 ? 13.737  -7.839   -34.495 1.00 68.80  ? 273 ILE K CG2 1 
ATOM   21154 C CD1 . ILE K  1 273 ? 10.201  -7.089   -35.742 1.00 83.81  ? 273 ILE K CD1 1 
ATOM   21155 N N   . SER K  1 274 ? 13.293  -11.410  -33.675 1.00 75.61  ? 274 SER K N   1 
ATOM   21156 C CA  . SER K  1 274 ? 13.812  -12.211  -32.576 1.00 63.43  ? 274 SER K CA  1 
ATOM   21157 C C   . SER K  1 274 ? 15.089  -12.954  -32.952 1.00 70.25  ? 274 SER K C   1 
ATOM   21158 O O   . SER K  1 274 ? 15.335  -13.237  -34.125 1.00 75.18  ? 274 SER K O   1 
ATOM   21159 C CB  . SER K  1 274 ? 12.748  -13.205  -32.108 1.00 61.37  ? 274 SER K CB  1 
ATOM   21160 O OG  . SER K  1 274 ? 13.326  -14.261  -31.361 1.00 76.80  ? 274 SER K OG  1 
ATOM   21161 N N   . ASP K  1 275 ? 15.897  -13.263  -31.944 1.00 94.48  ? 275 ASP K N   1 
ATOM   21162 C CA  . ASP K  1 275 ? 17.110  -14.045  -32.139 1.00 95.20  ? 275 ASP K CA  1 
ATOM   21163 C C   . ASP K  1 275 ? 16.793  -15.528  -32.007 1.00 79.40  ? 275 ASP K C   1 
ATOM   21164 O O   . ASP K  1 275 ? 17.524  -16.378  -32.515 1.00 98.14  ? 275 ASP K O   1 
ATOM   21165 C CB  . ASP K  1 275 ? 18.170  -13.655  -31.108 1.00 108.88 ? 275 ASP K CB  1 
ATOM   21166 C CG  . ASP K  1 275 ? 18.554  -12.190  -31.187 1.00 124.90 ? 275 ASP K CG  1 
ATOM   21167 O OD1 . ASP K  1 275 ? 18.083  -11.404  -30.338 1.00 133.87 ? 275 ASP K OD1 1 
ATOM   21168 O OD2 . ASP K  1 275 ? 19.330  -11.826  -32.096 1.00 119.22 ? 275 ASP K OD2 1 
ATOM   21169 N N   . THR K  1 276 ? 15.696  -15.825  -31.318 1.00 67.94  ? 276 THR K N   1 
ATOM   21170 C CA  . THR K  1 276 ? 15.290  -17.198  -31.039 1.00 67.21  ? 276 THR K CA  1 
ATOM   21171 C C   . THR K  1 276 ? 15.423  -18.104  -32.258 1.00 75.36  ? 276 THR K C   1 
ATOM   21172 O O   . THR K  1 276 ? 15.100  -17.705  -33.376 1.00 80.39  ? 276 THR K O   1 
ATOM   21173 C CB  . THR K  1 276 ? 13.839  -17.261  -30.522 1.00 61.32  ? 276 THR K CB  1 
ATOM   21174 O OG1 . THR K  1 276 ? 13.694  -16.389  -29.394 1.00 58.60  ? 276 THR K OG1 1 
ATOM   21175 C CG2 . THR K  1 276 ? 13.466  -18.682  -30.114 1.00 66.99  ? 276 THR K CG2 1 
ATOM   21176 N N   . PRO K  1 277 ? 15.915  -19.329  -32.034 1.00 76.98  ? 277 PRO K N   1 
ATOM   21177 C CA  . PRO K  1 277 ? 16.113  -20.375  -33.040 1.00 73.14  ? 277 PRO K CA  1 
ATOM   21178 C C   . PRO K  1 277 ? 14.830  -20.789  -33.758 1.00 72.15  ? 277 PRO K C   1 
ATOM   21179 O O   . PRO K  1 277 ? 13.813  -21.028  -33.108 1.00 74.51  ? 277 PRO K O   1 
ATOM   21180 C CB  . PRO K  1 277 ? 16.624  -21.551  -32.205 1.00 85.93  ? 277 PRO K CB  1 
ATOM   21181 C CG  . PRO K  1 277 ? 17.280  -20.924  -31.038 1.00 95.63  ? 277 PRO K CG  1 
ATOM   21182 C CD  . PRO K  1 277 ? 16.446  -19.727  -30.719 1.00 74.09  ? 277 PRO K CD  1 
ATOM   21183 N N   . VAL K  1 278 ? 14.883  -20.875  -35.085 1.00 66.73  ? 278 VAL K N   1 
ATOM   21184 C CA  . VAL K  1 278 ? 13.790  -21.465  -35.849 1.00 73.37  ? 278 VAL K CA  1 
ATOM   21185 C C   . VAL K  1 278 ? 13.845  -22.978  -35.671 1.00 76.54  ? 278 VAL K C   1 
ATOM   21186 O O   . VAL K  1 278 ? 14.928  -23.558  -35.589 1.00 84.39  ? 278 VAL K O   1 
ATOM   21187 C CB  . VAL K  1 278 ? 13.875  -21.113  -37.347 1.00 66.70  ? 278 VAL K CB  1 
ATOM   21188 C CG1 . VAL K  1 278 ? 15.235  -21.496  -37.912 1.00 85.06  ? 278 VAL K CG1 1 
ATOM   21189 C CG2 . VAL K  1 278 ? 12.754  -21.797  -38.120 1.00 56.04  ? 278 VAL K CG2 1 
ATOM   21190 N N   . HIS K  1 279 ? 12.682  -23.616  -35.605 1.00 76.23  ? 279 HIS K N   1 
ATOM   21191 C CA  . HIS K  1 279 ? 12.622  -25.040  -35.294 1.00 77.12  ? 279 HIS K CA  1 
ATOM   21192 C C   . HIS K  1 279 ? 11.617  -25.810  -36.140 1.00 74.95  ? 279 HIS K C   1 
ATOM   21193 O O   . HIS K  1 279 ? 10.668  -25.239  -36.678 1.00 96.29  ? 279 HIS K O   1 
ATOM   21194 C CB  . HIS K  1 279 ? 12.286  -25.240  -33.816 1.00 93.55  ? 279 HIS K CB  1 
ATOM   21195 C CG  . HIS K  1 279 ? 13.453  -25.661  -32.981 1.00 105.41 ? 279 HIS K CG  1 
ATOM   21196 N ND1 . HIS K  1 279 ? 13.707  -26.978  -32.667 1.00 93.38  ? 279 HIS K ND1 1 
ATOM   21197 C CD2 . HIS K  1 279 ? 14.435  -24.936  -32.391 1.00 106.94 ? 279 HIS K CD2 1 
ATOM   21198 C CE1 . HIS K  1 279 ? 14.795  -27.048  -31.920 1.00 111.42 ? 279 HIS K CE1 1 
ATOM   21199 N NE2 . HIS K  1 279 ? 15.252  -25.825  -31.736 1.00 112.15 ? 279 HIS K NE2 1 
ATOM   21200 N N   . ASP K  1 280 ? 11.839  -27.116  -36.242 1.00 83.85  ? 280 ASP K N   1 
ATOM   21201 C CA  . ASP K  1 280 ? 10.877  -28.016  -36.857 1.00 93.79  ? 280 ASP K CA  1 
ATOM   21202 C C   . ASP K  1 280 ? 9.918   -28.546  -35.798 1.00 95.28  ? 280 ASP K C   1 
ATOM   21203 O O   . ASP K  1 280 ? 10.057  -29.675  -35.327 1.00 108.95 ? 280 ASP K O   1 
ATOM   21204 C CB  . ASP K  1 280 ? 11.583  -29.182  -37.547 1.00 101.20 ? 280 ASP K CB  1 
ATOM   21205 C CG  . ASP K  1 280 ? 10.610  -30.226  -38.052 1.00 117.24 ? 280 ASP K CG  1 
ATOM   21206 O OD1 . ASP K  1 280 ? 9.403   -29.918  -38.123 1.00 118.19 ? 280 ASP K OD1 1 
ATOM   21207 O OD2 . ASP K  1 280 ? 11.045  -31.353  -38.369 1.00 131.84 ? 280 ASP K OD2 1 
ATOM   21208 N N   . CYS K  1 281 ? 8.949   -27.716  -35.428 1.00 88.18  ? 281 CYS K N   1 
ATOM   21209 C CA  . CYS K  1 281 ? 7.947   -28.072  -34.433 1.00 86.75  ? 281 CYS K CA  1 
ATOM   21210 C C   . CYS K  1 281 ? 6.630   -27.362  -34.752 1.00 79.73  ? 281 CYS K C   1 
ATOM   21211 O O   . CYS K  1 281 ? 6.608   -26.367  -35.481 1.00 83.79  ? 281 CYS K O   1 
ATOM   21212 C CB  . CYS K  1 281 ? 8.439   -27.684  -33.031 1.00 80.72  ? 281 CYS K CB  1 
ATOM   21213 S SG  . CYS K  1 281 ? 8.830   -25.925  -32.842 1.00 109.92 ? 281 CYS K SG  1 
ATOM   21214 N N   . ASN K  1 282 ? 5.533   -27.878  -34.206 1.00 77.34  ? 282 ASN K N   1 
ATOM   21215 C CA  . ASN K  1 282 ? 4.227   -27.252  -34.387 1.00 64.34  ? 282 ASN K CA  1 
ATOM   21216 C C   . ASN K  1 282 ? 3.861   -26.377  -33.187 1.00 63.96  ? 282 ASN K C   1 
ATOM   21217 O O   . ASN K  1 282 ? 4.384   -26.575  -32.091 1.00 73.33  ? 282 ASN K O   1 
ATOM   21218 C CB  . ASN K  1 282 ? 3.146   -28.309  -34.651 1.00 78.09  ? 282 ASN K CB  1 
ATOM   21219 C CG  . ASN K  1 282 ? 2.665   -28.307  -36.091 1.00 100.32 ? 282 ASN K CG  1 
ATOM   21220 O OD1 . ASN K  1 282 ? 2.556   -27.254  -36.714 1.00 101.07 ? 282 ASN K OD1 1 
ATOM   21221 N ND2 . ASN K  1 282 ? 2.374   -29.494  -36.626 1.00 120.04 ? 282 ASN K ND2 1 
ATOM   21222 N N   . THR K  1 283 ? 2.989   -25.396  -33.409 1.00 71.45  ? 283 THR K N   1 
ATOM   21223 C CA  . THR K  1 283 ? 2.492   -24.528  -32.343 1.00 64.88  ? 283 THR K CA  1 
ATOM   21224 C C   . THR K  1 283 ? 1.230   -23.844  -32.840 1.00 50.95  ? 283 THR K C   1 
ATOM   21225 O O   . THR K  1 283 ? 1.033   -23.706  -34.042 1.00 51.67  ? 283 THR K O   1 
ATOM   21226 C CB  . THR K  1 283 ? 3.520   -23.445  -31.925 1.00 59.77  ? 283 THR K CB  1 
ATOM   21227 O OG1 . THR K  1 283 ? 3.057   -22.764  -30.750 1.00 41.90  ? 283 THR K OG1 1 
ATOM   21228 C CG2 . THR K  1 283 ? 3.708   -22.430  -33.041 1.00 54.91  ? 283 THR K CG2 1 
ATOM   21229 N N   . THR K  1 284 ? 0.374   -23.422  -31.919 1.00 44.10  ? 284 THR K N   1 
ATOM   21230 C CA  . THR K  1 284 ? -0.854  -22.731  -32.287 1.00 61.34  ? 284 THR K CA  1 
ATOM   21231 C C   . THR K  1 284 ? -0.734  -21.271  -31.875 1.00 58.54  ? 284 THR K C   1 
ATOM   21232 O O   . THR K  1 284 ? -1.567  -20.437  -32.229 1.00 50.75  ? 284 THR K O   1 
ATOM   21233 C CB  . THR K  1 284 ? -2.075  -23.363  -31.602 1.00 50.04  ? 284 THR K CB  1 
ATOM   21234 O OG1 . THR K  1 284 ? -3.277  -22.778  -32.118 1.00 57.79  ? 284 THR K OG1 1 
ATOM   21235 C CG2 . THR K  1 284 ? -2.007  -23.146  -30.100 1.00 50.53  ? 284 THR K CG2 1 
ATOM   21236 N N   . CYS K  1 285 ? 0.324   -20.974  -31.128 1.00 44.19  ? 285 CYS K N   1 
ATOM   21237 C CA  . CYS K  1 285 ? 0.587   -19.623  -30.653 1.00 38.68  ? 285 CYS K CA  1 
ATOM   21238 C C   . CYS K  1 285 ? 2.088   -19.351  -30.599 1.00 44.04  ? 285 CYS K C   1 
ATOM   21239 O O   . CYS K  1 285 ? 2.840   -20.089  -29.960 1.00 48.12  ? 285 CYS K O   1 
ATOM   21240 C CB  . CYS K  1 285 ? -0.039  -19.416  -29.273 1.00 38.29  ? 285 CYS K CB  1 
ATOM   21241 S SG  . CYS K  1 285 ? 0.278   -17.794  -28.547 1.00 52.57  ? 285 CYS K SG  1 
ATOM   21242 N N   . GLN K  1 286 ? 2.518   -18.286  -31.268 1.00 43.02  ? 286 GLN K N   1 
ATOM   21243 C CA  . GLN K  1 286 ? 3.938   -17.971  -31.376 1.00 33.48  ? 286 GLN K CA  1 
ATOM   21244 C C   . GLN K  1 286 ? 4.286   -16.600  -30.798 1.00 46.05  ? 286 GLN K C   1 
ATOM   21245 O O   . GLN K  1 286 ? 3.637   -15.601  -31.107 1.00 58.51  ? 286 GLN K O   1 
ATOM   21246 C CB  . GLN K  1 286 ? 4.385   -18.044  -32.838 1.00 33.91  ? 286 GLN K CB  1 
ATOM   21247 C CG  . GLN K  1 286 ? 5.882   -17.893  -33.030 1.00 43.58  ? 286 GLN K CG  1 
ATOM   21248 C CD  . GLN K  1 286 ? 6.661   -19.001  -32.354 1.00 51.24  ? 286 GLN K CD  1 
ATOM   21249 O OE1 . GLN K  1 286 ? 6.481   -20.179  -32.664 1.00 57.80  ? 286 GLN K OE1 1 
ATOM   21250 N NE2 . GLN K  1 286 ? 7.531   -18.631  -31.424 1.00 40.79  ? 286 GLN K NE2 1 
ATOM   21251 N N   . THR K  1 287 ? 5.319   -16.563  -29.960 1.00 47.13  ? 287 THR K N   1 
ATOM   21252 C CA  . THR K  1 287 ? 5.822   -15.308  -29.412 1.00 47.05  ? 287 THR K CA  1 
ATOM   21253 C C   . THR K  1 287 ? 7.284   -15.133  -29.810 1.00 47.38  ? 287 THR K C   1 
ATOM   21254 O O   . THR K  1 287 ? 7.940   -16.096  -30.203 1.00 47.95  ? 287 THR K O   1 
ATOM   21255 C CB  . THR K  1 287 ? 5.717   -15.272  -27.874 1.00 52.09  ? 287 THR K CB  1 
ATOM   21256 O OG1 . THR K  1 287 ? 6.925   -15.779  -27.294 1.00 39.77  ? 287 THR K OG1 1 
ATOM   21257 C CG2 . THR K  1 287 ? 4.533   -16.097  -27.396 1.00 43.74  ? 287 THR K CG2 1 
ATOM   21258 N N   . PRO K  1 288 ? 7.798   -13.897  -29.717 1.00 51.30  ? 288 PRO K N   1 
ATOM   21259 C CA  . PRO K  1 288 ? 9.202   -13.623  -30.041 1.00 57.34  ? 288 PRO K CA  1 
ATOM   21260 C C   . PRO K  1 288 ? 10.174  -14.419  -29.173 1.00 52.51  ? 288 PRO K C   1 
ATOM   21261 O O   . PRO K  1 288 ? 11.293  -14.695  -29.605 1.00 59.39  ? 288 PRO K O   1 
ATOM   21262 C CB  . PRO K  1 288 ? 9.339   -12.127  -29.746 1.00 57.21  ? 288 PRO K CB  1 
ATOM   21263 C CG  . PRO K  1 288 ? 7.965   -11.584  -29.922 1.00 47.07  ? 288 PRO K CG  1 
ATOM   21264 C CD  . PRO K  1 288 ? 7.047   -12.662  -29.429 1.00 48.91  ? 288 PRO K CD  1 
ATOM   21265 N N   . LYS K  1 289 ? 9.750   -14.780  -27.967 1.00 45.74  ? 289 LYS K N   1 
ATOM   21266 C CA  . LYS K  1 289 ? 10.610  -15.502  -27.033 1.00 55.01  ? 289 LYS K CA  1 
ATOM   21267 C C   . LYS K  1 289 ? 10.539  -17.012  -27.243 1.00 50.92  ? 289 LYS K C   1 
ATOM   21268 O O   . LYS K  1 289 ? 11.495  -17.734  -26.959 1.00 61.73  ? 289 LYS K O   1 
ATOM   21269 C CB  . LYS K  1 289 ? 10.239  -15.150  -25.590 1.00 58.50  ? 289 LYS K CB  1 
ATOM   21270 C CG  . LYS K  1 289 ? 10.333  -13.663  -25.284 1.00 64.48  ? 289 LYS K CG  1 
ATOM   21271 C CD  . LYS K  1 289 ? 9.707   -13.310  -23.940 1.00 72.00  ? 289 LYS K CD  1 
ATOM   21272 C CE  . LYS K  1 289 ? 10.537  -13.818  -22.772 1.00 77.69  ? 289 LYS K CE  1 
ATOM   21273 N NZ  . LYS K  1 289 ? 10.018  -13.313  -21.469 1.00 81.14  ? 289 LYS K NZ  1 
ATOM   21274 N N   . GLY K  1 290 ? 9.401   -17.480  -27.744 1.00 46.53  ? 290 GLY K N   1 
ATOM   21275 C CA  . GLY K  1 290 ? 9.190   -18.896  -27.982 1.00 44.67  ? 290 GLY K CA  1 
ATOM   21276 C C   . GLY K  1 290 ? 7.720   -19.214  -28.174 1.00 54.34  ? 290 GLY K C   1 
ATOM   21277 O O   . GLY K  1 290 ? 6.860   -18.358  -27.971 1.00 57.06  ? 290 GLY K O   1 
ATOM   21278 N N   . ALA K  1 291 ? 7.430   -20.450  -28.564 1.00 52.23  ? 291 ALA K N   1 
ATOM   21279 C CA  . ALA K  1 291 ? 6.056   -20.871  -28.815 1.00 52.04  ? 291 ALA K CA  1 
ATOM   21280 C C   . ALA K  1 291 ? 5.344   -21.268  -27.526 1.00 56.48  ? 291 ALA K C   1 
ATOM   21281 O O   . ALA K  1 291 ? 5.984   -21.568  -26.519 1.00 55.83  ? 291 ALA K O   1 
ATOM   21282 C CB  . ALA K  1 291 ? 6.031   -22.021  -29.810 1.00 46.23  ? 291 ALA K CB  1 
ATOM   21283 N N   . ILE K  1 292 ? 4.014   -21.265  -27.565 1.00 53.75  ? 292 ILE K N   1 
ATOM   21284 C CA  . ILE K  1 292 ? 3.210   -21.666  -26.416 1.00 49.13  ? 292 ILE K CA  1 
ATOM   21285 C C   . ILE K  1 292 ? 2.296   -22.849  -26.744 1.00 66.21  ? 292 ILE K C   1 
ATOM   21286 O O   . ILE K  1 292 ? 1.384   -22.738  -27.564 1.00 71.43  ? 292 ILE K O   1 
ATOM   21287 C CB  . ILE K  1 292 ? 2.365   -20.494  -25.871 1.00 42.81  ? 292 ILE K CB  1 
ATOM   21288 C CG1 . ILE K  1 292 ? 3.268   -19.354  -25.397 1.00 34.46  ? 292 ILE K CG1 1 
ATOM   21289 C CG2 . ILE K  1 292 ? 1.488   -20.960  -24.728 1.00 58.54  ? 292 ILE K CG2 1 
ATOM   21290 C CD1 . ILE K  1 292 ? 2.508   -18.169  -24.830 1.00 58.94  ? 292 ILE K CD1 1 
ATOM   21291 N N   . ASN K  1 293 ? 2.563   -23.981  -26.100 1.00 87.68  ? 293 ASN K N   1 
ATOM   21292 C CA  . ASN K  1 293 ? 1.745   -25.184  -26.217 1.00 96.96  ? 293 ASN K CA  1 
ATOM   21293 C C   . ASN K  1 293 ? 0.836   -25.272  -24.996 1.00 100.72 ? 293 ASN K C   1 
ATOM   21294 O O   . ASN K  1 293 ? 1.208   -25.868  -23.985 1.00 109.52 ? 293 ASN K O   1 
ATOM   21295 C CB  . ASN K  1 293 ? 2.662   -26.413  -26.296 1.00 106.16 ? 293 ASN K CB  1 
ATOM   21296 C CG  . ASN K  1 293 ? 1.902   -27.727  -26.418 1.00 120.53 ? 293 ASN K CG  1 
ATOM   21297 O OD1 . ASN K  1 293 ? 0.703   -27.749  -26.700 1.00 111.97 ? 293 ASN K OD1 1 
ATOM   21298 N ND2 . ASN K  1 293 ? 2.613   -28.836  -26.204 1.00 120.95 ? 293 ASN K ND2 1 
ATOM   21299 N N   . THR K  1 294 ? -0.350  -24.672  -25.078 1.00 87.00  ? 294 THR K N   1 
ATOM   21300 C CA  . THR K  1 294 ? -1.185  -24.509  -23.888 1.00 99.02  ? 294 THR K CA  1 
ATOM   21301 C C   . THR K  1 294 ? -2.691  -24.626  -24.122 1.00 85.60  ? 294 THR K C   1 
ATOM   21302 O O   . THR K  1 294 ? -3.191  -24.386  -25.222 1.00 74.53  ? 294 THR K O   1 
ATOM   21303 C CB  . THR K  1 294 ? -0.928  -23.146  -23.221 1.00 86.58  ? 294 THR K CB  1 
ATOM   21304 O OG1 . THR K  1 294 ? -1.476  -23.146  -21.897 1.00 66.94  ? 294 THR K OG1 1 
ATOM   21305 C CG2 . THR K  1 294 ? -1.580  -22.040  -24.026 1.00 82.61  ? 294 THR K CG2 1 
ATOM   21306 N N   . SER K  1 295 ? -3.402  -24.989  -23.059 1.00 69.94  ? 295 SER K N   1 
ATOM   21307 C CA  . SER K  1 295 ? -4.858  -24.995  -23.051 1.00 80.16  ? 295 SER K CA  1 
ATOM   21308 C C   . SER K  1 295 ? -5.359  -23.872  -22.151 1.00 63.31  ? 295 SER K C   1 
ATOM   21309 O O   . SER K  1 295 ? -6.519  -23.470  -22.224 1.00 59.93  ? 295 SER K O   1 
ATOM   21310 C CB  . SER K  1 295 ? -5.387  -26.339  -22.545 1.00 76.85  ? 295 SER K CB  1 
ATOM   21311 O OG  . SER K  1 295 ? -6.016  -27.069  -23.583 1.00 100.46 ? 295 SER K OG  1 
ATOM   21312 N N   . LEU K  1 296 ? -4.465  -23.366  -21.306 1.00 54.78  ? 296 LEU K N   1 
ATOM   21313 C CA  . LEU K  1 296 ? -4.809  -22.337  -20.330 1.00 49.67  ? 296 LEU K CA  1 
ATOM   21314 C C   . LEU K  1 296 ? -5.293  -21.049  -20.992 1.00 53.08  ? 296 LEU K C   1 
ATOM   21315 O O   . LEU K  1 296 ? -4.840  -20.693  -22.079 1.00 51.93  ? 296 LEU K O   1 
ATOM   21316 C CB  . LEU K  1 296 ? -3.616  -22.055  -19.412 1.00 48.99  ? 296 LEU K CB  1 
ATOM   21317 C CG  . LEU K  1 296 ? -3.066  -23.274  -18.668 1.00 58.40  ? 296 LEU K CG  1 
ATOM   21318 C CD1 . LEU K  1 296 ? -1.946  -22.870  -17.716 1.00 57.53  ? 296 LEU K CD1 1 
ATOM   21319 C CD2 . LEU K  1 296 ? -4.181  -23.996  -17.921 1.00 48.06  ? 296 LEU K CD2 1 
ATOM   21320 N N   . PRO K  1 297 ? -6.223  -20.347  -20.327 1.00 51.57  ? 297 PRO K N   1 
ATOM   21321 C CA  . PRO K  1 297 ? -6.874  -19.145  -20.861 1.00 44.88  ? 297 PRO K CA  1 
ATOM   21322 C C   . PRO K  1 297 ? -5.959  -17.927  -20.886 1.00 46.51  ? 297 PRO K C   1 
ATOM   21323 O O   . PRO K  1 297 ? -6.191  -17.005  -21.668 1.00 47.77  ? 297 PRO K O   1 
ATOM   21324 C CB  . PRO K  1 297 ? -8.020  -18.896  -19.870 1.00 45.85  ? 297 PRO K CB  1 
ATOM   21325 C CG  . PRO K  1 297 ? -8.162  -20.168  -19.089 1.00 60.49  ? 297 PRO K CG  1 
ATOM   21326 C CD  . PRO K  1 297 ? -6.787  -20.739  -19.027 1.00 50.23  ? 297 PRO K CD  1 
ATOM   21327 N N   . PHE K  1 298 ? -4.937  -17.920  -20.038 1.00 47.53  ? 298 PHE K N   1 
ATOM   21328 C CA  . PHE K  1 298 ? -4.086  -16.747  -19.907 1.00 44.44  ? 298 PHE K CA  1 
ATOM   21329 C C   . PHE K  1 298 ? -2.607  -17.102  -19.912 1.00 43.18  ? 298 PHE K C   1 
ATOM   21330 O O   . PHE K  1 298 ? -2.200  -18.150  -19.410 1.00 52.72  ? 298 PHE K O   1 
ATOM   21331 C CB  . PHE K  1 298 ? -4.435  -15.979  -18.630 1.00 39.53  ? 298 PHE K CB  1 
ATOM   21332 C CG  . PHE K  1 298 ? -5.911  -15.875  -18.372 1.00 50.54  ? 298 PHE K CG  1 
ATOM   21333 C CD1 . PHE K  1 298 ? -6.691  -14.975  -19.078 1.00 37.02  ? 298 PHE K CD1 1 
ATOM   21334 C CD2 . PHE K  1 298 ? -6.518  -16.681  -17.424 1.00 49.13  ? 298 PHE K CD2 1 
ATOM   21335 C CE1 . PHE K  1 298 ? -8.050  -14.881  -18.842 1.00 50.75  ? 298 PHE K CE1 1 
ATOM   21336 C CE2 . PHE K  1 298 ? -7.876  -16.592  -17.183 1.00 46.54  ? 298 PHE K CE2 1 
ATOM   21337 C CZ  . PHE K  1 298 ? -8.644  -15.690  -17.894 1.00 41.84  ? 298 PHE K CZ  1 
ATOM   21338 N N   . GLN K  1 299 ? -1.812  -16.214  -20.494 1.00 44.59  ? 299 GLN K N   1 
ATOM   21339 C CA  . GLN K  1 299 ? -0.366  -16.343  -20.476 1.00 43.70  ? 299 GLN K CA  1 
ATOM   21340 C C   . GLN K  1 299 ? 0.227   -15.011  -20.023 1.00 46.96  ? 299 GLN K C   1 
ATOM   21341 O O   . GLN K  1 299 ? -0.418  -13.968  -20.150 1.00 73.48  ? 299 GLN K O   1 
ATOM   21342 C CB  . GLN K  1 299 ? 0.150   -16.752  -21.860 1.00 34.37  ? 299 GLN K CB  1 
ATOM   21343 C CG  . GLN K  1 299 ? -0.330  -15.871  -23.000 1.00 51.17  ? 299 GLN K CG  1 
ATOM   21344 C CD  . GLN K  1 299 ? 0.652   -14.769  -23.321 1.00 52.72  ? 299 GLN K CD  1 
ATOM   21345 O OE1 . GLN K  1 299 ? 1.779   -14.769  -22.824 1.00 41.43  ? 299 GLN K OE1 1 
ATOM   21346 N NE2 . GLN K  1 299 ? 0.235   -13.823  -24.155 1.00 46.75  ? 299 GLN K NE2 1 
ATOM   21347 N N   . ASN K  1 300 ? 1.437   -15.049  -19.472 1.00 48.93  ? 300 ASN K N   1 
ATOM   21348 C CA  . ASN K  1 300 ? 2.129   -13.831  -19.056 1.00 50.00  ? 300 ASN K CA  1 
ATOM   21349 C C   . ASN K  1 300 ? 3.531   -13.766  -19.651 1.00 42.22  ? 300 ASN K C   1 
ATOM   21350 O O   . ASN K  1 300 ? 4.402   -13.059  -19.145 1.00 51.07  ? 300 ASN K O   1 
ATOM   21351 C CB  . ASN K  1 300 ? 2.191   -13.719  -17.533 1.00 41.41  ? 300 ASN K CB  1 
ATOM   21352 C CG  . ASN K  1 300 ? 3.065   -14.783  -16.905 1.00 50.77  ? 300 ASN K CG  1 
ATOM   21353 O OD1 . ASN K  1 300 ? 3.459   -15.747  -17.561 1.00 56.91  ? 300 ASN K OD1 1 
ATOM   21354 N ND2 . ASN K  1 300 ? 3.374   -14.614  -15.625 1.00 47.78  ? 300 ASN K ND2 1 
ATOM   21355 N N   . ILE K  1 301 ? 3.735   -14.513  -20.731 1.00 40.86  ? 301 ILE K N   1 
ATOM   21356 C CA  . ILE K  1 301 ? 5.036   -14.601  -21.382 1.00 47.83  ? 301 ILE K CA  1 
ATOM   21357 C C   . ILE K  1 301 ? 5.367   -13.349  -22.189 1.00 48.40  ? 301 ILE K C   1 
ATOM   21358 O O   . ILE K  1 301 ? 6.396   -12.712  -21.965 1.00 50.80  ? 301 ILE K O   1 
ATOM   21359 C CB  . ILE K  1 301 ? 5.113   -15.830  -22.309 1.00 55.03  ? 301 ILE K CB  1 
ATOM   21360 C CG1 . ILE K  1 301 ? 4.979   -17.119  -21.496 1.00 41.52  ? 301 ILE K CG1 1 
ATOM   21361 C CG2 . ILE K  1 301 ? 6.413   -15.823  -23.102 1.00 41.49  ? 301 ILE K CG2 1 
ATOM   21362 C CD1 . ILE K  1 301 ? 4.920   -18.371  -22.340 1.00 60.01  ? 301 ILE K CD1 1 
ATOM   21363 N N   . HIS K  1 302 ? 4.492   -13.000  -23.126 1.00 51.84  ? 302 HIS K N   1 
ATOM   21364 C CA  . HIS K  1 302 ? 4.747   -11.875  -24.016 1.00 49.29  ? 302 HIS K CA  1 
ATOM   21365 C C   . HIS K  1 302 ? 3.449   -11.291  -24.571 1.00 48.23  ? 302 HIS K C   1 
ATOM   21366 O O   . HIS K  1 302 ? 2.526   -12.031  -24.913 1.00 41.55  ? 302 HIS K O   1 
ATOM   21367 C CB  . HIS K  1 302 ? 5.658   -12.314  -25.164 1.00 41.04  ? 302 HIS K CB  1 
ATOM   21368 C CG  . HIS K  1 302 ? 6.403   -11.189  -25.811 1.00 55.42  ? 302 HIS K CG  1 
ATOM   21369 N ND1 . HIS K  1 302 ? 5.835   -10.367  -26.759 1.00 60.16  ? 302 HIS K ND1 1 
ATOM   21370 C CD2 . HIS K  1 302 ? 7.676   -10.753  -25.648 1.00 58.10  ? 302 HIS K CD2 1 
ATOM   21371 C CE1 . HIS K  1 302 ? 6.725   -9.470   -27.151 1.00 52.72  ? 302 HIS K CE1 1 
ATOM   21372 N NE2 . HIS K  1 302 ? 7.848   -9.684   -26.493 1.00 43.93  ? 302 HIS K NE2 1 
ATOM   21373 N N   . PRO K  1 303 ? 3.376   -9.953   -24.654 1.00 48.42  ? 303 PRO K N   1 
ATOM   21374 C CA  . PRO K  1 303 ? 2.210   -9.226   -25.172 1.00 43.32  ? 303 PRO K CA  1 
ATOM   21375 C C   . PRO K  1 303 ? 2.029   -9.413   -26.677 1.00 48.71  ? 303 PRO K C   1 
ATOM   21376 O O   . PRO K  1 303 ? 0.909   -9.632   -27.139 1.00 42.49  ? 303 PRO K O   1 
ATOM   21377 C CB  . PRO K  1 303 ? 2.545   -7.761   -24.866 1.00 39.17  ? 303 PRO K CB  1 
ATOM   21378 C CG  . PRO K  1 303 ? 3.614   -7.810   -23.819 1.00 58.88  ? 303 PRO K CG  1 
ATOM   21379 C CD  . PRO K  1 303 ? 4.402   -9.038   -24.130 1.00 54.67  ? 303 PRO K CD  1 
ATOM   21380 N N   . ILE K  1 304 ? 3.120   -9.317   -27.430 1.00 28.83  ? 304 ILE K N   1 
ATOM   21381 C CA  . ILE K  1 304 ? 3.064   -9.512   -28.875 1.00 41.72  ? 304 ILE K CA  1 
ATOM   21382 C C   . ILE K  1 304 ? 2.996   -10.998  -29.198 1.00 41.13  ? 304 ILE K C   1 
ATOM   21383 O O   . ILE K  1 304 ? 3.864   -11.773  -28.796 1.00 52.64  ? 304 ILE K O   1 
ATOM   21384 C CB  . ILE K  1 304 ? 4.266   -8.869   -29.596 1.00 41.20  ? 304 ILE K CB  1 
ATOM   21385 C CG1 . ILE K  1 304 ? 4.097   -7.348   -29.667 1.00 34.23  ? 304 ILE K CG1 1 
ATOM   21386 C CG2 . ILE K  1 304 ? 4.402   -9.430   -31.001 1.00 54.78  ? 304 ILE K CG2 1 
ATOM   21387 C CD1 . ILE K  1 304 ? 4.076   -6.657   -28.321 1.00 44.26  ? 304 ILE K CD1 1 
ATOM   21388 N N   . THR K  1 305 ? 1.958   -11.389  -29.929 1.00 42.53  ? 305 THR K N   1 
ATOM   21389 C CA  . THR K  1 305 ? 1.678   -12.798  -30.161 1.00 37.08  ? 305 THR K CA  1 
ATOM   21390 C C   . THR K  1 305 ? 1.103   -13.025  -31.557 1.00 46.55  ? 305 THR K C   1 
ATOM   21391 O O   . THR K  1 305 ? 0.478   -12.134  -32.132 1.00 48.17  ? 305 THR K O   1 
ATOM   21392 C CB  . THR K  1 305 ? 0.684   -13.331  -29.106 1.00 40.59  ? 305 THR K CB  1 
ATOM   21393 O OG1 . THR K  1 305 ? 1.140   -14.592  -28.601 1.00 67.61  ? 305 THR K OG1 1 
ATOM   21394 C CG2 . THR K  1 305 ? -0.711  -13.484  -29.703 1.00 43.15  ? 305 THR K CG2 1 
ATOM   21395 N N   . ILE K  1 306 ? 1.322   -14.218  -32.100 1.00 37.19  ? 306 ILE K N   1 
ATOM   21396 C CA  . ILE K  1 306 ? 0.756   -14.585  -33.393 1.00 43.89  ? 306 ILE K CA  1 
ATOM   21397 C C   . ILE K  1 306 ? 0.067   -15.944  -33.319 1.00 48.08  ? 306 ILE K C   1 
ATOM   21398 O O   . ILE K  1 306 ? 0.600   -16.887  -32.734 1.00 47.95  ? 306 ILE K O   1 
ATOM   21399 C CB  . ILE K  1 306 ? 1.827   -14.624  -34.500 1.00 32.31  ? 306 ILE K CB  1 
ATOM   21400 C CG1 . ILE K  1 306 ? 2.603   -13.307  -34.543 1.00 32.86  ? 306 ILE K CG1 1 
ATOM   21401 C CG2 . ILE K  1 306 ? 1.185   -14.897  -35.849 1.00 37.86  ? 306 ILE K CG2 1 
ATOM   21402 C CD1 . ILE K  1 306 ? 3.556   -13.204  -35.714 1.00 39.39  ? 306 ILE K CD1 1 
ATOM   21403 N N   . GLY K  1 307 ? -1.118  -16.036  -33.914 1.00 40.45  ? 307 GLY K N   1 
ATOM   21404 C CA  . GLY K  1 307 ? -1.882  -17.271  -33.915 1.00 43.37  ? 307 GLY K CA  1 
ATOM   21405 C C   . GLY K  1 307 ? -3.117  -17.182  -33.040 1.00 46.16  ? 307 GLY K C   1 
ATOM   21406 O O   . GLY K  1 307 ? -3.630  -16.092  -32.786 1.00 55.59  ? 307 GLY K O   1 
ATOM   21407 N N   . LYS K  1 308 ? -3.602  -18.334  -32.589 1.00 46.72  ? 308 LYS K N   1 
ATOM   21408 C CA  . LYS K  1 308 ? -4.705  -18.383  -31.638 1.00 50.58  ? 308 LYS K CA  1 
ATOM   21409 C C   . LYS K  1 308 ? -4.132  -18.579  -30.239 1.00 44.12  ? 308 LYS K C   1 
ATOM   21410 O O   . LYS K  1 308 ? -3.838  -19.702  -29.830 1.00 54.79  ? 308 LYS K O   1 
ATOM   21411 C CB  . LYS K  1 308 ? -5.674  -19.515  -31.987 1.00 52.53  ? 308 LYS K CB  1 
ATOM   21412 C CG  . LYS K  1 308 ? -6.873  -19.597  -31.058 1.00 72.59  ? 308 LYS K CG  1 
ATOM   21413 C CD  . LYS K  1 308 ? -7.798  -20.752  -31.410 1.00 82.78  ? 308 LYS K CD  1 
ATOM   21414 C CE  . LYS K  1 308 ? -8.478  -20.535  -32.749 1.00 82.46  ? 308 LYS K CE  1 
ATOM   21415 N NZ  . LYS K  1 308 ? -9.817  -21.189  -32.787 1.00 86.61  ? 308 LYS K NZ  1 
ATOM   21416 N N   . CYS K  1 309 ? -3.974  -17.481  -29.508 1.00 43.15  ? 309 CYS K N   1 
ATOM   21417 C CA  . CYS K  1 309 ? -3.212  -17.503  -28.265 1.00 47.21  ? 309 CYS K CA  1 
ATOM   21418 C C   . CYS K  1 309 ? -4.043  -17.179  -27.030 1.00 43.98  ? 309 CYS K C   1 
ATOM   21419 O O   . CYS K  1 309 ? -5.092  -16.544  -27.128 1.00 42.55  ? 309 CYS K O   1 
ATOM   21420 C CB  . CYS K  1 309 ? -2.042  -16.524  -28.362 1.00 33.88  ? 309 CYS K CB  1 
ATOM   21421 S SG  . CYS K  1 309 ? -0.976  -16.795  -29.794 1.00 67.52  ? 309 CYS K SG  1 
ATOM   21422 N N   . PRO K  1 310 ? -3.567  -17.621  -25.856 1.00 48.46  ? 310 PRO K N   1 
ATOM   21423 C CA  . PRO K  1 310 ? -4.170  -17.225  -24.582 1.00 46.04  ? 310 PRO K CA  1 
ATOM   21424 C C   . PRO K  1 310 ? -4.044  -15.721  -24.416 1.00 49.47  ? 310 PRO K C   1 
ATOM   21425 O O   . PRO K  1 310 ? -3.200  -15.101  -25.063 1.00 49.82  ? 310 PRO K O   1 
ATOM   21426 C CB  . PRO K  1 310 ? -3.292  -17.928  -23.542 1.00 44.81  ? 310 PRO K CB  1 
ATOM   21427 C CG  . PRO K  1 310 ? -2.641  -19.036  -24.273 1.00 46.42  ? 310 PRO K CG  1 
ATOM   21428 C CD  . PRO K  1 310 ? -2.436  -18.543  -25.667 1.00 35.45  ? 310 PRO K CD  1 
ATOM   21429 N N   . LYS K  1 311 ? -4.869  -15.139  -23.557 1.00 44.86  ? 311 LYS K N   1 
ATOM   21430 C CA  . LYS K  1 311 ? -4.847  -13.698  -23.363 1.00 44.23  ? 311 LYS K CA  1 
ATOM   21431 C C   . LYS K  1 311 ? -3.659  -13.264  -22.505 1.00 46.03  ? 311 LYS K C   1 
ATOM   21432 O O   . LYS K  1 311 ? -3.335  -13.908  -21.508 1.00 48.82  ? 311 LYS K O   1 
ATOM   21433 C CB  . LYS K  1 311 ? -6.165  -13.231  -22.749 1.00 35.61  ? 311 LYS K CB  1 
ATOM   21434 C CG  . LYS K  1 311 ? -6.834  -12.124  -23.536 1.00 36.36  ? 311 LYS K CG  1 
ATOM   21435 C CD  . LYS K  1 311 ? -6.916  -12.443  -25.022 1.00 39.15  ? 311 LYS K CD  1 
ATOM   21436 C CE  . LYS K  1 311 ? -8.223  -13.121  -25.387 1.00 45.16  ? 311 LYS K CE  1 
ATOM   21437 N NZ  . LYS K  1 311 ? -8.443  -13.083  -26.859 1.00 41.44  ? 311 LYS K NZ  1 
ATOM   21438 N N   . TYR K  1 312 ? -3.005  -12.175  -22.908 1.00 40.70  ? 312 TYR K N   1 
ATOM   21439 C CA  . TYR K  1 312 ? -1.862  -11.646  -22.164 1.00 45.03  ? 312 TYR K CA  1 
ATOM   21440 C C   . TYR K  1 312 ? -2.301  -10.976  -20.871 1.00 44.69  ? 312 TYR K C   1 
ATOM   21441 O O   . TYR K  1 312 ? -3.139  -10.075  -20.878 1.00 48.65  ? 312 TYR K O   1 
ATOM   21442 C CB  . TYR K  1 312 ? -1.052  -10.651  -23.003 1.00 35.74  ? 312 TYR K CB  1 
ATOM   21443 C CG  . TYR K  1 312 ? 0.136   -10.060  -22.263 1.00 45.01  ? 312 TYR K CG  1 
ATOM   21444 C CD1 . TYR K  1 312 ? 1.248   -10.833  -21.973 1.00 46.40  ? 312 TYR K CD1 1 
ATOM   21445 C CD2 . TYR K  1 312 ? 0.147   -8.731   -21.858 1.00 51.23  ? 312 TYR K CD2 1 
ATOM   21446 C CE1 . TYR K  1 312 ? 2.337   -10.313  -21.294 1.00 44.95  ? 312 TYR K CE1 1 
ATOM   21447 C CE2 . TYR K  1 312 ? 1.237   -8.195   -21.179 1.00 46.40  ? 312 TYR K CE2 1 
ATOM   21448 C CZ  . TYR K  1 312 ? 2.328   -8.993   -20.901 1.00 52.82  ? 312 TYR K CZ  1 
ATOM   21449 O OH  . TYR K  1 312 ? 3.412   -8.472   -20.230 1.00 58.08  ? 312 TYR K OH  1 
ATOM   21450 N N   . VAL K  1 313 ? -1.722  -11.417  -19.762 1.00 56.29  ? 313 VAL K N   1 
ATOM   21451 C CA  . VAL K  1 313 ? -2.057  -10.872  -18.456 1.00 46.45  ? 313 VAL K CA  1 
ATOM   21452 C C   . VAL K  1 313 ? -0.785  -10.495  -17.707 1.00 46.53  ? 313 VAL K C   1 
ATOM   21453 O O   . VAL K  1 313 ? 0.256   -11.132  -17.872 1.00 51.91  ? 313 VAL K O   1 
ATOM   21454 C CB  . VAL K  1 313 ? -2.880  -11.877  -17.627 1.00 47.26  ? 313 VAL K CB  1 
ATOM   21455 C CG1 . VAL K  1 313 ? -3.140  -11.338  -16.236 1.00 56.97  ? 313 VAL K CG1 1 
ATOM   21456 C CG2 . VAL K  1 313 ? -4.192  -12.190  -18.330 1.00 55.71  ? 313 VAL K CG2 1 
ATOM   21457 N N   . LYS K  1 314 ? -0.874  -9.452   -16.890 1.00 42.68  ? 314 LYS K N   1 
ATOM   21458 C CA  . LYS K  1 314 ? 0.277   -8.953   -16.150 1.00 53.02  ? 314 LYS K CA  1 
ATOM   21459 C C   . LYS K  1 314 ? 0.447   -9.715   -14.841 1.00 53.48  ? 314 LYS K C   1 
ATOM   21460 O O   . LYS K  1 314 ? 1.325   -9.403   -14.036 1.00 62.87  ? 314 LYS K O   1 
ATOM   21461 C CB  . LYS K  1 314 ? 0.100   -7.463   -15.867 1.00 53.53  ? 314 LYS K CB  1 
ATOM   21462 C CG  . LYS K  1 314 ? 1.384   -6.712   -15.574 1.00 74.65  ? 314 LYS K CG  1 
ATOM   21463 C CD  . LYS K  1 314 ? 1.086   -5.236   -15.403 1.00 100.91 ? 314 LYS K CD  1 
ATOM   21464 C CE  . LYS K  1 314 ? 0.266   -4.717   -16.574 1.00 96.62  ? 314 LYS K CE  1 
ATOM   21465 N NZ  . LYS K  1 314 ? -0.549  -3.531   -16.197 1.00 76.39  ? 314 LYS K NZ  1 
ATOM   21466 N N   . SER K  1 315 ? -0.401  -10.717  -14.635 1.00 61.14  ? 315 SER K N   1 
ATOM   21467 C CA  . SER K  1 315 ? -0.374  -11.507  -13.411 1.00 62.05  ? 315 SER K CA  1 
ATOM   21468 C C   . SER K  1 315 ? 0.915   -12.310  -13.276 1.00 60.01  ? 315 SER K C   1 
ATOM   21469 O O   . SER K  1 315 ? 1.539   -12.680  -14.271 1.00 56.24  ? 315 SER K O   1 
ATOM   21470 C CB  . SER K  1 315 ? -1.579  -12.448  -13.352 1.00 55.81  ? 315 SER K CB  1 
ATOM   21471 O OG  . SER K  1 315 ? -2.793  -11.722  -13.285 1.00 71.15  ? 315 SER K OG  1 
ATOM   21472 N N   . THR K  1 316 ? 1.305   -12.570  -12.034 1.00 58.64  ? 316 THR K N   1 
ATOM   21473 C CA  . THR K  1 316 ? 2.460   -13.409  -11.746 1.00 64.40  ? 316 THR K CA  1 
ATOM   21474 C C   . THR K  1 316 ? 2.004   -14.840  -11.490 1.00 65.48  ? 316 THR K C   1 
ATOM   21475 O O   . THR K  1 316 ? 2.704   -15.798  -11.820 1.00 65.09  ? 316 THR K O   1 
ATOM   21476 C CB  . THR K  1 316 ? 3.237   -12.894  -10.522 1.00 64.55  ? 316 THR K CB  1 
ATOM   21477 O OG1 . THR K  1 316 ? 4.104   -13.925  -10.036 1.00 94.21  ? 316 THR K OG1 1 
ATOM   21478 C CG2 . THR K  1 316 ? 2.276   -12.487  -9.416  1.00 70.53  ? 316 THR K CG2 1 
ATOM   21479 N N   . LYS K  1 317 ? 0.820   -14.972  -10.901 1.00 73.78  ? 317 LYS K N   1 
ATOM   21480 C CA  . LYS K  1 317 ? 0.229   -16.276  -10.632 1.00 66.28  ? 317 LYS K CA  1 
ATOM   21481 C C   . LYS K  1 317 ? -1.294  -16.198  -10.634 1.00 55.23  ? 317 LYS K C   1 
ATOM   21482 O O   . LYS K  1 317 ? -1.877  -15.200  -10.212 1.00 63.92  ? 317 LYS K O   1 
ATOM   21483 C CB  . LYS K  1 317 ? 0.726   -16.829  -9.293  1.00 72.51  ? 317 LYS K CB  1 
ATOM   21484 C CG  . LYS K  1 317 ? 0.521   -15.886  -8.117  1.00 75.90  ? 317 LYS K CG  1 
ATOM   21485 C CD  . LYS K  1 317 ? 0.929   -16.537  -6.804  1.00 95.61  ? 317 LYS K CD  1 
ATOM   21486 C CE  . LYS K  1 317 ? 0.002   -17.688  -6.444  1.00 93.48  ? 317 LYS K CE  1 
ATOM   21487 N NZ  . LYS K  1 317 ? 0.364   -18.304  -5.137  1.00 75.06  ? 317 LYS K NZ  1 
ATOM   21488 N N   . LEU K  1 318 ? -1.931  -17.258  -11.121 1.00 56.38  ? 318 LEU K N   1 
ATOM   21489 C CA  . LEU K  1 318 ? -3.386  -17.351  -11.130 1.00 61.24  ? 318 LEU K CA  1 
ATOM   21490 C C   . LEU K  1 318 ? -3.818  -18.728  -10.644 1.00 56.22  ? 318 LEU K C   1 
ATOM   21491 O O   . LEU K  1 318 ? -4.522  -19.453  -11.347 1.00 56.17  ? 318 LEU K O   1 
ATOM   21492 C CB  . LEU K  1 318 ? -3.935  -17.096  -12.535 1.00 47.87  ? 318 LEU K CB  1 
ATOM   21493 C CG  . LEU K  1 318 ? -3.878  -15.658  -13.055 1.00 43.11  ? 318 LEU K CG  1 
ATOM   21494 C CD1 . LEU K  1 318 ? -4.256  -15.601  -14.528 1.00 59.46  ? 318 LEU K CD1 1 
ATOM   21495 C CD2 . LEU K  1 318 ? -4.783  -14.755  -12.230 1.00 42.29  ? 318 LEU K CD2 1 
ATOM   21496 N N   . ARG K  1 319 ? -3.389  -19.085  -9.438  1.00 59.60  ? 319 ARG K N   1 
ATOM   21497 C CA  . ARG K  1 319 ? -3.655  -20.412  -8.895  1.00 62.98  ? 319 ARG K CA  1 
ATOM   21498 C C   . ARG K  1 319 ? -5.114  -20.582  -8.476  1.00 53.00  ? 319 ARG K C   1 
ATOM   21499 O O   . ARG K  1 319 ? -5.616  -19.862  -7.612  1.00 45.51  ? 319 ARG K O   1 
ATOM   21500 C CB  . ARG K  1 319 ? -2.711  -20.718  -7.729  1.00 70.05  ? 319 ARG K CB  1 
ATOM   21501 C CG  . ARG K  1 319 ? -2.814  -22.142  -7.210  1.00 67.43  ? 319 ARG K CG  1 
ATOM   21502 C CD  . ARG K  1 319 ? -1.466  -22.658  -6.729  1.00 74.54  ? 319 ARG K CD  1 
ATOM   21503 N NE  . ARG K  1 319 ? -0.559  -22.942  -7.838  1.00 75.04  ? 319 ARG K NE  1 
ATOM   21504 C CZ  . ARG K  1 319 ? -0.513  -24.101  -8.487  1.00 77.16  ? 319 ARG K CZ  1 
ATOM   21505 N NH1 . ARG K  1 319 ? -1.327  -25.089  -8.141  1.00 81.37  ? 319 ARG K NH1 1 
ATOM   21506 N NH2 . ARG K  1 319 ? 0.344   -24.274  -9.484  1.00 81.92  ? 319 ARG K NH2 1 
ATOM   21507 N N   . LEU K  1 320 ? -5.782  -21.547  -9.100  1.00 51.57  ? 320 LEU K N   1 
ATOM   21508 C CA  . LEU K  1 320 ? -7.201  -21.792  -8.876  1.00 43.52  ? 320 LEU K CA  1 
ATOM   21509 C C   . LEU K  1 320 ? -7.411  -22.986  -7.950  1.00 49.87  ? 320 LEU K C   1 
ATOM   21510 O O   . LEU K  1 320 ? -7.013  -24.106  -8.268  1.00 59.88  ? 320 LEU K O   1 
ATOM   21511 C CB  . LEU K  1 320 ? -7.897  -22.048  -10.214 1.00 52.81  ? 320 LEU K CB  1 
ATOM   21512 C CG  . LEU K  1 320 ? -9.424  -22.115  -10.235 1.00 51.05  ? 320 LEU K CG  1 
ATOM   21513 C CD1 . LEU K  1 320 ? -10.019 -20.737  -9.996  1.00 41.74  ? 320 LEU K CD1 1 
ATOM   21514 C CD2 . LEU K  1 320 ? -9.909  -22.684  -11.559 1.00 40.20  ? 320 LEU K CD2 1 
ATOM   21515 N N   . ALA K  1 321 ? -8.042  -22.741  -6.806  1.00 51.02  ? 321 ALA K N   1 
ATOM   21516 C CA  . ALA K  1 321 ? -8.291  -23.790  -5.823  1.00 51.92  ? 321 ALA K CA  1 
ATOM   21517 C C   . ALA K  1 321 ? -9.256  -24.849  -6.349  1.00 51.53  ? 321 ALA K C   1 
ATOM   21518 O O   . ALA K  1 321 ? -10.341 -24.529  -6.829  1.00 56.84  ? 321 ALA K O   1 
ATOM   21519 C CB  . ALA K  1 321 ? -8.821  -23.188  -4.531  1.00 48.18  ? 321 ALA K CB  1 
ATOM   21520 N N   . THR K  1 322 ? -8.851  -26.111  -6.254  1.00 58.33  ? 322 THR K N   1 
ATOM   21521 C CA  . THR K  1 322 ? -9.695  -27.224  -6.673  1.00 59.26  ? 322 THR K CA  1 
ATOM   21522 C C   . THR K  1 322 ? -10.083 -28.051  -5.458  1.00 62.94  ? 322 THR K C   1 
ATOM   21523 O O   . THR K  1 322 ? -11.207 -28.546  -5.349  1.00 53.94  ? 322 THR K O   1 
ATOM   21524 C CB  . THR K  1 322 ? -8.972  -28.130  -7.682  1.00 53.24  ? 322 THR K CB  1 
ATOM   21525 O OG1 . THR K  1 322 ? -7.766  -28.638  -7.096  1.00 62.03  ? 322 THR K OG1 1 
ATOM   21526 C CG2 . THR K  1 322 ? -8.632  -27.353  -8.940  1.00 67.36  ? 322 THR K CG2 1 
ATOM   21527 N N   . GLY K  1 323 ? -9.133  -28.198  -4.545  1.00 64.72  ? 323 GLY K N   1 
ATOM   21528 C CA  . GLY K  1 323 ? -9.385  -28.891  -3.303  1.00 59.75  ? 323 GLY K CA  1 
ATOM   21529 C C   . GLY K  1 323 ? -10.027 -27.988  -2.273  1.00 64.63  ? 323 GLY K C   1 
ATOM   21530 O O   . GLY K  1 323 ? -10.658 -26.983  -2.603  1.00 63.80  ? 323 GLY K O   1 
ATOM   21531 N N   . LEU K  1 324 ? -9.833  -28.357  -1.014  1.00 60.10  ? 324 LEU K N   1 
ATOM   21532 C CA  . LEU K  1 324 ? -10.436 -27.675  0.117   1.00 66.34  ? 324 LEU K CA  1 
ATOM   21533 C C   . LEU K  1 324 ? -9.350  -26.948  0.910   1.00 71.02  ? 324 LEU K C   1 
ATOM   21534 O O   . LEU K  1 324 ? -8.208  -26.861  0.457   1.00 81.28  ? 324 LEU K O   1 
ATOM   21535 C CB  . LEU K  1 324 ? -11.200 -28.684  0.990   1.00 71.04  ? 324 LEU K CB  1 
ATOM   21536 C CG  . LEU K  1 324 ? -10.911 -30.194  0.932   1.00 68.13  ? 324 LEU K CG  1 
ATOM   21537 C CD1 . LEU K  1 324 ? -11.944 -30.933  1.759   1.00 67.78  ? 324 LEU K CD1 1 
ATOM   21538 C CD2 . LEU K  1 324 ? -10.895 -30.763  -0.481  1.00 62.23  ? 324 LEU K CD2 1 
ATOM   21539 N N   . ARG K  1 325 ? -9.700  -26.392  2.066   1.00 70.99  ? 325 ARG K N   1 
ATOM   21540 C CA  . ARG K  1 325 ? -8.683  -25.857  2.962   1.00 74.69  ? 325 ARG K CA  1 
ATOM   21541 C C   . ARG K  1 325 ? -7.741  -26.997  3.313   1.00 76.11  ? 325 ARG K C   1 
ATOM   21542 O O   . ARG K  1 325 ? -7.946  -28.129  2.874   1.00 72.05  ? 325 ARG K O   1 
ATOM   21543 C CB  . ARG K  1 325 ? -9.303  -25.289  4.239   1.00 70.87  ? 325 ARG K CB  1 
ATOM   21544 C CG  . ARG K  1 325 ? -9.881  -23.888  4.096   1.00 75.93  ? 325 ARG K CG  1 
ATOM   21545 C CD  . ARG K  1 325 ? -9.395  -22.964  5.212   1.00 85.88  ? 325 ARG K CD  1 
ATOM   21546 N NE  . ARG K  1 325 ? -10.346 -21.890  5.496   1.00 94.97  ? 325 ARG K NE  1 
ATOM   21547 C CZ  . ARG K  1 325 ? -10.013 -20.613  5.664   1.00 96.76  ? 325 ARG K CZ  1 
ATOM   21548 N NH1 . ARG K  1 325 ? -8.746  -20.235  5.571   1.00 83.65  ? 325 ARG K NH1 1 
ATOM   21549 N NH2 . ARG K  1 325 ? -10.949 -19.710  5.926   1.00 90.27  ? 325 ARG K NH2 1 
ATOM   21550 N N   . ASN K  1 326 ? -6.707  -26.708  4.094   1.00 91.29  ? 326 ASN K N   1 
ATOM   21551 C CA  . ASN K  1 326 ? -5.789  -27.753  4.528   1.00 91.78  ? 326 ASN K CA  1 
ATOM   21552 C C   . ASN K  1 326 ? -5.375  -27.599  5.984   1.00 92.67  ? 326 ASN K C   1 
ATOM   21553 O O   . ASN K  1 326 ? -4.999  -26.513  6.426   1.00 96.45  ? 326 ASN K O   1 
ATOM   21554 C CB  . ASN K  1 326 ? -4.549  -27.795  3.639   1.00 93.70  ? 326 ASN K CB  1 
ATOM   21555 C CG  . ASN K  1 326 ? -3.770  -29.084  3.796   1.00 102.89 ? 326 ASN K CG  1 
ATOM   21556 O OD1 . ASN K  1 326 ? -4.350  -30.152  4.002   1.00 108.23 ? 326 ASN K OD1 1 
ATOM   21557 N ND2 . ASN K  1 326 ? -2.450  -28.995  3.693   1.00 106.89 ? 326 ASN K ND2 1 
ATOM   21558 N N   . ILE K  1 327 ? -5.430  -28.700  6.724   1.00 99.20  ? 327 ILE K N   1 
ATOM   21559 C CA  . ILE K  1 327 ? -5.123  -28.668  8.143   1.00 101.23 ? 327 ILE K CA  1 
ATOM   21560 C C   . ILE K  1 327 ? -4.200  -29.817  8.535   1.00 90.35  ? 327 ILE K C   1 
ATOM   21561 O O   . ILE K  1 327 ? -3.981  -30.745  7.753   1.00 83.38  ? 327 ILE K O   1 
ATOM   21562 C CB  . ILE K  1 327 ? -6.408  -28.730  8.982   1.00 87.55  ? 327 ILE K CB  1 
ATOM   21563 C CG1 . ILE K  1 327 ? -7.416  -27.686  8.494   1.00 78.67  ? 327 ILE K CG1 1 
ATOM   21564 C CG2 . ILE K  1 327 ? -6.094  -28.514  10.447  1.00 97.46  ? 327 ILE K CG2 1 
ATOM   21565 C CD1 . ILE K  1 327 ? -7.012  -26.255  8.791   1.00 75.03  ? 327 ILE K CD1 1 
ATOM   21566 N N   . LEU L  2 2   ? -18.326 -21.058  4.968   1.00 72.91  ? 2   LEU L N   1 
ATOM   21567 C CA  . LEU L  2 2   ? -19.620 -20.397  4.846   1.00 75.10  ? 2   LEU L CA  1 
ATOM   21568 C C   . LEU L  2 2   ? -20.726 -21.264  5.434   1.00 67.42  ? 2   LEU L C   1 
ATOM   21569 O O   . LEU L  2 2   ? -21.786 -20.767  5.810   1.00 66.50  ? 2   LEU L O   1 
ATOM   21570 C CB  . LEU L  2 2   ? -19.927 -20.088  3.380   1.00 65.68  ? 2   LEU L CB  1 
ATOM   21571 C CG  . LEU L  2 2   ? -20.947 -18.979  3.114   1.00 70.15  ? 2   LEU L CG  1 
ATOM   21572 C CD1 . LEU L  2 2   ? -20.444 -17.652  3.661   1.00 72.18  ? 2   LEU L CD1 1 
ATOM   21573 C CD2 . LEU L  2 2   ? -21.249 -18.869  1.627   1.00 38.94  ? 2   LEU L CD2 1 
ATOM   21574 N N   . PHE L  2 3   ? -20.471 -22.566  5.507   1.00 64.60  ? 3   PHE L N   1 
ATOM   21575 C CA  . PHE L  2 3   ? -21.444 -23.506  6.049   1.00 71.48  ? 3   PHE L CA  1 
ATOM   21576 C C   . PHE L  2 3   ? -21.055 -23.981  7.448   1.00 77.57  ? 3   PHE L C   1 
ATOM   21577 O O   . PHE L  2 3   ? -21.728 -24.828  8.033   1.00 75.16  ? 3   PHE L O   1 
ATOM   21578 C CB  . PHE L  2 3   ? -21.630 -24.693  5.101   1.00 70.65  ? 3   PHE L CB  1 
ATOM   21579 C CG  . PHE L  2 3   ? -22.319 -24.335  3.814   1.00 73.36  ? 3   PHE L CG  1 
ATOM   21580 C CD1 . PHE L  2 3   ? -21.594 -23.874  2.727   1.00 69.20  ? 3   PHE L CD1 1 
ATOM   21581 C CD2 . PHE L  2 3   ? -23.694 -24.454  3.694   1.00 77.41  ? 3   PHE L CD2 1 
ATOM   21582 C CE1 . PHE L  2 3   ? -22.228 -23.541  1.544   1.00 60.96  ? 3   PHE L CE1 1 
ATOM   21583 C CE2 . PHE L  2 3   ? -24.333 -24.123  2.514   1.00 66.33  ? 3   PHE L CE2 1 
ATOM   21584 C CZ  . PHE L  2 3   ? -23.599 -23.666  1.438   1.00 67.99  ? 3   PHE L CZ  1 
ATOM   21585 N N   . GLY L  2 4   ? -19.965 -23.431  7.975   1.00 84.54  ? 4   GLY L N   1 
ATOM   21586 C CA  . GLY L  2 4   ? -19.558 -23.687  9.345   1.00 83.89  ? 4   GLY L CA  1 
ATOM   21587 C C   . GLY L  2 4   ? -18.967 -25.060  9.607   1.00 86.82  ? 4   GLY L C   1 
ATOM   21588 O O   . GLY L  2 4   ? -18.610 -25.379  10.742  1.00 93.79  ? 4   GLY L O   1 
ATOM   21589 N N   . ALA L  2 5   ? -18.859 -25.875  8.564   1.00 77.08  ? 5   ALA L N   1 
ATOM   21590 C CA  . ALA L  2 5   ? -18.337 -27.230  8.714   1.00 69.81  ? 5   ALA L CA  1 
ATOM   21591 C C   . ALA L  2 5   ? -16.811 -27.258  8.712   1.00 69.64  ? 5   ALA L C   1 
ATOM   21592 O O   . ALA L  2 5   ? -16.185 -27.487  9.747   1.00 67.58  ? 5   ALA L O   1 
ATOM   21593 C CB  . ALA L  2 5   ? -18.890 -28.139  7.624   1.00 64.42  ? 5   ALA L CB  1 
ATOM   21594 N N   . ILE L  2 6   ? -16.219 -27.028  7.545   1.00 76.61  ? 6   ILE L N   1 
ATOM   21595 C CA  . ILE L  2 6   ? -14.767 -27.048  7.407   1.00 65.49  ? 6   ILE L CA  1 
ATOM   21596 C C   . ILE L  2 6   ? -14.130 -25.865  8.128   1.00 70.80  ? 6   ILE L C   1 
ATOM   21597 O O   . ILE L  2 6   ? -14.489 -24.712  7.886   1.00 67.75  ? 6   ILE L O   1 
ATOM   21598 C CB  . ILE L  2 6   ? -14.337 -27.055  5.930   1.00 61.00  ? 6   ILE L CB  1 
ATOM   21599 C CG1 . ILE L  2 6   ? -14.919 -28.279  5.219   1.00 49.40  ? 6   ILE L CG1 1 
ATOM   21600 C CG2 . ILE L  2 6   ? -12.822 -27.045  5.816   1.00 51.05  ? 6   ILE L CG2 1 
ATOM   21601 C CD1 . ILE L  2 6   ? -14.417 -28.463  3.804   1.00 57.27  ? 6   ILE L CD1 1 
ATOM   21602 N N   . ALA L  2 7   ? -13.182 -26.163  9.012   1.00 72.75  ? 7   ALA L N   1 
ATOM   21603 C CA  . ALA L  2 7   ? -12.578 -25.152  9.871   1.00 70.92  ? 7   ALA L CA  1 
ATOM   21604 C C   . ALA L  2 7   ? -13.636 -24.538  10.783  1.00 75.44  ? 7   ALA L C   1 
ATOM   21605 O O   . ALA L  2 7   ? -13.501 -23.400  11.232  1.00 78.72  ? 7   ALA L O   1 
ATOM   21606 C CB  . ALA L  2 7   ? -11.890 -24.078  9.041   1.00 69.77  ? 7   ALA L CB  1 
ATOM   21607 N N   . GLY L  2 8   ? -14.689 -25.307  11.047  1.00 82.59  ? 8   GLY L N   1 
ATOM   21608 C CA  . GLY L  2 8   ? -15.768 -24.875  11.918  1.00 82.12  ? 8   GLY L CA  1 
ATOM   21609 C C   . GLY L  2 8   ? -15.930 -25.801  13.109  1.00 89.85  ? 8   GLY L C   1 
ATOM   21610 O O   . GLY L  2 8   ? -15.020 -25.923  13.930  1.00 91.33  ? 8   GLY L O   1 
ATOM   21611 N N   . PHE L  2 9   ? -17.084 -26.456  13.210  1.00 68.90  ? 9   PHE L N   1 
ATOM   21612 C CA  . PHE L  2 9   ? -17.310 -27.410  14.293  1.00 73.51  ? 9   PHE L CA  1 
ATOM   21613 C C   . PHE L  2 9   ? -16.529 -28.702  14.061  1.00 88.13  ? 9   PHE L C   1 
ATOM   21614 O O   . PHE L  2 9   ? -16.310 -29.483  14.988  1.00 106.31 ? 9   PHE L O   1 
ATOM   21615 C CB  . PHE L  2 9   ? -18.804 -27.683  14.514  1.00 82.54  ? 9   PHE L CB  1 
ATOM   21616 C CG  . PHE L  2 9   ? -19.527 -28.189  13.297  1.00 85.74  ? 9   PHE L CG  1 
ATOM   21617 C CD1 . PHE L  2 9   ? -19.380 -29.502  12.880  1.00 89.17  ? 9   PHE L CD1 1 
ATOM   21618 C CD2 . PHE L  2 9   ? -20.379 -27.359  12.588  1.00 91.08  ? 9   PHE L CD2 1 
ATOM   21619 C CE1 . PHE L  2 9   ? -20.053 -29.970  11.767  1.00 80.34  ? 9   PHE L CE1 1 
ATOM   21620 C CE2 . PHE L  2 9   ? -21.056 -27.822  11.475  1.00 92.78  ? 9   PHE L CE2 1 
ATOM   21621 C CZ  . PHE L  2 9   ? -20.892 -29.130  11.064  1.00 94.34  ? 9   PHE L CZ  1 
ATOM   21622 N N   . ILE L  2 10  ? -16.116 -28.919  12.816  1.00 69.58  ? 10  ILE L N   1 
ATOM   21623 C CA  . ILE L  2 10  ? -15.139 -29.953  12.500  1.00 70.06  ? 10  ILE L CA  1 
ATOM   21624 C C   . ILE L  2 10  ? -13.809 -29.249  12.262  1.00 80.97  ? 10  ILE L C   1 
ATOM   21625 O O   . ILE L  2 10  ? -13.531 -28.785  11.158  1.00 81.82  ? 10  ILE L O   1 
ATOM   21626 C CB  . ILE L  2 10  ? -15.532 -30.761  11.252  1.00 59.00  ? 10  ILE L CB  1 
ATOM   21627 C CG1 . ILE L  2 10  ? -16.976 -31.249  11.365  1.00 66.13  ? 10  ILE L CG1 1 
ATOM   21628 C CG2 . ILE L  2 10  ? -14.587 -31.938  11.058  1.00 53.29  ? 10  ILE L CG2 1 
ATOM   21629 C CD1 . ILE L  2 10  ? -17.436 -32.066  10.180  1.00 63.31  ? 10  ILE L CD1 1 
ATOM   21630 N N   . GLU L  2 11  ? -12.997 -29.169  13.310  1.00 98.60  ? 11  GLU L N   1 
ATOM   21631 C CA  . GLU L  2 11  ? -11.819 -28.305  13.324  1.00 102.01 ? 11  GLU L CA  1 
ATOM   21632 C C   . GLU L  2 11  ? -10.720 -28.687  12.333  1.00 82.49  ? 11  GLU L C   1 
ATOM   21633 O O   . GLU L  2 11  ? -10.064 -27.813  11.765  1.00 84.42  ? 11  GLU L O   1 
ATOM   21634 C CB  . GLU L  2 11  ? -11.238 -28.237  14.739  1.00 114.20 ? 11  GLU L CB  1 
ATOM   21635 C CG  . GLU L  2 11  ? -12.238 -27.800  15.796  1.00 127.24 ? 11  GLU L CG  1 
ATOM   21636 C CD  . GLU L  2 11  ? -11.672 -27.876  17.200  1.00 163.90 ? 11  GLU L CD  1 
ATOM   21637 O OE1 . GLU L  2 11  ? -12.413 -27.571  18.158  1.00 170.20 ? 11  GLU L OE1 1 
ATOM   21638 O OE2 . GLU L  2 11  ? -10.487 -28.242  17.345  1.00 162.13 ? 11  GLU L OE2 1 
ATOM   21639 N N   . GLY L  2 12  ? -10.512 -29.983  12.129  1.00 79.14  ? 12  GLY L N   1 
ATOM   21640 C CA  . GLY L  2 12  ? -9.390  -30.432  11.325  1.00 76.98  ? 12  GLY L CA  1 
ATOM   21641 C C   . GLY L  2 12  ? -9.709  -31.450  10.248  1.00 75.79  ? 12  GLY L C   1 
ATOM   21642 O O   . GLY L  2 12  ? -10.804 -32.013  10.203  1.00 79.80  ? 12  GLY L O   1 
ATOM   21643 N N   . GLY L  2 13  ? -8.734  -31.683  9.375   1.00 73.51  ? 13  GLY L N   1 
ATOM   21644 C CA  . GLY L  2 13  ? -8.863  -32.664  8.314   1.00 72.57  ? 13  GLY L CA  1 
ATOM   21645 C C   . GLY L  2 13  ? -8.136  -33.951  8.653   1.00 70.63  ? 13  GLY L C   1 
ATOM   21646 O O   . GLY L  2 13  ? -7.436  -34.030  9.662   1.00 78.28  ? 13  GLY L O   1 
ATOM   21647 N N   . TRP L  2 14  ? -8.298  -34.960  7.803   1.00 67.23  ? 14  TRP L N   1 
ATOM   21648 C CA  . TRP L  2 14  ? -7.713  -36.271  8.056   1.00 76.07  ? 14  TRP L CA  1 
ATOM   21649 C C   . TRP L  2 14  ? -6.701  -36.670  6.991   1.00 82.04  ? 14  TRP L C   1 
ATOM   21650 O O   . TRP L  2 14  ? -7.074  -37.068  5.887   1.00 78.82  ? 14  TRP L O   1 
ATOM   21651 C CB  . TRP L  2 14  ? -8.804  -37.340  8.136   1.00 76.87  ? 14  TRP L CB  1 
ATOM   21652 C CG  . TRP L  2 14  ? -9.762  -37.156  9.267   1.00 76.27  ? 14  TRP L CG  1 
ATOM   21653 C CD1 . TRP L  2 14  ? -9.547  -36.460  10.421  1.00 78.02  ? 14  TRP L CD1 1 
ATOM   21654 C CD2 . TRP L  2 14  ? -11.085 -37.696  9.364   1.00 72.24  ? 14  TRP L CD2 1 
ATOM   21655 N NE1 . TRP L  2 14  ? -10.658 -36.525  11.226  1.00 73.41  ? 14  TRP L NE1 1 
ATOM   21656 C CE2 . TRP L  2 14  ? -11.616 -37.279  10.601  1.00 78.80  ? 14  TRP L CE2 1 
ATOM   21657 C CE3 . TRP L  2 14  ? -11.873 -38.490  8.525   1.00 69.68  ? 14  TRP L CE3 1 
ATOM   21658 C CZ2 . TRP L  2 14  ? -12.899 -37.628  11.017  1.00 82.93  ? 14  TRP L CZ2 1 
ATOM   21659 C CZ3 . TRP L  2 14  ? -13.146 -38.835  8.940   1.00 82.99  ? 14  TRP L CZ3 1 
ATOM   21660 C CH2 . TRP L  2 14  ? -13.646 -38.405  10.175  1.00 88.61  ? 14  TRP L CH2 1 
ATOM   21661 N N   . THR L  2 15  ? -5.421  -36.573  7.331   1.00 89.73  ? 15  THR L N   1 
ATOM   21662 C CA  . THR L  2 15  ? -4.361  -37.028  6.443   1.00 87.95  ? 15  THR L CA  1 
ATOM   21663 C C   . THR L  2 15  ? -4.535  -38.514  6.158   1.00 96.97  ? 15  THR L C   1 
ATOM   21664 O O   . THR L  2 15  ? -4.098  -39.016  5.123   1.00 96.66  ? 15  THR L O   1 
ATOM   21665 C CB  . THR L  2 15  ? -2.976  -36.815  7.073   1.00 91.13  ? 15  THR L CB  1 
ATOM   21666 O OG1 . THR L  2 15  ? -2.874  -37.593  8.272   1.00 126.68 ? 15  THR L OG1 1 
ATOM   21667 C CG2 . THR L  2 15  ? -2.761  -35.347  7.409   1.00 90.75  ? 15  THR L CG2 1 
ATOM   21668 N N   . GLY L  2 16  ? -5.184  -39.208  7.088   1.00 93.11  ? 16  GLY L N   1 
ATOM   21669 C CA  . GLY L  2 16  ? -5.352  -40.648  7.007   1.00 100.70 ? 16  GLY L CA  1 
ATOM   21670 C C   . GLY L  2 16  ? -6.300  -41.107  5.917   1.00 93.10  ? 16  GLY L C   1 
ATOM   21671 O O   . GLY L  2 16  ? -6.087  -42.150  5.299   1.00 97.39  ? 16  GLY L O   1 
ATOM   21672 N N   . MET L  2 17  ? -7.358  -40.337  5.686   1.00 96.92  ? 17  MET L N   1 
ATOM   21673 C CA  . MET L  2 17  ? -8.300  -40.659  4.623   1.00 98.52  ? 17  MET L CA  1 
ATOM   21674 C C   . MET L  2 17  ? -7.755  -40.176  3.285   1.00 100.35 ? 17  MET L C   1 
ATOM   21675 O O   . MET L  2 17  ? -7.693  -38.975  3.026   1.00 102.19 ? 17  MET L O   1 
ATOM   21676 C CB  . MET L  2 17  ? -9.667  -40.035  4.898   1.00 81.95  ? 17  MET L CB  1 
ATOM   21677 C CG  . MET L  2 17  ? -10.715 -40.393  3.861   1.00 92.10  ? 17  MET L CG  1 
ATOM   21678 S SD  . MET L  2 17  ? -12.335 -39.716  4.253   1.00 92.47  ? 17  MET L SD  1 
ATOM   21679 C CE  . MET L  2 17  ? -11.935 -37.980  4.419   1.00 88.70  ? 17  MET L CE  1 
ATOM   21680 N N   . VAL L  2 18  ? -7.358  -41.124  2.443   1.00 111.63 ? 18  VAL L N   1 
ATOM   21681 C CA  . VAL L  2 18  ? -6.732  -40.805  1.166   1.00 112.97 ? 18  VAL L CA  1 
ATOM   21682 C C   . VAL L  2 18  ? -7.521  -41.378  -0.006  1.00 111.69 ? 18  VAL L C   1 
ATOM   21683 O O   . VAL L  2 18  ? -7.013  -41.464  -1.124  1.00 112.88 ? 18  VAL L O   1 
ATOM   21684 C CB  . VAL L  2 18  ? -5.294  -41.350  1.106   1.00 119.23 ? 18  VAL L CB  1 
ATOM   21685 C CG1 . VAL L  2 18  ? -4.456  -40.761  2.232   1.00 105.87 ? 18  VAL L CG1 1 
ATOM   21686 C CG2 . VAL L  2 18  ? -5.302  -42.869  1.183   1.00 119.60 ? 18  VAL L CG2 1 
ATOM   21687 N N   . ASP L  2 19  ? -8.765  -41.766  0.253   1.00 119.35 ? 19  ASP L N   1 
ATOM   21688 C CA  . ASP L  2 19  ? -9.605  -42.374  -0.772  1.00 123.65 ? 19  ASP L CA  1 
ATOM   21689 C C   . ASP L  2 19  ? -10.449 -41.329  -1.496  1.00 114.00 ? 19  ASP L C   1 
ATOM   21690 O O   . ASP L  2 19  ? -10.751 -41.474  -2.681  1.00 107.64 ? 19  ASP L O   1 
ATOM   21691 C CB  . ASP L  2 19  ? -10.510 -43.442  -0.153  1.00 134.30 ? 19  ASP L CB  1 
ATOM   21692 C CG  . ASP L  2 19  ? -9.749  -44.409  0.733   1.00 144.65 ? 19  ASP L CG  1 
ATOM   21693 O OD1 . ASP L  2 19  ? -8.538  -44.606  0.500   1.00 144.76 ? 19  ASP L OD1 1 
ATOM   21694 O OD2 . ASP L  2 19  ? -10.363 -44.973  1.663   1.00 141.91 ? 19  ASP L OD2 1 
ATOM   21695 N N   . GLY L  2 20  ? -10.827 -40.276  -0.777  1.00 103.60 ? 20  GLY L N   1 
ATOM   21696 C CA  . GLY L  2 20  ? -11.652 -39.223  -1.340  1.00 80.79  ? 20  GLY L CA  1 
ATOM   21697 C C   . GLY L  2 20  ? -11.548 -37.915  -0.578  1.00 75.77  ? 20  GLY L C   1 
ATOM   21698 O O   . GLY L  2 20  ? -10.685 -37.760  0.286   1.00 79.94  ? 20  GLY L O   1 
ATOM   21699 N N   . TRP L  2 21  ? -12.431 -36.973  -0.899  1.00 69.72  ? 21  TRP L N   1 
ATOM   21700 C CA  . TRP L  2 21  ? -12.426 -35.661  -0.258  1.00 72.30  ? 21  TRP L CA  1 
ATOM   21701 C C   . TRP L  2 21  ? -13.220 -35.643  1.045   1.00 65.25  ? 21  TRP L C   1 
ATOM   21702 O O   . TRP L  2 21  ? -12.829 -34.987  2.010   1.00 64.32  ? 21  TRP L O   1 
ATOM   21703 C CB  . TRP L  2 21  ? -12.955 -34.586  -1.211  1.00 74.79  ? 21  TRP L CB  1 
ATOM   21704 C CG  . TRP L  2 21  ? -11.927 -34.090  -2.178  1.00 69.45  ? 21  TRP L CG  1 
ATOM   21705 C CD1 . TRP L  2 21  ? -10.576 -34.091  -2.005  1.00 68.05  ? 21  TRP L CD1 1 
ATOM   21706 C CD2 . TRP L  2 21  ? -12.169 -33.502  -3.463  1.00 71.13  ? 21  TRP L CD2 1 
ATOM   21707 N NE1 . TRP L  2 21  ? -9.956  -33.549  -3.106  1.00 63.10  ? 21  TRP L NE1 1 
ATOM   21708 C CE2 . TRP L  2 21  ? -10.910 -33.179  -4.013  1.00 64.87  ? 21  TRP L CE2 1 
ATOM   21709 C CE3 . TRP L  2 21  ? -13.322 -33.221  -4.200  1.00 64.77  ? 21  TRP L CE3 1 
ATOM   21710 C CZ2 . TRP L  2 21  ? -10.778 -32.589  -5.269  1.00 69.27  ? 21  TRP L CZ2 1 
ATOM   21711 C CZ3 . TRP L  2 21  ? -13.186 -32.635  -5.447  1.00 54.11  ? 21  TRP L CZ3 1 
ATOM   21712 C CH2 . TRP L  2 21  ? -11.924 -32.326  -5.968  1.00 60.28  ? 21  TRP L CH2 1 
ATOM   21713 N N   . TYR L  2 22  ? -14.340 -36.358  1.062   1.00 69.60  ? 22  TYR L N   1 
ATOM   21714 C CA  . TYR L  2 22  ? -15.157 -36.470  2.263   1.00 69.46  ? 22  TYR L CA  1 
ATOM   21715 C C   . TYR L  2 22  ? -15.399 -37.938  2.592   1.00 78.03  ? 22  TYR L C   1 
ATOM   21716 O O   . TYR L  2 22  ? -15.498 -38.770  1.693   1.00 90.33  ? 22  TYR L O   1 
ATOM   21717 C CB  . TYR L  2 22  ? -16.491 -35.746  2.082   1.00 77.61  ? 22  TYR L CB  1 
ATOM   21718 C CG  . TYR L  2 22  ? -16.476 -34.688  1.003   1.00 79.63  ? 22  TYR L CG  1 
ATOM   21719 C CD1 . TYR L  2 22  ? -16.923 -34.976  -0.280  1.00 70.44  ? 22  TYR L CD1 1 
ATOM   21720 C CD2 . TYR L  2 22  ? -16.016 -33.404  1.264   1.00 72.94  ? 22  TYR L CD2 1 
ATOM   21721 C CE1 . TYR L  2 22  ? -16.913 -34.017  -1.272  1.00 71.09  ? 22  TYR L CE1 1 
ATOM   21722 C CE2 . TYR L  2 22  ? -16.002 -32.437  0.276   1.00 73.16  ? 22  TYR L CE2 1 
ATOM   21723 C CZ  . TYR L  2 22  ? -16.452 -32.750  -0.990  1.00 72.67  ? 22  TYR L CZ  1 
ATOM   21724 O OH  . TYR L  2 22  ? -16.443 -31.795  -1.980  1.00 55.14  ? 22  TYR L OH  1 
ATOM   21725 N N   . GLY L  2 23  ? -15.493 -38.253  3.880   1.00 98.23  ? 23  GLY L N   1 
ATOM   21726 C CA  . GLY L  2 23  ? -15.698 -39.626  4.306   1.00 103.50 ? 23  GLY L CA  1 
ATOM   21727 C C   . GLY L  2 23  ? -15.952 -39.776  5.793   1.00 112.25 ? 23  GLY L C   1 
ATOM   21728 O O   . GLY L  2 23  ? -16.225 -38.799  6.490   1.00 98.01  ? 23  GLY L O   1 
ATOM   21729 N N   . TYR L  2 24  ? -15.853 -41.010  6.282   1.00 105.45 ? 24  TYR L N   1 
ATOM   21730 C CA  . TYR L  2 24  ? -16.144 -41.311  7.679   1.00 89.65  ? 24  TYR L CA  1 
ATOM   21731 C C   . TYR L  2 24  ? -14.966 -41.972  8.390   1.00 102.57 ? 24  TYR L C   1 
ATOM   21732 O O   . TYR L  2 24  ? -13.967 -42.336  7.769   1.00 86.96  ? 24  TYR L O   1 
ATOM   21733 C CB  . TYR L  2 24  ? -17.359 -42.236  7.781   1.00 82.28  ? 24  TYR L CB  1 
ATOM   21734 C CG  . TYR L  2 24  ? -18.486 -41.912  6.827   1.00 83.20  ? 24  TYR L CG  1 
ATOM   21735 C CD1 . TYR L  2 24  ? -18.457 -42.357  5.512   1.00 81.08  ? 24  TYR L CD1 1 
ATOM   21736 C CD2 . TYR L  2 24  ? -19.588 -41.179  7.245   1.00 79.26  ? 24  TYR L CD2 1 
ATOM   21737 C CE1 . TYR L  2 24  ? -19.487 -42.072  4.638   1.00 94.31  ? 24  TYR L CE1 1 
ATOM   21738 C CE2 . TYR L  2 24  ? -20.624 -40.888  6.378   1.00 78.60  ? 24  TYR L CE2 1 
ATOM   21739 C CZ  . TYR L  2 24  ? -20.569 -41.337  5.075   1.00 94.08  ? 24  TYR L CZ  1 
ATOM   21740 O OH  . TYR L  2 24  ? -21.597 -41.051  4.204   1.00 78.81  ? 24  TYR L OH  1 
ATOM   21741 N N   . HIS L  2 25  ? -15.099 -42.125  9.703   1.00 107.05 ? 25  HIS L N   1 
ATOM   21742 C CA  . HIS L  2 25  ? -14.149 -42.890  10.502  1.00 101.87 ? 25  HIS L CA  1 
ATOM   21743 C C   . HIS L  2 25  ? -14.893 -43.615  11.614  1.00 112.57 ? 25  HIS L C   1 
ATOM   21744 O O   . HIS L  2 25  ? -15.168 -43.047  12.671  1.00 112.92 ? 25  HIS L O   1 
ATOM   21745 C CB  . HIS L  2 25  ? -13.059 -41.992  11.086  1.00 110.91 ? 25  HIS L CB  1 
ATOM   21746 C CG  . HIS L  2 25  ? -12.235 -42.657  12.149  1.00 113.05 ? 25  HIS L CG  1 
ATOM   21747 N ND1 . HIS L  2 25  ? -12.471 -42.470  13.492  1.00 108.39 ? 25  HIS L ND1 1 
ATOM   21748 C CD2 . HIS L  2 25  ? -11.187 -43.506  12.063  1.00 102.03 ? 25  HIS L CD2 1 
ATOM   21749 C CE1 . HIS L  2 25  ? -11.601 -43.174  14.193  1.00 114.37 ? 25  HIS L CE1 1 
ATOM   21750 N NE2 . HIS L  2 25  ? -10.808 -43.814  13.347  1.00 119.17 ? 25  HIS L NE2 1 
ATOM   21751 N N   . HIS L  2 26  ? -15.224 -44.873  11.355  1.00 128.57 ? 26  HIS L N   1 
ATOM   21752 C CA  . HIS L  2 26  ? -15.976 -45.689  12.292  1.00 126.68 ? 26  HIS L CA  1 
ATOM   21753 C C   . HIS L  2 26  ? -15.058 -46.136  13.412  1.00 137.41 ? 26  HIS L C   1 
ATOM   21754 O O   . HIS L  2 26  ? -13.838 -46.038  13.299  1.00 139.65 ? 26  HIS L O   1 
ATOM   21755 C CB  . HIS L  2 26  ? -16.523 -46.908  11.573  1.00 125.74 ? 26  HIS L CB  1 
ATOM   21756 C CG  . HIS L  2 26  ? -15.491 -47.953  11.307  1.00 125.61 ? 26  HIS L CG  1 
ATOM   21757 N ND1 . HIS L  2 26  ? -14.587 -47.863  10.270  1.00 122.48 ? 26  HIS L ND1 1 
ATOM   21758 C CD2 . HIS L  2 26  ? -15.215 -49.116  11.946  1.00 148.58 ? 26  HIS L CD2 1 
ATOM   21759 C CE1 . HIS L  2 26  ? -13.801 -48.924  10.280  1.00 139.27 ? 26  HIS L CE1 1 
ATOM   21760 N NE2 . HIS L  2 26  ? -14.161 -49.699  11.286  1.00 158.13 ? 26  HIS L NE2 1 
ATOM   21761 N N   . GLN L  2 27  ? -15.640 -46.647  14.488  1.00 157.45 ? 27  GLN L N   1 
ATOM   21762 C CA  . GLN L  2 27  ? -14.846 -47.042  15.644  1.00 156.75 ? 27  GLN L CA  1 
ATOM   21763 C C   . GLN L  2 27  ? -15.801 -47.899  16.476  1.00 147.81 ? 27  GLN L C   1 
ATOM   21764 O O   . GLN L  2 27  ? -16.339 -47.460  17.494  1.00 139.81 ? 27  GLN L O   1 
ATOM   21765 C CB  . GLN L  2 27  ? -14.322 -45.798  16.381  1.00 152.79 ? 27  GLN L CB  1 
ATOM   21766 C CG  . GLN L  2 27  ? -13.765 -46.015  17.800  1.00 161.83 ? 27  GLN L CG  1 
ATOM   21767 C CD  . GLN L  2 27  ? -12.368 -46.612  17.831  1.00 169.29 ? 27  GLN L CD  1 
ATOM   21768 O OE1 . GLN L  2 27  ? -11.381 -45.903  18.034  1.00 163.13 ? 27  GLN L OE1 1 
ATOM   21769 N NE2 . GLN L  2 27  ? -12.280 -47.924  17.651  1.00 170.26 ? 27  GLN L NE2 1 
ATOM   21770 N N   . ASN L  2 28  ? -16.001 -49.131  16.012  1.00 150.09 ? 28  ASN L N   1 
ATOM   21771 C CA  . ASN L  2 28  ? -16.854 -50.102  16.686  1.00 157.23 ? 28  ASN L CA  1 
ATOM   21772 C C   . ASN L  2 28  ? -15.967 -51.253  17.146  1.00 164.92 ? 28  ASN L C   1 
ATOM   21773 O O   . ASN L  2 28  ? -14.747 -51.116  17.221  1.00 164.91 ? 28  ASN L O   1 
ATOM   21774 C CB  . ASN L  2 28  ? -18.009 -50.627  15.825  1.00 142.41 ? 28  ASN L CB  1 
ATOM   21775 C CG  . ASN L  2 28  ? -17.537 -51.432  14.616  1.00 140.05 ? 28  ASN L CG  1 
ATOM   21776 O OD1 . ASN L  2 28  ? -18.352 -51.969  13.863  1.00 131.61 ? 28  ASN L OD1 1 
ATOM   21777 N ND2 . ASN L  2 28  ? -16.225 -51.519  14.428  1.00 146.30 ? 28  ASN L ND2 1 
ATOM   21778 N N   . GLU L  2 29  ? -16.587 -52.394  17.424  1.00 157.34 ? 29  GLU L N   1 
ATOM   21779 C CA  . GLU L  2 29  ? -15.902 -53.523  18.046  1.00 155.86 ? 29  GLU L CA  1 
ATOM   21780 C C   . GLU L  2 29  ? -15.082 -54.368  17.069  1.00 153.79 ? 29  GLU L C   1 
ATOM   21781 O O   . GLU L  2 29  ? -14.315 -55.235  17.488  1.00 156.12 ? 29  GLU L O   1 
ATOM   21782 C CB  . GLU L  2 29  ? -16.922 -54.402  18.768  1.00 169.83 ? 29  GLU L CB  1 
ATOM   21783 C CG  . GLU L  2 29  ? -17.828 -53.634  19.725  1.00 173.52 ? 29  GLU L CG  1 
ATOM   21784 C CD  . GLU L  2 29  ? -19.167 -54.318  19.936  1.00 182.88 ? 29  GLU L CD  1 
ATOM   21785 O OE1 . GLU L  2 29  ? -19.598 -55.068  19.037  1.00 176.33 ? 29  GLU L OE1 1 
ATOM   21786 O OE2 . GLU L  2 29  ? -19.792 -54.100  20.995  1.00 183.14 ? 29  GLU L OE2 1 
ATOM   21787 N N   . GLN L  2 30  ? -15.242 -54.117  15.774  1.00 153.11 ? 30  GLN L N   1 
ATOM   21788 C CA  . GLN L  2 30  ? -14.509 -54.877  14.767  1.00 150.88 ? 30  GLN L CA  1 
ATOM   21789 C C   . GLN L  2 30  ? -13.304 -54.115  14.225  1.00 152.31 ? 30  GLN L C   1 
ATOM   21790 O O   . GLN L  2 30  ? -12.652 -54.563  13.283  1.00 148.62 ? 30  GLN L O   1 
ATOM   21791 C CB  . GLN L  2 30  ? -15.429 -55.292  13.619  1.00 140.94 ? 30  GLN L CB  1 
ATOM   21792 C CG  . GLN L  2 30  ? -16.461 -56.333  14.003  1.00 131.38 ? 30  GLN L CG  1 
ATOM   21793 C CD  . GLN L  2 30  ? -17.871 -55.877  13.707  1.00 134.56 ? 30  GLN L CD  1 
ATOM   21794 O OE1 . GLN L  2 30  ? -18.410 -56.143  12.633  1.00 129.43 ? 30  GLN L OE1 1 
ATOM   21795 N NE2 . GLN L  2 30  ? -18.476 -55.179  14.660  1.00 140.59 ? 30  GLN L NE2 1 
ATOM   21796 N N   . GLY L  2 31  ? -13.009 -52.963  14.819  1.00 181.80 ? 31  GLY L N   1 
ATOM   21797 C CA  . GLY L  2 31  ? -11.849 -52.188  14.418  1.00 182.31 ? 31  GLY L CA  1 
ATOM   21798 C C   . GLY L  2 31  ? -12.158 -50.737  14.103  1.00 172.60 ? 31  GLY L C   1 
ATOM   21799 O O   . GLY L  2 31  ? -13.273 -50.267  14.323  1.00 160.88 ? 31  GLY L O   1 
ATOM   21800 N N   . SER L  2 32  ? -11.158 -50.028  13.588  1.00 164.89 ? 32  SER L N   1 
ATOM   21801 C CA  . SER L  2 32  ? -11.308 -48.619  13.243  1.00 153.98 ? 32  SER L CA  1 
ATOM   21802 C C   . SER L  2 32  ? -10.910 -48.386  11.790  1.00 147.36 ? 32  SER L C   1 
ATOM   21803 O O   . SER L  2 32  ? -10.853 -49.325  10.996  1.00 146.10 ? 32  SER L O   1 
ATOM   21804 C CB  . SER L  2 32  ? -10.446 -47.752  14.162  1.00 149.05 ? 32  SER L CB  1 
ATOM   21805 O OG  . SER L  2 32  ? -10.718 -48.025  15.524  1.00 154.99 ? 32  SER L OG  1 
ATOM   21806 N N   . GLY L  2 33  ? -10.635 -47.132  11.446  1.00 139.79 ? 33  GLY L N   1 
ATOM   21807 C CA  . GLY L  2 33  ? -10.182 -46.795  10.109  1.00 139.90 ? 33  GLY L CA  1 
ATOM   21808 C C   . GLY L  2 33  ? -11.002 -45.711  9.436   1.00 122.59 ? 33  GLY L C   1 
ATOM   21809 O O   . GLY L  2 33  ? -12.068 -45.330  9.920   1.00 112.21 ? 33  GLY L O   1 
ATOM   21810 N N   . TYR L  2 34  ? -10.498 -45.214  8.310   1.00 115.98 ? 34  TYR L N   1 
ATOM   21811 C CA  . TYR L  2 34  ? -11.190 -44.186  7.542   1.00 96.91  ? 34  TYR L CA  1 
ATOM   21812 C C   . TYR L  2 34  ? -11.778 -44.774  6.264   1.00 95.44  ? 34  TYR L C   1 
ATOM   21813 O O   . TYR L  2 34  ? -11.199 -45.679  5.663   1.00 94.38  ? 34  TYR L O   1 
ATOM   21814 C CB  . TYR L  2 34  ? -10.234 -43.046  7.185   1.00 88.03  ? 34  TYR L CB  1 
ATOM   21815 C CG  . TYR L  2 34  ? -9.494  -42.453  8.363   1.00 91.21  ? 34  TYR L CG  1 
ATOM   21816 C CD1 . TYR L  2 34  ? -8.278  -42.978  8.779   1.00 85.97  ? 34  TYR L CD1 1 
ATOM   21817 C CD2 . TYR L  2 34  ? -10.006 -41.361  9.053   1.00 88.97  ? 34  TYR L CD2 1 
ATOM   21818 C CE1 . TYR L  2 34  ? -7.595  -42.437  9.853   1.00 89.17  ? 34  TYR L CE1 1 
ATOM   21819 C CE2 . TYR L  2 34  ? -9.330  -40.814  10.128  1.00 76.41  ? 34  TYR L CE2 1 
ATOM   21820 C CZ  . TYR L  2 34  ? -8.126  -41.356  10.523  1.00 76.60  ? 34  TYR L CZ  1 
ATOM   21821 O OH  . TYR L  2 34  ? -7.451  -40.814  11.593  1.00 73.64  ? 34  TYR L OH  1 
ATOM   21822 N N   . ALA L  2 35  ? -12.927 -44.251  5.850   1.00 95.29  ? 35  ALA L N   1 
ATOM   21823 C CA  . ALA L  2 35  ? -13.563 -44.680  4.610   1.00 91.75  ? 35  ALA L CA  1 
ATOM   21824 C C   . ALA L  2 35  ? -14.215 -43.495  3.904   1.00 97.55  ? 35  ALA L C   1 
ATOM   21825 O O   . ALA L  2 35  ? -15.179 -42.919  4.405   1.00 108.58 ? 35  ALA L O   1 
ATOM   21826 C CB  . ALA L  2 35  ? -14.587 -45.769  4.884   1.00 97.04  ? 35  ALA L CB  1 
ATOM   21827 N N   . ALA L  2 36  ? -13.683 -43.136  2.741   1.00 93.45  ? 36  ALA L N   1 
ATOM   21828 C CA  . ALA L  2 36  ? -14.189 -41.994  1.988   1.00 97.00  ? 36  ALA L CA  1 
ATOM   21829 C C   . ALA L  2 36  ? -15.553 -42.283  1.372   1.00 90.30  ? 36  ALA L C   1 
ATOM   21830 O O   . ALA L  2 36  ? -15.794 -43.376  0.860   1.00 95.67  ? 36  ALA L O   1 
ATOM   21831 C CB  . ALA L  2 36  ? -13.199 -41.591  0.910   1.00 100.80 ? 36  ALA L CB  1 
ATOM   21832 N N   . ASP L  2 37  ? -16.441 -41.296  1.425   1.00 87.80  ? 37  ASP L N   1 
ATOM   21833 C CA  . ASP L  2 37  ? -17.767 -41.434  0.837   1.00 84.53  ? 37  ASP L CA  1 
ATOM   21834 C C   . ASP L  2 37  ? -17.674 -41.533  -0.681  1.00 90.66  ? 37  ASP L C   1 
ATOM   21835 O O   . ASP L  2 37  ? -17.174 -40.627  -1.350  1.00 89.08  ? 37  ASP L O   1 
ATOM   21836 C CB  . ASP L  2 37  ? -18.668 -40.266  1.241   1.00 75.81  ? 37  ASP L CB  1 
ATOM   21837 C CG  . ASP L  2 37  ? -20.096 -40.442  0.765   1.00 90.57  ? 37  ASP L CG  1 
ATOM   21838 O OD1 . ASP L  2 37  ? -20.898 -39.502  0.937   1.00 104.88 ? 37  ASP L OD1 1 
ATOM   21839 O OD2 . ASP L  2 37  ? -20.419 -41.518  0.219   1.00 102.55 ? 37  ASP L OD2 1 
ATOM   21840 N N   . LEU L  2 38  ? -18.166 -42.644  -1.214  1.00 103.14 ? 38  LEU L N   1 
ATOM   21841 C CA  . LEU L  2 38  ? -18.069 -42.942  -2.636  1.00 114.62 ? 38  LEU L CA  1 
ATOM   21842 C C   . LEU L  2 38  ? -18.817 -41.944  -3.523  1.00 104.08 ? 38  LEU L C   1 
ATOM   21843 O O   . LEU L  2 38  ? -18.217 -41.286  -4.376  1.00 97.44  ? 38  LEU L O   1 
ATOM   21844 C CB  . LEU L  2 38  ? -18.580 -44.362  -2.885  1.00 137.95 ? 38  LEU L CB  1 
ATOM   21845 C CG  . LEU L  2 38  ? -18.389 -45.013  -4.256  1.00 146.91 ? 38  LEU L CG  1 
ATOM   21846 C CD1 . LEU L  2 38  ? -17.284 -44.353  -5.070  1.00 144.10 ? 38  LEU L CD1 1 
ATOM   21847 C CD2 . LEU L  2 38  ? -18.145 -46.507  -4.083  1.00 143.71 ? 38  LEU L CD2 1 
ATOM   21848 N N   . LYS L  2 39  ? -20.125 -41.838  -3.319  1.00 126.78 ? 39  LYS L N   1 
ATOM   21849 C CA  . LYS L  2 39  ? -20.965 -40.998  -4.167  1.00 128.92 ? 39  LYS L CA  1 
ATOM   21850 C C   . LYS L  2 39  ? -20.635 -39.509  -4.059  1.00 123.01 ? 39  LYS L C   1 
ATOM   21851 O O   . LYS L  2 39  ? -20.646 -38.792  -5.060  1.00 128.61 ? 39  LYS L O   1 
ATOM   21852 C CB  . LYS L  2 39  ? -22.447 -41.233  -3.861  1.00 136.20 ? 39  LYS L CB  1 
ATOM   21853 C CG  . LYS L  2 39  ? -23.394 -40.489  -4.792  1.00 156.03 ? 39  LYS L CG  1 
ATOM   21854 C CD  . LYS L  2 39  ? -24.842 -40.885  -4.551  1.00 176.25 ? 39  LYS L CD  1 
ATOM   21855 C CE  . LYS L  2 39  ? -25.771 -40.235  -5.565  1.00 176.44 ? 39  LYS L CE  1 
ATOM   21856 N NZ  . LYS L  2 39  ? -27.181 -40.686  -5.394  1.00 161.53 ? 39  LYS L NZ  1 
ATOM   21857 N N   . SER L  2 40  ? -20.341 -39.047  -2.848  1.00 94.69  ? 40  SER L N   1 
ATOM   21858 C CA  . SER L  2 40  ? -20.086 -37.627  -2.617  1.00 82.24  ? 40  SER L CA  1 
ATOM   21859 C C   . SER L  2 40  ? -18.790 -37.159  -3.276  1.00 81.82  ? 40  SER L C   1 
ATOM   21860 O O   . SER L  2 40  ? -18.781 -36.181  -4.024  1.00 85.64  ? 40  SER L O   1 
ATOM   21861 C CB  . SER L  2 40  ? -20.056 -37.323  -1.117  1.00 84.84  ? 40  SER L CB  1 
ATOM   21862 O OG  . SER L  2 40  ? -20.025 -35.926  -0.879  1.00 100.65 ? 40  SER L OG  1 
ATOM   21863 N N   . THR L  2 41  ? -17.697 -37.860  -2.991  1.00 85.55  ? 41  THR L N   1 
ATOM   21864 C CA  . THR L  2 41  ? -16.394 -37.507  -3.543  1.00 80.72  ? 41  THR L CA  1 
ATOM   21865 C C   . THR L  2 41  ? -16.399 -37.550  -5.068  1.00 80.71  ? 41  THR L C   1 
ATOM   21866 O O   . THR L  2 41  ? -15.781 -36.710  -5.723  1.00 67.09  ? 41  THR L O   1 
ATOM   21867 C CB  . THR L  2 41  ? -15.284 -38.434  -3.015  1.00 62.31  ? 41  THR L CB  1 
ATOM   21868 O OG1 . THR L  2 41  ? -15.152 -38.265  -1.599  1.00 79.24  ? 41  THR L OG1 1 
ATOM   21869 C CG2 . THR L  2 41  ? -13.957 -38.111  -3.685  1.00 70.06  ? 41  THR L CG2 1 
ATOM   21870 N N   . GLN L  2 42  ? -17.101 -38.528  -5.628  1.00 92.93  ? 42  GLN L N   1 
ATOM   21871 C CA  . GLN L  2 42  ? -17.161 -38.686  -7.076  1.00 94.74  ? 42  GLN L CA  1 
ATOM   21872 C C   . GLN L  2 42  ? -17.825 -37.486  -7.747  1.00 82.74  ? 42  GLN L C   1 
ATOM   21873 O O   . GLN L  2 42  ? -17.307 -36.948  -8.725  1.00 82.88  ? 42  GLN L O   1 
ATOM   21874 C CB  . GLN L  2 42  ? -17.893 -39.976  -7.451  1.00 101.98 ? 42  GLN L CB  1 
ATOM   21875 C CG  . GLN L  2 42  ? -17.855 -40.289  -8.936  1.00 109.08 ? 42  GLN L CG  1 
ATOM   21876 C CD  . GLN L  2 42  ? -16.439 -40.388  -9.471  1.00 117.93 ? 42  GLN L CD  1 
ATOM   21877 O OE1 . GLN L  2 42  ? -15.513 -40.758  -8.748  1.00 121.55 ? 42  GLN L OE1 1 
ATOM   21878 N NE2 . GLN L  2 42  ? -16.263 -40.059  -10.746 1.00 111.24 ? 42  GLN L NE2 1 
ATOM   21879 N N   . ASN L  2 43  ? -18.973 -37.073  -7.218  1.00 74.43  ? 43  ASN L N   1 
ATOM   21880 C CA  . ASN L  2 43  ? -19.689 -35.918  -7.751  1.00 78.41  ? 43  ASN L CA  1 
ATOM   21881 C C   . ASN L  2 43  ? -18.867 -34.636  -7.683  1.00 73.98  ? 43  ASN L C   1 
ATOM   21882 O O   . ASN L  2 43  ? -18.807 -33.876  -8.648  1.00 66.92  ? 43  ASN L O   1 
ATOM   21883 C CB  . ASN L  2 43  ? -21.023 -35.723  -7.028  1.00 80.08  ? 43  ASN L CB  1 
ATOM   21884 C CG  . ASN L  2 43  ? -22.183 -36.371  -7.758  1.00 95.48  ? 43  ASN L CG  1 
ATOM   21885 O OD1 . ASN L  2 43  ? -22.253 -37.593  -7.878  1.00 113.26 ? 43  ASN L OD1 1 
ATOM   21886 N ND2 . ASN L  2 43  ? -23.103 -35.549  -8.250  1.00 100.02 ? 43  ASN L ND2 1 
ATOM   21887 N N   . ALA L  2 44  ? -18.237 -34.399  -6.536  1.00 72.38  ? 44  ALA L N   1 
ATOM   21888 C CA  . ALA L  2 44  ? -17.408 -33.215  -6.350  1.00 62.57  ? 44  ALA L CA  1 
ATOM   21889 C C   . ALA L  2 44  ? -16.320 -33.139  -7.416  1.00 62.67  ? 44  ALA L C   1 
ATOM   21890 O O   . ALA L  2 44  ? -16.134 -32.102  -8.051  1.00 62.99  ? 44  ALA L O   1 
ATOM   21891 C CB  . ALA L  2 44  ? -16.794 -33.209  -4.959  1.00 58.83  ? 44  ALA L CB  1 
ATOM   21892 N N   . ILE L  2 45  ? -15.606 -34.244  -7.607  1.00 54.55  ? 45  ILE L N   1 
ATOM   21893 C CA  . ILE L  2 45  ? -14.557 -34.314  -8.618  1.00 63.45  ? 45  ILE L CA  1 
ATOM   21894 C C   . ILE L  2 45  ? -15.095 -33.963  -10.003 1.00 73.30  ? 45  ILE L C   1 
ATOM   21895 O O   . ILE L  2 45  ? -14.514 -33.145  -10.714 1.00 71.78  ? 45  ILE L O   1 
ATOM   21896 C CB  . ILE L  2 45  ? -13.903 -35.708  -8.660  1.00 70.80  ? 45  ILE L CB  1 
ATOM   21897 C CG1 . ILE L  2 45  ? -12.994 -35.904  -7.445  1.00 63.95  ? 45  ILE L CG1 1 
ATOM   21898 C CG2 . ILE L  2 45  ? -13.111 -35.888  -9.945  1.00 71.90  ? 45  ILE L CG2 1 
ATOM   21899 C CD1 . ILE L  2 45  ? -12.239 -37.216  -7.451  1.00 80.94  ? 45  ILE L CD1 1 
ATOM   21900 N N   . ASP L  2 46  ? -16.209 -34.585  -10.377 1.00 77.06  ? 46  ASP L N   1 
ATOM   21901 C CA  . ASP L  2 46  ? -16.837 -34.321  -11.667 1.00 65.13  ? 46  ASP L CA  1 
ATOM   21902 C C   . ASP L  2 46  ? -17.182 -32.844  -11.835 1.00 56.75  ? 46  ASP L C   1 
ATOM   21903 O O   . ASP L  2 46  ? -16.872 -32.240  -12.862 1.00 66.25  ? 46  ASP L O   1 
ATOM   21904 C CB  . ASP L  2 46  ? -18.098 -35.172  -11.836 1.00 68.83  ? 46  ASP L CB  1 
ATOM   21905 C CG  . ASP L  2 46  ? -17.786 -36.633  -12.094 1.00 95.48  ? 46  ASP L CG  1 
ATOM   21906 O OD1 . ASP L  2 46  ? -16.630 -36.942  -12.452 1.00 99.19  ? 46  ASP L OD1 1 
ATOM   21907 O OD2 . ASP L  2 46  ? -18.700 -37.472  -11.944 1.00 111.64 ? 46  ASP L OD2 1 
ATOM   21908 N N   . GLU L  2 47  ? -17.821 -32.269  -10.822 1.00 57.62  ? 47  GLU L N   1 
ATOM   21909 C CA  . GLU L  2 47  ? -18.280 -30.885  -10.893 1.00 52.87  ? 47  GLU L CA  1 
ATOM   21910 C C   . GLU L  2 47  ? -17.137 -29.873  -10.818 1.00 54.45  ? 47  GLU L C   1 
ATOM   21911 O O   . GLU L  2 47  ? -17.160 -28.854  -11.509 1.00 48.11  ? 47  GLU L O   1 
ATOM   21912 C CB  . GLU L  2 47  ? -19.330 -30.605  -9.815  1.00 42.19  ? 47  GLU L CB  1 
ATOM   21913 C CG  . GLU L  2 47  ? -20.618 -31.393  -10.007 1.00 61.11  ? 47  GLU L CG  1 
ATOM   21914 C CD  . GLU L  2 47  ? -21.722 -30.959  -9.062  1.00 74.22  ? 47  GLU L CD  1 
ATOM   21915 O OE1 . GLU L  2 47  ? -21.414 -30.307  -8.043  1.00 64.96  ? 47  GLU L OE1 1 
ATOM   21916 O OE2 . GLU L  2 47  ? -22.899 -31.273  -9.341  1.00 86.69  ? 47  GLU L OE2 1 
ATOM   21917 N N   . ILE L  2 48  ? -16.142 -30.152  -9.984  1.00 53.11  ? 48  ILE L N   1 
ATOM   21918 C CA  . ILE L  2 48  ? -14.960 -29.301  -9.912  1.00 44.53  ? 48  ILE L CA  1 
ATOM   21919 C C   . ILE L  2 48  ? -14.189 -29.371  -11.226 1.00 47.84  ? 48  ILE L C   1 
ATOM   21920 O O   . ILE L  2 48  ? -13.663 -28.366  -11.704 1.00 47.14  ? 48  ILE L O   1 
ATOM   21921 C CB  . ILE L  2 48  ? -14.037 -29.691  -8.740  1.00 50.80  ? 48  ILE L CB  1 
ATOM   21922 C CG1 . ILE L  2 48  ? -14.685 -29.314  -7.406  1.00 56.55  ? 48  ILE L CG1 1 
ATOM   21923 C CG2 . ILE L  2 48  ? -12.685 -29.011  -8.875  1.00 42.13  ? 48  ILE L CG2 1 
ATOM   21924 C CD1 . ILE L  2 48  ? -15.034 -27.844  -7.290  1.00 57.42  ? 48  ILE L CD1 1 
ATOM   21925 N N   . THR L  2 49  ? -14.132 -30.566  -11.806 1.00 50.05  ? 49  THR L N   1 
ATOM   21926 C CA  . THR L  2 49  ? -13.513 -30.755  -13.111 1.00 45.45  ? 49  THR L CA  1 
ATOM   21927 C C   . THR L  2 49  ? -14.219 -29.897  -14.151 1.00 58.42  ? 49  THR L C   1 
ATOM   21928 O O   . THR L  2 49  ? -13.582 -29.143  -14.886 1.00 61.61  ? 49  THR L O   1 
ATOM   21929 C CB  . THR L  2 49  ? -13.572 -32.226  -13.557 1.00 49.60  ? 49  THR L CB  1 
ATOM   21930 O OG1 . THR L  2 49  ? -12.709 -33.013  -12.727 1.00 71.73  ? 49  THR L OG1 1 
ATOM   21931 C CG2 . THR L  2 49  ? -13.134 -32.363  -15.008 1.00 45.63  ? 49  THR L CG2 1 
ATOM   21932 N N   . ASN L  2 50  ? -15.541 -30.019  -14.204 1.00 43.91  ? 50  ASN L N   1 
ATOM   21933 C CA  . ASN L  2 50  ? -16.348 -29.233  -15.126 1.00 50.38  ? 50  ASN L CA  1 
ATOM   21934 C C   . ASN L  2 50  ? -16.108 -27.739  -14.933 1.00 52.91  ? 50  ASN L C   1 
ATOM   21935 O O   . ASN L  2 50  ? -16.055 -26.977  -15.898 1.00 50.89  ? 50  ASN L O   1 
ATOM   21936 C CB  . ASN L  2 50  ? -17.830 -29.563  -14.940 1.00 53.04  ? 50  ASN L CB  1 
ATOM   21937 C CG  . ASN L  2 50  ? -18.698 -28.988  -16.038 1.00 57.37  ? 50  ASN L CG  1 
ATOM   21938 O OD1 . ASN L  2 50  ? -18.925 -29.625  -17.066 1.00 70.18  ? 50  ASN L OD1 1 
ATOM   21939 N ND2 . ASN L  2 50  ? -19.194 -27.779  -15.824 1.00 58.73  ? 50  ASN L ND2 1 
ATOM   21940 N N   . LYS L  2 51  ? -15.958 -27.333  -13.677 1.00 52.61  ? 51  LYS L N   1 
ATOM   21941 C CA  . LYS L  2 51  ? -15.684 -25.943  -13.338 1.00 42.10  ? 51  LYS L CA  1 
ATOM   21942 C C   . LYS L  2 51  ? -14.394 -25.464  -13.993 1.00 44.70  ? 51  LYS L C   1 
ATOM   21943 O O   . LYS L  2 51  ? -14.369 -24.425  -14.653 1.00 55.10  ? 51  LYS L O   1 
ATOM   21944 C CB  . LYS L  2 51  ? -15.597 -25.781  -11.819 1.00 51.53  ? 51  LYS L CB  1 
ATOM   21945 C CG  . LYS L  2 51  ? -15.324 -24.366  -11.348 1.00 45.77  ? 51  LYS L CG  1 
ATOM   21946 C CD  . LYS L  2 51  ? -15.588 -24.239  -9.858  1.00 49.58  ? 51  LYS L CD  1 
ATOM   21947 C CE  . LYS L  2 51  ? -15.448 -22.804  -9.389  1.00 54.77  ? 51  LYS L CE  1 
ATOM   21948 N NZ  . LYS L  2 51  ? -16.144 -22.578  -8.093  1.00 64.71  ? 51  LYS L NZ  1 
ATOM   21949 N N   . VAL L  2 52  ? -13.326 -26.234  -13.811 1.00 47.33  ? 52  VAL L N   1 
ATOM   21950 C CA  . VAL L  2 52  ? -12.027 -25.894  -14.379 1.00 44.80  ? 52  VAL L CA  1 
ATOM   21951 C C   . VAL L  2 52  ? -12.077 -25.876  -15.904 1.00 54.05  ? 52  VAL L C   1 
ATOM   21952 O O   . VAL L  2 52  ? -11.492 -25.001  -16.542 1.00 63.48  ? 52  VAL L O   1 
ATOM   21953 C CB  . VAL L  2 52  ? -10.937 -26.878  -13.917 1.00 43.92  ? 52  VAL L CB  1 
ATOM   21954 C CG1 . VAL L  2 52  ? -9.579  -26.458  -14.459 1.00 47.11  ? 52  VAL L CG1 1 
ATOM   21955 C CG2 . VAL L  2 52  ? -10.906 -26.958  -12.398 1.00 45.09  ? 52  VAL L CG2 1 
ATOM   21956 N N   . ASN L  2 53  ? -12.776 -26.847  -16.483 1.00 50.65  ? 53  ASN L N   1 
ATOM   21957 C CA  . ASN L  2 53  ? -12.921 -26.922  -17.933 1.00 58.18  ? 53  ASN L CA  1 
ATOM   21958 C C   . ASN L  2 53  ? -13.645 -25.713  -18.518 1.00 61.78  ? 53  ASN L C   1 
ATOM   21959 O O   . ASN L  2 53  ? -13.305 -25.244  -19.601 1.00 54.46  ? 53  ASN L O   1 
ATOM   21960 C CB  . ASN L  2 53  ? -13.638 -28.211  -18.343 1.00 62.46  ? 53  ASN L CB  1 
ATOM   21961 C CG  . ASN L  2 53  ? -12.709 -29.409  -18.381 1.00 66.35  ? 53  ASN L CG  1 
ATOM   21962 O OD1 . ASN L  2 53  ? -11.494 -29.273  -18.237 1.00 56.21  ? 53  ASN L OD1 1 
ATOM   21963 N ND2 . ASN L  2 53  ? -13.279 -30.591  -18.582 1.00 61.28  ? 53  ASN L ND2 1 
ATOM   21964 N N   . SER L  2 54  ? -14.642 -25.211  -17.796 1.00 49.97  ? 54  SER L N   1 
ATOM   21965 C CA  . SER L  2 54  ? -15.415 -24.063  -18.259 1.00 44.63  ? 54  SER L CA  1 
ATOM   21966 C C   . SER L  2 54  ? -14.549 -22.813  -18.377 1.00 53.93  ? 54  SER L C   1 
ATOM   21967 O O   . SER L  2 54  ? -14.511 -22.171  -19.426 1.00 54.87  ? 54  SER L O   1 
ATOM   21968 C CB  . SER L  2 54  ? -16.597 -23.799  -17.325 1.00 41.06  ? 54  SER L CB  1 
ATOM   21969 O OG  . SER L  2 54  ? -17.501 -24.889  -17.330 1.00 54.87  ? 54  SER L OG  1 
ATOM   21970 N N   . VAL L  2 55  ? -13.857 -22.474  -17.294 1.00 48.19  ? 55  VAL L N   1 
ATOM   21971 C CA  . VAL L  2 55  ? -12.976 -21.312  -17.273 1.00 51.80  ? 55  VAL L CA  1 
ATOM   21972 C C   . VAL L  2 55  ? -11.982 -21.355  -18.431 1.00 53.03  ? 55  VAL L C   1 
ATOM   21973 O O   . VAL L  2 55  ? -11.568 -20.317  -18.950 1.00 47.21  ? 55  VAL L O   1 
ATOM   21974 C CB  . VAL L  2 55  ? -12.205 -21.218  -15.939 1.00 51.96  ? 55  VAL L CB  1 
ATOM   21975 C CG1 . VAL L  2 55  ? -11.180 -20.092  -15.988 1.00 53.19  ? 55  VAL L CG1 1 
ATOM   21976 C CG2 . VAL L  2 55  ? -13.171 -21.021  -14.781 1.00 34.37  ? 55  VAL L CG2 1 
ATOM   21977 N N   . ILE L  2 56  ? -11.612 -22.565  -18.836 1.00 48.70  ? 56  ILE L N   1 
ATOM   21978 C CA  . ILE L  2 56  ? -10.641 -22.763  -19.906 1.00 45.80  ? 56  ILE L CA  1 
ATOM   21979 C C   . ILE L  2 56  ? -11.296 -22.839  -21.284 1.00 52.03  ? 56  ILE L C   1 
ATOM   21980 O O   . ILE L  2 56  ? -10.900 -22.132  -22.211 1.00 46.39  ? 56  ILE L O   1 
ATOM   21981 C CB  . ILE L  2 56  ? -9.823  -24.049  -19.678 1.00 47.44  ? 56  ILE L CB  1 
ATOM   21982 C CG1 . ILE L  2 56  ? -8.919  -23.899  -18.452 1.00 55.90  ? 56  ILE L CG1 1 
ATOM   21983 C CG2 . ILE L  2 56  ? -9.002  -24.385  -20.910 1.00 45.01  ? 56  ILE L CG2 1 
ATOM   21984 C CD1 . ILE L  2 56  ? -8.127  -25.147  -18.121 1.00 48.64  ? 56  ILE L CD1 1 
ATOM   21985 N N   . GLU L  2 57  ? -12.302 -23.698  -21.408 1.00 50.97  ? 57  GLU L N   1 
ATOM   21986 C CA  . GLU L  2 57  ? -12.915 -23.997  -22.699 1.00 56.11  ? 57  GLU L CA  1 
ATOM   21987 C C   . GLU L  2 57  ? -13.593 -22.787  -23.340 1.00 54.47  ? 57  GLU L C   1 
ATOM   21988 O O   . GLU L  2 57  ? -13.692 -22.701  -24.564 1.00 60.93  ? 57  GLU L O   1 
ATOM   21989 C CB  . GLU L  2 57  ? -13.913 -25.151  -22.555 1.00 70.64  ? 57  GLU L CB  1 
ATOM   21990 C CG  . GLU L  2 57  ? -14.281 -25.831  -23.864 1.00 103.66 ? 57  GLU L CG  1 
ATOM   21991 C CD  . GLU L  2 57  ? -15.635 -25.400  -24.392 1.00 104.19 ? 57  GLU L CD  1 
ATOM   21992 O OE1 . GLU L  2 57  ? -16.501 -25.021  -23.576 1.00 90.18  ? 57  GLU L OE1 1 
ATOM   21993 O OE2 . GLU L  2 57  ? -15.836 -25.450  -25.624 1.00 89.14  ? 57  GLU L OE2 1 
ATOM   21994 N N   . LYS L  2 58  ? -14.055 -21.855  -22.513 1.00 43.93  ? 58  LYS L N   1 
ATOM   21995 C CA  . LYS L  2 58  ? -14.761 -20.680  -23.012 1.00 40.00  ? 58  LYS L CA  1 
ATOM   21996 C C   . LYS L  2 58  ? -13.814 -19.644  -23.609 1.00 53.15  ? 58  LYS L C   1 
ATOM   21997 O O   . LYS L  2 58  ? -14.243 -18.569  -24.028 1.00 58.16  ? 58  LYS L O   1 
ATOM   21998 C CB  . LYS L  2 58  ? -15.602 -20.044  -21.903 1.00 47.91  ? 58  LYS L CB  1 
ATOM   21999 C CG  . LYS L  2 58  ? -16.764 -20.906  -21.438 1.00 49.60  ? 58  LYS L CG  1 
ATOM   22000 C CD  . LYS L  2 58  ? -17.695 -21.239  -22.593 1.00 51.88  ? 58  LYS L CD  1 
ATOM   22001 C CE  . LYS L  2 58  ? -18.847 -22.120  -22.139 1.00 53.62  ? 58  LYS L CE  1 
ATOM   22002 N NZ  . LYS L  2 58  ? -19.765 -22.463  -23.261 1.00 50.64  ? 58  LYS L NZ  1 
ATOM   22003 N N   . MET L  2 59  ? -12.527 -19.971  -23.651 1.00 48.46  ? 59  MET L N   1 
ATOM   22004 C CA  . MET L  2 59  ? -11.537 -19.048  -24.194 1.00 42.79  ? 59  MET L CA  1 
ATOM   22005 C C   . MET L  2 59  ? -11.163 -19.406  -25.629 1.00 54.74  ? 59  MET L C   1 
ATOM   22006 O O   . MET L  2 59  ? -10.117 -20.007  -25.878 1.00 75.20  ? 59  MET L O   1 
ATOM   22007 C CB  . MET L  2 59  ? -10.289 -19.004  -23.307 1.00 63.48  ? 59  MET L CB  1 
ATOM   22008 C CG  . MET L  2 59  ? -9.296  -17.928  -23.709 1.00 57.07  ? 59  MET L CG  1 
ATOM   22009 S SD  . MET L  2 59  ? -10.098 -16.327  -23.928 1.00 63.60  ? 59  MET L SD  1 
ATOM   22010 C CE  . MET L  2 59  ? -9.437  -15.409  -22.540 1.00 38.93  ? 59  MET L CE  1 
ATOM   22011 N N   . ASN L  2 60  ? -12.027 -19.041  -26.571 1.00 62.27  ? 60  ASN L N   1 
ATOM   22012 C CA  . ASN L  2 60  ? -11.734 -19.255  -27.983 1.00 68.40  ? 60  ASN L CA  1 
ATOM   22013 C C   . ASN L  2 60  ? -11.293 -17.954  -28.649 1.00 64.57  ? 60  ASN L C   1 
ATOM   22014 O O   . ASN L  2 60  ? -12.114 -17.120  -29.030 1.00 74.27  ? 60  ASN L O   1 
ATOM   22015 C CB  . ASN L  2 60  ? -12.924 -19.896  -28.712 1.00 81.70  ? 60  ASN L CB  1 
ATOM   22016 C CG  . ASN L  2 60  ? -14.036 -18.910  -29.013 1.00 101.64 ? 60  ASN L CG  1 
ATOM   22017 O OD1 . ASN L  2 60  ? -14.106 -18.360  -30.112 1.00 105.22 ? 60  ASN L OD1 1 
ATOM   22018 N ND2 . ASN L  2 60  ? -14.915 -18.686  -28.043 1.00 94.27  ? 60  ASN L ND2 1 
ATOM   22019 N N   . THR L  2 61  ? -9.982  -17.784  -28.770 1.00 62.27  ? 61  THR L N   1 
ATOM   22020 C CA  . THR L  2 61  ? -9.412  -16.538  -29.266 1.00 63.52  ? 61  THR L CA  1 
ATOM   22021 C C   . THR L  2 61  ? -9.363  -16.477  -30.789 1.00 56.63  ? 61  THR L C   1 
ATOM   22022 O O   . THR L  2 61  ? -9.362  -17.505  -31.466 1.00 50.64  ? 61  THR L O   1 
ATOM   22023 C CB  . THR L  2 61  ? -7.996  -16.309  -28.701 1.00 67.69  ? 61  THR L CB  1 
ATOM   22024 O OG1 . THR L  2 61  ? -7.157  -17.420  -29.041 1.00 67.38  ? 61  THR L OG1 1 
ATOM   22025 C CG2 . THR L  2 61  ? -8.049  -16.170  -27.190 1.00 60.05  ? 61  THR L CG2 1 
ATOM   22026 N N   . GLN L  2 62  ? -9.329  -15.259  -31.317 1.00 61.35  ? 62  GLN L N   1 
ATOM   22027 C CA  . GLN L  2 62  ? -9.220  -15.044  -32.752 1.00 69.43  ? 62  GLN L CA  1 
ATOM   22028 C C   . GLN L  2 62  ? -7.769  -15.182  -33.186 1.00 66.17  ? 62  GLN L C   1 
ATOM   22029 O O   . GLN L  2 62  ? -6.856  -14.996  -32.383 1.00 62.10  ? 62  GLN L O   1 
ATOM   22030 C CB  . GLN L  2 62  ? -9.729  -13.649  -33.118 1.00 64.89  ? 62  GLN L CB  1 
ATOM   22031 C CG  . GLN L  2 62  ? -11.215 -13.442  -32.885 1.00 49.83  ? 62  GLN L CG  1 
ATOM   22032 C CD  . GLN L  2 62  ? -12.067 -14.294  -33.801 1.00 64.42  ? 62  GLN L CD  1 
ATOM   22033 O OE1 . GLN L  2 62  ? -12.259 -15.485  -33.559 1.00 74.06  ? 62  GLN L OE1 1 
ATOM   22034 N NE2 . GLN L  2 62  ? -12.584 -13.686  -34.863 1.00 58.97  ? 62  GLN L NE2 1 
ATOM   22035 N N   . PHE L  2 63  ? -7.556  -15.515  -34.455 1.00 65.20  ? 63  PHE L N   1 
ATOM   22036 C CA  . PHE L  2 63  ? -6.208  -15.514  -35.003 1.00 53.47  ? 63  PHE L CA  1 
ATOM   22037 C C   . PHE L  2 63  ? -5.807  -14.081  -35.312 1.00 48.18  ? 63  PHE L C   1 
ATOM   22038 O O   . PHE L  2 63  ? -6.275  -13.490  -36.285 1.00 62.17  ? 63  PHE L O   1 
ATOM   22039 C CB  . PHE L  2 63  ? -6.116  -16.367  -36.268 1.00 52.98  ? 63  PHE L CB  1 
ATOM   22040 C CG  . PHE L  2 63  ? -4.717  -16.500  -36.804 1.00 59.95  ? 63  PHE L CG  1 
ATOM   22041 C CD1 . PHE L  2 63  ? -3.982  -17.651  -36.580 1.00 54.70  ? 63  PHE L CD1 1 
ATOM   22042 C CD2 . PHE L  2 63  ? -4.133  -15.467  -37.520 1.00 55.17  ? 63  PHE L CD2 1 
ATOM   22043 C CE1 . PHE L  2 63  ? -2.694  -17.774  -37.067 1.00 58.19  ? 63  PHE L CE1 1 
ATOM   22044 C CE2 . PHE L  2 63  ? -2.846  -15.584  -38.008 1.00 59.93  ? 63  PHE L CE2 1 
ATOM   22045 C CZ  . PHE L  2 63  ? -2.126  -16.739  -37.781 1.00 64.18  ? 63  PHE L CZ  1 
ATOM   22046 N N   . THR L  2 64  ? -4.947  -13.522  -34.471 1.00 40.70  ? 64  THR L N   1 
ATOM   22047 C CA  . THR L  2 64  ? -4.492  -12.152  -34.653 1.00 63.01  ? 64  THR L CA  1 
ATOM   22048 C C   . THR L  2 64  ? -2.990  -12.040  -34.462 1.00 46.44  ? 64  THR L C   1 
ATOM   22049 O O   . THR L  2 64  ? -2.399  -12.753  -33.651 1.00 43.56  ? 64  THR L O   1 
ATOM   22050 C CB  . THR L  2 64  ? -5.191  -11.186  -33.677 1.00 63.07  ? 64  THR L CB  1 
ATOM   22051 O OG1 . THR L  2 64  ? -5.215  -11.764  -32.366 1.00 59.25  ? 64  THR L OG1 1 
ATOM   22052 C CG2 . THR L  2 64  ? -6.616  -10.910  -34.128 1.00 62.72  ? 64  THR L CG2 1 
ATOM   22053 N N   . ALA L  2 65  ? -2.376  -11.145  -35.226 1.00 45.73  ? 65  ALA L N   1 
ATOM   22054 C CA  . ALA L  2 65  ? -0.972  -10.826  -35.036 1.00 35.24  ? 65  ALA L CA  1 
ATOM   22055 C C   . ALA L  2 65  ? -0.844  -9.450   -34.408 1.00 38.08  ? 65  ALA L C   1 
ATOM   22056 O O   . ALA L  2 65  ? -0.664  -8.452   -35.107 1.00 54.86  ? 65  ALA L O   1 
ATOM   22057 C CB  . ALA L  2 65  ? -0.226  -10.879  -36.353 1.00 38.94  ? 65  ALA L CB  1 
ATOM   22058 N N   . VAL L  2 66  ? -0.957  -9.397   -33.087 1.00 36.97  ? 66  VAL L N   1 
ATOM   22059 C CA  . VAL L  2 66  ? -0.702  -8.161   -32.366 1.00 39.11  ? 66  VAL L CA  1 
ATOM   22060 C C   . VAL L  2 66  ? 0.727   -7.718   -32.658 1.00 50.09  ? 66  VAL L C   1 
ATOM   22061 O O   . VAL L  2 66  ? 1.572   -8.533   -33.018 1.00 60.35  ? 66  VAL L O   1 
ATOM   22062 C CB  . VAL L  2 66  ? -0.952  -8.323   -30.850 1.00 39.31  ? 66  VAL L CB  1 
ATOM   22063 C CG1 . VAL L  2 66  ? -0.723  -9.765   -30.418 1.00 42.72  ? 66  VAL L CG1 1 
ATOM   22064 C CG2 . VAL L  2 66  ? -0.104  -7.347   -30.042 1.00 39.42  ? 66  VAL L CG2 1 
ATOM   22065 N N   . GLY L  2 67  ? 0.989   -6.424   -32.517 1.00 45.13  ? 67  GLY L N   1 
ATOM   22066 C CA  . GLY L  2 67  ? 2.263   -5.860   -32.910 1.00 57.98  ? 67  GLY L CA  1 
ATOM   22067 C C   . GLY L  2 67  ? 2.187   -5.304   -34.319 1.00 58.51  ? 67  GLY L C   1 
ATOM   22068 O O   . GLY L  2 67  ? 1.896   -6.030   -35.269 1.00 39.34  ? 67  GLY L O   1 
ATOM   22069 N N   . LYS L  2 68  ? 2.438   -4.006   -34.448 1.00 60.15  ? 68  LYS L N   1 
ATOM   22070 C CA  . LYS L  2 68  ? 2.428   -3.331   -35.739 1.00 36.13  ? 68  LYS L CA  1 
ATOM   22071 C C   . LYS L  2 68  ? 3.700   -2.504   -35.900 1.00 54.62  ? 68  LYS L C   1 
ATOM   22072 O O   . LYS L  2 68  ? 4.418   -2.269   -34.929 1.00 56.44  ? 68  LYS L O   1 
ATOM   22073 C CB  . LYS L  2 68  ? 1.202   -2.424   -35.840 1.00 59.45  ? 68  LYS L CB  1 
ATOM   22074 C CG  . LYS L  2 68  ? -0.114  -3.154   -35.661 1.00 53.71  ? 68  LYS L CG  1 
ATOM   22075 C CD  . LYS L  2 68  ? -0.413  -3.959   -36.901 1.00 55.99  ? 68  LYS L CD  1 
ATOM   22076 C CE  . LYS L  2 68  ? -1.633  -4.828   -36.738 1.00 62.54  ? 68  LYS L CE  1 
ATOM   22077 N NZ  . LYS L  2 68  ? -1.185  -6.239   -36.814 1.00 60.93  ? 68  LYS L NZ  1 
ATOM   22078 N N   . GLU L  2 69  ? 3.980   -2.061   -37.121 1.00 56.64  ? 69  GLU L N   1 
ATOM   22079 C CA  . GLU L  2 69  ? 5.171   -1.256   -37.377 1.00 40.86  ? 69  GLU L CA  1 
ATOM   22080 C C   . GLU L  2 69  ? 4.807   0.125    -37.910 1.00 42.69  ? 69  GLU L C   1 
ATOM   22081 O O   . GLU L  2 69  ? 4.043   0.246    -38.866 1.00 49.53  ? 69  GLU L O   1 
ATOM   22082 C CB  . GLU L  2 69  ? 6.104   -1.972   -38.355 1.00 51.03  ? 69  GLU L CB  1 
ATOM   22083 C CG  . GLU L  2 69  ? 6.619   -3.310   -37.849 1.00 65.70  ? 69  GLU L CG  1 
ATOM   22084 C CD  . GLU L  2 69  ? 7.402   -4.069   -38.902 1.00 69.96  ? 69  GLU L CD  1 
ATOM   22085 O OE1 . GLU L  2 69  ? 7.171   -3.827   -40.105 1.00 76.51  ? 69  GLU L OE1 1 
ATOM   22086 O OE2 . GLU L  2 69  ? 8.244   -4.912   -38.526 1.00 59.18  ? 69  GLU L OE2 1 
ATOM   22087 N N   . PHE L  2 70  ? 5.356   1.162    -37.287 1.00 44.25  ? 70  PHE L N   1 
ATOM   22088 C CA  . PHE L  2 70  ? 5.087   2.535    -37.700 1.00 42.80  ? 70  PHE L CA  1 
ATOM   22089 C C   . PHE L  2 70  ? 6.383   3.328    -37.822 1.00 43.25  ? 70  PHE L C   1 
ATOM   22090 O O   . PHE L  2 70  ? 7.298   3.162    -37.015 1.00 54.35  ? 70  PHE L O   1 
ATOM   22091 C CB  . PHE L  2 70  ? 4.150   3.222    -36.704 1.00 45.36  ? 70  PHE L CB  1 
ATOM   22092 C CG  . PHE L  2 70  ? 2.881   2.462    -36.436 1.00 49.78  ? 70  PHE L CG  1 
ATOM   22093 C CD1 . PHE L  2 70  ? 1.814   2.536    -37.316 1.00 38.30  ? 70  PHE L CD1 1 
ATOM   22094 C CD2 . PHE L  2 70  ? 2.753   1.680    -35.300 1.00 44.77  ? 70  PHE L CD2 1 
ATOM   22095 C CE1 . PHE L  2 70  ? 0.645   1.840    -37.070 1.00 39.72  ? 70  PHE L CE1 1 
ATOM   22096 C CE2 . PHE L  2 70  ? 1.587   0.982    -35.049 1.00 38.48  ? 70  PHE L CE2 1 
ATOM   22097 C CZ  . PHE L  2 70  ? 0.532   1.062    -35.934 1.00 36.23  ? 70  PHE L CZ  1 
ATOM   22098 N N   . ASN L  2 71  ? 6.461   4.187    -38.833 1.00 46.55  ? 71  ASN L N   1 
ATOM   22099 C CA  . ASN L  2 71  ? 7.640   5.024    -39.015 1.00 47.57  ? 71  ASN L CA  1 
ATOM   22100 C C   . ASN L  2 71  ? 7.619   6.237    -38.090 1.00 49.74  ? 71  ASN L C   1 
ATOM   22101 O O   . ASN L  2 71  ? 6.642   6.468    -37.377 1.00 53.43  ? 71  ASN L O   1 
ATOM   22102 C CB  . ASN L  2 71  ? 7.797   5.450    -40.478 1.00 50.69  ? 71  ASN L CB  1 
ATOM   22103 C CG  . ASN L  2 71  ? 6.635   6.287    -40.974 1.00 53.88  ? 71  ASN L CG  1 
ATOM   22104 O OD1 . ASN L  2 71  ? 6.271   7.291    -40.363 1.00 59.83  ? 71  ASN L OD1 1 
ATOM   22105 N ND2 . ASN L  2 71  ? 6.052   5.881    -42.096 1.00 58.58  ? 71  ASN L ND2 1 
ATOM   22106 N N   . HIS L  2 72  ? 8.701   7.007    -38.109 1.00 48.47  ? 72  HIS L N   1 
ATOM   22107 C CA  . HIS L  2 72  ? 8.868   8.131    -37.193 1.00 57.10  ? 72  HIS L CA  1 
ATOM   22108 C C   . HIS L  2 72  ? 7.759   9.172    -37.318 1.00 52.33  ? 72  HIS L C   1 
ATOM   22109 O O   . HIS L  2 72  ? 7.524   9.944    -36.392 1.00 61.41  ? 72  HIS L O   1 
ATOM   22110 C CB  . HIS L  2 72  ? 10.234  8.788    -37.404 1.00 58.09  ? 72  HIS L CB  1 
ATOM   22111 C CG  . HIS L  2 72  ? 10.452  9.286    -38.797 1.00 81.79  ? 72  HIS L CG  1 
ATOM   22112 N ND1 . HIS L  2 72  ? 10.869  8.467    -39.825 1.00 83.71  ? 72  HIS L ND1 1 
ATOM   22113 C CD2 . HIS L  2 72  ? 10.309  10.522   -39.336 1.00 90.32  ? 72  HIS L CD2 1 
ATOM   22114 C CE1 . HIS L  2 72  ? 10.973  9.176    -40.935 1.00 88.12  ? 72  HIS L CE1 1 
ATOM   22115 N NE2 . HIS L  2 72  ? 10.640  10.423   -40.666 1.00 89.54  ? 72  HIS L NE2 1 
ATOM   22116 N N   . LEU L  2 73  ? 7.079   9.191    -38.460 1.00 46.57  ? 73  LEU L N   1 
ATOM   22117 C CA  . LEU L  2 73  ? 5.997   10.146   -38.688 1.00 54.94  ? 73  LEU L CA  1 
ATOM   22118 C C   . LEU L  2 73  ? 4.623   9.520    -38.472 1.00 47.75  ? 73  LEU L C   1 
ATOM   22119 O O   . LEU L  2 73  ? 3.622   9.994    -39.009 1.00 42.57  ? 73  LEU L O   1 
ATOM   22120 C CB  . LEU L  2 73  ? 6.089   10.740   -40.095 1.00 46.73  ? 73  LEU L CB  1 
ATOM   22121 C CG  . LEU L  2 73  ? 7.266   11.684   -40.346 1.00 50.13  ? 73  LEU L CG  1 
ATOM   22122 C CD1 . LEU L  2 73  ? 7.352   12.055   -41.816 1.00 58.72  ? 73  LEU L CD1 1 
ATOM   22123 C CD2 . LEU L  2 73  ? 7.147   12.927   -39.479 1.00 44.97  ? 73  LEU L CD2 1 
ATOM   22124 N N   . GLU L  2 74  ? 4.583   8.452    -37.683 1.00 45.72  ? 74  GLU L N   1 
ATOM   22125 C CA  . GLU L  2 74  ? 3.330   7.779    -37.363 1.00 44.95  ? 74  GLU L CA  1 
ATOM   22126 C C   . GLU L  2 74  ? 3.256   7.456    -35.875 1.00 52.40  ? 74  GLU L C   1 
ATOM   22127 O O   . GLU L  2 74  ? 2.689   6.440    -35.475 1.00 44.86  ? 74  GLU L O   1 
ATOM   22128 C CB  . GLU L  2 74  ? 3.179   6.504    -38.193 1.00 36.41  ? 74  GLU L CB  1 
ATOM   22129 C CG  . GLU L  2 74  ? 3.022   6.754    -39.684 1.00 46.16  ? 74  GLU L CG  1 
ATOM   22130 C CD  . GLU L  2 74  ? 2.957   5.470    -40.485 1.00 60.58  ? 74  GLU L CD  1 
ATOM   22131 O OE1 . GLU L  2 74  ? 3.822   4.594    -40.275 1.00 49.24  ? 74  GLU L OE1 1 
ATOM   22132 O OE2 . GLU L  2 74  ? 2.044   5.341    -41.327 1.00 43.26  ? 74  GLU L OE2 1 
ATOM   22133 N N   . LYS L  2 75  ? 3.834   8.332    -35.061 1.00 43.98  ? 75  LYS L N   1 
ATOM   22134 C CA  . LYS L  2 75  ? 3.865   8.137    -33.617 1.00 42.61  ? 75  LYS L CA  1 
ATOM   22135 C C   . LYS L  2 75  ? 2.462   8.131    -33.015 1.00 42.75  ? 75  LYS L C   1 
ATOM   22136 O O   . LYS L  2 75  ? 2.219   7.486    -31.995 1.00 45.73  ? 75  LYS L O   1 
ATOM   22137 C CB  . LYS L  2 75  ? 4.721   9.218    -32.952 1.00 49.28  ? 75  LYS L CB  1 
ATOM   22138 C CG  . LYS L  2 75  ? 4.724   9.162    -31.432 1.00 64.82  ? 75  LYS L CG  1 
ATOM   22139 C CD  . LYS L  2 75  ? 5.273   7.839    -30.917 1.00 54.04  ? 75  LYS L CD  1 
ATOM   22140 C CE  . LYS L  2 75  ? 6.787   7.772    -31.044 1.00 80.48  ? 75  LYS L CE  1 
ATOM   22141 N NZ  . LYS L  2 75  ? 7.329   6.493    -30.506 1.00 97.27  ? 75  LYS L NZ  1 
ATOM   22142 N N   . ARG L  2 76  ? 1.541   8.848    -33.650 1.00 42.97  ? 76  ARG L N   1 
ATOM   22143 C CA  . ARG L  2 76  ? 0.174   8.937    -33.149 1.00 41.60  ? 76  ARG L CA  1 
ATOM   22144 C C   . ARG L  2 76  ? -0.570  7.607    -33.234 1.00 45.35  ? 76  ARG L C   1 
ATOM   22145 O O   . ARG L  2 76  ? -1.136  7.146    -32.244 1.00 41.66  ? 76  ARG L O   1 
ATOM   22146 C CB  . ARG L  2 76  ? -0.600  10.038   -33.874 1.00 38.29  ? 76  ARG L CB  1 
ATOM   22147 C CG  . ARG L  2 76  ? -0.230  11.437   -33.419 1.00 40.13  ? 76  ARG L CG  1 
ATOM   22148 C CD  . ARG L  2 76  ? -0.946  12.482   -34.244 1.00 46.92  ? 76  ARG L CD  1 
ATOM   22149 N NE  . ARG L  2 76  ? -0.637  12.335   -35.661 1.00 41.10  ? 76  ARG L NE  1 
ATOM   22150 C CZ  . ARG L  2 76  ? -1.517  12.518   -36.636 1.00 43.67  ? 76  ARG L CZ  1 
ATOM   22151 N NH1 . ARG L  2 76  ? -2.767  12.856   -36.348 1.00 48.45  ? 76  ARG L NH1 1 
ATOM   22152 N NH2 . ARG L  2 76  ? -1.144  12.361   -37.898 1.00 47.50  ? 76  ARG L NH2 1 
ATOM   22153 N N   . ILE L  2 77  ? -0.573  6.993    -34.413 1.00 44.43  ? 77  ILE L N   1 
ATOM   22154 C CA  . ILE L  2 77  ? -1.207  5.688    -34.569 1.00 40.12  ? 77  ILE L CA  1 
ATOM   22155 C C   . ILE L  2 77  ? -0.446  4.618    -33.793 1.00 36.39  ? 77  ILE L C   1 
ATOM   22156 O O   . ILE L  2 77  ? -1.030  3.631    -33.349 1.00 41.56  ? 77  ILE L O   1 
ATOM   22157 C CB  . ILE L  2 77  ? -1.342  5.273    -36.049 1.00 33.39  ? 77  ILE L CB  1 
ATOM   22158 C CG1 . ILE L  2 77  ? -0.077  5.634    -36.826 1.00 55.99  ? 77  ILE L CG1 1 
ATOM   22159 C CG2 . ILE L  2 77  ? -2.556  5.936    -36.679 1.00 38.27  ? 77  ILE L CG2 1 
ATOM   22160 C CD1 . ILE L  2 77  ? -0.164  5.322    -38.305 1.00 60.73  ? 77  ILE L CD1 1 
ATOM   22161 N N   . GLU L  2 78  ? 0.857   4.820    -33.629 1.00 39.88  ? 78  GLU L N   1 
ATOM   22162 C CA  . GLU L  2 78  ? 1.667   3.917    -32.821 1.00 38.84  ? 78  GLU L CA  1 
ATOM   22163 C C   . GLU L  2 78  ? 1.177   3.943    -31.379 1.00 39.50  ? 78  GLU L C   1 
ATOM   22164 O O   . GLU L  2 78  ? 1.115   2.909    -30.712 1.00 44.05  ? 78  GLU L O   1 
ATOM   22165 C CB  . GLU L  2 78  ? 3.144   4.310    -32.881 1.00 42.94  ? 78  GLU L CB  1 
ATOM   22166 C CG  . GLU L  2 78  ? 4.056   3.407    -32.061 1.00 43.62  ? 78  GLU L CG  1 
ATOM   22167 C CD  . GLU L  2 78  ? 5.497   3.883    -32.042 1.00 70.78  ? 78  GLU L CD  1 
ATOM   22168 O OE1 . GLU L  2 78  ? 5.925   4.542    -33.013 1.00 92.19  ? 78  GLU L OE1 1 
ATOM   22169 O OE2 . GLU L  2 78  ? 6.204   3.593    -31.054 1.00 76.24  ? 78  GLU L OE2 1 
ATOM   22170 N N   . ASN L  2 79  ? 0.827   5.134    -30.905 1.00 31.89  ? 79  ASN L N   1 
ATOM   22171 C CA  . ASN L  2 79  ? 0.310   5.301    -29.553 1.00 41.83  ? 79  ASN L CA  1 
ATOM   22172 C C   . ASN L  2 79  ? -1.142  4.846    -29.426 1.00 50.86  ? 79  ASN L C   1 
ATOM   22173 O O   . ASN L  2 79  ? -1.550  4.333    -28.384 1.00 44.00  ? 79  ASN L O   1 
ATOM   22174 C CB  . ASN L  2 79  ? 0.472   6.749    -29.088 1.00 44.41  ? 79  ASN L CB  1 
ATOM   22175 C CG  . ASN L  2 79  ? 1.898   7.072    -28.686 1.00 62.40  ? 79  ASN L CG  1 
ATOM   22176 O OD1 . ASN L  2 79  ? 2.634   6.201    -28.224 1.00 59.57  ? 79  ASN L OD1 1 
ATOM   22177 N ND2 . ASN L  2 79  ? 2.294   8.327    -28.855 1.00 55.51  ? 79  ASN L ND2 1 
ATOM   22178 N N   . LEU L  2 80  ? -1.917  5.038    -30.489 1.00 39.94  ? 80  LEU L N   1 
ATOM   22179 C CA  . LEU L  2 80  ? -3.276  4.517    -30.537 1.00 34.41  ? 80  LEU L CA  1 
ATOM   22180 C C   . LEU L  2 80  ? -3.195  3.005    -30.367 1.00 43.99  ? 80  LEU L C   1 
ATOM   22181 O O   . LEU L  2 80  ? -3.899  2.419    -29.544 1.00 45.25  ? 80  LEU L O   1 
ATOM   22182 C CB  . LEU L  2 80  ? -3.935  4.858    -31.874 1.00 35.47  ? 80  LEU L CB  1 
ATOM   22183 C CG  . LEU L  2 80  ? -5.463  4.940    -31.944 1.00 40.85  ? 80  LEU L CG  1 
ATOM   22184 C CD1 . LEU L  2 80  ? -5.931  4.688    -33.368 1.00 29.50  ? 80  LEU L CD1 1 
ATOM   22185 C CD2 . LEU L  2 80  ? -6.131  3.970    -30.983 1.00 46.55  ? 80  LEU L CD2 1 
ATOM   22186 N N   . ASN L  2 81  ? -2.320  2.384    -31.152 1.00 38.14  ? 81  ASN L N   1 
ATOM   22187 C CA  . ASN L  2 81  ? -2.088  0.948    -31.078 1.00 31.26  ? 81  ASN L CA  1 
ATOM   22188 C C   . ASN L  2 81  ? -1.630  0.513    -29.691 1.00 46.06  ? 81  ASN L C   1 
ATOM   22189 O O   . ASN L  2 81  ? -2.084  -0.503   -29.166 1.00 44.42  ? 81  ASN L O   1 
ATOM   22190 C CB  . ASN L  2 81  ? -1.055  0.525    -32.123 1.00 32.46  ? 81  ASN L CB  1 
ATOM   22191 C CG  . ASN L  2 81  ? -0.714  -0.948   -32.043 1.00 43.98  ? 81  ASN L CG  1 
ATOM   22192 O OD1 . ASN L  2 81  ? -1.566  -1.807   -32.268 1.00 40.67  ? 81  ASN L OD1 1 
ATOM   22193 N ND2 . ASN L  2 81  ? 0.540   -1.249   -31.726 1.00 47.86  ? 81  ASN L ND2 1 
ATOM   22194 N N   . LYS L  2 82  ? -0.722  1.284    -29.101 1.00 37.83  ? 82  LYS L N   1 
ATOM   22195 C CA  . LYS L  2 82  ? -0.250  0.994    -27.754 1.00 42.23  ? 82  LYS L CA  1 
ATOM   22196 C C   . LYS L  2 82  ? -1.393  1.093    -26.752 1.00 43.10  ? 82  LYS L C   1 
ATOM   22197 O O   . LYS L  2 82  ? -1.448  0.335    -25.784 1.00 44.33  ? 82  LYS L O   1 
ATOM   22198 C CB  . LYS L  2 82  ? 0.881   1.941    -27.353 1.00 46.06  ? 82  LYS L CB  1 
ATOM   22199 C CG  . LYS L  2 82  ? 1.239   1.864    -25.878 1.00 54.64  ? 82  LYS L CG  1 
ATOM   22200 C CD  . LYS L  2 82  ? 2.376   2.803    -25.522 1.00 68.41  ? 82  LYS L CD  1 
ATOM   22201 C CE  . LYS L  2 82  ? 2.555   2.892    -24.014 1.00 84.31  ? 82  LYS L CE  1 
ATOM   22202 N NZ  . LYS L  2 82  ? 2.768   1.553    -23.398 1.00 72.29  ? 82  LYS L NZ  1 
ATOM   22203 N N   . LYS L  2 83  ? -2.306  2.030    -26.987 1.00 46.93  ? 83  LYS L N   1 
ATOM   22204 C CA  . LYS L  2 83  ? -3.445  2.211    -26.096 1.00 45.17  ? 83  LYS L CA  1 
ATOM   22205 C C   . LYS L  2 83  ? -4.377  1.004    -26.119 1.00 42.10  ? 83  LYS L C   1 
ATOM   22206 O O   . LYS L  2 83  ? -4.852  0.561    -25.074 1.00 40.05  ? 83  LYS L O   1 
ATOM   22207 C CB  . LYS L  2 83  ? -4.226  3.483    -26.438 1.00 31.32  ? 83  LYS L CB  1 
ATOM   22208 C CG  . LYS L  2 83  ? -5.462  3.671    -25.570 1.00 41.21  ? 83  LYS L CG  1 
ATOM   22209 C CD  . LYS L  2 83  ? -6.042  5.072    -25.674 1.00 40.34  ? 83  LYS L CD  1 
ATOM   22210 C CE  . LYS L  2 83  ? -6.761  5.293    -26.991 1.00 41.73  ? 83  LYS L CE  1 
ATOM   22211 N NZ  . LYS L  2 83  ? -7.578  6.535    -26.942 1.00 47.25  ? 83  LYS L NZ  1 
ATOM   22212 N N   . VAL L  2 84  ? -4.639  0.473    -27.309 1.00 40.95  ? 84  VAL L N   1 
ATOM   22213 C CA  . VAL L  2 84  ? -5.537  -0.670   -27.438 1.00 40.74  ? 84  VAL L CA  1 
ATOM   22214 C C   . VAL L  2 84  ? -4.904  -1.924   -26.843 1.00 34.29  ? 84  VAL L C   1 
ATOM   22215 O O   . VAL L  2 84  ? -5.605  -2.822   -26.377 1.00 43.28  ? 84  VAL L O   1 
ATOM   22216 C CB  . VAL L  2 84  ? -5.954  -0.924   -28.903 1.00 32.43  ? 84  VAL L CB  1 
ATOM   22217 C CG1 . VAL L  2 84  ? -4.775  -1.419   -29.720 1.00 49.63  ? 84  VAL L CG1 1 
ATOM   22218 C CG2 . VAL L  2 84  ? -7.095  -1.924   -28.958 1.00 48.54  ? 84  VAL L CG2 1 
ATOM   22219 N N   . ASP L  2 85  ? -3.576  -1.976   -26.857 1.00 42.18  ? 85  ASP L N   1 
ATOM   22220 C CA  . ASP L  2 85  ? -2.846  -3.081   -26.245 1.00 38.14  ? 85  ASP L CA  1 
ATOM   22221 C C   . ASP L  2 85  ? -2.865  -2.972   -24.725 1.00 36.51  ? 85  ASP L C   1 
ATOM   22222 O O   . ASP L  2 85  ? -3.077  -3.963   -24.026 1.00 43.90  ? 85  ASP L O   1 
ATOM   22223 C CB  . ASP L  2 85  ? -1.402  -3.123   -26.748 1.00 33.19  ? 85  ASP L CB  1 
ATOM   22224 C CG  . ASP L  2 85  ? -1.283  -3.752   -28.117 1.00 52.13  ? 85  ASP L CG  1 
ATOM   22225 O OD1 . ASP L  2 85  ? -2.264  -4.382   -28.561 1.00 48.51  ? 85  ASP L OD1 1 
ATOM   22226 O OD2 . ASP L  2 85  ? -0.210  -3.624   -28.745 1.00 64.28  ? 85  ASP L OD2 1 
ATOM   22227 N N   . ASP L  2 86  ? -2.640  -1.764   -24.221 1.00 34.38  ? 86  ASP L N   1 
ATOM   22228 C CA  . ASP L  2 86  ? -2.635  -1.522   -22.782 1.00 35.70  ? 86  ASP L CA  1 
ATOM   22229 C C   . ASP L  2 86  ? -4.036  -1.625   -22.193 1.00 46.43  ? 86  ASP L C   1 
ATOM   22230 O O   . ASP L  2 86  ? -4.201  -1.916   -21.008 1.00 40.40  ? 86  ASP L O   1 
ATOM   22231 C CB  . ASP L  2 86  ? -2.030  -0.152   -22.467 1.00 51.92  ? 86  ASP L CB  1 
ATOM   22232 C CG  . ASP L  2 86  ? -0.522  -0.133   -22.616 1.00 73.41  ? 86  ASP L CG  1 
ATOM   22233 O OD1 . ASP L  2 86  ? 0.082   -1.224   -22.688 1.00 75.81  ? 86  ASP L OD1 1 
ATOM   22234 O OD2 . ASP L  2 86  ? 0.059   0.972    -22.655 1.00 82.71  ? 86  ASP L OD2 1 
ATOM   22235 N N   . GLY L  2 87  ? -5.043  -1.383   -23.025 1.00 47.10  ? 87  GLY L N   1 
ATOM   22236 C CA  . GLY L  2 87  ? -6.424  -1.497   -22.597 1.00 34.95  ? 87  GLY L CA  1 
ATOM   22237 C C   . GLY L  2 87  ? -6.811  -2.944   -22.373 1.00 33.16  ? 87  GLY L C   1 
ATOM   22238 O O   . GLY L  2 87  ? -7.291  -3.310   -21.301 1.00 34.94  ? 87  GLY L O   1 
ATOM   22239 N N   . PHE L  2 88  ? -6.597  -3.770   -23.393 1.00 31.92  ? 88  PHE L N   1 
ATOM   22240 C CA  . PHE L  2 88  ? -6.876  -5.196   -23.291 1.00 30.14  ? 88  PHE L CA  1 
ATOM   22241 C C   . PHE L  2 88  ? -6.073  -5.819   -22.156 1.00 37.08  ? 88  PHE L C   1 
ATOM   22242 O O   . PHE L  2 88  ? -6.549  -6.723   -21.468 1.00 49.47  ? 88  PHE L O   1 
ATOM   22243 C CB  . PHE L  2 88  ? -6.560  -5.906   -24.609 1.00 27.60  ? 88  PHE L CB  1 
ATOM   22244 C CG  . PHE L  2 88  ? -7.482  -5.536   -25.735 1.00 35.83  ? 88  PHE L CG  1 
ATOM   22245 C CD1 . PHE L  2 88  ? -7.079  -5.675   -27.053 1.00 33.17  ? 88  PHE L CD1 1 
ATOM   22246 C CD2 . PHE L  2 88  ? -8.752  -5.047   -25.476 1.00 34.76  ? 88  PHE L CD2 1 
ATOM   22247 C CE1 . PHE L  2 88  ? -7.927  -5.337   -28.091 1.00 34.12  ? 88  PHE L CE1 1 
ATOM   22248 C CE2 . PHE L  2 88  ? -9.603  -4.707   -26.510 1.00 37.43  ? 88  PHE L CE2 1 
ATOM   22249 C CZ  . PHE L  2 88  ? -9.189  -4.851   -27.819 1.00 40.62  ? 88  PHE L CZ  1 
ATOM   22250 N N   . LEU L  2 89  ? -4.854  -5.327   -21.964 1.00 41.98  ? 89  LEU L N   1 
ATOM   22251 C CA  . LEU L  2 89  ? -3.987  -5.817   -20.899 1.00 36.51  ? 89  LEU L CA  1 
ATOM   22252 C C   . LEU L  2 89  ? -4.598  -5.560   -19.525 1.00 37.19  ? 89  LEU L C   1 
ATOM   22253 O O   . LEU L  2 89  ? -4.566  -6.427   -18.652 1.00 36.72  ? 89  LEU L O   1 
ATOM   22254 C CB  . LEU L  2 89  ? -2.605  -5.166   -20.991 1.00 37.89  ? 89  LEU L CB  1 
ATOM   22255 C CG  . LEU L  2 89  ? -1.631  -5.484   -19.854 1.00 39.38  ? 89  LEU L CG  1 
ATOM   22256 C CD1 . LEU L  2 89  ? -1.521  -6.985   -19.645 1.00 43.70  ? 89  LEU L CD1 1 
ATOM   22257 C CD2 . LEU L  2 89  ? -0.264  -4.875   -20.125 1.00 36.61  ? 89  LEU L CD2 1 
ATOM   22258 N N   . ASP L  2 90  ? -5.155  -4.368   -19.340 1.00 35.06  ? 90  ASP L N   1 
ATOM   22259 C CA  . ASP L  2 90  ? -5.750  -3.991   -18.062 1.00 34.67  ? 90  ASP L CA  1 
ATOM   22260 C C   . ASP L  2 90  ? -7.064  -4.718   -17.797 1.00 33.45  ? 90  ASP L C   1 
ATOM   22261 O O   . ASP L  2 90  ? -7.348  -5.107   -16.665 1.00 41.30  ? 90  ASP L O   1 
ATOM   22262 C CB  . ASP L  2 90  ? -5.959  -2.478   -17.989 1.00 39.85  ? 90  ASP L CB  1 
ATOM   22263 C CG  . ASP L  2 90  ? -4.674  -1.725   -17.716 1.00 55.62  ? 90  ASP L CG  1 
ATOM   22264 O OD1 . ASP L  2 90  ? -3.705  -2.354   -17.242 1.00 71.21  ? 90  ASP L OD1 1 
ATOM   22265 O OD2 . ASP L  2 90  ? -4.635  -0.504   -17.969 1.00 67.69  ? 90  ASP L OD2 1 
ATOM   22266 N N   . ILE L  2 91  ? -7.864  -4.897   -18.843 1.00 38.12  ? 91  ILE L N   1 
ATOM   22267 C CA  . ILE L  2 91  ? -9.134  -5.602   -18.716 1.00 44.14  ? 91  ILE L CA  1 
ATOM   22268 C C   . ILE L  2 91  ? -8.915  -7.062   -18.342 1.00 39.71  ? 91  ILE L C   1 
ATOM   22269 O O   . ILE L  2 91  ? -9.482  -7.557   -17.369 1.00 35.99  ? 91  ILE L O   1 
ATOM   22270 C CB  . ILE L  2 91  ? -9.950  -5.545   -20.020 1.00 38.93  ? 91  ILE L CB  1 
ATOM   22271 C CG1 . ILE L  2 91  ? -10.365 -4.106   -20.330 1.00 31.34  ? 91  ILE L CG1 1 
ATOM   22272 C CG2 . ILE L  2 91  ? -11.175 -6.443   -19.920 1.00 37.55  ? 91  ILE L CG2 1 
ATOM   22273 C CD1 . ILE L  2 91  ? -11.120 -3.957   -21.631 1.00 49.33  ? 91  ILE L CD1 1 
ATOM   22274 N N   . TRP L  2 92  ? -8.083  -7.745   -19.122 1.00 30.29  ? 92  TRP L N   1 
ATOM   22275 C CA  . TRP L  2 92  ? -7.838  -9.168   -18.923 1.00 24.68  ? 92  TRP L CA  1 
ATOM   22276 C C   . TRP L  2 92  ? -7.147  -9.478   -17.601 1.00 41.63  ? 92  TRP L C   1 
ATOM   22277 O O   . TRP L  2 92  ? -7.485  -10.456  -16.933 1.00 43.04  ? 92  TRP L O   1 
ATOM   22278 C CB  . TRP L  2 92  ? -7.048  -9.744   -20.096 1.00 31.09  ? 92  TRP L CB  1 
ATOM   22279 C CG  . TRP L  2 92  ? -7.904  -9.965   -21.293 1.00 33.64  ? 92  TRP L CG  1 
ATOM   22280 C CD1 . TRP L  2 92  ? -7.823  -9.324   -22.494 1.00 29.95  ? 92  TRP L CD1 1 
ATOM   22281 C CD2 . TRP L  2 92  ? -8.999  -10.880  -21.398 1.00 36.75  ? 92  TRP L CD2 1 
ATOM   22282 N NE1 . TRP L  2 92  ? -8.793  -9.795   -23.346 1.00 46.59  ? 92  TRP L NE1 1 
ATOM   22283 C CE2 . TRP L  2 92  ? -9.530  -10.750  -22.696 1.00 35.17  ? 92  TRP L CE2 1 
ATOM   22284 C CE3 . TRP L  2 92  ? -9.578  -11.803  -20.521 1.00 36.51  ? 92  TRP L CE3 1 
ATOM   22285 C CZ2 . TRP L  2 92  ? -10.610 -11.509  -23.140 1.00 35.98  ? 92  TRP L CZ2 1 
ATOM   22286 C CZ3 . TRP L  2 92  ? -10.652 -12.553  -20.962 1.00 43.81  ? 92  TRP L CZ3 1 
ATOM   22287 C CH2 . TRP L  2 92  ? -11.157 -12.402  -22.260 1.00 40.63  ? 92  TRP L CH2 1 
ATOM   22288 N N   . THR L  2 93  ? -6.180  -8.648   -17.226 1.00 46.97  ? 93  THR L N   1 
ATOM   22289 C CA  . THR L  2 93  ? -5.494  -8.821   -15.953 1.00 36.76  ? 93  THR L CA  1 
ATOM   22290 C C   . THR L  2 93  ? -6.480  -8.714   -14.798 1.00 36.72  ? 93  THR L C   1 
ATOM   22291 O O   . THR L  2 93  ? -6.544  -9.594   -13.941 1.00 37.79  ? 93  THR L O   1 
ATOM   22292 C CB  . THR L  2 93  ? -4.374  -7.783   -15.762 1.00 38.35  ? 93  THR L CB  1 
ATOM   22293 O OG1 . THR L  2 93  ? -3.357  -7.987   -16.750 1.00 43.77  ? 93  THR L OG1 1 
ATOM   22294 C CG2 . THR L  2 93  ? -3.757  -7.917   -14.377 1.00 38.22  ? 93  THR L CG2 1 
ATOM   22295 N N   . TYR L  2 94  ? -7.255  -7.635   -14.788 1.00 37.64  ? 94  TYR L N   1 
ATOM   22296 C CA  . TYR L  2 94  ? -8.214  -7.389   -13.718 1.00 35.47  ? 94  TYR L CA  1 
ATOM   22297 C C   . TYR L  2 94  ? -9.277  -8.483   -13.645 1.00 42.81  ? 94  TYR L C   1 
ATOM   22298 O O   . TYR L  2 94  ? -9.564  -9.007   -12.569 1.00 45.20  ? 94  TYR L O   1 
ATOM   22299 C CB  . TYR L  2 94  ? -8.873  -6.019   -13.896 1.00 32.42  ? 94  TYR L CB  1 
ATOM   22300 C CG  . TYR L  2 94  ? -9.739  -5.598   -12.731 1.00 43.96  ? 94  TYR L CG  1 
ATOM   22301 C CD1 . TYR L  2 94  ? -9.171  -5.126   -11.555 1.00 46.61  ? 94  TYR L CD1 1 
ATOM   22302 C CD2 . TYR L  2 94  ? -11.123 -5.667   -12.808 1.00 45.95  ? 94  TYR L CD2 1 
ATOM   22303 C CE1 . TYR L  2 94  ? -9.957  -4.738   -10.486 1.00 50.00  ? 94  TYR L CE1 1 
ATOM   22304 C CE2 . TYR L  2 94  ? -11.918 -5.280   -11.744 1.00 49.68  ? 94  TYR L CE2 1 
ATOM   22305 C CZ  . TYR L  2 94  ? -11.330 -4.817   -10.586 1.00 57.25  ? 94  TYR L CZ  1 
ATOM   22306 O OH  . TYR L  2 94  ? -12.117 -4.433   -9.525  1.00 53.14  ? 94  TYR L OH  1 
ATOM   22307 N N   . ASN L  2 95  ? -9.857  -8.827   -14.791 1.00 43.57  ? 95  ASN L N   1 
ATOM   22308 C CA  . ASN L  2 95  ? -10.891 -9.856   -14.838 1.00 40.51  ? 95  ASN L CA  1 
ATOM   22309 C C   . ASN L  2 95  ? -10.378 -11.228  -14.411 1.00 48.02  ? 95  ASN L C   1 
ATOM   22310 O O   . ASN L  2 95  ? -11.036 -11.933  -13.648 1.00 46.49  ? 95  ASN L O   1 
ATOM   22311 C CB  . ASN L  2 95  ? -11.520 -9.933   -16.232 1.00 40.40  ? 95  ASN L CB  1 
ATOM   22312 C CG  . ASN L  2 95  ? -12.400 -8.738   -16.542 1.00 53.51  ? 95  ASN L CG  1 
ATOM   22313 O OD1 . ASN L  2 95  ? -12.345 -7.716   -15.856 1.00 49.90  ? 95  ASN L OD1 1 
ATOM   22314 N ND2 . ASN L  2 95  ? -13.221 -8.860   -17.578 1.00 53.03  ? 95  ASN L ND2 1 
ATOM   22315 N N   . ALA L  2 96  ? -9.202  -11.599  -14.906 1.00 41.02  ? 96  ALA L N   1 
ATOM   22316 C CA  . ALA L  2 96  ? -8.606  -12.888  -14.573 1.00 40.70  ? 96  ALA L CA  1 
ATOM   22317 C C   . ALA L  2 96  ? -8.303  -12.988  -13.081 1.00 41.88  ? 96  ALA L C   1 
ATOM   22318 O O   . ALA L  2 96  ? -8.577  -14.009  -12.450 1.00 46.16  ? 96  ALA L O   1 
ATOM   22319 C CB  . ALA L  2 96  ? -7.345  -13.117  -15.391 1.00 44.51  ? 96  ALA L CB  1 
ATOM   22320 N N   . GLU L  2 97  ? -7.736  -11.923  -12.523 1.00 33.90  ? 97  GLU L N   1 
ATOM   22321 C CA  . GLU L  2 97  ? -7.413  -11.882  -11.101 1.00 44.09  ? 97  GLU L CA  1 
ATOM   22322 C C   . GLU L  2 97  ? -8.670  -12.023  -10.246 1.00 47.31  ? 97  GLU L C   1 
ATOM   22323 O O   . GLU L  2 97  ? -8.705  -12.814  -9.304  1.00 50.43  ? 97  GLU L O   1 
ATOM   22324 C CB  . GLU L  2 97  ? -6.682  -10.581  -10.754 1.00 51.30  ? 97  GLU L CB  1 
ATOM   22325 C CG  . GLU L  2 97  ? -5.284  -10.456  -11.348 1.00 44.79  ? 97  GLU L CG  1 
ATOM   22326 C CD  . GLU L  2 97  ? -4.249  -11.282  -10.606 1.00 58.37  ? 97  GLU L CD  1 
ATOM   22327 O OE1 . GLU L  2 97  ? -3.040  -11.019  -10.780 1.00 61.81  ? 97  GLU L OE1 1 
ATOM   22328 O OE2 . GLU L  2 97  ? -4.641  -12.188  -9.842  1.00 78.76  ? 97  GLU L OE2 1 
ATOM   22329 N N   . LEU L  2 98  ? -9.699  -11.250  -10.582 1.00 41.24  ? 98  LEU L N   1 
ATOM   22330 C CA  . LEU L  2 98  ? -10.966 -11.292  -9.858  1.00 38.44  ? 98  LEU L CA  1 
ATOM   22331 C C   . LEU L  2 98  ? -11.688 -12.623  -10.044 1.00 44.01  ? 98  LEU L C   1 
ATOM   22332 O O   . LEU L  2 98  ? -12.290 -13.146  -9.106  1.00 40.67  ? 98  LEU L O   1 
ATOM   22333 C CB  . LEU L  2 98  ? -11.877 -10.144  -10.300 1.00 38.40  ? 98  LEU L CB  1 
ATOM   22334 C CG  . LEU L  2 98  ? -11.846 -8.852   -9.477  1.00 47.89  ? 98  LEU L CG  1 
ATOM   22335 C CD1 . LEU L  2 98  ? -12.659 -8.991   -8.197  1.00 64.37  ? 98  LEU L CD1 1 
ATOM   22336 C CD2 . LEU L  2 98  ? -10.419 -8.425   -9.174  1.00 53.52  ? 98  LEU L CD2 1 
ATOM   22337 N N   . LEU L  2 99  ? -11.632 -13.164  -11.258 1.00 48.61  ? 99  LEU L N   1 
ATOM   22338 C CA  . LEU L  2 99  ? -12.291 -14.430  -11.558 1.00 51.95  ? 99  LEU L CA  1 
ATOM   22339 C C   . LEU L  2 99  ? -11.781 -15.539  -10.647 1.00 43.48  ? 99  LEU L C   1 
ATOM   22340 O O   . LEU L  2 99  ? -12.566 -16.300  -10.083 1.00 41.42  ? 99  LEU L O   1 
ATOM   22341 C CB  . LEU L  2 99  ? -12.078 -14.823  -13.021 1.00 48.45  ? 99  LEU L CB  1 
ATOM   22342 C CG  . LEU L  2 99  ? -12.735 -16.140  -13.446 1.00 49.19  ? 99  LEU L CG  1 
ATOM   22343 C CD1 . LEU L  2 99  ? -14.247 -16.048  -13.312 1.00 47.95  ? 99  LEU L CD1 1 
ATOM   22344 C CD2 . LEU L  2 99  ? -12.343 -16.516  -14.866 1.00 55.86  ? 99  LEU L CD2 1 
ATOM   22345 N N   . VAL L  2 100 ? -10.462 -15.626  -10.509 1.00 37.85  ? 100 VAL L N   1 
ATOM   22346 C CA  . VAL L  2 100 ? -9.848  -16.633  -9.653  1.00 50.65  ? 100 VAL L CA  1 
ATOM   22347 C C   . VAL L  2 100 ? -10.257 -16.445  -8.196  1.00 40.71  ? 100 VAL L C   1 
ATOM   22348 O O   . VAL L  2 100 ? -10.687 -17.393  -7.541  1.00 48.04  ? 100 VAL L O   1 
ATOM   22349 C CB  . VAL L  2 100 ? -8.311  -16.614  -9.765  1.00 44.64  ? 100 VAL L CB  1 
ATOM   22350 C CG1 . VAL L  2 100 ? -7.685  -17.462  -8.667  1.00 38.88  ? 100 VAL L CG1 1 
ATOM   22351 C CG2 . VAL L  2 100 ? -7.876  -17.097  -11.140 1.00 48.21  ? 100 VAL L CG2 1 
ATOM   22352 N N   . LEU L  2 101 ? -10.125 -15.220  -7.695  1.00 38.63  ? 101 LEU L N   1 
ATOM   22353 C CA  . LEU L  2 101 ? -10.513 -14.913  -6.322  1.00 44.27  ? 101 LEU L CA  1 
ATOM   22354 C C   . LEU L  2 101 ? -11.956 -15.325  -6.057  1.00 47.52  ? 101 LEU L C   1 
ATOM   22355 O O   . LEU L  2 101 ? -12.237 -16.069  -5.120  1.00 53.52  ? 101 LEU L O   1 
ATOM   22356 C CB  . LEU L  2 101 ? -10.340 -13.423  -6.022  1.00 40.40  ? 101 LEU L CB  1 
ATOM   22357 C CG  . LEU L  2 101 ? -8.928  -12.842  -6.087  1.00 43.39  ? 101 LEU L CG  1 
ATOM   22358 C CD1 . LEU L  2 101 ? -8.924  -11.413  -5.569  1.00 46.60  ? 101 LEU L CD1 1 
ATOM   22359 C CD2 . LEU L  2 101 ? -7.962  -13.700  -5.294  1.00 39.96  ? 101 LEU L CD2 1 
ATOM   22360 N N   . LEU L  2 102 ? -12.866 -14.833  -6.891  1.00 45.01  ? 102 LEU L N   1 
ATOM   22361 C CA  . LEU L  2 102 ? -14.287 -15.135  -6.750  1.00 40.97  ? 102 LEU L CA  1 
ATOM   22362 C C   . LEU L  2 102 ? -14.569 -16.634  -6.779  1.00 45.81  ? 102 LEU L C   1 
ATOM   22363 O O   . LEU L  2 102 ? -15.307 -17.153  -5.941  1.00 39.48  ? 102 LEU L O   1 
ATOM   22364 C CB  . LEU L  2 102 ? -15.087 -14.439  -7.852  1.00 49.15  ? 102 LEU L CB  1 
ATOM   22365 C CG  . LEU L  2 102 ? -15.780 -13.123  -7.492  1.00 64.28  ? 102 LEU L CG  1 
ATOM   22366 C CD1 . LEU L  2 102 ? -14.933 -12.266  -6.559  1.00 57.08  ? 102 LEU L CD1 1 
ATOM   22367 C CD2 . LEU L  2 102 ? -16.168 -12.360  -8.754  1.00 87.54  ? 102 LEU L CD2 1 
ATOM   22368 N N   . GLU L  2 103 ? -13.981 -17.325  -7.751  1.00 42.44  ? 103 GLU L N   1 
ATOM   22369 C CA  . GLU L  2 103 ? -14.214 -18.757  -7.913  1.00 42.08  ? 103 GLU L CA  1 
ATOM   22370 C C   . GLU L  2 103 ? -13.614 -19.588  -6.784  1.00 46.56  ? 103 GLU L C   1 
ATOM   22371 O O   . GLU L  2 103 ? -14.213 -20.571  -6.350  1.00 51.65  ? 103 GLU L O   1 
ATOM   22372 C CB  . GLU L  2 103 ? -13.699 -19.246  -9.268  1.00 39.73  ? 103 GLU L CB  1 
ATOM   22373 C CG  . GLU L  2 103 ? -14.577 -18.833  -10.434 1.00 58.33  ? 103 GLU L CG  1 
ATOM   22374 C CD  . GLU L  2 103 ? -16.047 -19.100  -10.171 1.00 78.07  ? 103 GLU L CD  1 
ATOM   22375 O OE1 . GLU L  2 103 ? -16.474 -20.268  -10.283 1.00 73.60  ? 103 GLU L OE1 1 
ATOM   22376 O OE2 . GLU L  2 103 ? -16.776 -18.139  -9.849  1.00 81.55  ? 103 GLU L OE2 1 
ATOM   22377 N N   . ASN L  2 104 ? -12.433 -19.201  -6.315  1.00 44.83  ? 104 ASN L N   1 
ATOM   22378 C CA  . ASN L  2 104 ? -11.806 -19.892  -5.194  1.00 46.02  ? 104 ASN L CA  1 
ATOM   22379 C C   . ASN L  2 104 ? -12.682 -19.833  -3.950  1.00 51.35  ? 104 ASN L C   1 
ATOM   22380 O O   . ASN L  2 104 ? -12.815 -20.818  -3.224  1.00 46.29  ? 104 ASN L O   1 
ATOM   22381 C CB  . ASN L  2 104 ? -10.420 -19.315  -4.900  1.00 33.92  ? 104 ASN L CB  1 
ATOM   22382 C CG  . ASN L  2 104 ? -9.379  -19.765  -5.903  1.00 39.98  ? 104 ASN L CG  1 
ATOM   22383 O OD1 . ASN L  2 104 ? -9.628  -20.655  -6.715  1.00 44.65  ? 104 ASN L OD1 1 
ATOM   22384 N ND2 . ASN L  2 104 ? -8.201  -19.155  -5.848  1.00 48.01  ? 104 ASN L ND2 1 
ATOM   22385 N N   . GLU L  2 105 ? -13.284 -18.673  -3.714  1.00 37.11  ? 105 GLU L N   1 
ATOM   22386 C CA  . GLU L  2 105 ? -14.204 -18.510  -2.598  1.00 51.56  ? 105 GLU L CA  1 
ATOM   22387 C C   . GLU L  2 105 ? -15.388 -19.458  -2.746  1.00 56.52  ? 105 GLU L C   1 
ATOM   22388 O O   . GLU L  2 105 ? -15.838 -20.064  -1.773  1.00 63.48  ? 105 GLU L O   1 
ATOM   22389 C CB  . GLU L  2 105 ? -14.695 -17.065  -2.507  1.00 59.40  ? 105 GLU L CB  1 
ATOM   22390 C CG  . GLU L  2 105 ? -15.648 -16.819  -1.352  1.00 65.82  ? 105 GLU L CG  1 
ATOM   22391 C CD  . GLU L  2 105 ? -15.068 -17.260  -0.022  1.00 102.22 ? 105 GLU L CD  1 
ATOM   22392 O OE1 . GLU L  2 105 ? -13.848 -17.087  0.183   1.00 98.96  ? 105 GLU L OE1 1 
ATOM   22393 O OE2 . GLU L  2 105 ? -15.832 -17.779  0.819   1.00 101.64 ? 105 GLU L OE2 1 
ATOM   22394 N N   . ARG L  2 106 ? -15.886 -19.585  -3.972  1.00 54.41  ? 106 ARG L N   1 
ATOM   22395 C CA  . ARG L  2 106 ? -17.015 -20.465  -4.251  1.00 51.75  ? 106 ARG L CA  1 
ATOM   22396 C C   . ARG L  2 106 ? -16.633 -21.938  -4.134  1.00 55.45  ? 106 ARG L C   1 
ATOM   22397 O O   . ARG L  2 106 ? -17.431 -22.759  -3.681  1.00 56.78  ? 106 ARG L O   1 
ATOM   22398 C CB  . ARG L  2 106 ? -17.590 -20.183  -5.641  1.00 53.11  ? 106 ARG L CB  1 
ATOM   22399 C CG  . ARG L  2 106 ? -18.252 -18.823  -5.775  1.00 54.29  ? 106 ARG L CG  1 
ATOM   22400 C CD  . ARG L  2 106 ? -19.137 -18.763  -7.009  1.00 72.94  ? 106 ARG L CD  1 
ATOM   22401 N NE  . ARG L  2 106 ? -20.130 -19.834  -7.018  1.00 79.80  ? 106 ARG L NE  1 
ATOM   22402 C CZ  . ARG L  2 106 ? -21.239 -19.831  -6.286  1.00 85.90  ? 106 ARG L CZ  1 
ATOM   22403 N NH1 . ARG L  2 106 ? -21.499 -18.816  -5.475  1.00 79.14  ? 106 ARG L NH1 1 
ATOM   22404 N NH2 . ARG L  2 106 ? -22.088 -20.848  -6.358  1.00 86.51  ? 106 ARG L NH2 1 
ATOM   22405 N N   . THR L  2 107 ? -15.415 -22.270  -4.547  1.00 48.78  ? 107 THR L N   1 
ATOM   22406 C CA  . THR L  2 107 ? -14.948 -23.651  -4.508  1.00 51.91  ? 107 THR L CA  1 
ATOM   22407 C C   . THR L  2 107 ? -14.832 -24.159  -3.074  1.00 58.76  ? 107 THR L C   1 
ATOM   22408 O O   . THR L  2 107 ? -15.230 -25.284  -2.772  1.00 52.83  ? 107 THR L O   1 
ATOM   22409 C CB  . THR L  2 107 ? -13.594 -23.812  -5.222  1.00 53.55  ? 107 THR L CB  1 
ATOM   22410 O OG1 . THR L  2 107 ? -13.738 -23.453  -6.602  1.00 55.81  ? 107 THR L OG1 1 
ATOM   22411 C CG2 . THR L  2 107 ? -13.108 -25.252  -5.128  1.00 46.71  ? 107 THR L CG2 1 
ATOM   22412 N N   . LEU L  2 108 ? -14.286 -23.324  -2.195  1.00 60.89  ? 108 LEU L N   1 
ATOM   22413 C CA  . LEU L  2 108 ? -14.151 -23.683  -0.789  1.00 49.16  ? 108 LEU L CA  1 
ATOM   22414 C C   . LEU L  2 108 ? -15.519 -23.815  -0.126  1.00 46.14  ? 108 LEU L C   1 
ATOM   22415 O O   . LEU L  2 108 ? -15.756 -24.739  0.651   1.00 55.18  ? 108 LEU L O   1 
ATOM   22416 C CB  . LEU L  2 108 ? -13.291 -22.658  -0.047  1.00 46.43  ? 108 LEU L CB  1 
ATOM   22417 C CG  . LEU L  2 108 ? -11.844 -22.543  -0.529  1.00 43.96  ? 108 LEU L CG  1 
ATOM   22418 C CD1 . LEU L  2 108 ? -11.048 -21.602  0.365   1.00 39.52  ? 108 LEU L CD1 1 
ATOM   22419 C CD2 . LEU L  2 108 ? -11.192 -23.918  -0.584  1.00 49.56  ? 108 LEU L CD2 1 
ATOM   22420 N N   . ASP L  2 109 ? -16.418 -22.887  -0.440  1.00 47.01  ? 109 ASP L N   1 
ATOM   22421 C CA  . ASP L  2 109 ? -17.779 -22.940  0.079   1.00 54.45  ? 109 ASP L CA  1 
ATOM   22422 C C   . ASP L  2 109 ? -18.513 -24.169  -0.448  1.00 55.75  ? 109 ASP L C   1 
ATOM   22423 O O   . ASP L  2 109 ? -19.378 -24.726  0.228   1.00 48.88  ? 109 ASP L O   1 
ATOM   22424 C CB  . ASP L  2 109 ? -18.546 -21.667  -0.282  1.00 61.25  ? 109 ASP L CB  1 
ATOM   22425 C CG  . ASP L  2 109 ? -18.099 -20.467  0.531   1.00 82.79  ? 109 ASP L CG  1 
ATOM   22426 O OD1 . ASP L  2 109 ? -17.373 -20.659  1.529   1.00 84.50  ? 109 ASP L OD1 1 
ATOM   22427 O OD2 . ASP L  2 109 ? -18.478 -19.331  0.175   1.00 82.08  ? 109 ASP L OD2 1 
ATOM   22428 N N   . TYR L  2 110 ? -18.159 -24.588  -1.659  1.00 57.26  ? 110 TYR L N   1 
ATOM   22429 C CA  . TYR L  2 110 ? -18.743 -25.780  -2.261  1.00 44.79  ? 110 TYR L CA  1 
ATOM   22430 C C   . TYR L  2 110 ? -18.357 -27.030  -1.477  1.00 60.61  ? 110 TYR L C   1 
ATOM   22431 O O   . TYR L  2 110 ? -19.208 -27.859  -1.154  1.00 47.61  ? 110 TYR L O   1 
ATOM   22432 C CB  . TYR L  2 110 ? -18.304 -25.913  -3.721  1.00 37.19  ? 110 TYR L CB  1 
ATOM   22433 C CG  . TYR L  2 110 ? -18.678 -27.233  -4.358  1.00 45.35  ? 110 TYR L CG  1 
ATOM   22434 C CD1 . TYR L  2 110 ? -19.931 -27.426  -4.924  1.00 39.02  ? 110 TYR L CD1 1 
ATOM   22435 C CD2 . TYR L  2 110 ? -17.773 -28.286  -4.397  1.00 47.54  ? 110 TYR L CD2 1 
ATOM   22436 C CE1 . TYR L  2 110 ? -20.274 -28.633  -5.509  1.00 40.56  ? 110 TYR L CE1 1 
ATOM   22437 C CE2 . TYR L  2 110 ? -18.106 -29.495  -4.978  1.00 52.07  ? 110 TYR L CE2 1 
ATOM   22438 C CZ  . TYR L  2 110 ? -19.357 -29.663  -5.532  1.00 51.41  ? 110 TYR L CZ  1 
ATOM   22439 O OH  . TYR L  2 110 ? -19.689 -30.867  -6.110  1.00 56.60  ? 110 TYR L OH  1 
ATOM   22440 N N   . HIS L  2 111 ? -17.069 -27.160  -1.175  1.00 56.06  ? 111 HIS L N   1 
ATOM   22441 C CA  . HIS L  2 111 ? -16.581 -28.287  -0.388  1.00 44.86  ? 111 HIS L CA  1 
ATOM   22442 C C   . HIS L  2 111 ? -17.144 -28.241  1.027   1.00 55.64  ? 111 HIS L C   1 
ATOM   22443 O O   . HIS L  2 111 ? -17.610 -29.251  1.554   1.00 50.13  ? 111 HIS L O   1 
ATOM   22444 C CB  . HIS L  2 111 ? -15.052 -28.299  -0.347  1.00 44.83  ? 111 HIS L CB  1 
ATOM   22445 C CG  . HIS L  2 111 ? -14.419 -28.680  -1.647  1.00 40.88  ? 111 HIS L CG  1 
ATOM   22446 N ND1 . HIS L  2 111 ? -14.538 -29.937  -2.191  1.00 52.27  ? 111 HIS L ND1 1 
ATOM   22447 C CD2 . HIS L  2 111 ? -13.649 -27.966  -2.507  1.00 52.14  ? 111 HIS L CD2 1 
ATOM   22448 C CE1 . HIS L  2 111 ? -13.876 -29.984  -3.337  1.00 55.34  ? 111 HIS L CE1 1 
ATOM   22449 N NE2 . HIS L  2 111 ? -13.330 -28.807  -3.548  1.00 58.46  ? 111 HIS L NE2 1 
ATOM   22450 N N   . ASP L  2 112 ? -17.093 -27.061  1.637   1.00 49.51  ? 112 ASP L N   1 
ATOM   22451 C CA  . ASP L  2 112 ? -17.648 -26.858  2.968   1.00 47.84  ? 112 ASP L CA  1 
ATOM   22452 C C   . ASP L  2 112 ? -19.091 -27.347  3.006   1.00 46.33  ? 112 ASP L C   1 
ATOM   22453 O O   . ASP L  2 112 ? -19.522 -27.984  3.967   1.00 58.12  ? 112 ASP L O   1 
ATOM   22454 C CB  . ASP L  2 112 ? -17.586 -25.375  3.340   1.00 57.65  ? 112 ASP L CB  1 
ATOM   22455 C CG  . ASP L  2 112 ? -17.920 -25.123  4.795   1.00 65.16  ? 112 ASP L CG  1 
ATOM   22456 O OD1 . ASP L  2 112 ? -18.240 -23.967  5.139   1.00 74.88  ? 112 ASP L OD1 1 
ATOM   22457 O OD2 . ASP L  2 112 ? -17.860 -26.079  5.594   1.00 81.67  ? 112 ASP L OD2 1 
ATOM   22458 N N   . SER L  2 113 ? -19.827 -27.048  1.941   1.00 62.60  ? 113 SER L N   1 
ATOM   22459 C CA  . SER L  2 113 ? -21.230 -27.426  1.831   1.00 53.25  ? 113 SER L CA  1 
ATOM   22460 C C   . SER L  2 113 ? -21.427 -28.940  1.836   1.00 60.74  ? 113 SER L C   1 
ATOM   22461 O O   . SER L  2 113 ? -22.282 -29.459  2.552   1.00 53.99  ? 113 SER L O   1 
ATOM   22462 C CB  . SER L  2 113 ? -21.835 -26.831  0.559   1.00 48.98  ? 113 SER L CB  1 
ATOM   22463 O OG  . SER L  2 113 ? -23.121 -27.366  0.309   1.00 66.67  ? 113 SER L OG  1 
ATOM   22464 N N   . ASN L  2 114 ? -20.638 -29.642  1.029   1.00 60.68  ? 114 ASN L N   1 
ATOM   22465 C CA  . ASN L  2 114 ? -20.756 -31.092  0.920   1.00 57.62  ? 114 ASN L CA  1 
ATOM   22466 C C   . ASN L  2 114 ? -20.524 -31.802  2.250   1.00 61.34  ? 114 ASN L C   1 
ATOM   22467 O O   . ASN L  2 114 ? -21.187 -32.792  2.558   1.00 60.23  ? 114 ASN L O   1 
ATOM   22468 C CB  . ASN L  2 114 ? -19.804 -31.629  -0.150  1.00 58.40  ? 114 ASN L CB  1 
ATOM   22469 C CG  . ASN L  2 114 ? -20.152 -31.133  -1.541  1.00 62.74  ? 114 ASN L CG  1 
ATOM   22470 O OD1 . ASN L  2 114 ? -21.281 -30.714  -1.797  1.00 68.53  ? 114 ASN L OD1 1 
ATOM   22471 N ND2 . ASN L  2 114 ? -19.184 -31.183  -2.447  1.00 62.09  ? 114 ASN L ND2 1 
ATOM   22472 N N   . VAL L  2 115 ? -19.579 -31.291  3.034   1.00 57.02  ? 115 VAL L N   1 
ATOM   22473 C CA  . VAL L  2 115 ? -19.324 -31.826  4.365   1.00 51.98  ? 115 VAL L CA  1 
ATOM   22474 C C   . VAL L  2 115 ? -20.554 -31.642  5.246   1.00 57.58  ? 115 VAL L C   1 
ATOM   22475 O O   . VAL L  2 115 ? -21.081 -32.605  5.803   1.00 63.39  ? 115 VAL L O   1 
ATOM   22476 C CB  . VAL L  2 115 ? -18.116 -31.141  5.028   1.00 56.53  ? 115 VAL L CB  1 
ATOM   22477 C CG1 . VAL L  2 115 ? -17.994 -31.568  6.483   1.00 67.25  ? 115 VAL L CG1 1 
ATOM   22478 C CG2 . VAL L  2 115 ? -16.841 -31.458  4.261   1.00 44.15  ? 115 VAL L CG2 1 
ATOM   22479 N N   . LYS L  2 116 ? -21.006 -30.397  5.362   1.00 50.46  ? 116 LYS L N   1 
ATOM   22480 C CA  . LYS L  2 116 ? -22.208 -30.067  6.122   1.00 58.13  ? 116 LYS L CA  1 
ATOM   22481 C C   . LYS L  2 116 ? -23.375 -30.972  5.738   1.00 60.12  ? 116 LYS L C   1 
ATOM   22482 O O   . LYS L  2 116 ? -24.112 -31.450  6.600   1.00 67.89  ? 116 LYS L O   1 
ATOM   22483 C CB  . LYS L  2 116 ? -22.586 -28.602  5.893   1.00 54.88  ? 116 LYS L CB  1 
ATOM   22484 C CG  . LYS L  2 116 ? -23.976 -28.215  6.381   1.00 56.12  ? 116 LYS L CG  1 
ATOM   22485 C CD  . LYS L  2 116 ? -23.947 -27.642  7.788   1.00 72.71  ? 116 LYS L CD  1 
ATOM   22486 C CE  . LYS L  2 116 ? -25.289 -27.020  8.149   1.00 86.30  ? 116 LYS L CE  1 
ATOM   22487 N NZ  . LYS L  2 116 ? -25.239 -26.273  9.436   1.00 110.37 ? 116 LYS L NZ  1 
ATOM   22488 N N   . ASN L  2 117 ? -23.535 -31.202  4.439   1.00 55.35  ? 117 ASN L N   1 
ATOM   22489 C CA  . ASN L  2 117 ? -24.607 -32.054  3.936   1.00 59.77  ? 117 ASN L CA  1 
ATOM   22490 C C   . ASN L  2 117 ? -24.429 -33.510  4.344   1.00 65.40  ? 117 ASN L C   1 
ATOM   22491 O O   . ASN L  2 117 ? -25.397 -34.193  4.675   1.00 72.01  ? 117 ASN L O   1 
ATOM   22492 C CB  . ASN L  2 117 ? -24.715 -31.945  2.414   1.00 60.23  ? 117 ASN L CB  1 
ATOM   22493 C CG  . ASN L  2 117 ? -25.354 -30.646  1.968   1.00 61.71  ? 117 ASN L CG  1 
ATOM   22494 O OD1 . ASN L  2 117 ? -25.913 -29.906  2.777   1.00 68.49  ? 117 ASN L OD1 1 
ATOM   22495 N ND2 . ASN L  2 117 ? -25.278 -30.362  0.673   1.00 68.10  ? 117 ASN L ND2 1 
ATOM   22496 N N   . LEU L  2 118 ? -23.188 -33.983  4.314   1.00 62.37  ? 118 LEU L N   1 
ATOM   22497 C CA  . LEU L  2 118 ? -22.889 -35.351  4.712   1.00 66.44  ? 118 LEU L CA  1 
ATOM   22498 C C   . LEU L  2 118 ? -23.208 -35.537  6.191   1.00 68.67  ? 118 LEU L C   1 
ATOM   22499 O O   . LEU L  2 118 ? -23.789 -36.546  6.593   1.00 79.42  ? 118 LEU L O   1 
ATOM   22500 C CB  . LEU L  2 118 ? -21.421 -35.678  4.436   1.00 63.95  ? 118 LEU L CB  1 
ATOM   22501 C CG  . LEU L  2 118 ? -21.131 -37.129  4.054   1.00 68.25  ? 118 LEU L CG  1 
ATOM   22502 C CD1 . LEU L  2 118 ? -22.045 -37.553  2.919   1.00 75.93  ? 118 LEU L CD1 1 
ATOM   22503 C CD2 . LEU L  2 118 ? -19.671 -37.310  3.670   1.00 77.97  ? 118 LEU L CD2 1 
ATOM   22504 N N   . TYR L  2 119 ? -22.826 -34.549  6.993   1.00 60.07  ? 119 TYR L N   1 
ATOM   22505 C CA  . TYR L  2 119 ? -23.122 -34.551  8.419   1.00 66.85  ? 119 TYR L CA  1 
ATOM   22506 C C   . TYR L  2 119 ? -24.627 -34.576  8.659   1.00 69.06  ? 119 TYR L C   1 
ATOM   22507 O O   . TYR L  2 119 ? -25.129 -35.397  9.426   1.00 82.38  ? 119 TYR L O   1 
ATOM   22508 C CB  . TYR L  2 119 ? -22.505 -33.321  9.088   1.00 71.29  ? 119 TYR L CB  1 
ATOM   22509 C CG  . TYR L  2 119 ? -22.828 -33.191  10.559  1.00 82.66  ? 119 TYR L CG  1 
ATOM   22510 C CD1 . TYR L  2 119 ? -22.012 -33.767  11.523  1.00 87.50  ? 119 TYR L CD1 1 
ATOM   22511 C CD2 . TYR L  2 119 ? -23.948 -32.488  10.985  1.00 85.03  ? 119 TYR L CD2 1 
ATOM   22512 C CE1 . TYR L  2 119 ? -22.302 -33.649  12.869  1.00 93.44  ? 119 TYR L CE1 1 
ATOM   22513 C CE2 . TYR L  2 119 ? -24.247 -32.365  12.329  1.00 99.93  ? 119 TYR L CE2 1 
ATOM   22514 C CZ  . TYR L  2 119 ? -23.421 -32.947  13.266  1.00 99.61  ? 119 TYR L CZ  1 
ATOM   22515 O OH  . TYR L  2 119 ? -23.714 -32.828  14.605  1.00 104.26 ? 119 TYR L OH  1 
ATOM   22516 N N   . GLU L  2 120 ? -25.341 -33.670  7.998   1.00 79.10  ? 120 GLU L N   1 
ATOM   22517 C CA  . GLU L  2 120 ? -26.790 -33.571  8.147   1.00 80.79  ? 120 GLU L CA  1 
ATOM   22518 C C   . GLU L  2 120 ? -27.511 -34.848  7.724   1.00 77.29  ? 120 GLU L C   1 
ATOM   22519 O O   . GLU L  2 120 ? -28.452 -35.284  8.387   1.00 94.08  ? 120 GLU L O   1 
ATOM   22520 C CB  . GLU L  2 120 ? -27.332 -32.376  7.357   1.00 87.82  ? 120 GLU L CB  1 
ATOM   22521 C CG  . GLU L  2 120 ? -27.273 -31.057  8.107   1.00 104.30 ? 120 GLU L CG  1 
ATOM   22522 C CD  . GLU L  2 120 ? -28.240 -31.010  9.274   1.00 127.10 ? 120 GLU L CD  1 
ATOM   22523 O OE1 . GLU L  2 120 ? -29.235 -31.765  9.254   1.00 120.32 ? 120 GLU L OE1 1 
ATOM   22524 O OE2 . GLU L  2 120 ? -28.009 -30.215  10.209  1.00 135.01 ? 120 GLU L OE2 1 
ATOM   22525 N N   . LYS L  2 121 ? -27.070 -35.443  6.621   1.00 74.34  ? 121 LYS L N   1 
ATOM   22526 C CA  . LYS L  2 121 ? -27.704 -36.652  6.107   1.00 84.04  ? 121 LYS L CA  1 
ATOM   22527 C C   . LYS L  2 121 ? -27.626 -37.793  7.117   1.00 92.97  ? 121 LYS L C   1 
ATOM   22528 O O   . LYS L  2 121 ? -28.543 -38.608  7.218   1.00 106.72 ? 121 LYS L O   1 
ATOM   22529 C CB  . LYS L  2 121 ? -27.076 -37.076  4.779   1.00 85.58  ? 121 LYS L CB  1 
ATOM   22530 C CG  . LYS L  2 121 ? -27.781 -38.249  4.119   1.00 102.22 ? 121 LYS L CG  1 
ATOM   22531 C CD  . LYS L  2 121 ? -27.142 -38.615  2.791   1.00 112.47 ? 121 LYS L CD  1 
ATOM   22532 C CE  . LYS L  2 121 ? -27.880 -39.769  2.133   1.00 120.85 ? 121 LYS L CE  1 
ATOM   22533 N NZ  . LYS L  2 121 ? -27.255 -40.172  0.844   1.00 132.51 ? 121 LYS L NZ  1 
ATOM   22534 N N   . VAL L  2 122 ? -26.526 -37.847  7.860   1.00 95.36  ? 122 VAL L N   1 
ATOM   22535 C CA  . VAL L  2 122 ? -26.357 -38.846  8.909   1.00 89.42  ? 122 VAL L CA  1 
ATOM   22536 C C   . VAL L  2 122 ? -27.208 -38.492  10.122  1.00 91.62  ? 122 VAL L C   1 
ATOM   22537 O O   . VAL L  2 122 ? -27.865 -39.353  10.708  1.00 111.88 ? 122 VAL L O   1 
ATOM   22538 C CB  . VAL L  2 122 ? -24.884 -38.953  9.351   1.00 81.74  ? 122 VAL L CB  1 
ATOM   22539 C CG1 . VAL L  2 122 ? -24.780 -39.645  10.704  1.00 91.72  ? 122 VAL L CG1 1 
ATOM   22540 C CG2 . VAL L  2 122 ? -24.061 -39.682  8.300   1.00 80.63  ? 122 VAL L CG2 1 
ATOM   22541 N N   . ARG L  2 123 ? -27.193 -37.213  10.483  1.00 86.91  ? 123 ARG L N   1 
ATOM   22542 C CA  . ARG L  2 123 ? -27.877 -36.738  11.680  1.00 92.19  ? 123 ARG L CA  1 
ATOM   22543 C C   . ARG L  2 123 ? -29.396 -36.849  11.579  1.00 94.57  ? 123 ARG L C   1 
ATOM   22544 O O   . ARG L  2 123 ? -30.055 -37.240  12.537  1.00 112.75 ? 123 ARG L O   1 
ATOM   22545 C CB  . ARG L  2 123 ? -27.485 -35.292  11.984  1.00 88.96  ? 123 ARG L CB  1 
ATOM   22546 C CG  . ARG L  2 123 ? -27.927 -34.820  13.356  1.00 92.01  ? 123 ARG L CG  1 
ATOM   22547 C CD  . ARG L  2 123 ? -28.330 -33.359  13.334  1.00 100.76 ? 123 ARG L CD  1 
ATOM   22548 N NE  . ARG L  2 123 ? -29.492 -33.129  12.482  1.00 123.87 ? 123 ARG L NE  1 
ATOM   22549 C CZ  . ARG L  2 123 ? -30.313 -32.091  12.601  1.00 139.29 ? 123 ARG L CZ  1 
ATOM   22550 N NH1 . ARG L  2 123 ? -30.109 -31.186  13.545  1.00 137.95 ? 123 ARG L NH1 1 
ATOM   22551 N NH2 . ARG L  2 123 ? -31.345 -31.962  11.779  1.00 139.29 ? 123 ARG L NH2 1 
ATOM   22552 N N   . SER L  2 124 ? -29.958 -36.495  10.429  1.00 96.34  ? 124 SER L N   1 
ATOM   22553 C CA  . SER L  2 124 ? -31.404 -36.586  10.251  1.00 117.75 ? 124 SER L CA  1 
ATOM   22554 C C   . SER L  2 124 ? -31.804 -38.016  9.920   1.00 120.22 ? 124 SER L C   1 
ATOM   22555 O O   . SER L  2 124 ? -32.883 -38.267  9.380   1.00 123.89 ? 124 SER L O   1 
ATOM   22556 C CB  . SER L  2 124 ? -31.884 -35.633  9.156   1.00 129.18 ? 124 SER L CB  1 
ATOM   22557 O OG  . SER L  2 124 ? -31.334 -35.981  7.898   1.00 128.73 ? 124 SER L OG  1 
ATOM   22558 N N   . GLN L  2 125 ? -30.924 -38.952  10.251  1.00 112.86 ? 125 GLN L N   1 
ATOM   22559 C CA  . GLN L  2 125 ? -31.157 -40.355  9.957   1.00 110.78 ? 125 GLN L CA  1 
ATOM   22560 C C   . GLN L  2 125 ? -31.013 -41.175  11.243  1.00 123.18 ? 125 GLN L C   1 
ATOM   22561 O O   . GLN L  2 125 ? -31.858 -42.022  11.553  1.00 122.80 ? 125 GLN L O   1 
ATOM   22562 C CB  . GLN L  2 125 ? -30.196 -40.828  8.873   1.00 94.88  ? 125 GLN L CB  1 
ATOM   22563 C CG  . GLN L  2 125 ? -30.464 -42.226  8.386   1.00 107.28 ? 125 GLN L CG  1 
ATOM   22564 C CD  . GLN L  2 125 ? -29.498 -42.643  7.305   1.00 120.75 ? 125 GLN L CD  1 
ATOM   22565 O OE1 . GLN L  2 125 ? -28.340 -42.226  7.296   1.00 107.32 ? 125 GLN L OE1 1 
ATOM   22566 N NE2 . GLN L  2 125 ? -29.967 -43.472  6.383   1.00 132.77 ? 125 GLN L NE2 1 
ATOM   22567 N N   . LEU L  2 126 ? -29.949 -40.916  11.999  1.00 125.30 ? 126 LEU L N   1 
ATOM   22568 C CA  . LEU L  2 126 ? -29.946 -41.258  13.414  1.00 109.42 ? 126 LEU L CA  1 
ATOM   22569 C C   . LEU L  2 126 ? -30.570 -40.067  14.109  1.00 123.47 ? 126 LEU L C   1 
ATOM   22570 O O   . LEU L  2 126 ? -30.090 -38.950  13.966  1.00 144.35 ? 126 LEU L O   1 
ATOM   22571 C CB  . LEU L  2 126 ? -28.520 -41.437  13.944  1.00 108.44 ? 126 LEU L CB  1 
ATOM   22572 C CG  . LEU L  2 126 ? -27.341 -41.789  13.011  1.00 98.87  ? 126 LEU L CG  1 
ATOM   22573 C CD1 . LEU L  2 126 ? -26.031 -41.497  13.716  1.00 105.74 ? 126 LEU L CD1 1 
ATOM   22574 C CD2 . LEU L  2 126 ? -27.368 -43.223  12.475  1.00 94.81  ? 126 LEU L CD2 1 
ATOM   22575 N N   . LYS L  2 127 ? -31.636 -40.293  14.859  1.00 114.54 ? 127 LYS L N   1 
ATOM   22576 C CA  . LYS L  2 127 ? -32.266 -39.191  15.571  1.00 124.75 ? 127 LYS L CA  1 
ATOM   22577 C C   . LYS L  2 127 ? -32.112 -39.365  17.082  1.00 139.92 ? 127 LYS L C   1 
ATOM   22578 O O   . LYS L  2 127 ? -31.297 -38.692  17.716  1.00 120.66 ? 127 LYS L O   1 
ATOM   22579 C CB  . LYS L  2 127 ? -33.734 -39.051  15.185  1.00 126.68 ? 127 LYS L CB  1 
ATOM   22580 C CG  . LYS L  2 127 ? -33.935 -38.935  13.677  1.00 123.33 ? 127 LYS L CG  1 
ATOM   22581 C CD  . LYS L  2 127 ? -34.997 -39.911  13.195  1.00 114.19 ? 127 LYS L CD  1 
ATOM   22582 C CE  . LYS L  2 127 ? -35.109 -39.859  11.678  1.00 133.11 ? 127 LYS L CE  1 
ATOM   22583 N NZ  . LYS L  2 127 ? -36.171 -40.743  11.114  1.00 130.10 ? 127 LYS L NZ  1 
ATOM   22584 N N   . ASN L  2 128 ? -32.881 -40.285  17.655  1.00 167.84 ? 128 ASN L N   1 
ATOM   22585 C CA  . ASN L  2 128 ? -32.751 -40.608  19.070  1.00 163.79 ? 128 ASN L CA  1 
ATOM   22586 C C   . ASN L  2 128 ? -31.692 -41.676  19.301  1.00 163.85 ? 128 ASN L C   1 
ATOM   22587 O O   . ASN L  2 128 ? -31.088 -41.731  20.367  1.00 157.70 ? 128 ASN L O   1 
ATOM   22588 C CB  . ASN L  2 128 ? -34.093 -41.051  19.653  1.00 152.38 ? 128 ASN L CB  1 
ATOM   22589 C CG  . ASN L  2 128 ? -35.089 -39.906  19.758  1.00 166.39 ? 128 ASN L CG  1 
ATOM   22590 O OD1 . ASN L  2 128 ? -34.757 -38.813  20.223  1.00 168.68 ? 128 ASN L OD1 1 
ATOM   22591 N ND2 . ASN L  2 128 ? -36.322 -40.160  19.340  1.00 176.81 ? 128 ASN L ND2 1 
ATOM   22592 N N   . ASN L  2 129 ? -31.459 -42.510  18.292  1.00 177.50 ? 129 ASN L N   1 
ATOM   22593 C CA  . ASN L  2 129 ? -30.571 -43.662  18.427  1.00 179.25 ? 129 ASN L CA  1 
ATOM   22594 C C   . ASN L  2 129 ? -29.106 -43.298  18.657  1.00 169.26 ? 129 ASN L C   1 
ATOM   22595 O O   . ASN L  2 129 ? -28.257 -44.179  18.776  1.00 169.00 ? 129 ASN L O   1 
ATOM   22596 C CB  . ASN L  2 129 ? -30.703 -44.576  17.207  1.00 169.36 ? 129 ASN L CB  1 
ATOM   22597 C CG  . ASN L  2 129 ? -32.108 -45.117  17.037  1.00 161.48 ? 129 ASN L CG  1 
ATOM   22598 O OD1 . ASN L  2 129 ? -32.359 -45.967  16.184  1.00 156.39 ? 129 ASN L OD1 1 
ATOM   22599 N ND2 . ASN L  2 129 ? -33.034 -44.629  17.856  1.00 168.05 ? 129 ASN L ND2 1 
ATOM   22600 N N   . ALA L  2 130 ? -28.815 -42.003  18.723  1.00 150.80 ? 130 ALA L N   1 
ATOM   22601 C CA  . ALA L  2 130 ? -27.455 -41.532  18.962  1.00 144.80 ? 130 ALA L CA  1 
ATOM   22602 C C   . ALA L  2 130 ? -27.464 -40.053  19.328  1.00 134.10 ? 130 ALA L C   1 
ATOM   22603 O O   . ALA L  2 130 ? -28.482 -39.378  19.181  1.00 136.47 ? 130 ALA L O   1 
ATOM   22604 C CB  . ALA L  2 130 ? -26.584 -41.773  17.738  1.00 140.55 ? 130 ALA L CB  1 
ATOM   22605 N N   . LYS L  2 131 ? -26.329 -39.550  19.805  1.00 142.31 ? 131 LYS L N   1 
ATOM   22606 C CA  . LYS L  2 131 ? -26.231 -38.148  20.199  1.00 157.51 ? 131 LYS L CA  1 
ATOM   22607 C C   . LYS L  2 131 ? -25.057 -37.444  19.527  1.00 163.78 ? 131 LYS L C   1 
ATOM   22608 O O   . LYS L  2 131 ? -24.032 -38.060  19.236  1.00 154.90 ? 131 LYS L O   1 
ATOM   22609 C CB  . LYS L  2 131 ? -26.104 -38.023  21.719  1.00 146.31 ? 131 LYS L CB  1 
ATOM   22610 C CG  . LYS L  2 131 ? -24.756 -38.463  22.266  1.00 151.02 ? 131 LYS L CG  1 
ATOM   22611 C CD  . LYS L  2 131 ? -24.539 -37.938  23.677  1.00 157.17 ? 131 LYS L CD  1 
ATOM   22612 C CE  . LYS L  2 131 ? -23.128 -38.227  24.166  1.00 157.02 ? 131 LYS L CE  1 
ATOM   22613 N NZ  . LYS L  2 131 ? -22.854 -37.589  25.484  1.00 146.37 ? 131 LYS L NZ  1 
ATOM   22614 N N   . GLU L  2 132 ? -25.214 -36.146  19.286  1.00 167.77 ? 132 GLU L N   1 
ATOM   22615 C CA  . GLU L  2 132 ? -24.142 -35.335  18.725  1.00 155.56 ? 132 GLU L CA  1 
ATOM   22616 C C   . GLU L  2 132 ? -23.107 -35.014  19.790  1.00 154.49 ? 132 GLU L C   1 
ATOM   22617 O O   . GLU L  2 132 ? -23.452 -34.730  20.936  1.00 162.89 ? 132 GLU L O   1 
ATOM   22618 C CB  . GLU L  2 132 ? -24.697 -34.026  18.169  1.00 165.17 ? 132 GLU L CB  1 
ATOM   22619 C CG  . GLU L  2 132 ? -25.735 -34.196  17.090  1.00 165.11 ? 132 GLU L CG  1 
ATOM   22620 C CD  . GLU L  2 132 ? -26.319 -32.875  16.651  1.00 169.95 ? 132 GLU L CD  1 
ATOM   22621 O OE1 . GLU L  2 132 ? -27.359 -32.898  15.968  1.00 165.59 ? 132 GLU L OE1 1 
ATOM   22622 O OE2 . GLU L  2 132 ? -25.745 -31.819  16.995  1.00 169.88 ? 132 GLU L OE2 1 
ATOM   22623 N N   . ILE L  2 133 ? -21.836 -35.057  19.406  1.00 137.42 ? 133 ILE L N   1 
ATOM   22624 C CA  . ILE L  2 133 ? -20.760 -34.659  20.302  1.00 154.30 ? 133 ILE L CA  1 
ATOM   22625 C C   . ILE L  2 133 ? -20.462 -33.172  20.119  1.00 153.63 ? 133 ILE L C   1 
ATOM   22626 O O   . ILE L  2 133 ? -20.114 -32.475  21.073  1.00 158.17 ? 133 ILE L O   1 
ATOM   22627 C CB  . ILE L  2 133 ? -19.479 -35.479  20.050  1.00 148.14 ? 133 ILE L CB  1 
ATOM   22628 C CG1 . ILE L  2 133 ? -19.738 -36.969  20.284  1.00 140.42 ? 133 ILE L CG1 1 
ATOM   22629 C CG2 . ILE L  2 133 ? -18.354 -35.001  20.951  1.00 140.32 ? 133 ILE L CG2 1 
ATOM   22630 C CD1 . ILE L  2 133 ? -19.972 -37.331  21.735  1.00 152.94 ? 133 ILE L CD1 1 
ATOM   22631 N N   . GLY L  2 134 ? -20.614 -32.691  18.888  1.00 150.12 ? 134 GLY L N   1 
ATOM   22632 C CA  . GLY L  2 134 ? -20.359 -31.298  18.564  1.00 145.83 ? 134 GLY L CA  1 
ATOM   22633 C C   . GLY L  2 134 ? -19.121 -31.166  17.701  1.00 131.18 ? 134 GLY L C   1 
ATOM   22634 O O   . GLY L  2 134 ? -18.860 -30.119  17.104  1.00 115.68 ? 134 GLY L O   1 
ATOM   22635 N N   . ASN L  2 135 ? -18.364 -32.255  17.629  1.00 118.13 ? 135 ASN L N   1 
ATOM   22636 C CA  . ASN L  2 135 ? -17.099 -32.281  16.913  1.00 103.82 ? 135 ASN L CA  1 
ATOM   22637 C C   . ASN L  2 135 ? -17.329 -32.742  15.495  1.00 105.94 ? 135 ASN L C   1 
ATOM   22638 O O   . ASN L  2 135 ? -16.378 -32.960  14.742  1.00 85.62  ? 135 ASN L O   1 
ATOM   22639 C CB  . ASN L  2 135 ? -16.141 -33.262  17.583  1.00 109.85 ? 135 ASN L CB  1 
ATOM   22640 C CG  . ASN L  2 135 ? -16.602 -34.703  17.445  1.00 121.39 ? 135 ASN L CG  1 
ATOM   22641 O OD1 . ASN L  2 135 ? -17.266 -35.056  16.479  1.00 119.35 ? 135 ASN L OD1 1 
ATOM   22642 N ND2 . ASN L  2 135 ? -16.264 -35.536  18.422  1.00 139.99 ? 135 ASN L ND2 1 
ATOM   22643 N N   . GLY L  2 136 ? -18.598 -32.925  15.148  1.00 103.54 ? 136 GLY L N   1 
ATOM   22644 C CA  . GLY L  2 136 ? -18.953 -33.514  13.873  1.00 95.24  ? 136 GLY L CA  1 
ATOM   22645 C C   . GLY L  2 136 ? -18.986 -35.035  13.944  1.00 104.02 ? 136 GLY L C   1 
ATOM   22646 O O   . GLY L  2 136 ? -18.930 -35.705  12.911  1.00 104.15 ? 136 GLY L O   1 
ATOM   22647 N N   . CYS L  2 137 ? -19.077 -35.573  15.162  1.00 130.80 ? 137 CYS L N   1 
ATOM   22648 C CA  . CYS L  2 137 ? -19.099 -37.015  15.394  1.00 127.33 ? 137 CYS L CA  1 
ATOM   22649 C C   . CYS L  2 137 ? -20.208 -37.388  16.363  1.00 129.74 ? 137 CYS L C   1 
ATOM   22650 O O   . CYS L  2 137 ? -20.502 -36.647  17.299  1.00 136.01 ? 137 CYS L O   1 
ATOM   22651 C CB  . CYS L  2 137 ? -17.766 -37.519  15.939  1.00 120.36 ? 137 CYS L CB  1 
ATOM   22652 S SG  . CYS L  2 137 ? -16.335 -37.010  14.997  1.00 148.54 ? 137 CYS L SG  1 
ATOM   22653 N N   . PHE L  2 138 ? -20.799 -38.555  16.136  1.00 121.56 ? 138 PHE L N   1 
ATOM   22654 C CA  . PHE L  2 138 ? -21.947 -39.007  16.899  1.00 140.00 ? 138 PHE L CA  1 
ATOM   22655 C C   . PHE L  2 138 ? -21.577 -40.142  17.849  1.00 146.26 ? 138 PHE L C   1 
ATOM   22656 O O   . PHE L  2 138 ? -20.578 -40.829  17.646  1.00 133.75 ? 138 PHE L O   1 
ATOM   22657 C CB  . PHE L  2 138 ? -23.035 -39.488  15.938  1.00 139.64 ? 138 PHE L CB  1 
ATOM   22658 C CG  . PHE L  2 138 ? -23.528 -38.428  14.991  1.00 122.55 ? 138 PHE L CG  1 
ATOM   22659 C CD1 . PHE L  2 138 ? -22.828 -38.118  13.833  1.00 113.96 ? 138 PHE L CD1 1 
ATOM   22660 C CD2 . PHE L  2 138 ? -24.704 -37.752  15.256  1.00 121.77 ? 138 PHE L CD2 1 
ATOM   22661 C CE1 . PHE L  2 138 ? -23.296 -37.143  12.964  1.00 113.38 ? 138 PHE L CE1 1 
ATOM   22662 C CE2 . PHE L  2 138 ? -25.175 -36.782  14.396  1.00 114.26 ? 138 PHE L CE2 1 
ATOM   22663 C CZ  . PHE L  2 138 ? -24.472 -36.476  13.248  1.00 113.16 ? 138 PHE L CZ  1 
ATOM   22664 N N   . GLU L  2 139 ? -22.389 -40.342  18.883  1.00 161.76 ? 139 GLU L N   1 
ATOM   22665 C CA  . GLU L  2 139 ? -22.212 -41.486  19.772  1.00 153.32 ? 139 GLU L CA  1 
ATOM   22666 C C   . GLU L  2 139 ? -23.469 -42.346  19.803  1.00 148.14 ? 139 GLU L C   1 
ATOM   22667 O O   . GLU L  2 139 ? -24.553 -41.871  20.144  1.00 151.65 ? 139 GLU L O   1 
ATOM   22668 C CB  . GLU L  2 139 ? -21.840 -41.039  21.186  1.00 165.77 ? 139 GLU L CB  1 
ATOM   22669 C CG  . GLU L  2 139 ? -21.638 -42.201  22.144  1.00 181.63 ? 139 GLU L CG  1 
ATOM   22670 C CD  . GLU L  2 139 ? -20.975 -41.789  23.442  1.00 186.56 ? 139 GLU L CD  1 
ATOM   22671 O OE1 . GLU L  2 139 ? -20.640 -40.595  23.589  1.00 174.74 ? 139 GLU L OE1 1 
ATOM   22672 O OE2 . GLU L  2 139 ? -20.785 -42.662  24.315  1.00 187.40 ? 139 GLU L OE2 1 
ATOM   22673 N N   . PHE L  2 140 ? -23.312 -43.615  19.441  1.00 167.55 ? 140 PHE L N   1 
ATOM   22674 C CA  . PHE L  2 140 ? -24.431 -44.547  19.378  1.00 178.13 ? 140 PHE L CA  1 
ATOM   22675 C C   . PHE L  2 140 ? -24.879 -45.012  20.759  1.00 179.90 ? 140 PHE L C   1 
ATOM   22676 O O   . PHE L  2 140 ? -24.055 -45.333  21.616  1.00 177.89 ? 140 PHE L O   1 
ATOM   22677 C CB  . PHE L  2 140 ? -24.061 -45.770  18.535  1.00 173.46 ? 140 PHE L CB  1 
ATOM   22678 C CG  . PHE L  2 140 ? -23.887 -45.474  17.074  1.00 165.94 ? 140 PHE L CG  1 
ATOM   22679 C CD1 . PHE L  2 140 ? -22.627 -45.270  16.538  1.00 165.78 ? 140 PHE L CD1 1 
ATOM   22680 C CD2 . PHE L  2 140 ? -24.986 -45.408  16.234  1.00 168.20 ? 140 PHE L CD2 1 
ATOM   22681 C CE1 . PHE L  2 140 ? -22.467 -45.000  15.191  1.00 165.19 ? 140 PHE L CE1 1 
ATOM   22682 C CE2 . PHE L  2 140 ? -24.833 -45.139  14.887  1.00 166.47 ? 140 PHE L CE2 1 
ATOM   22683 C CZ  . PHE L  2 140 ? -23.572 -44.934  14.365  1.00 164.11 ? 140 PHE L CZ  1 
ATOM   22684 N N   . TYR L  2 141 ? -26.191 -45.047  20.969  1.00 153.99 ? 141 TYR L N   1 
ATOM   22685 C CA  . TYR L  2 141 ? -26.753 -45.682  22.151  1.00 150.72 ? 141 TYR L CA  1 
ATOM   22686 C C   . TYR L  2 141 ? -27.012 -47.149  21.837  1.00 147.63 ? 141 TYR L C   1 
ATOM   22687 O O   . TYR L  2 141 ? -27.182 -47.970  22.737  1.00 156.49 ? 141 TYR L O   1 
ATOM   22688 C CB  . TYR L  2 141 ? -28.062 -45.012  22.572  1.00 155.36 ? 141 TYR L CB  1 
ATOM   22689 C CG  . TYR L  2 141 ? -27.924 -43.570  23.000  1.00 149.40 ? 141 TYR L CG  1 
ATOM   22690 C CD1 . TYR L  2 141 ? -28.759 -42.590  22.478  1.00 144.83 ? 141 TYR L CD1 1 
ATOM   22691 C CD2 . TYR L  2 141 ? -26.963 -43.186  23.925  1.00 144.54 ? 141 TYR L CD2 1 
ATOM   22692 C CE1 . TYR L  2 141 ? -28.641 -41.270  22.867  1.00 143.59 ? 141 TYR L CE1 1 
ATOM   22693 C CE2 . TYR L  2 141 ? -26.837 -41.868  24.319  1.00 143.87 ? 141 TYR L CE2 1 
ATOM   22694 C CZ  . TYR L  2 141 ? -27.679 -40.914  23.787  1.00 143.49 ? 141 TYR L CZ  1 
ATOM   22695 O OH  . TYR L  2 141 ? -27.559 -39.600  24.174  1.00 132.53 ? 141 TYR L OH  1 
ATOM   22696 N N   . HIS L  2 142 ? -27.042 -47.469  20.547  1.00 149.53 ? 142 HIS L N   1 
ATOM   22697 C CA  . HIS L  2 142 ? -27.322 -48.828  20.099  1.00 148.48 ? 142 HIS L CA  1 
ATOM   22698 C C   . HIS L  2 142 ? -26.113 -49.431  19.386  1.00 147.38 ? 142 HIS L C   1 
ATOM   22699 O O   . HIS L  2 142 ? -25.638 -48.896  18.384  1.00 161.62 ? 142 HIS L O   1 
ATOM   22700 C CB  . HIS L  2 142 ? -28.578 -48.854  19.215  1.00 144.48 ? 142 HIS L CB  1 
ATOM   22701 C CG  . HIS L  2 142 ? -28.313 -49.185  17.778  1.00 149.17 ? 142 HIS L CG  1 
ATOM   22702 N ND1 . HIS L  2 142 ? -28.490 -50.452  17.264  1.00 148.59 ? 142 HIS L ND1 1 
ATOM   22703 C CD2 . HIS L  2 142 ? -27.902 -48.413  16.745  1.00 143.94 ? 142 HIS L CD2 1 
ATOM   22704 C CE1 . HIS L  2 142 ? -28.191 -50.447  15.977  1.00 146.81 ? 142 HIS L CE1 1 
ATOM   22705 N NE2 . HIS L  2 142 ? -27.830 -49.224  15.637  1.00 145.76 ? 142 HIS L NE2 1 
ATOM   22706 N N   . LYS L  2 143 ? -25.611 -50.538  19.928  1.00 143.72 ? 143 LYS L N   1 
ATOM   22707 C CA  . LYS L  2 143 ? -24.429 -51.203  19.387  1.00 145.77 ? 143 LYS L CA  1 
ATOM   22708 C C   . LYS L  2 143 ? -24.461 -51.261  17.866  1.00 145.11 ? 143 LYS L C   1 
ATOM   22709 O O   . LYS L  2 143 ? -25.300 -51.942  17.277  1.00 139.60 ? 143 LYS L O   1 
ATOM   22710 C CB  . LYS L  2 143 ? -24.294 -52.616  19.962  1.00 151.42 ? 143 LYS L CB  1 
ATOM   22711 C CG  . LYS L  2 143 ? -23.883 -52.672  21.429  1.00 154.97 ? 143 LYS L CG  1 
ATOM   22712 C CD  . LYS L  2 143 ? -22.372 -52.552  21.607  1.00 157.82 ? 143 LYS L CD  1 
ATOM   22713 C CE  . LYS L  2 143 ? -21.896 -51.108  21.544  1.00 160.86 ? 143 LYS L CE  1 
ATOM   22714 N NZ  . LYS L  2 143 ? -20.425 -51.002  21.758  1.00 150.29 ? 143 LYS L NZ  1 
ATOM   22715 N N   . CYS L  2 144 ? -23.539 -50.541  17.235  1.00 153.36 ? 144 CYS L N   1 
ATOM   22716 C CA  . CYS L  2 144 ? -23.497 -50.463  15.781  1.00 163.52 ? 144 CYS L CA  1 
ATOM   22717 C C   . CYS L  2 144 ? -22.215 -51.070  15.223  1.00 151.53 ? 144 CYS L C   1 
ATOM   22718 O O   . CYS L  2 144 ? -21.169 -50.422  15.196  1.00 149.39 ? 144 CYS L O   1 
ATOM   22719 C CB  . CYS L  2 144 ? -23.639 -49.011  15.320  1.00 165.61 ? 144 CYS L CB  1 
ATOM   22720 S SG  . CYS L  2 144 ? -23.817 -48.806  13.534  1.00 172.23 ? 144 CYS L SG  1 
ATOM   22721 N N   . ASP L  2 145 ? -22.306 -52.320  14.781  1.00 158.58 ? 145 ASP L N   1 
ATOM   22722 C CA  . ASP L  2 145 ? -21.173 -53.005  14.170  1.00 162.29 ? 145 ASP L CA  1 
ATOM   22723 C C   . ASP L  2 145 ? -20.937 -52.546  12.730  1.00 160.25 ? 145 ASP L C   1 
ATOM   22724 O O   . ASP L  2 145 ? -21.462 -51.517  12.306  1.00 166.47 ? 145 ASP L O   1 
ATOM   22725 C CB  . ASP L  2 145 ? -21.346 -54.528  14.242  1.00 173.91 ? 145 ASP L CB  1 
ATOM   22726 C CG  . ASP L  2 145 ? -22.752 -54.981  13.887  1.00 181.09 ? 145 ASP L CG  1 
ATOM   22727 O OD1 . ASP L  2 145 ? -22.930 -56.185  13.604  1.00 172.53 ? 145 ASP L OD1 1 
ATOM   22728 O OD2 . ASP L  2 145 ? -23.680 -54.146  13.894  1.00 182.02 ? 145 ASP L OD2 1 
ATOM   22729 N N   . ASN L  2 146 ? -20.142 -53.311  11.987  1.00 151.20 ? 146 ASN L N   1 
ATOM   22730 C CA  . ASN L  2 146 ? -19.744 -52.931  10.632  1.00 142.25 ? 146 ASN L CA  1 
ATOM   22731 C C   . ASN L  2 146 ? -20.898 -52.798  9.641   1.00 150.21 ? 146 ASN L C   1 
ATOM   22732 O O   . ASN L  2 146 ? -20.938 -51.857  8.849   1.00 167.70 ? 146 ASN L O   1 
ATOM   22733 C CB  . ASN L  2 146 ? -18.703 -53.910  10.081  1.00 125.17 ? 146 ASN L CB  1 
ATOM   22734 C CG  . ASN L  2 146 ? -17.350 -53.760  10.747  1.00 124.46 ? 146 ASN L CG  1 
ATOM   22735 O OD1 . ASN L  2 146 ? -16.445 -54.564  10.525  1.00 127.34 ? 146 ASN L OD1 1 
ATOM   22736 N ND2 . ASN L  2 146 ? -17.205 -52.727  11.568  1.00 124.16 ? 146 ASN L ND2 1 
ATOM   22737 N N   . THR L  2 147 ? -21.828 -53.747  9.678   1.00 157.65 ? 147 THR L N   1 
ATOM   22738 C CA  . THR L  2 147 ? -22.948 -53.742  8.743   1.00 167.13 ? 147 THR L CA  1 
ATOM   22739 C C   . THR L  2 147 ? -24.034 -52.781  9.213   1.00 171.55 ? 147 THR L C   1 
ATOM   22740 O O   . THR L  2 147 ? -24.986 -52.493  8.487   1.00 174.83 ? 147 THR L O   1 
ATOM   22741 C CB  . THR L  2 147 ? -23.531 -55.152  8.550   1.00 164.59 ? 147 THR L CB  1 
ATOM   22742 O OG1 . THR L  2 147 ? -24.115 -55.604  9.778   1.00 176.19 ? 147 THR L OG1 1 
ATOM   22743 C CG2 . THR L  2 147 ? -22.435 -56.120  8.124   1.00 95.00  ? 147 THR L CG2 1 
ATOM   22744 N N   . CYS L  2 148 ? -23.879 -52.297  10.439  1.00 166.23 ? 148 CYS L N   1 
ATOM   22745 C CA  . CYS L  2 148 ? -24.722 -51.241  10.970  1.00 166.10 ? 148 CYS L CA  1 
ATOM   22746 C C   . CYS L  2 148 ? -24.184 -49.926  10.427  1.00 171.73 ? 148 CYS L C   1 
ATOM   22747 O O   . CYS L  2 148 ? -24.928 -49.099  9.899   1.00 168.76 ? 148 CYS L O   1 
ATOM   22748 C CB  . CYS L  2 148 ? -24.662 -51.257  12.498  1.00 168.70 ? 148 CYS L CB  1 
ATOM   22749 S SG  . CYS L  2 148 ? -25.514 -49.904  13.327  1.00 171.21 ? 148 CYS L SG  1 
ATOM   22750 N N   . MET L  2 149 ? -22.871 -49.761  10.547  1.00 172.18 ? 149 MET L N   1 
ATOM   22751 C CA  . MET L  2 149 ? -22.169 -48.599  10.017  1.00 159.87 ? 149 MET L CA  1 
ATOM   22752 C C   . MET L  2 149 ? -22.457 -48.375  8.535   1.00 154.64 ? 149 MET L C   1 
ATOM   22753 O O   . MET L  2 149 ? -22.369 -47.253  8.042   1.00 149.41 ? 149 MET L O   1 
ATOM   22754 C CB  . MET L  2 149 ? -20.661 -48.758  10.225  1.00 149.08 ? 149 MET L CB  1 
ATOM   22755 C CG  . MET L  2 149 ? -20.209 -48.657  11.672  1.00 147.64 ? 149 MET L CG  1 
ATOM   22756 S SD  . MET L  2 149 ? -20.479 -47.015  12.366  1.00 135.62 ? 149 MET L SD  1 
ATOM   22757 C CE  . MET L  2 149 ? -19.605 -47.156  13.922  1.00 141.82 ? 149 MET L CE  1 
ATOM   22758 N N   . GLU L  2 150 ? -22.796 -49.446  7.827   1.00 196.01 ? 150 GLU L N   1 
ATOM   22759 C CA  . GLU L  2 150 ? -23.036 -49.362  6.392   1.00 194.54 ? 150 GLU L CA  1 
ATOM   22760 C C   . GLU L  2 150 ? -24.400 -48.775  6.068   1.00 190.44 ? 150 GLU L C   1 
ATOM   22761 O O   . GLU L  2 150 ? -24.536 -47.959  5.156   1.00 189.38 ? 150 GLU L O   1 
ATOM   22762 C CB  . GLU L  2 150 ? -22.911 -50.740  5.752   1.00 202.65 ? 150 GLU L CB  1 
ATOM   22763 C CG  . GLU L  2 150 ? -21.797 -50.822  4.740   1.00 207.87 ? 150 GLU L CG  1 
ATOM   22764 C CD  . GLU L  2 150 ? -20.420 -50.887  5.383   1.00 207.36 ? 150 GLU L CD  1 
ATOM   22765 O OE1 . GLU L  2 150 ? -19.471 -51.364  4.724   1.00 209.92 ? 150 GLU L OE1 1 
ATOM   22766 O OE2 . GLU L  2 150 ? -20.286 -50.469  6.552   1.00 196.48 ? 150 GLU L OE2 1 
ATOM   22767 N N   . SER L  2 151 ? -25.412 -49.201  6.816   1.00 169.43 ? 151 SER L N   1 
ATOM   22768 C CA  . SER L  2 151 ? -26.770 -48.718  6.604   1.00 169.07 ? 151 SER L CA  1 
ATOM   22769 C C   . SER L  2 151 ? -26.801 -47.195  6.641   1.00 163.45 ? 151 SER L C   1 
ATOM   22770 O O   . SER L  2 151 ? -27.673 -46.565  6.041   1.00 169.26 ? 151 SER L O   1 
ATOM   22771 C CB  . SER L  2 151 ? -27.715 -49.293  7.661   1.00 171.83 ? 151 SER L CB  1 
ATOM   22772 O OG  . SER L  2 151 ? -27.373 -48.832  8.956   1.00 168.38 ? 151 SER L OG  1 
ATOM   22773 N N   . VAL L  2 152 ? -25.837 -46.611  7.344   1.00 132.72 ? 152 VAL L N   1 
ATOM   22774 C CA  . VAL L  2 152 ? -25.735 -45.163  7.448   1.00 126.48 ? 152 VAL L CA  1 
ATOM   22775 C C   . VAL L  2 152 ? -25.097 -44.573  6.194   1.00 129.80 ? 152 VAL L C   1 
ATOM   22776 O O   . VAL L  2 152 ? -25.602 -43.601  5.632   1.00 122.16 ? 152 VAL L O   1 
ATOM   22777 C CB  . VAL L  2 152 ? -24.907 -44.742  8.673   1.00 109.86 ? 152 VAL L CB  1 
ATOM   22778 C CG1 . VAL L  2 152 ? -25.060 -43.251  8.925   1.00 101.36 ? 152 VAL L CG1 1 
ATOM   22779 C CG2 . VAL L  2 152 ? -25.331 -45.537  9.897   1.00 115.40 ? 152 VAL L CG2 1 
ATOM   22780 N N   . LYS L  2 153 ? -23.986 -45.162  5.760   1.00 131.15 ? 153 LYS L N   1 
ATOM   22781 C CA  . LYS L  2 153 ? -23.286 -44.698  4.565   1.00 125.94 ? 153 LYS L CA  1 
ATOM   22782 C C   . LYS L  2 153 ? -24.153 -44.842  3.323   1.00 142.84 ? 153 LYS L C   1 
ATOM   22783 O O   . LYS L  2 153 ? -24.391 -43.869  2.605   1.00 143.69 ? 153 LYS L O   1 
ATOM   22784 C CB  . LYS L  2 153 ? -21.986 -45.475  4.361   1.00 119.51 ? 153 LYS L CB  1 
ATOM   22785 C CG  . LYS L  2 153 ? -20.928 -45.215  5.410   1.00 95.69  ? 153 LYS L CG  1 
ATOM   22786 C CD  . LYS L  2 153 ? -19.596 -45.809  4.987   1.00 99.28  ? 153 LYS L CD  1 
ATOM   22787 C CE  . LYS L  2 153 ? -18.536 -45.598  6.053   1.00 95.22  ? 153 LYS L CE  1 
ATOM   22788 N NZ  . LYS L  2 153 ? -18.887 -46.284  7.325   1.00 112.45 ? 153 LYS L NZ  1 
ATOM   22789 N N   . ASN L  2 154 ? -24.613 -46.065  3.071   1.00 192.16 ? 154 ASN L N   1 
ATOM   22790 C CA  . ASN L  2 154 ? -25.482 -46.346  1.930   1.00 192.09 ? 154 ASN L CA  1 
ATOM   22791 C C   . ASN L  2 154 ? -26.878 -45.729  2.108   1.00 196.37 ? 154 ASN L C   1 
ATOM   22792 O O   . ASN L  2 154 ? -27.806 -46.048  1.361   1.00 201.97 ? 154 ASN L O   1 
ATOM   22793 C CB  . ASN L  2 154 ? -25.552 -47.862  1.653   1.00 200.79 ? 154 ASN L CB  1 
ATOM   22794 C CG  . ASN L  2 154 ? -24.178 -48.464  1.330   1.00 200.66 ? 154 ASN L CG  1 
ATOM   22795 O OD1 . ASN L  2 154 ? -23.153 -47.830  1.570   1.00 194.77 ? 154 ASN L OD1 1 
ATOM   22796 N ND2 . ASN L  2 154 ? -24.156 -49.689  0.785   1.00 204.43 ? 154 ASN L ND2 1 
ATOM   22797 N N   . GLY L  2 155 ? -27.012 -44.852  3.103   1.00 172.75 ? 155 GLY L N   1 
ATOM   22798 C CA  . GLY L  2 155 ? -28.238 -44.101  3.329   1.00 168.88 ? 155 GLY L CA  1 
ATOM   22799 C C   . GLY L  2 155 ? -29.485 -44.917  3.621   1.00 172.40 ? 155 GLY L C   1 
ATOM   22800 O O   . GLY L  2 155 ? -30.572 -44.368  3.788   1.00 166.78 ? 155 GLY L O   1 
ATOM   22801 N N   . THR L  2 156 ? -29.329 -46.233  3.680   1.00 189.91 ? 156 THR L N   1 
ATOM   22802 C CA  . THR L  2 156 ? -30.442 -47.132  3.959   1.00 195.50 ? 156 THR L CA  1 
ATOM   22803 C C   . THR L  2 156 ? -30.404 -47.579  5.419   1.00 180.10 ? 156 THR L C   1 
ATOM   22804 O O   . THR L  2 156 ? -29.947 -48.683  5.725   1.00 171.26 ? 156 THR L O   1 
ATOM   22805 C CB  . THR L  2 156 ? -30.383 -48.369  3.056   1.00 202.79 ? 156 THR L CB  1 
ATOM   22806 O OG1 . THR L  2 156 ? -29.088 -48.973  3.163   1.00 195.16 ? 156 THR L OG1 1 
ATOM   22807 C CG2 . THR L  2 156 ? -30.626 -47.982  1.596   1.00 205.00 ? 156 THR L CG2 1 
ATOM   22808 N N   . TYR L  2 157 ? -30.883 -46.715  6.312   1.00 152.21 ? 157 TYR L N   1 
ATOM   22809 C CA  . TYR L  2 157 ? -30.783 -46.949  7.748   1.00 149.98 ? 157 TYR L CA  1 
ATOM   22810 C C   . TYR L  2 157 ? -32.120 -47.455  8.274   1.00 155.41 ? 157 TYR L C   1 
ATOM   22811 O O   . TYR L  2 157 ? -33.171 -47.168  7.704   1.00 146.30 ? 157 TYR L O   1 
ATOM   22812 C CB  . TYR L  2 157 ? -30.299 -45.685  8.471   1.00 147.78 ? 157 TYR L CB  1 
ATOM   22813 C CG  . TYR L  2 157 ? -30.051 -45.885  9.949   1.00 132.69 ? 157 TYR L CG  1 
ATOM   22814 C CD1 . TYR L  2 157 ? -28.809 -46.292  10.410  1.00 130.18 ? 157 TYR L CD1 1 
ATOM   22815 C CD2 . TYR L  2 157 ? -31.061 -45.679  10.879  1.00 125.12 ? 157 TYR L CD2 1 
ATOM   22816 C CE1 . TYR L  2 157 ? -28.576 -46.478  11.749  1.00 122.98 ? 157 TYR L CE1 1 
ATOM   22817 C CE2 . TYR L  2 157 ? -30.836 -45.868  12.229  1.00 130.20 ? 157 TYR L CE2 1 
ATOM   22818 C CZ  . TYR L  2 157 ? -29.587 -46.270  12.659  1.00 120.95 ? 157 TYR L CZ  1 
ATOM   22819 O OH  . TYR L  2 157 ? -29.336 -46.465  13.999  1.00 115.52 ? 157 TYR L OH  1 
ATOM   22820 N N   . ASP L  2 158 ? -32.072 -48.190  9.378   1.00 145.52 ? 158 ASP L N   1 
ATOM   22821 C CA  . ASP L  2 158 ? -33.231 -48.918  9.879   1.00 144.87 ? 158 ASP L CA  1 
ATOM   22822 C C   . ASP L  2 158 ? -33.270 -48.721  11.391  1.00 118.04 ? 158 ASP L C   1 
ATOM   22823 O O   . ASP L  2 158 ? -32.226 -48.597  12.033  1.00 113.77 ? 158 ASP L O   1 
ATOM   22824 C CB  . ASP L  2 158 ? -32.924 -50.409  10.023  1.00 123.21 ? 158 ASP L CB  1 
ATOM   22825 C CG  . ASP L  2 158 ? -31.488 -50.741  9.644   1.00 148.64 ? 158 ASP L CG  1 
ATOM   22826 O OD1 . ASP L  2 158 ? -30.573 -50.007  10.075  1.00 131.71 ? 158 ASP L OD1 1 
ATOM   22827 O OD2 . ASP L  2 158 ? -31.268 -51.730  8.913   1.00 148.83 ? 158 ASP L OD2 1 
ATOM   22828 N N   . TYR L  2 159 ? -34.453 -48.795  11.953  1.00 85.96  ? 159 TYR L N   1 
ATOM   22829 C CA  . TYR L  2 159 ? -34.538 -48.692  13.365  1.00 90.84  ? 159 TYR L CA  1 
ATOM   22830 C C   . TYR L  2 159 ? -34.859 -49.801  14.332  1.00 108.08 ? 159 TYR L C   1 
ATOM   22831 O O   . TYR L  2 159 ? -35.934 -49.825  14.913  1.00 96.65  ? 159 TYR L O   1 
ATOM   22832 C CB  . TYR L  2 159 ? -35.694 -47.740  13.231  1.00 28.62  ? 159 TYR L CB  1 
ATOM   22833 C CG  . TYR L  2 159 ? -35.550 -46.509  14.071  1.00 28.86  ? 159 TYR L CG  1 
ATOM   22834 C CD1 . TYR L  2 159 ? -36.628 -46.011  14.768  1.00 28.98  ? 159 TYR L CD1 1 
ATOM   22835 C CD2 . TYR L  2 159 ? -34.359 -45.843  14.168  1.00 28.97  ? 159 TYR L CD2 1 
ATOM   22836 C CE1 . TYR L  2 159 ? -36.529 -44.892  15.532  1.00 29.21  ? 159 TYR L CE1 1 
ATOM   22837 C CE2 . TYR L  2 159 ? -34.252 -44.724  14.944  1.00 29.21  ? 159 TYR L CE2 1 
ATOM   22838 C CZ  . TYR L  2 159 ? -35.348 -44.254  15.623  1.00 29.32  ? 159 TYR L CZ  1 
ATOM   22839 O OH  . TYR L  2 159 ? -35.279 -43.146  16.421  1.00 29.58  ? 159 TYR L OH  1 
ATOM   22840 N N   . PRO L  2 160 ? -33.903 -50.705  14.523  1.00 95.98  ? 160 PRO L N   1 
ATOM   22841 C CA  . PRO L  2 160 ? -33.738 -51.351  15.825  1.00 99.02  ? 160 PRO L CA  1 
ATOM   22842 C C   . PRO L  2 160 ? -33.065 -50.370  16.777  1.00 94.36  ? 160 PRO L C   1 
ATOM   22843 O O   . PRO L  2 160 ? -31.840 -50.228  16.769  1.00 72.98  ? 160 PRO L O   1 
ATOM   22844 C CB  . PRO L  2 160 ? -32.805 -52.523  15.519  1.00 82.70  ? 160 PRO L CB  1 
ATOM   22845 C CG  . PRO L  2 160 ? -33.055 -52.835  14.094  1.00 80.90  ? 160 PRO L CG  1 
ATOM   22846 C CD  . PRO L  2 160 ? -33.326 -51.510  13.432  1.00 64.44  ? 160 PRO L CD  1 
ATOM   22847 N N   . LYS L  2 161 ? -33.875 -49.684  17.575  1.00 103.63 ? 161 LYS L N   1 
ATOM   22848 C CA  . LYS L  2 161 ? -33.365 -48.706  18.524  1.00 98.96  ? 161 LYS L CA  1 
ATOM   22849 C C   . LYS L  2 161 ? -33.525 -49.193  19.959  1.00 120.98 ? 161 LYS L C   1 
ATOM   22850 O O   . LYS L  2 161 ? -34.026 -50.291  20.200  1.00 128.85 ? 161 LYS L O   1 
ATOM   22851 C CB  . LYS L  2 161 ? -34.091 -47.374  18.356  1.00 110.44 ? 161 LYS L CB  1 
ATOM   22852 C CG  . LYS L  2 161 ? -35.298 -47.208  19.270  1.00 101.42 ? 161 LYS L CG  1 
ATOM   22853 C CD  . LYS L  2 161 ? -35.286 -45.829  19.925  1.00 108.46 ? 161 LYS L CD  1 
ATOM   22854 C CE  . LYS L  2 161 ? -36.242 -45.755  21.110  1.00 89.50  ? 161 LYS L CE  1 
ATOM   22855 N NZ  . LYS L  2 161 ? -36.981 -44.460  21.187  1.00 85.75  ? 161 LYS L NZ  1 
ATOM   22856 N N   . TYR L  2 162 ? -33.093 -48.360  20.901  1.00 111.17 ? 162 TYR L N   1 
ATOM   22857 C CA  . TYR L  2 162 ? -33.212 -48.629  22.333  1.00 120.54 ? 162 TYR L CA  1 
ATOM   22858 C C   . TYR L  2 162 ? -34.059 -49.856  22.699  1.00 111.36 ? 162 TYR L C   1 
ATOM   22859 O O   . TYR L  2 162 ? -33.641 -50.704  23.499  1.00 102.91 ? 162 TYR L O   1 
ATOM   22860 C CB  . TYR L  2 162 ? -33.756 -47.387  23.040  1.00 102.69 ? 162 TYR L CB  1 
ATOM   22861 C CG  . TYR L  2 162 ? -33.055 -47.111  24.342  1.00 89.19  ? 162 TYR L CG  1 
ATOM   22862 C CD1 . TYR L  2 162 ? -32.069 -46.138  24.435  1.00 80.12  ? 162 TYR L CD1 1 
ATOM   22863 C CD2 . TYR L  2 162 ? -33.363 -47.842  25.475  1.00 106.72 ? 162 TYR L CD2 1 
ATOM   22864 C CE1 . TYR L  2 162 ? -31.422 -45.894  25.628  1.00 111.28 ? 162 TYR L CE1 1 
ATOM   22865 C CE2 . TYR L  2 162 ? -32.724 -47.608  26.669  1.00 101.71 ? 162 TYR L CE2 1 
ATOM   22866 C CZ  . TYR L  2 162 ? -31.752 -46.634  26.743  1.00 110.05 ? 162 TYR L CZ  1 
ATOM   22867 O OH  . TYR L  2 162 ? -31.107 -46.397  27.937  1.00 92.52  ? 162 TYR L OH  1 
HETATM 22868 C C1  . NAG M  3 .   ? -30.047 -47.862  -6.756  1.00 67.29  ? 601 NAG A C1  1 
HETATM 22869 C C2  . NAG M  3 .   ? -29.052 -46.717  -6.611  1.00 78.14  ? 601 NAG A C2  1 
HETATM 22870 C C3  . NAG M  3 .   ? -28.701 -46.122  -7.969  1.00 93.81  ? 601 NAG A C3  1 
HETATM 22871 C C4  . NAG M  3 .   ? -28.354 -47.217  -8.971  1.00 94.02  ? 601 NAG A C4  1 
HETATM 22872 C C5  . NAG M  3 .   ? -29.399 -48.326  -8.951  1.00 104.59 ? 601 NAG A C5  1 
HETATM 22873 C C6  . NAG M  3 .   ? -29.011 -49.459  -9.894  1.00 76.88  ? 601 NAG A C6  1 
HETATM 22874 C C7  . NAG M  3 .   ? -29.229 -45.579  -4.475  1.00 82.25  ? 601 NAG A C7  1 
HETATM 22875 C C8  . NAG M  3 .   ? -29.868 -44.477  -3.684  1.00 57.31  ? 601 NAG A C8  1 
HETATM 22876 N N2  . NAG M  3 .   ? -29.601 -45.690  -5.747  1.00 91.24  ? 601 NAG A N2  1 
HETATM 22877 O O3  . NAG M  3 .   ? -27.603 -45.248  -7.830  1.00 74.14  ? 601 NAG A O3  1 
HETATM 22878 O O4  . NAG M  3 .   ? -28.281 -46.663  -10.266 1.00 57.76  ? 601 NAG A O4  1 
HETATM 22879 O O5  . NAG M  3 .   ? -29.525 -48.829  -7.640  1.00 89.01  ? 601 NAG A O5  1 
HETATM 22880 O O6  . NAG M  3 .   ? -29.892 -49.476  -10.995 1.00 53.76  ? 601 NAG A O6  1 
HETATM 22881 O O7  . NAG M  3 .   ? -28.406 -46.328  -3.950  1.00 81.91  ? 601 NAG A O7  1 
HETATM 22882 C C1  . NAG N  3 .   ? 6.984   -38.453  -42.734 1.00 114.15 ? 602 NAG A C1  1 
HETATM 22883 C C2  . NAG N  3 .   ? 7.594   -37.619  -43.850 1.00 91.10  ? 602 NAG A C2  1 
HETATM 22884 C C3  . NAG N  3 .   ? 8.157   -36.313  -43.323 1.00 93.45  ? 602 NAG A C3  1 
HETATM 22885 C C4  . NAG N  3 .   ? 7.127   -35.580  -42.464 1.00 113.55 ? 602 NAG A C4  1 
HETATM 22886 C C5  . NAG N  3 .   ? 6.373   -36.506  -41.510 1.00 115.44 ? 602 NAG A C5  1 
HETATM 22887 C C6  . NAG N  3 .   ? 5.134   -35.789  -40.989 1.00 127.35 ? 602 NAG A C6  1 
HETATM 22888 C C7  . NAG N  3 .   ? 8.757   -38.279  -45.854 1.00 89.12  ? 602 NAG A C7  1 
HETATM 22889 C C8  . NAG N  3 .   ? 10.151  -38.205  -46.397 1.00 102.01 ? 602 NAG A C8  1 
HETATM 22890 N N2  . NAG N  3 .   ? 8.646   -38.336  -44.532 1.00 82.17  ? 602 NAG A N2  1 
HETATM 22891 O O3  . NAG N  3 .   ? 8.534   -35.551  -44.449 1.00 129.83 ? 602 NAG A O3  1 
HETATM 22892 O O4  . NAG N  3 .   ? 7.757   -34.545  -41.728 1.00 120.23 ? 602 NAG A O4  1 
HETATM 22893 O O5  . NAG N  3 .   ? 5.953   -37.705  -42.128 1.00 117.49 ? 602 NAG A O5  1 
HETATM 22894 O O6  . NAG N  3 .   ? 4.967   -34.585  -41.706 1.00 130.23 ? 602 NAG A O6  1 
HETATM 22895 O O7  . NAG N  3 .   ? 7.786   -38.275  -46.610 1.00 87.11  ? 602 NAG A O7  1 
HETATM 22896 C C1  . NAG O  3 .   ? 8.171   -33.280  -42.278 1.00 145.26 ? 603 NAG A C1  1 
HETATM 22897 C C2  . NAG O  3 .   ? 8.332   -31.859  -41.771 1.00 144.30 ? 603 NAG A C2  1 
HETATM 22898 C C3  . NAG O  3 .   ? 8.433   -30.978  -43.005 1.00 131.66 ? 603 NAG A C3  1 
HETATM 22899 C C4  . NAG O  3 .   ? 9.641   -31.448  -43.816 1.00 148.80 ? 603 NAG A C4  1 
HETATM 22900 C C5  . NAG O  3 .   ? 9.649   -32.969  -44.026 1.00 143.32 ? 603 NAG A C5  1 
HETATM 22901 C C6  . NAG O  3 .   ? 10.956  -33.468  -44.633 1.00 139.09 ? 603 NAG A C6  1 
HETATM 22902 C C7  . NAG O  3 .   ? 7.626   -31.021  -39.677 1.00 155.18 ? 603 NAG A C7  1 
HETATM 22903 C C8  . NAG O  3 .   ? 6.727   -31.326  -38.513 1.00 149.38 ? 603 NAG A C8  1 
HETATM 22904 N N2  . NAG O  3 .   ? 7.266   -31.478  -40.869 1.00 149.07 ? 603 NAG A N2  1 
HETATM 22905 O O3  . NAG O  3 .   ? 8.574   -29.620  -42.655 1.00 120.32 ? 603 NAG A O3  1 
HETATM 22906 O O4  . NAG O  3 .   ? 9.637   -30.789  -45.061 1.00 154.82 ? 603 NAG A O4  1 
HETATM 22907 O O5  . NAG O  3 .   ? 9.416   -33.666  -42.816 1.00 148.95 ? 603 NAG A O5  1 
HETATM 22908 O O6  . NAG O  3 .   ? 11.838  -32.385  -44.807 1.00 174.08 ? 603 NAG A O6  1 
HETATM 22909 O O7  . NAG O  3 .   ? 8.666   -30.380  -39.527 1.00 155.40 ? 603 NAG A O7  1 
HETATM 22910 C C1  . NAG P  3 .   ? -2.075  -67.433  -29.464 1.00 106.52 ? 604 NAG A C1  1 
HETATM 22911 C C2  . NAG P  3 .   ? -0.850  -68.065  -28.814 1.00 109.08 ? 604 NAG A C2  1 
HETATM 22912 C C3  . NAG P  3 .   ? 0.052   -68.717  -29.856 1.00 104.26 ? 604 NAG A C3  1 
HETATM 22913 C C4  . NAG P  3 .   ? -0.742  -69.664  -30.749 1.00 115.48 ? 604 NAG A C4  1 
HETATM 22914 C C5  . NAG P  3 .   ? -2.065  -69.033  -31.165 1.00 114.93 ? 604 NAG A C5  1 
HETATM 22915 C C6  . NAG P  3 .   ? -3.236  -69.696  -30.449 1.00 114.47 ? 604 NAG A C6  1 
HETATM 22916 C C7  . NAG P  3 .   ? -0.420  -66.752  -26.820 1.00 96.06  ? 604 NAG A C7  1 
HETATM 22917 C C8  . NAG P  3 .   ? 0.422   -65.699  -26.162 1.00 68.39  ? 604 NAG A C8  1 
HETATM 22918 N N2  . NAG P  3 .   ? -0.108  -67.063  -28.075 1.00 108.55 ? 604 NAG A N2  1 
HETATM 22919 O O3  . NAG P  3 .   ? 1.079   -69.433  -29.208 1.00 112.98 ? 604 NAG A O3  1 
HETATM 22920 O O4  . NAG P  3 .   ? 0.014   -69.972  -31.898 1.00 126.25 ? 604 NAG A O4  1 
HETATM 22921 O O5  . NAG P  3 .   ? -2.043  -67.658  -30.856 1.00 117.10 ? 604 NAG A O5  1 
HETATM 22922 O O6  . NAG P  3 .   ? -4.209  -70.079  -31.395 1.00 101.93 ? 604 NAG A O6  1 
HETATM 22923 O O7  . NAG P  3 .   ? -1.344  -67.285  -26.208 1.00 97.34  ? 604 NAG A O7  1 
HETATM 22924 C C1  . NAG Q  3 .   ? 1.334   -70.549  -31.899 1.00 134.34 ? 605 NAG A C1  1 
HETATM 22925 C C2  . NAG Q  3 .   ? 1.868   -70.161  -33.273 1.00 130.04 ? 605 NAG A C2  1 
HETATM 22926 C C3  . NAG Q  3 .   ? 3.056   -71.079  -33.513 1.00 134.45 ? 605 NAG A C3  1 
HETATM 22927 C C4  . NAG Q  3 .   ? 4.081   -70.842  -32.409 1.00 147.12 ? 605 NAG A C4  1 
HETATM 22928 C C5  . NAG Q  3 .   ? 3.437   -71.022  -31.031 1.00 145.52 ? 605 NAG A C5  1 
HETATM 22929 C C6  . NAG Q  3 .   ? 4.435   -70.760  -29.904 1.00 125.50 ? 605 NAG A C6  1 
HETATM 22930 C C7  . NAG Q  3 .   ? 0.916   -69.662  -35.444 1.00 133.22 ? 605 NAG A C7  1 
HETATM 22931 C C8  . NAG Q  3 .   ? -0.336  -69.656  -36.271 1.00 125.49 ? 605 NAG A C8  1 
HETATM 22932 N N2  . NAG Q  3 .   ? 0.869   -70.348  -34.304 1.00 140.74 ? 605 NAG A N2  1 
HETATM 22933 O O3  . NAG Q  3 .   ? 3.625   -70.883  -34.791 1.00 124.17 ? 605 NAG A O3  1 
HETATM 22934 O O4  . NAG Q  3 .   ? 5.161   -71.734  -32.568 1.00 148.29 ? 605 NAG A O4  1 
HETATM 22935 O O5  . NAG Q  3 .   ? 2.280   -70.211  -30.900 1.00 147.63 ? 605 NAG A O5  1 
HETATM 22936 O O6  . NAG Q  3 .   ? 5.355   -69.767  -30.296 1.00 137.86 ? 605 NAG A O6  1 
HETATM 22937 O O7  . NAG Q  3 .   ? 1.921   -69.057  -35.823 1.00 125.70 ? 605 NAG A O7  1 
HETATM 22938 C C1  . NAG R  3 .   ? -7.673  -65.327  -20.438 1.00 130.55 ? 606 NAG A C1  1 
HETATM 22939 C C2  . NAG R  3 .   ? -8.331  -65.572  -19.077 1.00 134.59 ? 606 NAG A C2  1 
HETATM 22940 C C3  . NAG R  3 .   ? -8.084  -66.968  -18.509 1.00 141.01 ? 606 NAG A C3  1 
HETATM 22941 C C4  . NAG R  3 .   ? -8.125  -68.039  -19.587 1.00 143.85 ? 606 NAG A C4  1 
HETATM 22942 C C5  . NAG R  3 .   ? -7.241  -67.639  -20.756 1.00 138.54 ? 606 NAG A C5  1 
HETATM 22943 C C6  . NAG R  3 .   ? -7.232  -68.738  -21.810 1.00 133.85 ? 606 NAG A C6  1 
HETATM 22944 C C7  . NAG R  3 .   ? -8.485  -63.488  -17.840 1.00 117.58 ? 606 NAG A C7  1 
HETATM 22945 C C8  . NAG R  3 .   ? -7.728  -62.204  -18.017 1.00 126.53 ? 606 NAG A C8  1 
HETATM 22946 N N2  . NAG R  3 .   ? -7.822  -64.604  -18.126 1.00 122.99 ? 606 NAG A N2  1 
HETATM 22947 O O3  . NAG R  3 .   ? -9.053  -67.260  -17.524 1.00 107.79 ? 606 NAG A O3  1 
HETATM 22948 O O4  . NAG R  3 .   ? -7.694  -69.273  -19.055 1.00 121.07 ? 606 NAG A O4  1 
HETATM 22949 O O5  . NAG R  3 .   ? -7.725  -66.437  -21.314 1.00 130.51 ? 606 NAG A O5  1 
HETATM 22950 O O6  . NAG R  3 .   ? -8.543  -68.932  -22.290 1.00 116.00 ? 606 NAG A O6  1 
HETATM 22951 O O7  . NAG R  3 .   ? -9.652  -63.478  -17.455 1.00 103.84 ? 606 NAG A O7  1 
HETATM 22952 C C1  . NAG S  3 .   ? -66.151 -43.375  -13.149 1.00 170.43 ? 601 NAG C C1  1 
HETATM 22953 C C2  . NAG S  3 .   ? -65.186 -42.453  -12.413 1.00 179.52 ? 601 NAG C C2  1 
HETATM 22954 C C3  . NAG S  3 .   ? -65.271 -41.030  -12.954 1.00 175.76 ? 601 NAG C C3  1 
HETATM 22955 C C4  . NAG S  3 .   ? -65.211 -41.021  -14.477 1.00 180.26 ? 601 NAG C C4  1 
HETATM 22956 C C5  . NAG S  3 .   ? -66.174 -42.044  -15.068 1.00 182.47 ? 601 NAG C C5  1 
HETATM 22957 C C6  . NAG S  3 .   ? -66.055 -42.092  -16.586 1.00 189.09 ? 601 NAG C C6  1 
HETATM 22958 C C7  . NAG S  3 .   ? -64.524 -42.262  -10.087 1.00 181.83 ? 601 NAG C C7  1 
HETATM 22959 C C8  . NAG S  3 .   ? -64.950 -42.294  -8.649  1.00 157.11 ? 601 NAG C C8  1 
HETATM 22960 N N2  . NAG S  3 .   ? -65.477 -42.462  -10.993 1.00 192.68 ? 601 NAG C N2  1 
HETATM 22961 O O3  . NAG S  3 .   ? -64.205 -40.267  -12.437 1.00 198.02 ? 601 NAG C O3  1 
HETATM 22962 O O4  . NAG S  3 .   ? -65.541 -39.735  -14.952 1.00 187.88 ? 601 NAG C O4  1 
HETATM 22963 O O5  . NAG S  3 .   ? -65.892 -43.318  -14.534 1.00 176.65 ? 601 NAG C O5  1 
HETATM 22964 O O6  . NAG S  3 .   ? -64.694 -42.154  -16.950 1.00 185.65 ? 601 NAG C O6  1 
HETATM 22965 O O7  . NAG S  3 .   ? -63.348 -42.058  -10.385 1.00 179.66 ? 601 NAG C O7  1 
HETATM 22966 C C1  . NAG T  3 .   ? -59.848 -57.347  -27.759 1.00 80.70  ? 602 NAG C C1  1 
HETATM 22967 C C2  . NAG T  3 .   ? -58.443 -56.794  -28.017 1.00 73.90  ? 602 NAG C C2  1 
HETATM 22968 C C3  . NAG T  3 .   ? -58.199 -56.175  -29.396 1.00 86.00  ? 602 NAG C C3  1 
HETATM 22969 C C4  . NAG T  3 .   ? -58.959 -56.890  -30.502 1.00 71.63  ? 602 NAG C C4  1 
HETATM 22970 C C5  . NAG T  3 .   ? -60.398 -57.034  -30.031 1.00 77.58  ? 602 NAG C C5  1 
HETATM 22971 C C6  . NAG T  3 .   ? -61.329 -57.572  -31.109 1.00 76.71  ? 602 NAG C C6  1 
HETATM 22972 C C7  . NAG T  3 .   ? -57.003 -55.901  -26.343 1.00 84.53  ? 602 NAG C C7  1 
HETATM 22973 C C8  . NAG T  3 .   ? -56.829 -55.026  -25.136 1.00 63.85  ? 602 NAG C C8  1 
HETATM 22974 N N2  . NAG T  3 .   ? -58.135 -55.790  -27.020 1.00 74.81  ? 602 NAG C N2  1 
HETATM 22975 O O3  . NAG T  3 .   ? -56.816 -56.169  -29.685 1.00 66.61  ? 602 NAG C O3  1 
HETATM 22976 O O4  . NAG T  3 .   ? -58.877 -56.114  -31.677 1.00 80.91  ? 602 NAG C O4  1 
HETATM 22977 O O5  . NAG T  3 .   ? -60.402 -57.912  -28.928 1.00 95.18  ? 602 NAG C O5  1 
HETATM 22978 O O6  . NAG T  3 .   ? -61.600 -58.928  -30.838 1.00 61.17  ? 602 NAG C O6  1 
HETATM 22979 O O7  . NAG T  3 .   ? -56.129 -56.690  -26.690 1.00 102.53 ? 602 NAG C O7  1 
HETATM 22980 C C1  . NAG U  3 .   ? -58.612 -56.923  -32.845 1.00 86.58  ? 603 NAG C C1  1 
HETATM 22981 C C2  . NAG U  3 .   ? -58.709 -56.017  -34.066 1.00 80.56  ? 603 NAG C C2  1 
HETATM 22982 C C3  . NAG U  3 .   ? -58.469 -56.754  -35.375 1.00 84.40  ? 603 NAG C C3  1 
HETATM 22983 C C4  . NAG U  3 .   ? -57.272 -57.695  -35.290 1.00 100.25 ? 603 NAG C C4  1 
HETATM 22984 C C5  . NAG U  3 .   ? -57.302 -58.468  -33.974 1.00 95.16  ? 603 NAG C C5  1 
HETATM 22985 C C6  . NAG U  3 .   ? -56.126 -59.437  -33.852 1.00 76.68  ? 603 NAG C C6  1 
HETATM 22986 C C7  . NAG U  3 .   ? -60.119 -54.069  -34.203 1.00 77.37  ? 603 NAG C C7  1 
HETATM 22987 C C8  . NAG U  3 .   ? -61.502 -53.528  -34.411 1.00 74.76  ? 603 NAG C C8  1 
HETATM 22988 N N2  . NAG U  3 .   ? -60.013 -55.390  -34.107 1.00 55.37  ? 603 NAG C N2  1 
HETATM 22989 O O3  . NAG U  3 .   ? -58.298 -55.784  -36.384 1.00 111.99 ? 603 NAG C O3  1 
HETATM 22990 O O4  . NAG U  3 .   ? -57.403 -58.676  -36.288 1.00 104.73 ? 603 NAG C O4  1 
HETATM 22991 O O5  . NAG U  3 .   ? -57.369 -57.595  -32.863 1.00 93.43  ? 603 NAG C O5  1 
HETATM 22992 O O6  . NAG U  3 .   ? -54.912 -58.723  -33.830 1.00 120.59 ? 603 NAG C O6  1 
HETATM 22993 O O7  . NAG U  3 .   ? -59.150 -53.311  -34.132 1.00 77.67  ? 603 NAG C O7  1 
HETATM 22994 C C1  . BMA V  4 .   ? -56.255 -58.546  -37.140 1.00 115.55 ? 604 BMA C C1  1 
HETATM 22995 C C2  . BMA V  4 .   ? -56.254 -59.881  -37.876 1.00 104.73 ? 604 BMA C C2  1 
HETATM 22996 C C3  . BMA V  4 .   ? -56.418 -59.672  -39.376 1.00 103.86 ? 604 BMA C C3  1 
HETATM 22997 C C4  . BMA V  4 .   ? -55.521 -58.545  -39.872 1.00 124.84 ? 604 BMA C C4  1 
HETATM 22998 C C5  . BMA V  4 .   ? -55.736 -57.273  -39.060 1.00 110.06 ? 604 BMA C C5  1 
HETATM 22999 C C6  . BMA V  4 .   ? -56.229 -56.136  -39.947 1.00 112.77 ? 604 BMA C C6  1 
HETATM 23000 O O2  . BMA V  4 .   ? -57.324 -60.697  -37.388 1.00 118.20 ? 604 BMA C O2  1 
HETATM 23001 O O3  . BMA V  4 .   ? -57.784 -59.358  -39.668 1.00 123.59 ? 604 BMA C O3  1 
HETATM 23002 O O4  . BMA V  4 .   ? -54.150 -58.948  -39.774 1.00 151.25 ? 604 BMA C O4  1 
HETATM 23003 O O5  . BMA V  4 .   ? -56.689 -57.519  -38.029 1.00 118.03 ? 604 BMA C O5  1 
HETATM 23004 O O6  . BMA V  4 .   ? -57.652 -56.026  -39.833 1.00 89.96  ? 604 BMA C O6  1 
HETATM 23005 C C1  . NAG W  3 .   ? -40.333 -21.574  -60.003 1.00 91.72  ? 605 NAG C C1  1 
HETATM 23006 C C2  . NAG W  3 .   ? -39.851 -21.521  -61.452 1.00 98.10  ? 605 NAG C C2  1 
HETATM 23007 C C3  . NAG W  3 .   ? -41.008 -21.614  -62.450 1.00 86.31  ? 605 NAG C C3  1 
HETATM 23008 C C4  . NAG W  3 .   ? -42.014 -22.706  -62.083 1.00 79.79  ? 605 NAG C C4  1 
HETATM 23009 C C5  . NAG W  3 .   ? -42.343 -22.572  -60.598 1.00 94.31  ? 605 NAG C C5  1 
HETATM 23010 C C6  . NAG W  3 .   ? -43.409 -23.559  -60.127 1.00 80.87  ? 605 NAG C C6  1 
HETATM 23011 C C7  . NAG W  3 .   ? -37.806 -20.205  -61.589 1.00 84.67  ? 605 NAG C C7  1 
HETATM 23012 C C8  . NAG W  3 .   ? -37.220 -18.835  -61.766 1.00 85.13  ? 605 NAG C C8  1 
HETATM 23013 N N2  . NAG W  3 .   ? -39.132 -20.282  -61.668 1.00 91.48  ? 605 NAG C N2  1 
HETATM 23014 O O3  . NAG W  3 .   ? -40.517 -21.802  -63.760 1.00 70.84  ? 605 NAG C O3  1 
HETATM 23015 O O4  . NAG W  3 .   ? -43.189 -22.516  -62.848 1.00 94.59  ? 605 NAG C O4  1 
HETATM 23016 O O5  . NAG W  3 .   ? -41.161 -22.704  -59.832 1.00 82.91  ? 605 NAG C O5  1 
HETATM 23017 O O6  . NAG W  3 .   ? -42.874 -24.860  -60.044 1.00 99.17  ? 605 NAG C O6  1 
HETATM 23018 O O7  . NAG W  3 .   ? -37.082 -21.178  -61.380 1.00 86.44  ? 605 NAG C O7  1 
HETATM 23019 C C1  . NAG X  3 .   ? -43.413 -23.511  -63.878 1.00 91.04  ? 606 NAG C C1  1 
HETATM 23020 C C2  . NAG X  3 .   ? -44.907 -23.853  -63.816 1.00 106.92 ? 606 NAG C C2  1 
HETATM 23021 C C3  . NAG X  3 .   ? -45.454 -24.550  -65.052 1.00 115.93 ? 606 NAG C C3  1 
HETATM 23022 C C4  . NAG X  3 .   ? -45.095 -23.708  -66.255 1.00 126.28 ? 606 NAG C C4  1 
HETATM 23023 C C5  . NAG X  3 .   ? -43.582 -23.560  -66.344 1.00 115.15 ? 606 NAG C C5  1 
HETATM 23024 C C6  . NAG X  3 .   ? -43.269 -22.625  -67.507 1.00 136.67 ? 606 NAG C C6  1 
HETATM 23025 C C7  . NAG X  3 .   ? -46.470 -24.422  -62.103 1.00 113.55 ? 606 NAG C C7  1 
HETATM 23026 C C8  . NAG X  3 .   ? -47.100 -25.586  -61.394 1.00 91.57  ? 606 NAG C C8  1 
HETATM 23027 N N2  . NAG X  3 .   ? -45.267 -24.621  -62.639 1.00 119.14 ? 606 NAG C N2  1 
HETATM 23028 O O3  . NAG X  3 .   ? -46.858 -24.655  -64.947 1.00 93.01  ? 606 NAG C O3  1 
HETATM 23029 O O4  . NAG X  3 .   ? -45.614 -24.297  -67.429 1.00 98.46  ? 606 NAG C O4  1 
HETATM 23030 O O5  . NAG X  3 .   ? -42.986 -23.051  -65.155 1.00 104.62 ? 606 NAG C O5  1 
HETATM 23031 O O6  . NAG X  3 .   ? -44.251 -21.613  -67.546 1.00 144.14 ? 606 NAG C O6  1 
HETATM 23032 O O7  . NAG X  3 .   ? -47.062 -23.344  -62.187 1.00 94.70  ? 606 NAG C O7  1 
HETATM 23033 C C1  . NAG Y  3 .   ? -38.832 -23.398  -24.337 1.00 95.86  ? 607 NAG C C1  1 
HETATM 23034 C C2  . NAG Y  3 .   ? -38.335 -22.175  -25.098 1.00 106.86 ? 607 NAG C C2  1 
HETATM 23035 C C3  . NAG Y  3 .   ? -38.780 -20.888  -24.413 1.00 109.89 ? 607 NAG C C3  1 
HETATM 23036 C C4  . NAG Y  3 .   ? -40.265 -20.935  -24.075 1.00 130.50 ? 607 NAG C C4  1 
HETATM 23037 C C5  . NAG Y  3 .   ? -40.627 -22.245  -23.387 1.00 124.33 ? 607 NAG C C5  1 
HETATM 23038 C C6  . NAG Y  3 .   ? -42.126 -22.327  -23.122 1.00 142.34 ? 607 NAG C C6  1 
HETATM 23039 C C7  . NAG Y  3 .   ? -36.267 -23.088  -25.980 1.00 123.83 ? 607 NAG C C7  1 
HETATM 23040 C C8  . NAG Y  3 .   ? -34.768 -23.023  -26.000 1.00 116.64 ? 607 NAG C C8  1 
HETATM 23041 N N2  . NAG Y  3 .   ? -36.888 -22.208  -25.199 1.00 97.43  ? 607 NAG C N2  1 
HETATM 23042 O O3  . NAG Y  3 .   ? -38.526 -19.792  -25.263 1.00 99.38  ? 607 NAG C O3  1 
HETATM 23043 O O4  . NAG Y  3 .   ? -40.588 -19.854  -23.229 1.00 129.24 ? 607 NAG C O4  1 
HETATM 23044 O O5  . NAG Y  3 .   ? -40.234 -23.328  -24.200 1.00 105.98 ? 607 NAG C O5  1 
HETATM 23045 O O6  . NAG Y  3 .   ? -42.574 -23.643  -23.359 1.00 146.36 ? 607 NAG C O6  1 
HETATM 23046 O O7  . NAG Y  3 .   ? -36.865 -23.920  -26.659 1.00 122.53 ? 607 NAG C O7  1 
HETATM 23047 C C1  . NAG Z  3 .   ? -48.819 -93.235  -28.267 1.00 145.63 ? 601 NAG E C1  1 
HETATM 23048 C C2  . NAG Z  3 .   ? -50.167 -92.890  -28.888 1.00 166.97 ? 601 NAG E C2  1 
HETATM 23049 C C3  . NAG Z  3 .   ? -50.372 -93.637  -30.200 1.00 172.29 ? 601 NAG E C3  1 
HETATM 23050 C C4  . NAG Z  3 .   ? -49.145 -93.515  -31.096 1.00 178.86 ? 601 NAG E C4  1 
HETATM 23051 C C5  . NAG Z  3 .   ? -47.869 -93.816  -30.320 1.00 156.39 ? 601 NAG E C5  1 
HETATM 23052 C C6  . NAG Z  3 .   ? -46.637 -93.613  -31.194 1.00 156.53 ? 601 NAG E C6  1 
HETATM 23053 C C7  . NAG Z  3 .   ? -52.344 -92.477  -27.898 1.00 163.17 ? 601 NAG E C7  1 
HETATM 23054 C C8  . NAG Z  3 .   ? -53.376 -92.910  -26.900 1.00 117.53 ? 601 NAG E C8  1 
HETATM 23055 N N2  . NAG Z  3 .   ? -51.236 -93.210  -27.962 1.00 177.27 ? 601 NAG E N2  1 
HETATM 23056 O O3  . NAG Z  3 .   ? -51.497 -93.113  -30.869 1.00 152.38 ? 601 NAG E O3  1 
HETATM 23057 O O4  . NAG Z  3 .   ? -49.261 -94.413  -32.177 1.00 194.76 ? 601 NAG E O4  1 
HETATM 23058 O O5  . NAG Z  3 .   ? -47.792 -92.968  -29.195 1.00 131.54 ? 601 NAG E O5  1 
HETATM 23059 O O6  . NAG Z  3 .   ? -46.302 -92.244  -31.223 1.00 185.42 ? 601 NAG E O6  1 
HETATM 23060 O O7  . NAG Z  3 .   ? -52.536 -91.491  -28.608 1.00 151.96 ? 601 NAG E O7  1 
HETATM 23061 C C1  . NAG AA 3 .   ? -22.621 -69.124  -74.212 1.00 119.90 ? 602 NAG E C1  1 
HETATM 23062 C C2  . NAG AA 3 .   ? -21.504 -68.509  -75.045 1.00 115.25 ? 602 NAG E C2  1 
HETATM 23063 C C3  . NAG AA 3 .   ? -20.226 -69.333  -74.938 1.00 133.22 ? 602 NAG E C3  1 
HETATM 23064 C C4  . NAG AA 3 .   ? -19.905 -69.655  -73.483 1.00 134.65 ? 602 NAG E C4  1 
HETATM 23065 C C5  . NAG AA 3 .   ? -21.135 -70.189  -72.759 1.00 129.53 ? 602 NAG E C5  1 
HETATM 23066 C C6  . NAG AA 3 .   ? -20.836 -70.435  -71.285 1.00 131.50 ? 602 NAG E C6  1 
HETATM 23067 C C7  . NAG AA 3 .   ? -22.899 -67.599  -76.808 1.00 129.69 ? 602 NAG E C7  1 
HETATM 23068 C C8  . NAG AA 3 .   ? -23.233 -67.585  -78.270 1.00 108.95 ? 602 NAG E C8  1 
HETATM 23069 N N2  . NAG AA 3 .   ? -21.916 -68.410  -76.432 1.00 122.68 ? 602 NAG E N2  1 
HETATM 23070 O O3  . NAG AA 3 .   ? -19.155 -68.614  -75.507 1.00 126.19 ? 602 NAG E O3  1 
HETATM 23071 O O4  . NAG AA 3 .   ? -18.874 -70.615  -73.432 1.00 134.18 ? 602 NAG E O4  1 
HETATM 23072 O O5  . NAG AA 3 .   ? -22.190 -69.261  -72.876 1.00 130.07 ? 602 NAG E O5  1 
HETATM 23073 O O6  . NAG AA 3 .   ? -21.606 -71.524  -70.824 1.00 128.95 ? 602 NAG E O6  1 
HETATM 23074 O O7  . NAG AA 3 .   ? -23.519 -66.887  -76.019 1.00 135.50 ? 602 NAG E O7  1 
HETATM 23075 C C1  . NAG BA 3 .   ? -17.541 -70.581  -73.960 1.00 129.61 ? 603 NAG E C1  1 
HETATM 23076 C C2  . NAG BA 3 .   ? -16.837 -71.715  -73.214 1.00 139.25 ? 603 NAG E C2  1 
HETATM 23077 C C3  . NAG BA 3 .   ? -15.465 -71.993  -73.826 1.00 127.81 ? 603 NAG E C3  1 
HETATM 23078 C C4  . NAG BA 3 .   ? -15.544 -72.110  -75.346 1.00 142.52 ? 603 NAG E C4  1 
HETATM 23079 C C5  . NAG BA 3 .   ? -16.370 -70.969  -75.932 1.00 149.51 ? 603 NAG E C5  1 
HETATM 23080 C C6  . NAG BA 3 .   ? -16.528 -71.091  -77.442 1.00 166.73 ? 603 NAG E C6  1 
HETATM 23081 C C7  . NAG BA 3 .   ? -17.114 -72.277  -70.872 1.00 157.79 ? 603 NAG E C7  1 
HETATM 23082 C C8  . NAG BA 3 .   ? -16.696 -71.995  -69.458 1.00 119.01 ? 603 NAG E C8  1 
HETATM 23083 N N2  . NAG BA 3 .   ? -16.711 -71.411  -71.802 1.00 158.70 ? 603 NAG E N2  1 
HETATM 23084 O O3  . NAG BA 3 .   ? -14.932 -73.188  -73.296 1.00 127.64 ? 603 NAG E O3  1 
HETATM 23085 O O4  . NAG BA 3 .   ? -14.240 -72.099  -75.883 1.00 134.71 ? 603 NAG E O4  1 
HETATM 23086 O O5  . NAG BA 3 .   ? -17.641 -70.938  -75.321 1.00 131.67 ? 603 NAG E O5  1 
HETATM 23087 O O6  . NAG BA 3 .   ? -16.410 -72.442  -77.822 1.00 193.72 ? 603 NAG E O6  1 
HETATM 23088 O O7  . NAG BA 3 .   ? -17.796 -73.269  -71.130 1.00 160.89 ? 603 NAG E O7  1 
HETATM 23089 C C1  . NAG CA 3 .   ? -51.805 -66.892  -52.710 1.00 28.72  ? 604 NAG E C1  1 
HETATM 23090 C C2  . NAG CA 3 .   ? -51.753 -66.127  -51.390 1.00 28.35  ? 604 NAG E C2  1 
HETATM 23091 C C3  . NAG CA 3 .   ? -52.789 -65.006  -51.329 1.00 28.49  ? 604 NAG E C3  1 
HETATM 23092 C C4  . NAG CA 3 .   ? -52.872 -64.215  -52.633 1.00 29.14  ? 604 NAG E C4  1 
HETATM 23093 C C5  . NAG CA 3 .   ? -52.891 -65.141  -53.846 1.00 29.44  ? 604 NAG E C5  1 
HETATM 23094 C C6  . NAG CA 3 .   ? -52.873 -64.359  -55.157 1.00 30.12  ? 604 NAG E C6  1 
HETATM 23095 C C7  . NAG CA 3 .   ? -51.045 -67.308  -49.352 1.00 27.45  ? 604 NAG E C7  1 
HETATM 23096 C C8  . NAG CA 3 .   ? -51.435 -68.290  -48.287 1.00 26.94  ? 604 NAG E C8  1 
HETATM 23097 N N2  . NAG CA 3 .   ? -51.965 -67.052  -50.287 1.00 27.79  ? 604 NAG E N2  1 
HETATM 23098 O O3  . NAG CA 3 .   ? -52.460 -64.124  -50.280 1.00 28.26  ? 604 NAG E O3  1 
HETATM 23099 O O4  . NAG CA 3 .   ? -54.043 -63.427  -52.622 1.00 29.27  ? 604 NAG E O4  1 
HETATM 23100 O O5  . NAG CA 3 .   ? -51.768 -65.995  -53.799 1.00 29.30  ? 604 NAG E O5  1 
HETATM 23101 O O6  . NAG CA 3 .   ? -51.613 -63.752  -55.339 1.00 30.36  ? 604 NAG E O6  1 
HETATM 23102 O O7  . NAG CA 3 .   ? -49.929 -66.790  -49.324 1.00 27.56  ? 604 NAG E O7  1 
HETATM 23103 C C1  . NAG DA 3 .   ? -48.286 -75.756  -45.853 1.00 161.25 ? 605 NAG E C1  1 
HETATM 23104 C C2  . NAG DA 3 .   ? -47.868 -77.017  -45.117 1.00 175.68 ? 605 NAG E C2  1 
HETATM 23105 C C3  . NAG DA 3 .   ? -48.825 -78.139  -45.450 1.00 189.66 ? 605 NAG E C3  1 
HETATM 23106 C C4  . NAG DA 3 .   ? -50.264 -77.713  -45.206 1.00 193.30 ? 605 NAG E C4  1 
HETATM 23107 C C5  . NAG DA 3 .   ? -50.572 -76.281  -45.641 1.00 189.75 ? 605 NAG E C5  1 
HETATM 23108 C C6  . NAG DA 3 .   ? -51.879 -75.873  -44.968 1.00 188.35 ? 605 NAG E C6  1 
HETATM 23109 C C7  . NAG DA 3 .   ? -45.653 -77.771  -44.599 1.00 158.36 ? 605 NAG E C7  1 
HETATM 23110 C C8  . NAG DA 3 .   ? -44.469 -78.537  -45.109 1.00 134.86 ? 605 NAG E C8  1 
HETATM 23111 N N2  . NAG DA 3 .   ? -46.538 -77.405  -45.514 1.00 170.02 ? 605 NAG E N2  1 
HETATM 23112 O O3  . NAG DA 3 .   ? -48.514 -79.243  -44.632 1.00 199.74 ? 605 NAG E O3  1 
HETATM 23113 O O4  . NAG DA 3 .   ? -51.110 -78.573  -45.935 1.00 185.13 ? 605 NAG E O4  1 
HETATM 23114 O O5  . NAG DA 3 .   ? -49.540 -75.365  -45.327 1.00 171.04 ? 605 NAG E O5  1 
HETATM 23115 O O6  . NAG DA 3 .   ? -51.911 -74.497  -44.663 1.00 171.38 ? 605 NAG E O6  1 
HETATM 23116 O O7  . NAG DA 3 .   ? -45.784 -77.508  -43.401 1.00 157.70 ? 605 NAG E O7  1 
HETATM 23117 C C1  . NAG EA 3 .   ? -73.071 -79.807  -11.194 1.00 188.41 ? 601 NAG F C1  1 
HETATM 23118 C C2  . NAG EA 3 .   ? -74.139 -80.606  -11.931 1.00 184.63 ? 601 NAG F C2  1 
HETATM 23119 C C3  . NAG EA 3 .   ? -75.389 -79.765  -12.160 1.00 171.40 ? 601 NAG F C3  1 
HETATM 23120 C C4  . NAG EA 3 .   ? -75.815 -79.060  -10.878 1.00 172.15 ? 601 NAG F C4  1 
HETATM 23121 C C5  . NAG EA 3 .   ? -74.630 -78.371  -10.213 1.00 181.53 ? 601 NAG F C5  1 
HETATM 23122 C C6  . NAG EA 3 .   ? -75.039 -77.737  -8.889  1.00 182.34 ? 601 NAG F C6  1 
HETATM 23123 C C7  . NAG EA 3 .   ? -74.026 -82.224  -13.736 1.00 172.99 ? 601 NAG F C7  1 
HETATM 23124 C C8  . NAG EA 3 .   ? -73.414 -82.602  -15.052 1.00 157.26 ? 601 NAG F C8  1 
HETATM 23125 N N2  . NAG EA 3 .   ? -73.618 -81.076  -13.200 1.00 180.57 ? 601 NAG F N2  1 
HETATM 23126 O O3  . NAG EA 3 .   ? -76.437 -80.594  -12.612 1.00 154.69 ? 601 NAG F O3  1 
HETATM 23127 O O4  . NAG EA 3 .   ? -76.809 -78.105  -11.175 1.00 160.00 ? 601 NAG F O4  1 
HETATM 23128 O O5  . NAG EA 3 .   ? -73.605 -79.312  -9.986  1.00 194.84 ? 601 NAG F O5  1 
HETATM 23129 O O6  . NAG EA 3 .   ? -74.607 -76.395  -8.857  1.00 180.19 ? 601 NAG F O6  1 
HETATM 23130 O O7  . NAG EA 3 .   ? -74.859 -82.954  -13.202 1.00 173.06 ? 601 NAG F O7  1 
HETATM 23131 C C1  . NAG FA 3 .   ? -25.208 8.455    13.494  1.00 158.07 ? 601 NAG G C1  1 
HETATM 23132 C C2  . NAG FA 3 .   ? -24.934 9.627    14.430  1.00 167.69 ? 601 NAG G C2  1 
HETATM 23133 C C3  . NAG FA 3 .   ? -23.439 9.823    14.662  1.00 166.33 ? 601 NAG G C3  1 
HETATM 23134 C C4  . NAG FA 3 .   ? -22.763 8.495    14.980  1.00 167.25 ? 601 NAG G C4  1 
HETATM 23135 C C5  . NAG FA 3 .   ? -23.174 7.417    13.991  1.00 172.76 ? 601 NAG G C5  1 
HETATM 23136 C C6  . NAG FA 3 .   ? -22.515 6.101    14.377  1.00 176.98 ? 601 NAG G C6  1 
HETATM 23137 C C7  . NAG FA 3 .   ? -26.641 11.347   14.404  1.00 168.37 ? 601 NAG G C7  1 
HETATM 23138 C C8  . NAG FA 3 .   ? -27.050 12.704   13.909  1.00 148.78 ? 601 NAG G C8  1 
HETATM 23139 N N2  . NAG FA 3 .   ? -25.520 10.840   13.894  1.00 181.45 ? 601 NAG G N2  1 
HETATM 23140 O O3  . NAG FA 3 .   ? -23.239 10.714   15.739  1.00 149.08 ? 601 NAG G O3  1 
HETATM 23141 O O4  . NAG FA 3 .   ? -21.359 8.630    14.936  1.00 141.45 ? 601 NAG G O4  1 
HETATM 23142 O O5  . NAG FA 3 .   ? -24.579 7.285    13.971  1.00 158.88 ? 601 NAG G O5  1 
HETATM 23143 O O6  . NAG FA 3 .   ? -23.503 5.116    14.561  1.00 156.82 ? 601 NAG G O6  1 
HETATM 23144 O O7  . NAG FA 3 .   ? -27.325 10.753   15.238  1.00 154.98 ? 601 NAG G O7  1 
HETATM 23145 C C1  . NAG GA 3 .   ? -34.218 3.592    -5.678  1.00 172.05 ? 602 NAG G C1  1 
HETATM 23146 C C2  . NAG GA 3 .   ? -33.852 5.050    -5.427  1.00 186.95 ? 602 NAG G C2  1 
HETATM 23147 C C3  . NAG GA 3 .   ? -34.968 5.980    -5.886  1.00 191.42 ? 602 NAG G C3  1 
HETATM 23148 C C4  . NAG GA 3 .   ? -35.438 5.617    -7.290  1.00 195.99 ? 602 NAG G C4  1 
HETATM 23149 C C5  . NAG GA 3 .   ? -35.692 4.119    -7.411  1.00 198.90 ? 602 NAG G C5  1 
HETATM 23150 C C6  . NAG GA 3 .   ? -36.082 3.744    -8.836  1.00 189.37 ? 602 NAG G C6  1 
HETATM 23151 C C7  . NAG GA 3 .   ? -32.850 6.285    -3.594  1.00 183.22 ? 602 NAG G C7  1 
HETATM 23152 C C8  . NAG GA 3 .   ? -32.641 6.392    -2.113  1.00 171.33 ? 602 NAG G C8  1 
HETATM 23153 N N2  . NAG GA 3 .   ? -33.581 5.258    -4.017  1.00 179.53 ? 602 NAG G N2  1 
HETATM 23154 O O3  . NAG GA 3 .   ? -34.505 7.312    -5.875  1.00 202.73 ? 602 NAG G O3  1 
HETATM 23155 O O4  . NAG GA 3 .   ? -36.624 6.320    -7.585  1.00 175.71 ? 602 NAG G O4  1 
HETATM 23156 O O5  . NAG GA 3 .   ? -34.528 3.414    -7.042  1.00 192.84 ? 602 NAG G O5  1 
HETATM 23157 O O6  . NAG GA 3 .   ? -37.485 3.790    -8.966  1.00 177.83 ? 602 NAG G O6  1 
HETATM 23158 O O7  . NAG GA 3 .   ? -32.360 7.117    -4.356  1.00 190.14 ? 602 NAG G O7  1 
HETATM 23159 C C1  . NAG HA 3 .   ? 5.905   14.675   -5.221  1.00 151.56 ? 603 NAG G C1  1 
HETATM 23160 C C2  . NAG HA 3 .   ? 5.704   13.632   -4.128  1.00 166.81 ? 603 NAG G C2  1 
HETATM 23161 C C3  . NAG HA 3 .   ? 7.018   12.942   -3.783  1.00 179.33 ? 603 NAG G C3  1 
HETATM 23162 C C4  . NAG HA 3 .   ? 7.746   12.491   -5.044  1.00 168.38 ? 603 NAG G C4  1 
HETATM 23163 C C5  . NAG HA 3 .   ? 7.803   13.614   -6.073  1.00 163.34 ? 603 NAG G C5  1 
HETATM 23164 C C6  . NAG HA 3 .   ? 8.457   13.139   -7.364  1.00 157.81 ? 603 NAG G C6  1 
HETATM 23165 C C7  . NAG HA 3 .   ? 3.934   14.805   -2.954  1.00 185.47 ? 603 NAG G C7  1 
HETATM 23166 C C8  . NAG HA 3 .   ? 3.467   15.419   -1.668  1.00 159.82 ? 603 NAG G C8  1 
HETATM 23167 N N2  . NAG HA 3 .   ? 5.145   14.256   -2.944  1.00 174.84 ? 603 NAG G N2  1 
HETATM 23168 O O3  . NAG HA 3 .   ? 6.761   11.824   -2.963  1.00 181.21 ? 603 NAG G O3  1 
HETATM 23169 O O4  . NAG HA 3 .   ? 9.057   12.091   -4.712  1.00 154.88 ? 603 NAG G O4  1 
HETATM 23170 O O5  . NAG HA 3 .   ? 6.496   14.067   -6.347  1.00 161.26 ? 603 NAG G O5  1 
HETATM 23171 O O6  . NAG HA 3 .   ? 9.826   13.480   -7.351  1.00 139.00 ? 603 NAG G O6  1 
HETATM 23172 O O7  . NAG HA 3 .   ? 3.215   14.822   -3.952  1.00 199.00 ? 603 NAG G O7  1 
HETATM 23173 C C1  . NAG IA 3 .   ? -25.705 -30.402  -23.680 1.00 81.64  ? 601 NAG I C1  1 
HETATM 23174 C C2  . NAG IA 3 .   ? -25.035 -29.031  -23.784 1.00 83.60  ? 601 NAG I C2  1 
HETATM 23175 C C3  . NAG IA 3 .   ? -24.232 -28.777  -25.061 1.00 86.51  ? 601 NAG I C3  1 
HETATM 23176 C C4  . NAG IA 3 .   ? -23.515 -30.001  -25.622 1.00 85.74  ? 601 NAG I C4  1 
HETATM 23177 C C5  . NAG IA 3 .   ? -24.353 -31.268  -25.468 1.00 77.83  ? 601 NAG I C5  1 
HETATM 23178 C C6  . NAG IA 3 .   ? -23.526 -32.503  -25.814 1.00 72.12  ? 601 NAG I C6  1 
HETATM 23179 C C7  . NAG IA 3 .   ? -25.679 -26.992  -22.803 1.00 93.29  ? 601 NAG I C7  1 
HETATM 23180 C C8  . NAG IA 3 .   ? -26.428 -25.692  -22.891 1.00 76.18  ? 601 NAG I C8  1 
HETATM 23181 N N2  . NAG IA 3 .   ? -26.007 -27.963  -23.640 1.00 77.91  ? 601 NAG I N2  1 
HETATM 23182 O O3  . NAG IA 3 .   ? -23.272 -27.778  -24.788 1.00 75.09  ? 601 NAG I O3  1 
HETATM 23183 O O4  . NAG IA 3 .   ? -23.262 -29.747  -26.991 1.00 95.79  ? 601 NAG I O4  1 
HETATM 23184 O O5  . NAG IA 3 .   ? -24.831 -31.411  -24.145 1.00 82.25  ? 601 NAG I O5  1 
HETATM 23185 O O6  . NAG IA 3 .   ? -22.192 -32.304  -25.393 1.00 97.91  ? 601 NAG I O6  1 
HETATM 23186 O O7  . NAG IA 3 .   ? -24.772 -27.163  -21.994 1.00 92.53  ? 601 NAG I O7  1 
HETATM 23187 C C1  . NAG JA 3 .   ? -21.951 -30.168  -27.417 1.00 92.55  ? 602 NAG I C1  1 
HETATM 23188 C C2  . NAG JA 3 .   ? -21.824 -29.978  -28.932 1.00 96.45  ? 602 NAG I C2  1 
HETATM 23189 C C3  . NAG JA 3 .   ? -20.415 -30.252  -29.433 1.00 117.99 ? 602 NAG I C3  1 
HETATM 23190 C C4  . NAG JA 3 .   ? -19.534 -29.278  -28.676 1.00 132.80 ? 602 NAG I C4  1 
HETATM 23191 C C5  . NAG JA 3 .   ? -19.574 -29.615  -27.185 1.00 108.08 ? 602 NAG I C5  1 
HETATM 23192 C C6  . NAG JA 3 .   ? -18.722 -28.632  -26.387 1.00 123.08 ? 602 NAG I C6  1 
HETATM 23193 C C7  . NAG JA 3 .   ? -23.485 -30.212  -30.663 1.00 121.91 ? 602 NAG I C7  1 
HETATM 23194 C C8  . NAG JA 3 .   ? -24.281 -31.139  -31.534 1.00 117.47 ? 602 NAG I C8  1 
HETATM 23195 N N2  . NAG JA 3 .   ? -22.807 -30.764  -29.658 1.00 116.26 ? 602 NAG I N2  1 
HETATM 23196 O O3  . NAG JA 3 .   ? -20.339 -29.987  -30.815 1.00 133.08 ? 602 NAG I O3  1 
HETATM 23197 O O4  . NAG JA 3 .   ? -18.225 -29.175  -29.219 1.00 138.01 ? 602 NAG I O4  1 
HETATM 23198 O O5  . NAG JA 3 .   ? -20.897 -29.576  -26.667 1.00 92.31  ? 602 NAG I O5  1 
HETATM 23199 O O6  . NAG JA 3 .   ? -18.939 -27.327  -26.873 1.00 145.48 ? 602 NAG I O6  1 
HETATM 23200 O O7  . NAG JA 3 .   ? -23.467 -29.001  -30.889 1.00 128.83 ? 602 NAG I O7  1 
HETATM 23201 C C1  . BMA KA 4 .   ? -17.264 -30.145  -28.763 1.00 137.58 ? 603 BMA I C1  1 
HETATM 23202 C C2  . BMA KA 4 .   ? -16.323 -30.040  -29.958 1.00 143.38 ? 603 BMA I C2  1 
HETATM 23203 C C3  . BMA KA 4 .   ? -15.089 -29.216  -29.616 1.00 139.38 ? 603 BMA I C3  1 
HETATM 23204 C C4  . BMA KA 4 .   ? -14.405 -29.751  -28.361 1.00 135.31 ? 603 BMA I C4  1 
HETATM 23205 C C5  . BMA KA 4 .   ? -15.431 -30.057  -27.276 1.00 138.78 ? 603 BMA I C5  1 
HETATM 23206 C C6  . BMA KA 4 .   ? -14.986 -29.499  -25.931 1.00 127.53 ? 603 BMA I C6  1 
HETATM 23207 O O2  . BMA KA 4 .   ? -17.012 -29.433  -31.055 1.00 137.23 ? 603 BMA I O2  1 
HETATM 23208 O O3  . BMA KA 4 .   ? -15.466 -27.851  -29.406 1.00 119.96 ? 603 BMA I O3  1 
HETATM 23209 O O4  . BMA KA 4 .   ? -13.682 -30.945  -28.685 1.00 115.87 ? 603 BMA I O4  1 
HETATM 23210 O O5  . BMA KA 4 .   ? -16.686 -29.486  -27.639 1.00 142.51 ? 603 BMA I O5  1 
HETATM 23211 O O6  . BMA KA 4 .   ? -15.439 -30.362  -24.883 1.00 108.63 ? 603 BMA I O6  1 
HETATM 23212 C C1  . NAG LA 3 .   ? -23.411 1.167    -65.103 1.00 114.09 ? 604 NAG I C1  1 
HETATM 23213 C C2  . NAG LA 3 .   ? -22.600 1.267    -66.397 1.00 108.07 ? 604 NAG I C2  1 
HETATM 23214 C C3  . NAG LA 3 .   ? -22.880 0.129    -67.378 1.00 122.70 ? 604 NAG I C3  1 
HETATM 23215 C C4  . NAG LA 3 .   ? -22.681 -1.169   -66.595 1.00 139.54 ? 604 NAG I C4  1 
HETATM 23216 C C5  . NAG LA 3 .   ? -23.670 -1.162   -65.436 1.00 124.27 ? 604 NAG I C5  1 
HETATM 23217 C C6  . NAG LA 3 .   ? -23.676 -2.505   -64.717 1.00 114.06 ? 604 NAG I C6  1 
HETATM 23218 C C7  . NAG LA 3 .   ? -21.789 3.466    -66.911 1.00 105.24 ? 604 NAG I C7  1 
HETATM 23219 C C8  . NAG LA 3 .   ? -22.119 4.884    -67.275 1.00 94.51  ? 604 NAG I C8  1 
HETATM 23220 N N2  . NAG LA 3 .   ? -22.769 2.571    -67.013 1.00 98.02  ? 604 NAG I N2  1 
HETATM 23221 O O3  . NAG LA 3 .   ? -21.974 0.261    -68.449 1.00 121.64 ? 604 NAG I O3  1 
HETATM 23222 O O4  . NAG LA 3 .   ? -22.754 -2.447   -67.226 1.00 150.10 ? 604 NAG I O4  1 
HETATM 23223 O O5  . NAG LA 3 .   ? -23.326 -0.128   -64.542 1.00 131.92 ? 604 NAG I O5  1 
HETATM 23224 O O6  . NAG LA 3 .   ? -22.370 -2.811   -64.284 1.00 104.57 ? 604 NAG I O6  1 
HETATM 23225 O O7  . NAG LA 3 .   ? -20.657 3.169    -66.531 1.00 122.44 ? 604 NAG I O7  1 
HETATM 23226 C C1  . NAG MA 3 .   ? -23.009 -2.609   -68.643 1.00 141.96 ? 605 NAG I C1  1 
HETATM 23227 C C2  . NAG MA 3 .   ? -24.441 -3.041   -68.912 1.00 137.05 ? 605 NAG I C2  1 
HETATM 23228 C C3  . NAG MA 3 .   ? -24.539 -3.553   -70.346 1.00 128.19 ? 605 NAG I C3  1 
HETATM 23229 C C4  . NAG MA 3 .   ? -23.791 -2.673   -71.354 1.00 135.49 ? 605 NAG I C4  1 
HETATM 23230 C C5  . NAG MA 3 .   ? -22.512 -2.024   -70.825 1.00 132.60 ? 605 NAG I C5  1 
HETATM 23231 C C6  . NAG MA 3 .   ? -22.099 -0.867   -71.729 1.00 135.99 ? 605 NAG I C6  1 
HETATM 23232 C C7  . NAG MA 3 .   ? -26.084 -4.378   -67.705 1.00 133.70 ? 605 NAG I C7  1 
HETATM 23233 C C8  . NAG MA 3 .   ? -26.335 -5.648   -66.945 1.00 129.39 ? 605 NAG I C8  1 
HETATM 23234 N N2  . NAG MA 3 .   ? -24.812 -4.089   -67.977 1.00 147.00 ? 605 NAG I N2  1 
HETATM 23235 O O3  . NAG MA 3 .   ? -25.899 -3.602   -70.720 1.00 129.74 ? 605 NAG I O3  1 
HETATM 23236 O O4  . NAG MA 3 .   ? -23.454 -3.451   -72.483 1.00 134.83 ? 605 NAG I O4  1 
HETATM 23237 O O5  . NAG MA 3 .   ? -22.694 -1.549   -69.512 1.00 135.50 ? 605 NAG I O5  1 
HETATM 23238 O O6  . NAG MA 3 .   ? -23.180 0.031    -71.861 1.00 132.91 ? 605 NAG I O6  1 
HETATM 23239 O O7  . NAG MA 3 .   ? -27.025 -3.662   -68.052 1.00 137.43 ? 605 NAG I O7  1 
HETATM 23240 C C1  . NAG NA 3 .   ? 3.542   -35.374  -0.470  1.00 103.47 ? 601 NAG K C1  1 
HETATM 23241 C C2  . NAG NA 3 .   ? 4.881   -34.724  -0.833  1.00 123.58 ? 601 NAG K C2  1 
HETATM 23242 C C3  . NAG NA 3 .   ? 5.586   -35.401  -1.997  1.00 126.02 ? 601 NAG K C3  1 
HETATM 23243 C C4  . NAG NA 3 .   ? 5.749   -36.866  -1.656  1.00 140.82 ? 601 NAG K C4  1 
HETATM 23244 C C5  . NAG NA 3 .   ? 4.392   -37.524  -1.441  1.00 142.93 ? 601 NAG K C5  1 
HETATM 23245 C C6  . NAG NA 3 .   ? 4.600   -38.850  -0.715  1.00 128.19 ? 601 NAG K C6  1 
HETATM 23246 C C7  . NAG NA 3 .   ? 5.697   -32.461  -1.076  1.00 119.38 ? 601 NAG K C7  1 
HETATM 23247 C C8  . NAG NA 3 .   ? 5.684   -31.341  -2.076  1.00 99.15  ? 601 NAG K C8  1 
HETATM 23248 N N2  . NAG NA 3 .   ? 4.691   -33.326  -1.161  1.00 113.42 ? 601 NAG K N2  1 
HETATM 23249 O O3  . NAG NA 3 .   ? 6.851   -34.815  -2.237  1.00 110.63 ? 601 NAG K O3  1 
HETATM 23250 O O4  . NAG NA 3 .   ? 6.436   -37.520  -2.702  1.00 112.93 ? 601 NAG K O4  1 
HETATM 23251 O O5  . NAG NA 3 .   ? 3.439   -36.769  -0.705  1.00 125.28 ? 601 NAG K O5  1 
HETATM 23252 O O6  . NAG NA 3 .   ? 5.949   -38.958  -0.320  1.00 102.20 ? 601 NAG K O6  1 
HETATM 23253 O O7  . NAG NA 3 .   ? 6.598   -32.555  -0.242  1.00 88.71  ? 601 NAG K O7  1 
HETATM 23254 C C1  . NAG OA 3 .   ? 1.153   -14.009  0.456   1.00 108.86 ? 602 NAG K C1  1 
HETATM 23255 C C2  . NAG OA 3 .   ? 0.429   -12.922  -0.329  1.00 115.33 ? 602 NAG K C2  1 
HETATM 23256 C C3  . NAG OA 3 .   ? 1.353   -11.743  -0.611  1.00 123.07 ? 602 NAG K C3  1 
HETATM 23257 C C4  . NAG OA 3 .   ? 2.089   -11.312  0.651   1.00 125.12 ? 602 NAG K C4  1 
HETATM 23258 C C5  . NAG OA 3 .   ? 2.697   -12.512  1.367   1.00 122.34 ? 602 NAG K C5  1 
HETATM 23259 C C6  . NAG OA 3 .   ? 3.365   -12.091  2.671   1.00 95.36  ? 602 NAG K C6  1 
HETATM 23260 C C7  . NAG OA 3 .   ? -1.057  -12.867  -2.246  1.00 130.88 ? 602 NAG K C7  1 
HETATM 23261 C C8  . NAG OA 3 .   ? -1.493  -13.526  -3.522  1.00 101.70 ? 602 NAG K C8  1 
HETATM 23262 N N2  . NAG OA 3 .   ? -0.076  -13.465  -1.575  1.00 132.87 ? 602 NAG K N2  1 
HETATM 23263 O O3  . NAG OA 3 .   ? 0.597   -10.662  -1.107  1.00 139.70 ? 602 NAG K O3  1 
HETATM 23264 O O4  . NAG OA 3 .   ? 3.110   -10.400  0.312   1.00 112.13 ? 602 NAG K O4  1 
HETATM 23265 O O5  . NAG OA 3 .   ? 1.687   -13.458  1.639   1.00 113.22 ? 602 NAG K O5  1 
HETATM 23266 O O6  . NAG OA 3 .   ? 3.344   -10.685  2.776   1.00 68.38  ? 602 NAG K O6  1 
HETATM 23267 O O7  . NAG OA 3 .   ? -1.595  -11.829  -1.864  1.00 138.75 ? 602 NAG K O7  1 
HETATM 23268 C C1  . NAG PA 3 .   ? 1.585   -30.070  -37.686 1.00 116.44 ? 603 NAG K C1  1 
HETATM 23269 C C2  . NAG PA 3 .   ? 0.357   -29.184  -37.863 1.00 108.17 ? 603 NAG K C2  1 
HETATM 23270 C C3  . NAG PA 3 .   ? -0.352  -29.490  -39.177 1.00 142.02 ? 603 NAG K C3  1 
HETATM 23271 C C4  . NAG PA 3 .   ? 0.639   -29.540  -40.334 1.00 153.37 ? 603 NAG K C4  1 
HETATM 23272 C C5  . NAG PA 3 .   ? 1.846   -30.402  -39.982 1.00 142.72 ? 603 NAG K C5  1 
HETATM 23273 C C6  . NAG PA 3 .   ? 2.875   -30.386  -41.107 1.00 143.67 ? 603 NAG K C6  1 
HETATM 23274 C C7  . NAG PA 3 .   ? -0.656  -28.475  -35.776 1.00 84.20  ? 603 NAG K C7  1 
HETATM 23275 C C8  . NAG PA 3 .   ? -1.635  -28.783  -34.682 1.00 95.14  ? 603 NAG K C8  1 
HETATM 23276 N N2  . NAG PA 3 .   ? -0.555  -29.373  -36.752 1.00 98.20  ? 603 NAG K N2  1 
HETATM 23277 O O3  . NAG PA 3 .   ? -1.320  -28.497  -39.431 1.00 140.57 ? 603 NAG K O3  1 
HETATM 23278 O O4  . NAG PA 3 .   ? 0.002   -30.068  -41.476 1.00 135.14 ? 603 NAG K O4  1 
HETATM 23279 O O5  . NAG PA 3 .   ? 2.439   -29.919  -38.797 1.00 126.55 ? 603 NAG K O5  1 
HETATM 23280 O O6  . NAG PA 3 .   ? 4.156   -30.642  -40.576 1.00 147.46 ? 603 NAG K O6  1 
HETATM 23281 O O7  . NAG PA 3 .   ? 0.006   -27.439  -35.748 1.00 91.98  ? 603 NAG K O7  1 
HETATM 23282 C C1  . NAG QA 3 .   ? 2.574   -30.239  -26.540 1.00 131.44 ? 604 NAG K C1  1 
HETATM 23283 C C2  . NAG QA 3 .   ? 1.551   -31.335  -26.266 1.00 138.57 ? 604 NAG K C2  1 
HETATM 23284 C C3  . NAG QA 3 .   ? 1.919   -32.621  -26.996 1.00 146.70 ? 604 NAG K C3  1 
HETATM 23285 C C4  . NAG QA 3 .   ? 2.262   -32.342  -28.455 1.00 138.38 ? 604 NAG K C4  1 
HETATM 23286 C C5  . NAG QA 3 .   ? 3.236   -31.175  -28.574 1.00 137.85 ? 604 NAG K C5  1 
HETATM 23287 C C6  . NAG QA 3 .   ? 3.515   -30.844  -30.035 1.00 153.85 ? 604 NAG K C6  1 
HETATM 23288 C C7  . NAG QA 3 .   ? 1.611   -30.603  -23.954 1.00 122.25 ? 604 NAG K C7  1 
HETATM 23289 C C8  . NAG QA 3 .   ? 1.494   -30.985  -22.508 1.00 131.22 ? 604 NAG K C8  1 
HETATM 23290 N N2  . NAG QA 3 .   ? 1.460   -31.583  -24.840 1.00 120.75 ? 604 NAG K N2  1 
HETATM 23291 O O3  . NAG QA 3 .   ? 0.838   -33.524  -26.932 1.00 136.75 ? 604 NAG K O3  1 
HETATM 23292 O O4  . NAG QA 3 .   ? 2.837   -33.494  -29.031 1.00 142.12 ? 604 NAG K O4  1 
HETATM 23293 O O5  . NAG QA 3 .   ? 2.693   -30.044  -27.931 1.00 128.63 ? 604 NAG K O5  1 
HETATM 23294 O O6  . NAG QA 3 .   ? 4.144   -29.584  -30.119 1.00 133.39 ? 604 NAG K O6  1 
HETATM 23295 O O7  . NAG QA 3 .   ? 1.836   -29.438  -24.275 1.00 108.75 ? 604 NAG K O7  1 
HETATM 23296 C C1  . NAG RA 3 .   ? -23.137 -50.615  0.358   1.00 163.36 ? 601 NAG L C1  1 
HETATM 23297 C C2  . NAG RA 3 .   ? -22.333 -50.091  -0.826  1.00 161.60 ? 601 NAG L C2  1 
HETATM 23298 C C3  . NAG RA 3 .   ? -21.267 -51.094  -1.249  1.00 155.88 ? 601 NAG L C3  1 
HETATM 23299 C C4  . NAG RA 3 .   ? -20.479 -51.596  -0.045  1.00 172.14 ? 601 NAG L C4  1 
HETATM 23300 C C5  . NAG RA 3 .   ? -21.415 -52.015  1.083   1.00 172.33 ? 601 NAG L C5  1 
HETATM 23301 C C6  . NAG RA 3 .   ? -20.627 -52.441  2.317   1.00 178.96 ? 601 NAG L C6  1 
HETATM 23302 C C7  . NAG RA 3 .   ? -23.989 -48.725  -1.956  1.00 155.16 ? 601 NAG L C7  1 
HETATM 23303 C C8  . NAG RA 3 .   ? -24.860 -48.543  -3.164  1.00 132.67 ? 601 NAG L C8  1 
HETATM 23304 N N2  . NAG RA 3 .   ? -23.217 -49.808  -1.939  1.00 155.20 ? 601 NAG L N2  1 
HETATM 23305 O O3  . NAG RA 3 .   ? -20.385 -50.485  -2.166  1.00 144.63 ? 601 NAG L O3  1 
HETATM 23306 O O4  . NAG RA 3 .   ? -19.684 -52.695  -0.428  1.00 167.68 ? 601 NAG L O4  1 
HETATM 23307 O O5  . NAG RA 3 .   ? -22.262 -50.938  1.415   1.00 174.14 ? 601 NAG L O5  1 
HETATM 23308 O O6  . NAG RA 3 .   ? -21.266 -53.540  2.926   1.00 187.67 ? 601 NAG L O6  1 
HETATM 23309 O O7  . NAG RA 3 .   ? -24.007 -47.901  -1.044  1.00 132.38 ? 601 NAG L O7  1 
HETATM 23310 O O   . HOH SA 5 .   ? -13.178 -45.789  -51.646 1.00 35.45  ? 334 HOH A O   1 
HETATM 23311 O O   . HOH SA 5 .   ? 7.453   -63.312  -43.101 1.00 81.02  ? 335 HOH A O   1 
HETATM 23312 O O   . HOH SA 5 .   ? -6.303  -33.561  -61.525 1.00 52.97  ? 336 HOH A O   1 
HETATM 23313 O O   . HOH SA 5 .   ? 6.151   -64.501  -41.238 1.00 54.43  ? 337 HOH A O   1 
HETATM 23314 O O   . HOH SA 5 .   ? -30.300 -60.496  -1.009  1.00 48.75  ? 338 HOH A O   1 
HETATM 23315 O O   . HOH SA 5 .   ? -0.902  -42.570  -41.785 1.00 65.19  ? 339 HOH A O   1 
HETATM 23316 O O   . HOH SA 5 .   ? 4.110   -63.031  -64.935 1.00 79.41  ? 340 HOH A O   1 
HETATM 23317 O O   . HOH SA 5 .   ? 13.510  -37.297  -51.535 1.00 92.37  ? 341 HOH A O   1 
HETATM 23318 O O   . HOH SA 5 .   ? -3.389  -50.824  -71.042 1.00 98.28  ? 342 HOH A O   1 
HETATM 23319 O O   . HOH SA 5 .   ? 13.294  -40.923  -64.348 1.00 81.27  ? 343 HOH A O   1 
HETATM 23320 O O   . HOH SA 5 .   ? -12.105 -42.799  -54.880 1.00 39.88  ? 344 HOH A O   1 
HETATM 23321 O O   . HOH SA 5 .   ? -8.578  -65.156  -58.543 1.00 45.74  ? 345 HOH A O   1 
HETATM 23322 O O   . HOH SA 5 .   ? -8.768  -55.597  -62.900 1.00 76.41  ? 346 HOH A O   1 
HETATM 23323 O O   . HOH SA 5 .   ? -39.299 -56.322  -4.475  1.00 50.67  ? 347 HOH A O   1 
HETATM 23324 O O   . HOH SA 5 .   ? -15.735 -60.418  6.149   1.00 49.35  ? 348 HOH A O   1 
HETATM 23325 O O   . HOH SA 5 .   ? -25.412 -63.757  -10.681 1.00 63.56  ? 349 HOH A O   1 
HETATM 23326 O O   . HOH SA 5 .   ? -36.156 -51.498  -10.363 1.00 58.09  ? 350 HOH A O   1 
HETATM 23327 O O   . HOH SA 5 .   ? -7.822  -65.912  -14.806 1.00 73.00  ? 351 HOH A O   1 
HETATM 23328 O O   . HOH SA 5 .   ? 2.669   -28.851  -47.625 1.00 48.96  ? 353 HOH A O   1 
HETATM 23329 O O   . HOH SA 5 .   ? -9.534  -54.108  -59.238 1.00 60.26  ? 354 HOH A O   1 
HETATM 23330 O O   . HOH SA 5 .   ? -2.964  -69.687  -26.582 1.00 44.10  ? 355 HOH A O   1 
HETATM 23331 O O   . HOH SA 5 .   ? -12.805 -65.318  -15.476 1.00 44.97  ? 356 HOH A O   1 
HETATM 23332 O O   . HOH SA 5 .   ? -9.673  -50.649  -58.714 1.00 38.86  ? 357 HOH A O   1 
HETATM 23333 O O   . HOH SA 5 .   ? 13.327  -41.803  -73.766 1.00 104.27 ? 358 HOH A O   1 
HETATM 23334 O O   . HOH SA 5 .   ? 15.640  -55.172  -64.913 1.00 110.12 ? 359 HOH A O   1 
HETATM 23335 O O   . HOH SA 5 .   ? -9.646  -53.132  -18.352 1.00 67.43  ? 360 HOH A O   1 
HETATM 23336 O O   . HOH SA 5 .   ? -20.973 -64.735  -24.449 1.00 53.01  ? 361 HOH A O   1 
HETATM 23337 O O   . HOH SA 5 .   ? 9.799   -53.340  -43.677 1.00 105.40 ? 362 HOH A O   1 
HETATM 23338 O O   . HOH SA 5 .   ? 4.498   -62.646  -40.582 1.00 60.77  ? 363 HOH A O   1 
HETATM 23339 O O   . HOH SA 5 .   ? 0.809   -45.786  -38.872 1.00 62.37  ? 364 HOH A O   1 
HETATM 23340 O O   . HOH SA 5 .   ? -30.698 -46.836  -12.742 1.00 49.15  ? 365 HOH A O   1 
HETATM 23341 O O   . HOH SA 5 .   ? 0.803   -41.668  -71.231 1.00 69.86  ? 366 HOH A O   1 
HETATM 23342 O O   . HOH SA 5 .   ? 16.797  -49.430  -65.724 1.00 138.83 ? 367 HOH A O   1 
HETATM 23343 O O   . HOH SA 5 .   ? -10.194 -47.375  -34.864 1.00 46.10  ? 368 HOH A O   1 
HETATM 23344 O O   . HOH SA 5 .   ? -27.733 -45.439  -13.337 1.00 42.73  ? 369 HOH A O   1 
HETATM 23345 O O   . HOH SA 5 .   ? -10.151 -59.005  -46.547 1.00 63.08  ? 370 HOH A O   1 
HETATM 23346 O O   . HOH TA 5 .   ? -38.330 -65.219  10.972  1.00 73.55  ? 182 HOH B O   1 
HETATM 23347 O O   . HOH TA 5 .   ? -19.079 -66.342  -37.198 1.00 67.87  ? 183 HOH B O   1 
HETATM 23348 O O   . HOH TA 5 .   ? -31.255 -63.604  -11.652 1.00 29.05  ? 184 HOH B O   1 
HETATM 23349 O O   . HOH TA 5 .   ? -44.424 -71.481  11.807  1.00 86.07  ? 185 HOH B O   1 
HETATM 23350 O O   . HOH TA 5 .   ? -33.484 -68.107  8.345   1.00 66.49  ? 186 HOH B O   1 
HETATM 23351 O O   . HOH TA 5 .   ? -45.093 -73.700  -3.263  1.00 68.08  ? 187 HOH B O   1 
HETATM 23352 O O   . HOH TA 5 .   ? -35.160 -54.600  -28.145 1.00 50.08  ? 188 HOH B O   1 
HETATM 23353 O O   . HOH TA 5 .   ? -42.647 -78.935  23.343  1.00 62.77  ? 189 HOH B O   1 
HETATM 23354 O O   . HOH TA 5 .   ? -37.285 -58.498  -11.728 1.00 67.95  ? 190 HOH B O   1 
HETATM 23355 O O   . HOH TA 5 .   ? -50.317 -79.847  5.644   1.00 89.97  ? 191 HOH B O   1 
HETATM 23356 O O   . HOH TA 5 .   ? -42.675 -63.740  0.069   1.00 74.30  ? 192 HOH B O   1 
HETATM 23357 O O   . HOH TA 5 .   ? -36.553 -63.091  -8.043  1.00 64.73  ? 193 HOH B O   1 
HETATM 23358 O O   . HOH TA 5 .   ? -50.016 -92.276  20.882  1.00 79.37  ? 211 HOH B O   1 
HETATM 23359 O O   . HOH TA 5 .   ? -48.448 -79.348  2.742   1.00 71.86  ? 212 HOH B O   1 
HETATM 23360 O O   . HOH TA 5 .   ? -49.586 -83.667  24.839  1.00 70.37  ? 238 HOH B O   1 
HETATM 23361 O O   . HOH TA 5 .   ? -17.372 -40.996  -37.963 1.00 56.71  ? 299 HOH B O   1 
HETATM 23362 O O   . HOH TA 5 .   ? -52.484 -82.011  23.972  1.00 77.17  ? 307 HOH B O   1 
HETATM 23363 O O   . HOH UA 5 .   ? -32.673 -27.084  -32.626 1.00 52.18  ? 334 HOH C O   1 
HETATM 23364 O O   . HOH UA 5 .   ? -28.882 -35.589  -48.126 1.00 57.16  ? 335 HOH C O   1 
HETATM 23365 O O   . HOH UA 5 .   ? -25.787 -36.260  -57.035 1.00 39.36  ? 336 HOH C O   1 
HETATM 23366 O O   . HOH UA 5 .   ? -15.175 -31.447  -51.789 1.00 43.36  ? 337 HOH C O   1 
HETATM 23367 O O   . HOH UA 5 .   ? -20.222 -20.076  -54.395 1.00 35.39  ? 338 HOH C O   1 
HETATM 23368 O O   . HOH UA 5 .   ? -40.029 -37.228  -26.157 1.00 52.92  ? 339 HOH C O   1 
HETATM 23369 O O   . HOH UA 5 .   ? -20.693 -18.962  -40.143 1.00 66.06  ? 340 HOH C O   1 
HETATM 23370 O O   . HOH UA 5 .   ? -22.061 -9.326   -54.234 1.00 69.04  ? 341 HOH C O   1 
HETATM 23371 O O   . HOH UA 5 .   ? -62.479 -58.413  -3.557  1.00 73.17  ? 342 HOH C O   1 
HETATM 23372 O O   . HOH UA 5 .   ? -16.565 -7.668   -64.366 1.00 51.40  ? 343 HOH C O   1 
HETATM 23373 O O   . HOH UA 5 .   ? -62.588 -56.921  -8.813  1.00 52.48  ? 344 HOH C O   1 
HETATM 23374 O O   . HOH UA 5 .   ? -52.073 -55.701  -22.999 1.00 67.39  ? 345 HOH C O   1 
HETATM 23375 O O   . HOH UA 5 .   ? -20.376 -19.455  -67.487 1.00 92.75  ? 346 HOH C O   1 
HETATM 23376 O O   . HOH UA 5 .   ? -9.831  -4.112   -67.797 1.00 55.84  ? 347 HOH C O   1 
HETATM 23377 O O   . HOH UA 5 .   ? -50.196 -32.788  -39.368 1.00 43.90  ? 348 HOH C O   1 
HETATM 23378 O O   . HOH UA 5 .   ? -17.195 -27.477  -40.739 1.00 33.80  ? 349 HOH C O   1 
HETATM 23379 O O   . HOH UA 5 .   ? -20.488 -13.422  -82.049 1.00 54.11  ? 350 HOH C O   1 
HETATM 23380 O O   . HOH UA 5 .   ? -46.233 -36.366  -28.486 1.00 68.78  ? 351 HOH C O   1 
HETATM 23381 O O   . HOH UA 5 .   ? -27.382 -10.405  -69.096 1.00 59.65  ? 352 HOH C O   1 
HETATM 23382 O O   . HOH UA 5 .   ? -5.305  -33.175  -54.768 1.00 47.92  ? 353 HOH C O   1 
HETATM 23383 O O   . HOH UA 5 .   ? -11.973 -22.096  -64.557 1.00 60.49  ? 354 HOH C O   1 
HETATM 23384 O O   . HOH UA 5 .   ? -26.811 -21.825  -75.483 1.00 45.32  ? 355 HOH C O   1 
HETATM 23385 O O   . HOH UA 5 .   ? -61.643 -61.646  -31.474 1.00 66.58  ? 356 HOH C O   1 
HETATM 23386 O O   . HOH UA 5 .   ? -62.256 -56.383  -5.333  1.00 64.23  ? 357 HOH C O   1 
HETATM 23387 O O   . HOH UA 5 .   ? -21.909 -40.920  -50.680 1.00 65.00  ? 358 HOH C O   1 
HETATM 23388 O O   . HOH UA 5 .   ? -14.819 -25.145  -51.138 1.00 94.83  ? 359 HOH C O   1 
HETATM 23389 O O   . HOH UA 5 .   ? -28.061 -18.668  -51.264 1.00 54.72  ? 360 HOH C O   1 
HETATM 23390 O O   . HOH UA 5 .   ? -15.419 -25.162  -39.903 1.00 48.66  ? 361 HOH C O   1 
HETATM 23391 O O   . HOH UA 5 .   ? -47.314 -28.013  -57.155 1.00 64.62  ? 362 HOH C O   1 
HETATM 23392 O O   . HOH UA 5 .   ? -54.785 -55.405  -31.247 1.00 45.37  ? 363 HOH C O   1 
HETATM 23393 O O   . HOH UA 5 .   ? -39.825 -20.906  -27.927 1.00 82.41  ? 364 HOH C O   1 
HETATM 23394 O O   . HOH UA 5 .   ? -47.929 -33.520  -29.373 1.00 43.62  ? 365 HOH C O   1 
HETATM 23395 O O   . HOH UA 5 .   ? -65.896 -54.346  -12.218 1.00 86.93  ? 366 HOH C O   1 
HETATM 23396 O O   . HOH UA 5 .   ? -24.804 -5.252   -75.463 1.00 92.23  ? 367 HOH C O   1 
HETATM 23397 O O   . HOH UA 5 .   ? -10.262 -35.325  -58.765 1.00 47.72  ? 368 HOH C O   1 
HETATM 23398 O O   . HOH UA 5 .   ? -7.381  -18.190  -75.697 1.00 45.28  ? 369 HOH C O   1 
HETATM 23399 O O   . HOH UA 5 .   ? -24.365 -31.093  -41.143 1.00 62.39  ? 370 HOH C O   1 
HETATM 23400 O O   . HOH UA 5 .   ? -39.377 -13.512  -60.932 1.00 112.31 ? 371 HOH C O   1 
HETATM 23401 O O   . HOH VA 5 .   ? -68.413 -55.013  -5.748  1.00 37.19  ? 182 HOH D O   1 
HETATM 23402 O O   . HOH VA 5 .   ? -48.203 -54.991  -16.202 1.00 25.72  ? 183 HOH D O   1 
HETATM 23403 O O   . HOH VA 5 .   ? -40.916 -53.362  -1.089  1.00 55.34  ? 184 HOH D O   1 
HETATM 23404 O O   . HOH VA 5 .   ? -27.618 -40.331  -59.746 1.00 67.51  ? 185 HOH D O   1 
HETATM 23405 O O   . HOH VA 5 .   ? -45.242 -55.759  10.144  1.00 78.82  ? 186 HOH D O   1 
HETATM 23406 O O   . HOH VA 5 .   ? -61.553 -65.822  21.880  1.00 132.96 ? 187 HOH D O   1 
HETATM 23407 O O   . HOH VA 5 .   ? -34.109 -45.544  -58.703 1.00 37.56  ? 188 HOH D O   1 
HETATM 23408 O O   . HOH VA 5 .   ? -70.231 -48.458  12.184  1.00 39.56  ? 189 HOH D O   1 
HETATM 23409 O O   . HOH VA 5 .   ? -56.988 -58.357  9.528   1.00 83.04  ? 244 HOH D O   1 
HETATM 23410 O O   . HOH VA 5 .   ? -59.012 -70.152  11.681  1.00 103.92 ? 265 HOH D O   1 
HETATM 23411 O O   . HOH WA 5 .   ? -31.930 -74.879  -20.167 1.00 54.75  ? 334 HOH E O   1 
HETATM 23412 O O   . HOH WA 5 .   ? -30.506 -34.838  -64.463 1.00 50.75  ? 335 HOH E O   1 
HETATM 23413 O O   . HOH WA 5 .   ? -37.594 -76.478  -25.524 1.00 40.72  ? 336 HOH E O   1 
HETATM 23414 O O   . HOH WA 5 .   ? -31.526 -48.314  -91.807 1.00 92.87  ? 337 HOH E O   1 
HETATM 23415 O O   . HOH WA 5 .   ? -37.251 -49.685  -59.103 1.00 47.19  ? 338 HOH E O   1 
HETATM 23416 O O   . HOH WA 5 .   ? -47.246 -86.673  -15.921 1.00 59.36  ? 339 HOH E O   1 
HETATM 23417 O O   . HOH WA 5 .   ? -15.918 -52.622  -72.583 1.00 56.12  ? 340 HOH E O   1 
HETATM 23418 O O   . HOH WA 5 .   ? -41.705 -57.445  -79.417 1.00 90.43  ? 341 HOH E O   1 
HETATM 23419 O O   . HOH WA 5 .   ? -6.990  -45.056  -77.390 1.00 85.27  ? 342 HOH E O   1 
HETATM 23420 O O   . HOH WA 5 .   ? -37.489 -63.988  -75.056 1.00 120.44 ? 343 HOH E O   1 
HETATM 23421 O O   . HOH WA 5 .   ? -21.116 -52.768  -62.735 1.00 58.60  ? 344 HOH E O   1 
HETATM 23422 O O   . HOH WA 5 .   ? -26.962 -48.154  -54.847 1.00 39.77  ? 345 HOH E O   1 
HETATM 23423 O O   . HOH WA 5 .   ? -32.502 -40.927  -68.404 1.00 44.75  ? 346 HOH E O   1 
HETATM 23424 O O   . HOH WA 5 .   ? -30.304 -32.819  -67.029 1.00 74.20  ? 347 HOH E O   1 
HETATM 23425 O O   . HOH WA 5 .   ? -46.594 -51.047  -71.957 1.00 78.25  ? 348 HOH E O   1 
HETATM 23426 O O   . HOH WA 5 .   ? -45.278 -79.445  -15.405 1.00 56.22  ? 349 HOH E O   1 
HETATM 23427 O O   . HOH WA 5 .   ? -4.875  -58.565  -77.056 1.00 87.37  ? 350 HOH E O   1 
HETATM 23428 O O   . HOH WA 5 .   ? -20.178 -67.209  -64.004 1.00 97.47  ? 351 HOH E O   1 
HETATM 23429 O O   . HOH WA 5 .   ? -39.859 -54.869  -72.180 1.00 83.61  ? 352 HOH E O   1 
HETATM 23430 O O   . HOH WA 5 .   ? -52.690 -87.643  -11.394 1.00 87.34  ? 353 HOH E O   1 
HETATM 23431 O O   . HOH WA 5 .   ? -11.973 -73.448  -72.055 1.00 67.27  ? 354 HOH E O   1 
HETATM 23432 O O   . HOH WA 5 .   ? -39.187 -83.885  -15.123 1.00 69.36  ? 355 HOH E O   1 
HETATM 23433 O O   . HOH WA 5 .   ? -37.466 -76.249  -33.719 1.00 60.39  ? 356 HOH E O   1 
HETATM 23434 O O   . HOH WA 5 .   ? -24.624 -47.798  -67.699 1.00 39.86  ? 357 HOH E O   1 
HETATM 23435 O O   . HOH WA 5 .   ? -49.185 -44.700  -68.381 1.00 86.69  ? 358 HOH E O   1 
HETATM 23436 O O   . HOH WA 5 .   ? -30.416 -39.663  -88.006 1.00 69.14  ? 359 HOH E O   1 
HETATM 23437 O O   . HOH WA 5 .   ? -28.083 -44.801  -65.861 1.00 49.73  ? 360 HOH E O   1 
HETATM 23438 O O   . HOH WA 5 .   ? -46.239 -82.807  -29.564 1.00 47.09  ? 361 HOH E O   1 
HETATM 23439 O O   . HOH WA 5 .   ? -4.184  -60.510  -75.522 1.00 88.82  ? 362 HOH E O   1 
HETATM 23440 O O   . HOH WA 5 .   ? -33.183 -85.141  -25.178 1.00 70.51  ? 363 HOH E O   1 
HETATM 23441 O O   . HOH WA 5 .   ? -43.660 -48.610  -58.428 1.00 61.84  ? 364 HOH E O   1 
HETATM 23442 O O   . HOH XA 5 .   ? -43.914 -72.687  -22.992 1.00 36.84  ? 182 HOH F O   1 
HETATM 23443 O O   . HOH XA 5 .   ? -68.282 -87.948  -8.469  1.00 97.89  ? 183 HOH F O   1 
HETATM 23444 O O   . HOH XA 5 .   ? -62.233 -83.339  5.639   1.00 119.69 ? 184 HOH F O   1 
HETATM 23445 O O   . HOH XA 5 .   ? -27.906 -60.051  -47.644 1.00 50.78  ? 185 HOH F O   1 
HETATM 23446 O O   . HOH XA 5 .   ? -63.905 -77.820  -4.239  1.00 97.74  ? 186 HOH F O   1 
HETATM 23447 O O   . HOH XA 5 .   ? -59.752 -74.174  -1.857  1.00 55.56  ? 187 HOH F O   1 
HETATM 23448 O O   . HOH XA 5 .   ? -65.595 -74.695  2.115   1.00 86.70  ? 188 HOH F O   1 
HETATM 23449 O O   . HOH XA 5 .   ? -68.317 -90.203  11.486  1.00 59.24  ? 189 HOH F O   1 
HETATM 23450 O O   . HOH XA 5 .   ? -57.794 -76.164  -11.714 1.00 51.51  ? 190 HOH F O   1 
HETATM 23451 O O   . HOH XA 5 .   ? -45.973 -67.315  -19.522 1.00 50.21  ? 191 HOH F O   1 
HETATM 23452 O O   . HOH XA 5 .   ? -70.428 -88.861  12.529  1.00 44.76  ? 192 HOH F O   1 
HETATM 23453 O O   . HOH XA 5 .   ? -56.520 -96.308  -10.115 1.00 75.48  ? 193 HOH F O   1 
HETATM 23454 O O   . HOH XA 5 .   ? -66.601 -88.695  10.232  1.00 98.54  ? 284 HOH F O   1 
HETATM 23455 O O   . HOH YA 5 .   ? -30.149 -7.532   14.842  1.00 78.91  ? 334 HOH G O   1 
HETATM 23456 O O   . HOH YA 5 .   ? -8.539  28.982   -30.213 1.00 104.84 ? 335 HOH G O   1 
HETATM 23457 O O   . HOH YA 5 .   ? 13.437  37.067   -40.879 1.00 56.20  ? 336 HOH G O   1 
HETATM 23458 O O   . HOH YA 5 .   ? -35.534 -1.309   12.878  1.00 69.63  ? 337 HOH G O   1 
HETATM 23459 O O   . HOH YA 5 .   ? -31.125 -4.850   8.892   1.00 85.59  ? 338 HOH G O   1 
HETATM 23460 O O   . HOH YA 5 .   ? 6.485   11.679   -25.699 1.00 73.32  ? 339 HOH G O   1 
HETATM 23461 O O   . HOH YA 5 .   ? -35.931 -0.682   10.110  1.00 68.40  ? 340 HOH G O   1 
HETATM 23462 O O   . HOH YA 5 .   ? 0.709   35.184   -59.769 1.00 65.49  ? 341 HOH G O   1 
HETATM 23463 O O   . HOH YA 5 .   ? -19.245 -3.908   -0.615  1.00 57.98  ? 342 HOH G O   1 
HETATM 23464 O O   . HOH YA 5 .   ? -37.931 -1.669   13.023  1.00 67.02  ? 343 HOH G O   1 
HETATM 23465 O O   . HOH YA 5 .   ? -4.650  4.756    -16.783 1.00 49.94  ? 344 HOH G O   1 
HETATM 23466 O O   . HOH YA 5 .   ? -6.732  29.021   -15.342 1.00 97.83  ? 345 HOH G O   1 
HETATM 23467 O O   . HOH YA 5 .   ? 13.452  31.201   -41.848 1.00 61.08  ? 346 HOH G O   1 
HETATM 23468 O O   . HOH YA 5 .   ? 12.528  19.044   -37.059 1.00 95.49  ? 347 HOH G O   1 
HETATM 23469 O O   . HOH YA 5 .   ? -23.726 4.363    -11.414 1.00 67.76  ? 348 HOH G O   1 
HETATM 23470 O O   . HOH YA 5 .   ? 16.701  22.931   -21.623 1.00 74.90  ? 349 HOH G O   1 
HETATM 23471 O O   . HOH YA 5 .   ? 1.244   20.620   -20.178 1.00 98.43  ? 350 HOH G O   1 
HETATM 23472 O O   . HOH YA 5 .   ? -2.223  28.574   -12.626 1.00 90.77  ? 351 HOH G O   1 
HETATM 23473 O O   . HOH YA 5 .   ? -20.564 10.952   15.590  1.00 61.05  ? 352 HOH G O   1 
HETATM 23474 O O   . HOH YA 5 .   ? 1.862   14.250   -45.956 1.00 49.55  ? 353 HOH G O   1 
HETATM 23475 O O   . HOH YA 5 .   ? 5.590   22.097   -55.286 1.00 60.22  ? 354 HOH G O   1 
HETATM 23476 O O   . HOH YA 5 .   ? -5.381  26.710   -18.785 1.00 61.68  ? 355 HOH G O   1 
HETATM 23477 O O   . HOH YA 5 .   ? 12.012  23.171   -47.661 1.00 49.93  ? 356 HOH G O   1 
HETATM 23478 O O   . HOH YA 5 .   ? -21.321 13.637   -14.773 1.00 72.62  ? 357 HOH G O   1 
HETATM 23479 O O   . HOH YA 5 .   ? 15.929  9.364    -47.811 1.00 47.15  ? 358 HOH G O   1 
HETATM 23480 O O   . HOH YA 5 .   ? -2.438  29.226   -14.999 1.00 64.53  ? 359 HOH G O   1 
HETATM 23481 O O   . HOH YA 5 .   ? 18.900  11.841   -39.459 1.00 92.45  ? 360 HOH G O   1 
HETATM 23482 O O   . HOH YA 5 .   ? 28.725  14.655   -47.857 1.00 73.51  ? 361 HOH G O   1 
HETATM 23483 O O   . HOH YA 5 .   ? 12.058  13.314   -39.749 1.00 56.03  ? 362 HOH G O   1 
HETATM 23484 O O   . HOH YA 5 .   ? 3.344   12.441   -44.813 1.00 39.17  ? 363 HOH G O   1 
HETATM 23485 O O   . HOH YA 5 .   ? -19.004 14.354   -13.783 1.00 64.80  ? 364 HOH G O   1 
HETATM 23486 O O   . HOH YA 5 .   ? 4.512   15.528   -11.188 1.00 89.67  ? 365 HOH G O   1 
HETATM 23487 O O   . HOH YA 5 .   ? 16.953  35.222   -56.801 1.00 75.60  ? 366 HOH G O   1 
HETATM 23488 O O   . HOH YA 5 .   ? 3.952   37.291   -52.531 1.00 35.40  ? 367 HOH G O   1 
HETATM 23489 O O   . HOH YA 5 .   ? 8.735   38.170   -29.921 1.00 110.87 ? 368 HOH G O   1 
HETATM 23490 O O   . HOH YA 5 .   ? 9.679   38.835   -44.954 1.00 86.73  ? 369 HOH G O   1 
HETATM 23491 O O   . HOH YA 5 .   ? -30.628 1.266    13.990  1.00 96.15  ? 370 HOH G O   1 
HETATM 23492 O O   . HOH YA 5 .   ? 2.691   14.399   -9.765  1.00 86.84  ? 371 HOH G O   1 
HETATM 23493 O O   . HOH YA 5 .   ? 3.928   39.781   -46.978 1.00 76.67  ? 372 HOH G O   1 
HETATM 23494 O O   . HOH YA 5 .   ? 17.271  20.820   -32.928 1.00 67.61  ? 373 HOH G O   1 
HETATM 23495 O O   . HOH YA 5 .   ? 10.096  31.011   -20.475 1.00 146.77 ? 374 HOH G O   1 
HETATM 23496 O O   . HOH YA 5 .   ? 9.251   15.255   -20.072 1.00 61.72  ? 375 HOH G O   1 
HETATM 23497 O O   . HOH YA 5 .   ? -36.319 -3.478   14.345  1.00 97.51  ? 376 HOH G O   1 
HETATM 23498 O O   . HOH YA 5 .   ? -0.090  24.608   -6.534  1.00 75.50  ? 377 HOH G O   1 
HETATM 23499 O O   . HOH YA 5 .   ? 0.922   37.455   -35.904 1.00 69.22  ? 378 HOH G O   1 
HETATM 23500 O O   . HOH ZA 5 .   ? -14.903 -21.671  27.752  1.00 105.95 ? 182 HOH H O   1 
HETATM 23501 O O   . HOH ZA 5 .   ? -25.366 -13.279  27.975  1.00 67.98  ? 183 HOH H O   1 
HETATM 23502 O O   . HOH ZA 5 .   ? -34.916 -5.578   12.219  1.00 81.48  ? 184 HOH H O   1 
HETATM 23503 O O   . HOH ZA 5 .   ? -23.724 -19.619  35.727  1.00 139.77 ? 185 HOH H O   1 
HETATM 23504 O O   . HOH ZA 5 .   ? -25.501 -23.989  30.552  1.00 113.67 ? 186 HOH H O   1 
HETATM 23505 O O   . HOH ZA 5 .   ? -22.130 -0.415   -20.454 1.00 37.33  ? 187 HOH H O   1 
HETATM 23506 O O   . HOH ZA 5 .   ? -27.428 -28.758  14.934  1.00 107.04 ? 188 HOH H O   1 
HETATM 23507 O O   . HOH ZA 5 .   ? -21.344 -16.607  6.255   1.00 60.24  ? 189 HOH H O   1 
HETATM 23508 O O   . HOH ZA 5 .   ? -12.665 -16.607  8.487   1.00 65.34  ? 190 HOH H O   1 
HETATM 23509 O O   . HOH ZA 5 .   ? -4.490  8.724    -26.289 1.00 75.84  ? 191 HOH H O   1 
HETATM 23510 O O   . HOH ZA 5 .   ? -10.405 15.248   -37.478 1.00 57.88  ? 192 HOH H O   1 
HETATM 23511 O O   . HOH ZA 5 .   ? -27.260 -23.539  35.607  1.00 119.25 ? 193 HOH H O   1 
HETATM 23512 O O   . HOH ZA 5 .   ? -4.353  7.204    -18.569 1.00 51.18  ? 194 HOH H O   1 
HETATM 23513 O O   . HOH ZA 5 .   ? -40.736 -30.409  33.286  1.00 68.88  ? 195 HOH H O   1 
HETATM 23514 O O   . HOH ZA 5 .   ? -17.837 6.043    -30.939 1.00 71.75  ? 196 HOH H O   1 
HETATM 23515 O O   . HOH ZA 5 .   ? -23.199 -15.335  37.406  1.00 98.99  ? 197 HOH H O   1 
HETATM 23516 O O   . HOH ZA 5 .   ? -25.446 -22.330  7.858   1.00 61.34  ? 198 HOH H O   1 
HETATM 23517 O O   . HOH ZA 5 .   ? -40.403 -30.703  30.706  1.00 69.02  ? 208 HOH H O   1 
HETATM 23518 O O   . HOH ZA 5 .   ? -31.454 -33.947  31.939  1.00 69.13  ? 231 HOH H O   1 
HETATM 23519 O O   . HOH ZA 5 .   ? -27.791 -33.852  30.927  1.00 110.58 ? 233 HOH H O   1 
HETATM 23520 O O   . HOH ZA 5 .   ? -5.002  5.552    -22.796 1.00 50.76  ? 246 HOH H O   1 
HETATM 23521 O O   . HOH ZA 5 .   ? -39.311 -27.805  33.728  1.00 69.48  ? 256 HOH H O   1 
HETATM 23522 O O   . HOH ZA 5 .   ? -12.777 -23.250  27.427  1.00 94.69  ? 277 HOH H O   1 
HETATM 23523 O O   . HOH AB 5 .   ? -30.600 -27.727  -7.452  1.00 50.84  ? 334 HOH I O   1 
HETATM 23524 O O   . HOH AB 5 .   ? -2.341  14.366   -53.490 1.00 49.34  ? 335 HOH I O   1 
HETATM 23525 O O   . HOH AB 5 .   ? 2.458   25.069   -76.222 1.00 38.60  ? 336 HOH I O   1 
HETATM 23526 O O   . HOH AB 5 .   ? -1.539  13.818   -55.932 1.00 58.08  ? 337 HOH I O   1 
HETATM 23527 O O   . HOH AB 5 .   ? -31.063 7.887    -38.227 1.00 120.72 ? 338 HOH I O   1 
HETATM 23528 O O   . HOH AB 5 .   ? -20.434 29.792   -69.158 1.00 100.10 ? 339 HOH I O   1 
HETATM 23529 O O   . HOH AB 5 .   ? -19.200 27.751   -71.590 1.00 100.87 ? 340 HOH I O   1 
HETATM 23530 O O   . HOH AB 5 .   ? -9.161  11.259   -42.062 1.00 61.67  ? 341 HOH I O   1 
HETATM 23531 O O   . HOH AB 5 .   ? -38.710 -29.977  -9.394  1.00 65.79  ? 342 HOH I O   1 
HETATM 23532 O O   . HOH AB 5 .   ? -10.881 20.350   -68.753 1.00 54.79  ? 343 HOH I O   1 
HETATM 23533 O O   . HOH AB 5 .   ? -22.331 -20.558  -27.151 1.00 66.36  ? 344 HOH I O   1 
HETATM 23534 O O   . HOH AB 5 .   ? -22.969 -0.888   -62.056 1.00 115.71 ? 345 HOH I O   1 
HETATM 23535 O O   . HOH AB 5 .   ? -23.918 -25.335  -25.112 1.00 76.43  ? 346 HOH I O   1 
HETATM 23536 O O   . HOH AB 5 .   ? -48.691 -29.825  -18.866 1.00 76.74  ? 347 HOH I O   1 
HETATM 23537 O O   . HOH AB 5 .   ? -13.131 16.828   -41.002 1.00 77.94  ? 348 HOH I O   1 
HETATM 23538 O O   . HOH AB 5 .   ? -19.665 -25.439  -16.001 1.00 99.96  ? 349 HOH I O   1 
HETATM 23539 O O   . HOH AB 5 .   ? -33.696 -8.285   -32.877 1.00 65.21  ? 350 HOH I O   1 
HETATM 23540 O O   . HOH AB 5 .   ? -20.847 20.632   -41.315 1.00 53.46  ? 351 HOH I O   1 
HETATM 23541 O O   . HOH AB 5 .   ? -31.311 -2.734   -28.948 1.00 43.41  ? 352 HOH I O   1 
HETATM 23542 O O   . HOH AB 5 .   ? -21.557 9.615    -52.988 1.00 103.74 ? 353 HOH I O   1 
HETATM 23543 O O   . HOH AB 5 .   ? -54.613 -36.645  10.274  1.00 81.41  ? 354 HOH I O   1 
HETATM 23544 O O   . HOH AB 5 .   ? -25.193 -2.764   -74.861 1.00 65.10  ? 356 HOH I O   1 
HETATM 23545 O O   . HOH AB 5 .   ? -14.767 37.886   -72.761 1.00 68.13  ? 357 HOH I O   1 
HETATM 23546 O O   . HOH AB 5 .   ? -38.791 -17.582  -16.284 1.00 58.16  ? 358 HOH I O   1 
HETATM 23547 O O   . HOH AB 5 .   ? -29.528 10.847   -58.136 1.00 116.85 ? 359 HOH I O   1 
HETATM 23548 O O   . HOH AB 5 .   ? -21.453 -25.941  -25.949 1.00 66.36  ? 360 HOH I O   1 
HETATM 23549 O O   . HOH AB 5 .   ? -22.472 19.906   -61.780 1.00 75.77  ? 361 HOH I O   1 
HETATM 23550 O O   . HOH AB 5 .   ? -14.139 37.869   -75.328 1.00 69.68  ? 362 HOH I O   1 
HETATM 23551 O O   . HOH AB 5 .   ? -4.534  29.024   -49.889 1.00 91.08  ? 363 HOH I O   1 
HETATM 23552 O O   . HOH AB 5 .   ? -52.899 -43.748  9.217   1.00 54.96  ? 364 HOH I O   1 
HETATM 23553 O O   . HOH AB 5 .   ? 2.926   11.162   -60.772 1.00 73.95  ? 365 HOH I O   1 
HETATM 23554 O O   . HOH AB 5 .   ? -37.624 -13.833  -30.194 1.00 32.84  ? 366 HOH I O   1 
HETATM 23555 O O   . HOH AB 5 .   ? 4.701   15.458   -80.099 1.00 73.13  ? 367 HOH I O   1 
HETATM 23556 O O   . HOH AB 5 .   ? -39.210 -21.116  -19.848 1.00 70.33  ? 368 HOH I O   1 
HETATM 23557 O O   . HOH AB 5 .   ? -12.713 25.074   -45.767 1.00 91.90  ? 369 HOH I O   1 
HETATM 23558 O O   . HOH AB 5 .   ? -11.253 25.651   -72.874 1.00 84.80  ? 370 HOH I O   1 
HETATM 23559 O O   . HOH AB 5 .   ? -26.721 -21.560  -20.417 1.00 48.09  ? 371 HOH I O   1 
HETATM 23560 O O   . HOH BB 5 .   ? -23.385 -20.139  -21.157 1.00 38.14  ? 182 HOH J O   1 
HETATM 23561 O O   . HOH BB 5 .   ? -43.540 -25.071  18.358  1.00 98.97  ? 183 HOH J O   1 
HETATM 23562 O O   . HOH BB 5 .   ? -29.756 -4.738   -22.193 1.00 53.48  ? 184 HOH J O   1 
HETATM 23563 O O   . HOH BB 5 .   ? -10.237 -9.509   -25.729 1.00 34.92  ? 185 HOH J O   1 
HETATM 23564 O O   . HOH BB 5 .   ? -12.460 -2.502   -42.934 1.00 36.00  ? 186 HOH J O   1 
HETATM 23565 O O   . HOH BB 5 .   ? -24.073 0.641    -29.644 1.00 69.42  ? 187 HOH J O   1 
HETATM 23566 O O   . HOH BB 5 .   ? -48.447 -46.113  22.252  1.00 51.55  ? 188 HOH J O   1 
HETATM 23567 O O   . HOH BB 5 .   ? -11.164 -3.694   -40.844 1.00 25.91  ? 189 HOH J O   1 
HETATM 23568 O O   . HOH BB 5 .   ? -1.052  -5.144   -32.522 1.00 62.71  ? 190 HOH J O   1 
HETATM 23569 O O   . HOH BB 5 .   ? -53.364 -15.306  5.932   1.00 62.63  ? 199 HOH J O   1 
HETATM 23570 O O   . HOH BB 5 .   ? -23.338 7.323    -27.851 1.00 63.27  ? 205 HOH J O   1 
HETATM 23571 O O   . HOH BB 5 .   ? -51.896 -21.081  5.977   1.00 127.18 ? 210 HOH J O   1 
HETATM 23572 O O   . HOH BB 5 .   ? -58.197 -37.163  0.698   1.00 111.63 ? 234 HOH J O   1 
HETATM 23573 O O   . HOH BB 5 .   ? -44.323 -23.586  16.587  1.00 99.09  ? 248 HOH J O   1 
HETATM 23574 O O   . HOH BB 5 .   ? -31.251 -21.649  3.705   1.00 58.83  ? 252 HOH J O   1 
HETATM 23575 O O   . HOH BB 5 .   ? -27.332 -5.457   -19.529 1.00 65.52  ? 257 HOH J O   1 
HETATM 23576 O O   . HOH BB 5 .   ? -52.414 -36.828  13.946  1.00 101.82 ? 260 HOH J O   1 
HETATM 23577 O O   . HOH BB 5 .   ? -1.202  -2.870   -38.922 1.00 94.61  ? 295 HOH J O   1 
HETATM 23578 O O   . HOH BB 5 .   ? -54.208 -35.688  20.974  1.00 75.75  ? 313 HOH J O   1 
HETATM 23579 O O   . HOH BB 5 .   ? -20.468 1.024    -39.969 1.00 35.75  ? 318 HOH J O   1 
HETATM 23580 O O   . HOH BB 5 .   ? -22.181 -0.934   -30.018 1.00 61.85  ? 319 HOH J O   1 
HETATM 23581 O O   . HOH CB 5 .   ? 18.259  8.037    -47.746 1.00 49.34  ? 334 HOH K O   1 
HETATM 23582 O O   . HOH CB 5 .   ? 25.465  9.776    -58.339 1.00 34.22  ? 335 HOH K O   1 
HETATM 23583 O O   . HOH CB 5 .   ? -7.684  -18.345  9.121   1.00 58.85  ? 336 HOH K O   1 
HETATM 23584 O O   . HOH CB 5 .   ? -4.225  -8.912   -23.547 1.00 27.44  ? 337 HOH K O   1 
HETATM 23585 O O   . HOH CB 5 .   ? 14.011  -12.362  -53.392 1.00 44.12  ? 338 HOH K O   1 
HETATM 23586 O O   . HOH CB 5 .   ? 3.505   -26.475  -22.541 1.00 46.67  ? 339 HOH K O   1 
HETATM 23587 O O   . HOH CB 5 .   ? 25.153  -5.912   -50.479 1.00 54.42  ? 340 HOH K O   1 
HETATM 23588 O O   . HOH CB 5 .   ? 23.408  0.224    -45.340 1.00 81.79  ? 341 HOH K O   1 
HETATM 23589 O O   . HOH CB 5 .   ? 1.969   -13.561  -4.551  1.00 76.63  ? 342 HOH K O   1 
HETATM 23590 O O   . HOH CB 5 .   ? 7.900   -1.578   -57.956 1.00 71.69  ? 343 HOH K O   1 
HETATM 23591 O O   . HOH CB 5 .   ? -1.203  -16.205  -2.412  1.00 67.11  ? 344 HOH K O   1 
HETATM 23592 O O   . HOH CB 5 .   ? 23.403  -2.220   -66.121 1.00 75.56  ? 345 HOH K O   1 
HETATM 23593 O O   . HOH CB 5 .   ? -5.481  4.904    -61.571 1.00 44.11  ? 346 HOH K O   1 
HETATM 23594 O O   . HOH CB 5 .   ? -2.802  -10.981  -25.333 1.00 42.03  ? 347 HOH K O   1 
HETATM 23595 O O   . HOH CB 5 .   ? 22.308  -6.239   -59.892 1.00 80.78  ? 348 HOH K O   1 
HETATM 23596 O O   . HOH CB 5 .   ? 23.197  -4.095   -47.042 1.00 60.96  ? 350 HOH K O   1 
HETATM 23597 O O   . HOH CB 5 .   ? 19.846  17.373   -65.870 1.00 63.63  ? 351 HOH K O   1 
HETATM 23598 O O   . HOH CB 5 .   ? 3.168   -27.782  -2.841  1.00 76.92  ? 352 HOH K O   1 
HETATM 23599 O O   . HOH CB 5 .   ? -14.753 -35.854  4.947   1.00 57.71  ? 353 HOH K O   1 
HETATM 23600 O O   . HOH CB 5 .   ? 27.654  5.764    -44.703 1.00 65.25  ? 354 HOH K O   1 
HETATM 23601 O O   . HOH CB 5 .   ? 19.491  -3.921   -49.527 1.00 45.18  ? 355 HOH K O   1 
HETATM 23602 O O   . HOH CB 5 .   ? 13.451  -19.704  -43.001 1.00 45.26  ? 356 HOH K O   1 
HETATM 23603 O O   . HOH CB 5 .   ? 7.512   17.565   -70.793 1.00 44.01  ? 357 HOH K O   1 
HETATM 23604 O O   . HOH CB 5 .   ? -1.501  -10.724  -38.773 1.00 88.22  ? 358 HOH K O   1 
HETATM 23605 O O   . HOH CB 5 .   ? 4.629   12.376   -73.757 1.00 46.54  ? 359 HOH K O   1 
HETATM 23606 O O   . HOH CB 5 .   ? 6.349   -24.764  -24.976 1.00 76.45  ? 360 HOH K O   1 
HETATM 23607 O O   . HOH CB 5 .   ? 8.935   15.278   -69.435 1.00 53.36  ? 361 HOH K O   1 
HETATM 23608 O O   . HOH CB 5 .   ? 1.259   -13.095  -21.470 1.00 53.00  ? 362 HOH K O   1 
HETATM 23609 O O   . HOH CB 5 .   ? 12.570  13.940   -71.391 1.00 57.63  ? 363 HOH K O   1 
HETATM 23610 O O   . HOH CB 5 .   ? -3.525  -4.546   -61.283 1.00 49.03  ? 364 HOH K O   1 
HETATM 23611 O O   . HOH CB 5 .   ? 7.336   11.519   -74.731 1.00 62.03  ? 365 HOH K O   1 
HETATM 23612 O O   . HOH CB 5 .   ? 10.293  11.894   -58.934 1.00 71.87  ? 366 HOH K O   1 
HETATM 23613 O O   . HOH CB 5 .   ? 1.832   -23.973  2.318   1.00 63.25  ? 367 HOH K O   1 
HETATM 23614 O O   . HOH CB 5 .   ? 2.366   3.874    -45.404 1.00 43.73  ? 368 HOH K O   1 
HETATM 23615 O O   . HOH CB 5 .   ? -17.806 -46.999  25.304  1.00 84.53  ? 369 HOH K O   1 
HETATM 23616 O O   . HOH DB 5 .   ? -11.653 -22.406  -7.706  1.00 50.58  ? 182 HOH L O   1 
HETATM 23617 O O   . HOH DB 5 .   ? -28.233 -31.032  15.064  1.00 106.70 ? 183 HOH L O   1 
HETATM 23618 O O   . HOH DB 5 .   ? -27.849 -29.903  4.555   1.00 46.69  ? 184 HOH L O   1 
HETATM 23619 O O   . HOH DB 5 .   ? -5.248  -39.180  9.740   1.00 71.14  ? 203 HOH L O   1 
HETATM 23620 O O   . HOH DB 5 .   ? 3.912   -3.121   -32.504 1.00 48.35  ? 219 HOH L O   1 
HETATM 23621 O O   . HOH DB 5 .   ? -32.070 -51.463  21.300  1.00 44.64  ? 227 HOH L O   1 
HETATM 23622 O O   . HOH DB 5 .   ? -28.710 -46.340  26.644  1.00 72.01  ? 235 HOH L O   1 
HETATM 23623 O O   . HOH DB 5 .   ? -29.117 -40.396  16.591  1.00 127.20 ? 247 HOH L O   1 
HETATM 23624 O O   . HOH DB 5 .   ? -27.736 -48.553  12.953  1.00 110.96 ? 262 HOH L O   1 
HETATM 23625 O O   . HOH DB 5 .   ? -18.872 -49.304  24.614  1.00 91.92  ? 276 HOH L O   1 
HETATM 23626 O O   . HOH DB 5 .   ? -4.164  1.671    -19.151 1.00 37.22  ? 279 HOH L O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . ASP A  7   ? 1.5725 1.5583 1.4041 -0.1052 -0.0955 0.1583  7   ASP A N   
2     C CA  . ASP A  7   ? 1.7188 1.7038 1.5652 -0.1006 -0.0921 0.1591  7   ASP A CA  
3     C C   . ASP A  7   ? 1.5609 1.5445 1.4079 -0.0991 -0.0886 0.1482  7   ASP A C   
4     O O   . ASP A  7   ? 1.7371 1.7172 1.5792 -0.0997 -0.0836 0.1407  7   ASP A O   
5     C CB  . ASP A  7   ? 1.7560 1.7367 1.6109 -0.0983 -0.0860 0.1638  7   ASP A CB  
6     C CG  . ASP A  7   ? 1.7898 1.7729 1.6511 -0.0977 -0.0894 0.1764  7   ASP A CG  
7     O OD1 . ASP A  7   ? 1.7630 1.7504 1.6174 -0.1006 -0.0964 0.1812  7   ASP A OD1 
8     O OD2 . ASP A  7   ? 1.8944 1.8750 1.7674 -0.0946 -0.0851 0.1816  7   ASP A OD2 
9     N N   . THR A  8   ? 1.6959 1.6826 1.5491 -0.0971 -0.0913 0.1476  8   THR A N   
10    C CA  . THR A  8   ? 1.7254 1.7115 1.5791 -0.0957 -0.0888 0.1378  8   THR A CA  
11    C C   . THR A  8   ? 1.5375 1.5233 1.4054 -0.0914 -0.0860 0.1383  8   THR A C   
12    O O   . THR A  8   ? 1.4537 1.4417 1.3306 -0.0897 -0.0886 0.1462  8   THR A O   
13    C CB  . THR A  8   ? 1.5605 1.5504 1.4051 -0.0981 -0.0945 0.1336  8   THR A CB  
14    O OG1 . THR A  8   ? 1.4653 1.4591 1.3176 -0.0964 -0.0989 0.1376  8   THR A OG1 
15    C CG2 . THR A  8   ? 1.6157 1.6070 1.4480 -0.1026 -0.0991 0.1365  8   THR A CG2 
16    N N   . LEU A  9   ? 1.4899 1.4730 1.3599 -0.0898 -0.0805 0.1299  9   LEU A N   
17    C CA  . LEU A  9   ? 1.5721 1.5545 1.4545 -0.0859 -0.0772 0.1290  9   LEU A CA  
18    C C   . LEU A  9   ? 1.1056 1.0886 0.9853 -0.0854 -0.0762 0.1191  9   LEU A C   
19    O O   . LEU A  9   ? 1.2992 1.2795 1.1760 -0.0856 -0.0711 0.1116  9   LEU A O   
20    C CB  . LEU A  9   ? 1.7681 1.7457 1.6590 -0.0839 -0.0699 0.1303  9   LEU A CB  
21    C CG  . LEU A  9   ? 1.3442 1.3205 1.2478 -0.0801 -0.0657 0.1289  9   LEU A CG  
22    C CD1 . LEU A  9   ? 1.2231 1.2027 1.1363 -0.0780 -0.0699 0.1370  9   LEU A CD1 
23    C CD2 . LEU A  9   ? 1.6457 1.6169 1.5560 -0.0788 -0.0579 0.1291  9   LEU A CD2 
24    N N   . CYS A  10  ? 1.3863 1.3732 1.2671 -0.0849 -0.0811 0.1192  10  CYS A N   
25    C CA  . CYS A  10  ? 1.4501 1.4379 1.3277 -0.0845 -0.0806 0.1101  10  CYS A CA  
26    C C   . CYS A  10  ? 1.3300 1.3180 1.2196 -0.0808 -0.0786 0.1097  10  CYS A C   
27    O O   . CYS A  10  ? 1.2524 1.2391 1.1528 -0.0785 -0.0763 0.1154  10  CYS A O   
28    C CB  . CYS A  10  ? 1.4399 1.4317 1.3086 -0.0870 -0.0873 0.1092  10  CYS A CB  
29    S SG  . CYS A  10  ? 1.7825 1.7750 1.6385 -0.0916 -0.0916 0.1130  10  CYS A SG  
30    N N   . ILE A  11  ? 1.4412 1.4308 1.3291 -0.0802 -0.0791 0.1028  11  ILE A N   
31    C CA  . ILE A  11  ? 1.4144 1.4041 1.3125 -0.0769 -0.0769 0.1013  11  ILE A CA  
32    C C   . ILE A  11  ? 1.2549 1.2479 1.1495 -0.0769 -0.0807 0.0967  11  ILE A C   
33    O O   . ILE A  11  ? 1.3111 1.3052 1.1953 -0.0792 -0.0823 0.0914  11  ILE A O   
34    C CB  . ILE A  11  ? 1.2327 1.2186 1.1341 -0.0755 -0.0692 0.0951  11  ILE A CB  
35    C CG1 . ILE A  11  ? 1.3100 1.2950 1.2241 -0.0720 -0.0659 0.0960  11  ILE A CG1 
36    C CG2 . ILE A  11  ? 1.1770 1.1635 1.0694 -0.0768 -0.0681 0.0853  11  ILE A CG2 
37    C CD1 . ILE A  11  ? 1.2165 1.1982 1.1413 -0.0703 -0.0617 0.1027  11  ILE A CD1 
38    N N   . GLY A  12  ? 1.5496 1.5441 1.4531 -0.0744 -0.0817 0.0987  12  GLY A N   
39    C CA  . GLY A  12  ? 1.4919 1.4895 1.3933 -0.0741 -0.0850 0.0948  12  GLY A CA  
40    C C   . GLY A  12  ? 1.4629 1.4610 1.3759 -0.0708 -0.0841 0.0963  12  GLY A C   
41    O O   . GLY A  12  ? 1.3858 1.3814 1.3079 -0.0686 -0.0794 0.0981  12  GLY A O   
42    N N   . TYR A  13  ? 1.1218 1.1232 1.0347 -0.0705 -0.0883 0.0955  13  TYR A N   
43    C CA  . TYR A  13  ? 1.0274 1.0293 0.9506 -0.0673 -0.0873 0.0960  13  TYR A CA  
44    C C   . TYR A  13  ? 0.9672 0.9726 0.8956 -0.0669 -0.0931 0.1029  13  TYR A C   
45    O O   . TYR A  13  ? 1.1424 1.1493 1.0700 -0.0685 -0.0970 0.1098  13  TYR A O   
46    C CB  . TYR A  13  ? 0.8871 0.8892 0.8073 -0.0665 -0.0854 0.0871  13  TYR A CB  
47    C CG  . TYR A  13  ? 0.9214 0.9246 0.8289 -0.0691 -0.0871 0.0812  13  TYR A CG  
48    C CD1 . TYR A  13  ? 0.8647 0.8709 0.7672 -0.0701 -0.0919 0.0795  13  TYR A CD1 
49    C CD2 . TYR A  13  ? 0.7271 0.7280 0.6278 -0.0707 -0.0837 0.0771  13  TYR A CD2 
50    C CE1 . TYR A  13  ? 0.7536 0.7605 0.6450 -0.0725 -0.0931 0.0741  13  TYR A CE1 
51    C CE2 . TYR A  13  ? 0.7873 0.7891 0.6770 -0.0730 -0.0850 0.0717  13  TYR A CE2 
52    C CZ  . TYR A  13  ? 0.8435 0.8482 0.7286 -0.0738 -0.0896 0.0702  13  TYR A CZ  
53    O OH  . TYR A  13  ? 0.9186 0.9239 0.7930 -0.0761 -0.0906 0.0649  13  TYR A OH  
54    N N   . HIS A  14  ? 1.0934 1.1002 1.0270 -0.0649 -0.0935 0.1010  14  HIS A N   
55    C CA  . HIS A  14  ? 0.8841 0.8938 0.8255 -0.0638 -0.0978 0.1075  14  HIS A CA  
56    C C   . HIS A  14  ? 1.1298 1.1428 1.0662 -0.0647 -0.1024 0.1043  14  HIS A C   
57    O O   . HIS A  14  ? 1.3564 1.3688 1.2872 -0.0647 -0.1007 0.0965  14  HIS A O   
58    C CB  . HIS A  14  ? 1.1020 1.1097 1.0564 -0.0601 -0.0932 0.1087  14  HIS A CB  
59    C CG  . HIS A  14  ? 1.1921 1.2023 1.1567 -0.0586 -0.0965 0.1164  14  HIS A CG  
60    N ND1 . HIS A  14  ? 1.3418 1.3530 1.3115 -0.0589 -0.0988 0.1255  14  HIS A ND1 
61    C CD2 . HIS A  14  ? 1.3114 1.3234 1.2829 -0.0567 -0.0977 0.1167  14  HIS A CD2 
62    C CE1 . HIS A  14  ? 1.4408 1.4545 1.4200 -0.0573 -0.1014 0.1311  14  HIS A CE1 
63    N NE2 . HIS A  14  ? 1.2905 1.3047 1.2710 -0.0559 -0.1008 0.1258  14  HIS A NE2 
64    N N   . ALA A  15  ? 0.8671 0.8838 0.8057 -0.0656 -0.1083 0.1103  15  ALA A N   
65    C CA  . ALA A  15  ? 1.0749 1.0947 1.0097 -0.0665 -0.1128 0.1078  15  ALA A CA  
66    C C   . ALA A  15  ? 1.0499 1.0733 0.9927 -0.0661 -0.1177 0.1156  15  ALA A C   
67    O O   . ALA A  15  ? 1.0739 1.0977 1.0232 -0.0657 -0.1184 0.1233  15  ALA A O   
68    C CB  . ALA A  15  ? 0.9890 1.0099 0.9101 -0.0703 -0.1161 0.1045  15  ALA A CB  
69    N N   . ASN A  16  ? 1.1055 1.1316 1.0479 -0.0663 -0.1210 0.1137  16  ASN A N   
70    C CA  . ASN A  16  ? 1.2103 1.2399 1.1614 -0.0656 -0.1253 0.1205  16  ASN A CA  
71    C C   . ASN A  16  ? 1.2715 1.3044 1.2188 -0.0670 -0.1299 0.1179  16  ASN A C   
72    O O   . ASN A  16  ? 1.3148 1.3473 1.2514 -0.0690 -0.1304 0.1114  16  ASN A O   
73    C CB  . ASN A  16  ? 1.2397 1.2677 1.2048 -0.0614 -0.1210 0.1228  16  ASN A CB  
74    C CG  . ASN A  16  ? 1.2779 1.3031 1.2436 -0.0590 -0.1158 0.1147  16  ASN A CG  
75    O OD1 . ASN A  16  ? 1.1979 1.2231 1.1549 -0.0601 -0.1162 0.1078  16  ASN A OD1 
76    N ND2 . ASN A  16  ? 1.2170 1.2396 1.1932 -0.0556 -0.1107 0.1155  16  ASN A ND2 
77    N N   . ASN A  17  ? 1.2352 1.2712 1.1915 -0.0659 -0.1330 0.1230  17  ASN A N   
78    C CA  . ASN A  17  ? 1.3463 1.3853 1.3004 -0.0671 -0.1373 0.1211  17  ASN A CA  
79    C C   . ASN A  17  ? 1.4789 1.5161 1.4369 -0.0640 -0.1334 0.1149  17  ASN A C   
80    O O   . ASN A  17  ? 1.6310 1.6705 1.5917 -0.0637 -0.1359 0.1145  17  ASN A O   
81    C CB  . ASN A  17  ? 1.5898 1.6335 1.5519 -0.0676 -0.1427 0.1298  17  ASN A CB  
82    C CG  . ASN A  17  ? 1.6229 1.6660 1.6002 -0.0635 -0.1399 0.1349  17  ASN A CG  
83    O OD1 . ASN A  17  ? 1.6539 1.6935 1.6360 -0.0603 -0.1342 0.1308  17  ASN A OD1 
84    N ND2 . ASN A  17  ? 1.7487 1.7954 1.7336 -0.0638 -0.1437 0.1440  17  ASN A ND2 
85    N N   . SER A  18  ? 1.3296 1.3627 1.2879 -0.0618 -0.1271 0.1101  18  SER A N   
86    C CA  . SER A  18  ? 1.2673 1.2985 1.2294 -0.0587 -0.1230 0.1045  18  SER A CA  
87    C C   . SER A  18  ? 1.2275 1.2591 1.1799 -0.0601 -0.1239 0.0970  18  SER A C   
88    O O   . SER A  18  ? 1.0816 1.1131 1.0230 -0.0629 -0.1250 0.0939  18  SER A O   
89    C CB  . SER A  18  ? 1.1892 1.2162 1.1542 -0.0563 -0.1160 0.1015  18  SER A CB  
90    O OG  . SER A  18  ? 1.0926 1.1182 1.0617 -0.0535 -0.1122 0.0965  18  SER A OG  
91    N N   . THR A  19  ? 1.2420 1.2740 1.1987 -0.0581 -0.1232 0.0943  19  THR A N   
92    C CA  . THR A  19  ? 1.2668 1.2997 1.2159 -0.0592 -0.1246 0.0883  19  THR A CA  
93    C C   . THR A  19  ? 1.1570 1.1875 1.1085 -0.0560 -0.1192 0.0822  19  THR A C   
94    O O   . THR A  19  ? 1.1921 1.2227 1.1384 -0.0561 -0.1189 0.0765  19  THR A O   
95    C CB  . THR A  19  ? 1.2627 1.2991 1.2145 -0.0603 -0.1300 0.0918  19  THR A CB  
96    O OG1 . THR A  19  ? 1.3449 1.3815 1.3084 -0.0570 -0.1285 0.0938  19  THR A OG1 
97    C CG2 . THR A  19  ? 1.3596 1.3988 1.3113 -0.0632 -0.1352 0.0993  19  THR A CG2 
98    N N   . ASP A  20  ? 1.0553 1.0837 1.0151 -0.0533 -0.1149 0.0837  20  ASP A N   
99    C CA  . ASP A  20  ? 1.0499 1.0758 1.0119 -0.0505 -0.1092 0.0781  20  ASP A CA  
100   C C   . ASP A  20  ? 1.0080 1.0328 0.9589 -0.0517 -0.1072 0.0708  20  ASP A C   
101   O O   . ASP A  20  ? 0.9961 1.0203 0.9402 -0.0538 -0.1074 0.0704  20  ASP A O   
102   C CB  . ASP A  20  ? 1.0424 1.0656 1.0125 -0.0484 -0.1045 0.0807  20  ASP A CB  
103   C CG  . ASP A  20  ? 1.0282 1.0523 1.0107 -0.0466 -0.1055 0.0876  20  ASP A CG  
104   O OD1 . ASP A  20  ? 1.0239 1.0458 1.0138 -0.0451 -0.1020 0.0908  20  ASP A OD1 
105   O OD2 . ASP A  20  ? 1.0771 1.1038 1.0620 -0.0468 -0.1096 0.0897  20  ASP A OD2 
106   N N   . THR A  21  ? 0.9516 0.9763 0.9010 -0.0502 -0.1054 0.0651  21  THR A N   
107   C CA  . THR A  21  ? 0.8925 0.9165 0.8327 -0.0508 -0.1031 0.0581  21  THR A CA  
108   C C   . THR A  21  ? 0.8331 0.8556 0.7769 -0.0480 -0.0976 0.0536  21  THR A C   
109   O O   . THR A  21  ? 0.9628 0.9854 0.9135 -0.0457 -0.0967 0.0540  21  THR A O   
110   C CB  . THR A  21  ? 0.9361 0.9620 0.8690 -0.0524 -0.1064 0.0550  21  THR A CB  
111   O OG1 . THR A  21  ? 1.2493 1.2765 1.1882 -0.0508 -0.1079 0.0561  21  THR A OG1 
112   C CG2 . THR A  21  ? 0.9076 0.9348 0.8343 -0.0560 -0.1112 0.0581  21  THR A CG2 
113   N N   . VAL A  22  ? 0.8384 0.8595 0.7772 -0.0483 -0.0940 0.0494  22  VAL A N   
114   C CA  . VAL A  22  ? 0.7591 0.7791 0.6997 -0.0461 -0.0888 0.0445  22  VAL A CA  
115   C C   . VAL A  22  ? 0.7221 0.7429 0.6533 -0.0470 -0.0878 0.0380  22  VAL A C   
116   O O   . VAL A  22  ? 0.7306 0.7522 0.6541 -0.0493 -0.0905 0.0374  22  VAL A O   
117   C CB  . VAL A  22  ? 0.6860 0.7035 0.6310 -0.0456 -0.0844 0.0455  22  VAL A CB  
118   C CG1 . VAL A  22  ? 0.6261 0.6428 0.5801 -0.0451 -0.0856 0.0528  22  VAL A CG1 
119   C CG2 . VAL A  22  ? 0.5473 0.5641 0.4845 -0.0478 -0.0835 0.0435  22  VAL A CG2 
120   N N   . ASP A  23  ? 0.7198 0.7406 0.6516 -0.0452 -0.0840 0.0332  23  ASP A N   
121   C CA  . ASP A  23  ? 0.6949 0.7167 0.6187 -0.0456 -0.0825 0.0272  23  ASP A CA  
122   C C   . ASP A  23  ? 0.6196 0.6403 0.5428 -0.0456 -0.0777 0.0241  23  ASP A C   
123   O O   . ASP A  23  ? 0.6116 0.6307 0.5414 -0.0444 -0.0747 0.0254  23  ASP A O   
124   C CB  . ASP A  23  ? 0.7997 0.8232 0.7239 -0.0437 -0.0823 0.0239  23  ASP A CB  
125   C CG  . ASP A  23  ? 0.9337 0.9585 0.8565 -0.0442 -0.0868 0.0256  23  ASP A CG  
126   O OD1 . ASP A  23  ? 1.0833 1.1079 1.0050 -0.0462 -0.0904 0.0295  23  ASP A OD1 
127   O OD2 . ASP A  23  ? 1.0475 1.0735 0.9704 -0.0428 -0.0868 0.0231  23  ASP A OD2 
128   N N   . THR A  24  ? 0.5708 0.5923 0.4862 -0.0470 -0.0769 0.0200  24  THR A N   
129   C CA  . THR A  24  ? 0.6833 0.7043 0.5972 -0.0471 -0.0724 0.0162  24  THR A CA  
130   C C   . THR A  24  ? 0.6258 0.6494 0.5347 -0.0466 -0.0712 0.0103  24  THR A C   
131   O O   . THR A  24  ? 0.5498 0.5749 0.4566 -0.0460 -0.0736 0.0096  24  THR A O   
132   C CB  . THR A  24  ? 0.7681 0.7879 0.6776 -0.0496 -0.0722 0.0169  24  THR A CB  
133   O OG1 . THR A  24  ? 0.8832 0.9045 0.7841 -0.0511 -0.0739 0.0139  24  THR A OG1 
134   C CG2 . THR A  24  ? 0.7211 0.7391 0.6339 -0.0505 -0.0749 0.0233  24  THR A CG2 
135   N N   . VAL A  25  ? 0.7274 0.7514 0.6344 -0.0468 -0.0673 0.0063  25  VAL A N   
136   C CA  . VAL A  25  ? 0.7834 0.8102 0.6854 -0.0465 -0.0661 0.0010  25  VAL A CA  
137   C C   . VAL A  25  ? 0.7589 0.7868 0.6533 -0.0481 -0.0688 0.0000  25  VAL A C   
138   O O   . VAL A  25  ? 0.6922 0.7222 0.5833 -0.0474 -0.0697 -0.0026 25  VAL A O   
139   C CB  . VAL A  25  ? 0.7001 0.7274 0.6013 -0.0470 -0.0616 -0.0029 25  VAL A CB  
140   C CG1 . VAL A  25  ? 0.6286 0.6592 0.5284 -0.0456 -0.0598 -0.0075 25  VAL A CG1 
141   C CG2 . VAL A  25  ? 0.7832 0.8080 0.6911 -0.0467 -0.0587 -0.0009 25  VAL A CG2 
142   N N   . LEU A  26  ? 0.7415 0.7675 0.6331 -0.0503 -0.0699 0.0022  26  LEU A N   
143   C CA  . LEU A  26  ? 0.6978 0.7244 0.5816 -0.0523 -0.0717 0.0008  26  LEU A CA  
144   C C   . LEU A  26  ? 0.8048 0.8307 0.6866 -0.0532 -0.0763 0.0041  26  LEU A C   
145   O O   . LEU A  26  ? 0.8079 0.8346 0.6833 -0.0545 -0.0778 0.0023  26  LEU A O   
146   C CB  . LEU A  26  ? 0.7010 0.7260 0.5821 -0.0545 -0.0700 0.0010  26  LEU A CB  
147   C CG  . LEU A  26  ? 0.7013 0.7261 0.5849 -0.0541 -0.0654 -0.0015 26  LEU A CG  
148   C CD1 . LEU A  26  ? 0.6186 0.6418 0.4988 -0.0564 -0.0639 -0.0016 26  LEU A CD1 
149   C CD2 . LEU A  26  ? 0.7979 0.8259 0.6799 -0.0530 -0.0633 -0.0068 26  LEU A CD2 
150   N N   . GLU A  27  ? 0.8026 0.8273 0.6899 -0.0527 -0.0783 0.0089  27  GLU A N   
151   C CA  . GLU A  27  ? 0.6592 0.6835 0.5449 -0.0540 -0.0829 0.0124  27  GLU A CA  
152   C C   . GLU A  27  ? 0.7813 0.8058 0.6740 -0.0523 -0.0848 0.0158  27  GLU A C   
153   O O   . GLU A  27  ? 0.8291 0.8529 0.7290 -0.0505 -0.0830 0.0175  27  GLU A O   
154   C CB  . GLU A  27  ? 0.9507 0.9732 0.8342 -0.0565 -0.0843 0.0161  27  GLU A CB  
155   C CG  . GLU A  27  ? 1.2151 1.2377 1.0931 -0.0590 -0.0887 0.0182  27  GLU A CG  
156   C CD  . GLU A  27  ? 1.3330 1.3541 1.2071 -0.0618 -0.0897 0.0209  27  GLU A CD  
157   O OE1 . GLU A  27  ? 1.2464 1.2674 1.1172 -0.0639 -0.0936 0.0240  27  GLU A OE1 
158   O OE2 . GLU A  27  ? 1.2752 1.2952 1.1492 -0.0619 -0.0865 0.0199  27  GLU A OE2 
159   N N   . LYS A  28  ? 0.9091 0.9344 0.7997 -0.0529 -0.0884 0.0167  28  LYS A N   
160   C CA  . LYS A  28  ? 0.9242 0.9498 0.8211 -0.0515 -0.0906 0.0199  28  LYS A CA  
161   C C   . LYS A  28  ? 0.9512 0.9763 0.8491 -0.0535 -0.0948 0.0256  28  LYS A C   
162   O O   . LYS A  28  ? 0.8849 0.9096 0.7768 -0.0562 -0.0966 0.0264  28  LYS A O   
163   C CB  . LYS A  28  ? 0.8246 0.8518 0.7194 -0.0506 -0.0916 0.0170  28  LYS A CB  
164   C CG  . LYS A  28  ? 0.8786 0.9067 0.7768 -0.0476 -0.0881 0.0134  28  LYS A CG  
165   C CD  . LYS A  28  ? 1.0711 1.1006 0.9674 -0.0467 -0.0891 0.0110  28  LYS A CD  
166   C CE  . LYS A  28  ? 1.2411 1.2716 1.1425 -0.0435 -0.0865 0.0091  28  LYS A CE  
167   N NZ  . LYS A  28  ? 1.1878 1.2189 1.0886 -0.0426 -0.0824 0.0058  28  LYS A NZ  
168   N N   . ASN A  29  ? 1.0676 1.0928 0.9731 -0.0522 -0.0964 0.0296  29  ASN A N   
169   C CA  . ASN A  29  ? 0.8836 0.9090 0.7913 -0.0538 -0.1006 0.0356  29  ASN A CA  
170   C C   . ASN A  29  ? 0.9013 0.9257 0.8057 -0.0562 -0.1013 0.0383  29  ASN A C   
171   O O   . ASN A  29  ? 0.9557 0.9805 0.8538 -0.0591 -0.1046 0.0394  29  ASN A O   
172   C CB  . ASN A  29  ? 0.9086 0.9354 0.8126 -0.0554 -0.1047 0.0356  29  ASN A CB  
173   C CG  . ASN A  29  ? 1.2615 1.2893 1.1719 -0.0531 -0.1053 0.0360  29  ASN A CG  
174   O OD1 . ASN A  29  ? 1.3469 1.3749 1.2654 -0.0521 -0.1064 0.0406  29  ASN A OD1 
175   N ND2 . ASN A  29  ? 1.1808 1.2091 1.0880 -0.0523 -0.1043 0.0314  29  ASN A ND2 
176   N N   . VAL A  30  ? 0.8557 0.8786 0.7641 -0.0552 -0.0980 0.0392  30  VAL A N   
177   C CA  . VAL A  30  ? 0.7209 0.7426 0.6275 -0.0571 -0.0982 0.0423  30  VAL A CA  
178   C C   . VAL A  30  ? 0.8572 0.8788 0.7720 -0.0567 -0.1002 0.0495  30  VAL A C   
179   O O   . VAL A  30  ? 0.8186 0.8395 0.7423 -0.0542 -0.0978 0.0510  30  VAL A O   
180   C CB  . VAL A  30  ? 0.7476 0.7676 0.6536 -0.0564 -0.0931 0.0390  30  VAL A CB  
181   C CG1 . VAL A  30  ? 0.6122 0.6306 0.5174 -0.0582 -0.0930 0.0428  30  VAL A CG1 
182   C CG2 . VAL A  30  ? 0.8174 0.8379 0.7152 -0.0570 -0.0913 0.0323  30  VAL A CG2 
183   N N   . THR A  31  ? 0.9130 0.9355 0.8252 -0.0593 -0.1045 0.0540  31  THR A N   
184   C CA  . THR A  31  ? 0.8913 0.9144 0.8112 -0.0591 -0.1070 0.0615  31  THR A CA  
185   C C   . THR A  31  ? 0.7990 0.8198 0.7233 -0.0584 -0.1037 0.0642  31  THR A C   
186   O O   . THR A  31  ? 0.8553 0.8749 0.7735 -0.0602 -0.1027 0.0634  31  THR A O   
187   C CB  . THR A  31  ? 0.9396 0.9645 0.8544 -0.0625 -0.1128 0.0656  31  THR A CB  
188   O OG1 . THR A  31  ? 0.8404 0.8672 0.7514 -0.0634 -0.1158 0.0631  31  THR A OG1 
189   C CG2 . THR A  31  ? 0.9017 0.9277 0.8250 -0.0623 -0.1154 0.0738  31  THR A CG2 
190   N N   . VAL A  32  ? 0.8590 0.8791 0.7940 -0.0558 -0.1017 0.0675  32  VAL A N   
191   C CA  . VAL A  32  ? 0.8512 0.8689 0.7918 -0.0548 -0.0980 0.0704  32  VAL A CA  
192   C C   . VAL A  32  ? 0.9121 0.9304 0.8609 -0.0547 -0.1005 0.0791  32  VAL A C   
193   O O   . VAL A  32  ? 1.0127 1.0334 0.9658 -0.0544 -0.1044 0.0828  32  VAL A O   
194   C CB  . VAL A  32  ? 0.7446 0.7600 0.6908 -0.0520 -0.0919 0.0665  32  VAL A CB  
195   C CG1 . VAL A  32  ? 0.6199 0.6347 0.5579 -0.0524 -0.0889 0.0585  32  VAL A CG1 
196   C CG2 . VAL A  32  ? 0.7581 0.7746 0.7122 -0.0496 -0.0923 0.0672  32  VAL A CG2 
197   N N   . THR A  33  ? 0.8560 0.8723 0.8072 -0.0548 -0.0982 0.0824  33  THR A N   
198   C CA  . THR A  33  ? 0.9170 0.9339 0.8766 -0.0545 -0.1002 0.0911  33  THR A CA  
199   C C   . THR A  33  ? 0.9760 0.9923 0.9482 -0.0512 -0.0979 0.0937  33  THR A C   
200   O O   . THR A  33  ? 1.1802 1.1987 1.1595 -0.0507 -0.1013 0.1001  33  THR A O   
201   C CB  . THR A  33  ? 0.9285 0.9429 0.8881 -0.0552 -0.0975 0.0940  33  THR A CB  
202   O OG1 . THR A  33  ? 0.9248 0.9356 0.8876 -0.0533 -0.0907 0.0898  33  THR A OG1 
203   C CG2 . THR A  33  ? 1.0142 1.0291 0.9615 -0.0586 -0.0998 0.0922  33  THR A CG2 
204   N N   . HIS A  34  ? 0.9790 0.9926 0.9540 -0.0492 -0.0921 0.0887  34  HIS A N   
205   C CA  . HIS A  34  ? 0.9633 0.9758 0.9500 -0.0461 -0.0890 0.0903  34  HIS A CA  
206   C C   . HIS A  34  ? 0.9417 0.9529 0.9271 -0.0446 -0.0849 0.0826  34  HIS A C   
207   O O   . HIS A  34  ? 0.8072 0.8176 0.7841 -0.0456 -0.0830 0.0762  34  HIS A O   
208   C CB  . HIS A  34  ? 0.8697 0.8791 0.8647 -0.0449 -0.0846 0.0946  34  HIS A CB  
209   C CG  . HIS A  34  ? 1.0176 1.0281 1.0143 -0.0462 -0.0881 0.1026  34  HIS A CG  
210   N ND1 . HIS A  34  ? 1.0115 1.0221 0.9990 -0.0489 -0.0898 0.1026  34  HIS A ND1 
211   C CD2 . HIS A  34  ? 1.1012 1.1129 1.1077 -0.0453 -0.0902 0.1111  34  HIS A CD2 
212   C CE1 . HIS A  34  ? 1.1766 1.1886 1.1680 -0.0496 -0.0929 0.1108  34  HIS A CE1 
213   N NE2 . HIS A  34  ? 1.3255 1.3383 1.3285 -0.0474 -0.0933 0.1161  34  HIS A NE2 
214   N N   . SER A  35  ? 0.8903 0.9014 0.8844 -0.0422 -0.0836 0.0834  35  SER A N   
215   C CA  . SER A  35  ? 0.7591 0.7690 0.7532 -0.0406 -0.0795 0.0767  35  SER A CA  
216   C C   . SER A  35  ? 0.7294 0.7387 0.7351 -0.0378 -0.0776 0.0793  35  SER A C   
217   O O   . SER A  35  ? 0.9382 0.9479 0.9524 -0.0371 -0.0793 0.0863  35  SER A O   
218   C CB  . SER A  35  ? 0.7710 0.7833 0.7554 -0.0416 -0.0824 0.0711  35  SER A CB  
219   O OG  . SER A  35  ? 0.8727 0.8882 0.8572 -0.0422 -0.0884 0.0745  35  SER A OG  
220   N N   . VAL A  36  ? 0.7804 0.7886 0.7865 -0.0364 -0.0739 0.0737  36  VAL A N   
221   C CA  . VAL A  36  ? 0.8782 0.8857 0.8944 -0.0338 -0.0717 0.0751  36  VAL A CA  
222   C C   . VAL A  36  ? 0.7989 0.8075 0.8111 -0.0331 -0.0715 0.0690  36  VAL A C   
223   O O   . VAL A  36  ? 0.7394 0.7485 0.7422 -0.0341 -0.0710 0.0630  36  VAL A O   
224   C CB  . VAL A  36  ? 0.7659 0.7692 0.7898 -0.0324 -0.0647 0.0753  36  VAL A CB  
225   C CG1 . VAL A  36  ? 0.8894 0.8910 0.9160 -0.0333 -0.0640 0.0804  36  VAL A CG1 
226   C CG2 . VAL A  36  ? 0.6869 0.6884 0.7051 -0.0326 -0.0596 0.0671  36  VAL A CG2 
227   N N   . ASN A  37  ? 0.8553 0.8644 0.8749 -0.0312 -0.0718 0.0708  37  ASN A N   
228   C CA  . ASN A  37  ? 0.8006 0.8106 0.8173 -0.0302 -0.0714 0.0655  37  ASN A CA  
229   C C   . ASN A  37  ? 0.7406 0.7476 0.7618 -0.0284 -0.0647 0.0620  37  ASN A C   
230   O O   . ASN A  37  ? 0.7876 0.7925 0.8190 -0.0269 -0.0617 0.0655  37  ASN A O   
231   C CB  . ASN A  37  ? 0.6727 0.6853 0.6938 -0.0294 -0.0759 0.0690  37  ASN A CB  
232   C CG  . ASN A  37  ? 0.8988 0.9131 0.9142 -0.0290 -0.0770 0.0636  37  ASN A CG  
233   O OD1 . ASN A  37  ? 1.2141 1.2301 1.2328 -0.0282 -0.0799 0.0654  37  ASN A OD1 
234   N ND2 . ASN A  37  ? 0.7174 0.7313 0.7243 -0.0295 -0.0746 0.0572  37  ASN A ND2 
235   N N   . LEU A  38  ? 0.7203 0.7273 0.7341 -0.0287 -0.0622 0.0550  38  LEU A N   
236   C CA  . LEU A  38  ? 0.6258 0.6303 0.6424 -0.0275 -0.0559 0.0510  38  LEU A CA  
237   C C   . LEU A  38  ? 0.5460 0.5516 0.5654 -0.0257 -0.0561 0.0495  38  LEU A C   
238   O O   . LEU A  38  ? 0.6193 0.6229 0.6422 -0.0245 -0.0512 0.0469  38  LEU A O   
239   C CB  . LEU A  38  ? 0.5681 0.5726 0.5756 -0.0289 -0.0531 0.0443  38  LEU A CB  
240   C CG  . LEU A  38  ? 0.4990 0.5017 0.5041 -0.0307 -0.0513 0.0447  38  LEU A CG  
241   C CD1 . LEU A  38  ? 0.6784 0.6822 0.6732 -0.0322 -0.0499 0.0381  38  LEU A CD1 
242   C CD2 . LEU A  38  ? 0.5431 0.5418 0.5571 -0.0300 -0.0455 0.0467  38  LEU A CD2 
243   N N   . LEU A  39  ? 0.5932 0.6017 0.6109 -0.0256 -0.0616 0.0512  39  LEU A N   
244   C CA  . LEU A  39  ? 0.5552 0.5647 0.5749 -0.0240 -0.0621 0.0499  39  LEU A CA  
245   C C   . LEU A  39  ? 0.6807 0.6901 0.7111 -0.0225 -0.0638 0.0560  39  LEU A C   
246   O O   . LEU A  39  ? 0.7874 0.7985 0.8197 -0.0233 -0.0685 0.0610  39  LEU A O   
247   C CB  . LEU A  39  ? 0.4960 0.5088 0.5067 -0.0248 -0.0665 0.0469  39  LEU A CB  
248   C CG  . LEU A  39  ? 0.6219 0.6360 0.6346 -0.0231 -0.0676 0.0460  39  LEU A CG  
249   C CD1 . LEU A  39  ? 0.5766 0.5890 0.5913 -0.0215 -0.0620 0.0419  39  LEU A CD1 
250   C CD2 . LEU A  39  ? 0.6486 0.6657 0.6525 -0.0241 -0.0718 0.0433  39  LEU A CD2 
251   N N   . GLU A  40  ? 0.7294 0.7369 0.7668 -0.0206 -0.0598 0.0555  40  GLU A N   
252   C CA  . GLU A  40  ? 0.6741 0.6816 0.7221 -0.0190 -0.0609 0.0608  40  GLU A CA  
253   C C   . GLU A  40  ? 0.6415 0.6517 0.6873 -0.0184 -0.0648 0.0598  40  GLU A C   
254   O O   . GLU A  40  ? 0.6891 0.6997 0.7296 -0.0180 -0.0633 0.0545  40  GLU A O   
255   C CB  . GLU A  40  ? 0.6365 0.6404 0.6930 -0.0172 -0.0544 0.0605  40  GLU A CB  
256   C CG  . GLU A  40  ? 0.7054 0.7087 0.7744 -0.0155 -0.0546 0.0664  40  GLU A CG  
257   C CD  . GLU A  40  ? 0.8736 0.8770 0.9490 -0.0159 -0.0568 0.0735  40  GLU A CD  
258   O OE1 . GLU A  40  ? 1.0070 1.0073 1.0894 -0.0154 -0.0523 0.0758  40  GLU A OE1 
259   O OE2 . GLU A  40  ? 0.8503 0.8571 0.9239 -0.0169 -0.0631 0.0770  40  GLU A OE2 
260   N N   . ASP A  41  ? 0.8386 0.8510 0.8885 -0.0186 -0.0699 0.0651  41  ASP A N   
261   C CA  . ASP A  41  ? 0.7446 0.7596 0.7931 -0.0184 -0.0738 0.0646  41  ASP A CA  
262   C C   . ASP A  41  ? 0.8392 0.8552 0.8987 -0.0174 -0.0762 0.0709  41  ASP A C   
263   O O   . ASP A  41  ? 0.9641 0.9829 1.0229 -0.0181 -0.0813 0.0729  41  ASP A O   
264   C CB  . ASP A  41  ? 0.8027 0.8205 0.8409 -0.0206 -0.0790 0.0631  41  ASP A CB  
265   C CG  . ASP A  41  ? 1.2455 1.2646 1.2839 -0.0226 -0.0829 0.0682  41  ASP A CG  
266   O OD1 . ASP A  41  ? 1.1762 1.1942 1.2233 -0.0220 -0.0818 0.0733  41  ASP A OD1 
267   O OD2 . ASP A  41  ? 1.2183 1.2395 1.2483 -0.0247 -0.0870 0.0672  41  ASP A OD2 
268   N N   . LYS A  42  ? 0.8827 0.8961 0.9524 -0.0159 -0.0722 0.0741  42  LYS A N   
269   C CA  . LYS A  42  ? 0.7974 0.8118 0.8787 -0.0148 -0.0741 0.0807  42  LYS A CA  
270   C C   . LYS A  42  ? 0.7079 0.7190 0.7996 -0.0124 -0.0682 0.0814  42  LYS A C   
271   O O   . LYS A  42  ? 0.8143 0.8222 0.9098 -0.0118 -0.0633 0.0818  42  LYS A O   
272   C CB  . LYS A  42  ? 1.1046 1.1202 1.1892 -0.0161 -0.0773 0.0871  42  LYS A CB  
273   C CG  . LYS A  42  ? 1.3816 1.4014 1.4702 -0.0169 -0.0839 0.0928  42  LYS A CG  
274   C CD  . LYS A  42  ? 1.5597 1.5815 1.6463 -0.0191 -0.0881 0.0974  42  LYS A CD  
275   C CE  . LYS A  42  ? 1.3980 1.4200 1.4707 -0.0213 -0.0893 0.0924  42  LYS A CE  
276   N NZ  . LYS A  42  ? 1.3636 1.3871 1.4339 -0.0234 -0.0927 0.0966  42  LYS A NZ  
277   N N   . HIS A  43  ? 0.5463 0.5581 0.6426 -0.0110 -0.0685 0.0814  43  HIS A N   
278   C CA  . HIS A  43  ? 0.7293 0.7382 0.8359 -0.0086 -0.0633 0.0823  43  HIS A CA  
279   C C   . HIS A  43  ? 0.7462 0.7568 0.8650 -0.0078 -0.0661 0.0898  43  HIS A C   
280   O O   . HIS A  43  ? 0.7381 0.7526 0.8559 -0.0090 -0.0725 0.0929  43  HIS A O   
281   C CB  . HIS A  43  ? 0.6733 0.6814 0.7764 -0.0075 -0.0610 0.0767  43  HIS A CB  
282   C CG  . HIS A  43  ? 0.7094 0.7210 0.8098 -0.0078 -0.0664 0.0768  43  HIS A CG  
283   N ND1 . HIS A  43  ? 0.7999 0.8123 0.9090 -0.0064 -0.0672 0.0797  43  HIS A ND1 
284   C CD2 . HIS A  43  ? 0.6816 0.6961 0.7719 -0.0095 -0.0711 0.0743  43  HIS A CD2 
285   C CE1 . HIS A  43  ? 0.7141 0.7295 0.8182 -0.0073 -0.0722 0.0788  43  HIS A CE1 
286   N NE2 . HIS A  43  ? 0.6742 0.6909 0.7670 -0.0091 -0.0746 0.0756  43  HIS A NE2 
287   N N   . ASN A  44  ? 0.7658 0.7736 0.8960 -0.0059 -0.0613 0.0926  44  ASN A N   
288   C CA  . ASN A  44  ? 0.7083 0.7179 0.8514 -0.0049 -0.0636 0.1000  44  ASN A CA  
289   C C   . ASN A  44  ? 0.7653 0.7765 0.9119 -0.0038 -0.0652 0.0997  44  ASN A C   
290   O O   . ASN A  44  ? 0.8108 0.8238 0.9681 -0.0030 -0.0672 0.1055  44  ASN A O   
291   C CB  . ASN A  44  ? 0.5994 0.6053 0.7543 -0.0032 -0.0577 0.1038  44  ASN A CB  
292   C CG  . ASN A  44  ? 0.8291 0.8302 0.9861 -0.0015 -0.0500 0.0990  44  ASN A CG  
293   O OD1 . ASN A  44  ? 0.9809 0.9783 1.1462 -0.0003 -0.0442 0.1007  44  ASN A OD1 
294   N ND2 . ASN A  44  ? 0.7630 0.7642 0.9123 -0.0015 -0.0497 0.0929  44  ASN A ND2 
295   N N   . GLY A  45  ? 0.7280 0.7385 0.8658 -0.0038 -0.0642 0.0931  45  GLY A N   
296   C CA  . GLY A  45  ? 0.7041 0.7159 0.8441 -0.0029 -0.0656 0.0923  45  GLY A CA  
297   C C   . GLY A  45  ? 0.7261 0.7354 0.8788 -0.0004 -0.0608 0.0946  45  GLY A C   
298   O O   . GLY A  45  ? 0.7175 0.7285 0.8761 0.0003  -0.0628 0.0967  45  GLY A O   
299   N N   . LYS A  46  ? 0.6371 0.6421 0.7938 0.0006  -0.0543 0.0940  46  LYS A N   
300   C CA  . LYS A  46  ? 0.7634 0.7653 0.9320 0.0028  -0.0487 0.0958  46  LYS A CA  
301   C C   . LYS A  46  ? 0.6577 0.6546 0.8224 0.0035  -0.0411 0.0896  46  LYS A C   
302   O O   . LYS A  46  ? 0.7570 0.7520 0.9149 0.0024  -0.0386 0.0864  46  LYS A O   
303   C CB  . LYS A  46  ? 0.9205 0.9220 1.1018 0.0035  -0.0479 0.1032  46  LYS A CB  
304   C CG  . LYS A  46  ? 0.9450 0.9517 1.1317 0.0028  -0.0553 0.1102  46  LYS A CG  
305   C CD  . LYS A  46  ? 1.1780 1.1849 1.3732 0.0029  -0.0552 0.1168  46  LYS A CD  
306   C CE  . LYS A  46  ? 1.3460 1.3578 1.5359 0.0006  -0.0630 0.1203  46  LYS A CE  
307   N NZ  . LYS A  46  ? 1.2089 1.2207 1.4049 0.0005  -0.0627 0.1262  46  LYS A NZ  
308   N N   . LEU A  47  ? 0.5888 0.5837 0.7578 0.0051  -0.0373 0.0877  47  LEU A N   
309   C CA  . LEU A  47  ? 0.6791 0.6692 0.8454 0.0056  -0.0297 0.0822  47  LEU A CA  
310   C C   . LEU A  47  ? 0.6707 0.6567 0.8468 0.0063  -0.0237 0.0851  47  LEU A C   
311   O O   . LEU A  47  ? 0.7350 0.7176 0.9198 0.0078  -0.0182 0.0856  47  LEU A O   
312   C CB  . LEU A  47  ? 0.6661 0.6553 0.8343 0.0071  -0.0276 0.0799  47  LEU A CB  
313   C CG  . LEU A  47  ? 0.6673 0.6606 0.8272 0.0066  -0.0336 0.0778  47  LEU A CG  
314   C CD1 . LEU A  47  ? 0.5368 0.5283 0.6943 0.0077  -0.0300 0.0732  47  LEU A CD1 
315   C CD2 . LEU A  47  ? 0.5067 0.5024 0.6532 0.0045  -0.0376 0.0745  47  LEU A CD2 
316   N N   . CYS A  48  ? 0.7007 0.6868 0.8755 0.0052  -0.0245 0.0869  48  CYS A N   
317   C CA  . CYS A  48  ? 0.7354 0.7174 0.9194 0.0057  -0.0187 0.0899  48  CYS A CA  
318   C C   . CYS A  48  ? 0.6796 0.6563 0.8614 0.0058  -0.0102 0.0839  48  CYS A C   
319   O O   . CYS A  48  ? 0.7169 0.6936 0.8880 0.0051  -0.0095 0.0773  48  CYS A O   
320   C CB  . CYS A  48  ? 0.6068 0.5899 0.7876 0.0042  -0.0210 0.0920  48  CYS A CB  
321   S SG  . CYS A  48  ? 0.9202 0.9100 1.1011 0.0035  -0.0314 0.0983  48  CYS A SG  
322   N N   . LYS A  49  ? 0.7469 0.7191 0.9388 0.0066  -0.0037 0.0861  49  LYS A N   
323   C CA  . LYS A  49  ? 0.7741 0.7409 0.9650 0.0065  0.0049  0.0807  49  LYS A CA  
324   C C   . LYS A  49  ? 0.7317 0.6965 0.9128 0.0044  0.0079  0.0757  49  LYS A C   
325   O O   . LYS A  49  ? 0.7509 0.7172 0.9300 0.0034  0.0048  0.0780  49  LYS A O   
326   C CB  . LYS A  49  ? 0.8734 0.8356 1.0793 0.0081  0.0115  0.0848  49  LYS A CB  
327   C CG  . LYS A  49  ? 0.7803 0.7451 0.9994 0.0099  0.0075  0.0935  49  LYS A CG  
328   C CD  . LYS A  49  ? 0.9299 0.8904 1.1616 0.0108  0.0136  0.0981  49  LYS A CD  
329   C CE  . LYS A  49  ? 1.0842 1.0455 1.3319 0.0131  0.0131  0.1056  49  LYS A CE  
330   N NZ  . LYS A  49  ? 1.0375 0.9925 1.2970 0.0143  0.0225  0.1068  49  LYS A NZ  
331   N N   . LEU A  50  ? 0.8190 0.7804 0.9941 0.0036  0.0139  0.0690  50  LEU A N   
332   C CA  . LEU A  50  ? 0.8156 0.7747 0.9822 0.0014  0.0177  0.0639  50  LEU A CA  
333   C C   . LEU A  50  ? 1.0456 1.0005 1.2142 0.0001  0.0236  0.0635  50  LEU A C   
334   O O   . LEU A  50  ? 1.3242 1.2806 1.4869 -0.0013 0.0210  0.0632  50  LEU A O   
335   C CB  . LEU A  50  ? 0.8090 0.7684 0.9632 0.0001  0.0193  0.0558  50  LEU A CB  
336   C CG  . LEU A  50  ? 0.7394 0.7043 0.8807 -0.0008 0.0122  0.0529  50  LEU A CG  
337   C CD1 . LEU A  50  ? 0.6770 0.6418 0.8080 -0.0017 0.0149  0.0454  50  LEU A CD1 
338   C CD2 . LEU A  50  ? 0.7389 0.7061 0.8738 -0.0024 0.0083  0.0532  50  LEU A CD2 
339   N N   . ARG A  51  ? 1.0077 0.9570 1.1849 0.0006  0.0317  0.0633  51  ARG A N   
340   C CA  . ARG A  51  ? 1.1697 1.1141 1.3487 -0.0008 0.0386  0.0621  51  ARG A CA  
341   C C   . ARG A  51  ? 1.1525 1.0966 1.3468 0.0016  0.0375  0.0710  51  ARG A C   
342   O O   . ARG A  51  ? 1.3443 1.2914 1.5406 0.0019  0.0321  0.0762  51  ARG A O   
343   C CB  . ARG A  51  ? 1.2977 1.2371 1.4782 -0.0011 0.0469  0.0573  51  ARG A CB  
344   C CG  . ARG A  51  ? 1.4499 1.3906 1.6166 -0.0029 0.0473  0.0491  51  ARG A CG  
345   C CD  . ARG A  51  ? 1.8158 1.7507 1.9806 -0.0050 0.0569  0.0433  51  ARG A CD  
346   N NE  . ARG A  51  ? 2.0133 1.9467 2.1752 -0.0070 0.0587  0.0423  51  ARG A NE  
347   C CZ  . ARG A  51  ? 1.8445 1.7726 2.0150 -0.0073 0.0653  0.0442  51  ARG A CZ  
348   N NH1 . ARG A  51  ? 1.6814 1.6048 1.8643 -0.0058 0.0712  0.0471  51  ARG A NH1 
349   N NH2 . ARG A  51  ? 1.6941 1.6214 1.8609 -0.0092 0.0664  0.0431  51  ARG A NH2 
350   N N   . GLY A  52  ? 1.0040 0.9445 1.2091 0.0032  0.0427  0.0727  52  GLY A N   
351   C CA  . GLY A  52  ? 1.2226 1.1637 1.4426 0.0058  0.0412  0.0811  52  GLY A CA  
352   C C   . GLY A  52  ? 1.1145 1.0554 1.3393 0.0074  0.0422  0.0808  52  GLY A C   
353   O O   . GLY A  52  ? 1.1248 1.0654 1.3630 0.0096  0.0425  0.0870  52  GLY A O   
354   N N   . VAL A  53  ? 1.0535 0.9946 1.2672 0.0062  0.0428  0.0737  53  VAL A N   
355   C CA  . VAL A  53  ? 0.7814 0.7221 0.9977 0.0075  0.0441  0.0724  53  VAL A CA  
356   C C   . VAL A  53  ? 0.6491 0.5964 0.8611 0.0084  0.0347  0.0741  53  VAL A C   
357   O O   . VAL A  53  ? 0.7137 0.6652 0.9149 0.0071  0.0286  0.0723  53  VAL A O   
358   C CB  . VAL A  53  ? 0.6882 0.6255 0.8949 0.0058  0.0502  0.0638  53  VAL A CB  
359   C CG1 . VAL A  53  ? 0.6628 0.5991 0.8730 0.0072  0.0522  0.0629  53  VAL A CG1 
360   C CG2 . VAL A  53  ? 0.5897 0.5206 0.7987 0.0043  0.0595  0.0613  53  VAL A CG2 
361   N N   . ALA A  54  ? 0.6838 0.6318 0.9047 0.0104  0.0337  0.0777  54  ALA A N   
362   C CA  . ALA A  54  ? 0.6863 0.6403 0.9046 0.0112  0.0252  0.0796  54  ALA A CA  
363   C C   . ALA A  54  ? 0.6706 0.6253 0.8773 0.0106  0.0250  0.0727  54  ALA A C   
364   O O   . ALA A  54  ? 0.6335 0.5840 0.8381 0.0102  0.0319  0.0678  54  ALA A O   
365   C CB  . ALA A  54  ? 0.7273 0.6822 0.9606 0.0136  0.0240  0.0866  54  ALA A CB  
366   N N   . PRO A  55  ? 0.5674 0.5276 0.7666 0.0105  0.0171  0.0724  55  PRO A N   
367   C CA  . PRO A  55  ? 0.5173 0.4788 0.7063 0.0102  0.0162  0.0668  55  PRO A CA  
368   C C   . PRO A  55  ? 0.5884 0.5487 0.7855 0.0121  0.0182  0.0682  55  PRO A C   
369   O O   . PRO A  55  ? 0.6719 0.6324 0.8818 0.0137  0.0174  0.0744  55  PRO A O   
370   C CB  . PRO A  55  ? 0.5355 0.5031 0.7167 0.0097  0.0070  0.0677  55  PRO A CB  
371   C CG  . PRO A  55  ? 0.3468 0.3166 0.5380 0.0104  0.0027  0.0752  55  PRO A CG  
372   C CD  . PRO A  55  ? 0.5365 0.5019 0.7353 0.0103  0.0088  0.0771  55  PRO A CD  
373   N N   . LEU A  56  ? 0.6107 0.5699 0.8007 0.0119  0.0209  0.0627  56  LEU A N   
374   C CA  . LEU A  56  ? 0.5093 0.4676 0.7053 0.0137  0.0225  0.0635  56  LEU A CA  
375   C C   . LEU A  56  ? 0.4661 0.4298 0.6577 0.0142  0.0146  0.0643  56  LEU A C   
376   O O   . LEU A  56  ? 0.6765 0.6422 0.8560 0.0135  0.0126  0.0595  56  LEU A O   
377   C CB  . LEU A  56  ? 0.6221 0.5763 0.8125 0.0131  0.0297  0.0572  56  LEU A CB  
378   C CG  . LEU A  56  ? 0.5057 0.4584 0.7013 0.0147  0.0323  0.0572  56  LEU A CG  
379   C CD1 . LEU A  56  ? 0.6731 0.6227 0.8852 0.0164  0.0358  0.0628  56  LEU A CD1 
380   C CD2 . LEU A  56  ? 0.5797 0.5291 0.7671 0.0137  0.0387  0.0504  56  LEU A CD2 
381   N N   . HIS A  57  ? 0.5651 0.5313 0.7668 0.0156  0.0102  0.0704  57  HIS A N   
382   C CA  . HIS A  57  ? 0.6014 0.5726 0.8000 0.0159  0.0029  0.0716  57  HIS A CA  
383   C C   . HIS A  57  ? 0.7852 0.7553 0.9877 0.0175  0.0050  0.0708  57  HIS A C   
384   O O   . HIS A  57  ? 0.7845 0.7520 0.9992 0.0189  0.0088  0.0741  57  HIS A O   
385   C CB  . HIS A  57  ? 0.6538 0.6288 0.8605 0.0161  -0.0035 0.0785  57  HIS A CB  
386   C CG  . HIS A  57  ? 0.6853 0.6657 0.8861 0.0157  -0.0117 0.0791  57  HIS A CG  
387   N ND1 . HIS A  57  ? 0.6753 0.6575 0.8801 0.0168  -0.0141 0.0804  57  HIS A ND1 
388   C CD2 . HIS A  57  ? 0.7888 0.7731 0.9803 0.0141  -0.0178 0.0783  57  HIS A CD2 
389   C CE1 . HIS A  57  ? 0.8270 0.8139 1.0251 0.0158  -0.0212 0.0804  57  HIS A CE1 
390   N NE2 . HIS A  57  ? 0.8891 0.8773 1.0789 0.0142  -0.0236 0.0791  57  HIS A NE2 
391   N N   . LEU A  58  ? 0.8274 0.7993 1.0196 0.0173  0.0028  0.0666  58  LEU A N   
392   C CA  . LEU A  58  ? 0.7261 0.6968 0.9205 0.0187  0.0051  0.0654  58  LEU A CA  
393   C C   . LEU A  58  ? 0.8509 0.8254 1.0505 0.0197  -0.0009 0.0693  58  LEU A C   
394   O O   . LEU A  58  ? 0.8805 0.8540 1.0848 0.0210  0.0009  0.0694  58  LEU A O   
395   C CB  . LEU A  58  ? 0.7718 0.7421 0.9528 0.0181  0.0070  0.0586  58  LEU A CB  
396   C CG  . LEU A  58  ? 0.6777 0.6429 0.8567 0.0178  0.0155  0.0544  58  LEU A CG  
397   C CD1 . LEU A  58  ? 0.7002 0.6618 0.8873 0.0173  0.0202  0.0565  58  LEU A CD1 
398   C CD2 . LEU A  58  ? 0.7491 0.7154 0.9128 0.0163  0.0156  0.0482  58  LEU A CD2 
399   N N   . GLY A  59  ? 0.8495 0.8285 1.0483 0.0188  -0.0081 0.0723  59  GLY A N   
400   C CA  . GLY A  59  ? 0.7845 0.7673 0.9886 0.0193  -0.0140 0.0762  59  GLY A CA  
401   C C   . GLY A  59  ? 0.8781 0.8626 1.0748 0.0196  -0.0162 0.0728  59  GLY A C   
402   O O   . GLY A  59  ? 1.0581 1.0448 1.2429 0.0185  -0.0195 0.0694  59  GLY A O   
403   N N   . LYS A  60  ? 0.9786 0.9618 1.1824 0.0211  -0.0140 0.0738  60  LYS A N   
404   C CA  . LYS A  60  ? 1.1227 1.1072 1.3207 0.0215  -0.0158 0.0710  60  LYS A CA  
405   C C   . LYS A  60  ? 1.0607 1.0417 1.2506 0.0221  -0.0098 0.0652  60  LYS A C   
406   O O   . LYS A  60  ? 1.1611 1.1428 1.3448 0.0226  -0.0105 0.0624  60  LYS A O   
407   C CB  . LYS A  60  ? 1.1913 1.1766 1.4010 0.0227  -0.0169 0.0750  60  LYS A CB  
408   C CG  . LYS A  60  ? 1.6411 1.6283 1.8457 0.0230  -0.0199 0.0730  60  LYS A CG  
409   C CD  . LYS A  60  ? 1.7763 1.7682 1.9732 0.0213  -0.0274 0.0730  60  LYS A CD  
410   C CE  . LYS A  60  ? 1.9054 1.9009 2.1115 0.0204  -0.0328 0.0790  60  LYS A CE  
411   N NZ  . LYS A  60  ? 1.8155 1.8154 2.0136 0.0184  -0.0401 0.0788  60  LYS A NZ  
412   N N   . CYS A  61  ? 0.8707 0.8479 1.0605 0.0219  -0.0039 0.0635  61  CYS A N   
413   C CA  . CYS A  61  ? 0.8545 0.8283 1.0373 0.0222  0.0023  0.0582  61  CYS A CA  
414   C C   . CYS A  61  ? 0.8300 0.8041 1.0002 0.0206  0.0028  0.0537  61  CYS A C   
415   O O   . CYS A  61  ? 0.8601 0.8354 1.0293 0.0194  0.0006  0.0549  61  CYS A O   
416   C CB  . CYS A  61  ? 0.8007 0.7694 0.9932 0.0230  0.0098  0.0591  61  CYS A CB  
417   S SG  . CYS A  61  ? 1.0228 0.9904 1.2297 0.0251  0.0110  0.0634  61  CYS A SG  
418   N N   . ASN A  62  ? 0.6203 0.5935 0.7809 0.0206  0.0059  0.0486  62  ASN A N   
419   C CA  . ASN A  62  ? 0.7599 0.7329 0.9092 0.0190  0.0075  0.0441  62  ASN A CA  
420   C C   . ASN A  62  ? 0.6948 0.6631 0.8452 0.0186  0.0156  0.0416  62  ASN A C   
421   O O   . ASN A  62  ? 0.5987 0.5635 0.7578 0.0196  0.0202  0.0430  62  ASN A O   
422   C CB  . ASN A  62  ? 0.8270 0.8030 0.9637 0.0189  0.0051  0.0401  62  ASN A CB  
423   C CG  . ASN A  62  ? 0.7910 0.7658 0.9276 0.0203  0.0078  0.0387  62  ASN A CG  
424   O OD1 . ASN A  62  ? 0.7604 0.7313 0.9031 0.0210  0.0135  0.0388  62  ASN A OD1 
425   N ND2 . ASN A  62  ? 0.7612 0.7391 0.8910 0.0209  0.0039  0.0375  62  ASN A ND2 
426   N N   . ILE A  63  ? 0.6579 0.6260 0.7992 0.0168  0.0175  0.0377  63  ILE A N   
427   C CA  . ILE A  63  ? 0.6150 0.5786 0.7559 0.0159  0.0253  0.0346  63  ILE A CA  
428   C C   . ILE A  63  ? 0.5502 0.5111 0.6921 0.0169  0.0302  0.0329  63  ILE A C   
429   O O   . ILE A  63  ? 0.5539 0.5103 0.7037 0.0171  0.0363  0.0335  63  ILE A O   
430   C CB  . ILE A  63  ? 0.6652 0.6301 0.7935 0.0137  0.0260  0.0296  63  ILE A CB  
431   C CG1 . ILE A  63  ? 0.4930 0.4601 0.6204 0.0126  0.0217  0.0313  63  ILE A CG1 
432   C CG2 . ILE A  63  ? 0.5915 0.5518 0.7190 0.0123  0.0342  0.0262  63  ILE A CG2 
433   C CD1 . ILE A  63  ? 0.7038 0.6673 0.8415 0.0123  0.0250  0.0343  63  ILE A CD1 
434   N N   . ALA A  64  ? 0.5984 0.5621 0.7327 0.0175  0.0277  0.0309  64  ALA A N   
435   C CA  . ALA A  64  ? 0.6344 0.5959 0.7687 0.0185  0.0320  0.0293  64  ALA A CA  
436   C C   . ALA A  64  ? 0.7067 0.6650 0.8549 0.0202  0.0343  0.0334  64  ALA A C   
437   O O   . ALA A  64  ? 0.7155 0.6692 0.8680 0.0202  0.0411  0.0325  64  ALA A O   
438   C CB  . ALA A  64  ? 0.5517 0.5172 0.6774 0.0194  0.0278  0.0278  64  ALA A CB  
439   N N   . GLY A  65  ? 0.6239 0.5846 0.7789 0.0215  0.0287  0.0378  65  GLY A N   
440   C CA  . GLY A  65  ? 0.5206 0.4792 0.6893 0.0231  0.0300  0.0421  65  GLY A CA  
441   C C   . GLY A  65  ? 0.5920 0.5464 0.7710 0.0228  0.0351  0.0442  65  GLY A C   
442   O O   . GLY A  65  ? 0.6733 0.6238 0.8612 0.0238  0.0402  0.0455  65  GLY A O   
443   N N   . TRP A  66  ? 0.5998 0.5548 0.7777 0.0215  0.0338  0.0446  66  TRP A N   
444   C CA  . TRP A  66  ? 0.6448 0.5960 0.8328 0.0212  0.0384  0.0470  66  TRP A CA  
445   C C   . TRP A  66  ? 0.5446 0.4902 0.7319 0.0203  0.0476  0.0432  66  TRP A C   
446   O O   . TRP A  66  ? 0.7289 0.6701 0.9274 0.0211  0.0529  0.0455  66  TRP A O   
447   C CB  . TRP A  66  ? 0.6469 0.6001 0.8327 0.0198  0.0350  0.0480  66  TRP A CB  
448   C CG  . TRP A  66  ? 0.6564 0.6052 0.8492 0.0191  0.0410  0.0488  66  TRP A CG  
449   C CD1 . TRP A  66  ? 0.8084 0.7542 1.0158 0.0203  0.0440  0.0535  66  TRP A CD1 
450   C CD2 . TRP A  66  ? 0.7376 0.6843 0.9232 0.0170  0.0448  0.0449  66  TRP A CD2 
451   N NE1 . TRP A  66  ? 0.8257 0.7675 1.0357 0.0191  0.0498  0.0528  66  TRP A NE1 
452   C CE2 . TRP A  66  ? 0.7271 0.6693 0.9237 0.0170  0.0504  0.0474  66  TRP A CE2 
453   C CE3 . TRP A  66  ? 0.7177 0.6661 0.8891 0.0150  0.0442  0.0396  66  TRP A CE3 
454   C CZ2 . TRP A  66  ? 0.6603 0.5993 0.8538 0.0150  0.0554  0.0446  66  TRP A CZ2 
455   C CZ3 . TRP A  66  ? 0.7087 0.6542 0.8769 0.0130  0.0489  0.0368  66  TRP A CZ3 
456   C CH2 . TRP A  66  ? 0.7031 0.6439 0.8822 0.0129  0.0546  0.0391  66  TRP A CH2 
457   N N   . ILE A  67  ? 0.5600 0.5055 0.7341 0.0187  0.0495  0.0375  67  ILE A N   
458   C CA  . ILE A  67  ? 0.7268 0.6673 0.8986 0.0174  0.0581  0.0334  67  ILE A CA  
459   C C   . ILE A  67  ? 0.7581 0.6960 0.9317 0.0185  0.0624  0.0324  67  ILE A C   
460   O O   . ILE A  67  ? 0.6737 0.6063 0.8530 0.0182  0.0700  0.0316  67  ILE A O   
461   C CB  . ILE A  67  ? 0.5508 0.4927 0.7077 0.0149  0.0588  0.0277  67  ILE A CB  
462   C CG1 . ILE A  67  ? 0.8501 0.7960 1.0030 0.0141  0.0527  0.0285  67  ILE A CG1 
463   C CG2 . ILE A  67  ? 0.6451 0.5815 0.8014 0.0129  0.0677  0.0240  67  ILE A CG2 
464   C CD1 . ILE A  67  ? 1.1156 1.0633 1.2544 0.0117  0.0529  0.0231  67  ILE A CD1 
465   N N   . LEU A  68  ? 0.5790 0.5205 0.7477 0.0197  0.0579  0.0322  68  LEU A N   
466   C CA  . LEU A  68  ? 0.6408 0.5801 0.8109 0.0208  0.0614  0.0314  68  LEU A CA  
467   C C   . LEU A  68  ? 0.7275 0.6639 0.9134 0.0227  0.0634  0.0363  68  LEU A C   
468   O O   . LEU A  68  ? 0.6714 0.6037 0.8616 0.0233  0.0694  0.0356  68  LEU A O   
469   C CB  . LEU A  68  ? 0.5755 0.5194 0.7372 0.0218  0.0559  0.0306  68  LEU A CB  
470   C CG  . LEU A  68  ? 0.6560 0.6023 0.8019 0.0202  0.0555  0.0253  68  LEU A CG  
471   C CD1 . LEU A  68  ? 0.6020 0.5523 0.7416 0.0216  0.0510  0.0251  68  LEU A CD1 
472   C CD2 . LEU A  68  ? 0.3733 0.3152 0.5151 0.0185  0.0639  0.0211  68  LEU A CD2 
473   N N   . GLY A  69  ? 0.7668 0.7055 0.9614 0.0237  0.0583  0.0413  69  GLY A N   
474   C CA  . GLY A  69  ? 0.7324 0.6693 0.9428 0.0255  0.0594  0.0465  69  GLY A CA  
475   C C   . GLY A  69  ? 0.8392 0.7796 1.0530 0.0274  0.0540  0.0493  69  GLY A C   
476   O O   . GLY A  69  ? 0.9183 0.8563 1.1414 0.0288  0.0570  0.0514  69  GLY A O   
477   N N   . ASN A  70  ? 0.8404 0.7861 1.0466 0.0272  0.0464  0.0493  70  ASN A N   
478   C CA  . ASN A  70  ? 0.9185 0.8677 1.1276 0.0287  0.0407  0.0520  70  ASN A CA  
479   C C   . ASN A  70  ? 1.0293 0.9784 1.2548 0.0300  0.0398  0.0580  70  ASN A C   
480   O O   . ASN A  70  ? 0.9881 0.9375 1.2201 0.0296  0.0387  0.0612  70  ASN A O   
481   C CB  . ASN A  70  ? 0.9179 0.8728 1.1177 0.0281  0.0326  0.0515  70  ASN A CB  
482   C CG  . ASN A  70  ? 0.9242 0.8824 1.1245 0.0293  0.0273  0.0531  70  ASN A CG  
483   O OD1 . ASN A  70  ? 0.8883 0.8467 1.1002 0.0304  0.0263  0.0572  70  ASN A OD1 
484   N ND2 . ASN A  70  ? 0.9744 0.9355 1.1625 0.0289  0.0240  0.0499  70  ASN A ND2 
485   N N   . PRO A  71  ? 1.1775 1.1261 1.4098 0.0316  0.0403  0.0598  71  PRO A N   
486   C CA  . PRO A  71  ? 1.0255 0.9743 1.2740 0.0328  0.0395  0.0657  71  PRO A CA  
487   C C   . PRO A  71  ? 1.0949 1.0486 1.3477 0.0324  0.0320  0.0701  71  PRO A C   
488   O O   . PRO A  71  ? 1.3260 1.2797 1.5920 0.0329  0.0322  0.0751  71  PRO A O   
489   C CB  . PRO A  71  ? 0.9651 0.9147 1.2154 0.0342  0.0385  0.0659  71  PRO A CB  
490   C CG  . PRO A  71  ? 1.1134 1.0602 1.3520 0.0339  0.0432  0.0602  71  PRO A CG  
491   C CD  . PRO A  71  ? 1.1549 1.1028 1.3803 0.0322  0.0419  0.0565  71  PRO A CD  
492   N N   . GLU A  72  ? 1.1090 1.0671 1.3510 0.0314  0.0256  0.0685  72  GLU A N   
493   C CA  . GLU A  72  ? 1.1829 1.1457 1.4274 0.0306  0.0183  0.0724  72  GLU A CA  
494   C C   . GLU A  72  ? 1.0675 1.0293 1.3116 0.0295  0.0195  0.0729  72  GLU A C   
495   O O   . GLU A  72  ? 1.0405 1.0045 1.2929 0.0294  0.0162  0.0777  72  GLU A O   
496   C CB  . GLU A  72  ? 1.1673 1.1347 1.4002 0.0298  0.0113  0.0704  72  GLU A CB  
497   C CG  . GLU A  72  ? 1.3209 1.2897 1.5551 0.0308  0.0092  0.0706  72  GLU A CG  
498   C CD  . GLU A  72  ? 1.4536 1.4229 1.7037 0.0318  0.0086  0.0761  72  GLU A CD  
499   O OE1 . GLU A  72  ? 1.3186 1.2901 1.5771 0.0314  0.0058  0.0807  72  GLU A OE1 
500   O OE2 . GLU A  72  ? 1.4128 1.3807 1.6671 0.0330  0.0110  0.0760  72  GLU A OE2 
501   N N   . CYS A  73  ? 1.2361 1.1948 1.4706 0.0287  0.0242  0.0679  73  CYS A N   
502   C CA  . CYS A  73  ? 1.3272 1.2848 1.5604 0.0275  0.0259  0.0677  73  CYS A CA  
503   C C   . CYS A  73  ? 1.4556 1.4086 1.7020 0.0281  0.0324  0.0706  73  CYS A C   
504   O O   . CYS A  73  ? 1.4503 1.3987 1.6942 0.0275  0.0392  0.0674  73  CYS A O   
505   C CB  . CYS A  73  ? 1.0196 0.9756 1.2378 0.0261  0.0287  0.0611  73  CYS A CB  
506   S SG  . CYS A  73  ? 1.1283 1.0894 1.3309 0.0254  0.0218  0.0575  73  CYS A SG  
507   N N   . GLU A  74  ? 1.7179 1.6721 1.9784 0.0294  0.0306  0.0766  74  GLU A N   
508   C CA  . GLU A  74  ? 1.8326 1.7825 2.1072 0.0305  0.0371  0.0798  74  GLU A CA  
509   C C   . GLU A  74  ? 1.9615 1.9117 2.2414 0.0299  0.0366  0.0833  74  GLU A C   
510   O O   . GLU A  74  ? 1.9216 1.8669 2.2048 0.0297  0.0435  0.0825  74  GLU A O   
511   C CB  . GLU A  74  ? 1.8856 1.8372 2.1741 0.0322  0.0354  0.0851  74  GLU A CB  
512   C CG  . GLU A  74  ? 1.9948 1.9408 2.2943 0.0336  0.0438  0.0858  74  GLU A CG  
513   C CD  . GLU A  74  ? 2.0575 2.0040 2.3606 0.0349  0.0437  0.0859  74  GLU A CD  
514   O OE1 . GLU A  74  ? 2.0127 1.9631 2.3077 0.0346  0.0377  0.0845  74  GLU A OE1 
515   O OE2 . GLU A  74  ? 2.0002 1.9427 2.3141 0.0361  0.0498  0.0874  74  GLU A OE2 
516   N N   . SER A  75  ? 1.8602 1.8160 2.1409 0.0296  0.0284  0.0872  75  SER A N   
517   C CA  . SER A  75  ? 2.0624 2.0194 2.3534 0.0296  0.0271  0.0930  75  SER A CA  
518   C C   . SER A  75  ? 2.1729 2.1321 2.4559 0.0280  0.0234  0.0926  75  SER A C   
519   O O   . SER A  75  ? 2.1714 2.1355 2.4573 0.0277  0.0164  0.0972  75  SER A O   
520   C CB  . SER A  75  ? 2.0510 2.0129 2.3546 0.0307  0.0212  0.1001  75  SER A CB  
521   O OG  . SER A  75  ? 1.9724 1.9403 2.2676 0.0297  0.0122  0.1001  75  SER A OG  
522   N N   . LEU A  76  ? 2.4027 2.3580 2.6762 0.0269  0.0282  0.0874  76  LEU A N   
523   C CA  . LEU A  76  ? 2.4114 2.3683 2.6769 0.0252  0.0255  0.0864  76  LEU A CA  
524   C C   . LEU A  76  ? 2.4389 2.3900 2.7025 0.0244  0.0336  0.0831  76  LEU A C   
525   O O   . LEU A  76  ? 2.4179 2.3691 2.6778 0.0232  0.0331  0.0829  76  LEU A O   
526   C CB  . LEU A  76  ? 2.2877 2.2476 2.5365 0.0238  0.0207  0.0812  76  LEU A CB  
527   C CG  . LEU A  76  ? 2.1158 2.0823 2.3607 0.0232  0.0110  0.0837  76  LEU A CG  
528   C CD1 . LEU A  76  ? 1.6309 1.5990 1.8592 0.0219  0.0085  0.0776  76  LEU A CD1 
529   C CD2 . LEU A  76  ? 2.1847 2.1527 2.4330 0.0224  0.0084  0.0879  76  LEU A CD2 
530   N N   . SER A  77  ? 2.3261 2.2721 2.5920 0.0250  0.0412  0.0801  77  SER A N   
531   C CA  . SER A  77  ? 2.1772 2.1177 2.4374 0.0236  0.0491  0.0749  77  SER A CA  
532   C C   . SER A  77  ? 2.2368 2.1718 2.5110 0.0245  0.0569  0.0779  77  SER A C   
533   O O   . SER A  77  ? 1.9873 1.9176 2.2655 0.0249  0.0641  0.0760  77  SER A O   
534   C CB  . SER A  77  ? 1.8153 1.7536 2.0659 0.0232  0.0528  0.0685  77  SER A CB  
535   O OG  . SER A  77  ? 1.6777 1.6137 1.9385 0.0249  0.0564  0.0704  77  SER A OG  
536   N N   . THR A  78  ? 2.8849 2.8207 3.1673 0.0247  0.0557  0.0830  78  THR A N   
537   C CA  . THR A  78  ? 2.7808 2.7107 3.0743 0.0251  0.0641  0.0849  78  THR A CA  
538   C C   . THR A  78  ? 2.7632 2.6923 3.0519 0.0234  0.0647  0.0840  78  THR A C   
539   O O   . THR A  78  ? 2.6571 2.5876 2.9542 0.0240  0.0625  0.0898  78  THR A O   
540   C CB  . THR A  78  ? 2.7283 2.6587 3.0410 0.0275  0.0641  0.0931  78  THR A CB  
541   O OG1 . THR A  78  ? 2.8628 2.7910 3.1848 0.0277  0.0673  0.0972  78  THR A OG1 
542   N N   . ALA A  79  ? 2.5485 2.4753 2.8234 0.0212  0.0679  0.0766  79  ALA A N   
543   C CA  . ALA A  79  ? 2.2067 2.1331 2.4737 0.0192  0.0679  0.0744  79  ALA A CA  
544   C C   . ALA A  79  ? 2.0125 1.9322 2.2751 0.0173  0.0777  0.0682  79  ALA A C   
545   O O   . ALA A  79  ? 1.8523 1.7676 2.1171 0.0175  0.0842  0.0656  79  ALA A O   
546   C CB  . ALA A  79  ? 2.0981 2.0299 2.3490 0.0178  0.0603  0.0706  79  ALA A CB  
547   N N   . SER A  80  ? 1.2121 1.1309 1.4680 0.0154  0.0787  0.0658  80  SER A N   
548   C CA  . SER A  80  ? 1.0692 0.9818 1.3203 0.0131  0.0878  0.0598  80  SER A CA  
549   C C   . SER A  80  ? 0.9552 0.8702 1.1899 0.0103  0.0852  0.0540  80  SER A C   
550   O O   . SER A  80  ? 0.8307 0.7423 1.0568 0.0079  0.0910  0.0474  80  SER A O   
551   C CB  . SER A  80  ? 1.2332 1.1411 1.4977 0.0136  0.0939  0.0640  80  SER A CB  
552   O OG  . SER A  80  ? 1.4240 1.3309 1.7048 0.0164  0.0950  0.0706  80  SER A OG  
553   N N   . SER A  81  ? 0.9000 0.8210 1.1304 0.0106  0.0762  0.0566  81  SER A N   
554   C CA  . SER A  81  ? 0.8451 0.7689 1.0609 0.0083  0.0729  0.0519  81  SER A CA  
555   C C   . SER A  81  ? 0.7797 0.7108 0.9915 0.0091  0.0621  0.0552  81  SER A C   
556   O O   . SER A  81  ? 0.6182 0.5518 0.8398 0.0112  0.0576  0.0619  81  SER A O   
557   C CB  . SER A  81  ? 0.8102 0.7302 1.0271 0.0065  0.0781  0.0511  81  SER A CB  
558   O OG  . SER A  81  ? 0.7900 0.7100 1.0197 0.0082  0.0766  0.0586  81  SER A OG  
559   N N   . TRP A  82  ? 0.6972 0.6316 0.8945 0.0072  0.0582  0.0506  82  TRP A N   
560   C CA  . TRP A  82  ? 0.5495 0.4904 0.7416 0.0075  0.0485  0.0530  82  TRP A CA  
561   C C   . TRP A  82  ? 0.5454 0.4884 0.7231 0.0051  0.0466  0.0477  82  TRP A C   
562   O O   . TRP A  82  ? 0.7274 0.6687 0.8959 0.0033  0.0508  0.0413  82  TRP A O   
563   C CB  . TRP A  82  ? 0.5665 0.5115 0.7571 0.0091  0.0429  0.0538  82  TRP A CB  
564   C CG  . TRP A  82  ? 0.6285 0.5728 0.8098 0.0084  0.0456  0.0475  82  TRP A CG  
565   C CD1 . TRP A  82  ? 0.6677 0.6151 0.8345 0.0069  0.0429  0.0421  82  TRP A CD1 
566   C CD2 . TRP A  82  ? 0.6288 0.5693 0.8148 0.0093  0.0515  0.0462  82  TRP A CD2 
567   N NE1 . TRP A  82  ? 0.5674 0.5134 0.7295 0.0067  0.0467  0.0377  82  TRP A NE1 
568   C CE2 . TRP A  82  ? 0.5987 0.5403 0.7721 0.0081  0.0520  0.0399  82  TRP A CE2 
569   C CE3 . TRP A  82  ? 0.5970 0.5334 0.7968 0.0109  0.0566  0.0498  82  TRP A CE3 
570   C CZ2 . TRP A  82  ? 0.6334 0.5721 0.8072 0.0084  0.0573  0.0372  82  TRP A CZ2 
571   C CZ3 . TRP A  82  ? 0.6392 0.5724 0.8394 0.0112  0.0620  0.0468  82  TRP A CZ3 
572   C CH2 . TRP A  82  ? 0.5084 0.4427 0.6955 0.0099  0.0623  0.0406  82  TRP A CH2 
573   N N   . SER A  83  ? 0.5131 0.4599 0.6889 0.0049  0.0403  0.0507  83  SER A N   
574   C CA  . SER A  83  ? 0.6243 0.5733 0.7872 0.0026  0.0380  0.0464  83  SER A CA  
575   C C   . SER A  83  ? 0.5650 0.5189 0.7157 0.0023  0.0327  0.0425  83  SER A C   
576   O O   . SER A  83  ? 0.6622 0.6169 0.8013 0.0003  0.0335  0.0367  83  SER A O   
577   C CB  . SER A  83  ? 0.6225 0.5737 0.7879 0.0025  0.0332  0.0512  83  SER A CB  
578   O OG  . SER A  83  ? 0.5367 0.4920 0.7078 0.0044  0.0261  0.0571  83  SER A OG  
579   N N   . TYR A  84  ? 0.5389 0.4959 0.6925 0.0042  0.0273  0.0458  84  TYR A N   
580   C CA  . TYR A  84  ? 0.5619 0.5232 0.7052 0.0042  0.0225  0.0426  84  TYR A CA  
581   C C   . TYR A  84  ? 0.5733 0.5358 0.7234 0.0065  0.0199  0.0459  84  TYR A C   
582   O O   . TYR A  84  ? 0.6585 0.6193 0.8212 0.0080  0.0211  0.0510  84  TYR A O   
583   C CB  . TYR A  84  ? 0.5592 0.5255 0.6941 0.0033  0.0153  0.0426  84  TYR A CB  
584   C CG  . TYR A  84  ? 0.5502 0.5190 0.6922 0.0043  0.0091  0.0493  84  TYR A CG  
585   C CD1 . TYR A  84  ? 0.4393 0.4123 0.5806 0.0053  0.0024  0.0516  84  TYR A CD1 
586   C CD2 . TYR A  84  ? 0.5637 0.5307 0.7131 0.0040  0.0102  0.0534  84  TYR A CD2 
587   C CE1 . TYR A  84  ? 0.4422 0.4179 0.5896 0.0059  -0.0034 0.0576  84  TYR A CE1 
588   C CE2 . TYR A  84  ? 0.4539 0.4238 0.6097 0.0048  0.0043  0.0598  84  TYR A CE2 
589   C CZ  . TYR A  84  ? 0.5098 0.4841 0.6643 0.0056  -0.0025 0.0618  84  TYR A CZ  
590   O OH  . TYR A  84  ? 0.4812 0.4586 0.6417 0.0060  -0.0084 0.0680  84  TYR A OH  
591   N N   . ILE A  85  ? 0.4665 0.4322 0.6086 0.0068  0.0165  0.0432  85  ILE A N   
592   C CA  . ILE A  85  ? 0.4836 0.4504 0.6310 0.0088  0.0143  0.0457  85  ILE A CA  
593   C C   . ILE A  85  ? 0.5013 0.4736 0.6455 0.0093  0.0056  0.0480  85  ILE A C   
594   O O   . ILE A  85  ? 0.5406 0.5160 0.6737 0.0081  0.0020  0.0449  85  ILE A O   
595   C CB  . ILE A  85  ? 0.5749 0.5403 0.7170 0.0090  0.0183  0.0408  85  ILE A CB  
596   C CG1 . ILE A  85  ? 0.5024 0.4621 0.6486 0.0084  0.0273  0.0387  85  ILE A CG1 
597   C CG2 . ILE A  85  ? 0.4449 0.4118 0.5919 0.0111  0.0156  0.0433  85  ILE A CG2 
598   C CD1 . ILE A  85  ? 0.5120 0.4703 0.6523 0.0083  0.0317  0.0338  85  ILE A CD1 
599   N N   . VAL A  86  ? 0.5286 0.5020 0.6827 0.0108  0.0024  0.0534  86  VAL A N   
600   C CA  . VAL A  86  ? 0.4790 0.4574 0.6309 0.0110  -0.0056 0.0558  86  VAL A CA  
601   C C   . VAL A  86  ? 0.5440 0.5234 0.6975 0.0125  -0.0068 0.0558  86  VAL A C   
602   O O   . VAL A  86  ? 0.5711 0.5481 0.7347 0.0139  -0.0037 0.0582  86  VAL A O   
603   C CB  . VAL A  86  ? 0.5704 0.5503 0.7318 0.0111  -0.0097 0.0625  86  VAL A CB  
604   C CG1 . VAL A  86  ? 0.3945 0.3796 0.5526 0.0109  -0.0180 0.0645  86  VAL A CG1 
605   C CG2 . VAL A  86  ? 0.5767 0.5555 0.7370 0.0097  -0.0084 0.0629  86  VAL A CG2 
606   N N   . GLU A  87  ? 0.6624 0.6451 0.8061 0.0122  -0.0111 0.0530  87  GLU A N   
607   C CA  . GLU A  87  ? 0.5335 0.5174 0.6775 0.0135  -0.0127 0.0528  87  GLU A CA  
608   C C   . GLU A  87  ? 0.6259 0.6144 0.7683 0.0131  -0.0206 0.0553  87  GLU A C   
609   O O   . GLU A  87  ? 0.8041 0.7952 0.9384 0.0117  -0.0244 0.0541  87  GLU A O   
610   C CB  . GLU A  87  ? 0.6495 0.6331 0.7828 0.0134  -0.0100 0.0468  87  GLU A CB  
611   C CG  . GLU A  87  ? 0.6719 0.6527 0.8090 0.0150  -0.0053 0.0458  87  GLU A CG  
612   C CD  . GLU A  87  ? 0.7900 0.7707 0.9161 0.0148  -0.0024 0.0400  87  GLU A CD  
613   O OE1 . GLU A  87  ? 0.8474 0.8247 0.9749 0.0152  0.0037  0.0381  87  GLU A OE1 
614   O OE2 . GLU A  87  ? 0.7797 0.7637 0.8955 0.0141  -0.0061 0.0376  87  GLU A OE2 
615   N N   . THR A  88  ? 0.7852 0.7747 0.9352 0.0142  -0.0229 0.0587  88  THR A N   
616   C CA  . THR A  88  ? 0.9157 0.9095 1.0640 0.0137  -0.0302 0.0608  88  THR A CA  
617   C C   . THR A  88  ? 0.9487 0.9439 1.0874 0.0139  -0.0315 0.0566  88  THR A C   
618   O O   . THR A  88  ? 1.0252 1.0184 1.1635 0.0152  -0.0275 0.0541  88  THR A O   
619   C CB  . THR A  88  ? 0.9710 0.9658 1.1321 0.0144  -0.0325 0.0665  88  THR A CB  
620   O OG1 . THR A  88  ? 1.0733 1.0662 1.2385 0.0161  -0.0292 0.0656  88  THR A OG1 
621   C CG2 . THR A  88  ? 0.7465 0.7396 0.9183 0.0146  -0.0305 0.0710  88  THR A CG2 
622   N N   . PRO A  89  ? 1.1743 1.1730 1.3052 0.0126  -0.0371 0.0558  89  PRO A N   
623   C CA  . PRO A  89  ? 1.2026 1.2028 1.3242 0.0128  -0.0386 0.0520  89  PRO A CA  
624   C C   . PRO A  89  ? 1.3101 1.3102 1.4374 0.0143  -0.0386 0.0531  89  PRO A C   
625   O O   . PRO A  89  ? 1.3618 1.3623 1.4829 0.0150  -0.0383 0.0500  89  PRO A O   
626   C CB  . PRO A  89  ? 1.0479 1.0518 1.1637 0.0110  -0.0451 0.0526  89  PRO A CB  
627   C CG  . PRO A  89  ? 1.1623 1.1662 1.2804 0.0098  -0.0457 0.0550  89  PRO A CG  
628   C CD  . PRO A  89  ? 1.2463 1.2476 1.3767 0.0109  -0.0421 0.0586  89  PRO A CD  
629   N N   . SER A  90  ? 1.3328 1.3324 1.4720 0.0148  -0.0388 0.0577  90  SER A N   
630   C CA  . SER A  90  ? 1.3296 1.3291 1.4753 0.0160  -0.0391 0.0592  90  SER A CA  
631   C C   . SER A  90  ? 1.4842 1.4800 1.6378 0.0178  -0.0327 0.0595  90  SER A C   
632   O O   . SER A  90  ? 1.6295 1.6248 1.7923 0.0188  -0.0324 0.0623  90  SER A O   
633   C CB  . SER A  90  ? 1.4690 1.4714 1.6228 0.0151  -0.0446 0.0644  90  SER A CB  
634   O OG  . SER A  90  ? 1.7649 1.7676 1.9245 0.0160  -0.0451 0.0656  90  SER A OG  
635   N N   . SER A  91  ? 1.3367 1.3295 1.4865 0.0181  -0.0274 0.0566  91  SER A N   
636   C CA  . SER A  91  ? 1.1725 1.1613 1.3285 0.0195  -0.0207 0.0562  91  SER A CA  
637   C C   . SER A  91  ? 1.3246 1.3123 1.4733 0.0205  -0.0177 0.0518  91  SER A C   
638   O O   . SER A  91  ? 1.3521 1.3405 1.4896 0.0200  -0.0174 0.0477  91  SER A O   
639   C CB  . SER A  91  ? 1.0881 1.0741 1.2450 0.0190  -0.0162 0.0557  91  SER A CB  
640   O OG  . SER A  91  ? 1.1143 1.1011 1.2591 0.0178  -0.0162 0.0515  91  SER A OG  
641   N N   . ASP A  92  ? 1.4756 1.4617 1.6308 0.0221  -0.0154 0.0528  92  ASP A N   
642   C CA  . ASP A  92  ? 1.5244 1.5095 1.6735 0.0232  -0.0126 0.0491  92  ASP A CA  
643   C C   . ASP A  92  ? 1.4004 1.3814 1.5565 0.0246  -0.0062 0.0493  92  ASP A C   
644   O O   . ASP A  92  ? 1.5100 1.4898 1.6615 0.0255  -0.0031 0.0464  92  ASP A O   
645   C CB  . ASP A  92  ? 1.7496 1.7376 1.8966 0.0235  -0.0175 0.0496  92  ASP A CB  
646   C CG  . ASP A  92  ? 1.8803 1.8719 2.0179 0.0221  -0.0230 0.0483  92  ASP A CG  
647   O OD1 . ASP A  92  ? 1.9127 1.9047 2.0429 0.0211  -0.0224 0.0459  92  ASP A OD1 
648   O OD2 . ASP A  92  ? 1.8987 1.8929 2.0364 0.0218  -0.0278 0.0495  92  ASP A OD2 
649   N N   . ASN A  93  ? 1.2967 1.2756 1.4641 0.0248  -0.0040 0.0527  93  ASN A N   
650   C CA  . ASN A  93  ? 1.3196 1.2942 1.4942 0.0260  0.0027  0.0528  93  ASN A CA  
651   C C   . ASN A  93  ? 1.1740 1.1453 1.3423 0.0254  0.0089  0.0487  93  ASN A C   
652   O O   . ASN A  93  ? 1.0191 0.9879 1.1924 0.0248  0.0124  0.0496  93  ASN A O   
653   C CB  . ASN A  93  ? 1.3122 1.2857 1.5018 0.0264  0.0032  0.0580  93  ASN A CB  
654   C CG  . ASN A  93  ? 1.3878 1.3640 1.5850 0.0271  -0.0016 0.0619  93  ASN A CG  
655   O OD1 . ASN A  93  ? 1.4445 1.4232 1.6484 0.0265  -0.0061 0.0661  93  ASN A OD1 
656   N ND2 . ASN A  93  ? 1.3865 1.3622 1.5826 0.0282  -0.0007 0.0605  93  ASN A ND2 
657   N N   . GLY A  94  ? 1.2110 1.1825 1.3684 0.0254  0.0104  0.0443  94  GLY A N   
658   C CA  . GLY A  94  ? 1.0571 1.0260 1.2074 0.0246  0.0161  0.0401  94  GLY A CA  
659   C C   . GLY A  94  ? 1.0065 0.9722 1.1572 0.0256  0.0218  0.0383  94  GLY A C   
660   O O   . GLY A  94  ? 0.9003 0.8627 1.0615 0.0265  0.0256  0.0405  94  GLY A O   
661   N N   . THR A  95  ? 0.8081 0.7750 0.9477 0.0256  0.0226  0.0344  95  THR A N   
662   C CA  . THR A  95  ? 0.8354 0.7996 0.9740 0.0265  0.0278  0.0326  95  THR A CA  
663   C C   . THR A  95  ? 0.8249 0.7900 0.9678 0.0285  0.0253  0.0349  95  THR A C   
664   O O   . THR A  95  ? 0.9564 0.9247 1.0921 0.0290  0.0216  0.0338  95  THR A O   
665   C CB  . THR A  95  ? 0.7734 0.7387 0.8983 0.0256  0.0297  0.0278  95  THR A CB  
666   O OG1 . THR A  95  ? 0.7378 0.7080 0.8542 0.0254  0.0237  0.0270  95  THR A OG1 
667   C CG2 . THR A  95  ? 0.7729 0.7359 0.8947 0.0236  0.0345  0.0251  95  THR A CG2 
668   N N   . CYS A  96  ? 0.8137 0.7761 0.9688 0.0295  0.0274  0.0380  96  CYS A N   
669   C CA  . CYS A  96  ? 0.8551 0.8181 1.0158 0.0312  0.0253  0.0404  96  CYS A CA  
670   C C   . CYS A  96  ? 0.8221 0.7841 0.9762 0.0322  0.0285  0.0377  96  CYS A C   
671   O O   . CYS A  96  ? 0.7654 0.7293 0.9187 0.0334  0.0255  0.0384  96  CYS A O   
672   C CB  . CYS A  96  ? 0.7955 0.7558 0.9713 0.0320  0.0273  0.0444  96  CYS A CB  
673   S SG  . CYS A  96  ? 0.9695 0.9239 1.1509 0.0315  0.0362  0.0436  96  CYS A SG  
674   N N   . TYR A  97  ? 0.7598 0.7188 0.9093 0.0317  0.0346  0.0346  97  TYR A N   
675   C CA  . TYR A  97  ? 0.7007 0.6593 0.8423 0.0324  0.0375  0.0319  97  TYR A CA  
676   C C   . TYR A  97  ? 0.7325 0.6946 0.8601 0.0313  0.0353  0.0285  97  TYR A C   
677   O O   . TYR A  97  ? 0.8733 0.8355 0.9961 0.0296  0.0366  0.0264  97  TYR A O   
678   C CB  . TYR A  97  ? 0.7517 0.7052 0.8955 0.0321  0.0456  0.0304  97  TYR A CB  
679   C CG  . TYR A  97  ? 0.7491 0.7017 0.8882 0.0333  0.0486  0.0288  97  TYR A CG  
680   C CD1 . TYR A  97  ? 0.8211 0.7707 0.9691 0.0349  0.0513  0.0309  97  TYR A CD1 
681   C CD2 . TYR A  97  ? 0.7725 0.7274 0.8985 0.0328  0.0488  0.0255  97  TYR A CD2 
682   C CE1 . TYR A  97  ? 0.7964 0.7450 0.9401 0.0360  0.0542  0.0297  97  TYR A CE1 
683   C CE2 . TYR A  97  ? 0.7666 0.7208 0.8882 0.0339  0.0515  0.0244  97  TYR A CE2 
684   C CZ  . TYR A  97  ? 0.7607 0.7116 0.8911 0.0355  0.0543  0.0265  97  TYR A CZ  
685   O OH  . TYR A  97  ? 0.7174 0.6674 0.8434 0.0366  0.0571  0.0255  97  TYR A OH  
686   N N   . PRO A  98  ? 0.6853 0.6505 0.8065 0.0325  0.0321  0.0280  98  PRO A N   
687   C CA  . PRO A  98  ? 0.5754 0.5446 0.6840 0.0318  0.0294  0.0253  98  PRO A CA  
688   C C   . PRO A  98  ? 0.7444 0.7128 0.8446 0.0303  0.0343  0.0216  98  PRO A C   
689   O O   . PRO A  98  ? 0.6748 0.6398 0.7760 0.0305  0.0400  0.0207  98  PRO A O   
690   C CB  . PRO A  98  ? 0.6599 0.6310 0.7654 0.0337  0.0275  0.0257  98  PRO A CB  
691   C CG  . PRO A  98  ? 0.7963 0.7655 0.9135 0.0350  0.0266  0.0291  98  PRO A CG  
692   C CD  . PRO A  98  ? 0.8010 0.7659 0.9272 0.0345  0.0313  0.0301  98  PRO A CD  
693   N N   . GLY A  99  ? 0.7502 0.7216 0.8420 0.0288  0.0323  0.0195  99  GLY A N   
694   C CA  . GLY A  99  ? 0.7192 0.6904 0.8023 0.0270  0.0365  0.0158  99  GLY A CA  
695   C C   . GLY A  99  ? 0.7869 0.7610 0.8638 0.0250  0.0339  0.0140  99  GLY A C   
696   O O   . GLY A  99  ? 0.7118 0.6878 0.7912 0.0250  0.0289  0.0157  99  GLY A O   
697   N N   . ASP A  100 ? 0.7958 0.7703 0.8644 0.0230  0.0374  0.0105  100 ASP A N   
698   C CA  . ASP A  100 ? 0.7031 0.6805 0.7651 0.0209  0.0354  0.0083  100 ASP A CA  
699   C C   . ASP A  100 ? 0.5968 0.5703 0.6628 0.0187  0.0397  0.0072  100 ASP A C   
700   O O   . ASP A  100 ? 0.5897 0.5592 0.6573 0.0179  0.0458  0.0059  100 ASP A O   
701   C CB  . ASP A  100 ? 0.7972 0.7784 0.8465 0.0200  0.0359  0.0050  100 ASP A CB  
702   C CG  . ASP A  100 ? 1.0567 1.0423 1.0989 0.0183  0.0324  0.0032  100 ASP A CG  
703   O OD1 . ASP A  100 ? 1.2639 1.2500 1.3101 0.0184  0.0285  0.0049  100 ASP A OD1 
704   O OD2 . ASP A  100 ? 0.9881 0.9766 1.0205 0.0168  0.0336  0.0002  100 ASP A OD2 
705   N N   . PHE A  101 ? 0.6001 0.5745 0.6679 0.0178  0.0366  0.0079  101 PHE A N   
706   C CA  . PHE A  101 ? 0.6308 0.6019 0.7020 0.0156  0.0404  0.0068  101 PHE A CA  
707   C C   . PHE A  101 ? 0.5352 0.5090 0.5953 0.0130  0.0411  0.0027  101 PHE A C   
708   O O   . PHE A  101 ? 0.5195 0.4969 0.5756 0.0124  0.0365  0.0025  101 PHE A O   
709   C CB  . PHE A  101 ? 0.4714 0.4418 0.5516 0.0161  0.0369  0.0103  101 PHE A CB  
710   C CG  . PHE A  101 ? 0.4765 0.4418 0.5650 0.0149  0.0418  0.0108  101 PHE A CG  
711   C CD1 . PHE A  101 ? 0.5283 0.4904 0.6296 0.0165  0.0423  0.0149  101 PHE A CD1 
712   C CD2 . PHE A  101 ? 0.6267 0.5905 0.7107 0.0123  0.0462  0.0074  101 PHE A CD2 
713   C CE1 . PHE A  101 ? 0.4798 0.4372 0.5894 0.0156  0.0471  0.0157  101 PHE A CE1 
714   C CE2 . PHE A  101 ? 0.4681 0.4269 0.5601 0.0113  0.0512  0.0079  101 PHE A CE2 
715   C CZ  . PHE A  101 ? 0.3905 0.3461 0.4955 0.0130  0.0517  0.0122  101 PHE A CZ  
716   N N   . ILE A  102 ? 0.4380 0.4101 0.4932 0.0112  0.0469  -0.0007 102 ILE A N   
717   C CA  . ILE A  102 ? 0.4860 0.4611 0.5302 0.0085  0.0478  -0.0048 102 ILE A CA  
718   C C   . ILE A  102 ? 0.4783 0.4525 0.5237 0.0063  0.0480  -0.0058 102 ILE A C   
719   O O   . ILE A  102 ? 0.5852 0.5544 0.6386 0.0056  0.0518  -0.0051 102 ILE A O   
720   C CB  . ILE A  102 ? 0.6240 0.5970 0.6631 0.0067  0.0545  -0.0082 102 ILE A CB  
721   C CG1 . ILE A  102 ? 0.6052 0.5781 0.6444 0.0090  0.0550  -0.0069 102 ILE A CG1 
722   C CG2 . ILE A  102 ? 0.4151 0.3924 0.4419 0.0038  0.0546  -0.0124 102 ILE A CG2 
723   C CD1 . ILE A  102 ? 0.5432 0.5223 0.5761 0.0109  0.0490  -0.0059 102 ILE A CD1 
724   N N   . ASP A  103 ? 0.5526 0.5317 0.5901 0.0052  0.0439  -0.0073 103 ASP A N   
725   C CA  . ASP A  103 ? 0.5096 0.4883 0.5471 0.0030  0.0437  -0.0083 103 ASP A CA  
726   C C   . ASP A  103 ? 0.5230 0.4985 0.5723 0.0044  0.0421  -0.0043 103 ASP A C   
727   O O   . ASP A  103 ? 0.5682 0.5398 0.6224 0.0029  0.0456  -0.0045 103 ASP A O   
728   C CB  . ASP A  103 ? 0.5588 0.5346 0.5932 -0.0003 0.0505  -0.0124 103 ASP A CB  
729   C CG  . ASP A  103 ? 0.6646 0.6444 0.6869 -0.0022 0.0518  -0.0165 103 ASP A CG  
730   O OD1 . ASP A  103 ? 0.8104 0.7961 0.8257 -0.0015 0.0466  -0.0166 103 ASP A OD1 
731   O OD2 . ASP A  103 ? 0.6966 0.6736 0.7165 -0.0044 0.0580  -0.0195 103 ASP A OD2 
732   N N   . TYR A  104 ? 0.5557 0.5328 0.6092 0.0072  0.0370  -0.0006 104 TYR A N   
733   C CA  . TYR A  104 ? 0.4326 0.4074 0.4973 0.0086  0.0348  0.0038  104 TYR A CA  
734   C C   . TYR A  104 ? 0.5336 0.5097 0.5981 0.0073  0.0317  0.0043  104 TYR A C   
735   O O   . TYR A  104 ? 0.4441 0.4167 0.5165 0.0068  0.0338  0.0060  104 TYR A O   
736   C CB  . TYR A  104 ? 0.3540 0.3308 0.4222 0.0115  0.0298  0.0072  104 TYR A CB  
737   C CG  . TYR A  104 ? 0.5058 0.4810 0.5850 0.0128  0.0269  0.0119  104 TYR A CG  
738   C CD1 . TYR A  104 ? 0.4684 0.4387 0.5582 0.0129  0.0311  0.0139  104 TYR A CD1 
739   C CD2 . TYR A  104 ? 0.4111 0.3899 0.4904 0.0139  0.0200  0.0144  104 TYR A CD2 
740   C CE1 . TYR A  104 ? 0.3996 0.3691 0.4999 0.0140  0.0282  0.0186  104 TYR A CE1 
741   C CE2 . TYR A  104 ? 0.4927 0.4707 0.5819 0.0148  0.0171  0.0188  104 TYR A CE2 
742   C CZ  . TYR A  104 ? 0.4504 0.4238 0.5501 0.0149  0.0210  0.0210  104 TYR A CZ  
743   O OH  . TYR A  104 ? 0.5989 0.5720 0.7087 0.0159  0.0179  0.0257  104 TYR A OH  
744   N N   . GLU A  105 ? 0.5519 0.5330 0.6077 0.0069  0.0270  0.0029  105 GLU A N   
745   C CA  . GLU A  105 ? 0.5213 0.5041 0.5759 0.0056  0.0238  0.0032  105 GLU A CA  
746   C C   . GLU A  105 ? 0.5797 0.5594 0.6341 0.0029  0.0291  0.0006  105 GLU A C   
747   O O   . GLU A  105 ? 0.5276 0.5059 0.5865 0.0021  0.0286  0.0021  105 GLU A O   
748   C CB  . GLU A  105 ? 0.5335 0.5222 0.5778 0.0053  0.0188  0.0014  105 GLU A CB  
749   C CG  . GLU A  105 ? 0.4999 0.4915 0.5439 0.0078  0.0136  0.0037  105 GLU A CG  
750   C CD  . GLU A  105 ? 0.7556 0.7471 0.7980 0.0092  0.0161  0.0028  105 GLU A CD  
751   O OE1 . GLU A  105 ? 0.8794 0.8710 0.9158 0.0078  0.0203  -0.0006 105 GLU A OE1 
752   O OE2 . GLU A  105 ? 0.7081 0.6995 0.7549 0.0115  0.0139  0.0056  105 GLU A OE2 
753   N N   . GLU A  106 ? 0.4782 0.4569 0.5273 0.0013  0.0344  -0.0033 106 GLU A N   
754   C CA  . GLU A  106 ? 0.3978 0.3732 0.4464 -0.0016 0.0403  -0.0063 106 GLU A CA  
755   C C   . GLU A  106 ? 0.4336 0.4027 0.4944 -0.0011 0.0446  -0.0036 106 GLU A C   
756   O O   . GLU A  106 ? 0.5072 0.4737 0.5717 -0.0025 0.0465  -0.0034 106 GLU A O   
757   C CB  . GLU A  106 ? 0.4988 0.4747 0.5389 -0.0035 0.0450  -0.0110 106 GLU A CB  
758   C CG  . GLU A  106 ? 0.6525 0.6342 0.6805 -0.0054 0.0423  -0.0146 106 GLU A CG  
759   C CD  . GLU A  106 ? 0.6659 0.6472 0.6918 -0.0082 0.0433  -0.0167 106 GLU A CD  
760   O OE1 . GLU A  106 ? 0.7211 0.6973 0.7518 -0.0099 0.0490  -0.0176 106 GLU A OE1 
761   O OE2 . GLU A  106 ? 0.5804 0.5666 0.6002 -0.0087 0.0387  -0.0174 106 GLU A OE2 
762   N N   . LEU A  107 ? 0.5354 0.5020 0.6025 0.0010  0.0462  -0.0015 107 LEU A N   
763   C CA  . LEU A  107 ? 0.5545 0.5154 0.6341 0.0018  0.0502  0.0016  107 LEU A CA  
764   C C   . LEU A  107 ? 0.5029 0.4639 0.5901 0.0027  0.0461  0.0059  107 LEU A C   
765   O O   . LEU A  107 ? 0.4897 0.4469 0.5836 0.0018  0.0497  0.0068  107 LEU A O   
766   C CB  . LEU A  107 ? 0.5028 0.4625 0.5881 0.0044  0.0506  0.0040  107 LEU A CB  
767   C CG  . LEU A  107 ? 0.6733 0.6266 0.7673 0.0044  0.0581  0.0044  107 LEU A CG  
768   C CD1 . LEU A  107 ? 0.5108 0.4630 0.6157 0.0075  0.0563  0.0093  107 LEU A CD1 
769   C CD2 . LEU A  107 ? 0.4931 0.4420 0.5923 0.0025  0.0631  0.0039  107 LEU A CD2 
770   N N   . ARG A  108 ? 0.3824 0.3479 0.4686 0.0044  0.0387  0.0085  108 ARG A N   
771   C CA  . ARG A  108 ? 0.5057 0.4721 0.5982 0.0051  0.0340  0.0128  108 ARG A CA  
772   C C   . ARG A  108 ? 0.5671 0.5334 0.6566 0.0028  0.0346  0.0113  108 ARG A C   
773   O O   . ARG A  108 ? 0.5067 0.4706 0.6044 0.0028  0.0351  0.0144  108 ARG A O   
774   C CB  . ARG A  108 ? 0.4963 0.4680 0.5853 0.0067  0.0261  0.0147  108 ARG A CB  
775   C CG  . ARG A  108 ? 0.4829 0.4548 0.5752 0.0091  0.0250  0.0165  108 ARG A CG  
776   C CD  . ARG A  108 ? 0.4812 0.4583 0.5677 0.0101  0.0180  0.0170  108 ARG A CD  
777   N NE  . ARG A  108 ? 0.5852 0.5645 0.6743 0.0102  0.0122  0.0202  108 ARG A NE  
778   C CZ  . ARG A  108 ? 0.5862 0.5657 0.6836 0.0117  0.0085  0.0248  108 ARG A CZ  
779   N NH1 . ARG A  108 ? 0.4551 0.4329 0.5594 0.0134  0.0100  0.0267  108 ARG A NH1 
780   N NH2 . ARG A  108 ? 0.5466 0.5283 0.6453 0.0113  0.0033  0.0275  108 ARG A NH2 
781   N N   . GLU A  109 ? 0.5549 0.5239 0.6329 0.0009  0.0346  0.0066  109 GLU A N   
782   C CA  . GLU A  109 ? 0.5432 0.5123 0.6171 -0.0016 0.0354  0.0046  109 GLU A CA  
783   C C   . GLU A  109 ? 0.5454 0.5086 0.6254 -0.0031 0.0430  0.0037  109 GLU A C   
784   O O   . GLU A  109 ? 0.4757 0.4372 0.5594 -0.0041 0.0436  0.0050  109 GLU A O   
785   C CB  . GLU A  109 ? 0.5483 0.5216 0.6088 -0.0035 0.0346  -0.0006 109 GLU A CB  
786   C CG  . GLU A  109 ? 0.7440 0.7180 0.7997 -0.0062 0.0351  -0.0030 109 GLU A CG  
787   C CD  . GLU A  109 ? 0.9030 0.8796 0.9597 -0.0055 0.0287  0.0002  109 GLU A CD  
788   O OE1 . GLU A  109 ? 1.0140 0.9914 1.0763 -0.0031 0.0243  0.0045  109 GLU A OE1 
789   O OE2 . GLU A  109 ? 0.9293 0.9072 0.9810 -0.0075 0.0282  -0.0018 109 GLU A OE2 
790   N N   . GLN A  110 ? 0.5159 0.4758 0.5968 -0.0035 0.0490  0.0016  110 GLN A N   
791   C CA  . GLN A  110 ? 0.6296 0.5835 0.7160 -0.0051 0.0570  0.0003  110 GLN A CA  
792   C C   . GLN A  110 ? 0.6073 0.5570 0.7083 -0.0031 0.0581  0.0059  110 GLN A C   
793   O O   . GLN A  110 ? 0.6012 0.5465 0.7082 -0.0041 0.0629  0.0064  110 GLN A O   
794   C CB  . GLN A  110 ? 0.6094 0.5609 0.6923 -0.0061 0.0631  -0.0036 110 GLN A CB  
795   C CG  . GLN A  110 ? 0.6483 0.6048 0.7175 -0.0074 0.0611  -0.0081 110 GLN A CG  
796   C CD  . GLN A  110 ? 0.7108 0.6658 0.7723 -0.0111 0.0673  -0.0140 110 GLN A CD  
797   O OE1 . GLN A  110 ? 0.8401 0.7900 0.9060 -0.0130 0.0734  -0.0151 110 GLN A OE1 
798   N NE2 . GLN A  110 ? 0.6862 0.6458 0.7361 -0.0124 0.0659  -0.0178 110 GLN A NE2 
799   N N   . LEU A  111 ? 0.6455 0.5967 0.7523 -0.0002 0.0537  0.0102  111 LEU A N   
800   C CA  . LEU A  111 ? 0.4935 0.4418 0.6146 0.0019  0.0541  0.0160  111 LEU A CA  
801   C C   . LEU A  111 ? 0.5092 0.4600 0.6339 0.0025  0.0482  0.0203  111 LEU A C   
802   O O   . LEU A  111 ? 0.5516 0.5003 0.6880 0.0039  0.0482  0.0254  111 LEU A O   
803   C CB  . LEU A  111 ? 0.4928 0.4418 0.6187 0.0046  0.0520  0.0187  111 LEU A CB  
804   C CG  . LEU A  111 ? 0.4357 0.3793 0.5697 0.0053  0.0590  0.0190  111 LEU A CG  
805   C CD1 . LEU A  111 ? 0.7109 0.6490 0.8472 0.0031  0.0675  0.0164  111 LEU A CD1 
806   C CD2 . LEU A  111 ? 0.5812 0.5260 0.7082 0.0057  0.0597  0.0158  111 LEU A CD2 
807   N N   . SER A  112 ? 0.4897 0.4451 0.6043 0.0014  0.0430  0.0183  112 SER A N   
808   C CA  . SER A  112 ? 0.5307 0.4890 0.6470 0.0019  0.0367  0.0222  112 SER A CA  
809   C C   . SER A  112 ? 0.5604 0.5150 0.6861 0.0015  0.0398  0.0253  112 SER A C   
810   O O   . SER A  112 ? 0.5801 0.5358 0.7132 0.0028  0.0356  0.0307  112 SER A O   
811   C CB  . SER A  112 ? 0.5872 0.5502 0.6907 0.0003  0.0324  0.0186  112 SER A CB  
812   O OG  . SER A  112 ? 0.5777 0.5388 0.6758 -0.0024 0.0372  0.0144  112 SER A OG  
813   N N   . SER A  113 ? 0.5674 0.5176 0.6928 -0.0004 0.0471  0.0219  113 SER A N   
814   C CA  . SER A  113 ? 0.5690 0.5149 0.7039 -0.0008 0.0512  0.0248  113 SER A CA  
815   C C   . SER A  113 ? 0.6384 0.5779 0.7781 -0.0016 0.0608  0.0224  113 SER A C   
816   O O   . SER A  113 ? 0.6945 0.6327 0.8256 -0.0039 0.0653  0.0164  113 SER A O   
817   C CB  . SER A  113 ? 0.8295 0.7766 0.9582 -0.0029 0.0499  0.0232  113 SER A CB  
818   O OG  . SER A  113 ? 0.7403 0.6838 0.8791 -0.0028 0.0529  0.0271  113 SER A OG  
819   N N   . VAL A  114 ? 0.6539 0.5895 0.8074 0.0000  0.0640  0.0272  114 VAL A N   
820   C CA  . VAL A  114 ? 0.7774 0.7066 0.9372 -0.0004 0.0733  0.0256  114 VAL A CA  
821   C C   . VAL A  114 ? 0.7835 0.7077 0.9548 -0.0004 0.0783  0.0291  114 VAL A C   
822   O O   . VAL A  114 ? 0.5622 0.4876 0.7431 0.0016  0.0745  0.0355  114 VAL A O   
823   C CB  . VAL A  114 ? 0.7516 0.6800 0.9181 0.0020  0.0737  0.0279  114 VAL A CB  
824   C CG1 . VAL A  114 ? 0.7898 0.7129 0.9725 0.0035  0.0792  0.0326  114 VAL A CG1 
825   C CG2 . VAL A  114 ? 0.6726 0.6001 0.8299 0.0006  0.0776  0.0217  114 VAL A CG2 
826   N N   . SER A  115 ? 0.8907 0.8095 1.0611 -0.0028 0.0869  0.0248  115 SER A N   
827   C CA  . SER A  115 ? 1.0157 0.9291 1.1971 -0.0029 0.0928  0.0276  115 SER A CA  
828   C C   . SER A  115 ? 1.0356 0.9447 1.2318 -0.0005 0.0974  0.0320  115 SER A C   
829   O O   . SER A  115 ? 1.0741 0.9833 1.2825 0.0019  0.0953  0.0390  115 SER A O   
830   C CB  . SER A  115 ? 1.0687 0.9776 1.2437 -0.0065 0.1008  0.0212  115 SER A CB  
831   O OG  . SER A  115 ? 1.0520 0.9575 1.2345 -0.0069 0.1040  0.0239  115 SER A OG  
832   N N   . SER A  116 ? 1.0661 0.9715 1.2612 -0.0012 0.1037  0.0281  116 SER A N   
833   C CA  . SER A  116 ? 1.0325 0.9343 1.2408 0.0012  0.1076  0.0319  116 SER A CA  
834   C C   . SER A  116 ? 1.0739 0.9782 1.2773 0.0021  0.1053  0.0300  116 SER A C   
835   O O   . SER A  116 ? 1.0982 1.0040 1.2882 0.0000  0.1052  0.0239  116 SER A O   
836   C CB  . SER A  116 ? 1.1213 1.0148 1.3363 -0.0002 0.1193  0.0297  116 SER A CB  
837   O OG  . SER A  116 ? 1.2451 1.1362 1.4485 -0.0033 0.1247  0.0218  116 SER A OG  
838   N N   . PHE A  117 ? 0.9535 0.8581 1.1681 0.0052  0.1035  0.0355  117 PHE A N   
839   C CA  . PHE A  117 ? 0.7695 0.6769 0.9808 0.0064  0.1004  0.0347  117 PHE A CA  
840   C C   . PHE A  117 ? 0.7391 0.6432 0.9653 0.0090  0.1039  0.0393  117 PHE A C   
841   O O   . PHE A  117 ? 0.8712 0.7773 1.1087 0.0116  0.0997  0.0462  117 PHE A O   
842   C CB  . PHE A  117 ? 0.6839 0.5991 0.8897 0.0077  0.0892  0.0372  117 PHE A CB  
843   C CG  . PHE A  117 ? 0.7542 0.6726 0.9526 0.0084  0.0856  0.0350  117 PHE A CG  
844   C CD1 . PHE A  117 ? 0.6902 0.6095 0.8977 0.0111  0.0837  0.0392  117 PHE A CD1 
845   C CD2 . PHE A  117 ? 0.8433 0.7643 1.0260 0.0064  0.0841  0.0289  117 PHE A CD2 
846   C CE1 . PHE A  117 ? 0.5869 0.5090 0.7877 0.0118  0.0806  0.0373  117 PHE A CE1 
847   C CE2 . PHE A  117 ? 0.6419 0.5660 0.8182 0.0072  0.0810  0.0272  117 PHE A CE2 
848   C CZ  . PHE A  117 ? 0.5855 0.5099 0.7707 0.0099  0.0793  0.0313  117 PHE A CZ  
849   N N   . GLU A  118 ? 0.8295 0.7285 1.0558 0.0083  0.1117  0.0356  118 GLU A N   
850   C CA  . GLU A  118 ? 0.9132 0.8089 1.1532 0.0107  0.1155  0.0395  118 GLU A CA  
851   C C   . GLU A  118 ? 0.7762 0.6723 1.0102 0.0109  0.1160  0.0362  118 GLU A C   
852   O O   . GLU A  118 ? 0.7990 0.6938 1.0207 0.0084  0.1194  0.0296  118 GLU A O   
853   C CB  . GLU A  118 ? 1.0647 0.9524 1.3151 0.0100  0.1263  0.0395  118 GLU A CB  
854   C CG  . GLU A  118 ? 1.1858 1.0677 1.4279 0.0069  0.1355  0.0319  118 GLU A CG  
855   C CD  . GLU A  118 ? 1.4857 1.3595 1.7409 0.0071  0.1463  0.0329  118 GLU A CD  
856   O OE1 . GLU A  118 ? 1.6830 1.5557 1.9539 0.0097  0.1466  0.0396  118 GLU A OE1 
857   O OE2 . GLU A  118 ? 1.4802 1.3488 1.7300 0.0047  0.1544  0.0270  118 GLU A OE2 
858   N N   . ARG A  119 ? 0.8080 0.7061 1.0508 0.0138  0.1126  0.0410  119 ARG A N   
859   C CA  . ARG A  119 ? 0.7452 0.6435 0.9838 0.0143  0.1130  0.0386  119 ARG A CA  
860   C C   . ARG A  119 ? 0.7166 0.6079 0.9656 0.0148  0.1226  0.0388  119 ARG A C   
861   O O   . ARG A  119 ? 1.0388 0.9285 1.3033 0.0171  0.1238  0.0446  119 ARG A O   
862   C CB  . ARG A  119 ? 0.7315 0.6361 0.9729 0.0170  0.1037  0.0433  119 ARG A CB  
863   C CG  . ARG A  119 ? 0.7685 0.6735 1.0059 0.0177  0.1039  0.0412  119 ARG A CG  
864   C CD  . ARG A  119 ? 0.9113 0.8216 1.1547 0.0205  0.0957  0.0466  119 ARG A CD  
865   N NE  . ARG A  119 ? 0.9869 0.8952 1.2484 0.0227  0.0976  0.0529  119 ARG A NE  
866   C CZ  . ARG A  119 ? 1.1828 1.0901 1.4530 0.0247  0.0988  0.0554  119 ARG A CZ  
867   N NH1 . ARG A  119 ? 1.3007 1.2065 1.5877 0.0266  0.1005  0.0614  119 ARG A NH1 
868   N NH2 . ARG A  119 ? 1.0348 0.9428 1.2974 0.0248  0.0983  0.0522  119 ARG A NH2 
869   N N   . PHE A  120 ? 0.7885 0.6758 1.0288 0.0125  0.1293  0.0324  120 PHE A N   
870   C CA  . PHE A  120 ? 0.7713 0.6516 1.0199 0.0126  0.1391  0.0317  120 PHE A CA  
871   C C   . PHE A  120 ? 0.8108 0.6913 1.0523 0.0127  0.1397  0.0285  120 PHE A C   
872   O O   . PHE A  120 ? 0.8350 0.7200 1.0622 0.0116  0.1349  0.0248  120 PHE A O   
873   C CB  . PHE A  120 ? 0.7689 0.6425 1.0149 0.0094  0.1488  0.0269  120 PHE A CB  
874   C CG  . PHE A  120 ? 0.7786 0.6527 1.0062 0.0058  0.1501  0.0190  120 PHE A CG  
875   C CD1 . PHE A  120 ? 0.8792 0.7493 1.1009 0.0039  0.1569  0.0138  120 PHE A CD1 
876   C CD2 . PHE A  120 ? 0.9549 0.8337 1.1713 0.0041  0.1444  0.0168  120 PHE A CD2 
877   C CE1 . PHE A  120 ? 0.8755 0.7466 1.0803 0.0005  0.1579  0.0068  120 PHE A CE1 
878   C CE2 . PHE A  120 ? 0.8367 0.7165 1.0366 0.0007  0.1454  0.0098  120 PHE A CE2 
879   C CZ  . PHE A  120 ? 0.8026 0.6787 0.9967 -0.0011 0.1521  0.0049  120 PHE A CZ  
880   N N   . GLU A  121 ? 0.8604 0.7364 1.1123 0.0140  0.1456  0.0301  121 GLU A N   
881   C CA  . GLU A  121 ? 0.7959 0.6713 1.0422 0.0141  0.1472  0.0273  121 GLU A CA  
882   C C   . GLU A  121 ? 0.8370 0.7078 1.0713 0.0104  0.1552  0.0196  121 GLU A C   
883   O O   . GLU A  121 ? 0.9830 0.8467 1.2229 0.0091  0.1649  0.0180  121 GLU A O   
884   C CB  . GLU A  121 ? 0.9336 0.8055 1.1957 0.0168  0.1510  0.0318  121 GLU A CB  
885   C CG  . GLU A  121 ? 1.0799 0.9530 1.3382 0.0179  0.1500  0.0307  121 GLU A CG  
886   C CD  . GLU A  121 ? 1.2484 1.1188 1.5233 0.0208  0.1526  0.0358  121 GLU A CD  
887   O OE1 . GLU A  121 ? 1.3340 1.2001 1.6228 0.0215  0.1580  0.0390  121 GLU A OE1 
888   O OE2 . GLU A  121 ? 1.1399 1.0127 1.4143 0.0224  0.1495  0.0368  121 GLU A OE2 
889   N N   . ILE A  122 ? 0.7926 0.6676 1.0103 0.0086  0.1511  0.0150  122 ILE A N   
890   C CA  . ILE A  122 ? 0.8786 0.7505 1.0833 0.0048  0.1576  0.0077  122 ILE A CA  
891   C C   . ILE A  122 ? 1.0182 0.8861 1.2226 0.0047  0.1637  0.0057  122 ILE A C   
892   O O   . ILE A  122 ? 1.0257 0.8875 1.2277 0.0019  0.1730  0.0013  122 ILE A O   
893   C CB  . ILE A  122 ? 0.8635 0.7419 1.0507 0.0029  0.1509  0.0038  122 ILE A CB  
894   C CG1 . ILE A  122 ? 0.7485 0.6243 0.9220 -0.0012 0.1574  -0.0036 122 ILE A CG1 
895   C CG2 . ILE A  122 ? 0.9359 0.8208 1.1197 0.0057  0.1420  0.0064  122 ILE A CG2 
896   C CD1 . ILE A  122 ? 0.6565 0.5389 0.8132 -0.0032 0.1513  -0.0075 122 ILE A CD1 
897   N N   . PHE A  123 ? 0.9946 0.8659 1.2013 0.0076  0.1586  0.0088  123 PHE A N   
898   C CA  . PHE A  123 ? 0.8385 0.7062 1.0466 0.0081  0.1639  0.0078  123 PHE A CA  
899   C C   . PHE A  123 ? 1.0633 0.9306 1.2878 0.0121  0.1622  0.0144  123 PHE A C   
900   O O   . PHE A  123 ? 1.0795 0.9523 1.3041 0.0146  0.1544  0.0175  123 PHE A O   
901   C CB  . PHE A  123 ? 0.9478 0.8199 1.1403 0.0074  0.1599  0.0043  123 PHE A CB  
902   C CG  . PHE A  123 ? 0.9277 0.8005 1.1038 0.0033  0.1619  -0.0023 123 PHE A CG  
903   C CD1 . PHE A  123 ? 0.8514 0.7315 1.0150 0.0027  0.1539  -0.0037 123 PHE A CD1 
904   C CD2 . PHE A  123 ? 0.9199 0.7862 1.0933 -0.0002 0.1719  -0.0071 123 PHE A CD2 
905   C CE1 . PHE A  123 ? 0.8655 0.7466 1.0143 -0.0011 0.1555  -0.0096 123 PHE A CE1 
906   C CE2 . PHE A  123 ? 0.9248 0.7920 1.0830 -0.0043 0.1736  -0.0133 123 PHE A CE2 
907   C CZ  . PHE A  123 ? 0.9412 0.8161 1.0872 -0.0048 0.1653  -0.0144 123 PHE A CZ  
908   N N   . PRO A  124 ? 1.2358 1.0967 1.4745 0.0127  0.1698  0.0165  124 PRO A N   
909   C CA  . PRO A  124 ? 1.1788 1.0390 1.4343 0.0163  0.1691  0.0229  124 PRO A CA  
910   C C   . PRO A  124 ? 1.2046 1.0661 1.4573 0.0178  0.1677  0.0227  124 PRO A C   
911   O O   . PRO A  124 ? 1.2143 1.0722 1.4588 0.0159  0.1737  0.0179  124 PRO A O   
912   C CB  . PRO A  124 ? 1.3494 1.2010 1.6166 0.0156  0.1802  0.0229  124 PRO A CB  
913   C CG  . PRO A  124 ? 1.3292 1.1786 1.5893 0.0123  0.1838  0.0188  124 PRO A CG  
914   C CD  . PRO A  124 ? 1.2444 1.0982 1.4845 0.0098  0.1796  0.0131  124 PRO A CD  
915   N N   . LYS A  125 ? 1.1819 1.0486 1.4413 0.0210  0.1599  0.0279  125 LYS A N   
916   C CA  . LYS A  125 ? 1.2138 1.0824 1.4700 0.0225  0.1574  0.0280  125 LYS A CA  
917   C C   . LYS A  125 ? 1.5191 1.3809 1.7795 0.0223  0.1669  0.0263  125 LYS A C   
918   O O   . LYS A  125 ? 1.4902 1.3520 1.7412 0.0218  0.1679  0.0232  125 LYS A O   
919   C CB  . LYS A  125 ? 1.1995 1.0734 1.4661 0.0260  0.1490  0.0345  125 LYS A CB  
920   C CG  . LYS A  125 ? 1.1617 1.0381 1.4251 0.0276  0.1460  0.0347  125 LYS A CG  
921   C CD  . LYS A  125 ? 1.1190 1.0023 1.3873 0.0301  0.1357  0.0398  125 LYS A CD  
922   C CE  . LYS A  125 ? 1.2351 1.1179 1.5229 0.0325  0.1354  0.0463  125 LYS A CE  
923   N NZ  . LYS A  125 ? 1.1071 0.9968 1.3993 0.0346  0.1254  0.0511  125 LYS A NZ  
924   N N   . THR A  126 ? 3.3856 3.2416 3.6602 0.0227  0.1741  0.0285  126 THR A N   
925   C CA  . THR A  126 ? 3.3016 3.1514 3.5842 0.0233  0.1823  0.0285  126 THR A CA  
926   C C   . THR A  126 ? 3.3206 3.1629 3.5967 0.0201  0.1935  0.0225  126 THR A C   
927   O O   . THR A  126 ? 3.3104 3.1482 3.5893 0.0203  0.1996  0.0216  126 THR A O   
928   C CB  . THR A  126 ? 1.7326 1.5807 2.0367 0.0262  0.1838  0.0352  126 THR A CB  
929   O OG1 . THR A  126 ? 1.7346 1.5819 2.0444 0.0255  0.1846  0.0368  126 THR A OG1 
930   C CG2 . THR A  126 ? 1.7174 1.5725 2.0275 0.0294  0.1739  0.0407  126 THR A CG2 
931   N N   . SER A  127 ? 1.4900 1.3308 1.7572 0.0169  0.1961  0.0182  127 SER A N   
932   C CA  . SER A  127 ? 1.3881 1.2216 1.6492 0.0133  0.2070  0.0123  127 SER A CA  
933   C C   . SER A  127 ? 1.3784 1.2142 1.6181 0.0098  0.2059  0.0056  127 SER A C   
934   O O   . SER A  127 ? 1.4608 1.2915 1.6924 0.0067  0.2139  0.0002  127 SER A O   
935   C CB  . SER A  127 ? 1.4999 1.3279 1.7703 0.0121  0.2136  0.0126  127 SER A CB  
936   O OG  . SER A  127 ? 1.3963 1.2290 1.6626 0.0115  0.2072  0.0131  127 SER A OG  
937   N N   . SER A  128 ? 1.4142 1.2578 1.6449 0.0103  0.1957  0.0061  128 SER A N   
938   C CA  . SER A  128 ? 1.2578 1.1048 1.4691 0.0071  0.1935  0.0004  128 SER A CA  
939   C C   . SER A  128 ? 1.1786 1.0293 1.3790 0.0076  0.1900  -0.0010 128 SER A C   
940   O O   . SER A  128 ? 1.0635 0.9144 1.2489 0.0045  0.1923  -0.0065 128 SER A O   
941   C CB  . SER A  128 ? 1.1389 0.9923 1.3461 0.0072  0.1850  0.0015  128 SER A CB  
942   O OG  . SER A  128 ? 1.0425 0.8922 1.2574 0.0060  0.1891  0.0019  128 SER A OG  
943   N N   . TRP A  129 ? 1.2075 1.0614 1.4155 0.0115  0.1844  0.0039  129 TRP A N   
944   C CA  . TRP A  129 ? 1.2505 1.1075 1.4496 0.0124  0.1813  0.0031  129 TRP A CA  
945   C C   . TRP A  129 ? 1.2506 1.1027 1.4599 0.0142  0.1869  0.0051  129 TRP A C   
946   O O   . TRP A  129 ? 1.1245 0.9789 1.3432 0.0178  0.1822  0.0100  129 TRP A O   
947   C CB  . TRP A  129 ? 1.2829 1.1483 1.4796 0.0150  0.1696  0.0065  129 TRP A CB  
948   C CG  . TRP A  129 ? 1.1351 1.0052 1.3259 0.0138  0.1637  0.0058  129 TRP A CG  
949   C CD1 . TRP A  129 ? 1.0882 0.9623 1.2867 0.0159  0.1566  0.0102  129 TRP A CD1 
950   C CD2 . TRP A  129 ? 0.9859 0.8572 1.1619 0.0101  0.1647  0.0004  129 TRP A CD2 
951   N NE1 . TRP A  129 ? 1.0589 0.9363 1.2482 0.0138  0.1532  0.0079  129 TRP A NE1 
952   C CE2 . TRP A  129 ? 0.9919 0.8678 1.1676 0.0103  0.1580  0.0019  129 TRP A CE2 
953   C CE3 . TRP A  129 ? 0.9575 0.8266 1.1203 0.0066  0.1704  -0.0055 129 TRP A CE3 
954   C CZ2 . TRP A  129 ? 1.0445 0.9228 1.2076 0.0071  0.1570  -0.0024 129 TRP A CZ2 
955   C CZ3 . TRP A  129 ? 0.9937 0.8655 1.1439 0.0033  0.1692  -0.0097 129 TRP A CZ3 
956   C CH2 . TRP A  129 ? 1.0808 0.9571 1.2314 0.0037  0.1626  -0.0081 129 TRP A CH2 
957   N N   . PRO A  130 ? 1.3872 1.2324 1.5941 0.0117  0.1970  0.0011  130 PRO A N   
958   C CA  . PRO A  130 ? 1.3069 1.1464 1.5231 0.0130  0.2037  0.0024  130 PRO A CA  
959   C C   . PRO A  130 ? 1.3731 1.2144 1.5797 0.0135  0.2026  0.0010  130 PRO A C   
960   O O   . PRO A  130 ? 1.4668 1.3052 1.6820 0.0156  0.2055  0.0034  130 PRO A O   
961   C CB  . PRO A  130 ? 1.3673 1.1985 1.5835 0.0095  0.2154  -0.0020 130 PRO A CB  
962   C CG  . PRO A  130 ? 1.3353 1.1687 1.5351 0.0055  0.2147  -0.0073 130 PRO A CG  
963   C CD  . PRO A  130 ? 1.4443 1.2864 1.6398 0.0071  0.2031  -0.0050 130 PRO A CD  
964   N N   . ASN A  131 ? 1.5136 1.3596 1.7029 0.0115  0.1987  -0.0026 131 ASN A N   
965   C CA  . ASN A  131 ? 1.5758 1.4236 1.7547 0.0117  0.1978  -0.0040 131 ASN A CA  
966   C C   . ASN A  131 ? 1.3400 1.1960 1.5159 0.0148  0.1868  -0.0007 131 ASN A C   
967   O O   . ASN A  131 ? 1.2187 1.0780 1.3828 0.0147  0.1842  -0.0022 131 ASN A O   
968   C CB  . ASN A  131 ? 1.5686 1.4158 1.7296 0.0073  0.2020  -0.0104 131 ASN A CB  
969   C CG  . ASN A  131 ? 1.6795 1.5191 1.8419 0.0036  0.2123  -0.0143 131 ASN A CG  
970   O OD1 . ASN A  131 ? 1.6842 1.5198 1.8601 0.0042  0.2154  -0.0123 131 ASN A OD1 
971   N ND2 . ASN A  131 ? 1.7109 1.5485 1.8593 -0.0005 0.2179  -0.0199 131 ASN A ND2 
972   N N   . HIS A  132 ? 1.0774 0.9366 1.2640 0.0173  0.1804  0.0038  132 HIS A N   
973   C CA  . HIS A  132 ? 0.9243 0.7911 1.1086 0.0200  0.1698  0.0068  132 HIS A CA  
974   C C   . HIS A  132 ? 0.9833 0.8512 1.1847 0.0233  0.1656  0.0128  132 HIS A C   
975   O O   . HIS A  132 ? 1.1450 1.0090 1.3583 0.0232  0.1693  0.0144  132 HIS A O   
976   C CB  . HIS A  132 ? 0.9785 0.8509 1.1505 0.0181  0.1640  0.0045  132 HIS A CB  
977   C CG  . HIS A  132 ? 1.0268 0.8985 1.1827 0.0143  0.1683  -0.0014 132 HIS A CG  
978   N ND1 . HIS A  132 ? 1.0469 0.9233 1.1885 0.0138  0.1649  -0.0034 132 HIS A ND1 
979   C CD2 . HIS A  132 ? 0.9360 0.8029 1.0880 0.0106  0.1760  -0.0057 132 HIS A CD2 
980   C CE1 . HIS A  132 ? 0.9989 0.8738 1.1283 0.0100  0.1699  -0.0085 132 HIS A CE1 
981   N NE2 . HIS A  132 ? 0.8454 0.7145 0.9806 0.0078  0.1767  -0.0102 132 HIS A NE2 
982   N N   . ASP A  133 ? 0.8850 0.7581 1.0877 0.0261  0.1578  0.0161  133 ASP A N   
983   C CA  . ASP A  133 ? 1.0018 0.8768 1.2198 0.0290  0.1529  0.0217  133 ASP A CA  
984   C C   . ASP A  133 ? 1.0163 0.8964 1.2339 0.0289  0.1456  0.0232  133 ASP A C   
985   O O   . ASP A  133 ? 0.9152 0.8009 1.1214 0.0286  0.1390  0.0220  133 ASP A O   
986   C CB  . ASP A  133 ? 1.0180 0.8961 1.2382 0.0319  0.1482  0.0246  133 ASP A CB  
987   C CG  . ASP A  133 ? 1.2922 1.1710 1.5299 0.0346  0.1452  0.0304  133 ASP A CG  
988   O OD1 . ASP A  133 ? 1.2298 1.1111 1.4738 0.0349  0.1408  0.0329  133 ASP A OD1 
989   O OD2 . ASP A  133 ? 1.3968 1.2737 1.6420 0.0364  0.1471  0.0324  133 ASP A OD2 
990   N N   . SER A  134 ? 1.0102 0.8882 1.2403 0.0291  0.1470  0.0259  134 SER A N   
991   C CA  . SER A  134 ? 0.9517 0.8340 1.1824 0.0289  0.1406  0.0275  134 SER A CA  
992   C C   . SER A  134 ? 0.9745 0.8603 1.2190 0.0318  0.1340  0.0337  134 SER A C   
993   O O   . SER A  134 ? 1.1142 1.0017 1.3656 0.0319  0.1311  0.0365  134 SER A O   
994   C CB  . SER A  134 ? 1.0120 0.8899 1.2455 0.0267  0.1468  0.0258  134 SER A CB  
995   O OG  . SER A  134 ? 1.2005 1.0722 1.4485 0.0274  0.1543  0.0279  134 SER A OG  
996   N N   . ASN A  135 ? 1.0046 0.8918 1.2530 0.0339  0.1318  0.0360  135 ASN A N   
997   C CA  . ASN A  135 ? 1.1527 1.0433 1.4146 0.0365  0.1260  0.0418  135 ASN A CA  
998   C C   . ASN A  135 ? 1.1521 1.0484 1.4084 0.0379  0.1179  0.0428  135 ASN A C   
999   O O   . ASN A  135 ? 1.2799 1.1809 1.5429 0.0392  0.1107  0.0468  135 ASN A O   
1000  C CB  . ASN A  135 ? 1.2801 1.1658 1.5578 0.0379  0.1322  0.0448  135 ASN A CB  
1001  C CG  . ASN A  135 ? 1.2256 1.1057 1.5119 0.0369  0.1397  0.0449  135 ASN A CG  
1002  O OD1 . ASN A  135 ? 1.0199 0.9015 1.3089 0.0363  0.1374  0.0463  135 ASN A OD1 
1003  N ND2 . ASN A  135 ? 1.0835 0.9570 1.3742 0.0366  0.1490  0.0434  135 ASN A ND2 
1004  N N   . LYS A  136 ? 1.0535 0.9497 1.2978 0.0375  0.1192  0.0392  136 LYS A N   
1005  C CA  . LYS A  136 ? 1.2287 1.1296 1.4677 0.0390  0.1126  0.0399  136 LYS A CA  
1006  C C   . LYS A  136 ? 1.2228 1.1295 1.4492 0.0381  0.1052  0.0384  136 LYS A C   
1007  O O   . LYS A  136 ? 1.1930 1.1038 1.4133 0.0391  0.0999  0.0384  136 LYS A O   
1008  C CB  . LYS A  136 ? 1.3613 1.2594 1.5935 0.0392  0.1174  0.0372  136 LYS A CB  
1009  C CG  . LYS A  136 ? 1.4282 1.3204 1.6722 0.0400  0.1250  0.0385  136 LYS A CG  
1010  C CD  . LYS A  136 ? 1.4758 1.3684 1.7220 0.0420  0.1241  0.0400  136 LYS A CD  
1011  C CE  . LYS A  136 ? 1.7632 1.6516 2.0261 0.0434  0.1291  0.0432  136 LYS A CE  
1012  N NZ  . LYS A  136 ? 1.7790 1.6692 2.0561 0.0441  0.1256  0.0477  136 LYS A NZ  
1013  N N   . GLY A  137 ? 1.0548 0.9617 1.2777 0.0363  0.1052  0.0369  137 GLY A N   
1014  C CA  . GLY A  137 ? 0.9723 0.8843 1.1828 0.0352  0.0991  0.0349  137 GLY A CA  
1015  C C   . GLY A  137 ? 0.9414 0.8587 1.1568 0.0361  0.0905  0.0387  137 GLY A C   
1016  O O   . GLY A  137 ? 1.0010 0.9197 1.2163 0.0350  0.0883  0.0390  137 GLY A O   
1017  N N   . VAL A  138 ? 0.7613 0.6815 0.9807 0.0380  0.0857  0.0414  138 VAL A N   
1018  C CA  . VAL A  138 ? 0.8682 0.7936 1.0915 0.0386  0.0772  0.0448  138 VAL A CA  
1019  C C   . VAL A  138 ? 0.8719 0.8018 1.0860 0.0393  0.0713  0.0440  138 VAL A C   
1020  O O   . VAL A  138 ? 0.9224 0.8512 1.1290 0.0397  0.0740  0.0415  138 VAL A O   
1021  C CB  . VAL A  138 ? 0.9583 0.8832 1.1989 0.0400  0.0765  0.0500  138 VAL A CB  
1022  C CG1 . VAL A  138 ? 1.0388 0.9591 1.2894 0.0395  0.0828  0.0511  138 VAL A CG1 
1023  C CG2 . VAL A  138 ? 0.9921 0.9158 1.2371 0.0417  0.0781  0.0509  138 VAL A CG2 
1024  N N   . THR A  139 ? 0.7452 0.6800 0.9600 0.0395  0.0635  0.0462  139 THR A N   
1025  C CA  . THR A  139 ? 0.8648 0.8039 1.0711 0.0400  0.0578  0.0454  139 THR A CA  
1026  C C   . THR A  139 ? 0.9444 0.8880 1.1567 0.0403  0.0500  0.0490  139 THR A C   
1027  O O   . THR A  139 ? 0.8891 0.8337 1.1087 0.0396  0.0480  0.0516  139 THR A O   
1028  C CB  . THR A  139 ? 0.9789 0.9201 1.1694 0.0387  0.0567  0.0413  139 THR A CB  
1029  O OG1 . THR A  139 ? 0.8141 0.7597 0.9975 0.0393  0.0507  0.0411  139 THR A OG1 
1030  C CG2 . THR A  139 ? 1.0027 0.9449 1.1924 0.0370  0.0551  0.0412  139 THR A CG2 
1031  N N   . ALA A  140 ? 1.1021 1.0485 1.3113 0.0411  0.0458  0.0493  140 ALA A N   
1032  C CA  . ALA A  140 ? 1.0766 1.0274 1.2900 0.0411  0.0383  0.0522  140 ALA A CA  
1033  C C   . ALA A  140 ? 1.0892 1.0438 1.2938 0.0396  0.0331  0.0511  140 ALA A C   
1034  O O   . ALA A  140 ? 1.0473 1.0056 1.2551 0.0391  0.0269  0.0535  140 ALA A O   
1035  C CB  . ALA A  140 ? 1.1531 1.1054 1.3650 0.0422  0.0360  0.0523  140 ALA A CB  
1036  N N   . ALA A  141 ? 1.0787 1.0326 1.2723 0.0389  0.0357  0.0474  141 ALA A N   
1037  C CA  . ALA A  141 ? 1.0330 0.9901 1.2174 0.0375  0.0314  0.0459  141 ALA A CA  
1038  C C   . ALA A  141 ? 1.0321 0.9893 1.2230 0.0363  0.0305  0.0479  141 ALA A C   
1039  O O   . ALA A  141 ? 1.0556 1.0163 1.2438 0.0353  0.0250  0.0487  141 ALA A O   
1040  C CB  . ALA A  141 ? 1.0026 0.9591 1.1737 0.0370  0.0347  0.0413  141 ALA A CB  
1041  N N   . CYS A  142 ? 0.8645 0.8176 1.0641 0.0364  0.0361  0.0490  142 CYS A N   
1042  C CA  . CYS A  142 ? 0.9587 0.9113 1.1656 0.0355  0.0362  0.0513  142 CYS A CA  
1043  C C   . CYS A  142 ? 0.9705 0.9225 1.1937 0.0365  0.0361  0.0563  142 CYS A C   
1044  O O   . CYS A  142 ? 0.8754 0.8233 1.1072 0.0368  0.0419  0.0574  142 CYS A O   
1045  C CB  . CYS A  142 ? 1.0768 1.0252 1.2805 0.0346  0.0432  0.0484  142 CYS A CB  
1046  S SG  . CYS A  142 ? 1.2646 1.2141 1.4496 0.0332  0.0437  0.0425  142 CYS A SG  
1047  N N   . PRO A  143 ? 1.0078 0.9637 1.2353 0.0367  0.0295  0.0594  143 PRO A N   
1048  C CA  . PRO A  143 ? 1.0518 1.0082 1.2944 0.0376  0.0284  0.0643  143 PRO A CA  
1049  C C   . PRO A  143 ? 1.1752 1.1320 1.4286 0.0371  0.0278  0.0684  143 PRO A C   
1050  O O   . PRO A  143 ? 1.2559 1.2156 1.5058 0.0359  0.0233  0.0690  143 PRO A O   
1051  C CB  . PRO A  143 ? 1.1427 1.1040 1.3832 0.0374  0.0208  0.0654  143 PRO A CB  
1052  C CG  . PRO A  143 ? 1.1349 1.0973 1.3595 0.0370  0.0194  0.0608  143 PRO A CG  
1053  C CD  . PRO A  143 ? 1.1087 1.0693 1.3263 0.0361  0.0227  0.0581  143 PRO A CD  
1054  N N   . HIS A  144 ? 1.2735 1.2273 1.5402 0.0381  0.0323  0.0713  144 HIS A N   
1055  C CA  . HIS A  144 ? 1.4612 1.4159 1.7406 0.0380  0.0313  0.0763  144 HIS A CA  
1056  C C   . HIS A  144 ? 1.5819 1.5393 1.8746 0.0389  0.0280  0.0813  144 HIS A C   
1057  O O   . HIS A  144 ? 1.5329 1.4874 1.8354 0.0401  0.0327  0.0826  144 HIS A O   
1058  C CB  . HIS A  144 ? 1.3646 1.3138 1.6499 0.0384  0.0395  0.0761  144 HIS A CB  
1059  C CG  . HIS A  144 ? 1.4481 1.3982 1.7411 0.0378  0.0386  0.0799  144 HIS A CG  
1060  N ND1 . HIS A  144 ? 1.4991 1.4459 1.8061 0.0387  0.0439  0.0833  144 HIS A ND1 
1061  C CD2 . HIS A  144 ? 1.4700 1.4237 1.7589 0.0366  0.0330  0.0809  144 HIS A CD2 
1062  C CE1 . HIS A  144 ? 1.5314 1.4799 1.8427 0.0381  0.0416  0.0864  144 HIS A CE1 
1063  N NE2 . HIS A  144 ? 1.5042 1.4568 1.8045 0.0368  0.0350  0.0850  144 HIS A NE2 
1064  N N   . ALA A  145 ? 1.3446 1.3077 1.6373 0.0379  0.0199  0.0838  145 ALA A N   
1065  C CA  . ALA A  145 ? 1.4126 1.3792 1.7166 0.0382  0.0156  0.0883  145 ALA A CA  
1066  C C   . ALA A  145 ? 1.4766 1.4413 1.7812 0.0394  0.0183  0.0865  145 ALA A C   
1067  O O   . ALA A  145 ? 1.3768 1.3391 1.6931 0.0407  0.0226  0.0888  145 ALA A O   
1068  C CB  . ALA A  145 ? 1.2328 1.1994 1.5535 0.0388  0.0171  0.0941  145 ALA A CB  
1069  N N   . GLY A  146 ? 1.6277 1.5933 1.9196 0.0390  0.0160  0.0825  146 GLY A N   
1070  C CA  . GLY A  146 ? 1.6108 1.5748 1.9021 0.0401  0.0182  0.0807  146 GLY A CA  
1071  C C   . GLY A  146 ? 1.5930 1.5509 1.8810 0.0413  0.0268  0.0772  146 GLY A C   
1072  O O   . GLY A  146 ? 1.5971 1.5537 1.8749 0.0417  0.0283  0.0733  146 GLY A O   
1073  N N   . ALA A  147 ? 1.4475 1.4019 1.7443 0.0419  0.0325  0.0788  147 ALA A N   
1074  C CA  . ALA A  147 ? 1.4485 1.3967 1.7432 0.0428  0.0412  0.0757  147 ALA A CA  
1075  C C   . ALA A  147 ? 1.3864 1.3330 1.6649 0.0421  0.0432  0.0703  147 ALA A C   
1076  O O   . ALA A  147 ? 1.3216 1.2707 1.5933 0.0408  0.0394  0.0696  147 ALA A O   
1077  C CB  . ALA A  147 ? 1.4388 1.3836 1.7467 0.0434  0.0468  0.0786  147 ALA A CB  
1078  N N   . LYS A  148 ? 1.1612 1.1037 1.4336 0.0427  0.0491  0.0666  148 LYS A N   
1079  C CA  . LYS A  148 ? 1.1550 1.0958 1.4124 0.0419  0.0518  0.0615  148 LYS A CA  
1080  C C   . LYS A  148 ? 1.2034 1.1404 1.4621 0.0411  0.0576  0.0606  148 LYS A C   
1081  O O   . LYS A  148 ? 1.0755 1.0078 1.3423 0.0417  0.0644  0.0611  148 LYS A O   
1082  C CB  . LYS A  148 ? 1.0502 0.9884 1.3007 0.0427  0.0559  0.0583  148 LYS A CB  
1083  C CG  . LYS A  148 ? 1.1900 1.1313 1.4383 0.0436  0.0510  0.0588  148 LYS A CG  
1084  C CD  . LYS A  148 ? 1.2821 1.2206 1.5230 0.0445  0.0556  0.0555  148 LYS A CD  
1085  C CE  . LYS A  148 ? 1.2480 1.1810 1.4974 0.0453  0.0636  0.0559  148 LYS A CE  
1086  N NZ  . LYS A  148 ? 1.2400 1.1700 1.4815 0.0460  0.0685  0.0528  148 LYS A NZ  
1087  N N   . SER A  149 ? 1.2554 1.1941 1.5059 0.0397  0.0552  0.0589  149 SER A N   
1088  C CA  . SER A  149 ? 1.1284 1.0639 1.3799 0.0386  0.0600  0.0581  149 SER A CA  
1089  C C   . SER A  149 ? 1.0579 0.9930 1.2933 0.0371  0.0613  0.0528  149 SER A C   
1090  O O   . SER A  149 ? 0.8861 0.8222 1.1108 0.0372  0.0607  0.0497  149 SER A O   
1091  C CB  . SER A  149 ? 1.1112 1.0496 1.3708 0.0382  0.0553  0.0623  149 SER A CB  
1092  O OG  . SER A  149 ? 1.2396 1.1743 1.5034 0.0375  0.0607  0.0623  149 SER A OG  
1093  N N   . PHE A  150 ? 1.1002 1.0341 1.3342 0.0357  0.0632  0.0519  150 PHE A N   
1094  C CA  . PHE A  150 ? 0.9607 0.8942 1.1802 0.0340  0.0650  0.0468  150 PHE A CA  
1095  C C   . PHE A  150 ? 0.8717 0.8052 1.0917 0.0325  0.0648  0.0471  150 PHE A C   
1096  O O   . PHE A  150 ? 0.9152 0.8487 1.1469 0.0330  0.0636  0.0513  150 PHE A O   
1097  C CB  . PHE A  150 ? 0.8313 0.7595 1.0472 0.0337  0.0736  0.0431  150 PHE A CB  
1098  C CG  . PHE A  150 ? 0.7645 0.6931 0.9643 0.0320  0.0749  0.0377  150 PHE A CG  
1099  C CD1 . PHE A  150 ? 0.7075 0.6403 0.8959 0.0322  0.0700  0.0359  150 PHE A CD1 
1100  C CD2 . PHE A  150 ? 0.7314 0.6562 0.9275 0.0300  0.0813  0.0345  150 PHE A CD2 
1101  C CE1 . PHE A  150 ? 0.6125 0.5462 0.7865 0.0306  0.0711  0.0313  150 PHE A CE1 
1102  C CE2 . PHE A  150 ? 0.7451 0.6707 0.9263 0.0282  0.0824  0.0296  150 PHE A CE2 
1103  C CZ  . PHE A  150 ? 0.6555 0.5858 0.8258 0.0286  0.0772  0.0281  150 PHE A CZ  
1104  N N   . TYR A  151 ? 0.9091 0.8427 1.1165 0.0308  0.0660  0.0426  151 TYR A N   
1105  C CA  . TYR A  151 ? 0.8181 0.7512 1.0250 0.0291  0.0666  0.0423  151 TYR A CA  
1106  C C   . TYR A  151 ? 0.7669 0.6941 0.9850 0.0290  0.0743  0.0435  151 TYR A C   
1107  O O   . TYR A  151 ? 0.6703 0.5931 0.8896 0.0291  0.0811  0.0416  151 TYR A O   
1108  C CB  . TYR A  151 ? 0.8209 0.7548 1.0121 0.0271  0.0674  0.0368  151 TYR A CB  
1109  C CG  . TYR A  151 ? 0.6271 0.5665 0.8068 0.0273  0.0606  0.0353  151 TYR A CG  
1110  C CD1 . TYR A  151 ? 0.6653 0.6095 0.8431 0.0271  0.0531  0.0371  151 TYR A CD1 
1111  C CD2 . TYR A  151 ? 0.6051 0.5447 0.7759 0.0275  0.0619  0.0323  151 TYR A CD2 
1112  C CE1 . TYR A  151 ? 0.6478 0.5967 0.8155 0.0273  0.0473  0.0357  151 TYR A CE1 
1113  C CE2 . TYR A  151 ? 0.5937 0.5382 0.7546 0.0279  0.0560  0.0311  151 TYR A CE2 
1114  C CZ  . TYR A  151 ? 0.6713 0.6203 0.8308 0.0277  0.0488  0.0328  151 TYR A CZ  
1115  O OH  . TYR A  151 ? 0.6037 0.5573 0.7536 0.0280  0.0434  0.0316  151 TYR A OH  
1116  N N   . LYS A  152 ? 0.8401 0.7672 1.0664 0.0288  0.0734  0.0467  152 LYS A N   
1117  C CA  . LYS A  152 ? 0.8846 0.8062 1.1228 0.0288  0.0807  0.0484  152 LYS A CA  
1118  C C   . LYS A  152 ? 0.7901 0.7070 1.0207 0.0266  0.0884  0.0431  152 LYS A C   
1119  O O   . LYS A  152 ? 0.8745 0.7857 1.1106 0.0264  0.0965  0.0421  152 LYS A O   
1120  C CB  . LYS A  152 ? 0.7987 0.7221 1.0478 0.0293  0.0772  0.0537  152 LYS A CB  
1121  C CG  . LYS A  152 ? 1.1734 1.1017 1.4313 0.0312  0.0698  0.0593  152 LYS A CG  
1122  C CD  . LYS A  152 ? 1.4399 1.3658 1.7090 0.0331  0.0731  0.0617  152 LYS A CD  
1123  C CE  . LYS A  152 ? 1.5627 1.4936 1.8407 0.0346  0.0657  0.0673  152 LYS A CE  
1124  N NZ  . LYS A  152 ? 1.5850 1.5138 1.8742 0.0364  0.0689  0.0696  152 LYS A NZ  
1125  N N   . ASN A  153 ? 0.7643 0.6837 0.9821 0.0247  0.0858  0.0395  153 ASN A N   
1126  C CA  . ASN A  153 ? 0.7663 0.6818 0.9765 0.0221  0.0924  0.0345  153 ASN A CA  
1127  C C   . ASN A  153 ? 0.7107 0.6247 0.9092 0.0209  0.0966  0.0290  153 ASN A C   
1128  O O   . ASN A  153 ? 0.7148 0.6260 0.9056 0.0184  0.1021  0.0243  153 ASN A O   
1129  C CB  . ASN A  153 ? 0.6413 0.5602 0.8434 0.0204  0.0881  0.0332  153 ASN A CB  
1130  C CG  . ASN A  153 ? 0.7127 0.6327 0.9261 0.0213  0.0848  0.0386  153 ASN A CG  
1131  O OD1 . ASN A  153 ? 0.8656 0.7825 1.0932 0.0227  0.0880  0.0426  153 ASN A OD1 
1132  N ND2 . ASN A  153 ? 0.8430 0.7674 1.0502 0.0206  0.0784  0.0388  153 ASN A ND2 
1133  N N   . LEU A  154 ? 0.8237 0.7396 1.0209 0.0226  0.0940  0.0296  154 LEU A N   
1134  C CA  . LEU A  154 ? 0.8413 0.7561 1.0281 0.0218  0.0977  0.0251  154 LEU A CA  
1135  C C   . LEU A  154 ? 0.8261 0.7381 1.0210 0.0238  0.1007  0.0271  154 LEU A C   
1136  O O   . LEU A  154 ? 0.9250 0.8382 1.1310 0.0261  0.0972  0.0320  154 LEU A O   
1137  C CB  . LEU A  154 ? 0.8104 0.7313 0.9833 0.0215  0.0909  0.0230  154 LEU A CB  
1138  C CG  . LEU A  154 ? 0.7045 0.6286 0.8673 0.0194  0.0877  0.0204  154 LEU A CG  
1139  C CD1 . LEU A  154 ? 0.6409 0.5714 0.7924 0.0199  0.0803  0.0194  154 LEU A CD1 
1140  C CD2 . LEU A  154 ? 0.7332 0.6537 0.8887 0.0164  0.0950  0.0153  154 LEU A CD2 
1141  N N   . ILE A  155 ? 0.7902 0.6985 0.9796 0.0227  0.1073  0.0233  155 ILE A N   
1142  C CA  . ILE A  155 ? 0.9555 0.8609 1.1513 0.0245  0.1107  0.0247  155 ILE A CA  
1143  C C   . ILE A  155 ? 0.7874 0.6949 0.9705 0.0244  0.1100  0.0215  155 ILE A C   
1144  O O   . ILE A  155 ? 0.7664 0.6730 0.9376 0.0220  0.1135  0.0167  155 ILE A O   
1145  C CB  . ILE A  155 ? 0.9762 0.8741 1.1796 0.0235  0.1209  0.0237  155 ILE A CB  
1146  C CG1 . ILE A  155 ? 0.9720 0.8677 1.1897 0.0241  0.1220  0.0276  155 ILE A CG1 
1147  C CG2 . ILE A  155 ? 0.7941 0.6890 1.0030 0.0252  0.1246  0.0247  155 ILE A CG2 
1148  C CD1 . ILE A  155 ? 1.1678 1.0559 1.3942 0.0232  0.1323  0.0268  155 ILE A CD1 
1149  N N   . TRP A  156 ? 0.7864 0.6967 0.9723 0.0268  0.1054  0.0243  156 TRP A N   
1150  C CA  . TRP A  156 ? 0.8198 0.7321 0.9947 0.0271  0.1043  0.0220  156 TRP A CA  
1151  C C   . TRP A  156 ? 0.8109 0.7178 0.9879 0.0272  0.1123  0.0207  156 TRP A C   
1152  O O   . TRP A  156 ? 0.9543 0.8596 1.1411 0.0294  0.1130  0.0237  156 TRP A O   
1153  C CB  . TRP A  156 ? 0.7871 0.7046 0.9635 0.0296  0.0962  0.0253  156 TRP A CB  
1154  C CG  . TRP A  156 ? 0.8193 0.7397 0.9835 0.0300  0.0943  0.0230  156 TRP A CG  
1155  C CD1 . TRP A  156 ? 0.7771 0.6961 0.9302 0.0285  0.0990  0.0189  156 TRP A CD1 
1156  C CD2 . TRP A  156 ? 0.7659 0.6911 0.9280 0.0320  0.0872  0.0250  156 TRP A CD2 
1157  N NE1 . TRP A  156 ? 0.6516 0.5745 0.7962 0.0296  0.0952  0.0185  156 TRP A NE1 
1158  C CE2 . TRP A  156 ? 0.6972 0.6238 0.8472 0.0318  0.0882  0.0221  156 TRP A CE2 
1159  C CE3 . TRP A  156 ? 0.7729 0.7016 0.9423 0.0337  0.0803  0.0289  156 TRP A CE3 
1160  C CZ2 . TRP A  156 ? 0.8841 0.8148 1.0293 0.0335  0.0828  0.0230  156 TRP A CZ2 
1161  C CZ3 . TRP A  156 ? 0.8385 0.7713 1.0028 0.0351  0.0750  0.0295  156 TRP A CZ3 
1162  C CH2 . TRP A  156 ? 0.9317 0.8653 1.0842 0.0351  0.0764  0.0266  156 TRP A CH2 
1163  N N   . LEU A  157 ? 0.6708 0.5749 0.8382 0.0246  0.1183  0.0160  157 LEU A N   
1164  C CA  . LEU A  157 ? 0.7394 0.6378 0.9076 0.0240  0.1268  0.0141  157 LEU A CA  
1165  C C   . LEU A  157 ? 0.8353 0.7353 0.9969 0.0253  0.1258  0.0137  157 LEU A C   
1166  O O   . LEU A  157 ? 0.8982 0.8020 1.0461 0.0244  0.1233  0.0111  157 LEU A O   
1167  C CB  . LEU A  157 ? 0.6917 0.5869 0.8506 0.0203  0.1334  0.0089  157 LEU A CB  
1168  C CG  . LEU A  157 ? 0.7929 0.6804 0.9602 0.0188  0.1429  0.0079  157 LEU A CG  
1169  C CD1 . LEU A  157 ? 0.8770 0.7632 1.0589 0.0200  0.1421  0.0117  157 LEU A CD1 
1170  C CD2 . LEU A  157 ? 0.7150 0.6005 0.8704 0.0148  0.1484  0.0022  157 LEU A CD2 
1171  N N   . VAL A  158 ? 0.8918 0.7890 1.0635 0.0276  0.1279  0.0166  158 VAL A N   
1172  C CA  . VAL A  158 ? 0.8805 0.7783 1.0472 0.0289  0.1281  0.0163  158 VAL A CA  
1173  C C   . VAL A  158 ? 0.9403 0.8315 1.1080 0.0278  0.1377  0.0142  158 VAL A C   
1174  O O   . VAL A  158 ? 1.0398 0.9257 1.2148 0.0265  0.1439  0.0137  158 VAL A O   
1175  C CB  . VAL A  158 ? 0.8276 0.7276 1.0043 0.0322  0.1228  0.0211  158 VAL A CB  
1176  C CG1 . VAL A  158 ? 0.8882 0.7947 1.0635 0.0331  0.1133  0.0230  158 VAL A CG1 
1177  C CG2 . VAL A  158 ? 1.0218 0.9172 1.2158 0.0334  0.1266  0.0243  158 VAL A CG2 
1178  N N   . LYS A  159 ? 1.0891 0.9804 1.2492 0.0282  0.1391  0.0130  159 LYS A N   
1179  C CA  . LYS A  159 ? 1.2140 1.0992 1.3732 0.0269  0.1483  0.0107  159 LYS A CA  
1180  C C   . LYS A  159 ? 1.2144 1.0945 1.3897 0.0290  0.1522  0.0140  159 LYS A C   
1181  O O   . LYS A  159 ? 1.0231 0.9054 1.2064 0.0320  0.1476  0.0179  159 LYS A O   
1182  C CB  . LYS A  159 ? 1.2111 1.0982 1.3571 0.0268  0.1484  0.0087  159 LYS A CB  
1183  C CG  . LYS A  159 ? 1.1863 1.0751 1.3368 0.0302  0.1448  0.0122  159 LYS A CG  
1184  C CD  . LYS A  159 ? 1.2357 1.1248 1.3745 0.0300  0.1471  0.0103  159 LYS A CD  
1185  C CE  . LYS A  159 ? 1.2366 1.1288 1.3782 0.0334  0.1421  0.0138  159 LYS A CE  
1186  N NZ  . LYS A  159 ? 1.3574 1.2471 1.5160 0.0358  0.1416  0.0177  159 LYS A NZ  
1187  N N   . LYS A  160 ? 1.3041 1.1776 1.4842 0.0274  0.1610  0.0123  160 LYS A N   
1188  C CA  . LYS A  160 ? 1.4241 1.2922 1.6197 0.0290  0.1660  0.0151  160 LYS A CA  
1189  C C   . LYS A  160 ? 1.4989 1.3646 1.6920 0.0299  0.1699  0.0147  160 LYS A C   
1190  O O   . LYS A  160 ? 1.4385 1.3008 1.6221 0.0276  0.1763  0.0108  160 LYS A O   
1191  C CB  . LYS A  160 ? 1.2671 1.1288 1.4685 0.0267  0.1745  0.0133  160 LYS A CB  
1192  C CG  . LYS A  160 ? 1.2851 1.1405 1.5027 0.0281  0.1811  0.0158  160 LYS A CG  
1193  C CD  . LYS A  160 ? 1.4714 1.3221 1.6846 0.0275  0.1884  0.0135  160 LYS A CD  
1194  C CE  . LYS A  160 ? 1.4403 1.2887 1.6682 0.0306  0.1897  0.0177  160 LYS A CE  
1195  N NZ  . LYS A  160 ? 1.4661 1.3184 1.6882 0.0326  0.1848  0.0188  160 LYS A NZ  
1196  N N   . GLY A  161 ? 1.4974 1.3649 1.6988 0.0331  0.1659  0.0187  161 GLY A N   
1197  C CA  . GLY A  161 ? 1.4601 1.3253 1.6609 0.0344  0.1692  0.0190  161 GLY A CA  
1198  C C   . GLY A  161 ? 1.5897 1.4546 1.7737 0.0325  0.1723  0.0149  161 GLY A C   
1199  O O   . GLY A  161 ? 1.6848 1.5441 1.8675 0.0312  0.1806  0.0128  161 GLY A O   
1200  N N   . ASN A  162 ? 1.5399 1.4111 1.7112 0.0323  0.1658  0.0139  162 ASN A N   
1201  C CA  . ASN A  162 ? 1.7312 1.6036 1.8864 0.0309  0.1673  0.0108  162 ASN A CA  
1202  C C   . ASN A  162 ? 1.6968 1.5671 1.8409 0.0268  0.1726  0.0059  162 ASN A C   
1203  O O   . ASN A  162 ? 1.5750 1.4439 1.7083 0.0250  0.1771  0.0031  162 ASN A O   
1204  C CB  . ASN A  162 ? 1.9141 1.7827 2.0710 0.0322  0.1722  0.0116  162 ASN A CB  
1205  C CG  . ASN A  162 ? 1.9552 1.8287 2.1091 0.0351  0.1660  0.0141  162 ASN A CG  
1206  O OD1 . ASN A  162 ? 2.1380 2.0092 2.2925 0.0365  0.1690  0.0150  162 ASN A OD1 
1207  N ND2 . ASN A  162 ? 1.8403 1.7203 1.9909 0.0361  0.1573  0.0153  162 ASN A ND2 
1208  N N   . SER A  163 ? 1.7103 1.5807 1.8569 0.0251  0.1721  0.0049  163 SER A N   
1209  C CA  . SER A  163 ? 1.7227 1.5912 1.8591 0.0210  0.1771  0.0001  163 SER A CA  
1210  C C   . SER A  163 ? 1.5532 1.4260 1.6869 0.0198  0.1717  -0.0007 163 SER A C   
1211  O O   . SER A  163 ? 1.4288 1.3022 1.5740 0.0214  0.1683  0.0023  163 SER A O   
1212  C CB  . SER A  163 ? 1.5796 1.4395 1.7242 0.0193  0.1873  -0.0014 163 SER A CB  
1213  O OG  . SER A  163 ? 1.4850 1.3419 1.6171 0.0154  0.1942  -0.0064 163 SER A OG  
1214  N N   . TYR A  164 ? 1.2593 1.1354 1.3778 0.0168  0.1709  -0.0044 164 TYR A N   
1215  C CA  . TYR A  164 ? 1.1818 1.0611 1.2969 0.0150  0.1672  -0.0059 164 TYR A CA  
1216  C C   . TYR A  164 ? 1.1026 0.9808 1.2044 0.0103  0.1725  -0.0115 164 TYR A C   
1217  O O   . TYR A  164 ? 0.9624 0.8459 1.0500 0.0089  0.1691  -0.0136 164 TYR A O   
1218  C CB  . TYR A  164 ? 1.2267 1.1143 1.3373 0.0171  0.1568  -0.0037 164 TYR A CB  
1219  C CG  . TYR A  164 ? 1.0979 0.9886 1.2080 0.0159  0.1525  -0.0044 164 TYR A CG  
1220  C CD1 . TYR A  164 ? 1.0781 0.9732 1.1948 0.0185  0.1444  -0.0007 164 TYR A CD1 
1221  C CD2 . TYR A  164 ? 0.9981 0.8873 1.1011 0.0119  0.1567  -0.0087 164 TYR A CD2 
1222  C CE1 . TYR A  164 ? 1.0284 0.9261 1.1444 0.0173  0.1407  -0.0012 164 TYR A CE1 
1223  C CE2 . TYR A  164 ? 0.9762 0.8680 1.0788 0.0107  0.1532  -0.0093 164 TYR A CE2 
1224  C CZ  . TYR A  164 ? 1.0604 0.9564 1.1695 0.0135  0.1452  -0.0055 164 TYR A CZ  
1225  O OH  . TYR A  164 ? 0.9623 0.8607 1.0706 0.0122  0.1418  -0.0062 164 TYR A OH  
1226  N N   . PRO A  165 ? 0.9381 0.8093 1.0446 0.0078  0.1811  -0.0139 165 PRO A N   
1227  C CA  . PRO A  165 ? 1.0462 0.9157 1.1404 0.0028  0.1868  -0.0195 165 PRO A CA  
1228  C C   . PRO A  165 ? 1.1134 0.9878 1.2015 0.0009  0.1818  -0.0212 165 PRO A C   
1229  O O   . PRO A  165 ? 1.0122 0.8885 1.1092 0.0032  0.1766  -0.0182 165 PRO A O   
1230  C CB  . PRO A  165 ? 1.0024 0.8627 1.1066 0.0012  0.1966  -0.0209 165 PRO A CB  
1231  C CG  . PRO A  165 ? 1.2189 1.0765 1.3408 0.0056  0.1960  -0.0156 165 PRO A CG  
1232  C CD  . PRO A  165 ? 1.0216 0.8867 1.1453 0.0092  0.1851  -0.0115 165 PRO A CD  
1233  N N   . LYS A  166 ? 0.9206 0.7970 0.9938 -0.0032 0.1834  -0.0259 166 LYS A N   
1234  C CA  . LYS A  166 ? 1.0402 0.9208 1.1079 -0.0054 0.1796  -0.0279 166 LYS A CA  
1235  C C   . LYS A  166 ? 1.1585 1.0335 1.2383 -0.0059 0.1834  -0.0278 166 LYS A C   
1236  O O   . LYS A  166 ? 1.0443 0.9119 1.1278 -0.0083 0.1925  -0.0302 166 LYS A O   
1237  C CB  . LYS A  166 ? 0.9673 0.8498 1.0181 -0.0104 0.1825  -0.0335 166 LYS A CB  
1238  C CG  . LYS A  166 ? 1.1263 1.0094 1.1736 -0.0140 0.1829  -0.0369 166 LYS A CG  
1239  C CD  . LYS A  166 ? 1.2738 1.1570 1.3060 -0.0197 0.1880  -0.0429 166 LYS A CD  
1240  C CE  . LYS A  166 ? 1.2875 1.1796 1.3050 -0.0201 0.1816  -0.0433 166 LYS A CE  
1241  N NZ  . LYS A  166 ? 1.4458 1.3391 1.4483 -0.0260 0.1857  -0.0491 166 LYS A NZ  
1242  N N   . LEU A  167 ? 1.1630 1.0414 1.2495 -0.0038 0.1768  -0.0248 167 LEU A N   
1243  C CA  . LEU A  167 ? 1.0960 0.9699 1.1935 -0.0044 0.1799  -0.0245 167 LEU A CA  
1244  C C   . LEU A  167 ? 1.0790 0.9546 1.1669 -0.0085 0.1803  -0.0289 167 LEU A C   
1245  O O   . LEU A  167 ? 0.9948 0.8771 1.0698 -0.0098 0.1750  -0.0307 167 LEU A O   
1246  C CB  . LEU A  167 ? 0.8506 0.7265 0.9618 0.0001  0.1732  -0.0187 167 LEU A CB  
1247  C CG  . LEU A  167 ? 0.9765 0.8608 1.0840 0.0020  0.1623  -0.0164 167 LEU A CG  
1248  C CD1 . LEU A  167 ? 0.9798 0.8670 1.0787 -0.0012 0.1606  -0.0197 167 LEU A CD1 
1249  C CD2 . LEU A  167 ? 0.9347 0.8194 1.0574 0.0061  0.1575  -0.0106 167 LEU A CD2 
1250  N N   . SER A  168 ? 1.0532 0.9228 1.1477 -0.0107 0.1866  -0.0306 168 SER A N   
1251  C CA  . SER A  168 ? 1.0095 0.8800 1.0959 -0.0149 0.1880  -0.0350 168 SER A CA  
1252  C C   . SER A  168 ? 1.0099 0.8750 1.1086 -0.0152 0.1919  -0.0342 168 SER A C   
1253  O O   . SER A  168 ? 1.3188 1.1766 1.4204 -0.0180 0.2014  -0.0372 168 SER A O   
1254  C CB  . SER A  168 ? 1.1346 1.0026 1.2078 -0.0200 0.1954  -0.0412 168 SER A CB  
1255  O OG  . SER A  168 ? 1.1395 1.0112 1.2009 -0.0241 0.1941  -0.0455 168 SER A OG  
1256  N N   . LYS A  169 ? 0.9054 0.7742 1.0115 -0.0122 0.1847  -0.0301 169 LYS A N   
1257  C CA  . LYS A  169 ? 1.0305 0.8953 1.1481 -0.0122 0.1871  -0.0287 169 LYS A CA  
1258  C C   . LYS A  169 ? 1.0590 0.9277 1.1680 -0.0150 0.1840  -0.0316 169 LYS A C   
1259  O O   . LYS A  169 ? 1.0571 0.9331 1.1547 -0.0153 0.1767  -0.0324 169 LYS A O   
1260  C CB  . LYS A  169 ? 0.9201 0.7863 1.0529 -0.0071 0.1813  -0.0217 169 LYS A CB  
1261  C CG  . LYS A  169 ? 1.0631 0.9218 1.2123 -0.0052 0.1882  -0.0186 169 LYS A CG  
1262  C CD  . LYS A  169 ? 1.2006 1.0532 1.3576 -0.0072 0.1951  -0.0197 169 LYS A CD  
1263  C CE  . LYS A  169 ? 1.2641 1.1107 1.4400 -0.0043 0.1999  -0.0151 169 LYS A CE  
1264  N NZ  . LYS A  169 ? 1.3428 1.1844 1.5203 -0.0042 0.2066  -0.0160 169 LYS A NZ  
1265  N N   . SER A  170 ? 1.1987 1.0623 1.3133 -0.0172 0.1896  -0.0330 170 SER A N   
1266  C CA  . SER A  170 ? 1.1753 1.0419 1.2831 -0.0199 0.1873  -0.0357 170 SER A CA  
1267  C C   . SER A  170 ? 0.9829 0.8443 1.1035 -0.0197 0.1911  -0.0339 170 SER A C   
1268  O O   . SER A  170 ? 1.0834 0.9368 1.2115 -0.0210 0.2005  -0.0350 170 SER A O   
1269  C CB  . SER A  170 ? 1.1235 0.9899 1.2154 -0.0255 0.1922  -0.0429 170 SER A CB  
1270  O OG  . SER A  170 ? 1.4362 1.2941 1.5308 -0.0283 0.2034  -0.0462 170 SER A OG  
1271  N N   . TYR A  171 ? 0.8932 0.7592 1.0163 -0.0181 0.1838  -0.0310 171 TYR A N   
1272  C CA  . TYR A  171 ? 0.9741 0.8363 1.1093 -0.0176 0.1861  -0.0286 171 TYR A CA  
1273  C C   . TYR A  171 ? 0.8902 0.7531 1.0167 -0.0217 0.1873  -0.0332 171 TYR A C   
1274  O O   . TYR A  171 ? 0.8121 0.6816 0.9254 -0.0233 0.1814  -0.0357 171 TYR A O   
1275  C CB  . TYR A  171 ? 0.9491 0.8157 1.0948 -0.0127 0.1772  -0.0214 171 TYR A CB  
1276  C CG  . TYR A  171 ? 0.8256 0.6913 0.9794 -0.0124 0.1763  -0.0190 171 TYR A CG  
1277  C CD1 . TYR A  171 ? 0.9025 0.7621 1.0727 -0.0107 0.1816  -0.0152 171 TYR A CD1 
1278  C CD2 . TYR A  171 ? 0.9114 0.7826 1.0567 -0.0136 0.1702  -0.0202 171 TYR A CD2 
1279  C CE1 . TYR A  171 ? 0.9415 0.8004 1.1191 -0.0104 0.1808  -0.0126 171 TYR A CE1 
1280  C CE2 . TYR A  171 ? 0.9225 0.7929 1.0750 -0.0134 0.1694  -0.0179 171 TYR A CE2 
1281  C CZ  . TYR A  171 ? 0.9620 0.8262 1.1306 -0.0117 0.1747  -0.0140 171 TYR A CZ  
1282  O OH  . TYR A  171 ? 1.0372 0.9008 1.2132 -0.0114 0.1740  -0.0114 171 TYR A OH  
1283  N N   . ILE A  172 ? 0.9669 0.8230 1.1010 -0.0235 0.1950  -0.0342 172 ILE A N   
1284  C CA  . ILE A  172 ? 1.0220 0.8780 1.1492 -0.0276 0.1969  -0.0384 172 ILE A CA  
1285  C C   . ILE A  172 ? 1.0099 0.8657 1.1484 -0.0254 0.1941  -0.0338 172 ILE A C   
1286  O O   . ILE A  172 ? 0.9347 0.7853 1.0885 -0.0228 0.1978  -0.0295 172 ILE A O   
1287  C CB  . ILE A  172 ? 0.9604 0.8083 1.0850 -0.0325 0.2091  -0.0446 172 ILE A CB  
1288  C CG1 . ILE A  172 ? 1.0011 0.8493 1.1175 -0.0370 0.2109  -0.0494 172 ILE A CG1 
1289  C CG2 . ILE A  172 ? 1.1298 0.9688 1.2714 -0.0308 0.2174  -0.0415 172 ILE A CG2 
1290  C CD1 . ILE A  172 ? 1.1202 0.9677 1.2212 -0.0429 0.2164  -0.0574 172 ILE A CD1 
1291  N N   . ASN A  173 ? 0.8872 0.7487 1.0182 -0.0263 0.1876  -0.0346 173 ASN A N   
1292  C CA  . ASN A  173 ? 0.9853 0.8476 1.1256 -0.0242 0.1839  -0.0300 173 ASN A CA  
1293  C C   . ASN A  173 ? 1.0790 0.9332 1.2281 -0.0262 0.1933  -0.0310 173 ASN A C   
1294  O O   . ASN A  173 ? 0.9606 0.8137 1.1021 -0.0303 0.1967  -0.0360 173 ASN A O   
1295  C CB  . ASN A  173 ? 0.9005 0.7708 1.0297 -0.0251 0.1751  -0.0312 173 ASN A CB  
1296  C CG  . ASN A  173 ? 0.9568 0.8290 1.0952 -0.0223 0.1696  -0.0256 173 ASN A CG  
1297  O OD1 . ASN A  173 ? 1.0401 0.9078 1.1935 -0.0198 0.1723  -0.0208 173 ASN A OD1 
1298  N ND2 . ASN A  173 ? 0.9040 0.7830 1.0337 -0.0227 0.1618  -0.0262 173 ASN A ND2 
1299  N N   . ASP A  174 ? 1.2057 1.0544 1.3710 -0.0233 0.1975  -0.0262 174 ASP A N   
1300  C CA  . ASP A  174 ? 1.1934 1.0342 1.3692 -0.0246 0.2067  -0.0263 174 ASP A CA  
1301  C C   . ASP A  174 ? 1.2222 1.0649 1.4064 -0.0223 0.2019  -0.0211 174 ASP A C   
1302  O O   . ASP A  174 ? 1.4341 1.2709 1.6278 -0.0229 0.2085  -0.0201 174 ASP A O   
1303  C CB  . ASP A  174 ? 1.2908 1.1242 1.4805 -0.0226 0.2145  -0.0236 174 ASP A CB  
1304  C CG  . ASP A  174 ? 1.4982 1.3347 1.7010 -0.0169 0.2079  -0.0153 174 ASP A CG  
1305  O OD1 . ASP A  174 ? 1.6267 1.4611 1.8443 -0.0143 0.2084  -0.0096 174 ASP A OD1 
1306  O OD2 . ASP A  174 ? 1.4285 1.2697 1.6269 -0.0150 0.2021  -0.0143 174 ASP A OD2 
1307  N N   . LYS A  175 ? 1.0701 0.9211 1.2509 -0.0198 0.1905  -0.0176 175 LYS A N   
1308  C CA  . LYS A  175 ? 1.0567 0.9107 1.2438 -0.0178 0.1848  -0.0128 175 LYS A CA  
1309  C C   . LYS A  175 ? 1.2078 1.0624 1.3843 -0.0220 0.1858  -0.0179 175 LYS A C   
1310  O O   . LYS A  175 ? 1.2657 1.1194 1.4296 -0.0262 0.1899  -0.0251 175 LYS A O   
1311  C CB  . LYS A  175 ? 0.9029 0.7654 1.0889 -0.0141 0.1725  -0.0078 175 LYS A CB  
1312  C CG  . LYS A  175 ? 0.9367 0.7996 1.1313 -0.0103 0.1706  -0.0032 175 LYS A CG  
1313  C CD  . LYS A  175 ? 0.9020 0.7604 1.1160 -0.0071 0.1738  0.0035  175 LYS A CD  
1314  C CE  . LYS A  175 ? 0.8472 0.7071 1.0696 -0.0033 0.1708  0.0083  175 LYS A CE  
1315  N NZ  . LYS A  175 ? 1.1605 1.0171 1.4024 0.0000  0.1731  0.0154  175 LYS A NZ  
1316  N N   . GLY A  176 ? 0.8920 0.7481 1.0735 -0.0208 0.1821  -0.0143 176 GLY A N   
1317  C CA  . GLY A  176 ? 1.2301 1.0870 1.4027 -0.0245 0.1826  -0.0186 176 GLY A CA  
1318  C C   . GLY A  176 ? 1.2311 1.0970 1.3950 -0.0234 0.1710  -0.0172 176 GLY A C   
1319  O O   . GLY A  176 ? 1.2794 1.1472 1.4390 -0.0251 0.1690  -0.0184 176 GLY A O   
1320  N N   . LYS A  177 ? 1.1328 1.0043 1.2944 -0.0207 0.1635  -0.0148 177 LYS A N   
1321  C CA  . LYS A  177 ? 0.9881 0.8682 1.1419 -0.0193 0.1524  -0.0132 177 LYS A CA  
1322  C C   . LYS A  177 ? 0.8969 0.7815 1.0417 -0.0188 0.1485  -0.0152 177 LYS A C   
1323  O O   . LYS A  177 ? 1.0170 0.8980 1.1652 -0.0183 0.1533  -0.0156 177 LYS A O   
1324  C CB  . LYS A  177 ? 0.8991 0.7815 1.0653 -0.0149 0.1459  -0.0049 177 LYS A CB  
1325  C CG  . LYS A  177 ? 0.9078 0.7874 1.0876 -0.0113 0.1476  0.0003  177 LYS A CG  
1326  C CD  . LYS A  177 ? 0.9421 0.8236 1.1350 -0.0075 0.1420  0.0085  177 LYS A CD  
1327  C CE  . LYS A  177 ? 1.0947 0.9713 1.2971 -0.0080 0.1472  0.0106  177 LYS A CE  
1328  N NZ  . LYS A  177 ? 1.2559 1.1238 1.4672 -0.0089 0.1588  0.0094  177 LYS A NZ  
1329  N N   . GLU A  178 ? 0.7496 0.6417 0.8830 -0.0190 0.1401  -0.0164 178 GLU A N   
1330  C CA  . GLU A  178 ? 0.8305 0.7273 0.9552 -0.0183 0.1359  -0.0178 178 GLU A CA  
1331  C C   . GLU A  178 ? 0.8901 0.7866 1.0256 -0.0139 0.1335  -0.0120 178 GLU A C   
1332  O O   . GLU A  178 ? 0.7468 0.6424 0.8947 -0.0111 0.1314  -0.0061 178 GLU A O   
1333  C CB  . GLU A  178 ? 0.8493 0.7544 0.9627 -0.0183 0.1265  -0.0185 178 GLU A CB  
1334  C CG  . GLU A  178 ? 1.1249 1.0314 1.2272 -0.0226 0.1280  -0.0242 178 GLU A CG  
1335  C CD  . GLU A  178 ? 1.1158 1.0304 1.2090 -0.0222 0.1186  -0.0240 178 GLU A CD  
1336  O OE1 . GLU A  178 ? 1.0667 0.9838 1.1661 -0.0191 0.1120  -0.0186 178 GLU A OE1 
1337  O OE2 . GLU A  178 ? 1.1030 1.0215 1.1832 -0.0251 0.1177  -0.0291 178 GLU A OE2 
1338  N N   . VAL A  179 ? 0.7142 0.6115 0.8451 -0.0136 0.1339  -0.0137 179 VAL A N   
1339  C CA  . VAL A  179 ? 0.7533 0.6509 0.8932 -0.0096 0.1312  -0.0086 179 VAL A CA  
1340  C C   . VAL A  179 ? 0.6910 0.5958 0.8217 -0.0082 0.1230  -0.0086 179 VAL A C   
1341  O O   . VAL A  179 ? 0.6332 0.5398 0.7520 -0.0102 0.1240  -0.0133 179 VAL A O   
1342  C CB  . VAL A  179 ? 0.7084 0.5992 0.8542 -0.0099 0.1403  -0.0098 179 VAL A CB  
1343  C CG1 . VAL A  179 ? 0.7500 0.6421 0.9023 -0.0061 0.1369  -0.0054 179 VAL A CG1 
1344  C CG2 . VAL A  179 ? 0.6803 0.5637 0.8386 -0.0104 0.1481  -0.0083 179 VAL A CG2 
1345  N N   . LEU A  180 ? 0.5686 0.4776 0.7047 -0.0047 0.1150  -0.0031 180 LEU A N   
1346  C CA  . LEU A  180 ? 0.6066 0.5220 0.7356 -0.0030 0.1073  -0.0024 180 LEU A CA  
1347  C C   . LEU A  180 ? 0.6056 0.5192 0.7389 -0.0010 0.1093  -0.0011 180 LEU A C   
1348  O O   . LEU A  180 ? 0.6522 0.5634 0.7985 0.0017  0.1096  0.0037  180 LEU A O   
1349  C CB  . LEU A  180 ? 0.5550 0.4754 0.6882 -0.0004 0.0982  0.0027  180 LEU A CB  
1350  C CG  . LEU A  180 ? 0.4681 0.3949 0.5954 0.0016  0.0901  0.0040  180 LEU A CG  
1351  C CD1 . LEU A  180 ? 0.5124 0.4439 0.6238 -0.0006 0.0873  -0.0010 180 LEU A CD1 
1352  C CD2 . LEU A  180 ? 0.4979 0.4281 0.6326 0.0043  0.0824  0.0098  180 LEU A CD2 
1353  N N   . VAL A  181 ? 0.6088 0.5237 0.7313 -0.0023 0.1107  -0.0054 181 VAL A N   
1354  C CA  . VAL A  181 ? 0.6417 0.5551 0.7669 -0.0006 0.1126  -0.0044 181 VAL A CA  
1355  C C   . VAL A  181 ? 0.5231 0.4431 0.6414 0.0015  0.1045  -0.0033 181 VAL A C   
1356  O O   . VAL A  181 ? 0.6058 0.5306 0.7114 0.0000  0.1012  -0.0065 181 VAL A O   
1357  C CB  . VAL A  181 ? 0.5097 0.4188 0.6284 -0.0035 0.1212  -0.0099 181 VAL A CB  
1358  C CG1 . VAL A  181 ? 0.6432 0.5498 0.7665 -0.0015 0.1238  -0.0084 181 VAL A CG1 
1359  C CG2 . VAL A  181 ? 0.6239 0.5264 0.7477 -0.0061 0.1295  -0.0118 181 VAL A CG2 
1360  N N   . LEU A  182 ? 0.5587 0.4791 0.6858 0.0049  0.1015  0.0013  182 LEU A N   
1361  C CA  . LEU A  182 ? 0.6276 0.5536 0.7494 0.0070  0.0944  0.0026  182 LEU A CA  
1362  C C   . LEU A  182 ? 0.5505 0.4744 0.6735 0.0082  0.0979  0.0025  182 LEU A C   
1363  O O   . LEU A  182 ? 0.6818 0.6001 0.8148 0.0088  0.1036  0.0039  182 LEU A O   
1364  C CB  . LEU A  182 ? 0.5523 0.4816 0.6822 0.0098  0.0868  0.0081  182 LEU A CB  
1365  C CG  . LEU A  182 ? 0.6636 0.5961 0.7914 0.0089  0.0819  0.0087  182 LEU A CG  
1366  C CD1 . LEU A  182 ? 0.6175 0.5466 0.7590 0.0096  0.0834  0.0127  182 LEU A CD1 
1367  C CD2 . LEU A  182 ? 0.6500 0.5893 0.7731 0.0105  0.0726  0.0106  182 LEU A CD2 
1368  N N   . TRP A  183 ? 0.6156 0.5437 0.7284 0.0086  0.0945  0.0009  183 TRP A N   
1369  C CA  . TRP A  183 ? 0.6547 0.5814 0.7677 0.0099  0.0970  0.0010  183 TRP A CA  
1370  C C   . TRP A  183 ? 0.5884 0.5212 0.6944 0.0118  0.0899  0.0019  183 TRP A C   
1371  O O   . TRP A  183 ? 0.5690 0.5071 0.6684 0.0116  0.0838  0.0017  183 TRP A O   
1372  C CB  . TRP A  183 ? 0.6802 0.6034 0.7856 0.0069  0.1049  -0.0040 183 TRP A CB  
1373  C CG  . TRP A  183 ? 0.6266 0.5546 0.7162 0.0045  0.1031  -0.0084 183 TRP A CG  
1374  C CD1 . TRP A  183 ? 0.5637 0.4956 0.6436 0.0050  0.1009  -0.0096 183 TRP A CD1 
1375  C CD2 . TRP A  183 ? 0.7604 0.6899 0.8425 0.0013  0.1035  -0.0119 183 TRP A CD2 
1376  N NE1 . TRP A  183 ? 0.6051 0.5412 0.6721 0.0023  0.0997  -0.0135 183 TRP A NE1 
1377  C CE2 . TRP A  183 ? 0.6200 0.5547 0.6879 -0.0001 0.1012  -0.0151 183 TRP A CE2 
1378  C CE3 . TRP A  183 ? 0.6027 0.5296 0.6887 -0.0005 0.1055  -0.0125 183 TRP A CE3 
1379  C CZ2 . TRP A  183 ? 0.6223 0.5600 0.6801 -0.0034 0.1008  -0.0190 183 TRP A CZ2 
1380  C CZ3 . TRP A  183 ? 0.6736 0.6033 0.7494 -0.0037 0.1053  -0.0166 183 TRP A CZ3 
1381  C CH2 . TRP A  183 ? 0.7449 0.6800 0.8068 -0.0052 0.1029  -0.0198 183 TRP A CH2 
1382  N N   . GLY A  184 ? 0.6067 0.5386 0.7144 0.0137  0.0909  0.0031  184 GLY A N   
1383  C CA  . GLY A  184 ? 0.5454 0.4827 0.6477 0.0157  0.0847  0.0043  184 GLY A CA  
1384  C C   . GLY A  184 ? 0.6343 0.5713 0.7289 0.0156  0.0880  0.0020  184 GLY A C   
1385  O O   . GLY A  184 ? 0.6730 0.6049 0.7703 0.0149  0.0950  0.0008  184 GLY A O   
1386  N N   . ILE A  185 ? 0.5927 0.5353 0.6775 0.0162  0.0832  0.0014  185 ILE A N   
1387  C CA  . ILE A  185 ? 0.5326 0.4759 0.6101 0.0166  0.0853  0.0000  185 ILE A CA  
1388  C C   . ILE A  185 ? 0.5908 0.5366 0.6714 0.0201  0.0801  0.0036  185 ILE A C   
1389  O O   . ILE A  185 ? 0.5793 0.5304 0.6566 0.0211  0.0734  0.0047  185 ILE A O   
1390  C CB  . ILE A  185 ? 0.6356 0.5836 0.6981 0.0143  0.0844  -0.0038 185 ILE A CB  
1391  C CG1 . ILE A  185 ? 0.5908 0.5367 0.6498 0.0105  0.0889  -0.0076 185 ILE A CG1 
1392  C CG2 . ILE A  185 ? 0.5330 0.4815 0.5881 0.0145  0.0871  -0.0050 185 ILE A CG2 
1393  C CD1 . ILE A  185 ? 0.5924 0.5314 0.6554 0.0088  0.0977  -0.0093 185 ILE A CD1 
1394  N N   . HIS A  186 ? 0.7250 0.6671 0.8124 0.0218  0.0834  0.0053  186 HIS A N   
1395  C CA  . HIS A  186 ? 0.7168 0.6608 0.8083 0.0250  0.0792  0.0087  186 HIS A CA  
1396  C C   . HIS A  186 ? 0.6441 0.5913 0.7251 0.0257  0.0786  0.0075  186 HIS A C   
1397  O O   . HIS A  186 ? 0.6750 0.6202 0.7503 0.0244  0.0840  0.0052  186 HIS A O   
1398  C CB  . HIS A  186 ? 0.7915 0.7302 0.8962 0.0267  0.0826  0.0115  186 HIS A CB  
1399  C CG  . HIS A  186 ? 0.8333 0.7735 0.9421 0.0297  0.0789  0.0147  186 HIS A CG  
1400  N ND1 . HIS A  186 ? 0.7694 0.7074 0.8784 0.0310  0.0825  0.0149  186 HIS A ND1 
1401  C CD2 . HIS A  186 ? 0.7783 0.7220 0.8912 0.0316  0.0721  0.0176  186 HIS A CD2 
1402  C CE1 . HIS A  186 ? 0.8151 0.7550 0.9282 0.0335  0.0781  0.0179  186 HIS A CE1 
1403  N NE2 . HIS A  186 ? 0.7328 0.6761 0.8482 0.0339  0.0718  0.0195  186 HIS A NE2 
1404  N N   . HIS A  187 ? 0.7742 0.7262 0.8524 0.0276  0.0721  0.0093  187 HIS A N   
1405  C CA  . HIS A  187 ? 0.6242 0.5796 0.6936 0.0287  0.0710  0.0089  187 HIS A CA  
1406  C C   . HIS A  187 ? 0.8484 0.8033 0.9249 0.0319  0.0689  0.0124  187 HIS A C   
1407  O O   . HIS A  187 ? 0.8877 0.8455 0.9667 0.0335  0.0629  0.0145  187 HIS A O   
1408  C CB  . HIS A  187 ? 0.6121 0.5739 0.6713 0.0282  0.0656  0.0078  187 HIS A CB  
1409  C CG  . HIS A  187 ? 0.7343 0.6972 0.7868 0.0249  0.0671  0.0044  187 HIS A CG  
1410  N ND1 . HIS A  187 ? 0.7088 0.6727 0.7511 0.0227  0.0709  0.0012  187 HIS A ND1 
1411  C CD2 . HIS A  187 ? 0.8065 0.7697 0.8609 0.0233  0.0653  0.0037  187 HIS A CD2 
1412  C CE1 . HIS A  187 ? 0.7288 0.6935 0.7670 0.0198  0.0715  -0.0015 187 HIS A CE1 
1413  N NE2 . HIS A  187 ? 0.7966 0.7608 0.8421 0.0202  0.0682  -0.0001 187 HIS A NE2 
1414  N N   . PRO A  188 ? 0.7786 0.7295 0.8584 0.0328  0.0739  0.0129  188 PRO A N   
1415  C CA  . PRO A  188 ? 0.7946 0.7443 0.8815 0.0357  0.0728  0.0160  188 PRO A CA  
1416  C C   . PRO A  188 ? 0.8016 0.7564 0.8818 0.0376  0.0678  0.0169  188 PRO A C   
1417  O O   . PRO A  188 ? 0.7090 0.6679 0.7782 0.0367  0.0665  0.0151  188 PRO A O   
1418  C CB  . PRO A  188 ? 0.7898 0.7348 0.8774 0.0357  0.0800  0.0153  188 PRO A CB  
1419  C CG  . PRO A  188 ? 0.8009 0.7429 0.8871 0.0327  0.0851  0.0125  188 PRO A CG  
1420  C CD  . PRO A  188 ? 0.7028 0.6496 0.7799 0.0308  0.0814  0.0103  188 PRO A CD  
1421  N N   . SER A  189 ? 0.8477 0.8023 0.9350 0.0400  0.0651  0.0199  189 SER A N   
1422  C CA  . SER A  189 ? 0.7890 0.7479 0.8714 0.0420  0.0605  0.0210  189 SER A CA  
1423  C C   . SER A  189 ? 0.8744 0.8331 0.9508 0.0432  0.0639  0.0208  189 SER A C   
1424  O O   . SER A  189 ? 0.8523 0.8153 0.9197 0.0439  0.0617  0.0206  189 SER A O   
1425  C CB  . SER A  189 ? 0.8090 0.7677 0.9014 0.0438  0.0563  0.0240  189 SER A CB  
1426  O OG  . SER A  189 ? 0.9253 0.8793 1.0276 0.0448  0.0600  0.0257  189 SER A OG  
1427  N N   . THR A  190 ? 0.9467 0.9005 1.0282 0.0436  0.0694  0.0212  190 THR A N   
1428  C CA  . THR A  190 ? 0.9565 0.9096 1.0332 0.0448  0.0731  0.0214  190 THR A CA  
1429  C C   . THR A  190 ? 0.9419 0.8909 1.0164 0.0430  0.0802  0.0193  190 THR A C   
1430  O O   . THR A  190 ? 0.9768 0.9221 1.0575 0.0414  0.0831  0.0185  190 THR A O   
1431  C CB  . THR A  190 ? 0.9660 0.9168 1.0513 0.0475  0.0728  0.0243  190 THR A CB  
1432  O OG1 . THR A  190 ? 1.2920 1.2393 1.3766 0.0481  0.0788  0.0243  190 THR A OG1 
1433  C CG2 . THR A  190 ? 0.9403 0.8882 1.0389 0.0476  0.0717  0.0259  190 THR A CG2 
1434  N N   . SER A  191 ? 1.1147 1.0646 1.1803 0.0431  0.0831  0.0186  191 SER A N   
1435  C CA  . SER A  191 ? 1.1054 1.0516 1.1677 0.0412  0.0901  0.0165  191 SER A CA  
1436  C C   . SER A  191 ? 0.9855 0.9251 1.0592 0.0420  0.0949  0.0178  191 SER A C   
1437  O O   . SER A  191 ? 0.9551 0.8904 1.0297 0.0401  0.1010  0.0160  191 SER A O   
1438  C CB  . SER A  191 ? 0.9976 0.9466 1.0482 0.0414  0.0918  0.0161  191 SER A CB  
1439  O OG  . SER A  191 ? 1.1404 1.0892 1.1937 0.0446  0.0912  0.0189  191 SER A OG  
1440  N N   . ALA A  192 ? 1.0494 0.9884 1.1319 0.0447  0.0924  0.0207  192 ALA A N   
1441  C CA  . ALA A  192 ? 1.1826 1.1158 1.2772 0.0457  0.0961  0.0223  192 ALA A CA  
1442  C C   . ALA A  192 ? 1.1785 1.1093 1.2827 0.0443  0.0962  0.0221  192 ALA A C   
1443  O O   . ALA A  192 ? 1.1286 1.0542 1.2400 0.0436  0.1016  0.0219  192 ALA A O   
1444  C CB  . ALA A  192 ? 1.1652 1.0990 1.2664 0.0488  0.0930  0.0255  192 ALA A CB  
1445  N N   . ASP A  193 ? 1.1701 1.1047 1.2745 0.0440  0.0902  0.0224  193 ASP A N   
1446  C CA  . ASP A  193 ? 1.0704 1.0034 1.1829 0.0426  0.0896  0.0224  193 ASP A CA  
1447  C C   . ASP A  193 ? 0.9300 0.8608 1.0376 0.0397  0.0947  0.0192  193 ASP A C   
1448  O O   . ASP A  193 ? 0.8216 0.7485 0.9375 0.0386  0.0978  0.0191  193 ASP A O   
1449  C CB  . ASP A  193 ? 1.0275 0.9655 1.1396 0.0427  0.0820  0.0232  193 ASP A CB  
1450  C CG  . ASP A  193 ? 1.3506 1.2887 1.4745 0.0446  0.0779  0.0266  193 ASP A CG  
1451  O OD1 . ASP A  193 ? 1.3470 1.2837 1.4750 0.0466  0.0787  0.0283  193 ASP A OD1 
1452  O OD2 . ASP A  193 ? 1.6469 1.5865 1.7757 0.0440  0.0738  0.0275  193 ASP A OD2 
1453  N N   . GLN A  194 ? 0.9004 0.8337 0.9948 0.0383  0.0957  0.0166  194 GLN A N   
1454  C CA  . GLN A  194 ? 0.8907 0.8223 0.9787 0.0351  0.1005  0.0131  194 GLN A CA  
1455  C C   . GLN A  194 ? 1.0065 0.9314 1.0994 0.0343  0.1087  0.0123  194 GLN A C   
1456  O O   . GLN A  194 ? 0.9912 0.9122 1.0896 0.0325  0.1125  0.0111  194 GLN A O   
1457  C CB  . GLN A  194 ? 0.9871 0.9234 1.0596 0.0339  0.0997  0.0107  194 GLN A CB  
1458  C CG  . GLN A  194 ? 0.9639 0.8983 1.0286 0.0302  0.1055  0.0069  194 GLN A CG  
1459  C CD  . GLN A  194 ? 1.0106 0.9452 1.0762 0.0277  0.1047  0.0049  194 GLN A CD  
1460  O OE1 . GLN A  194 ? 0.9994 0.9313 1.0616 0.0247  0.1100  0.0018  194 GLN A OE1 
1461  N NE2 . GLN A  194 ? 0.8770 0.8147 0.9471 0.0289  0.0983  0.0067  194 GLN A NE2 
1462  N N   . GLN A  195 ? 1.3867 1.3102 1.4777 0.0356  0.1117  0.0130  195 GLN A N   
1463  C CA  . GLN A  195 ? 1.4950 1.4119 1.5901 0.0350  0.1197  0.0122  195 GLN A CA  
1464  C C   . GLN A  195 ? 1.3337 1.2461 1.4452 0.0366  0.1209  0.0149  195 GLN A C   
1465  O O   . GLN A  195 ? 1.2128 1.1194 1.3304 0.0355  0.1276  0.0142  195 GLN A O   
1466  C CB  . GLN A  195 ? 1.4834 1.4002 1.5718 0.0361  0.1222  0.0125  195 GLN A CB  
1467  C CG  . GLN A  195 ? 1.8015 1.7211 1.8932 0.0397  0.1172  0.0160  195 GLN A CG  
1468  C CD  . GLN A  195 ? 2.0357 1.9559 2.1192 0.0407  0.1194  0.0163  195 GLN A CD  
1469  O OE1 . GLN A  195 ? 1.8673 1.7893 1.9527 0.0435  0.1163  0.0189  195 GLN A OE1 
1470  N NE2 . GLN A  195 ? 2.1120 2.0307 2.1865 0.0383  0.1249  0.0135  195 GLN A NE2 
1471  N N   . SER A  196 ? 1.0690 0.9842 1.1877 0.0389  0.1145  0.0180  196 SER A N   
1472  C CA  . SER A  196 ? 1.0149 0.9270 1.1494 0.0404  0.1146  0.0209  196 SER A CA  
1473  C C   . SER A  196 ? 1.1609 1.0710 1.3015 0.0385  0.1159  0.0202  196 SER A C   
1474  O O   . SER A  196 ? 1.1697 1.0752 1.3224 0.0387  0.1197  0.0216  196 SER A O   
1475  C CB  . SER A  196 ? 0.9953 0.9117 1.1347 0.0428  0.1068  0.0241  196 SER A CB  
1476  O OG  . SER A  196 ? 1.0861 1.0004 1.2406 0.0439  0.1061  0.0270  196 SER A OG  
1477  N N   . LEU A  197 ? 1.1788 1.0923 1.3111 0.0366  0.1130  0.0181  197 LEU A N   
1478  C CA  . LEU A  197 ? 1.0184 0.9307 1.1558 0.0348  0.1136  0.0175  197 LEU A CA  
1479  C C   . LEU A  197 ? 1.0191 0.9272 1.1513 0.0317  0.1212  0.0137  197 LEU A C   
1480  O O   . LEU A  197 ? 0.9942 0.8978 1.1351 0.0307  0.1255  0.0137  197 LEU A O   
1481  C CB  . LEU A  197 ? 0.9283 0.8464 1.0608 0.0344  0.1060  0.0176  197 LEU A CB  
1482  C CG  . LEU A  197 ? 0.9127 0.8340 1.0540 0.0367  0.0988  0.0214  197 LEU A CG  
1483  C CD1 . LEU A  197 ? 0.8644 0.7918 0.9976 0.0363  0.0915  0.0209  197 LEU A CD1 
1484  C CD2 . LEU A  197 ? 0.8708 0.7888 1.0270 0.0369  0.1000  0.0239  197 LEU A CD2 
1485  N N   . TYR A  198 ? 0.9924 0.9021 1.1104 0.0301  0.1228  0.0105  198 TYR A N   
1486  C CA  . TYR A  198 ? 1.0545 0.9610 1.1658 0.0266  0.1294  0.0064  198 TYR A CA  
1487  C C   . TYR A  198 ? 1.1615 1.0657 1.2647 0.0257  0.1354  0.0043  198 TYR A C   
1488  O O   . TYR A  198 ? 1.1373 1.0391 1.2330 0.0224  0.1410  0.0005  198 TYR A O   
1489  C CB  . TYR A  198 ? 1.2283 1.1396 1.3290 0.0243  0.1257  0.0038  198 TYR A CB  
1490  C CG  . TYR A  198 ? 1.0495 0.9648 1.1555 0.0256  0.1181  0.0062  198 TYR A CG  
1491  C CD1 . TYR A  198 ? 0.8684 0.7903 0.9684 0.0271  0.1104  0.0074  198 TYR A CD1 
1492  C CD2 . TYR A  198 ? 0.9938 0.9064 1.1110 0.0254  0.1187  0.0075  198 TYR A CD2 
1493  C CE1 . TYR A  198 ? 0.9603 0.8857 1.0646 0.0281  0.1036  0.0095  198 TYR A CE1 
1494  C CE2 . TYR A  198 ? 0.8983 0.8146 1.0199 0.0264  0.1117  0.0098  198 TYR A CE2 
1495  C CZ  . TYR A  198 ? 0.9047 0.8274 1.0196 0.0277  0.1042  0.0107  198 TYR A CZ  
1496  O OH  . TYR A  198 ? 0.8664 0.7927 0.9853 0.0286  0.0974  0.0128  198 TYR A OH  
1497  N N   . GLN A  199 ? 1.2377 1.1423 1.3422 0.0284  0.1342  0.0067  199 GLN A N   
1498  C CA  . GLN A  199 ? 1.2919 1.1942 1.3897 0.0280  0.1397  0.0053  199 GLN A CA  
1499  C C   . GLN A  199 ? 1.2255 1.1327 1.3063 0.0261  0.1384  0.0027  199 GLN A C   
1500  O O   . GLN A  199 ? 1.2530 1.1634 1.3279 0.0279  0.1359  0.0040  199 GLN A O   
1501  C CB  . GLN A  199 ? 1.4363 1.3310 1.5381 0.0257  0.1492  0.0032  199 GLN A CB  
1502  C CG  . GLN A  199 ? 1.5457 1.4352 1.6566 0.0277  0.1540  0.0052  199 GLN A CG  
1503  C CD  . GLN A  199 ? 1.5422 1.4340 1.6459 0.0295  0.1528  0.0063  199 GLN A CD  
1504  O OE1 . GLN A  199 ? 1.5617 1.4550 1.6520 0.0276  0.1547  0.0038  199 GLN A OE1 
1505  N NE2 . GLN A  199 ? 1.3890 1.2813 1.5017 0.0330  0.1495  0.0101  199 GLN A NE2 
1506  N N   . ASN A  200 ? 1.3013 1.2090 1.3745 0.0226  0.1403  -0.0009 200 ASN A N   
1507  C CA  . ASN A  200 ? 1.2433 1.1557 1.3004 0.0202  0.1395  -0.0037 200 ASN A CA  
1508  C C   . ASN A  200 ? 1.3094 1.2297 1.3614 0.0223  0.1306  -0.0018 200 ASN A C   
1509  O O   . ASN A  200 ? 1.4146 1.3369 1.4735 0.0239  0.1251  0.0002  200 ASN A O   
1510  C CB  . ASN A  200 ? 1.2593 1.1706 1.3107 0.0158  0.1430  -0.0080 200 ASN A CB  
1511  C CG  . ASN A  200 ? 1.2635 1.1664 1.3231 0.0140  0.1515  -0.0096 200 ASN A CG  
1512  O OD1 . ASN A  200 ? 1.4256 1.3236 1.4934 0.0158  0.1555  -0.0079 200 ASN A OD1 
1513  N ND2 . ASN A  200 ? 1.2093 1.1105 1.2671 0.0105  0.1545  -0.0130 200 ASN A ND2 
1514  N N   . ALA A  201 ? 1.1994 1.1243 1.2394 0.0222  0.1293  -0.0022 201 ALA A N   
1515  C CA  . ALA A  201 ? 1.1725 1.1048 1.2073 0.0242  0.1214  -0.0003 201 ALA A CA  
1516  C C   . ALA A  201 ? 1.2942 1.2318 1.3192 0.0214  0.1183  -0.0030 201 ALA A C   
1517  O O   . ALA A  201 ? 1.3400 1.2822 1.3657 0.0226  0.1117  -0.0018 201 ALA A O   
1518  C CB  . ALA A  201 ? 1.1874 1.1221 1.2152 0.0260  0.1213  0.0013  201 ALA A CB  
1519  N N   . ASP A  202 ? 1.3190 1.2560 1.3349 0.0175  0.1231  -0.0067 202 ASP A N   
1520  C CA  . ASP A  202 ? 1.3281 1.2701 1.3343 0.0143  0.1209  -0.0097 202 ASP A CA  
1521  C C   . ASP A  202 ? 1.2415 1.1787 1.2519 0.0111  0.1250  -0.0128 202 ASP A C   
1522  O O   . ASP A  202 ? 1.1998 1.1328 1.2068 0.0077  0.1319  -0.0160 202 ASP A O   
1523  C CB  . ASP A  202 ? 1.5406 1.4864 1.5322 0.0118  0.1228  -0.0118 202 ASP A CB  
1524  C CG  . ASP A  202 ? 1.6493 1.6026 1.6304 0.0096  0.1182  -0.0136 202 ASP A CG  
1525  O OD1 . ASP A  202 ? 1.6342 1.5922 1.6172 0.0119  0.1113  -0.0115 202 ASP A OD1 
1526  O OD2 . ASP A  202 ? 1.5972 1.5518 1.5681 0.0054  0.1215  -0.0172 202 ASP A OD2 
1527  N N   . THR A  203 ? 1.1451 1.0828 1.1627 0.0120  0.1208  -0.0119 203 THR A N   
1528  C CA  . THR A  203 ? 0.9946 0.9276 1.0182 0.0095  0.1244  -0.0141 203 THR A CA  
1529  C C   . THR A  203 ? 0.9464 0.8841 0.9639 0.0070  0.1208  -0.0164 203 THR A C   
1530  O O   . THR A  203 ? 1.0009 0.9456 1.0106 0.0076  0.1148  -0.0159 203 THR A O   
1531  C CB  . THR A  203 ? 0.9481 0.8767 0.9878 0.0125  0.1236  -0.0108 203 THR A CB  
1532  O OG1 . THR A  203 ? 0.8446 0.7783 0.8869 0.0154  0.1153  -0.0077 203 THR A OG1 
1533  C CG2 . THR A  203 ? 0.9490 0.8728 0.9956 0.0148  0.1275  -0.0085 203 THR A CG2 
1534  N N   . TYR A  204 ? 0.9280 0.8615 0.9494 0.0044  0.1245  -0.0188 204 TYR A N   
1535  C CA  . TYR A  204 ? 0.8968 0.8339 0.9133 0.0018  0.1217  -0.0212 204 TYR A CA  
1536  C C   . TYR A  204 ? 0.9226 0.8542 0.9493 0.0008  0.1247  -0.0218 204 TYR A C   
1537  O O   . TYR A  204 ? 0.8367 0.7612 0.8704 0.0001  0.1315  -0.0223 204 TYR A O   
1538  C CB  . TYR A  204 ? 0.8845 0.8242 0.8866 -0.0027 0.1248  -0.0258 204 TYR A CB  
1539  C CG  . TYR A  204 ? 0.9884 0.9211 0.9906 -0.0066 0.1340  -0.0296 204 TYR A CG  
1540  C CD1 . TYR A  204 ? 0.9285 0.8585 0.9322 -0.0098 0.1369  -0.0327 204 TYR A CD1 
1541  C CD2 . TYR A  204 ? 1.0241 0.9527 1.0250 -0.0071 0.1402  -0.0302 204 TYR A CD2 
1542  C CE1 . TYR A  204 ? 1.0185 0.9418 1.0224 -0.0135 0.1458  -0.0363 204 TYR A CE1 
1543  C CE2 . TYR A  204 ? 1.1153 1.0372 1.1162 -0.0108 0.1490  -0.0339 204 TYR A CE2 
1544  C CZ  . TYR A  204 ? 1.1426 1.0618 1.1451 -0.0140 0.1518  -0.0370 204 TYR A CZ  
1545  O OH  . TYR A  204 ? 1.1719 1.0841 1.1745 -0.0179 0.1610  -0.0408 204 TYR A OH  
1546  N N   . VAL A  205 ? 0.8025 0.7373 0.8301 0.0007  0.1196  -0.0215 205 VAL A N   
1547  C CA  . VAL A  205 ? 0.7791 0.7095 0.8149 -0.0007 0.1222  -0.0222 205 VAL A CA  
1548  C C   . VAL A  205 ? 0.7959 0.7287 0.8221 -0.0050 0.1228  -0.0266 205 VAL A C   
1549  O O   . VAL A  205 ? 0.8129 0.7528 0.8295 -0.0055 0.1175  -0.0274 205 VAL A O   
1550  C CB  . VAL A  205 ? 0.6687 0.6005 0.7148 0.0027  0.1156  -0.0180 205 VAL A CB  
1551  C CG1 . VAL A  205 ? 0.6676 0.5940 0.7240 0.0017  0.1190  -0.0180 205 VAL A CG1 
1552  C CG2 . VAL A  205 ? 0.8084 0.7399 0.8621 0.0071  0.1130  -0.0135 205 VAL A CG2 
1553  N N   . PHE A  206 ? 0.7884 0.7155 0.8176 -0.0081 0.1295  -0.0295 206 PHE A N   
1554  C CA  . PHE A  206 ? 0.8249 0.7537 0.8463 -0.0123 0.1305  -0.0337 206 PHE A CA  
1555  C C   . PHE A  206 ? 0.8983 0.8221 0.9300 -0.0130 0.1330  -0.0336 206 PHE A C   
1556  O O   . PHE A  206 ? 0.9067 0.8232 0.9480 -0.0128 0.1393  -0.0331 206 PHE A O   
1557  C CB  . PHE A  206 ? 0.7726 0.7003 0.7828 -0.0169 0.1371  -0.0388 206 PHE A CB  
1558  C CG  . PHE A  206 ? 0.9371 0.8654 0.9402 -0.0218 0.1395  -0.0436 206 PHE A CG  
1559  C CD1 . PHE A  206 ? 0.8753 0.7962 0.8824 -0.0250 0.1478  -0.0467 206 PHE A CD1 
1560  C CD2 . PHE A  206 ? 1.0042 0.9404 0.9970 -0.0232 0.1338  -0.0451 206 PHE A CD2 
1561  C CE1 . PHE A  206 ? 0.9250 0.8462 0.9256 -0.0297 0.1504  -0.0514 206 PHE A CE1 
1562  C CE2 . PHE A  206 ? 0.8703 0.8071 0.8567 -0.0279 0.1361  -0.0496 206 PHE A CE2 
1563  C CZ  . PHE A  206 ? 1.0401 0.9693 1.0303 -0.0312 0.1444  -0.0528 206 PHE A CZ  
1564  N N   . VAL A  207 ? 0.7330 0.6608 0.7627 -0.0136 0.1282  -0.0339 207 VAL A N   
1565  C CA  . VAL A  207 ? 0.7974 0.7211 0.8358 -0.0143 0.1301  -0.0337 207 VAL A CA  
1566  C C   . VAL A  207 ? 0.9136 0.8392 0.9424 -0.0190 0.1315  -0.0386 207 VAL A C   
1567  O O   . VAL A  207 ? 0.9487 0.8815 0.9682 -0.0196 0.1257  -0.0395 207 VAL A O   
1568  C CB  . VAL A  207 ? 0.6832 0.6095 0.7304 -0.0104 0.1225  -0.0287 207 VAL A CB  
1569  C CG1 . VAL A  207 ? 0.5415 0.4638 0.5974 -0.0113 0.1246  -0.0284 207 VAL A CG1 
1570  C CG2 . VAL A  207 ? 0.7663 0.6911 0.8232 -0.0059 0.1208  -0.0239 207 VAL A CG2 
1571  N N   . GLY A  208 ? 0.8598 0.7790 0.8912 -0.0223 0.1395  -0.0418 208 GLY A N   
1572  C CA  . GLY A  208 ? 0.8052 0.7255 0.8276 -0.0272 0.1419  -0.0469 208 GLY A CA  
1573  C C   . GLY A  208 ? 0.9424 0.8562 0.9729 -0.0291 0.1477  -0.0482 208 GLY A C   
1574  O O   . GLY A  208 ? 1.0042 0.9105 1.0453 -0.0283 0.1537  -0.0470 208 GLY A O   
1575  N N   . SER A  209 ? 0.8531 0.7696 0.8788 -0.0317 0.1459  -0.0506 209 SER A N   
1576  C CA  . SER A  209 ? 0.8744 0.7850 0.9056 -0.0343 0.1518  -0.0526 209 SER A CA  
1577  C C   . SER A  209 ? 0.9901 0.9031 1.0083 -0.0400 0.1542  -0.0589 209 SER A C   
1578  O O   . SER A  209 ? 1.0486 0.9663 1.0545 -0.0422 0.1532  -0.0619 209 SER A O   
1579  C CB  . SER A  209 ? 0.9232 0.8346 0.9642 -0.0312 0.1464  -0.0482 209 SER A CB  
1580  O OG  . SER A  209 ? 0.7641 0.6833 0.7968 -0.0315 0.1388  -0.0486 209 SER A OG  
1581  N N   . SER A  210 ? 1.1925 1.1024 1.2134 -0.0425 0.1574  -0.0610 210 SER A N   
1582  C CA  . SER A  210 ? 1.2573 1.1696 1.2664 -0.0481 0.1596  -0.0670 210 SER A CA  
1583  C C   . SER A  210 ? 1.3233 1.2457 1.3225 -0.0478 0.1503  -0.0669 210 SER A C   
1584  O O   . SER A  210 ? 1.1261 1.0530 1.1128 -0.0520 0.1504  -0.0716 210 SER A O   
1585  C CB  . SER A  210 ? 1.3244 1.2308 1.3397 -0.0505 0.1651  -0.0688 210 SER A CB  
1586  O OG  . SER A  210 ? 1.5940 1.4909 1.6169 -0.0518 0.1750  -0.0700 210 SER A OG  
1587  N N   . ARG A  211 ? 1.1496 1.0757 1.1545 -0.0428 0.1422  -0.0614 211 ARG A N   
1588  C CA  . ARG A  211 ? 1.2230 1.1583 1.2202 -0.0420 0.1332  -0.0607 211 ARG A CA  
1589  C C   . ARG A  211 ? 1.1931 1.1337 1.1890 -0.0377 0.1264  -0.0567 211 ARG A C   
1590  O O   . ARG A  211 ? 1.3561 1.3044 1.3417 -0.0381 0.1212  -0.0576 211 ARG A O   
1591  C CB  . ARG A  211 ? 1.1976 1.1332 1.2016 -0.0405 0.1293  -0.0582 211 ARG A CB  
1592  C CG  . ARG A  211 ? 1.3435 1.2760 1.3615 -0.0351 0.1266  -0.0518 211 ARG A CG  
1593  C CD  . ARG A  211 ? 1.6072 1.5372 1.6334 -0.0347 0.1260  -0.0499 211 ARG A CD  
1594  N NE  . ARG A  211 ? 1.7395 1.6754 1.7575 -0.0366 0.1213  -0.0520 211 ARG A NE  
1595  C CZ  . ARG A  211 ? 1.6276 1.5637 1.6506 -0.0357 0.1182  -0.0499 211 ARG A CZ  
1596  N NH1 . ARG A  211 ? 1.4751 1.4062 1.5113 -0.0328 0.1191  -0.0454 211 ARG A NH1 
1597  N NH2 . ARG A  211 ? 1.5352 1.4768 1.5501 -0.0377 0.1143  -0.0521 211 ARG A NH2 
1598  N N   . TYR A  212 ? 1.1158 1.0523 1.1225 -0.0336 0.1266  -0.0522 212 TYR A N   
1599  C CA  . TYR A  212 ? 0.8824 0.8231 0.8893 -0.0292 0.1205  -0.0481 212 TYR A CA  
1600  C C   . TYR A  212 ? 0.9109 0.8509 0.9122 -0.0301 0.1244  -0.0498 212 TYR A C   
1601  O O   . TYR A  212 ? 1.0336 0.9672 1.0365 -0.0326 0.1326  -0.0524 212 TYR A O   
1602  C CB  . TYR A  212 ? 0.7761 0.7131 0.7975 -0.0244 0.1183  -0.0423 212 TYR A CB  
1603  C CG  . TYR A  212 ? 0.8873 0.8292 0.9096 -0.0199 0.1110  -0.0378 212 TYR A CG  
1604  C CD1 . TYR A  212 ? 0.7930 0.7404 0.8156 -0.0175 0.1026  -0.0350 212 TYR A CD1 
1605  C CD2 . TYR A  212 ? 0.9143 0.8550 0.9373 -0.0181 0.1126  -0.0366 212 TYR A CD2 
1606  C CE1 . TYR A  212 ? 0.8644 0.8159 0.8878 -0.0136 0.0963  -0.0311 212 TYR A CE1 
1607  C CE2 . TYR A  212 ? 0.7958 0.7406 0.8198 -0.0141 0.1061  -0.0327 212 TYR A CE2 
1608  C CZ  . TYR A  212 ? 0.8354 0.7855 0.8596 -0.0119 0.0981  -0.0300 212 TYR A CZ  
1609  O OH  . TYR A  212 ? 0.7648 0.7188 0.7900 -0.0081 0.0920  -0.0263 212 TYR A OH  
1610  N N   . SER A  213 ? 0.7360 0.6824 0.7308 -0.0281 0.1188  -0.0483 213 SER A N   
1611  C CA  . SER A  213 ? 0.8385 0.7850 0.8276 -0.0286 0.1218  -0.0493 213 SER A CA  
1612  C C   . SER A  213 ? 0.8935 0.8470 0.8791 -0.0249 0.1140  -0.0458 213 SER A C   
1613  O O   . SER A  213 ? 1.0027 0.9636 0.9807 -0.0251 0.1081  -0.0461 213 SER A O   
1614  C CB  . SER A  213 ? 0.7580 0.7055 0.7349 -0.0344 0.1268  -0.0554 213 SER A CB  
1615  O OG  . SER A  213 ? 0.8213 0.7684 0.7927 -0.0352 0.1302  -0.0564 213 SER A OG  
1616  N N   . LYS A  214 ? 0.7824 0.7334 0.7739 -0.0214 0.1143  -0.0425 214 LYS A N   
1617  C CA  . LYS A  214 ? 0.8678 0.8248 0.8563 -0.0178 0.1078  -0.0392 214 LYS A CA  
1618  C C   . LYS A  214 ? 0.9939 0.9469 0.9871 -0.0152 0.1107  -0.0368 214 LYS A C   
1619  O O   . LYS A  214 ? 0.8620 0.8081 0.8661 -0.0139 0.1146  -0.0353 214 LYS A O   
1620  C CB  . LYS A  214 ? 0.8102 0.7710 0.8037 -0.0141 0.0996  -0.0352 214 LYS A CB  
1621  C CG  . LYS A  214 ? 0.9435 0.9108 0.9326 -0.0109 0.0932  -0.0323 214 LYS A CG  
1622  C CD  . LYS A  214 ? 1.0990 1.0731 1.0847 -0.0101 0.0856  -0.0315 214 LYS A CD  
1623  C CE  . LYS A  214 ? 1.1623 1.1360 1.1580 -0.0057 0.0802  -0.0267 214 LYS A CE  
1624  N NZ  . LYS A  214 ? 1.1524 1.1277 1.1494 -0.0020 0.0774  -0.0233 214 LYS A NZ  
1625  N N   . LYS A  215 ? 0.8838 0.8415 0.8689 -0.0145 0.1087  -0.0365 215 LYS A N   
1626  C CA  . LYS A  215 ? 0.8758 0.8307 0.8641 -0.0120 0.1110  -0.0342 215 LYS A CA  
1627  C C   . LYS A  215 ? 0.8421 0.8011 0.8339 -0.0070 0.1036  -0.0293 215 LYS A C   
1628  O O   . LYS A  215 ? 0.9186 0.8849 0.9034 -0.0064 0.0976  -0.0288 215 LYS A O   
1629  C CB  . LYS A  215 ? 0.9432 0.9000 0.9196 -0.0149 0.1147  -0.0373 215 LYS A CB  
1630  C CG  . LYS A  215 ? 0.9717 0.9248 0.9507 -0.0130 0.1183  -0.0355 215 LYS A CG  
1631  C CD  . LYS A  215 ? 1.0584 1.0133 1.0250 -0.0165 0.1224  -0.0388 215 LYS A CD  
1632  C CE  . LYS A  215 ? 1.2928 1.2424 1.2625 -0.0152 0.1276  -0.0376 215 LYS A CE  
1633  N NZ  . LYS A  215 ? 1.1744 1.1256 1.1316 -0.0189 0.1318  -0.0408 215 LYS A NZ  
1634  N N   . PHE A  216 ? 0.7980 0.7524 0.8009 -0.0036 0.1042  -0.0258 216 PHE A N   
1635  C CA  . PHE A  216 ? 0.8007 0.7582 0.8082 0.0010  0.0976  -0.0213 216 PHE A CA  
1636  C C   . PHE A  216 ? 0.8109 0.7681 0.8173 0.0032  0.0988  -0.0194 216 PHE A C   
1637  O O   . PHE A  216 ? 0.8886 0.8401 0.8984 0.0028  0.1050  -0.0199 216 PHE A O   
1638  C CB  . PHE A  216 ? 0.9068 0.8601 0.9284 0.0035  0.0963  -0.0181 216 PHE A CB  
1639  C CG  . PHE A  216 ? 0.8616 0.8147 0.8852 0.0016  0.0951  -0.0193 216 PHE A CG  
1640  C CD1 . PHE A  216 ? 0.8612 0.8085 0.8886 -0.0012 0.1015  -0.0218 216 PHE A CD1 
1641  C CD2 . PHE A  216 ? 0.7874 0.7461 0.8093 0.0027  0.0878  -0.0180 216 PHE A CD2 
1642  C CE1 . PHE A  216 ? 0.8267 0.7738 0.8562 -0.0028 0.1006  -0.0227 216 PHE A CE1 
1643  C CE2 . PHE A  216 ? 0.9373 0.8958 0.9611 0.0010  0.0868  -0.0191 216 PHE A CE2 
1644  C CZ  . PHE A  216 ? 0.8153 0.7680 0.8429 -0.0017 0.0932  -0.0214 216 PHE A CZ  
1645  N N   . LYS A  217 ? 0.8652 0.8285 0.8668 0.0057  0.0929  -0.0173 217 LYS A N   
1646  C CA  . LYS A  217 ? 0.8191 0.7826 0.8204 0.0084  0.0932  -0.0149 217 LYS A CA  
1647  C C   . LYS A  217 ? 0.8739 0.8379 0.8844 0.0129  0.0878  -0.0104 217 LYS A C   
1648  O O   . LYS A  217 ? 0.8780 0.8471 0.8869 0.0142  0.0814  -0.0091 217 LYS A O   
1649  C CB  . LYS A  217 ? 0.9569 0.9271 0.9450 0.0075  0.0914  -0.0159 217 LYS A CB  
1650  C CG  . LYS A  217 ? 0.9861 0.9547 0.9666 0.0044  0.0980  -0.0189 217 LYS A CG  
1651  C CD  . LYS A  217 ? 1.1624 1.1253 1.1488 0.0064  0.1025  -0.0170 217 LYS A CD  
1652  C CE  . LYS A  217 ? 1.2522 1.2133 1.2301 0.0032  0.1091  -0.0200 217 LYS A CE  
1653  N NZ  . LYS A  217 ? 1.3813 1.3370 1.3647 0.0052  0.1135  -0.0181 217 LYS A NZ  
1654  N N   . PRO A  218 ? 0.9420 0.9005 0.9619 0.0151  0.0905  -0.0081 218 PRO A N   
1655  C CA  . PRO A  218 ? 0.8874 0.8459 0.9166 0.0191  0.0859  -0.0039 218 PRO A CA  
1656  C C   . PRO A  218 ? 0.9258 0.8905 0.9487 0.0215  0.0806  -0.0021 218 PRO A C   
1657  O O   . PRO A  218 ? 0.7922 0.7584 0.8082 0.0216  0.0825  -0.0024 218 PRO A O   
1658  C CB  . PRO A  218 ? 0.8338 0.7859 0.8715 0.0203  0.0913  -0.0026 218 PRO A CB  
1659  C CG  . PRO A  218 ? 0.8901 0.8374 0.9268 0.0168  0.0985  -0.0060 218 PRO A CG  
1660  C CD  . PRO A  218 ? 0.9460 0.8979 0.9688 0.0136  0.0984  -0.0095 218 PRO A CD  
1661  N N   . GLU A  219 ? 0.9361 0.9043 0.9616 0.0233  0.0741  -0.0001 219 GLU A N   
1662  C CA  . GLU A  219 ? 0.7473 0.7211 0.7681 0.0257  0.0690  0.0018  219 GLU A CA  
1663  C C   . GLU A  219 ? 0.7964 0.7678 0.8264 0.0293  0.0674  0.0055  219 GLU A C   
1664  O O   . GLU A  219 ? 0.7558 0.7270 0.7932 0.0306  0.0633  0.0074  219 GLU A O   
1665  C CB  . GLU A  219 ? 0.7272 0.7064 0.7441 0.0253  0.0630  0.0015  219 GLU A CB  
1666  C CG  . GLU A  219 ? 0.9046 0.8863 0.9126 0.0216  0.0642  -0.0022 219 GLU A CG  
1667  C CD  . GLU A  219 ? 1.0355 1.0226 1.0401 0.0212  0.0584  -0.0025 219 GLU A CD  
1668  O OE1 . GLU A  219 ? 0.8577 0.8459 0.8672 0.0237  0.0534  0.0001  219 GLU A OE1 
1669  O OE2 . GLU A  219 ? 1.0744 1.0644 1.0712 0.0183  0.0588  -0.0055 219 GLU A OE2 
1670  N N   . ILE A  220 ? 0.9005 0.8703 0.9300 0.0307  0.0706  0.0065  220 ILE A N   
1671  C CA  . ILE A  220 ? 0.8523 0.8193 0.8907 0.0339  0.0700  0.0097  220 ILE A CA  
1672  C C   . ILE A  220 ? 0.7713 0.7431 0.8071 0.0366  0.0646  0.0120  220 ILE A C   
1673  O O   . ILE A  220 ? 0.7966 0.7720 0.8237 0.0371  0.0647  0.0119  220 ILE A O   
1674  C CB  . ILE A  220 ? 0.7622 0.7246 0.8019 0.0342  0.0764  0.0098  220 ILE A CB  
1675  C CG1 . ILE A  220 ? 0.7773 0.7344 0.8204 0.0314  0.0822  0.0075  220 ILE A CG1 
1676  C CG2 . ILE A  220 ? 0.8410 0.8006 0.8903 0.0374  0.0758  0.0131  220 ILE A CG2 
1677  C CD1 . ILE A  220 ? 1.0640 1.0169 1.1058 0.0309  0.0891  0.0067  220 ILE A CD1 
1678  N N   . ALA A  221 ? 0.7250 0.6968 0.7685 0.0383  0.0602  0.0142  221 ALA A N   
1679  C CA  . ALA A  221 ? 0.6942 0.6699 0.7364 0.0408  0.0553  0.0163  221 ALA A CA  
1680  C C   . ALA A  221 ? 0.8559 0.8301 0.9084 0.0422  0.0514  0.0185  221 ALA A C   
1681  O O   . ALA A  221 ? 0.8378 0.8087 0.8981 0.0412  0.0520  0.0185  221 ALA A O   
1682  C CB  . ALA A  221 ? 0.6645 0.6465 0.6966 0.0400  0.0515  0.0149  221 ALA A CB  
1683  N N   . ILE A  222 ? 0.9619 0.9386 1.0144 0.0445  0.0476  0.0204  222 ILE A N   
1684  C CA  . ILE A  222 ? 0.9484 0.9241 1.0100 0.0456  0.0437  0.0224  222 ILE A CA  
1685  C C   . ILE A  222 ? 0.8836 0.8633 0.9427 0.0448  0.0379  0.0220  222 ILE A C   
1686  O O   . ILE A  222 ? 0.9884 0.9724 1.0405 0.0455  0.0351  0.0219  222 ILE A O   
1687  C CB  . ILE A  222 ? 1.0491 1.0245 1.1132 0.0484  0.0431  0.0247  222 ILE A CB  
1688  C CG1 . ILE A  222 ? 1.0107 0.9819 1.0779 0.0493  0.0489  0.0253  222 ILE A CG1 
1689  C CG2 . ILE A  222 ? 0.6904 0.6650 0.7635 0.0491  0.0390  0.0265  222 ILE A CG2 
1690  C CD1 . ILE A  222 ? 1.0229 0.9889 1.1004 0.0484  0.0516  0.0257  222 ILE A CD1 
1691  N N   . ARG A  223 ? 0.7550 0.7333 0.8199 0.0432  0.0364  0.0219  223 ARG A N   
1692  C CA  . ARG A  223 ? 0.8456 0.8272 0.9092 0.0423  0.0310  0.0216  223 ARG A CA  
1693  C C   . ARG A  223 ? 0.8770 0.8581 0.9486 0.0435  0.0270  0.0240  223 ARG A C   
1694  O O   . ARG A  223 ? 0.9214 0.8989 1.0019 0.0442  0.0286  0.0257  223 ARG A O   
1695  C CB  . ARG A  223 ? 0.7833 0.7640 0.8480 0.0398  0.0315  0.0202  223 ARG A CB  
1696  C CG  . ARG A  223 ? 0.7509 0.7330 0.8066 0.0380  0.0346  0.0173  223 ARG A CG  
1697  C CD  . ARG A  223 ? 0.6979 0.6757 0.7551 0.0375  0.0411  0.0166  223 ARG A CD  
1698  N NE  . ARG A  223 ? 0.6662 0.6447 0.7163 0.0350  0.0440  0.0136  223 ARG A NE  
1699  C CZ  . ARG A  223 ? 0.7064 0.6816 0.7556 0.0338  0.0499  0.0121  223 ARG A CZ  
1700  N NH1 . ARG A  223 ? 0.7738 0.7449 0.8291 0.0352  0.0536  0.0135  223 ARG A NH1 
1701  N NH2 . ARG A  223 ? 0.7017 0.6779 0.7440 0.0312  0.0524  0.0091  223 ARG A NH2 
1702  N N   . PRO A  224 ? 0.8330 0.8177 0.9015 0.0435  0.0219  0.0241  224 PRO A N   
1703  C CA  . PRO A  224 ? 0.8619 0.8464 0.9371 0.0440  0.0177  0.0261  224 PRO A CA  
1704  C C   . PRO A  224 ? 0.8964 0.8779 0.9817 0.0428  0.0176  0.0273  224 PRO A C   
1705  O O   . PRO A  224 ? 0.8300 0.8115 0.9152 0.0410  0.0176  0.0264  224 PRO A O   
1706  C CB  . PRO A  224 ? 0.7466 0.7355 0.8155 0.0432  0.0129  0.0252  224 PRO A CB  
1707  C CG  . PRO A  224 ? 0.9696 0.9613 1.0280 0.0435  0.0146  0.0233  224 PRO A CG  
1708  C CD  . PRO A  224 ? 0.8727 0.8620 0.9309 0.0428  0.0198  0.0223  224 PRO A CD  
1709  N N   . LYS A  225 ? 1.0924 1.0717 1.1867 0.0437  0.0174  0.0295  225 LYS A N   
1710  C CA  . LYS A  225 ? 1.0812 1.0577 1.1862 0.0429  0.0176  0.0312  225 LYS A CA  
1711  C C   . LYS A  225 ? 1.0769 1.0553 1.1835 0.0410  0.0132  0.0315  225 LYS A C   
1712  O O   . LYS A  225 ? 1.0665 1.0475 1.1716 0.0407  0.0082  0.0320  225 LYS A O   
1713  C CB  . LYS A  225 ? 1.2102 1.1849 1.3242 0.0441  0.0172  0.0336  225 LYS A CB  
1714  C CG  . LYS A  225 ? 1.4546 1.4263 1.5701 0.0459  0.0224  0.0337  225 LYS A CG  
1715  C CD  . LYS A  225 ? 1.6062 1.5761 1.7311 0.0469  0.0219  0.0360  225 LYS A CD  
1716  C CE  . LYS A  225 ? 1.7739 1.7406 1.9005 0.0487  0.0274  0.0362  225 LYS A CE  
1717  N NZ  . LYS A  225 ? 1.8127 1.7761 1.9417 0.0482  0.0326  0.0357  225 LYS A NZ  
1718  N N   . VAL A  226 ? 0.8691 0.8458 0.9785 0.0397  0.0153  0.0313  226 VAL A N   
1719  C CA  . VAL A  226 ? 0.8686 0.8463 0.9816 0.0380  0.0118  0.0322  226 VAL A CA  
1720  C C   . VAL A  226 ? 0.9042 0.8785 1.0292 0.0378  0.0142  0.0345  226 VAL A C   
1721  O O   . VAL A  226 ? 0.9243 0.8957 1.0508 0.0377  0.0193  0.0338  226 VAL A O   
1722  C CB  . VAL A  226 ? 0.8473 0.8265 0.9523 0.0364  0.0122  0.0298  226 VAL A CB  
1723  C CG1 . VAL A  226 ? 0.7509 0.7309 0.8601 0.0347  0.0088  0.0311  226 VAL A CG1 
1724  C CG2 . VAL A  226 ? 0.8250 0.8078 0.9184 0.0366  0.0102  0.0276  226 VAL A CG2 
1725  N N   . ARG A  227 ? 1.0441 1.0188 1.1778 0.0378  0.0106  0.0374  227 ARG A N   
1726  C CA  . ARG A  227 ? 0.9151 0.8871 1.0613 0.0379  0.0125  0.0401  227 ARG A CA  
1727  C C   . ARG A  227 ? 0.9784 0.9469 1.1285 0.0395  0.0180  0.0402  227 ARG A C   
1728  O O   . ARG A  227 ? 0.9029 0.8680 1.0595 0.0395  0.0226  0.0408  227 ARG A O   
1729  C CB  . ARG A  227 ? 0.8003 0.7710 0.9490 0.0365  0.0143  0.0402  227 ARG A CB  
1730  C CG  . ARG A  227 ? 0.8169 0.7908 0.9643 0.0349  0.0089  0.0409  227 ARG A CG  
1731  C CD  . ARG A  227 ? 0.9000 0.8723 1.0481 0.0337  0.0115  0.0405  227 ARG A CD  
1732  N NE  . ARG A  227 ? 0.8194 0.7927 0.9760 0.0327  0.0082  0.0438  227 ARG A NE  
1733  C CZ  . ARG A  227 ? 0.9819 0.9534 1.1512 0.0332  0.0093  0.0472  227 ARG A CZ  
1734  N NH1 . ARG A  227 ? 1.0719 1.0403 1.2467 0.0345  0.0138  0.0476  227 ARG A NH1 
1735  N NH2 . ARG A  227 ? 0.8885 0.8614 1.0651 0.0323  0.0059  0.0504  227 ARG A NH2 
1736  N N   . ASP A  228 ? 1.1130 1.0820 1.2590 0.0408  0.0178  0.0395  228 ASP A N   
1737  C CA  . ASP A  228 ? 1.2047 1.1705 1.3546 0.0425  0.0225  0.0398  228 ASP A CA  
1738  C C   . ASP A  228 ? 1.2241 1.1875 1.3675 0.0428  0.0287  0.0373  228 ASP A C   
1739  O O   . ASP A  228 ? 1.3581 1.3190 1.5026 0.0442  0.0328  0.0372  228 ASP A O   
1740  C CB  . ASP A  228 ? 1.5100 1.4734 1.6740 0.0426  0.0237  0.0429  228 ASP A CB  
1741  C CG  . ASP A  228 ? 1.8614 1.8261 2.0317 0.0432  0.0199  0.0452  228 ASP A CG  
1742  O OD1 . ASP A  228 ? 1.8819 1.8456 2.0510 0.0446  0.0217  0.0447  228 ASP A OD1 
1743  O OD2 . ASP A  228 ? 2.0011 1.9679 2.1778 0.0421  0.0153  0.0474  228 ASP A OD2 
1744  N N   . GLN A  229 ? 1.0443 1.0085 1.1808 0.0415  0.0293  0.0352  229 GLN A N   
1745  C CA  . GLN A  229 ? 0.9993 0.9614 1.1292 0.0413  0.0351  0.0326  229 GLN A CA  
1746  C C   . GLN A  229 ? 0.9254 0.8907 1.0422 0.0415  0.0342  0.0302  229 GLN A C   
1747  O O   . GLN A  229 ? 0.9977 0.9666 1.1081 0.0407  0.0301  0.0292  229 GLN A O   
1748  C CB  . GLN A  229 ? 0.9313 0.8920 1.0621 0.0394  0.0373  0.0316  229 GLN A CB  
1749  C CG  . GLN A  229 ? 0.8307 0.7892 0.9747 0.0391  0.0373  0.0345  229 GLN A CG  
1750  C CD  . GLN A  229 ? 0.8888 0.8435 1.0427 0.0404  0.0415  0.0363  229 GLN A CD  
1751  O OE1 . GLN A  229 ? 0.8343 0.7863 0.9850 0.0410  0.0467  0.0347  229 GLN A OE1 
1752  N NE2 . GLN A  229 ? 1.0875 1.0418 1.2532 0.0408  0.0392  0.0397  229 GLN A NE2 
1753  N N   . GLU A  230 ? 0.9341 0.8980 1.0471 0.0428  0.0382  0.0293  230 GLU A N   
1754  C CA  . GLU A  230 ? 0.9239 0.8907 1.0246 0.0431  0.0380  0.0273  230 GLU A CA  
1755  C C   . GLU A  230 ? 0.9313 0.8978 1.0248 0.0414  0.0420  0.0245  230 GLU A C   
1756  O O   . GLU A  230 ? 0.9900 0.9595 1.0728 0.0411  0.0418  0.0226  230 GLU A O   
1757  C CB  . GLU A  230 ? 1.0369 1.0029 1.1369 0.0453  0.0401  0.0281  230 GLU A CB  
1758  N N   . GLY A  231 ? 0.6978 0.6604 0.7974 0.0402  0.0459  0.0243  231 GLY A N   
1759  C CA  . GLY A  231 ? 0.7657 0.7274 0.8594 0.0382  0.0500  0.0215  231 GLY A CA  
1760  C C   . GLY A  231 ? 0.8332 0.7966 0.9261 0.0362  0.0471  0.0207  231 GLY A C   
1761  O O   . GLY A  231 ? 0.7385 0.7032 0.8370 0.0365  0.0424  0.0227  231 GLY A O   
1762  N N   . ARG A  232 ? 0.7859 0.7494 0.8718 0.0341  0.0500  0.0178  232 ARG A N   
1763  C CA  . ARG A  232 ? 0.7139 0.6789 0.7986 0.0321  0.0479  0.0167  232 ARG A CA  
1764  C C   . ARG A  232 ? 0.7291 0.6897 0.8170 0.0301  0.0536  0.0152  232 ARG A C   
1765  O O   . ARG A  232 ? 0.6695 0.6265 0.7580 0.0299  0.0595  0.0142  232 ARG A O   
1766  C CB  . ARG A  232 ? 0.7561 0.7262 0.8281 0.0311  0.0451  0.0143  232 ARG A CB  
1767  C CG  . ARG A  232 ? 0.7190 0.6936 0.7884 0.0328  0.0389  0.0158  232 ARG A CG  
1768  C CD  . ARG A  232 ? 0.6605 0.6355 0.7371 0.0330  0.0339  0.0180  232 ARG A CD  
1769  N NE  . ARG A  232 ? 0.7883 0.7672 0.8625 0.0344  0.0283  0.0192  232 ARG A NE  
1770  C CZ  . ARG A  232 ? 0.8418 0.8202 0.9208 0.0364  0.0268  0.0215  232 ARG A CZ  
1771  N NH1 . ARG A  232 ? 0.7310 0.7053 0.8177 0.0374  0.0305  0.0228  232 ARG A NH1 
1772  N NH2 . ARG A  232 ? 0.8563 0.8380 0.9326 0.0374  0.0220  0.0222  232 ARG A NH2 
1773  N N   . MET A  233 ? 0.7820 0.7427 0.8720 0.0285  0.0521  0.0150  233 MET A N   
1774  C CA  . MET A  233 ? 0.7456 0.7023 0.8387 0.0264  0.0575  0.0135  233 MET A CA  
1775  C C   . MET A  233 ? 0.6557 0.6149 0.7430 0.0242  0.0556  0.0115  233 MET A C   
1776  O O   . MET A  233 ? 0.6078 0.5685 0.6990 0.0243  0.0510  0.0133  233 MET A O   
1777  C CB  . MET A  233 ? 0.6534 0.6059 0.7610 0.0273  0.0590  0.0167  233 MET A CB  
1778  C CG  . MET A  233 ? 0.7123 0.6597 0.8243 0.0255  0.0656  0.0154  233 MET A CG  
1779  S SD  . MET A  233 ? 0.9471 0.8896 1.0771 0.0269  0.0677  0.0197  233 MET A SD  
1780  C CE  . MET A  233 ? 0.7897 0.7305 0.9227 0.0293  0.0699  0.0209  233 MET A CE  
1781  N N   . ASN A  234 ? 0.6698 0.6293 0.7475 0.0219  0.0591  0.0076  234 ASN A N   
1782  C CA  . ASN A  234 ? 0.6643 0.6261 0.7360 0.0195  0.0578  0.0052  234 ASN A CA  
1783  C C   . ASN A  234 ? 0.5907 0.5476 0.6689 0.0176  0.0625  0.0046  234 ASN A C   
1784  O O   . ASN A  234 ? 0.5580 0.5100 0.6399 0.0170  0.0689  0.0038  234 ASN A O   
1785  C CB  . ASN A  234 ? 0.5512 0.5163 0.6093 0.0177  0.0591  0.0014  234 ASN A CB  
1786  C CG  . ASN A  234 ? 0.5626 0.5333 0.6138 0.0196  0.0539  0.0022  234 ASN A CG  
1787  O OD1 . ASN A  234 ? 0.6193 0.5912 0.6754 0.0219  0.0492  0.0052  234 ASN A OD1 
1788  N ND2 . ASN A  234 ? 0.7514 0.7255 0.7913 0.0183  0.0547  -0.0006 234 ASN A ND2 
1789  N N   . TYR A  235 ? 0.4552 0.4134 0.5349 0.0167  0.0594  0.0051  235 TYR A N   
1790  C CA  . TYR A  235 ? 0.4823 0.4361 0.5691 0.0151  0.0633  0.0050  235 TYR A CA  
1791  C C   . TYR A  235 ? 0.5449 0.4996 0.6229 0.0119  0.0654  0.0009  235 TYR A C   
1792  O O   . TYR A  235 ? 0.5974 0.5570 0.6677 0.0112  0.0607  -0.0002 235 TYR A O   
1793  C CB  . TYR A  235 ? 0.5406 0.4946 0.6375 0.0166  0.0587  0.0093  235 TYR A CB  
1794  C CG  . TYR A  235 ? 0.6961 0.6501 0.8015 0.0195  0.0559  0.0133  235 TYR A CG  
1795  C CD1 . TYR A  235 ? 0.5985 0.5572 0.7007 0.0212  0.0492  0.0149  235 TYR A CD1 
1796  C CD2 . TYR A  235 ? 0.5411 0.4902 0.6575 0.0206  0.0603  0.0155  235 TYR A CD2 
1797  C CE1 . TYR A  235 ? 0.6472 0.6058 0.7568 0.0236  0.0468  0.0183  235 TYR A CE1 
1798  C CE2 . TYR A  235 ? 0.5791 0.5283 0.7032 0.0231  0.0578  0.0191  235 TYR A CE2 
1799  C CZ  . TYR A  235 ? 0.6551 0.6091 0.7757 0.0245  0.0510  0.0205  235 TYR A CZ  
1800  O OH  . TYR A  235 ? 0.5762 0.5303 0.7044 0.0268  0.0486  0.0239  235 TYR A OH  
1801  N N   . TYR A  236 ? 0.5217 0.4715 0.6010 0.0097  0.0727  -0.0015 236 TYR A N   
1802  C CA  . TYR A  236 ? 0.5884 0.5384 0.6596 0.0062  0.0757  -0.0058 236 TYR A CA  
1803  C C   . TYR A  236 ? 0.6680 0.6129 0.7477 0.0048  0.0799  -0.0056 236 TYR A C   
1804  O O   . TYR A  236 ? 0.6279 0.5682 0.7194 0.0063  0.0826  -0.0026 236 TYR A O   
1805  C CB  . TYR A  236 ? 0.4733 0.4226 0.5356 0.0042  0.0811  -0.0100 236 TYR A CB  
1806  C CG  . TYR A  236 ? 0.6800 0.6347 0.7329 0.0053  0.0772  -0.0103 236 TYR A CG  
1807  C CD1 . TYR A  236 ? 0.6282 0.5824 0.6847 0.0082  0.0765  -0.0077 236 TYR A CD1 
1808  C CD2 . TYR A  236 ? 0.6876 0.6480 0.7284 0.0036  0.0743  -0.0132 236 TYR A CD2 
1809  C CE1 . TYR A  236 ? 0.6866 0.6456 0.7349 0.0094  0.0732  -0.0078 236 TYR A CE1 
1810  C CE2 . TYR A  236 ? 0.7186 0.6842 0.7514 0.0048  0.0709  -0.0132 236 TYR A CE2 
1811  C CZ  . TYR A  236 ? 0.7147 0.6795 0.7513 0.0078  0.0704  -0.0105 236 TYR A CZ  
1812  O OH  . TYR A  236 ? 0.6648 0.6345 0.6937 0.0091  0.0672  -0.0102 236 TYR A OH  
1813  N N   . TRP A  237 ? 0.6517 0.5975 0.7257 0.0020  0.0806  -0.0085 237 TRP A N   
1814  C CA  . TRP A  237 ? 0.5051 0.4460 0.5863 0.0005  0.0850  -0.0085 237 TRP A CA  
1815  C C   . TRP A  237 ? 0.4782 0.4189 0.5501 -0.0036 0.0890  -0.0139 237 TRP A C   
1816  O O   . TRP A  237 ? 0.6265 0.5721 0.6864 -0.0051 0.0867  -0.0170 237 TRP A O   
1817  C CB  . TRP A  237 ? 0.4770 0.4196 0.5656 0.0022  0.0792  -0.0044 237 TRP A CB  
1818  C CG  . TRP A  237 ? 0.5261 0.4748 0.6054 0.0014  0.0727  -0.0055 237 TRP A CG  
1819  C CD1 . TRP A  237 ? 0.5550 0.5095 0.6297 0.0033  0.0654  -0.0040 237 TRP A CD1 
1820  C CD2 . TRP A  237 ? 0.6033 0.5529 0.6772 -0.0014 0.0731  -0.0083 237 TRP A CD2 
1821  N NE1 . TRP A  237 ? 0.5491 0.5080 0.6159 0.0019  0.0613  -0.0057 237 TRP A NE1 
1822  C CE2 . TRP A  237 ? 0.5913 0.5474 0.6574 -0.0010 0.0659  -0.0084 237 TRP A CE2 
1823  C CE3 . TRP A  237 ? 0.6885 0.6339 0.7635 -0.0043 0.0793  -0.0109 237 TRP A CE3 
1824  C CZ2 . TRP A  237 ? 0.6439 0.6026 0.7034 -0.0034 0.0644  -0.0108 237 TRP A CZ2 
1825  C CZ3 . TRP A  237 ? 0.7116 0.6595 0.7799 -0.0067 0.0777  -0.0134 237 TRP A CZ3 
1826  C CH2 . TRP A  237 ? 0.6460 0.6007 0.7068 -0.0062 0.0703  -0.0133 237 TRP A CH2 
1827  N N   . THR A  238 ? 0.5777 0.5129 0.6556 -0.0054 0.0950  -0.0148 238 THR A N   
1828  C CA  . THR A  238 ? 0.6160 0.5502 0.6861 -0.0096 0.0995  -0.0199 238 THR A CA  
1829  C C   . THR A  238 ? 0.6296 0.5577 0.7095 -0.0107 0.1048  -0.0192 238 THR A C   
1830  O O   . THR A  238 ? 0.6293 0.5530 0.7218 -0.0084 0.1067  -0.0153 238 THR A O   
1831  C CB  . THR A  238 ? 0.6602 0.5931 0.7218 -0.0123 0.1056  -0.0247 238 THR A CB  
1832  O OG1 . THR A  238 ? 0.7330 0.6662 0.7857 -0.0167 0.1089  -0.0299 238 THR A OG1 
1833  C CG2 . THR A  238 ? 0.6047 0.5300 0.6756 -0.0119 0.1132  -0.0240 238 THR A CG2 
1834  N N   . LEU A  239 ? 0.7664 0.6943 0.8407 -0.0141 0.1072  -0.0230 239 LEU A N   
1835  C CA  . LEU A  239 ? 0.7973 0.7193 0.8799 -0.0155 0.1126  -0.0228 239 LEU A CA  
1836  C C   . LEU A  239 ? 0.7882 0.7051 0.8667 -0.0196 0.1222  -0.0284 239 LEU A C   
1837  O O   . LEU A  239 ? 0.9369 0.8561 1.0043 -0.0233 0.1232  -0.0334 239 LEU A O   
1838  C CB  . LEU A  239 ? 0.7466 0.6719 0.8272 -0.0163 0.1081  -0.0225 239 LEU A CB  
1839  C CG  . LEU A  239 ? 0.5611 0.4908 0.6463 -0.0126 0.0990  -0.0170 239 LEU A CG  
1840  C CD1 . LEU A  239 ? 0.7531 0.6861 0.8340 -0.0140 0.0951  -0.0176 239 LEU A CD1 
1841  C CD2 . LEU A  239 ? 0.6336 0.5590 0.7345 -0.0096 0.1001  -0.0113 239 LEU A CD2 
1842  N N   . VAL A  240 ? 0.7725 0.6825 0.8599 -0.0192 0.1293  -0.0277 240 VAL A N   
1843  C CA  . VAL A  240 ? 0.8832 0.7876 0.9674 -0.0232 0.1391  -0.0330 240 VAL A CA  
1844  C C   . VAL A  240 ? 0.7819 0.6812 0.8717 -0.0255 0.1445  -0.0340 240 VAL A C   
1845  O O   . VAL A  240 ? 0.7241 0.6196 0.8272 -0.0230 0.1454  -0.0295 240 VAL A O   
1846  C CB  . VAL A  240 ? 0.8147 0.7137 0.9049 -0.0222 0.1452  -0.0324 240 VAL A CB  
1847  C CG1 . VAL A  240 ? 0.7356 0.6357 0.8364 -0.0170 0.1399  -0.0258 240 VAL A CG1 
1848  C CG2 . VAL A  240 ? 0.8652 0.7553 0.9630 -0.0245 0.1557  -0.0343 240 VAL A CG2 
1849  N N   . GLU A  241 ? 0.8855 0.7849 0.9650 -0.0301 0.1481  -0.0400 241 GLU A N   
1850  C CA  . GLU A  241 ? 0.8628 0.7577 0.9456 -0.0328 0.1533  -0.0419 241 GLU A CA  
1851  C C   . GLU A  241 ? 0.9268 0.8122 1.0212 -0.0332 0.1633  -0.0415 241 GLU A C   
1852  O O   . GLU A  241 ? 1.0060 0.8880 1.1019 -0.0331 0.1681  -0.0423 241 GLU A O   
1853  C CB  . GLU A  241 ? 1.0745 0.9717 1.1427 -0.0382 0.1555  -0.0490 241 GLU A CB  
1854  C CG  . GLU A  241 ? 1.2897 1.1964 1.3462 -0.0382 0.1461  -0.0497 241 GLU A CG  
1855  C CD  . GLU A  241 ? 1.5551 1.4649 1.6146 -0.0367 0.1400  -0.0467 241 GLU A CD  
1856  O OE1 . GLU A  241 ? 1.6358 1.5529 1.6908 -0.0346 0.1311  -0.0445 241 GLU A OE1 
1857  O OE2 . GLU A  241 ? 1.6649 1.5697 1.7313 -0.0378 0.1444  -0.0465 241 GLU A OE2 
1858  N N   . PRO A  242 ? 1.1002 0.9812 1.2032 -0.0336 0.1668  -0.0402 242 PRO A N   
1859  C CA  . PRO A  242 ? 1.1116 0.9831 1.2256 -0.0343 0.1772  -0.0402 242 PRO A CA  
1860  C C   . PRO A  242 ? 1.0853 0.9526 1.1906 -0.0394 0.1863  -0.0476 242 PRO A C   
1861  O O   . PRO A  242 ? 0.9048 0.7744 0.9979 -0.0437 0.1869  -0.0533 242 PRO A O   
1862  C CB  . PRO A  242 ? 0.8544 0.7237 0.9744 -0.0350 0.1784  -0.0391 242 PRO A CB  
1863  C CG  . PRO A  242 ? 0.9044 0.7817 1.0222 -0.0323 0.1672  -0.0352 242 PRO A CG  
1864  C CD  . PRO A  242 ? 0.9642 0.8488 1.0676 -0.0331 0.1611  -0.0382 242 PRO A CD  
1865  N N   . GLY A  243 ? 0.9933 0.8545 1.1048 -0.0389 0.1932  -0.0475 243 GLY A N   
1866  C CA  . GLY A  243 ? 1.0274 0.8842 1.1310 -0.0438 0.2022  -0.0544 243 GLY A CA  
1867  C C   . GLY A  243 ? 1.0046 0.8669 1.0949 -0.0447 0.1985  -0.0572 243 GLY A C   
1868  O O   . GLY A  243 ? 1.0629 0.9225 1.1455 -0.0486 0.2051  -0.0626 243 GLY A O   
1869  N N   . ASP A  244 ? 1.0353 0.9056 1.1230 -0.0411 0.1879  -0.0533 244 ASP A N   
1870  C CA  . ASP A  244 ? 0.9127 0.7889 0.9888 -0.0412 0.1834  -0.0550 244 ASP A CA  
1871  C C   . ASP A  244 ? 0.9126 0.7872 0.9973 -0.0369 0.1829  -0.0504 244 ASP A C   
1872  O O   . ASP A  244 ? 0.9468 0.8183 1.0459 -0.0330 0.1826  -0.0448 244 ASP A O   
1873  C CB  . ASP A  244 ? 0.9359 0.8220 1.0037 -0.0400 0.1723  -0.0538 244 ASP A CB  
1874  C CG  . ASP A  244 ? 1.1405 1.0330 1.1945 -0.0409 0.1682  -0.0562 244 ASP A CG  
1875  O OD1 . ASP A  244 ? 1.2113 1.1119 1.2581 -0.0399 0.1595  -0.0554 244 ASP A OD1 
1876  O OD2 . ASP A  244 ? 1.0556 0.9453 1.1062 -0.0425 0.1737  -0.0589 244 ASP A OD2 
1877  N N   . LYS A  245 ? 0.9391 0.8157 1.0150 -0.0376 0.1828  -0.0525 245 LYS A N   
1878  C CA  . LYS A  245 ? 0.9535 0.8290 1.0366 -0.0336 0.1821  -0.0484 245 LYS A CA  
1879  C C   . LYS A  245 ? 0.8626 0.7464 0.9365 -0.0315 0.1733  -0.0472 245 LYS A C   
1880  O O   . LYS A  245 ? 0.8653 0.7546 0.9251 -0.0344 0.1706  -0.0511 245 LYS A O   
1881  C CB  . LYS A  245 ? 1.0669 0.9347 1.1512 -0.0359 0.1928  -0.0516 245 LYS A CB  
1882  C CG  . LYS A  245 ? 1.0954 0.9655 1.1636 -0.0401 0.1949  -0.0576 245 LYS A CG  
1883  C CD  . LYS A  245 ? 1.0826 0.9444 1.1527 -0.0424 0.2057  -0.0605 245 LYS A CD  
1884  C CE  . LYS A  245 ? 1.3237 1.1882 1.3775 -0.0465 0.2075  -0.0661 245 LYS A CE  
1885  N NZ  . LYS A  245 ? 1.1344 0.9906 1.1891 -0.0494 0.2186  -0.0695 245 LYS A NZ  
1886  N N   . ILE A  246 ? 0.8238 0.7087 0.9063 -0.0266 0.1689  -0.0416 246 ILE A N   
1887  C CA  . ILE A  246 ? 0.8220 0.7140 0.8974 -0.0243 0.1609  -0.0399 246 ILE A CA  
1888  C C   . ILE A  246 ? 0.9057 0.7947 0.9838 -0.0227 0.1645  -0.0389 246 ILE A C   
1889  O O   . ILE A  246 ? 0.8656 0.7489 0.9569 -0.0203 0.1683  -0.0356 246 ILE A O   
1890  C CB  . ILE A  246 ? 0.7318 0.6290 0.8136 -0.0198 0.1512  -0.0340 246 ILE A CB  
1891  C CG1 . ILE A  246 ? 0.7734 0.6778 0.8480 -0.0174 0.1434  -0.0324 246 ILE A CG1 
1892  C CG2 . ILE A  246 ? 0.6606 0.5528 0.7599 -0.0161 0.1527  -0.0285 246 ILE A CG2 
1893  C CD1 . ILE A  246 ? 0.6788 0.5881 0.7591 -0.0132 0.1340  -0.0269 246 ILE A CD1 
1894  N N   . THR A  247 ? 1.0447 0.9375 1.1103 -0.0241 0.1634  -0.0417 247 THR A N   
1895  C CA  . THR A  247 ? 0.9942 0.8844 1.0605 -0.0230 0.1669  -0.0413 247 THR A CA  
1896  C C   . THR A  247 ? 0.8873 0.7836 0.9528 -0.0187 0.1585  -0.0371 247 THR A C   
1897  O O   . THR A  247 ? 0.9590 0.8629 1.0165 -0.0182 0.1508  -0.0368 247 THR A O   
1898  C CB  . THR A  247 ? 0.9534 0.8427 1.0062 -0.0279 0.1731  -0.0475 247 THR A CB  
1899  O OG1 . THR A  247 ? 1.1467 1.0283 1.2025 -0.0317 0.1829  -0.0513 247 THR A OG1 
1900  N N   . PHE A  248 ? 0.9150 0.8079 0.9892 -0.0157 0.1604  -0.0338 248 PHE A N   
1901  C CA  . PHE A  248 ? 0.9278 0.8255 1.0011 -0.0119 0.1538  -0.0303 248 PHE A CA  
1902  C C   . PHE A  248 ? 0.9382 0.8333 1.0069 -0.0127 0.1591  -0.0321 248 PHE A C   
1903  O O   . PHE A  248 ? 0.9508 0.8388 1.0228 -0.0147 0.1680  -0.0343 248 PHE A O   
1904  C CB  . PHE A  248 ? 0.6500 0.5470 0.7384 -0.0071 0.1497  -0.0240 248 PHE A CB  
1905  C CG  . PHE A  248 ? 0.8050 0.7050 0.8979 -0.0062 0.1439  -0.0218 248 PHE A CG  
1906  C CD1 . PHE A  248 ? 0.8183 0.7136 0.9182 -0.0078 0.1484  -0.0224 248 PHE A CD1 
1907  C CD2 . PHE A  248 ? 0.8150 0.7222 0.9050 -0.0038 0.1342  -0.0191 248 PHE A CD2 
1908  C CE1 . PHE A  248 ? 0.6991 0.5970 0.8028 -0.0070 0.1432  -0.0202 248 PHE A CE1 
1909  C CE2 . PHE A  248 ? 0.7356 0.6454 0.8293 -0.0031 0.1290  -0.0171 248 PHE A CE2 
1910  C CZ  . PHE A  248 ? 0.6775 0.5827 0.7779 -0.0047 0.1334  -0.0175 248 PHE A CZ  
1911  N N   . GLU A  249 ? 0.8561 0.7569 0.9172 -0.0110 0.1538  -0.0311 249 GLU A N   
1912  C CA  . GLU A  249 ? 0.9701 0.8695 1.0249 -0.0118 0.1580  -0.0327 249 GLU A CA  
1913  C C   . GLU A  249 ? 0.9333 0.8385 0.9861 -0.0079 0.1507  -0.0291 249 GLU A C   
1914  O O   . GLU A  249 ? 0.9487 0.8613 0.9925 -0.0078 0.1439  -0.0291 249 GLU A O   
1915  C CB  . GLU A  249 ? 0.9981 0.8992 1.0374 -0.0170 0.1615  -0.0387 249 GLU A CB  
1916  C CG  . GLU A  249 ? 1.2288 1.1287 1.2601 -0.0184 0.1662  -0.0407 249 GLU A CG  
1917  C CD  . GLU A  249 ? 1.3794 1.2811 1.3956 -0.0241 0.1697  -0.0466 249 GLU A CD  
1918  O OE1 . GLU A  249 ? 1.4055 1.3097 1.4113 -0.0252 0.1703  -0.0480 249 GLU A OE1 
1919  O OE2 . GLU A  249 ? 1.2142 1.1149 1.2287 -0.0275 0.1718  -0.0499 249 GLU A OE2 
1920  N N   . ALA A  250 ? 0.9092 0.8110 0.9706 -0.0048 0.1522  -0.0259 250 ALA A N   
1921  C CA  . ALA A  250 ? 0.8309 0.7375 0.8926 -0.0008 0.1454  -0.0219 250 ALA A CA  
1922  C C   . ALA A  250 ? 0.9970 0.9001 1.0604 0.0006  0.1497  -0.0210 250 ALA A C   
1923  O O   . ALA A  250 ? 1.0833 0.9793 1.1546 0.0001  0.1571  -0.0213 250 ALA A O   
1924  C CB  . ALA A  250 ? 0.8321 0.7399 0.9062 0.0030  0.1393  -0.0171 250 ALA A CB  
1925  N N   . THR A  251 ? 0.9333 0.8416 0.9894 0.0023  0.1453  -0.0198 251 THR A N   
1926  C CA  . THR A  251 ? 0.8405 0.7464 0.8987 0.0043  0.1479  -0.0181 251 THR A CA  
1927  C C   . THR A  251 ? 0.8767 0.7849 0.9444 0.0093  0.1413  -0.0128 251 THR A C   
1928  O O   . THR A  251 ? 0.9916 0.8997 1.0602 0.0116  0.1411  -0.0107 251 THR A O   
1929  C CB  . THR A  251 ? 0.8870 0.7966 0.9300 0.0027  0.1483  -0.0204 251 THR A CB  
1930  O OG1 . THR A  251 ? 0.9772 0.8952 1.0113 0.0031  0.1404  -0.0201 251 THR A OG1 
1931  C CG2 . THR A  251 ? 0.8449 0.7511 0.8795 -0.0024 0.1562  -0.0257 251 THR A CG2 
1932  N N   . GLY A  252 ? 0.9368 0.8470 1.0113 0.0106  0.1359  -0.0106 252 GLY A N   
1933  C CA  . GLY A  252 ? 0.9251 0.8376 1.0087 0.0148  0.1294  -0.0058 252 GLY A CA  
1934  C C   . GLY A  252 ? 0.9177 0.8364 0.9995 0.0155  0.1211  -0.0046 252 GLY A C   
1935  O O   . GLY A  252 ? 0.9370 0.8588 1.0094 0.0129  0.1199  -0.0076 252 GLY A O   
1936  N N   . ASN A  253 ? 0.9064 0.8269 0.9972 0.0188  0.1154  -0.0004 253 ASN A N   
1937  C CA  . ASN A  253 ? 0.7977 0.7242 0.8865 0.0197  0.1071  0.0009  253 ASN A CA  
1938  C C   . ASN A  253 ? 0.8248 0.7509 0.9163 0.0178  0.1065  0.0000  253 ASN A C   
1939  O O   . ASN A  253 ? 0.7447 0.6758 0.8326 0.0178  0.1003  0.0003  253 ASN A O   
1940  C CB  . ASN A  253 ? 0.7581 0.6908 0.8322 0.0191  0.1034  -0.0010 253 ASN A CB  
1941  C CG  . ASN A  253 ? 0.7704 0.7039 0.8410 0.0211  0.1038  0.0001  253 ASN A CG  
1942  O OD1 . ASN A  253 ? 0.8234 0.7611 0.8931 0.0236  0.0980  0.0025  253 ASN A OD1 
1943  N ND2 . ASN A  253 ? 0.7902 0.7195 0.8588 0.0198  0.1109  -0.0017 253 ASN A ND2 
1944  N N   . LEU A  254 ? 0.8821 0.8021 0.9800 0.0161  0.1132  -0.0011 254 LEU A N   
1945  C CA  . LEU A  254 ? 0.7401 0.6592 0.8409 0.0142  0.1136  -0.0020 254 LEU A CA  
1946  C C   . LEU A  254 ? 0.6132 0.5298 0.7297 0.0163  0.1124  0.0023  254 LEU A C   
1947  O O   . LEU A  254 ? 0.7756 0.6865 0.9024 0.0169  0.1179  0.0035  254 LEU A O   
1948  C CB  . LEU A  254 ? 0.7043 0.6186 0.8008 0.0104  0.1220  -0.0065 254 LEU A CB  
1949  C CG  . LEU A  254 ? 0.6978 0.6099 0.7983 0.0083  0.1239  -0.0076 254 LEU A CG  
1950  C CD1 . LEU A  254 ? 0.7300 0.6484 0.8233 0.0077  0.1167  -0.0081 254 LEU A CD1 
1951  C CD2 . LEU A  254 ? 0.6777 0.5846 0.7741 0.0044  0.1330  -0.0123 254 LEU A CD2 
1952  N N   . VAL A  255 ? 0.5395 0.4604 0.6579 0.0174  0.1051  0.0046  255 VAL A N   
1953  C CA  . VAL A  255 ? 0.5378 0.4571 0.6701 0.0188  0.1034  0.0085  255 VAL A CA  
1954  C C   . VAL A  255 ? 0.6860 0.6019 0.8202 0.0162  0.1080  0.0066  255 VAL A C   
1955  O O   . VAL A  255 ? 0.7019 0.6209 0.8306 0.0147  0.1046  0.0054  255 VAL A O   
1956  C CB  . VAL A  255 ? 0.6112 0.5365 0.7442 0.0206  0.0939  0.0116  255 VAL A CB  
1957  C CG1 . VAL A  255 ? 0.6841 0.6081 0.8316 0.0219  0.0922  0.0160  255 VAL A CG1 
1958  C CG2 . VAL A  255 ? 0.5211 0.4497 0.6516 0.0231  0.0896  0.0132  255 VAL A CG2 
1959  N N   . VAL A  256 ? 0.7911 0.7004 0.9331 0.0155  0.1159  0.0063  256 VAL A N   
1960  C CA  . VAL A  256 ? 0.6918 0.5968 0.8350 0.0128  0.1219  0.0038  256 VAL A CA  
1961  C C   . VAL A  256 ? 0.7015 0.6066 0.8552 0.0135  0.1191  0.0073  256 VAL A C   
1962  O O   . VAL A  256 ? 0.7589 0.6655 0.9230 0.0164  0.1145  0.0123  256 VAL A O   
1963  C CB  . VAL A  256 ? 0.7931 0.6906 0.9422 0.0118  0.1319  0.0025  256 VAL A CB  
1964  C CG1 . VAL A  256 ? 0.8108 0.7080 0.9490 0.0108  0.1351  -0.0011 256 VAL A CG1 
1965  C CG2 . VAL A  256 ? 0.8355 0.7300 1.0014 0.0150  0.1326  0.0077  256 VAL A CG2 
1966  N N   . PRO A  257 ? 0.6959 0.5996 0.8467 0.0109  0.1218  0.0048  257 PRO A N   
1967  C CA  . PRO A  257 ? 0.5934 0.4965 0.7541 0.0113  0.1202  0.0079  257 PRO A CA  
1968  C C   . PRO A  257 ? 0.7176 0.6146 0.8946 0.0127  0.1260  0.0113  257 PRO A C   
1969  O O   . PRO A  257 ? 0.7978 0.6892 0.9763 0.0116  0.1342  0.0091  257 PRO A O   
1970  C CB  . PRO A  257 ? 0.6621 0.5640 0.8143 0.0076  0.1238  0.0032  257 PRO A CB  
1971  C CG  . PRO A  257 ? 0.6577 0.5624 0.7937 0.0055  0.1238  -0.0019 257 PRO A CG  
1972  C CD  . PRO A  257 ? 0.6151 0.5182 0.7524 0.0071  0.1259  -0.0013 257 PRO A CD  
1973  N N   . ARG A  258 ? 0.8739 0.7722 1.0631 0.0150  0.1218  0.0168  258 ARG A N   
1974  C CA  . ARG A  258 ? 0.7845 0.6776 0.9902 0.0163  0.1269  0.0206  258 ARG A CA  
1975  C C   . ARG A  258 ? 0.7392 0.6309 0.9504 0.0154  0.1279  0.0219  258 ARG A C   
1976  O O   . ARG A  258 ? 0.7937 0.6793 1.0113 0.0142  0.1360  0.0211  258 ARG A O   
1977  C CB  . ARG A  258 ? 0.7207 0.6164 0.9377 0.0199  0.1216  0.0266  258 ARG A CB  
1978  C CG  . ARG A  258 ? 0.8166 0.7077 1.0518 0.0216  0.1263  0.0313  258 ARG A CG  
1979  C CD  . ARG A  258 ? 0.8485 0.7431 1.0944 0.0248  0.1203  0.0371  258 ARG A CD  
1980  N NE  . ARG A  258 ? 1.0262 0.9191 1.2894 0.0264  0.1214  0.0429  258 ARG A NE  
1981  C CZ  . ARG A  258 ? 1.1580 1.0461 1.4345 0.0277  0.1278  0.0453  258 ARG A CZ  
1982  N NH1 . ARG A  258 ? 1.1080 0.9922 1.3821 0.0275  0.1337  0.0423  258 ARG A NH1 
1983  N NH2 . ARG A  258 ? 1.1939 1.0812 1.4863 0.0292  0.1282  0.0509  258 ARG A NH2 
1984  N N   . TYR A  259 ? 0.7147 0.6121 0.9233 0.0158  0.1197  0.0239  259 TYR A N   
1985  C CA  . TYR A  259 ? 0.6660 0.5628 0.8781 0.0148  0.1197  0.0250  259 TYR A CA  
1986  C C   . TYR A  259 ? 0.7665 0.6664 0.9632 0.0120  0.1173  0.0202  259 TYR A C   
1987  O O   . TYR A  259 ? 0.7159 0.6214 0.9018 0.0121  0.1108  0.0187  259 TYR A O   
1988  C CB  . TYR A  259 ? 0.7165 0.6173 0.9395 0.0175  0.1123  0.0319  259 TYR A CB  
1989  C CG  . TYR A  259 ? 0.9287 0.8265 1.1694 0.0200  0.1151  0.0374  259 TYR A CG  
1990  C CD1 . TYR A  259 ? 0.8697 0.7690 1.1149 0.0222  0.1127  0.0398  259 TYR A CD1 
1991  C CD2 . TYR A  259 ? 1.0475 0.9410 1.3007 0.0201  0.1202  0.0403  259 TYR A CD2 
1992  C CE1 . TYR A  259 ? 1.0458 0.9427 1.3075 0.0245  0.1152  0.0449  259 TYR A CE1 
1993  C CE2 . TYR A  259 ? 1.0164 0.9074 1.2863 0.0225  0.1228  0.0456  259 TYR A CE2 
1994  C CZ  . TYR A  259 ? 1.0691 0.9619 1.3431 0.0246  0.1202  0.0479  259 TYR A CZ  
1995  O OH  . TYR A  259 ? 1.0783 0.9691 1.3694 0.0269  0.1227  0.0532  259 TYR A OH  
1996  N N   . ALA A  260 ? 0.7617 0.6578 0.9577 0.0096  0.1228  0.0177  260 ALA A N   
1997  C CA  . ALA A  260 ? 0.6547 0.5537 0.8377 0.0068  0.1206  0.0135  260 ALA A CA  
1998  C C   . ALA A  260 ? 0.7412 0.6409 0.9309 0.0071  0.1178  0.0170  260 ALA A C   
1999  O O   . ALA A  260 ? 0.7525 0.6514 0.9563 0.0096  0.1169  0.0229  260 ALA A O   
2000  C CB  . ALA A  260 ? 0.6855 0.5796 0.8603 0.0031  0.1294  0.0069  260 ALA A CB  
2001  N N   . PHE A  261 ? 0.7754 0.6770 0.9553 0.0046  0.1166  0.0136  261 PHE A N   
2002  C CA  . PHE A  261 ? 0.5909 0.4934 0.7760 0.0048  0.1137  0.0168  261 PHE A CA  
2003  C C   . PHE A  261 ? 0.6851 0.5843 0.8648 0.0013  0.1195  0.0123  261 PHE A C   
2004  O O   . PHE A  261 ? 0.7880 0.6901 0.9539 -0.0012 0.1179  0.0073  261 PHE A O   
2005  C CB  . PHE A  261 ? 0.5444 0.4547 0.7237 0.0060  0.1029  0.0190  261 PHE A CB  
2006  C CG  . PHE A  261 ? 0.5690 0.4828 0.7538 0.0092  0.0968  0.0236  261 PHE A CG  
2007  C CD1 . PHE A  261 ? 0.6307 0.5474 0.8069 0.0096  0.0942  0.0212  261 PHE A CD1 
2008  C CD2 . PHE A  261 ? 0.5381 0.4524 0.7367 0.0118  0.0937  0.0303  261 PHE A CD2 
2009  C CE1 . PHE A  261 ? 0.6821 0.6018 0.8634 0.0125  0.0889  0.0252  261 PHE A CE1 
2010  C CE2 . PHE A  261 ? 0.3962 0.3139 0.5998 0.0144  0.0882  0.0343  261 PHE A CE2 
2011  C CZ  . PHE A  261 ? 0.6604 0.5806 0.8553 0.0148  0.0859  0.0317  261 PHE A CZ  
2012  N N   . ALA A  262 ? 0.8359 0.7291 1.0269 0.0011  0.1263  0.0140  262 ALA A N   
2013  C CA  . ALA A  262 ? 0.7787 0.6687 0.9667 -0.0020 0.1314  0.0107  262 ALA A CA  
2014  C C   . ALA A  262 ? 0.8739 0.7693 1.0590 -0.0017 0.1234  0.0130  262 ALA A C   
2015  O O   . ALA A  262 ? 0.8023 0.6999 0.9971 0.0011  0.1182  0.0194  262 ALA A O   
2016  C CB  . ALA A  262 ? 0.9026 0.7850 1.1049 -0.0017 0.1402  0.0130  262 ALA A CB  
2017  N N   . MET A  263 ? 0.7548 0.6524 0.9265 -0.0047 0.1224  0.0077  263 MET A N   
2018  C CA  . MET A  263 ? 0.8089 0.7126 0.9753 -0.0045 0.1139  0.0092  263 MET A CA  
2019  C C   . MET A  263 ? 0.8120 0.7152 0.9698 -0.0080 0.1162  0.0046  263 MET A C   
2020  O O   . MET A  263 ? 0.9556 0.8576 1.1029 -0.0113 0.1206  -0.0019 263 MET A O   
2021  C CB  . MET A  263 ? 0.8056 0.7163 0.9618 -0.0035 0.1057  0.0084  263 MET A CB  
2022  C CG  . MET A  263 ? 0.8015 0.7186 0.9529 -0.0028 0.0964  0.0105  263 MET A CG  
2023  S SD  . MET A  263 ? 0.9642 0.8888 1.1031 -0.0020 0.0881  0.0088  263 MET A SD  
2024  C CE  . MET A  263 ? 0.8940 0.8183 1.0175 -0.0061 0.0932  0.0002  263 MET A CE  
2025  N N   . GLU A  264 ? 0.7619 0.6660 0.9241 -0.0075 0.1132  0.0080  264 GLU A N   
2026  C CA  . GLU A  264 ? 0.9233 0.8280 1.0773 -0.0106 0.1139  0.0042  264 GLU A CA  
2027  C C   . GLU A  264 ? 0.8813 0.7931 1.0301 -0.0096 0.1037  0.0066  264 GLU A C   
2028  O O   . GLU A  264 ? 0.8333 0.7464 0.9909 -0.0071 0.0993  0.0128  264 GLU A O   
2029  C CB  . GLU A  264 ? 0.9332 0.8314 1.0975 -0.0114 0.1210  0.0058  264 GLU A CB  
2030  C CG  . GLU A  264 ? 1.2726 1.1652 1.4320 -0.0154 0.1309  -0.0009 264 GLU A CG  
2031  C CD  . GLU A  264 ? 1.5041 1.3888 1.6768 -0.0154 0.1396  0.0012  264 GLU A CD  
2032  O OE1 . GLU A  264 ? 1.4806 1.3615 1.6506 -0.0186 0.1455  -0.0026 264 GLU A OE1 
2033  O OE2 . GLU A  264 ? 1.5879 1.4701 1.7741 -0.0123 0.1407  0.0069  264 GLU A OE2 
2034  N N   . ARG A  265 ? 0.9080 0.8246 1.0424 -0.0115 0.1001  0.0018  265 ARG A N   
2035  C CA  . ARG A  265 ? 0.9252 0.8488 1.0536 -0.0105 0.0904  0.0036  265 ARG A CA  
2036  C C   . ARG A  265 ? 0.9829 0.9079 1.1038 -0.0132 0.0897  0.0007  265 ARG A C   
2037  O O   . ARG A  265 ? 1.0734 0.9963 1.1876 -0.0166 0.0954  -0.0050 265 ARG A O   
2038  C CB  . ARG A  265 ? 0.7662 0.6951 0.8845 -0.0100 0.0854  0.0012  265 ARG A CB  
2039  C CG  . ARG A  265 ? 0.8953 0.8225 1.0054 -0.0125 0.0914  -0.0051 265 ARG A CG  
2040  C CD  . ARG A  265 ? 0.9755 0.9083 1.0762 -0.0117 0.0862  -0.0067 265 ARG A CD  
2041  N NE  . ARG A  265 ? 0.9393 0.8767 1.0259 -0.0144 0.0839  -0.0117 265 ARG A NE  
2042  C CZ  . ARG A  265 ? 0.8853 0.8222 0.9629 -0.0176 0.0887  -0.0177 265 ARG A CZ  
2043  N NH1 . ARG A  265 ? 0.9563 0.8878 1.0371 -0.0185 0.0964  -0.0195 265 ARG A NH1 
2044  N NH2 . ARG A  265 ? 0.9890 0.9308 1.0544 -0.0199 0.0860  -0.0217 265 ARG A NH2 
2045  N N   . ASN A  266 ? 0.9488 0.8775 1.0710 -0.0119 0.0828  0.0047  266 ASN A N   
2046  C CA  . ASN A  266 ? 1.2316 1.1626 1.3462 -0.0141 0.0807  0.0024  266 ASN A CA  
2047  C C   . ASN A  266 ? 1.0933 1.0319 1.1973 -0.0137 0.0719  0.0016  266 ASN A C   
2048  O O   . ASN A  266 ? 1.0102 0.9522 1.1173 -0.0110 0.0652  0.0061  266 ASN A O   
2049  C CB  . ASN A  266 ? 1.3674 1.2962 1.4918 -0.0133 0.0806  0.0075  266 ASN A CB  
2050  C CG  . ASN A  266 ? 1.2122 1.1405 1.3497 -0.0096 0.0778  0.0150  266 ASN A CG  
2051  O OD1 . ASN A  266 ? 1.0481 0.9713 1.1975 -0.0087 0.0826  0.0185  266 ASN A OD1 
2052  N ND2 . ASN A  266 ? 1.1093 1.0428 1.2448 -0.0074 0.0700  0.0175  266 ASN A ND2 
2053  N N   . ALA A  267 ? 1.0401 0.9814 1.1319 -0.0166 0.0720  -0.0041 267 ALA A N   
2054  C CA  . ALA A  267 ? 1.3206 1.2689 1.4018 -0.0164 0.0644  -0.0054 267 ALA A CA  
2055  C C   . ALA A  267 ? 1.1691 1.1208 1.2510 -0.0153 0.0573  -0.0015 267 ALA A C   
2056  O O   . ALA A  267 ? 0.9943 0.9433 1.0817 -0.0157 0.0588  0.0007  267 ALA A O   
2057  C CB  . ALA A  267 ? 1.3347 1.2851 1.4032 -0.0199 0.0667  -0.0124 267 ALA A CB  
2058  N N   . GLY A  268 ? 1.1852 1.1427 1.2616 -0.0138 0.0498  -0.0005 268 GLY A N   
2059  C CA  . GLY A  268 ? 1.2518 1.2132 1.3260 -0.0134 0.0430  0.0019  268 GLY A CA  
2060  C C   . GLY A  268 ? 1.2480 1.2102 1.3309 -0.0104 0.0375  0.0087  268 GLY A C   
2061  O O   . GLY A  268 ? 1.1546 1.1170 1.2403 -0.0105 0.0349  0.0118  268 GLY A O   
2062  N N   . SER A  269 ? 0.9861 0.9489 1.0729 -0.0081 0.0356  0.0111  269 SER A N   
2063  C CA  . SER A  269 ? 0.8179 0.7826 0.9116 -0.0055 0.0294  0.0173  269 SER A CA  
2064  C C   . SER A  269 ? 0.7776 0.7472 0.8654 -0.0042 0.0236  0.0169  269 SER A C   
2065  O O   . SER A  269 ? 0.9284 0.9008 1.0057 -0.0052 0.0231  0.0122  269 SER A O   
2066  C CB  . SER A  269 ? 0.7689 0.7292 0.8764 -0.0037 0.0328  0.0219  269 SER A CB  
2067  O OG  . SER A  269 ? 0.6442 0.6067 0.7585 -0.0017 0.0266  0.0280  269 SER A OG  
2068  N N   . GLY A  270 ? 0.5498 0.5204 0.6444 -0.0019 0.0192  0.0218  270 GLY A N   
2069  C CA  . GLY A  270 ? 0.5938 0.5687 0.6836 -0.0005 0.0138  0.0218  270 GLY A CA  
2070  C C   . GLY A  270 ? 0.5342 0.5089 0.6336 0.0019  0.0114  0.0268  270 GLY A C   
2071  O O   . GLY A  270 ? 0.6154 0.5865 0.7257 0.0028  0.0145  0.0302  270 GLY A O   
2072  N N   . ILE A  271 ? 0.6328 0.6114 0.7282 0.0030  0.0060  0.0271  271 ILE A N   
2073  C CA  . ILE A  271 ? 0.4403 0.4193 0.5437 0.0052  0.0032  0.0314  271 ILE A CA  
2074  C C   . ILE A  271 ? 0.4854 0.4688 0.5862 0.0055  -0.0048 0.0339  271 ILE A C   
2075  O O   . ILE A  271 ? 0.8141 0.8009 0.9052 0.0051  -0.0080 0.0311  271 ILE A O   
2076  C CB  . ILE A  271 ? 0.4418 0.4204 0.5433 0.0064  0.0054  0.0290  271 ILE A CB  
2077  C CG1 . ILE A  271 ? 0.5576 0.5315 0.6614 0.0058  0.0135  0.0264  271 ILE A CG1 
2078  C CG2 . ILE A  271 ? 0.5876 0.5669 0.6972 0.0085  0.0022  0.0334  271 ILE A CG2 
2079  C CD1 . ILE A  271 ? 0.6663 0.6406 0.7636 0.0061  0.0162  0.0222  271 ILE A CD1 
2080  N N   . ILE A  272 ? 0.4891 0.4727 0.5988 0.0060  -0.0078 0.0394  272 ILE A N   
2081  C CA  . ILE A  272 ? 0.5790 0.5666 0.6867 0.0059  -0.0153 0.0420  272 ILE A CA  
2082  C C   . ILE A  272 ? 0.5826 0.5717 0.6953 0.0076  -0.0185 0.0448  272 ILE A C   
2083  O O   . ILE A  272 ? 0.5520 0.5391 0.6755 0.0088  -0.0167 0.0484  272 ILE A O   
2084  C CB  . ILE A  272 ? 0.5368 0.5245 0.6502 0.0051  -0.0176 0.0466  272 ILE A CB  
2085  C CG1 . ILE A  272 ? 0.5907 0.5773 0.6982 0.0033  -0.0149 0.0437  272 ILE A CG1 
2086  C CG2 . ILE A  272 ? 0.5392 0.5311 0.6509 0.0049  -0.0253 0.0495  272 ILE A CG2 
2087  C CD1 . ILE A  272 ? 0.6113 0.5982 0.7231 0.0025  -0.0174 0.0480  272 ILE A CD1 
2088  N N   . ILE A  273 ? 0.6220 0.6145 0.7270 0.0076  -0.0229 0.0430  273 ILE A N   
2089  C CA  . ILE A  273 ? 0.7075 0.7017 0.8164 0.0088  -0.0265 0.0454  273 ILE A CA  
2090  C C   . ILE A  273 ? 0.7963 0.7937 0.9066 0.0079  -0.0333 0.0493  273 ILE A C   
2091  O O   . ILE A  273 ? 0.8925 0.8927 0.9940 0.0068  -0.0373 0.0476  273 ILE A O   
2092  C CB  . ILE A  273 ? 0.7174 0.7132 0.8177 0.0094  -0.0270 0.0413  273 ILE A CB  
2093  C CG1 . ILE A  273 ? 0.6909 0.6839 0.7896 0.0101  -0.0204 0.0376  273 ILE A CG1 
2094  C CG2 . ILE A  273 ? 0.8076 0.8050 0.9121 0.0105  -0.0307 0.0439  273 ILE A CG2 
2095  C CD1 . ILE A  273 ? 0.9133 0.9059 1.0035 0.0087  -0.0173 0.0333  273 ILE A CD1 
2096  N N   . SER A  274 ? 0.8290 0.8259 0.9504 0.0084  -0.0344 0.0547  274 SER A N   
2097  C CA  . SER A  274 ? 0.7461 0.7461 0.8695 0.0073  -0.0406 0.0589  274 SER A CA  
2098  C C   . SER A  274 ? 0.8469 0.8474 0.9826 0.0082  -0.0425 0.0645  274 SER A C   
2099  O O   . SER A  274 ? 0.8963 0.8942 1.0410 0.0097  -0.0382 0.0659  274 SER A O   
2100  C CB  . SER A  274 ? 0.7660 0.7655 0.8890 0.0059  -0.0404 0.0602  274 SER A CB  
2101  O OG  . SER A  274 ? 0.7986 0.8005 0.9271 0.0051  -0.0455 0.0657  274 SER A OG  
2102  N N   . ASP A  275 ? 1.0994 1.1036 1.2354 0.0071  -0.0490 0.0676  275 ASP A N   
2103  C CA  . ASP A  275 ? 1.1128 1.1186 1.2603 0.0075  -0.0518 0.0733  275 ASP A CA  
2104  C C   . ASP A  275 ? 0.9481 0.9541 1.1035 0.0070  -0.0526 0.0787  275 ASP A C   
2105  O O   . ASP A  275 ? 1.1444 1.1508 1.3118 0.0078  -0.0529 0.0839  275 ASP A O   
2106  C CB  . ASP A  275 ? 1.2926 1.3024 1.4364 0.0063  -0.0585 0.0740  275 ASP A CB  
2107  C CG  . ASP A  275 ? 1.5359 1.5455 1.6726 0.0070  -0.0578 0.0691  275 ASP A CG  
2108  O OD1 . ASP A  275 ? 1.7394 1.7501 1.8647 0.0060  -0.0594 0.0652  275 ASP A OD1 
2109  O OD2 . ASP A  275 ? 1.4759 1.4843 1.6186 0.0086  -0.0556 0.0694  275 ASP A OD2 
2110  N N   . THR A  276 ? 0.8735 0.8794 1.0225 0.0057  -0.0528 0.0776  276 THR A N   
2111  C CA  . THR A  276 ? 0.8668 0.8732 1.0217 0.0050  -0.0541 0.0826  276 THR A CA  
2112  C C   . THR A  276 ? 0.8849 0.8885 1.0538 0.0068  -0.0493 0.0867  276 THR A C   
2113  O O   . THR A  276 ? 0.8124 0.8121 0.9830 0.0082  -0.0430 0.0838  276 THR A O   
2114  C CB  . THR A  276 ? 0.7458 0.7511 0.8918 0.0037  -0.0528 0.0797  276 THR A CB  
2115  O OG1 . THR A  276 ? 0.6359 0.6434 0.7689 0.0023  -0.0562 0.0753  276 THR A OG1 
2116  C CG2 . THR A  276 ? 0.7227 0.7293 0.8735 0.0027  -0.0554 0.0852  276 THR A CG2 
2117  N N   . PRO A  277 ? 0.9521 0.9578 1.1308 0.0066  -0.0523 0.0935  277 PRO A N   
2118  C CA  . PRO A  277 ? 0.9003 0.9039 1.0937 0.0083  -0.0484 0.0985  277 PRO A CA  
2119  C C   . PRO A  277 ? 0.8375 0.8362 1.0325 0.0090  -0.0413 0.0972  277 PRO A C   
2120  O O   . PRO A  277 ? 0.8292 0.8276 1.0176 0.0077  -0.0415 0.0960  277 PRO A O   
2121  C CB  . PRO A  277 ? 1.0332 1.0413 1.2336 0.0074  -0.0545 0.1059  277 PRO A CB  
2122  C CG  . PRO A  277 ? 1.0776 1.0901 1.2683 0.0054  -0.0618 0.1045  277 PRO A CG  
2123  C CD  . PRO A  277 ? 0.8904 0.9011 1.0667 0.0047  -0.0600 0.0970  277 PRO A CD  
2124  N N   . VAL A  278 ? 0.7784 0.7732 0.9822 0.0108  -0.0349 0.0973  278 VAL A N   
2125  C CA  . VAL A  278 ? 0.8963 0.8863 1.1041 0.0114  -0.0277 0.0969  278 VAL A CA  
2126  C C   . VAL A  278 ? 0.9383 0.9293 1.1576 0.0117  -0.0290 0.1045  278 VAL A C   
2127  O O   . VAL A  278 ? 0.9682 0.9626 1.1969 0.0123  -0.0330 0.1105  278 VAL A O   
2128  C CB  . VAL A  278 ? 0.7981 0.7833 1.0122 0.0132  -0.0202 0.0948  278 VAL A CB  
2129  C CG1 . VAL A  278 ? 1.0567 1.0435 1.2839 0.0148  -0.0217 0.1002  278 VAL A CG1 
2130  C CG2 . VAL A  278 ? 0.6779 0.6579 0.8968 0.0135  -0.0125 0.0945  278 VAL A CG2 
2131  N N   . HIS A  279 ? 0.9888 0.9771 1.2073 0.0112  -0.0255 0.1045  279 HIS A N   
2132  C CA  . HIS A  279 ? 0.9419 0.9314 1.1702 0.0113  -0.0269 0.1118  279 HIS A CA  
2133  C C   . HIS A  279 ? 1.0084 0.9922 1.2434 0.0122  -0.0188 0.1124  279 HIS A C   
2134  O O   . HIS A  279 ? 1.1108 1.0901 1.3395 0.0118  -0.0128 0.1062  279 HIS A O   
2135  C CB  . HIS A  279 ? 1.0593 1.0529 1.2787 0.0092  -0.0338 0.1129  279 HIS A CB  
2136  C CG  . HIS A  279 ? 1.1835 1.1833 1.4064 0.0087  -0.0422 0.1186  279 HIS A CG  
2137  N ND1 . HIS A  279 ? 1.1609 1.1635 1.3927 0.0087  -0.0454 0.1265  279 HIS A ND1 
2138  C CD2 . HIS A  279 ? 1.1939 1.1977 1.4123 0.0081  -0.0479 0.1176  279 HIS A CD2 
2139  C CE1 . HIS A  279 ? 1.3440 1.3524 1.5767 0.0079  -0.0529 0.1301  279 HIS A CE1 
2140  N NE2 . HIS A  279 ? 1.2296 1.2386 1.4541 0.0074  -0.0545 0.1246  279 HIS A NE2 
2141  N N   . ASP A  280 ? 1.0485 1.0328 1.2966 0.0132  -0.0187 0.1200  280 ASP A N   
2142  C CA  . ASP A  280 ? 1.2176 1.1969 1.4729 0.0139  -0.0115 0.1215  280 ASP A CA  
2143  C C   . ASP A  280 ? 1.1508 1.1309 1.3991 0.0122  -0.0136 0.1220  280 ASP A C   
2144  O O   . ASP A  280 ? 1.3912 1.3735 1.6469 0.0124  -0.0164 0.1290  280 ASP A O   
2145  C CB  . ASP A  280 ? 1.2858 1.2652 1.5595 0.0160  -0.0100 0.1300  280 ASP A CB  
2146  C CG  . ASP A  280 ? 1.4838 1.4580 1.7659 0.0168  -0.0025 0.1323  280 ASP A CG  
2147  O OD1 . ASP A  280 ? 1.3883 1.3577 1.6626 0.0158  0.0031  0.1263  280 ASP A OD1 
2148  O OD2 . ASP A  280 ? 1.5953 1.5702 1.8920 0.0184  -0.0022 0.1402  280 ASP A OD2 
2149  N N   . CYS A  281 ? 1.0592 1.0376 1.2933 0.0105  -0.0124 0.1145  281 CYS A N   
2150  C CA  . CYS A  281 ? 1.0696 1.0486 1.2958 0.0087  -0.0142 0.1141  281 CYS A CA  
2151  C C   . CYS A  281 ? 0.9577 0.9318 1.1742 0.0075  -0.0078 0.1062  281 CYS A C   
2152  O O   . CYS A  281 ? 1.0166 0.9882 1.2291 0.0076  -0.0038 0.1003  281 CYS A O   
2153  C CB  . CYS A  281 ? 0.9366 0.9217 1.1525 0.0070  -0.0235 0.1141  281 CYS A CB  
2154  S SG  . CYS A  281 ? 1.5146 1.5014 1.7177 0.0063  -0.0260 0.1062  281 CYS A SG  
2155  N N   . ASN A  282 ? 0.9372 0.9102 1.1498 0.0062  -0.0070 0.1062  282 ASN A N   
2156  C CA  . ASN A  282 ? 0.8458 0.8146 1.0493 0.0047  -0.0011 0.0989  282 ASN A CA  
2157  C C   . ASN A  282 ? 0.8901 0.8621 1.0774 0.0025  -0.0062 0.0938  282 ASN A C   
2158  O O   . ASN A  282 ? 0.9006 0.8768 1.0846 0.0018  -0.0130 0.0970  282 ASN A O   
2159  C CB  . ASN A  282 ? 0.9823 0.9469 1.1925 0.0047  0.0045  0.1017  282 ASN A CB  
2160  C CG  . ASN A  282 ? 1.1808 1.1387 1.3982 0.0055  0.0145  0.0993  282 ASN A CG  
2161  O OD1 . ASN A  282 ? 1.2484 1.2043 1.4604 0.0051  0.0181  0.0928  282 ASN A OD1 
2162  N ND2 . ASN A  282 ? 1.4559 1.4105 1.6856 0.0065  0.0192  0.1045  282 ASN A ND2 
2163  N N   . THR A  283 ? 0.8817 0.8518 1.0591 0.0015  -0.0027 0.0858  283 THR A N   
2164  C CA  . THR A  283 ? 0.8206 0.7934 0.9829 -0.0005 -0.0065 0.0804  283 THR A CA  
2165  C C   . THR A  283 ? 0.7319 0.7008 0.8862 -0.0019 0.0001  0.0727  283 THR A C   
2166  O O   . THR A  283 ? 0.7960 0.7609 0.9547 -0.0014 0.0069  0.0703  283 THR A O   
2167  C CB  . THR A  283 ? 0.7480 0.7254 0.9035 -0.0004 -0.0129 0.0787  283 THR A CB  
2168  O OG1 . THR A  283 ? 0.4796 0.4601 0.6220 -0.0023 -0.0175 0.0752  283 THR A OG1 
2169  C CG2 . THR A  283 ? 0.6334 0.6089 0.7874 0.0003  -0.0087 0.0735  283 THR A CG2 
2170  N N   . THR A  284 ? 0.6333 0.6039 0.7760 -0.0040 -0.0019 0.0688  284 THR A N   
2171  C CA  . THR A  284 ? 0.7042 0.6722 0.8381 -0.0056 0.0034  0.0612  284 THR A CA  
2172  C C   . THR A  284 ? 0.7016 0.6732 0.8232 -0.0064 -0.0002 0.0555  284 THR A C   
2173  O O   . THR A  284 ? 0.6415 0.6120 0.7555 -0.0076 0.0037  0.0490  284 THR A O   
2174  C CB  . THR A  284 ? 0.6278 0.5947 0.7575 -0.0075 0.0047  0.0605  284 THR A CB  
2175  O OG1 . THR A  284 ? 0.8577 0.8222 0.9795 -0.0094 0.0102  0.0530  284 THR A OG1 
2176  C CG2 . THR A  284 ? 0.6578 0.6297 0.7794 -0.0085 -0.0033 0.0616  284 THR A CG2 
2177  N N   . CYS A  285 ? 0.5202 0.4964 0.6400 -0.0057 -0.0075 0.0581  285 CYS A N   
2178  C CA  . CYS A  285 ? 0.4676 0.4474 0.5763 -0.0062 -0.0113 0.0534  285 CYS A CA  
2179  C C   . CYS A  285 ? 0.5192 0.5020 0.6317 -0.0045 -0.0165 0.0567  285 CYS A C   
2180  O O   . CYS A  285 ? 0.5889 0.5739 0.7065 -0.0041 -0.0214 0.0625  285 CYS A O   
2181  C CB  . CYS A  285 ? 0.5152 0.4981 0.6133 -0.0080 -0.0157 0.0515  285 CYS A CB  
2182  S SG  . CYS A  285 ? 0.7811 0.7687 0.8661 -0.0085 -0.0207 0.0463  285 CYS A SG  
2183  N N   . GLN A  286 ? 0.5107 0.4937 0.6207 -0.0037 -0.0153 0.0531  286 GLN A N   
2184  C CA  . GLN A  286 ? 0.4113 0.3966 0.5255 -0.0021 -0.0192 0.0559  286 GLN A CA  
2185  C C   . GLN A  286 ? 0.5956 0.5845 0.6992 -0.0024 -0.0232 0.0518  286 GLN A C   
2186  O O   . GLN A  286 ? 0.5923 0.5808 0.6881 -0.0029 -0.0203 0.0460  286 GLN A O   
2187  C CB  . GLN A  286 ? 0.4515 0.4333 0.5752 -0.0004 -0.0138 0.0566  286 GLN A CB  
2188  C CG  . GLN A  286 ? 0.4554 0.4392 0.5853 0.0014  -0.0174 0.0602  286 GLN A CG  
2189  C CD  . GLN A  286 ? 0.6502 0.6364 0.7880 0.0017  -0.0227 0.0674  286 GLN A CD  
2190  O OE1 . GLN A  286 ? 0.6628 0.6469 0.8100 0.0021  -0.0204 0.0719  286 GLN A OE1 
2191  N NE2 . GLN A  286 ? 0.5361 0.5267 0.6700 0.0014  -0.0297 0.0687  286 GLN A NE2 
2192  N N   . THR A  287 ? 0.5900 0.5825 0.6932 -0.0021 -0.0299 0.0549  287 THR A N   
2193  C CA  . THR A  287 ? 0.4967 0.4926 0.5913 -0.0022 -0.0338 0.0516  287 THR A CA  
2194  C C   . THR A  287 ? 0.5388 0.5357 0.6400 -0.0006 -0.0361 0.0546  287 THR A C   
2195  O O   . THR A  287 ? 0.6088 0.6049 0.7208 0.0003  -0.0364 0.0599  287 THR A O   
2196  C CB  . THR A  287 ? 0.5719 0.5714 0.6583 -0.0038 -0.0399 0.0518  287 THR A CB  
2197  O OG1 . THR A  287 ? 0.4445 0.4465 0.5357 -0.0037 -0.0456 0.0569  287 THR A OG1 
2198  C CG2 . THR A  287 ? 0.4745 0.4728 0.5593 -0.0054 -0.0386 0.0521  287 THR A CG2 
2199  N N   . PRO A  288 ? 0.6782 0.6769 0.7733 -0.0001 -0.0377 0.0513  288 PRO A N   
2200  C CA  . PRO A  288 ? 0.6723 0.6721 0.7729 0.0013  -0.0400 0.0536  288 PRO A CA  
2201  C C   . PRO A  288 ? 0.6433 0.6461 0.7483 0.0008  -0.0464 0.0591  288 PRO A C   
2202  O O   . PRO A  288 ? 0.6287 0.6318 0.7419 0.0019  -0.0477 0.0627  288 PRO A O   
2203  C CB  . PRO A  288 ? 0.6395 0.6412 0.7301 0.0014  -0.0412 0.0487  288 PRO A CB  
2204  C CG  . PRO A  288 ? 0.5118 0.5122 0.5945 0.0007  -0.0369 0.0435  288 PRO A CG  
2205  C CD  . PRO A  288 ? 0.6311 0.6307 0.7143 -0.0008 -0.0368 0.0451  288 PRO A CD  
2206  N N   . LYS A  289 ? 0.6640 0.6687 0.7635 -0.0010 -0.0502 0.0597  289 LYS A N   
2207  C CA  . LYS A  289 ? 0.6754 0.6832 0.7775 -0.0020 -0.0566 0.0647  289 LYS A CA  
2208  C C   . LYS A  289 ? 0.5951 0.6021 0.7076 -0.0019 -0.0563 0.0707  289 LYS A C   
2209  O O   . LYS A  289 ? 0.7228 0.7320 0.8419 -0.0021 -0.0605 0.0761  289 LYS A O   
2210  C CB  . LYS A  289 ? 0.6736 0.6841 0.7644 -0.0040 -0.0610 0.0625  289 LYS A CB  
2211  C CG  . LYS A  289 ? 0.8054 0.8170 0.8863 -0.0040 -0.0616 0.0570  289 LYS A CG  
2212  C CD  . LYS A  289 ? 0.8547 0.8684 0.9243 -0.0060 -0.0646 0.0543  289 LYS A CD  
2213  C CE  . LYS A  289 ? 0.8807 0.8973 0.9496 -0.0077 -0.0712 0.0578  289 LYS A CE  
2214  N NZ  . LYS A  289 ? 0.9597 0.9781 1.0171 -0.0096 -0.0739 0.0547  289 LYS A NZ  
2215  N N   . GLY A  290 ? 0.5211 0.5248 0.6349 -0.0018 -0.0511 0.0699  290 GLY A N   
2216  C CA  . GLY A  290 ? 0.5712 0.5737 0.6949 -0.0016 -0.0500 0.0754  290 GLY A CA  
2217  C C   . GLY A  290 ? 0.5874 0.5866 0.7084 -0.0022 -0.0448 0.0730  290 GLY A C   
2218  O O   . GLY A  290 ? 0.7413 0.7398 0.8521 -0.0030 -0.0430 0.0671  290 GLY A O   
2219  N N   . ALA A  291 ? 0.6340 0.6312 0.7644 -0.0018 -0.0423 0.0776  291 ALA A N   
2220  C CA  . ALA A  291 ? 0.6286 0.6222 0.7579 -0.0023 -0.0369 0.0756  291 ALA A CA  
2221  C C   . ALA A  291 ? 0.7107 0.7060 0.8325 -0.0043 -0.0403 0.0759  291 ALA A C   
2222  O O   . ALA A  291 ? 0.5602 0.5592 0.6806 -0.0052 -0.0468 0.0794  291 ALA A O   
2223  C CB  . ALA A  291 ? 0.5023 0.4925 0.6452 -0.0009 -0.0321 0.0804  291 ALA A CB  
2224  N N   . ILE A  292 ? 0.6135 0.6061 0.7304 -0.0053 -0.0358 0.0721  292 ILE A N   
2225  C CA  . ILE A  292 ? 0.5485 0.5422 0.6586 -0.0072 -0.0382 0.0722  292 ILE A CA  
2226  C C   . ILE A  292 ? 0.8793 0.8694 0.9959 -0.0073 -0.0335 0.0749  292 ILE A C   
2227  O O   . ILE A  292 ? 0.9531 0.9392 1.0703 -0.0072 -0.0267 0.0713  292 ILE A O   
2228  C CB  . ILE A  292 ? 0.6980 0.6924 0.7943 -0.0087 -0.0379 0.0648  292 ILE A CB  
2229  C CG1 . ILE A  292 ? 0.5762 0.5742 0.6657 -0.0086 -0.0428 0.0625  292 ILE A CG1 
2230  C CG2 . ILE A  292 ? 0.8690 0.8641 0.9590 -0.0106 -0.0397 0.0649  292 ILE A CG2 
2231  C CD1 . ILE A  292 ? 0.6433 0.6425 0.7199 -0.0099 -0.0428 0.0557  292 ILE A CD1 
2232  N N   . ASN A  293 ? 1.3898 1.3814 1.5113 -0.0075 -0.0371 0.0813  293 ASN A N   
2233  C CA  . ASN A  293 ? 1.4747 1.4633 1.6024 -0.0076 -0.0333 0.0847  293 ASN A CA  
2234  C C   . ASN A  293 ? 1.4631 1.4527 1.5809 -0.0098 -0.0354 0.0830  293 ASN A C   
2235  O O   . ASN A  293 ? 1.5278 1.5204 1.6447 -0.0106 -0.0411 0.0875  293 ASN A O   
2236  C CB  . ASN A  293 ? 1.5539 1.5438 1.6944 -0.0064 -0.0359 0.0936  293 ASN A CB  
2237  C CG  . ASN A  293 ? 1.7262 1.7130 1.8743 -0.0062 -0.0319 0.0980  293 ASN A CG  
2238  O OD1 . ASN A  293 ? 1.5391 1.5220 1.6838 -0.0069 -0.0264 0.0942  293 ASN A OD1 
2239  N ND2 . ASN A  293 ? 1.7335 1.7220 1.8922 -0.0052 -0.0347 0.1063  293 ASN A ND2 
2240  N N   . THR A  294 ? 1.0811 1.0682 1.1911 -0.0109 -0.0309 0.0765  294 THR A N   
2241  C CA  . THR A  294 ? 1.1719 1.1604 1.2709 -0.0131 -0.0332 0.0737  294 THR A CA  
2242  C C   . THR A  294 ? 1.0746 1.0592 1.1708 -0.0143 -0.0268 0.0697  294 THR A C   
2243  O O   . THR A  294 ? 1.0506 1.0316 1.1497 -0.0138 -0.0202 0.0664  294 THR A O   
2244  C CB  . THR A  294 ? 1.1101 1.1021 1.1972 -0.0140 -0.0372 0.0683  294 THR A CB  
2245  O OG1 . THR A  294 ? 0.9675 0.9613 1.0449 -0.0161 -0.0404 0.0669  294 THR A OG1 
2246  N N   . SER A  295 ? 0.8870 0.8725 0.9772 -0.0160 -0.0287 0.0700  295 SER A N   
2247  C CA  . SER A  295 ? 1.0086 0.9910 1.0940 -0.0175 -0.0235 0.0656  295 SER A CA  
2248  C C   . SER A  295 ? 0.7743 0.7596 0.8458 -0.0194 -0.0262 0.0593  295 SER A C   
2249  O O   . SER A  295 ? 0.7713 0.7549 0.8370 -0.0208 -0.0221 0.0539  295 SER A O   
2250  C CB  . SER A  295 ? 1.0339 1.0147 1.1239 -0.0181 -0.0230 0.0708  295 SER A CB  
2251  O OG  . SER A  295 ? 1.3289 1.3046 1.4278 -0.0174 -0.0155 0.0717  295 SER A OG  
2252  N N   . LEU A  296 ? 0.6326 0.6222 0.6991 -0.0195 -0.0331 0.0601  296 LEU A N   
2253  C CA  . LEU A  296 ? 0.6320 0.6246 0.6858 -0.0211 -0.0362 0.0549  296 LEU A CA  
2254  C C   . LEU A  296 ? 0.6435 0.6359 0.6917 -0.0211 -0.0325 0.0476  296 LEU A C   
2255  O O   . LEU A  296 ? 0.6460 0.6372 0.6991 -0.0196 -0.0299 0.0469  296 LEU A O   
2256  C CB  . LEU A  296 ? 0.5661 0.5629 0.6166 -0.0211 -0.0439 0.0575  296 LEU A CB  
2257  C CG  . LEU A  296 ? 0.6831 0.6811 0.7381 -0.0214 -0.0484 0.0649  296 LEU A CG  
2258  C CD1 . LEU A  296 ? 0.7544 0.7567 0.8046 -0.0219 -0.0558 0.0664  296 LEU A CD1 
2259  C CD2 . LEU A  296 ? 0.5891 0.5858 0.6406 -0.0231 -0.0473 0.0654  296 LEU A CD2 
2260  N N   . PRO A  297 ? 0.6337 0.6272 0.6716 -0.0228 -0.0323 0.0422  297 PRO A N   
2261  C CA  . PRO A  297 ? 0.5809 0.5747 0.6128 -0.0232 -0.0287 0.0352  297 PRO A CA  
2262  C C   . PRO A  297 ? 0.6682 0.6653 0.6963 -0.0221 -0.0321 0.0331  297 PRO A C   
2263  O O   . PRO A  297 ? 0.6682 0.6653 0.6944 -0.0218 -0.0290 0.0286  297 PRO A O   
2264  C CB  . PRO A  297 ? 0.5672 0.5621 0.5895 -0.0255 -0.0289 0.0313  297 PRO A CB  
2265  C CG  . PRO A  297 ? 0.7803 0.7742 0.8053 -0.0263 -0.0306 0.0363  297 PRO A CG  
2266  C CD  . PRO A  297 ? 0.6919 0.6866 0.7236 -0.0247 -0.0351 0.0428  297 PRO A CD  
2267  N N   . PHE A  298 ? 0.6357 0.6355 0.6626 -0.0218 -0.0384 0.0363  298 PHE A N   
2268  C CA  . PHE A  298 ? 0.5941 0.5971 0.6167 -0.0209 -0.0417 0.0342  298 PHE A CA  
2269  C C   . PHE A  298 ? 0.5918 0.5958 0.6205 -0.0195 -0.0461 0.0394  298 PHE A C   
2270  O O   . PHE A  298 ? 0.6965 0.7004 0.7297 -0.0198 -0.0489 0.0448  298 PHE A O   
2271  C CB  . PHE A  298 ? 0.5267 0.5329 0.5382 -0.0224 -0.0452 0.0309  298 PHE A CB  
2272  C CG  . PHE A  298 ? 0.5390 0.5446 0.5446 -0.0242 -0.0418 0.0266  298 PHE A CG  
2273  C CD1 . PHE A  298 ? 0.5028 0.5085 0.5051 -0.0243 -0.0375 0.0211  298 PHE A CD1 
2274  C CD2 . PHE A  298 ? 0.5231 0.5283 0.5265 -0.0259 -0.0430 0.0283  298 PHE A CD2 
2275  C CE1 . PHE A  298 ? 0.5668 0.5723 0.5638 -0.0262 -0.0344 0.0171  298 PHE A CE1 
2276  C CE2 . PHE A  298 ? 0.6143 0.6189 0.6124 -0.0276 -0.0397 0.0243  298 PHE A CE2 
2277  C CZ  . PHE A  298 ? 0.4900 0.4948 0.4850 -0.0278 -0.0355 0.0187  298 PHE A CZ  
2278  N N   . GLN A  299 ? 0.5894 0.5947 0.6184 -0.0181 -0.0465 0.0378  299 GLN A N   
2279  C CA  . GLN A  299 ? 0.5005 0.5070 0.5347 -0.0169 -0.0506 0.0420  299 GLN A CA  
2280  C C   . GLN A  299 ? 0.5404 0.5498 0.5680 -0.0165 -0.0535 0.0387  299 GLN A C   
2281  O O   . GLN A  299 ? 0.8983 0.9081 0.9208 -0.0162 -0.0508 0.0336  299 GLN A O   
2282  C CB  . GLN A  299 ? 0.4752 0.4790 0.5205 -0.0150 -0.0470 0.0447  299 GLN A CB  
2283  C CG  . GLN A  299 ? 0.5532 0.5554 0.5981 -0.0141 -0.0416 0.0399  299 GLN A CG  
2284  C CD  . GLN A  299 ? 0.5564 0.5607 0.5991 -0.0128 -0.0435 0.0380  299 GLN A CD  
2285  O OE1 . GLN A  299 ? 0.4734 0.4800 0.5163 -0.0125 -0.0486 0.0406  299 GLN A OE1 
2286  N NE2 . GLN A  299 ? 0.5183 0.5218 0.5588 -0.0122 -0.0393 0.0335  299 GLN A NE2 
2287  N N   . ASN A  300 ? 0.5671 0.5788 0.5950 -0.0165 -0.0590 0.0418  300 ASN A N   
2288  C CA  . ASN A  300 ? 0.5385 0.5527 0.5606 -0.0162 -0.0618 0.0391  300 ASN A CA  
2289  C C   . ASN A  300 ? 0.4460 0.4605 0.4752 -0.0146 -0.0636 0.0421  300 ASN A C   
2290  O O   . ASN A  300 ? 0.4587 0.4754 0.4847 -0.0146 -0.0671 0.0416  300 ASN A O   
2291  C CB  . ASN A  300 ? 0.4833 0.5000 0.4973 -0.0181 -0.0668 0.0389  300 ASN A CB  
2292  C CG  . ASN A  300 ? 0.6084 0.6259 0.6266 -0.0191 -0.0715 0.0447  300 ASN A CG  
2293  O OD1 . ASN A  300 ? 0.7071 0.7233 0.7345 -0.0183 -0.0709 0.0493  300 ASN A OD1 
2294  N ND2 . ASN A  300 ? 0.5405 0.5602 0.5519 -0.0208 -0.0761 0.0447  300 ASN A ND2 
2295  N N   . ILE A  301 ? 0.4674 0.4797 0.5065 -0.0134 -0.0608 0.0453  301 ILE A N   
2296  C CA  . ILE A  301 ? 0.5372 0.5497 0.5844 -0.0119 -0.0622 0.0487  301 ILE A CA  
2297  C C   . ILE A  301 ? 0.5007 0.5130 0.5467 -0.0102 -0.0597 0.0449  301 ILE A C   
2298  O O   . ILE A  301 ? 0.5205 0.5345 0.5658 -0.0097 -0.0628 0.0450  301 ILE A O   
2299  C CB  . ILE A  301 ? 0.5846 0.5945 0.6434 -0.0110 -0.0596 0.0536  301 ILE A CB  
2300  C CG1 . ILE A  301 ? 0.4331 0.4437 0.4941 -0.0124 -0.0627 0.0584  301 ILE A CG1 
2301  C CG2 . ILE A  301 ? 0.4710 0.4811 0.5385 -0.0093 -0.0604 0.0566  301 ILE A CG2 
2302  C CD1 . ILE A  301 ? 0.7086 0.7168 0.7812 -0.0115 -0.0599 0.0635  301 ILE A CD1 
2303  N N   . HIS A  302 ? 0.5547 0.5648 0.6005 -0.0095 -0.0541 0.0414  302 HIS A N   
2304  C CA  . HIS A  302 ? 0.5850 0.5948 0.6300 -0.0079 -0.0513 0.0381  302 HIS A CA  
2305  C C   . HIS A  302 ? 0.5997 0.6083 0.6398 -0.0082 -0.0460 0.0330  302 HIS A C   
2306  O O   . HIS A  302 ? 0.6440 0.6504 0.6862 -0.0089 -0.0426 0.0331  302 HIS A O   
2307  C CB  . HIS A  302 ? 0.5187 0.5266 0.5747 -0.0062 -0.0496 0.0415  302 HIS A CB  
2308  C CG  . HIS A  302 ? 0.6196 0.6280 0.6752 -0.0046 -0.0488 0.0393  302 HIS A CG  
2309  N ND1 . HIS A  302 ? 0.6149 0.6219 0.6682 -0.0038 -0.0438 0.0352  302 HIS A ND1 
2310  C CD2 . HIS A  302 ? 0.5808 0.5908 0.6380 -0.0038 -0.0522 0.0408  302 HIS A CD2 
2311  C CE1 . HIS A  302 ? 0.6483 0.6560 0.7018 -0.0023 -0.0442 0.0343  302 HIS A CE1 
2312  N NE2 . HIS A  302 ? 0.4923 0.5018 0.5483 -0.0023 -0.0492 0.0376  302 HIS A NE2 
2313  N N   . PRO A  303 ? 0.5163 0.5265 0.5498 -0.0076 -0.0453 0.0286  303 PRO A N   
2314  C CA  . PRO A  303 ? 0.4940 0.5038 0.5220 -0.0080 -0.0407 0.0236  303 PRO A CA  
2315  C C   . PRO A  303 ? 0.5502 0.5568 0.5847 -0.0071 -0.0350 0.0232  303 PRO A C   
2316  O O   . PRO A  303 ? 0.5433 0.5481 0.5768 -0.0081 -0.0306 0.0209  303 PRO A O   
2317  C CB  . PRO A  303 ? 0.4772 0.4901 0.4981 -0.0073 -0.0424 0.0203  303 PRO A CB  
2318  C CG  . PRO A  303 ? 0.5980 0.6127 0.6185 -0.0072 -0.0482 0.0230  303 PRO A CG  
2319  C CD  . PRO A  303 ? 0.6256 0.6384 0.6559 -0.0069 -0.0493 0.0283  303 PRO A CD  
2320  N N   . ILE A  304 ? 0.4649 0.4705 0.5057 -0.0053 -0.0348 0.0254  304 ILE A N   
2321  C CA  . ILE A  304 ? 0.5601 0.5624 0.6076 -0.0044 -0.0293 0.0253  304 ILE A CA  
2322  C C   . ILE A  304 ? 0.5263 0.5254 0.5832 -0.0046 -0.0276 0.0295  304 ILE A C   
2323  O O   . ILE A  304 ? 0.6554 0.6548 0.7184 -0.0041 -0.0312 0.0344  304 ILE A O   
2324  C CB  . ILE A  304 ? 0.4859 0.4882 0.5372 -0.0024 -0.0294 0.0261  304 ILE A CB  
2325  C CG1 . ILE A  304 ? 0.4412 0.4458 0.4839 -0.0020 -0.0289 0.0215  304 ILE A CG1 
2326  C CG2 . ILE A  304 ? 0.7199 0.7182 0.7804 -0.0014 -0.0242 0.0275  304 ILE A CG2 
2327  C CD1 . ILE A  304 ? 0.7118 0.7203 0.7459 -0.0026 -0.0338 0.0201  304 ILE A CD1 
2328  N N   . THR A  305 ? 0.4608 0.4569 0.5188 -0.0054 -0.0220 0.0276  305 THR A N   
2329  C CA  . THR A  305 ? 0.3557 0.3487 0.4221 -0.0058 -0.0199 0.0313  305 THR A CA  
2330  C C   . THR A  305 ? 0.6533 0.6420 0.7246 -0.0057 -0.0124 0.0296  305 THR A C   
2331  O O   . THR A  305 ? 0.7013 0.6897 0.7667 -0.0063 -0.0087 0.0246  305 THR A O   
2332  C CB  . THR A  305 ? 0.5289 0.5226 0.5902 -0.0078 -0.0213 0.0309  305 THR A CB  
2333  O OG1 . THR A  305 ? 0.8151 0.8084 0.8836 -0.0076 -0.0241 0.0368  305 THR A OG1 
2334  C CG2 . THR A  305 ? 0.5367 0.5277 0.5961 -0.0092 -0.0150 0.0271  305 THR A CG2 
2335  N N   . ILE A  306 ? 0.5679 0.5532 0.6499 -0.0051 -0.0100 0.0340  306 ILE A N   
2336  C CA  . ILE A  306 ? 0.4977 0.4783 0.5852 -0.0052 -0.0024 0.0326  306 ILE A CA  
2337  C C   . ILE A  306 ? 0.4657 0.4432 0.5592 -0.0060 0.0002  0.0355  306 ILE A C   
2338  O O   . ILE A  306 ? 0.5473 0.5255 0.6468 -0.0054 -0.0035 0.0410  306 ILE A O   
2339  C CB  . ILE A  306 ? 0.3879 0.3664 0.4847 -0.0031 -0.0003 0.0351  306 ILE A CB  
2340  C CG1 . ILE A  306 ? 0.5318 0.5133 0.6233 -0.0021 -0.0031 0.0329  306 ILE A CG1 
2341  C CG2 . ILE A  306 ? 0.4253 0.3988 0.5265 -0.0035 0.0081  0.0329  306 ILE A CG2 
2342  C CD1 . ILE A  306 ? 0.4571 0.4364 0.5568 -0.0002 -0.0002 0.0344  306 ILE A CD1 
2343  N N   . GLY A  307 ? 0.5423 0.5166 0.6341 -0.0076 0.0066  0.0317  307 GLY A N   
2344  C CA  . GLY A  307 ? 0.5724 0.5433 0.6696 -0.0085 0.0100  0.0338  307 GLY A CA  
2345  C C   . GLY A  307 ? 0.5940 0.5662 0.6819 -0.0109 0.0096  0.0303  307 GLY A C   
2346  O O   . GLY A  307 ? 0.7787 0.7531 0.8562 -0.0122 0.0094  0.0248  307 GLY A O   
2347  N N   . LYS A  308 ? 0.5905 0.5613 0.6823 -0.0114 0.0094  0.0338  308 LYS A N   
2348  C CA  . LYS A  308 ? 0.6191 0.5908 0.7029 -0.0136 0.0089  0.0311  308 LYS A CA  
2349  C C   . LYS A  308 ? 0.5023 0.4783 0.5831 -0.0134 0.0010  0.0346  308 LYS A C   
2350  O O   . LYS A  308 ? 0.7123 0.6875 0.7992 -0.0131 -0.0006 0.0400  308 LYS A O   
2351  C CB  . LYS A  308 ? 0.6476 0.6144 0.7378 -0.0146 0.0150  0.0322  308 LYS A CB  
2352  C CG  . LYS A  308 ? 0.8488 0.8157 0.9310 -0.0172 0.0162  0.0285  308 LYS A CG  
2353  C CD  . LYS A  308 ? 0.9818 0.9465 1.0705 -0.0173 0.0165  0.0336  308 LYS A CD  
2354  C CE  . LYS A  308 ? 0.9385 0.9012 1.0219 -0.0200 0.0207  0.0296  308 LYS A CE  
2355  N NZ  . LYS A  308 ? 1.1393 1.0971 1.2250 -0.0212 0.0295  0.0254  308 LYS A NZ  
2356  N N   . CYS A  309 ? 0.7135 0.6939 0.7849 -0.0136 -0.0038 0.0317  309 CYS A N   
2357  C CA  . CYS A  309 ? 0.6423 0.6268 0.7110 -0.0133 -0.0116 0.0351  309 CYS A CA  
2358  C C   . CYS A  309 ? 0.5505 0.5376 0.6087 -0.0152 -0.0144 0.0322  309 CYS A C   
2359  O O   . CYS A  309 ? 0.6273 0.6145 0.6784 -0.0168 -0.0113 0.0266  309 CYS A O   
2360  C CB  . CYS A  309 ? 0.4657 0.4531 0.5330 -0.0117 -0.0155 0.0349  309 CYS A CB  
2361  S SG  . CYS A  309 ? 0.8820 0.8665 0.9612 -0.0094 -0.0121 0.0379  309 CYS A SG  
2362  N N   . PRO A  310 ? 0.5654 0.5551 0.6227 -0.0153 -0.0204 0.0361  310 PRO A N   
2363  C CA  . PRO A  310 ? 0.5495 0.5421 0.5966 -0.0171 -0.0239 0.0336  310 PRO A CA  
2364  C C   . PRO A  310 ? 0.5568 0.5527 0.5948 -0.0171 -0.0257 0.0285  310 PRO A C   
2365  O O   . PRO A  310 ? 0.5351 0.5316 0.5753 -0.0155 -0.0260 0.0284  310 PRO A O   
2366  C CB  . PRO A  310 ? 0.4399 0.4345 0.4891 -0.0168 -0.0303 0.0394  310 PRO A CB  
2367  C CG  . PRO A  310 ? 0.6120 0.6039 0.6736 -0.0153 -0.0289 0.0453  310 PRO A CG  
2368  C CD  . PRO A  310 ? 0.5196 0.5095 0.5857 -0.0140 -0.0242 0.0431  310 PRO A CD  
2369  N N   . LYS A  311 ? 0.5687 0.5669 0.5970 -0.0187 -0.0268 0.0246  311 LYS A N   
2370  C CA  . LYS A  311 ? 0.4953 0.4968 0.5152 -0.0187 -0.0281 0.0198  311 LYS A CA  
2371  C C   . LYS A  311 ? 0.4595 0.4643 0.4773 -0.0177 -0.0346 0.0220  311 LYS A C   
2372  O O   . LYS A  311 ? 0.5802 0.5859 0.5979 -0.0183 -0.0388 0.0254  311 LYS A O   
2373  C CB  . LYS A  311 ? 0.4571 0.4602 0.4679 -0.0208 -0.0270 0.0150  311 LYS A CB  
2374  C CG  . LYS A  311 ? 0.5005 0.5045 0.5068 -0.0212 -0.0229 0.0092  311 LYS A CG  
2375  C CD  . LYS A  311 ? 0.4083 0.4085 0.4217 -0.0207 -0.0171 0.0091  311 LYS A CD  
2376  C CE  . LYS A  311 ? 0.5453 0.5425 0.5592 -0.0227 -0.0116 0.0069  311 LYS A CE  
2377  N NZ  . LYS A  311 ? 0.5937 0.5877 0.6120 -0.0226 -0.0053 0.0050  311 LYS A NZ  
2378  N N   . TYR A  312 ? 0.4671 0.4737 0.4832 -0.0164 -0.0352 0.0200  312 TYR A N   
2379  C CA  . TYR A  312 ? 0.4505 0.4599 0.4646 -0.0156 -0.0408 0.0217  312 TYR A CA  
2380  C C   . TYR A  312 ? 0.5350 0.5478 0.5391 -0.0168 -0.0441 0.0189  312 TYR A C   
2381  O O   . TYR A  312 ? 0.6810 0.6952 0.6785 -0.0174 -0.0421 0.0142  312 TYR A O   
2382  C CB  . TYR A  312 ? 0.3748 0.3848 0.3906 -0.0137 -0.0402 0.0206  312 TYR A CB  
2383  C CG  . TYR A  312 ? 0.4499 0.4627 0.4635 -0.0129 -0.0456 0.0220  312 TYR A CG  
2384  C CD1 . TYR A  312 ? 0.4919 0.5044 0.5108 -0.0126 -0.0496 0.0271  312 TYR A CD1 
2385  C CD2 . TYR A  312 ? 0.5613 0.5769 0.5676 -0.0125 -0.0466 0.0183  312 TYR A CD2 
2386  C CE1 . TYR A  312 ? 0.4131 0.4280 0.4299 -0.0123 -0.0543 0.0280  312 TYR A CE1 
2387  C CE2 . TYR A  312 ? 0.4661 0.4838 0.4706 -0.0119 -0.0512 0.0194  312 TYR A CE2 
2388  C CZ  . TYR A  312 ? 0.5278 0.5450 0.5373 -0.0119 -0.0549 0.0241  312 TYR A CZ  
2389  O OH  . TYR A  312 ? 0.5875 0.6068 0.5951 -0.0116 -0.0592 0.0249  312 TYR A OH  
2390  N N   . VAL A  313 ? 0.5928 0.6067 0.5958 -0.0174 -0.0491 0.0220  313 VAL A N   
2391  C CA  . VAL A  313 ? 0.4958 0.5125 0.4898 -0.0188 -0.0522 0.0197  313 VAL A CA  
2392  C C   . VAL A  313 ? 0.4534 0.4721 0.4460 -0.0183 -0.0575 0.0216  313 VAL A C   
2393  O O   . VAL A  313 ? 0.6233 0.6413 0.6222 -0.0177 -0.0598 0.0259  313 VAL A O   
2394  C CB  . VAL A  313 ? 0.5689 0.5847 0.5612 -0.0208 -0.0528 0.0210  313 VAL A CB  
2395  C CG1 . VAL A  313 ? 0.7134 0.7319 0.6965 -0.0222 -0.0561 0.0189  313 VAL A CG1 
2396  C CG2 . VAL A  313 ? 0.6118 0.6255 0.6050 -0.0215 -0.0472 0.0187  313 VAL A CG2 
2397  N N   . LYS A  314 ? 0.5645 0.5859 0.5490 -0.0187 -0.0593 0.0183  314 LYS A N   
2398  C CA  . LYS A  314 ? 0.5888 0.6120 0.5711 -0.0184 -0.0637 0.0193  314 LYS A CA  
2399  C C   . LYS A  314 ? 0.5576 0.5813 0.5373 -0.0204 -0.0679 0.0218  314 LYS A C   
2400  O O   . LYS A  314 ? 0.6837 0.7088 0.6607 -0.0208 -0.0718 0.0225  314 LYS A O   
2401  C CB  . LYS A  314 ? 0.5324 0.5582 0.5075 -0.0179 -0.0634 0.0147  314 LYS A CB  
2402  C CG  . LYS A  314 ? 0.7071 0.7343 0.6817 -0.0169 -0.0664 0.0152  314 LYS A CG  
2403  C CD  . LYS A  314 ? 1.1108 1.1404 1.0790 -0.0160 -0.0653 0.0108  314 LYS A CD  
2404  C CE  . LYS A  314 ? 1.2025 1.2321 1.1716 -0.0149 -0.0606 0.0081  314 LYS A CE  
2405  N NZ  . LYS A  314 ? 0.9717 1.0042 0.9336 -0.0146 -0.0594 0.0039  314 LYS A NZ  
2406  N N   . SER A  315 ? 0.6105 0.6328 0.5907 -0.0218 -0.0670 0.0230  315 SER A N   
2407  C CA  . SER A  315 ? 0.6404 0.6631 0.6178 -0.0239 -0.0707 0.0254  315 SER A CA  
2408  C C   . SER A  315 ? 0.6529 0.6754 0.6358 -0.0240 -0.0747 0.0308  315 SER A C   
2409  O O   . SER A  315 ? 0.5868 0.6082 0.5779 -0.0225 -0.0739 0.0336  315 SER A O   
2410  C CB  . SER A  315 ? 0.6671 0.6880 0.6447 -0.0251 -0.0683 0.0259  315 SER A CB  
2411  O OG  . SER A  315 ? 0.9233 0.9449 0.8950 -0.0255 -0.0650 0.0208  315 SER A OG  
2412  N N   . THR A  316 ? 0.7366 0.7603 0.7149 -0.0259 -0.0790 0.0322  316 THR A N   
2413  C CA  . THR A  316 ? 0.6573 0.6815 0.6400 -0.0266 -0.0833 0.0374  316 THR A CA  
2414  C C   . THR A  316 ? 0.6904 0.7135 0.6762 -0.0280 -0.0840 0.0417  316 THR A C   
2415  O O   . THR A  316 ? 0.8426 0.8655 0.8359 -0.0278 -0.0857 0.0469  316 THR A O   
2416  C CB  . THR A  316 ? 0.7699 0.7961 0.7457 -0.0283 -0.0878 0.0366  316 THR A CB  
2417  O OG1 . THR A  316 ? 0.9603 0.9871 0.9391 -0.0299 -0.0923 0.0419  316 THR A OG1 
2418  C CG2 . THR A  316 ? 0.8748 0.9015 0.8409 -0.0300 -0.0876 0.0330  316 THR A CG2 
2419  N N   . LYS A  317 ? 0.8303 0.8528 0.8103 -0.0293 -0.0825 0.0396  317 LYS A N   
2420  C CA  . LYS A  317 ? 0.7866 0.8080 0.7690 -0.0305 -0.0825 0.0433  317 LYS A CA  
2421  C C   . LYS A  317 ? 0.7412 0.7610 0.7197 -0.0308 -0.0781 0.0397  317 LYS A C   
2422  O O   . LYS A  317 ? 0.7228 0.7436 0.6937 -0.0312 -0.0771 0.0346  317 LYS A O   
2423  C CB  . LYS A  317 ? 0.8193 0.8421 0.7971 -0.0330 -0.0877 0.0462  317 LYS A CB  
2424  C CG  . LYS A  317 ? 0.9842 1.0084 0.9510 -0.0347 -0.0892 0.0417  317 LYS A CG  
2425  C CD  . LYS A  317 ? 1.2582 1.2836 1.2203 -0.0375 -0.0940 0.0445  317 LYS A CD  
2426  C CE  . LYS A  317 ? 1.1820 1.2061 1.1442 -0.0388 -0.0933 0.0472  317 LYS A CE  
2427  N NZ  . LYS A  317 ? 0.9353 0.9606 0.8921 -0.0418 -0.0980 0.0499  317 LYS A NZ  
2428  N N   . LEU A  318 ? 0.7959 0.8136 0.7800 -0.0307 -0.0755 0.0425  318 LEU A N   
2429  C CA  . LEU A  318 ? 0.6510 0.6671 0.6324 -0.0313 -0.0713 0.0394  318 LEU A CA  
2430  C C   . LEU A  318 ? 0.6703 0.6850 0.6538 -0.0327 -0.0718 0.0439  318 LEU A C   
2431  O O   . LEU A  318 ? 0.7461 0.7582 0.7350 -0.0322 -0.0677 0.0450  318 LEU A O   
2432  C CB  . LEU A  318 ? 0.6016 0.6158 0.5884 -0.0295 -0.0657 0.0372  318 LEU A CB  
2433  C CG  . LEU A  318 ? 0.6581 0.6736 0.6416 -0.0283 -0.0639 0.0318  318 LEU A CG  
2434  C CD1 . LEU A  318 ? 0.6486 0.6619 0.6385 -0.0267 -0.0585 0.0307  318 LEU A CD1 
2435  C CD2 . LEU A  318 ? 0.4621 0.4792 0.4356 -0.0296 -0.0634 0.0265  318 LEU A CD2 
2436  N N   . ARG A  319 ? 0.7670 0.7832 0.7462 -0.0345 -0.0766 0.0465  319 ARG A N   
2437  C CA  . ARG A  319 ? 0.7400 0.7551 0.7210 -0.0359 -0.0775 0.0513  319 ARG A CA  
2438  C C   . ARG A  319 ? 0.6331 0.6466 0.6091 -0.0371 -0.0740 0.0482  319 ARG A C   
2439  O O   . ARG A  319 ? 0.4728 0.4874 0.4399 -0.0383 -0.0742 0.0434  319 ARG A O   
2440  C CB  . ARG A  319 ? 0.8426 0.8600 0.8203 -0.0378 -0.0838 0.0552  319 ARG A CB  
2441  C CG  . ARG A  319 ? 0.8134 0.8301 0.7934 -0.0391 -0.0852 0.0610  319 ARG A CG  
2442  C CD  . ARG A  319 ? 0.8499 0.8692 0.8306 -0.0405 -0.0915 0.0666  319 ARG A CD  
2443  N NE  . ARG A  319 ? 0.9765 0.9963 0.9679 -0.0387 -0.0925 0.0716  319 ARG A NE  
2444  C CZ  . ARG A  319 ? 0.9837 1.0020 0.9848 -0.0374 -0.0905 0.0767  319 ARG A CZ  
2445  N NH1 . ARG A  319 ? 0.9774 0.9933 0.9788 -0.0377 -0.0871 0.0773  319 ARG A NH1 
2446  N NH2 . ARG A  319 ? 1.0659 1.0849 1.0768 -0.0358 -0.0915 0.0812  319 ARG A NH2 
2447  N N   . LEU A  320 ? 0.6900 0.7009 0.6722 -0.0368 -0.0707 0.0510  320 LEU A N   
2448  C CA  . LEU A  320 ? 0.6031 0.6120 0.5818 -0.0379 -0.0667 0.0484  320 LEU A CA  
2449  C C   . LEU A  320 ? 0.7007 0.7093 0.6782 -0.0397 -0.0692 0.0532  320 LEU A C   
2450  O O   . LEU A  320 ? 0.7866 0.7948 0.7712 -0.0393 -0.0709 0.0596  320 LEU A O   
2451  C CB  . LEU A  320 ? 0.6551 0.6608 0.6419 -0.0364 -0.0606 0.0481  320 LEU A CB  
2452  C CG  . LEU A  320 ? 0.7331 0.7366 0.7172 -0.0374 -0.0552 0.0441  320 LEU A CG  
2453  C CD1 . LEU A  320 ? 0.5895 0.5949 0.5649 -0.0380 -0.0542 0.0367  320 LEU A CD1 
2454  C CD2 . LEU A  320 ? 0.5911 0.5911 0.5844 -0.0361 -0.0493 0.0449  320 LEU A CD2 
2455  N N   . ALA A  321 ? 0.6386 0.6475 0.6072 -0.0418 -0.0696 0.0503  321 ALA A N   
2456  C CA  . ALA A  321 ? 0.6546 0.6632 0.6212 -0.0437 -0.0719 0.0547  321 ALA A CA  
2457  C C   . ALA A  321 ? 0.7244 0.7296 0.6974 -0.0433 -0.0674 0.0574  321 ALA A C   
2458  O O   . ALA A  321 ? 0.7990 0.8022 0.7718 -0.0431 -0.0621 0.0531  321 ALA A O   
2459  C CB  . ALA A  321 ? 0.5365 0.5462 0.4916 -0.0460 -0.0735 0.0507  321 ALA A CB  
2460  N N   . THR A  322 ? 0.7879 0.7926 0.7667 -0.0433 -0.0694 0.0647  322 THR A N   
2461  C CA  . THR A  322 ? 0.7515 0.7530 0.7366 -0.0430 -0.0652 0.0681  322 THR A CA  
2462  C C   . THR A  322 ? 0.7596 0.7609 0.7397 -0.0453 -0.0673 0.0712  322 THR A C   
2463  O O   . THR A  322 ? 0.6377 0.6364 0.6174 -0.0459 -0.0632 0.0705  322 THR A O   
2464  C CB  . THR A  322 ? 0.7943 0.7948 0.7920 -0.0410 -0.0649 0.0749  322 THR A CB  
2465  O OG1 . THR A  322 ? 0.9157 0.9194 0.9143 -0.0413 -0.0714 0.0808  322 THR A OG1 
2466  C CG2 . THR A  322 ? 0.8607 0.8604 0.8643 -0.0387 -0.0615 0.0719  322 THR A CG2 
2467  N N   . GLY A  323 ? 0.8594 0.8637 0.8358 -0.0465 -0.0737 0.0749  323 GLY A N   
2468  C CA  . GLY A  323 ? 0.8516 0.8561 0.8221 -0.0489 -0.0763 0.0778  323 GLY A CA  
2469  C C   . GLY A  323 ? 0.8796 0.8847 0.8379 -0.0510 -0.0764 0.0711  323 GLY A C   
2470  O O   . GLY A  323 ? 0.8012 0.8059 0.7567 -0.0505 -0.0733 0.0644  323 GLY A O   
2471  N N   . LEU A  324 ? 0.7946 0.8007 0.7457 -0.0535 -0.0801 0.0732  324 LEU A N   
2472  C CA  . LEU A  324 ? 0.7394 0.7460 0.6789 -0.0557 -0.0804 0.0675  324 LEU A CA  
2473  C C   . LEU A  324 ? 0.8702 0.8801 0.8028 -0.0572 -0.0862 0.0667  324 LEU A C   
2474  O O   . LEU A  324 ? 1.0226 1.0343 0.9594 -0.0561 -0.0891 0.0687  324 LEU A O   
2475  C CB  . LEU A  324 ? 0.8218 0.8267 0.7572 -0.0578 -0.0797 0.0697  324 LEU A CB  
2476  C CG  . LEU A  324 ? 0.9354 0.9407 0.8742 -0.0586 -0.0832 0.0784  324 LEU A CG  
2477  C CD1 . LEU A  324 ? 0.9898 0.9943 0.9206 -0.0614 -0.0837 0.0791  324 LEU A CD1 
2478  C CD2 . LEU A  324 ? 0.8128 0.8160 0.7639 -0.0563 -0.0799 0.0835  324 LEU A CD2 
2479  N N   . ARG A  325 ? 0.8095 0.8198 0.7315 -0.0597 -0.0875 0.0635  325 ARG A N   
2480  C CA  . ARG A  325 ? 0.8833 0.8962 0.7978 -0.0616 -0.0928 0.0629  325 ARG A CA  
2481  C C   . ARG A  325 ? 1.0306 1.0452 0.9477 -0.0628 -0.0981 0.0707  325 ARG A C   
2482  O O   . ARG A  325 ? 1.0319 1.0457 0.9570 -0.0617 -0.0975 0.0766  325 ARG A O   
2483  C CB  . ARG A  325 ? 0.8809 0.8936 0.7840 -0.0642 -0.0925 0.0583  325 ARG A CB  
2484  C CG  . ARG A  325 ? 0.8004 0.8133 0.6992 -0.0634 -0.0896 0.0501  325 ARG A CG  
2485  C CD  . ARG A  325 ? 1.0276 1.0427 0.9190 -0.0648 -0.0933 0.0473  325 ARG A CD  
2486  N NE  . ARG A  325 ? 1.1176 1.1323 0.9990 -0.0670 -0.0924 0.0426  325 ARG A NE  
2487  C CZ  . ARG A  325 ? 1.1866 1.2015 1.0647 -0.0663 -0.0892 0.0360  325 ARG A CZ  
2488  N NH1 . ARG A  325 ? 1.0480 1.0634 0.9314 -0.0636 -0.0866 0.0331  325 ARG A NH1 
2489  N NH2 . ARG A  325 ? 1.1198 1.1344 0.9891 -0.0684 -0.0885 0.0324  325 ARG A NH2 
2490  N N   . ASN A  326 ? 1.1253 1.1423 1.0359 -0.0649 -0.1031 0.0708  326 ASN A N   
2491  C CA  . ASN A  326 ? 1.1210 1.1402 1.0331 -0.0666 -0.1086 0.0781  326 ASN A CA  
2492  C C   . ASN A  326 ? 1.2596 1.2802 1.1603 -0.0704 -0.1129 0.0774  326 ASN A C   
2493  O O   . ASN A  326 ? 1.2746 1.2958 1.1681 -0.0715 -0.1134 0.0718  326 ASN A O   
2494  C CB  . ASN A  326 ? 1.2782 1.2996 1.1988 -0.0647 -0.1110 0.0811  326 ASN A CB  
2495  C CG  . ASN A  326 ? 1.3126 1.3361 1.2382 -0.0656 -0.1157 0.0899  326 ASN A CG  
2496  O OD1 . ASN A  326 ? 1.2595 1.2822 1.1874 -0.0660 -0.1152 0.0949  326 ASN A OD1 
2497  N ND2 . ASN A  326 ? 1.3494 1.3760 1.2772 -0.0660 -0.1202 0.0921  326 ASN A ND2 
2498  N N   . ILE A  327 ? 1.3699 1.3912 1.2693 -0.0726 -0.1159 0.0836  327 ILE A N   
2499  C CA  . ILE A  327 ? 1.2855 1.3074 1.1735 -0.0766 -0.1189 0.0830  327 ILE A CA  
2500  C C   . ILE A  327 ? 1.2003 1.2249 1.0896 -0.0787 -0.1246 0.0913  327 ILE A C   
2501  O O   . ILE A  327 ? 0.9881 1.0145 0.8874 -0.0769 -0.1262 0.0968  327 ILE A O   
2502  C CB  . ILE A  327 ? 1.1022 1.1210 0.9851 -0.0772 -0.1146 0.0803  327 ILE A CB  
2503  C CG1 . ILE A  327 ? 0.9677 0.9852 0.8434 -0.0773 -0.1113 0.0713  327 ILE A CG1 
2504  C CG2 . ILE A  327 ? 1.2205 1.2395 1.0970 -0.0807 -0.1174 0.0849  327 ILE A CG2 
2505  C CD1 . ILE A  327 ? 0.8196 0.8349 0.7009 -0.0739 -0.1051 0.0668  327 ILE A CD1 
2506  N N   . GLY B  1   ? 1.3135 1.3215 1.1917 -0.0666 -0.0689 0.0249  1   GLY B N   
2507  C CA  . GLY B  1   ? 1.0672 1.0777 0.9425 -0.0658 -0.0684 0.0190  1   GLY B CA  
2508  C C   . GLY B  1   ? 0.9024 0.9132 0.7756 -0.0660 -0.0636 0.0132  1   GLY B C   
2509  O O   . GLY B  1   ? 0.9968 1.0096 0.8643 -0.0665 -0.0635 0.0084  1   GLY B O   
2510  N N   . LEU B  2   ? 0.8729 0.8817 0.7510 -0.0657 -0.0597 0.0136  2   LEU B N   
2511  C CA  . LEU B  2   ? 0.8960 0.9052 0.7729 -0.0661 -0.0549 0.0080  2   LEU B CA  
2512  C C   . LEU B  2   ? 0.8850 0.8916 0.7599 -0.0681 -0.0523 0.0086  2   LEU B C   
2513  O O   . LEU B  2   ? 0.8208 0.8281 0.6919 -0.0693 -0.0493 0.0038  2   LEU B O   
2514  C CB  . LEU B  2   ? 0.8994 0.9087 0.7836 -0.0641 -0.0516 0.0063  2   LEU B CB  
2515  C CG  . LEU B  2   ? 0.9321 0.9438 0.8144 -0.0641 -0.0480 -0.0005 2   LEU B CG  
2516  C CD1 . LEU B  2   ? 0.7773 0.7928 0.6542 -0.0637 -0.0506 -0.0039 2   LEU B CD1 
2517  C CD2 . LEU B  2   ? 0.5901 0.6016 0.4795 -0.0625 -0.0445 -0.0017 2   LEU B CD2 
2518  N N   . PHE B  3   ? 0.9775 0.9814 0.8551 -0.0686 -0.0533 0.0145  3   PHE B N   
2519  C CA  . PHE B  3   ? 0.9912 0.9922 0.8675 -0.0704 -0.0506 0.0157  3   PHE B CA  
2520  C C   . PHE B  3   ? 1.1237 1.1241 0.9929 -0.0726 -0.0541 0.0185  3   PHE B C   
2521  O O   . PHE B  3   ? 1.1701 1.1681 1.0379 -0.0742 -0.0525 0.0205  3   PHE B O   
2522  C CB  . PHE B  3   ? 1.0141 1.0120 0.8991 -0.0694 -0.0482 0.0203  3   PHE B CB  
2523  C CG  . PHE B  3   ? 1.0390 1.0365 0.9300 -0.0681 -0.0433 0.0168  3   PHE B CG  
2524  C CD1 . PHE B  3   ? 1.0226 1.0214 0.9190 -0.0658 -0.0439 0.0168  3   PHE B CD1 
2525  C CD2 . PHE B  3   ? 1.0531 1.0491 0.9443 -0.0692 -0.0380 0.0133  3   PHE B CD2 
2526  C CE1 . PHE B  3   ? 0.9884 0.9868 0.8900 -0.0648 -0.0393 0.0134  3   PHE B CE1 
2527  C CE2 . PHE B  3   ? 0.9949 0.9906 0.8912 -0.0683 -0.0335 0.0098  3   PHE B CE2 
2528  C CZ  . PHE B  3   ? 0.9759 0.9729 0.8773 -0.0662 -0.0341 0.0099  3   PHE B CZ  
2529  N N   . GLY B  4   ? 1.0581 1.0608 0.9228 -0.0728 -0.0586 0.0187  4   GLY B N   
2530  C CA  . GLY B  4   ? 0.9865 0.9889 0.8434 -0.0752 -0.0619 0.0206  4   GLY B CA  
2531  C C   . GLY B  4   ? 1.0085 1.0091 0.8669 -0.0760 -0.0651 0.0282  4   GLY B C   
2532  O O   . GLY B  4   ? 1.0589 1.0594 0.9107 -0.0781 -0.0683 0.0302  4   GLY B O   
2533  N N   . ALA B  5   ? 1.0581 1.0575 0.9254 -0.0742 -0.0641 0.0324  5   ALA B N   
2534  C CA  . ALA B  5   ? 0.9067 0.9046 0.7767 -0.0747 -0.0667 0.0402  5   ALA B CA  
2535  C C   . ALA B  5   ? 0.9188 0.9189 0.7895 -0.0743 -0.0725 0.0443  5   ALA B C   
2536  O O   . ALA B  5   ? 0.9161 0.9170 0.7804 -0.0765 -0.0766 0.0465  5   ALA B O   
2537  C CB  . ALA B  5   ? 0.7893 0.7847 0.6690 -0.0730 -0.0629 0.0435  5   ALA B CB  
2538  N N   . ILE B  6   ? 0.9433 0.9443 0.8219 -0.0718 -0.0727 0.0452  6   ILE B N   
2539  C CA  . ILE B  6   ? 0.7713 0.7744 0.6517 -0.0713 -0.0779 0.0491  6   ILE B CA  
2540  C C   . ILE B  6   ? 0.9509 0.9565 0.8235 -0.0723 -0.0808 0.0445  6   ILE B C   
2541  O O   . ILE B  6   ? 0.9935 0.9999 0.8646 -0.0714 -0.0784 0.0383  6   ILE B O   
2542  C CB  . ILE B  6   ? 0.7702 0.7737 0.6613 -0.0682 -0.0769 0.0507  6   ILE B CB  
2543  C CG1 . ILE B  6   ? 0.7192 0.7199 0.6186 -0.0671 -0.0737 0.0555  6   ILE B CG1 
2544  C CG2 . ILE B  6   ? 0.6946 0.7005 0.5875 -0.0678 -0.0823 0.0545  6   ILE B CG2 
2545  C CD1 . ILE B  6   ? 0.7180 0.7187 0.6283 -0.0642 -0.0728 0.0582  6   ILE B CD1 
2546  N N   . ALA B  7   ? 0.9036 0.9104 0.7712 -0.0744 -0.0858 0.0478  7   ALA B N   
2547  C CA  . ALA B  7   ? 0.8879 0.8964 0.7472 -0.0759 -0.0884 0.0438  7   ALA B CA  
2548  C C   . ALA B  7   ? 1.0011 1.0087 0.8523 -0.0775 -0.0854 0.0380  7   ALA B C   
2549  O O   . ALA B  7   ? 1.1060 1.1149 0.9518 -0.0779 -0.0855 0.0328  7   ALA B O   
2550  C CB  . ALA B  7   ? 0.8612 0.8716 0.7243 -0.0736 -0.0888 0.0408  7   ALA B CB  
2551  N N   . GLY B  8   ? 0.9189 0.9243 0.7696 -0.0784 -0.0826 0.0390  8   GLY B N   
2552  C CA  . GLY B  8   ? 0.9918 0.9963 0.8353 -0.0801 -0.0796 0.0340  8   GLY B CA  
2553  C C   . GLY B  8   ? 1.1932 1.1960 1.0301 -0.0832 -0.0811 0.0374  8   GLY B C   
2554  O O   . GLY B  8   ? 1.2107 1.2143 1.0420 -0.0853 -0.0854 0.0396  8   GLY B O   
2555  N N   . PHE B  9   ? 0.9377 0.9382 0.7750 -0.0837 -0.0775 0.0378  9   PHE B N   
2556  C CA  . PHE B  9   ? 0.9390 0.9378 0.7703 -0.0866 -0.0785 0.0412  9   PHE B CA  
2557  C C   . PHE B  9   ? 1.0959 1.0947 0.9314 -0.0868 -0.0821 0.0497  9   PHE B C   
2558  O O   . PHE B  9   ? 1.3138 1.3120 1.1437 -0.0894 -0.0847 0.0537  9   PHE B O   
2559  C CB  . PHE B  9   ? 1.0234 1.0197 0.8537 -0.0872 -0.0733 0.0389  9   PHE B CB  
2560  C CG  . PHE B  9   ? 1.0254 1.0203 0.8655 -0.0847 -0.0694 0.0402  9   PHE B CG  
2561  C CD1 . PHE B  9   ? 1.1209 1.1143 0.9670 -0.0842 -0.0699 0.0474  9   PHE B CD1 
2562  C CD2 . PHE B  9   ? 1.1822 1.1773 1.0256 -0.0830 -0.0648 0.0343  9   PHE B CD2 
2563  C CE1 . PHE B  9   ? 1.1225 1.1141 0.9777 -0.0820 -0.0658 0.0485  9   PHE B CE1 
2564  C CE2 . PHE B  9   ? 1.1722 1.1656 1.0241 -0.0811 -0.0609 0.0352  9   PHE B CE2 
2565  C CZ  . PHE B  9   ? 1.2306 1.2221 1.0886 -0.0806 -0.0612 0.0422  9   PHE B CZ  
2566  N N   . ILE B  10  ? 1.0095 1.0089 0.8548 -0.0840 -0.0822 0.0526  10  ILE B N   
2567  C CA  . ILE B  10  ? 0.9830 0.9832 0.8334 -0.0837 -0.0863 0.0606  10  ILE B CA  
2568  C C   . ILE B  10  ? 1.0129 1.0161 0.8641 -0.0830 -0.0903 0.0598  10  ILE B C   
2569  O O   . ILE B  10  ? 1.0377 1.0415 0.8961 -0.0801 -0.0889 0.0583  10  ILE B O   
2570  C CB  . ILE B  10  ? 0.8644 0.8631 0.7263 -0.0809 -0.0833 0.0647  10  ILE B CB  
2571  C CG1 . ILE B  10  ? 0.8714 0.8668 0.7334 -0.0812 -0.0779 0.0636  10  ILE B CG1 
2572  C CG2 . ILE B  10  ? 0.8107 0.8105 0.6777 -0.0809 -0.0875 0.0737  10  ILE B CG2 
2573  C CD1 . ILE B  10  ? 0.8701 0.8636 0.7434 -0.0787 -0.0743 0.0673  10  ILE B CD1 
2574  N N   . GLU B  11  ? 1.1335 1.1383 0.9771 -0.0857 -0.0950 0.0608  11  GLU B N   
2575  C CA  . GLU B  11  ? 1.2389 1.2463 1.0816 -0.0855 -0.0985 0.0590  11  GLU B CA  
2576  C C   . GLU B  11  ? 1.0614 1.0708 0.9121 -0.0842 -0.1024 0.0654  11  GLU B C   
2577  O O   . GLU B  11  ? 1.0288 1.0402 0.8810 -0.0833 -0.1046 0.0639  11  GLU B O   
2578  C CB  . GLU B  11  ? 1.4476 1.4557 1.2787 -0.0892 -0.1017 0.0572  11  GLU B CB  
2579  C CG  . GLU B  11  ? 1.6364 1.6426 1.4589 -0.0910 -0.0984 0.0517  11  GLU B CG  
2580  C CD  . GLU B  11  ? 1.9974 2.0029 1.8106 -0.0951 -0.1010 0.0545  11  GLU B CD  
2581  O OE1 . GLU B  11  ? 2.0731 2.0767 1.8793 -0.0968 -0.0982 0.0508  11  GLU B OE1 
2582  O OE2 . GLU B  11  ? 2.0037 2.0107 1.8166 -0.0968 -0.1058 0.0604  11  GLU B OE2 
2583  N N   . GLY B  12  ? 1.0196 1.0286 0.8757 -0.0840 -0.1031 0.0725  12  GLY B N   
2584  C CA  . GLY B  12  ? 1.0128 1.0242 0.8758 -0.0833 -0.1074 0.0794  12  GLY B CA  
2585  C C   . GLY B  12  ? 0.9776 0.9881 0.8527 -0.0804 -0.1054 0.0851  12  GLY B C   
2586  O O   . GLY B  12  ? 1.0098 1.0176 0.8869 -0.0798 -0.1015 0.0862  12  GLY B O   
2587  N N   . GLY B  13  ? 0.9516 0.9642 0.8350 -0.0785 -0.1079 0.0888  13  GLY B N   
2588  C CA  . GLY B  13  ? 0.9665 0.9786 0.8621 -0.0757 -0.1064 0.0948  13  GLY B CA  
2589  C C   . GLY B  13  ? 1.0315 1.0460 0.9297 -0.0771 -0.1114 0.1042  13  GLY B C   
2590  O O   . GLY B  13  ? 1.0628 1.0798 0.9535 -0.0802 -0.1166 0.1057  13  GLY B O   
2591  N N   . TRP B  14  ? 1.0427 1.0563 0.9515 -0.0748 -0.1097 0.1105  14  TRP B N   
2592  C CA  . TRP B  14  ? 0.9905 1.0066 0.9029 -0.0758 -0.1141 0.1202  14  TRP B CA  
2593  C C   . TRP B  14  ? 1.0804 1.0992 1.0045 -0.0735 -0.1166 0.1258  14  TRP B C   
2594  O O   . TRP B  14  ? 1.0227 1.0399 0.9582 -0.0703 -0.1130 0.1288  14  TRP B O   
2595  C CB  . TRP B  14  ? 1.0109 1.0241 0.9262 -0.0755 -0.1106 0.1246  14  TRP B CB  
2596  C CG  . TRP B  14  ? 0.9511 0.9616 0.8553 -0.0779 -0.1082 0.1196  14  TRP B CG  
2597  C CD1 . TRP B  14  ? 0.9784 0.9898 0.8699 -0.0811 -0.1107 0.1147  14  TRP B CD1 
2598  C CD2 . TRP B  14  ? 0.8643 0.8707 0.7692 -0.0773 -0.1025 0.1191  14  TRP B CD2 
2599  N NE1 . TRP B  14  ? 0.9507 0.9589 0.8351 -0.0825 -0.1070 0.1112  14  TRP B NE1 
2600  C CE2 . TRP B  14  ? 0.9472 0.9524 0.8396 -0.0803 -0.1020 0.1138  14  TRP B CE2 
2601  C CE3 . TRP B  14  ? 0.9057 0.9092 0.8208 -0.0746 -0.0975 0.1226  14  TRP B CE3 
2602  C CZ2 . TRP B  14  ? 1.0409 1.0423 0.9307 -0.0806 -0.0970 0.1118  14  TRP B CZ2 
2603  C CZ3 . TRP B  14  ? 1.0376 1.0372 0.9501 -0.0751 -0.0924 0.1205  14  TRP B CZ3 
2604  C CH2 . TRP B  14  ? 1.1581 1.1567 1.0580 -0.0781 -0.0923 0.1153  14  TRP B CH2 
2605  N N   . THR B  15  ? 1.1647 1.1876 1.0860 -0.0753 -0.1227 0.1272  15  THR B N   
2606  C CA  . THR B  15  ? 1.1455 1.1718 1.0773 -0.0736 -0.1261 0.1335  15  THR B CA  
2607  C C   . THR B  15  ? 1.2694 1.2960 1.2096 -0.0728 -0.1262 0.1432  15  THR B C   
2608  O O   . THR B  15  ? 1.2786 1.3063 1.2314 -0.0700 -0.1259 0.1486  15  THR B O   
2609  C CB  . THR B  15  ? 1.1133 1.1444 1.0392 -0.0768 -0.1334 0.1347  15  THR B CB  
2610  O OG1 . THR B  15  ? 1.5074 1.5402 1.4253 -0.0806 -0.1374 0.1391  15  THR B OG1 
2611  C CG2 . THR B  15  ? 1.2031 1.2335 1.1201 -0.0778 -0.1330 0.1252  15  THR B CG2 
2612  N N   . GLY B  16  ? 1.1985 1.2242 1.1319 -0.0751 -0.1264 0.1454  16  GLY B N   
2613  C CA  . GLY B  16  ? 1.3115 1.3375 1.2515 -0.0746 -0.1265 0.1547  16  GLY B CA  
2614  C C   . GLY B  16  ? 1.2011 1.2230 1.1529 -0.0706 -0.1197 0.1560  16  GLY B C   
2615  O O   . GLY B  16  ? 1.3478 1.3708 1.3108 -0.0686 -0.1200 0.1643  16  GLY B O   
2616  N N   . MET B  17  ? 1.1933 1.2106 1.1428 -0.0694 -0.1134 0.1479  17  MET B N   
2617  C CA  . MET B  17  ? 1.1978 1.2109 1.1579 -0.0659 -0.1063 0.1481  17  MET B CA  
2618  C C   . MET B  17  ? 1.2468 1.2601 1.2174 -0.0626 -0.1047 0.1468  17  MET B C   
2619  O O   . MET B  17  ? 1.3243 1.3371 1.2914 -0.0622 -0.1035 0.1389  17  MET B O   
2620  C CB  . MET B  17  ? 1.1021 1.1103 1.0553 -0.0662 -0.1002 0.1399  17  MET B CB  
2621  C CG  . MET B  17  ? 1.2902 1.2938 1.2534 -0.0632 -0.0925 0.1396  17  MET B CG  
2622  S SD  . MET B  17  ? 1.3577 1.3562 1.3124 -0.0641 -0.0857 0.1301  17  MET B SD  
2623  C CE  . MET B  17  ? 1.1709 1.1712 1.1166 -0.0650 -0.0873 0.1198  17  MET B CE  
2624  N N   . VAL B  18  ? 1.3301 1.3443 1.3137 -0.0602 -0.1046 0.1548  18  VAL B N   
2625  C CA  . VAL B  18  ? 1.4374 1.4521 1.4318 -0.0571 -0.1034 0.1547  18  VAL B CA  
2626  C C   . VAL B  18  ? 1.4288 1.4391 1.4357 -0.0536 -0.0961 0.1566  18  VAL B C   
2627  O O   . VAL B  18  ? 1.4261 1.4367 1.4443 -0.0509 -0.0949 0.1588  18  VAL B O   
2628  C CB  . VAL B  18  ? 1.4732 1.4936 1.4733 -0.0573 -0.1103 0.1627  18  VAL B CB  
2629  C CG1 . VAL B  18  ? 1.3389 1.3635 1.3267 -0.0610 -0.1174 0.1605  18  VAL B CG1 
2630  C CG2 . VAL B  18  ? 1.4155 1.4370 1.4231 -0.0569 -0.1115 0.1736  18  VAL B CG2 
2631  N N   . ASP B  19  ? 1.5270 1.5331 1.5319 -0.0539 -0.0911 0.1555  19  ASP B N   
2632  C CA  . ASP B  19  ? 1.5582 1.5597 1.5744 -0.0510 -0.0837 0.1573  19  ASP B CA  
2633  C C   . ASP B  19  ? 1.4601 1.4573 1.4753 -0.0498 -0.0770 0.1473  19  ASP B C   
2634  O O   . ASP B  19  ? 1.4305 1.4246 1.4562 -0.0471 -0.0714 0.1473  19  ASP B O   
2635  C CB  . ASP B  19  ? 1.7343 1.7333 1.7497 -0.0518 -0.0814 0.1619  19  ASP B CB  
2636  C CG  . ASP B  19  ? 1.8333 1.8369 1.8474 -0.0536 -0.0884 0.1713  19  ASP B CG  
2637  O OD1 . ASP B  19  ? 1.8900 1.8983 1.9092 -0.0531 -0.0938 0.1766  19  ASP B OD1 
2638  O OD2 . ASP B  19  ? 1.7705 1.7731 1.7783 -0.0555 -0.0885 0.1733  19  ASP B OD2 
2639  N N   . GLY B  20  ? 1.2942 1.2913 1.2967 -0.0520 -0.0776 0.1390  20  GLY B N   
2640  C CA  . GLY B  20  ? 1.1301 1.1239 1.1304 -0.0514 -0.0718 0.1294  20  GLY B CA  
2641  C C   . GLY B  20  ? 1.1117 1.1075 1.0990 -0.0536 -0.0747 0.1212  20  GLY B C   
2642  O O   . GLY B  20  ? 1.1038 1.1035 1.0844 -0.0555 -0.0813 0.1228  20  GLY B O   
2643  N N   . TRP B  21  ? 0.9815 0.9747 0.9653 -0.0534 -0.0697 0.1125  21  TRP B N   
2644  C CA  . TRP B  21  ? 0.9746 0.9695 0.9468 -0.0551 -0.0717 0.1045  21  TRP B CA  
2645  C C   . TRP B  21  ? 0.8496 0.8438 0.8105 -0.0580 -0.0720 0.1020  21  TRP B C   
2646  O O   . TRP B  21  ? 0.8299 0.8267 0.7808 -0.0602 -0.0764 0.0993  21  TRP B O   
2647  C CB  . TRP B  21  ? 1.0336 1.0266 1.0071 -0.0536 -0.0665 0.0964  21  TRP B CB  
2648  C CG  . TRP B  21  ? 0.9657 0.9607 0.9457 -0.0515 -0.0681 0.0966  21  TRP B CG  
2649  C CD1 . TRP B  21  ? 0.9117 0.9106 0.8925 -0.0515 -0.0744 0.1006  21  TRP B CD1 
2650  C CD2 . TRP B  21  ? 0.9187 0.9118 0.9051 -0.0493 -0.0631 0.0924  21  TRP B CD2 
2651  N NE1 . TRP B  21  ? 0.9096 0.9090 0.8971 -0.0492 -0.0736 0.0993  21  TRP B NE1 
2652  C CE2 . TRP B  21  ? 0.8726 0.8685 0.8635 -0.0478 -0.0667 0.0943  21  TRP B CE2 
2653  C CE3 . TRP B  21  ? 0.8327 0.8221 0.8211 -0.0486 -0.0559 0.0871  21  TRP B CE3 
2654  C CZ2 . TRP B  21  ? 0.8225 0.8174 0.8198 -0.0456 -0.0634 0.0913  21  TRP B CZ2 
2655  C CZ3 . TRP B  21  ? 0.7631 0.7517 0.7577 -0.0465 -0.0527 0.0840  21  TRP B CZ3 
2656  C CH2 . TRP B  21  ? 0.7965 0.7878 0.7954 -0.0450 -0.0564 0.0862  21  TRP B CH2 
2657  N N   . TYR B  22  ? 0.9336 0.9241 0.8964 -0.0581 -0.0669 0.1027  22  TYR B N   
2658  C CA  . TYR B  22  ? 1.0150 1.0045 0.9681 -0.0608 -0.0667 0.1010  22  TYR B CA  
2659  C C   . TYR B  22  ? 1.1370 1.1249 1.0945 -0.0610 -0.0663 0.1095  22  TYR B C   
2660  O O   . TYR B  22  ? 1.2090 1.1948 1.1778 -0.0588 -0.0629 0.1141  22  TYR B O   
2661  C CB  . TYR B  22  ? 1.0436 1.0300 0.9932 -0.0611 -0.0603 0.0925  22  TYR B CB  
2662  C CG  . TYR B  22  ? 1.0449 1.0313 0.9978 -0.0593 -0.0575 0.0863  22  TYR B CG  
2663  C CD1 . TYR B  22  ? 0.9803 0.9637 0.9435 -0.0571 -0.0518 0.0864  22  TYR B CD1 
2664  C CD2 . TYR B  22  ? 0.9866 0.9760 0.9325 -0.0598 -0.0604 0.0804  22  TYR B CD2 
2665  C CE1 . TYR B  22  ? 0.9052 0.8886 0.8711 -0.0556 -0.0492 0.0808  22  TYR B CE1 
2666  C CE2 . TYR B  22  ? 0.9247 0.9143 0.8736 -0.0581 -0.0579 0.0750  22  TYR B CE2 
2667  C CZ  . TYR B  22  ? 0.9305 0.9172 0.8893 -0.0561 -0.0524 0.0752  22  TYR B CZ  
2668  O OH  . TYR B  22  ? 0.7486 0.7355 0.7100 -0.0546 -0.0499 0.0699  22  TYR B OH  
2669  N N   . GLY B  23  ? 1.4932 1.4821 1.4420 -0.0637 -0.0697 0.1115  23  GLY B N   
2670  C CA  . GLY B  23  ? 1.5588 1.5468 1.5104 -0.0642 -0.0703 0.1200  23  GLY B CA  
2671  C C   . GLY B  23  ? 1.5609 1.5507 1.5009 -0.0675 -0.0750 0.1215  23  GLY B C   
2672  O O   . GLY B  23  ? 1.4129 1.4053 1.3433 -0.0695 -0.0791 0.1173  23  GLY B O   
2673  N N   . TYR B  24  ? 1.3872 1.3753 1.3283 -0.0682 -0.0742 0.1278  24  TYR B N   
2674  C CA  . TYR B  24  ? 1.2410 1.2297 1.1708 -0.0716 -0.0770 0.1287  24  TYR B CA  
2675  C C   . TYR B  24  ? 1.2710 1.2641 1.1980 -0.0733 -0.0848 0.1365  24  TYR B C   
2676  O O   . TYR B  24  ? 1.1500 1.1460 1.0852 -0.0717 -0.0881 0.1424  24  TYR B O   
2677  C CB  . TYR B  24  ? 1.1910 1.1753 1.1225 -0.0717 -0.0716 0.1309  24  TYR B CB  
2678  C CG  . TYR B  24  ? 1.0915 1.0712 1.0290 -0.0697 -0.0634 0.1253  24  TYR B CG  
2679  C CD1 . TYR B  24  ? 1.0750 1.0533 1.0259 -0.0665 -0.0598 0.1282  24  TYR B CD1 
2680  C CD2 . TYR B  24  ? 1.1078 1.0849 1.0379 -0.0712 -0.0590 0.1172  24  TYR B CD2 
2681  C CE1 . TYR B  24  ? 1.1529 1.1269 1.1089 -0.0650 -0.0522 0.1228  24  TYR B CE1 
2682  C CE2 . TYR B  24  ? 1.1437 1.1169 1.0790 -0.0697 -0.0516 0.1119  24  TYR B CE2 
2683  C CZ  . TYR B  24  ? 1.1944 1.1661 1.1425 -0.0667 -0.0482 0.1147  24  TYR B CZ  
2684  O OH  . TYR B  24  ? 1.0947 1.0624 1.0476 -0.0656 -0.0407 0.1093  24  TYR B OH  
2685  N N   . HIS B  25  ? 1.3251 1.3189 1.2404 -0.0767 -0.0877 0.1363  25  HIS B N   
2686  C CA  . HIS B  25  ? 1.2803 1.2780 1.1920 -0.0790 -0.0946 0.1441  25  HIS B CA  
2687  C C   . HIS B  25  ? 1.4760 1.4719 1.3801 -0.0816 -0.0940 0.1468  25  HIS B C   
2688  O O   . HIS B  25  ? 1.3833 1.3787 1.2752 -0.0845 -0.0945 0.1413  25  HIS B O   
2689  C CB  . HIS B  25  ? 1.3369 1.3388 1.2398 -0.0813 -0.1009 0.1407  25  HIS B CB  
2690  C CG  . HIS B  25  ? 1.4989 1.5044 1.3949 -0.0846 -0.1077 0.1473  25  HIS B CG  
2691  N ND1 . HIS B  25  ? 1.4448 1.4500 1.3273 -0.0885 -0.1093 0.1446  25  HIS B ND1 
2692  C CD2 . HIS B  25  ? 1.4063 1.4160 1.3073 -0.0848 -0.1132 0.1564  25  HIS B CD2 
2693  C CE1 . HIS B  25  ? 1.4805 1.4894 1.3593 -0.0911 -0.1155 0.1517  25  HIS B CE1 
2694  N NE2 . HIS B  25  ? 1.5194 1.5314 1.4093 -0.0890 -0.1182 0.1590  25  HIS B NE2 
2695  N N   . HIS B  26  ? 1.6608 1.6557 1.5727 -0.0804 -0.0928 0.1554  26  HIS B N   
2696  C CA  . HIS B  26  ? 1.5978 1.5905 1.5045 -0.0823 -0.0914 0.1588  26  HIS B CA  
2697  C C   . HIS B  26  ? 1.6948 1.6918 1.5923 -0.0859 -0.0990 0.1641  26  HIS B C   
2698  O O   . HIS B  26  ? 1.6911 1.6928 1.5895 -0.0864 -0.1051 0.1674  26  HIS B O   
2699  C CB  . HIS B  26  ? 1.5922 1.5823 1.5116 -0.0795 -0.0871 0.1664  26  HIS B CB  
2700  C CG  . HIS B  26  ? 1.6603 1.6545 1.5874 -0.0786 -0.0922 0.1778  26  HIS B CG  
2701  N ND1 . HIS B  26  ? 1.6506 1.6475 1.5882 -0.0760 -0.0942 0.1807  26  HIS B ND1 
2702  C CD2 . HIS B  26  ? 1.8449 1.8410 1.7710 -0.0801 -0.0958 0.1873  26  HIS B CD2 
2703  C CE1 . HIS B  26  ? 1.7928 1.7935 1.7358 -0.0759 -0.0988 0.1915  26  HIS B CE1 
2704  N NE2 . HIS B  26  ? 1.8960 1.8964 1.8321 -0.0783 -0.1000 0.1957  26  HIS B NE2 
2705  N N   . GLN B  27  ? 2.0654 2.0607 1.9536 -0.0887 -0.0985 0.1648  27  GLN B N   
2706  C CA  . GLN B  27  ? 2.1071 2.1061 1.9850 -0.0927 -0.1054 0.1691  27  GLN B CA  
2707  C C   . GLN B  27  ? 2.1002 2.0970 1.9747 -0.0943 -0.1038 0.1747  27  GLN B C   
2708  O O   . GLN B  27  ? 2.0663 2.0622 1.9281 -0.0978 -0.1044 0.1715  27  GLN B O   
2709  C CB  . GLN B  27  ? 2.1373 2.1371 2.0015 -0.0960 -0.1076 0.1600  27  GLN B CB  
2710  C CG  . GLN B  27  ? 2.1686 2.1716 2.0202 -0.1007 -0.1140 0.1629  27  GLN B CG  
2711  C CD  . GLN B  27  ? 2.2385 2.2475 2.0938 -0.1013 -0.1214 0.1713  27  GLN B CD  
2712  O OE1 . GLN B  27  ? 2.2061 2.2184 2.0575 -0.1028 -0.1260 0.1685  27  GLN B OE1 
2713  N NE2 . GLN B  27  ? 2.3018 2.3120 2.1650 -0.1002 -0.1224 0.1817  27  GLN B NE2 
2714  N N   . ASN B  28  ? 2.0874 2.0832 1.9733 -0.0916 -0.1015 0.1829  28  ASN B N   
2715  C CA  . ASN B  28  ? 2.1005 2.0936 1.9845 -0.0926 -0.0991 0.1884  28  ASN B CA  
2716  C C   . ASN B  28  ? 2.1438 2.1417 2.0273 -0.0943 -0.1057 0.1998  28  ASN B C   
2717  O O   . ASN B  28  ? 2.1362 2.1396 2.0179 -0.0957 -0.1126 0.2024  28  ASN B O   
2718  C CB  . ASN B  28  ? 1.8953 1.8832 1.7910 -0.0889 -0.0909 0.1892  28  ASN B CB  
2719  C CG  . ASN B  28  ? 1.8715 1.8609 1.7830 -0.0852 -0.0911 0.1985  28  ASN B CG  
2720  O OD1 . ASN B  28  ? 1.7911 1.7764 1.7127 -0.0823 -0.0847 0.2010  28  ASN B OD1 
2721  N ND2 . ASN B  28  ? 1.9153 1.9106 1.8294 -0.0853 -0.0981 0.2037  28  ASN B ND2 
2722  N N   . GLU B  29  ? 1.9704 1.9662 1.8552 -0.0944 -0.1036 0.2067  29  GLU B N   
2723  C CA  . GLU B  29  ? 1.9929 1.9932 1.8752 -0.0966 -0.1098 0.2175  29  GLU B CA  
2724  C C   . GLU B  29  ? 1.9802 1.9844 1.8773 -0.0934 -0.1125 0.2282  29  GLU B C   
2725  O O   . GLU B  29  ? 1.8613 1.8704 1.7581 -0.0950 -0.1185 0.2379  29  GLU B O   
2726  C CB  . GLU B  29  ? 2.1546 2.1511 2.0322 -0.0979 -0.1064 0.2210  29  GLU B CB  
2727  C CG  . GLU B  29  ? 2.1579 2.1496 2.0229 -0.1004 -0.1022 0.2107  29  GLU B CG  
2728  C CD  . GLU B  29  ? 2.3173 2.3036 2.1832 -0.0999 -0.0958 0.2131  29  GLU B CD  
2729  O OE1 . GLU B  29  ? 2.2789 2.2631 2.1581 -0.0963 -0.0916 0.2188  29  GLU B OE1 
2730  O OE2 . GLU B  29  ? 2.2941 2.2781 2.1477 -0.1032 -0.0947 0.2093  29  GLU B OE2 
2731  N N   . GLN B  30  ? 2.1503 2.1525 2.0606 -0.0891 -0.1080 0.2263  30  GLN B N   
2732  C CA  . GLN B  30  ? 2.0080 2.0136 1.9334 -0.0858 -0.1099 0.2358  30  GLN B CA  
2733  C C   . GLN B  30  ? 2.0916 2.1021 2.0195 -0.0854 -0.1149 0.2333  30  GLN B C   
2734  O O   . GLN B  30  ? 2.1132 2.1265 2.0542 -0.0825 -0.1162 0.2396  30  GLN B O   
2735  C CB  . GLN B  30  ? 1.8846 1.8848 1.8246 -0.0811 -0.1014 0.2367  30  GLN B CB  
2736  C CG  . GLN B  30  ? 1.7690 1.7651 1.7101 -0.0809 -0.0967 0.2420  30  GLN B CG  
2737  C CD  . GLN B  30  ? 1.8528 1.8411 1.7942 -0.0796 -0.0873 0.2332  30  GLN B CD  
2738  O OE1 . GLN B  30  ? 1.8080 1.7926 1.7621 -0.0758 -0.0809 0.2332  30  GLN B OE1 
2739  N NE2 . GLN B  30  ? 1.9195 1.9053 1.8468 -0.0828 -0.0863 0.2253  30  GLN B NE2 
2740  N N   . GLY B  31  ? 2.2410 2.2522 2.1565 -0.0884 -0.1175 0.2241  31  GLY B N   
2741  C CA  . GLY B  31  ? 2.1903 2.2060 2.1068 -0.0884 -0.1224 0.2213  31  GLY B CA  
2742  C C   . GLY B  31  ? 2.1123 2.1248 2.0250 -0.0879 -0.1188 0.2085  31  GLY B C   
2743  O O   . GLY B  31  ? 2.0614 2.0685 1.9692 -0.0880 -0.1129 0.2013  31  GLY B O   
2744  N N   . SER B  32  ? 2.0497 2.0657 1.9648 -0.0874 -0.1223 0.2060  32  SER B N   
2745  C CA  . SER B  32  ? 1.9340 1.9477 1.8459 -0.0868 -0.1195 0.1944  32  SER B CA  
2746  C C   . SER B  32  ? 1.8726 1.8867 1.7986 -0.0825 -0.1177 0.1945  32  SER B C   
2747  O O   . SER B  32  ? 1.8984 1.9130 1.8374 -0.0796 -0.1166 0.2026  32  SER B O   
2748  C CB  . SER B  32  ? 1.8462 1.8634 1.7448 -0.0908 -0.1256 0.1894  32  SER B CB  
2749  O OG  . SER B  32  ? 1.9529 1.9700 1.8384 -0.0950 -0.1276 0.1900  32  SER B OG  
2750  N N   . GLY B  33  ? 1.8954 1.9093 1.8191 -0.0822 -0.1173 0.1857  33  GLY B N   
2751  C CA  . GLY B  33  ? 1.8233 1.8377 1.7591 -0.0785 -0.1159 0.1851  33  GLY B CA  
2752  C C   . GLY B  33  ? 1.5746 1.5843 1.5114 -0.0764 -0.1091 0.1747  33  GLY B C   
2753  O O   . GLY B  33  ? 1.4256 1.4312 1.3551 -0.0774 -0.1047 0.1685  33  GLY B O   
2754  N N   . TYR B  34  ? 1.3851 1.3955 1.3308 -0.0736 -0.1083 0.1730  34  TYR B N   
2755  C CA  . TYR B  34  ? 1.1969 1.2033 1.1444 -0.0714 -0.1021 0.1636  34  TYR B CA  
2756  C C   . TYR B  34  ? 1.1825 1.1854 1.1446 -0.0674 -0.0958 0.1666  34  TYR B C   
2757  O O   . TYR B  34  ? 1.1393 1.1442 1.1124 -0.0655 -0.0973 0.1753  34  TYR B O   
2758  C CB  . TYR B  34  ? 1.2152 1.2245 1.1614 -0.0713 -0.1053 0.1583  34  TYR B CB  
2759  C CG  . TYR B  34  ? 1.2211 1.2340 1.1540 -0.0752 -0.1116 0.1556  34  TYR B CG  
2760  C CD1 . TYR B  34  ? 1.0763 1.0944 1.0086 -0.0770 -0.1190 0.1626  34  TYR B CD1 
2761  C CD2 . TYR B  34  ? 1.1801 1.1911 1.1012 -0.0771 -0.1101 0.1462  34  TYR B CD2 
2762  C CE1 . TYR B  34  ? 1.1846 1.2058 1.1045 -0.0809 -0.1246 0.1599  34  TYR B CE1 
2763  C CE2 . TYR B  34  ? 1.0818 1.0957 0.9910 -0.0808 -0.1155 0.1436  34  TYR B CE2 
2764  C CZ  . TYR B  34  ? 1.1177 1.1365 1.0261 -0.0827 -0.1226 0.1503  34  TYR B CZ  
2765  O OH  . TYR B  34  ? 0.9964 1.0178 0.8928 -0.0866 -0.1276 0.1475  34  TYR B OH  
2766  N N   . ALA B  35  ? 1.3259 1.3238 1.2882 -0.0663 -0.0886 0.1593  35  ALA B N   
2767  C CA  . ALA B  35  ? 1.2735 1.2674 1.2488 -0.0628 -0.0817 0.1606  35  ALA B CA  
2768  C C   . ALA B  35  ? 1.3430 1.3337 1.3178 -0.0616 -0.0761 0.1501  35  ALA B C   
2769  O O   . ALA B  35  ? 1.4166 1.4045 1.3829 -0.0631 -0.0728 0.1429  35  ALA B O   
2770  C CB  . ALA B  35  ? 1.3804 1.3706 1.3579 -0.0628 -0.0773 0.1652  35  ALA B CB  
2771  N N   . ALA B  36  ? 1.1663 1.1575 1.1502 -0.0590 -0.0751 0.1494  36  ALA B N   
2772  C CA  . ALA B  36  ? 1.2852 1.2739 1.2690 -0.0578 -0.0702 0.1399  36  ALA B CA  
2773  C C   . ALA B  36  ? 1.2107 1.1936 1.1997 -0.0566 -0.0614 0.1374  36  ALA B C   
2774  O O   . ALA B  36  ? 1.2949 1.2755 1.2939 -0.0549 -0.0583 0.1440  36  ALA B O   
2775  C CB  . ALA B  36  ? 1.3388 1.3297 1.3309 -0.0555 -0.0717 0.1403  36  ALA B CB  
2776  N N   . ASP B  37  ? 1.1981 1.1787 1.1803 -0.0575 -0.0575 0.1277  37  ASP B N   
2777  C CA  . ASP B  37  ? 1.2237 1.1989 1.2097 -0.0568 -0.0490 0.1241  37  ASP B CA  
2778  C C   . ASP B  37  ? 1.2912 1.2643 1.2902 -0.0537 -0.0444 0.1247  37  ASP B C   
2779  O O   . ASP B  37  ? 1.1627 1.1373 1.1627 -0.0527 -0.0451 0.1204  37  ASP B O   
2780  C CB  . ASP B  37  ? 1.0243 0.9984 0.9999 -0.0587 -0.0464 0.1134  37  ASP B CB  
2781  C CG  . ASP B  37  ? 1.2309 1.1997 1.2094 -0.0585 -0.0379 0.1094  37  ASP B CG  
2782  O OD1 . ASP B  37  ? 1.4232 1.3911 1.3946 -0.0599 -0.0351 0.1007  37  ASP B OD1 
2783  O OD2 . ASP B  37  ? 1.4023 1.3679 1.3905 -0.0570 -0.0338 0.1151  37  ASP B OD2 
2784  N N   . LEU B  38  ? 1.3936 1.3629 1.4025 -0.0522 -0.0394 0.1301  38  LEU B N   
2785  C CA  . LEU B  38  ? 1.5669 1.5339 1.5892 -0.0492 -0.0347 0.1319  38  LEU B CA  
2786  C C   . LEU B  38  ? 1.4502 1.4142 1.4723 -0.0489 -0.0284 0.1221  38  LEU B C   
2787  O O   . LEU B  38  ? 1.3276 1.2930 1.3530 -0.0476 -0.0289 0.1194  38  LEU B O   
2788  C CB  . LEU B  38  ? 1.8675 1.8306 1.9000 -0.0479 -0.0301 0.1398  38  LEU B CB  
2789  C CG  . LEU B  38  ? 2.0036 1.9672 2.0508 -0.0448 -0.0300 0.1482  38  LEU B CG  
2790  C CD1 . LEU B  38  ? 1.9885 1.9481 2.0452 -0.0436 -0.0251 0.1558  38  LEU B CD1 
2791  C CD2 . LEU B  38  ? 1.9898 1.9518 2.0437 -0.0429 -0.0260 0.1430  38  LEU B CD2 
2792  N N   . LYS B  39  ? 1.7318 1.6918 1.7498 -0.0504 -0.0226 0.1168  39  LYS B N   
2793  C CA  . LYS B  39  ? 1.7659 1.7230 1.7842 -0.0504 -0.0161 0.1077  39  LYS B CA  
2794  C C   . LYS B  39  ? 1.7327 1.6934 1.7420 -0.0514 -0.0195 0.0996  39  LYS B C   
2795  O O   . LYS B  39  ? 1.6395 1.5997 1.6520 -0.0504 -0.0165 0.0946  39  LYS B O   
2796  C CB  . LYS B  39  ? 1.9043 1.8569 1.9193 -0.0523 -0.0096 0.1038  39  LYS B CB  
2797  C CG  . LYS B  39  ? 2.1275 2.0768 2.1437 -0.0526 -0.0022 0.0950  39  LYS B CG  
2798  C CD  . LYS B  39  ? 2.2959 2.2406 2.3104 -0.0544 0.0045  0.0921  39  LYS B CD  
2799  C CE  . LYS B  39  ? 2.3243 2.2658 2.3406 -0.0549 0.0121  0.0836  39  LYS B CE  
2800  N NZ  . LYS B  39  ? 2.2403 2.1770 2.2558 -0.0568 0.0191  0.0809  39  LYS B NZ  
2801  N N   . SER B  40  ? 1.3793 1.3438 1.3776 -0.0533 -0.0255 0.0984  40  SER B N   
2802  C CA  . SER B  40  ? 1.2148 1.1827 1.2041 -0.0543 -0.0286 0.0907  40  SER B CA  
2803  C C   . SER B  40  ? 1.0760 1.0471 1.0695 -0.0523 -0.0328 0.0923  40  SER B C   
2804  O O   . SER B  40  ? 1.0816 1.0531 1.0753 -0.0516 -0.0310 0.0862  40  SER B O   
2805  C CB  . SER B  40  ? 1.1812 1.1519 1.1580 -0.0568 -0.0339 0.0896  40  SER B CB  
2806  O OG  . SER B  40  ? 1.2835 1.2570 1.2517 -0.0578 -0.0357 0.0816  40  SER B OG  
2807  N N   . THR B  41  ? 1.1140 1.0877 1.1108 -0.0516 -0.0384 0.1004  41  THR B N   
2808  C CA  . THR B  41  ? 1.0877 1.0648 1.0887 -0.0499 -0.0428 0.1025  41  THR B CA  
2809  C C   . THR B  41  ? 1.1273 1.1017 1.1400 -0.0473 -0.0375 0.1023  41  THR B C   
2810  O O   . THR B  41  ? 0.9914 0.9675 1.0052 -0.0462 -0.0385 0.0991  41  THR B O   
2811  C CB  . THR B  41  ? 0.9157 0.8958 0.9195 -0.0497 -0.0493 0.1122  41  THR B CB  
2812  O OG1 . THR B  41  ? 1.1035 1.0864 1.0956 -0.0524 -0.0548 0.1119  41  THR B OG1 
2813  C CG2 . THR B  41  ? 0.9601 0.9436 0.9696 -0.0479 -0.0533 0.1145  41  THR B CG2 
2814  N N   . GLN B  42  ? 1.2545 1.2245 1.2756 -0.0464 -0.0315 0.1056  42  GLN B N   
2815  C CA  . GLN B  42  ? 1.2896 1.2564 1.3223 -0.0440 -0.0257 0.1057  42  GLN B CA  
2816  C C   . GLN B  42  ? 1.1763 1.1417 1.2055 -0.0444 -0.0210 0.0956  42  GLN B C   
2817  O O   . GLN B  42  ? 1.1199 1.0856 1.1540 -0.0428 -0.0201 0.0938  42  GLN B O   
2818  C CB  . GLN B  42  ? 1.3278 1.2898 1.3698 -0.0432 -0.0197 0.1110  42  GLN B CB  
2819  C CG  . GLN B  42  ? 1.4132 1.3717 1.4683 -0.0407 -0.0136 0.1123  42  GLN B CG  
2820  C CD  . GLN B  42  ? 1.5078 1.4697 1.5705 -0.0384 -0.0183 0.1179  42  GLN B CD  
2821  O OE1 . GLN B  42  ? 1.5560 1.5221 1.6176 -0.0384 -0.0255 0.1242  42  GLN B OE1 
2822  N NE2 . GLN B  42  ? 1.5052 1.4653 1.5757 -0.0366 -0.0142 0.1157  42  GLN B NE2 
2823  N N   . ASN B  43  ? 1.0612 1.0250 1.0819 -0.0466 -0.0181 0.0893  43  ASN B N   
2824  C CA  . ASN B  43  ? 1.1059 1.0689 1.1224 -0.0474 -0.0139 0.0796  43  ASN B CA  
2825  C C   . ASN B  43  ? 1.0932 1.0609 1.1036 -0.0473 -0.0191 0.0753  43  ASN B C   
2826  O O   . ASN B  43  ? 0.9878 0.9553 1.0005 -0.0464 -0.0165 0.0708  43  ASN B O   
2827  C CB  . ASN B  43  ? 1.1056 1.0669 1.1137 -0.0501 -0.0106 0.0740  43  ASN B CB  
2828  C CG  . ASN B  43  ? 1.2720 1.2277 1.2867 -0.0503 -0.0019 0.0730  43  ASN B CG  
2829  O OD1 . ASN B  43  ? 1.3945 1.3470 1.4170 -0.0493 0.0004  0.0797  43  ASN B OD1 
2830  N ND2 . ASN B  43  ? 1.3126 1.2670 1.3241 -0.0515 0.0032  0.0645  43  ASN B ND2 
2831  N N   . ALA B  44  ? 1.0406 1.0123 1.0431 -0.0483 -0.0261 0.0767  44  ALA B N   
2832  C CA  . ALA B  44  ? 0.8658 0.8420 0.8622 -0.0483 -0.0313 0.0731  44  ALA B CA  
2833  C C   . ALA B  44  ? 0.8585 0.8356 0.8637 -0.0457 -0.0323 0.0760  44  ALA B C   
2834  O O   . ALA B  44  ? 0.9431 0.9212 0.9475 -0.0451 -0.0316 0.0707  44  ALA B O   
2835  C CB  . ALA B  44  ? 0.7975 0.7773 0.7855 -0.0498 -0.0385 0.0756  44  ALA B CB  
2836  N N   . ILE B  45  ? 0.8521 0.8289 0.8660 -0.0443 -0.0341 0.0845  45  ILE B N   
2837  C CA  . ILE B  45  ? 0.9411 0.9186 0.9645 -0.0419 -0.0350 0.0881  45  ILE B CA  
2838  C C   . ILE B  45  ? 0.9020 0.8760 0.9317 -0.0406 -0.0278 0.0837  45  ILE B C   
2839  O O   . ILE B  45  ? 0.8886 0.8639 0.9196 -0.0394 -0.0282 0.0808  45  ILE B O   
2840  C CB  . ILE B  45  ? 0.9708 0.9481 1.0039 -0.0405 -0.0369 0.0985  45  ILE B CB  
2841  C CG1 . ILE B  45  ? 0.9309 0.9128 0.9581 -0.0417 -0.0453 0.1032  45  ILE B CG1 
2842  C CG2 . ILE B  45  ? 0.9260 0.9029 0.9711 -0.0378 -0.0355 0.1018  45  ILE B CG2 
2843  C CD1 . ILE B  45  ? 1.0319 1.0148 1.0684 -0.0405 -0.0481 0.1138  45  ILE B CD1 
2844  N N   . ASP B  46  ? 0.9692 0.9386 1.0027 -0.0409 -0.0209 0.0830  46  ASP B N   
2845  C CA  . ASP B  46  ? 0.9500 0.9155 0.9891 -0.0401 -0.0134 0.0785  46  ASP B CA  
2846  C C   . ASP B  46  ? 0.9113 0.8785 0.9419 -0.0412 -0.0127 0.0690  46  ASP B C   
2847  O O   . ASP B  46  ? 0.8932 0.8601 0.9274 -0.0401 -0.0106 0.0662  46  ASP B O   
2848  C CB  . ASP B  46  ? 1.0185 0.9788 1.0611 -0.0410 -0.0061 0.0786  46  ASP B CB  
2849  C CG  . ASP B  46  ? 1.2739 1.2317 1.3281 -0.0392 -0.0049 0.0880  46  ASP B CG  
2850  O OD1 . ASP B  46  ? 1.2433 1.2030 1.3046 -0.0371 -0.0084 0.0939  46  ASP B OD1 
2851  O OD2 . ASP B  46  ? 1.4120 1.3660 1.4684 -0.0399 -0.0003 0.0897  46  ASP B OD2 
2852  N N   . GLU B  47  ? 0.9112 0.8801 0.9306 -0.0435 -0.0144 0.0643  47  GLU B N   
2853  C CA  . GLU B  47  ? 0.7495 0.7202 0.7607 -0.0447 -0.0135 0.0554  47  GLU B CA  
2854  C C   . GLU B  47  ? 0.7831 0.7585 0.7907 -0.0437 -0.0195 0.0543  47  GLU B C   
2855  O O   . GLU B  47  ? 0.7548 0.7310 0.7610 -0.0434 -0.0178 0.0488  47  GLU B O   
2856  C CB  . GLU B  47  ? 0.6878 0.6591 0.6888 -0.0473 -0.0133 0.0509  47  GLU B CB  
2857  C CG  . GLU B  47  ? 0.8741 0.8407 0.8780 -0.0486 -0.0064 0.0502  47  GLU B CG  
2858  C CD  . GLU B  47  ? 1.0624 1.0297 1.0562 -0.0513 -0.0056 0.0446  47  GLU B CD  
2859  O OE1 . GLU B  47  ? 0.9488 0.9201 0.9338 -0.0522 -0.0111 0.0431  47  GLU B OE1 
2860  O OE2 . GLU B  47  ? 1.1633 1.1270 1.1581 -0.0527 0.0008  0.0417  47  GLU B OE2 
2861  N N   . ILE B  48  ? 0.6307 0.6090 0.6368 -0.0434 -0.0263 0.0595  48  ILE B N   
2862  C CA  . ILE B  48  ? 0.6392 0.6217 0.6429 -0.0425 -0.0320 0.0592  48  ILE B CA  
2863  C C   . ILE B  48  ? 0.7228 0.7044 0.7366 -0.0400 -0.0304 0.0615  48  ILE B C   
2864  O O   . ILE B  48  ? 0.7266 0.7101 0.7390 -0.0392 -0.0314 0.0579  48  ILE B O   
2865  C CB  . ILE B  48  ? 0.7623 0.7479 0.7625 -0.0430 -0.0394 0.0647  48  ILE B CB  
2866  C CG1 . ILE B  48  ? 0.7638 0.7509 0.7523 -0.0455 -0.0414 0.0611  48  ILE B CG1 
2867  C CG2 . ILE B  48  ? 0.5714 0.5606 0.5716 -0.0418 -0.0447 0.0654  48  ILE B CG2 
2868  C CD1 . ILE B  48  ? 0.7246 0.7138 0.7046 -0.0462 -0.0412 0.0527  48  ILE B CD1 
2869  N N   . THR B  49  ? 0.7565 0.7349 0.7806 -0.0388 -0.0277 0.0676  49  THR B N   
2870  C CA  . THR B  49  ? 0.7820 0.7589 0.8169 -0.0364 -0.0252 0.0700  49  THR B CA  
2871  C C   . THR B  49  ? 0.8359 0.8106 0.8704 -0.0364 -0.0190 0.0625  49  THR B C   
2872  O O   . THR B  49  ? 0.7965 0.7725 0.8327 -0.0352 -0.0193 0.0604  49  THR B O   
2873  C CB  . THR B  49  ? 0.7685 0.7418 0.8149 -0.0352 -0.0220 0.0774  49  THR B CB  
2874  O OG1 . THR B  49  ? 0.9361 0.9121 0.9839 -0.0350 -0.0284 0.0852  49  THR B OG1 
2875  C CG2 . THR B  49  ? 0.5937 0.5648 0.6515 -0.0329 -0.0180 0.0788  49  THR B CG2 
2876  N N   . ASN B  50  ? 0.7032 0.6749 0.7356 -0.0380 -0.0132 0.0584  50  ASN B N   
2877  C CA  . ASN B  50  ? 0.7683 0.7381 0.7994 -0.0386 -0.0072 0.0510  50  ASN B CA  
2878  C C   . ASN B  50  ? 0.7775 0.7516 0.7995 -0.0391 -0.0105 0.0448  50  ASN B C   
2879  O O   . ASN B  50  ? 0.7919 0.7658 0.8149 -0.0386 -0.0078 0.0406  50  ASN B O   
2880  C CB  . ASN B  50  ? 0.7587 0.7252 0.7869 -0.0409 -0.0015 0.0474  50  ASN B CB  
2881  C CG  . ASN B  50  ? 0.8054 0.7692 0.8343 -0.0417 0.0057  0.0405  50  ASN B CG  
2882  O OD1 . ASN B  50  ? 0.8677 0.8271 0.9055 -0.0410 0.0118  0.0419  50  ASN B OD1 
2883  N ND2 . ASN B  50  ? 0.7243 0.6910 0.7438 -0.0432 0.0053  0.0332  50  ASN B ND2 
2884  N N   . LYS B  51  ? 0.7578 0.7356 0.7709 -0.0402 -0.0162 0.0443  51  LYS B N   
2885  C CA  . LYS B  51  ? 0.6954 0.6775 0.6998 -0.0406 -0.0198 0.0390  51  LYS B CA  
2886  C C   . LYS B  51  ? 0.6983 0.6822 0.7067 -0.0384 -0.0227 0.0407  51  LYS B C   
2887  O O   . LYS B  51  ? 0.6018 0.5868 0.6084 -0.0380 -0.0213 0.0357  51  LYS B O   
2888  C CB  . LYS B  51  ? 0.7305 0.7157 0.7258 -0.0420 -0.0256 0.0394  51  LYS B CB  
2889  C CG  . LYS B  51  ? 0.6288 0.6184 0.6151 -0.0423 -0.0293 0.0342  51  LYS B CG  
2890  C CD  . LYS B  51  ? 0.7231 0.7150 0.7002 -0.0442 -0.0332 0.0335  51  LYS B CD  
2891  C CE  . LYS B  51  ? 0.7631 0.7591 0.7314 -0.0446 -0.0359 0.0280  51  LYS B CE  
2892  N NZ  . LYS B  51  ? 0.8097 0.8071 0.7688 -0.0468 -0.0375 0.0254  51  LYS B NZ  
2893  N N   . VAL B  52  ? 0.6451 0.6295 0.6593 -0.0370 -0.0268 0.0478  52  VAL B N   
2894  C CA  . VAL B  52  ? 0.5973 0.5834 0.6160 -0.0350 -0.0298 0.0502  52  VAL B CA  
2895  C C   . VAL B  52  ? 0.7009 0.6840 0.7281 -0.0334 -0.0240 0.0491  52  VAL B C   
2896  O O   . VAL B  52  ? 0.7369 0.7214 0.7644 -0.0323 -0.0244 0.0467  52  VAL B O   
2897  C CB  . VAL B  52  ? 0.5146 0.5019 0.5388 -0.0340 -0.0350 0.0586  52  VAL B CB  
2898  C CG1 . VAL B  52  ? 0.4844 0.4738 0.5129 -0.0321 -0.0384 0.0606  52  VAL B CG1 
2899  C CG2 . VAL B  52  ? 0.5740 0.5640 0.5895 -0.0359 -0.0405 0.0597  52  VAL B CG2 
2900  N N   . ASN B  53  ? 0.6475 0.6262 0.6817 -0.0335 -0.0183 0.0510  53  ASN B N   
2901  C CA  . ASN B  53  ? 0.7805 0.7556 0.8229 -0.0323 -0.0120 0.0499  53  ASN B CA  
2902  C C   . ASN B  53  ? 0.8383 0.8135 0.8746 -0.0333 -0.0081 0.0414  53  ASN B C   
2903  O O   . ASN B  53  ? 0.8758 0.8502 0.9160 -0.0322 -0.0055 0.0396  53  ASN B O   
2904  C CB  . ASN B  53  ? 0.8396 0.8096 0.8900 -0.0324 -0.0061 0.0532  53  ASN B CB  
2905  C CG  . ASN B  53  ? 0.9162 0.8856 0.9770 -0.0305 -0.0084 0.0624  53  ASN B CG  
2906  O OD1 . ASN B  53  ? 0.7222 0.6948 0.7848 -0.0291 -0.0140 0.0661  53  ASN B OD1 
2907  N ND2 . ASN B  53  ? 0.8766 0.8419 0.9446 -0.0304 -0.0039 0.0662  53  ASN B ND2 
2908  N N   . SER B  54  ? 0.7357 0.7121 0.7625 -0.0356 -0.0077 0.0362  54  SER B N   
2909  C CA  . SER B  54  ? 0.6433 0.6205 0.6638 -0.0369 -0.0044 0.0282  54  SER B CA  
2910  C C   . SER B  54  ? 0.7113 0.6926 0.7278 -0.0358 -0.0084 0.0258  54  SER B C   
2911  O O   . SER B  54  ? 0.7960 0.7768 0.8140 -0.0352 -0.0052 0.0225  54  SER B O   
2912  C CB  . SER B  54  ? 0.6500 0.6283 0.6613 -0.0395 -0.0039 0.0237  54  SER B CB  
2913  O OG  . SER B  54  ? 0.7623 0.7364 0.7773 -0.0407 0.0008  0.0251  54  SER B OG  
2914  N N   . VAL B  55  ? 0.6317 0.6169 0.6429 -0.0355 -0.0153 0.0276  55  VAL B N   
2915  C CA  . VAL B  55  ? 0.5997 0.5888 0.6071 -0.0344 -0.0195 0.0257  55  VAL B CA  
2916  C C   . VAL B  55  ? 0.7097 0.6976 0.7257 -0.0321 -0.0186 0.0284  55  VAL B C   
2917  O O   . VAL B  55  ? 0.6304 0.6201 0.6445 -0.0313 -0.0189 0.0253  55  VAL B O   
2918  C CB  . VAL B  55  ? 0.5478 0.5405 0.5501 -0.0344 -0.0269 0.0286  55  VAL B CB  
2919  C CG1 . VAL B  55  ? 0.6613 0.6575 0.6609 -0.0331 -0.0309 0.0273  55  VAL B CG1 
2920  C CG2 . VAL B  55  ? 0.5004 0.4946 0.4935 -0.0367 -0.0277 0.0253  55  VAL B CG2 
2921  N N   . ILE B  56  ? 0.6434 0.6281 0.6691 -0.0310 -0.0173 0.0343  56  ILE B N   
2922  C CA  . ILE B  56  ? 0.6318 0.6152 0.6668 -0.0288 -0.0164 0.0376  56  ILE B CA  
2923  C C   . ILE B  56  ? 0.7012 0.6803 0.7416 -0.0287 -0.0085 0.0348  56  ILE B C   
2924  O O   . ILE B  56  ? 0.6520 0.6311 0.6940 -0.0277 -0.0068 0.0325  56  ILE B O   
2925  C CB  . ILE B  56  ? 0.7131 0.6956 0.7569 -0.0275 -0.0192 0.0460  56  ILE B CB  
2926  C CG1 . ILE B  56  ? 0.7105 0.6974 0.7493 -0.0276 -0.0273 0.0490  56  ILE B CG1 
2927  C CG2 . ILE B  56  ? 0.6807 0.6612 0.7355 -0.0252 -0.0171 0.0494  56  ILE B CG2 
2928  C CD1 . ILE B  56  ? 0.6720 0.6589 0.7185 -0.0267 -0.0307 0.0574  56  ILE B CD1 
2929  N N   . GLU B  57  ? 0.6437 0.6191 0.6869 -0.0300 -0.0035 0.0349  57  GLU B N   
2930  C CA  . GLU B  57  ? 0.6700 0.6406 0.7195 -0.0301 0.0045  0.0330  57  GLU B CA  
2931  C C   . GLU B  57  ? 0.6754 0.6466 0.7182 -0.0315 0.0082  0.0249  57  GLU B C   
2932  O O   . GLU B  57  ? 0.7523 0.7205 0.7998 -0.0312 0.0137  0.0230  57  GLU B O   
2933  C CB  . GLU B  57  ? 0.8694 0.8359 0.9224 -0.0314 0.0091  0.0346  57  GLU B CB  
2934  C CG  . GLU B  57  ? 1.3357 1.2964 1.3984 -0.0310 0.0172  0.0350  57  GLU B CG  
2935  C CD  . GLU B  57  ? 1.4566 1.4148 1.5145 -0.0336 0.0241  0.0275  57  GLU B CD  
2936  O OE1 . GLU B  57  ? 1.2994 1.2596 1.3484 -0.0358 0.0232  0.0235  57  GLU B OE1 
2937  O OE2 . GLU B  57  ? 1.2979 1.2523 1.3612 -0.0336 0.0306  0.0255  57  GLU B OE2 
2938  N N   . LYS B  58  ? 0.6670 0.6421 0.6989 -0.0330 0.0051  0.0203  58  LYS B N   
2939  C CA  . LYS B  58  ? 0.6354 0.6120 0.6603 -0.0345 0.0080  0.0128  58  LYS B CA  
2940  C C   . LYS B  58  ? 0.6742 0.6534 0.6985 -0.0329 0.0060  0.0115  58  LYS B C   
2941  O O   . LYS B  58  ? 0.7022 0.6830 0.7209 -0.0339 0.0080  0.0058  58  LYS B O   
2942  C CB  . LYS B  58  ? 0.6181 0.5984 0.6321 -0.0367 0.0055  0.0085  58  LYS B CB  
2943  C CG  . LYS B  58  ? 0.7363 0.7139 0.7498 -0.0388 0.0089  0.0081  58  LYS B CG  
2944  C CD  . LYS B  58  ? 0.7526 0.7256 0.7702 -0.0403 0.0173  0.0049  58  LYS B CD  
2945  C CE  . LYS B  58  ? 0.7878 0.7578 0.8053 -0.0424 0.0210  0.0045  58  LYS B CE  
2946  N NZ  . LYS B  58  ? 0.7927 0.7578 0.8141 -0.0441 0.0296  0.0011  58  LYS B NZ  
2947  N N   . MET B  59  ? 0.6061 0.5857 0.6362 -0.0304 0.0020  0.0171  59  MET B N   
2948  C CA  . MET B  59  ? 0.5855 0.5672 0.6161 -0.0286 0.0001  0.0165  59  MET B CA  
2949  C C   . MET B  59  ? 0.7839 0.7613 0.8242 -0.0274 0.0054  0.0180  59  MET B C   
2950  O O   . MET B  59  ? 0.9431 0.9191 0.9921 -0.0254 0.0039  0.0239  59  MET B O   
2951  C CB  . MET B  59  ? 0.7725 0.7576 0.8031 -0.0269 -0.0075 0.0212  59  MET B CB  
2952  C CG  . MET B  59  ? 0.7468 0.7345 0.7759 -0.0253 -0.0101 0.0199  59  MET B CG  
2953  S SD  . MET B  59  ? 0.8598 0.8517 0.8767 -0.0267 -0.0102 0.0121  59  MET B SD  
2954  C CE  . MET B  59  ? 0.6093 0.6063 0.6194 -0.0262 -0.0187 0.0137  59  MET B CE  
2955  N N   . ASN B  60  ? 0.7380 0.7134 0.7768 -0.0287 0.0116  0.0127  60  ASN B N   
2956  C CA  . ASN B  60  ? 0.9167 0.8880 0.9638 -0.0278 0.0171  0.0132  60  ASN B CA  
2957  C C   . ASN B  60  ? 0.8276 0.8013 0.8709 -0.0272 0.0168  0.0094  60  ASN B C   
2958  O O   . ASN B  60  ? 0.9151 0.8896 0.9517 -0.0291 0.0200  0.0033  60  ASN B O   
2959  C CB  . ASN B  60  ? 1.0888 1.0550 1.1387 -0.0298 0.0252  0.0106  60  ASN B CB  
2960  C CG  . ASN B  60  ? 1.4502 1.4176 1.4910 -0.0326 0.0288  0.0026  60  ASN B CG  
2961  O OD1 . ASN B  60  ? 1.4840 1.4502 1.5250 -0.0330 0.0330  -0.0008 60  ASN B OD1 
2962  N ND2 . ASN B  60  ? 1.3132 1.2832 1.3458 -0.0347 0.0271  -0.0003 60  ASN B ND2 
2963  N N   . THR B  61  ? 0.7692 0.7442 0.8167 -0.0246 0.0129  0.0133  61  THR B N   
2964  C CA  . THR B  61  ? 0.8152 0.7929 0.8590 -0.0237 0.0117  0.0104  61  THR B CA  
2965  C C   . THR B  61  ? 0.8253 0.7991 0.8747 -0.0234 0.0183  0.0089  61  THR B C   
2966  O O   . THR B  61  ? 0.6997 0.6686 0.7583 -0.0230 0.0227  0.0117  61  THR B O   
2967  C CB  . THR B  61  ? 0.8761 0.8569 0.9215 -0.0212 0.0047  0.0149  61  THR B CB  
2968  O OG1 . THR B  61  ? 1.0441 1.0219 1.1009 -0.0194 0.0049  0.0212  61  THR B OG1 
2969  C CG2 . THR B  61  ? 0.6545 0.6395 0.6930 -0.0218 -0.0017 0.0156  61  THR B CG2 
2970  N N   . GLN B  62  ? 0.8380 0.8139 0.8817 -0.0237 0.0190  0.0044  62  GLN B N   
2971  C CA  . GLN B  62  ? 0.8677 0.8402 0.9154 -0.0235 0.0248  0.0026  62  GLN B CA  
2972  C C   . GLN B  62  ? 0.8500 0.8219 0.9060 -0.0204 0.0227  0.0076  62  GLN B C   
2973  O O   . GLN B  62  ? 0.6905 0.6659 0.7461 -0.0187 0.0160  0.0109  62  GLN B O   
2974  C CB  . GLN B  62  ? 0.7772 0.7528 0.8153 -0.0249 0.0260  -0.0038 62  GLN B CB  
2975  C CG  . GLN B  62  ? 0.5878 0.5643 0.6180 -0.0283 0.0289  -0.0093 62  GLN B CG  
2976  C CD  . GLN B  62  ? 0.8921 0.8627 0.9271 -0.0303 0.0370  -0.0110 62  GLN B CD  
2977  O OE1 . GLN B  62  ? 1.0410 1.0081 1.0822 -0.0303 0.0385  -0.0078 62  GLN B OE1 
2978  N NE2 . GLN B  62  ? 0.8500 0.8195 0.8820 -0.0321 0.0424  -0.0160 62  GLN B NE2 
2979  N N   . PHE B  63  ? 0.8437 0.8111 0.9074 -0.0198 0.0284  0.0080  63  PHE B N   
2980  C CA  . PHE B  63  ? 0.7381 0.7049 0.8093 -0.0170 0.0270  0.0121  63  PHE B CA  
2981  C C   . PHE B  63  ? 0.6448 0.6150 0.7092 -0.0166 0.0253  0.0085  63  PHE B C   
2982  O O   . PHE B  63  ? 0.8687 0.8374 0.9304 -0.0178 0.0305  0.0040  63  PHE B O   
2983  C CB  . PHE B  63  ? 0.7573 0.7180 0.8396 -0.0165 0.0341  0.0139  63  PHE B CB  
2984  C CG  . PHE B  63  ? 0.8215 0.7815 0.9128 -0.0136 0.0326  0.0186  63  PHE B CG  
2985  C CD1 . PHE B  63  ? 0.7012 0.6599 0.8033 -0.0117 0.0307  0.0256  63  PHE B CD1 
2986  C CD2 . PHE B  63  ? 0.7574 0.7184 0.8466 -0.0128 0.0330  0.0164  63  PHE B CD2 
2987  C CE1 . PHE B  63  ? 0.7802 0.7387 0.8909 -0.0091 0.0292  0.0300  63  PHE B CE1 
2988  C CE2 . PHE B  63  ? 0.7930 0.7534 0.8907 -0.0101 0.0317  0.0207  63  PHE B CE2 
2989  C CZ  . PHE B  63  ? 0.7556 0.7148 0.8641 -0.0084 0.0298  0.0274  63  PHE B CZ  
2990  N N   . THR B  64  ? 0.5726 0.5473 0.6339 -0.0150 0.0182  0.0105  64  THR B N   
2991  C CA  . THR B  64  ? 0.8846 0.8628 0.9396 -0.0143 0.0162  0.0077  64  THR B CA  
2992  C C   . THR B  64  ? 0.5866 0.5664 0.6466 -0.0115 0.0112  0.0123  64  THR B C   
2993  O O   . THR B  64  ? 0.3970 0.3775 0.4614 -0.0105 0.0067  0.0171  64  THR B O   
2994  C CB  . THR B  64  ? 0.8920 0.8753 0.9348 -0.0158 0.0126  0.0036  64  THR B CB  
2995  O OG1 . THR B  64  ? 0.7013 0.6865 0.7433 -0.0159 0.0075  0.0064  64  THR B OG1 
2996  C CG2 . THR B  64  ? 0.8273 0.8099 0.8639 -0.0187 0.0180  -0.0022 64  THR B CG2 
2997  N N   . ALA B  65  ? 0.5916 0.5720 0.6508 -0.0104 0.0120  0.0108  65  ALA B N   
2998  C CA  . ALA B  65  ? 0.5593 0.5416 0.6221 -0.0079 0.0072  0.0145  65  ALA B CA  
2999  C C   . ALA B  65  ? 0.5913 0.5787 0.6440 -0.0077 0.0027  0.0117  65  ALA B C   
3000  O O   . ALA B  65  ? 0.5762 0.5644 0.6253 -0.0073 0.0044  0.0088  65  ALA B O   
3001  C CB  . ALA B  65  ? 0.5725 0.5513 0.6430 -0.0064 0.0114  0.0156  65  ALA B CB  
3002  N N   . VAL B  66  ? 0.4686 0.4594 0.5169 -0.0080 -0.0029 0.0127  66  VAL B N   
3003  C CA  . VAL B  66  ? 0.4923 0.4879 0.5321 -0.0076 -0.0076 0.0108  66  VAL B CA  
3004  C C   . VAL B  66  ? 0.6457 0.6416 0.6891 -0.0053 -0.0089 0.0125  66  VAL B C   
3005  O O   . VAL B  66  ? 0.9245 0.9174 0.9773 -0.0040 -0.0077 0.0162  66  VAL B O   
3006  C CB  . VAL B  66  ? 0.4199 0.4183 0.4570 -0.0079 -0.0138 0.0130  66  VAL B CB  
3007  C CG1 . VAL B  66  ? 0.4239 0.4271 0.4509 -0.0080 -0.0174 0.0099  66  VAL B CG1 
3008  C CG2 . VAL B  66  ? 0.5035 0.5002 0.5411 -0.0098 -0.0125 0.0134  66  VAL B CG2 
3009  N N   . GLY B  67  ? 0.5495 0.5489 0.5857 -0.0047 -0.0109 0.0100  67  GLY B N   
3010  C CA  . GLY B  67  ? 0.7270 0.7269 0.7659 -0.0025 -0.0124 0.0116  67  GLY B CA  
3011  C C   . GLY B  67  ? 0.6491 0.6467 0.6898 -0.0020 -0.0069 0.0096  67  GLY B C   
3012  O O   . GLY B  67  ? 0.4258 0.4193 0.4728 -0.0024 -0.0022 0.0102  67  GLY B O   
3013  N N   . LYS B  68  ? 0.6629 0.6631 0.6981 -0.0011 -0.0074 0.0074  68  LYS B N   
3014  C CA  . LYS B  68  ? 0.4057 0.4042 0.4412 -0.0007 -0.0026 0.0053  68  LYS B CA  
3015  C C   . LYS B  68  ? 0.5915 0.5912 0.6283 0.0017  -0.0049 0.0069  68  LYS B C   
3016  O O   . LYS B  68  ? 0.5946 0.5969 0.6306 0.0027  -0.0102 0.0088  68  LYS B O   
3017  C CB  . LYS B  68  ? 0.6833 0.6842 0.7091 -0.0024 0.0000  0.0002  68  LYS B CB  
3018  C CG  . LYS B  68  ? 0.6295 0.6293 0.6533 -0.0051 0.0024  -0.0019 68  LYS B CG  
3019  C CD  . LYS B  68  ? 0.7145 0.7098 0.7421 -0.0063 0.0094  -0.0035 68  LYS B CD  
3020  C CE  . LYS B  68  ? 0.8335 0.8265 0.8622 -0.0086 0.0119  -0.0043 68  LYS B CE  
3021  N NZ  . LYS B  68  ? 0.7823 0.7717 0.8211 -0.0077 0.0112  0.0005  68  LYS B NZ  
3022  N N   . GLU B  69  ? 0.6108 0.6086 0.6497 0.0025  -0.0007 0.0060  69  GLU B N   
3023  C CA  . GLU B  69  ? 0.4834 0.4819 0.5240 0.0048  -0.0023 0.0075  69  GLU B CA  
3024  C C   . GLU B  69  ? 0.5041 0.5047 0.5369 0.0049  0.0000  0.0038  69  GLU B C   
3025  O O   . GLU B  69  ? 0.5378 0.5368 0.5686 0.0036  0.0051  0.0011  69  GLU B O   
3026  C CB  . GLU B  69  ? 0.6217 0.6158 0.6732 0.0061  0.0004  0.0106  69  GLU B CB  
3027  C CG  . GLU B  69  ? 0.7992 0.7917 0.8594 0.0062  -0.0022 0.0150  69  GLU B CG  
3028  C CD  . GLU B  69  ? 0.8406 0.8288 0.9122 0.0074  0.0010  0.0180  69  GLU B CD  
3029  O OE1 . GLU B  69  ? 0.8377 0.8230 0.9102 0.0073  0.0067  0.0161  69  GLU B OE1 
3030  O OE2 . GLU B  69  ? 0.7793 0.7670 0.8588 0.0082  -0.0020 0.0224  69  GLU B OE2 
3031  N N   . PHE B  70  ? 0.5030 0.5073 0.5312 0.0063  -0.0038 0.0039  70  PHE B N   
3032  C CA  . PHE B  70  ? 0.4536 0.4606 0.4745 0.0067  -0.0022 0.0010  70  PHE B CA  
3033  C C   . PHE B  70  ? 0.5599 0.5673 0.5830 0.0093  -0.0039 0.0030  70  PHE B C   
3034  O O   . PHE B  70  ? 0.6329 0.6407 0.6592 0.0105  -0.0081 0.0058  70  PHE B O   
3035  C CB  . PHE B  70  ? 0.5388 0.5507 0.5500 0.0056  -0.0048 -0.0015 70  PHE B CB  
3036  C CG  . PHE B  70  ? 0.5136 0.5254 0.5224 0.0029  -0.0037 -0.0035 70  PHE B CG  
3037  C CD1 . PHE B  70  ? 0.4000 0.4112 0.4054 0.0009  0.0012  -0.0068 70  PHE B CD1 
3038  C CD2 . PHE B  70  ? 0.4663 0.4786 0.4760 0.0023  -0.0074 -0.0021 70  PHE B CD2 
3039  C CE1 . PHE B  70  ? 0.4966 0.5075 0.4999 -0.0017 0.0025  -0.0088 70  PHE B CE1 
3040  C CE2 . PHE B  70  ? 0.3968 0.4088 0.4043 -0.0001 -0.0062 -0.0039 70  PHE B CE2 
3041  C CZ  . PHE B  70  ? 0.4208 0.4321 0.4253 -0.0021 -0.0012 -0.0072 70  PHE B CZ  
3042  N N   . ASN B  71  ? 0.4769 0.4840 0.4980 0.0100  -0.0004 0.0017  71  ASN B N   
3043  C CA  . ASN B  71  ? 0.5189 0.5264 0.5416 0.0124  -0.0015 0.0033  71  ASN B CA  
3044  C C   . ASN B  71  ? 0.5261 0.5387 0.5411 0.0133  -0.0051 0.0025  71  ASN B C   
3045  O O   . ASN B  71  ? 0.5662 0.5821 0.5744 0.0120  -0.0066 0.0005  71  ASN B O   
3046  C CB  . ASN B  71  ? 0.6260 0.6310 0.6499 0.0129  0.0039  0.0025  71  ASN B CB  
3047  C CG  . ASN B  71  ? 0.6612 0.6686 0.6762 0.0114  0.0070  -0.0013 71  ASN B CG  
3048  O OD1 . ASN B  71  ? 0.7938 0.8060 0.8011 0.0115  0.0046  -0.0027 71  ASN B OD1 
3049  N ND2 . ASN B  71  ? 0.6472 0.6515 0.6633 0.0098  0.0123  -0.0031 71  ASN B ND2 
3050  N N   . HIS B  72  ? 0.5458 0.5588 0.5621 0.0156  -0.0063 0.0041  72  HIS B N   
3051  C CA  . HIS B  72  ? 0.6983 0.7156 0.7088 0.0169  -0.0097 0.0039  72  HIS B CA  
3052  C C   . HIS B  72  ? 0.6005 0.6220 0.6017 0.0162  -0.0083 0.0010  72  HIS B C   
3053  O O   . HIS B  72  ? 0.7386 0.7642 0.7341 0.0167  -0.0112 0.0005  72  HIS B O   
3054  C CB  . HIS B  72  ? 0.7563 0.7726 0.7704 0.0194  -0.0103 0.0061  72  HIS B CB  
3055  C CG  . HIS B  72  ? 0.9697 0.9841 0.9851 0.0203  -0.0056 0.0058  72  HIS B CG  
3056  N ND1 . HIS B  72  ? 1.0418 1.0515 1.0646 0.0202  -0.0024 0.0069  72  HIS B ND1 
3057  C CD2 . HIS B  72  ? 0.9998 1.0163 1.0099 0.0213  -0.0035 0.0047  72  HIS B CD2 
3058  C CE1 . HIS B  72  ? 1.0392 1.0480 1.0610 0.0209  0.0015  0.0061  72  HIS B CE1 
3059  N NE2 . HIS B  72  ? 0.9507 0.9637 0.9648 0.0216  0.0009  0.0049  72  HIS B NE2 
3060  N N   . LEU B  73  ? 0.5834 0.6038 0.5830 0.0150  -0.0037 -0.0010 73  LEU B N   
3061  C CA  . LEU B  73  ? 0.4813 0.5059 0.4721 0.0140  -0.0022 -0.0038 73  LEU B CA  
3062  C C   . LEU B  73  ? 0.5022 0.5281 0.4891 0.0110  -0.0015 -0.0064 73  LEU B C   
3063  O O   . LEU B  73  ? 0.5662 0.5947 0.5468 0.0094  0.0009  -0.0091 73  LEU B O   
3064  C CB  . LEU B  73  ? 0.5636 0.5869 0.5539 0.0143  0.0025  -0.0045 73  LEU B CB  
3065  C CG  . LEU B  73  ? 0.6306 0.6539 0.6224 0.0172  0.0022  -0.0024 73  LEU B CG  
3066  C CD1 . LEU B  73  ? 0.5767 0.5980 0.5684 0.0172  0.0073  -0.0031 73  LEU B CD1 
3067  C CD2 . LEU B  73  ? 0.6022 0.6313 0.5875 0.0185  -0.0010 -0.0023 73  LEU B CD2 
3068  N N   . GLU B  74  ? 0.5263 0.5504 0.5168 0.0101  -0.0037 -0.0056 74  GLU B N   
3069  C CA  . GLU B  74  ? 0.4286 0.4535 0.4160 0.0074  -0.0032 -0.0079 74  GLU B CA  
3070  C C   . GLU B  74  ? 0.5391 0.5661 0.5256 0.0073  -0.0081 -0.0071 74  GLU B C   
3071  O O   . GLU B  74  ? 0.5775 0.6032 0.5651 0.0055  -0.0085 -0.0076 74  GLU B O   
3072  C CB  . GLU B  74  ? 0.4065 0.4260 0.4001 0.0058  0.0005  -0.0080 74  GLU B CB  
3073  C CG  . GLU B  74  ? 0.4926 0.5097 0.4865 0.0053  0.0061  -0.0095 74  GLU B CG  
3074  C CD  . GLU B  74  ? 0.7782 0.7894 0.7792 0.0040  0.0100  -0.0092 74  GLU B CD  
3075  O OE1 . GLU B  74  ? 0.6457 0.6536 0.6550 0.0053  0.0086  -0.0060 74  GLU B OE1 
3076  O OE2 . GLU B  74  ? 0.4644 0.4744 0.4632 0.0017  0.0147  -0.0121 74  GLU B OE2 
3077  N N   . LYS B  75  ? 0.5119 0.5419 0.4963 0.0092  -0.0117 -0.0058 75  LYS B N   
3078  C CA  . LYS B  75  ? 0.5412 0.5731 0.5245 0.0092  -0.0164 -0.0050 75  LYS B CA  
3079  C C   . LYS B  75  ? 0.5302 0.5656 0.5070 0.0070  -0.0168 -0.0078 75  LYS B C   
3080  O O   . LYS B  75  ? 0.5285 0.5642 0.5049 0.0061  -0.0197 -0.0074 75  LYS B O   
3081  C CB  . LYS B  75  ? 0.5036 0.5381 0.4852 0.0117  -0.0193 -0.0037 75  LYS B CB  
3082  C CG  . LYS B  75  ? 0.6761 0.7129 0.6555 0.0115  -0.0238 -0.0032 75  LYS B CG  
3083  C CD  . LYS B  75  ? 0.6241 0.6573 0.6093 0.0108  -0.0260 -0.0013 75  LYS B CD  
3084  C CE  . LYS B  75  ? 0.8964 0.9267 0.8880 0.0127  -0.0272 0.0016  75  LYS B CE  
3085  N NZ  . LYS B  75  ? 1.1261 1.1536 1.1234 0.0119  -0.0297 0.0038  75  LYS B NZ  
3086  N N   . ARG B  76  ? 0.4588 0.4968 0.4302 0.0058  -0.0139 -0.0104 76  ARG B N   
3087  C CA  . ARG B  76  ? 0.5203 0.5622 0.4851 0.0036  -0.0141 -0.0132 76  ARG B CA  
3088  C C   . ARG B  76  ? 0.4387 0.4775 0.4055 0.0009  -0.0125 -0.0144 76  ARG B C   
3089  O O   . ARG B  76  ? 0.4512 0.4914 0.4160 -0.0004 -0.0147 -0.0150 76  ARG B O   
3090  C CB  . ARG B  76  ? 0.3695 0.4157 0.3280 0.0030  -0.0117 -0.0156 76  ARG B CB  
3091  C CG  . ARG B  76  ? 0.3923 0.4424 0.3483 0.0057  -0.0133 -0.0143 76  ARG B CG  
3092  C CD  . ARG B  76  ? 0.5552 0.6100 0.5048 0.0049  -0.0110 -0.0163 76  ARG B CD  
3093  N NE  . ARG B  76  ? 0.5772 0.6288 0.5281 0.0038  -0.0064 -0.0174 76  ARG B NE  
3094  C CZ  . ARG B  76  ? 0.4615 0.5157 0.4071 0.0015  -0.0034 -0.0201 76  ARG B CZ  
3095  N NH1 . ARG B  76  ? 0.5426 0.6031 0.4815 0.0001  -0.0047 -0.0219 76  ARG B NH1 
3096  N NH2 . ARG B  76  ? 0.3862 0.4369 0.3333 0.0003  0.0010  -0.0211 76  ARG B NH2 
3097  N N   . ILE B  77  ? 0.4790 0.5136 0.4498 0.0000  -0.0083 -0.0148 77  ILE B N   
3098  C CA  . ILE B  77  ? 0.4495 0.4805 0.4233 -0.0023 -0.0063 -0.0156 77  ILE B CA  
3099  C C   . ILE B  77  ? 0.4075 0.4352 0.3877 -0.0014 -0.0094 -0.0123 77  ILE B C   
3100  O O   . ILE B  77  ? 0.3656 0.3919 0.3471 -0.0031 -0.0096 -0.0125 77  ILE B O   
3101  C CB  . ILE B  77  ? 0.3568 0.3836 0.3340 -0.0033 -0.0007 -0.0166 77  ILE B CB  
3102  C CG1 . ILE B  77  ? 0.7189 0.7434 0.7007 -0.0008 0.0002  -0.0143 77  ILE B CG1 
3103  C CG2 . ILE B  77  ? 0.4526 0.4824 0.4224 -0.0058 0.0027  -0.0206 77  ILE B CG2 
3104  C CD1 . ILE B  77  ? 0.7240 0.7443 0.7087 -0.0017 0.0060  -0.0154 77  ILE B CD1 
3105  N N   . GLU B  78  ? 0.3612 0.3880 0.3456 0.0012  -0.0118 -0.0093 78  GLU B N   
3106  C CA  . GLU B  78  ? 0.4512 0.4759 0.4412 0.0020  -0.0153 -0.0061 78  GLU B CA  
3107  C C   . GLU B  78  ? 0.4304 0.4584 0.4154 0.0012  -0.0194 -0.0066 78  GLU B C   
3108  O O   . GLU B  78  ? 0.4364 0.4628 0.4240 0.0002  -0.0211 -0.0053 78  GLU B O   
3109  C CB  . GLU B  78  ? 0.4621 0.4859 0.4563 0.0047  -0.0172 -0.0032 78  GLU B CB  
3110  C CG  . GLU B  78  ? 0.5715 0.5934 0.5715 0.0052  -0.0210 0.0001  78  GLU B CG  
3111  C CD  . GLU B  78  ? 0.8750 0.8963 0.8787 0.0076  -0.0231 0.0027  78  GLU B CD  
3112  O OE1 . GLU B  78  ? 1.0725 1.0932 1.0774 0.0090  -0.0205 0.0025  78  GLU B OE1 
3113  O OE2 . GLU B  78  ? 0.9792 1.0008 0.9847 0.0080  -0.0272 0.0048  78  GLU B OE2 
3114  N N   . ASN B  79  ? 0.4599 0.4927 0.4379 0.0016  -0.0207 -0.0084 79  ASN B N   
3115  C CA  . ASN B  79  ? 0.4866 0.5229 0.4596 0.0009  -0.0242 -0.0091 79  ASN B CA  
3116  C C   . ASN B  79  ? 0.4583 0.4956 0.4274 -0.0019 -0.0225 -0.0119 79  ASN B C   
3117  O O   . ASN B  79  ? 0.4738 0.5118 0.4415 -0.0031 -0.0249 -0.0119 79  ASN B O   
3118  C CB  . ASN B  79  ? 0.4255 0.4666 0.3930 0.0024  -0.0259 -0.0098 79  ASN B CB  
3119  C CG  . ASN B  79  ? 0.6572 0.6974 0.6280 0.0049  -0.0287 -0.0070 79  ASN B CG  
3120  O OD1 . ASN B  79  ? 0.6608 0.6980 0.6363 0.0050  -0.0309 -0.0047 79  ASN B OD1 
3121  N ND2 . ASN B  79  ? 0.6691 0.7120 0.6374 0.0068  -0.0286 -0.0071 79  ASN B ND2 
3122  N N   . LEU B  80  ? 0.2092 0.2467 0.1765 -0.0032 -0.0184 -0.0144 80  LEU B N   
3123  C CA  . LEU B  80  ? 0.2327 0.2706 0.1970 -0.0061 -0.0161 -0.0172 80  LEU B CA  
3124  C C   . LEU B  80  ? 0.5715 0.6045 0.5418 -0.0071 -0.0160 -0.0154 80  LEU B C   
3125  O O   . LEU B  80  ? 0.5206 0.5541 0.4891 -0.0087 -0.0173 -0.0160 80  LEU B O   
3126  C CB  . LEU B  80  ? 0.4248 0.4626 0.3874 -0.0075 -0.0112 -0.0199 80  LEU B CB  
3127  C CG  . LEU B  80  ? 0.4861 0.5267 0.4427 -0.0106 -0.0089 -0.0238 80  LEU B CG  
3128  C CD1 . LEU B  80  ? 0.4197 0.4576 0.3771 -0.0125 -0.0033 -0.0260 80  LEU B CD1 
3129  C CD2 . LEU B  80  ? 0.3573 0.3970 0.3140 -0.0124 -0.0102 -0.0241 80  LEU B CD2 
3130  N N   . ASN B  81  ? 0.5657 0.5940 0.5432 -0.0060 -0.0144 -0.0131 81  ASN B N   
3131  C CA  . ASN B  81  ? 0.2928 0.3165 0.2773 -0.0065 -0.0143 -0.0107 81  ASN B CA  
3132  C C   . ASN B  81  ? 0.3903 0.4149 0.3752 -0.0060 -0.0194 -0.0082 81  ASN B C   
3133  O O   . ASN B  81  ? 0.5051 0.5282 0.4913 -0.0075 -0.0200 -0.0076 81  ASN B O   
3134  C CB  . ASN B  81  ? 0.4808 0.5001 0.4734 -0.0049 -0.0122 -0.0080 81  ASN B CB  
3135  C CG  . ASN B  81  ? 0.5013 0.5163 0.5019 -0.0051 -0.0123 -0.0049 81  ASN B CG  
3136  O OD1 . ASN B  81  ? 0.4943 0.5069 0.4963 -0.0070 -0.0093 -0.0058 81  ASN B OD1 
3137  N ND2 . ASN B  81  ? 0.4061 0.4200 0.4123 -0.0033 -0.0156 -0.0010 81  ASN B ND2 
3138  N N   . LYS B  82  ? 0.3978 0.4246 0.3816 -0.0041 -0.0231 -0.0068 82  LYS B N   
3139  C CA  . LYS B  82  ? 0.5258 0.5535 0.5092 -0.0038 -0.0280 -0.0048 82  LYS B CA  
3140  C C   . LYS B  82  ? 0.5773 0.6081 0.5538 -0.0057 -0.0292 -0.0072 82  LYS B C   
3141  O O   . LYS B  82  ? 0.4918 0.5221 0.4687 -0.0066 -0.0318 -0.0059 82  LYS B O   
3142  C CB  . LYS B  82  ? 0.5417 0.5713 0.5245 -0.0016 -0.0311 -0.0034 82  LYS B CB  
3143  C CG  . LYS B  82  ? 0.6701 0.7012 0.6507 -0.0017 -0.0359 -0.0022 82  LYS B CG  
3144  C CD  . LYS B  82  ? 0.7879 0.8205 0.7680 0.0004  -0.0385 -0.0011 82  LYS B CD  
3145  C CE  . LYS B  82  ? 1.1066 1.1412 1.0831 0.0000  -0.0427 -0.0007 82  LYS B CE  
3146  N NZ  . LYS B  82  ? 0.8933 0.9254 0.8731 -0.0015 -0.0451 0.0017  82  LYS B NZ  
3147  N N   . LYS B  83  ? 0.5294 0.5637 0.4998 -0.0063 -0.0273 -0.0106 83  LYS B N   
3148  C CA  . LYS B  83  ? 0.4856 0.5234 0.4496 -0.0081 -0.0282 -0.0131 83  LYS B CA  
3149  C C   . LYS B  83  ? 0.4300 0.4651 0.3952 -0.0106 -0.0262 -0.0138 83  LYS B C   
3150  O O   . LYS B  83  ? 0.3986 0.4345 0.3617 -0.0118 -0.0284 -0.0138 83  LYS B O   
3151  C CB  . LYS B  83  ? 0.3520 0.3944 0.3096 -0.0083 -0.0265 -0.0164 83  LYS B CB  
3152  C CG  . LYS B  83  ? 0.4473 0.4936 0.3985 -0.0103 -0.0272 -0.0191 83  LYS B CG  
3153  C CD  . LYS B  83  ? 0.4355 0.4875 0.3804 -0.0101 -0.0267 -0.0217 83  LYS B CD  
3154  C CE  . LYS B  83  ? 0.4089 0.4613 0.3528 -0.0115 -0.0223 -0.0242 83  LYS B CE  
3155  N NZ  . LYS B  83  ? 0.4110 0.4698 0.3482 -0.0120 -0.0220 -0.0267 83  LYS B NZ  
3156  N N   . VAL B  84  ? 0.3199 0.3519 0.2888 -0.0113 -0.0219 -0.0144 84  VAL B N   
3157  C CA  . VAL B  84  ? 0.4555 0.4846 0.4262 -0.0137 -0.0193 -0.0151 84  VAL B CA  
3158  C C   . VAL B  84  ? 0.4656 0.4911 0.4422 -0.0133 -0.0217 -0.0112 84  VAL B C   
3159  O O   . VAL B  84  ? 0.4835 0.5078 0.4602 -0.0151 -0.0214 -0.0112 84  VAL B O   
3160  C CB  . VAL B  84  ? 0.3825 0.4086 0.3560 -0.0146 -0.0136 -0.0167 84  VAL B CB  
3161  C CG1 . VAL B  84  ? 0.6006 0.6224 0.5824 -0.0127 -0.0127 -0.0134 84  VAL B CG1 
3162  C CG2 . VAL B  84  ? 0.5420 0.5657 0.5160 -0.0173 -0.0106 -0.0182 84  VAL B CG2 
3163  N N   . ASP B  85  ? 0.4599 0.4841 0.4414 -0.0111 -0.0241 -0.0077 85  ASP B N   
3164  C CA  . ASP B  85  ? 0.3390 0.3606 0.3259 -0.0108 -0.0270 -0.0036 85  ASP B CA  
3165  C C   . ASP B  85  ? 0.4046 0.4290 0.3865 -0.0113 -0.0318 -0.0033 85  ASP B C   
3166  O O   . ASP B  85  ? 0.4835 0.5066 0.4667 -0.0124 -0.0333 -0.0016 85  ASP B O   
3167  C CB  . ASP B  85  ? 0.4420 0.4617 0.4356 -0.0085 -0.0282 -0.0002 85  ASP B CB  
3168  C CG  . ASP B  85  ? 0.6053 0.6209 0.6061 -0.0082 -0.0236 0.0007  85  ASP B CG  
3169  O OD1 . ASP B  85  ? 0.5767 0.5903 0.5781 -0.0099 -0.0197 -0.0008 85  ASP B OD1 
3170  O OD2 . ASP B  85  ? 0.6818 0.6960 0.6877 -0.0064 -0.0237 0.0029  85  ASP B OD2 
3171  N N   . ASP B  86  ? 0.4082 0.4364 0.3846 -0.0103 -0.0340 -0.0048 86  ASP B N   
3172  C CA  . ASP B  86  ? 0.3972 0.4281 0.3686 -0.0107 -0.0381 -0.0048 86  ASP B CA  
3173  C C   . ASP B  86  ? 0.5070 0.5397 0.4727 -0.0130 -0.0372 -0.0078 86  ASP B C   
3174  O O   . ASP B  86  ? 0.5454 0.5791 0.5082 -0.0139 -0.0401 -0.0074 86  ASP B O   
3175  C CB  . ASP B  86  ? 0.5877 0.6220 0.5554 -0.0090 -0.0401 -0.0057 86  ASP B CB  
3176  C CG  . ASP B  86  ? 0.8477 0.8803 0.8205 -0.0071 -0.0423 -0.0024 86  ASP B CG  
3177  O OD1 . ASP B  86  ? 0.9089 0.9383 0.8876 -0.0072 -0.0432 0.0007  86  ASP B OD1 
3178  O OD2 . ASP B  86  ? 0.8770 0.9116 0.8481 -0.0054 -0.0429 -0.0029 86  ASP B OD2 
3179  N N   . GLY B  87  ? 0.4519 0.4852 0.4161 -0.0140 -0.0331 -0.0108 87  GLY B N   
3180  C CA  . GLY B  87  ? 0.3134 0.3484 0.2726 -0.0163 -0.0318 -0.0138 87  GLY B CA  
3181  C C   . GLY B  87  ? 0.4414 0.4727 0.4040 -0.0179 -0.0311 -0.0122 87  GLY B C   
3182  O O   . GLY B  87  ? 0.4539 0.4860 0.4133 -0.0193 -0.0330 -0.0124 87  GLY B O   
3183  N N   . PHE B  88  ? 0.3926 0.4196 0.3618 -0.0178 -0.0282 -0.0106 88  PHE B N   
3184  C CA  . PHE B  88  ? 0.4266 0.4498 0.4003 -0.0191 -0.0272 -0.0085 88  PHE B CA  
3185  C C   . PHE B  88  ? 0.4672 0.4900 0.4424 -0.0186 -0.0322 -0.0046 88  PHE B C   
3186  O O   . PHE B  88  ? 0.4947 0.5163 0.4698 -0.0200 -0.0329 -0.0035 88  PHE B O   
3187  C CB  . PHE B  88  ? 0.4590 0.4777 0.4407 -0.0185 -0.0233 -0.0068 88  PHE B CB  
3188  C CG  . PHE B  88  ? 0.3746 0.3929 0.3549 -0.0197 -0.0178 -0.0107 88  PHE B CG  
3189  C CD1 . PHE B  88  ? 0.3031 0.3184 0.2891 -0.0189 -0.0141 -0.0102 88  PHE B CD1 
3190  C CD2 . PHE B  88  ? 0.4167 0.4379 0.3901 -0.0219 -0.0163 -0.0151 88  PHE B CD2 
3191  C CE1 . PHE B  88  ? 0.4184 0.4332 0.4027 -0.0203 -0.0089 -0.0140 88  PHE B CE1 
3192  C CE2 . PHE B  88  ? 0.5032 0.5242 0.4749 -0.0234 -0.0113 -0.0188 88  PHE B CE2 
3193  C CZ  . PHE B  88  ? 0.4848 0.5025 0.4618 -0.0226 -0.0076 -0.0184 88  PHE B CZ  
3194  N N   . LEU B  89  ? 0.3843 0.4081 0.3607 -0.0166 -0.0355 -0.0025 89  LEU B N   
3195  C CA  . LEU B  89  ? 0.3202 0.3439 0.2975 -0.0163 -0.0404 0.0010  89  LEU B CA  
3196  C C   . LEU B  89  ? 0.3988 0.4253 0.3686 -0.0178 -0.0430 -0.0007 89  LEU B C   
3197  O O   . LEU B  89  ? 0.4913 0.5168 0.4613 -0.0188 -0.0454 0.0015  89  LEU B O   
3198  C CB  . LEU B  89  ? 0.3604 0.3849 0.3396 -0.0142 -0.0431 0.0028  89  LEU B CB  
3199  C CG  . LEU B  89  ? 0.4314 0.4563 0.4106 -0.0142 -0.0483 0.0059  89  LEU B CG  
3200  C CD1 . LEU B  89  ? 0.5187 0.5408 0.5032 -0.0152 -0.0493 0.0098  89  LEU B CD1 
3201  C CD2 . LEU B  89  ? 0.4788 0.5042 0.4608 -0.0122 -0.0503 0.0075  89  LEU B CD2 
3202  N N   . ASP B  90  ? 0.4144 0.4444 0.3777 -0.0178 -0.0425 -0.0045 90  ASP B N   
3203  C CA  . ASP B  90  ? 0.3869 0.4198 0.3432 -0.0190 -0.0447 -0.0064 90  ASP B CA  
3204  C C   . ASP B  90  ? 0.4173 0.4496 0.3717 -0.0213 -0.0426 -0.0080 90  ASP B C   
3205  O O   . ASP B  90  ? 0.4563 0.4889 0.4077 -0.0226 -0.0448 -0.0075 90  ASP B O   
3206  C CB  . ASP B  90  ? 0.4198 0.4571 0.3705 -0.0181 -0.0446 -0.0097 90  ASP B CB  
3207  C CG  . ASP B  90  ? 0.6513 0.6896 0.6024 -0.0161 -0.0475 -0.0082 90  ASP B CG  
3208  O OD1 . ASP B  90  ? 0.8078 0.8441 0.7618 -0.0158 -0.0505 -0.0049 90  ASP B OD1 
3209  O OD2 . ASP B  90  ? 0.8403 0.8815 0.7888 -0.0148 -0.0469 -0.0101 90  ASP B OD2 
3210  N N   . ILE B  91  ? 0.4692 0.5004 0.4253 -0.0220 -0.0381 -0.0099 91  ILE B N   
3211  C CA  . ILE B  91  ? 0.3821 0.4122 0.3368 -0.0244 -0.0355 -0.0116 91  ILE B CA  
3212  C C   . ILE B  91  ? 0.5069 0.5331 0.4662 -0.0250 -0.0365 -0.0077 91  ILE B C   
3213  O O   . ILE B  91  ? 0.4789 0.5052 0.4352 -0.0266 -0.0377 -0.0077 91  ILE B O   
3214  C CB  . ILE B  91  ? 0.3617 0.3908 0.3180 -0.0251 -0.0301 -0.0143 91  ILE B CB  
3215  C CG1 . ILE B  91  ? 0.3400 0.3737 0.2909 -0.0250 -0.0292 -0.0183 91  ILE B CG1 
3216  C CG2 . ILE B  91  ? 0.6035 0.6307 0.5595 -0.0277 -0.0272 -0.0157 91  ILE B CG2 
3217  C CD1 . ILE B  91  ? 0.5917 0.6247 0.5434 -0.0260 -0.0240 -0.0212 91  ILE B CD1 
3218  N N   . TRP B  92  ? 0.4260 0.4489 0.3928 -0.0238 -0.0359 -0.0042 92  TRP B N   
3219  C CA  . TRP B  92  ? 0.4108 0.4301 0.3831 -0.0242 -0.0365 0.0000  92  TRP B CA  
3220  C C   . TRP B  92  ? 0.4333 0.4536 0.4038 -0.0243 -0.0420 0.0030  92  TRP B C   
3221  O O   . TRP B  92  ? 0.4709 0.4898 0.4415 -0.0257 -0.0428 0.0049  92  TRP B O   
3222  C CB  . TRP B  92  ? 0.4033 0.4192 0.3846 -0.0227 -0.0347 0.0032  92  TRP B CB  
3223  C CG  . TRP B  92  ? 0.3604 0.3739 0.3447 -0.0234 -0.0287 0.0010  92  TRP B CG  
3224  C CD1 . TRP B  92  ? 0.3757 0.3888 0.3617 -0.0225 -0.0253 -0.0010 92  TRP B CD1 
3225  C CD2 . TRP B  92  ? 0.3445 0.3553 0.3300 -0.0253 -0.0250 0.0004  92  TRP B CD2 
3226  N NE1 . TRP B  92  ? 0.6047 0.6150 0.5928 -0.0239 -0.0197 -0.0030 92  TRP B NE1 
3227  C CE2 . TRP B  92  ? 0.4439 0.4528 0.4320 -0.0256 -0.0194 -0.0022 92  TRP B CE2 
3228  C CE3 . TRP B  92  ? 0.4574 0.4672 0.4421 -0.0268 -0.0258 0.0017  92  TRP B CE3 
3229  C CZ2 . TRP B  92  ? 0.4363 0.4420 0.4262 -0.0275 -0.0143 -0.0036 92  TRP B CZ2 
3230  C CZ3 . TRP B  92  ? 0.4701 0.4769 0.4568 -0.0285 -0.0209 0.0005  92  TRP B CZ3 
3231  C CH2 . TRP B  92  ? 0.4947 0.4995 0.4840 -0.0288 -0.0152 -0.0022 92  TRP B CH2 
3232  N N   . THR B  93  ? 0.3967 0.4193 0.3652 -0.0230 -0.0455 0.0034  93  THR B N   
3233  C CA  . THR B  93  ? 0.4112 0.4348 0.3771 -0.0234 -0.0505 0.0057  93  THR B CA  
3234  C C   . THR B  93  ? 0.4192 0.4446 0.3776 -0.0253 -0.0512 0.0032  93  THR B C   
3235  O O   . THR B  93  ? 0.4420 0.4664 0.3997 -0.0267 -0.0533 0.0055  93  THR B O   
3236  C CB  . THR B  93  ? 0.4315 0.4573 0.3958 -0.0218 -0.0536 0.0057  93  THR B CB  
3237  O OG1 . THR B  93  ? 0.4630 0.4871 0.4347 -0.0201 -0.0533 0.0084  93  THR B OG1 
3238  C CG2 . THR B  93  ? 0.4269 0.4538 0.3877 -0.0226 -0.0585 0.0075  93  THR B CG2 
3239  N N   . TYR B  94  ? 0.4657 0.4939 0.4186 -0.0255 -0.0495 -0.0014 94  TYR B N   
3240  C CA  . TYR B  94  ? 0.4236 0.4538 0.3694 -0.0272 -0.0499 -0.0041 94  TYR B CA  
3241  C C   . TYR B  94  ? 0.4439 0.4719 0.3904 -0.0292 -0.0475 -0.0040 94  TYR B C   
3242  O O   . TYR B  94  ? 0.4005 0.4283 0.3439 -0.0307 -0.0494 -0.0032 94  TYR B O   
3243  C CB  . TYR B  94  ? 0.3452 0.3793 0.2860 -0.0269 -0.0481 -0.0088 94  TYR B CB  
3244  C CG  . TYR B  94  ? 0.4629 0.4997 0.3965 -0.0285 -0.0489 -0.0116 94  TYR B CG  
3245  C CD1 . TYR B  94  ? 0.4460 0.4846 0.3755 -0.0282 -0.0526 -0.0112 94  TYR B CD1 
3246  C CD2 . TYR B  94  ? 0.5125 0.5502 0.4435 -0.0302 -0.0458 -0.0147 94  TYR B CD2 
3247  C CE1 . TYR B  94  ? 0.4008 0.4418 0.3240 -0.0296 -0.0531 -0.0137 94  TYR B CE1 
3248  C CE2 . TYR B  94  ? 0.5378 0.5782 0.4626 -0.0316 -0.0465 -0.0172 94  TYR B CE2 
3249  C CZ  . TYR B  94  ? 0.6030 0.6450 0.5240 -0.0312 -0.0502 -0.0166 94  TYR B CZ  
3250  O OH  . TYR B  94  ? 0.7227 0.7672 0.6378 -0.0325 -0.0506 -0.0191 94  TYR B OH  
3251  N N   . ASN B  95  ? 0.4516 0.4776 0.4023 -0.0293 -0.0432 -0.0048 95  ASN B N   
3252  C CA  . ASN B  95  ? 0.3895 0.4131 0.3415 -0.0312 -0.0403 -0.0048 95  ASN B CA  
3253  C C   . ASN B  95  ? 0.4938 0.5141 0.4502 -0.0314 -0.0422 0.0004  95  ASN B C   
3254  O O   . ASN B  95  ? 0.5650 0.5844 0.5194 -0.0331 -0.0423 0.0009  95  ASN B O   
3255  C CB  . ASN B  95  ? 0.4585 0.4802 0.4143 -0.0313 -0.0349 -0.0068 95  ASN B CB  
3256  C CG  . ASN B  95  ? 0.5811 0.6064 0.5314 -0.0320 -0.0325 -0.0123 95  ASN B CG  
3257  O OD1 . ASN B  95  ? 0.4714 0.5006 0.4158 -0.0318 -0.0350 -0.0142 95  ASN B OD1 
3258  N ND2 . ASN B  95  ? 0.6600 0.6839 0.6122 -0.0329 -0.0276 -0.0147 95  ASN B ND2 
3259  N N   . ALA B  96  ? 0.4118 0.4305 0.3745 -0.0298 -0.0438 0.0044  96  ALA B N   
3260  C CA  . ALA B  96  ? 0.5016 0.5178 0.4693 -0.0299 -0.0460 0.0099  96  ALA B CA  
3261  C C   . ALA B  96  ? 0.5357 0.5535 0.4978 -0.0310 -0.0509 0.0112  96  ALA B C   
3262  O O   . ALA B  96  ? 0.5554 0.5718 0.5178 -0.0323 -0.0517 0.0138  96  ALA B O   
3263  C CB  . ALA B  96  ? 0.5250 0.5399 0.5003 -0.0279 -0.0470 0.0137  96  ALA B CB  
3264  N N   . GLU B  97  ? 0.3773 0.3981 0.3346 -0.0304 -0.0539 0.0096  97  GLU B N   
3265  C CA  . GLU B  97  ? 0.4897 0.5121 0.4412 -0.0316 -0.0583 0.0102  97  GLU B CA  
3266  C C   . GLU B  97  ? 0.5825 0.6052 0.5280 -0.0337 -0.0571 0.0078  97  GLU B C   
3267  O O   . GLU B  97  ? 0.5715 0.5934 0.5150 -0.0352 -0.0595 0.0101  97  GLU B O   
3268  C CB  . GLU B  97  ? 0.5039 0.5293 0.4510 -0.0306 -0.0607 0.0080  97  GLU B CB  
3269  C CG  . GLU B  97  ? 0.4672 0.4924 0.4194 -0.0288 -0.0628 0.0108  97  GLU B CG  
3270  C CD  . GLU B  97  ? 0.6823 0.7067 0.6360 -0.0296 -0.0673 0.0155  97  GLU B CD  
3271  O OE1 . GLU B  97  ? 0.7359 0.7608 0.6923 -0.0285 -0.0698 0.0174  97  GLU B OE1 
3272  O OE2 . GLU B  97  ? 0.9779 1.0014 0.9300 -0.0314 -0.0684 0.0174  97  GLU B OE2 
3273  N N   . LEU B  98  ? 0.5375 0.5614 0.4800 -0.0339 -0.0535 0.0031  98  LEU B N   
3274  C CA  . LEU B  98  ? 0.4346 0.4592 0.3715 -0.0360 -0.0523 0.0003  98  LEU B CA  
3275  C C   . LEU B  98  ? 0.5780 0.5993 0.5184 -0.0373 -0.0494 0.0019  98  LEU B C   
3276  O O   . LEU B  98  ? 0.5785 0.5995 0.5153 -0.0391 -0.0496 0.0018  98  LEU B O   
3277  C CB  . LEU B  98  ? 0.4062 0.4340 0.3383 -0.0361 -0.0498 -0.0053 98  LEU B CB  
3278  C CG  . LEU B  98  ? 0.5012 0.5325 0.4264 -0.0361 -0.0527 -0.0075 98  LEU B CG  
3279  C CD1 . LEU B  98  ? 0.5518 0.5852 0.4777 -0.0339 -0.0541 -0.0079 98  LEU B CD1 
3280  C CD2 . LEU B  98  ? 0.8155 0.8494 0.7350 -0.0376 -0.0504 -0.0121 98  LEU B CD2 
3281  N N   . LEU B  99  ? 0.5561 0.5749 0.5038 -0.0363 -0.0465 0.0035  99  LEU B N   
3282  C CA  . LEU B  99  ? 0.5678 0.5831 0.5199 -0.0373 -0.0434 0.0056  99  LEU B CA  
3283  C C   . LEU B  99  ? 0.5098 0.5236 0.4628 -0.0380 -0.0470 0.0108  99  LEU B C   
3284  O O   . LEU B  99  ? 0.4914 0.5038 0.4429 -0.0396 -0.0461 0.0114  99  LEU B O   
3285  C CB  . LEU B  99  ? 0.5447 0.5572 0.5052 -0.0360 -0.0399 0.0071  99  LEU B CB  
3286  C CG  . LEU B  99  ? 0.6447 0.6530 0.6107 -0.0368 -0.0362 0.0094  99  LEU B CG  
3287  C CD1 . LEU B  99  ? 0.5698 0.5781 0.5314 -0.0390 -0.0322 0.0047  99  LEU B CD1 
3288  C CD2 . LEU B  99  ? 0.6635 0.6690 0.6384 -0.0353 -0.0328 0.0112  99  LEU B CD2 
3289  N N   . VAL B  100 ? 0.4531 0.4674 0.4084 -0.0368 -0.0512 0.0146  100 VAL B N   
3290  C CA  . VAL B  100 ? 0.5684 0.5820 0.5245 -0.0375 -0.0552 0.0198  100 VAL B CA  
3291  C C   . VAL B  100 ? 0.5269 0.5421 0.4741 -0.0395 -0.0577 0.0181  100 VAL B C   
3292  O O   . VAL B  100 ? 0.5730 0.5868 0.5192 -0.0410 -0.0583 0.0205  100 VAL B O   
3293  C CB  . VAL B  100 ? 0.4554 0.4698 0.4151 -0.0361 -0.0594 0.0236  100 VAL B CB  
3294  C CG1 . VAL B  100 ? 0.5418 0.5564 0.5001 -0.0374 -0.0642 0.0283  100 VAL B CG1 
3295  C CG2 . VAL B  100 ? 0.4376 0.4499 0.4072 -0.0342 -0.0571 0.0265  100 VAL B CG2 
3296  N N   . LEU B  101 ? 0.5577 0.5758 0.4986 -0.0394 -0.0592 0.0141  101 LEU B N   
3297  C CA  . LEU B  101 ? 0.5576 0.5773 0.4900 -0.0413 -0.0611 0.0121  101 LEU B CA  
3298  C C   . LEU B  101 ? 0.5388 0.5572 0.4692 -0.0429 -0.0576 0.0102  101 LEU B C   
3299  O O   . LEU B  101 ? 0.6445 0.6615 0.5735 -0.0445 -0.0587 0.0128  101 LEU B O   
3300  C CB  . LEU B  101 ? 0.4913 0.5143 0.4181 -0.0407 -0.0619 0.0076  101 LEU B CB  
3301  C CG  . LEU B  101 ? 0.5434 0.5677 0.4710 -0.0393 -0.0656 0.0092  101 LEU B CG  
3302  C CD1 . LEU B  101 ? 0.6231 0.6504 0.5444 -0.0390 -0.0663 0.0048  101 LEU B CD1 
3303  C CD2 . LEU B  101 ? 0.4675 0.4908 0.3950 -0.0405 -0.0701 0.0140  101 LEU B CD2 
3304  N N   . LEU B  102 ? 0.5693 0.5882 0.4997 -0.0427 -0.0533 0.0059  102 LEU B N   
3305  C CA  . LEU B  102 ? 0.6251 0.6431 0.5536 -0.0444 -0.0496 0.0034  102 LEU B CA  
3306  C C   . LEU B  102 ? 0.5707 0.5849 0.5037 -0.0453 -0.0484 0.0077  102 LEU B C   
3307  O O   . LEU B  102 ? 0.6762 0.6895 0.6056 -0.0471 -0.0482 0.0078  102 LEU B O   
3308  C CB  . LEU B  102 ? 0.6196 0.6383 0.5492 -0.0441 -0.0449 -0.0013 102 LEU B CB  
3309  C CG  . LEU B  102 ? 0.8910 0.9139 0.8159 -0.0434 -0.0453 -0.0059 102 LEU B CG  
3310  C CD1 . LEU B  102 ? 1.1369 1.1607 1.0620 -0.0439 -0.0404 -0.0106 102 LEU B CD1 
3311  C CD2 . LEU B  102 ? 0.7544 0.7800 0.6717 -0.0444 -0.0484 -0.0075 102 LEU B CD2 
3312  N N   . GLU B  103 ? 0.4513 0.4631 0.3924 -0.0439 -0.0474 0.0114  103 GLU B N   
3313  C CA  . GLU B  103 ? 0.6388 0.6470 0.5855 -0.0443 -0.0459 0.0159  103 GLU B CA  
3314  C C   . GLU B  103 ? 0.6130 0.6209 0.5579 -0.0452 -0.0506 0.0209  103 GLU B C   
3315  O O   . GLU B  103 ? 0.6718 0.6776 0.6172 -0.0465 -0.0496 0.0233  103 GLU B O   
3316  C CB  . GLU B  103 ? 0.5462 0.5520 0.5025 -0.0424 -0.0438 0.0189  103 GLU B CB  
3317  C CG  . GLU B  103 ? 0.7894 0.7942 0.7482 -0.0422 -0.0379 0.0145  103 GLU B CG  
3318  C CD  . GLU B  103 ? 1.0521 1.0556 1.0078 -0.0443 -0.0338 0.0112  103 GLU B CD  
3319  O OE1 . GLU B  103 ? 1.0138 1.0138 0.9739 -0.0449 -0.0313 0.0142  103 GLU B OE1 
3320  O OE2 . GLU B  103 ? 0.9603 0.9664 0.9093 -0.0454 -0.0330 0.0058  103 GLU B OE2 
3321  N N   . ASN B  104 ? 0.4708 0.4810 0.4137 -0.0446 -0.0556 0.0225  104 ASN B N   
3322  C CA  . ASN B  104 ? 0.4994 0.5099 0.4397 -0.0458 -0.0603 0.0269  104 ASN B CA  
3323  C C   . ASN B  104 ? 0.6287 0.6396 0.5605 -0.0482 -0.0605 0.0245  104 ASN B C   
3324  O O   . ASN B  104 ? 0.7170 0.7267 0.6477 -0.0496 -0.0623 0.0283  104 ASN B O   
3325  C CB  . ASN B  104 ? 0.3778 0.3908 0.3168 -0.0451 -0.0653 0.0281  104 ASN B CB  
3326  C CG  . ASN B  104 ? 0.5292 0.5414 0.4773 -0.0433 -0.0665 0.0331  104 ASN B CG  
3327  O OD1 . ASN B  104 ? 0.5885 0.5982 0.5440 -0.0426 -0.0638 0.0362  104 ASN B OD1 
3328  N ND2 . ASN B  104 ? 0.6226 0.6368 0.5704 -0.0425 -0.0703 0.0338  104 ASN B ND2 
3329  N N   . GLU B  105 ? 0.5410 0.5536 0.4669 -0.0486 -0.0587 0.0183  105 GLU B N   
3330  C CA  . GLU B  105 ? 0.5985 0.6116 0.5166 -0.0508 -0.0583 0.0154  105 GLU B CA  
3331  C C   . GLU B  105 ? 0.6797 0.6901 0.5996 -0.0519 -0.0540 0.0154  105 GLU B C   
3332  O O   . GLU B  105 ? 0.8006 0.8104 0.7158 -0.0539 -0.0541 0.0154  105 GLU B O   
3333  C CB  . GLU B  105 ? 0.7090 0.7251 0.6215 -0.0507 -0.0572 0.0089  105 GLU B CB  
3334  C CG  . GLU B  105 ? 0.8692 0.8860 0.7740 -0.0529 -0.0565 0.0058  105 GLU B CG  
3335  C CD  . GLU B  105 ? 1.2837 1.3004 1.1835 -0.0544 -0.0609 0.0087  105 GLU B CD  
3336  O OE1 . GLU B  105 ? 1.1889 1.2065 1.0886 -0.0537 -0.0648 0.0109  105 GLU B OE1 
3337  O OE2 . GLU B  105 ? 1.3376 1.3532 1.2333 -0.0564 -0.0603 0.0087  105 GLU B OE2 
3338  N N   . ARG B  106 ? 0.5948 0.6034 0.5216 -0.0508 -0.0499 0.0153  106 ARG B N   
3339  C CA  . ARG B  106 ? 0.7105 0.7162 0.6401 -0.0518 -0.0453 0.0153  106 ARG B CA  
3340  C C   . ARG B  106 ? 0.7583 0.7610 0.6929 -0.0518 -0.0464 0.0223  106 ARG B C   
3341  O O   . ARG B  106 ? 0.8152 0.8157 0.7491 -0.0533 -0.0445 0.0235  106 ARG B O   
3342  C CB  . ARG B  106 ? 0.7190 0.7237 0.6538 -0.0508 -0.0401 0.0123  106 ARG B CB  
3343  C CG  . ARG B  106 ? 0.7274 0.7352 0.6570 -0.0511 -0.0384 0.0053  106 ARG B CG  
3344  C CD  . ARG B  106 ? 0.9418 0.9483 0.8755 -0.0512 -0.0325 0.0020  106 ARG B CD  
3345  N NE  . ARG B  106 ? 1.0051 1.0080 0.9411 -0.0527 -0.0285 0.0028  106 ARG B NE  
3346  C CZ  . ARG B  106 ? 1.1290 1.1321 1.0597 -0.0549 -0.0268 -0.0002 106 ARG B CZ  
3347  N NH1 . ARG B  106 ? 1.0675 1.0745 0.9906 -0.0557 -0.0288 -0.0043 106 ARG B NH1 
3348  N NH2 . ARG B  106 ? 1.0802 1.0797 1.0136 -0.0562 -0.0229 0.0008  106 ARG B NH2 
3349  N N   . THR B  107 ? 0.6468 0.6496 0.5863 -0.0503 -0.0497 0.0271  107 THR B N   
3350  C CA  . THR B  107 ? 0.6596 0.6602 0.6049 -0.0501 -0.0511 0.0344  107 THR B CA  
3351  C C   . THR B  107 ? 0.7139 0.7150 0.6532 -0.0521 -0.0550 0.0373  107 THR B C   
3352  O O   . THR B  107 ? 0.7467 0.7455 0.6878 -0.0529 -0.0538 0.0410  107 THR B O   
3353  C CB  . THR B  107 ? 0.7294 0.7307 0.6817 -0.0480 -0.0539 0.0388  107 THR B CB  
3354  O OG1 . THR B  107 ? 0.7530 0.7533 0.7116 -0.0462 -0.0497 0.0365  107 THR B OG1 
3355  C CG2 . THR B  107 ? 0.6323 0.6319 0.5909 -0.0478 -0.0556 0.0467  107 THR B CG2 
3356  N N   . LEU B  108 ? 0.6549 0.6589 0.5868 -0.0529 -0.0595 0.0357  108 LEU B N   
3357  C CA  . LEU B  108 ? 0.6138 0.6185 0.5384 -0.0551 -0.0630 0.0373  108 LEU B CA  
3358  C C   . LEU B  108 ? 0.6991 0.7024 0.6183 -0.0570 -0.0596 0.0338  108 LEU B C   
3359  O O   . LEU B  108 ? 0.7553 0.7573 0.6723 -0.0586 -0.0604 0.0370  108 LEU B O   
3360  C CB  . LEU B  108 ? 0.5864 0.5943 0.5041 -0.0556 -0.0676 0.0351  108 LEU B CB  
3361  C CG  . LEU B  108 ? 0.5990 0.6085 0.5210 -0.0540 -0.0713 0.0380  108 LEU B CG  
3362  C CD1 . LEU B  108 ? 0.6173 0.6295 0.5317 -0.0549 -0.0754 0.0356  108 LEU B CD1 
3363  C CD2 . LEU B  108 ? 0.6244 0.6329 0.5524 -0.0540 -0.0739 0.0458  108 LEU B CD2 
3364  N N   . ASP B  109 ? 0.6472 0.6511 0.5644 -0.0568 -0.0558 0.0273  109 ASP B N   
3365  C CA  . ASP B  109 ? 0.6842 0.6871 0.5969 -0.0586 -0.0522 0.0236  109 ASP B CA  
3366  C C   . ASP B  109 ? 0.7174 0.7165 0.6362 -0.0587 -0.0481 0.0267  109 ASP B C   
3367  O O   . ASP B  109 ? 0.7292 0.7267 0.6449 -0.0605 -0.0464 0.0267  109 ASP B O   
3368  C CB  . ASP B  109 ? 0.7877 0.7925 0.6977 -0.0584 -0.0490 0.0163  109 ASP B CB  
3369  C CG  . ASP B  109 ? 1.0493 1.0577 0.9517 -0.0588 -0.0523 0.0127  109 ASP B CG  
3370  O OD1 . ASP B  109 ? 1.0536 1.0625 0.9516 -0.0597 -0.0566 0.0153  109 ASP B OD1 
3371  O OD2 . ASP B  109 ? 1.0127 1.0234 0.9135 -0.0582 -0.0506 0.0074  109 ASP B OD2 
3372  N N   . TYR B  110 ? 0.6682 0.6658 0.5960 -0.0568 -0.0464 0.0294  110 TYR B N   
3373  C CA  . TYR B  110 ? 0.5983 0.5921 0.5333 -0.0566 -0.0422 0.0329  110 TYR B CA  
3374  C C   . TYR B  110 ? 0.8569 0.8493 0.7924 -0.0574 -0.0452 0.0400  110 TYR B C   
3375  O O   . TYR B  110 ? 0.7172 0.7069 0.6529 -0.0585 -0.0425 0.0414  110 TYR B O   
3376  C CB  . TYR B  110 ? 0.5642 0.5567 0.5089 -0.0543 -0.0399 0.0344  110 TYR B CB  
3377  C CG  . TYR B  110 ? 0.6374 0.6257 0.5907 -0.0538 -0.0361 0.0392  110 TYR B CG  
3378  C CD1 . TYR B  110 ? 0.5606 0.5459 0.5161 -0.0545 -0.0295 0.0359  110 TYR B CD1 
3379  C CD2 . TYR B  110 ? 0.6136 0.6012 0.5732 -0.0527 -0.0389 0.0471  110 TYR B CD2 
3380  C CE1 . TYR B  110 ? 0.5062 0.4874 0.4700 -0.0540 -0.0255 0.0403  110 TYR B CE1 
3381  C CE2 . TYR B  110 ? 0.7738 0.7576 0.7419 -0.0520 -0.0352 0.0518  110 TYR B CE2 
3382  C CZ  . TYR B  110 ? 0.7420 0.7223 0.7122 -0.0526 -0.0283 0.0483  110 TYR B CZ  
3383  O OH  . TYR B  110 ? 0.8346 0.8108 0.8135 -0.0519 -0.0242 0.0531  110 TYR B OH  
3384  N N   . HIS B  111 ? 0.7548 0.7492 0.6905 -0.0568 -0.0509 0.0444  111 HIS B N   
3385  C CA  . HIS B  111 ? 0.7062 0.7001 0.6418 -0.0577 -0.0545 0.0514  111 HIS B CA  
3386  C C   . HIS B  111 ? 0.8296 0.8240 0.7552 -0.0604 -0.0559 0.0496  111 HIS B C   
3387  O O   . HIS B  111 ? 0.7636 0.7559 0.6890 -0.0615 -0.0552 0.0534  111 HIS B O   
3388  C CB  . HIS B  111 ? 0.5785 0.5752 0.5159 -0.0568 -0.0606 0.0559  111 HIS B CB  
3389  C CG  . HIS B  111 ? 0.6530 0.6490 0.6013 -0.0543 -0.0597 0.0596  111 HIS B CG  
3390  N ND1 . HIS B  111 ? 0.7515 0.7449 0.7088 -0.0533 -0.0576 0.0658  111 HIS B ND1 
3391  C CD2 . HIS B  111 ? 0.7262 0.7237 0.6785 -0.0524 -0.0604 0.0584  111 HIS B CD2 
3392  C CE1 . HIS B  111 ? 0.7925 0.7859 0.7586 -0.0510 -0.0570 0.0680  111 HIS B CE1 
3393  N NE2 . HIS B  111 ? 0.7451 0.7409 0.7084 -0.0504 -0.0588 0.0635  111 HIS B NE2 
3394  N N   . ASP B  112 ? 0.6869 0.6837 0.6043 -0.0613 -0.0576 0.0440  112 ASP B N   
3395  C CA  . ASP B  112 ? 0.6395 0.6368 0.5472 -0.0638 -0.0584 0.0415  112 ASP B CA  
3396  C C   . ASP B  112 ? 0.7226 0.7170 0.6303 -0.0648 -0.0530 0.0396  112 ASP B C   
3397  O O   . ASP B  112 ? 0.8225 0.8157 0.7256 -0.0668 -0.0533 0.0414  112 ASP B O   
3398  C CB  . ASP B  112 ? 0.8874 0.8877 0.7880 -0.0641 -0.0595 0.0347  112 ASP B CB  
3399  C CG  . ASP B  112 ? 0.8539 0.8547 0.7442 -0.0667 -0.0610 0.0324  112 ASP B CG  
3400  O OD1 . ASP B  112 ? 0.8844 0.8871 0.7692 -0.0671 -0.0604 0.0264  112 ASP B OD1 
3401  O OD2 . ASP B  112 ? 1.0211 1.0207 0.9091 -0.0683 -0.0628 0.0369  112 ASP B OD2 
3402  N N   . SER B  113 ? 0.8123 0.8055 0.7250 -0.0636 -0.0479 0.0361  113 SER B N   
3403  C CA  . SER B  113 ? 0.7596 0.7500 0.6730 -0.0647 -0.0421 0.0337  113 SER B CA  
3404  C C   . SER B  113 ? 0.8323 0.8191 0.7508 -0.0648 -0.0408 0.0403  113 SER B C   
3405  O O   . SER B  113 ? 0.8707 0.8557 0.7857 -0.0666 -0.0390 0.0405  113 SER B O   
3406  C CB  . SER B  113 ? 0.6504 0.6403 0.5689 -0.0634 -0.0370 0.0289  113 SER B CB  
3407  O OG  . SER B  113 ? 0.9003 0.8870 0.8208 -0.0645 -0.0312 0.0273  113 SER B OG  
3408  N N   . ASN B  114 ? 0.7056 0.6914 0.6327 -0.0629 -0.0416 0.0460  114 ASN B N   
3409  C CA  . ASN B  114 ? 0.8477 0.8304 0.7812 -0.0627 -0.0402 0.0530  114 ASN B CA  
3410  C C   . ASN B  114 ? 0.8980 0.8811 0.8256 -0.0645 -0.0443 0.0577  114 ASN B C   
3411  O O   . ASN B  114 ? 0.9235 0.9037 0.8524 -0.0653 -0.0419 0.0610  114 ASN B O   
3412  C CB  . ASN B  114 ? 0.8118 0.7942 0.7556 -0.0601 -0.0411 0.0587  114 ASN B CB  
3413  C CG  . ASN B  114 ? 0.9210 0.9021 0.8714 -0.0584 -0.0360 0.0546  114 ASN B CG  
3414  O OD1 . ASN B  114 ? 0.9619 0.9415 0.9108 -0.0593 -0.0308 0.0487  114 ASN B OD1 
3415  N ND2 . ASN B  114 ? 0.9177 0.8995 0.8756 -0.0562 -0.0374 0.0577  114 ASN B ND2 
3416  N N   . VAL B  115 ? 0.8652 0.8517 0.7862 -0.0652 -0.0503 0.0579  115 VAL B N   
3417  C CA  . VAL B  115 ? 0.8104 0.7976 0.7244 -0.0674 -0.0545 0.0616  115 VAL B CA  
3418  C C   . VAL B  115 ? 0.7907 0.7764 0.6970 -0.0697 -0.0514 0.0569  115 VAL B C   
3419  O O   . VAL B  115 ? 0.8694 0.8529 0.7748 -0.0709 -0.0504 0.0605  115 VAL B O   
3420  C CB  . VAL B  115 ? 0.8124 0.8034 0.7201 -0.0681 -0.0610 0.0614  115 VAL B CB  
3421  C CG1 . VAL B  115 ? 0.9084 0.9000 0.8073 -0.0709 -0.0647 0.0639  115 VAL B CG1 
3422  C CG2 . VAL B  115 ? 0.6760 0.6686 0.5914 -0.0661 -0.0645 0.0668  115 VAL B CG2 
3423  N N   . LYS B  116 ? 0.7434 0.7305 0.6443 -0.0702 -0.0500 0.0491  116 LYS B N   
3424  C CA  . LYS B  116 ? 0.8222 0.8084 0.7162 -0.0722 -0.0468 0.0439  116 LYS B CA  
3425  C C   . LYS B  116 ? 0.8894 0.8716 0.7883 -0.0724 -0.0410 0.0450  116 LYS B C   
3426  O O   . LYS B  116 ? 0.9017 0.8821 0.7960 -0.0744 -0.0396 0.0453  116 LYS B O   
3427  C CB  . LYS B  116 ? 0.8532 0.8417 0.7440 -0.0720 -0.0451 0.0355  116 LYS B CB  
3428  C CG  . LYS B  116 ? 0.7496 0.7372 0.6353 -0.0739 -0.0408 0.0296  116 LYS B CG  
3429  C CD  . LYS B  116 ? 1.0320 1.0215 0.9072 -0.0760 -0.0437 0.0270  116 LYS B CD  
3430  C CE  . LYS B  116 ? 1.1890 1.1785 1.0598 -0.0775 -0.0394 0.0202  116 LYS B CE  
3431  N NZ  . LYS B  116 ? 1.4499 1.4416 1.3110 -0.0793 -0.0419 0.0170  116 LYS B NZ  
3432  N N   . ASN B  117 ? 0.7906 0.7711 0.6987 -0.0704 -0.0373 0.0455  117 ASN B N   
3433  C CA  . ASN B  117 ? 0.9495 0.9259 0.8634 -0.0705 -0.0312 0.0464  117 ASN B CA  
3434  C C   . ASN B  117 ? 0.9707 0.9446 0.8875 -0.0707 -0.0320 0.0547  117 ASN B C   
3435  O O   . ASN B  117 ? 1.0126 0.9834 0.9291 -0.0719 -0.0282 0.0553  117 ASN B O   
3436  C CB  . ASN B  117 ? 0.8484 0.8235 0.7716 -0.0684 -0.0270 0.0450  117 ASN B CB  
3437  C CG  . ASN B  117 ? 0.7706 0.7473 0.6912 -0.0688 -0.0239 0.0362  117 ASN B CG  
3438  O OD1 . ASN B  117 ? 0.6443 0.6225 0.5569 -0.0706 -0.0238 0.0310  117 ASN B OD1 
3439  N ND2 . ASN B  117 ? 1.0292 1.0057 0.9566 -0.0670 -0.0214 0.0345  117 ASN B ND2 
3440  N N   . LEU B  118 ? 0.9481 0.9235 0.8679 -0.0695 -0.0371 0.0614  118 LEU B N   
3441  C CA  . LEU B  118 ? 0.8524 0.8262 0.7750 -0.0696 -0.0388 0.0700  118 LEU B CA  
3442  C C   . LEU B  118 ? 0.8604 0.8344 0.7728 -0.0725 -0.0409 0.0702  118 LEU B C   
3443  O O   . LEU B  118 ? 0.9775 0.9487 0.8905 -0.0733 -0.0388 0.0740  118 LEU B O   
3444  C CB  . LEU B  118 ? 0.9452 0.9216 0.8721 -0.0681 -0.0445 0.0767  118 LEU B CB  
3445  C CG  . LEU B  118 ? 1.0549 1.0294 0.9912 -0.0668 -0.0443 0.0861  118 LEU B CG  
3446  C CD1 . LEU B  118 ? 1.0240 0.9942 0.9699 -0.0651 -0.0367 0.0854  118 LEU B CD1 
3447  C CD2 . LEU B  118 ? 1.0789 1.0566 1.0200 -0.0652 -0.0499 0.0918  118 LEU B CD2 
3448  N N   . TYR B  119 ? 0.8631 0.8403 0.7661 -0.0739 -0.0449 0.0659  119 TYR B N   
3449  C CA  . TYR B  119 ? 0.9419 0.9194 0.8344 -0.0767 -0.0468 0.0650  119 TYR B CA  
3450  C C   . TYR B  119 ? 0.9837 0.9582 0.8740 -0.0780 -0.0407 0.0604  119 TYR B C   
3451  O O   . TYR B  119 ? 1.1562 1.1284 1.0434 -0.0796 -0.0398 0.0634  119 TYR B O   
3452  C CB  . TYR B  119 ? 0.9587 0.9399 0.8424 -0.0778 -0.0511 0.0601  119 TYR B CB  
3453  C CG  . TYR B  119 ? 1.0902 1.0716 0.9627 -0.0808 -0.0526 0.0582  119 TYR B CG  
3454  C CD1 . TYR B  119 ? 1.1572 1.1396 1.0245 -0.0825 -0.0579 0.0636  119 TYR B CD1 
3455  C CD2 . TYR B  119 ? 1.0942 1.0748 0.9614 -0.0821 -0.0487 0.0511  119 TYR B CD2 
3456  C CE1 . TYR B  119 ? 1.2606 1.2428 1.1173 -0.0854 -0.0590 0.0618  119 TYR B CE1 
3457  C CE2 . TYR B  119 ? 1.2835 1.2641 1.1407 -0.0849 -0.0497 0.0494  119 TYR B CE2 
3458  C CZ  . TYR B  119 ? 1.3370 1.3181 1.1888 -0.0865 -0.0548 0.0547  119 TYR B CZ  
3459  O OH  . TYR B  119 ? 1.3405 1.3214 1.1822 -0.0894 -0.0556 0.0528  119 TYR B OH  
3460  N N   . GLU B  120 ? 1.1215 1.0959 1.0131 -0.0775 -0.0364 0.0531  120 GLU B N   
3461  C CA  . GLU B  120 ? 1.1515 1.1235 1.0412 -0.0789 -0.0305 0.0480  120 GLU B CA  
3462  C C   . GLU B  120 ? 0.9838 0.9512 0.8806 -0.0785 -0.0256 0.0525  120 GLU B C   
3463  O O   . GLU B  120 ? 1.2564 1.2214 1.1498 -0.0804 -0.0226 0.0519  120 GLU B O   
3464  C CB  . GLU B  120 ? 1.2253 1.1987 1.1162 -0.0782 -0.0271 0.0398  120 GLU B CB  
3465  C CG  . GLU B  120 ? 1.3115 1.2886 1.1933 -0.0794 -0.0298 0.0335  120 GLU B CG  
3466  C CD  . GLU B  120 ? 1.6302 1.6067 1.5039 -0.0821 -0.0282 0.0303  120 GLU B CD  
3467  O OE1 . GLU B  120 ? 1.5525 1.5256 1.4281 -0.0830 -0.0236 0.0309  120 GLU B OE1 
3468  O OE2 . GLU B  120 ? 1.7480 1.7271 1.6135 -0.0833 -0.0313 0.0272  120 GLU B OE2 
3469  N N   . LYS B  121 ? 0.9564 0.9226 0.8633 -0.0762 -0.0246 0.0570  121 LYS B N   
3470  C CA  . LYS B  121 ? 1.2081 1.1698 1.1229 -0.0756 -0.0196 0.0615  121 LYS B CA  
3471  C C   . LYS B  121 ? 1.2591 1.2193 1.1712 -0.0768 -0.0217 0.0686  121 LYS B C   
3472  O O   . LYS B  121 ? 1.3086 1.2649 1.2229 -0.0774 -0.0170 0.0703  121 LYS B O   
3473  C CB  . LYS B  121 ? 1.1430 1.1039 1.0693 -0.0727 -0.0187 0.0657  121 LYS B CB  
3474  C CG  . LYS B  121 ? 1.3934 1.3492 1.3290 -0.0719 -0.0125 0.0697  121 LYS B CG  
3475  C CD  . LYS B  121 ? 1.5270 1.4820 1.4742 -0.0690 -0.0114 0.0736  121 LYS B CD  
3476  C CE  . LYS B  121 ? 1.5959 1.5456 1.5527 -0.0682 -0.0046 0.0775  121 LYS B CE  
3477  N NZ  . LYS B  121 ? 1.6772 1.6257 1.6458 -0.0653 -0.0032 0.0817  121 LYS B NZ  
3478  N N   . VAL B  122 ? 1.2776 1.2409 1.1850 -0.0771 -0.0287 0.0729  122 VAL B N   
3479  C CA  . VAL B  122 ? 1.2289 1.1916 1.1325 -0.0786 -0.0314 0.0796  122 VAL B CA  
3480  C C   . VAL B  122 ? 1.2739 1.2360 1.1666 -0.0815 -0.0305 0.0748  122 VAL B C   
3481  O O   . VAL B  122 ? 1.5421 1.5014 1.4335 -0.0828 -0.0282 0.0779  122 VAL B O   
3482  C CB  . VAL B  122 ? 1.1037 1.0703 1.0048 -0.0785 -0.0395 0.0852  122 VAL B CB  
3483  C CG1 . VAL B  122 ? 1.2811 1.2478 1.1741 -0.0810 -0.0429 0.0899  122 VAL B CG1 
3484  C CG2 . VAL B  122 ? 1.0595 1.0263 0.9720 -0.0757 -0.0406 0.0924  122 VAL B CG2 
3485  N N   . ARG B  123 ? 1.0941 1.0589 0.9795 -0.0825 -0.0320 0.0674  123 ARG B N   
3486  C CA  . ARG B  123 ? 1.2575 1.2223 1.1324 -0.0853 -0.0315 0.0624  123 ARG B CA  
3487  C C   . ARG B  123 ? 1.2606 1.2218 1.1366 -0.0862 -0.0242 0.0582  123 ARG B C   
3488  O O   . ARG B  123 ? 1.4444 1.4037 1.3149 -0.0883 -0.0228 0.0586  123 ARG B O   
3489  C CB  . ARG B  123 ? 1.3114 1.2801 1.1794 -0.0859 -0.0344 0.0554  123 ARG B CB  
3490  C CG  . ARG B  123 ? 1.3286 1.2978 1.1854 -0.0888 -0.0350 0.0514  123 ARG B CG  
3491  C CD  . ARG B  123 ? 1.4675 1.4392 1.3202 -0.0891 -0.0340 0.0424  123 ARG B CD  
3492  N NE  . ARG B  123 ? 1.6361 1.6065 1.4938 -0.0885 -0.0276 0.0371  123 ARG B NE  
3493  C CZ  . ARG B  123 ? 1.8104 1.7823 1.6642 -0.0894 -0.0252 0.0292  123 ARG B CZ  
3494  N NH1 . ARG B  123 ? 1.6934 1.6681 1.5387 -0.0907 -0.0283 0.0257  123 ARG B NH1 
3495  N NH2 . ARG B  123 ? 1.8653 1.8362 1.7239 -0.0891 -0.0195 0.0247  123 ARG B NH2 
3496  N N   . SER B  124 ? 1.4025 1.3629 1.2855 -0.0848 -0.0194 0.0540  124 SER B N   
3497  C CA  . SER B  124 ? 1.5790 1.5360 1.4635 -0.0858 -0.0122 0.0497  124 SER B CA  
3498  C C   . SER B  124 ? 1.6252 1.5776 1.5170 -0.0852 -0.0085 0.0564  124 SER B C   
3499  O O   . SER B  124 ? 1.6818 1.6307 1.5782 -0.0854 -0.0018 0.0539  124 SER B O   
3500  C CB  . SER B  124 ? 1.6122 1.5700 1.5012 -0.0849 -0.0083 0.0426  124 SER B CB  
3501  O OG  . SER B  124 ? 1.6230 1.5802 1.5217 -0.0823 -0.0079 0.0461  124 SER B OG  
3502  N N   . GLN B  125 ? 1.5050 1.4573 1.3977 -0.0846 -0.0127 0.0650  125 GLN B N   
3503  C CA  . GLN B  125 ? 1.4730 1.4213 1.3731 -0.0837 -0.0098 0.0726  125 GLN B CA  
3504  C C   . GLN B  125 ? 1.6345 1.5824 1.5280 -0.0855 -0.0131 0.0785  125 GLN B C   
3505  O O   . GLN B  125 ? 1.6337 1.5778 1.5278 -0.0864 -0.0090 0.0808  125 GLN B O   
3506  C CB  . GLN B  125 ? 1.2508 1.1996 1.1612 -0.0807 -0.0114 0.0786  125 GLN B CB  
3507  C CG  . GLN B  125 ? 1.3568 1.3013 1.2769 -0.0794 -0.0074 0.0861  125 GLN B CG  
3508  C CD  . GLN B  125 ? 1.6194 1.5646 1.5500 -0.0764 -0.0090 0.0919  125 GLN B CD  
3509  O OE1 . GLN B  125 ? 1.5574 1.5068 1.4867 -0.0756 -0.0152 0.0934  125 GLN B OE1 
3510  N NE2 . GLN B  125 ? 1.7272 1.6683 1.6686 -0.0747 -0.0031 0.0951  125 GLN B NE2 
3511  N N   . LEU B  126 ? 1.5904 1.5422 1.4772 -0.0861 -0.0203 0.0807  126 LEU B N   
3512  C CA  . LEU B  126 ? 1.4317 1.3836 1.3086 -0.0887 -0.0233 0.0831  126 LEU B CA  
3513  C C   . LEU B  126 ? 1.5756 1.5287 1.4429 -0.0909 -0.0226 0.0737  126 LEU B C   
3514  O O   . LEU B  126 ? 1.6761 1.6328 1.5403 -0.0907 -0.0256 0.0689  126 LEU B O   
3515  C CB  . LEU B  126 ? 1.4637 1.4194 1.3371 -0.0889 -0.0314 0.0893  126 LEU B CB  
3516  C CG  . LEU B  126 ? 1.4233 1.3811 1.3056 -0.0862 -0.0350 0.0954  126 LEU B CG  
3517  C CD1 . LEU B  126 ? 1.4477 1.4101 1.3233 -0.0873 -0.0431 0.0978  126 LEU B CD1 
3518  C CD2 . LEU B  126 ? 1.3636 1.3188 1.2560 -0.0844 -0.0331 0.1047  126 LEU B CD2 
3519  N N   . LYS B  127 ? 1.5489 1.4992 1.4120 -0.0929 -0.0184 0.0713  127 LYS B N   
3520  C CA  . LYS B  127 ? 1.5723 1.5238 1.4263 -0.0951 -0.0176 0.0629  127 LYS B CA  
3521  C C   . LYS B  127 ? 1.8450 1.7968 1.6880 -0.0979 -0.0212 0.0651  127 LYS B C   
3522  O O   . LYS B  127 ? 1.7655 1.7206 1.6021 -0.0986 -0.0270 0.0652  127 LYS B O   
3523  C CB  . LYS B  127 ? 1.5413 1.4897 1.3978 -0.0957 -0.0099 0.0570  127 LYS B CB  
3524  C CG  . LYS B  127 ? 1.5532 1.5009 1.4206 -0.0933 -0.0059 0.0552  127 LYS B CG  
3525  C CD  . LYS B  127 ? 1.4954 1.4379 1.3700 -0.0931 0.0010  0.0573  127 LYS B CD  
3526  C CE  . LYS B  127 ? 1.6807 1.6223 1.5660 -0.0909 0.0050  0.0557  127 LYS B CE  
3527  N NZ  . LYS B  127 ? 1.6759 1.6122 1.5686 -0.0908 0.0125  0.0570  127 LYS B NZ  
3528  N N   . ASN B  128 ? 2.1100 2.0582 1.9511 -0.0994 -0.0175 0.0669  128 ASN B N   
3529  C CA  . ASN B  128 ? 2.1274 2.0753 1.9585 -0.1021 -0.0204 0.0697  128 ASN B CA  
3530  C C   . ASN B  128 ? 2.1374 2.0859 1.9692 -0.1018 -0.0256 0.0799  128 ASN B C   
3531  O O   . ASN B  128 ? 2.1706 2.1206 1.9934 -0.1040 -0.0304 0.0821  128 ASN B O   
3532  C CB  . ASN B  128 ? 2.0996 2.0434 1.9284 -0.1040 -0.0145 0.0680  128 ASN B CB  
3533  C CG  . ASN B  128 ? 2.2227 2.1669 2.0485 -0.1051 -0.0104 0.0577  128 ASN B CG  
3534  O OD1 . ASN B  128 ? 2.2404 2.1878 2.0596 -0.1059 -0.0133 0.0523  128 ASN B OD1 
3535  N ND2 . ASN B  128 ? 2.3185 2.2594 2.1490 -0.1051 -0.0035 0.0550  128 ASN B ND2 
3536  N N   . ASN B  129 ? 2.3756 2.3229 2.2180 -0.0993 -0.0247 0.0860  129 ASN B N   
3537  C CA  . ASN B  129 ? 2.4880 2.4359 2.3325 -0.0988 -0.0290 0.0965  129 ASN B CA  
3538  C C   . ASN B  129 ? 2.4546 2.4073 2.2952 -0.0990 -0.0371 0.0989  129 ASN B C   
3539  O O   . ASN B  129 ? 2.3022 2.2563 2.1443 -0.0988 -0.0415 0.1075  129 ASN B O   
3540  C CB  . ASN B  129 ? 2.3327 2.2783 2.1907 -0.0957 -0.0256 0.1022  129 ASN B CB  
3541  C CG  . ASN B  129 ? 2.2395 2.1799 2.1015 -0.0958 -0.0177 0.1012  129 ASN B CG  
3542  O OD1 . ASN B  129 ? 2.1598 2.0974 2.0322 -0.0937 -0.0140 0.1060  129 ASN B OD1 
3543  N ND2 . ASN B  129 ? 2.3266 2.2654 2.1802 -0.0984 -0.0149 0.0951  129 ASN B ND2 
3544  N N   . ALA B  130 ? 2.1090 2.0644 1.9449 -0.0994 -0.0388 0.0913  130 ALA B N   
3545  C CA  . ALA B  130 ? 1.9275 1.8873 1.7592 -0.0998 -0.0460 0.0924  130 ALA B CA  
3546  C C   . ALA B  130 ? 1.7250 1.6869 1.5495 -0.1009 -0.0465 0.0828  130 ALA B C   
3547  O O   . ALA B  130 ? 1.7493 1.7097 1.5737 -0.1009 -0.0415 0.0756  130 ALA B O   
3548  C CB  . ALA B  130 ? 1.8409 1.8027 1.6834 -0.0967 -0.0482 0.0970  130 ALA B CB  
3549  N N   . LYS B  131 ? 1.8772 1.8427 1.6958 -0.1020 -0.0526 0.0829  131 LYS B N   
3550  C CA  . LYS B  131 ? 2.0706 2.0380 1.8823 -0.1030 -0.0534 0.0744  131 LYS B CA  
3551  C C   . LYS B  131 ? 2.1673 2.1385 1.9822 -0.1013 -0.0577 0.0737  131 LYS B C   
3552  O O   . LYS B  131 ? 1.9783 1.9512 1.7966 -0.1006 -0.0622 0.0805  131 LYS B O   
3553  C CB  . LYS B  131 ? 1.9900 1.9575 1.7887 -0.1068 -0.0559 0.0733  131 LYS B CB  
3554  C CG  . LYS B  131 ? 2.0680 2.0381 1.8620 -0.1084 -0.0630 0.0795  131 LYS B CG  
3555  C CD  . LYS B  131 ? 2.0773 2.0478 1.8580 -0.1121 -0.0652 0.0761  131 LYS B CD  
3556  C CE  . LYS B  131 ? 2.0174 1.9909 1.7932 -0.1140 -0.0723 0.0813  131 LYS B CE  
3557  N NZ  . LYS B  131 ? 1.9307 1.9045 1.6934 -0.1178 -0.0743 0.0771  131 LYS B NZ  
3558  N N   . GLU B  132 ? 2.1682 2.1408 1.9821 -0.1006 -0.0563 0.0657  132 GLU B N   
3559  C CA  . GLU B  132 ? 1.9767 1.9528 1.7928 -0.0991 -0.0601 0.0642  132 GLU B CA  
3560  C C   . GLU B  132 ? 1.9622 1.9406 1.7684 -0.1017 -0.0659 0.0646  132 GLU B C   
3561  O O   . GLU B  132 ? 2.0839 2.0614 1.8804 -0.1045 -0.0655 0.0614  132 GLU B O   
3562  C CB  . GLU B  132 ? 2.0446 2.0215 1.8624 -0.0977 -0.0566 0.0554  132 GLU B CB  
3563  C CG  . GLU B  132 ? 2.0099 1.9847 1.8368 -0.0955 -0.0507 0.0537  132 GLU B CG  
3564  C CD  . GLU B  132 ? 2.1159 2.0921 1.9432 -0.0945 -0.0475 0.0450  132 GLU B CD  
3565  O OE1 . GLU B  132 ? 2.0865 2.0611 1.9192 -0.0935 -0.0421 0.0421  132 GLU B OE1 
3566  O OE2 . GLU B  132 ? 2.1678 2.1468 1.9901 -0.0949 -0.0504 0.0410  132 GLU B OE2 
3567  N N   . ILE B  133 ? 1.8003 1.7814 1.6090 -0.1010 -0.0710 0.0685  133 ILE B N   
3568  C CA  . ILE B  133 ? 1.9828 1.9662 1.7827 -0.1035 -0.0764 0.0684  133 ILE B CA  
3569  C C   . ILE B  133 ? 2.0144 1.9998 1.8126 -0.1027 -0.0764 0.0607  133 ILE B C   
3570  O O   . ILE B  133 ? 2.0845 2.0707 1.8735 -0.1051 -0.0782 0.0570  133 ILE B O   
3571  C CB  . ILE B  133 ? 1.9614 1.9472 1.7645 -0.1034 -0.0823 0.0766  133 ILE B CB  
3572  C CG1 . ILE B  133 ? 1.9181 1.9024 1.7226 -0.1043 -0.0826 0.0849  133 ILE B CG1 
3573  C CG2 . ILE B  133 ? 1.8828 1.8711 1.6766 -0.1063 -0.0877 0.0758  133 ILE B CG2 
3574  C CD1 . ILE B  133 ? 2.0298 2.0127 1.8226 -0.1083 -0.0834 0.0854  133 ILE B CD1 
3575  N N   . GLY B  134 ? 1.8531 1.8393 1.6604 -0.0993 -0.0743 0.0585  134 GLY B N   
3576  C CA  . GLY B  134 ? 1.7629 1.7511 1.5699 -0.0981 -0.0741 0.0517  134 GLY B CA  
3577  C C   . GLY B  134 ? 1.6036 1.5945 1.4168 -0.0961 -0.0780 0.0545  134 GLY B C   
3578  O O   . GLY B  134 ? 1.4692 1.4617 1.2854 -0.0942 -0.0774 0.0498  134 GLY B O   
3579  N N   . ASN B  135 ? 1.4887 1.4802 1.3042 -0.0966 -0.0821 0.0623  135 ASN B N   
3580  C CA  . ASN B  135 ? 1.3348 1.3290 1.1564 -0.0948 -0.0861 0.0657  135 ASN B CA  
3581  C C   . ASN B  135 ? 1.2806 1.2741 1.1147 -0.0915 -0.0839 0.0700  135 ASN B C   
3582  O O   . ASN B  135 ? 0.9652 0.9603 0.8053 -0.0904 -0.0873 0.0760  135 ASN B O   
3583  C CB  . ASN B  135 ? 1.4374 1.4333 1.2539 -0.0975 -0.0923 0.0717  135 ASN B CB  
3584  C CG  . ASN B  135 ? 1.6163 1.6155 1.4371 -0.0964 -0.0968 0.0737  135 ASN B CG  
3585  O OD1 . ASN B  135 ? 1.4708 1.4708 1.2974 -0.0936 -0.0953 0.0701  135 ASN B OD1 
3586  N ND2 . ASN B  135 ? 1.8352 1.8365 1.6531 -0.0987 -0.1024 0.0795  135 ASN B ND2 
3587  N N   . GLY B  136 ? 1.2585 1.2495 1.0964 -0.0901 -0.0781 0.0668  136 GLY B N   
3588  C CA  . GLY B  136 ? 1.2033 1.1928 1.0526 -0.0872 -0.0750 0.0703  136 GLY B CA  
3589  C C   . GLY B  136 ? 1.4283 1.4163 1.2802 -0.0879 -0.0758 0.0789  136 GLY B C   
3590  O O   . GLY B  136 ? 1.3685 1.3557 1.2306 -0.0856 -0.0746 0.0840  136 GLY B O   
3591  N N   . CYS B  137 ? 1.7623 1.7499 1.6051 -0.0910 -0.0777 0.0805  137 CYS B N   
3592  C CA  . CYS B  137 ? 1.6286 1.6152 1.4724 -0.0921 -0.0790 0.0889  137 CYS B CA  
3593  C C   . CYS B  137 ? 1.6638 1.6469 1.5023 -0.0939 -0.0748 0.0875  137 CYS B C   
3594  O O   . CYS B  137 ? 1.6767 1.6593 1.5064 -0.0958 -0.0735 0.0810  137 CYS B O   
3595  C CB  . CYS B  137 ? 1.5065 1.4962 1.3441 -0.0946 -0.0861 0.0937  137 CYS B CB  
3596  S SG  . CYS B  137 ? 1.8741 1.8640 1.7141 -0.0956 -0.0892 0.1053  137 CYS B SG  
3597  N N   . PHE B  138 ? 1.5568 1.5376 1.4008 -0.0932 -0.0727 0.0938  138 PHE B N   
3598  C CA  . PHE B  138 ? 1.7485 1.7259 1.5883 -0.0948 -0.0686 0.0933  138 PHE B CA  
3599  C C   . PHE B  138 ? 1.8842 1.8617 1.7192 -0.0973 -0.0723 0.1013  138 PHE B C   
3600  O O   . PHE B  138 ? 1.8006 1.7806 1.6393 -0.0968 -0.0770 0.1087  138 PHE B O   
3601  C CB  . PHE B  138 ? 1.6762 1.6501 1.5262 -0.0923 -0.0620 0.0937  138 PHE B CB  
3602  C CG  . PHE B  138 ? 1.5900 1.5636 1.4445 -0.0902 -0.0578 0.0858  138 PHE B CG  
3603  C CD1 . PHE B  138 ? 1.4394 1.4148 1.3022 -0.0875 -0.0588 0.0861  138 PHE B CD1 
3604  C CD2 . PHE B  138 ? 1.5764 1.5479 1.4266 -0.0912 -0.0528 0.0781  138 PHE B CD2 
3605  C CE1 . PHE B  138 ? 1.4606 1.4357 1.3271 -0.0858 -0.0549 0.0789  138 PHE B CE1 
3606  C CE2 . PHE B  138 ? 1.3965 1.3682 1.2506 -0.0895 -0.0491 0.0709  138 PHE B CE2 
3607  C CZ  . PHE B  138 ? 1.4241 1.3975 1.2861 -0.0868 -0.0502 0.0714  138 PHE B CZ  
3608  N N   . GLU B  139 ? 2.0373 2.0124 1.8640 -0.0999 -0.0702 0.0998  139 GLU B N   
3609  C CA  . GLU B  139 ? 1.8713 1.8462 1.6934 -0.1022 -0.0730 0.1074  139 GLU B CA  
3610  C C   . GLU B  139 ? 1.7922 1.7627 1.6169 -0.1019 -0.0672 0.1095  139 GLU B C   
3611  O O   . GLU B  139 ? 1.8440 1.8117 1.6649 -0.1028 -0.0623 0.1030  139 GLU B O   
3612  C CB  . GLU B  139 ? 1.9430 1.9191 1.7508 -0.1063 -0.0767 0.1047  139 GLU B CB  
3613  C CG  . GLU B  139 ? 2.2359 2.2119 2.0379 -0.1091 -0.0796 0.1124  139 GLU B CG  
3614  C CD  . GLU B  139 ? 2.2394 2.2172 2.0278 -0.1133 -0.0843 0.1106  139 GLU B CD  
3615  O OE1 . GLU B  139 ? 2.0225 2.0016 1.8063 -0.1139 -0.0851 0.1033  139 GLU B OE1 
3616  O OE2 . GLU B  139 ? 2.2726 2.2505 2.0548 -0.1161 -0.0870 0.1165  139 GLU B OE2 
3617  N N   . PHE B  140 ? 2.0951 2.0652 1.9270 -0.1008 -0.0678 0.1188  140 PHE B N   
3618  C CA  . PHE B  140 ? 2.2062 2.1721 2.0421 -0.1002 -0.0623 0.1219  140 PHE B CA  
3619  C C   . PHE B  140 ? 2.2834 2.2476 2.1083 -0.1038 -0.0625 0.1233  140 PHE B C   
3620  O O   . PHE B  140 ? 2.2494 2.2162 2.0669 -0.1063 -0.0683 0.1278  140 PHE B O   
3621  C CB  . PHE B  140 ? 2.2217 2.1877 2.0695 -0.0976 -0.0628 0.1320  140 PHE B CB  
3622  C CG  . PHE B  140 ? 2.1594 2.1257 2.0195 -0.0938 -0.0607 0.1308  140 PHE B CG  
3623  C CD1 . PHE B  140 ? 2.1228 2.0934 1.9869 -0.0926 -0.0661 0.1335  140 PHE B CD1 
3624  C CD2 . PHE B  140 ? 2.1395 2.1018 2.0071 -0.0917 -0.0532 0.1268  140 PHE B CD2 
3625  C CE1 . PHE B  140 ? 2.0575 2.0282 1.9329 -0.0892 -0.0640 0.1325  140 PHE B CE1 
3626  C CE2 . PHE B  140 ? 2.0720 2.0344 1.9506 -0.0885 -0.0511 0.1256  140 PHE B CE2 
3627  C CZ  . PHE B  140 ? 2.0026 1.9691 1.8851 -0.0871 -0.0565 0.1285  140 PHE B CZ  
3628  N N   . TYR B  141 ? 2.0309 1.9909 1.8548 -0.1042 -0.0561 0.1194  141 TYR B N   
3629  C CA  . TYR B  141 ? 1.9797 1.9373 1.7948 -0.1072 -0.0553 0.1216  141 TYR B CA  
3630  C C   . TYR B  141 ? 1.8833 1.8389 1.7059 -0.1059 -0.0537 0.1315  141 TYR B C   
3631  O O   . TYR B  141 ? 2.0691 2.0236 1.8859 -0.1081 -0.0545 0.1365  141 TYR B O   
3632  C CB  . TYR B  141 ? 1.9742 1.9283 1.7846 -0.1083 -0.0490 0.1128  141 TYR B CB  
3633  C CG  . TYR B  141 ? 1.8715 1.8275 1.6740 -0.1098 -0.0502 0.1031  141 TYR B CG  
3634  C CD1 . TYR B  141 ? 1.7216 1.6764 1.5267 -0.1085 -0.0451 0.0942  141 TYR B CD1 
3635  C CD2 . TYR B  141 ? 1.7926 1.7517 1.5849 -0.1124 -0.0562 0.1030  141 TYR B CD2 
3636  C CE1 . TYR B  141 ? 1.7110 1.6678 1.5093 -0.1097 -0.0460 0.0859  141 TYR B CE1 
3637  C CE2 . TYR B  141 ? 1.7393 1.6998 1.5247 -0.1136 -0.0569 0.0944  141 TYR B CE2 
3638  C CZ  . TYR B  141 ? 1.7625 1.7219 1.5512 -0.1121 -0.0518 0.0860  141 TYR B CZ  
3639  O OH  . TYR B  141 ? 1.6986 1.6598 1.4810 -0.1131 -0.0524 0.0778  141 TYR B OH  
3640  N N   . HIS B  142 ? 2.0614 2.0165 1.8973 -0.1022 -0.0512 0.1342  142 HIS B N   
3641  C CA  . HIS B  142 ? 1.9995 1.9523 1.8445 -0.1005 -0.0488 0.1434  142 HIS B CA  
3642  C C   . HIS B  142 ? 2.0192 1.9757 1.8728 -0.0983 -0.0539 0.1519  142 HIS B C   
3643  O O   . HIS B  142 ? 2.1357 2.0939 1.9967 -0.0958 -0.0542 0.1496  142 HIS B O   
3644  C CB  . HIS B  142 ? 1.9620 1.9099 1.8163 -0.0981 -0.0402 0.1396  142 HIS B CB  
3645  C CG  . HIS B  142 ? 2.0295 1.9777 1.8983 -0.0942 -0.0389 0.1431  142 HIS B CG  
3646  N ND1 . HIS B  142 ? 2.0416 1.9890 1.9200 -0.0922 -0.0384 0.1534  142 HIS B ND1 
3647  C CD2 . HIS B  142 ? 2.0934 2.0426 1.9686 -0.0920 -0.0378 0.1379  142 HIS B CD2 
3648  C CE1 . HIS B  142 ? 2.0483 1.9959 1.9386 -0.0889 -0.0369 0.1542  142 HIS B CE1 
3649  N NE2 . HIS B  142 ? 2.1013 2.0500 1.9896 -0.0888 -0.0366 0.1447  142 HIS B NE2 
3650  N N   . LYS B  143 ? 1.9781 1.9361 1.8310 -0.0992 -0.0577 0.1621  143 LYS B N   
3651  C CA  . LYS B  143 ? 1.9353 1.8975 1.7961 -0.0974 -0.0631 0.1712  143 LYS B CA  
3652  C C   . LYS B  143 ? 1.9151 1.8763 1.7912 -0.0930 -0.0595 0.1718  143 LYS B C   
3653  O O   . LYS B  143 ? 1.8597 1.8169 1.7452 -0.0908 -0.0534 0.1747  143 LYS B O   
3654  C CB  . LYS B  143 ? 1.9547 1.9175 1.8157 -0.0982 -0.0655 0.1829  143 LYS B CB  
3655  C CG  . LYS B  143 ? 2.0134 1.9786 1.8592 -0.1028 -0.0710 0.1840  143 LYS B CG  
3656  C CD  . LYS B  143 ? 2.1301 2.1019 1.9725 -0.1042 -0.0800 0.1879  143 LYS B CD  
3657  C CE  . LYS B  143 ? 2.0725 2.0462 1.9096 -0.1050 -0.0821 0.1779  143 LYS B CE  
3658  N NZ  . LYS B  143 ? 1.9707 1.9506 1.8043 -0.1066 -0.0907 0.1814  143 LYS B NZ  
3659  N N   . CYS B  144 ? 1.9859 1.9508 1.8643 -0.0920 -0.0632 0.1691  144 CYS B N   
3660  C CA  . CYS B  144 ? 2.1099 2.0743 2.0022 -0.0880 -0.0603 0.1691  144 CYS B CA  
3661  C C   . CYS B  144 ? 1.9740 1.9430 1.8747 -0.0862 -0.0660 0.1786  144 CYS B C   
3662  O O   . CYS B  144 ? 1.9506 1.9242 1.8489 -0.0867 -0.0718 0.1773  144 CYS B O   
3663  C CB  . CYS B  144 ? 2.0813 2.0461 1.9715 -0.0877 -0.0591 0.1579  144 CYS B CB  
3664  S SG  . CYS B  144 ? 2.1693 2.1280 2.0636 -0.0863 -0.0490 0.1487  144 CYS B SG  
3665  N N   . ASP B  145 ? 2.2080 2.1758 2.1192 -0.0841 -0.0640 0.1881  145 ASP B N   
3666  C CA  . ASP B  145 ? 2.2496 2.2217 2.1705 -0.0821 -0.0688 0.1978  145 ASP B CA  
3667  C C   . ASP B  145 ? 2.1800 2.1519 2.1134 -0.0784 -0.0661 0.1952  145 ASP B C   
3668  O O   . ASP B  145 ? 2.2864 2.2559 2.2183 -0.0780 -0.0623 0.1851  145 ASP B O   
3669  C CB  . ASP B  145 ? 2.4581 2.4295 2.3856 -0.0811 -0.0681 0.2097  145 ASP B CB  
3670  C CG  . ASP B  145 ? 2.4746 2.4391 2.4084 -0.0794 -0.0586 0.2087  145 ASP B CG  
3671  O OD1 . ASP B  145 ? 2.3237 2.2869 2.2670 -0.0775 -0.0566 0.2184  145 ASP B OD1 
3672  O OD2 . ASP B  145 ? 2.4487 2.4089 2.3780 -0.0801 -0.0532 0.1986  145 ASP B OD2 
3673  N N   . ASN B  146 ? 2.0139 1.9883 1.9593 -0.0757 -0.0682 0.2044  146 ASN B N   
3674  C CA  . ASN B  146 ? 1.9257 1.9004 1.8830 -0.0723 -0.0665 0.2031  146 ASN B CA  
3675  C C   . ASN B  146 ? 2.0328 2.0011 1.9993 -0.0696 -0.0568 0.1982  146 ASN B C   
3676  O O   . ASN B  146 ? 2.1310 2.0983 2.0997 -0.0684 -0.0543 0.1902  146 ASN B O   
3677  C CB  . ASN B  146 ? 1.6570 1.6361 1.6257 -0.0702 -0.0709 0.2150  146 ASN B CB  
3678  C CG  . ASN B  146 ? 1.6889 1.6753 1.6505 -0.0725 -0.0809 0.2180  146 ASN B CG  
3679  O OD1 . ASN B  146 ? 1.7520 1.7429 1.7207 -0.0716 -0.0857 0.2280  146 ASN B OD1 
3680  N ND2 . ASN B  146 ? 1.7252 1.7129 1.6729 -0.0757 -0.0840 0.2096  146 ASN B ND2 
3681  N N   . THR B  147 ? 2.1933 2.1572 2.1652 -0.0686 -0.0513 0.2031  147 THR B N   
3682  C CA  . THR B  147 ? 2.2661 2.2235 2.2455 -0.0667 -0.0416 0.1980  147 THR B CA  
3683  C C   . THR B  147 ? 2.2227 2.1769 2.1903 -0.0693 -0.0381 0.1865  147 THR B C   
3684  O O   . THR B  147 ? 2.2028 2.1521 2.1740 -0.0684 -0.0305 0.1797  147 THR B O   
3685  C CB  . THR B  147 ? 2.2345 2.1878 2.2233 -0.0650 -0.0362 0.2066  147 THR B CB  
3686  O OG1 . THR B  147 ? 2.3269 2.2795 2.3055 -0.0678 -0.0372 0.2086  147 THR B OG1 
3687  N N   . CYS B  148 ? 2.0231 1.9801 1.9766 -0.0727 -0.0434 0.1844  148 CYS B N   
3688  C CA  . CYS B  148 ? 2.0633 2.0182 2.0052 -0.0752 -0.0411 0.1732  148 CYS B CA  
3689  C C   . CYS B  148 ? 2.1742 2.1323 2.1125 -0.0754 -0.0441 0.1648  148 CYS B C   
3690  O O   . CYS B  148 ? 2.1704 2.1267 2.1028 -0.0764 -0.0410 0.1546  148 CYS B O   
3691  C CB  . CYS B  148 ? 2.0505 2.0063 1.9790 -0.0789 -0.0446 0.1745  148 CYS B CB  
3692  S SG  . CYS B  148 ? 2.1840 2.1421 2.0958 -0.0825 -0.0481 0.1628  148 CYS B SG  
3693  N N   . MET B  149 ? 2.1543 2.1173 2.0959 -0.0744 -0.0505 0.1695  149 MET B N   
3694  C CA  . MET B  149 ? 1.9927 1.9583 1.9344 -0.0736 -0.0526 0.1630  149 MET B CA  
3695  C C   . MET B  149 ? 1.9016 1.8632 1.8528 -0.0710 -0.0450 0.1574  149 MET B C   
3696  O O   . MET B  149 ? 1.8900 1.8497 1.8361 -0.0718 -0.0415 0.1474  149 MET B O   
3697  C CB  . MET B  149 ? 1.8868 1.8579 1.8334 -0.0725 -0.0597 0.1704  149 MET B CB  
3698  C CG  . MET B  149 ? 1.8528 1.8290 1.7874 -0.0758 -0.0681 0.1716  149 MET B CG  
3699  S SD  . MET B  149 ? 1.9145 1.8886 1.8324 -0.0795 -0.0666 0.1608  149 MET B SD  
3700  C CE  . MET B  149 ? 1.7519 1.7322 1.6575 -0.0829 -0.0765 0.1611  149 MET B CE  
3701  N N   . GLU B  150 ? 2.5925 2.5528 2.5576 -0.0679 -0.0423 0.1641  150 GLU B N   
3702  C CA  . GLU B  150 ? 2.6121 2.5691 2.5876 -0.0652 -0.0357 0.1598  150 GLU B CA  
3703  C C   . GLU B  150 ? 2.6288 2.5805 2.6017 -0.0660 -0.0277 0.1506  150 GLU B C   
3704  O O   . GLU B  150 ? 2.6017 2.5526 2.5756 -0.0654 -0.0247 0.1425  150 GLU B O   
3705  C CB  . GLU B  150 ? 2.6681 2.6235 2.6590 -0.0620 -0.0330 0.1694  150 GLU B CB  
3706  C CG  . GLU B  150 ? 2.7448 2.7026 2.7456 -0.0593 -0.0347 0.1711  150 GLU B CG  
3707  C CD  . GLU B  150 ? 2.7708 2.7352 2.7708 -0.0594 -0.0440 0.1786  150 GLU B CD  
3708  O OE1 . GLU B  150 ? 2.6645 2.6321 2.6674 -0.0583 -0.0473 0.1773  150 GLU B OE1 
3709  O OE2 . GLU B  150 ? 2.7284 2.6948 2.7247 -0.0608 -0.0480 0.1859  150 GLU B OE2 
3710  N N   . SER B  151 ? 2.1775 2.1257 2.1473 -0.0674 -0.0241 0.1520  151 SER B N   
3711  C CA  . SER B  151 ? 2.1575 2.1006 2.1251 -0.0684 -0.0163 0.1436  151 SER B CA  
3712  C C   . SER B  151 ? 2.0811 2.0261 2.0401 -0.0698 -0.0172 0.1322  151 SER B C   
3713  O O   . SER B  151 ? 2.2002 2.1423 2.1607 -0.0698 -0.0110 0.1244  151 SER B O   
3714  C CB  . SER B  151 ? 2.1524 2.0930 2.1134 -0.0706 -0.0146 0.1455  151 SER B CB  
3715  O OG  . SER B  151 ? 2.1237 2.0678 2.0708 -0.0736 -0.0206 0.1429  151 SER B OG  
3716  N N   . VAL B  152 ? 1.7587 1.7089 1.7091 -0.0711 -0.0250 0.1317  152 VAL B N   
3717  C CA  . VAL B  152 ? 1.7284 1.6812 1.6711 -0.0722 -0.0269 0.1221  152 VAL B CA  
3718  C C   . VAL B  152 ? 1.7170 1.6712 1.6680 -0.0696 -0.0268 0.1203  152 VAL B C   
3719  O O   . VAL B  152 ? 1.5740 1.5272 1.5249 -0.0694 -0.0230 0.1119  152 VAL B O   
3720  C CB  . VAL B  152 ? 1.5170 1.4745 1.4479 -0.0745 -0.0350 0.1225  152 VAL B CB  
3721  C CG1 . VAL B  152 ? 1.3045 1.2639 1.2265 -0.0759 -0.0358 0.1120  152 VAL B CG1 
3722  C CG2 . VAL B  152 ? 1.6334 1.5897 1.5572 -0.0769 -0.0358 0.1266  152 VAL B CG2 
3723  N N   . LYS B  153 ? 1.6392 1.5959 1.5974 -0.0677 -0.0311 0.1283  153 LYS B N   
3724  C CA  . LYS B  153 ? 1.5758 1.5338 1.5427 -0.0651 -0.0311 0.1276  153 LYS B CA  
3725  C C   . LYS B  153 ? 1.8458 1.7988 1.8230 -0.0632 -0.0223 0.1250  153 LYS B C   
3726  O O   . LYS B  153 ? 1.9511 1.9036 1.9289 -0.0627 -0.0195 0.1174  153 LYS B O   
3727  C CB  . LYS B  153 ? 1.4838 1.4453 1.4576 -0.0634 -0.0369 0.1376  153 LYS B CB  
3728  C CG  . LYS B  153 ? 1.3109 1.2779 1.2751 -0.0654 -0.0459 0.1396  153 LYS B CG  
3729  C CD  . LYS B  153 ? 1.3874 1.3583 1.3595 -0.0636 -0.0514 0.1485  153 LYS B CD  
3730  C CE  . LYS B  153 ? 1.3216 1.2980 1.2840 -0.0660 -0.0603 0.1508  153 LYS B CE  
3731  N NZ  . LYS B  153 ? 1.4498 1.4260 1.4041 -0.0686 -0.0622 0.1547  153 LYS B NZ  
3732  N N   . ASN B  154 ? 2.5239 2.4731 2.5092 -0.0622 -0.0180 0.1317  154 ASN B N   
3733  C CA  . ASN B  154 ? 2.6090 2.5527 2.6041 -0.0606 -0.0091 0.1296  154 ASN B CA  
3734  C C   . ASN B  154 ? 2.6285 2.5694 2.6170 -0.0627 -0.0035 0.1188  154 ASN B C   
3735  O O   . ASN B  154 ? 2.6944 2.6313 2.6893 -0.0620 0.0039  0.1147  154 ASN B O   
3736  C CB  . ASN B  154 ? 2.6943 2.6342 2.6979 -0.0596 -0.0053 0.1386  154 ASN B CB  
3737  C CG  . ASN B  154 ? 2.6765 2.6185 2.6909 -0.0568 -0.0087 0.1492  154 ASN B CG  
3738  O OD1 . ASN B  154 ? 2.6924 2.6386 2.7039 -0.0572 -0.0159 0.1562  154 ASN B OD1 
3739  N ND2 . ASN B  154 ? 2.6364 2.5756 2.6636 -0.0541 -0.0035 0.1504  154 ASN B ND2 
3740  N N   . GLY B  155 ? 2.1747 2.1178 2.1503 -0.0654 -0.0069 0.1142  155 GLY B N   
3741  C CA  . GLY B  155 ? 2.1484 2.0896 2.1171 -0.0675 -0.0023 0.1042  155 GLY B CA  
3742  C C   . GLY B  155 ? 2.2375 2.1735 2.2075 -0.0686 0.0044  0.1050  155 GLY B C   
3743  O O   . GLY B  155 ? 2.1479 2.0818 2.1131 -0.0705 0.0090  0.0972  155 GLY B O   
3744  N N   . THR B  156 ? 2.4584 2.3923 2.4353 -0.0673 0.0049  0.1146  156 THR B N   
3745  C CA  . THR B  156 ? 2.4964 2.4251 2.4753 -0.0682 0.0111  0.1167  156 THR B CA  
3746  C C   . THR B  156 ? 2.2954 2.2255 2.2650 -0.0702 0.0065  0.1209  156 THR B C   
3747  O O   . THR B  156 ? 2.2134 2.1435 2.1868 -0.0692 0.0044  0.1307  156 THR B O   
3748  C CB  . THR B  156 ? 2.6087 2.5336 2.6020 -0.0654 0.0155  0.1251  156 THR B CB  
3749  O OG1 . THR B  156 ? 2.5377 2.4663 2.5349 -0.0635 0.0087  0.1348  156 THR B OG1 
3750  C CG2 . THR B  156 ? 2.6646 2.5868 2.6669 -0.0638 0.0217  0.1202  156 THR B CG2 
3751  N N   . TYR B  157 ? 2.1211 2.0527 2.0786 -0.0729 0.0052  0.1134  157 TYR B N   
3752  C CA  . TYR B  157 ? 2.0142 1.9472 1.9614 -0.0752 0.0009  0.1161  157 TYR B CA  
3753  C C   . TYR B  157 ? 2.1237 2.0520 2.0678 -0.0772 0.0074  0.1129  157 TYR B C   
3754  O O   . TYR B  157 ? 1.9894 1.9166 1.9296 -0.0787 0.0115  0.1035  157 TYR B O   
3755  C CB  . TYR B  157 ? 1.9365 1.8746 1.8718 -0.0770 -0.0056 0.1102  157 TYR B CB  
3756  C CG  . TYR B  157 ? 1.7796 1.7197 1.7039 -0.0795 -0.0109 0.1130  157 TYR B CG  
3757  C CD1 . TYR B  157 ? 1.8047 1.7486 1.7275 -0.0792 -0.0184 0.1210  157 TYR B CD1 
3758  C CD2 . TYR B  157 ? 1.7071 1.6456 1.6222 -0.0822 -0.0084 0.1076  157 TYR B CD2 
3759  C CE1 . TYR B  157 ? 1.7240 1.6696 1.6361 -0.0818 -0.0231 0.1233  157 TYR B CE1 
3760  C CE2 . TYR B  157 ? 1.7583 1.6983 1.6630 -0.0846 -0.0129 0.1100  157 TYR B CE2 
3761  C CZ  . TYR B  157 ? 1.6814 1.6249 1.5845 -0.0845 -0.0203 0.1178  157 TYR B CZ  
3762  O OH  . TYR B  157 ? 1.5189 1.4639 1.4112 -0.0871 -0.0247 0.1201  157 TYR B OH  
3763  N N   . ASP B  158 ? 2.0228 1.9485 1.9687 -0.0773 0.0084  0.1208  158 ASP B N   
3764  C CA  . ASP B  158 ? 1.9210 1.8422 1.8637 -0.0792 0.0143  0.1186  158 ASP B CA  
3765  C C   . ASP B  158 ? 1.6413 1.5648 1.5697 -0.0825 0.0113  0.1121  158 ASP B C   
3766  O O   . ASP B  158 ? 1.8426 1.7710 1.7641 -0.0831 0.0051  0.1091  158 ASP B O   
3767  C CB  . ASP B  158 ? 1.6312 1.5497 1.5783 -0.0785 0.0150  0.1295  158 ASP B CB  
3768  C CG  . ASP B  158 ? 1.7967 1.7149 1.7572 -0.0751 0.0151  0.1383  158 ASP B CG  
3769  O OD1 . ASP B  158 ? 1.5917 1.5048 1.5623 -0.0737 0.0223  0.1410  158 ASP B OD1 
3770  O OD2 . ASP B  158 ? 1.6011 1.5242 1.5622 -0.0739 0.0080  0.1424  158 ASP B OD2 
3771  N N   . TYR B  159 ? 1.5976 1.5175 1.5218 -0.0846 0.0160  0.1099  159 TYR B N   
3772  C CA  . TYR B  159 ? 1.6411 1.5629 1.5518 -0.0877 0.0131  0.1050  159 TYR B CA  
3773  C C   . TYR B  159 ? 1.8758 1.7939 1.7821 -0.0896 0.0161  0.1079  159 TYR B C   
3774  O O   . TYR B  159 ? 1.8886 1.8049 1.7892 -0.0919 0.0201  0.1008  159 TYR B O   
3775  C CB  . TYR B  159 ? 1.5403 1.4634 1.4464 -0.0890 0.0152  0.0930  159 TYR B CB  
3776  C CG  . TYR B  159 ? 1.2841 1.2118 1.1775 -0.0911 0.0090  0.0888  159 TYR B CG  
3777  C CD1 . TYR B  159 ? 1.3679 1.3005 1.2589 -0.0903 0.0014  0.0908  159 TYR B CD1 
3778  C CD2 . TYR B  159 ? 1.3304 1.2573 1.2145 -0.0940 0.0108  0.0831  159 TYR B CD2 
3779  C CE1 . TYR B  159 ? 1.4269 1.3633 1.3065 -0.0923 -0.0039 0.0870  159 TYR B CE1 
3780  C CE2 . TYR B  159 ? 1.4454 1.3762 1.3182 -0.0959 0.0054  0.0794  159 TYR B CE2 
3781  C CZ  . TYR B  159 ? 1.4548 1.3903 1.3254 -0.0951 -0.0018 0.0813  159 TYR B CZ  
3782  O OH  . TYR B  159 ? 1.4617 1.4007 1.3213 -0.0970 -0.0067 0.0776  159 TYR B OH  
3783  N N   . PRO B  160 ? 2.0174 1.9348 1.9260 -0.0889 0.0138  0.1185  160 PRO B N   
3784  C CA  . PRO B  160 ? 2.2086 2.1226 2.1132 -0.0906 0.0162  0.1224  160 PRO B CA  
3785  C C   . PRO B  160 ? 2.1069 2.0242 1.9989 -0.0930 0.0093  0.1251  160 PRO B C   
3786  O O   . PRO B  160 ? 2.0818 1.9964 1.9699 -0.0945 0.0107  0.1291  160 PRO B O   
3787  C CB  . PRO B  160 ? 2.3297 2.2413 2.2455 -0.0880 0.0177  0.1337  160 PRO B CB  
3788  C CG  . PRO B  160 ? 2.1595 2.0744 2.0836 -0.0851 0.0141  0.1365  160 PRO B CG  
3789  C CD  . PRO B  160 ? 2.1082 2.0278 2.0246 -0.0862 0.0093  0.1279  160 PRO B CD  
3790  N N   . LYS B  161 ? 1.8234 1.7459 1.7090 -0.0935 0.0021  0.1230  161 LYS B N   
3791  C CA  . LYS B  161 ? 1.5864 1.5122 1.4628 -0.0953 -0.0053 0.1288  161 LYS B CA  
3792  C C   . LYS B  161 ? 1.6835 1.6109 1.5451 -0.0988 -0.0081 0.1226  161 LYS B C   
3793  O O   . LYS B  161 ? 1.2085 1.1362 1.0659 -0.0999 -0.0060 0.1128  161 LYS B O   
3794  C CB  . LYS B  161 ? 0.9734 0.9042 0.8529 -0.0936 -0.0125 0.1336  161 LYS B CB  
3795  C CG  . LYS B  161 ? 1.3657 1.2953 1.2600 -0.0899 -0.0101 0.1392  161 LYS B CG  
3796  C CD  . LYS B  161 ? 1.3090 1.2441 1.2059 -0.0884 -0.0177 0.1440  161 LYS B CD  
3797  C CE  . LYS B  161 ? 1.5428 1.4776 1.4511 -0.0858 -0.0183 0.1558  161 LYS B CE  
3798  N NZ  . LYS B  161 ? 1.0507 0.9896 0.9667 -0.0833 -0.0229 0.1594  161 LYS B NZ  
3799  N N   . TYR B  162 ? 1.9215 1.8500 1.7755 -0.1007 -0.0126 0.1290  162 TYR B N   
3800  C CA  . TYR B  162 ? 1.6627 1.5944 1.5030 -0.1038 -0.0182 0.1258  162 TYR B CA  
3801  C C   . TYR B  162 ? 1.1957 1.1296 1.0319 -0.1049 -0.0245 0.1360  162 TYR B C   
3802  O O   . TYR B  162 ? 0.8456 0.7788 0.6900 -0.1030 -0.0245 0.1453  162 TYR B O   
3803  C CB  . TYR B  162 ? 1.4666 1.3956 1.2977 -0.1067 -0.0140 0.1183  162 TYR B CB  
3804  C CG  . TYR B  162 ? 1.6642 1.5961 1.4813 -0.1100 -0.0195 0.1157  162 TYR B CG  
3805  C CD1 . TYR B  162 ? 1.4923 1.4250 1.3023 -0.1120 -0.0241 0.1232  162 TYR B CD1 
3806  C CD2 . TYR B  162 ? 1.5841 1.5180 1.3951 -0.1111 -0.0200 0.1058  162 TYR B CD2 
3807  C CE1 . TYR B  162 ? 1.5306 1.4657 1.3277 -0.1152 -0.0289 0.1207  162 TYR B CE1 
3808  C CE2 . TYR B  162 ? 1.3121 1.2483 1.1107 -0.1140 -0.0247 0.1034  162 TYR B CE2 
3809  C CZ  . TYR B  162 ? 1.5211 1.4577 1.3126 -0.1162 -0.0289 0.1107  162 TYR B CZ  
3810  O OH  . TYR B  162 ? 1.2280 1.1667 1.0069 -0.1194 -0.0332 0.1082  162 TYR B OH  
3811  N N   . ASP C  7   ? 2.0220 2.0192 1.7525 -0.1165 -0.0187 -0.0522 7   ASP C N   
3812  C CA  . ASP C  7   ? 2.1104 2.1047 1.8413 -0.1172 -0.0198 -0.0479 7   ASP C CA  
3813  C C   . ASP C  7   ? 2.2856 2.2830 2.0255 -0.1143 -0.0207 -0.0468 7   ASP C C   
3814  O O   . ASP C  7   ? 2.3046 2.3005 2.0470 -0.1146 -0.0199 -0.0446 7   ASP C O   
3815  C CB  . ASP C  7   ? 1.9158 1.9074 1.6436 -0.1198 -0.0161 -0.0485 7   ASP C CB  
3816  C CG  . ASP C  7   ? 1.9512 1.9461 1.6817 -0.1195 -0.0116 -0.0540 7   ASP C CG  
3817  O OD1 . ASP C  7   ? 1.6517 1.6480 1.3872 -0.1191 -0.0091 -0.0550 7   ASP C OD1 
3818  O OD2 . ASP C  7   ? 2.0097 2.0057 1.7375 -0.1198 -0.0105 -0.0572 7   ASP C OD2 
3819  N N   . THR C  8   ? 2.3528 2.3542 2.0973 -0.1116 -0.0220 -0.0485 8   THR C N   
3820  C CA  . THR C  8   ? 2.3214 2.3255 2.0738 -0.1088 -0.0233 -0.0473 8   THR C CA  
3821  C C   . THR C  8   ? 2.1577 2.1632 1.9114 -0.1068 -0.0273 -0.0458 8   THR C C   
3822  O O   . THR C  8   ? 2.1330 2.1399 1.8845 -0.1064 -0.0277 -0.0480 8   THR C O   
3823  C CB  . THR C  8   ? 2.3020 2.3112 2.0609 -0.1072 -0.0201 -0.0517 8   THR C CB  
3824  O OG1 . THR C  8   ? 2.2862 2.2994 2.0461 -0.1055 -0.0203 -0.0549 8   THR C OG1 
3825  C CG2 . THR C  8   ? 2.4204 2.4288 2.1778 -0.1093 -0.0158 -0.0541 8   THR C CG2 
3826  N N   . LEU C  9   ? 1.9981 2.0031 1.7558 -0.1054 -0.0299 -0.0420 9   LEU C N   
3827  C CA  . LEU C  9   ? 1.6671 1.6739 1.4276 -0.1031 -0.0334 -0.0407 9   LEU C CA  
3828  C C   . LEU C  9   ? 1.5844 1.5941 1.3535 -0.1004 -0.0332 -0.0405 9   LEU C C   
3829  O O   . LEU C  9   ? 1.3902 1.3979 1.1621 -0.1005 -0.0334 -0.0372 9   LEU C O   
3830  C CB  . LEU C  9   ? 1.7348 1.7379 1.4913 -0.1043 -0.0374 -0.0357 9   LEU C CB  
3831  C CG  . LEU C  9   ? 1.5821 1.5870 1.3423 -0.1019 -0.0411 -0.0340 9   LEU C CG  
3832  C CD1 . LEU C  9   ? 1.5076 1.5157 1.2678 -0.1005 -0.0408 -0.0381 9   LEU C CD1 
3833  C CD2 . LEU C  9   ? 1.4138 1.4155 1.1700 -0.1034 -0.0452 -0.0290 9   LEU C CD2 
3834  N N   . CYS C  10  ? 1.6620 1.6763 1.4354 -0.0981 -0.0325 -0.0439 10  CYS C N   
3835  C CA  . CYS C  10  ? 1.5074 1.5246 1.2884 -0.0958 -0.0320 -0.0443 10  CYS C CA  
3836  C C   . CYS C  10  ? 1.2736 1.2924 1.0581 -0.0932 -0.0353 -0.0425 10  CYS C C   
3837  O O   . CYS C  10  ? 1.2313 1.2496 1.0124 -0.0931 -0.0378 -0.0419 10  CYS C O   
3838  C CB  . CYS C  10  ? 1.3742 1.3962 1.1583 -0.0951 -0.0285 -0.0493 10  CYS C CB  
3839  S SG  . CYS C  10  ? 1.6902 1.7108 1.4722 -0.0980 -0.0240 -0.0515 10  CYS C SG  
3840  N N   . ILE C  11  ? 1.2003 1.2207 0.9914 -0.0914 -0.0352 -0.0418 11  ILE C N   
3841  C CA  . ILE C  11  ? 1.2811 1.3026 1.0760 -0.0889 -0.0382 -0.0399 11  ILE C CA  
3842  C C   . ILE C  11  ? 1.2380 1.2644 1.0392 -0.0865 -0.0367 -0.0429 11  ILE C C   
3843  O O   . ILE C  11  ? 1.2352 1.2628 1.0396 -0.0868 -0.0338 -0.0446 11  ILE C O   
3844  C CB  . ILE C  11  ? 1.2566 1.2745 1.0535 -0.0889 -0.0404 -0.0347 11  ILE C CB  
3845  C CG1 . ILE C  11  ? 1.2237 1.2372 1.0140 -0.0915 -0.0420 -0.0315 11  ILE C CG1 
3846  C CG2 . ILE C  11  ? 1.2238 1.2429 1.0245 -0.0865 -0.0435 -0.0327 11  ILE C CG2 
3847  C CD1 . ILE C  11  ? 1.0779 1.0883 0.8701 -0.0916 -0.0446 -0.0257 11  ILE C CD1 
3848  N N   . GLY C  12  ? 1.5039 1.5331 1.3067 -0.0844 -0.0386 -0.0435 12  GLY C N   
3849  C CA  . GLY C  12  ? 1.4734 1.5074 1.2818 -0.0821 -0.0375 -0.0460 12  GLY C CA  
3850  C C   . GLY C  12  ? 1.4318 1.4674 1.2426 -0.0795 -0.0403 -0.0450 12  GLY C C   
3851  O O   . GLY C  12  ? 1.3417 1.3745 1.1504 -0.0795 -0.0433 -0.0419 12  GLY C O   
3852  N N   . TYR C  13  ? 1.1288 1.1693 0.9439 -0.0775 -0.0393 -0.0475 13  TYR C N   
3853  C CA  . TYR C  13  ? 1.0769 1.1193 0.8950 -0.0748 -0.0416 -0.0467 13  TYR C CA  
3854  C C   . TYR C  13  ? 0.9921 1.0395 0.8102 -0.0733 -0.0409 -0.0499 13  TYR C C   
3855  O O   . TYR C  13  ? 1.0253 1.0740 0.8403 -0.0745 -0.0392 -0.0524 13  TYR C O   
3856  C CB  . TYR C  13  ? 0.8535 0.8969 0.6776 -0.0734 -0.0413 -0.0458 13  TYR C CB  
3857  C CG  . TYR C  13  ? 0.7967 0.8419 0.6231 -0.0745 -0.0378 -0.0483 13  TYR C CG  
3858  C CD1 . TYR C  13  ? 0.8176 0.8684 0.6468 -0.0735 -0.0360 -0.0518 13  TYR C CD1 
3859  C CD2 . TYR C  13  ? 0.6955 0.7369 0.5213 -0.0766 -0.0363 -0.0471 13  TYR C CD2 
3860  C CE1 . TYR C  13  ? 0.6841 0.7366 0.5151 -0.0749 -0.0328 -0.0543 13  TYR C CE1 
3861  C CE2 . TYR C  13  ? 0.8536 0.8964 0.6815 -0.0778 -0.0329 -0.0496 13  TYR C CE2 
3862  C CZ  . TYR C  13  ? 0.8170 0.8654 0.6474 -0.0770 -0.0312 -0.0533 13  TYR C CZ  
3863  O OH  . TYR C  13  ? 0.7609 0.8110 0.5933 -0.0786 -0.0278 -0.0560 13  TYR C OH  
3864  N N   . HIS C  14  ? 1.0479 1.0982 0.8697 -0.0707 -0.0421 -0.0498 14  HIS C N   
3865  C CA  . HIS C  14  ? 0.9354 0.9904 0.7591 -0.0688 -0.0413 -0.0518 14  HIS C CA  
3866  C C   . HIS C  14  ? 1.0474 1.1084 0.8755 -0.0678 -0.0389 -0.0546 14  HIS C C   
3867  O O   . HIS C  14  ? 1.1292 1.1907 0.9587 -0.0683 -0.0384 -0.0552 14  HIS C O   
3868  C CB  . HIS C  14  ? 1.0916 1.1462 0.9176 -0.0665 -0.0437 -0.0495 14  HIS C CB  
3869  C CG  . HIS C  14  ? 1.1352 1.1938 0.9636 -0.0644 -0.0427 -0.0508 14  HIS C CG  
3870  N ND1 . HIS C  14  ? 1.2769 1.3340 1.1023 -0.0648 -0.0426 -0.0509 14  HIS C ND1 
3871  C CD2 . HIS C  14  ? 1.2289 1.2928 1.0621 -0.0619 -0.0417 -0.0520 14  HIS C CD2 
3872  C CE1 . HIS C  14  ? 1.4143 1.4756 1.2426 -0.0625 -0.0415 -0.0522 14  HIS C CE1 
3873  N NE2 . HIS C  14  ? 1.3605 1.4262 1.1936 -0.0607 -0.0411 -0.0527 14  HIS C NE2 
3874  N N   . ALA C  15  ? 0.9059 0.9715 0.7358 -0.0666 -0.0375 -0.0563 15  ALA C N   
3875  C CA  . ALA C  15  ? 0.9918 1.0641 0.8260 -0.0654 -0.0356 -0.0587 15  ALA C CA  
3876  C C   . ALA C  15  ? 0.9640 1.0406 0.8004 -0.0631 -0.0354 -0.0591 15  ALA C C   
3877  O O   . ALA C  15  ? 1.0420 1.1163 0.8760 -0.0630 -0.0358 -0.0585 15  ALA C O   
3878  C CB  . ALA C  15  ? 0.8604 0.9345 0.6932 -0.0679 -0.0331 -0.0614 15  ALA C CB  
3879  N N   . ASN C  16  ? 0.9428 1.0258 0.7837 -0.0613 -0.0347 -0.0603 16  ASN C N   
3880  C CA  . ASN C  16  ? 1.1910 1.2784 1.0342 -0.0588 -0.0346 -0.0605 16  ASN C CA  
3881  C C   . ASN C  16  ? 1.2683 1.3638 1.1158 -0.0575 -0.0335 -0.0622 16  ASN C C   
3882  O O   . ASN C  16  ? 1.2360 1.3339 1.0844 -0.0589 -0.0324 -0.0637 16  ASN C O   
3883  C CB  . ASN C  16  ? 1.2557 1.3401 1.0996 -0.0565 -0.0368 -0.0579 16  ASN C CB  
3884  C CG  . ASN C  16  ? 1.2229 1.3066 1.0694 -0.0556 -0.0382 -0.0564 16  ASN C CG  
3885  O OD1 . ASN C  16  ? 1.1689 1.2553 1.0171 -0.0563 -0.0373 -0.0576 16  ASN C OD1 
3886  N ND2 . ASN C  16  ? 1.1233 1.2034 0.9700 -0.0542 -0.0403 -0.0540 16  ASN C ND2 
3887  N N   . ASN C  17  ? 1.1786 1.2783 1.0284 -0.0548 -0.0337 -0.0619 17  ASN C N   
3888  C CA  . ASN C  17  ? 1.2679 1.3759 1.1215 -0.0534 -0.0330 -0.0631 17  ASN C CA  
3889  C C   . ASN C  17  ? 1.4331 1.5424 1.2898 -0.0518 -0.0342 -0.0619 17  ASN C C   
3890  O O   . ASN C  17  ? 1.5622 1.6781 1.4220 -0.0499 -0.0342 -0.0621 17  ASN C O   
3891  C CB  . ASN C  17  ? 1.5851 1.6970 1.4394 -0.0512 -0.0327 -0.0632 17  ASN C CB  
3892  C CG  . ASN C  17  ? 1.6917 1.8000 1.5460 -0.0487 -0.0343 -0.0609 17  ASN C CG  
3893  O OD1 . ASN C  17  ? 1.6976 1.8024 1.5526 -0.0481 -0.0358 -0.0592 17  ASN C OD1 
3894  N ND2 . ASN C  17  ? 1.8358 1.9448 1.6891 -0.0474 -0.0338 -0.0611 17  ASN C ND2 
3895  N N   . SER C  18  ? 1.3276 1.4309 1.1834 -0.0524 -0.0353 -0.0604 18  SER C N   
3896  C CA  . SER C  18  ? 1.1530 1.2567 1.0115 -0.0509 -0.0365 -0.0592 18  SER C CA  
3897  C C   . SER C  18  ? 1.0706 1.1793 0.9310 -0.0520 -0.0353 -0.0611 18  SER C C   
3898  O O   . SER C  18  ? 0.9670 1.0752 0.8259 -0.0548 -0.0339 -0.0629 18  SER C O   
3899  C CB  . SER C  18  ? 1.1853 1.2811 1.0421 -0.0515 -0.0381 -0.0571 18  SER C CB  
3900  O OG  . SER C  18  ? 1.0334 1.1293 0.8928 -0.0497 -0.0392 -0.0558 18  SER C OG  
3901  N N   . THR C  19  ? 1.1454 1.2589 1.0089 -0.0501 -0.0357 -0.0608 19  THR C N   
3902  C CA  . THR C  19  ? 1.1845 1.3028 1.0496 -0.0512 -0.0346 -0.0626 19  THR C CA  
3903  C C   . THR C  19  ? 1.1397 1.2547 1.0056 -0.0507 -0.0354 -0.0614 19  THR C C   
3904  O O   . THR C  19  ? 1.1660 1.2840 1.0330 -0.0517 -0.0345 -0.0629 19  THR C O   
3905  C CB  . THR C  19  ? 1.1348 1.2624 1.0024 -0.0497 -0.0343 -0.0633 19  THR C CB  
3906  O OG1 . THR C  19  ? 1.1095 1.2376 0.9787 -0.0463 -0.0358 -0.0610 19  THR C OG1 
3907  C CG2 . THR C  19  ? 1.2448 1.3763 1.1116 -0.0506 -0.0333 -0.0649 19  THR C CG2 
3908  N N   . ASP C  20  ? 1.0150 1.1239 0.8805 -0.0492 -0.0371 -0.0589 20  ASP C N   
3909  C CA  . ASP C  20  ? 0.8782 0.9833 0.7445 -0.0487 -0.0381 -0.0576 20  ASP C CA  
3910  C C   . ASP C  20  ? 0.8277 0.9305 0.6927 -0.0515 -0.0369 -0.0593 20  ASP C C   
3911  O O   . ASP C  20  ? 1.0247 1.1242 0.8872 -0.0538 -0.0362 -0.0601 20  ASP C O   
3912  C CB  . ASP C  20  ? 1.0309 1.1291 0.8961 -0.0475 -0.0401 -0.0548 20  ASP C CB  
3913  C CG  . ASP C  20  ? 1.1230 1.2227 0.9895 -0.0445 -0.0412 -0.0532 20  ASP C CG  
3914  O OD1 . ASP C  20  ? 0.9601 1.0546 0.8256 -0.0438 -0.0428 -0.0511 20  ASP C OD1 
3915  O OD2 . ASP C  20  ? 1.0138 1.1200 0.8823 -0.0430 -0.0406 -0.0539 20  ASP C OD2 
3916  N N   . THR C  21  ? 0.8474 0.9518 0.7138 -0.0515 -0.0364 -0.0599 21  THR C N   
3917  C CA  . THR C  21  ? 0.8281 0.9298 0.6932 -0.0542 -0.0351 -0.0617 21  THR C CA  
3918  C C   . THR C  21  ? 0.8049 0.9020 0.6714 -0.0532 -0.0358 -0.0601 21  THR C C   
3919  O O   . THR C  21  ? 0.9070 1.0063 0.7752 -0.0510 -0.0368 -0.0591 21  THR C O   
3920  C CB  . THR C  21  ? 0.8820 0.9903 0.7477 -0.0561 -0.0328 -0.0651 21  THR C CB  
3921  O OG1 . THR C  21  ? 1.0578 1.1722 0.9259 -0.0541 -0.0332 -0.0648 21  THR C OG1 
3922  C CG2 . THR C  21  ? 0.8792 0.9911 0.7439 -0.0578 -0.0316 -0.0669 21  THR C CG2 
3923  N N   . VAL C  22  ? 0.8059 0.8967 0.6729 -0.0548 -0.0349 -0.0592 22  VAL C N   
3924  C CA  . VAL C  22  ? 0.6011 0.6873 0.4711 -0.0540 -0.0348 -0.0572 22  VAL C CA  
3925  C C   . VAL C  22  ? 0.6967 0.7810 0.5680 -0.0567 -0.0316 -0.0590 22  VAL C C   
3926  O O   . VAL C  22  ? 0.7325 0.8182 0.6021 -0.0592 -0.0297 -0.0615 22  VAL C O   
3927  C CB  . VAL C  22  ? 0.6649 0.7444 0.5352 -0.0530 -0.0370 -0.0535 22  VAL C CB  
3928  C CG1 . VAL C  22  ? 0.6011 0.6820 0.4695 -0.0510 -0.0398 -0.0522 22  VAL C CG1 
3929  C CG2 . VAL C  22  ? 0.5818 0.6566 0.4510 -0.0554 -0.0358 -0.0532 22  VAL C CG2 
3930  N N   . ASP C  23  ? 0.5838 0.6648 0.4582 -0.0562 -0.0307 -0.0578 23  ASP C N   
3931  C CA  . ASP C  23  ? 0.6204 0.6985 0.4966 -0.0586 -0.0273 -0.0592 23  ASP C CA  
3932  C C   . ASP C  23  ? 0.5755 0.6458 0.4542 -0.0583 -0.0274 -0.0557 23  ASP C C   
3933  O O   . ASP C  23  ? 0.5135 0.5811 0.3935 -0.0560 -0.0300 -0.0523 23  ASP C O   
3934  C CB  . ASP C  23  ? 0.7945 0.8752 0.6727 -0.0585 -0.0255 -0.0608 23  ASP C CB  
3935  C CG  . ASP C  23  ? 0.9502 1.0389 0.8262 -0.0597 -0.0246 -0.0645 23  ASP C CG  
3936  O OD1 . ASP C  23  ? 1.1033 1.1957 0.9765 -0.0602 -0.0256 -0.0657 23  ASP C OD1 
3937  O OD2 . ASP C  23  ? 1.0021 1.0933 0.8790 -0.0602 -0.0229 -0.0662 23  ASP C OD2 
3938  N N   . THR C  24  ? 0.6341 0.7009 0.5137 -0.0608 -0.0244 -0.0566 24  THR C N   
3939  C CA  . THR C  24  ? 0.6692 0.7288 0.5519 -0.0607 -0.0240 -0.0532 24  THR C CA  
3940  C C   . THR C  24  ? 0.6471 0.7044 0.5332 -0.0622 -0.0198 -0.0547 24  THR C C   
3941  O O   . THR C  24  ? 0.6224 0.6839 0.5080 -0.0634 -0.0176 -0.0583 24  THR C O   
3942  C CB  . THR C  24  ? 0.8642 0.9206 0.7449 -0.0623 -0.0240 -0.0522 24  THR C CB  
3943  O OG1 . THR C  24  ? 0.8966 0.9540 0.7762 -0.0653 -0.0203 -0.0559 24  THR C OG1 
3944  C CG2 . THR C  24  ? 0.7285 0.7875 0.6051 -0.0614 -0.0275 -0.0517 24  THR C CG2 
3945  N N   . VAL C  25  ? 0.7579 0.8088 0.6477 -0.0622 -0.0186 -0.0517 25  VAL C N   
3946  C CA  . VAL C  25  ? 0.7680 0.8158 0.6616 -0.0636 -0.0141 -0.0529 25  VAL C CA  
3947  C C   . VAL C  25  ? 0.7817 0.8301 0.6734 -0.0671 -0.0104 -0.0567 25  VAL C C   
3948  O O   . VAL C  25  ? 0.7115 0.7607 0.6043 -0.0690 -0.0065 -0.0600 25  VAL C O   
3949  C CB  . VAL C  25  ? 0.6841 0.7247 0.5826 -0.0627 -0.0138 -0.0482 25  VAL C CB  
3950  C CG1 . VAL C  25  ? 0.6282 0.6659 0.5316 -0.0631 -0.0096 -0.0489 25  VAL C CG1 
3951  C CG2 . VAL C  25  ? 0.7996 0.8395 0.6989 -0.0596 -0.0185 -0.0438 25  VAL C CG2 
3952  N N   . LEU C  26  ? 0.7487 0.7970 0.6375 -0.0680 -0.0116 -0.0564 26  LEU C N   
3953  C CA  . LEU C  26  ? 0.7187 0.7669 0.6059 -0.0713 -0.0081 -0.0595 26  LEU C CA  
3954  C C   . LEU C  26  ? 0.7911 0.8466 0.6737 -0.0728 -0.0082 -0.0641 26  LEU C C   
3955  O O   . LEU C  26  ? 0.7767 0.8334 0.6583 -0.0759 -0.0048 -0.0677 26  LEU C O   
3956  C CB  . LEU C  26  ? 0.6550 0.6986 0.5417 -0.0716 -0.0088 -0.0565 26  LEU C CB  
3957  C CG  . LEU C  26  ? 0.7540 0.7900 0.6454 -0.0715 -0.0069 -0.0527 26  LEU C CG  
3958  C CD1 . LEU C  26  ? 0.8715 0.9055 0.7679 -0.0698 -0.0061 -0.0511 26  LEU C CD1 
3959  C CD2 . LEU C  26  ? 0.6352 0.6679 0.5258 -0.0703 -0.0103 -0.0479 26  LEU C CD2 
3960  N N   . GLU C  27  ? 0.8346 0.8950 0.7148 -0.0708 -0.0121 -0.0637 27  GLU C N   
3961  C CA  . GLU C  27  ? 0.7102 0.7776 0.5864 -0.0720 -0.0127 -0.0673 27  GLU C CA  
3962  C C   . GLU C  27  ? 0.8014 0.8750 0.6766 -0.0698 -0.0155 -0.0677 27  GLU C C   
3963  O O   . GLU C  27  ? 0.8258 0.8980 0.7021 -0.0668 -0.0184 -0.0644 27  GLU C O   
3964  C CB  . GLU C  27  ? 0.9097 0.9763 0.7828 -0.0723 -0.0144 -0.0662 27  GLU C CB  
3965  C CG  . GLU C  27  ? 1.0757 1.1481 0.9455 -0.0745 -0.0135 -0.0702 27  GLU C CG  
3966  C CD  . GLU C  27  ? 1.3314 1.4015 1.1987 -0.0754 -0.0141 -0.0693 27  GLU C CD  
3967  O OE1 . GLU C  27  ? 1.2858 1.3607 1.1502 -0.0765 -0.0142 -0.0718 27  GLU C OE1 
3968  O OE2 . GLU C  27  ? 1.2935 1.3569 1.1617 -0.0750 -0.0143 -0.0660 27  GLU C OE2 
3969  N N   . LYS C  28  ? 0.8132 0.8938 0.6863 -0.0712 -0.0146 -0.0715 28  LYS C N   
3970  C CA  . LYS C  28  ? 0.8215 0.9088 0.6938 -0.0692 -0.0171 -0.0720 28  LYS C CA  
3971  C C   . LYS C  28  ? 0.8032 0.8957 0.6724 -0.0686 -0.0196 -0.0723 28  LYS C C   
3972  O O   . LYS C  28  ? 0.9055 0.9980 0.7729 -0.0705 -0.0187 -0.0737 28  LYS C O   
3973  C CB  . LYS C  28  ? 0.8805 0.9728 0.7529 -0.0712 -0.0146 -0.0756 28  LYS C CB  
3974  C CG  . LYS C  28  ? 0.9210 1.0103 0.7963 -0.0703 -0.0134 -0.0747 28  LYS C CG  
3975  C CD  . LYS C  28  ? 1.1100 1.2047 0.9846 -0.0725 -0.0109 -0.0786 28  LYS C CD  
3976  C CE  . LYS C  28  ? 1.2307 1.3239 1.1077 -0.0709 -0.0105 -0.0775 28  LYS C CE  
3977  N NZ  . LYS C  28  ? 1.1420 1.2262 1.0226 -0.0705 -0.0087 -0.0751 28  LYS C NZ  
3978  N N   . ASN C  29  ? 0.9063 1.0030 0.7751 -0.0658 -0.0224 -0.0712 29  ASN C N   
3979  C CA  . ASN C  29  ? 0.8564 0.9583 0.7230 -0.0648 -0.0247 -0.0713 29  ASN C CA  
3980  C C   . ASN C  29  ? 0.9157 1.0140 0.7804 -0.0656 -0.0251 -0.0705 29  ASN C C   
3981  O O   . ASN C  29  ? 1.0359 1.1376 0.8987 -0.0675 -0.0240 -0.0730 29  ASN C O   
3982  C CB  . ASN C  29  ? 0.9016 1.0123 0.7671 -0.0664 -0.0236 -0.0749 29  ASN C CB  
3983  C CG  . ASN C  29  ? 1.2567 1.3726 1.1233 -0.0646 -0.0247 -0.0747 29  ASN C CG  
3984  O OD1 . ASN C  29  ? 1.2646 1.3832 1.1312 -0.0616 -0.0273 -0.0727 29  ASN C OD1 
3985  N ND2 . ASN C  29  ? 1.2620 1.3793 1.1294 -0.0665 -0.0224 -0.0769 29  ASN C ND2 
3986  N N   . VAL C  30  ? 0.8976 0.9892 0.7627 -0.0641 -0.0266 -0.0671 30  VAL C N   
3987  C CA  . VAL C  30  ? 0.7257 0.8136 0.5886 -0.0647 -0.0273 -0.0659 30  VAL C CA  
3988  C C   . VAL C  30  ? 0.6814 0.7711 0.5426 -0.0622 -0.0304 -0.0643 30  VAL C C   
3989  O O   . VAL C  30  ? 0.7095 0.7978 0.5718 -0.0597 -0.0326 -0.0617 30  VAL C O   
3990  C CB  . VAL C  30  ? 0.6819 0.7613 0.5460 -0.0649 -0.0273 -0.0629 30  VAL C CB  
3991  C CG1 . VAL C  30  ? 0.6054 0.6813 0.4668 -0.0653 -0.0285 -0.0613 30  VAL C CG1 
3992  C CG2 . VAL C  30  ? 0.7142 0.7912 0.5803 -0.0674 -0.0237 -0.0645 30  VAL C CG2 
3993  N N   . THR C  31  ? 0.7789 0.8715 0.6375 -0.0631 -0.0304 -0.0658 31  THR C N   
3994  C CA  . THR C  31  ? 0.8479 0.9422 0.7051 -0.0610 -0.0326 -0.0645 31  THR C CA  
3995  C C   . THR C  31  ? 0.7819 0.8691 0.6373 -0.0606 -0.0345 -0.0615 31  THR C C   
3996  O O   . THR C  31  ? 0.9348 1.0178 0.7885 -0.0626 -0.0336 -0.0613 31  THR C O   
3997  C CB  . THR C  31  ? 0.8458 0.9454 0.7027 -0.0621 -0.0312 -0.0666 31  THR C CB  
3998  O OG1 . THR C  31  ? 0.7264 0.8334 0.5854 -0.0626 -0.0296 -0.0691 31  THR C OG1 
3999  C CG2 . THR C  31  ? 0.6910 0.7921 0.5484 -0.0597 -0.0326 -0.0647 31  THR C CG2 
4000  N N   . VAL C  32  ? 0.7193 0.8054 0.5754 -0.0579 -0.0368 -0.0590 32  VAL C N   
4001  C CA  . VAL C  32  ? 0.7912 0.8711 0.6453 -0.0576 -0.0389 -0.0561 32  VAL C CA  
4002  C C   . VAL C  32  ? 0.7810 0.8623 0.6348 -0.0560 -0.0398 -0.0551 32  VAL C C   
4003  O O   . VAL C  32  ? 0.8742 0.9609 0.7304 -0.0543 -0.0392 -0.0559 32  VAL C O   
4004  C CB  . VAL C  32  ? 0.7905 0.8665 0.6474 -0.0560 -0.0405 -0.0531 32  VAL C CB  
4005  C CG1 . VAL C  32  ? 0.6762 0.7492 0.5354 -0.0576 -0.0386 -0.0530 32  VAL C CG1 
4006  C CG2 . VAL C  32  ? 0.6877 0.7679 0.5469 -0.0533 -0.0414 -0.0531 32  VAL C CG2 
4007  N N   . THR C  33  ? 0.7738 0.8500 0.6246 -0.0567 -0.0411 -0.0534 33  THR C N   
4008  C CA  . THR C  33  ? 0.8585 0.9350 0.7083 -0.0557 -0.0417 -0.0527 33  THR C CA  
4009  C C   . THR C  33  ? 0.8349 0.9118 0.6872 -0.0528 -0.0433 -0.0508 33  THR C C   
4010  O O   . THR C  33  ? 0.9816 1.0616 0.8348 -0.0511 -0.0430 -0.0511 33  THR C O   
4011  C CB  . THR C  33  ? 0.8241 0.8946 0.6694 -0.0577 -0.0427 -0.0514 33  THR C CB  
4012  O OG1 . THR C  33  ? 0.7975 0.8629 0.6421 -0.0577 -0.0451 -0.0487 33  THR C OG1 
4013  C CG2 . THR C  33  ? 0.8834 0.9533 0.7258 -0.0606 -0.0409 -0.0533 33  THR C CG2 
4014  N N   . HIS C  34  ? 0.8533 0.9270 0.7066 -0.0521 -0.0451 -0.0488 34  HIS C N   
4015  C CA  . HIS C  34  ? 0.7874 0.8609 0.6430 -0.0495 -0.0468 -0.0469 34  HIS C CA  
4016  C C   . HIS C  34  ? 0.8521 0.9253 0.7104 -0.0485 -0.0476 -0.0460 34  HIS C C   
4017  O O   . HIS C  34  ? 0.8259 0.8968 0.6834 -0.0502 -0.0475 -0.0462 34  HIS C O   
4018  C CB  . HIS C  34  ? 0.8487 0.9169 0.7017 -0.0498 -0.0490 -0.0445 34  HIS C CB  
4019  C CG  . HIS C  34  ? 1.0599 1.1277 0.9097 -0.0510 -0.0482 -0.0454 34  HIS C CG  
4020  N ND1 . HIS C  34  ? 0.9518 1.0179 0.7981 -0.0537 -0.0473 -0.0464 34  HIS C ND1 
4021  C CD2 . HIS C  34  ? 1.1345 1.2030 0.9836 -0.0499 -0.0480 -0.0456 34  HIS C CD2 
4022  C CE1 . HIS C  34  ? 1.0475 1.1134 0.8912 -0.0543 -0.0466 -0.0472 34  HIS C CE1 
4023  N NE2 . HIS C  34  ? 1.2697 1.3370 1.1150 -0.0521 -0.0470 -0.0468 34  HIS C NE2 
4024  N N   . SER C  35  ? 0.9262 1.0015 0.7875 -0.0459 -0.0482 -0.0452 35  SER C N   
4025  C CA  . SER C  35  ? 0.8222 0.8973 0.6860 -0.0448 -0.0488 -0.0445 35  SER C CA  
4026  C C   . SER C  35  ? 0.7123 0.7885 0.5787 -0.0419 -0.0499 -0.0430 35  SER C C   
4027  O O   . SER C  35  ? 0.8711 0.9493 0.7377 -0.0405 -0.0498 -0.0430 35  SER C O   
4028  C CB  . SER C  35  ? 0.8089 0.8883 0.6739 -0.0455 -0.0466 -0.0470 35  SER C CB  
4029  O OG  . SER C  35  ? 0.8786 0.9644 0.7451 -0.0444 -0.0451 -0.0486 35  SER C OG  
4030  N N   . VAL C  36  ? 0.6918 0.7668 0.5603 -0.0409 -0.0510 -0.0419 36  VAL C N   
4031  C CA  . VAL C  36  ? 0.7741 0.8501 0.6451 -0.0381 -0.0519 -0.0405 36  VAL C CA  
4032  C C   . VAL C  36  ? 0.7256 0.8042 0.5994 -0.0372 -0.0509 -0.0412 36  VAL C C   
4033  O O   . VAL C  36  ? 0.6581 0.7356 0.5330 -0.0388 -0.0495 -0.0417 36  VAL C O   
4034  C CB  . VAL C  36  ? 0.6519 0.7226 0.5231 -0.0377 -0.0546 -0.0376 36  VAL C CB  
4035  C CG1 . VAL C  36  ? 0.7635 0.8314 0.6316 -0.0389 -0.0556 -0.0370 36  VAL C CG1 
4036  C CG2 . VAL C  36  ? 0.6870 0.7537 0.5608 -0.0387 -0.0546 -0.0359 36  VAL C CG2 
4037  N N   . ASN C  37  ? 0.8009 0.8828 0.6766 -0.0347 -0.0509 -0.0410 37  ASN C N   
4038  C CA  . ASN C  37  ? 0.7873 0.8716 0.6657 -0.0338 -0.0498 -0.0414 37  ASN C CA  
4039  C C   . ASN C  37  ? 0.7152 0.7954 0.5969 -0.0323 -0.0510 -0.0388 37  ASN C C   
4040  O O   . ASN C  37  ? 0.7508 0.8298 0.6329 -0.0304 -0.0526 -0.0371 37  ASN C O   
4041  C CB  . ASN C  37  ? 0.6935 0.7845 0.5724 -0.0320 -0.0488 -0.0426 37  ASN C CB  
4042  C CG  . ASN C  37  ? 0.7936 0.8882 0.6736 -0.0322 -0.0474 -0.0441 37  ASN C CG  
4043  O OD1 . ASN C  37  ? 1.0198 1.1200 0.9008 -0.0306 -0.0467 -0.0445 37  ASN C OD1 
4044  N ND2 . ASN C  37  ? 0.7738 0.8652 0.6550 -0.0339 -0.0463 -0.0443 37  ASN C ND2 
4045  N N   . LEU C  38  ? 0.6210 0.6988 0.5050 -0.0331 -0.0498 -0.0384 38  LEU C N   
4046  C CA  . LEU C  38  ? 0.5543 0.6284 0.4421 -0.0318 -0.0506 -0.0359 38  LEU C CA  
4047  C C   . LEU C  38  ? 0.5178 0.5952 0.4078 -0.0298 -0.0496 -0.0363 38  LEU C C   
4048  O O   . LEU C  38  ? 0.5483 0.6232 0.4415 -0.0283 -0.0501 -0.0343 38  LEU C O   
4049  C CB  . LEU C  38  ? 0.4938 0.5632 0.3837 -0.0336 -0.0496 -0.0350 38  LEU C CB  
4050  C CG  . LEU C  38  ? 0.4704 0.5357 0.3589 -0.0354 -0.0509 -0.0336 38  LEU C CG  
4051  C CD1 . LEU C  38  ? 0.7086 0.7704 0.5992 -0.0373 -0.0492 -0.0332 38  LEU C CD1 
4052  C CD2 . LEU C  38  ? 0.5293 0.5912 0.4185 -0.0343 -0.0539 -0.0305 38  LEU C CD2 
4053  N N   . LEU C  39  ? 0.6043 0.6874 0.4925 -0.0299 -0.0482 -0.0388 39  LEU C N   
4054  C CA  . LEU C  39  ? 0.5482 0.6352 0.4379 -0.0283 -0.0471 -0.0393 39  LEU C CA  
4055  C C   . LEU C  39  ? 0.6857 0.7769 0.5746 -0.0258 -0.0482 -0.0388 39  LEU C C   
4056  O O   . LEU C  39  ? 0.8152 0.9104 0.7016 -0.0260 -0.0484 -0.0401 39  LEU C O   
4057  C CB  . LEU C  39  ? 0.5935 0.6846 0.4821 -0.0303 -0.0446 -0.0422 39  LEU C CB  
4058  C CG  . LEU C  39  ? 0.5723 0.6684 0.4616 -0.0290 -0.0435 -0.0430 39  LEU C CG  
4059  C CD1 . LEU C  39  ? 0.6478 0.7400 0.5405 -0.0276 -0.0432 -0.0411 39  LEU C CD1 
4060  C CD2 . LEU C  39  ? 0.6416 0.7419 0.5292 -0.0316 -0.0411 -0.0462 39  LEU C CD2 
4061  N N   . GLU C  40  ? 0.6635 0.7537 0.5548 -0.0233 -0.0489 -0.0369 40  GLU C N   
4062  C CA  . GLU C  40  ? 0.6516 0.7457 0.5428 -0.0207 -0.0496 -0.0362 40  GLU C CA  
4063  C C   . GLU C  40  ? 0.6919 0.7924 0.5831 -0.0201 -0.0480 -0.0375 40  GLU C C   
4064  O O   . GLU C  40  ? 0.5959 0.6959 0.4886 -0.0202 -0.0468 -0.0376 40  GLU C O   
4065  C CB  . GLU C  40  ? 0.5639 0.6540 0.4578 -0.0185 -0.0509 -0.0336 40  GLU C CB  
4066  C CG  . GLU C  40  ? 0.7249 0.8182 0.6189 -0.0156 -0.0514 -0.0327 40  GLU C CG  
4067  C CD  . GLU C  40  ? 0.9092 1.0042 0.8007 -0.0156 -0.0520 -0.0333 40  GLU C CD  
4068  O OE1 . GLU C  40  ? 0.9442 1.0362 0.8360 -0.0145 -0.0533 -0.0319 40  GLU C OE1 
4069  O OE2 . GLU C  40  ? 0.9981 1.0974 0.8874 -0.0168 -0.0512 -0.0352 40  GLU C OE2 
4070  N N   . ASP C  41  ? 0.7485 0.8548 0.6378 -0.0195 -0.0480 -0.0384 41  ASP C N   
4071  C CA  . ASP C  41  ? 0.7338 0.8472 0.6227 -0.0192 -0.0468 -0.0395 41  ASP C CA  
4072  C C   . ASP C  41  ? 0.7521 0.8704 0.6412 -0.0163 -0.0474 -0.0383 41  ASP C C   
4073  O O   . ASP C  41  ? 0.9836 1.1090 0.8718 -0.0163 -0.0468 -0.0392 41  ASP C O   
4074  C CB  . ASP C  41  ? 0.8493 0.9665 0.7358 -0.0222 -0.0456 -0.0424 41  ASP C CB  
4075  C CG  . ASP C  41  ? 1.1908 1.3087 1.0764 -0.0228 -0.0459 -0.0428 41  ASP C CG  
4076  O OD1 . ASP C  41  ? 1.1415 1.2570 1.0278 -0.0211 -0.0470 -0.0412 41  ASP C OD1 
4077  O OD2 . ASP C  41  ? 1.2096 1.3305 1.0942 -0.0252 -0.0447 -0.0450 41  ASP C OD2 
4078  N N   . LYS C  42  ? 0.8237 0.9385 0.7145 -0.0139 -0.0484 -0.0361 42  LYS C N   
4079  C CA  . LYS C  42  ? 0.8086 0.9271 0.6999 -0.0111 -0.0488 -0.0347 42  LYS C CA  
4080  C C   . LYS C  42  ? 0.7313 0.8465 0.6252 -0.0083 -0.0493 -0.0323 42  LYS C C   
4081  O O   . LYS C  42  ? 0.8761 0.9849 0.7707 -0.0083 -0.0502 -0.0313 42  LYS C O   
4082  C CB  . LYS C  42  ? 0.9697 1.0873 0.8594 -0.0116 -0.0493 -0.0352 42  LYS C CB  
4083  C CG  . LYS C  42  ? 1.2978 1.4224 1.1873 -0.0103 -0.0488 -0.0353 42  LYS C CG  
4084  C CD  . LYS C  42  ? 1.5228 1.6467 1.4111 -0.0119 -0.0485 -0.0365 42  LYS C CD  
4085  C CE  . LYS C  42  ? 1.4170 1.5398 1.3042 -0.0154 -0.0478 -0.0386 42  LYS C CE  
4086  N NZ  . LYS C  42  ? 1.3374 1.4588 1.2232 -0.0170 -0.0475 -0.0397 42  LYS C NZ  
4087  N N   . HIS C  43  ? 0.6012 0.7207 0.4963 -0.0061 -0.0486 -0.0312 43  HIS C N   
4088  C CA  . HIS C  43  ? 0.5760 0.6930 0.4738 -0.0033 -0.0488 -0.0288 43  HIS C CA  
4089  C C   . HIS C  43  ? 0.6838 0.8046 0.5823 -0.0004 -0.0487 -0.0274 43  HIS C C   
4090  O O   . HIS C  43  ? 0.6926 0.8194 0.5900 -0.0005 -0.0483 -0.0280 43  HIS C O   
4091  C CB  . HIS C  43  ? 0.6273 0.7458 0.5262 -0.0027 -0.0480 -0.0284 43  HIS C CB  
4092  C CG  . HIS C  43  ? 0.7051 0.8320 0.6028 -0.0026 -0.0471 -0.0289 43  HIS C CG  
4093  N ND1 . HIS C  43  ? 0.7437 0.8754 0.6425 0.0003  -0.0468 -0.0270 43  HIS C ND1 
4094  C CD2 . HIS C  43  ? 0.6935 0.8250 0.5889 -0.0051 -0.0465 -0.0311 43  HIS C CD2 
4095  C CE1 . HIS C  43  ? 0.7394 0.8786 0.6367 -0.0005 -0.0462 -0.0278 43  HIS C CE1 
4096  N NE2 . HIS C  43  ? 0.7058 0.8451 0.6010 -0.0038 -0.0461 -0.0305 43  HIS C NE2 
4097  N N   . ASN C  44  ? 0.6964 0.8137 0.5971 0.0020  -0.0489 -0.0254 44  ASN C N   
4098  C CA  . ASN C  44  ? 0.6523 0.7723 0.5542 0.0048  -0.0483 -0.0239 44  ASN C CA  
4099  C C   . ASN C  44  ? 0.7317 0.8580 0.6352 0.0074  -0.0474 -0.0222 44  ASN C C   
4100  O O   . ASN C  44  ? 0.7410 0.8702 0.6459 0.0101  -0.0467 -0.0205 44  ASN C O   
4101  C CB  . ASN C  44  ? 0.6348 0.7482 0.5382 0.0060  -0.0487 -0.0226 44  ASN C CB  
4102  C CG  . ASN C  44  ? 0.8121 0.9216 0.7179 0.0072  -0.0489 -0.0211 44  ASN C CG  
4103  O OD1 . ASN C  44  ? 0.8842 0.9883 0.7913 0.0079  -0.0493 -0.0202 44  ASN C OD1 
4104  N ND2 . ASN C  44  ? 0.8168 0.9289 0.7229 0.0072  -0.0485 -0.0210 44  ASN C ND2 
4105  N N   . GLY C  45  ? 0.7377 0.8659 0.6408 0.0066  -0.0472 -0.0225 45  GLY C N   
4106  C CA  . GLY C  45  ? 0.7058 0.8402 0.6097 0.0085  -0.0464 -0.0210 45  GLY C CA  
4107  C C   . GLY C  45  ? 0.6947 0.8270 0.6015 0.0120  -0.0459 -0.0183 45  GLY C C   
4108  O O   . GLY C  45  ? 0.6301 0.7679 0.5379 0.0144  -0.0452 -0.0164 45  GLY C O   
4109  N N   . LYS C  46  ? 0.8001 0.9246 0.7082 0.0121  -0.0463 -0.0180 46  LYS C N   
4110  C CA  . LYS C  46  ? 0.8384 0.9601 0.7494 0.0151  -0.0457 -0.0156 46  LYS C CA  
4111  C C   . LYS C  46  ? 0.6388 0.7550 0.5510 0.0145  -0.0459 -0.0155 46  LYS C C   
4112  O O   . LYS C  46  ? 0.6723 0.7840 0.5838 0.0119  -0.0468 -0.0170 46  LYS C O   
4113  C CB  . LYS C  46  ? 0.9147 1.0319 0.8268 0.0161  -0.0459 -0.0151 46  LYS C CB  
4114  C CG  . LYS C  46  ? 0.9641 1.0857 0.8758 0.0169  -0.0453 -0.0151 46  LYS C CG  
4115  C CD  . LYS C  46  ? 1.1533 1.2690 1.0651 0.0165  -0.0455 -0.0156 46  LYS C CD  
4116  C CE  . LYS C  46  ? 1.2938 1.4125 1.2067 0.0187  -0.0441 -0.0146 46  LYS C CE  
4117  N NZ  . LYS C  46  ? 1.2541 1.3677 1.1659 0.0173  -0.0442 -0.0159 46  LYS C NZ  
4118  N N   . LEU C  47  ? 0.6425 0.7591 0.5567 0.0169  -0.0450 -0.0135 47  LEU C N   
4119  C CA  . LEU C  47  ? 0.6101 0.7208 0.5262 0.0168  -0.0450 -0.0131 47  LEU C CA  
4120  C C   . LEU C  47  ? 0.6688 0.7736 0.5875 0.0181  -0.0454 -0.0119 47  LEU C C   
4121  O O   . LEU C  47  ? 0.6351 0.7399 0.5558 0.0209  -0.0445 -0.0099 47  LEU C O   
4122  C CB  . LEU C  47  ? 0.4933 0.6070 0.4104 0.0186  -0.0437 -0.0115 47  LEU C CB  
4123  C CG  . LEU C  47  ? 0.6045 0.7242 0.5189 0.0170  -0.0432 -0.0128 47  LEU C CG  
4124  C CD1 . LEU C  47  ? 0.5406 0.6614 0.4557 0.0182  -0.0418 -0.0115 47  LEU C CD1 
4125  C CD2 . LEU C  47  ? 0.5409 0.6584 0.4533 0.0132  -0.0438 -0.0155 47  LEU C CD2 
4126  N N   . CYS C  48  ? 0.6629 0.7625 0.5811 0.0158  -0.0467 -0.0132 48  CYS C N   
4127  C CA  . CYS C  48  ? 0.7309 0.8250 0.6507 0.0162  -0.0473 -0.0125 48  CYS C CA  
4128  C C   . CYS C  48  ? 0.7232 0.8114 0.6460 0.0163  -0.0477 -0.0115 48  CYS C C   
4129  O O   . CYS C  48  ? 0.6685 0.7567 0.5923 0.0160  -0.0473 -0.0113 48  CYS C O   
4130  C CB  . CYS C  48  ? 0.5935 0.6854 0.5110 0.0136  -0.0487 -0.0143 48  CYS C CB  
4131  S SG  . CYS C  48  ? 1.0780 1.1764 0.9921 0.0129  -0.0484 -0.0158 48  CYS C SG  
4132  N N   . LYS C  49  ? 0.7226 0.8061 0.6469 0.0166  -0.0483 -0.0109 49  LYS C N   
4133  C CA  . LYS C  49  ? 0.7333 0.8114 0.6608 0.0165  -0.0489 -0.0099 49  LYS C CA  
4134  C C   . LYS C  49  ? 0.6307 0.7054 0.5577 0.0133  -0.0508 -0.0109 49  LYS C C   
4135  O O   . LYS C  49  ? 0.7072 0.7821 0.6313 0.0112  -0.0518 -0.0123 49  LYS C O   
4136  C CB  . LYS C  49  ? 0.7680 0.8425 0.6973 0.0176  -0.0489 -0.0090 49  LYS C CB  
4137  C CG  . LYS C  49  ? 0.8099 0.8876 0.7394 0.0206  -0.0470 -0.0081 49  LYS C CG  
4138  C CD  . LYS C  49  ? 0.8956 0.9690 0.8270 0.0214  -0.0466 -0.0074 49  LYS C CD  
4139  C CE  . LYS C  49  ? 1.0691 1.1441 0.9987 0.0220  -0.0456 -0.0080 49  LYS C CE  
4140  N NZ  . LYS C  49  ? 1.0981 1.1681 1.0290 0.0218  -0.0453 -0.0080 49  LYS C NZ  
4141  N N   . LEU C  50  ? 0.7425 0.8140 0.6725 0.0130  -0.0510 -0.0100 50  LEU C N   
4142  C CA  . LEU C  50  ? 0.8684 0.9374 0.7984 0.0103  -0.0523 -0.0106 50  LEU C CA  
4143  C C   . LEU C  50  ? 1.0024 1.0664 0.9337 0.0084  -0.0545 -0.0101 50  LEU C C   
4144  O O   . LEU C  50  ? 1.1735 1.2365 1.1029 0.0059  -0.0559 -0.0109 50  LEU C O   
4145  C CB  . LEU C  50  ? 0.7122 0.7808 0.6449 0.0107  -0.0510 -0.0100 50  LEU C CB  
4146  C CG  . LEU C  50  ? 0.7208 0.7901 0.6524 0.0085  -0.0508 -0.0112 50  LEU C CG  
4147  C CD1 . LEU C  50  ? 0.6645 0.7319 0.5997 0.0088  -0.0494 -0.0104 50  LEU C CD1 
4148  C CD2 . LEU C  50  ? 0.7617 0.8282 0.6925 0.0058  -0.0528 -0.0117 50  LEU C CD2 
4149  N N   . ARG C  51  ? 0.8971 0.9579 0.8315 0.0095  -0.0548 -0.0086 51  ARG C N   
4150  C CA  . ARG C  51  ? 1.0515 1.1081 0.9867 0.0077  -0.0570 -0.0081 51  ARG C CA  
4151  C C   . ARG C  51  ? 1.1515 1.2084 1.0845 0.0084  -0.0568 -0.0087 51  ARG C C   
4152  O O   . ARG C  51  ? 1.3485 1.4064 1.2778 0.0070  -0.0574 -0.0100 51  ARG C O   
4153  C CB  . ARG C  51  ? 1.2363 1.2892 1.1765 0.0082  -0.0575 -0.0062 51  ARG C CB  
4154  C CG  . ARG C  51  ? 1.4133 1.4662 1.3566 0.0086  -0.0566 -0.0054 51  ARG C CG  
4155  C CD  . ARG C  51  ? 1.8430 1.8918 1.7914 0.0080  -0.0578 -0.0035 51  ARG C CD  
4156  N NE  . ARG C  51  ? 1.9869 2.0335 1.9348 0.0051  -0.0606 -0.0032 51  ARG C NE  
4157  C CZ  . ARG C  51  ? 1.8332 1.8770 1.7825 0.0039  -0.0627 -0.0022 51  ARG C CZ  
4158  N NH1 . ARG C  51  ? 1.6800 1.7226 1.6315 0.0054  -0.0624 -0.0015 51  ARG C NH1 
4159  N NH2 . ARG C  51  ? 1.6270 1.6694 1.5755 0.0011  -0.0653 -0.0018 51  ARG C NH2 
4160  N N   . GLY C  52  ? 0.9661 1.0221 0.9018 0.0106  -0.0557 -0.0076 52  GLY C N   
4161  C CA  . GLY C  52  ? 1.0197 1.0761 0.9542 0.0120  -0.0545 -0.0080 52  GLY C CA  
4162  C C   . GLY C  52  ? 1.0528 1.1112 0.9898 0.0155  -0.0521 -0.0068 52  GLY C C   
4163  O O   . GLY C  52  ? 1.0970 1.1562 1.0338 0.0174  -0.0505 -0.0067 52  GLY C O   
4164  N N   . VAL C  53  ? 1.0076 1.0667 0.9470 0.0164  -0.0515 -0.0059 53  VAL C N   
4165  C CA  . VAL C  53  ? 0.7573 0.8182 0.6988 0.0196  -0.0492 -0.0046 53  VAL C CA  
4166  C C   . VAL C  53  ? 0.6049 0.6714 0.5441 0.0207  -0.0478 -0.0050 53  VAL C C   
4167  O O   . VAL C  53  ? 0.6416 0.7098 0.5788 0.0189  -0.0485 -0.0061 53  VAL C O   
4168  C CB  . VAL C  53  ? 0.5823 0.6401 0.5283 0.0200  -0.0492 -0.0032 53  VAL C CB  
4169  C CG1 . VAL C  53  ? 0.5740 0.6284 0.5211 0.0170  -0.0516 -0.0034 53  VAL C CG1 
4170  C CG2 . VAL C  53  ? 0.5692 0.6301 0.5158 0.0217  -0.0473 -0.0027 53  VAL C CG2 
4171  N N   . ALA C  54  ? 0.7237 0.7931 0.6634 0.0237  -0.0458 -0.0040 54  ALA C N   
4172  C CA  . ALA C  54  ? 0.7358 0.8113 0.6732 0.0248  -0.0445 -0.0042 54  ALA C CA  
4173  C C   . ALA C  54  ? 0.6792 0.7564 0.6173 0.0252  -0.0437 -0.0037 54  ALA C C   
4174  O O   . ALA C  54  ? 0.6762 0.7500 0.6174 0.0257  -0.0433 -0.0027 54  ALA C O   
4175  C CB  . ALA C  54  ? 0.7187 0.7970 0.6564 0.0279  -0.0427 -0.0029 54  ALA C CB  
4176  N N   . PRO C  55  ? 0.6141 0.6966 0.5492 0.0248  -0.0432 -0.0045 55  PRO C N   
4177  C CA  . PRO C  55  ? 0.4919 0.5766 0.4269 0.0250  -0.0420 -0.0043 55  PRO C CA  
4178  C C   . PRO C  55  ? 0.4814 0.5683 0.4180 0.0283  -0.0401 -0.0021 55  PRO C C   
4179  O O   . PRO C  55  ? 0.7039 0.7925 0.6408 0.0305  -0.0395 -0.0010 55  PRO C O   
4180  C CB  . PRO C  55  ? 0.5369 0.6273 0.4679 0.0235  -0.0422 -0.0059 55  PRO C CB  
4181  C CG  . PRO C  55  ? 0.5324 0.6252 0.4619 0.0242  -0.0427 -0.0060 55  PRO C CG  
4182  C CD  . PRO C  55  ? 0.5806 0.6673 0.5121 0.0238  -0.0438 -0.0059 55  PRO C CD  
4183  N N   . LEU C  56  ? 0.5337 0.6205 0.4712 0.0286  -0.0388 -0.0016 56  LEU C N   
4184  C CA  . LEU C  56  ? 0.5405 0.6297 0.4790 0.0316  -0.0369 0.0005  56  LEU C CA  
4185  C C   . LEU C  56  ? 0.5606 0.6571 0.4954 0.0316  -0.0362 0.0003  56  LEU C C   
4186  O O   . LEU C  56  ? 0.6735 0.7714 0.6065 0.0298  -0.0358 -0.0009 56  LEU C O   
4187  C CB  . LEU C  56  ? 0.5060 0.5909 0.4476 0.0319  -0.0358 0.0012  56  LEU C CB  
4188  C CG  . LEU C  56  ? 0.5198 0.6065 0.4623 0.0347  -0.0336 0.0034  56  LEU C CG  
4189  C CD1 . LEU C  56  ? 0.7064 0.7924 0.6511 0.0377  -0.0331 0.0055  56  LEU C CD1 
4190  C CD2 . LEU C  56  ? 0.5460 0.6283 0.4913 0.0344  -0.0324 0.0037  56  LEU C CD2 
4191  N N   . HIS C  57  ? 0.6613 0.7628 0.5951 0.0336  -0.0359 0.0016  57  HIS C N   
4192  C CA  . HIS C  57  ? 0.6621 0.7714 0.5925 0.0337  -0.0356 0.0017  57  HIS C CA  
4193  C C   . HIS C  57  ? 0.6314 0.7437 0.5624 0.0364  -0.0337 0.0043  57  HIS C C   
4194  O O   . HIS C  57  ? 0.6912 0.8028 0.6248 0.0394  -0.0328 0.0067  57  HIS C O   
4195  C CB  . HIS C  57  ? 0.6714 0.7851 0.6006 0.0343  -0.0363 0.0019  57  HIS C CB  
4196  C CG  . HIS C  57  ? 0.7668 0.8886 0.6925 0.0333  -0.0366 0.0013  57  HIS C CG  
4197  N ND1 . HIS C  57  ? 0.7667 0.8952 0.6916 0.0353  -0.0356 0.0035  57  HIS C ND1 
4198  C CD2 . HIS C  57  ? 0.7964 0.9209 0.7190 0.0304  -0.0378 -0.0012 57  HIS C CD2 
4199  C CE1 . HIS C  57  ? 0.8822 1.0174 0.8037 0.0335  -0.0363 0.0024  57  HIS C CE1 
4200  N NE2 . HIS C  57  ? 0.8286 0.9614 0.7487 0.0305  -0.0375 -0.0006 57  HIS C NE2 
4201  N N   . LEU C  58  ? 0.6496 0.7652 0.5781 0.0351  -0.0331 0.0037  58  LEU C N   
4202  C CA  . LEU C  58  ? 0.8206 0.9386 0.7491 0.0371  -0.0313 0.0060  58  LEU C CA  
4203  C C   . LEU C  58  ? 0.9056 1.0328 0.8316 0.0385  -0.0312 0.0078  58  LEU C C   
4204  O O   . LEU C  58  ? 0.9146 1.0446 0.8408 0.0408  -0.0299 0.0104  58  LEU C O   
4205  C CB  . LEU C  58  ? 0.7391 0.8553 0.6663 0.0349  -0.0303 0.0045  58  LEU C CB  
4206  C CG  . LEU C  58  ? 0.6292 0.7367 0.5595 0.0336  -0.0302 0.0032  58  LEU C CG  
4207  C CD1 . LEU C  58  ? 0.7000 0.8059 0.6292 0.0317  -0.0286 0.0020  58  LEU C CD1 
4208  C CD2 . LEU C  58  ? 0.6624 0.7647 0.5973 0.0365  -0.0298 0.0053  58  LEU C CD2 
4209  N N   . GLY C  59  ? 0.7866 0.9185 0.7104 0.0370  -0.0326 0.0065  59  GLY C N   
4210  C CA  . GLY C  59  ? 0.7685 0.9096 0.6903 0.0381  -0.0328 0.0083  59  GLY C CA  
4211  C C   . GLY C  59  ? 0.9162 1.0629 0.8343 0.0369  -0.0322 0.0084  59  GLY C C   
4212  O O   . GLY C  59  ? 1.0549 1.2022 0.9699 0.0334  -0.0325 0.0056  59  GLY C O   
4213  N N   . LYS C  60  ? 0.9826 1.1334 0.9012 0.0398  -0.0311 0.0119  60  LYS C N   
4214  C CA  . LYS C  60  ? 1.1865 1.3437 1.1013 0.0387  -0.0306 0.0125  60  LYS C CA  
4215  C C   . LYS C  60  ? 1.0929 1.2447 1.0070 0.0374  -0.0289 0.0114  60  LYS C C   
4216  O O   . LYS C  60  ? 1.2058 1.3616 1.1162 0.0359  -0.0282 0.0112  60  LYS C O   
4217  C CB  . LYS C  60  ? 1.1987 1.3627 1.1143 0.0424  -0.0301 0.0171  60  LYS C CB  
4218  C CG  . LYS C  60  ? 1.5668 1.7396 1.4779 0.0411  -0.0301 0.0180  60  LYS C CG  
4219  C CD  . LYS C  60  ? 1.7217 1.9015 1.6292 0.0378  -0.0319 0.0157  60  LYS C CD  
4220  C CE  . LYS C  60  ? 1.8631 2.0478 1.7730 0.0400  -0.0332 0.0176  60  LYS C CE  
4221  N NZ  . LYS C  60  ? 1.6690 1.8608 1.5757 0.0368  -0.0349 0.0154  60  LYS C NZ  
4222  N N   . CYS C  61  ? 0.9098 1.0523 0.8273 0.0379  -0.0283 0.0105  61  CYS C N   
4223  C CA  . CYS C  61  ? 0.8456 0.9824 0.7635 0.0370  -0.0266 0.0097  61  CYS C CA  
4224  C C   . CYS C  61  ? 0.8925 1.0235 0.8101 0.0334  -0.0269 0.0058  61  CYS C C   
4225  O O   . CYS C  61  ? 0.9397 1.0696 0.8578 0.0321  -0.0285 0.0040  61  CYS C O   
4226  C CB  . CYS C  61  ? 0.7516 0.8823 0.6743 0.0405  -0.0254 0.0122  61  CYS C CB  
4227  S SG  . CYS C  61  ? 1.0230 1.1593 0.9467 0.0450  -0.0244 0.0172  61  CYS C SG  
4228  N N   . ASN C  62  ? 0.7046 0.8321 0.6216 0.0318  -0.0251 0.0046  62  ASN C N   
4229  C CA  . ASN C  62  ? 0.7839 0.9049 0.7018 0.0288  -0.0248 0.0014  62  ASN C CA  
4230  C C   . ASN C  62  ? 0.7341 0.8467 0.6570 0.0304  -0.0237 0.0023  62  ASN C C   
4231  O O   . ASN C  62  ? 0.6821 0.7939 0.6071 0.0335  -0.0228 0.0051  62  ASN C O   
4232  C CB  . ASN C  62  ? 0.8255 0.9490 0.7390 0.0252  -0.0235 -0.0012 62  ASN C CB  
4233  C CG  . ASN C  62  ? 0.7167 0.8413 0.6286 0.0259  -0.0211 0.0002  62  ASN C CG  
4234  O OD1 . ASN C  62  ? 0.7371 0.8582 0.6522 0.0288  -0.0201 0.0027  62  ASN C OD1 
4235  N ND2 . ASN C  62  ? 0.7120 0.8415 0.6187 0.0230  -0.0201 -0.0014 62  ASN C ND2 
4236  N N   . ILE C  63  ? 0.5821 0.6884 0.5069 0.0282  -0.0236 0.0001  63  ILE C N   
4237  C CA  . ILE C  63  ? 0.5644 0.6627 0.4945 0.0294  -0.0227 0.0009  63  ILE C CA  
4238  C C   . ILE C  63  ? 0.5135 0.6110 0.4444 0.0312  -0.0202 0.0028  63  ILE C C   
4239  O O   . ILE C  63  ? 0.5450 0.6393 0.4798 0.0340  -0.0199 0.0051  63  ILE C O   
4240  C CB  . ILE C  63  ? 0.6672 0.7599 0.5989 0.0263  -0.0224 -0.0017 63  ILE C CB  
4241  C CG1 . ILE C  63  ? 0.5602 0.6532 0.4914 0.0246  -0.0249 -0.0034 63  ILE C CG1 
4242  C CG2 . ILE C  63  ? 0.5288 0.6139 0.4664 0.0276  -0.0217 -0.0006 63  ILE C CG2 
4243  C CD1 . ILE C  63  ? 0.7117 0.8021 0.6464 0.0267  -0.0270 -0.0019 63  ILE C CD1 
4244  N N   . ALA C  64  ? 0.5160 0.6164 0.4430 0.0294  -0.0184 0.0017  64  ALA C N   
4245  C CA  . ALA C  64  ? 0.5724 0.6722 0.4994 0.0307  -0.0157 0.0033  64  ALA C CA  
4246  C C   . ALA C  64  ? 0.6614 0.7643 0.5890 0.0346  -0.0160 0.0069  64  ALA C C   
4247  O O   . ALA C  64  ? 0.6445 0.7431 0.5760 0.0370  -0.0147 0.0089  64  ALA C O   
4248  C CB  . ALA C  64  ? 0.5471 0.6512 0.4684 0.0278  -0.0140 0.0015  64  ALA C CB  
4249  N N   . GLY C  65  ? 0.5801 0.6905 0.5042 0.0352  -0.0175 0.0078  65  GLY C N   
4250  C CA  . GLY C  65  ? 0.6042 0.7184 0.5290 0.0389  -0.0176 0.0115  65  GLY C CA  
4251  C C   . GLY C  65  ? 0.6964 0.8055 0.6269 0.0418  -0.0183 0.0131  65  GLY C C   
4252  O O   . GLY C  65  ? 0.8232 0.9310 0.7563 0.0450  -0.0171 0.0160  65  GLY C O   
4253  N N   . TRP C  66  ? 0.5886 0.6947 0.5209 0.0406  -0.0202 0.0112  66  TRP C N   
4254  C CA  . TRP C  66  ? 0.6766 0.7780 0.6137 0.0427  -0.0211 0.0123  66  TRP C CA  
4255  C C   . TRP C  66  ? 0.5978 0.6917 0.5398 0.0438  -0.0196 0.0131  66  TRP C C   
4256  O O   . TRP C  66  ? 0.7612 0.8529 0.7066 0.0466  -0.0190 0.0153  66  TRP C O   
4257  C CB  . TRP C  66  ? 0.6588 0.7588 0.5962 0.0406  -0.0235 0.0100  66  TRP C CB  
4258  C CG  . TRP C  66  ? 0.7333 0.8270 0.6756 0.0417  -0.0243 0.0104  66  TRP C CG  
4259  C CD1 . TRP C  66  ? 0.8783 0.9714 0.8231 0.0447  -0.0243 0.0125  66  TRP C CD1 
4260  C CD2 . TRP C  66  ? 0.7093 0.7964 0.6544 0.0397  -0.0252 0.0086  66  TRP C CD2 
4261  N NE1 . TRP C  66  ? 0.7759 0.8626 0.7246 0.0444  -0.0252 0.0119  66  TRP C NE1 
4262  C CE2 . TRP C  66  ? 0.6776 0.7607 0.6266 0.0414  -0.0259 0.0097  66  TRP C CE2 
4263  C CE3 . TRP C  66  ? 0.7316 0.8160 0.6765 0.0367  -0.0254 0.0063  66  TRP C CE3 
4264  C CZ2 . TRP C  66  ? 0.7193 0.7963 0.6718 0.0400  -0.0271 0.0086  66  TRP C CZ2 
4265  C CZ3 . TRP C  66  ? 0.6905 0.7686 0.6392 0.0355  -0.0264 0.0055  66  TRP C CZ3 
4266  C CH2 . TRP C  66  ? 0.6529 0.7277 0.6053 0.0371  -0.0275 0.0067  66  TRP C CH2 
4267  N N   . ILE C  67  ? 0.6190 0.7088 0.5615 0.0414  -0.0187 0.0112  67  ILE C N   
4268  C CA  . ILE C  67  ? 0.7121 0.7947 0.6596 0.0421  -0.0173 0.0117  67  ILE C CA  
4269  C C   . ILE C  67  ? 0.7184 0.8012 0.6661 0.0442  -0.0145 0.0139  67  ILE C C   
4270  O O   . ILE C  67  ? 0.6517 0.7302 0.6039 0.0464  -0.0135 0.0157  67  ILE C O   
4271  C CB  . ILE C  67  ? 0.5405 0.6184 0.4893 0.0390  -0.0171 0.0092  67  ILE C CB  
4272  C CG1 . ILE C  67  ? 0.8590 0.9383 0.8060 0.0364  -0.0195 0.0068  67  ILE C CG1 
4273  C CG2 . ILE C  67  ? 0.5828 0.6533 0.5381 0.0398  -0.0167 0.0099  67  ILE C CG2 
4274  C CD1 . ILE C  67  ? 1.0443 1.1191 0.9928 0.0335  -0.0192 0.0046  67  ILE C CD1 
4275  N N   . LEU C  68  ? 0.6771 0.7649 0.6199 0.0434  -0.0133 0.0137  68  LEU C N   
4276  C CA  . LEU C  68  ? 0.6567 0.7452 0.5989 0.0451  -0.0106 0.0159  68  LEU C CA  
4277  C C   . LEU C  68  ? 0.7322 0.8235 0.6753 0.0490  -0.0106 0.0194  68  LEU C C   
4278  O O   . LEU C  68  ? 0.7395 0.8288 0.6847 0.0513  -0.0085 0.0216  68  LEU C O   
4279  C CB  . LEU C  68  ? 0.5499 0.6437 0.4858 0.0429  -0.0094 0.0148  68  LEU C CB  
4280  C CG  . LEU C  68  ? 0.6363 0.7264 0.5716 0.0393  -0.0079 0.0116  68  LEU C CG  
4281  C CD1 . LEU C  68  ? 0.5305 0.6259 0.4592 0.0372  -0.0063 0.0107  68  LEU C CD1 
4282  C CD2 . LEU C  68  ? 0.4538 0.5360 0.3946 0.0402  -0.0057 0.0121  68  LEU C CD2 
4283  N N   . GLY C  69  ? 0.7306 0.8265 0.6724 0.0496  -0.0127 0.0198  69  GLY C N   
4284  C CA  . GLY C  69  ? 0.7581 0.8568 0.7012 0.0533  -0.0126 0.0231  69  GLY C CA  
4285  C C   . GLY C  69  ? 0.8756 0.9828 0.8139 0.0542  -0.0122 0.0252  69  GLY C C   
4286  O O   . GLY C  69  ? 0.9344 1.0434 0.8735 0.0573  -0.0107 0.0286  69  GLY C O   
4287  N N   . ASN C  70  ? 0.8414 0.9542 0.7749 0.0515  -0.0136 0.0233  70  ASN C N   
4288  C CA  . ASN C  70  ? 0.9561 1.0780 0.8848 0.0519  -0.0137 0.0252  70  ASN C CA  
4289  C C   . ASN C  70  ? 1.0617 1.1874 0.9926 0.0557  -0.0142 0.0288  70  ASN C C   
4290  O O   . ASN C  70  ? 0.9408 1.0648 0.8745 0.0564  -0.0156 0.0283  70  ASN C O   
4291  C CB  . ASN C  70  ? 0.9425 1.0696 0.8664 0.0482  -0.0156 0.0222  70  ASN C CB  
4292  C CG  . ASN C  70  ? 0.9825 1.1193 0.9011 0.0478  -0.0157 0.0239  70  ASN C CG  
4293  O OD1 . ASN C  70  ? 0.9852 1.1274 0.9042 0.0509  -0.0159 0.0276  70  ASN C OD1 
4294  N ND2 . ASN C  70  ? 0.8845 1.0239 0.7981 0.0440  -0.0155 0.0212  70  ASN C ND2 
4295  N N   . PRO C  71  ? 1.2172 1.3479 1.1469 0.0582  -0.0130 0.0325  71  PRO C N   
4296  C CA  . PRO C  71  ? 1.0501 1.1845 0.9823 0.0621  -0.0129 0.0366  71  PRO C CA  
4297  C C   . PRO C  71  ? 1.0903 1.2296 1.0223 0.0618  -0.0153 0.0360  71  PRO C C   
4298  O O   . PRO C  71  ? 1.3361 1.4752 1.2718 0.0647  -0.0153 0.0381  71  PRO C O   
4299  C CB  . PRO C  71  ? 1.0802 1.2219 1.0089 0.0634  -0.0118 0.0400  71  PRO C CB  
4300  C CG  . PRO C  71  ? 1.0838 1.2214 1.0104 0.0613  -0.0101 0.0384  71  PRO C CG  
4301  C CD  . PRO C  71  ? 1.0832 1.2160 1.0092 0.0573  -0.0112 0.0333  71  PRO C CD  
4302  N N   . GLU C  72  ? 1.0596 1.2028 0.9873 0.0582  -0.0171 0.0330  72  GLU C N   
4303  C CA  . GLU C  72  ? 1.1747 1.3228 1.1017 0.0575  -0.0194 0.0322  72  GLU C CA  
4304  C C   . GLU C  72  ? 1.0740 1.2157 1.0033 0.0558  -0.0207 0.0287  72  GLU C C   
4305  O O   . GLU C  72  ? 0.9432 1.0880 0.8724 0.0553  -0.0223 0.0279  72  GLU C O   
4306  C CB  . GLU C  72  ? 1.1407 1.2973 1.0618 0.0544  -0.0208 0.0310  72  GLU C CB  
4307  C CG  . GLU C  72  ? 1.3521 1.5167 1.2702 0.0556  -0.0200 0.0346  72  GLU C CG  
4308  C CD  . GLU C  72  ? 1.5613 1.7320 1.4819 0.0597  -0.0202 0.0395  72  GLU C CD  
4309  O OE1 . GLU C  72  ? 1.5294 1.7004 1.4529 0.0607  -0.0212 0.0394  72  GLU C OE1 
4310  O OE2 . GLU C  72  ? 1.4049 1.5804 1.3247 0.0618  -0.0191 0.0434  72  GLU C OE2 
4311  N N   . CYS C  73  ? 1.1488 1.2817 1.0804 0.0550  -0.0199 0.0267  73  CYS C N   
4312  C CA  . CYS C  73  ? 1.2552 1.3821 1.1885 0.0529  -0.0212 0.0234  73  CYS C CA  
4313  C C   . CYS C  73  ? 1.4206 1.5408 1.3594 0.0554  -0.0207 0.0244  73  CYS C C   
4314  O O   . CYS C  73  ? 1.4641 1.5767 1.4055 0.0546  -0.0203 0.0229  73  CYS C O   
4315  C CB  . CYS C  73  ? 1.0434 1.1653 0.9756 0.0497  -0.0209 0.0203  73  CYS C CB  
4316  S SG  . CYS C  73  ? 1.1165 1.2448 1.0422 0.0455  -0.0215 0.0177  73  CYS C SG  
4317  N N   . GLU C  74  ? 1.6588 1.7818 1.5995 0.0582  -0.0205 0.0268  74  GLU C N   
4318  C CA  . GLU C  74  ? 1.8187 1.9368 1.7642 0.0615  -0.0188 0.0291  74  GLU C CA  
4319  C C   . GLU C  74  ? 1.9118 2.0290 1.8594 0.0621  -0.0197 0.0286  74  GLU C C   
4320  O O   . GLU C  74  ? 1.8436 1.9636 1.7931 0.0651  -0.0187 0.0313  74  GLU C O   
4321  C CB  . GLU C  74  ? 1.8309 1.9540 1.7761 0.0646  -0.0169 0.0332  74  GLU C CB  
4322  C CG  . GLU C  74  ? 1.8576 1.9799 1.8070 0.0689  -0.0148 0.0370  74  GLU C CG  
4323  C CD  . GLU C  74  ? 1.9602 2.0913 1.9073 0.0707  -0.0144 0.0404  74  GLU C CD  
4324  O OE1 . GLU C  74  ? 1.9407 2.0778 1.8857 0.0696  -0.0161 0.0399  74  GLU C OE1 
4325  O OE2 . GLU C  74  ? 1.8950 2.0278 1.8419 0.0725  -0.0127 0.0433  74  GLU C OE2 
4326  N N   . SER C  75  ? 1.8807 1.9939 1.8278 0.0590  -0.0214 0.0250  75  SER C N   
4327  C CA  . SER C  75  ? 2.0999 2.2141 2.0468 0.0582  -0.0229 0.0236  75  SER C CA  
4328  C C   . SER C  75  ? 2.2212 2.3286 2.1720 0.0590  -0.0225 0.0232  75  SER C C   
4329  O O   . SER C  75  ? 2.1877 2.2900 2.1386 0.0564  -0.0239 0.0203  75  SER C O   
4330  C CB  . SER C  75  ? 2.0482 2.1633 1.9915 0.0542  -0.0252 0.0201  75  SER C CB  
4331  O OG  . SER C  75  ? 1.9320 2.0505 1.8721 0.0528  -0.0252 0.0198  75  SER C OG  
4332  N N   . LEU C  76  ? 2.3583 2.4661 2.3121 0.0625  -0.0204 0.0262  76  LEU C N   
4333  C CA  . LEU C  76  ? 2.2951 2.3975 2.2525 0.0636  -0.0194 0.0261  76  LEU C CA  
4334  C C   . LEU C  76  ? 2.3172 2.4111 2.2763 0.0616  -0.0199 0.0238  76  LEU C C   
4335  O O   . LEU C  76  ? 2.2538 2.3430 2.2146 0.0609  -0.0200 0.0224  76  LEU C O   
4336  C CB  . LEU C  76  ? 2.1879 2.2924 2.1442 0.0627  -0.0204 0.0247  76  LEU C CB  
4337  C CG  . LEU C  76  ? 1.9858 2.0862 1.9455 0.0643  -0.0187 0.0252  76  LEU C CG  
4338  C CD1 . LEU C  76  ? 1.6473 1.7494 1.6105 0.0687  -0.0156 0.0293  76  LEU C CD1 
4339  C CD2 . LEU C  76  ? 1.9606 2.0636 1.9189 0.0633  -0.0196 0.0238  76  LEU C CD2 
4340  N N   . SER C  77  ? 2.7566 2.8489 2.7153 0.0606  -0.0201 0.0234  77  SER C N   
4341  C CA  . SER C  77  ? 2.6544 2.7392 2.6163 0.0601  -0.0196 0.0228  77  SER C CA  
4342  C C   . SER C  77  ? 2.4566 2.5358 2.4189 0.0566  -0.0218 0.0195  77  SER C C   
4343  O O   . SER C  77  ? 2.2682 2.3414 2.2335 0.0560  -0.0216 0.0191  77  SER C O   
4344  C CB  . SER C  77  ? 2.5082 2.5901 2.4743 0.0635  -0.0168 0.0254  77  SER C CB  
4345  O OG  . SER C  77  ? 2.1356 2.2141 2.1039 0.0637  -0.0164 0.0248  77  SER C OG  
4346  N N   . THR C  78  ? 2.7083 2.7894 2.6678 0.0544  -0.0239 0.0175  78  THR C N   
4347  C CA  . THR C  78  ? 2.6328 2.7111 2.5909 0.0507  -0.0264 0.0146  78  THR C CA  
4348  C C   . THR C  78  ? 2.5394 2.6105 2.5002 0.0487  -0.0276 0.0130  78  THR C C   
4349  O O   . THR C  78  ? 2.4745 2.5415 2.4379 0.0492  -0.0269 0.0132  78  THR C O   
4350  C CB  . THR C  78  ? 2.4844 2.5644 2.4405 0.0489  -0.0272 0.0138  78  THR C CB  
4351  O OG1 . THR C  78  ? 2.5310 2.6132 2.4876 0.0512  -0.0251 0.0159  78  THR C OG1 
4352  C CG2 . THR C  78  ? 1.8147 1.9000 1.7663 0.0470  -0.0288 0.0121  78  THR C CG2 
4353  N N   . ALA C  79  ? 2.1455 2.2153 2.1055 0.0460  -0.0293 0.0115  79  ALA C N   
4354  C CA  . ALA C  79  ? 1.8195 1.8852 1.7798 0.0430  -0.0316 0.0094  79  ALA C CA  
4355  C C   . ALA C  79  ? 1.5745 1.6341 1.5387 0.0417  -0.0322 0.0093  79  ALA C C   
4356  O O   . ALA C  79  ? 1.4875 1.5449 1.4550 0.0435  -0.0305 0.0108  79  ALA C O   
4357  C CB  . ALA C  79  ? 1.6253 1.6942 1.5818 0.0405  -0.0334 0.0076  79  ALA C CB  
4358  N N   . SER C  80  ? 1.0659 1.1227 1.0299 0.0387  -0.0347 0.0076  80  SER C N   
4359  C CA  . SER C  80  ? 1.0093 1.0610 0.9771 0.0370  -0.0358 0.0075  80  SER C CA  
4360  C C   . SER C  80  ? 0.8603 0.9118 0.8268 0.0340  -0.0381 0.0061  80  SER C C   
4361  O O   . SER C  80  ? 0.8539 0.9022 0.8236 0.0327  -0.0390 0.0064  80  SER C O   
4362  C CB  . SER C  80  ? 1.1062 1.1539 1.0758 0.0362  -0.0367 0.0072  80  SER C CB  
4363  O OG  . SER C  80  ? 1.2165 1.2645 1.1829 0.0337  -0.0389 0.0055  80  SER C OG  
4364  N N   . SER C  81  ? 0.7471 0.8024 0.7092 0.0330  -0.0390 0.0049  81  SER C N   
4365  C CA  . SER C  81  ? 0.6568 0.7120 0.6174 0.0301  -0.0408 0.0035  81  SER C CA  
4366  C C   . SER C  81  ? 0.6034 0.6636 0.5590 0.0294  -0.0411 0.0021  81  SER C C   
4367  O O   . SER C  81  ? 0.5691 0.6325 0.5222 0.0306  -0.0405 0.0021  81  SER C O   
4368  C CB  . SER C  81  ? 0.7391 0.7903 0.7010 0.0276  -0.0434 0.0029  81  SER C CB  
4369  O OG  . SER C  81  ? 0.7478 0.7994 0.7072 0.0272  -0.0442 0.0021  81  SER C OG  
4370  N N   . TRP C  82  ? 0.4632 0.5239 0.4176 0.0272  -0.0419 0.0011  82  TRP C N   
4371  C CA  . TRP C  82  ? 0.5833 0.6483 0.5331 0.0260  -0.0424 -0.0005 82  TRP C CA  
4372  C C   . TRP C  82  ? 0.5325 0.5961 0.4819 0.0230  -0.0437 -0.0018 82  TRP C C   
4373  O O   . TRP C  82  ? 0.4657 0.5263 0.4181 0.0223  -0.0434 -0.0013 82  TRP C O   
4374  C CB  . TRP C  82  ? 0.5674 0.6376 0.5150 0.0278  -0.0403 -0.0002 82  TRP C CB  
4375  C CG  . TRP C  82  ? 0.4698 0.5392 0.4194 0.0282  -0.0386 0.0004  82  TRP C CG  
4376  C CD1 . TRP C  82  ? 0.5562 0.6256 0.5051 0.0263  -0.0382 -0.0007 82  TRP C CD1 
4377  C CD2 . TRP C  82  ? 0.4958 0.5640 0.4484 0.0307  -0.0367 0.0023  82  TRP C CD2 
4378  N NE1 . TRP C  82  ? 0.5015 0.5697 0.4527 0.0273  -0.0362 0.0003  82  TRP C NE1 
4379  C CE2 . TRP C  82  ? 0.5172 0.5847 0.4706 0.0301  -0.0353 0.0021  82  TRP C CE2 
4380  C CE3 . TRP C  82  ? 0.5450 0.6123 0.4996 0.0334  -0.0358 0.0040  82  TRP C CE3 
4381  C CZ2 . TRP C  82  ? 0.5343 0.6003 0.4903 0.0320  -0.0332 0.0037  82  TRP C CZ2 
4382  C CZ3 . TRP C  82  ? 0.5670 0.6330 0.5244 0.0354  -0.0338 0.0056  82  TRP C CZ3 
4383  C CH2 . TRP C  82  ? 0.4640 0.5294 0.4220 0.0347  -0.0325 0.0055  82  TRP C CH2 
4384  N N   . SER C  83  ? 0.5585 0.6241 0.5042 0.0212  -0.0450 -0.0033 83  SER C N   
4385  C CA  . SER C  83  ? 0.5372 0.6015 0.4822 0.0183  -0.0463 -0.0045 83  SER C CA  
4386  C C   . SER C  83  ? 0.5203 0.5874 0.4639 0.0177  -0.0446 -0.0054 83  SER C C   
4387  O O   . SER C  83  ? 0.5388 0.6035 0.4839 0.0160  -0.0445 -0.0058 83  SER C O   
4388  C CB  . SER C  83  ? 0.5174 0.5828 0.4589 0.0165  -0.0481 -0.0059 83  SER C CB  
4389  O OG  . SER C  83  ? 0.6500 0.7205 0.5879 0.0176  -0.0472 -0.0066 83  SER C OG  
4390  N N   . TYR C  84  ? 0.4705 0.5427 0.4113 0.0191  -0.0431 -0.0057 84  TYR C N   
4391  C CA  . TYR C  84  ? 0.4409 0.5163 0.3799 0.0185  -0.0414 -0.0067 84  TYR C CA  
4392  C C   . TYR C  84  ? 0.4970 0.5773 0.4341 0.0209  -0.0398 -0.0059 84  TYR C C   
4393  O O   . TYR C  84  ? 0.5624 0.6438 0.4999 0.0231  -0.0400 -0.0046 84  TYR C O   
4394  C CB  . TYR C  84  ? 0.4888 0.5664 0.4241 0.0158  -0.0421 -0.0089 84  TYR C CB  
4395  C CG  . TYR C  84  ? 0.4463 0.5284 0.3780 0.0159  -0.0431 -0.0096 84  TYR C CG  
4396  C CD1 . TYR C  84  ? 0.5391 0.6276 0.4674 0.0163  -0.0421 -0.0103 84  TYR C CD1 
4397  C CD2 . TYR C  84  ? 0.4468 0.5270 0.3785 0.0157  -0.0449 -0.0095 84  TYR C CD2 
4398  C CE1 . TYR C  84  ? 0.5357 0.6285 0.4612 0.0165  -0.0428 -0.0108 84  TYR C CE1 
4399  C CE2 . TYR C  84  ? 0.4329 0.5169 0.3615 0.0158  -0.0455 -0.0102 84  TYR C CE2 
4400  C CZ  . TYR C  84  ? 0.5051 0.5955 0.4309 0.0163  -0.0444 -0.0108 84  TYR C CZ  
4401  O OH  . TYR C  84  ? 0.5821 0.6766 0.5055 0.0166  -0.0449 -0.0113 84  TYR C OH  
4402  N N   . ILE C  85  ? 0.4163 0.4997 0.3516 0.0204  -0.0381 -0.0066 85  ILE C N   
4403  C CA  . ILE C  85  ? 0.5145 0.6031 0.4480 0.0225  -0.0366 -0.0056 85  ILE C CA  
4404  C C   . ILE C  85  ? 0.5681 0.6636 0.4969 0.0212  -0.0367 -0.0071 85  ILE C C   
4405  O O   . ILE C  85  ? 0.5017 0.5977 0.4285 0.0184  -0.0365 -0.0093 85  ILE C O   
4406  C CB  . ILE C  85  ? 0.4836 0.5708 0.4187 0.0231  -0.0344 -0.0049 85  ILE C CB  
4407  C CG1 . ILE C  85  ? 0.3950 0.4759 0.3352 0.0247  -0.0343 -0.0032 85  ILE C CG1 
4408  C CG2 . ILE C  85  ? 0.4902 0.5833 0.4228 0.0250  -0.0330 -0.0038 85  ILE C CG2 
4409  C CD1 . ILE C  85  ? 0.4643 0.5430 0.4067 0.0252  -0.0319 -0.0025 85  ILE C CD1 
4410  N N   . VAL C  86  ? 0.5269 0.6276 0.4541 0.0233  -0.0367 -0.0059 86  VAL C N   
4411  C CA  . VAL C  86  ? 0.5626 0.6707 0.4857 0.0224  -0.0369 -0.0069 86  VAL C CA  
4412  C C   . VAL C  86  ? 0.5295 0.6431 0.4510 0.0238  -0.0353 -0.0056 86  VAL C C   
4413  O O   . VAL C  86  ? 0.6326 0.7467 0.5558 0.0269  -0.0347 -0.0030 86  VAL C O   
4414  C CB  . VAL C  86  ? 0.5449 0.6559 0.4675 0.0234  -0.0383 -0.0065 86  VAL C CB  
4415  C CG1 . VAL C  86  ? 0.4920 0.6109 0.4107 0.0223  -0.0385 -0.0075 86  VAL C CG1 
4416  C CG2 . VAL C  86  ? 0.5842 0.6898 0.5077 0.0218  -0.0399 -0.0078 86  VAL C CG2 
4417  N N   . GLU C  87  ? 0.5427 0.6604 0.4607 0.0214  -0.0347 -0.0073 87  GLU C N   
4418  C CA  . GLU C  87  ? 0.5996 0.7233 0.5152 0.0221  -0.0334 -0.0063 87  GLU C CA  
4419  C C   . GLU C  87  ? 0.7781 0.9101 0.6897 0.0206  -0.0343 -0.0073 87  GLU C C   
4420  O O   . GLU C  87  ? 0.7383 0.8707 0.6482 0.0177  -0.0350 -0.0099 87  GLU C O   
4421  C CB  . GLU C  87  ? 0.6337 0.7548 0.5485 0.0200  -0.0315 -0.0077 87  GLU C CB  
4422  C CG  . GLU C  87  ? 0.7867 0.9075 0.7024 0.0223  -0.0297 -0.0054 87  GLU C CG  
4423  C CD  . GLU C  87  ? 0.7916 0.9087 0.7069 0.0201  -0.0275 -0.0070 87  GLU C CD  
4424  O OE1 . GLU C  87  ? 0.7833 0.8961 0.7014 0.0218  -0.0260 -0.0055 87  GLU C OE1 
4425  O OE2 . GLU C  87  ? 0.6952 0.8134 0.6076 0.0166  -0.0270 -0.0099 87  GLU C OE2 
4426  N N   . THR C  88  ? 0.8414 0.9804 0.7519 0.0227  -0.0342 -0.0050 88  THR C N   
4427  C CA  . THR C  88  ? 0.8565 1.0044 0.7635 0.0214  -0.0351 -0.0055 88  THR C CA  
4428  C C   . THR C  88  ? 0.9247 1.0768 0.8277 0.0186  -0.0340 -0.0071 88  THR C C   
4429  O O   . THR C  88  ? 1.0430 1.1938 0.9457 0.0192  -0.0324 -0.0062 88  THR C O   
4430  C CB  . THR C  88  ? 0.9984 1.1526 0.9064 0.0250  -0.0356 -0.0020 88  THR C CB  
4431  O OG1 . THR C  88  ? 1.1097 1.2661 1.0176 0.0269  -0.0343 0.0006  88  THR C OG1 
4432  C CG2 . THR C  88  ? 0.8431 0.9926 0.7552 0.0278  -0.0362 -0.0005 88  THR C CG2 
4433  N N   . PRO C  89  ? 1.1927 1.3496 1.0922 0.0153  -0.0347 -0.0097 89  PRO C N   
4434  C CA  . PRO C  89  ? 1.1955 1.3566 1.0906 0.0120  -0.0336 -0.0117 89  PRO C CA  
4435  C C   . PRO C  89  ? 1.2775 1.4459 1.1707 0.0136  -0.0332 -0.0089 89  PRO C C   
4436  O O   . PRO C  89  ? 1.2880 1.4593 1.1775 0.0111  -0.0319 -0.0101 89  PRO C O   
4437  C CB  . PRO C  89  ? 1.0735 1.2400 0.9659 0.0089  -0.0348 -0.0142 89  PRO C CB  
4438  C CG  . PRO C  89  ? 1.0978 1.2592 0.9933 0.0099  -0.0361 -0.0146 89  PRO C CG  
4439  C CD  . PRO C  89  ? 1.2067 1.3652 1.1062 0.0144  -0.0363 -0.0110 89  PRO C CD  
4440  N N   . SER C  90  ? 1.1977 1.3689 1.0935 0.0176  -0.0340 -0.0051 90  SER C N   
4441  C CA  . SER C  90  ? 1.2701 1.4488 1.1644 0.0196  -0.0339 -0.0018 90  SER C CA  
4442  C C   . SER C  90  ? 1.4135 1.5873 1.3108 0.0232  -0.0325 0.0012  90  SER C C   
4443  O O   . SER C  90  ? 1.5910 1.7698 1.4889 0.0262  -0.0325 0.0050  90  SER C O   
4444  C CB  . SER C  90  ? 1.4428 1.6299 1.3380 0.0215  -0.0357 0.0007  90  SER C CB  
4445  O OG  . SER C  90  ? 1.7149 1.9102 1.6086 0.0231  -0.0357 0.0041  90  SER C OG  
4446  N N   . SER C  91  ? 1.4209 1.5851 1.3204 0.0229  -0.0313 -0.0003 91  SER C N   
4447  C CA  . SER C  91  ? 1.3125 1.4713 1.2151 0.0260  -0.0298 0.0023  91  SER C CA  
4448  C C   . SER C  91  ? 1.3747 1.5327 1.2745 0.0242  -0.0277 0.0015  91  SER C C   
4449  O O   . SER C  91  ? 1.3073 1.4606 1.2060 0.0210  -0.0266 -0.0018 91  SER C O   
4450  C CB  . SER C  91  ? 1.1444 1.2932 1.0515 0.0269  -0.0298 0.0015  91  SER C CB  
4451  O OG  . SER C  91  ? 1.1431 1.2868 1.0494 0.0233  -0.0293 -0.0023 91  SER C OG  
4452  N N   . ASP C  92  ? 1.5018 1.6641 1.4006 0.0263  -0.0269 0.0047  92  ASP C N   
4453  C CA  . ASP C  92  ? 1.5968 1.7592 1.4922 0.0246  -0.0248 0.0042  92  ASP C CA  
4454  C C   . ASP C  92  ? 1.4571 1.6160 1.3552 0.0282  -0.0231 0.0075  92  ASP C C   
4455  O O   . ASP C  92  ? 1.5719 1.7301 1.4676 0.0272  -0.0211 0.0074  92  ASP C O   
4456  C CB  . ASP C  92  ? 1.8097 1.9827 1.6994 0.0224  -0.0254 0.0043  92  ASP C CB  
4457  C CG  . ASP C  92  ? 1.9150 2.0910 1.8015 0.0181  -0.0265 0.0003  92  ASP C CG  
4458  O OD1 . ASP C  92  ? 1.9423 2.1113 1.8302 0.0161  -0.0260 -0.0030 92  ASP C OD1 
4459  O OD2 . ASP C  92  ? 1.9213 2.1070 1.8041 0.0166  -0.0278 0.0006  92  ASP C OD2 
4460  N N   . ASN C  93  ? 1.2496 1.4062 1.1525 0.0322  -0.0238 0.0104  93  ASN C N   
4461  C CA  . ASN C  93  ? 1.3419 1.4946 1.2478 0.0357  -0.0221 0.0136  93  ASN C CA  
4462  C C   . ASN C  93  ? 1.1804 1.3225 1.0897 0.0353  -0.0205 0.0117  93  ASN C C   
4463  O O   . ASN C  93  ? 1.0394 1.1755 0.9537 0.0373  -0.0209 0.0122  93  ASN C O   
4464  C CB  . ASN C  93  ? 1.2944 1.4489 1.2044 0.0402  -0.0230 0.0174  93  ASN C CB  
4465  C CG  . ASN C  93  ? 1.3444 1.5093 1.2518 0.0417  -0.0237 0.0208  93  ASN C CG  
4466  O OD1 . ASN C  93  ? 1.3745 1.5445 1.2830 0.0431  -0.0253 0.0222  93  ASN C OD1 
4467  N ND2 . ASN C  93  ? 1.2916 1.4600 1.1957 0.0414  -0.0223 0.0223  93  ASN C ND2 
4468  N N   . GLY C  94  ? 1.1591 1.2991 1.0657 0.0325  -0.0186 0.0095  94  GLY C N   
4469  C CA  . GLY C  94  ? 1.0242 1.1547 0.9340 0.0318  -0.0168 0.0079  94  GLY C CA  
4470  C C   . GLY C  94  ? 1.0545 1.1832 0.9640 0.0330  -0.0141 0.0096  94  GLY C C   
4471  O O   . GLY C  94  ? 1.0857 1.2142 0.9978 0.0367  -0.0137 0.0132  94  GLY C O   
4472  N N   . THR C  95  ? 0.8602 0.9873 0.7667 0.0298  -0.0119 0.0071  95  THR C N   
4473  C CA  . THR C  95  ? 0.9134 1.0390 0.8188 0.0304  -0.0091 0.0085  95  THR C CA  
4474  C C   . THR C  95  ? 0.8657 1.0007 0.7657 0.0308  -0.0092 0.0109  95  THR C C   
4475  O O   . THR C  95  ? 0.9085 1.0489 0.8026 0.0274  -0.0091 0.0089  95  THR C O   
4476  C CB  . THR C  95  ? 0.7377 0.8584 0.6416 0.0266  -0.0063 0.0050  95  THR C CB  
4477  O OG1 . THR C  95  ? 0.5949 0.7073 0.5043 0.0263  -0.0063 0.0031  95  THR C OG1 
4478  N N   . CYS C  96  ? 0.8510 0.9881 0.7531 0.0350  -0.0096 0.0152  96  CYS C N   
4479  C CA  . CYS C  96  ? 0.8241 0.9699 0.7217 0.0359  -0.0096 0.0183  96  CYS C CA  
4480  C C   . CYS C  96  ? 0.7886 0.9336 0.6823 0.0342  -0.0065 0.0179  96  CYS C C   
4481  O O   . CYS C  96  ? 0.7834 0.9359 0.6710 0.0325  -0.0065 0.0185  96  CYS C O   
4482  C CB  . CYS C  96  ? 0.8001 0.9477 0.7016 0.0411  -0.0103 0.0232  96  CYS C CB  
4483  S SG  . CYS C  96  ? 1.0348 1.1713 0.9441 0.0448  -0.0085 0.0247  96  CYS C SG  
4484  N N   . TYR C  97  ? 0.7530 0.8887 0.6501 0.0344  -0.0040 0.0168  97  TYR C N   
4485  C CA  . TYR C  97  ? 0.7363 0.8700 0.6299 0.0324  -0.0006 0.0159  97  TYR C CA  
4486  C C   . TYR C  97  ? 0.7060 0.8360 0.5975 0.0275  0.0008  0.0108  97  TYR C C   
4487  O O   . TYR C  97  ? 0.7684 0.8910 0.6647 0.0271  0.0009  0.0086  97  TYR C O   
4488  C CB  . TYR C  97  ? 0.7564 0.8827 0.6550 0.0356  0.0019  0.0182  97  TYR C CB  
4489  C CG  . TYR C  97  ? 0.7572 0.8834 0.6517 0.0345  0.0052  0.0186  97  TYR C CG  
4490  C CD1 . TYR C  97  ? 0.8073 0.9356 0.7015 0.0378  0.0062  0.0230  97  TYR C CD1 
4491  C CD2 . TYR C  97  ? 0.7858 0.9096 0.6764 0.0299  0.0076  0.0146  97  TYR C CD2 
4492  C CE1 . TYR C  97  ? 0.9698 1.0980 0.8598 0.0365  0.0094  0.0233  97  TYR C CE1 
4493  C CE2 . TYR C  97  ? 0.7572 0.8808 0.6437 0.0286  0.0109  0.0147  97  TYR C CE2 
4494  C CZ  . TYR C  97  ? 0.8389 0.9647 0.7249 0.0319  0.0117  0.0191  97  TYR C CZ  
4495  O OH  . TYR C  97  ? 0.8028 0.9282 0.6844 0.0304  0.0151  0.0192  97  TYR C OH  
4496  N N   . PRO C  98  ? 0.7657 0.9009 0.6499 0.0236  0.0018  0.0089  98  PRO C N   
4497  C CA  . PRO C  98  ? 0.6150 0.7474 0.4966 0.0186  0.0035  0.0038  98  PRO C CA  
4498  C C   . PRO C  98  ? 0.7813 0.9027 0.6678 0.0184  0.0067  0.0020  98  PRO C C   
4499  O O   . PRO C  98  ? 0.8616 0.9791 0.7501 0.0206  0.0089  0.0041  98  PRO C O   
4500  C CB  . PRO C  98  ? 0.6350 0.7738 0.5081 0.0152  0.0051  0.0031  98  PRO C CB  
4501  C CG  . PRO C  98  ? 0.8562 1.0043 0.7271 0.0180  0.0025  0.0076  98  PRO C CG  
4502  C CD  . PRO C  98  ? 0.8811 1.0251 0.7592 0.0237  0.0017  0.0116  98  PRO C CD  
4503  N N   . GLY C  99  ? 0.7659 0.8825 0.6545 0.0158  0.0070  -0.0018 99  GLY C N   
4504  C CA  . GLY C  99  ? 0.6800 0.7864 0.5739 0.0155  0.0099  -0.0034 99  GLY C CA  
4505  C C   . GLY C  99  ? 0.7834 0.8854 0.6810 0.0138  0.0089  -0.0063 99  GLY C C   
4506  O O   . GLY C  99  ? 0.6304 0.7371 0.5265 0.0129  0.0059  -0.0072 99  GLY C O   
4507  N N   . ASP C  100 ? 0.8798 0.9730 0.7827 0.0134  0.0115  -0.0077 100 ASP C N   
4508  C CA  . ASP C  100 ? 0.7665 0.8549 0.6734 0.0117  0.0110  -0.0102 100 ASP C CA  
4509  C C   . ASP C  100 ? 0.6952 0.7785 0.6103 0.0153  0.0088  -0.0079 100 ASP C C   
4510  O O   . ASP C  100 ? 0.7606 0.8394 0.6802 0.0181  0.0101  -0.0056 100 ASP C O   
4511  C CB  . ASP C  100 ? 0.8031 0.8853 0.7104 0.0082  0.0155  -0.0135 100 ASP C CB  
4512  C CG  . ASP C  100 ? 1.1269 1.2059 1.0366 0.0056  0.0153  -0.0166 100 ASP C CG  
4513  O OD1 . ASP C  100 ? 1.2626 1.3458 1.1713 0.0055  0.0117  -0.0168 100 ASP C OD1 
4514  O OD2 . ASP C  100 ? 1.1666 1.2388 1.0794 0.0037  0.0188  -0.0186 100 ASP C OD2 
4515  N N   . PHE C  101 ? 0.4796 0.5637 0.3964 0.0152  0.0056  -0.0085 101 PHE C N   
4516  C CA  . PHE C  101 ? 0.5640 0.6433 0.4883 0.0180  0.0034  -0.0067 101 PHE C CA  
4517  C C   . PHE C  101 ? 0.5602 0.6323 0.4892 0.0159  0.0049  -0.0089 101 PHE C C   
4518  O O   . PHE C  101 ? 0.6444 0.7171 0.5725 0.0135  0.0038  -0.0111 101 PHE C O   
4519  C CB  . PHE C  101 ? 0.4991 0.5834 0.4225 0.0192  -0.0009 -0.0058 101 PHE C CB  
4520  C CG  . PHE C  101 ? 0.5175 0.5987 0.4469 0.0228  -0.0032 -0.0030 101 PHE C CG  
4521  C CD1 . PHE C  101 ? 0.5420 0.6278 0.4705 0.0259  -0.0054 -0.0002 101 PHE C CD1 
4522  C CD2 . PHE C  101 ? 0.5580 0.6317 0.4941 0.0232  -0.0031 -0.0030 101 PHE C CD2 
4523  C CE1 . PHE C  101 ? 0.4244 0.5072 0.3584 0.0290  -0.0072 0.0021  101 PHE C CE1 
4524  C CE2 . PHE C  101 ? 0.5240 0.5952 0.4655 0.0261  -0.0053 -0.0006 101 PHE C CE2 
4525  C CZ  . PHE C  101 ? 0.3619 0.4373 0.3020 0.0290  -0.0072 0.0018  101 PHE C CZ  
4526  N N   . ILE C  102 ? 0.4674 0.5328 0.4017 0.0169  0.0076  -0.0081 102 ILE C N   
4527  C CA  . ILE C  102 ? 0.4793 0.5378 0.4187 0.0150  0.0096  -0.0098 102 ILE C CA  
4528  C C   . ILE C  102 ? 0.4567 0.5131 0.4012 0.0156  0.0061  -0.0093 102 ILE C C   
4529  O O   . ILE C  102 ? 0.5336 0.5896 0.4815 0.0186  0.0033  -0.0067 102 ILE C O   
4530  C CB  . ILE C  102 ? 0.6644 0.7165 0.6094 0.0164  0.0129  -0.0085 102 ILE C CB  
4531  C CG1 . ILE C  102 ? 0.6456 0.6999 0.5853 0.0161  0.0162  -0.0085 102 ILE C CG1 
4532  C CG2 . ILE C  102 ? 0.4939 0.5392 0.4439 0.0142  0.0156  -0.0103 102 ILE C CG2 
4533  C CD1 . ILE C  102 ? 0.6290 0.6858 0.5618 0.0119  0.0189  -0.0121 102 ILE C CD1 
4534  N N   . ASP C  103 ? 0.5640 0.6187 0.5087 0.0127  0.0066  -0.0118 103 ASP C N   
4535  C CA  . ASP C  103 ? 0.5415 0.5942 0.4905 0.0128  0.0035  -0.0114 103 ASP C CA  
4536  C C   . ASP C  103 ? 0.5202 0.5782 0.4666 0.0146  -0.0011 -0.0101 103 ASP C C   
4537  O O   . ASP C  103 ? 0.5263 0.5823 0.4772 0.0165  -0.0039 -0.0081 103 ASP C O   
4538  C CB  . ASP C  103 ? 0.5892 0.6349 0.5471 0.0146  0.0037  -0.0092 103 ASP C CB  
4539  C CG  . ASP C  103 ? 0.6067 0.6467 0.5682 0.0129  0.0083  -0.0104 103 ASP C CG  
4540  O OD1 . ASP C  103 ? 0.6367 0.6769 0.5949 0.0097  0.0108  -0.0133 103 ASP C OD1 
4541  O OD2 . ASP C  103 ? 0.7323 0.7675 0.7002 0.0147  0.0097  -0.0085 103 ASP C OD2 
4542  N N   . TYR C  104 ? 0.4438 0.5086 0.3831 0.0137  -0.0016 -0.0111 104 TYR C N   
4543  C CA  . TYR C  104 ? 0.4459 0.5163 0.3825 0.0154  -0.0055 -0.0099 104 TYR C CA  
4544  C C   . TYR C  104 ? 0.4893 0.5595 0.4270 0.0143  -0.0084 -0.0108 104 TYR C C   
4545  O O   . TYR C  104 ? 0.5028 0.5729 0.4431 0.0164  -0.0115 -0.0090 104 TYR C O   
4546  C CB  . TYR C  104 ? 0.4081 0.4862 0.3370 0.0145  -0.0052 -0.0107 104 TYR C CB  
4547  C CG  . TYR C  104 ? 0.4346 0.5191 0.3609 0.0162  -0.0088 -0.0093 104 TYR C CG  
4548  C CD1 . TYR C  104 ? 0.4044 0.4883 0.3341 0.0199  -0.0108 -0.0063 104 TYR C CD1 
4549  C CD2 . TYR C  104 ? 0.4009 0.4919 0.3216 0.0141  -0.0100 -0.0112 104 TYR C CD2 
4550  C CE1 . TYR C  104 ? 0.4333 0.5226 0.3611 0.0215  -0.0137 -0.0050 104 TYR C CE1 
4551  C CE2 . TYR C  104 ? 0.4895 0.5863 0.4084 0.0157  -0.0132 -0.0098 104 TYR C CE2 
4552  C CZ  . TYR C  104 ? 0.4369 0.5327 0.3593 0.0195  -0.0149 -0.0067 104 TYR C CZ  
4553  O OH  . TYR C  104 ? 0.5919 0.6932 0.5128 0.0211  -0.0175 -0.0053 104 TYR C OH  
4554  N N   . GLU C  105 ? 0.4118 0.4819 0.3474 0.0109  -0.0074 -0.0137 105 GLU C N   
4555  C CA  . GLU C  105 ? 0.4781 0.5480 0.4143 0.0096  -0.0099 -0.0147 105 GLU C CA  
4556  C C   . GLU C  105 ? 0.5174 0.5810 0.4610 0.0110  -0.0113 -0.0128 105 GLU C C   
4557  O O   . GLU C  105 ? 0.4790 0.5429 0.4236 0.0115  -0.0145 -0.0122 105 GLU C O   
4558  C CB  . GLU C  105 ? 0.4517 0.5214 0.3853 0.0056  -0.0077 -0.0181 105 GLU C CB  
4559  C CG  . GLU C  105 ? 0.4394 0.5156 0.3656 0.0035  -0.0063 -0.0203 105 GLU C CG  
4560  C CD  . GLU C  105 ? 0.7389 0.8147 0.6638 0.0037  -0.0028 -0.0202 105 GLU C CD  
4561  O OE1 . GLU C  105 ? 0.8108 0.8801 0.7403 0.0038  -0.0002 -0.0198 105 GLU C OE1 
4562  O OE2 . GLU C  105 ? 0.5624 0.6444 0.4815 0.0035  -0.0028 -0.0203 105 GLU C OE2 
4563  N N   . GLU C  106 ? 0.5058 0.5639 0.4544 0.0116  -0.0088 -0.0119 106 GLU C N   
4564  C CA  . GLU C  106 ? 0.4419 0.4944 0.3979 0.0131  -0.0102 -0.0098 106 GLU C CA  
4565  C C   . GLU C  106 ? 0.4615 0.5152 0.4189 0.0162  -0.0133 -0.0072 106 GLU C C   
4566  O O   . GLU C  106 ? 0.4838 0.5361 0.4440 0.0167  -0.0163 -0.0061 106 GLU C O   
4567  C CB  . GLU C  106 ? 0.4177 0.4644 0.3791 0.0132  -0.0066 -0.0092 106 GLU C CB  
4568  C CG  . GLU C  106 ? 0.7634 0.8063 0.7270 0.0103  -0.0041 -0.0111 106 GLU C CG  
4569  C CD  . GLU C  106 ? 0.6860 0.7260 0.6543 0.0099  -0.0068 -0.0101 106 GLU C CD  
4570  O OE1 . GLU C  106 ? 0.6686 0.7068 0.6416 0.0120  -0.0095 -0.0075 106 GLU C OE1 
4571  O OE2 . GLU C  106 ? 0.5356 0.5752 0.5029 0.0073  -0.0063 -0.0120 106 GLU C OE2 
4572  N N   . LEU C  107 ? 0.5942 0.6505 0.5493 0.0182  -0.0124 -0.0061 107 LEU C N   
4573  C CA  . LEU C  107 ? 0.5810 0.6385 0.5373 0.0213  -0.0148 -0.0037 107 LEU C CA  
4574  C C   . LEU C  107 ? 0.4985 0.5600 0.4518 0.0212  -0.0183 -0.0040 107 LEU C C   
4575  O O   . LEU C  107 ? 0.5292 0.5892 0.4854 0.0225  -0.0209 -0.0025 107 LEU C O   
4576  C CB  . LEU C  107 ? 0.4790 0.5396 0.4325 0.0232  -0.0130 -0.0026 107 LEU C CB  
4577  C CG  . LEU C  107 ? 0.5078 0.5692 0.4630 0.0266  -0.0147 0.0000  107 LEU C CG  
4578  C CD1 . LEU C  107 ? 0.4861 0.5412 0.4487 0.0279  -0.0151 0.0017  107 LEU C CD1 
4579  C CD2 . LEU C  107 ? 0.5547 0.6195 0.5069 0.0284  -0.0126 0.0012  107 LEU C CD2 
4580  N N   . ARG C  108 ? 0.3868 0.4534 0.3342 0.0195  -0.0183 -0.0060 108 ARG C N   
4581  C CA  . ARG C  108 ? 0.5202 0.5909 0.4643 0.0192  -0.0213 -0.0065 108 ARG C CA  
4582  C C   . ARG C  108 ? 0.4762 0.5431 0.4235 0.0179  -0.0235 -0.0068 108 ARG C C   
4583  O O   . ARG C  108 ? 0.4748 0.5423 0.4225 0.0189  -0.0262 -0.0060 108 ARG C O   
4584  C CB  . ARG C  108 ? 0.4462 0.5229 0.3840 0.0170  -0.0206 -0.0088 108 ARG C CB  
4585  C CG  . ARG C  108 ? 0.4964 0.5779 0.4302 0.0179  -0.0188 -0.0083 108 ARG C CG  
4586  C CD  . ARG C  108 ? 0.5802 0.6670 0.5080 0.0150  -0.0178 -0.0109 108 ARG C CD  
4587  N NE  . ARG C  108 ? 0.6452 0.7363 0.5702 0.0140  -0.0205 -0.0119 108 ARG C NE  
4588  C CZ  . ARG C  108 ? 0.5754 0.6734 0.4969 0.0152  -0.0220 -0.0111 108 ARG C CZ  
4589  N NH1 . ARG C  108 ? 0.5295 0.6309 0.4498 0.0174  -0.0213 -0.0091 108 ARG C NH1 
4590  N NH2 . ARG C  108 ? 0.4814 0.5829 0.4009 0.0141  -0.0242 -0.0121 108 ARG C NH2 
4591  N N   . GLU C  109 ? 0.5515 0.6146 0.5011 0.0157  -0.0220 -0.0080 109 GLU C N   
4592  C CA  . GLU C  109 ? 0.5286 0.5880 0.4813 0.0144  -0.0239 -0.0081 109 GLU C CA  
4593  C C   . GLU C  109 ? 0.4933 0.5488 0.4515 0.0163  -0.0259 -0.0056 109 GLU C C   
4594  O O   . GLU C  109 ? 0.4171 0.4719 0.3761 0.0160  -0.0288 -0.0051 109 GLU C O   
4595  C CB  . GLU C  109 ? 0.4637 0.5193 0.4187 0.0119  -0.0214 -0.0095 109 GLU C CB  
4596  C CG  . GLU C  109 ? 0.6860 0.7380 0.6446 0.0105  -0.0232 -0.0093 109 GLU C CG  
4597  C CD  . GLU C  109 ? 0.8824 0.9379 0.8363 0.0087  -0.0252 -0.0110 109 GLU C CD  
4598  O OE1 . GLU C  109 ? 1.0254 1.0862 0.9737 0.0088  -0.0256 -0.0121 109 GLU C OE1 
4599  O OE2 . GLU C  109 ? 0.8407 0.8935 0.7966 0.0071  -0.0262 -0.0111 109 GLU C OE2 
4600  N N   . GLN C  110 ? 0.4453 0.4983 0.4072 0.0182  -0.0243 -0.0039 110 GLN C N   
4601  C CA  . GLN C  110 ? 0.5317 0.5810 0.4991 0.0199  -0.0259 -0.0016 110 GLN C CA  
4602  C C   . GLN C  110 ? 0.6543 0.7064 0.6197 0.0219  -0.0282 -0.0006 110 GLN C C   
4603  O O   . GLN C  110 ? 0.7350 0.7850 0.7033 0.0224  -0.0306 0.0006  110 GLN C O   
4604  C CB  . GLN C  110 ? 0.5201 0.5661 0.4920 0.0214  -0.0231 -0.0002 110 GLN C CB  
4605  C CG  . GLN C  110 ? 0.5821 0.6259 0.5551 0.0196  -0.0198 -0.0015 110 GLN C CG  
4606  C CD  . GLN C  110 ? 0.7078 0.7457 0.6886 0.0195  -0.0191 0.0000  110 GLN C CD  
4607  O OE1 . GLN C  110 ? 0.8599 0.8957 0.8452 0.0205  -0.0215 0.0020  110 GLN C OE1 
4608  N NE2 . GLN C  110 ? 0.6362 0.6716 0.6188 0.0182  -0.0157 -0.0008 110 GLN C NE2 
4609  N N   . LEU C  111 ? 0.6372 0.6942 0.5977 0.0229  -0.0274 -0.0011 111 LEU C N   
4610  C CA  . LEU C  111 ? 0.4295 0.4894 0.3880 0.0250  -0.0290 -0.0001 111 LEU C CA  
4611  C C   . LEU C  111 ? 0.4506 0.5135 0.4055 0.0237  -0.0315 -0.0013 111 LEU C C   
4612  O O   . LEU C  111 ? 0.5483 0.6129 0.5022 0.0251  -0.0330 -0.0006 111 LEU C O   
4613  C CB  . LEU C  111 ? 0.5079 0.5722 0.4632 0.0268  -0.0270 0.0004  111 LEU C CB  
4614  C CG  . LEU C  111 ? 0.4891 0.5517 0.4475 0.0298  -0.0257 0.0027  111 LEU C CG  
4615  C CD1 . LEU C  111 ? 0.7029 0.7598 0.6672 0.0303  -0.0269 0.0040  111 LEU C CD1 
4616  C CD2 . LEU C  111 ? 0.4495 0.5119 0.4077 0.0300  -0.0224 0.0028  111 LEU C CD2 
4617  N N   . SER C  112 ? 0.5177 0.5810 0.4708 0.0210  -0.0317 -0.0032 112 SER C N   
4618  C CA  . SER C  112 ? 0.5084 0.5748 0.4575 0.0195  -0.0337 -0.0047 112 SER C CA  
4619  C C   . SER C  112 ? 0.4503 0.5150 0.4008 0.0200  -0.0365 -0.0038 112 SER C C   
4620  O O   . SER C  112 ? 0.5570 0.6251 0.5043 0.0202  -0.0379 -0.0043 112 SER C O   
4621  C CB  . SER C  112 ? 0.5780 0.6435 0.5262 0.0164  -0.0334 -0.0066 112 SER C CB  
4622  O OG  . SER C  112 ? 0.5178 0.5778 0.4708 0.0155  -0.0343 -0.0059 112 SER C OG  
4623  N N   . SER C  113 ? 0.5160 0.5755 0.4715 0.0201  -0.0374 -0.0025 113 SER C N   
4624  C CA  . SER C  113 ? 0.5853 0.6429 0.5422 0.0203  -0.0399 -0.0016 113 SER C CA  
4625  C C   . SER C  113 ? 0.7057 0.7593 0.6680 0.0219  -0.0398 0.0004  113 SER C C   
4626  O O   . SER C  113 ? 0.6601 0.7102 0.6267 0.0215  -0.0391 0.0012  113 SER C O   
4627  C CB  . SER C  113 ? 0.6908 0.7465 0.6477 0.0176  -0.0421 -0.0024 113 SER C CB  
4628  O OG  . SER C  113 ? 0.5887 0.6432 0.5456 0.0174  -0.0446 -0.0019 113 SER C OG  
4629  N N   . VAL C  114 ? 0.6493 0.7032 0.6114 0.0237  -0.0404 0.0013  114 VAL C N   
4630  C CA  . VAL C  114 ? 0.7054 0.7560 0.6723 0.0253  -0.0400 0.0031  114 VAL C CA  
4631  C C   . VAL C  114 ? 0.7007 0.7493 0.6685 0.0249  -0.0424 0.0034  114 VAL C C   
4632  O O   . VAL C  114 ? 0.6827 0.7336 0.6468 0.0250  -0.0431 0.0027  114 VAL C O   
4633  C CB  . VAL C  114 ? 0.7270 0.7797 0.6934 0.0282  -0.0374 0.0040  114 VAL C CB  
4634  C CG1 . VAL C  114 ? 0.7366 0.7883 0.7042 0.0301  -0.0378 0.0051  114 VAL C CG1 
4635  C CG2 . VAL C  114 ? 0.6332 0.6838 0.6032 0.0289  -0.0351 0.0048  114 VAL C CG2 
4636  N N   . SER C  115 ? 0.7801 0.8245 0.7527 0.0243  -0.0434 0.0046  115 SER C N   
4637  C CA  . SER C  115 ? 0.9119 0.9542 0.8854 0.0235  -0.0457 0.0048  115 SER C CA  
4638  C C   . SER C  115 ? 0.8725 0.9144 0.8469 0.0258  -0.0444 0.0056  115 SER C C   
4639  O O   . SER C  115 ? 0.9753 1.0179 0.9472 0.0259  -0.0450 0.0050  115 SER C O   
4640  C CB  . SER C  115 ? 0.9569 0.9953 0.9354 0.0216  -0.0476 0.0060  115 SER C CB  
4641  O OG  . SER C  115 ? 1.0450 1.0821 1.0231 0.0199  -0.0503 0.0058  115 SER C OG  
4642  N N   . SER C  116 ? 0.8389 0.8795 0.8172 0.0278  -0.0423 0.0069  116 SER C N   
4643  C CA  . SER C  116 ? 0.9388 0.9792 0.9181 0.0303  -0.0405 0.0078  116 SER C CA  
4644  C C   . SER C  116 ? 1.0072 1.0491 0.9869 0.0328  -0.0374 0.0086  116 SER C C   
4645  O O   . SER C  116 ? 1.0245 1.0655 1.0065 0.0324  -0.0366 0.0089  116 SER C O   
4646  C CB  . SER C  116 ? 0.9515 0.9876 0.9358 0.0300  -0.0413 0.0087  116 SER C CB  
4647  O OG  . SER C  116 ? 1.2364 1.2701 1.2258 0.0297  -0.0411 0.0099  116 SER C OG  
4648  N N   . PHE C  117 ? 0.8868 0.9311 0.8645 0.0353  -0.0355 0.0091  117 PHE C N   
4649  C CA  . PHE C  117 ? 0.7342 0.7810 0.7110 0.0375  -0.0327 0.0099  117 PHE C CA  
4650  C C   . PHE C  117 ? 0.6911 0.7383 0.6688 0.0406  -0.0306 0.0114  117 PHE C C   
4651  O O   . PHE C  117 ? 0.7905 0.8405 0.7652 0.0417  -0.0304 0.0113  117 PHE C O   
4652  C CB  . PHE C  117 ? 0.6894 0.7413 0.6607 0.0369  -0.0328 0.0087  117 PHE C CB  
4653  C CG  . PHE C  117 ? 0.6434 0.6981 0.6133 0.0382  -0.0303 0.0093  117 PHE C CG  
4654  C CD1 . PHE C  117 ? 0.5213 0.5794 0.4894 0.0409  -0.0284 0.0105  117 PHE C CD1 
4655  C CD2 . PHE C  117 ? 0.6092 0.6631 0.5795 0.0366  -0.0299 0.0085  117 PHE C CD2 
4656  C CE1 . PHE C  117 ? 0.5098 0.5707 0.4761 0.0418  -0.0263 0.0111  117 PHE C CE1 
4657  C CE2 . PHE C  117 ? 0.6482 0.7045 0.6167 0.0374  -0.0274 0.0088  117 PHE C CE2 
4658  C CZ  . PHE C  117 ? 0.6640 0.7240 0.6303 0.0400  -0.0258 0.0100  117 PHE C CZ  
4659  N N   . GLU C  118 ? 0.7691 0.8133 0.7510 0.0420  -0.0289 0.0128  118 GLU C N   
4660  C CA  . GLU C  118 ? 0.8578 0.9021 0.8409 0.0450  -0.0265 0.0144  118 GLU C CA  
4661  C C   . GLU C  118 ? 0.6972 0.7425 0.6809 0.0471  -0.0236 0.0159  118 GLU C C   
4662  O O   . GLU C  118 ? 0.7033 0.7465 0.6892 0.0462  -0.0232 0.0158  118 GLU C O   
4663  C CB  . GLU C  118 ? 1.0253 1.0649 1.0131 0.0451  -0.0267 0.0149  118 GLU C CB  
4664  C CG  . GLU C  118 ? 1.1324 1.1679 1.1256 0.0451  -0.0258 0.0158  118 GLU C CG  
4665  C CD  . GLU C  118 ? 1.3835 1.4155 1.3810 0.0464  -0.0246 0.0168  118 GLU C CD  
4666  O OE1 . GLU C  118 ? 1.5913 1.6235 1.5874 0.0471  -0.0244 0.0166  118 GLU C OE1 
4667  O OE2 . GLU C  118 ? 1.2781 1.3067 1.2803 0.0466  -0.0237 0.0177  118 GLU C OE2 
4668  N N   . ARG C  119 ? 0.7422 0.7907 0.7239 0.0498  -0.0216 0.0173  119 ARG C N   
4669  C CA  . ARG C  119 ? 0.6975 0.7477 0.6788 0.0518  -0.0189 0.0188  119 ARG C CA  
4670  C C   . ARG C  119 ? 0.6516 0.6987 0.6371 0.0544  -0.0165 0.0209  119 ARG C C   
4671  O O   . ARG C  119 ? 0.8100 0.8578 0.7956 0.0565  -0.0156 0.0220  119 ARG C O   
4672  C CB  . ARG C  119 ? 0.7200 0.7767 0.6959 0.0529  -0.0184 0.0193  119 ARG C CB  
4673  C CG  . ARG C  119 ? 0.7403 0.7995 0.7153 0.0555  -0.0155 0.0215  119 ARG C CG  
4674  C CD  . ARG C  119 ? 0.8770 0.9433 0.8470 0.0566  -0.0154 0.0223  119 ARG C CD  
4675  N NE  . ARG C  119 ? 0.9633 1.0323 0.9328 0.0596  -0.0128 0.0250  119 ARG C NE  
4676  C CZ  . ARG C  119 ? 1.0797 1.1489 1.0511 0.0627  -0.0112 0.0275  119 ARG C CZ  
4677  N NH1 . ARG C  119 ? 1.1711 1.2378 1.1450 0.0632  -0.0118 0.0273  119 ARG C NH1 
4678  N NH2 . ARG C  119 ? 1.0548 1.1266 1.0255 0.0653  -0.0088 0.0302  119 ARG C NH2 
4679  N N   . PHE C  120 ? 0.6752 0.7186 0.6643 0.0544  -0.0152 0.0214  120 PHE C N   
4680  C CA  . PHE C  120 ? 0.6863 0.7263 0.6798 0.0567  -0.0128 0.0232  120 PHE C CA  
4681  C C   . PHE C  120 ? 0.6574 0.6982 0.6508 0.0584  -0.0098 0.0247  120 PHE C C   
4682  O O   . PHE C  120 ? 0.6473 0.6894 0.6386 0.0570  -0.0097 0.0240  120 PHE C O   
4683  C CB  . PHE C  120 ? 0.6988 0.7331 0.6981 0.0550  -0.0139 0.0225  120 PHE C CB  
4684  C CG  . PHE C  120 ? 0.7244 0.7566 0.7259 0.0532  -0.0141 0.0219  120 PHE C CG  
4685  C CD1 . PHE C  120 ? 0.7632 0.7925 0.7687 0.0543  -0.0116 0.0231  120 PHE C CD1 
4686  C CD2 . PHE C  120 ? 0.8550 0.8880 0.8548 0.0503  -0.0167 0.0201  120 PHE C CD2 
4687  C CE1 . PHE C  120 ? 0.6703 0.6975 0.6783 0.0526  -0.0115 0.0226  120 PHE C CE1 
4688  C CE2 . PHE C  120 ? 0.7714 0.8023 0.7738 0.0487  -0.0166 0.0196  120 PHE C CE2 
4689  C CZ  . PHE C  120 ? 0.6860 0.7139 0.6925 0.0499  -0.0139 0.0209  120 PHE C CZ  
4690  N N   . GLU C  121 ? 0.7590 0.7986 0.7545 0.0612  -0.0071 0.0269  121 GLU C N   
4691  C CA  . GLU C  121 ? 0.7117 0.7517 0.7072 0.0630  -0.0041 0.0286  121 GLU C CA  
4692  C C   . GLU C  121 ? 0.7564 0.7910 0.7568 0.0619  -0.0032 0.0282  121 GLU C C   
4693  O O   . GLU C  121 ? 0.8981 0.9283 0.9038 0.0625  -0.0026 0.0288  121 GLU C O   
4694  C CB  . GLU C  121 ? 0.8470 0.8876 0.8432 0.0666  -0.0014 0.0313  121 GLU C CB  
4695  C CG  . GLU C  121 ? 1.0288 1.0714 1.0230 0.0685  0.0016  0.0334  121 GLU C CG  
4696  C CD  . GLU C  121 ? 1.1477 1.1914 1.1426 0.0722  0.0041  0.0364  121 GLU C CD  
4697  O OE1 . GLU C  121 ? 1.1917 1.2330 1.1899 0.0732  0.0041  0.0368  121 GLU C OE1 
4698  O OE2 . GLU C  121 ? 1.1088 1.1558 1.1008 0.0740  0.0062  0.0385  121 GLU C OE2 
4699  N N   . ILE C  122 ? 0.7859 0.8210 0.7848 0.0601  -0.0032 0.0271  122 ILE C N   
4700  C CA  . ILE C  122 ? 0.7758 0.8061 0.7797 0.0589  -0.0022 0.0267  122 ILE C CA  
4701  C C   . ILE C  122 ? 0.9118 0.9403 0.9177 0.0612  0.0016  0.0287  122 ILE C C   
4702  O O   . ILE C  122 ? 0.8341 0.8577 0.8459 0.0615  0.0028  0.0293  122 ILE C O   
4703  C CB  . ILE C  122 ? 0.7271 0.7582 0.7289 0.0562  -0.0029 0.0248  122 ILE C CB  
4704  C CG1 . ILE C  122 ? 0.7231 0.7492 0.7305 0.0553  -0.0013 0.0248  122 ILE C CG1 
4705  C CG2 . ILE C  122 ? 0.7207 0.7568 0.7157 0.0565  -0.0015 0.0248  122 ILE C CG2 
4706  C CD1 . ILE C  122 ? 0.6537 0.6799 0.6599 0.0526  -0.0015 0.0230  122 ILE C CD1 
4707  N N   . PHE C  123 ? 0.9531 0.9855 0.9539 0.0629  0.0036  0.0299  123 PHE C N   
4708  C CA  . PHE C  123 ? 0.7474 0.7787 0.7493 0.0653  0.0073  0.0321  123 PHE C CA  
4709  C C   . PHE C  123 ? 0.9354 0.9705 0.9342 0.0683  0.0082  0.0345  123 PHE C C   
4710  O O   . PHE C  123 ? 0.8643 0.9049 0.8572 0.0687  0.0084  0.0351  123 PHE C O   
4711  C CB  . PHE C  123 ? 0.7663 0.7984 0.7652 0.0642  0.0094  0.0317  123 PHE C CB  
4712  C CG  . PHE C  123 ? 0.7905 0.8184 0.7932 0.0616  0.0093  0.0298  123 PHE C CG  
4713  C CD1 . PHE C  123 ? 0.8148 0.8444 0.8140 0.0589  0.0084  0.0276  123 PHE C CD1 
4714  C CD2 . PHE C  123 ? 0.8555 0.8776 0.8656 0.0619  0.0102  0.0302  123 PHE C CD2 
4715  C CE1 . PHE C  123 ? 0.7791 0.8047 0.7824 0.0567  0.0086  0.0261  123 PHE C CE1 
4716  C CE2 . PHE C  123 ? 0.8976 0.9160 0.9119 0.0596  0.0101  0.0288  123 PHE C CE2 
4717  C CZ  . PHE C  123 ? 0.7858 0.8060 0.7968 0.0571  0.0094  0.0268  123 PHE C CZ  
4718  N N   . PRO C  124 ? 1.0869 1.1194 1.0898 0.0703  0.0088  0.0359  124 PRO C N   
4719  C CA  . PRO C  124 ? 1.0625 1.0981 1.0637 0.0735  0.0103  0.0385  124 PRO C CA  
4720  C C   . PRO C  124 ? 1.1031 1.1413 1.1011 0.0754  0.0133  0.0408  124 PRO C C   
4721  O O   . PRO C  124 ? 1.0307 1.0654 1.0310 0.0755  0.0157  0.0412  124 PRO C O   
4722  C CB  . PRO C  124 ? 1.2063 1.2366 1.2138 0.0750  0.0114  0.0393  124 PRO C CB  
4723  C CG  . PRO C  124 ? 1.1936 1.2199 1.2051 0.0720  0.0090  0.0366  124 PRO C CG  
4724  C CD  . PRO C  124 ? 1.0729 1.0995 1.0827 0.0696  0.0084  0.0351  124 PRO C CD  
4725  N N   . LYS C  125 ? 1.0607 1.1051 1.0536 0.0770  0.0133  0.0426  125 LYS C N   
4726  C CA  . LYS C  125 ? 1.1863 1.2343 1.1751 0.0784  0.0158  0.0448  125 LYS C CA  
4727  C C   . LYS C  125 ? 1.3452 1.3895 1.3375 0.0812  0.0196  0.0476  125 LYS C C   
4728  O O   . LYS C  125 ? 1.1802 1.2251 1.1703 0.0816  0.0220  0.0488  125 LYS C O   
4729  C CB  . LYS C  125 ? 1.0675 1.1232 1.0509 0.0797  0.0148  0.0466  125 LYS C CB  
4730  C CG  . LYS C  125 ? 1.1599 1.2205 1.1381 0.0806  0.0167  0.0490  125 LYS C CG  
4731  C CD  . LYS C  125 ? 1.1038 1.1729 1.0761 0.0807  0.0148  0.0500  125 LYS C CD  
4732  C CE  . LYS C  125 ? 1.1676 1.2392 1.1418 0.0840  0.0148  0.0529  125 LYS C CE  
4733  N NZ  . LYS C  125 ? 1.1373 1.2178 1.1063 0.0844  0.0131  0.0544  125 LYS C NZ  
4734  N N   . THR C  126 ? 2.0803 2.1207 2.0781 0.0831  0.0203  0.0485  126 THR C N   
4735  C CA  . THR C  126 ? 2.0803 2.1181 2.0813 0.0863  0.0240  0.0516  126 THR C CA  
4736  C C   . THR C  126 ? 2.1176 2.1479 2.1251 0.0860  0.0260  0.0509  126 THR C C   
4737  O O   . THR C  126 ? 2.2717 2.2992 2.2827 0.0886  0.0290  0.0533  126 THR C O   
4738  C CB  . THR C  126 ? 1.6455 1.6838 1.6489 0.0889  0.0243  0.0535  126 THR C CB  
4739  O OG1 . THR C  126 ? 1.5081 1.5456 1.5128 0.0869  0.0211  0.0507  126 THR C OG1 
4740  N N   . SER C  127 ? 1.3751 1.4021 1.3845 0.0830  0.0244  0.0479  127 SER C N   
4741  C CA  . SER C  127 ? 1.2607 1.2810 1.2769 0.0826  0.0260  0.0473  127 SER C CA  
4742  C C   . SER C  127 ? 1.1981 1.2170 1.2139 0.0798  0.0257  0.0452  127 SER C C   
4743  O O   . SER C  127 ? 1.3149 1.3294 1.3346 0.0797  0.0281  0.0454  127 SER C O   
4744  C CB  . SER C  127 ? 1.3275 1.3446 1.3488 0.0818  0.0239  0.0458  127 SER C CB  
4745  O OG  . SER C  127 ? 1.1644 1.1836 1.1834 0.0790  0.0199  0.0432  127 SER C OG  
4746  N N   . SER C  128 ? 1.1925 1.2153 1.2034 0.0776  0.0231  0.0434  128 SER C N   
4747  C CA  . SER C  128 ? 1.0557 1.0788 1.0641 0.0752  0.0235  0.0418  128 SER C CA  
4748  C C   . SER C  128 ? 1.0821 1.1092 1.0846 0.0769  0.0261  0.0440  128 SER C C   
4749  O O   . SER C  128 ? 1.1072 1.1381 1.1070 0.0793  0.0263  0.0464  128 SER C O   
4750  C CB  . SER C  128 ? 1.0024 1.0281 1.0081 0.0722  0.0198  0.0390  128 SER C CB  
4751  O OG  . SER C  128 ? 0.9931 1.0171 1.0024 0.0718  0.0169  0.0381  128 SER C OG  
4752  N N   . TRP C  129 ? 1.1530 1.1791 1.1537 0.0755  0.0282  0.0433  129 TRP C N   
4753  C CA  . TRP C  129 ? 1.1472 1.1773 1.1415 0.0763  0.0306  0.0451  129 TRP C CA  
4754  C C   . TRP C  129 ? 1.1150 1.1451 1.1099 0.0800  0.0336  0.0489  129 TRP C C   
4755  O O   . TRP C  129 ? 1.1367 1.1724 1.1269 0.0818  0.0334  0.0512  129 TRP C O   
4756  C CB  . TRP C  129 ? 1.2154 1.2529 1.2024 0.0753  0.0279  0.0446  129 TRP C CB  
4757  C CG  . TRP C  129 ? 1.0287 1.0665 1.0161 0.0725  0.0242  0.0414  129 TRP C CG  
4758  C CD1 . TRP C  129 ? 0.9001 0.9420 0.8857 0.0725  0.0208  0.0410  129 TRP C CD1 
4759  C CD2 . TRP C  129 ? 0.9714 1.0052 0.9615 0.0695  0.0237  0.0383  129 TRP C CD2 
4760  N NE1 . TRP C  129 ? 0.9508 0.9914 0.9374 0.0695  0.0182  0.0378  129 TRP C NE1 
4761  C CE2 . TRP C  129 ? 0.9117 0.9474 0.9011 0.0677  0.0199  0.0363  129 TRP C CE2 
4762  C CE3 . TRP C  129 ? 0.9284 0.9571 0.9215 0.0682  0.0263  0.0373  129 TRP C CE3 
4763  C CZ2 . TRP C  129 ? 0.9862 1.0191 0.9780 0.0647  0.0185  0.0334  129 TRP C CZ2 
4764  C CZ3 . TRP C  129 ? 0.8057 0.8316 0.8015 0.0653  0.0251  0.0344  129 TRP C CZ3 
4765  C CH2 . TRP C  129 ? 0.9290 0.9570 0.9241 0.0636  0.0211  0.0326  129 TRP C CH2 
4766  N N   . PRO C  130 ? 1.2456 1.2696 1.2465 0.0812  0.0365  0.0497  130 PRO C N   
4767  C CA  . PRO C  130 ? 1.2348 1.2581 1.2365 0.0846  0.0398  0.0533  130 PRO C CA  
4768  C C   . PRO C  130 ? 1.2584 1.2827 1.2555 0.0846  0.0432  0.0545  130 PRO C C   
4769  O O   . PRO C  130 ? 1.3102 1.3349 1.3065 0.0873  0.0461  0.0578  130 PRO C O   
4770  C CB  . PRO C  130 ? 1.2403 1.2563 1.2510 0.0853  0.0413  0.0530  130 PRO C CB  
4771  C CG  . PRO C  130 ? 1.2174 1.2309 1.2316 0.0823  0.0381  0.0495  130 PRO C CG  
4772  C CD  . PRO C  130 ? 1.3411 1.3585 1.3491 0.0796  0.0365  0.0475  130 PRO C CD  
4773  N N   . ASN C  131 ? 1.3224 1.3467 1.3165 0.0814  0.0431  0.0518  131 ASN C N   
4774  C CA  . ASN C  131 ? 1.3606 1.3854 1.3499 0.0806  0.0465  0.0523  131 ASN C CA  
4775  C C   . ASN C  131 ? 1.2403 1.2723 1.2203 0.0786  0.0450  0.0516  131 ASN C C   
4776  O O   . ASN C  131 ? 1.1535 1.1864 1.1283 0.0771  0.0474  0.0513  131 ASN C O   
4777  C CB  . ASN C  131 ? 1.4743 1.4926 1.4679 0.0783  0.0486  0.0496  131 ASN C CB  
4778  C CG  . ASN C  131 ? 1.5856 1.5970 1.5883 0.0801  0.0505  0.0505  131 ASN C CG  
4779  O OD1 . ASN C  131 ? 1.6362 1.6473 1.6411 0.0832  0.0515  0.0533  131 ASN C OD1 
4780  N ND2 . ASN C  131 ? 1.5345 1.5405 1.5429 0.0781  0.0511  0.0481  131 ASN C ND2 
4781  N N   . HIS C  132 ? 1.1137 1.1507 1.0916 0.0785  0.0411  0.0513  132 HIS C N   
4782  C CA  . HIS C  132 ? 0.9911 1.0354 0.9606 0.0765  0.0392  0.0505  132 HIS C CA  
4783  C C   . HIS C  132 ? 1.0334 1.0843 1.0007 0.0787  0.0365  0.0530  132 HIS C C   
4784  O O   . HIS C  132 ? 1.0446 1.0937 1.0172 0.0810  0.0353  0.0540  132 HIS C O   
4785  C CB  . HIS C  132 ? 0.9459 0.9893 0.9151 0.0726  0.0370  0.0461  132 HIS C CB  
4786  C CG  . HIS C  132 ? 0.9230 0.9593 0.8963 0.0706  0.0395  0.0436  132 HIS C CG  
4787  N ND1 . HIS C  132 ? 0.8944 0.9306 0.8631 0.0677  0.0418  0.0417  132 HIS C ND1 
4788  C CD2 . HIS C  132 ? 0.8369 0.8662 0.8186 0.0710  0.0402  0.0429  132 HIS C CD2 
4789  C CE1 . HIS C  132 ? 0.9196 0.9488 0.8941 0.0666  0.0439  0.0399  132 HIS C CE1 
4790  N NE2 . HIS C  132 ? 0.8717 0.8967 0.8542 0.0686  0.0429  0.0407  132 HIS C NE2 
4791  N N   . ASP C  133 ? 0.9079 0.9663 0.8674 0.0780  0.0356  0.0540  133 ASP C N   
4792  C CA  . ASP C  133 ? 1.0012 1.0666 0.9584 0.0800  0.0331  0.0565  133 ASP C CA  
4793  C C   . ASP C  133 ? 1.0020 1.0700 0.9588 0.0779  0.0290  0.0536  133 ASP C C   
4794  O O   . ASP C  133 ? 0.9928 1.0632 0.9450 0.0744  0.0278  0.0506  133 ASP C O   
4795  C CB  . ASP C  133 ? 1.0417 1.1149 0.9910 0.0803  0.0338  0.0593  133 ASP C CB  
4796  C CG  . ASP C  133 ? 1.2304 1.3106 1.1787 0.0833  0.0320  0.0633  133 ASP C CG  
4797  O OD1 . ASP C  133 ? 1.1589 1.2411 1.1089 0.0833  0.0289  0.0622  133 ASP C OD1 
4798  O OD2 . ASP C  133 ? 1.3989 1.4826 1.3449 0.0858  0.0339  0.0675  133 ASP C OD2 
4799  N N   . SER C  134 ? 0.9757 1.0429 0.9373 0.0799  0.0272  0.0542  134 SER C N   
4800  C CA  . SER C  134 ? 0.9049 0.9738 0.8664 0.0781  0.0234  0.0516  134 SER C CA  
4801  C C   . SER C  134 ? 0.9299 1.0068 0.8885 0.0799  0.0213  0.0540  134 SER C C   
4802  O O   . SER C  134 ? 0.9268 1.0044 0.8874 0.0799  0.0187  0.0531  134 SER C O   
4803  C CB  . SER C  134 ? 1.0166 1.0785 0.9858 0.0785  0.0226  0.0499  134 SER C CB  
4804  O OG  . SER C  134 ? 1.0958 1.1555 1.0698 0.0822  0.0242  0.0531  134 SER C OG  
4805  N N   . ASN C  135 ? 1.0894 1.1722 1.0431 0.0812  0.0225  0.0573  135 ASN C N   
4806  C CA  . ASN C  135 ? 1.1339 1.2248 1.0853 0.0833  0.0208  0.0605  135 ASN C CA  
4807  C C   . ASN C  135 ? 1.1183 1.2179 1.0614 0.0814  0.0198  0.0611  135 ASN C C   
4808  O O   . ASN C  135 ? 1.2648 1.3717 1.2054 0.0816  0.0173  0.0622  135 ASN C O   
4809  C CB  . ASN C  135 ? 1.2651 1.3554 1.2201 0.0880  0.0233  0.0654  135 ASN C CB  
4810  C CG  . ASN C  135 ? 1.1967 1.2794 1.1598 0.0899  0.0240  0.0650  135 ASN C CG  
4811  O OD1 . ASN C  135 ? 0.9691 1.0507 0.9346 0.0890  0.0216  0.0626  135 ASN C OD1 
4812  N ND2 . ASN C  135 ? 1.0496 1.1272 1.0167 0.0924  0.0273  0.0672  135 ASN C ND2 
4813  N N   . LYS C  136 ? 1.0550 1.1538 0.9941 0.0793  0.0218  0.0602  136 LYS C N   
4814  C CA  . LYS C  136 ? 1.1698 1.2768 1.1006 0.0771  0.0212  0.0607  136 LYS C CA  
4815  C C   . LYS C  136 ? 1.2328 1.3419 1.1595 0.0724  0.0188  0.0559  136 LYS C C   
4816  O O   . LYS C  136 ? 1.1344 1.2500 1.0540 0.0698  0.0182  0.0555  136 LYS C O   
4817  C CB  . LYS C  136 ? 1.3409 1.4464 1.2686 0.0768  0.0247  0.0620  136 LYS C CB  
4818  C CG  . LYS C  136 ? 1.4091 1.5130 1.3402 0.0814  0.0273  0.0670  136 LYS C CG  
4819  C CD  . LYS C  136 ? 1.5173 1.6283 1.4419 0.0820  0.0286  0.0710  136 LYS C CD  
4820  C CE  . LYS C  136 ? 1.7694 1.8814 1.6978 0.0871  0.0301  0.0769  136 LYS C CE  
4821  N NZ  . LYS C  136 ? 1.7548 1.8700 1.6873 0.0897  0.0275  0.0785  136 LYS C NZ  
4822  N N   . GLY C  137 ? 1.1268 1.2304 1.0579 0.0713  0.0174  0.0524  137 GLY C N   
4823  C CA  . GLY C  137 ? 0.9603 1.0645 0.8884 0.0669  0.0155  0.0477  137 GLY C CA  
4824  C C   . GLY C  137 ? 0.8888 1.0006 0.8144 0.0662  0.0118  0.0475  137 GLY C C   
4825  O O   . GLY C  137 ? 0.9272 1.0368 0.8560 0.0656  0.0096  0.0451  137 GLY C O   
4826  N N   . VAL C  138 ? 0.9052 1.0262 0.8250 0.0663  0.0111  0.0500  138 VAL C N   
4827  C CA  . VAL C  138 ? 0.8750 1.0041 0.7920 0.0654  0.0077  0.0498  138 VAL C CA  
4828  C C   . VAL C  138 ? 0.8683 1.0047 0.7769 0.0615  0.0071  0.0484  138 VAL C C   
4829  O O   . VAL C  138 ? 0.9247 1.0603 0.8294 0.0598  0.0094  0.0481  138 VAL C O   
4830  C CB  . VAL C  138 ? 1.0000 1.1346 0.9191 0.0698  0.0067  0.0550  138 VAL C CB  
4831  C CG1 . VAL C  138 ? 1.0624 1.1897 0.9897 0.0734  0.0076  0.0561  138 VAL C CG1 
4832  C CG2 . VAL C  138 ? 0.9792 1.1196 0.8946 0.0714  0.0084  0.0595  138 VAL C CG2 
4833  N N   . THR C  139 ? 0.7331 0.8767 0.6389 0.0599  0.0040  0.0476  139 THR C N   
4834  C CA  . THR C  139 ? 0.9812 1.1320 0.8790 0.0557  0.0031  0.0458  139 THR C CA  
4835  C C   . THR C  139 ? 1.0343 1.1951 0.9300 0.0555  -0.0003 0.0470  139 THR C C   
4836  O O   . THR C  139 ? 0.9303 1.0908 0.8307 0.0575  -0.0022 0.0473  139 THR C O   
4837  C CB  . THR C  139 ? 1.0780 1.2235 0.9741 0.0509  0.0038  0.0398  139 THR C CB  
4838  O OG1 . THR C  139 ? 0.9264 1.0794 0.8147 0.0466  0.0027  0.0377  139 THR C OG1 
4839  C CG2 . THR C  139 ? 0.9942 1.1346 0.8956 0.0508  0.0019  0.0369  139 THR C CG2 
4840  N N   . ALA C  140 ? 1.2289 1.3988 1.1175 0.0530  -0.0011 0.0476  140 ALA C N   
4841  C CA  . ALA C  140 ? 1.1560 1.3362 1.0421 0.0523  -0.0044 0.0486  140 ALA C CA  
4842  C C   . ALA C  140 ? 1.2085 1.3874 1.0942 0.0486  -0.0063 0.0432  140 ALA C C   
4843  O O   . ALA C  140 ? 1.0797 1.2655 0.9648 0.0482  -0.0091 0.0434  140 ALA C O   
4844  C CB  . ALA C  140 ? 1.1514 1.3417 1.0297 0.0501  -0.0047 0.0505  140 ALA C CB  
4845  N N   . ALA C  141 ? 1.2152 1.3851 1.1015 0.0460  -0.0046 0.0386  141 ALA C N   
4846  C CA  . ALA C  141 ? 1.0944 1.2619 0.9805 0.0425  -0.0060 0.0334  141 ALA C CA  
4847  C C   . ALA C  141 ? 1.0160 1.1799 0.9090 0.0452  -0.0078 0.0335  141 ALA C C   
4848  O O   . ALA C  141 ? 0.9278 1.0941 0.8205 0.0433  -0.0101 0.0311  141 ALA C O   
4849  C CB  . ALA C  141 ? 1.0429 1.2019 0.9283 0.0392  -0.0033 0.0289  141 ALA C CB  
4850  N N   . CYS C  142 ? 0.9819 1.1399 0.8808 0.0494  -0.0066 0.0362  142 CYS C N   
4851  C CA  . CYS C  142 ? 1.0455 1.1996 0.9508 0.0520  -0.0080 0.0364  142 CYS C CA  
4852  C C   . CYS C  142 ? 1.0141 1.1731 0.9223 0.0568  -0.0086 0.0418  142 CYS C C   
4853  O O   . CYS C  142 ? 0.9640 1.1177 0.8771 0.0604  -0.0070 0.0443  142 CYS C O   
4854  C CB  . CYS C  142 ? 1.1616 1.3042 1.0722 0.0528  -0.0062 0.0347  142 CYS C CB  
4855  S SG  . CYS C  142 ? 1.2394 1.3756 1.1480 0.0476  -0.0050 0.0289  142 CYS C SG  
4856  N N   . PRO C  143 ? 1.0925 1.2615 0.9979 0.0567  -0.0107 0.0436  143 PRO C N   
4857  C CA  . PRO C  143 ? 1.0991 1.2741 1.0070 0.0611  -0.0111 0.0492  143 PRO C CA  
4858  C C   . PRO C  143 ? 1.2020 1.3740 1.1163 0.0641  -0.0120 0.0499  143 PRO C C   
4859  O O   . PRO C  143 ? 1.1930 1.3645 1.1077 0.0621  -0.0139 0.0466  143 PRO C O   
4860  C CB  . PRO C  143 ? 1.1250 1.3121 1.0274 0.0592  -0.0133 0.0502  143 PRO C CB  
4861  C CG  . PRO C  143 ? 1.1593 1.3463 1.0558 0.0535  -0.0137 0.0451  143 PRO C CG  
4862  C CD  . PRO C  143 ? 1.1797 1.3554 1.0795 0.0524  -0.0128 0.0407  143 PRO C CD  
4863  N N   . HIS C  144 ? 1.2316 1.4015 1.1508 0.0687  -0.0104 0.0540  144 HIS C N   
4864  C CA  . HIS C  144 ? 1.3069 1.4751 1.2318 0.0718  -0.0109 0.0554  144 HIS C CA  
4865  C C   . HIS C  144 ? 1.4910 1.6682 1.4170 0.0754  -0.0110 0.0611  144 HIS C C   
4866  O O   . HIS C  144 ? 1.5080 1.6848 1.4363 0.0790  -0.0088 0.0655  144 HIS C O   
4867  C CB  . HIS C  144 ? 1.2018 1.3593 1.1325 0.0741  -0.0087 0.0551  144 HIS C CB  
4868  C CG  . HIS C  144 ? 1.3552 1.5084 1.2908 0.0752  -0.0094 0.0538  144 HIS C CG  
4869  N ND1 . HIS C  144 ? 1.5448 1.6927 1.4864 0.0789  -0.0075 0.0560  144 HIS C ND1 
4870  C CD2 . HIS C  144 ? 1.3266 1.4800 1.2619 0.0728  -0.0117 0.0504  144 HIS C CD2 
4871  C CE1 . HIS C  144 ? 1.5290 1.6741 1.4735 0.0786  -0.0086 0.0539  144 HIS C CE1 
4872  N NE2 . HIS C  144 ? 1.3752 1.5235 1.3159 0.0750  -0.0112 0.0506  144 HIS C NE2 
4873  N N   . ALA C  145 ? 1.4830 1.6685 1.4074 0.0745  -0.0134 0.0613  145 ALA C N   
4874  C CA  . ALA C  145 ? 1.5054 1.7007 1.4308 0.0776  -0.0139 0.0668  145 ALA C CA  
4875  C C   . ALA C  145 ? 1.5625 1.7631 1.4845 0.0785  -0.0128 0.0709  145 ALA C C   
4876  O O   . ALA C  145 ? 1.4194 1.6192 1.3449 0.0827  -0.0106 0.0756  145 ALA C O   
4877  C CB  . ALA C  145 ? 1.3242 1.5160 1.2569 0.0823  -0.0123 0.0699  145 ALA C CB  
4878  N N   . GLY C  146 ? 1.7655 1.9714 1.6806 0.0744  -0.0141 0.0691  146 GLY C N   
4879  C CA  . GLY C  146 ? 1.7411 1.9528 1.6518 0.0745  -0.0134 0.0725  146 GLY C CA  
4880  C C   . GLY C  146 ? 1.7733 1.9764 1.6836 0.0747  -0.0104 0.0719  146 GLY C C   
4881  O O   . GLY C  146 ? 1.7847 1.9890 1.6891 0.0716  -0.0100 0.0705  146 GLY C O   
4882  N N   . ALA C  147 ? 1.4563 1.6505 1.3729 0.0782  -0.0082 0.0728  147 ALA C N   
4883  C CA  . ALA C  147 ? 1.4812 1.6669 1.3984 0.0789  -0.0052 0.0726  147 ALA C CA  
4884  C C   . ALA C  147 ? 1.3866 1.5652 1.3008 0.0743  -0.0051 0.0663  147 ALA C C   
4885  O O   . ALA C  147 ? 1.3451 1.5217 1.2594 0.0717  -0.0068 0.0619  147 ALA C O   
4886  C CB  . ALA C  147 ? 1.5136 1.6915 1.4387 0.0835  -0.0031 0.0746  147 ALA C CB  
4887  N N   . LYS C  148 ? 1.1173 1.2923 1.0290 0.0735  -0.0028 0.0662  148 LYS C N   
4888  C CA  . LYS C  148 ? 1.1040 1.2718 1.0134 0.0695  -0.0019 0.0607  148 LYS C CA  
4889  C C   . LYS C  148 ? 1.2000 1.3564 1.1161 0.0708  -0.0007 0.0584  148 LYS C C   
4890  O O   . LYS C  148 ? 1.1290 1.2801 1.0494 0.0742  0.0017  0.0610  148 LYS C O   
4891  C CB  . LYS C  148 ? 1.0557 1.2233 0.9604 0.0682  0.0005  0.0614  148 LYS C CB  
4892  C CG  . LYS C  148 ? 1.2985 1.4773 1.1958 0.0662  -0.0007 0.0634  148 LYS C CG  
4893  C CD  . LYS C  148 ? 1.3485 1.5260 1.2407 0.0645  0.0019  0.0635  148 LYS C CD  
4894  C CE  . LYS C  148 ? 1.3524 1.5246 1.2490 0.0690  0.0050  0.0676  148 LYS C CE  
4895  N NZ  . LYS C  148 ? 1.3793 1.5494 1.2711 0.0673  0.0078  0.0675  148 LYS C NZ  
4896  N N   . SER C  149 ? 1.1474 1.3000 1.0643 0.0681  -0.0023 0.0536  149 SER C N   
4897  C CA  . SER C  149 ? 1.0521 1.1945 0.9751 0.0689  -0.0016 0.0514  149 SER C CA  
4898  C C   . SER C  149 ? 1.1508 1.2866 1.0727 0.0649  -0.0011 0.0462  149 SER C C   
4899  O O   . SER C  149 ? 1.0318 1.1691 0.9487 0.0621  -0.0001 0.0449  149 SER C O   
4900  C CB  . SER C  149 ? 1.0648 1.2080 0.9915 0.0699  -0.0039 0.0509  149 SER C CB  
4901  O OG  . SER C  149 ? 1.2656 1.3996 1.1985 0.0714  -0.0030 0.0498  149 SER C OG  
4902  N N   . PHE C  150 ? 1.0617 1.1902 0.9882 0.0645  -0.0017 0.0434  150 PHE C N   
4903  C CA  . PHE C  150 ? 0.8030 0.9247 0.7296 0.0610  -0.0012 0.0389  150 PHE C CA  
4904  C C   . PHE C  150 ? 0.9022 1.0188 0.8334 0.0605  -0.0030 0.0363  150 PHE C C   
4905  O O   . PHE C  150 ? 1.0306 1.1487 0.9646 0.0628  -0.0044 0.0378  150 PHE C O   
4906  C CB  . PHE C  150 ? 0.8226 0.9374 0.7515 0.0620  0.0021  0.0396  150 PHE C CB  
4907  C CG  . PHE C  150 ? 0.7139 0.8230 0.6422 0.0583  0.0032  0.0354  150 PHE C CG  
4908  C CD1 . PHE C  150 ? 0.7144 0.8273 0.6363 0.0546  0.0034  0.0332  150 PHE C CD1 
4909  C CD2 . PHE C  150 ? 0.7878 0.8878 0.7220 0.0585  0.0041  0.0339  150 PHE C CD2 
4910  C CE1 . PHE C  150 ? 0.6418 0.7492 0.5635 0.0512  0.0049  0.0294  150 PHE C CE1 
4911  C CE2 . PHE C  150 ? 0.8561 0.9510 0.7903 0.0553  0.0053  0.0304  150 PHE C CE2 
4912  C CZ  . PHE C  150 ? 0.7459 0.8443 0.6740 0.0517  0.0058  0.0281  150 PHE C CZ  
4913  N N   . TYR C  151 ? 0.9145 1.0252 0.8463 0.0575  -0.0029 0.0324  151 TYR C N   
4914  C CA  . TYR C  151 ? 0.7648 0.8703 0.7010 0.0568  -0.0046 0.0300  151 TYR C CA  
4915  C C   . TYR C  151 ? 0.7297 0.8294 0.6723 0.0602  -0.0038 0.0321  151 TYR C C   
4916  O O   . TYR C  151 ? 0.7903 0.8865 0.7351 0.0620  -0.0013 0.0339  151 TYR C O   
4917  C CB  . TYR C  151 ? 0.8071 0.9071 0.7434 0.0532  -0.0042 0.0261  151 TYR C CB  
4918  C CG  . TYR C  151 ? 0.6668 0.7715 0.5967 0.0494  -0.0044 0.0236  151 TYR C CG  
4919  C CD1 . TYR C  151 ? 0.6741 0.7833 0.6011 0.0473  -0.0070 0.0216  151 TYR C CD1 
4920  C CD2 . TYR C  151 ? 0.6476 0.7521 0.5743 0.0479  -0.0018 0.0231  151 TYR C CD2 
4921  C CE1 . TYR C  151 ? 0.6316 0.7452 0.5529 0.0436  -0.0070 0.0191  151 TYR C CE1 
4922  C CE2 . TYR C  151 ? 0.5803 0.6890 0.5011 0.0441  -0.0017 0.0206  151 TYR C CE2 
4923  C CZ  . TYR C  151 ? 0.6297 0.7429 0.5478 0.0420  -0.0044 0.0186  151 TYR C CZ  
4924  O OH  . TYR C  151 ? 0.7079 0.8253 0.6200 0.0381  -0.0042 0.0158  151 TYR C OH  
4925  N N   . LYS C  152 ? 0.6462 0.7450 0.5918 0.0610  -0.0058 0.0318  152 LYS C N   
4926  C CA  . LYS C  152 ? 0.8164 0.9098 0.7679 0.0639  -0.0050 0.0335  152 LYS C CA  
4927  C C   . LYS C  152 ? 0.8076 0.8924 0.7636 0.0627  -0.0043 0.0316  152 LYS C C   
4928  O O   . LYS C  152 ? 0.8348 0.9148 0.7951 0.0649  -0.0024 0.0332  152 LYS C O   
4929  C CB  . LYS C  152 ? 0.7762 0.8711 0.7292 0.0646  -0.0072 0.0333  152 LYS C CB  
4930  C CG  . LYS C  152 ? 1.1483 1.2518 1.0981 0.0662  -0.0079 0.0357  152 LYS C CG  
4931  C CD  . LYS C  152 ? 1.4948 1.6005 1.4456 0.0700  -0.0055 0.0401  152 LYS C CD  
4932  C CE  . LYS C  152 ? 1.5644 1.6790 1.5126 0.0717  -0.0062 0.0429  152 LYS C CE  
4933  N NZ  . LYS C  152 ? 1.5464 1.6634 1.4957 0.0756  -0.0038 0.0476  152 LYS C NZ  
4934  N N   . ASN C  153 ? 0.7042 0.7869 0.6594 0.0593  -0.0057 0.0282  153 ASN C N   
4935  C CA  . ASN C  153 ? 0.7383 0.8132 0.6982 0.0580  -0.0054 0.0264  153 ASN C CA  
4936  C C   . ASN C  153 ? 0.7440 0.8157 0.7042 0.0573  -0.0027 0.0262  153 ASN C C   
4937  O O   . ASN C  153 ? 0.7275 0.7931 0.6920 0.0562  -0.0022 0.0249  153 ASN C O   
4938  C CB  . ASN C  153 ? 0.6128 0.6866 0.5724 0.0548  -0.0081 0.0231  153 ASN C CB  
4939  C CG  . ASN C  153 ? 0.8019 0.8778 0.7616 0.0553  -0.0106 0.0231  153 ASN C CG  
4940  O OD1 . ASN C  153 ? 0.8636 0.9394 0.8255 0.0581  -0.0102 0.0252  153 ASN C OD1 
4941  N ND2 . ASN C  153 ? 0.7887 0.8662 0.7461 0.0527  -0.0129 0.0206  153 ASN C ND2 
4942  N N   . LEU C  154 ? 0.7227 0.7989 0.6786 0.0578  -0.0009 0.0276  154 LEU C N   
4943  C CA  . LEU C  154 ? 0.7357 0.8093 0.6913 0.0572  0.0021  0.0275  154 LEU C CA  
4944  C C   . LEU C  154 ? 0.7951 0.8711 0.7494 0.0602  0.0044  0.0311  154 LEU C C   
4945  O O   . LEU C  154 ? 0.9230 1.0050 0.8747 0.0621  0.0037  0.0333  154 LEU C O   
4946  C CB  . LEU C  154 ? 0.7766 0.8529 0.7269 0.0535  0.0022  0.0248  154 LEU C CB  
4947  C CG  . LEU C  154 ? 0.6675 0.7411 0.6188 0.0503  0.0004  0.0213  154 LEU C CG  
4948  C CD1 . LEU C  154 ? 0.6181 0.6954 0.5633 0.0468  0.0008  0.0188  154 LEU C CD1 
4949  C CD2 . LEU C  154 ? 0.7353 0.8006 0.6931 0.0499  0.0015  0.0205  154 LEU C CD2 
4950  N N   . ILE C  155 ? 0.8455 0.9170 0.8019 0.0607  0.0074  0.0317  155 ILE C N   
4951  C CA  . ILE C  155 ? 0.8913 0.9647 0.8463 0.0634  0.0100  0.0351  155 ILE C CA  
4952  C C   . ILE C  155 ? 0.7377 0.8115 0.6885 0.0614  0.0127  0.0343  155 ILE C C   
4953  O O   . ILE C  155 ? 0.6508 0.7188 0.6041 0.0597  0.0144  0.0323  155 ILE C O   
4954  C CB  . ILE C  155 ? 0.9436 1.0109 0.9054 0.0664  0.0118  0.0372  155 ILE C CB  
4955  C CG1 . ILE C  155 ? 0.9770 1.0440 0.9427 0.0683  0.0096  0.0380  155 ILE C CG1 
4956  C CG2 . ILE C  155 ? 0.7133 0.7823 0.6736 0.0691  0.0148  0.0407  155 ILE C CG2 
4957  C CD1 . ILE C  155 ? 1.1500 1.2110 1.1223 0.0710  0.0113  0.0398  155 ILE C CD1 
4958  N N   . TRP C  156 ? 0.7530 0.8338 0.6973 0.0615  0.0130  0.0359  156 TRP C N   
4959  C CA  . TRP C  156 ? 0.7235 0.8053 0.6629 0.0594  0.0156  0.0351  156 TRP C CA  
4960  C C   . TRP C  156 ? 0.7656 0.8442 0.7068 0.0619  0.0191  0.0380  156 TRP C C   
4961  O O   . TRP C  156 ? 0.9580 1.0413 0.8963 0.0642  0.0198  0.0415  156 TRP C O   
4962  C CB  . TRP C  156 ? 0.7549 0.8461 0.6862 0.0580  0.0144  0.0356  156 TRP C CB  
4963  C CG  . TRP C  156 ? 0.7254 0.8179 0.6506 0.0548  0.0167  0.0339  156 TRP C CG  
4964  C CD1 . TRP C  156 ? 0.7991 0.8852 0.7255 0.0535  0.0202  0.0324  156 TRP C CD1 
4965  C CD2 . TRP C  156 ? 0.7707 0.8714 0.6877 0.0522  0.0160  0.0334  156 TRP C CD2 
4966  N NE1 . TRP C  156 ? 0.7786 0.8679 0.6977 0.0502  0.0218  0.0309  156 TRP C NE1 
4967  C CE2 . TRP C  156 ? 0.7709 0.8694 0.6840 0.0493  0.0192  0.0315  156 TRP C CE2 
4968  C CE3 . TRP C  156 ? 0.7073 0.8171 0.6198 0.0520  0.0130  0.0345  156 TRP C CE3 
4969  C CZ2 . TRP C  156 ? 0.8573 0.9623 0.7620 0.0460  0.0195  0.0304  156 TRP C CZ2 
4970  C CZ3 . TRP C  156 ? 0.7682 0.8849 0.6726 0.0488  0.0131  0.0336  156 TRP C CZ3 
4971  C CH2 . TRP C  156 ? 0.8360 0.9503 0.7364 0.0457  0.0163  0.0314  156 TRP C CH2 
4972  N N   . LEU C  157 ? 0.6814 0.7520 0.6276 0.0616  0.0214  0.0367  157 LEU C N   
4973  C CA  . LEU C  157 ? 0.6526 0.7191 0.6013 0.0638  0.0250  0.0392  157 LEU C CA  
4974  C C   . LEU C  157 ? 0.8235 0.8931 0.7654 0.0625  0.0277  0.0397  157 LEU C C   
4975  O O   . LEU C  157 ? 0.9269 0.9963 0.8649 0.0588  0.0286  0.0365  157 LEU C O   
4976  C CB  . LEU C  157 ? 0.7068 0.7642 0.6627 0.0633  0.0266  0.0373  157 LEU C CB  
4977  C CG  . LEU C  157 ? 0.7771 0.8297 0.7411 0.0666  0.0264  0.0392  157 LEU C CG  
4978  C CD1 . LEU C  157 ? 0.7927 0.8495 0.7569 0.0688  0.0233  0.0410  157 LEU C CD1 
4979  C CD2 . LEU C  157 ? 0.6690 0.7142 0.6398 0.0651  0.0263  0.0366  157 LEU C CD2 
4980  N N   . VAL C  158 ? 0.8775 0.9495 0.8178 0.0654  0.0294  0.0436  158 VAL C N   
4981  C CA  . VAL C  158 ? 0.8761 0.9507 0.8100 0.0643  0.0323  0.0446  158 VAL C CA  
4982  C C   . VAL C  158 ? 0.9728 1.0417 0.9105 0.0669  0.0361  0.0470  158 VAL C C   
4983  O O   . VAL C  158 ? 0.9442 1.0084 0.8893 0.0698  0.0363  0.0484  158 VAL C O   
4984  C CB  . VAL C  158 ? 0.8744 0.9591 0.8014 0.0651  0.0306  0.0476  158 VAL C CB  
4985  C CG1 . VAL C  158 ? 0.9870 1.0776 0.9099 0.0622  0.0270  0.0450  158 VAL C CG1 
4986  C CG2 . VAL C  158 ? 0.9701 1.0564 0.9009 0.0700  0.0299  0.0523  158 VAL C CG2 
4987  N N   . LYS C  159 ? 1.0638 1.1333 0.9963 0.0656  0.0393  0.0475  159 LYS C N   
4988  C CA  . LYS C  159 ? 1.1918 1.2559 1.1274 0.0678  0.0434  0.0496  159 LYS C CA  
4989  C C   . LYS C  159 ? 1.1915 1.2578 1.1293 0.0725  0.0433  0.0548  159 LYS C C   
4990  O O   . LYS C  159 ? 0.9708 1.0449 0.9041 0.0737  0.0413  0.0575  159 LYS C O   
4991  C CB  . LYS C  159 ? 1.1417 1.2068 1.0701 0.0652  0.0468  0.0491  159 LYS C CB  
4992  C CG  . LYS C  159 ? 1.0803 1.1548 0.9999 0.0653  0.0460  0.0521  159 LYS C CG  
4993  C CD  . LYS C  159 ? 1.2188 1.2934 1.1314 0.0627  0.0498  0.0517  159 LYS C CD  
4994  C CE  . LYS C  159 ? 1.2534 1.3378 1.1575 0.0630  0.0489  0.0553  159 LYS C CE  
4995  N NZ  . LYS C  159 ? 1.2888 1.3735 1.1852 0.0601  0.0526  0.0547  159 LYS C NZ  
4996  N N   . LYS C  160 ? 1.1939 1.2532 1.1389 0.0752  0.0456  0.0561  160 LYS C N   
4997  C CA  . LYS C  160 ? 1.3422 1.4024 1.2901 0.0798  0.0463  0.0609  160 LYS C CA  
4998  C C   . LYS C  160 ? 1.4190 1.4797 1.3630 0.0809  0.0502  0.0641  160 LYS C C   
4999  O O   . LYS C  160 ? 1.3037 1.3576 1.2515 0.0815  0.0538  0.0640  160 LYS C O   
5000  C CB  . LYS C  160 ? 1.2170 1.2696 1.1749 0.0820  0.0467  0.0607  160 LYS C CB  
5001  C CG  . LYS C  160 ? 1.2387 1.2910 1.2001 0.0867  0.0482  0.0654  160 LYS C CG  
5002  C CD  . LYS C  160 ? 1.3050 1.3498 1.2761 0.0884  0.0485  0.0648  160 LYS C CD  
5003  C CE  . LYS C  160 ? 1.4099 1.4549 1.3839 0.0871  0.0444  0.0619  160 LYS C CE  
5004  N NZ  . LYS C  160 ? 1.4412 1.4802 1.4239 0.0889  0.0445  0.0619  160 LYS C NZ  
5005  N N   . GLY C  161 ? 1.4947 1.5638 1.4313 0.0812  0.0494  0.0669  161 GLY C N   
5006  C CA  . GLY C  161 ? 1.3812 1.4521 1.3134 0.0824  0.0527  0.0705  161 GLY C CA  
5007  C C   . GLY C  161 ? 1.4882 1.5537 1.4182 0.0794  0.0565  0.0679  161 GLY C C   
5008  O O   . GLY C  161 ? 1.5175 1.5771 1.4509 0.0812  0.0603  0.0694  161 GLY C O   
5009  N N   . ASN C  162 ? 1.4186 1.4859 1.3429 0.0749  0.0558  0.0639  162 ASN C N   
5010  C CA  . ASN C  162 ? 1.5458 1.6084 1.4671 0.0715  0.0597  0.0610  162 ASN C CA  
5011  C C   . ASN C  162 ? 1.5445 1.5969 1.4743 0.0710  0.0616  0.0576  162 ASN C C   
5012  O O   . ASN C  162 ? 1.5422 1.5890 1.4723 0.0698  0.0658  0.0565  162 ASN C O   
5013  C CB  . ASN C  162 ? 1.7358 1.7990 1.6528 0.0729  0.0635  0.0647  162 ASN C CB  
5014  C CG  . ASN C  162 ? 1.8968 1.9677 1.8024 0.0696  0.0635  0.0647  162 ASN C CG  
5015  O OD1 . ASN C  162 ? 2.1288 2.2012 2.0294 0.0700  0.0664  0.0676  162 ASN C OD1 
5016  N ND2 . ASN C  162 ? 1.7798 1.8556 1.6810 0.0661  0.0603  0.0616  162 ASN C ND2 
5017  N N   . SER C  163 ? 1.5304 1.5806 1.4670 0.0717  0.0587  0.0560  163 SER C N   
5018  C CA  . SER C  163 ? 1.5097 1.5509 1.4548 0.0712  0.0600  0.0531  163 SER C CA  
5019  C C   . SER C  163 ? 1.3671 1.4081 1.3157 0.0695  0.0562  0.0497  163 SER C C   
5020  O O   . SER C  163 ? 1.3088 1.3529 1.2593 0.0713  0.0525  0.0509  163 SER C O   
5021  C CB  . SER C  163 ? 1.4315 1.4674 1.3848 0.0754  0.0617  0.0561  163 SER C CB  
5022  O OG  . SER C  163 ? 1.3054 1.3328 1.2667 0.0746  0.0636  0.0536  163 SER C OG  
5023  N N   . TYR C  164 ? 1.1640 1.2010 1.1132 0.0659  0.0572  0.0455  164 TYR C N   
5024  C CA  . TYR C  164 ? 1.0608 1.0963 1.0142 0.0642  0.0540  0.0423  164 TYR C CA  
5025  C C   . TYR C  164 ? 1.0494 1.0761 1.0103 0.0631  0.0566  0.0399  164 TYR C C   
5026  O O   . TYR C  164 ? 0.9489 0.9734 0.9081 0.0597  0.0586  0.0368  164 TYR C O   
5027  C CB  . TYR C  164 ? 1.1508 1.1918 1.0965 0.0604  0.0521  0.0394  164 TYR C CB  
5028  C CG  . TYR C  164 ? 1.1053 1.1469 1.0542 0.0593  0.0479  0.0371  164 TYR C CG  
5029  C CD1 . TYR C  164 ? 0.9885 1.0375 0.9332 0.0594  0.0438  0.0376  164 TYR C CD1 
5030  C CD2 . TYR C  164 ? 0.9879 1.0228 0.9443 0.0583  0.0481  0.0345  164 TYR C CD2 
5031  C CE1 . TYR C  164 ? 0.8892 0.9386 0.8366 0.0584  0.0401  0.0354  164 TYR C CE1 
5032  C CE2 . TYR C  164 ? 0.9240 0.9594 0.8831 0.0572  0.0443  0.0325  164 TYR C CE2 
5033  C CZ  . TYR C  164 ? 0.9872 1.0297 0.9416 0.0573  0.0404  0.0329  164 TYR C CZ  
5034  O OH  . TYR C  164 ? 0.9390 0.9819 0.8959 0.0562  0.0367  0.0309  164 TYR C OH  
5035  N N   . PRO C  165 ? 0.9262 0.9479 0.8960 0.0659  0.0567  0.0415  165 PRO C N   
5036  C CA  . PRO C  165 ? 1.0524 1.0660 1.0308 0.0654  0.0589  0.0398  165 PRO C CA  
5037  C C   . PRO C  165 ? 0.9658 0.9783 0.9479 0.0631  0.0557  0.0367  165 PRO C C   
5038  O O   . PRO C  165 ? 0.8888 0.9057 0.8693 0.0632  0.0514  0.0366  165 PRO C O   
5039  C CB  . PRO C  165 ? 0.9871 0.9975 0.9729 0.0692  0.0590  0.0428  165 PRO C CB  
5040  C CG  . PRO C  165 ? 1.1283 1.1447 1.1086 0.0719  0.0581  0.0463  165 PRO C CG  
5041  C CD  . PRO C  165 ? 0.8573 0.8809 0.8295 0.0699  0.0550  0.0451  165 PRO C CD  
5042  N N   . LYS C  166 ? 0.8480 0.8547 0.8353 0.0611  0.0579  0.0344  166 LYS C N   
5043  C CA  . LYS C  166 ? 1.0202 1.0253 1.0121 0.0592  0.0551  0.0319  166 LYS C CA  
5044  C C   . LYS C  166 ? 1.1192 1.1248 1.1167 0.0614  0.0508  0.0333  166 LYS C C   
5045  O O   . LYS C  166 ? 0.9755 0.9773 0.9800 0.0638  0.0515  0.0351  166 LYS C O   
5046  C CB  . LYS C  166 ? 0.8818 0.8797 0.8810 0.0577  0.0584  0.0302  166 LYS C CB  
5047  C CG  . LYS C  166 ? 1.0362 1.0317 1.0430 0.0567  0.0553  0.0288  166 LYS C CG  
5048  C CD  . LYS C  166 ? 1.1909 1.1793 1.2065 0.0559  0.0585  0.0280  166 LYS C CD  
5049  C CE  . LYS C  166 ? 1.2500 1.2368 1.2623 0.0526  0.0621  0.0253  166 LYS C CE  
5050  N NZ  . LYS C  166 ? 1.3259 1.3059 1.3477 0.0519  0.0651  0.0246  166 LYS C NZ  
5051  N N   . LEU C  167 ? 1.0485 1.0587 1.0429 0.0606  0.0465  0.0323  167 LEU C N   
5052  C CA  . LEU C  167 ? 1.0088 1.0193 1.0082 0.0622  0.0424  0.0332  167 LEU C CA  
5053  C C   . LEU C  167 ? 0.9814 0.9881 0.9875 0.0602  0.0407  0.0310  167 LEU C C   
5054  O O   . LEU C  167 ? 0.8287 0.8343 0.8338 0.0574  0.0417  0.0287  167 LEU C O   
5055  C CB  . LEU C  167 ? 0.7326 0.7502 0.7255 0.0627  0.0387  0.0337  167 LEU C CB  
5056  C CG  . LEU C  167 ? 0.8387 0.8609 0.8254 0.0597  0.0363  0.0311  167 LEU C CG  
5057  C CD1 . LEU C  167 ? 0.8660 0.8852 0.8577 0.0575  0.0341  0.0286  167 LEU C CD1 
5058  C CD2 . LEU C  167 ? 0.7606 0.7897 0.7420 0.0611  0.0331  0.0325  167 LEU C CD2 
5059  N N   . SER C  168 ? 0.8778 0.8825 0.8909 0.0616  0.0382  0.0319  168 SER C N   
5060  C CA  . SER C  168 ? 0.8880 0.8892 0.9080 0.0598  0.0363  0.0304  168 SER C CA  
5061  C C   . SER C  168 ? 0.9748 0.9764 0.9991 0.0609  0.0321  0.0312  168 SER C C   
5062  O O   . SER C  168 ? 1.1803 1.1783 1.2119 0.0622  0.0323  0.0325  168 SER C O   
5063  C CB  . SER C  168 ? 0.9875 0.9825 1.0150 0.0596  0.0400  0.0305  168 SER C CB  
5064  O OG  . SER C  168 ? 1.1645 1.1570 1.1967 0.0572  0.0391  0.0287  168 SER C OG  
5065  N N   . LYS C  169 ? 0.8779 0.8841 0.8974 0.0601  0.0284  0.0303  169 LYS C N   
5066  C CA  . LYS C  169 ? 0.8540 0.8608 0.8764 0.0606  0.0243  0.0306  169 LYS C CA  
5067  C C   . LYS C  169 ? 0.9295 0.9353 0.9549 0.0579  0.0214  0.0286  169 LYS C C   
5068  O O   . LYS C  169 ? 0.8799 0.8862 0.9028 0.0557  0.0221  0.0269  169 LYS C O   
5069  C CB  . LYS C  169 ? 0.7005 0.7131 0.7158 0.0617  0.0222  0.0311  169 LYS C CB  
5070  C CG  . LYS C  169 ? 0.9649 0.9777 0.9815 0.0649  0.0226  0.0335  169 LYS C CG  
5071  C CD  . LYS C  169 ? 0.9753 0.9853 0.9984 0.0650  0.0200  0.0336  169 LYS C CD  
5072  C CE  . LYS C  169 ? 1.1118 1.1226 1.1351 0.0678  0.0201  0.0356  169 LYS C CE  
5073  N NZ  . LYS C  169 ? 1.2719 1.2806 1.2965 0.0703  0.0243  0.0378  169 LYS C NZ  
5074  N N   . SER C  170 ? 1.0263 1.0308 1.0569 0.0579  0.0183  0.0289  170 SER C N   
5075  C CA  . SER C  170 ? 0.8301 0.8339 0.8640 0.0554  0.0152  0.0275  170 SER C CA  
5076  C C   . SER C  170 ? 0.7956 0.7999 0.8318 0.0555  0.0111  0.0278  170 SER C C   
5077  O O   . SER C  170 ? 0.9287 0.9306 0.9698 0.0569  0.0112  0.0291  170 SER C O   
5078  C CB  . SER C  170 ? 0.8259 0.8247 0.8675 0.0544  0.0172  0.0275  170 SER C CB  
5079  O OG  . SER C  170 ? 1.2261 1.2215 1.2740 0.0562  0.0189  0.0293  170 SER C OG  
5080  N N   . TYR C  171 ? 0.7802 0.7876 0.8126 0.0539  0.0078  0.0264  171 TYR C N   
5081  C CA  . TYR C  171 ? 0.7621 0.7703 0.7955 0.0537  0.0038  0.0264  171 TYR C CA  
5082  C C   . TYR C  171 ? 0.7549 0.7613 0.7933 0.0511  0.0009  0.0257  171 TYR C C   
5083  O O   . TYR C  171 ? 0.7247 0.7310 0.7626 0.0493  0.0011  0.0246  171 TYR C O   
5084  C CB  . TYR C  171 ? 0.8210 0.8342 0.8463 0.0538  0.0020  0.0256  171 TYR C CB  
5085  C CG  . TYR C  171 ? 0.7981 0.8124 0.8234 0.0525  -0.0023 0.0248  171 TYR C CG  
5086  C CD1 . TYR C  171 ? 0.7989 0.8130 0.8254 0.0537  -0.0035 0.0256  171 TYR C CD1 
5087  C CD2 . TYR C  171 ? 0.7940 0.8094 0.8180 0.0499  -0.0048 0.0232  171 TYR C CD2 
5088  C CE1 . TYR C  171 ? 0.8078 0.8227 0.8338 0.0522  -0.0072 0.0247  171 TYR C CE1 
5089  C CE2 . TYR C  171 ? 0.8089 0.8253 0.8326 0.0486  -0.0086 0.0225  171 TYR C CE2 
5090  C CZ  . TYR C  171 ? 0.8507 0.8668 0.8752 0.0497  -0.0098 0.0232  171 TYR C CZ  
5091  O OH  . TYR C  171 ? 0.9080 0.9249 0.9318 0.0481  -0.0135 0.0223  171 TYR C OH  
5092  N N   . ILE C  172 ? 0.7756 0.7804 0.8187 0.0509  -0.0016 0.0263  172 ILE C N   
5093  C CA  . ILE C  172 ? 0.7493 0.7528 0.7971 0.0485  -0.0048 0.0259  172 ILE C CA  
5094  C C   . ILE C  172 ? 0.8075 0.8136 0.8517 0.0473  -0.0090 0.0250  172 ILE C C   
5095  O O   . ILE C  172 ? 0.8300 0.8368 0.8725 0.0484  -0.0097 0.0252  172 ILE C O   
5096  C CB  . ILE C  172 ? 0.7919 0.7915 0.8489 0.0485  -0.0047 0.0274  172 ILE C CB  
5097  C CG1 . ILE C  172 ? 0.9180 0.9169 0.9801 0.0459  -0.0081 0.0274  172 ILE C CG1 
5098  C CG2 . ILE C  172 ? 0.9948 0.9939 1.0527 0.0499  -0.0050 0.0281  172 ILE C CG2 
5099  C CD1 . ILE C  172 ? 0.9412 0.9368 1.0117 0.0454  -0.0065 0.0287  172 ILE C CD1 
5100  N N   . ASN C  173 ? 0.8223 0.8295 0.8654 0.0450  -0.0114 0.0240  173 ASN C N   
5101  C CA  . ASN C  173 ? 0.7677 0.7774 0.8068 0.0436  -0.0153 0.0230  173 ASN C CA  
5102  C C   . ASN C  173 ? 0.9063 0.9145 0.9501 0.0426  -0.0183 0.0236  173 ASN C C   
5103  O O   . ASN C  173 ? 0.8562 0.8629 0.9048 0.0407  -0.0205 0.0241  173 ASN C O   
5104  C CB  . ASN C  173 ? 0.7354 0.7465 0.7725 0.0414  -0.0169 0.0219  173 ASN C CB  
5105  C CG  . ASN C  173 ? 0.8549 0.8690 0.8864 0.0401  -0.0203 0.0207  173 ASN C CG  
5106  O OD1 . ASN C  173 ? 0.9374 0.9524 0.9669 0.0408  -0.0215 0.0206  173 ASN C OD1 
5107  N ND2 . ASN C  173 ? 0.8279 0.8433 0.8571 0.0381  -0.0216 0.0196  173 ASN C ND2 
5108  N N   . ASP C  174 ? 1.1580 1.1664 1.2002 0.0440  -0.0182 0.0237  174 ASP C N   
5109  C CA  . ASP C  174 ? 1.1316 1.1385 1.1774 0.0429  -0.0207 0.0240  174 ASP C CA  
5110  C C   . ASP C  174 ? 1.0931 1.1022 1.1340 0.0410  -0.0244 0.0226  174 ASP C C   
5111  O O   . ASP C  174 ? 1.1817 1.1899 1.2245 0.0395  -0.0268 0.0225  174 ASP C O   
5112  C CB  . ASP C  174 ? 1.1953 1.2007 1.2422 0.0451  -0.0184 0.0246  174 ASP C CB  
5113  C CG  . ASP C  174 ? 1.4654 1.4734 1.5054 0.0473  -0.0166 0.0241  174 ASP C CG  
5114  O OD1 . ASP C  174 ? 1.5373 1.5463 1.5742 0.0470  -0.0181 0.0234  174 ASP C OD1 
5115  O OD2 . ASP C  174 ? 1.4507 1.4598 1.4883 0.0491  -0.0137 0.0246  174 ASP C OD2 
5116  N N   . LYS C  175 ? 0.9697 0.9818 1.0045 0.0408  -0.0246 0.0215  175 LYS C N   
5117  C CA  . LYS C  175 ? 0.9626 0.9769 0.9926 0.0390  -0.0278 0.0202  175 LYS C CA  
5118  C C   . LYS C  175 ? 0.9584 0.9720 0.9914 0.0360  -0.0311 0.0203  175 LYS C C   
5119  O O   . LYS C  175 ? 0.9560 0.9677 0.9948 0.0356  -0.0307 0.0214  175 LYS C O   
5120  C CB  . LYS C  175 ? 0.8453 0.8631 0.8680 0.0398  -0.0269 0.0191  175 LYS C CB  
5121  C CG  . LYS C  175 ? 0.8073 0.8266 0.8270 0.0428  -0.0235 0.0195  175 LYS C CG  
5122  C CD  . LYS C  175 ? 0.7578 0.7773 0.7759 0.0439  -0.0237 0.0194  175 LYS C CD  
5123  C CE  . LYS C  175 ? 0.8071 0.8286 0.8219 0.0470  -0.0204 0.0202  175 LYS C CE  
5124  N NZ  . LYS C  175 ? 1.1208 1.1427 1.1342 0.0482  -0.0202 0.0202  175 LYS C NZ  
5125  N N   . GLY C  176 ? 0.6786 0.6937 0.7079 0.0340  -0.0343 0.0192  176 GLY C N   
5126  C CA  . GLY C  176 ? 1.0238 1.0387 1.0553 0.0311  -0.0377 0.0194  176 GLY C CA  
5127  C C   . GLY C  176 ? 1.0610 1.0781 1.0879 0.0303  -0.0381 0.0184  176 GLY C C   
5128  O O   . GLY C  176 ? 1.1347 1.1524 1.1612 0.0279  -0.0411 0.0183  176 GLY C O   
5129  N N   . LYS C  177 ? 0.9862 1.0048 1.0094 0.0323  -0.0351 0.0178  177 LYS C N   
5130  C CA  . LYS C  177 ? 0.8110 0.8321 0.8292 0.0315  -0.0350 0.0166  177 LYS C CA  
5131  C C   . LYS C  177 ? 0.6399 0.6613 0.6579 0.0333  -0.0312 0.0166  177 LYS C C   
5132  O O   . LYS C  177 ? 0.7467 0.7670 0.7666 0.0354  -0.0286 0.0174  177 LYS C O   
5133  C CB  . LYS C  177 ? 0.8557 0.8799 0.8667 0.0316  -0.0360 0.0150  177 LYS C CB  
5134  C CG  . LYS C  177 ? 0.7677 0.7928 0.7766 0.0343  -0.0337 0.0151  177 LYS C CG  
5135  C CD  . LYS C  177 ? 0.8902 0.9181 0.8929 0.0343  -0.0348 0.0138  177 LYS C CD  
5136  C CE  . LYS C  177 ? 1.0237 1.0502 1.0272 0.0324  -0.0379 0.0135  177 LYS C CE  
5137  N NZ  . LYS C  177 ? 1.0706 1.0940 1.0788 0.0331  -0.0374 0.0145  177 LYS C NZ  
5138  N N   . GLU C  178 ? 0.6301 0.6528 0.6455 0.0322  -0.0306 0.0156  178 GLU C N   
5139  C CA  . GLU C  178 ? 0.6330 0.6561 0.6472 0.0333  -0.0269 0.0153  178 GLU C CA  
5140  C C   . GLU C  178 ? 0.7263 0.7520 0.7355 0.0356  -0.0250 0.0149  178 GLU C C   
5141  O O   . GLU C  178 ? 0.6960 0.7241 0.7011 0.0360  -0.0266 0.0144  178 GLU C O   
5142  C CB  . GLU C  178 ? 0.7526 0.7772 0.7635 0.0315  -0.0268 0.0138  178 GLU C CB  
5143  C CG  . GLU C  178 ? 1.0314 1.0536 1.0473 0.0293  -0.0283 0.0144  178 GLU C CG  
5144  C CD  . GLU C  178 ? 1.0724 1.0961 1.0846 0.0274  -0.0281 0.0128  178 GLU C CD  
5145  O OE1 . GLU C  178 ? 0.9282 0.9552 0.9337 0.0270  -0.0291 0.0112  178 GLU C OE1 
5146  O OE2 . GLU C  178 ? 1.2176 1.2391 1.2338 0.0264  -0.0267 0.0131  178 GLU C OE2 
5147  N N   . VAL C  179 ? 0.6543 0.6796 0.6640 0.0371  -0.0215 0.0154  179 VAL C N   
5148  C CA  . VAL C  179 ? 0.6589 0.6871 0.6638 0.0393  -0.0195 0.0154  179 VAL C CA  
5149  C C   . VAL C  179 ? 0.5460 0.5765 0.5463 0.0390  -0.0170 0.0143  179 VAL C C   
5150  O O   . VAL C  179 ? 0.5023 0.5307 0.5052 0.0386  -0.0145 0.0143  179 VAL C O   
5151  C CB  . VAL C  179 ? 0.6282 0.6539 0.6371 0.0418  -0.0173 0.0172  179 VAL C CB  
5152  C CG1 . VAL C  179 ? 0.6637 0.6925 0.6678 0.0440  -0.0147 0.0175  179 VAL C CG1 
5153  C CG2 . VAL C  179 ? 0.6578 0.6818 0.6699 0.0421  -0.0196 0.0179  179 VAL C CG2 
5154  N N   . LEU C  180 ? 0.4855 0.5207 0.4791 0.0390  -0.0176 0.0133  180 LEU C N   
5155  C CA  . LEU C  180 ? 0.4930 0.5313 0.4814 0.0385  -0.0154 0.0121  180 LEU C CA  
5156  C C   . LEU C  180 ? 0.4645 0.5040 0.4516 0.0409  -0.0124 0.0134  180 LEU C C   
5157  O O   . LEU C  180 ? 0.6587 0.7009 0.6435 0.0430  -0.0127 0.0145  180 LEU C O   
5158  C CB  . LEU C  180 ? 0.4507 0.4941 0.4327 0.0375  -0.0173 0.0107  180 LEU C CB  
5159  C CG  . LEU C  180 ? 0.5091 0.5566 0.4851 0.0367  -0.0154 0.0094  180 LEU C CG  
5160  C CD1 . LEU C  180 ? 0.4929 0.5383 0.4698 0.0340  -0.0141 0.0077  180 LEU C CD1 
5161  C CD2 . LEU C  180 ? 0.4035 0.4567 0.3735 0.0364  -0.0174 0.0084  180 LEU C CD2 
5162  N N   . VAL C  181 ? 0.4253 0.4626 0.4139 0.0407  -0.0093 0.0134  181 VAL C N   
5163  C CA  . VAL C  181 ? 0.5234 0.5617 0.5104 0.0428  -0.0061 0.0146  181 VAL C CA  
5164  C C   . VAL C  181 ? 0.5966 0.6386 0.5772 0.0415  -0.0042 0.0132  181 VAL C C   
5165  O O   . VAL C  181 ? 0.5689 0.6095 0.5494 0.0391  -0.0031 0.0114  181 VAL C O   
5166  C CB  . VAL C  181 ? 0.5039 0.5367 0.4973 0.0436  -0.0036 0.0158  181 VAL C CB  
5167  C CG1 . VAL C  181 ? 0.4756 0.5094 0.4673 0.0460  -0.0005 0.0173  181 VAL C CG1 
5168  C CG2 . VAL C  181 ? 0.5460 0.5751 0.5462 0.0442  -0.0057 0.0170  181 VAL C CG2 
5169  N N   . LEU C  182 ? 0.6559 0.7028 0.6311 0.0429  -0.0037 0.0140  182 LEU C N   
5170  C CA  . LEU C  182 ? 0.6138 0.6651 0.5825 0.0416  -0.0020 0.0128  182 LEU C CA  
5171  C C   . LEU C  182 ? 0.5632 0.6147 0.5308 0.0434  0.0014  0.0145  182 LEU C C   
5172  O O   . LEU C  182 ? 0.6519 0.7028 0.6218 0.0463  0.0016  0.0169  182 LEU C O   
5173  C CB  . LEU C  182 ? 0.4368 0.4948 0.3995 0.0414  -0.0044 0.0124  182 LEU C CB  
5174  C CG  . LEU C  182 ? 0.6010 0.6596 0.5634 0.0393  -0.0075 0.0104  182 LEU C CG  
5175  C CD1 . LEU C  182 ? 0.6983 0.7577 0.6623 0.0411  -0.0104 0.0117  182 LEU C CD1 
5176  C CD2 . LEU C  182 ? 0.6025 0.6666 0.5581 0.0369  -0.0077 0.0084  182 LEU C CD2 
5177  N N   . TRP C  183 ? 0.5334 0.5857 0.4974 0.0416  0.0041  0.0131  183 TRP C N   
5178  C CA  . TRP C  183 ? 0.6193 0.6722 0.5811 0.0429  0.0073  0.0145  183 TRP C CA  
5179  C C   . TRP C  183 ? 0.5963 0.6536 0.5507 0.0403  0.0090  0.0127  183 TRP C C   
5180  O O   . TRP C  183 ? 0.6341 0.6927 0.5860 0.0374  0.0080  0.0101  183 TRP C O   
5181  C CB  . TRP C  183 ? 0.6176 0.6635 0.5857 0.0434  0.0103  0.0151  183 TRP C CB  
5182  C CG  . TRP C  183 ? 0.5443 0.5863 0.5138 0.0404  0.0123  0.0126  183 TRP C CG  
5183  C CD1 . TRP C  183 ? 0.6054 0.6471 0.5715 0.0385  0.0161  0.0112  183 TRP C CD1 
5184  C CD2 . TRP C  183 ? 0.6803 0.7182 0.6552 0.0388  0.0111  0.0112  183 TRP C CD2 
5185  N NE1 . TRP C  183 ? 0.5773 0.6145 0.5465 0.0360  0.0174  0.0090  183 TRP C NE1 
5186  C CE2 . TRP C  183 ? 0.6405 0.6755 0.6153 0.0361  0.0143  0.0091  183 TRP C CE2 
5187  C CE3 . TRP C  183 ? 0.6647 0.7009 0.6443 0.0392  0.0076  0.0116  183 TRP C CE3 
5188  C CZ2 . TRP C  183 ? 0.5800 0.6107 0.5599 0.0342  0.0142  0.0077  183 TRP C CZ2 
5189  C CZ3 . TRP C  183 ? 0.5663 0.5987 0.5506 0.0371  0.0072  0.0103  183 TRP C CZ3 
5190  C CH2 . TRP C  183 ? 0.5758 0.6054 0.5603 0.0348  0.0105  0.0085  183 TRP C CH2 
5191  N N   . GLY C  184 ? 0.5791 0.6386 0.5298 0.0412  0.0115  0.0140  184 GLY C N   
5192  C CA  . GLY C  184 ? 0.5920 0.6562 0.5351 0.0386  0.0131  0.0124  184 GLY C CA  
5193  C C   . GLY C  184 ? 0.6019 0.6631 0.5438 0.0380  0.0176  0.0123  184 GLY C C   
5194  O O   . GLY C  184 ? 0.6299 0.6878 0.5757 0.0406  0.0193  0.0147  184 GLY C O   
5195  N N   . ILE C  185 ? 0.5957 0.6581 0.5325 0.0344  0.0196  0.0095  185 ILE C N   
5196  C CA  . ILE C  185 ? 0.4594 0.5199 0.3936 0.0332  0.0241  0.0091  185 ILE C CA  
5197  C C   . ILE C  185 ? 0.5585 0.6269 0.4831 0.0316  0.0243  0.0090  185 ILE C C   
5198  O O   . ILE C  185 ? 0.6284 0.7006 0.5480 0.0283  0.0235  0.0063  185 ILE C O   
5199  C CB  . ILE C  185 ? 0.5643 0.6187 0.5007 0.0299  0.0272  0.0057  185 ILE C CB  
5200  C CG1 . ILE C  185 ? 0.5588 0.6062 0.5049 0.0312  0.0265  0.0060  185 ILE C CG1 
5201  C CG2 . ILE C  185 ? 0.5498 0.6016 0.4839 0.0288  0.0323  0.0053  185 ILE C CG2 
5202  C CD1 . ILE C  185 ? 0.5776 0.6208 0.5299 0.0348  0.0273  0.0091  185 ILE C CD1 
5203  N N   . HIS C  186 ? 0.6548 0.7259 0.5770 0.0339  0.0253  0.0120  186 HIS C N   
5204  C CA  . HIS C  186 ? 0.6845 0.7638 0.5976 0.0326  0.0253  0.0125  186 HIS C CA  
5205  C C   . HIS C  186 ? 0.6100 0.6881 0.5177 0.0291  0.0296  0.0102  186 HIS C C   
5206  O O   . HIS C  186 ? 0.6461 0.7182 0.5566 0.0296  0.0333  0.0106  186 HIS C O   
5207  C CB  . HIS C  186 ? 0.7535 0.8371 0.6661 0.0367  0.0242  0.0173  186 HIS C CB  
5208  C CG  . HIS C  186 ? 0.7853 0.8776 0.6890 0.0356  0.0241  0.0184  186 HIS C CG  
5209  N ND1 . HIS C  186 ? 0.7996 0.8925 0.6998 0.0361  0.0271  0.0204  186 HIS C ND1 
5210  C CD2 . HIS C  186 ? 0.7585 0.8594 0.6561 0.0338  0.0214  0.0180  186 HIS C CD2 
5211  C CE1 . HIS C  186 ? 0.8273 0.9292 0.7195 0.0347  0.0261  0.0213  186 HIS C CE1 
5212  N NE2 . HIS C  186 ? 0.7169 0.8238 0.6075 0.0333  0.0226  0.0198  186 HIS C NE2 
5213  N N   . HIS C  187 ? 0.6674 0.7514 0.5675 0.0252  0.0293  0.0077  187 HIS C N   
5214  C CA  . HIS C  187 ? 0.6994 0.7832 0.5931 0.0212  0.0333  0.0052  187 HIS C CA  
5215  C C   . HIS C  187 ? 0.8197 0.9130 0.7043 0.0206  0.0325  0.0071  187 HIS C C   
5216  O O   . HIS C  187 ? 0.8699 0.9706 0.7490 0.0184  0.0299  0.0060  187 HIS C O   
5217  C CB  . HIS C  187 ? 0.7260 0.8082 0.6179 0.0164  0.0342  0.0002  187 HIS C CB  
5218  C CG  . HIS C  187 ? 0.6679 0.7417 0.5686 0.0169  0.0346  -0.0014 187 HIS C CG  
5219  N ND1 . HIS C  187 ? 0.7366 0.8017 0.6419 0.0162  0.0391  -0.0028 187 HIS C ND1 
5220  C CD2 . HIS C  187 ? 0.7754 0.8482 0.6813 0.0179  0.0312  -0.0017 187 HIS C CD2 
5221  C CE1 . HIS C  187 ? 0.8446 0.9041 0.7577 0.0168  0.0382  -0.0037 187 HIS C CE1 
5222  N NE2 . HIS C  187 ? 0.8120 0.8760 0.7254 0.0178  0.0334  -0.0030 187 HIS C NE2 
5223  N N   . PRO C  188 ? 0.8105 0.9036 0.6938 0.0227  0.0347  0.0102  188 PRO C N   
5224  C CA  . PRO C  188 ? 0.8468 0.9489 0.7220 0.0225  0.0340  0.0127  188 PRO C CA  
5225  C C   . PRO C  188 ? 0.9297 1.0364 0.7953 0.0167  0.0355  0.0090  188 PRO C C   
5226  O O   . PRO C  188 ? 0.7875 0.8887 0.6529 0.0129  0.0384  0.0045  188 PRO C O   
5227  C CB  . PRO C  188 ? 0.8295 0.9274 0.7059 0.0251  0.0375  0.0157  188 PRO C CB  
5228  C CG  . PRO C  188 ? 0.8609 0.9498 0.7479 0.0284  0.0380  0.0162  188 PRO C CG  
5229  C CD  . PRO C  188 ? 0.7873 0.8719 0.6774 0.0255  0.0377  0.0117  188 PRO C CD  
5230  N N   . SER C  189 ? 0.9273 1.0442 0.7854 0.0159  0.0334  0.0110  189 SER C N   
5231  C CA  . SER C  189 ? 0.8843 1.0069 0.7327 0.0102  0.0343  0.0077  189 SER C CA  
5232  C C   . SER C  189 ? 0.9857 1.1059 0.8283 0.0075  0.0392  0.0068  189 SER C C   
5233  O O   . SER C  189 ? 0.9997 1.1184 0.8371 0.0022  0.0421  0.0022  189 SER C O   
5234  C CB  . SER C  189 ? 0.8913 1.0264 0.7341 0.0102  0.0298  0.0103  189 SER C CB  
5235  O OG  . SER C  189 ? 1.0035 1.1428 0.8459 0.0144  0.0289  0.0161  189 SER C OG  
5236  N N   . THR C  190 ? 1.0922 1.2118 0.9358 0.0112  0.0403  0.0112  190 THR C N   
5237  C CA  . THR C  190 ? 1.0555 1.1731 0.8933 0.0090  0.0450  0.0109  190 THR C CA  
5238  C C   . THR C  190 ? 0.9847 1.0928 0.8298 0.0129  0.0483  0.0130  190 THR C C   
5239  O O   . THR C  190 ? 1.0314 1.1371 0.8846 0.0181  0.0462  0.0162  190 THR C O   
5240  C CB  . THR C  190 ? 0.9968 1.1253 0.8258 0.0086  0.0434  0.0146  190 THR C CB  
5241  O OG1 . THR C  190 ? 1.3732 1.4987 1.2010 0.0103  0.0469  0.0174  190 THR C OG1 
5242  N N   . SER C  191 ? 1.1156 1.2183 0.9578 0.0103  0.0536  0.0109  191 SER C N   
5243  C CA  . SER C  191 ? 1.1641 1.2577 1.0126 0.0136  0.0573  0.0127  191 SER C CA  
5244  C C   . SER C  191 ? 1.0556 1.1531 0.9047 0.0186  0.0558  0.0190  191 SER C C   
5245  O O   . SER C  191 ? 1.1112 1.2023 0.9677 0.0228  0.0572  0.0215  191 SER C O   
5246  C CB  . SER C  191 ? 1.1105 1.1983 0.9546 0.0094  0.0635  0.0092  191 SER C CB  
5247  O OG  . SER C  191 ? 1.2716 1.3666 1.1046 0.0065  0.0644  0.0101  191 SER C OG  
5248  N N   . ALA C  192 ? 1.1102 1.2185 0.9515 0.0181  0.0529  0.0216  192 ALA C N   
5249  C CA  . ALA C  192 ? 1.2155 1.3286 1.0572 0.0229  0.0511  0.0280  192 ALA C CA  
5250  C C   . ALA C  192 ? 1.2407 1.3541 1.0912 0.0281  0.0469  0.0309  192 ALA C C   
5251  O O   . ALA C  192 ? 1.1788 1.2900 1.0350 0.0331  0.0470  0.0352  192 ALA C O   
5252  C CB  . ALA C  192 ? 1.3051 1.4302 1.1362 0.0208  0.0491  0.0302  192 ALA C CB  
5253  N N   . ASP C  193 ? 1.3054 1.4215 1.1571 0.0267  0.0435  0.0283  193 ASP C N   
5254  C CA  . ASP C  193 ? 1.1455 1.2614 1.0054 0.0309  0.0396  0.0302  193 ASP C CA  
5255  C C   . ASP C  193 ? 0.9203 1.0248 0.7903 0.0333  0.0416  0.0291  193 ASP C C   
5256  O O   . ASP C  193 ? 0.7177 0.8203 0.5952 0.0379  0.0397  0.0320  193 ASP C O   
5257  C CB  . ASP C  193 ? 1.1211 1.2422 0.9794 0.0282  0.0358  0.0273  193 ASP C CB  
5258  C CG  . ASP C  193 ? 1.3281 1.4612 1.1819 0.0293  0.0315  0.0309  193 ASP C CG  
5259  O OD1 . ASP C  193 ? 1.4722 1.6117 1.3192 0.0288  0.0321  0.0338  193 ASP C OD1 
5260  O OD2 . ASP C  193 ? 1.5987 1.7350 1.4557 0.0305  0.0277  0.0310  193 ASP C OD2 
5261  N N   . GLN C  194 ? 0.9105 1.0075 0.7809 0.0301  0.0456  0.0249  194 GLN C N   
5262  C CA  . GLN C  194 ? 0.9976 1.0838 0.8776 0.0319  0.0477  0.0237  194 GLN C CA  
5263  C C   . GLN C  194 ? 1.1266 1.2088 1.0112 0.0365  0.0497  0.0280  194 GLN C C   
5264  O O   . GLN C  194 ? 1.0953 1.1739 0.9884 0.0405  0.0482  0.0300  194 GLN C O   
5265  C CB  . GLN C  194 ? 0.9676 1.0471 0.8465 0.0273  0.0521  0.0186  194 GLN C CB  
5266  C CG  . GLN C  194 ? 0.9603 1.0287 0.8489 0.0291  0.0551  0.0178  194 GLN C CG  
5267  C CD  . GLN C  194 ? 0.9787 1.0439 0.8761 0.0308  0.0519  0.0170  194 GLN C CD  
5268  O OE1 . GLN C  194 ? 1.0630 1.1205 0.9692 0.0331  0.0532  0.0174  194 GLN C OE1 
5269  N NE2 . GLN C  194 ? 0.8018 0.8731 0.6968 0.0297  0.0477  0.0160  194 GLN C NE2 
5270  N N   . GLN C  195 ? 1.3409 1.4237 1.2199 0.0357  0.0532  0.0293  195 GLN C N   
5271  C CA  . GLN C  195 ? 1.4756 1.5546 1.3583 0.0398  0.0556  0.0334  195 GLN C CA  
5272  C C   . GLN C  195 ? 1.3408 1.4265 1.2243 0.0444  0.0520  0.0389  195 GLN C C   
5273  O O   . GLN C  195 ? 1.3174 1.3995 1.2069 0.0488  0.0529  0.0424  195 GLN C O   
5274  C CB  . GLN C  195 ? 1.5021 1.5802 1.3779 0.0374  0.0604  0.0332  195 GLN C CB  
5275  C CG  . GLN C  195 ? 1.7673 1.8554 1.6313 0.0342  0.0593  0.0337  195 GLN C CG  
5276  C CD  . GLN C  195 ? 1.9972 2.0837 1.8539 0.0310  0.0643  0.0326  195 GLN C CD  
5277  O OE1 . GLN C  195 ? 1.9401 2.0342 1.7867 0.0279  0.0641  0.0329  195 GLN C OE1 
5278  N NE2 . GLN C  195 ? 2.0160 2.0926 1.8778 0.0314  0.0690  0.0314  195 GLN C NE2 
5279  N N   . SER C  196 ? 0.9966 1.0920 0.8744 0.0434  0.0482  0.0396  196 SER C N   
5280  C CA  . SER C  196 ? 0.9735 1.0758 0.8523 0.0477  0.0447  0.0448  196 SER C CA  
5281  C C   . SER C  196 ? 1.1589 1.2572 1.0476 0.0512  0.0422  0.0452  196 SER C C   
5282  O O   . SER C  196 ? 1.2431 1.3420 1.1363 0.0559  0.0413  0.0496  196 SER C O   
5283  C CB  . SER C  196 ? 0.9635 1.0772 0.8343 0.0453  0.0411  0.0452  196 SER C CB  
5284  O OG  . SER C  196 ? 1.1477 1.2678 1.0207 0.0496  0.0376  0.0500  196 SER C OG  
5285  N N   . LEU C  197 ? 1.1073 1.2013 0.9992 0.0489  0.0413  0.0407  197 LEU C N   
5286  C CA  . LEU C  197 ? 0.9804 1.0709 0.8810 0.0515  0.0386  0.0405  197 LEU C CA  
5287  C C   . LEU C  197 ? 0.9590 1.0388 0.8684 0.0532  0.0413  0.0398  197 LEU C C   
5288  O O   . LEU C  197 ? 0.9372 1.0143 0.8538 0.0571  0.0402  0.0421  197 LEU C O   
5289  C CB  . LEU C  197 ? 1.0642 1.1568 0.9637 0.0482  0.0356  0.0364  197 LEU C CB  
5290  C CG  . LEU C  197 ? 0.9332 1.0364 0.8273 0.0477  0.0316  0.0376  197 LEU C CG  
5291  C CD1 . LEU C  197 ? 0.8770 0.9818 0.7686 0.0434  0.0296  0.0328  197 LEU C CD1 
5292  C CD2 . LEU C  197 ? 0.8830 0.9884 0.7826 0.0526  0.0286  0.0416  197 LEU C CD2 
5293  N N   . TYR C  198 ? 0.8694 0.9432 0.7785 0.0503  0.0450  0.0366  198 TYR C N   
5294  C CA  . TYR C  198 ? 0.9902 1.0540 0.9082 0.0517  0.0475  0.0358  198 TYR C CA  
5295  C C   . TYR C  198 ? 1.1630 1.2223 1.0811 0.0527  0.0523  0.0375  198 TYR C C   
5296  O O   . TYR C  198 ? 1.2060 1.2584 1.1319 0.0552  0.0541  0.0385  198 TYR C O   
5297  C CB  . TYR C  198 ? 1.1431 1.2019 1.0635 0.0480  0.0479  0.0308  198 TYR C CB  
5298  C CG  . TYR C  198 ? 1.0234 1.0869 0.9427 0.0465  0.0434  0.0289  198 TYR C CG  
5299  C CD1 . TYR C  198 ? 0.9381 1.0055 0.8505 0.0421  0.0431  0.0254  198 TYR C CD1 
5300  C CD2 . TYR C  198 ? 0.9239 0.9881 0.8489 0.0495  0.0396  0.0304  198 TYR C CD2 
5301  C CE1 . TYR C  198 ? 0.9899 1.0615 0.9013 0.0407  0.0391  0.0237  198 TYR C CE1 
5302  C CE2 . TYR C  198 ? 0.9171 0.9855 0.8409 0.0481  0.0356  0.0287  198 TYR C CE2 
5303  C CZ  . TYR C  198 ? 0.9620 1.0341 0.8791 0.0438  0.0354  0.0254  198 TYR C CZ  
5304  O OH  . TYR C  198 ? 0.9617 1.0378 0.8777 0.0424  0.0316  0.0237  198 TYR C OH  
5305  N N   . GLN C  199 ? 1.1847 1.2483 1.0938 0.0507  0.0544  0.0380  199 GLN C N   
5306  C CA  . GLN C  199 ? 1.2751 1.3353 1.1830 0.0514  0.0591  0.0397  199 GLN C CA  
5307  C C   . GLN C  199 ? 1.2408 1.2928 1.1502 0.0483  0.0637  0.0359  199 GLN C C   
5308  O O   . GLN C  199 ? 1.3517 1.4006 1.2592 0.0482  0.0681  0.0367  199 GLN C O   
5309  C CB  . GLN C  199 ? 1.4033 1.4584 1.3199 0.0564  0.0599  0.0432  199 GLN C CB  
5310  C CG  . GLN C  199 ? 1.4770 1.5249 1.3957 0.0567  0.0653  0.0436  199 GLN C CG  
5311  C CD  . GLN C  199 ? 1.4887 1.5408 1.3995 0.0571  0.0677  0.0468  199 GLN C CD  
5312  O OE1 . GLN C  199 ? 1.5436 1.5912 1.4530 0.0561  0.0723  0.0465  199 GLN C OE1 
5313  N NE2 . GLN C  199 ? 1.3417 1.4027 1.2472 0.0585  0.0645  0.0501  199 GLN C NE2 
5314  N N   . ASN C  200 ? 1.2300 1.2785 1.1431 0.0460  0.0629  0.0318  200 ASN C N   
5315  C CA  . ASN C  200 ? 1.2773 1.3180 1.1928 0.0429  0.0672  0.0280  200 ASN C CA  
5316  C C   . ASN C  200 ? 1.3124 1.3574 1.2201 0.0379  0.0667  0.0240  200 ASN C C   
5317  O O   . ASN C  200 ? 1.3077 1.3603 1.2107 0.0374  0.0625  0.0243  200 ASN C O   
5318  C CB  . ASN C  200 ? 1.2576 1.2903 1.1847 0.0443  0.0671  0.0268  200 ASN C CB  
5319  C CG  . ASN C  200 ? 1.1833 1.2144 1.1181 0.0494  0.0654  0.0308  200 ASN C CG  
5320  O OD1 . ASN C  200 ? 1.3634 1.4003 1.2970 0.0519  0.0616  0.0335  200 ASN C OD1 
5321  N ND2 . ASN C  200 ? 1.0613 1.0845 1.0042 0.0510  0.0685  0.0312  200 ASN C ND2 
5322  N N   . ALA C  201 ? 1.2165 1.2564 1.1227 0.0340  0.0711  0.0202  201 ALA C N   
5323  C CA  . ALA C  201 ? 1.1492 1.1925 1.0479 0.0288  0.0712  0.0160  201 ALA C CA  
5324  C C   . ALA C  201 ? 1.3264 1.3644 1.2315 0.0270  0.0711  0.0121  201 ALA C C   
5325  O O   . ALA C  201 ? 1.3331 1.3751 1.2373 0.0258  0.0673  0.0106  201 ALA C O   
5326  C CB  . ALA C  201 ? 1.2076 1.2500 1.0982 0.0251  0.0765  0.0142  201 ALA C CB  
5327  N N   . ASP C  202 ? 1.3738 1.4028 1.2857 0.0268  0.0755  0.0107  202 ASP C N   
5328  C CA  . ASP C  202 ? 1.3432 1.3664 1.2622 0.0252  0.0759  0.0075  202 ASP C CA  
5329  C C   . ASP C  202 ? 1.2221 1.2428 1.1519 0.0295  0.0722  0.0099  202 ASP C C   
5330  O O   . ASP C  202 ? 1.2364 1.2510 1.1741 0.0321  0.0742  0.0117  202 ASP C O   
5331  C CB  . ASP C  202 ? 1.4032 1.4180 1.3250 0.0230  0.0826  0.0051  202 ASP C CB  
5332  C CG  . ASP C  202 ? 1.6104 1.6208 1.5359 0.0198  0.0840  0.0009  202 ASP C CG  
5333  O OD1 . ASP C  202 ? 1.6540 1.6691 1.5742 0.0169  0.0817  -0.0016 202 ASP C OD1 
5334  O OD2 . ASP C  202 ? 1.6510 1.6534 1.5853 0.0202  0.0874  0.0002  202 ASP C OD2 
5335  N N   . THR C  203 ? 1.1162 1.1416 1.0462 0.0299  0.0669  0.0100  203 THR C N   
5336  C CA  . THR C  203 ? 1.0249 1.0488 0.9639 0.0336  0.0629  0.0122  203 THR C CA  
5337  C C   . THR C  203 ? 0.8658 0.8870 0.8104 0.0320  0.0612  0.0096  203 THR C C   
5338  O O   . THR C  203 ? 0.9426 0.9636 0.8836 0.0281  0.0628  0.0060  203 THR C O   
5339  C CB  . THR C  203 ? 0.9928 1.0245 0.9284 0.0363  0.0579  0.0153  203 THR C CB  
5340  O OG1 . THR C  203 ? 0.8958 0.9341 0.8242 0.0335  0.0551  0.0132  203 THR C OG1 
5341  C CG2 . THR C  203 ? 0.9877 1.0224 0.9183 0.0383  0.0594  0.0185  203 THR C CG2 
5342  N N   . TYR C  204 ? 0.8453 0.8644 0.7985 0.0349  0.0580  0.0113  204 TYR C N   
5343  C CA  . TYR C  204 ? 0.8864 0.9031 0.8452 0.0337  0.0558  0.0094  204 TYR C CA  
5344  C C   . TYR C  204 ? 0.8887 0.9068 0.8529 0.0369  0.0505  0.0118  204 TYR C C   
5345  O O   . TYR C  204 ? 0.8376 0.8559 0.8045 0.0404  0.0496  0.0149  204 TYR C O   
5346  C CB  . TYR C  204 ? 0.8592 0.8674 0.8260 0.0327  0.0599  0.0081  204 TYR C CB  
5347  C CG  . TYR C  204 ? 0.9414 0.9447 0.9181 0.0363  0.0602  0.0110  204 TYR C CG  
5348  C CD1 . TYR C  204 ? 0.8959 0.8971 0.8812 0.0379  0.0567  0.0120  204 TYR C CD1 
5349  C CD2 . TYR C  204 ? 0.9826 0.9833 0.9596 0.0379  0.0639  0.0127  204 TYR C CD2 
5350  C CE1 . TYR C  204 ? 1.0109 1.0079 1.0052 0.0408  0.0568  0.0145  204 TYR C CE1 
5351  C CE2 . TYR C  204 ? 1.0146 1.0107 1.0007 0.0410  0.0643  0.0153  204 TYR C CE2 
5352  C CZ  . TYR C  204 ? 1.1319 1.1263 1.1266 0.0424  0.0607  0.0161  204 TYR C CZ  
5353  O OH  . TYR C  204 ? 1.1429 1.1330 1.1466 0.0452  0.0609  0.0185  204 TYR C OH  
5354  N N   . VAL C  205 ? 0.7998 0.8190 0.7657 0.0356  0.0472  0.0102  205 VAL C N   
5355  C CA  . VAL C  205 ? 0.7251 0.7451 0.6963 0.0381  0.0423  0.0120  205 VAL C CA  
5356  C C   . VAL C  205 ? 0.6834 0.6981 0.6628 0.0370  0.0418  0.0107  205 VAL C C   
5357  O O   . VAL C  205 ? 0.7529 0.7663 0.7312 0.0338  0.0434  0.0079  205 VAL C O   
5358  C CB  . VAL C  205 ? 0.6202 0.6478 0.5848 0.0378  0.0379  0.0118  205 VAL C CB  
5359  C CG1 . VAL C  205 ? 0.6308 0.6589 0.6007 0.0403  0.0332  0.0137  205 VAL C CG1 
5360  C CG2 . VAL C  205 ? 0.7261 0.7596 0.6822 0.0385  0.0385  0.0132  205 VAL C CG2 
5361  N N   . PHE C  206 ? 0.6403 0.6520 0.6281 0.0394  0.0398  0.0128  206 PHE C N   
5362  C CA  . PHE C  206 ? 0.6871 0.6944 0.6831 0.0385  0.0387  0.0121  206 PHE C CA  
5363  C C   . PHE C  206 ? 0.7233 0.7320 0.7235 0.0403  0.0334  0.0137  206 PHE C C   
5364  O O   . PHE C  206 ? 0.7406 0.7491 0.7438 0.0431  0.0322  0.0161  206 PHE C O   
5365  C CB  . PHE C  206 ? 0.7298 0.7302 0.7340 0.0390  0.0428  0.0127  206 PHE C CB  
5366  C CG  . PHE C  206 ? 0.8042 0.8004 0.8180 0.0387  0.0413  0.0129  206 PHE C CG  
5367  C CD1 . PHE C  206 ? 0.8428 0.8374 0.8643 0.0411  0.0386  0.0154  206 PHE C CD1 
5368  C CD2 . PHE C  206 ? 0.8271 0.8212 0.8424 0.0358  0.0427  0.0107  206 PHE C CD2 
5369  C CE1 . PHE C  206 ? 0.8056 0.7970 0.8358 0.0406  0.0370  0.0159  206 PHE C CE1 
5370  C CE2 . PHE C  206 ? 0.7898 0.7805 0.8142 0.0356  0.0412  0.0114  206 PHE C CE2 
5371  C CZ  . PHE C  206 ? 0.8997 0.8893 0.9316 0.0380  0.0382  0.0140  206 PHE C CZ  
5372  N N   . VAL C  207 ? 0.7081 0.7179 0.7083 0.0385  0.0305  0.0122  207 VAL C N   
5373  C CA  . VAL C  207 ? 0.6661 0.6770 0.6699 0.0396  0.0255  0.0134  207 VAL C CA  
5374  C C   . VAL C  207 ? 0.7087 0.7153 0.7207 0.0383  0.0248  0.0130  207 VAL C C   
5375  O O   . VAL C  207 ? 0.7523 0.7580 0.7636 0.0358  0.0260  0.0110  207 VAL C O   
5376  C CB  . VAL C  207 ? 0.4804 0.4976 0.4767 0.0388  0.0220  0.0123  207 VAL C CB  
5377  C CG1 . VAL C  207 ? 0.4729 0.4909 0.4727 0.0398  0.0171  0.0134  207 VAL C CG1 
5378  C CG2 . VAL C  207 ? 0.6506 0.6727 0.6390 0.0400  0.0226  0.0129  207 VAL C CG2 
5379  N N   . GLY C  208 ? 0.7156 0.7195 0.7353 0.0401  0.0228  0.0152  208 GLY C N   
5380  C CA  . GLY C  208 ? 0.7208 0.7209 0.7491 0.0390  0.0220  0.0155  208 GLY C CA  
5381  C C   . GLY C  208 ? 0.6947 0.6950 0.7281 0.0401  0.0172  0.0172  208 GLY C C   
5382  O O   . GLY C  208 ? 0.7304 0.7316 0.7641 0.0423  0.0158  0.0188  208 GLY C O   
5383  N N   . SER C  209 ? 0.7714 0.7708 0.8086 0.0385  0.0148  0.0170  209 SER C N   
5384  C CA  . SER C  209 ? 0.7565 0.7557 0.7995 0.0390  0.0104  0.0187  209 SER C CA  
5385  C C   . SER C  209 ? 0.7994 0.7946 0.8514 0.0377  0.0108  0.0195  209 SER C C   
5386  O O   . SER C  209 ? 0.7908 0.7830 0.8456 0.0371  0.0150  0.0191  209 SER C O   
5387  C CB  . SER C  209 ? 0.6676 0.6710 0.7048 0.0381  0.0059  0.0177  209 SER C CB  
5388  O OG  . SER C  209 ? 0.8247 0.8285 0.8603 0.0357  0.0057  0.0161  209 SER C OG  
5389  N N   . SER C  210 ? 0.9442 0.9397 1.0009 0.0373  0.0065  0.0208  210 SER C N   
5390  C CA  . SER C  210 ? 0.9004 0.8928 0.9660 0.0361  0.0064  0.0221  210 SER C CA  
5391  C C   . SER C  210 ? 1.0133 1.0054 1.0766 0.0340  0.0081  0.0203  210 SER C C   
5392  O O   . SER C  210 ? 0.8537 0.8426 0.9239 0.0332  0.0103  0.0210  210 SER C O   
5393  C CB  . SER C  210 ? 0.9838 0.9772 1.0536 0.0358  0.0010  0.0238  210 SER C CB  
5394  O OG  . SER C  210 ? 1.2346 1.2274 1.3080 0.0374  -0.0001 0.0254  210 SER C OG  
5395  N N   . ARG C  211 ? 0.9498 0.9454 1.0038 0.0331  0.0072  0.0181  211 ARG C N   
5396  C CA  . ARG C  211 ? 1.0857 1.0814 1.1365 0.0309  0.0087  0.0161  211 ARG C CA  
5397  C C   . ARG C  211 ? 1.0536 1.0502 1.0969 0.0305  0.0131  0.0136  211 ARG C C   
5398  O O   . ARG C  211 ? 1.2313 1.2251 1.2760 0.0293  0.0175  0.0125  211 ARG C O   
5399  C CB  . ARG C  211 ? 1.2472 1.2467 1.2930 0.0297  0.0041  0.0153  211 ARG C CB  
5400  C CG  . ARG C  211 ? 1.3214 1.3216 1.3713 0.0303  -0.0011 0.0174  211 ARG C CG  
5401  C CD  . ARG C  211 ? 1.5228 1.5274 1.5654 0.0296  -0.0053 0.0163  211 ARG C CD  
5402  N NE  . ARG C  211 ? 1.7033 1.7084 1.7446 0.0273  -0.0064 0.0153  211 ARG C NE  
5403  C CZ  . ARG C  211 ? 1.5427 1.5513 1.5765 0.0263  -0.0086 0.0135  211 ARG C CZ  
5404  N NH1 . ARG C  211 ? 1.3291 1.3412 1.3562 0.0273  -0.0099 0.0127  211 ARG C NH1 
5405  N NH2 . ARG C  211 ? 1.4347 1.4434 1.4680 0.0242  -0.0093 0.0127  211 ARG C NH2 
5406  N N   . TYR C  212 ? 1.0504 1.0508 1.0858 0.0314  0.0119  0.0128  212 TYR C N   
5407  C CA  . TYR C  212 ? 0.8268 0.8293 0.8538 0.0308  0.0151  0.0105  212 TYR C CA  
5408  C C   . TYR C  212 ? 0.7946 0.7943 0.8231 0.0319  0.0199  0.0109  212 TYR C C   
5409  O O   . TYR C  212 ? 0.8878 0.8863 0.9203 0.0342  0.0196  0.0130  212 TYR C O   
5410  C CB  . TYR C  212 ? 0.6644 0.6726 0.6829 0.0315  0.0119  0.0099  212 TYR C CB  
5411  C CG  . TYR C  212 ? 0.7639 0.7753 0.7733 0.0307  0.0146  0.0078  212 TYR C CG  
5412  C CD1 . TYR C  212 ? 0.6761 0.6914 0.6785 0.0286  0.0135  0.0055  212 TYR C CD1 
5413  C CD2 . TYR C  212 ? 0.7697 0.7805 0.7774 0.0319  0.0181  0.0082  212 TYR C CD2 
5414  C CE1 . TYR C  212 ? 0.6815 0.7002 0.6755 0.0276  0.0157  0.0037  212 TYR C CE1 
5415  C CE2 . TYR C  212 ? 0.7688 0.7830 0.7680 0.0310  0.0203  0.0065  212 TYR C CE2 
5416  C CZ  . TYR C  212 ? 0.7538 0.7721 0.7462 0.0288  0.0191  0.0042  212 TYR C CZ  
5417  O OH  . TYR C  212 ? 0.6846 0.7067 0.6687 0.0277  0.0212  0.0026  212 TYR C OH  
5418  N N   . SER C  213 ? 0.7001 0.6987 0.7254 0.0302  0.0244  0.0088  213 SER C N   
5419  C CA  . SER C  213 ? 0.7695 0.7655 0.7951 0.0309  0.0293  0.0089  213 SER C CA  
5420  C C   . SER C  213 ? 0.7737 0.7710 0.7910 0.0287  0.0334  0.0059  213 SER C C   
5421  O O   . SER C  213 ? 0.9295 0.9248 0.9471 0.0262  0.0358  0.0039  213 SER C O   
5422  C CB  . SER C  213 ? 0.7152 0.7051 0.7515 0.0313  0.0322  0.0103  213 SER C CB  
5423  O OG  . SER C  213 ? 0.6509 0.6382 0.6875 0.0320  0.0371  0.0103  213 SER C OG  
5424  N N   . LYS C  214 ? 0.7552 0.7557 0.7652 0.0296  0.0341  0.0058  214 LYS C N   
5425  C CA  . LYS C  214 ? 0.7357 0.7379 0.7373 0.0273  0.0379  0.0031  214 LYS C CA  
5426  C C   . LYS C  214 ? 0.8923 0.8961 0.8890 0.0288  0.0402  0.0039  214 LYS C C   
5427  O O   . LYS C  214 ? 0.7338 0.7403 0.7296 0.0314  0.0374  0.0061  214 LYS C O   
5428  C CB  . LYS C  214 ? 0.7008 0.7085 0.6945 0.0252  0.0352  0.0009  214 LYS C CB  
5429  C CG  . LYS C  214 ? 0.8497 0.8590 0.8349 0.0222  0.0391  -0.0022 214 LYS C CG  
5430  C CD  . LYS C  214 ? 1.1296 1.1403 1.1120 0.0190  0.0384  -0.0051 214 LYS C CD  
5431  C CE  . LYS C  214 ? 1.1636 1.1819 1.1367 0.0182  0.0349  -0.0061 214 LYS C CE  
5432  N NZ  . LYS C  214 ? 1.0879 1.1098 1.0519 0.0167  0.0377  -0.0077 214 LYS C NZ  
5433  N N   . LYS C  215 ? 0.8562 0.8581 0.8497 0.0269  0.0454  0.0020  215 LYS C N   
5434  C CA  . LYS C  215 ? 0.6994 0.7026 0.6875 0.0278  0.0481  0.0026  215 LYS C CA  
5435  C C   . LYS C  215 ? 0.7097 0.7186 0.6862 0.0252  0.0485  0.0002  215 LYS C C   
5436  O O   . LYS C  215 ? 0.8386 0.8471 0.8121 0.0218  0.0507  -0.0029 215 LYS C O   
5437  C CB  . LYS C  215 ? 0.8912 0.8879 0.8840 0.0274  0.0541  0.0024  215 LYS C CB  
5438  C CG  . LYS C  215 ? 0.9131 0.9104 0.9014 0.0286  0.0571  0.0034  215 LYS C CG  
5439  C CD  . LYS C  215 ? 1.0298 1.0200 1.0238 0.0283  0.0630  0.0032  215 LYS C CD  
5440  C CE  . LYS C  215 ? 1.1539 1.1441 1.1453 0.0301  0.0656  0.0049  215 LYS C CE  
5441  N NZ  . LYS C  215 ? 0.9913 0.9741 0.9895 0.0303  0.0711  0.0051  215 LYS C NZ  
5442  N N   . PHE C  216 ? 0.7679 0.7823 0.7381 0.0269  0.0466  0.0017  216 PHE C N   
5443  C CA  . PHE C  216 ? 0.7533 0.7743 0.7126 0.0247  0.0462  0.0000  216 PHE C CA  
5444  C C   . PHE C  216 ? 0.8268 0.8487 0.7799 0.0241  0.0503  0.0000  216 PHE C C   
5445  O O   . PHE C  216 ? 0.7825 0.8031 0.7375 0.0269  0.0512  0.0027  216 PHE C O   
5446  C CB  . PHE C  216 ? 0.7900 0.8179 0.7460 0.0267  0.0406  0.0018  216 PHE C CB  
5447  C CG  . PHE C  216 ? 0.8397 0.8672 0.8009 0.0272  0.0363  0.0019  216 PHE C CG  
5448  C CD1 . PHE C  216 ? 0.8083 0.8327 0.7777 0.0303  0.0340  0.0045  216 PHE C CD1 
5449  C CD2 . PHE C  216 ? 0.7449 0.7753 0.7026 0.0244  0.0346  -0.0007 216 PHE C CD2 
5450  C CE1 . PHE C  216 ? 0.8093 0.8335 0.7830 0.0305  0.0301  0.0045  216 PHE C CE1 
5451  C CE2 . PHE C  216 ? 0.8564 0.8864 0.8185 0.0247  0.0307  -0.0006 216 PHE C CE2 
5452  C CZ  . PHE C  216 ? 0.7899 0.8169 0.7599 0.0277  0.0284  0.0021  216 PHE C CZ  
5453  N N   . LYS C  217 ? 0.8786 0.9024 0.8241 0.0202  0.0530  -0.0032 217 LYS C N   
5454  C CA  . LYS C  217 ? 0.8078 0.8335 0.7455 0.0189  0.0566  -0.0035 217 LYS C CA  
5455  C C   . LYS C  217 ? 0.8498 0.8848 0.7772 0.0175  0.0537  -0.0039 217 LYS C C   
5456  O O   . LYS C  217 ? 0.8505 0.8885 0.7737 0.0143  0.0527  -0.0069 217 LYS C O   
5457  C CB  . LYS C  217 ? 0.9724 0.9927 0.9094 0.0151  0.0627  -0.0070 217 LYS C CB  
5458  C CG  . LYS C  217 ? 0.9845 0.9973 0.9280 0.0167  0.0674  -0.0059 217 LYS C CG  
5459  C CD  . LYS C  217 ? 1.0320 1.0474 0.9707 0.0186  0.0684  -0.0033 217 LYS C CD  
5460  C CE  . LYS C  217 ? 1.2789 1.2867 1.2239 0.0199  0.0734  -0.0023 217 LYS C CE  
5461  N NZ  . LYS C  217 ? 1.3335 1.3436 1.2736 0.0217  0.0747  0.0002  217 LYS C NZ  
5462  N N   . PRO C  218 ? 0.9480 0.9877 0.8713 0.0200  0.0524  -0.0008 218 PRO C N   
5463  C CA  . PRO C  218 ? 0.9542 1.0034 0.8681 0.0191  0.0495  -0.0004 218 PRO C CA  
5464  C C   . PRO C  218 ? 0.9291 0.9808 0.8339 0.0139  0.0526  -0.0042 218 PRO C C   
5465  O O   . PRO C  218 ? 0.8991 0.9474 0.8016 0.0122  0.0575  -0.0053 218 PRO C O   
5466  C CB  . PRO C  218 ? 0.8420 0.8936 0.7545 0.0227  0.0495  0.0037  218 PRO C CB  
5467  C CG  . PRO C  218 ? 0.9350 0.9794 0.8578 0.0264  0.0500  0.0060  218 PRO C CG  
5468  C CD  . PRO C  218 ? 0.8742 0.9107 0.8024 0.0240  0.0535  0.0028  218 PRO C CD  
5469  N N   . GLU C  219 ? 1.0216 1.0791 0.9214 0.0113  0.0498  -0.0063 219 GLU C N   
5470  C CA  . GLU C  219 ? 0.8900 0.9507 0.7807 0.0060  0.0523  -0.0101 219 GLU C CA  
5471  C C   . GLU C  219 ? 0.8261 0.8967 0.7074 0.0057  0.0502  -0.0082 219 GLU C C   
5472  O O   . GLU C  219 ? 0.8472 0.9251 0.7258 0.0061  0.0455  -0.0075 219 GLU C O   
5473  C CB  . GLU C  219 ? 0.8465 0.9075 0.7375 0.0029  0.0509  -0.0138 219 GLU C CB  
5474  C CG  . GLU C  219 ? 0.9944 1.0462 0.8952 0.0033  0.0526  -0.0151 219 GLU C CG  
5475  C CD  . GLU C  219 ? 1.0904 1.1426 0.9914 0.0003  0.0512  -0.0185 219 GLU C CD  
5476  O OE1 . GLU C  219 ? 1.0449 1.1047 0.9390 -0.0017 0.0485  -0.0196 219 GLU C OE1 
5477  O OE2 . GLU C  219 ? 0.9909 1.0359 0.8993 0.0001  0.0530  -0.0198 219 GLU C OE2 
5478  N N   . ILE C  220 ? 0.9967 1.0676 0.8730 0.0052  0.0535  -0.0074 220 ILE C N   
5479  C CA  . ILE C  220 ? 0.9146 0.9950 0.7824 0.0053  0.0516  -0.0048 220 ILE C CA  
5480  C C   . ILE C  220 ? 0.8476 0.9340 0.7048 -0.0006 0.0525  -0.0084 220 ILE C C   
5481  O O   . ILE C  220 ? 0.9271 1.0097 0.7805 -0.0046 0.0575  -0.0119 220 ILE C O   
5482  C CB  . ILE C  220 ? 0.8463 0.9246 0.7135 0.0077  0.0544  -0.0016 220 ILE C CB  
5483  C CG1 . ILE C  220 ? 0.8303 0.9032 0.7080 0.0135  0.0533  0.0021  220 ILE C CG1 
5484  C CG2 . ILE C  220 ? 0.9465 1.0350 0.8049 0.0078  0.0524  0.0014  220 ILE C CG2 
5485  C CD1 . ILE C  220 ? 1.0874 1.1556 0.9665 0.0157  0.0572  0.0046  220 ILE C CD1 
5486  N N   . ALA C  221 ? 0.7659 0.8620 0.6184 -0.0011 0.0479  -0.0077 221 ALA C N   
5487  C CA  . ALA C  221 ? 0.7948 0.8979 0.6371 -0.0068 0.0481  -0.0110 221 ALA C CA  
5488  C C   . ALA C  221 ? 0.9401 1.0548 0.7781 -0.0060 0.0423  -0.0085 221 ALA C C   
5489  O O   . ALA C  221 ? 0.9759 1.0927 0.8191 -0.0010 0.0384  -0.0044 221 ALA C O   
5490  C CB  . ALA C  221 ? 0.8104 0.9084 0.6534 -0.0113 0.0505  -0.0168 221 ALA C CB  
5491  N N   . ILE C  222 ? 0.9879 1.1102 0.8166 -0.0110 0.0420  -0.0110 222 ILE C N   
5492  C CA  . ILE C  222 ? 1.0099 1.1439 0.8345 -0.0107 0.0367  -0.0088 222 ILE C CA  
5493  C C   . ILE C  222 ? 0.9586 1.0943 0.7840 -0.0134 0.0343  -0.0125 222 ILE C C   
5494  O O   . ILE C  222 ? 0.9385 1.0737 0.7590 -0.0191 0.0367  -0.0176 222 ILE C O   
5495  C CB  . ILE C  222 ? 1.1696 1.3130 0.9829 -0.0144 0.0369  -0.0083 222 ILE C CB  
5496  C CG1 . ILE C  222 ? 1.0731 1.2154 0.8853 -0.0116 0.0391  -0.0042 222 ILE C CG1 
5497  C CG2 . ILE C  222 ? 1.0199 1.1758 0.8297 -0.0141 0.0313  -0.0059 222 ILE C CG2 
5498  C CD1 . ILE C  222 ? 1.1580 1.3020 0.9768 -0.0045 0.0356  0.0022  222 ILE C CD1 
5499  N N   . ARG C  223 ? 0.9152 1.0528 0.7467 -0.0094 0.0299  -0.0100 223 ARG C N   
5500  C CA  . ARG C  223 ? 1.0058 1.1456 0.8382 -0.0114 0.0272  -0.0130 223 ARG C CA  
5501  C C   . ARG C  223 ? 0.9911 1.1436 0.8183 -0.0117 0.0224  -0.0108 223 ARG C C   
5502  O O   . ARG C  223 ? 1.0336 1.1921 0.8604 -0.0081 0.0201  -0.0058 223 ARG C O   
5503  C CB  . ARG C  223 ? 0.8914 1.0243 0.7341 -0.0072 0.0255  -0.0121 223 ARG C CB  
5504  C CG  . ARG C  223 ? 0.8082 0.9288 0.6575 -0.0065 0.0296  -0.0138 223 ARG C CG  
5505  C CD  . ARG C  223 ? 0.7226 0.8394 0.5749 -0.0024 0.0313  -0.0098 223 ARG C CD  
5506  N NE  . ARG C  223 ? 0.8208 0.9263 0.6819 -0.0003 0.0338  -0.0103 223 ARG C NE  
5507  C CZ  . ARG C  223 ? 0.7895 0.8891 0.6544 0.0024  0.0366  -0.0082 223 ARG C CZ  
5508  N NH1 . ARG C  223 ? 0.9014 1.0046 0.7617 0.0035  0.0375  -0.0053 223 ARG C NH1 
5509  N NH2 . ARG C  223 ? 0.8255 0.9154 0.6988 0.0040  0.0384  -0.0088 223 ARG C NH2 
5510  N N   . PRO C  224 ? 0.9012 1.0581 0.7250 -0.0159 0.0210  -0.0146 224 PRO C N   
5511  C CA  . PRO C  224 ? 0.8989 1.0681 0.7185 -0.0165 0.0164  -0.0129 224 PRO C CA  
5512  C C   . PRO C  224 ? 1.0085 1.1805 0.8345 -0.0101 0.0120  -0.0075 224 PRO C C   
5513  O O   . PRO C  224 ? 1.0193 1.1848 0.8531 -0.0071 0.0112  -0.0075 224 PRO C O   
5514  C CB  . PRO C  224 ? 0.8998 1.0687 0.7189 -0.0209 0.0161  -0.0182 224 PRO C CB  
5515  C CG  . PRO C  224 ? 0.9855 1.1447 0.8038 -0.0247 0.0215  -0.0231 224 PRO C CG  
5516  C CD  . PRO C  224 ? 0.9739 1.1240 0.7982 -0.0204 0.0240  -0.0206 224 PRO C CD  
5517  N N   . LYS C  225 ? 1.1034 1.2853 0.9262 -0.0082 0.0094  -0.0029 225 LYS C N   
5518  C CA  . LYS C  225 ? 1.0212 1.2058 0.8499 -0.0020 0.0058  0.0027  225 LYS C CA  
5519  C C   . LYS C  225 ? 1.0173 1.2022 0.8513 -0.0007 0.0025  0.0018  225 LYS C C   
5520  O O   . LYS C  225 ? 1.0038 1.1955 0.8343 -0.0040 0.0004  -0.0003 225 LYS C O   
5521  C CB  . LYS C  225 ? 1.2060 1.4025 1.0297 -0.0009 0.0034  0.0076  225 LYS C CB  
5522  C CG  . LYS C  225 ? 1.4827 1.6785 1.3029 -0.0003 0.0063  0.0101  225 LYS C CG  
5523  C CD  . LYS C  225 ? 1.6201 1.8282 1.4356 0.0009  0.0036  0.0154  225 LYS C CD  
5524  C CE  . LYS C  225 ? 1.7862 1.9933 1.5980 0.0014  0.0066  0.0180  225 LYS C CE  
5525  N NZ  . LYS C  225 ? 1.7839 1.9811 1.6034 0.0069  0.0086  0.0206  225 LYS C NZ  
5526  N N   . VAL C  226 ? 0.9381 1.1154 0.7805 0.0040  0.0022  0.0035  226 VAL C N   
5527  C CA  . VAL C  226 ? 0.9679 1.1457 0.8158 0.0062  -0.0011 0.0038  226 VAL C CA  
5528  C C   . VAL C  226 ? 0.9614 1.1399 0.8147 0.0126  -0.0030 0.0096  226 VAL C C   
5529  O O   . VAL C  226 ? 0.9418 1.1123 0.8003 0.0159  -0.0011 0.0111  226 VAL C O   
5530  C CB  . VAL C  226 ? 0.9530 1.1199 0.8061 0.0054  0.0003  -0.0003 226 VAL C CB  
5531  C CG1 . VAL C  226 ? 0.7691 0.9367 0.6274 0.0076  -0.0032 0.0002  226 VAL C CG1 
5532  C CG2 . VAL C  226 ? 0.8789 1.0441 0.7270 -0.0008 0.0029  -0.0060 226 VAL C CG2 
5533  N N   . ARG C  227 ? 1.0202 1.2086 0.8727 0.0143  -0.0064 0.0129  227 ARG C N   
5534  C CA  . ARG C  227 ? 0.9635 1.1535 0.8208 0.0203  -0.0078 0.0187  227 ARG C CA  
5535  C C   . ARG C  227 ? 1.0545 1.2442 0.9103 0.0222  -0.0055 0.0222  227 ARG C C   
5536  O O   . ARG C  227 ? 1.0564 1.2409 0.9177 0.0269  -0.0046 0.0255  227 ARG C O   
5537  C CB  . ARG C  227 ? 0.8482 1.0291 0.7141 0.0238  -0.0081 0.0186  227 ARG C CB  
5538  C CG  . ARG C  227 ? 0.8243 1.0061 0.6924 0.0228  -0.0107 0.0161  227 ARG C CG  
5539  C CD  . ARG C  227 ? 0.8638 1.0353 0.7394 0.0254  -0.0105 0.0153  227 ARG C CD  
5540  N NE  . ARG C  227 ? 0.7302 0.9044 0.6100 0.0282  -0.0135 0.0172  227 ARG C NE  
5541  C CZ  . ARG C  227 ? 1.0041 1.1810 0.8873 0.0330  -0.0144 0.0220  227 ARG C CZ  
5542  N NH1 . ARG C  227 ? 1.1146 1.2922 0.9974 0.0354  -0.0128 0.0257  227 ARG C NH1 
5543  N NH2 . ARG C  227 ? 0.9461 1.1250 0.8331 0.0352  -0.0168 0.0232  227 ARG C NH2 
5544  N N   . ASP C  228 ? 1.1098 1.3048 0.9578 0.0184  -0.0043 0.0214  228 ASP C N   
5545  C CA  . ASP C  228 ? 1.2524 1.4488 1.0973 0.0197  -0.0023 0.0250  228 ASP C CA  
5546  C C   . ASP C  228 ? 1.2029 1.3881 1.0494 0.0198  0.0020  0.0233  228 ASP C C   
5547  O O   . ASP C  228 ? 1.3886 1.5742 1.2321 0.0203  0.0041  0.0257  228 ASP C O   
5548  C CB  . ASP C  228 ? 1.6163 1.8177 1.4651 0.0256  -0.0042 0.0318  228 ASP C CB  
5549  C CG  . ASP C  228 ? 1.9501 2.1653 1.7939 0.0248  -0.0071 0.0350  228 ASP C CG  
5550  O OD1 . ASP C  228 ? 2.0130 2.2335 1.8497 0.0223  -0.0062 0.0359  228 ASP C OD1 
5551  O OD2 . ASP C  228 ? 2.0628 2.2836 1.9096 0.0267  -0.0104 0.0368  228 ASP C OD2 
5552  N N   . GLN C  229 ? 1.0334 1.2088 0.8848 0.0193  0.0032  0.0195  229 GLN C N   
5553  C CA  . GLN C  229 ? 1.1156 1.2801 0.9697 0.0195  0.0072  0.0180  229 GLN C CA  
5554  C C   . GLN C  229 ? 1.0292 1.1905 0.8781 0.0136  0.0102  0.0124  229 GLN C C   
5555  O O   . GLN C  229 ? 0.9812 1.1418 0.8297 0.0102  0.0095  0.0081  229 GLN C O   
5556  C CB  . GLN C  229 ? 0.9574 1.1127 0.8208 0.0230  0.0069  0.0177  229 GLN C CB  
5557  C CG  . GLN C  229 ? 0.9301 1.0886 0.7989 0.0283  0.0038  0.0224  229 GLN C CG  
5558  C CD  . GLN C  229 ? 0.9516 1.1132 0.8202 0.0322  0.0045  0.0280  229 GLN C CD  
5559  O OE1 . GLN C  229 ? 1.0196 1.1767 0.8872 0.0323  0.0077  0.0285  229 GLN C OE1 
5560  N NE2 . GLN C  229 ? 1.0730 1.2419 0.9427 0.0355  0.0016  0.0323  229 GLN C NE2 
5561  N N   . GLU C  230 ? 0.9958 1.1552 0.8406 0.0122  0.0137  0.0124  230 GLU C N   
5562  C CA  . GLU C  230 ? 0.9395 1.0944 0.7799 0.0067  0.0175  0.0071  230 GLU C CA  
5563  C C   . GLU C  230 ? 0.9655 1.1075 0.8130 0.0078  0.0208  0.0051  230 GLU C C   
5564  O O   . GLU C  230 ? 1.0543 1.1906 0.9004 0.0038  0.0242  0.0004  230 GLU C O   
5565  C CB  . GLU C  230 ? 1.1959 1.3550 1.0279 0.0042  0.0200  0.0079  230 GLU C CB  
5566  C CG  . GLU C  230 ? 1.2455 1.4179 1.0694 0.0018  0.0169  0.0093  230 GLU C CG  
5567  C CD  . GLU C  230 ? 1.4444 1.6209 1.2595 -0.0012 0.0194  0.0099  230 GLU C CD  
5568  O OE1 . GLU C  230 ? 1.3239 1.5035 1.1314 -0.0073 0.0207  0.0057  230 GLU C OE1 
5569  O OE2 . GLU C  230 ? 1.3124 1.4890 1.1281 0.0024  0.0202  0.0146  230 GLU C OE2 
5570  N N   . GLY C  231 ? 0.8208 0.9583 0.6761 0.0133  0.0200  0.0086  231 GLY C N   
5571  C CA  . GLY C  231 ? 0.8347 0.9607 0.6977 0.0149  0.0224  0.0073  231 GLY C CA  
5572  C C   . GLY C  231 ? 0.8317 0.9549 0.7008 0.0155  0.0197  0.0056  231 GLY C C   
5573  O O   . GLY C  231 ? 0.8116 0.9417 0.6793 0.0155  0.0159  0.0060  231 GLY C O   
5574  N N   . ARG C  232 ? 0.7415 0.8548 0.6174 0.0161  0.0216  0.0038  232 ARG C N   
5575  C CA  . ARG C  232 ? 0.7378 0.8477 0.6195 0.0165  0.0193  0.0021  232 ARG C CA  
5576  C C   . ARG C  232 ? 0.7184 0.8203 0.6095 0.0208  0.0193  0.0042  232 ARG C C   
5577  O O   . ARG C  232 ? 0.6169 0.7138 0.5105 0.0225  0.0222  0.0057  232 ARG C O   
5578  C CB  . ARG C  232 ? 0.7653 0.8713 0.6457 0.0115  0.0214  -0.0032 232 ARG C CB  
5579  C CG  . ARG C  232 ? 0.7628 0.8763 0.6340 0.0066  0.0216  -0.0060 232 ARG C CG  
5580  C CD  . ARG C  232 ? 0.7060 0.8252 0.5762 0.0056  0.0175  -0.0072 232 ARG C CD  
5581  N NE  . ARG C  232 ? 0.7913 0.9190 0.6526 0.0011  0.0172  -0.0093 232 ARG C NE  
5582  C CZ  . ARG C  232 ? 0.8896 1.0269 0.7455 0.0017  0.0151  -0.0065 232 ARG C CZ  
5583  N NH1 . ARG C  232 ? 0.9011 1.0402 0.7597 0.0067  0.0135  -0.0014 232 ARG C NH1 
5584  N NH2 . ARG C  232 ? 0.9466 1.0917 0.7944 -0.0027 0.0148  -0.0086 232 ARG C NH2 
5585  N N   . MET C  233 ? 0.7207 0.8216 0.6169 0.0223  0.0161  0.0043  233 MET C N   
5586  C CA  . MET C  233 ? 0.7363 0.8301 0.6413 0.0259  0.0157  0.0061  233 MET C CA  
5587  C C   . MET C  233 ? 0.7559 0.8451 0.6654 0.0245  0.0144  0.0032  233 MET C C   
5588  O O   . MET C  233 ? 0.6592 0.7526 0.5678 0.0240  0.0110  0.0026  233 MET C O   
5589  C CB  . MET C  233 ? 0.6077 0.7056 0.5146 0.0305  0.0126  0.0104  233 MET C CB  
5590  C CG  . MET C  233 ? 0.6447 0.7357 0.5600 0.0344  0.0129  0.0128  233 MET C CG  
5591  S SD  . MET C  233 ? 0.8741 0.9697 0.7907 0.0396  0.0106  0.0180  233 MET C SD  
5592  C CE  . MET C  233 ? 0.8574 0.9589 0.7668 0.0395  0.0131  0.0203  233 MET C CE  
5593  N N   . ASN C  234 ? 0.6270 0.7078 0.5416 0.0237  0.0171  0.0016  234 ASN C N   
5594  C CA  . ASN C  234 ? 0.6229 0.6990 0.5425 0.0224  0.0160  -0.0006 234 ASN C CA  
5595  C C   . ASN C  234 ? 0.6218 0.6943 0.5490 0.0262  0.0134  0.0019  234 ASN C C   
5596  O O   . ASN C  234 ? 0.6044 0.6739 0.5356 0.0292  0.0144  0.0046  234 ASN C O   
5597  C CB  . ASN C  234 ? 0.6453 0.7143 0.5670 0.0196  0.0202  -0.0035 234 ASN C CB  
5598  C CG  . ASN C  234 ? 0.6932 0.7652 0.6072 0.0152  0.0228  -0.0068 234 ASN C CG  
5599  O OD1 . ASN C  234 ? 0.6046 0.6845 0.5115 0.0139  0.0211  -0.0071 234 ASN C OD1 
5600  N ND2 . ASN C  234 ? 0.7852 0.8512 0.7006 0.0126  0.0272  -0.0093 234 ASN C ND2 
5601  N N   . TYR C  235 ? 0.5558 0.6287 0.4850 0.0258  0.0102  0.0010  235 TYR C N   
5602  C CA  . TYR C  235 ? 0.5262 0.5963 0.4620 0.0289  0.0074  0.0032  235 TYR C CA  
5603  C C   . TYR C  235 ? 0.5913 0.6542 0.5335 0.0278  0.0076  0.0017  235 TYR C C   
5604  O O   . TYR C  235 ? 0.6035 0.6660 0.5445 0.0247  0.0077  -0.0011 235 TYR C O   
5605  C CB  . TYR C  235 ? 0.5304 0.6068 0.4636 0.0298  0.0034  0.0039  235 TYR C CB  
5606  C CG  . TYR C  235 ? 0.7203 0.8047 0.6473 0.0307  0.0030  0.0055  235 TYR C CG  
5607  C CD1 . TYR C  235 ? 0.7032 0.7938 0.6229 0.0277  0.0030  0.0036  235 TYR C CD1 
5608  C CD2 . TYR C  235 ? 0.6154 0.7011 0.5437 0.0346  0.0027  0.0092  235 TYR C CD2 
5609  C CE1 . TYR C  235 ? 0.6145 0.7129 0.5287 0.0285  0.0025  0.0054  235 TYR C CE1 
5610  C CE2 . TYR C  235 ? 0.6906 0.7838 0.6136 0.0356  0.0024  0.0112  235 TYR C CE2 
5611  C CZ  . TYR C  235 ? 0.6856 0.7854 0.6016 0.0326  0.0022  0.0094  235 TYR C CZ  
5612  O OH  . TYR C  235 ? 0.7041 0.8119 0.6149 0.0335  0.0016  0.0117  235 TYR C OH  
5613  N N   . TYR C  236 ? 0.5270 0.5844 0.4762 0.0302  0.0078  0.0037  236 TYR C N   
5614  C CA  . TYR C  236 ? 0.4994 0.5501 0.4556 0.0294  0.0079  0.0029  236 TYR C CA  
5615  C C   . TYR C  236 ? 0.5642 0.6132 0.5261 0.0319  0.0045  0.0049  236 TYR C C   
5616  O O   . TYR C  236 ? 0.5309 0.5821 0.4927 0.0347  0.0032  0.0072  236 TYR C O   
5617  C CB  . TYR C  236 ? 0.4601 0.5049 0.4205 0.0294  0.0121  0.0030  236 TYR C CB  
5618  C CG  . TYR C  236 ? 0.6171 0.6629 0.5720 0.0267  0.0161  0.0008  236 TYR C CG  
5619  C CD1 . TYR C  236 ? 0.6218 0.6717 0.5707 0.0273  0.0176  0.0016  236 TYR C CD1 
5620  C CD2 . TYR C  236 ? 0.5929 0.6353 0.5485 0.0234  0.0184  -0.0020 236 TYR C CD2 
5621  C CE1 . TYR C  236 ? 0.6494 0.7002 0.5928 0.0245  0.0212  -0.0006 236 TYR C CE1 
5622  C CE2 . TYR C  236 ? 0.6136 0.6566 0.5639 0.0207  0.0223  -0.0044 236 TYR C CE2 
5623  C CZ  . TYR C  236 ? 0.6634 0.7106 0.6074 0.0211  0.0236  -0.0037 236 TYR C CZ  
5624  O OH  . TYR C  236 ? 0.5966 0.6446 0.5349 0.0180  0.0275  -0.0062 236 TYR C OH  
5625  N N   . TRP C  237 ? 0.5819 0.6271 0.5486 0.0307  0.0031  0.0041  237 TRP C N   
5626  C CA  . TRP C  237 ? 0.4931 0.5365 0.4649 0.0324  -0.0003 0.0058  237 TRP C CA  
5627  C C   . TRP C  237 ? 0.4440 0.4812 0.4232 0.0314  -0.0001 0.0057  237 TRP C C   
5628  O O   . TRP C  237 ? 0.6072 0.6420 0.5873 0.0292  0.0024  0.0041  237 TRP C O   
5629  C CB  . TRP C  237 ? 0.4787 0.5268 0.4467 0.0318  -0.0040 0.0050  237 TRP C CB  
5630  C CG  . TRP C  237 ? 0.5455 0.5939 0.5115 0.0285  -0.0044 0.0024  237 TRP C CG  
5631  C CD1 . TRP C  237 ? 0.5741 0.6262 0.5338 0.0262  -0.0031 0.0001  237 TRP C CD1 
5632  C CD2 . TRP C  237 ? 0.5292 0.5740 0.4996 0.0271  -0.0061 0.0018  237 TRP C CD2 
5633  N NE1 . TRP C  237 ? 0.5780 0.6289 0.5380 0.0235  -0.0036 -0.0020 237 TRP C NE1 
5634  C CE2 . TRP C  237 ? 0.5351 0.5815 0.5018 0.0241  -0.0055 -0.0009 237 TRP C CE2 
5635  C CE3 . TRP C  237 ? 0.5601 0.6007 0.5373 0.0279  -0.0081 0.0033  237 TRP C CE3 
5636  C CZ2 . TRP C  237 ? 0.6291 0.6728 0.5987 0.0221  -0.0067 -0.0018 237 TRP C CZ2 
5637  C CZ3 . TRP C  237 ? 0.5981 0.6365 0.5780 0.0259  -0.0096 0.0025  237 TRP C CZ3 
5638  C CH2 . TRP C  237 ? 0.5088 0.5486 0.4850 0.0231  -0.0088 0.0000  237 TRP C CH2 
5639  N N   . THR C  238 ? 0.4332 0.4680 0.4180 0.0329  -0.0026 0.0074  238 THR C N   
5640  C CA  . THR C  238 ? 0.4815 0.5111 0.4738 0.0321  -0.0031 0.0079  238 THR C CA  
5641  C C   . THR C  238 ? 0.5716 0.6007 0.5675 0.0333  -0.0070 0.0095  238 THR C C   
5642  O O   . THR C  238 ? 0.6208 0.6526 0.6141 0.0351  -0.0086 0.0103  238 THR C O   
5643  C CB  . THR C  238 ? 0.5873 0.6120 0.5854 0.0329  0.0006  0.0089  238 THR C CB  
5644  O OG1 . THR C  238 ? 0.6584 0.6786 0.6642 0.0320  0.0000  0.0095  238 THR C OG1 
5645  C CG2 . THR C  238 ? 0.5109 0.5352 0.5108 0.0359  0.0008  0.0111  238 THR C CG2 
5646  N N   . LEU C  239 ? 0.5469 0.5726 0.5487 0.0322  -0.0086 0.0099  239 LEU C N   
5647  C CA  . LEU C  239 ? 0.5940 0.6190 0.5991 0.0328  -0.0124 0.0112  239 LEU C CA  
5648  C C   . LEU C  239 ? 0.7325 0.7529 0.7462 0.0337  -0.0120 0.0133  239 LEU C C   
5649  O O   . LEU C  239 ? 0.9711 0.9882 0.9902 0.0324  -0.0114 0.0136  239 LEU C O   
5650  C CB  . LEU C  239 ? 0.6767 0.7025 0.6808 0.0305  -0.0156 0.0102  239 LEU C CB  
5651  C CG  . LEU C  239 ? 0.5369 0.5677 0.5328 0.0297  -0.0168 0.0084  239 LEU C CG  
5652  C CD1 . LEU C  239 ? 0.7324 0.7634 0.7279 0.0273  -0.0194 0.0074  239 LEU C CD1 
5653  C CD2 . LEU C  239 ? 0.6327 0.6666 0.6255 0.0316  -0.0186 0.0090  239 LEU C CD2 
5654  N N   . VAL C  240 ? 0.6656 0.6857 0.6808 0.0359  -0.0121 0.0147  240 VAL C N   
5655  C CA  . VAL C  240 ? 0.6939 0.7099 0.7172 0.0368  -0.0117 0.0167  240 VAL C CA  
5656  C C   . VAL C  240 ? 0.6788 0.6938 0.7064 0.0357  -0.0159 0.0176  240 VAL C C   
5657  O O   . VAL C  240 ? 0.7064 0.7234 0.7310 0.0359  -0.0187 0.0174  240 VAL C O   
5658  C CB  . VAL C  240 ? 0.6355 0.6514 0.6589 0.0395  -0.0101 0.0179  240 VAL C CB  
5659  C CG1 . VAL C  240 ? 0.7583 0.7698 0.7904 0.0402  -0.0093 0.0197  240 VAL C CG1 
5660  C CG2 . VAL C  240 ? 0.4989 0.5164 0.5171 0.0404  -0.0063 0.0172  240 VAL C CG2 
5661  N N   . GLU C  241 ? 0.7069 0.7189 0.7415 0.0346  -0.0161 0.0186  241 GLU C N   
5662  C CA  . GLU C  241 ? 0.8079 0.8190 0.8468 0.0333  -0.0201 0.0197  241 GLU C CA  
5663  C C   . GLU C  241 ? 0.8796 0.8899 0.9216 0.0346  -0.0214 0.0210  241 GLU C C   
5664  O O   . GLU C  241 ? 0.7806 0.7895 0.8243 0.0366  -0.0186 0.0217  241 GLU C O   
5665  C CB  . GLU C  241 ? 1.0022 1.0104 1.0489 0.0320  -0.0198 0.0210  241 GLU C CB  
5666  C CG  . GLU C  241 ? 1.1880 1.1964 1.2324 0.0305  -0.0183 0.0197  241 GLU C CG  
5667  C CD  . GLU C  241 ? 1.4531 1.4641 1.4928 0.0286  -0.0218 0.0187  241 GLU C CD  
5668  O OE1 . GLU C  241 ? 1.4616 1.4740 1.4962 0.0276  -0.0205 0.0168  241 GLU C OE1 
5669  O OE2 . GLU C  241 ? 1.5762 1.5878 1.6172 0.0280  -0.0257 0.0196  241 GLU C OE2 
5670  N N   . PRO C  242 ? 0.9886 0.9997 1.0309 0.0335  -0.0254 0.0214  242 PRO C N   
5671  C CA  . PRO C  242 ? 0.8795 0.8894 0.9251 0.0342  -0.0267 0.0224  242 PRO C CA  
5672  C C   . PRO C  242 ? 0.8762 0.8828 0.9308 0.0347  -0.0253 0.0244  242 PRO C C   
5673  O O   . PRO C  242 ? 0.8286 0.8340 0.8886 0.0333  -0.0260 0.0255  242 PRO C O   
5674  C CB  . PRO C  242 ? 0.5751 0.5861 0.6201 0.0320  -0.0314 0.0224  242 PRO C CB  
5675  C CG  . PRO C  242 ? 0.7246 0.7381 0.7629 0.0309  -0.0322 0.0208  242 PRO C CG  
5676  C CD  . PRO C  242 ? 0.7681 0.7810 0.8071 0.0313  -0.0288 0.0205  242 PRO C CD  
5677  N N   . GLY C  243 ? 0.8303 0.8356 0.8869 0.0366  -0.0232 0.0250  243 GLY C N   
5678  C CA  . GLY C  243 ? 0.8422 0.8445 0.9074 0.0372  -0.0215 0.0268  243 GLY C CA  
5679  C C   . GLY C  243 ? 0.7846 0.7853 0.8511 0.0384  -0.0170 0.0268  243 GLY C C   
5680  O O   . GLY C  243 ? 0.9766 0.9746 1.0501 0.0391  -0.0148 0.0282  243 GLY C O   
5681  N N   . ASP C  244 ? 0.8062 0.8086 0.8659 0.0385  -0.0154 0.0252  244 ASP C N   
5682  C CA  . ASP C  244 ? 0.7882 0.7894 0.8477 0.0393  -0.0109 0.0249  244 ASP C CA  
5683  C C   . ASP C  244 ? 0.6974 0.6996 0.7516 0.0416  -0.0080 0.0243  244 ASP C C   
5684  O O   . ASP C  244 ? 0.8070 0.8114 0.8562 0.0424  -0.0096 0.0239  244 ASP C O   
5685  C CB  . ASP C  244 ? 0.8421 0.8448 0.8972 0.0377  -0.0108 0.0233  244 ASP C CB  
5686  C CG  . ASP C  244 ? 1.0107 1.0115 1.0665 0.0378  -0.0061 0.0228  244 ASP C CG  
5687  O OD1 . ASP C  244 ? 1.1195 1.1212 1.1721 0.0364  -0.0054 0.0214  244 ASP C OD1 
5688  O OD2 . ASP C  244 ? 0.8482 0.8465 0.9080 0.0393  -0.0029 0.0238  244 ASP C OD2 
5689  N N   . LYS C  245 ? 0.6659 0.6662 0.7213 0.0426  -0.0037 0.0245  245 LYS C N   
5690  C CA  . LYS C  245 ? 0.8063 0.8075 0.8566 0.0448  -0.0007 0.0243  245 LYS C CA  
5691  C C   . LYS C  245 ? 0.7079 0.7100 0.7530 0.0445  0.0028  0.0229  245 LYS C C   
5692  O O   . LYS C  245 ? 0.7979 0.7981 0.8458 0.0430  0.0044  0.0225  245 LYS C O   
5693  C CB  . LYS C  245 ? 0.9867 0.9848 1.0431 0.0466  0.0016  0.0260  245 LYS C CB  
5694  C CG  . LYS C  245 ? 0.9010 0.8955 0.9629 0.0466  0.0055  0.0265  245 LYS C CG  
5695  C CD  . LYS C  245 ? 0.9853 0.9768 1.0534 0.0484  0.0076  0.0282  245 LYS C CD  
5696  C CE  . LYS C  245 ? 1.1051 1.0930 1.1787 0.0484  0.0119  0.0287  245 LYS C CE  
5697  N NZ  . LYS C  245 ? 1.0420 1.0266 1.1233 0.0498  0.0135  0.0305  245 LYS C NZ  
5698  N N   . ILE C  246 ? 0.6590 0.6641 0.6967 0.0457  0.0040  0.0224  246 ILE C N   
5699  C CA  . ILE C  246 ? 0.6309 0.6374 0.6626 0.0453  0.0072  0.0210  246 ILE C CA  
5700  C C   . ILE C  246 ? 0.7147 0.7206 0.7449 0.0475  0.0110  0.0220  246 ILE C C   
5701  O O   . ILE C  246 ? 0.6231 0.6303 0.6520 0.0495  0.0104  0.0232  246 ILE C O   
5702  C CB  . ILE C  246 ? 0.6780 0.6896 0.7010 0.0443  0.0051  0.0194  246 ILE C CB  
5703  C CG1 . ILE C  246 ? 0.7353 0.7486 0.7520 0.0435  0.0083  0.0179  246 ILE C CG1 
5704  C CG2 . ILE C  246 ? 0.5172 0.5320 0.5366 0.0463  0.0031  0.0203  246 ILE C CG2 
5705  C CD1 . ILE C  246 ? 0.5619 0.5807 0.5700 0.0425  0.0064  0.0164  246 ILE C CD1 
5706  N N   . THR C  247 ? 0.8526 0.8565 0.8830 0.0469  0.0151  0.0215  247 THR C N   
5707  C CA  . THR C  247 ? 0.8987 0.9016 0.9281 0.0488  0.0191  0.0225  247 THR C CA  
5708  C C   . THR C  247 ? 0.7972 0.8036 0.8174 0.0483  0.0214  0.0212  247 THR C C   
5709  O O   . THR C  247 ? 0.7655 0.7727 0.7823 0.0459  0.0220  0.0192  247 THR C O   
5710  C CB  . THR C  247 ? 0.8839 0.8813 0.9211 0.0487  0.0227  0.0231  247 THR C CB  
5711  O OG1 . THR C  247 ? 0.9382 0.9328 0.9839 0.0496  0.0208  0.0248  247 THR C OG1 
5712  C CG2 . THR C  247 ? 1.0340 1.0303 1.0686 0.0501  0.0273  0.0236  247 THR C CG2 
5713  N N   . PHE C  248 ? 0.8162 0.8247 0.8323 0.0504  0.0226  0.0225  248 PHE C N   
5714  C CA  . PHE C  248 ? 0.8106 0.8227 0.8181 0.0501  0.0249  0.0219  248 PHE C CA  
5715  C C   . PHE C  248 ? 0.8383 0.8475 0.8467 0.0513  0.0297  0.0230  248 PHE C C   
5716  O O   . PHE C  248 ? 0.9560 0.9628 0.9692 0.0537  0.0304  0.0251  248 PHE C O   
5717  C CB  . PHE C  248 ? 0.5792 0.5972 0.5802 0.0515  0.0223  0.0227  248 PHE C CB  
5718  C CG  . PHE C  248 ? 0.6171 0.6386 0.6153 0.0500  0.0182  0.0212  248 PHE C CG  
5719  C CD1 . PHE C  248 ? 0.6351 0.6555 0.6382 0.0503  0.0146  0.0216  248 PHE C CD1 
5720  C CD2 . PHE C  248 ? 0.6557 0.6818 0.6464 0.0480  0.0179  0.0194  248 PHE C CD2 
5721  C CE1 . PHE C  248 ? 0.5816 0.6051 0.5820 0.0488  0.0110  0.0202  248 PHE C CE1 
5722  C CE2 . PHE C  248 ? 0.6613 0.6906 0.6496 0.0465  0.0143  0.0180  248 PHE C CE2 
5723  C CZ  . PHE C  248 ? 0.5709 0.5988 0.5640 0.0470  0.0109  0.0185  248 PHE C CZ  
5724  N N   . GLU C  249 ? 0.7376 0.7469 0.7413 0.0495  0.0331  0.0215  249 GLU C N   
5725  C CA  . GLU C  249 ? 0.7495 0.7559 0.7536 0.0502  0.0380  0.0222  249 GLU C CA  
5726  C C   . GLU C  249 ? 0.7616 0.7716 0.7561 0.0486  0.0405  0.0210  249 GLU C C   
5727  O O   . GLU C  249 ? 0.8451 0.8548 0.8368 0.0456  0.0418  0.0183  249 GLU C O   
5728  C CB  . GLU C  249 ? 0.8913 0.8910 0.9036 0.0491  0.0407  0.0215  249 GLU C CB  
5729  C CG  . GLU C  249 ? 1.1296 1.1257 1.1427 0.0495  0.0462  0.0220  249 GLU C CG  
5730  C CD  . GLU C  249 ? 1.2412 1.2308 1.2632 0.0485  0.0490  0.0214  249 GLU C CD  
5731  O OE1 . GLU C  249 ? 1.3937 1.3800 1.4156 0.0478  0.0540  0.0208  249 GLU C OE1 
5732  O OE2 . GLU C  249 ? 1.0811 1.0690 1.1104 0.0483  0.0462  0.0216  249 GLU C OE2 
5733  N N   . ALA C  250 ? 0.8224 0.8358 0.8117 0.0505  0.0412  0.0229  250 ALA C N   
5734  C CA  . ALA C  250 ? 0.7845 0.8026 0.7638 0.0490  0.0428  0.0220  250 ALA C CA  
5735  C C   . ALA C  250 ? 0.9491 0.9670 0.9254 0.0506  0.0467  0.0240  250 ALA C C   
5736  O O   . ALA C  250 ? 0.8461 0.8627 0.8262 0.0538  0.0468  0.0269  250 ALA C O   
5737  C CB  . ALA C  250 ? 0.7009 0.7264 0.6740 0.0492  0.0385  0.0223  250 ALA C CB  
5738  N N   . THR C  251 ? 0.9039 0.9231 0.8733 0.0481  0.0498  0.0224  251 THR C N   
5739  C CA  . THR C  251 ? 0.8061 0.8265 0.7705 0.0491  0.0532  0.0242  251 THR C CA  
5740  C C   . THR C  251 ? 0.8569 0.8858 0.8111 0.0485  0.0511  0.0248  251 THR C C   
5741  O O   . THR C  251 ? 0.9231 0.9547 0.8707 0.0483  0.0536  0.0258  251 THR C O   
5742  C CB  . THR C  251 ? 0.7941 0.8098 0.7576 0.0465  0.0587  0.0222  251 THR C CB  
5743  O OG1 . THR C  251 ? 0.9345 0.9509 0.8944 0.0425  0.0589  0.0184  251 THR C OG1 
5744  C CG2 . THR C  251 ? 0.7830 0.7904 0.7570 0.0477  0.0612  0.0225  251 THR C CG2 
5745  N N   . GLY C  252 ? 0.8517 0.8852 0.8049 0.0482  0.0466  0.0242  252 GLY C N   
5746  C CA  . GLY C  252 ? 0.8483 0.8903 0.7928 0.0477  0.0441  0.0247  252 GLY C CA  
5747  C C   . GLY C  252 ? 0.8789 0.9241 0.8210 0.0447  0.0410  0.0217  252 GLY C C   
5748  O O   . GLY C  252 ? 0.8659 0.9064 0.8123 0.0428  0.0413  0.0189  252 GLY C O   
5749  N N   . ASN C  253 ? 0.7853 0.8386 0.7206 0.0445  0.0381  0.0223  253 ASN C N   
5750  C CA  . ASN C  253 ? 0.7190 0.7764 0.6506 0.0414  0.0354  0.0194  253 ASN C CA  
5751  C C   . ASN C  253 ? 0.8092 0.8651 0.7469 0.0423  0.0315  0.0188  253 ASN C C   
5752  O O   . ASN C  253 ? 0.7709 0.8289 0.7066 0.0397  0.0295  0.0162  253 ASN C O   
5753  C CB  . ASN C  253 ? 0.7894 0.8442 0.7177 0.0369  0.0386  0.0154  253 ASN C CB  
5754  C CG  . ASN C  253 ? 0.7718 0.8285 0.6928 0.0354  0.0424  0.0155  253 ASN C CG  
5755  O OD1 . ASN C  253 ? 0.8076 0.8702 0.7202 0.0324  0.0423  0.0140  253 ASN C OD1 
5756  N ND2 . ASN C  253 ? 0.7256 0.7775 0.6498 0.0373  0.0458  0.0174  253 ASN C ND2 
5757  N N   . LEU C  254 ? 0.8623 0.9146 0.8071 0.0458  0.0306  0.0213  254 LEU C N   
5758  C CA  . LEU C  254 ? 0.6845 0.7348 0.6354 0.0465  0.0272  0.0208  254 LEU C CA  
5759  C C   . LEU C  254 ? 0.6321 0.6878 0.5822 0.0491  0.0233  0.0231  254 LEU C C   
5760  O O   . LEU C  254 ? 0.7674 0.8230 0.7199 0.0526  0.0234  0.0263  254 LEU C O   
5761  C CB  . LEU C  254 ? 0.7031 0.7453 0.6633 0.0482  0.0286  0.0215  254 LEU C CB  
5762  C CG  . LEU C  254 ? 0.6347 0.6747 0.6015 0.0490  0.0250  0.0214  254 LEU C CG  
5763  C CD1 . LEU C  254 ? 0.7089 0.7495 0.6746 0.0457  0.0231  0.0183  254 LEU C CD1 
5764  C CD2 . LEU C  254 ? 0.5868 0.6194 0.5628 0.0505  0.0264  0.0224  254 LEU C CD2 
5765  N N   . VAL C  255 ? 0.6342 0.6945 0.5811 0.0475  0.0201  0.0215  255 VAL C N   
5766  C CA  . VAL C  255 ? 0.5462 0.6106 0.4936 0.0497  0.0164  0.0233  255 VAL C CA  
5767  C C   . VAL C  255 ? 0.6478 0.7066 0.6032 0.0509  0.0146  0.0232  255 VAL C C   
5768  O O   . VAL C  255 ? 0.6304 0.6880 0.5872 0.0488  0.0125  0.0208  255 VAL C O   
5769  C CB  . VAL C  255 ? 0.5559 0.6270 0.4973 0.0474  0.0136  0.0216  255 VAL C CB  
5770  C CG1 . VAL C  255 ? 0.6100 0.6855 0.5522 0.0500  0.0101  0.0236  255 VAL C CG1 
5771  C CG2 . VAL C  255 ? 0.5451 0.6220 0.4784 0.0457  0.0153  0.0214  255 VAL C CG2 
5772  N N   . VAL C  256 ? 0.7367 0.7921 0.6973 0.0540  0.0155  0.0258  256 VAL C N   
5773  C CA  . VAL C  256 ? 0.6604 0.7100 0.6288 0.0549  0.0142  0.0257  256 VAL C CA  
5774  C C   . VAL C  256 ? 0.6590 0.7112 0.6280 0.0554  0.0102  0.0256  256 VAL C C   
5775  O O   . VAL C  256 ? 0.7074 0.7655 0.6721 0.0565  0.0088  0.0268  256 VAL C O   
5776  C CB  . VAL C  256 ? 0.7134 0.7588 0.6870 0.0580  0.0164  0.0284  256 VAL C CB  
5777  C CG1 . VAL C  256 ? 0.6902 0.7326 0.6635 0.0575  0.0206  0.0284  256 VAL C CG1 
5778  C CG2 . VAL C  256 ? 0.8135 0.8633 0.7851 0.0613  0.0159  0.0315  256 VAL C CG2 
5779  N N   . PRO C  257 ? 0.6042 0.6520 0.5785 0.0544  0.0084  0.0243  257 PRO C N   
5780  C CA  . PRO C  257 ? 0.5652 0.6144 0.5406 0.0547  0.0047  0.0241  257 PRO C CA  
5781  C C   . PRO C  257 ? 0.6335 0.6826 0.6115 0.0582  0.0047  0.0268  257 PRO C C   
5782  O O   . PRO C  257 ? 0.7186 0.7637 0.7007 0.0599  0.0070  0.0284  257 PRO C O   
5783  C CB  . PRO C  257 ? 0.5449 0.5883 0.5262 0.0529  0.0035  0.0224  257 PRO C CB  
5784  C CG  . PRO C  257 ? 0.6849 0.7254 0.6668 0.0510  0.0062  0.0211  257 PRO C CG  
5785  C CD  . PRO C  257 ? 0.5624 0.6039 0.5419 0.0527  0.0097  0.0228  257 PRO C CD  
5786  N N   . ARG C  258 ? 0.6938 0.7470 0.6695 0.0591  0.0024  0.0273  258 ARG C N   
5787  C CA  . ARG C  258 ? 0.6992 0.7519 0.6779 0.0621  0.0024  0.0297  258 ARG C CA  
5788  C C   . ARG C  258 ? 0.6432 0.6937 0.6249 0.0612  -0.0006 0.0283  258 ARG C C   
5789  O O   . ARG C  258 ? 0.6952 0.7412 0.6824 0.0622  -0.0005 0.0289  258 ARG C O   
5790  C CB  . ARG C  258 ? 0.6927 0.7520 0.6665 0.0643  0.0026  0.0319  258 ARG C CB  
5791  C CG  . ARG C  258 ? 0.7606 0.8195 0.7374 0.0675  0.0029  0.0344  258 ARG C CG  
5792  C CD  . ARG C  258 ? 0.8221 0.8881 0.7946 0.0698  0.0034  0.0369  258 ARG C CD  
5793  N NE  . ARG C  258 ? 0.9080 0.9748 0.8827 0.0722  0.0028  0.0386  258 ARG C NE  
5794  C CZ  . ARG C  258 ? 1.0512 1.1164 1.0291 0.0755  0.0052  0.0415  258 ARG C CZ  
5795  N NH1 . ARG C  258 ? 1.1264 1.1893 1.1055 0.0768  0.0080  0.0432  258 ARG C NH1 
5796  N NH2 . ARG C  258 ? 1.1083 1.1740 1.0881 0.0774  0.0049  0.0426  258 ARG C NH2 
5797  N N   . TYR C  259 ? 0.6235 0.6775 0.6017 0.0592  -0.0033 0.0264  259 TYR C N   
5798  C CA  . TYR C  259 ? 0.6347 0.6869 0.6150 0.0578  -0.0062 0.0249  259 TYR C CA  
5799  C C   . TYR C  259 ? 0.7157 0.7660 0.6963 0.0544  -0.0078 0.0222  259 TYR C C   
5800  O O   . TYR C  259 ? 0.7384 0.7917 0.7148 0.0527  -0.0077 0.0210  259 TYR C O   
5801  C CB  . TYR C  259 ? 0.7156 0.7733 0.6919 0.0584  -0.0080 0.0250  259 TYR C CB  
5802  C CG  . TYR C  259 ? 0.9133 0.9723 0.8905 0.0618  -0.0068 0.0277  259 TYR C CG  
5803  C CD1 . TYR C  259 ? 0.8857 0.9491 0.8600 0.0641  -0.0048 0.0301  259 TYR C CD1 
5804  C CD2 . TYR C  259 ? 0.9395 0.9952 0.9204 0.0625  -0.0076 0.0278  259 TYR C CD2 
5805  C CE1 . TYR C  259 ? 0.9740 1.0386 0.9497 0.0674  -0.0034 0.0328  259 TYR C CE1 
5806  C CE2 . TYR C  259 ? 0.9396 0.9961 0.9216 0.0656  -0.0061 0.0301  259 TYR C CE2 
5807  C CZ  . TYR C  259 ? 0.9995 1.0605 0.9792 0.0682  -0.0039 0.0328  259 TYR C CZ  
5808  O OH  . TYR C  259 ? 1.0728 1.1346 1.0541 0.0715  -0.0022 0.0354  259 TYR C OH  
5809  N N   . ALA C  260 ? 0.6834 0.7289 0.6689 0.0533  -0.0093 0.0215  260 ALA C N   
5810  C CA  . ALA C  260 ? 0.5498 0.5935 0.5361 0.0501  -0.0112 0.0193  260 ALA C CA  
5811  C C   . ALA C  260 ? 0.6058 0.6504 0.5912 0.0489  -0.0146 0.0182  260 ALA C C   
5812  O O   . ALA C  260 ? 0.6184 0.6652 0.6022 0.0504  -0.0152 0.0189  260 ALA C O   
5813  C CB  . ALA C  260 ? 0.6170 0.6547 0.6098 0.0496  -0.0103 0.0195  260 ALA C CB  
5814  N N   . PHE C  261 ? 0.6478 0.6905 0.6344 0.0462  -0.0166 0.0165  261 PHE C N   
5815  C CA  . PHE C  261 ? 0.5017 0.5452 0.4871 0.0447  -0.0198 0.0153  261 PHE C CA  
5816  C C   . PHE C  261 ? 0.5639 0.6029 0.5543 0.0426  -0.0219 0.0148  261 PHE C C   
5817  O O   . PHE C  261 ? 0.7608 0.7985 0.7523 0.0406  -0.0222 0.0139  261 PHE C O   
5818  C CB  . PHE C  261 ? 0.4762 0.5244 0.4557 0.0430  -0.0208 0.0136  261 PHE C CB  
5819  C CG  . PHE C  261 ? 0.5528 0.6064 0.5273 0.0447  -0.0193 0.0143  261 PHE C CG  
5820  C CD1 . PHE C  261 ? 0.5909 0.6464 0.5633 0.0448  -0.0169 0.0144  261 PHE C CD1 
5821  C CD2 . PHE C  261 ? 0.5578 0.6149 0.5298 0.0461  -0.0202 0.0148  261 PHE C CD2 
5822  C CE1 . PHE C  261 ? 0.6744 0.7354 0.6420 0.0462  -0.0157 0.0152  261 PHE C CE1 
5823  C CE2 . PHE C  261 ? 0.4772 0.5398 0.4450 0.0478  -0.0190 0.0158  261 PHE C CE2 
5824  C CZ  . PHE C  261 ? 0.5768 0.6416 0.5423 0.0478  -0.0169 0.0160  261 PHE C CZ  
5825  N N   . ALA C  262 ? 0.6619 0.6985 0.6553 0.0431  -0.0232 0.0154  262 ALA C N   
5826  C CA  . ALA C  262 ? 0.6916 0.7248 0.6889 0.0408  -0.0258 0.0150  262 ALA C CA  
5827  C C   . ALA C  262 ? 0.7311 0.7667 0.7243 0.0385  -0.0285 0.0133  262 ALA C C   
5828  O O   . ALA C  262 ? 0.6943 0.7329 0.6831 0.0389  -0.0292 0.0127  262 ALA C O   
5829  C CB  . ALA C  262 ? 0.7826 0.8134 0.7830 0.0416  -0.0265 0.0158  262 ALA C CB  
5830  N N   . MET C  263 ? 0.6446 0.6788 0.6395 0.0362  -0.0297 0.0127  263 MET C N   
5831  C CA  . MET C  263 ? 0.7077 0.7443 0.6984 0.0341  -0.0316 0.0111  263 MET C CA  
5832  C C   . MET C  263 ? 0.6974 0.7314 0.6913 0.0314  -0.0341 0.0110  263 MET C C   
5833  O O   . MET C  263 ? 0.7986 0.8297 0.7975 0.0309  -0.0334 0.0118  263 MET C O   
5834  C CB  . MET C  263 ? 0.7199 0.7593 0.7070 0.0341  -0.0294 0.0103  263 MET C CB  
5835  C CG  . MET C  263 ? 0.6953 0.7376 0.6775 0.0320  -0.0308 0.0085  263 MET C CG  
5836  S SD  . MET C  263 ? 0.9237 0.9689 0.9021 0.0316  -0.0280 0.0072  263 MET C SD  
5837  C CE  . MET C  263 ? 0.8147 0.8548 0.7995 0.0304  -0.0265 0.0077  263 MET C CE  
5838  N N   . GLU C  264 ? 0.6693 0.7043 0.6604 0.0297  -0.0369 0.0100  264 GLU C N   
5839  C CA  . GLU C  264 ? 0.7281 0.7614 0.7212 0.0270  -0.0395 0.0100  264 GLU C CA  
5840  C C   . GLU C  264 ? 0.7528 0.7890 0.7405 0.0254  -0.0403 0.0082  264 GLU C C   
5841  O O   . GLU C  264 ? 0.8542 0.8930 0.8371 0.0253  -0.0414 0.0072  264 GLU C O   
5842  C CB  . GLU C  264 ? 0.7812 0.8128 0.7760 0.0260  -0.0424 0.0105  264 GLU C CB  
5843  C CG  . GLU C  264 ? 1.0933 1.1212 1.0953 0.0252  -0.0434 0.0122  264 GLU C CG  
5844  C CD  . GLU C  264 ? 1.3200 1.3464 1.3236 0.0247  -0.0454 0.0127  264 GLU C CD  
5845  O OE1 . GLU C  264 ? 1.3570 1.3817 1.3642 0.0227  -0.0480 0.0136  264 GLU C OE1 
5846  O OE2 . GLU C  264 ? 1.4080 1.4351 1.4094 0.0263  -0.0443 0.0122  264 GLU C OE2 
5847  N N   . ARG C  265 ? 0.8215 0.8573 0.8103 0.0242  -0.0394 0.0080  265 ARG C N   
5848  C CA  . ARG C  265 ? 0.8469 0.8854 0.8307 0.0227  -0.0395 0.0062  265 ARG C CA  
5849  C C   . ARG C  265 ? 0.8403 0.8772 0.8252 0.0200  -0.0419 0.0061  265 ARG C C   
5850  O O   . ARG C  265 ? 0.8443 0.8780 0.8349 0.0193  -0.0425 0.0076  265 ARG C O   
5851  C CB  . ARG C  265 ? 0.7121 0.7517 0.6947 0.0232  -0.0362 0.0054  265 ARG C CB  
5852  C CG  . ARG C  265 ? 0.7488 0.7848 0.7375 0.0239  -0.0340 0.0068  265 ARG C CG  
5853  C CD  . ARG C  265 ? 0.8240 0.8611 0.8108 0.0240  -0.0304 0.0057  265 ARG C CD  
5854  N NE  . ARG C  265 ? 0.8929 0.9279 0.8822 0.0219  -0.0296 0.0052  265 ARG C NE  
5855  C CZ  . ARG C  265 ? 0.8975 0.9286 0.8931 0.0219  -0.0280 0.0064  265 ARG C CZ  
5856  N NH1 . ARG C  265 ? 0.8899 0.9189 0.8899 0.0238  -0.0272 0.0082  265 ARG C NH1 
5857  N NH2 . ARG C  265 ? 0.9794 1.0086 0.9772 0.0201  -0.0269 0.0060  265 ARG C NH2 
5858  N N   . ASN C  266 ? 0.9246 0.9641 0.9044 0.0187  -0.0433 0.0046  266 ASN C N   
5859  C CA  . ASN C  266 ? 1.0296 1.0681 1.0095 0.0161  -0.0453 0.0044  266 ASN C CA  
5860  C C   . ASN C  266 ? 1.0203 1.0607 0.9970 0.0150  -0.0435 0.0026  266 ASN C C   
5861  O O   . ASN C  266 ? 1.0084 1.0524 0.9798 0.0155  -0.0424 0.0009  266 ASN C O   
5862  C CB  . ASN C  266 ? 1.2157 1.2552 1.1923 0.0149  -0.0485 0.0040  266 ASN C CB  
5863  C CG  . ASN C  266 ? 1.0776 1.1200 1.0496 0.0165  -0.0481 0.0029  266 ASN C CG  
5864  O OD1 . ASN C  266 ? 0.8466 0.8882 0.8188 0.0170  -0.0494 0.0034  266 ASN C OD1 
5865  N ND2 . ASN C  266 ? 1.1105 1.1563 1.0783 0.0173  -0.0461 0.0015  266 ASN C ND2 
5866  N N   . ALA C  267 ? 0.9775 1.0155 0.9576 0.0135  -0.0431 0.0031  267 ALA C N   
5867  C CA  . ALA C  267 ? 1.1764 1.2155 1.1543 0.0123  -0.0407 0.0014  267 ALA C CA  
5868  C C   . ALA C  267 ? 1.1094 1.1511 1.0816 0.0104  -0.0422 -0.0004 267 ALA C C   
5869  O O   . ALA C  267 ? 0.9345 0.9760 0.9059 0.0096  -0.0453 0.0001  267 ALA C O   
5870  C CB  . ALA C  267 ? 1.2274 1.2626 1.2112 0.0113  -0.0395 0.0026  267 ALA C CB  
5871  N N   . GLY C  268 ? 1.0959 1.1401 1.0641 0.0097  -0.0400 -0.0026 268 GLY C N   
5872  C CA  . GLY C  268 ? 1.1868 1.2330 1.1506 0.0076  -0.0409 -0.0044 268 GLY C CA  
5873  C C   . GLY C  268 ? 1.1533 1.2044 1.1104 0.0078  -0.0415 -0.0063 268 GLY C C   
5874  O O   . GLY C  268 ? 1.1024 1.1548 1.0563 0.0062  -0.0431 -0.0073 268 GLY C O   
5875  N N   . SER C  269 ? 0.9229 0.9769 0.8780 0.0097  -0.0402 -0.0066 269 SER C N   
5876  C CA  . SER C  269 ? 0.7710 0.8303 0.7203 0.0100  -0.0405 -0.0082 269 SER C CA  
5877  C C   . SER C  269 ? 0.7799 0.8427 0.7259 0.0095  -0.0377 -0.0100 269 SER C C   
5878  O O   . SER C  269 ? 0.9079 0.9689 0.8553 0.0080  -0.0356 -0.0108 269 SER C O   
5879  C CB  . SER C  269 ? 0.7054 0.7661 0.6544 0.0126  -0.0414 -0.0069 269 SER C CB  
5880  O OG  . SER C  269 ? 0.5470 0.6127 0.4909 0.0128  -0.0419 -0.0081 269 SER C OG  
5881  N N   . GLY C  270 ? 0.5934 0.6614 0.5351 0.0105  -0.0376 -0.0107 270 GLY C N   
5882  C CA  . GLY C  270 ? 0.5978 0.6701 0.5358 0.0098  -0.0353 -0.0124 270 GLY C CA  
5883  C C   . GLY C  270 ? 0.4604 0.5383 0.3952 0.0119  -0.0352 -0.0120 270 GLY C C   
5884  O O   . GLY C  270 ? 0.5129 0.5908 0.4490 0.0142  -0.0364 -0.0102 270 GLY C O   
5885  N N   . ILE C  271 ? 0.4909 0.5737 0.4217 0.0108  -0.0336 -0.0136 271 ILE C N   
5886  C CA  . ILE C  271 ? 0.4253 0.5143 0.3530 0.0126  -0.0335 -0.0130 271 ILE C CA  
5887  C C   . ILE C  271 ? 0.5309 0.6261 0.4536 0.0107  -0.0339 -0.0151 271 ILE C C   
5888  O O   . ILE C  271 ? 0.7569 0.8533 0.6773 0.0081  -0.0324 -0.0173 271 ILE C O   
5889  C CB  . ILE C  271 ? 0.4863 0.5760 0.4140 0.0135  -0.0309 -0.0124 271 ILE C CB  
5890  C CG1 . ILE C  271 ? 0.4426 0.5263 0.3756 0.0155  -0.0303 -0.0104 271 ILE C CG1 
5891  C CG2 . ILE C  271 ? 0.6046 0.7014 0.5290 0.0153  -0.0308 -0.0115 271 ILE C CG2 
5892  C CD1 . ILE C  271 ? 0.5787 0.6609 0.5125 0.0153  -0.0273 -0.0104 271 ILE C CD1 
5893  N N   . ILE C  272 ? 0.6040 0.7030 0.5252 0.0119  -0.0357 -0.0145 272 ILE C N   
5894  C CA  . ILE C  272 ? 0.6425 0.7477 0.5595 0.0103  -0.0363 -0.0162 272 ILE C CA  
5895  C C   . ILE C  272 ? 0.5778 0.6905 0.4920 0.0117  -0.0356 -0.0154 272 ILE C C   
5896  O O   . ILE C  272 ? 0.5859 0.7001 0.5014 0.0148  -0.0360 -0.0129 272 ILE C O   
5897  C CB  . ILE C  272 ? 0.4707 0.5759 0.3875 0.0105  -0.0385 -0.0161 272 ILE C CB  
5898  C CG1 . ILE C  272 ? 0.5505 0.6491 0.4694 0.0087  -0.0394 -0.0170 272 ILE C CG1 
5899  C CG2 . ILE C  272 ? 0.6232 0.7354 0.5360 0.0091  -0.0390 -0.0177 272 ILE C CG2 
5900  C CD1 . ILE C  272 ? 0.6633 0.7618 0.5814 0.0083  -0.0415 -0.0173 272 ILE C CD1 
5901  N N   . ILE C  273 ? 0.6031 0.7205 0.5137 0.0093  -0.0345 -0.0173 273 ILE C N   
5902  C CA  . ILE C  273 ? 0.6410 0.7666 0.5485 0.0100  -0.0342 -0.0166 273 ILE C CA  
5903  C C   . ILE C  273 ? 0.7181 0.8499 0.6230 0.0092  -0.0359 -0.0174 273 ILE C C   
5904  O O   . ILE C  273 ? 0.6525 0.7863 0.5548 0.0059  -0.0357 -0.0201 273 ILE C O   
5905  C CB  . ILE C  273 ? 0.6532 0.7810 0.5577 0.0076  -0.0321 -0.0182 273 ILE C CB  
5906  C CG1 . ILE C  273 ? 0.7227 0.8443 0.6299 0.0085  -0.0302 -0.0173 273 ILE C CG1 
5907  C CG2 . ILE C  273 ? 0.8355 0.9726 0.7365 0.0082  -0.0322 -0.0172 273 ILE C CG2 
5908  C CD1 . ILE C  273 ? 0.9117 1.0251 0.8218 0.0068  -0.0294 -0.0189 273 ILE C CD1 
5909  N N   . SER C  274 ? 0.8251 0.9597 0.7312 0.0121  -0.0371 -0.0151 274 SER C N   
5910  C CA  . SER C  274 ? 0.7983 0.9382 0.7028 0.0117  -0.0386 -0.0156 274 SER C CA  
5911  C C   . SER C  274 ? 0.8409 0.9866 0.7462 0.0152  -0.0391 -0.0125 274 SER C C   
5912  O O   . SER C  274 ? 0.9082 1.0518 0.8161 0.0183  -0.0386 -0.0099 274 SER C O   
5913  C CB  . SER C  274 ? 0.7255 0.8598 0.6317 0.0110  -0.0398 -0.0167 274 SER C CB  
5914  O OG  . SER C  274 ? 0.8209 0.9594 0.7265 0.0117  -0.0410 -0.0164 274 SER C OG  
5915  N N   . ASP C  275 ? 1.0612 1.2143 0.9647 0.0146  -0.0400 -0.0128 275 ASP C N   
5916  C CA  . ASP C  275 ? 1.0442 1.2032 0.9489 0.0178  -0.0404 -0.0098 275 ASP C CA  
5917  C C   . ASP C  275 ? 0.9446 1.1001 0.8518 0.0194  -0.0412 -0.0093 275 ASP C C   
5918  O O   . ASP C  275 ? 1.1144 1.2717 1.0240 0.0227  -0.0411 -0.0065 275 ASP C O   
5919  C CB  . ASP C  275 ? 1.3163 1.4856 1.2181 0.0165  -0.0410 -0.0101 275 ASP C CB  
5920  C CG  . ASP C  275 ? 1.5288 1.7022 1.4274 0.0145  -0.0401 -0.0108 275 ASP C CG  
5921  O OD1 . ASP C  275 ? 1.6956 1.8694 1.5913 0.0106  -0.0400 -0.0141 275 ASP C OD1 
5922  O OD2 . ASP C  275 ? 1.3270 1.5031 1.2260 0.0167  -0.0395 -0.0080 275 ASP C OD2 
5923  N N   . THR C  276 ? 0.8720 1.0225 0.7787 0.0169  -0.0419 -0.0120 276 THR C N   
5924  C CA  . THR C  276 ? 0.8252 0.9721 0.7336 0.0176  -0.0426 -0.0121 276 THR C CA  
5925  C C   . THR C  276 ? 0.8366 0.9796 0.7484 0.0213  -0.0422 -0.0093 276 THR C C   
5926  O O   . THR C  276 ? 0.7297 0.8684 0.6431 0.0224  -0.0415 -0.0082 276 THR C O   
5927  C CB  . THR C  276 ? 0.7332 0.8729 0.6408 0.0146  -0.0432 -0.0148 276 THR C CB  
5928  O OG1 . THR C  276 ? 0.7448 0.8878 0.6494 0.0112  -0.0433 -0.0175 276 THR C OG1 
5929  C CG2 . THR C  276 ? 0.7230 0.8592 0.6317 0.0150  -0.0441 -0.0150 276 THR C CG2 
5930  N N   . PRO C  277 ? 0.8623 1.0069 0.7754 0.0231  -0.0423 -0.0082 277 PRO C N   
5931  C CA  . PRO C  277 ? 0.8108 0.9520 0.7273 0.0264  -0.0416 -0.0058 277 PRO C CA  
5932  C C   . PRO C  277 ? 0.8158 0.9473 0.7336 0.0258  -0.0418 -0.0066 277 PRO C C   
5933  O O   . PRO C  277 ? 0.8965 1.0242 0.8130 0.0231  -0.0429 -0.0090 277 PRO C O   
5934  C CB  . PRO C  277 ? 0.9267 1.0712 0.8436 0.0273  -0.0416 -0.0054 277 PRO C CB  
5935  C CG  . PRO C  277 ? 1.1172 1.2697 1.0316 0.0254  -0.0422 -0.0066 277 PRO C CG  
5936  C CD  . PRO C  277 ? 0.8996 1.0499 0.8113 0.0219  -0.0429 -0.0093 277 PRO C CD  
5937  N N   . VAL C  278 ? 0.7538 0.8817 0.6744 0.0283  -0.0409 -0.0046 278 VAL C N   
5938  C CA  . VAL C  278 ? 0.8201 0.9394 0.7425 0.0280  -0.0412 -0.0050 278 VAL C CA  
5939  C C   . VAL C  278 ? 0.8341 0.9514 0.7574 0.0288  -0.0412 -0.0049 278 VAL C C   
5940  O O   . VAL C  278 ? 0.9575 1.0792 0.8817 0.0311  -0.0401 -0.0034 278 VAL C O   
5941  C CB  . VAL C  278 ? 0.8234 0.9396 0.7487 0.0304  -0.0401 -0.0028 278 VAL C CB  
5942  C CG1 . VAL C  278 ? 1.0738 1.1943 1.0009 0.0341  -0.0386 0.0001  278 VAL C CG1 
5943  C CG2 . VAL C  278 ? 0.5789 0.6866 0.5064 0.0300  -0.0405 -0.0032 278 VAL C CG2 
5944  N N   . HIS C  279 ? 0.8552 0.9661 0.7783 0.0268  -0.0422 -0.0066 279 HIS C N   
5945  C CA  . HIS C  279 ? 0.8940 1.0027 0.8171 0.0267  -0.0421 -0.0071 279 HIS C CA  
5946  C C   . HIS C  279 ? 0.9214 1.0220 0.8459 0.0261  -0.0425 -0.0074 279 HIS C C   
5947  O O   . HIS C  279 ? 0.9863 1.0826 0.9113 0.0248  -0.0435 -0.0077 279 HIS C O   
5948  C CB  . HIS C  279 ? 1.0340 1.1449 0.9539 0.0239  -0.0432 -0.0094 279 HIS C CB  
5949  C CG  . HIS C  279 ? 1.1950 1.3129 1.1144 0.0252  -0.0423 -0.0089 279 HIS C CG  
5950  N ND1 . HIS C  279 ? 1.2334 1.3510 1.1530 0.0256  -0.0416 -0.0092 279 HIS C ND1 
5951  C CD2 . HIS C  279 ? 1.1841 1.3098 1.1031 0.0261  -0.0419 -0.0081 279 HIS C CD2 
5952  C CE1 . HIS C  279 ? 1.3446 1.4695 1.2643 0.0269  -0.0408 -0.0084 279 HIS C CE1 
5953  N NE2 . HIS C  279 ? 1.2201 1.3503 1.1394 0.0272  -0.0411 -0.0076 279 HIS C NE2 
5954  N N   . ASP C  280 ? 1.0248 1.1235 0.9500 0.0269  -0.0417 -0.0073 280 ASP C N   
5955  C CA  . ASP C  280 ? 1.1305 1.2219 1.0563 0.0257  -0.0422 -0.0080 280 ASP C CA  
5956  C C   . ASP C  280 ? 1.1789 1.2679 1.1014 0.0221  -0.0439 -0.0104 280 ASP C C   
5957  O O   . ASP C  280 ? 1.5332 1.6215 1.4545 0.0216  -0.0434 -0.0113 280 ASP C O   
5958  C CB  . ASP C  280 ? 1.3260 1.4160 1.2540 0.0281  -0.0400 -0.0069 280 ASP C CB  
5959  C CG  . ASP C  280 ? 1.4806 1.5633 1.4087 0.0264  -0.0404 -0.0079 280 ASP C CG  
5960  O OD1 . ASP C  280 ? 1.4749 1.5536 1.4024 0.0240  -0.0425 -0.0088 280 ASP C OD1 
5961  O OD2 . ASP C  280 ? 1.5035 1.5844 1.4324 0.0273  -0.0386 -0.0079 280 ASP C OD2 
5962  N N   . CYS C  281 ? 1.0190 1.1069 0.9403 0.0197  -0.0458 -0.0114 281 CYS C N   
5963  C CA  . CYS C  281 ? 1.0717 1.1574 0.9900 0.0162  -0.0475 -0.0135 281 CYS C CA  
5964  C C   . CYS C  281 ? 0.9376 1.0186 0.8563 0.0140  -0.0494 -0.0136 281 CYS C C   
5965  O O   . CYS C  281 ? 0.8888 0.9696 0.8098 0.0150  -0.0493 -0.0125 281 CYS C O   
5966  C CB  . CYS C  281 ? 0.9878 1.0791 0.9034 0.0153  -0.0475 -0.0147 281 CYS C CB  
5967  S SG  . CYS C  281 ? 1.4457 1.5422 1.3617 0.0158  -0.0474 -0.0142 281 CYS C SG  
5968  N N   . ASN C  282 ? 0.8769 0.9543 0.7937 0.0111  -0.0511 -0.0149 282 ASN C N   
5969  C CA  . ASN C  282 ? 0.7348 0.8081 0.6521 0.0088  -0.0530 -0.0149 282 ASN C CA  
5970  C C   . ASN C  282 ? 0.8463 0.9217 0.7616 0.0068  -0.0537 -0.0160 282 ASN C C   
5971  O O   . ASN C  282 ? 0.9334 1.0110 0.8456 0.0055  -0.0538 -0.0174 282 ASN C O   
5972  C CB  . ASN C  282 ? 0.9837 1.0518 0.8999 0.0066  -0.0545 -0.0153 282 ASN C CB  
5973  C CG  . ASN C  282 ? 1.2159 1.2818 1.1336 0.0081  -0.0535 -0.0147 282 ASN C CG  
5974  O OD1 . ASN C  282 ? 1.1349 1.2017 1.0555 0.0109  -0.0520 -0.0133 282 ASN C OD1 
5975  N ND2 . ASN C  282 ? 1.3952 1.4580 1.3106 0.0062  -0.0541 -0.0157 282 ASN C ND2 
5976  N N   . THR C  283 ? 0.8419 0.9163 0.7592 0.0064  -0.0542 -0.0154 283 THR C N   
5977  C CA  . THR C  283 ? 0.7925 0.8679 0.7082 0.0042  -0.0546 -0.0165 283 THR C CA  
5978  C C   . THR C  283 ? 0.5942 0.6652 0.5125 0.0029  -0.0557 -0.0155 283 THR C C   
5979  O O   . THR C  283 ? 0.6751 0.7436 0.5968 0.0041  -0.0558 -0.0140 283 THR C O   
5980  C CB  . THR C  283 ? 0.6611 0.7422 0.5762 0.0052  -0.0529 -0.0171 283 THR C CB  
5981  O OG1 . THR C  283 ? 0.5524 0.6343 0.4656 0.0026  -0.0532 -0.0186 283 THR C OG1 
5982  C CG2 . THR C  283 ? 0.5851 0.6661 0.5035 0.0071  -0.0519 -0.0157 283 THR C CG2 
5983  N N   . THR C  284 ? 0.5107 0.5809 0.4278 0.0003  -0.0565 -0.0164 284 THR C N   
5984  C CA  . THR C  284 ? 0.6692 0.7354 0.5892 -0.0009 -0.0573 -0.0152 284 THR C CA  
5985  C C   . THR C  284 ? 0.6427 0.7109 0.5635 -0.0011 -0.0557 -0.0159 284 THR C C   
5986  O O   . THR C  284 ? 0.5905 0.6559 0.5144 -0.0016 -0.0556 -0.0149 284 THR C O   
5987  C CB  . THR C  284 ? 0.6712 0.7343 0.5899 -0.0038 -0.0594 -0.0153 284 THR C CB  
5988  O OG1 . THR C  284 ? 0.6612 0.7204 0.5836 -0.0046 -0.0603 -0.0135 284 THR C OG1 
5989  C CG2 . THR C  284 ? 0.6315 0.6970 0.5467 -0.0056 -0.0589 -0.0172 284 THR C CG2 
5990  N N   . CYS C  285 ? 0.5676 0.6408 0.4856 -0.0007 -0.0542 -0.0175 285 CYS C N   
5991  C CA  . CYS C  285 ? 0.5132 0.5889 0.4312 -0.0012 -0.0524 -0.0186 285 CYS C CA  
5992  C C   . CYS C  285 ? 0.4748 0.5565 0.3910 0.0005  -0.0509 -0.0193 285 CYS C C   
5993  O O   . CYS C  285 ? 0.5441 0.6293 0.4576 0.0008  -0.0511 -0.0201 285 CYS C O   
5994  C CB  . CYS C  285 ? 0.4606 0.5362 0.3762 -0.0042 -0.0525 -0.0202 285 CYS C CB  
5995  S SG  . CYS C  285 ? 0.9026 0.9813 0.8177 -0.0054 -0.0500 -0.0221 285 CYS C SG  
5996  N N   . GLN C  286 ? 0.5688 0.6517 0.4867 0.0017  -0.0493 -0.0189 286 GLN C N   
5997  C CA  . GLN C  286 ? 0.4678 0.5565 0.3842 0.0035  -0.0479 -0.0191 286 GLN C CA  
5998  C C   . GLN C  286 ? 0.4848 0.5770 0.3999 0.0022  -0.0462 -0.0207 286 GLN C C   
5999  O O   . GLN C  286 ? 0.6082 0.6975 0.5251 0.0013  -0.0451 -0.0208 286 GLN C O   
6000  C CB  . GLN C  286 ? 0.4360 0.5238 0.3553 0.0065  -0.0475 -0.0170 286 GLN C CB  
6001  C CG  . GLN C  286 ? 0.4808 0.5747 0.3989 0.0087  -0.0463 -0.0166 286 GLN C CG  
6002  C CD  . GLN C  286 ? 0.6357 0.7334 0.5515 0.0093  -0.0470 -0.0169 286 GLN C CD  
6003  O OE1 . GLN C  286 ? 0.6727 0.7678 0.5893 0.0101  -0.0479 -0.0161 286 GLN C OE1 
6004  N NE2 . GLN C  286 ? 0.5423 0.6463 0.4554 0.0087  -0.0464 -0.0181 286 GLN C NE2 
6005  N N   . THR C  287 ? 0.5205 0.6190 0.4323 0.0019  -0.0457 -0.0220 287 THR C N   
6006  C CA  . THR C  287 ? 0.5109 0.6136 0.4208 0.0004  -0.0440 -0.0236 287 THR C CA  
6007  C C   . THR C  287 ? 0.6033 0.7125 0.5122 0.0026  -0.0434 -0.0228 287 THR C C   
6008  O O   . THR C  287 ? 0.6375 0.7484 0.5468 0.0050  -0.0442 -0.0212 287 THR C O   
6009  C CB  . THR C  287 ? 0.5626 0.6680 0.4694 -0.0025 -0.0441 -0.0261 287 THR C CB  
6010  O OG1 . THR C  287 ? 0.5615 0.6738 0.4658 -0.0018 -0.0445 -0.0265 287 THR C OG1 
6011  C CG2 . THR C  287 ? 0.4393 0.5394 0.3465 -0.0039 -0.0455 -0.0263 287 THR C CG2 
6012  N N   . PRO C  288 ? 0.6190 0.7317 0.5265 0.0017  -0.0418 -0.0237 288 PRO C N   
6013  C CA  . PRO C  288 ? 0.5941 0.7136 0.5003 0.0035  -0.0412 -0.0227 288 PRO C CA  
6014  C C   . PRO C  288 ? 0.5736 0.6998 0.4777 0.0039  -0.0422 -0.0229 288 PRO C C   
6015  O O   . PRO C  288 ? 0.5283 0.6594 0.4325 0.0063  -0.0422 -0.0210 288 PRO C O   
6016  C CB  . PRO C  288 ? 0.6734 0.7952 0.5775 0.0011  -0.0393 -0.0246 288 PRO C CB  
6017  C CG  . PRO C  288 ? 0.5260 0.6402 0.4322 -0.0005 -0.0385 -0.0255 288 PRO C CG  
6018  C CD  . PRO C  288 ? 0.4884 0.5983 0.3958 -0.0010 -0.0402 -0.0255 288 PRO C CD  
6019  N N   . LYS C  289 ? 0.6272 0.7535 0.5296 0.0015  -0.0429 -0.0249 289 LYS C N   
6020  C CA  . LYS C  289 ? 0.5923 0.7250 0.4929 0.0015  -0.0436 -0.0253 289 LYS C CA  
6021  C C   . LYS C  289 ? 0.5631 0.6934 0.4654 0.0037  -0.0449 -0.0237 289 LYS C C   
6022  O O   . LYS C  289 ? 0.6859 0.8213 0.5879 0.0051  -0.0452 -0.0229 289 LYS C O   
6023  C CB  . LYS C  289 ? 0.6083 0.7425 0.5062 -0.0022 -0.0435 -0.0283 289 LYS C CB  
6024  C CG  . LYS C  289 ? 0.7613 0.8980 0.6573 -0.0048 -0.0420 -0.0302 289 LYS C CG  
6025  C CD  . LYS C  289 ? 0.7406 0.8769 0.6345 -0.0086 -0.0416 -0.0334 289 LYS C CD  
6026  C CE  . LYS C  289 ? 0.9526 1.0962 0.8442 -0.0095 -0.0423 -0.0344 289 LYS C CE  
6027  N NZ  . LYS C  289 ? 1.0247 1.1685 0.9141 -0.0135 -0.0415 -0.0377 289 LYS C NZ  
6028  N N   . GLY C  290 ? 0.5417 0.6642 0.4458 0.0037  -0.0454 -0.0234 290 GLY C N   
6029  C CA  . GLY C  290 ? 0.5670 0.6864 0.4722 0.0051  -0.0465 -0.0223 290 GLY C CA  
6030  C C   . GLY C  290 ? 0.5502 0.6615 0.4565 0.0037  -0.0473 -0.0226 290 GLY C C   
6031  O O   . GLY C  290 ? 0.6000 0.7084 0.5063 0.0016  -0.0471 -0.0237 290 GLY C O   
6032  N N   . ALA C  291 ? 0.6011 0.7088 0.5084 0.0048  -0.0482 -0.0216 291 ALA C N   
6033  C CA  . ALA C  291 ? 0.5488 0.6492 0.4571 0.0035  -0.0494 -0.0216 291 ALA C CA  
6034  C C   . ALA C  291 ? 0.6007 0.7000 0.5065 0.0005  -0.0502 -0.0235 291 ALA C C   
6035  O O   . ALA C  291 ? 0.5691 0.6728 0.4725 -0.0001 -0.0500 -0.0247 291 ALA C O   
6036  C CB  . ALA C  291 ? 0.4603 0.5573 0.3705 0.0055  -0.0500 -0.0198 291 ALA C CB  
6037  N N   . ILE C  292 ? 0.6261 0.7195 0.5326 -0.0013 -0.0512 -0.0235 292 ILE C N   
6038  C CA  . ILE C  292 ? 0.6261 0.7177 0.5303 -0.0041 -0.0520 -0.0249 292 ILE C CA  
6039  C C   . ILE C  292 ? 0.8098 0.8960 0.7142 -0.0045 -0.0537 -0.0240 292 ILE C C   
6040  O O   . ILE C  292 ? 0.7727 0.8541 0.6795 -0.0046 -0.0545 -0.0226 292 ILE C O   
6041  C CB  . ILE C  292 ? 0.6260 0.7160 0.5304 -0.0064 -0.0515 -0.0259 292 ILE C CB  
6042  C CG1 . ILE C  292 ? 0.5238 0.6194 0.4273 -0.0066 -0.0497 -0.0273 292 ILE C CG1 
6043  C CG2 . ILE C  292 ? 0.7668 0.8547 0.6690 -0.0092 -0.0523 -0.0271 292 ILE C CG2 
6044  C CD1 . ILE C  292 ? 0.6521 0.7460 0.5557 -0.0091 -0.0486 -0.0286 292 ILE C CD1 
6045  N N   . ASN C  293 ? 1.0953 1.1824 0.9972 -0.0051 -0.0541 -0.0248 293 ASN C N   
6046  C CA  . ASN C  293 ? 1.2266 1.3089 1.1277 -0.0061 -0.0557 -0.0243 293 ASN C CA  
6047  C C   . ASN C  293 ? 1.2158 1.2963 1.1142 -0.0093 -0.0564 -0.0256 293 ASN C C   
6048  O O   . ASN C  293 ? 1.3571 1.4400 1.2527 -0.0102 -0.0561 -0.0270 293 ASN C O   
6049  C CB  . ASN C  293 ? 1.3803 1.4642 1.2802 -0.0047 -0.0552 -0.0244 293 ASN C CB  
6050  C CG  . ASN C  293 ? 1.5424 1.6213 1.4409 -0.0060 -0.0566 -0.0242 293 ASN C CG  
6051  O OD1 . ASN C  293 ? 1.4953 1.5696 1.3941 -0.0078 -0.0582 -0.0236 293 ASN C OD1 
6052  N ND2 . ASN C  293 ? 1.4586 1.5384 1.3556 -0.0053 -0.0559 -0.0248 293 ASN C ND2 
6053  N N   . THR C  294 ? 0.9437 1.0204 0.8436 -0.0108 -0.0573 -0.0248 294 THR C N   
6054  C CA  . THR C  294 ? 1.2333 1.3087 1.1311 -0.0137 -0.0576 -0.0258 294 THR C CA  
6055  C C   . THR C  294 ? 1.1511 1.2208 1.0499 -0.0154 -0.0594 -0.0242 294 THR C C   
6056  O O   . THR C  294 ? 0.9651 1.0320 0.8672 -0.0145 -0.0603 -0.0223 294 THR C O   
6057  C CB  . THR C  294 ? 1.1287 1.2072 1.0268 -0.0143 -0.0559 -0.0272 294 THR C CB  
6058  O OG1 . THR C  294 ? 1.0558 1.1339 0.9515 -0.0170 -0.0558 -0.0286 294 THR C OG1 
6059  C CG2 . THR C  294 ? 0.9409 1.0169 0.8428 -0.0138 -0.0556 -0.0258 294 THR C CG2 
6060  N N   . SER C  295 ? 0.8871 0.9554 0.7834 -0.0180 -0.0600 -0.0249 295 SER C N   
6061  C CA  . SER C  295 ? 0.8910 0.9546 0.7883 -0.0199 -0.0617 -0.0232 295 SER C CA  
6062  C C   . SER C  295 ? 0.7650 0.8285 0.6630 -0.0214 -0.0604 -0.0238 295 SER C C   
6063  O O   . SER C  295 ? 0.7408 0.8007 0.6409 -0.0226 -0.0612 -0.0221 295 SER C O   
6064  C CB  . SER C  295 ? 0.9311 0.9925 0.8246 -0.0218 -0.0634 -0.0232 295 SER C CB  
6065  O OG  . SER C  295 ? 1.2732 1.3311 1.1678 -0.0216 -0.0655 -0.0212 295 SER C OG  
6066  N N   . LEU C  296 ? 0.6718 0.7395 0.5681 -0.0215 -0.0584 -0.0262 296 LEU C N   
6067  C CA  . LEU C  296 ? 0.6312 0.6993 0.5277 -0.0232 -0.0567 -0.0274 296 LEU C CA  
6068  C C   . LEU C  296 ? 0.5608 0.6270 0.4617 -0.0226 -0.0557 -0.0262 296 LEU C C   
6069  O O   . LEU C  296 ? 0.5442 0.6111 0.4477 -0.0205 -0.0555 -0.0254 296 LEU C O   
6070  C CB  . LEU C  296 ? 0.6319 0.7055 0.5258 -0.0234 -0.0548 -0.0303 296 LEU C CB  
6071  C CG  . LEU C  296 ? 0.5830 0.6588 0.4728 -0.0239 -0.0554 -0.0316 296 LEU C CG  
6072  C CD1 . LEU C  296 ? 0.6537 0.7353 0.5416 -0.0242 -0.0535 -0.0342 296 LEU C CD1 
6073  C CD2 . LEU C  296 ? 0.6642 0.7360 0.5518 -0.0263 -0.0566 -0.0311 296 LEU C CD2 
6074  N N   . PRO C  297 ? 0.4809 0.5445 0.3830 -0.0245 -0.0548 -0.0260 297 PRO C N   
6075  C CA  . PRO C  297 ? 0.5307 0.5917 0.4374 -0.0243 -0.0535 -0.0248 297 PRO C CA  
6076  C C   . PRO C  297 ? 0.6405 0.7050 0.5479 -0.0237 -0.0507 -0.0269 297 PRO C C   
6077  O O   . PRO C  297 ? 0.5804 0.6433 0.4916 -0.0228 -0.0495 -0.0259 297 PRO C O   
6078  C CB  . PRO C  297 ? 0.5177 0.5755 0.4248 -0.0267 -0.0530 -0.0243 297 PRO C CB  
6079  C CG  . PRO C  297 ? 0.7158 0.7737 0.6186 -0.0281 -0.0549 -0.0246 297 PRO C CG  
6080  C CD  . PRO C  297 ? 0.5916 0.6542 0.4909 -0.0270 -0.0549 -0.0268 297 PRO C CD  
6081  N N   . PHE C  298 ? 0.5563 0.6254 0.4599 -0.0243 -0.0495 -0.0297 298 PHE C N   
6082  C CA  . PHE C  298 ? 0.5516 0.6243 0.4552 -0.0244 -0.0469 -0.0319 298 PHE C CA  
6083  C C   . PHE C  298 ? 0.5045 0.5835 0.4053 -0.0231 -0.0469 -0.0335 298 PHE C C   
6084  O O   . PHE C  298 ? 0.5960 0.6772 0.4941 -0.0229 -0.0483 -0.0338 298 PHE C O   
6085  C CB  . PHE C  298 ? 0.5254 0.5980 0.4280 -0.0273 -0.0446 -0.0341 298 PHE C CB  
6086  C CG  . PHE C  298 ? 0.5373 0.6040 0.4424 -0.0286 -0.0446 -0.0323 298 PHE C CG  
6087  C CD1 . PHE C  298 ? 0.4232 0.4859 0.3331 -0.0282 -0.0434 -0.0307 298 PHE C CD1 
6088  C CD2 . PHE C  298 ? 0.5255 0.5906 0.4284 -0.0303 -0.0457 -0.0322 298 PHE C CD2 
6089  C CE1 . PHE C  298 ? 0.5181 0.5756 0.4308 -0.0293 -0.0434 -0.0286 298 PHE C CE1 
6090  C CE2 . PHE C  298 ? 0.6046 0.6645 0.5100 -0.0315 -0.0458 -0.0302 298 PHE C CE2 
6091  C CZ  . PHE C  298 ? 0.5159 0.5721 0.4263 -0.0309 -0.0447 -0.0283 298 PHE C CZ  
6092  N N   . GLN C  299 ? 0.5034 0.5853 0.4051 -0.0222 -0.0452 -0.0342 299 GLN C N   
6093  C CA  . GLN C  299 ? 0.4664 0.5548 0.3660 -0.0208 -0.0451 -0.0353 299 GLN C CA  
6094  C C   . GLN C  299 ? 0.5111 0.6034 0.4098 -0.0221 -0.0426 -0.0376 299 GLN C C   
6095  O O   . GLN C  299 ? 0.8824 0.9717 0.7831 -0.0230 -0.0407 -0.0378 299 GLN C O   
6096  C CB  . GLN C  299 ? 0.3843 0.4723 0.2860 -0.0177 -0.0463 -0.0330 299 GLN C CB  
6097  C CG  . GLN C  299 ? 0.5097 0.5939 0.4153 -0.0168 -0.0453 -0.0315 299 GLN C CG  
6098  C CD  . GLN C  299 ? 0.5565 0.6448 0.4620 -0.0156 -0.0437 -0.0322 299 GLN C CD  
6099  O OE1 . GLN C  299 ? 0.5186 0.6128 0.4212 -0.0161 -0.0429 -0.0340 299 GLN C OE1 
6100  N NE2 . GLN C  299 ? 0.4917 0.5771 0.4006 -0.0142 -0.0431 -0.0306 299 GLN C NE2 
6101  N N   . ASN C  300 ? 0.5500 0.6489 0.4457 -0.0224 -0.0423 -0.0394 300 ASN C N   
6102  C CA  . ASN C  300 ? 0.5316 0.6352 0.4259 -0.0239 -0.0401 -0.0418 300 ASN C CA  
6103  C C   . ASN C  300 ? 0.4247 0.5348 0.3182 -0.0218 -0.0404 -0.0413 300 ASN C C   
6104  O O   . ASN C  300 ? 0.5452 0.6611 0.4365 -0.0231 -0.0392 -0.0432 300 ASN C O   
6105  C CB  . ASN C  300 ? 0.4143 0.5208 0.3057 -0.0271 -0.0391 -0.0447 300 ASN C CB  
6106  C CG  . ASN C  300 ? 0.5346 0.6462 0.4236 -0.0265 -0.0408 -0.0449 300 ASN C CG  
6107  O OD1 . ASN C  300 ? 0.6054 0.7177 0.4951 -0.0238 -0.0426 -0.0429 300 ASN C OD1 
6108  N ND2 . ASN C  300 ? 0.4952 0.6106 0.3818 -0.0291 -0.0399 -0.0475 300 ASN C ND2 
6109  N N   . ILE C  301 ? 0.4680 0.5769 0.3630 -0.0187 -0.0421 -0.0387 301 ILE C N   
6110  C CA  . ILE C  301 ? 0.4953 0.6100 0.3901 -0.0162 -0.0425 -0.0377 301 ILE C CA  
6111  C C   . ILE C  301 ? 0.5500 0.6655 0.4456 -0.0158 -0.0408 -0.0376 301 ILE C C   
6112  O O   . ILE C  301 ? 0.6228 0.7447 0.5165 -0.0163 -0.0400 -0.0386 301 ILE C O   
6113  C CB  . ILE C  301 ? 0.6172 0.7298 0.5137 -0.0130 -0.0444 -0.0349 301 ILE C CB  
6114  C CG1 . ILE C  301 ? 0.4368 0.5494 0.3318 -0.0134 -0.0458 -0.0352 301 ILE C CG1 
6115  C CG2 . ILE C  301 ? 0.4696 0.5875 0.3663 -0.0102 -0.0444 -0.0335 301 ILE C CG2 
6116  C CD1 . ILE C  301 ? 0.6438 0.7537 0.5403 -0.0108 -0.0474 -0.0329 301 ILE C CD1 
6117  N N   . HIS C  302 ? 0.5635 0.6727 0.4621 -0.0151 -0.0404 -0.0362 302 HIS C N   
6118  C CA  . HIS C  302 ? 0.5752 0.6843 0.4749 -0.0145 -0.0387 -0.0359 302 HIS C CA  
6119  C C   . HIS C  302 ? 0.5739 0.6752 0.4769 -0.0150 -0.0376 -0.0353 302 HIS C C   
6120  O O   . HIS C  302 ? 0.6041 0.7001 0.5096 -0.0141 -0.0390 -0.0336 302 HIS C O   
6121  C CB  . HIS C  302 ? 0.4470 0.5586 0.3476 -0.0110 -0.0397 -0.0334 302 HIS C CB  
6122  C CG  . HIS C  302 ? 0.6003 0.7150 0.5005 -0.0106 -0.0380 -0.0335 302 HIS C CG  
6123  N ND1 . HIS C  302 ? 0.6129 0.7227 0.5155 -0.0102 -0.0365 -0.0328 302 HIS C ND1 
6124  C CD2 . HIS C  302 ? 0.6290 0.7512 0.5264 -0.0106 -0.0375 -0.0341 302 HIS C CD2 
6125  C CE1 . HIS C  302 ? 0.6711 0.7851 0.5723 -0.0101 -0.0350 -0.0331 302 HIS C CE1 
6126  N NE2 . HIS C  302 ? 0.5491 0.6708 0.4470 -0.0103 -0.0357 -0.0338 302 HIS C NE2 
6127  N N   . PRO C  303 ? 0.6078 0.7086 0.5109 -0.0166 -0.0350 -0.0367 303 PRO C N   
6128  C CA  . PRO C  303 ? 0.4909 0.5846 0.3976 -0.0172 -0.0333 -0.0362 303 PRO C CA  
6129  C C   . PRO C  303 ? 0.5404 0.6307 0.4509 -0.0141 -0.0340 -0.0332 303 PRO C C   
6130  O O   . PRO C  303 ? 0.4786 0.5629 0.3929 -0.0135 -0.0346 -0.0314 303 PRO C O   
6131  C CB  . PRO C  303 ? 0.4141 0.5097 0.3192 -0.0196 -0.0300 -0.0388 303 PRO C CB  
6132  C CG  . PRO C  303 ? 0.6907 0.7939 0.5910 -0.0213 -0.0302 -0.0412 303 PRO C CG  
6133  C CD  . PRO C  303 ? 0.6681 0.7753 0.5677 -0.0184 -0.0332 -0.0391 303 PRO C CD  
6134  N N   . ILE C  304 ? 0.4580 0.5524 0.3675 -0.0121 -0.0340 -0.0325 304 ILE C N   
6135  C CA  . ILE C  304 ? 0.4776 0.5691 0.3905 -0.0091 -0.0345 -0.0297 304 ILE C CA  
6136  C C   . ILE C  304 ? 0.5024 0.5931 0.4163 -0.0068 -0.0376 -0.0275 304 ILE C C   
6137  O O   . ILE C  304 ? 0.6988 0.7945 0.6101 -0.0060 -0.0390 -0.0276 304 ILE C O   
6138  C CB  . ILE C  304 ? 0.4500 0.5460 0.3614 -0.0077 -0.0333 -0.0295 304 ILE C CB  
6139  C CG1 . ILE C  304 ? 0.3407 0.4354 0.2520 -0.0097 -0.0300 -0.0312 304 ILE C CG1 
6140  C CG2 . ILE C  304 ? 0.6260 0.7200 0.5405 -0.0041 -0.0344 -0.0264 304 ILE C CG2 
6141  C CD1 . ILE C  304 ? 0.6249 0.7219 0.5329 -0.0135 -0.0284 -0.0346 304 ILE C CD1 
6142  N N   . THR C  305 ? 0.4657 0.5504 0.3837 -0.0058 -0.0385 -0.0255 305 THR C N   
6143  C CA  . THR C  305 ? 0.3922 0.4753 0.3111 -0.0044 -0.0413 -0.0237 305 THR C CA  
6144  C C   . THR C  305 ? 0.5693 0.6476 0.4928 -0.0022 -0.0419 -0.0210 305 THR C C   
6145  O O   . THR C  305 ? 0.6105 0.6852 0.5372 -0.0024 -0.0404 -0.0205 305 THR C O   
6146  C CB  . THR C  305 ? 0.4972 0.5777 0.4155 -0.0066 -0.0425 -0.0244 305 THR C CB  
6147  O OG1 . THR C  305 ? 0.6769 0.7600 0.5926 -0.0062 -0.0446 -0.0245 305 THR C OG1 
6148  C CG2 . THR C  305 ? 0.4753 0.5491 0.3981 -0.0067 -0.0433 -0.0224 305 THR C CG2 
6149  N N   . ILE C  306 ? 0.4467 0.5248 0.3706 -0.0003 -0.0440 -0.0195 306 ILE C N   
6150  C CA  . ILE C  306 ? 0.5072 0.5808 0.4353 0.0015  -0.0449 -0.0170 306 ILE C CA  
6151  C C   . ILE C  306 ? 0.5668 0.6377 0.4954 0.0012  -0.0476 -0.0160 306 ILE C C   
6152  O O   . ILE C  306 ? 0.4926 0.5661 0.4180 0.0013  -0.0487 -0.0166 306 ILE C O   
6153  C CB  . ILE C  306 ? 0.3973 0.4732 0.3260 0.0044  -0.0442 -0.0158 306 ILE C CB  
6154  C CG1 . ILE C  306 ? 0.4949 0.5740 0.4224 0.0044  -0.0416 -0.0168 306 ILE C CG1 
6155  C CG2 . ILE C  306 ? 0.3633 0.4343 0.2968 0.0060  -0.0448 -0.0134 306 ILE C CG2 
6156  C CD1 . ILE C  306 ? 0.4665 0.5473 0.3949 0.0073  -0.0407 -0.0153 306 ILE C CD1 
6157  N N   . GLY C  307 ? 0.5668 0.6325 0.4993 0.0009  -0.0486 -0.0143 307 GLY C N   
6158  C CA  . GLY C  307 ? 0.5021 0.5650 0.4350 0.0003  -0.0513 -0.0132 307 GLY C CA  
6159  C C   . GLY C  307 ? 0.5879 0.6481 0.5211 -0.0023 -0.0521 -0.0133 307 GLY C C   
6160  O O   . GLY C  307 ? 0.7174 0.7762 0.6526 -0.0033 -0.0506 -0.0135 307 GLY C O   
6161  N N   . LYS C  308 ? 0.6154 0.6746 0.5467 -0.0035 -0.0545 -0.0131 308 LYS C N   
6162  C CA  . LYS C  308 ? 0.5977 0.6547 0.5287 -0.0061 -0.0555 -0.0131 308 LYS C CA  
6163  C C   . LYS C  308 ? 0.5467 0.6071 0.4725 -0.0075 -0.0549 -0.0156 308 LYS C C   
6164  O O   . LYS C  308 ? 0.6543 0.7160 0.5768 -0.0078 -0.0564 -0.0161 308 LYS C O   
6165  C CB  . LYS C  308 ? 0.6037 0.6574 0.5357 -0.0068 -0.0585 -0.0111 308 LYS C CB  
6166  C CG  . LYS C  308 ? 0.8940 0.9455 0.8258 -0.0094 -0.0597 -0.0106 308 LYS C CG  
6167  C CD  . LYS C  308 ? 0.9862 1.0349 0.9185 -0.0104 -0.0629 -0.0086 308 LYS C CD  
6168  C CE  . LYS C  308 ? 0.9985 1.0444 0.9366 -0.0094 -0.0638 -0.0058 308 LYS C CE  
6169  N NZ  . LYS C  308 ? 1.0830 1.1259 1.0227 -0.0113 -0.0667 -0.0034 308 LYS C NZ  
6170  N N   . CYS C  309 ? 0.5827 0.6446 0.5079 -0.0085 -0.0527 -0.0172 309 CYS C N   
6171  C CA  . CYS C  309 ? 0.6208 0.6869 0.5414 -0.0096 -0.0519 -0.0198 309 CYS C CA  
6172  C C   . CYS C  309 ? 0.5195 0.5842 0.4390 -0.0124 -0.0514 -0.0208 309 CYS C C   
6173  O O   . CYS C  309 ? 0.5790 0.6399 0.5020 -0.0133 -0.0510 -0.0196 309 CYS C O   
6174  C CB  . CYS C  309 ? 0.4488 0.5192 0.3685 -0.0086 -0.0494 -0.0213 309 CYS C CB  
6175  S SG  . CYS C  309 ? 0.7920 0.8642 0.7130 -0.0052 -0.0495 -0.0199 309 CYS C SG  
6176  N N   . PRO C  310 ? 0.4551 0.5229 0.3703 -0.0137 -0.0514 -0.0228 310 PRO C N   
6177  C CA  . PRO C  310 ? 0.5179 0.5850 0.4317 -0.0164 -0.0505 -0.0242 310 PRO C CA  
6178  C C   . PRO C  310 ? 0.5543 0.6221 0.4695 -0.0171 -0.0475 -0.0256 310 PRO C C   
6179  O O   . PRO C  310 ? 0.5935 0.6640 0.5090 -0.0157 -0.0462 -0.0262 310 PRO C O   
6180  C CB  . PRO C  310 ? 0.4573 0.5288 0.3662 -0.0172 -0.0508 -0.0264 310 PRO C CB  
6181  C CG  . PRO C  310 ? 0.4555 0.5283 0.3635 -0.0151 -0.0526 -0.0254 310 PRO C CG  
6182  C CD  . PRO C  310 ? 0.4030 0.4750 0.3145 -0.0127 -0.0522 -0.0239 310 PRO C CD  
6183  N N   . LYS C  311 ? 0.5601 0.6254 0.4760 -0.0194 -0.0462 -0.0261 311 LYS C N   
6184  C CA  . LYS C  311 ? 0.5386 0.6038 0.4559 -0.0204 -0.0429 -0.0276 311 LYS C CA  
6185  C C   . LYS C  311 ? 0.5059 0.5769 0.4189 -0.0214 -0.0412 -0.0310 311 LYS C C   
6186  O O   . LYS C  311 ? 0.6879 0.7616 0.5973 -0.0226 -0.0420 -0.0325 311 LYS C O   
6187  C CB  . LYS C  311 ? 0.4540 0.5145 0.3738 -0.0224 -0.0418 -0.0271 311 LYS C CB  
6188  C CG  . LYS C  311 ? 0.4705 0.5271 0.3956 -0.0220 -0.0397 -0.0257 311 LYS C CG  
6189  C CD  . LYS C  311 ? 0.4731 0.5281 0.4017 -0.0194 -0.0414 -0.0229 311 LYS C CD  
6190  C CE  . LYS C  311 ? 0.4931 0.5436 0.4254 -0.0191 -0.0439 -0.0194 311 LYS C CE  
6191  N NZ  . LYS C  311 ? 0.5395 0.5880 0.4765 -0.0169 -0.0448 -0.0168 311 LYS C NZ  
6192  N N   . TYR C  312 ? 0.4484 0.5213 0.3618 -0.0212 -0.0388 -0.0323 312 TYR C N   
6193  C CA  . TYR C  312 ? 0.4278 0.5067 0.3372 -0.0224 -0.0373 -0.0354 312 TYR C CA  
6194  C C   . TYR C  312 ? 0.4323 0.5108 0.3403 -0.0257 -0.0349 -0.0380 312 TYR C C   
6195  O O   . TYR C  312 ? 0.5373 0.6116 0.4481 -0.0270 -0.0325 -0.0381 312 TYR C O   
6196  C CB  . TYR C  312 ? 0.3722 0.4537 0.2820 -0.0213 -0.0356 -0.0358 312 TYR C CB  
6197  C CG  . TYR C  312 ? 0.4860 0.5741 0.3915 -0.0228 -0.0341 -0.0388 312 TYR C CG  
6198  C CD1 . TYR C  312 ? 0.4283 0.5225 0.3305 -0.0222 -0.0359 -0.0394 312 TYR C CD1 
6199  C CD2 . TYR C  312 ? 0.5258 0.6144 0.4309 -0.0250 -0.0308 -0.0412 312 TYR C CD2 
6200  C CE1 . TYR C  312 ? 0.4494 0.5503 0.3480 -0.0236 -0.0347 -0.0419 312 TYR C CE1 
6201  C CE2 . TYR C  312 ? 0.4939 0.5889 0.3948 -0.0268 -0.0296 -0.0440 312 TYR C CE2 
6202  C CZ  . TYR C  312 ? 0.5306 0.6320 0.4284 -0.0261 -0.0317 -0.0442 312 TYR C CZ  
6203  O OH  . TYR C  312 ? 0.5696 0.6780 0.4636 -0.0279 -0.0308 -0.0468 312 TYR C OH  
6204  N N   . VAL C  313 ? 0.5759 0.6587 0.4800 -0.0272 -0.0354 -0.0400 313 VAL C N   
6205  C CA  . VAL C  313 ? 0.4901 0.5729 0.3926 -0.0305 -0.0332 -0.0427 313 VAL C CA  
6206  C C   . VAL C  313 ? 0.4821 0.5722 0.3804 -0.0320 -0.0321 -0.0459 313 VAL C C   
6207  O O   . VAL C  313 ? 0.4916 0.5871 0.3877 -0.0305 -0.0339 -0.0458 313 VAL C O   
6208  C CB  . VAL C  313 ? 0.4198 0.4999 0.3218 -0.0314 -0.0348 -0.0420 313 VAL C CB  
6209  C CG1 . VAL C  313 ? 0.6341 0.7144 0.5344 -0.0348 -0.0324 -0.0448 313 VAL C CG1 
6210  C CG2 . VAL C  313 ? 0.5338 0.6070 0.4399 -0.0303 -0.0360 -0.0386 313 VAL C CG2 
6211  N N   . LYS C  314 ? 0.5577 0.6479 0.4551 -0.0351 -0.0290 -0.0488 314 LYS C N   
6212  C CA  . LYS C  314 ? 0.6049 0.7021 0.4985 -0.0371 -0.0277 -0.0521 314 LYS C CA  
6213  C C   . LYS C  314 ? 0.6106 0.7110 0.5012 -0.0387 -0.0288 -0.0536 314 LYS C C   
6214  O O   . LYS C  314 ? 0.7675 0.8742 0.6551 -0.0407 -0.0280 -0.0563 314 LYS C O   
6215  C CB  . LYS C  314 ? 0.6359 0.7316 0.5296 -0.0402 -0.0237 -0.0549 314 LYS C CB  
6216  C CG  . LYS C  314 ? 0.6740 0.7752 0.5655 -0.0408 -0.0222 -0.0567 314 LYS C CG  
6217  C CD  . LYS C  314 ? 1.0961 1.1940 0.9883 -0.0438 -0.0178 -0.0592 314 LYS C CD  
6218  C CE  . LYS C  314 ? 1.0896 1.1787 0.9869 -0.0425 -0.0166 -0.0568 314 LYS C CE  
6219  N NZ  . LYS C  314 ? 0.9212 1.0053 0.8200 -0.0457 -0.0125 -0.0590 314 LYS C NZ  
6220  N N   . SER C  315 ? 0.6406 0.7369 0.5324 -0.0380 -0.0306 -0.0517 315 SER C N   
6221  C CA  . SER C  315 ? 0.6649 0.7631 0.5540 -0.0395 -0.0314 -0.0530 315 SER C CA  
6222  C C   . SER C  315 ? 0.6046 0.7102 0.4910 -0.0382 -0.0335 -0.0533 315 SER C C   
6223  O O   . SER C  315 ? 0.4666 0.5743 0.3536 -0.0354 -0.0352 -0.0514 315 SER C O   
6224  C CB  . SER C  315 ? 0.6542 0.7461 0.5450 -0.0389 -0.0330 -0.0506 315 SER C CB  
6225  O OG  . SER C  315 ? 0.8515 0.9370 0.7450 -0.0403 -0.0309 -0.0502 315 SER C OG  
6226  N N   . THR C  316 ? 0.6708 0.7805 0.5546 -0.0404 -0.0332 -0.0557 316 THR C N   
6227  C CA  . THR C  316 ? 0.7593 0.8760 0.6409 -0.0394 -0.0350 -0.0558 316 THR C CA  
6228  C C   . THR C  316 ? 0.6593 0.7733 0.5407 -0.0382 -0.0371 -0.0542 316 THR C C   
6229  O O   . THR C  316 ? 0.6502 0.7672 0.5312 -0.0359 -0.0391 -0.0528 316 THR C O   
6230  C CB  . THR C  316 ? 0.7586 0.8819 0.6375 -0.0424 -0.0335 -0.0593 316 THR C CB  
6231  O OG1 . THR C  316 ? 0.8937 1.0229 0.7712 -0.0415 -0.0353 -0.0592 316 THR C OG1 
6232  C CG2 . THR C  316 ? 0.8837 1.0029 0.7622 -0.0459 -0.0313 -0.0615 316 THR C CG2 
6233  N N   . LYS C  317 ? 0.7598 0.8679 0.6415 -0.0400 -0.0365 -0.0543 317 LYS C N   
6234  C CA  . LYS C  317 ? 0.6772 0.7819 0.5583 -0.0394 -0.0383 -0.0528 317 LYS C CA  
6235  C C   . LYS C  317 ? 0.6606 0.7571 0.5434 -0.0403 -0.0380 -0.0514 317 LYS C C   
6236  O O   . LYS C  317 ? 0.7020 0.7961 0.5856 -0.0424 -0.0356 -0.0527 317 LYS C O   
6237  C CB  . LYS C  317 ? 0.7566 0.8656 0.6349 -0.0412 -0.0381 -0.0551 317 LYS C CB  
6238  C CG  . LYS C  317 ? 1.0256 1.1354 0.9029 -0.0449 -0.0354 -0.0582 317 LYS C CG  
6239  C CD  . LYS C  317 ? 1.2270 1.3406 1.1018 -0.0466 -0.0353 -0.0602 317 LYS C CD  
6240  C CE  . LYS C  317 ? 1.2494 1.3576 1.1235 -0.0466 -0.0364 -0.0587 317 LYS C CE  
6241  N NZ  . LYS C  317 ? 0.9862 1.0978 0.8584 -0.0482 -0.0359 -0.0604 317 LYS C NZ  
6242  N N   . LEU C  318 ? 0.5976 0.6899 0.4808 -0.0387 -0.0403 -0.0488 318 LEU C N   
6243  C CA  . LEU C  318 ? 0.6406 0.7257 0.5254 -0.0395 -0.0405 -0.0469 318 LEU C CA  
6244  C C   . LEU C  318 ? 0.5979 0.6811 0.4804 -0.0397 -0.0424 -0.0459 318 LEU C C   
6245  O O   . LEU C  318 ? 0.6634 0.7425 0.5467 -0.0385 -0.0446 -0.0431 318 LEU C O   
6246  C CB  . LEU C  318 ? 0.5784 0.6594 0.4667 -0.0374 -0.0414 -0.0440 318 LEU C CB  
6247  C CG  . LEU C  318 ? 0.6130 0.6939 0.5041 -0.0374 -0.0391 -0.0445 318 LEU C CG  
6248  C CD1 . LEU C  318 ? 0.5880 0.6656 0.4825 -0.0348 -0.0404 -0.0415 318 LEU C CD1 
6249  C CD2 . LEU C  318 ? 0.5025 0.5797 0.3948 -0.0401 -0.0364 -0.0456 318 LEU C CD2 
6250  N N   . ARG C  319 ? 0.7440 0.8303 0.6235 -0.0415 -0.0417 -0.0482 319 ARG C N   
6251  C CA  . ARG C  319 ? 0.7069 0.7918 0.5837 -0.0420 -0.0432 -0.0476 319 ARG C CA  
6252  C C   . ARG C  319 ? 0.5403 0.6187 0.4173 -0.0436 -0.0433 -0.0461 319 ARG C C   
6253  O O   . ARG C  319 ? 0.4733 0.5503 0.3506 -0.0459 -0.0412 -0.0473 319 ARG C O   
6254  C CB  . ARG C  319 ? 0.7948 0.8854 0.6688 -0.0433 -0.0422 -0.0506 319 ARG C CB  
6255  C CG  . ARG C  319 ? 0.7556 0.8452 0.6267 -0.0436 -0.0435 -0.0502 319 ARG C CG  
6256  C CD  . ARG C  319 ? 0.8140 0.9104 0.6854 -0.0430 -0.0425 -0.0516 319 ARG C CD  
6257  N NE  . ARG C  319 ? 0.9355 1.0350 0.8091 -0.0398 -0.0433 -0.0502 319 ARG C NE  
6258  C CZ  . ARG C  319 ? 0.9402 1.0379 0.8139 -0.0380 -0.0447 -0.0483 319 ARG C CZ  
6259  N NH1 . ARG C  319 ? 0.8637 0.9567 0.7354 -0.0390 -0.0455 -0.0475 319 ARG C NH1 
6260  N NH2 . ARG C  319 ? 0.9618 1.0624 0.8375 -0.0352 -0.0453 -0.0472 319 ARG C NH2 
6261  N N   . LEU C  320 ? 0.5809 0.6554 0.4577 -0.0426 -0.0458 -0.0433 320 LEU C N   
6262  C CA  . LEU C  320 ? 0.5671 0.6356 0.4442 -0.0440 -0.0465 -0.0411 320 LEU C CA  
6263  C C   . LEU C  320 ? 0.5434 0.6111 0.4164 -0.0456 -0.0473 -0.0415 320 LEU C C   
6264  O O   . LEU C  320 ? 0.6844 0.7531 0.5550 -0.0446 -0.0490 -0.0412 320 LEU C O   
6265  C CB  . LEU C  320 ? 0.6336 0.6982 0.5132 -0.0421 -0.0489 -0.0375 320 LEU C CB  
6266  C CG  . LEU C  320 ? 0.6565 0.7152 0.5376 -0.0432 -0.0498 -0.0344 320 LEU C CG  
6267  C CD1 . LEU C  320 ? 0.5367 0.5933 0.4216 -0.0440 -0.0473 -0.0343 320 LEU C CD1 
6268  C CD2 . LEU C  320 ? 0.5400 0.5961 0.4228 -0.0415 -0.0528 -0.0311 320 LEU C CD2 
6269  N N   . ALA C  321 ? 0.4742 0.5399 0.3463 -0.0480 -0.0457 -0.0422 321 ALA C N   
6270  C CA  . ALA C  321 ? 0.5913 0.6561 0.4593 -0.0498 -0.0461 -0.0427 321 ALA C CA  
6271  C C   . ALA C  321 ? 0.7012 0.7614 0.5678 -0.0496 -0.0489 -0.0394 321 ALA C C   
6272  O O   . ALA C  321 ? 0.7548 0.8107 0.6238 -0.0497 -0.0498 -0.0364 321 ALA C O   
6273  C CB  . ALA C  321 ? 0.4350 0.4985 0.3027 -0.0524 -0.0435 -0.0440 321 ALA C CB  
6274  N N   . THR C  322 ? 0.7670 0.8283 0.6298 -0.0496 -0.0502 -0.0399 322 THR C N   
6275  C CA  . THR C  322 ? 0.6618 0.7190 0.5224 -0.0500 -0.0529 -0.0372 322 THR C CA  
6276  C C   . THR C  322 ? 0.7343 0.7899 0.5903 -0.0526 -0.0525 -0.0379 322 THR C C   
6277  O O   . THR C  322 ? 0.7924 0.8436 0.6469 -0.0539 -0.0540 -0.0354 322 THR C O   
6278  C CB  . THR C  322 ? 0.6523 0.7111 0.5120 -0.0481 -0.0547 -0.0371 322 THR C CB  
6279  O OG1 . THR C  322 ? 0.7720 0.8351 0.6294 -0.0479 -0.0532 -0.0401 322 THR C OG1 
6280  C CG2 . THR C  322 ? 0.8030 0.8629 0.6671 -0.0455 -0.0551 -0.0361 322 THR C CG2 
6281  N N   . GLY C  323 ? 0.7265 0.7858 0.5805 -0.0532 -0.0505 -0.0412 323 GLY C N   
6282  C CA  . GLY C  323 ? 0.7579 0.8160 0.6076 -0.0557 -0.0496 -0.0422 323 GLY C CA  
6283  C C   . GLY C  323 ? 0.7602 0.8171 0.6109 -0.0576 -0.0474 -0.0428 323 GLY C C   
6284  O O   . GLY C  323 ? 0.6792 0.7347 0.5338 -0.0573 -0.0469 -0.0416 323 GLY C O   
6285  N N   . LEU C  324 ? 0.7573 0.8147 0.6048 -0.0597 -0.0458 -0.0448 324 LEU C N   
6286  C CA  . LEU C  324 ? 0.7421 0.7983 0.5902 -0.0617 -0.0433 -0.0457 324 LEU C CA  
6287  C C   . LEU C  324 ? 0.7825 0.8441 0.6306 -0.0623 -0.0405 -0.0498 324 LEU C C   
6288  O O   . LEU C  324 ? 0.9528 1.0191 0.8005 -0.0610 -0.0407 -0.0517 324 LEU C O   
6289  C CB  . LEU C  324 ? 0.8825 0.9342 0.7268 -0.0641 -0.0435 -0.0442 324 LEU C CB  
6290  C CG  . LEU C  324 ? 0.8019 0.8542 0.6409 -0.0649 -0.0441 -0.0455 324 LEU C CG  
6291  C CD1 . LEU C  324 ? 0.9539 1.0030 0.7895 -0.0677 -0.0429 -0.0453 324 LEU C CD1 
6292  C CD2 . LEU C  324 ? 0.7659 0.8166 0.6032 -0.0638 -0.0472 -0.0432 324 LEU C CD2 
6293  N N   . ARG C  325 ? 0.7628 0.8238 0.6117 -0.0643 -0.0379 -0.0511 325 ARG C N   
6294  C CA  . ARG C  325 ? 0.7941 0.8603 0.6430 -0.0654 -0.0352 -0.0552 325 ARG C CA  
6295  C C   . ARG C  325 ? 0.9186 0.9884 0.7641 -0.0655 -0.0354 -0.0571 325 ARG C C   
6296  O O   . ARG C  325 ? 1.0273 1.0942 0.8695 -0.0657 -0.0369 -0.0556 325 ARG C O   
6297  C CB  . ARG C  325 ? 0.8231 0.8869 0.6722 -0.0681 -0.0323 -0.0562 325 ARG C CB  
6298  C CG  . ARG C  325 ? 0.8481 0.9111 0.7014 -0.0683 -0.0305 -0.0563 325 ARG C CG  
6299  C CD  . ARG C  325 ? 1.0094 1.0698 0.8629 -0.0711 -0.0272 -0.0574 325 ARG C CD  
6300  N NE  . ARG C  325 ? 1.1686 1.2289 1.0261 -0.0716 -0.0247 -0.0585 325 ARG C NE  
6301  C CZ  . ARG C  325 ? 1.1732 1.2388 1.0319 -0.0722 -0.0228 -0.0621 325 ARG C CZ  
6302  N NH1 . ARG C  325 ? 0.9188 0.9906 0.7754 -0.0722 -0.0232 -0.0649 325 ARG C NH1 
6303  N NH2 . ARG C  325 ? 1.0935 1.1583 0.9555 -0.0729 -0.0203 -0.0631 325 ARG C NH2 
6304  N N   . ASN C  326 ? 1.0352 1.1113 0.8816 -0.0656 -0.0338 -0.0603 326 ASN C N   
6305  C CA  . ASN C  326 ? 1.0764 1.1566 0.9209 -0.0654 -0.0336 -0.0621 326 ASN C CA  
6306  C C   . ASN C  326 ? 1.0972 1.1806 0.9408 -0.0679 -0.0308 -0.0654 326 ASN C C   
6307  O O   . ASN C  326 ? 1.0857 1.1730 0.9313 -0.0687 -0.0291 -0.0677 326 ASN C O   
6308  C CB  . ASN C  326 ? 1.1812 1.2672 1.0297 -0.0625 -0.0340 -0.0619 326 ASN C CB  
6309  C CG  . ASN C  326 ? 1.2286 1.3172 1.0769 -0.0614 -0.0340 -0.0619 326 ASN C CG  
6310  O OD1 . ASN C  326 ? 1.1967 1.2812 1.0419 -0.0620 -0.0346 -0.0608 326 ASN C OD1 
6311  N ND2 . ASN C  326 ? 1.2783 1.3739 1.1297 -0.0599 -0.0333 -0.0631 326 ASN C ND2 
6312  N N   . ILE C  327 ? 1.1841 1.2656 1.0245 -0.0694 -0.0302 -0.0658 327 ILE C N   
6313  C CA  . ILE C  327 ? 1.0916 1.1755 0.9308 -0.0720 -0.0275 -0.0689 327 ILE C CA  
6314  C C   . ILE C  327 ? 1.1436 1.2275 0.9803 -0.0724 -0.0271 -0.0691 327 ILE C C   
6315  O O   . ILE C  327 ? 0.9934 1.0830 0.8319 -0.0717 -0.0262 -0.0705 327 ILE C O   
6316  C CB  . ILE C  327 ? 1.0429 1.1216 0.8818 -0.0745 -0.0258 -0.0686 327 ILE C CB  
6317  C CG1 . ILE C  327 ? 0.8337 0.9095 0.6756 -0.0736 -0.0264 -0.0666 327 ILE C CG1 
6318  C CG2 . ILE C  327 ? 1.1007 1.1830 0.9401 -0.0771 -0.0226 -0.0722 327 ILE C CG2 
6319  C CD1 . ILE C  327 ? 0.7431 0.8116 0.5845 -0.0752 -0.0257 -0.0644 327 ILE C CD1 
6320  N N   . GLY D  1   ? 1.1045 1.1397 0.9669 -0.0742 -0.0229 -0.0447 1   GLY D N   
6321  C CA  . GLY D  1   ? 1.1503 1.1847 1.0166 -0.0755 -0.0185 -0.0468 1   GLY D CA  
6322  C C   . GLY D  1   ? 1.0999 1.1279 0.9703 -0.0756 -0.0170 -0.0428 1   GLY D C   
6323  O O   . GLY D  1   ? 0.9365 0.9621 0.8088 -0.0775 -0.0128 -0.0440 1   GLY D O   
6324  N N   . LEU D  2   ? 0.9677 0.9930 0.8397 -0.0737 -0.0203 -0.0378 2   LEU D N   
6325  C CA  . LEU D  2   ? 0.9460 0.9656 0.8228 -0.0734 -0.0192 -0.0333 2   LEU D CA  
6326  C C   . LEU D  2   ? 0.8622 0.8779 0.7367 -0.0745 -0.0203 -0.0295 2   LEU D C   
6327  O O   . LEU D  2   ? 0.8258 0.8369 0.7037 -0.0751 -0.0180 -0.0266 2   LEU D O   
6328  C CB  . LEU D  2   ? 0.8273 0.8462 0.7082 -0.0707 -0.0219 -0.0298 2   LEU D CB  
6329  C CG  . LEU D  2   ? 0.8035 0.8178 0.6914 -0.0702 -0.0193 -0.0267 2   LEU D CG  
6330  C CD1 . LEU D  2   ? 0.8098 0.8245 0.7005 -0.0714 -0.0139 -0.0311 2   LEU D CD1 
6331  C CD2 . LEU D  2   ? 0.5780 0.5919 0.4698 -0.0675 -0.0224 -0.0229 2   LEU D CD2 
6332  N N   . PHE D  3   ? 0.8096 0.8269 0.6782 -0.0747 -0.0237 -0.0293 3   PHE D N   
6333  C CA  . PHE D  3   ? 0.8957 0.9097 0.7612 -0.0759 -0.0250 -0.0257 3   PHE D CA  
6334  C C   . PHE D  3   ? 1.0977 1.1124 0.9584 -0.0784 -0.0226 -0.0293 3   PHE D C   
6335  O O   . PHE D  3   ? 1.0459 1.0581 0.9030 -0.0797 -0.0234 -0.0270 3   PHE D O   
6336  C CB  . PHE D  3   ? 0.9084 0.9228 0.7707 -0.0748 -0.0304 -0.0224 3   PHE D CB  
6337  C CG  . PHE D  3   ? 0.9249 0.9377 0.7922 -0.0727 -0.0329 -0.0177 3   PHE D CG  
6338  C CD1 . PHE D  3   ? 0.8814 0.8970 0.7513 -0.0706 -0.0340 -0.0191 3   PHE D CD1 
6339  C CD2 . PHE D  3   ? 0.9635 0.9722 0.8329 -0.0727 -0.0341 -0.0119 3   PHE D CD2 
6340  C CE1 . PHE D  3   ? 0.8494 0.8635 0.7241 -0.0687 -0.0361 -0.0148 3   PHE D CE1 
6341  C CE2 . PHE D  3   ? 0.9333 0.9408 0.8077 -0.0708 -0.0364 -0.0074 3   PHE D CE2 
6342  C CZ  . PHE D  3   ? 0.8972 0.9074 0.7744 -0.0688 -0.0374 -0.0090 3   PHE D CZ  
6343  N N   . GLY D  4   ? 1.0422 1.0606 0.9027 -0.0792 -0.0197 -0.0348 4   GLY D N   
6344  C CA  . GLY D  4   ? 0.9211 0.9404 0.7780 -0.0816 -0.0169 -0.0386 4   GLY D CA  
6345  C C   . GLY D  4   ? 1.0231 1.0451 0.8735 -0.0822 -0.0194 -0.0399 4   GLY D C   
6346  O O   . GLY D  4   ? 1.0034 1.0264 0.8507 -0.0842 -0.0171 -0.0430 4   GLY D O   
6347  N N   . ALA D  5   ? 1.0537 1.0766 0.9021 -0.0805 -0.0237 -0.0377 5   ALA D N   
6348  C CA  . ALA D  5   ? 0.9598 0.9846 0.8020 -0.0810 -0.0260 -0.0388 5   ALA D CA  
6349  C C   . ALA D  5   ? 0.8791 0.9100 0.7202 -0.0805 -0.0256 -0.0439 5   ALA D C   
6350  O O   . ALA D  5   ? 0.8430 0.8762 0.6817 -0.0821 -0.0234 -0.0475 5   ALA D O   
6351  C CB  . ALA D  5   ? 0.8886 0.9117 0.7289 -0.0797 -0.0307 -0.0345 5   ALA D CB  
6352  N N   . ILE D  6   ? 0.9585 0.9922 0.8017 -0.0782 -0.0278 -0.0439 6   ILE D N   
6353  C CA  . ILE D  6   ? 0.8197 0.8595 0.6623 -0.0774 -0.0277 -0.0481 6   ILE D CA  
6354  C C   . ILE D  6   ? 0.8941 0.9370 0.7397 -0.0784 -0.0239 -0.0521 6   ILE D C   
6355  O O   . ILE D  6   ? 0.9396 0.9811 0.7895 -0.0781 -0.0223 -0.0515 6   ILE D O   
6356  C CB  . ILE D  6   ? 0.7182 0.7599 0.5625 -0.0746 -0.0309 -0.0468 6   ILE D CB  
6357  C CG1 . ILE D  6   ? 0.6370 0.6759 0.4780 -0.0740 -0.0346 -0.0432 6   ILE D CG1 
6358  C CG2 . ILE D  6   ? 0.7077 0.7558 0.5517 -0.0737 -0.0306 -0.0508 6   ILE D CG2 
6359  C CD1 . ILE D  6   ? 0.7350 0.7759 0.5771 -0.0714 -0.0377 -0.0422 6   ILE D CD1 
6360  N N   . ALA D  7   ? 0.8097 0.8568 0.6529 -0.0796 -0.0223 -0.0561 7   ALA D N   
6361  C CA  . ALA D  7   ? 0.7975 0.8479 0.6428 -0.0812 -0.0186 -0.0602 7   ALA D CA  
6362  C C   . ALA D  7   ? 1.0157 1.0612 0.8624 -0.0834 -0.0153 -0.0596 7   ALA D C   
6363  O O   . ALA D  7   ? 1.0349 1.0813 0.8846 -0.0846 -0.0121 -0.0620 7   ALA D O   
6364  C CB  . ALA D  7   ? 0.7696 0.8237 0.6188 -0.0796 -0.0186 -0.0614 7   ALA D CB  
6365  N N   . GLY D  8   ? 1.0614 1.1017 0.9058 -0.0840 -0.0161 -0.0563 8   GLY D N   
6366  C CA  . GLY D  8   ? 1.0678 1.1030 0.9133 -0.0860 -0.0131 -0.0551 8   GLY D CA  
6367  C C   . GLY D  8   ? 1.2824 1.3164 1.1234 -0.0882 -0.0119 -0.0559 8   GLY D C   
6368  O O   . GLY D  8   ? 1.2253 1.2634 1.0646 -0.0895 -0.0102 -0.0601 8   GLY D O   
6369  N N   . PHE D  9   ? 0.9536 0.9821 0.7926 -0.0886 -0.0129 -0.0517 9   PHE D N   
6370  C CA  . PHE D  9   ? 0.9828 1.0097 0.8170 -0.0907 -0.0120 -0.0521 9   PHE D CA  
6371  C C   . PHE D  9   ? 1.0475 1.0776 0.8768 -0.0902 -0.0148 -0.0532 9   PHE D C   
6372  O O   . PHE D  9   ? 1.3034 1.3338 1.1287 -0.0919 -0.0137 -0.0550 9   PHE D O   
6373  C CB  . PHE D  9   ? 1.0681 1.0883 0.9015 -0.0914 -0.0121 -0.0472 9   PHE D CB  
6374  C CG  . PHE D  9   ? 0.9844 1.0021 0.8174 -0.0895 -0.0165 -0.0420 9   PHE D CG  
6375  C CD1 . PHE D  9   ? 1.0090 1.0273 0.8368 -0.0893 -0.0201 -0.0409 9   PHE D CD1 
6376  C CD2 . PHE D  9   ? 1.0740 1.0888 0.9121 -0.0882 -0.0169 -0.0382 9   PHE D CD2 
6377  C CE1 . PHE D  9   ? 1.0314 1.0477 0.8587 -0.0878 -0.0241 -0.0363 9   PHE D CE1 
6378  C CE2 . PHE D  9   ? 1.1374 1.1503 0.9754 -0.0866 -0.0211 -0.0333 9   PHE D CE2 
6379  C CZ  . PHE D  9   ? 1.1463 1.1600 0.9788 -0.0865 -0.0248 -0.0324 9   PHE D CZ  
6380  N N   . ILE D  10  ? 0.8441 0.8764 0.6739 -0.0878 -0.0183 -0.0522 10  ILE D N   
6381  C CA  . ILE D  10  ? 0.9351 0.9711 0.7612 -0.0871 -0.0204 -0.0539 10  ILE D CA  
6382  C C   . ILE D  10  ? 0.9840 1.0266 0.8133 -0.0859 -0.0197 -0.0579 10  ILE D C   
6383  O O   . ILE D  10  ? 0.9767 1.0210 0.8087 -0.0837 -0.0216 -0.0570 10  ILE D O   
6384  C CB  . ILE D  10  ? 0.8553 0.8894 0.6796 -0.0853 -0.0247 -0.0501 10  ILE D CB  
6385  C CG1 . ILE D  10  ? 0.8729 0.9006 0.6947 -0.0865 -0.0258 -0.0455 10  ILE D CG1 
6386  C CG2 . ILE D  10  ? 0.6708 0.7080 0.4909 -0.0849 -0.0263 -0.0520 10  ILE D CG2 
6387  C CD1 . ILE D  10  ? 0.8797 0.9056 0.6992 -0.0853 -0.0301 -0.0417 10  ILE D CD1 
6388  N N   . GLU D  11  ? 1.3025 1.3488 1.1314 -0.0875 -0.0168 -0.0620 11  GLU D N   
6389  C CA  . GLU D  11  ? 1.2819 1.3346 1.1140 -0.0870 -0.0155 -0.0659 11  GLU D CA  
6390  C C   . GLU D  11  ? 1.1615 1.2193 0.9938 -0.0845 -0.0182 -0.0665 11  GLU D C   
6391  O O   . GLU D  11  ? 1.2188 1.2806 1.0545 -0.0832 -0.0184 -0.0677 11  GLU D O   
6392  C CB  . GLU D  11  ? 1.5376 1.5934 1.3690 -0.0895 -0.0121 -0.0700 11  GLU D CB  
6393  C CG  . GLU D  11  ? 1.7398 1.7909 1.5713 -0.0921 -0.0088 -0.0698 11  GLU D CG  
6394  C CD  . GLU D  11  ? 2.1476 2.2016 1.9781 -0.0947 -0.0055 -0.0739 11  GLU D CD  
6395  O OE1 . GLU D  11  ? 2.1952 2.2456 2.0257 -0.0970 -0.0025 -0.0742 11  GLU D OE1 
6396  O OE2 . GLU D  11  ? 2.0332 2.0935 1.8632 -0.0945 -0.0058 -0.0768 11  GLU D OE2 
6397  N N   . GLY D  12  ? 1.0133 1.0709 0.8418 -0.0839 -0.0202 -0.0657 12  GLY D N   
6398  C CA  . GLY D  12  ? 0.9411 1.0037 0.7697 -0.0817 -0.0221 -0.0665 12  GLY D CA  
6399  C C   . GLY D  12  ? 0.9042 0.9638 0.7303 -0.0800 -0.0255 -0.0634 12  GLY D C   
6400  O O   . GLY D  12  ? 0.9688 1.0226 0.7921 -0.0808 -0.0265 -0.0606 12  GLY D O   
6401  N N   . GLY D  13  ? 0.8225 0.8864 0.6497 -0.0777 -0.0271 -0.0640 13  GLY D N   
6402  C CA  . GLY D  13  ? 0.8281 0.8898 0.6530 -0.0761 -0.0300 -0.0616 13  GLY D CA  
6403  C C   . GLY D  13  ? 0.8742 0.9375 0.6957 -0.0764 -0.0297 -0.0632 13  GLY D C   
6404  O O   . GLY D  13  ? 0.9722 1.0392 0.7936 -0.0774 -0.0273 -0.0661 13  GLY D O   
6405  N N   . TRP D  14  ? 0.8253 0.8859 0.6440 -0.0755 -0.0319 -0.0612 14  TRP D N   
6406  C CA  . TRP D  14  ? 0.8657 0.9270 0.6824 -0.0756 -0.0310 -0.0621 14  TRP D CA  
6407  C C   . TRP D  14  ? 0.9797 1.0445 0.7999 -0.0727 -0.0318 -0.0617 14  TRP D C   
6408  O O   . TRP D  14  ? 1.0719 1.1337 0.8915 -0.0716 -0.0341 -0.0592 14  TRP D O   
6409  C CB  . TRP D  14  ? 0.9765 1.0312 0.7869 -0.0777 -0.0320 -0.0603 14  TRP D CB  
6410  C CG  . TRP D  14  ? 0.9925 1.0437 0.8000 -0.0805 -0.0308 -0.0602 14  TRP D CG  
6411  C CD1 . TRP D  14  ? 0.9441 0.9976 0.7533 -0.0817 -0.0280 -0.0625 14  TRP D CD1 
6412  C CD2 . TRP D  14  ? 0.8918 0.9366 0.6951 -0.0824 -0.0320 -0.0573 14  TRP D CD2 
6413  N NE1 . TRP D  14  ? 0.8383 0.8869 0.6449 -0.0842 -0.0271 -0.0612 14  TRP D NE1 
6414  C CE2 . TRP D  14  ? 0.9668 1.0102 0.7698 -0.0846 -0.0297 -0.0578 14  TRP D CE2 
6415  C CE3 . TRP D  14  ? 0.8939 0.9343 0.6938 -0.0826 -0.0349 -0.0541 14  TRP D CE3 
6416  C CZ2 . TRP D  14  ? 1.0001 1.0377 0.7996 -0.0867 -0.0301 -0.0551 14  TRP D CZ2 
6417  C CZ3 . TRP D  14  ? 1.1182 1.1532 0.9144 -0.0849 -0.0355 -0.0514 14  TRP D CZ3 
6418  C CH2 . TRP D  14  ? 1.0962 1.1299 0.8923 -0.0868 -0.0331 -0.0518 14  TRP D CH2 
6419  N N   . THR D  15  ? 0.9590 1.0300 0.7825 -0.0716 -0.0300 -0.0640 15  THR D N   
6420  C CA  . THR D  15  ? 1.1002 1.1747 0.9264 -0.0689 -0.0304 -0.0639 15  THR D CA  
6421  C C   . THR D  15  ? 1.2014 1.2718 1.0233 -0.0694 -0.0306 -0.0632 15  THR D C   
6422  O O   . THR D  15  ? 1.2008 1.2710 1.0235 -0.0675 -0.0316 -0.0622 15  THR D O   
6423  C CB  . THR D  15  ? 1.1081 1.1904 0.9378 -0.0680 -0.0283 -0.0666 15  THR D CB  
6424  O OG1 . THR D  15  ? 1.3405 1.4227 1.1671 -0.0702 -0.0261 -0.0687 15  THR D OG1 
6425  C CG2 . THR D  15  ? 1.0547 1.1413 0.8882 -0.0680 -0.0278 -0.0676 15  THR D CG2 
6426  N N   . GLY D  16  ? 1.1793 1.2460 0.9962 -0.0723 -0.0295 -0.0640 16  GLY D N   
6427  C CA  . GLY D  16  ? 1.2612 1.3237 1.0731 -0.0734 -0.0293 -0.0638 16  GLY D CA  
6428  C C   . GLY D  16  ? 1.2303 1.2873 1.0397 -0.0734 -0.0320 -0.0608 16  GLY D C   
6429  O O   . GLY D  16  ? 1.2473 1.3026 1.0547 -0.0731 -0.0322 -0.0607 16  GLY D O   
6430  N N   . MET D  17  ? 1.1386 1.1928 0.9478 -0.0740 -0.0341 -0.0586 17  MET D N   
6431  C CA  . MET D  17  ? 1.1395 1.1889 0.9465 -0.0741 -0.0371 -0.0556 17  MET D CA  
6432  C C   . MET D  17  ? 1.1918 1.2436 1.0038 -0.0709 -0.0387 -0.0544 17  MET D C   
6433  O O   . MET D  17  ? 1.2072 1.2613 1.0236 -0.0694 -0.0394 -0.0538 17  MET D O   
6434  C CB  . MET D  17  ? 0.9931 1.0384 0.7975 -0.0760 -0.0388 -0.0535 17  MET D CB  
6435  C CG  . MET D  17  ? 1.2377 1.2784 1.0396 -0.0764 -0.0422 -0.0501 17  MET D CG  
6436  S SD  . MET D  17  ? 1.2090 1.2451 1.0073 -0.0787 -0.0444 -0.0474 17  MET D SD  
6437  C CE  . MET D  17  ? 1.1265 1.1665 0.9319 -0.0767 -0.0434 -0.0480 17  MET D CE  
6438  N N   . VAL D  18  ? 1.3505 1.4013 1.1616 -0.0701 -0.0392 -0.0542 18  VAL D N   
6439  C CA  . VAL D  18  ? 1.4279 1.4811 1.2436 -0.0670 -0.0404 -0.0533 18  VAL D CA  
6440  C C   . VAL D  18  ? 1.3515 1.3999 1.1648 -0.0674 -0.0431 -0.0507 18  VAL D C   
6441  O O   . VAL D  18  ? 1.4021 1.4515 1.2180 -0.0652 -0.0440 -0.0502 18  VAL D O   
6442  C CB  . VAL D  18  ? 1.4581 1.5154 1.2757 -0.0651 -0.0382 -0.0555 18  VAL D CB  
6443  C CG1 . VAL D  18  ? 1.3160 1.3789 1.1363 -0.0647 -0.0358 -0.0579 18  VAL D CG1 
6444  C CG2 . VAL D  18  ? 1.3897 1.4435 1.2019 -0.0668 -0.0373 -0.0565 18  VAL D CG2 
6445  N N   . ASP D  19  ? 1.3237 1.3672 1.1320 -0.0702 -0.0446 -0.0492 19  ASP D N   
6446  C CA  . ASP D  19  ? 1.4411 1.4802 1.2464 -0.0711 -0.0474 -0.0467 19  ASP D CA  
6447  C C   . ASP D  19  ? 1.3825 1.4208 1.1906 -0.0703 -0.0504 -0.0437 19  ASP D C   
6448  O O   . ASP D  19  ? 1.2879 1.3247 1.0967 -0.0696 -0.0528 -0.0418 19  ASP D O   
6449  C CB  . ASP D  19  ? 1.6085 1.6428 1.4063 -0.0749 -0.0477 -0.0464 19  ASP D CB  
6450  C CG  . ASP D  19  ? 1.7300 1.7648 1.5247 -0.0761 -0.0444 -0.0496 19  ASP D CG  
6451  O OD1 . ASP D  19  ? 1.8183 1.8565 1.6161 -0.0739 -0.0424 -0.0516 19  ASP D OD1 
6452  O OD2 . ASP D  19  ? 1.6704 1.7025 1.4597 -0.0791 -0.0437 -0.0499 19  ASP D OD2 
6453  N N   . GLY D  20  ? 1.3606 1.3999 1.1703 -0.0704 -0.0502 -0.0435 20  GLY D N   
6454  C CA  . GLY D  20  ? 1.1161 1.1546 0.9283 -0.0697 -0.0528 -0.0408 20  GLY D CA  
6455  C C   . GLY D  20  ? 0.9884 1.0294 0.8039 -0.0691 -0.0514 -0.0418 20  GLY D C   
6456  O O   . GLY D  20  ? 0.8828 0.9270 0.6993 -0.0689 -0.0485 -0.0446 20  GLY D O   
6457  N N   . TRP D  21  ? 0.9689 1.0086 0.7858 -0.0689 -0.0535 -0.0395 21  TRP D N   
6458  C CA  . TRP D  21  ? 0.9511 0.9926 0.7721 -0.0684 -0.0517 -0.0402 21  TRP D CA  
6459  C C   . TRP D  21  ? 0.8344 0.8735 0.6530 -0.0710 -0.0502 -0.0399 21  TRP D C   
6460  O O   . TRP D  21  ? 0.8342 0.8753 0.6544 -0.0713 -0.0475 -0.0422 21  TRP D O   
6461  C CB  . TRP D  21  ? 0.9915 1.0325 0.8179 -0.0667 -0.0534 -0.0374 21  TRP D CB  
6462  C CG  . TRP D  21  ? 0.9261 0.9708 0.7564 -0.0638 -0.0535 -0.0386 21  TRP D CG  
6463  C CD1 . TRP D  21  ? 0.7218 0.7711 0.5532 -0.0624 -0.0515 -0.0418 21  TRP D CD1 
6464  C CD2 . TRP D  21  ? 0.8598 0.9041 0.6943 -0.0618 -0.0555 -0.0362 21  TRP D CD2 
6465  N NE1 . TRP D  21  ? 0.8412 0.8928 0.6772 -0.0597 -0.0521 -0.0414 21  TRP D NE1 
6466  C CE2 . TRP D  21  ? 0.7607 0.8093 0.5978 -0.0593 -0.0548 -0.0383 21  TRP D CE2 
6467  C CE3 . TRP D  21  ? 0.8473 0.8882 0.6838 -0.0618 -0.0579 -0.0323 21  TRP D CE3 
6468  C CZ2 . TRP D  21  ? 0.8349 0.8843 0.6763 -0.0570 -0.0561 -0.0369 21  TRP D CZ2 
6469  C CZ3 . TRP D  21  ? 0.8114 0.8531 0.6524 -0.0595 -0.0592 -0.0309 21  TRP D CZ3 
6470  C CH2 . TRP D  21  ? 0.7531 0.7988 0.5963 -0.0571 -0.0583 -0.0333 21  TRP D CH2 
6471  N N   . TYR D  22  ? 0.9424 0.9771 0.7571 -0.0731 -0.0520 -0.0371 22  TYR D N   
6472  C CA  . TYR D  22  ? 0.9955 1.0274 0.8073 -0.0757 -0.0507 -0.0365 22  TYR D CA  
6473  C C   . TYR D  22  ? 1.0733 1.1027 0.8779 -0.0781 -0.0513 -0.0366 22  TYR D C   
6474  O O   . TYR D  22  ? 1.2073 1.2355 1.0092 -0.0782 -0.0538 -0.0354 22  TYR D O   
6475  C CB  . TYR D  22  ? 1.0163 1.0450 0.8309 -0.0760 -0.0521 -0.0322 22  TYR D CB  
6476  C CG  . TYR D  22  ? 1.0180 1.0480 0.8391 -0.0734 -0.0532 -0.0307 22  TYR D CG  
6477  C CD1 . TYR D  22  ? 0.9531 0.9818 0.7748 -0.0725 -0.0567 -0.0276 22  TYR D CD1 
6478  C CD2 . TYR D  22  ? 0.9155 0.9478 0.7419 -0.0720 -0.0508 -0.0324 22  TYR D CD2 
6479  C CE1 . TYR D  22  ? 0.8937 0.9235 0.7215 -0.0702 -0.0576 -0.0262 22  TYR D CE1 
6480  C CE2 . TYR D  22  ? 0.9010 0.9342 0.7330 -0.0698 -0.0516 -0.0310 22  TYR D CE2 
6481  C CZ  . TYR D  22  ? 0.9333 0.9652 0.7662 -0.0687 -0.0550 -0.0279 22  TYR D CZ  
6482  O OH  . TYR D  22  ? 0.7968 0.8295 0.6355 -0.0665 -0.0557 -0.0265 22  TYR D OH  
6483  N N   . GLY D  23  ? 1.3584 1.3868 1.1596 -0.0802 -0.0489 -0.0381 23  GLY D N   
6484  C CA  . GLY D  23  ? 1.4246 1.4505 1.2186 -0.0828 -0.0490 -0.0385 23  GLY D CA  
6485  C C   . GLY D  23  ? 1.3789 1.4035 1.1699 -0.0852 -0.0462 -0.0397 23  GLY D C   
6486  O O   . GLY D  23  ? 1.2062 1.2309 1.0005 -0.0851 -0.0446 -0.0394 23  GLY D O   
6487  N N   . TYR D  24  ? 1.1430 1.1661 0.9277 -0.0873 -0.0455 -0.0412 24  TYR D N   
6488  C CA  . TYR D  24  ? 1.1585 1.1798 0.9395 -0.0898 -0.0428 -0.0422 24  TYR D CA  
6489  C C   . TYR D  24  ? 1.2593 1.2830 1.0382 -0.0901 -0.0397 -0.0468 24  TYR D C   
6490  O O   . TYR D  24  ? 1.2039 1.2302 0.9835 -0.0886 -0.0397 -0.0489 24  TYR D O   
6491  C CB  . TYR D  24  ? 1.0995 1.1158 0.8738 -0.0928 -0.0447 -0.0390 24  TYR D CB  
6492  C CG  . TYR D  24  ? 1.0511 1.0653 0.8268 -0.0925 -0.0485 -0.0340 24  TYR D CG  
6493  C CD1 . TYR D  24  ? 1.1417 1.1559 0.9166 -0.0918 -0.0517 -0.0327 24  TYR D CD1 
6494  C CD2 . TYR D  24  ? 1.0300 1.0421 0.8078 -0.0930 -0.0488 -0.0305 24  TYR D CD2 
6495  C CE1 . TYR D  24  ? 1.1789 1.1915 0.9554 -0.0916 -0.0553 -0.0281 24  TYR D CE1 
6496  C CE2 . TYR D  24  ? 1.0283 1.0388 0.8080 -0.0927 -0.0523 -0.0257 24  TYR D CE2 
6497  C CZ  . TYR D  24  ? 1.1404 1.1512 0.9193 -0.0921 -0.0556 -0.0245 24  TYR D CZ  
6498  O OH  . TYR D  24  ? 1.0946 1.1042 0.8757 -0.0918 -0.0592 -0.0195 24  TYR D OH  
6499  N N   . HIS D  25  ? 1.1988 1.2216 0.9754 -0.0922 -0.0369 -0.0482 25  HIS D N   
6500  C CA  . HIS D  25  ? 1.3194 1.3438 1.0934 -0.0930 -0.0338 -0.0523 25  HIS D CA  
6501  C C   . HIS D  25  ? 1.4715 1.4918 1.2393 -0.0964 -0.0322 -0.0520 25  HIS D C   
6502  O O   . HIS D  25  ? 1.2454 1.2655 1.0143 -0.0974 -0.0300 -0.0524 25  HIS D O   
6503  C CB  . HIS D  25  ? 1.3356 1.3654 1.1154 -0.0913 -0.0310 -0.0556 25  HIS D CB  
6504  C CG  . HIS D  25  ? 1.4105 1.4421 1.1883 -0.0925 -0.0275 -0.0594 25  HIS D CG  
6505  N ND1 . HIS D  25  ? 1.3288 1.3598 1.1058 -0.0945 -0.0247 -0.0606 25  HIS D ND1 
6506  C CD2 . HIS D  25  ? 1.2389 1.2727 1.0156 -0.0919 -0.0263 -0.0621 25  HIS D CD2 
6507  C CE1 . HIS D  25  ? 1.3761 1.4090 1.1515 -0.0951 -0.0219 -0.0639 25  HIS D CE1 
6508  N NE2 . HIS D  25  ? 1.4280 1.4627 1.2034 -0.0935 -0.0228 -0.0648 25  HIS D NE2 
6509  N N   . HIS D  26  ? 1.7024 1.7194 1.4635 -0.0983 -0.0332 -0.0514 26  HIS D N   
6510  C CA  . HIS D  26  ? 1.6976 1.7104 1.4519 -0.1018 -0.0319 -0.0508 26  HIS D CA  
6511  C C   . HIS D  26  ? 1.7712 1.7855 1.5244 -0.1026 -0.0276 -0.0551 26  HIS D C   
6512  O O   . HIS D  26  ? 1.7850 1.8036 1.5418 -0.1007 -0.0261 -0.0583 26  HIS D O   
6513  C CB  . HIS D  26  ? 1.6571 1.6660 1.4043 -0.1037 -0.0344 -0.0490 26  HIS D CB  
6514  C CG  . HIS D  26  ? 1.6441 1.6539 1.3886 -0.1037 -0.0330 -0.0525 26  HIS D CG  
6515  N ND1 . HIS D  26  ? 1.6696 1.6826 1.4181 -0.1010 -0.0339 -0.0537 26  HIS D ND1 
6516  C CD2 . HIS D  26  ? 1.8520 1.8598 1.5906 -0.1060 -0.0304 -0.0550 26  HIS D CD2 
6517  C CE1 . HIS D  26  ? 1.7836 1.7964 1.5293 -0.1016 -0.0318 -0.0566 26  HIS D CE1 
6518  N NE2 . HIS D  26  ? 1.9644 1.9741 1.7036 -0.1047 -0.0297 -0.0576 26  HIS D NE2 
6519  N N   . GLN D  27  ? 1.8635 1.8745 1.6119 -0.1055 -0.0257 -0.0550 27  GLN D N   
6520  C CA  . GLN D  27  ? 1.9225 1.9348 1.6700 -0.1065 -0.0215 -0.0589 27  GLN D CA  
6521  C C   . GLN D  27  ? 1.9276 1.9348 1.6670 -0.1103 -0.0201 -0.0583 27  GLN D C   
6522  O O   . GLN D  27  ? 1.8223 1.8286 1.5612 -0.1118 -0.0174 -0.0589 27  GLN D O   
6523  C CB  . GLN D  27  ? 1.8593 1.8751 1.6134 -0.1054 -0.0192 -0.0603 27  GLN D CB  
6524  C CG  . GLN D  27  ? 1.8588 1.8763 1.6128 -0.1067 -0.0148 -0.0641 27  GLN D CG  
6525  C CD  . GLN D  27  ? 1.9944 2.0160 1.7498 -0.1054 -0.0131 -0.0678 27  GLN D CD  
6526  O OE1 . GLN D  27  ? 1.9684 1.9956 1.7301 -0.1033 -0.0119 -0.0702 27  GLN D OE1 
6527  N NE2 . GLN D  27  ? 2.0105 2.0293 1.7600 -0.1066 -0.0129 -0.0683 27  GLN D NE2 
6528  N N   . ASN D  28  ? 2.0852 2.0889 1.8179 -0.1119 -0.0219 -0.0572 28  ASN D N   
6529  C CA  . ASN D  28  ? 2.0627 2.0613 1.7868 -0.1157 -0.0208 -0.0565 28  ASN D CA  
6530  C C   . ASN D  28  ? 2.1484 2.1467 1.8685 -0.1170 -0.0174 -0.0606 28  ASN D C   
6531  O O   . ASN D  28  ? 2.1856 2.1881 1.9105 -0.1148 -0.0154 -0.0640 28  ASN D O   
6532  C CB  . ASN D  28  ? 1.8457 1.8403 1.5641 -0.1174 -0.0250 -0.0522 28  ASN D CB  
6533  C CG  . ASN D  28  ? 1.7969 1.7915 1.5129 -0.1171 -0.0269 -0.0530 28  ASN D CG  
6534  O OD1 . ASN D  28  ? 1.7200 1.7116 1.4308 -0.1190 -0.0301 -0.0501 28  ASN D OD1 
6535  N ND2 . ASN D  28  ? 1.9018 1.8999 1.6217 -0.1150 -0.0248 -0.0568 28  ASN D ND2 
6536  N N   . GLU D  29  ? 2.0253 2.0188 1.7368 -0.1205 -0.0168 -0.0601 29  GLU D N   
6537  C CA  . GLU D  29  ? 2.0334 2.0257 1.7404 -0.1223 -0.0129 -0.0639 29  GLU D CA  
6538  C C   . GLU D  29  ? 1.9604 1.9533 1.6664 -0.1216 -0.0130 -0.0661 29  GLU D C   
6539  O O   . GLU D  29  ? 1.7648 1.7572 1.4687 -0.1224 -0.0093 -0.0696 29  GLU D O   
6540  C CB  . GLU D  29  ? 2.1559 2.1424 1.8535 -0.1266 -0.0120 -0.0626 29  GLU D CB  
6541  C CG  . GLU D  29  ? 2.1701 2.1554 1.8683 -0.1276 -0.0118 -0.0600 29  GLU D CG  
6542  C CD  . GLU D  29  ? 2.2665 2.2462 1.9555 -0.1314 -0.0133 -0.0565 29  GLU D CD  
6543  O OE1 . GLU D  29  ? 2.1935 2.1709 1.8769 -0.1329 -0.0162 -0.0548 29  GLU D OE1 
6544  O OE2 . GLU D  29  ? 2.2099 2.1876 1.8973 -0.1330 -0.0115 -0.0554 29  GLU D OE2 
6545  N N   . GLN D  30  ? 1.9994 1.9930 1.7071 -0.1200 -0.0169 -0.0639 30  GLN D N   
6546  C CA  . GLN D  30  ? 1.9007 1.8947 1.6077 -0.1193 -0.0171 -0.0657 30  GLN D CA  
6547  C C   . GLN D  30  ? 1.9383 1.9381 1.6547 -0.1148 -0.0168 -0.0675 30  GLN D C   
6548  O O   . GLN D  30  ? 1.8717 1.8722 1.5892 -0.1135 -0.0171 -0.0685 30  GLN D O   
6549  C CB  . GLN D  30  ? 1.7130 1.7037 1.4148 -0.1208 -0.0214 -0.0625 30  GLN D CB  
6550  C CG  . GLN D  30  ? 1.6093 1.5943 1.3006 -0.1256 -0.0216 -0.0613 30  GLN D CG  
6551  C CD  . GLN D  30  ? 1.7054 1.6885 1.3942 -0.1270 -0.0261 -0.0561 30  GLN D CD  
6552  O OE1 . GLN D  30  ? 1.5803 1.5622 1.2665 -0.1278 -0.0299 -0.0538 30  GLN D OE1 
6553  N NE2 . GLN D  30  ? 1.7567 1.7397 1.4469 -0.1272 -0.0257 -0.0542 30  GLN D NE2 
6554  N N   . GLY D  31  ? 2.2198 2.2237 1.9431 -0.1126 -0.0161 -0.0676 31  GLY D N   
6555  C CA  . GLY D  31  ? 2.2481 2.2579 1.9801 -0.1086 -0.0157 -0.0692 31  GLY D CA  
6556  C C   . GLY D  31  ? 2.1215 2.1344 1.8599 -0.1063 -0.0186 -0.0668 31  GLY D C   
6557  O O   . GLY D  31  ? 2.0087 2.0191 1.7454 -0.1076 -0.0204 -0.0639 31  GLY D O   
6558  N N   . SER D  32  ? 1.9777 1.9960 1.7236 -0.1028 -0.0187 -0.0680 32  SER D N   
6559  C CA  . SER D  32  ? 1.8494 1.8708 1.6017 -0.1004 -0.0210 -0.0661 32  SER D CA  
6560  C C   . SER D  32  ? 1.7832 1.8067 1.5403 -0.0975 -0.0236 -0.0647 32  SER D C   
6561  O O   . SER D  32  ? 1.7824 1.8037 1.5367 -0.0979 -0.0242 -0.0644 32  SER D O   
6562  C CB  . SER D  32  ? 1.6931 1.7199 1.4517 -0.0989 -0.0182 -0.0686 32  SER D CB  
6563  O OG  . SER D  32  ? 1.7493 1.7744 1.5049 -0.1015 -0.0153 -0.0699 32  SER D OG  
6564  N N   . GLY D  33  ? 1.7614 1.7890 1.5255 -0.0948 -0.0248 -0.0640 33  GLY D N   
6565  C CA  . GLY D  33  ? 1.7348 1.7648 1.5040 -0.0918 -0.0270 -0.0627 33  GLY D CA  
6566  C C   . GLY D  33  ? 1.4907 1.5203 1.2626 -0.0908 -0.0304 -0.0595 33  GLY D C   
6567  O O   . GLY D  33  ? 1.3449 1.3716 1.1136 -0.0926 -0.0315 -0.0579 33  GLY D O   
6568  N N   . TYR D  34  ? 1.3803 1.4127 1.1578 -0.0878 -0.0320 -0.0586 34  TYR D N   
6569  C CA  . TYR D  34  ? 1.1908 1.2229 0.9711 -0.0866 -0.0352 -0.0557 34  TYR D CA  
6570  C C   . TYR D  34  ? 1.2214 1.2502 0.9995 -0.0867 -0.0383 -0.0529 34  TYR D C   
6571  O O   . TYR D  34  ? 1.2601 1.2887 1.0374 -0.0863 -0.0379 -0.0538 34  TYR D O   
6572  C CB  . TYR D  34  ? 1.1802 1.2180 0.9687 -0.0832 -0.0348 -0.0566 34  TYR D CB  
6573  C CG  . TYR D  34  ? 1.1155 1.1576 0.9068 -0.0830 -0.0317 -0.0595 34  TYR D CG  
6574  C CD1 . TYR D  34  ? 0.9638 1.0098 0.7567 -0.0823 -0.0289 -0.0625 34  TYR D CD1 
6575  C CD2 . TYR D  34  ? 1.0283 1.0708 0.8206 -0.0837 -0.0315 -0.0595 34  TYR D CD2 
6576  C CE1 . TYR D  34  ? 1.1120 1.1623 0.9075 -0.0823 -0.0263 -0.0651 34  TYR D CE1 
6577  C CE2 . TYR D  34  ? 0.8685 0.9150 0.6633 -0.0839 -0.0287 -0.0624 34  TYR D CE2 
6578  C CZ  . TYR D  34  ? 1.0166 1.0672 0.8130 -0.0832 -0.0262 -0.0651 34  TYR D CZ  
6579  O OH  . TYR D  34  ? 0.9680 1.0232 0.7670 -0.0836 -0.0236 -0.0680 34  TYR D OH  
6580  N N   . ALA D  35  ? 1.1637 1.1900 0.9409 -0.0873 -0.0415 -0.0497 35  ALA D N   
6581  C CA  . ALA D  35  ? 1.1950 1.2186 0.9705 -0.0875 -0.0449 -0.0468 35  ALA D CA  
6582  C C   . ALA D  35  ? 1.2317 1.2558 1.0114 -0.0858 -0.0480 -0.0438 35  ALA D C   
6583  O O   . ALA D  35  ? 1.3229 1.3453 1.1017 -0.0870 -0.0489 -0.0417 35  ALA D O   
6584  C CB  . ALA D  35  ? 1.2526 1.2711 1.0196 -0.0913 -0.0461 -0.0454 35  ALA D CB  
6585  N N   . ALA D  36  ? 1.0576 1.0839 0.8425 -0.0831 -0.0491 -0.0433 36  ALA D N   
6586  C CA  . ALA D  36  ? 1.1700 1.1969 0.9593 -0.0813 -0.0518 -0.0407 36  ALA D CA  
6587  C C   . ALA D  36  ? 1.1476 1.1706 0.9331 -0.0832 -0.0557 -0.0367 36  ALA D C   
6588  O O   . ALA D  36  ? 1.2410 1.2617 1.0223 -0.0848 -0.0570 -0.0360 36  ALA D O   
6589  C CB  . ALA D  36  ? 1.2612 1.2916 1.0569 -0.0779 -0.0517 -0.0413 36  ALA D CB  
6590  N N   . ASP D  37  ? 1.1296 1.1519 0.9186 -0.0828 -0.0569 -0.0336 37  ASP D N   
6591  C CA  . ASP D  37  ? 1.0805 1.0996 0.8682 -0.0843 -0.0604 -0.0289 37  ASP D CA  
6592  C C   . ASP D  37  ? 1.2099 1.2297 0.9997 -0.0827 -0.0634 -0.0275 37  ASP D C   
6593  O O   . ASP D  37  ? 1.2130 1.2353 1.0090 -0.0798 -0.0634 -0.0278 37  ASP D O   
6594  C CB  . ASP D  37  ? 1.0316 1.0501 0.8239 -0.0838 -0.0605 -0.0258 37  ASP D CB  
6595  C CG  . ASP D  37  ? 1.2202 1.2357 1.0114 -0.0854 -0.0641 -0.0205 37  ASP D CG  
6596  O OD1 . ASP D  37  ? 1.3646 1.3793 1.1602 -0.0848 -0.0643 -0.0174 37  ASP D OD1 
6597  O OD2 . ASP D  37  ? 1.3240 1.3380 1.1100 -0.0872 -0.0666 -0.0194 37  ASP D OD2 
6598  N N   . LEU D  38  ? 1.3598 1.3772 1.1441 -0.0850 -0.0659 -0.0261 38  LEU D N   
6599  C CA  . LEU D  38  ? 1.5190 1.5368 1.3044 -0.0840 -0.0686 -0.0252 38  LEU D CA  
6600  C C   . LEU D  38  ? 1.4434 1.4616 1.2351 -0.0823 -0.0714 -0.0211 38  LEU D C   
6601  O O   . LEU D  38  ? 1.2852 1.3056 1.0826 -0.0793 -0.0715 -0.0217 38  LEU D O   
6602  C CB  . LEU D  38  ? 1.8102 1.8251 1.5878 -0.0874 -0.0705 -0.0247 38  LEU D CB  
6603  C CG  . LEU D  38  ? 1.9821 1.9972 1.7601 -0.0868 -0.0698 -0.0266 38  LEU D CG  
6604  C CD1 . LEU D  38  ? 1.9138 1.9258 1.6840 -0.0908 -0.0713 -0.0260 38  LEU D CD1 
6605  C CD2 . LEU D  38  ? 1.9706 1.9875 1.7551 -0.0840 -0.0720 -0.0250 38  LEU D CD2 
6606  N N   . LYS D  39  ? 2.1526 2.1687 1.9435 -0.0841 -0.0736 -0.0169 39  LYS D N   
6607  C CA  . LYS D  39  ? 2.1356 2.1518 1.9323 -0.0828 -0.0765 -0.0124 39  LYS D CA  
6608  C C   . LYS D  39  ? 2.1104 2.1285 1.9153 -0.0796 -0.0744 -0.0126 39  LYS D C   
6609  O O   . LYS D  39  ? 2.0938 2.1131 1.9047 -0.0773 -0.0758 -0.0110 39  LYS D O   
6610  C CB  . LYS D  39  ? 2.3240 2.3377 2.1182 -0.0855 -0.0790 -0.0075 39  LYS D CB  
6611  C CG  . LYS D  39  ? 2.5552 2.5692 2.3555 -0.0844 -0.0823 -0.0023 39  LYS D CG  
6612  C CD  . LYS D  39  ? 2.8371 2.8490 2.6343 -0.0873 -0.0851 0.0028  39  LYS D CD  
6613  C CE  . LYS D  39  ? 2.8508 2.8633 2.6544 -0.0862 -0.0886 0.0082  39  LYS D CE  
6614  N NZ  . LYS D  39  ? 2.6653 2.6764 2.4661 -0.0891 -0.0918 0.0137  39  LYS D NZ  
6615  N N   . SER D  40  ? 1.3786 1.3970 1.1838 -0.0795 -0.0710 -0.0147 40  SER D N   
6616  C CA  . SER D  40  ? 1.2256 1.2456 1.0380 -0.0770 -0.0688 -0.0152 40  SER D CA  
6617  C C   . SER D  40  ? 1.0824 1.1057 0.8985 -0.0741 -0.0675 -0.0186 40  SER D C   
6618  O O   . SER D  40  ? 1.0404 1.0649 0.8629 -0.0717 -0.0680 -0.0173 40  SER D O   
6619  C CB  . SER D  40  ? 1.0991 1.1186 0.9102 -0.0781 -0.0653 -0.0170 40  SER D CB  
6620  O OG  . SER D  40  ? 1.1773 1.1978 0.9952 -0.0762 -0.0632 -0.0169 40  SER D OG  
6621  N N   . THR D  41  ? 1.0072 1.0321 0.8197 -0.0742 -0.0658 -0.0227 41  THR D N   
6622  C CA  . THR D  41  ? 0.9917 1.0201 0.8074 -0.0714 -0.0645 -0.0259 41  THR D CA  
6623  C C   . THR D  41  ? 1.0425 1.0711 0.8608 -0.0698 -0.0673 -0.0241 41  THR D C   
6624  O O   . THR D  41  ? 0.9842 1.0152 0.8078 -0.0671 -0.0669 -0.0247 41  THR D O   
6625  C CB  . THR D  41  ? 0.9450 0.9749 0.7562 -0.0720 -0.0623 -0.0301 41  THR D CB  
6626  O OG1 . THR D  41  ? 0.9691 0.9994 0.7789 -0.0731 -0.0594 -0.0321 41  THR D OG1 
6627  C CG2 . THR D  41  ? 0.8657 0.8994 0.6808 -0.0689 -0.0612 -0.0327 41  THR D CG2 
6628  N N   . GLN D  42  ? 1.2222 1.2483 1.0365 -0.0717 -0.0702 -0.0218 42  GLN D N   
6629  C CA  . GLN D  42  ? 1.1870 1.2131 1.0032 -0.0707 -0.0730 -0.0202 42  GLN D CA  
6630  C C   . GLN D  42  ? 1.0927 1.1190 0.9160 -0.0688 -0.0745 -0.0166 42  GLN D C   
6631  O O   . GLN D  42  ? 1.0774 1.1054 0.9054 -0.0663 -0.0749 -0.0168 42  GLN D O   
6632  C CB  . GLN D  42  ? 1.2754 1.2989 1.0855 -0.0737 -0.0759 -0.0185 42  GLN D CB  
6633  C CG  . GLN D  42  ? 1.3945 1.4181 1.2060 -0.0729 -0.0786 -0.0173 42  GLN D CG  
6634  C CD  . GLN D  42  ? 1.5063 1.5320 1.3199 -0.0704 -0.0762 -0.0209 42  GLN D CD  
6635  O OE1 . GLN D  42  ? 1.5191 1.5456 1.3313 -0.0702 -0.0728 -0.0242 42  GLN D OE1 
6636  N NE2 . GLN D  42  ? 1.4416 1.4682 1.2596 -0.0684 -0.0777 -0.0199 42  GLN D NE2 
6637  N N   . ASN D  43  ? 1.0499 1.0744 0.8741 -0.0701 -0.0752 -0.0134 43  ASN D N   
6638  C CA  . ASN D  43  ? 1.0682 1.0925 0.8995 -0.0685 -0.0763 -0.0098 43  ASN D CA  
6639  C C   . ASN D  43  ? 1.0087 1.0353 0.8461 -0.0656 -0.0733 -0.0120 43  ASN D C   
6640  O O   . ASN D  43  ? 0.9001 0.9275 0.7431 -0.0633 -0.0740 -0.0108 43  ASN D O   
6641  C CB  . ASN D  43  ? 1.1244 1.1463 0.9557 -0.0704 -0.0770 -0.0058 43  ASN D CB  
6642  C CG  . ASN D  43  ? 1.2274 1.2476 1.0573 -0.0721 -0.0813 -0.0011 43  ASN D CG  
6643  O OD1 . ASN D  43  ? 1.4385 1.4580 1.2620 -0.0744 -0.0831 -0.0014 43  ASN D OD1 
6644  N ND2 . ASN D  43  ? 1.1803 1.2001 1.0165 -0.0711 -0.0827 0.0033  43  ASN D ND2 
6645  N N   . ALA D  44  ? 1.0188 1.0464 0.8547 -0.0657 -0.0699 -0.0153 44  ALA D N   
6646  C CA  . ALA D  44  ? 0.8411 0.8712 0.6819 -0.0635 -0.0669 -0.0179 44  ALA D CA  
6647  C C   . ALA D  44  ? 0.8105 0.8435 0.6534 -0.0610 -0.0672 -0.0198 44  ALA D C   
6648  O O   . ALA D  44  ? 0.8234 0.8574 0.6720 -0.0588 -0.0669 -0.0192 44  ALA D O   
6649  C CB  . ALA D  44  ? 0.7248 0.7562 0.5629 -0.0645 -0.0636 -0.0216 44  ALA D CB  
6650  N N   . ILE D  45  ? 0.7719 0.8057 0.6102 -0.0614 -0.0677 -0.0220 45  ILE D N   
6651  C CA  . ILE D  45  ? 0.9031 0.9394 0.7430 -0.0591 -0.0679 -0.0236 45  ILE D CA  
6652  C C   . ILE D  45  ? 0.8960 0.9313 0.7402 -0.0577 -0.0705 -0.0204 45  ILE D C   
6653  O O   . ILE D  45  ? 0.9113 0.9485 0.7603 -0.0551 -0.0699 -0.0208 45  ILE D O   
6654  C CB  . ILE D  45  ? 0.9143 0.9507 0.7485 -0.0600 -0.0681 -0.0258 45  ILE D CB  
6655  C CG1 . ILE D  45  ? 0.8479 0.8864 0.6795 -0.0604 -0.0648 -0.0296 45  ILE D CG1 
6656  C CG2 . ILE D  45  ? 0.9016 0.9395 0.7380 -0.0578 -0.0687 -0.0264 45  ILE D CG2 
6657  C CD1 . ILE D  45  ? 1.0930 1.1316 0.9218 -0.0609 -0.0634 -0.0315 45  ILE D CD1 
6658  N N   . ASP D  46  ? 0.9120 0.9444 0.7544 -0.0595 -0.0735 -0.0170 46  ASP D N   
6659  C CA  . ASP D  46  ? 0.8879 0.9194 0.7344 -0.0586 -0.0763 -0.0136 46  ASP D CA  
6660  C C   . ASP D  46  ? 0.8780 0.9098 0.7318 -0.0567 -0.0754 -0.0117 46  ASP D C   
6661  O O   . ASP D  46  ? 0.9352 0.9680 0.7938 -0.0544 -0.0758 -0.0112 46  ASP D O   
6662  C CB  . ASP D  46  ? 0.9795 1.0083 0.8228 -0.0614 -0.0797 -0.0100 46  ASP D CB  
6663  C CG  . ASP D  46  ? 1.2363 1.2644 1.0729 -0.0632 -0.0810 -0.0116 46  ASP D CG  
6664  O OD1 . ASP D  46  ? 1.2741 1.3039 1.1099 -0.0618 -0.0796 -0.0149 46  ASP D OD1 
6665  O OD2 . ASP D  46  ? 1.2227 1.2488 1.0549 -0.0662 -0.0832 -0.0095 46  ASP D OD2 
6666  N N   . GLU D  47  ? 0.8472 0.8779 0.7018 -0.0576 -0.0740 -0.0108 47  GLU D N   
6667  C CA  . GLU D  47  ? 0.7344 0.7647 0.5958 -0.0562 -0.0728 -0.0089 47  GLU D CA  
6668  C C   . GLU D  47  ? 0.7569 0.7899 0.6215 -0.0539 -0.0695 -0.0125 47  GLU D C   
6669  O O   . GLU D  47  ? 0.6968 0.7302 0.5673 -0.0520 -0.0690 -0.0114 47  GLU D O   
6670  C CB  . GLU D  47  ? 0.6699 0.6980 0.5314 -0.0580 -0.0720 -0.0068 47  GLU D CB  
6671  C CG  . GLU D  47  ? 0.9088 0.9344 0.7684 -0.0601 -0.0755 -0.0022 47  GLU D CG  
6672  C CD  . GLU D  47  ? 0.9447 0.9680 0.8057 -0.0614 -0.0746 0.0007  47  GLU D CD  
6673  O OE1 . GLU D  47  ? 0.8796 0.9030 0.7411 -0.0614 -0.0710 -0.0017 47  GLU D OE1 
6674  O OE2 . GLU D  47  ? 1.0778 1.0994 0.9396 -0.0625 -0.0774 0.0054  47  GLU D OE2 
6675  N N   . ILE D  48  ? 0.6854 0.7206 0.5462 -0.0543 -0.0673 -0.0165 48  ILE D N   
6676  C CA  . ILE D  48  ? 0.5797 0.6182 0.4428 -0.0524 -0.0645 -0.0200 48  ILE D CA  
6677  C C   . ILE D  48  ? 0.6971 0.7374 0.5621 -0.0500 -0.0657 -0.0203 48  ILE D C   
6678  O O   . ILE D  48  ? 0.6737 0.7158 0.5431 -0.0480 -0.0644 -0.0210 48  ILE D O   
6679  C CB  . ILE D  48  ? 0.6409 0.6818 0.4995 -0.0534 -0.0622 -0.0241 48  ILE D CB  
6680  C CG1 . ILE D  48  ? 0.7185 0.7579 0.5763 -0.0554 -0.0602 -0.0242 48  ILE D CG1 
6681  C CG2 . ILE D  48  ? 0.5406 0.5858 0.4012 -0.0513 -0.0600 -0.0274 48  ILE D CG2 
6682  C CD1 . ILE D  48  ? 0.6886 0.7276 0.5521 -0.0547 -0.0581 -0.0236 48  ILE D CD1 
6683  N N   . THR D  49  ? 0.6395 0.6793 0.5010 -0.0504 -0.0681 -0.0199 49  THR D N   
6684  C CA  . THR D  49  ? 0.6120 0.6529 0.4752 -0.0484 -0.0693 -0.0198 49  THR D CA  
6685  C C   . THR D  49  ? 0.7152 0.7548 0.5845 -0.0470 -0.0706 -0.0166 49  THR D C   
6686  O O   . THR D  49  ? 0.6762 0.7176 0.5495 -0.0447 -0.0697 -0.0172 49  THR D O   
6687  C CB  . THR D  49  ? 0.6986 0.7383 0.5570 -0.0496 -0.0717 -0.0195 49  THR D CB  
6688  O OG1 . THR D  49  ? 0.7595 0.8007 0.6129 -0.0504 -0.0700 -0.0229 49  THR D OG1 
6689  C CG2 . THR D  49  ? 0.6129 0.6532 0.4739 -0.0476 -0.0730 -0.0190 49  THR D CG2 
6690  N N   . ASN D  50  ? 0.6065 0.6431 0.4765 -0.0485 -0.0727 -0.0129 50  ASN D N   
6691  C CA  . ASN D  50  ? 0.7417 0.7769 0.6180 -0.0474 -0.0740 -0.0093 50  ASN D CA  
6692  C C   . ASN D  50  ? 0.6805 0.7165 0.5621 -0.0458 -0.0709 -0.0101 50  ASN D C   
6693  O O   . ASN D  50  ? 0.6080 0.6442 0.4949 -0.0438 -0.0709 -0.0089 50  ASN D O   
6694  C CB  . ASN D  50  ? 0.7715 0.8038 0.6478 -0.0496 -0.0764 -0.0051 50  ASN D CB  
6695  C CG  . ASN D  50  ? 0.8233 0.8543 0.7059 -0.0485 -0.0784 -0.0009 50  ASN D CG  
6696  O OD1 . ASN D  50  ? 0.8952 0.9259 0.7777 -0.0486 -0.0814 0.0008  50  ASN D OD1 
6697  N ND2 . ASN D  50  ? 0.6909 0.7211 0.5793 -0.0476 -0.0765 0.0006  50  ASN D ND2 
6698  N N   . LYS D  51  ? 0.6728 0.7092 0.5529 -0.0467 -0.0682 -0.0122 51  LYS D N   
6699  C CA  . LYS D  51  ? 0.6841 0.7213 0.5684 -0.0457 -0.0649 -0.0135 51  LYS D CA  
6700  C C   . LYS D  51  ? 0.6611 0.7016 0.5468 -0.0434 -0.0636 -0.0163 51  LYS D C   
6701  O O   . LYS D  51  ? 0.5987 0.6393 0.4895 -0.0418 -0.0626 -0.0156 51  LYS D O   
6702  C CB  . LYS D  51  ? 0.7045 0.7420 0.5858 -0.0475 -0.0623 -0.0159 51  LYS D CB  
6703  C CG  . LYS D  51  ? 0.5573 0.5957 0.4425 -0.0470 -0.0585 -0.0177 51  LYS D CG  
6704  C CD  . LYS D  51  ? 0.7116 0.7493 0.5944 -0.0492 -0.0561 -0.0192 51  LYS D CD  
6705  C CE  . LYS D  51  ? 0.6859 0.7239 0.5726 -0.0491 -0.0523 -0.0209 51  LYS D CE  
6706  N NZ  . LYS D  51  ? 0.7568 0.7926 0.6427 -0.0514 -0.0501 -0.0211 51  LYS D NZ  
6707  N N   . VAL D  52  ? 0.6213 0.6646 0.5024 -0.0433 -0.0636 -0.0192 52  VAL D N   
6708  C CA  . VAL D  52  ? 0.5778 0.6246 0.4597 -0.0411 -0.0625 -0.0216 52  VAL D CA  
6709  C C   . VAL D  52  ? 0.6738 0.7199 0.5592 -0.0391 -0.0644 -0.0194 52  VAL D C   
6710  O O   . VAL D  52  ? 0.7927 0.8404 0.6817 -0.0371 -0.0632 -0.0200 52  VAL D O   
6711  C CB  . VAL D  52  ? 0.5185 0.5683 0.3952 -0.0412 -0.0623 -0.0246 52  VAL D CB  
6712  C CG1 . VAL D  52  ? 0.4923 0.5461 0.3703 -0.0388 -0.0610 -0.0268 52  VAL D CG1 
6713  C CG2 . VAL D  52  ? 0.5826 0.6332 0.4559 -0.0433 -0.0604 -0.0268 52  VAL D CG2 
6714  N N   . ASN D  53  ? 0.5906 0.6343 0.4749 -0.0397 -0.0674 -0.0169 53  ASN D N   
6715  C CA  . ASN D  53  ? 0.6472 0.6900 0.5347 -0.0382 -0.0695 -0.0147 53  ASN D CA  
6716  C C   . ASN D  53  ? 0.7774 0.8187 0.6716 -0.0371 -0.0691 -0.0121 53  ASN D C   
6717  O O   . ASN D  53  ? 0.7310 0.7728 0.6290 -0.0351 -0.0691 -0.0116 53  ASN D O   
6718  C CB  . ASN D  53  ? 0.7734 0.8141 0.6582 -0.0397 -0.0728 -0.0125 53  ASN D CB  
6719  C CG  . ASN D  53  ? 0.8820 0.9242 0.7616 -0.0399 -0.0732 -0.0150 53  ASN D CG  
6720  O OD1 . ASN D  53  ? 0.7441 0.7891 0.6228 -0.0384 -0.0711 -0.0179 53  ASN D OD1 
6721  N ND2 . ASN D  53  ? 0.9484 0.9886 0.8245 -0.0418 -0.0757 -0.0137 53  ASN D ND2 
6722  N N   . SER D  54  ? 0.7019 0.7411 0.5978 -0.0385 -0.0685 -0.0104 54  SER D N   
6723  C CA  . SER D  54  ? 0.5487 0.5860 0.4512 -0.0377 -0.0677 -0.0078 54  SER D CA  
6724  C C   . SER D  54  ? 0.6303 0.6695 0.5358 -0.0359 -0.0644 -0.0103 54  SER D C   
6725  O O   . SER D  54  ? 0.5948 0.6337 0.5051 -0.0341 -0.0642 -0.0091 54  SER D O   
6726  C CB  . SER D  54  ? 0.5579 0.5926 0.4615 -0.0396 -0.0672 -0.0057 54  SER D CB  
6727  O OG  . SER D  54  ? 0.7283 0.7613 0.6295 -0.0412 -0.0706 -0.0028 54  SER D OG  
6728  N N   . VAL D  55  ? 0.5770 0.6182 0.4796 -0.0366 -0.0617 -0.0137 55  VAL D N   
6729  C CA  . VAL D  55  ? 0.5853 0.6287 0.4898 -0.0354 -0.0584 -0.0164 55  VAL D CA  
6730  C C   . VAL D  55  ? 0.6306 0.6764 0.5357 -0.0330 -0.0591 -0.0171 55  VAL D C   
6731  O O   . VAL D  55  ? 0.6298 0.6764 0.5383 -0.0316 -0.0571 -0.0178 55  VAL D O   
6732  C CB  . VAL D  55  ? 0.6004 0.6466 0.5006 -0.0368 -0.0560 -0.0203 55  VAL D CB  
6733  C CG1 . VAL D  55  ? 0.6287 0.6779 0.5302 -0.0357 -0.0530 -0.0232 55  VAL D CG1 
6734  C CG2 . VAL D  55  ? 0.4314 0.4750 0.3315 -0.0391 -0.0548 -0.0197 55  VAL D CG2 
6735  N N   . ILE D  56  ? 0.6627 0.7093 0.5645 -0.0327 -0.0616 -0.0170 56  ILE D N   
6736  C CA  . ILE D  56  ? 0.5667 0.6155 0.4690 -0.0305 -0.0621 -0.0176 56  ILE D CA  
6737  C C   . ILE D  56  ? 0.6282 0.6744 0.5346 -0.0293 -0.0643 -0.0143 56  ILE D C   
6738  O O   . ILE D  56  ? 0.5571 0.6039 0.4673 -0.0273 -0.0635 -0.0140 56  ILE D O   
6739  C CB  . ILE D  56  ? 0.5139 0.5649 0.4107 -0.0306 -0.0633 -0.0194 56  ILE D CB  
6740  C CG1 . ILE D  56  ? 0.6071 0.6616 0.5003 -0.0314 -0.0610 -0.0229 56  ILE D CG1 
6741  C CG2 . ILE D  56  ? 0.5205 0.5731 0.4182 -0.0282 -0.0640 -0.0194 56  ILE D CG2 
6742  C CD1 . ILE D  56  ? 0.6063 0.6629 0.4946 -0.0316 -0.0617 -0.0246 56  ILE D CD1 
6743  N N   . GLU D  57  ? 0.6024 0.6460 0.5083 -0.0306 -0.0671 -0.0117 57  GLU D N   
6744  C CA  . GLU D  57  ? 0.6446 0.6862 0.5539 -0.0299 -0.0697 -0.0085 57  GLU D CA  
6745  C C   . GLU D  57  ? 0.6133 0.6531 0.5296 -0.0288 -0.0688 -0.0061 57  GLU D C   
6746  O O   . GLU D  57  ? 0.7552 0.7945 0.6754 -0.0273 -0.0699 -0.0043 57  GLU D O   
6747  C CB  . GLU D  57  ? 0.8840 0.9235 0.7908 -0.0321 -0.0729 -0.0063 57  GLU D CB  
6748  C CG  . GLU D  57  ? 1.2609 1.2994 1.1695 -0.0317 -0.0759 -0.0038 57  GLU D CG  
6749  C CD  . GLU D  57  ? 1.3557 1.3918 1.2700 -0.0321 -0.0776 0.0005  57  GLU D CD  
6750  O OE1 . GLU D  57  ? 1.2258 1.2605 1.1411 -0.0334 -0.0773 0.0020  57  GLU D OE1 
6751  O OE2 . GLU D  57  ? 1.2010 1.2365 1.1189 -0.0311 -0.0793 0.0025  57  GLU D OE2 
6752  N N   . LYS D  58  ? 0.5911 0.6300 0.5093 -0.0295 -0.0666 -0.0061 58  LYS D N   
6753  C CA  . LYS D  58  ? 0.5528 0.5896 0.4779 -0.0287 -0.0652 -0.0038 58  LYS D CA  
6754  C C   . LYS D  58  ? 0.6442 0.6825 0.5720 -0.0266 -0.0624 -0.0057 58  LYS D C   
6755  O O   . LYS D  58  ? 0.5860 0.6225 0.5196 -0.0258 -0.0607 -0.0042 58  LYS D O   
6756  C CB  . LYS D  58  ? 0.4762 0.5111 0.4025 -0.0304 -0.0633 -0.0032 58  LYS D CB  
6757  C CG  . LYS D  58  ? 0.6422 0.6752 0.5675 -0.0323 -0.0661 -0.0001 58  LYS D CG  
6758  C CD  . LYS D  58  ? 0.6326 0.6639 0.5624 -0.0318 -0.0693 0.0043  58  LYS D CD  
6759  C CE  . LYS D  58  ? 0.7093 0.7391 0.6376 -0.0339 -0.0723 0.0075  58  LYS D CE  
6760  N NZ  . LYS D  58  ? 0.6830 0.7118 0.6158 -0.0337 -0.0757 0.0120  58  LYS D NZ  
6761  N N   . MET D  59  ? 0.5655 0.6070 0.4893 -0.0257 -0.0619 -0.0088 59  MET D N   
6762  C CA  . MET D  59  ? 0.5702 0.6136 0.4958 -0.0238 -0.0594 -0.0106 59  MET D CA  
6763  C C   . MET D  59  ? 0.6777 0.7214 0.6050 -0.0217 -0.0611 -0.0094 59  MET D C   
6764  O O   . MET D  59  ? 0.9348 0.9812 0.8586 -0.0207 -0.0614 -0.0112 59  MET D O   
6765  C CB  . MET D  59  ? 0.7886 0.8359 0.7092 -0.0240 -0.0574 -0.0146 59  MET D CB  
6766  C CG  . MET D  59  ? 0.6870 0.7366 0.6089 -0.0224 -0.0547 -0.0165 59  MET D CG  
6767  S SD  . MET D  59  ? 0.7566 0.8032 0.6845 -0.0225 -0.0515 -0.0156 59  MET D SD  
6768  C CE  . MET D  59  ? 0.5863 0.6361 0.5104 -0.0241 -0.0478 -0.0200 59  MET D CE  
6769  N N   . ASN D  60  ? 0.7577 0.7986 0.6907 -0.0210 -0.0620 -0.0062 60  ASN D N   
6770  C CA  . ASN D  60  ? 0.8706 0.9117 0.8060 -0.0189 -0.0632 -0.0051 60  ASN D CA  
6771  C C   . ASN D  60  ? 0.7209 0.7620 0.6605 -0.0171 -0.0602 -0.0055 60  ASN D C   
6772  O O   . ASN D  60  ? 0.8066 0.8451 0.7519 -0.0170 -0.0593 -0.0034 60  ASN D O   
6773  C CB  . ASN D  60  ? 1.0919 1.1303 1.0308 -0.0194 -0.0664 -0.0013 60  ASN D CB  
6774  C CG  . ASN D  60  ? 1.2611 1.2998 1.2015 -0.0176 -0.0679 -0.0005 60  ASN D CG  
6775  O OD1 . ASN D  60  ? 1.2913 1.3321 1.2279 -0.0167 -0.0678 -0.0027 60  ASN D OD1 
6776  N ND2 . ASN D  60  ? 1.1965 1.2330 1.1428 -0.0172 -0.0692 0.0028  60  ASN D ND2 
6777  N N   . THR D  61  ? 0.7720 0.8162 0.7090 -0.0158 -0.0586 -0.0081 61  THR D N   
6778  C CA  . THR D  61  ? 0.7838 0.8285 0.7235 -0.0143 -0.0556 -0.0090 61  THR D CA  
6779  C C   . THR D  61  ? 0.7159 0.7595 0.6599 -0.0122 -0.0563 -0.0070 61  THR D C   
6780  O O   . THR D  61  ? 0.6426 0.6860 0.5862 -0.0116 -0.0590 -0.0057 61  THR D O   
6781  C CB  . THR D  61  ? 0.7868 0.8359 0.7215 -0.0139 -0.0537 -0.0125 61  THR D CB  
6782  O OG1 . THR D  61  ? 0.7609 0.8124 0.6923 -0.0128 -0.0556 -0.0129 61  THR D OG1 
6783  C CG2 . THR D  61  ? 0.6349 0.6853 0.5659 -0.0161 -0.0525 -0.0148 61  THR D CG2 
6784  N N   . GLN D  62  ? 0.7510 0.7936 0.6992 -0.0111 -0.0537 -0.0067 62  GLN D N   
6785  C CA  . GLN D  62  ? 0.8444 0.8860 0.7970 -0.0090 -0.0538 -0.0050 62  GLN D CA  
6786  C C   . GLN D  62  ? 0.7295 0.7744 0.6786 -0.0073 -0.0531 -0.0070 62  GLN D C   
6787  O O   . GLN D  62  ? 0.7180 0.7662 0.6624 -0.0076 -0.0517 -0.0097 62  GLN D O   
6788  C CB  . GLN D  62  ? 0.7365 0.7755 0.6948 -0.0087 -0.0508 -0.0042 62  GLN D CB  
6789  C CG  . GLN D  62  ? 0.5797 0.6151 0.5429 -0.0100 -0.0512 -0.0015 62  GLN D CG  
6790  C CD  . GLN D  62  ? 0.7607 0.7944 0.7278 -0.0096 -0.0548 0.0021  62  GLN D CD  
6791  O OE1 . GLN D  62  ? 0.9326 0.9669 0.8965 -0.0105 -0.0581 0.0026  62  GLN D OE1 
6792  N NE2 . GLN D  62  ? 0.7148 0.7461 0.6888 -0.0084 -0.0542 0.0045  62  GLN D NE2 
6793  N N   . PHE D  63  ? 0.7040 0.7483 0.6556 -0.0054 -0.0541 -0.0055 63  PHE D N   
6794  C CA  . PHE D  63  ? 0.6724 0.7196 0.6217 -0.0034 -0.0530 -0.0068 63  PHE D CA  
6795  C C   . PHE D  63  ? 0.5658 0.6133 0.5173 -0.0024 -0.0495 -0.0075 63  PHE D C   
6796  O O   . PHE D  63  ? 0.8159 0.8606 0.7727 -0.0015 -0.0487 -0.0058 63  PHE D O   
6797  C CB  . PHE D  63  ? 0.6445 0.6908 0.5958 -0.0018 -0.0550 -0.0050 63  PHE D CB  
6798  C CG  . PHE D  63  ? 0.7619 0.8111 0.7108 0.0004  -0.0539 -0.0061 63  PHE D CG  
6799  C CD1 . PHE D  63  ? 0.5984 0.6499 0.5430 0.0007  -0.0553 -0.0071 63  PHE D CD1 
6800  C CD2 . PHE D  63  ? 0.6391 0.6888 0.5903 0.0022  -0.0514 -0.0061 63  PHE D CD2 
6801  C CE1 . PHE D  63  ? 0.6186 0.6729 0.5616 0.0029  -0.0541 -0.0078 63  PHE D CE1 
6802  C CE2 . PHE D  63  ? 0.7016 0.7542 0.6507 0.0043  -0.0504 -0.0068 63  PHE D CE2 
6803  C CZ  . PHE D  63  ? 0.6603 0.7153 0.6055 0.0047  -0.0518 -0.0075 63  PHE D CZ  
6804  N N   . THR D  64  ? 0.4432 0.4940 0.3905 -0.0029 -0.0474 -0.0102 64  THR D N   
6805  C CA  . THR D  64  ? 0.7134 0.7648 0.6617 -0.0025 -0.0440 -0.0113 64  THR D CA  
6806  C C   . THR D  64  ? 0.5937 0.6501 0.5370 -0.0016 -0.0428 -0.0134 64  THR D C   
6807  O O   . THR D  64  ? 0.5085 0.5684 0.4472 -0.0021 -0.0440 -0.0148 64  THR D O   
6808  C CB  . THR D  64  ? 0.7442 0.7941 0.6931 -0.0048 -0.0418 -0.0125 64  THR D CB  
6809  O OG1 . THR D  64  ? 0.6442 0.6959 0.5887 -0.0067 -0.0429 -0.0140 64  THR D OG1 
6810  C CG2 . THR D  64  ? 0.7827 0.8274 0.7381 -0.0052 -0.0419 -0.0099 64  THR D CG2 
6811  N N   . ALA D  65  ? 0.5335 0.5906 0.4781 -0.0002 -0.0405 -0.0135 65  ALA D N   
6812  C CA  . ALA D  65  ? 0.5087 0.5709 0.4489 0.0005  -0.0392 -0.0152 65  ALA D CA  
6813  C C   . ALA D  65  ? 0.5456 0.6088 0.4845 -0.0013 -0.0359 -0.0174 65  ALA D C   
6814  O O   . ALA D  65  ? 0.5461 0.6083 0.4868 -0.0007 -0.0334 -0.0173 65  ALA D O   
6815  C CB  . ALA D  65  ? 0.5086 0.5712 0.4503 0.0033  -0.0389 -0.0137 65  ALA D CB  
6816  N N   . VAL D  66  ? 0.4705 0.5353 0.4062 -0.0037 -0.0357 -0.0195 66  VAL D N   
6817  C CA  . VAL D  66  ? 0.4219 0.4880 0.3554 -0.0059 -0.0325 -0.0221 66  VAL D CA  
6818  C C   . VAL D  66  ? 0.5919 0.6632 0.5220 -0.0049 -0.0313 -0.0231 66  VAL D C   
6819  O O   . VAL D  66  ? 0.7560 0.8309 0.6842 -0.0029 -0.0331 -0.0223 66  VAL D O   
6820  C CB  . VAL D  66  ? 0.4494 0.5173 0.3796 -0.0086 -0.0328 -0.0243 66  VAL D CB  
6821  C CG1 . VAL D  66  ? 0.5071 0.5775 0.4347 -0.0079 -0.0362 -0.0238 66  VAL D CG1 
6822  C CG2 . VAL D  66  ? 0.4468 0.5191 0.3726 -0.0106 -0.0301 -0.0275 66  VAL D CG2 
6823  N N   . GLY D  67  ? 0.4857 0.5574 0.4150 -0.0063 -0.0280 -0.0249 67  GLY D N   
6824  C CA  . GLY D  67  ? 0.7606 0.8373 0.6865 -0.0057 -0.0266 -0.0257 67  GLY D CA  
6825  C C   . GLY D  67  ? 0.5955 0.6693 0.5250 -0.0035 -0.0253 -0.0238 67  GLY D C   
6826  O O   . GLY D  67  ? 0.4317 0.5032 0.3645 -0.0010 -0.0271 -0.0212 67  GLY D O   
6827  N N   . LYS D  68  ? 0.5684 0.6421 0.4970 -0.0048 -0.0218 -0.0253 68  LYS D N   
6828  C CA  . LYS D  68  ? 0.4702 0.5411 0.4019 -0.0030 -0.0200 -0.0238 68  LYS D CA  
6829  C C   . LYS D  68  ? 0.5474 0.6234 0.4744 -0.0033 -0.0180 -0.0251 68  LYS D C   
6830  O O   . LYS D  68  ? 0.4894 0.5707 0.4111 -0.0054 -0.0178 -0.0274 68  LYS D O   
6831  C CB  . LYS D  68  ? 0.5601 0.6243 0.4967 -0.0044 -0.0171 -0.0240 68  LYS D CB  
6832  C CG  . LYS D  68  ? 0.5226 0.5820 0.4641 -0.0043 -0.0190 -0.0224 68  LYS D CG  
6833  C CD  . LYS D  68  ? 0.5902 0.6456 0.5376 -0.0014 -0.0204 -0.0190 68  LYS D CD  
6834  C CE  . LYS D  68  ? 0.6736 0.7260 0.6245 -0.0012 -0.0235 -0.0171 68  LYS D CE  
6835  N NZ  . LYS D  68  ? 0.7214 0.7776 0.6693 0.0001  -0.0274 -0.0164 68  LYS D NZ  
6836  N N   . GLU D  69  ? 0.5907 0.6654 0.5196 -0.0013 -0.0167 -0.0235 69  GLU D N   
6837  C CA  . GLU D  69  ? 0.5347 0.6141 0.4591 -0.0015 -0.0148 -0.0243 69  GLU D CA  
6838  C C   . GLU D  69  ? 0.4728 0.5480 0.3987 -0.0028 -0.0106 -0.0253 69  GLU D C   
6839  O O   . GLU D  69  ? 0.5565 0.6256 0.4881 -0.0014 -0.0096 -0.0237 69  GLU D O   
6840  C CB  . GLU D  69  ? 0.6125 0.6948 0.5370 0.0022  -0.0168 -0.0214 69  GLU D CB  
6841  C CG  . GLU D  69  ? 0.7718 0.8584 0.6947 0.0036  -0.0205 -0.0204 69  GLU D CG  
6842  C CD  . GLU D  69  ? 0.8609 0.9491 0.7850 0.0074  -0.0221 -0.0174 69  GLU D CD  
6843  O OE1 . GLU D  69  ? 0.8444 0.9284 0.7722 0.0092  -0.0209 -0.0156 69  GLU D OE1 
6844  O OE2 . GLU D  69  ? 0.7207 0.8142 0.6422 0.0086  -0.0243 -0.0167 69  GLU D OE2 
6845  N N   . PHE D  70  ? 0.4932 0.5715 0.4141 -0.0057 -0.0079 -0.0282 70  PHE D N   
6846  C CA  . PHE D  70  ? 0.5208 0.5954 0.4423 -0.0074 -0.0034 -0.0296 70  PHE D CA  
6847  C C   . PHE D  70  ? 0.5471 0.6275 0.4624 -0.0083 -0.0018 -0.0307 70  PHE D C   
6848  O O   . PHE D  70  ? 0.5583 0.6458 0.4679 -0.0096 -0.0034 -0.0319 70  PHE D O   
6849  C CB  . PHE D  70  ? 0.5491 0.6201 0.4712 -0.0111 -0.0007 -0.0327 70  PHE D CB  
6850  C CG  . PHE D  70  ? 0.5484 0.6145 0.4762 -0.0105 -0.0024 -0.0315 70  PHE D CG  
6851  C CD1 . PHE D  70  ? 0.4344 0.4932 0.3693 -0.0090 -0.0013 -0.0294 70  PHE D CD1 
6852  C CD2 . PHE D  70  ? 0.5184 0.5870 0.4443 -0.0116 -0.0050 -0.0324 70  PHE D CD2 
6853  C CE1 . PHE D  70  ? 0.4698 0.5245 0.4099 -0.0086 -0.0030 -0.0280 70  PHE D CE1 
6854  C CE2 . PHE D  70  ? 0.4250 0.4891 0.3557 -0.0112 -0.0066 -0.0311 70  PHE D CE2 
6855  C CZ  . PHE D  70  ? 0.3946 0.4520 0.3324 -0.0098 -0.0057 -0.0289 70  PHE D CZ  
6856  N N   . ASN D  71  ? 0.4752 0.5526 0.3915 -0.0079 0.0013  -0.0303 71  ASN D N   
6857  C CA  . ASN D  71  ? 0.5590 0.6415 0.4693 -0.0089 0.0031  -0.0312 71  ASN D CA  
6858  C C   . ASN D  71  ? 0.5880 0.6712 0.4936 -0.0138 0.0067  -0.0355 71  ASN D C   
6859  O O   . ASN D  71  ? 0.5326 0.6116 0.4404 -0.0162 0.0083  -0.0377 71  ASN D O   
6860  C CB  . ASN D  71  ? 0.5264 0.6055 0.4395 -0.0065 0.0051  -0.0290 71  ASN D CB  
6861  C CG  . ASN D  71  ? 0.6196 0.6899 0.5383 -0.0073 0.0089  -0.0297 71  ASN D CG  
6862  O OD1 . ASN D  71  ? 0.7148 0.7827 0.6323 -0.0109 0.0123  -0.0329 71  ASN D OD1 
6863  N ND2 . ASN D  71  ? 0.7484 0.8137 0.6735 -0.0040 0.0086  -0.0267 71  ASN D ND2 
6864  N N   . HIS D  72  ? 0.5807 0.6693 0.4800 -0.0155 0.0082  -0.0367 72  HIS D N   
6865  C CA  . HIS D  72  ? 0.7072 0.7977 0.6008 -0.0206 0.0114  -0.0410 72  HIS D CA  
6866  C C   . HIS D  72  ? 0.6794 0.7614 0.5762 -0.0230 0.0166  -0.0435 72  HIS D C   
6867  O O   . HIS D  72  ? 0.6863 0.7682 0.5800 -0.0274 0.0195  -0.0474 72  HIS D O   
6868  C CB  . HIS D  72  ? 0.7277 0.8254 0.6141 -0.0217 0.0120  -0.0413 72  HIS D CB  
6869  C CG  . HIS D  72  ? 1.0306 1.1253 0.9184 -0.0195 0.0142  -0.0392 72  HIS D CG  
6870  N ND1 . HIS D  72  ? 1.1287 1.2241 1.0194 -0.0147 0.0115  -0.0349 72  HIS D ND1 
6871  C CD2 . HIS D  72  ? 1.0211 1.1118 0.9078 -0.0216 0.0191  -0.0409 72  HIS D CD2 
6872  C CE1 . HIS D  72  ? 1.1598 1.2518 1.0511 -0.0138 0.0144  -0.0339 72  HIS D CE1 
6873  N NE2 . HIS D  72  ? 0.9457 1.0349 0.8346 -0.0179 0.0191  -0.0375 72  HIS D NE2 
6874  N N   . LEU D  73  ? 0.5338 0.6089 0.4372 -0.0203 0.0180  -0.0412 73  LEU D N   
6875  C CA  . LEU D  73  ? 0.6112 0.6779 0.5187 -0.0221 0.0232  -0.0429 73  LEU D CA  
6876  C C   . LEU D  73  ? 0.6141 0.6744 0.5293 -0.0211 0.0225  -0.0420 73  LEU D C   
6877  O O   . LEU D  73  ? 0.5907 0.6434 0.5118 -0.0212 0.0261  -0.0420 73  LEU D O   
6878  C CB  . LEU D  73  ? 0.6645 0.7273 0.5743 -0.0202 0.0259  -0.0412 73  LEU D CB  
6879  C CG  . LEU D  73  ? 0.7510 0.8184 0.6532 -0.0222 0.0283  -0.0427 73  LEU D CG  
6880  C CD1 . LEU D  73  ? 0.7217 0.7851 0.6269 -0.0196 0.0305  -0.0403 73  LEU D CD1 
6881  C CD2 . LEU D  73  ? 0.5965 0.6632 0.4939 -0.0278 0.0330  -0.0477 73  LEU D CD2 
6882  N N   . GLU D  74  ? 0.5019 0.5654 0.4173 -0.0201 0.0180  -0.0411 74  GLU D N   
6883  C CA  . GLU D  74  ? 0.4583 0.5167 0.3803 -0.0192 0.0168  -0.0400 74  GLU D CA  
6884  C C   . GLU D  74  ? 0.5954 0.6571 0.5141 -0.0220 0.0153  -0.0425 74  GLU D C   
6885  O O   . GLU D  74  ? 0.5212 0.5823 0.4430 -0.0206 0.0120  -0.0409 74  GLU D O   
6886  C CB  . GLU D  74  ? 0.4612 0.5191 0.3882 -0.0146 0.0123  -0.0356 74  GLU D CB  
6887  C CG  . GLU D  74  ? 0.4580 0.5116 0.3896 -0.0117 0.0137  -0.0330 74  GLU D CG  
6888  C CD  . GLU D  74  ? 0.7008 0.7546 0.6367 -0.0074 0.0092  -0.0289 74  GLU D CD  
6889  O OE1 . GLU D  74  ? 0.5965 0.6563 0.5284 -0.0061 0.0054  -0.0280 74  GLU D OE1 
6890  O OE2 . GLU D  74  ? 0.6272 0.6750 0.5704 -0.0054 0.0096  -0.0266 74  GLU D OE2 
6891  N N   . LYS D  75  ? 0.5116 0.5767 0.4238 -0.0261 0.0180  -0.0464 75  LYS D N   
6892  C CA  . LYS D  75  ? 0.5682 0.6372 0.4766 -0.0291 0.0169  -0.0491 75  LYS D CA  
6893  C C   . LYS D  75  ? 0.5262 0.5885 0.4400 -0.0302 0.0185  -0.0498 75  LYS D C   
6894  O O   . LYS D  75  ? 0.4918 0.5560 0.4048 -0.0312 0.0162  -0.0505 75  LYS D O   
6895  C CB  . LYS D  75  ? 0.5397 0.6134 0.4402 -0.0336 0.0199  -0.0533 75  LYS D CB  
6896  C CG  . LYS D  75  ? 0.7622 0.8394 0.6588 -0.0373 0.0195  -0.0566 75  LYS D CG  
6897  C CD  . LYS D  75  ? 0.8015 0.8853 0.6965 -0.0352 0.0137  -0.0547 75  LYS D CD  
6898  C CE  . LYS D  75  ? 0.9413 1.0345 0.8298 -0.0349 0.0113  -0.0543 75  LYS D CE  
6899  N NZ  . LYS D  75  ? 1.1074 1.2070 0.9947 -0.0330 0.0060  -0.0526 75  LYS D NZ  
6900  N N   . ARG D  76  ? 0.5408 0.5952 0.4604 -0.0302 0.0225  -0.0495 76  ARG D N   
6901  C CA  . ARG D  76  ? 0.5356 0.5833 0.4610 -0.0312 0.0246  -0.0498 76  ARG D CA  
6902  C C   . ARG D  76  ? 0.5316 0.5775 0.4630 -0.0278 0.0200  -0.0459 76  ARG D C   
6903  O O   . ARG D  76  ? 0.5414 0.5865 0.4739 -0.0289 0.0190  -0.0464 76  ARG D O   
6904  C CB  . ARG D  76  ? 0.4545 0.4945 0.3848 -0.0321 0.0305  -0.0504 76  ARG D CB  
6905  C CG  . ARG D  76  ? 0.4716 0.5120 0.3964 -0.0367 0.0361  -0.0552 76  ARG D CG  
6906  C CD  . ARG D  76  ? 0.4371 0.4696 0.3669 -0.0373 0.0422  -0.0556 76  ARG D CD  
6907  N NE  . ARG D  76  ? 0.4762 0.5075 0.4090 -0.0337 0.0414  -0.0523 76  ARG D NE  
6908  C CZ  . ARG D  76  ? 0.4514 0.4757 0.3928 -0.0313 0.0434  -0.0497 76  ARG D CZ  
6909  N NH1 . ARG D  76  ? 0.5692 0.5870 0.5172 -0.0322 0.0463  -0.0497 76  ARG D NH1 
6910  N NH2 . ARG D  76  ? 0.5240 0.5477 0.4677 -0.0282 0.0425  -0.0468 76  ARG D NH2 
6911  N N   . ILE D  77  ? 0.5045 0.5498 0.4395 -0.0238 0.0173  -0.0421 77  ILE D N   
6912  C CA  . ILE D  77  ? 0.4837 0.5280 0.4236 -0.0207 0.0126  -0.0384 77  ILE D CA  
6913  C C   . ILE D  77  ? 0.3896 0.4408 0.3240 -0.0205 0.0078  -0.0386 77  ILE D C   
6914  O O   . ILE D  77  ? 0.4784 0.5290 0.4150 -0.0196 0.0046  -0.0371 77  ILE D O   
6915  C CB  . ILE D  77  ? 0.3847 0.4265 0.3298 -0.0167 0.0110  -0.0345 77  ILE D CB  
6916  C CG1 . ILE D  77  ? 0.6843 0.7301 0.6249 -0.0158 0.0116  -0.0348 77  ILE D CG1 
6917  C CG2 . ILE D  77  ? 0.5033 0.5371 0.4565 -0.0163 0.0146  -0.0332 77  ILE D CG2 
6918  C CD1 . ILE D  77  ? 0.7299 0.7731 0.6755 -0.0120 0.0105  -0.0311 77  ILE D CD1 
6919  N N   . GLU D  78  ? 0.4146 0.4724 0.3419 -0.0213 0.0074  -0.0404 78  GLU D N   
6920  C CA  . GLU D  78  ? 0.4246 0.4895 0.3466 -0.0214 0.0034  -0.0409 78  GLU D CA  
6921  C C   . GLU D  78  ? 0.4782 0.5431 0.3987 -0.0247 0.0041  -0.0436 78  GLU D C   
6922  O O   . GLU D  78  ? 0.4885 0.5556 0.4085 -0.0242 0.0005  -0.0430 78  GLU D O   
6923  C CB  . GLU D  78  ? 0.4545 0.5267 0.3696 -0.0221 0.0034  -0.0423 78  GLU D CB  
6924  C CG  . GLU D  78  ? 0.5534 0.6335 0.4634 -0.0220 -0.0006 -0.0425 78  GLU D CG  
6925  C CD  . GLU D  78  ? 0.9215 1.0093 0.8247 -0.0230 -0.0005 -0.0437 78  GLU D CD  
6926  O OE1 . GLU D  78  ? 1.0397 1.1272 0.9426 -0.0222 0.0014  -0.0431 78  GLU D OE1 
6927  O OE2 . GLU D  78  ? 1.0756 1.1701 0.9740 -0.0246 -0.0023 -0.0453 78  GLU D OE2 
6928  N N   . ASN D  79  ? 0.5005 0.5626 0.4203 -0.0283 0.0090  -0.0469 79  ASN D N   
6929  C CA  . ASN D  79  ? 0.4801 0.5415 0.3988 -0.0317 0.0104  -0.0497 79  ASN D CA  
6930  C C   . ASN D  79  ? 0.5254 0.5800 0.4512 -0.0307 0.0102  -0.0476 79  ASN D C   
6931  O O   . ASN D  79  ? 0.6033 0.6583 0.5287 -0.0320 0.0089  -0.0484 79  ASN D O   
6932  C CB  . ASN D  79  ? 0.4564 0.5170 0.3719 -0.0360 0.0161  -0.0540 79  ASN D CB  
6933  C CG  . ASN D  79  ? 0.7117 0.7807 0.6187 -0.0382 0.0157  -0.0568 79  ASN D CG  
6934  O OD1 . ASN D  79  ? 0.7311 0.8068 0.6344 -0.0375 0.0114  -0.0562 79  ASN D OD1 
6935  N ND2 . ASN D  79  ? 0.7402 0.8089 0.6441 -0.0410 0.0201  -0.0596 79  ASN D ND2 
6936  N N   . LEU D  80  ? 0.4880 0.5366 0.4205 -0.0285 0.0114  -0.0449 80  LEU D N   
6937  C CA  . LEU D  80  ? 0.4407 0.4833 0.3805 -0.0271 0.0106  -0.0421 80  LEU D CA  
6938  C C   . LEU D  80  ? 0.4834 0.5294 0.4226 -0.0248 0.0046  -0.0396 80  LEU D C   
6939  O O   . LEU D  80  ? 0.4176 0.4625 0.3580 -0.0255 0.0031  -0.0393 80  LEU D O   
6940  C CB  . LEU D  80  ? 0.4024 0.4392 0.3494 -0.0246 0.0121  -0.0391 80  LEU D CB  
6941  C CG  . LEU D  80  ? 0.4779 0.5074 0.4334 -0.0242 0.0138  -0.0369 80  LEU D CG  
6942  C CD1 . LEU D  80  ? 0.3571 0.3830 0.3195 -0.0207 0.0126  -0.0327 80  LEU D CD1 
6943  C CD2 . LEU D  80  ? 0.4520 0.4817 0.4083 -0.0245 0.0106  -0.0359 80  LEU D CD2 
6944  N N   . ASN D  81  ? 0.4483 0.4982 0.3856 -0.0221 0.0013  -0.0379 81  ASN D N   
6945  C CA  . ASN D  81  ? 0.3722 0.4256 0.3084 -0.0199 -0.0041 -0.0358 81  ASN D CA  
6946  C C   . ASN D  81  ? 0.4969 0.5553 0.4274 -0.0222 -0.0056 -0.0383 81  ASN D C   
6947  O O   . ASN D  81  ? 0.4473 0.5056 0.3785 -0.0218 -0.0086 -0.0371 81  ASN D O   
6948  C CB  . ASN D  81  ? 0.3815 0.4387 0.3159 -0.0170 -0.0064 -0.0341 81  ASN D CB  
6949  C CG  . ASN D  81  ? 0.5145 0.5753 0.4476 -0.0149 -0.0116 -0.0321 81  ASN D CG  
6950  O OD1 . ASN D  81  ? 0.5980 0.6555 0.5354 -0.0134 -0.0140 -0.0295 81  ASN D OD1 
6951  N ND2 . ASN D  81  ? 0.4966 0.5643 0.4239 -0.0148 -0.0132 -0.0333 81  ASN D ND2 
6952  N N   . LYS D  82  ? 0.4401 0.5029 0.3648 -0.0248 -0.0034 -0.0418 82  LYS D N   
6953  C CA  . LYS D  82  ? 0.4782 0.5461 0.3976 -0.0273 -0.0044 -0.0444 82  LYS D CA  
6954  C C   . LYS D  82  ? 0.5305 0.5939 0.4522 -0.0296 -0.0027 -0.0456 82  LYS D C   
6955  O O   . LYS D  82  ? 0.4949 0.5606 0.4147 -0.0304 -0.0050 -0.0461 82  LYS D O   
6956  C CB  . LYS D  82  ? 0.4175 0.4909 0.3306 -0.0300 -0.0020 -0.0480 82  LYS D CB  
6957  C CG  . LYS D  82  ? 0.6241 0.7023 0.5323 -0.0333 -0.0022 -0.0512 82  LYS D CG  
6958  C CD  . LYS D  82  ? 0.6709 0.7551 0.5728 -0.0362 0.0000  -0.0546 82  LYS D CD  
6959  C CE  . LYS D  82  ? 1.0811 1.1692 0.9787 -0.0401 0.0005  -0.0582 82  LYS D CE  
6960  N NZ  . LYS D  82  ? 0.9558 1.0479 0.8526 -0.0386 -0.0041 -0.0568 82  LYS D NZ  
6961  N N   . LYS D  83  ? 0.5190 0.5759 0.4451 -0.0307 0.0014  -0.0459 83  LYS D N   
6962  C CA  . LYS D  83  ? 0.4897 0.5418 0.4188 -0.0328 0.0035  -0.0466 83  LYS D CA  
6963  C C   . LYS D  83  ? 0.4930 0.5424 0.4265 -0.0305 -0.0003 -0.0430 83  LYS D C   
6964  O O   . LYS D  83  ? 0.4388 0.4881 0.3716 -0.0320 -0.0011 -0.0436 83  LYS D O   
6965  C CB  . LYS D  83  ? 0.4101 0.4556 0.3439 -0.0341 0.0091  -0.0473 83  LYS D CB  
6966  C CG  . LYS D  83  ? 0.4583 0.4984 0.3959 -0.0361 0.0116  -0.0478 83  LYS D CG  
6967  C CD  . LYS D  83  ? 0.3725 0.4068 0.3135 -0.0382 0.0181  -0.0495 83  LYS D CD  
6968  C CE  . LYS D  83  ? 0.4803 0.5090 0.4290 -0.0352 0.0189  -0.0458 83  LYS D CE  
6969  N NZ  . LYS D  83  ? 0.5262 0.5483 0.4796 -0.0372 0.0255  -0.0471 83  LYS D NZ  
6970  N N   . VAL D  84  ? 0.4279 0.4752 0.3657 -0.0271 -0.0027 -0.0392 84  VAL D N   
6971  C CA  . VAL D  84  ? 0.4388 0.4837 0.3807 -0.0251 -0.0064 -0.0356 84  VAL D CA  
6972  C C   . VAL D  84  ? 0.4288 0.4792 0.3657 -0.0247 -0.0110 -0.0356 84  VAL D C   
6973  O O   . VAL D  84  ? 0.4893 0.5383 0.4274 -0.0245 -0.0135 -0.0341 84  VAL D O   
6974  C CB  . VAL D  84  ? 0.3385 0.3802 0.2862 -0.0218 -0.0079 -0.0316 84  VAL D CB  
6975  C CG1 . VAL D  84  ? 0.5374 0.5838 0.4817 -0.0195 -0.0106 -0.0311 84  VAL D CG1 
6976  C CG2 . VAL D  84  ? 0.5613 0.5997 0.5137 -0.0205 -0.0112 -0.0280 84  VAL D CG2 
6977  N N   . ASP D  85  ? 0.3894 0.4459 0.3208 -0.0245 -0.0119 -0.0374 85  ASP D N   
6978  C CA  . ASP D  85  ? 0.3455 0.4076 0.2721 -0.0242 -0.0157 -0.0377 85  ASP D CA  
6979  C C   . ASP D  85  ? 0.4602 0.5243 0.3832 -0.0275 -0.0145 -0.0409 85  ASP D C   
6980  O O   . ASP D  85  ? 0.4954 0.5605 0.4171 -0.0276 -0.0172 -0.0404 85  ASP D O   
6981  C CB  . ASP D  85  ? 0.3572 0.4255 0.2795 -0.0228 -0.0168 -0.0383 85  ASP D CB  
6982  C CG  . ASP D  85  ? 0.5936 0.6610 0.5189 -0.0191 -0.0193 -0.0348 85  ASP D CG  
6983  O OD1 . ASP D  85  ? 0.5971 0.6599 0.5272 -0.0176 -0.0209 -0.0320 85  ASP D OD1 
6984  O OD2 . ASP D  85  ? 0.7651 0.8365 0.6881 -0.0177 -0.0195 -0.0347 85  ASP D OD2 
6985  N N   . ASP D  86  ? 0.4473 0.5117 0.3683 -0.0304 -0.0104 -0.0442 86  ASP D N   
6986  C CA  . ASP D  86  ? 0.3598 0.4260 0.2774 -0.0340 -0.0088 -0.0476 86  ASP D CA  
6987  C C   . ASP D  86  ? 0.4927 0.5527 0.4145 -0.0350 -0.0077 -0.0467 86  ASP D C   
6988  O O   . ASP D  86  ? 0.5021 0.5631 0.4217 -0.0371 -0.0077 -0.0484 86  ASP D O   
6989  C CB  . ASP D  86  ? 0.5639 0.6320 0.4783 -0.0370 -0.0044 -0.0515 86  ASP D CB  
6990  C CG  . ASP D  86  ? 0.8733 0.9494 0.7821 -0.0369 -0.0058 -0.0528 86  ASP D CG  
6991  O OD1 . ASP D  86  ? 0.9480 1.0286 0.8551 -0.0347 -0.0100 -0.0511 86  ASP D OD1 
6992  O OD2 . ASP D  86  ? 0.9538 1.0318 0.8600 -0.0390 -0.0027 -0.0554 86  ASP D OD2 
6993  N N   . GLY D  87  ? 0.5838 0.6374 0.5118 -0.0334 -0.0067 -0.0439 87  GLY D N   
6994  C CA  . GLY D  87  ? 0.4696 0.5172 0.4025 -0.0340 -0.0058 -0.0423 87  GLY D CA  
6995  C C   . GLY D  87  ? 0.4585 0.5066 0.3916 -0.0325 -0.0106 -0.0396 87  GLY D C   
6996  O O   . GLY D  87  ? 0.5206 0.5680 0.4528 -0.0342 -0.0107 -0.0401 87  GLY D O   
6997  N N   . PHE D  88  ? 0.3936 0.4429 0.3276 -0.0294 -0.0144 -0.0366 88  PHE D N   
6998  C CA  . PHE D  88  ? 0.4014 0.4513 0.3350 -0.0280 -0.0191 -0.0342 88  PHE D CA  
6999  C C   . PHE D  88  ? 0.4694 0.5247 0.3965 -0.0295 -0.0205 -0.0368 88  PHE D C   
7000  O O   . PHE D  88  ? 0.5568 0.6118 0.4831 -0.0299 -0.0228 -0.0360 88  PHE D O   
7001  C CB  . PHE D  88  ? 0.4159 0.4665 0.3509 -0.0247 -0.0224 -0.0312 88  PHE D CB  
7002  C CG  . PHE D  88  ? 0.5155 0.5607 0.4574 -0.0230 -0.0217 -0.0280 88  PHE D CG  
7003  C CD1 . PHE D  88  ? 0.3848 0.4305 0.3285 -0.0203 -0.0231 -0.0262 88  PHE D CD1 
7004  C CD2 . PHE D  88  ? 0.4732 0.5130 0.4202 -0.0241 -0.0196 -0.0268 88  PHE D CD2 
7005  C CE1 . PHE D  88  ? 0.3564 0.3973 0.3067 -0.0189 -0.0224 -0.0233 88  PHE D CE1 
7006  C CE2 . PHE D  88  ? 0.4688 0.5040 0.4228 -0.0225 -0.0189 -0.0236 88  PHE D CE2 
7007  C CZ  . PHE D  88  ? 0.4620 0.4978 0.4176 -0.0199 -0.0204 -0.0219 88  PHE D CZ  
7008  N N   . LEU D  89  ? 0.4657 0.5263 0.3883 -0.0303 -0.0193 -0.0398 89  LEU D N   
7009  C CA  . LEU D  89  ? 0.4038 0.4703 0.3206 -0.0318 -0.0205 -0.0424 89  LEU D CA  
7010  C C   . LEU D  89  ? 0.4948 0.5598 0.4108 -0.0351 -0.0184 -0.0446 89  LEU D C   
7011  O O   . LEU D  89  ? 0.5030 0.5698 0.4165 -0.0358 -0.0204 -0.0450 89  LEU D O   
7012  C CB  . LEU D  89  ? 0.4141 0.4867 0.3268 -0.0323 -0.0193 -0.0451 89  LEU D CB  
7013  C CG  . LEU D  89  ? 0.5139 0.5934 0.4209 -0.0341 -0.0201 -0.0479 89  LEU D CG  
7014  C CD1 . LEU D  89  ? 0.4900 0.5714 0.3959 -0.0324 -0.0243 -0.0461 89  LEU D CD1 
7015  C CD2 . LEU D  89  ? 0.4218 0.5078 0.3252 -0.0343 -0.0194 -0.0497 89  LEU D CD2 
7016  N N   . ASP D  90  ? 0.4086 0.4699 0.3268 -0.0371 -0.0140 -0.0461 90  ASP D N   
7017  C CA  . ASP D  90  ? 0.3955 0.4548 0.3133 -0.0403 -0.0113 -0.0484 90  ASP D CA  
7018  C C   . ASP D  90  ? 0.4239 0.4779 0.3454 -0.0398 -0.0126 -0.0454 90  ASP D C   
7019  O O   . ASP D  90  ? 0.4880 0.5423 0.4076 -0.0417 -0.0127 -0.0465 90  ASP D O   
7020  C CB  . ASP D  90  ? 0.4593 0.5156 0.3787 -0.0427 -0.0058 -0.0509 90  ASP D CB  
7021  C CG  . ASP D  90  ? 0.7442 0.8065 0.6583 -0.0447 -0.0040 -0.0550 90  ASP D CG  
7022  O OD1 . ASP D  90  ? 0.8621 0.9310 0.7712 -0.0450 -0.0066 -0.0563 90  ASP D OD1 
7023  O OD2 . ASP D  90  ? 0.8428 0.9034 0.7577 -0.0461 0.0001  -0.0568 90  ASP D OD2 
7024  N N   . ILE D  91  ? 0.4168 0.4662 0.3437 -0.0374 -0.0137 -0.0415 91  ILE D N   
7025  C CA  . ILE D  91  ? 0.4843 0.5291 0.4150 -0.0367 -0.0154 -0.0380 91  ILE D CA  
7026  C C   . ILE D  91  ? 0.5445 0.5923 0.4714 -0.0360 -0.0201 -0.0370 91  ILE D C   
7027  O O   . ILE D  91  ? 0.5148 0.5615 0.4408 -0.0375 -0.0205 -0.0370 91  ILE D O   
7028  C CB  . ILE D  91  ? 0.4702 0.5104 0.4074 -0.0341 -0.0162 -0.0338 91  ILE D CB  
7029  C CG1 . ILE D  91  ? 0.4194 0.4555 0.3610 -0.0349 -0.0111 -0.0345 91  ILE D CG1 
7030  C CG2 . ILE D  91  ? 0.5270 0.5635 0.4676 -0.0335 -0.0189 -0.0299 91  ILE D CG2 
7031  C CD1 . ILE D  91  ? 0.5916 0.6235 0.5402 -0.0324 -0.0116 -0.0305 91  ILE D CD1 
7032  N N   . TRP D  92  ? 0.4379 0.4895 0.3629 -0.0338 -0.0234 -0.0362 92  TRP D N   
7033  C CA  . TRP D  92  ? 0.2992 0.3533 0.2209 -0.0329 -0.0276 -0.0351 92  TRP D CA  
7034  C C   . TRP D  92  ? 0.4036 0.4623 0.3197 -0.0350 -0.0274 -0.0385 92  TRP D C   
7035  O O   . TRP D  92  ? 0.5724 0.6309 0.4867 -0.0355 -0.0296 -0.0378 92  TRP D O   
7036  C CB  . TRP D  92  ? 0.3850 0.4419 0.3062 -0.0300 -0.0305 -0.0337 92  TRP D CB  
7037  C CG  . TRP D  92  ? 0.4755 0.5280 0.4020 -0.0278 -0.0322 -0.0297 92  TRP D CG  
7038  C CD1 . TRP D  92  ? 0.4237 0.4748 0.3538 -0.0260 -0.0313 -0.0285 92  TRP D CD1 
7039  C CD2 . TRP D  92  ? 0.4153 0.4643 0.3441 -0.0274 -0.0349 -0.0264 92  TRP D CD2 
7040  N NE1 . TRP D  92  ? 0.4663 0.5134 0.4011 -0.0245 -0.0334 -0.0246 92  TRP D NE1 
7041  C CE2 . TRP D  92  ? 0.4694 0.5152 0.4034 -0.0253 -0.0358 -0.0232 92  TRP D CE2 
7042  C CE3 . TRP D  92  ? 0.4216 0.4698 0.3484 -0.0287 -0.0368 -0.0257 92  TRP D CE3 
7043  C CZ2 . TRP D  92  ? 0.4364 0.4788 0.3737 -0.0246 -0.0386 -0.0194 92  TRP D CZ2 
7044  C CZ3 . TRP D  92  ? 0.5480 0.5926 0.4777 -0.0280 -0.0396 -0.0219 92  TRP D CZ3 
7045  C CH2 . TRP D  92  ? 0.5164 0.5584 0.4514 -0.0260 -0.0406 -0.0188 92  TRP D CH2 
7046  N N   . THR D  93  ? 0.4762 0.5389 0.3895 -0.0364 -0.0249 -0.0420 93  THR D N   
7047  C CA  . THR D  93  ? 0.4135 0.4809 0.3218 -0.0387 -0.0245 -0.0454 93  THR D CA  
7048  C C   . THR D  93  ? 0.4347 0.4984 0.3436 -0.0414 -0.0226 -0.0461 93  THR D C   
7049  O O   . THR D  93  ? 0.4764 0.5412 0.3828 -0.0422 -0.0242 -0.0464 93  THR D O   
7050  C CB  . THR D  93  ? 0.4571 0.5295 0.3626 -0.0402 -0.0219 -0.0490 93  THR D CB  
7051  O OG1 . THR D  93  ? 0.4469 0.5235 0.3514 -0.0377 -0.0239 -0.0482 93  THR D OG1 
7052  C CG2 . THR D  93  ? 0.4785 0.5559 0.3795 -0.0429 -0.0213 -0.0524 93  THR D CG2 
7053  N N   . TYR D  94  ? 0.5096 0.5687 0.4222 -0.0426 -0.0189 -0.0464 94  TYR D N   
7054  C CA  . TYR D  94  ? 0.4715 0.5266 0.3852 -0.0451 -0.0164 -0.0470 94  TYR D CA  
7055  C C   . TYR D  94  ? 0.4543 0.5057 0.3699 -0.0441 -0.0193 -0.0433 94  TYR D C   
7056  O O   . TYR D  94  ? 0.4806 0.5320 0.3940 -0.0457 -0.0196 -0.0440 94  TYR D O   
7057  C CB  . TYR D  94  ? 0.3775 0.4277 0.2956 -0.0463 -0.0117 -0.0475 94  TYR D CB  
7058  C CG  . TYR D  94  ? 0.4751 0.5214 0.3944 -0.0491 -0.0082 -0.0487 94  TYR D CG  
7059  C CD1 . TYR D  94  ? 0.4862 0.5356 0.4015 -0.0524 -0.0055 -0.0532 94  TYR D CD1 
7060  C CD2 . TYR D  94  ? 0.5484 0.5883 0.4731 -0.0486 -0.0076 -0.0452 94  TYR D CD2 
7061  C CE1 . TYR D  94  ? 0.5664 0.6122 0.4829 -0.0551 -0.0021 -0.0544 94  TYR D CE1 
7062  C CE2 . TYR D  94  ? 0.4794 0.5156 0.4054 -0.0510 -0.0042 -0.0460 94  TYR D CE2 
7063  C CZ  . TYR D  94  ? 0.6457 0.6847 0.5676 -0.0543 -0.0013 -0.0508 94  TYR D CZ  
7064  O OH  . TYR D  94  ? 0.6655 0.7007 0.5888 -0.0568 0.0023  -0.0518 94  TYR D OH  
7065  N N   . ASN D  95  ? 0.4045 0.4528 0.3240 -0.0414 -0.0215 -0.0393 95  ASN D N   
7066  C CA  . ASN D  95  ? 0.5039 0.5488 0.4252 -0.0405 -0.0246 -0.0354 95  ASN D CA  
7067  C C   . ASN D  95  ? 0.5051 0.5536 0.4213 -0.0403 -0.0284 -0.0356 95  ASN D C   
7068  O O   . ASN D  95  ? 0.5710 0.6179 0.4862 -0.0414 -0.0294 -0.0345 95  ASN D O   
7069  C CB  . ASN D  95  ? 0.5367 0.5783 0.4633 -0.0379 -0.0263 -0.0312 95  ASN D CB  
7070  C CG  . ASN D  95  ? 0.6414 0.6779 0.5742 -0.0381 -0.0226 -0.0300 95  ASN D CG  
7071  O OD1 . ASN D  95  ? 0.6246 0.6603 0.5575 -0.0402 -0.0182 -0.0328 95  ASN D OD1 
7072  N ND2 . ASN D  95  ? 0.6991 0.7322 0.6374 -0.0361 -0.0241 -0.0257 95  ASN D ND2 
7073  N N   . ALA D  96  ? 0.4228 0.4764 0.3359 -0.0390 -0.0302 -0.0368 96  ALA D N   
7074  C CA  . ALA D  96  ? 0.4882 0.5454 0.3967 -0.0386 -0.0335 -0.0371 96  ALA D CA  
7075  C C   . ALA D  96  ? 0.5514 0.6111 0.4558 -0.0413 -0.0321 -0.0403 96  ALA D C   
7076  O O   . ALA D  96  ? 0.5683 0.6279 0.4702 -0.0419 -0.0339 -0.0398 96  ALA D O   
7077  C CB  . ALA D  96  ? 0.4678 0.5298 0.3744 -0.0365 -0.0351 -0.0377 96  ALA D CB  
7078  N N   . GLU D  97  ? 0.4679 0.5298 0.3714 -0.0431 -0.0286 -0.0438 97  GLU D N   
7079  C CA  . GLU D  97  ? 0.5297 0.5943 0.4297 -0.0459 -0.0269 -0.0471 97  GLU D CA  
7080  C C   . GLU D  97  ? 0.5348 0.5942 0.4362 -0.0477 -0.0257 -0.0461 97  GLU D C   
7081  O O   . GLU D  97  ? 0.5060 0.5664 0.4043 -0.0489 -0.0266 -0.0468 97  GLU D O   
7082  C CB  . GLU D  97  ? 0.5684 0.6361 0.4677 -0.0478 -0.0232 -0.0510 97  GLU D CB  
7083  C CG  . GLU D  97  ? 0.5103 0.5844 0.4073 -0.0465 -0.0242 -0.0524 97  GLU D CG  
7084  C CD  . GLU D  97  ? 0.7248 0.8055 0.6172 -0.0469 -0.0260 -0.0543 97  GLU D CD  
7085  O OE1 . GLU D  97  ? 0.7580 0.8448 0.6484 -0.0466 -0.0262 -0.0560 97  GLU D OE1 
7086  O OE2 . GLU D  97  ? 0.9086 0.9884 0.7996 -0.0476 -0.0272 -0.0539 97  GLU D OE2 
7087  N N   . LEU D  98  ? 0.4581 0.5120 0.3642 -0.0477 -0.0236 -0.0443 98  LEU D N   
7088  C CA  . LEU D  98  ? 0.4824 0.5310 0.3906 -0.0492 -0.0223 -0.0427 98  LEU D CA  
7089  C C   . LEU D  98  ? 0.5696 0.6160 0.4776 -0.0479 -0.0264 -0.0388 98  LEU D C   
7090  O O   . LEU D  98  ? 0.5275 0.5721 0.4342 -0.0494 -0.0264 -0.0384 98  LEU D O   
7091  C CB  . LEU D  98  ? 0.4241 0.4674 0.3383 -0.0492 -0.0190 -0.0413 98  LEU D CB  
7092  C CG  . LEU D  98  ? 0.4779 0.5203 0.3927 -0.0520 -0.0136 -0.0449 98  LEU D CG  
7093  C CD1 . LEU D  98  ? 0.7806 0.8199 0.6954 -0.0544 -0.0116 -0.0451 98  LEU D CD1 
7094  C CD2 . LEU D  98  ? 0.5757 0.6245 0.4859 -0.0533 -0.0125 -0.0497 98  LEU D CD2 
7095  N N   . LEU D  99  ? 0.5632 0.6098 0.4723 -0.0453 -0.0297 -0.0361 99  LEU D N   
7096  C CA  . LEU D  99  ? 0.6302 0.6749 0.5388 -0.0443 -0.0337 -0.0324 99  LEU D CA  
7097  C C   . LEU D  99  ? 0.5914 0.6393 0.4942 -0.0454 -0.0354 -0.0342 99  LEU D C   
7098  O O   . LEU D  99  ? 0.6510 0.6965 0.5527 -0.0464 -0.0367 -0.0324 99  LEU D O   
7099  C CB  . LEU D  99  ? 0.5908 0.6360 0.5011 -0.0415 -0.0368 -0.0300 99  LEU D CB  
7100  C CG  . LEU D  99  ? 0.5796 0.6231 0.4893 -0.0406 -0.0410 -0.0263 99  LEU D CG  
7101  C CD1 . LEU D  99  ? 0.5087 0.5469 0.4224 -0.0413 -0.0410 -0.0226 99  LEU D CD1 
7102  C CD2 . LEU D  99  ? 0.5727 0.6172 0.4835 -0.0381 -0.0438 -0.0246 99  LEU D CD2 
7103  N N   . VAL D  100 ? 0.4806 0.5340 0.3798 -0.0452 -0.0354 -0.0374 100 VAL D N   
7104  C CA  . VAL D  100 ? 0.5583 0.6151 0.4524 -0.0462 -0.0367 -0.0393 100 VAL D CA  
7105  C C   . VAL D  100 ? 0.5254 0.5812 0.4178 -0.0491 -0.0342 -0.0412 100 VAL D C   
7106  O O   . VAL D  100 ? 0.6246 0.6793 0.5144 -0.0500 -0.0355 -0.0405 100 VAL D O   
7107  C CB  . VAL D  100 ? 0.4366 0.5000 0.3280 -0.0454 -0.0368 -0.0423 100 VAL D CB  
7108  C CG1 . VAL D  100 ? 0.5586 0.6257 0.4452 -0.0467 -0.0372 -0.0446 100 VAL D CG1 
7109  C CG2 . VAL D  100 ? 0.4759 0.5402 0.3682 -0.0424 -0.0396 -0.0403 100 VAL D CG2 
7110  N N   . LEU D  101 ? 0.5309 0.5870 0.4249 -0.0506 -0.0304 -0.0437 101 LEU D N   
7111  C CA  . LEU D  101 ? 0.5472 0.6020 0.4401 -0.0536 -0.0274 -0.0458 101 LEU D CA  
7112  C C   . LEU D  101 ? 0.6067 0.6554 0.5015 -0.0540 -0.0278 -0.0423 101 LEU D C   
7113  O O   . LEU D  101 ? 0.6202 0.6683 0.5122 -0.0555 -0.0282 -0.0424 101 LEU D O   
7114  C CB  . LEU D  101 ? 0.4810 0.5360 0.3760 -0.0552 -0.0230 -0.0487 101 LEU D CB  
7115  C CG  . LEU D  101 ? 0.5388 0.6002 0.4317 -0.0554 -0.0221 -0.0525 101 LEU D CG  
7116  C CD1 . LEU D  101 ? 0.6268 0.6877 0.5212 -0.0579 -0.0173 -0.0557 101 LEU D CD1 
7117  C CD2 . LEU D  101 ? 0.4809 0.5481 0.3689 -0.0562 -0.0236 -0.0549 101 LEU D CD2 
7118  N N   . LEU D  102 ? 0.5772 0.6215 0.4770 -0.0527 -0.0278 -0.0389 102 LEU D N   
7119  C CA  . LEU D  102 ? 0.5958 0.6345 0.4983 -0.0530 -0.0282 -0.0349 102 LEU D CA  
7120  C C   . LEU D  102 ? 0.6193 0.6577 0.5186 -0.0524 -0.0325 -0.0322 102 LEU D C   
7121  O O   . LEU D  102 ? 0.5510 0.5865 0.4496 -0.0538 -0.0326 -0.0305 102 LEU D O   
7122  C CB  . LEU D  102 ? 0.5704 0.6051 0.4793 -0.0513 -0.0277 -0.0316 102 LEU D CB  
7123  C CG  . LEU D  102 ? 0.8049 0.8370 0.7158 -0.0495 -0.0318 -0.0263 102 LEU D CG  
7124  C CD1 . LEU D  102 ? 0.7323 0.7592 0.6468 -0.0504 -0.0308 -0.0226 102 LEU D CD1 
7125  C CD2 . LEU D  102 ? 1.0081 1.0401 0.9231 -0.0471 -0.0328 -0.0246 102 LEU D CD2 
7126  N N   . GLU D  103 ? 0.5747 0.6160 0.4721 -0.0506 -0.0359 -0.0319 103 GLU D N   
7127  C CA  . GLU D  103 ? 0.5633 0.6043 0.4575 -0.0502 -0.0399 -0.0296 103 GLU D CA  
7128  C C   . GLU D  103 ? 0.6115 0.6552 0.4998 -0.0519 -0.0400 -0.0324 103 GLU D C   
7129  O O   . GLU D  103 ? 0.6968 0.7386 0.5824 -0.0529 -0.0417 -0.0307 103 GLU D O   
7130  C CB  . GLU D  103 ? 0.4752 0.5180 0.3697 -0.0477 -0.0431 -0.0282 103 GLU D CB  
7131  C CG  . GLU D  103 ? 0.8333 0.8726 0.7334 -0.0461 -0.0441 -0.0242 103 GLU D CG  
7132  C CD  . GLU D  103 ? 1.0823 1.1169 0.9844 -0.0471 -0.0450 -0.0201 103 GLU D CD  
7133  O OE1 . GLU D  103 ? 1.0457 1.0795 0.9452 -0.0473 -0.0484 -0.0178 103 GLU D OE1 
7134  O OE2 . GLU D  103 ? 1.0826 1.1142 0.9890 -0.0477 -0.0422 -0.0192 103 GLU D OE2 
7135  N N   . ASN D  104 ? 0.5864 0.6348 0.4726 -0.0523 -0.0381 -0.0366 104 ASN D N   
7136  C CA  . ASN D  104 ? 0.5807 0.6323 0.4619 -0.0538 -0.0379 -0.0395 104 ASN D CA  
7137  C C   . ASN D  104 ? 0.6894 0.7381 0.5698 -0.0564 -0.0358 -0.0398 104 ASN D C   
7138  O O   . ASN D  104 ? 0.6896 0.7386 0.5659 -0.0576 -0.0366 -0.0403 104 ASN D O   
7139  C CB  . ASN D  104 ? 0.3658 0.4233 0.2459 -0.0539 -0.0361 -0.0438 104 ASN D CB  
7140  C CG  . ASN D  104 ? 0.4986 0.5601 0.3777 -0.0515 -0.0385 -0.0439 104 ASN D CG  
7141  O OD1 . ASN D  104 ? 0.5298 0.5899 0.4079 -0.0502 -0.0415 -0.0414 104 ASN D OD1 
7142  N ND2 . ASN D  104 ? 0.5315 0.5980 0.4109 -0.0510 -0.0372 -0.0466 104 ASN D ND2 
7143  N N   . GLU D  105 ? 0.5556 0.6012 0.4398 -0.0572 -0.0329 -0.0394 105 GLU D N   
7144  C CA  . GLU D  105 ? 0.6069 0.6492 0.4912 -0.0596 -0.0303 -0.0394 105 GLU D CA  
7145  C C   . GLU D  105 ? 0.6897 0.7270 0.5746 -0.0595 -0.0325 -0.0346 105 GLU D C   
7146  O O   . GLU D  105 ? 0.6905 0.7256 0.5736 -0.0613 -0.0315 -0.0343 105 GLU D O   
7147  C CB  . GLU D  105 ? 0.6621 0.7028 0.5508 -0.0605 -0.0260 -0.0408 105 GLU D CB  
7148  C CG  . GLU D  105 ? 0.8096 0.8454 0.7001 -0.0625 -0.0230 -0.0397 105 GLU D CG  
7149  C CD  . GLU D  105 ? 1.2324 1.2633 1.1293 -0.0615 -0.0215 -0.0364 105 GLU D CD  
7150  O OE1 . GLU D  105 ? 1.2049 1.2366 1.1045 -0.0595 -0.0225 -0.0357 105 GLU D OE1 
7151  O OE2 . GLU D  105 ? 1.3220 1.3483 1.2215 -0.0626 -0.0194 -0.0343 105 GLU D OE2 
7152  N N   . ARG D  106 ? 0.7061 0.7419 0.5934 -0.0574 -0.0355 -0.0309 106 ARG D N   
7153  C CA  . ARG D  106 ? 0.6886 0.7205 0.5760 -0.0573 -0.0383 -0.0261 106 ARG D CA  
7154  C C   . ARG D  106 ? 0.7505 0.7842 0.6318 -0.0576 -0.0417 -0.0263 106 ARG D C   
7155  O O   . ARG D  106 ? 0.8608 0.8920 0.7399 -0.0588 -0.0431 -0.0239 106 ARG D O   
7156  C CB  . ARG D  106 ? 0.6280 0.6580 0.5204 -0.0551 -0.0404 -0.0221 106 ARG D CB  
7157  C CG  . ARG D  106 ? 0.7226 0.7494 0.6217 -0.0548 -0.0372 -0.0207 106 ARG D CG  
7158  C CD  . ARG D  106 ? 0.9439 0.9682 0.8481 -0.0529 -0.0397 -0.0156 106 ARG D CD  
7159  N NE  . ARG D  106 ? 0.8980 0.9201 0.8008 -0.0534 -0.0432 -0.0113 106 ARG D NE  
7160  C CZ  . ARG D  106 ? 1.0622 1.0808 0.9664 -0.0547 -0.0422 -0.0084 106 ARG D CZ  
7161  N NH1 . ARG D  106 ? 1.0491 1.0657 0.9564 -0.0556 -0.0376 -0.0096 106 ARG D NH1 
7162  N NH2 . ARG D  106 ? 1.1723 1.1894 1.0747 -0.0552 -0.0457 -0.0043 106 ARG D NH2 
7163  N N   . THR D  107 ? 0.5876 0.6257 0.4664 -0.0566 -0.0427 -0.0291 107 THR D N   
7164  C CA  . THR D  107 ? 0.5911 0.6309 0.4644 -0.0567 -0.0455 -0.0296 107 THR D CA  
7165  C C   . THR D  107 ? 0.7161 0.7565 0.5849 -0.0591 -0.0438 -0.0320 107 THR D C   
7166  O O   . THR D  107 ? 0.6872 0.7262 0.5520 -0.0602 -0.0457 -0.0308 107 THR D O   
7167  C CB  . THR D  107 ? 0.6146 0.6590 0.4869 -0.0549 -0.0464 -0.0320 107 THR D CB  
7168  O OG1 . THR D  107 ? 0.5761 0.6197 0.4523 -0.0527 -0.0483 -0.0295 107 THR D OG1 
7169  C CG2 . THR D  107 ? 0.5416 0.5877 0.4085 -0.0552 -0.0486 -0.0328 107 THR D CG2 
7170  N N   . LEU D  108 ? 0.7188 0.7613 0.5882 -0.0601 -0.0403 -0.0356 108 LEU D N   
7171  C CA  . LEU D  108 ? 0.6516 0.6947 0.5173 -0.0625 -0.0383 -0.0381 108 LEU D CA  
7172  C C   . LEU D  108 ? 0.6303 0.6681 0.4960 -0.0642 -0.0377 -0.0351 108 LEU D C   
7173  O O   . LEU D  108 ? 0.7053 0.7422 0.5668 -0.0658 -0.0382 -0.0351 108 LEU D O   
7174  C CB  . LEU D  108 ? 0.5786 0.6252 0.4454 -0.0634 -0.0346 -0.0425 108 LEU D CB  
7175  C CG  . LEU D  108 ? 0.6593 0.7120 0.5255 -0.0620 -0.0350 -0.0455 108 LEU D CG  
7176  C CD1 . LEU D  108 ? 0.5258 0.5824 0.3924 -0.0635 -0.0314 -0.0499 108 LEU D CD1 
7177  C CD2 . LEU D  108 ? 0.6475 0.7027 0.5092 -0.0615 -0.0375 -0.0460 108 LEU D CD2 
7178  N N   . ASP D  109 ? 0.5998 0.6342 0.4707 -0.0638 -0.0367 -0.0325 109 ASP D N   
7179  C CA  . ASP D  109 ? 0.6816 0.7110 0.5535 -0.0651 -0.0362 -0.0289 109 ASP D CA  
7180  C C   . ASP D  109 ? 0.6714 0.6986 0.5406 -0.0648 -0.0404 -0.0248 109 ASP D C   
7181  O O   . ASP D  109 ? 0.6964 0.7207 0.5635 -0.0664 -0.0407 -0.0225 109 ASP D O   
7182  C CB  . ASP D  109 ? 0.7602 0.7864 0.6388 -0.0644 -0.0340 -0.0267 109 ASP D CB  
7183  C CG  . ASP D  109 ? 0.9610 0.9881 0.8418 -0.0656 -0.0291 -0.0307 109 ASP D CG  
7184  O OD1 . ASP D  109 ? 1.0296 1.0592 0.9065 -0.0673 -0.0274 -0.0348 109 ASP D OD1 
7185  O OD2 . ASP D  109 ? 0.9130 0.9380 0.7993 -0.0650 -0.0268 -0.0299 109 ASP D OD2 
7186  N N   . TYR D  110 ? 0.7221 0.7510 0.5913 -0.0630 -0.0437 -0.0237 110 TYR D N   
7187  C CA  . TYR D  110 ? 0.6378 0.6652 0.5042 -0.0630 -0.0479 -0.0202 110 TYR D CA  
7188  C C   . TYR D  110 ? 0.8174 0.8458 0.6766 -0.0647 -0.0486 -0.0222 110 TYR D C   
7189  O O   . TYR D  110 ? 0.7660 0.7917 0.6220 -0.0662 -0.0502 -0.0195 110 TYR D O   
7190  C CB  . TYR D  110 ? 0.5364 0.5655 0.4044 -0.0607 -0.0508 -0.0193 110 TYR D CB  
7191  C CG  . TYR D  110 ? 0.5846 0.6128 0.4488 -0.0609 -0.0550 -0.0167 110 TYR D CG  
7192  C CD1 . TYR D  110 ? 0.5970 0.6222 0.4632 -0.0611 -0.0576 -0.0115 110 TYR D CD1 
7193  C CD2 . TYR D  110 ? 0.5719 0.6026 0.4307 -0.0612 -0.0562 -0.0193 110 TYR D CD2 
7194  C CE1 . TYR D  110 ? 0.5098 0.5343 0.3721 -0.0617 -0.0615 -0.0092 110 TYR D CE1 
7195  C CE2 . TYR D  110 ? 0.6596 0.6893 0.5146 -0.0617 -0.0598 -0.0172 110 TYR D CE2 
7196  C CZ  . TYR D  110 ? 0.7369 0.7636 0.5935 -0.0621 -0.0625 -0.0123 110 TYR D CZ  
7197  O OH  . TYR D  110 ? 0.8615 0.8873 0.7140 -0.0631 -0.0661 -0.0104 110 TYR D OH  
7198  N N   . HIS D  111 ? 0.6980 0.7304 0.5548 -0.0645 -0.0472 -0.0268 111 HIS D N   
7199  C CA  . HIS D  111 ? 0.6090 0.6425 0.4595 -0.0661 -0.0473 -0.0292 111 HIS D CA  
7200  C C   . HIS D  111 ? 0.7247 0.7562 0.5735 -0.0685 -0.0448 -0.0296 111 HIS D C   
7201  O O   . HIS D  111 ? 0.7359 0.7654 0.5798 -0.0703 -0.0457 -0.0286 111 HIS D O   
7202  C CB  . HIS D  111 ? 0.5963 0.6351 0.4458 -0.0652 -0.0462 -0.0338 111 HIS D CB  
7203  C CG  . HIS D  111 ? 0.6977 0.7385 0.5475 -0.0629 -0.0488 -0.0335 111 HIS D CG  
7204  N ND1 . HIS D  111 ? 0.7677 0.8075 0.6137 -0.0630 -0.0517 -0.0321 111 HIS D ND1 
7205  C CD2 . HIS D  111 ? 0.7114 0.7551 0.5649 -0.0607 -0.0487 -0.0344 111 HIS D CD2 
7206  C CE1 . HIS D  111 ? 0.7940 0.8359 0.6415 -0.0609 -0.0532 -0.0322 111 HIS D CE1 
7207  N NE2 . HIS D  111 ? 0.6885 0.7328 0.5406 -0.0593 -0.0516 -0.0335 111 HIS D NE2 
7208  N N   . ASP D  112 ? 0.6642 0.6959 0.5166 -0.0688 -0.0413 -0.0312 112 ASP D N   
7209  C CA  . ASP D  112 ? 0.6256 0.6550 0.4772 -0.0711 -0.0383 -0.0317 112 ASP D CA  
7210  C C   . ASP D  112 ? 0.6512 0.6757 0.5021 -0.0720 -0.0400 -0.0267 112 ASP D C   
7211  O O   . ASP D  112 ? 0.7194 0.7420 0.5664 -0.0741 -0.0394 -0.0264 112 ASP D O   
7212  C CB  . ASP D  112 ? 0.7686 0.7982 0.6254 -0.0711 -0.0345 -0.0334 112 ASP D CB  
7213  C CG  . ASP D  112 ? 0.8531 0.8810 0.7090 -0.0736 -0.0308 -0.0349 112 ASP D CG  
7214  O OD1 . ASP D  112 ? 0.9462 0.9726 0.8065 -0.0741 -0.0275 -0.0353 112 ASP D OD1 
7215  O OD2 . ASP D  112 ? 1.0012 1.0289 0.8520 -0.0752 -0.0310 -0.0358 112 ASP D OD2 
7216  N N   . SER D  113 ? 0.8377 0.8602 0.6925 -0.0706 -0.0422 -0.0225 113 SER D N   
7217  C CA  . SER D  113 ? 0.6916 0.7100 0.5466 -0.0712 -0.0442 -0.0170 113 SER D CA  
7218  C C   . SER D  113 ? 0.8080 0.8259 0.6562 -0.0726 -0.0475 -0.0158 113 SER D C   
7219  O O   . SER D  113 ? 0.8969 0.9120 0.7420 -0.0745 -0.0475 -0.0136 113 SER D O   
7220  C CB  . SER D  113 ? 0.6433 0.6605 0.5041 -0.0692 -0.0463 -0.0129 113 SER D CB  
7221  O OG  . SER D  113 ? 0.9832 0.9972 0.8439 -0.0697 -0.0491 -0.0073 113 SER D OG  
7222  N N   . ASN D  114 ? 0.7083 0.7288 0.5539 -0.0716 -0.0501 -0.0172 114 ASN D N   
7223  C CA  . ASN D  114 ? 0.8327 0.8527 0.6716 -0.0730 -0.0531 -0.0164 114 ASN D CA  
7224  C C   . ASN D  114 ? 0.8129 0.8327 0.6460 -0.0753 -0.0510 -0.0191 114 ASN D C   
7225  O O   . ASN D  114 ? 0.8555 0.8731 0.6835 -0.0773 -0.0526 -0.0170 114 ASN D O   
7226  C CB  . ASN D  114 ? 0.7184 0.7413 0.5560 -0.0714 -0.0553 -0.0182 114 ASN D CB  
7227  C CG  . ASN D  114 ? 0.8413 0.8641 0.6841 -0.0693 -0.0578 -0.0150 114 ASN D CG  
7228  O OD1 . ASN D  114 ? 0.9471 0.9674 0.7934 -0.0693 -0.0589 -0.0106 114 ASN D OD1 
7229  N ND2 . ASN D  114 ? 0.8925 0.9181 0.7360 -0.0675 -0.0587 -0.0171 114 ASN D ND2 
7230  N N   . VAL D  115 ? 0.7122 0.7344 0.5459 -0.0753 -0.0475 -0.0236 115 VAL D N   
7231  C CA  . VAL D  115 ? 0.7636 0.7857 0.5926 -0.0775 -0.0451 -0.0264 115 VAL D CA  
7232  C C   . VAL D  115 ? 0.7573 0.7753 0.5862 -0.0793 -0.0438 -0.0234 115 VAL D C   
7233  O O   . VAL D  115 ? 0.9547 0.9705 0.7783 -0.0814 -0.0445 -0.0221 115 VAL D O   
7234  C CB  . VAL D  115 ? 0.7503 0.7763 0.5810 -0.0771 -0.0415 -0.0317 115 VAL D CB  
7235  C CG1 . VAL D  115 ? 0.8189 0.8446 0.6456 -0.0795 -0.0387 -0.0343 115 VAL D CG1 
7236  C CG2 . VAL D  115 ? 0.5387 0.5691 0.3691 -0.0753 -0.0426 -0.0346 115 VAL D CG2 
7237  N N   . LYS D  116 ? 0.6909 0.7078 0.5259 -0.0786 -0.0417 -0.0222 116 LYS D N   
7238  C CA  . LYS D  116 ? 0.8133 0.8260 0.6495 -0.0800 -0.0401 -0.0189 116 LYS D CA  
7239  C C   . LYS D  116 ? 0.9282 0.9379 0.7616 -0.0809 -0.0438 -0.0134 116 LYS D C   
7240  O O   . LYS D  116 ? 0.9125 0.9195 0.7425 -0.0829 -0.0432 -0.0116 116 LYS D O   
7241  C CB  . LYS D  116 ? 0.8168 0.8285 0.6609 -0.0786 -0.0379 -0.0176 116 LYS D CB  
7242  C CG  . LYS D  116 ? 0.8374 0.8446 0.6843 -0.0795 -0.0367 -0.0129 116 LYS D CG  
7243  C CD  . LYS D  116 ? 0.9731 0.9790 0.8205 -0.0812 -0.0317 -0.0157 116 LYS D CD  
7244  C CE  . LYS D  116 ? 1.1719 1.1731 1.0237 -0.0815 -0.0299 -0.0109 116 LYS D CE  
7245  N NZ  . LYS D  116 ? 1.3571 1.3568 1.2105 -0.0830 -0.0244 -0.0138 116 LYS D NZ  
7246  N N   . ASN D  117 ? 0.8315 0.8418 0.6660 -0.0794 -0.0477 -0.0107 117 ASN D N   
7247  C CA  . ASN D  117 ? 0.9047 0.9127 0.7366 -0.0803 -0.0517 -0.0054 117 ASN D CA  
7248  C C   . ASN D  117 ? 0.9976 1.0055 0.8207 -0.0826 -0.0532 -0.0066 117 ASN D C   
7249  O O   . ASN D  117 ? 1.1240 1.1293 0.9433 -0.0845 -0.0547 -0.0030 117 ASN D O   
7250  C CB  . ASN D  117 ? 0.8271 0.8363 0.6626 -0.0782 -0.0553 -0.0028 117 ASN D CB  
7251  C CG  . ASN D  117 ? 0.7885 0.7965 0.6325 -0.0764 -0.0544 0.0004  117 ASN D CG  
7252  O OD1 . ASN D  117 ? 0.8208 0.8266 0.6680 -0.0768 -0.0513 0.0015  117 ASN D OD1 
7253  N ND2 . ASN D  117 ? 1.0090 1.0183 0.8571 -0.0744 -0.0569 0.0019  117 ASN D ND2 
7254  N N   . LEU D  118 ? 0.8455 0.8563 0.6653 -0.0824 -0.0526 -0.0117 118 LEU D N   
7255  C CA  . LEU D  118 ? 0.8191 0.8297 0.6307 -0.0845 -0.0534 -0.0134 118 LEU D CA  
7256  C C   . LEU D  118 ? 0.8822 0.8907 0.6904 -0.0868 -0.0504 -0.0142 118 LEU D C   
7257  O O   . LEU D  118 ? 1.1046 1.1109 0.9067 -0.0892 -0.0516 -0.0126 118 LEU D O   
7258  C CB  . LEU D  118 ? 0.9485 0.9627 0.7586 -0.0835 -0.0528 -0.0187 118 LEU D CB  
7259  C CG  . LEU D  118 ? 0.9922 1.0064 0.7953 -0.0848 -0.0551 -0.0195 118 LEU D CG  
7260  C CD1 . LEU D  118 ? 0.9637 0.9763 0.7662 -0.0850 -0.0596 -0.0148 118 LEU D CD1 
7261  C CD2 . LEU D  118 ? 1.0362 1.0541 0.8394 -0.0832 -0.0542 -0.0243 118 LEU D CD2 
7262  N N   . TYR D  119 ? 0.7855 0.7948 0.5978 -0.0863 -0.0464 -0.0168 119 TYR D N   
7263  C CA  . TYR D  119 ? 0.9064 0.9137 0.7166 -0.0884 -0.0430 -0.0177 119 TYR D CA  
7264  C C   . TYR D  119 ? 0.9639 0.9670 0.7739 -0.0896 -0.0440 -0.0119 119 TYR D C   
7265  O O   . TYR D  119 ? 1.1686 1.1694 0.9729 -0.0920 -0.0438 -0.0108 119 TYR D O   
7266  C CB  . TYR D  119 ? 0.8581 0.8671 0.6736 -0.0875 -0.0387 -0.0214 119 TYR D CB  
7267  C CG  . TYR D  119 ? 1.1372 1.1440 0.9513 -0.0897 -0.0348 -0.0223 119 TYR D CG  
7268  C CD1 . TYR D  119 ? 1.1712 1.1796 0.9809 -0.0912 -0.0325 -0.0269 119 TYR D CD1 
7269  C CD2 . TYR D  119 ? 1.0184 1.0216 0.8360 -0.0901 -0.0333 -0.0186 119 TYR D CD2 
7270  C CE1 . TYR D  119 ? 1.1855 1.1919 0.9940 -0.0932 -0.0289 -0.0279 119 TYR D CE1 
7271  C CE2 . TYR D  119 ? 1.1737 1.1747 0.9902 -0.0920 -0.0296 -0.0195 119 TYR D CE2 
7272  C CZ  . TYR D  119 ? 1.3027 1.3054 1.1146 -0.0937 -0.0274 -0.0242 119 TYR D CZ  
7273  O OH  . TYR D  119 ? 1.4209 1.4214 1.2318 -0.0957 -0.0236 -0.0252 119 TYR D OH  
7274  N N   . GLU D  120 ? 1.0508 1.0530 0.8673 -0.0880 -0.0450 -0.0079 120 GLU D N   
7275  C CA  . GLU D  120 ? 1.0431 1.0417 0.8609 -0.0887 -0.0459 -0.0018 120 GLU D CA  
7276  C C   . GLU D  120 ? 1.0251 1.0225 0.8366 -0.0904 -0.0503 0.0022  120 GLU D C   
7277  O O   . GLU D  120 ? 1.1090 1.1036 0.9173 -0.0924 -0.0504 0.0056  120 GLU D O   
7278  C CB  . GLU D  120 ? 1.2552 1.2534 1.0819 -0.0864 -0.0462 0.0017  120 GLU D CB  
7279  C CG  . GLU D  120 ? 1.3418 1.3390 1.1747 -0.0857 -0.0412 0.0000  120 GLU D CG  
7280  C CD  . GLU D  120 ? 1.6932 1.6866 1.5255 -0.0875 -0.0386 0.0028  120 GLU D CD  
7281  O OE1 . GLU D  120 ? 1.6302 1.6216 1.4594 -0.0887 -0.0413 0.0078  120 GLU D OE1 
7282  O OE2 . GLU D  120 ? 1.7884 1.7811 1.6234 -0.0878 -0.0338 -0.0001 120 GLU D OE2 
7283  N N   . LYS D  121 ? 1.0722 1.0717 0.8818 -0.0898 -0.0539 0.0017  121 LYS D N   
7284  C CA  . LYS D  121 ? 1.1541 1.1528 0.9576 -0.0916 -0.0583 0.0051  121 LYS D CA  
7285  C C   . LYS D  121 ? 1.2423 1.2396 1.0368 -0.0946 -0.0573 0.0032  121 LYS D C   
7286  O O   . LYS D  121 ? 1.3252 1.3205 1.1145 -0.0969 -0.0597 0.0071  121 LYS D O   
7287  C CB  . LYS D  121 ? 1.1468 1.1481 0.9497 -0.0904 -0.0617 0.0039  121 LYS D CB  
7288  C CG  . LYS D  121 ? 1.3672 1.3677 1.1643 -0.0925 -0.0664 0.0075  121 LYS D CG  
7289  C CD  . LYS D  121 ? 1.4064 1.4094 1.2035 -0.0913 -0.0693 0.0061  121 LYS D CD  
7290  C CE  . LYS D  121 ? 1.5555 1.5577 1.3466 -0.0937 -0.0739 0.0096  121 LYS D CE  
7291  N NZ  . LYS D  121 ? 1.7289 1.7332 1.5198 -0.0928 -0.0766 0.0079  121 LYS D NZ  
7292  N N   . VAL D  122 ? 1.3057 1.3042 1.0984 -0.0947 -0.0538 -0.0028 122 VAL D N   
7293  C CA  . VAL D  122 ? 1.3072 1.3043 1.0920 -0.0975 -0.0521 -0.0051 122 VAL D CA  
7294  C C   . VAL D  122 ? 1.3725 1.3666 1.1575 -0.0989 -0.0494 -0.0029 122 VAL D C   
7295  O O   . VAL D  122 ? 1.6394 1.6310 1.4180 -0.1016 -0.0498 -0.0009 122 VAL D O   
7296  C CB  . VAL D  122 ? 1.1583 1.1580 0.9420 -0.0971 -0.0490 -0.0121 122 VAL D CB  
7297  C CG1 . VAL D  122 ? 1.3226 1.3207 1.1003 -0.0997 -0.0459 -0.0145 122 VAL D CG1 
7298  C CG2 . VAL D  122 ? 1.0367 1.0387 0.8178 -0.0964 -0.0516 -0.0143 122 VAL D CG2 
7299  N N   . ARG D  123 ? 1.0950 1.0892 0.8874 -0.0972 -0.0463 -0.0032 123 ARG D N   
7300  C CA  . ARG D  123 ? 1.2693 1.2606 1.0629 -0.0983 -0.0429 -0.0017 123 ARG D CA  
7301  C C   . ARG D  123 ? 1.3292 1.3174 1.1229 -0.0992 -0.0453 0.0058  123 ARG D C   
7302  O O   . ARG D  123 ? 1.4669 1.4524 1.2565 -0.1014 -0.0441 0.0077  123 ARG D O   
7303  C CB  . ARG D  123 ? 1.1798 1.1718 0.9817 -0.0964 -0.0390 -0.0039 123 ARG D CB  
7304  C CG  . ARG D  123 ? 1.3043 1.2936 1.1072 -0.0977 -0.0344 -0.0040 123 ARG D CG  
7305  C CD  . ARG D  123 ? 1.4346 1.4230 1.2465 -0.0959 -0.0318 -0.0025 123 ARG D CD  
7306  N NE  . ARG D  123 ? 1.5918 1.5783 1.4076 -0.0948 -0.0348 0.0044  123 ARG D NE  
7307  C CZ  . ARG D  123 ? 1.7024 1.6866 1.5254 -0.0938 -0.0326 0.0078  123 ARG D CZ  
7308  N NH1 . ARG D  123 ? 1.6425 1.6257 1.4693 -0.0939 -0.0272 0.0046  123 ARG D NH1 
7309  N NH2 . ARG D  123 ? 1.7511 1.7341 1.5779 -0.0927 -0.0355 0.0144  123 ARG D NH2 
7310  N N   . SER D  124 ? 1.3646 1.3533 1.1631 -0.0974 -0.0486 0.0101  124 SER D N   
7311  C CA  . SER D  124 ? 1.4820 1.4685 1.2812 -0.0981 -0.0513 0.0176  124 SER D CA  
7312  C C   . SER D  124 ? 1.5435 1.5299 1.3338 -0.1006 -0.0556 0.0199  124 SER D C   
7313  O O   . SER D  124 ? 1.6179 1.6036 1.4081 -0.1012 -0.0593 0.0263  124 SER D O   
7314  C CB  . SER D  124 ? 1.6049 1.5923 1.4129 -0.0953 -0.0533 0.0216  124 SER D CB  
7315  O OG  . SER D  124 ? 1.5611 1.5513 1.3683 -0.0944 -0.0570 0.0205  124 SER D OG  
7316  N N   . GLN D  125 ? 1.4959 1.4830 1.2789 -0.1023 -0.0550 0.0147  125 GLN D N   
7317  C CA  . GLN D  125 ? 1.4991 1.4859 1.2727 -0.1050 -0.0584 0.0156  125 GLN D CA  
7318  C C   . GLN D  125 ? 1.5916 1.5760 1.3580 -0.1078 -0.0553 0.0134  125 GLN D C   
7319  O O   . GLN D  125 ? 1.5828 1.5648 1.3445 -0.1102 -0.0564 0.0178  125 GLN D O   
7320  C CB  . GLN D  125 ? 1.2288 1.2183 1.0001 -0.1045 -0.0602 0.0111  125 GLN D CB  
7321  C CG  . GLN D  125 ? 1.3416 1.3318 1.1092 -0.1056 -0.0657 0.0146  125 GLN D CG  
7322  C CD  . GLN D  125 ? 1.4876 1.4802 1.2532 -0.1050 -0.0667 0.0098  125 GLN D CD  
7323  O OE1 . GLN D  125 ? 1.5146 1.5080 1.2789 -0.1046 -0.0635 0.0039  125 GLN D OE1 
7324  N NE2 . GLN D  125 ? 1.5176 1.5114 1.2832 -0.1049 -0.0712 0.0124  125 GLN D NE2 
7325  N N   . LEU D  126 ? 1.5189 1.5041 1.2843 -0.1076 -0.0514 0.0068  126 LEU D N   
7326  C CA  . LEU D  126 ? 1.5207 1.5037 1.2819 -0.1097 -0.0474 0.0048  126 LEU D CA  
7327  C C   . LEU D  126 ? 1.7766 1.7580 1.5452 -0.1085 -0.0444 0.0073  126 LEU D C   
7328  O O   . LEU D  126 ? 2.0593 2.0424 1.8355 -0.1059 -0.0424 0.0051  126 LEU D O   
7329  C CB  . LEU D  126 ? 1.4500 1.4348 1.2097 -0.1096 -0.0440 -0.0028 126 LEU D CB  
7330  C CG  . LEU D  126 ? 1.3462 1.3344 1.1057 -0.1083 -0.0455 -0.0071 126 LEU D CG  
7331  C CD1 . LEU D  126 ? 1.3527 1.3432 1.1140 -0.1073 -0.0412 -0.0138 126 LEU D CD1 
7332  C CD2 . LEU D  126 ? 1.3746 1.3624 1.1255 -0.1104 -0.0488 -0.0070 126 LEU D CD2 
7333  N N   . LYS D  127 ? 1.6487 1.6269 1.4149 -0.1103 -0.0440 0.0118  127 LYS D N   
7334  C CA  . LYS D  127 ? 1.6058 1.5819 1.3787 -0.1093 -0.0405 0.0143  127 LYS D CA  
7335  C C   . LYS D  127 ? 1.8797 1.8535 1.6487 -0.1114 -0.0358 0.0112  127 LYS D C   
7336  O O   . LYS D  127 ? 1.6972 1.6720 1.4689 -0.1107 -0.0316 0.0056  127 LYS D O   
7337  C CB  . LYS D  127 ? 1.6023 1.5765 1.3773 -0.1093 -0.0435 0.0227  127 LYS D CB  
7338  C CG  . LYS D  127 ? 1.5718 1.5486 1.3501 -0.1075 -0.0486 0.0259  127 LYS D CG  
7339  C CD  . LYS D  127 ? 1.6616 1.6378 1.4344 -0.1095 -0.0537 0.0324  127 LYS D CD  
7340  C CE  . LYS D  127 ? 1.7357 1.7147 1.5117 -0.1080 -0.0588 0.0349  127 LYS D CE  
7341  N NZ  . LYS D  127 ? 1.6746 1.6537 1.4457 -0.1101 -0.0641 0.0414  127 LYS D NZ  
7342  N N   . ASN D  128 ? 2.1256 2.0966 1.8880 -0.1140 -0.0364 0.0149  128 ASN D N   
7343  C CA  . ASN D  128 ? 2.1315 2.1002 1.8893 -0.1162 -0.0321 0.0122  128 ASN D CA  
7344  C C   . ASN D  128 ? 2.1537 2.1237 1.9038 -0.1180 -0.0317 0.0061  128 ASN D C   
7345  O O   . ASN D  128 ? 2.0233 1.9927 1.7718 -0.1190 -0.0273 0.0014  128 ASN D O   
7346  C CB  . ASN D  128 ? 2.0503 2.0153 1.8041 -0.1184 -0.0328 0.0187  128 ASN D CB  
7347  C CG  . ASN D  128 ? 2.0926 2.0558 1.8550 -0.1166 -0.0315 0.0243  128 ASN D CG  
7348  O OD1 . ASN D  128 ? 2.0304 1.9933 1.7999 -0.1150 -0.0272 0.0216  128 ASN D OD1 
7349  N ND2 . ASN D  128 ? 2.2591 2.2211 2.0208 -0.1170 -0.0351 0.0320  128 ASN D ND2 
7350  N N   . ASN D  129 ? 2.9288 2.9006 2.6743 -0.1184 -0.0360 0.0060  129 ASN D N   
7351  C CA  . ASN D  129 ? 2.9994 2.9718 2.7370 -0.1203 -0.0357 0.0009  129 ASN D CA  
7352  C C   . ASN D  129 ? 2.8360 2.8113 2.5769 -0.1188 -0.0323 -0.0065 129 ASN D C   
7353  O O   . ASN D  129 ? 2.8346 2.8109 2.5701 -0.1200 -0.0316 -0.0111 129 ASN D O   
7354  C CB  . ASN D  129 ? 2.9579 2.9314 2.6904 -0.1211 -0.0410 0.0028  129 ASN D CB  
7355  C CG  . ASN D  129 ? 2.9216 2.8927 2.6494 -0.1232 -0.0446 0.0099  129 ASN D CG  
7356  O OD1 . ASN D  129 ? 2.8730 2.8447 2.5957 -0.1246 -0.0489 0.0118  129 ASN D OD1 
7357  N ND2 . ASN D  129 ? 3.0114 2.9799 2.7408 -0.1237 -0.0428 0.0140  129 ASN D ND2 
7358  N N   . ALA D  130 ? 2.0018 1.9787 1.7516 -0.1162 -0.0302 -0.0076 130 ALA D N   
7359  C CA  . ALA D  130 ? 1.8488 1.8290 1.6024 -0.1148 -0.0270 -0.0143 130 ALA D CA  
7360  C C   . ALA D  130 ? 1.6632 1.6439 1.4259 -0.1129 -0.0240 -0.0147 130 ALA D C   
7361  O O   . ALA D  130 ? 1.6564 1.6350 1.4231 -0.1122 -0.0246 -0.0096 130 ALA D O   
7362  C CB  . ALA D  130 ? 1.7247 1.7085 1.4788 -0.1131 -0.0300 -0.0167 130 ALA D CB  
7363  N N   . LYS D  131 ? 1.6806 1.6641 1.4465 -0.1122 -0.0205 -0.0206 131 LYS D N   
7364  C CA  . LYS D  131 ? 1.8399 1.8241 1.6140 -0.1108 -0.0172 -0.0217 131 LYS D CA  
7365  C C   . LYS D  131 ? 2.0314 2.0204 1.8109 -0.1084 -0.0172 -0.0260 131 LYS D C   
7366  O O   . LYS D  131 ? 1.9529 1.9451 1.7297 -0.1082 -0.0181 -0.0299 131 LYS D O   
7367  C CB  . LYS D  131 ? 1.8045 1.7873 1.5778 -0.1127 -0.0120 -0.0247 131 LYS D CB  
7368  C CG  . LYS D  131 ? 1.9381 1.9244 1.7092 -0.1134 -0.0097 -0.0315 131 LYS D CG  
7369  C CD  . LYS D  131 ? 1.9332 1.9190 1.7063 -0.1149 -0.0042 -0.0348 131 LYS D CD  
7370  C CE  . LYS D  131 ? 1.7940 1.7841 1.5662 -0.1153 -0.0020 -0.0415 131 LYS D CE  
7371  N NZ  . LYS D  131 ? 1.8017 1.7921 1.5767 -0.1167 0.0032  -0.0450 131 LYS D NZ  
7372  N N   . GLU D  132 ? 2.5117 2.5011 2.2988 -0.1066 -0.0162 -0.0252 132 GLU D N   
7373  C CA  . GLU D  132 ? 2.3531 2.3471 2.1457 -0.1045 -0.0158 -0.0292 132 GLU D CA  
7374  C C   . GLU D  132 ? 2.3814 2.3781 2.1748 -0.1055 -0.0114 -0.0354 132 GLU D C   
7375  O O   . GLU D  132 ? 2.4317 2.4261 2.2254 -0.1072 -0.0076 -0.0360 132 GLU D O   
7376  C CB  . GLU D  132 ? 2.4609 2.4541 2.2612 -0.1026 -0.0157 -0.0264 132 GLU D CB  
7377  C CG  . GLU D  132 ? 2.4934 2.4844 2.2943 -0.1014 -0.0200 -0.0199 132 GLU D CG  
7378  C CD  . GLU D  132 ? 2.5580 2.5479 2.3672 -0.0996 -0.0192 -0.0172 132 GLU D CD  
7379  O OE1 . GLU D  132 ? 2.4256 2.4132 2.2363 -0.0988 -0.0220 -0.0112 132 GLU D OE1 
7380  O OE2 . GLU D  132 ? 2.5332 2.5246 2.3474 -0.0991 -0.0156 -0.0209 132 GLU D OE2 
7381  N N   . ILE D  133 ? 2.0640 2.0658 1.8581 -0.1044 -0.0118 -0.0399 133 ILE D N   
7382  C CA  . ILE D  133 ? 2.1657 2.1712 1.9615 -0.1051 -0.0080 -0.0457 133 ILE D CA  
7383  C C   . ILE D  133 ? 2.1389 2.1466 1.9422 -0.1038 -0.0062 -0.0473 133 ILE D C   
7384  O O   . ILE D  133 ? 2.1605 2.1693 1.9664 -0.1051 -0.0021 -0.0507 133 ILE D O   
7385  C CB  . ILE D  133 ? 2.0708 2.0810 1.8636 -0.1047 -0.0092 -0.0497 133 ILE D CB  
7386  C CG1 . ILE D  133 ? 2.1200 2.1277 1.9051 -0.1063 -0.0104 -0.0487 133 ILE D CG1 
7387  C CG2 . ILE D  133 ? 1.9750 1.9899 1.7705 -0.1053 -0.0055 -0.0554 133 ILE D CG2 
7388  C CD1 . ILE D  133 ? 2.2630 2.2683 2.0450 -0.1091 -0.0066 -0.0500 133 ILE D CD1 
7389  N N   . GLY D  134 ? 1.8680 1.8764 1.6747 -0.1015 -0.0091 -0.0450 134 GLY D N   
7390  C CA  . GLY D  134 ? 1.7832 1.7935 1.5967 -0.1002 -0.0076 -0.0463 134 GLY D CA  
7391  C C   . GLY D  134 ? 1.6152 1.6313 1.4304 -0.0982 -0.0096 -0.0493 134 GLY D C   
7392  O O   . GLY D  134 ? 1.3624 1.3801 1.1827 -0.0967 -0.0096 -0.0495 134 GLY D O   
7393  N N   . ASN D  135 ? 1.3882 1.4073 1.1990 -0.0983 -0.0111 -0.0515 135 ASN D N   
7394  C CA  . ASN D  135 ? 1.2270 1.2517 1.0391 -0.0963 -0.0129 -0.0541 135 ASN D CA  
7395  C C   . ASN D  135 ? 1.2579 1.2816 1.0680 -0.0945 -0.0175 -0.0507 135 ASN D C   
7396  O O   . ASN D  135 ? 1.1652 1.1925 0.9740 -0.0933 -0.0194 -0.0524 135 ASN D O   
7397  C CB  . ASN D  135 ? 1.2933 1.3223 1.1027 -0.0974 -0.0113 -0.0588 135 ASN D CB  
7398  C CG  . ASN D  135 ? 1.4294 1.4650 1.2414 -0.0955 -0.0123 -0.0619 135 ASN D CG  
7399  O OD1 . ASN D  135 ? 1.2876 1.3246 1.1035 -0.0935 -0.0138 -0.0610 135 ASN D OD1 
7400  N ND2 . ASN D  135 ? 1.6028 1.6426 1.4129 -0.0959 -0.0113 -0.0654 135 ASN D ND2 
7401  N N   . GLY D  136 ? 1.2313 1.2501 1.0414 -0.0943 -0.0193 -0.0457 136 GLY D N   
7402  C CA  . GLY D  136 ? 1.1289 1.1465 0.9371 -0.0930 -0.0238 -0.0421 136 GLY D CA  
7403  C C   . GLY D  136 ? 1.3329 1.3492 1.1338 -0.0944 -0.0253 -0.0418 136 GLY D C   
7404  O O   . GLY D  136 ? 1.3275 1.3438 1.1259 -0.0935 -0.0287 -0.0402 136 GLY D O   
7405  N N   . CYS D  137 ? 1.8700 1.8850 1.6674 -0.0967 -0.0225 -0.0435 137 CYS D N   
7406  C CA  . CYS D  137 ? 1.9107 1.9242 1.7009 -0.0985 -0.0232 -0.0436 137 CYS D CA  
7407  C C   . CYS D  137 ? 1.8754 1.8836 1.6617 -0.1009 -0.0222 -0.0406 137 CYS D C   
7408  O O   . CYS D  137 ? 1.8362 1.8430 1.6253 -0.1018 -0.0192 -0.0405 137 CYS D O   
7409  C CB  . CYS D  137 ? 1.8088 1.8263 1.5976 -0.0990 -0.0207 -0.0491 137 CYS D CB  
7410  S SG  . CYS D  137 ? 2.0088 2.0325 1.8004 -0.0962 -0.0223 -0.0521 137 CYS D SG  
7411  N N   . PHE D  138 ? 1.6916 1.6970 1.4716 -0.1022 -0.0247 -0.0380 138 PHE D N   
7412  C CA  . PHE D  138 ? 1.8654 1.8659 1.6410 -0.1046 -0.0243 -0.0346 138 PHE D CA  
7413  C C   . PHE D  138 ? 2.0684 2.0682 1.8371 -0.1071 -0.0223 -0.0375 138 PHE D C   
7414  O O   . PHE D  138 ? 2.0821 2.0846 1.8486 -0.1069 -0.0224 -0.0410 138 PHE D O   
7415  C CB  . PHE D  138 ? 1.8153 1.8129 1.5882 -0.1047 -0.0288 -0.0290 138 PHE D CB  
7416  C CG  . PHE D  138 ? 1.6147 1.6126 1.3944 -0.1024 -0.0308 -0.0255 138 PHE D CG  
7417  C CD1 . PHE D  138 ? 1.4954 1.4967 1.2787 -0.0999 -0.0330 -0.0266 138 PHE D CD1 
7418  C CD2 . PHE D  138 ? 1.5197 1.5144 1.3024 -0.1026 -0.0304 -0.0210 138 PHE D CD2 
7419  C CE1 . PHE D  138 ? 1.4070 1.4084 1.1966 -0.0978 -0.0347 -0.0235 138 PHE D CE1 
7420  C CE2 . PHE D  138 ? 1.3560 1.3508 1.1453 -0.1004 -0.0320 -0.0177 138 PHE D CE2 
7421  C CZ  . PHE D  138 ? 1.4088 1.4069 1.2015 -0.0981 -0.0341 -0.0191 138 PHE D CZ  
7422  N N   . GLU D  139 ? 2.1897 2.1857 1.9554 -0.1094 -0.0202 -0.0359 139 GLU D N   
7423  C CA  . GLU D  139 ? 2.0804 2.0749 1.8390 -0.1120 -0.0183 -0.0380 139 GLU D CA  
7424  C C   . GLU D  139 ? 1.9340 1.9235 1.6858 -0.1143 -0.0203 -0.0331 139 GLU D C   
7425  O O   . GLU D  139 ? 1.9518 1.9381 1.7047 -0.1149 -0.0201 -0.0290 139 GLU D O   
7426  C CB  . GLU D  139 ? 2.1073 2.1022 1.8677 -0.1131 -0.0133 -0.0416 139 GLU D CB  
7427  C CG  . GLU D  139 ? 2.3839 2.3772 2.1373 -0.1158 -0.0110 -0.0438 139 GLU D CG  
7428  C CD  . GLU D  139 ? 2.4454 2.4404 2.2013 -0.1167 -0.0060 -0.0483 139 GLU D CD  
7429  O OE1 . GLU D  139 ? 2.2641 2.2618 2.0270 -0.1154 -0.0044 -0.0499 139 GLU D OE1 
7430  O OE2 . GLU D  139 ? 2.4156 2.4094 2.1664 -0.1189 -0.0037 -0.0504 139 GLU D OE2 
7431  N N   . PHE D  140 ? 2.3742 2.3629 2.1189 -0.1156 -0.0222 -0.0335 140 PHE D N   
7432  C CA  . PHE D  140 ? 2.5047 2.4892 2.2420 -0.1181 -0.0245 -0.0291 140 PHE D CA  
7433  C C   . PHE D  140 ? 2.6102 2.5913 2.3426 -0.1210 -0.0211 -0.0292 140 PHE D C   
7434  O O   . PHE D  140 ? 2.5725 2.5545 2.3035 -0.1219 -0.0174 -0.0340 140 PHE D O   
7435  C CB  . PHE D  140 ? 2.5409 2.5257 2.2720 -0.1189 -0.0273 -0.0300 140 PHE D CB  
7436  C CG  . PHE D  140 ? 2.4704 2.4577 2.2053 -0.1165 -0.0312 -0.0287 140 PHE D CG  
7437  C CD1 . PHE D  140 ? 2.5068 2.4982 2.2456 -0.1142 -0.0308 -0.0330 140 PHE D CD1 
7438  C CD2 . PHE D  140 ? 2.4136 2.3993 2.1481 -0.1165 -0.0355 -0.0230 140 PHE D CD2 
7439  C CE1 . PHE D  140 ? 2.4551 2.4486 2.1972 -0.1119 -0.0343 -0.0317 140 PHE D CE1 
7440  C CE2 . PHE D  140 ? 2.3572 2.3451 2.0952 -0.1144 -0.0390 -0.0218 140 PHE D CE2 
7441  C CZ  . PHE D  140 ? 2.3426 2.3343 2.0844 -0.1121 -0.0384 -0.0263 140 PHE D CZ  
7442  N N   . TYR D  141 ? 2.0784 2.0557 1.8083 -0.1225 -0.0223 -0.0238 141 TYR D N   
7443  C CA  . TYR D  141 ? 2.0146 1.9881 1.7384 -0.1255 -0.0196 -0.0231 141 TYR D CA  
7444  C C   . TYR D  141 ? 1.9467 1.9182 1.6605 -0.1282 -0.0220 -0.0222 141 TYR D C   
7445  O O   . TYR D  141 ? 2.0554 2.0240 1.7624 -0.1311 -0.0198 -0.0229 141 TYR D O   
7446  C CB  . TYR D  141 ? 2.0359 2.0062 1.7619 -0.1258 -0.0196 -0.0174 141 TYR D CB  
7447  C CG  . TYR D  141 ? 1.9571 1.9286 1.6926 -0.1237 -0.0165 -0.0182 141 TYR D CG  
7448  C CD1 . TYR D  141 ? 1.9071 1.8780 1.6488 -0.1218 -0.0183 -0.0133 141 TYR D CD1 
7449  C CD2 . TYR D  141 ? 1.8267 1.7999 1.5650 -0.1236 -0.0119 -0.0240 141 TYR D CD2 
7450  C CE1 . TYR D  141 ? 1.8647 1.8363 1.6149 -0.1201 -0.0151 -0.0144 141 TYR D CE1 
7451  C CE2 . TYR D  141 ? 1.8197 1.7940 1.5662 -0.1220 -0.0090 -0.0251 141 TYR D CE2 
7452  C CZ  . TYR D  141 ? 1.8456 1.8188 1.5979 -0.1203 -0.0105 -0.0203 141 TYR D CZ  
7453  O OH  . TYR D  141 ? 1.6772 1.6511 1.4376 -0.1189 -0.0072 -0.0216 141 TYR D OH  
7454  N N   . HIS D  142 ? 1.9654 1.9382 1.6782 -0.1275 -0.0264 -0.0207 142 HIS D N   
7455  C CA  . HIS D  142 ? 1.9760 1.9469 1.6794 -0.1302 -0.0291 -0.0197 142 HIS D CA  
7456  C C   . HIS D  142 ? 2.0158 1.9894 1.7181 -0.1295 -0.0294 -0.0246 142 HIS D C   
7457  O O   . HIS D  142 ? 2.1295 2.1062 1.8374 -0.1267 -0.0315 -0.0251 142 HIS D O   
7458  C CB  . HIS D  142 ? 1.9723 1.9421 1.6745 -0.1306 -0.0342 -0.0129 142 HIS D CB  
7459  C CG  . HIS D  142 ? 2.0556 2.0276 1.7574 -0.1298 -0.0385 -0.0127 142 HIS D CG  
7460  N ND1 . HIS D  142 ? 2.0686 2.0393 1.7614 -0.1327 -0.0408 -0.0126 142 HIS D ND1 
7461  C CD2 . HIS D  142 ? 2.0470 2.0222 1.7561 -0.1266 -0.0407 -0.0126 142 HIS D CD2 
7462  C CE1 . HIS D  142 ? 2.0184 1.9914 1.7133 -0.1312 -0.0443 -0.0125 142 HIS D CE1 
7463  N NE2 . HIS D  142 ? 2.0794 2.0552 1.7842 -0.1274 -0.0443 -0.0125 142 HIS D NE2 
7464  N N   . LYS D  143 ? 1.8535 1.8256 1.5487 -0.1319 -0.0270 -0.0283 143 LYS D N   
7465  C CA  . LYS D  143 ? 1.8492 1.8235 1.5432 -0.1314 -0.0265 -0.0332 143 LYS D CA  
7466  C C   . LYS D  143 ? 1.8417 1.8175 1.5367 -0.1301 -0.0312 -0.0313 143 LYS D C   
7467  O O   . LYS D  143 ? 1.7351 1.7087 1.4240 -0.1324 -0.0347 -0.0278 143 LYS D O   
7468  C CB  . LYS D  143 ? 1.8230 1.7942 1.5073 -0.1351 -0.0243 -0.0357 143 LYS D CB  
7469  C CG  . LYS D  143 ? 1.8212 1.7914 1.5049 -0.1361 -0.0189 -0.0390 143 LYS D CG  
7470  C CD  . LYS D  143 ? 1.8971 1.8710 1.5859 -0.1340 -0.0155 -0.0451 143 LYS D CD  
7471  C CE  . LYS D  143 ? 1.8540 1.8323 1.5536 -0.1302 -0.0152 -0.0457 143 LYS D CE  
7472  N NZ  . LYS D  143 ? 1.7383 1.7207 1.4427 -0.1283 -0.0121 -0.0514 143 LYS D NZ  
7473  N N   . CYS D  144 ? 2.0395 2.0194 1.7422 -0.1266 -0.0314 -0.0337 144 CYS D N   
7474  C CA  . CYS D  144 ? 2.1560 2.1376 1.8607 -0.1250 -0.0356 -0.0322 144 CYS D CA  
7475  C C   . CYS D  144 ? 2.0719 2.0557 1.7764 -0.1241 -0.0345 -0.0371 144 CYS D C   
7476  O O   . CYS D  144 ? 2.0377 2.0251 1.7491 -0.1211 -0.0326 -0.0404 144 CYS D O   
7477  C CB  . CYS D  144 ? 2.1772 2.1615 1.8916 -0.1215 -0.0372 -0.0298 144 CYS D CB  
7478  S SG  . CYS D  144 ? 2.2432 2.2293 1.9604 -0.1197 -0.0427 -0.0267 144 CYS D SG  
7479  N N   . ASP D  145 ? 2.3612 2.3427 2.0578 -0.1267 -0.0356 -0.0375 145 ASP D N   
7480  C CA  . ASP D  145 ? 2.4028 2.3856 2.0987 -0.1261 -0.0346 -0.0419 145 ASP D CA  
7481  C C   . ASP D  145 ? 2.2657 2.2513 1.9668 -0.1233 -0.0382 -0.0408 145 ASP D C   
7482  O O   . ASP D  145 ? 2.2878 2.2749 1.9945 -0.1213 -0.0409 -0.0373 145 ASP D O   
7483  C CB  . ASP D  145 ? 2.5835 2.5624 2.2688 -0.1302 -0.0339 -0.0431 145 ASP D CB  
7484  C CG  . ASP D  145 ? 2.5556 2.5313 2.2339 -0.1335 -0.0379 -0.0381 145 ASP D CG  
7485  O OD1 . ASP D  145 ? 2.4423 2.4152 2.1120 -0.1369 -0.0384 -0.0388 145 ASP D OD1 
7486  O OD2 . ASP D  145 ? 2.4953 2.4713 2.1767 -0.1328 -0.0405 -0.0334 145 ASP D OD2 
7487  N N   . ASN D  146 ? 1.9186 1.9046 1.6179 -0.1232 -0.0380 -0.0437 146 ASN D N   
7488  C CA  . ASN D  146 ? 1.8144 1.8031 1.5188 -0.1204 -0.0407 -0.0433 146 ASN D CA  
7489  C C   . ASN D  146 ? 1.9334 1.9211 1.6367 -0.1213 -0.0460 -0.0382 146 ASN D C   
7490  O O   . ASN D  146 ? 2.1113 2.1016 1.8215 -0.1183 -0.0485 -0.0362 146 ASN D O   
7491  C CB  . ASN D  146 ? 1.6335 1.6222 1.3355 -0.1206 -0.0390 -0.0475 146 ASN D CB  
7492  C CG  . ASN D  146 ? 1.6407 1.6323 1.3473 -0.1183 -0.0344 -0.0522 146 ASN D CG  
7493  O OD1 . ASN D  146 ? 1.6059 1.5975 1.3115 -0.1183 -0.0319 -0.0556 146 ASN D OD1 
7494  N ND2 . ASN D  146 ? 1.6942 1.6883 1.4066 -0.1164 -0.0329 -0.0522 146 ASN D ND2 
7495  N N   . THR D  147 ? 2.6335 2.6175 2.3279 -0.1253 -0.0477 -0.0361 147 THR D N   
7496  C CA  . THR D  147 ? 2.7021 2.6854 2.3949 -0.1266 -0.0529 -0.0310 147 THR D CA  
7497  C C   . THR D  147 ? 2.7215 2.7049 2.4177 -0.1261 -0.0546 -0.0260 147 THR D C   
7498  O O   . THR D  147 ? 2.6960 2.6796 2.3932 -0.1262 -0.0589 -0.0211 147 THR D O   
7499  C CB  . THR D  147 ? 2.6026 2.5824 2.2844 -0.1315 -0.0543 -0.0304 147 THR D CB  
7500  O OG1 . THR D  147 ? 2.7221 2.6990 2.3977 -0.1345 -0.0522 -0.0298 147 THR D OG1 
7501  N N   . CYS D  148 ? 2.1402 2.1233 1.8381 -0.1255 -0.0511 -0.0271 148 CYS D N   
7502  C CA  . CYS D  148 ? 2.1297 2.1131 1.8325 -0.1244 -0.0518 -0.0229 148 CYS D CA  
7503  C C   . CYS D  148 ? 2.1823 2.1693 1.8957 -0.1199 -0.0521 -0.0232 148 CYS D C   
7504  O O   . CYS D  148 ? 2.1866 2.1744 1.9050 -0.1184 -0.0550 -0.0188 148 CYS D O   
7505  C CB  . CYS D  148 ? 2.0954 2.0771 1.7964 -0.1256 -0.0475 -0.0244 148 CYS D CB  
7506  S SG  . CYS D  148 ? 2.0315 2.0131 1.7392 -0.1240 -0.0473 -0.0199 148 CYS D SG  
7507  N N   . MET D  149 ? 2.1912 2.1806 1.9081 -0.1177 -0.0489 -0.0283 149 MET D N   
7508  C CA  . MET D  149 ? 1.9859 1.9791 1.7124 -0.1135 -0.0489 -0.0294 149 MET D CA  
7509  C C   . MET D  149 ? 1.8935 1.8879 1.6228 -0.1121 -0.0533 -0.0265 149 MET D C   
7510  O O   . MET D  149 ? 1.7629 1.7597 1.5002 -0.1090 -0.0543 -0.0252 149 MET D O   
7511  C CB  . MET D  149 ? 1.9006 1.8964 1.6290 -0.1119 -0.0453 -0.0353 149 MET D CB  
7512  C CG  . MET D  149 ? 1.9025 1.8983 1.6308 -0.1125 -0.0406 -0.0383 149 MET D CG  
7513  S SD  . MET D  149 ? 1.7760 1.7736 1.5127 -0.1103 -0.0393 -0.0368 149 MET D SD  
7514  C CE  . MET D  149 ? 1.7935 1.7918 1.5294 -0.1112 -0.0337 -0.0418 149 MET D CE  
7515  N N   . GLU D  150 ? 2.3103 2.3030 2.0331 -0.1146 -0.0558 -0.0257 150 GLU D N   
7516  C CA  . GLU D  150 ? 2.3495 2.3432 2.0743 -0.1136 -0.0600 -0.0233 150 GLU D CA  
7517  C C   . GLU D  150 ? 2.3751 2.3682 2.1020 -0.1139 -0.0638 -0.0170 150 GLU D C   
7518  O O   . GLU D  150 ? 2.3450 2.3402 2.0786 -0.1113 -0.0663 -0.0147 150 GLU D O   
7519  C CB  . GLU D  150 ? 2.4521 2.4441 2.1689 -0.1166 -0.0612 -0.0248 150 GLU D CB  
7520  C CG  . GLU D  150 ? 2.5388 2.5329 2.2588 -0.1144 -0.0620 -0.0271 150 GLU D CG  
7521  C CD  . GLU D  150 ? 2.5185 2.5139 2.2399 -0.1127 -0.0576 -0.0329 150 GLU D CD  
7522  O OE1 . GLU D  150 ? 2.5238 2.5199 2.2456 -0.1119 -0.0573 -0.0353 150 GLU D OE1 
7523  O OE2 . GLU D  150 ? 2.4392 2.4352 2.1620 -0.1120 -0.0541 -0.0349 150 GLU D OE2 
7524  N N   . SER D  151 ? 2.3389 2.3293 2.0602 -0.1170 -0.0643 -0.0140 151 SER D N   
7525  C CA  . SER D  151 ? 2.2752 2.2651 1.9982 -0.1175 -0.0678 -0.0075 151 SER D CA  
7526  C C   . SER D  151 ? 2.1661 2.1578 1.8995 -0.1137 -0.0672 -0.0057 151 SER D C   
7527  O O   . SER D  151 ? 2.2465 2.2388 1.9844 -0.1127 -0.0703 -0.0007 151 SER D O   
7528  C CB  . SER D  151 ? 2.2813 2.2680 1.9971 -0.1211 -0.0673 -0.0050 151 SER D CB  
7529  O OG  . SER D  151 ? 2.2381 2.2242 1.9559 -0.1203 -0.0628 -0.0071 151 SER D OG  
7530  N N   . VAL D  152 ? 1.8137 1.8065 1.5512 -0.1116 -0.0629 -0.0100 152 VAL D N   
7531  C CA  . VAL D  152 ? 1.7393 1.7339 1.4864 -0.1081 -0.0616 -0.0093 152 VAL D CA  
7532  C C   . VAL D  152 ? 1.7095 1.7071 1.4629 -0.1050 -0.0633 -0.0102 152 VAL D C   
7533  O O   . VAL D  152 ? 1.5512 1.5497 1.3115 -0.1028 -0.0648 -0.0070 152 VAL D O   
7534  C CB  . VAL D  152 ? 1.5635 1.5586 1.3124 -0.1073 -0.0565 -0.0139 152 VAL D CB  
7535  C CG1 . VAL D  152 ? 1.2578 1.2540 1.0157 -0.1046 -0.0550 -0.0125 152 VAL D CG1 
7536  C CG2 . VAL D  152 ? 1.6052 1.5973 1.3467 -0.1106 -0.0543 -0.0142 152 VAL D CG2 
7537  N N   . LYS D  153 ? 1.7187 1.7176 1.4695 -0.1048 -0.0628 -0.0146 153 LYS D N   
7538  C CA  . LYS D  153 ? 1.6516 1.6533 1.4079 -0.1018 -0.0641 -0.0158 153 LYS D CA  
7539  C C   . LYS D  153 ? 1.9153 1.9166 1.6720 -0.1022 -0.0690 -0.0111 153 LYS D C   
7540  O O   . LYS D  153 ? 1.9439 1.9468 1.7079 -0.0996 -0.0706 -0.0086 153 LYS D O   
7541  N N   . ASN D  154 ? 2.4582 2.4577 2.2071 -0.1055 -0.0713 -0.0099 154 ASN D N   
7542  C CA  . ASN D  154 ? 2.6611 2.6604 2.4094 -0.1066 -0.0763 -0.0053 154 ASN D CA  
7543  C C   . ASN D  154 ? 2.6737 2.6727 2.4266 -0.1061 -0.0783 0.0009  154 ASN D C   
7544  O O   . ASN D  154 ? 2.7707 2.7704 2.5257 -0.1062 -0.0824 0.0053  154 ASN D O   
7545  C CB  . ASN D  154 ? 2.7871 2.7842 2.5250 -0.1110 -0.0780 -0.0052 154 ASN D CB  
7546  C CG  . ASN D  154 ? 2.8446 2.8419 2.5786 -0.1114 -0.0765 -0.0106 154 ASN D CG  
7547  O OD1 . ASN D  154 ? 2.8940 2.8906 2.6250 -0.1117 -0.0726 -0.0152 154 ASN D OD1 
7548  N ND2 . ASN D  154 ? 2.8319 2.8301 2.5664 -0.1113 -0.0795 -0.0101 154 ASN D ND2 
7549  N N   . GLY D  155 ? 2.1314 2.1296 1.8864 -0.1056 -0.0753 0.0011  155 GLY D N   
7550  C CA  . GLY D  155 ? 2.0290 2.0265 1.7888 -0.1051 -0.0764 0.0068  155 GLY D CA  
7551  C C   . GLY D  155 ? 2.0937 2.0891 1.8468 -0.1088 -0.0792 0.0117  155 GLY D C   
7552  O O   . GLY D  155 ? 1.9670 1.9619 1.7236 -0.1087 -0.0807 0.0173  155 GLY D O   
7553  N N   . THR D  156 ? 2.5281 2.5224 2.2717 -0.1121 -0.0798 0.0096  156 THR D N   
7554  C CA  . THR D  156 ? 2.5521 2.5446 2.2879 -0.1162 -0.0825 0.0137  156 THR D CA  
7555  C C   . THR D  156 ? 2.3483 2.3381 2.0780 -0.1183 -0.0788 0.0118  156 THR D C   
7556  O O   . THR D  156 ? 2.3532 2.3416 2.0746 -0.1210 -0.0775 0.0079  156 THR D O   
7557  C CB  . THR D  156 ? 2.6972 2.6898 2.4256 -0.1191 -0.0858 0.0128  156 THR D CB  
7558  O OG1 . THR D  156 ? 2.6696 2.6619 2.3943 -0.1191 -0.0826 0.0059  156 THR D OG1 
7559  C CG2 . THR D  156 ? 2.7279 2.7230 2.4620 -0.1174 -0.0900 0.0158  156 THR D CG2 
7560  N N   . TYR D  157 ? 1.9977 1.9866 1.7316 -0.1173 -0.0769 0.0145  157 TYR D N   
7561  C CA  . TYR D  157 ? 2.0076 1.9941 1.7372 -0.1189 -0.0728 0.0125  157 TYR D CA  
7562  C C   . TYR D  157 ? 2.2102 2.1945 1.9366 -0.1213 -0.0741 0.0186  157 TYR D C   
7563  O O   . TYR D  157 ? 2.0951 2.0796 1.8283 -0.1196 -0.0748 0.0236  157 TYR D O   
7564  C CB  . TYR D  157 ? 1.7877 1.7749 1.5250 -0.1155 -0.0681 0.0090  157 TYR D CB  
7565  C CG  . TYR D  157 ? 1.7073 1.6922 1.4410 -0.1170 -0.0636 0.0064  157 TYR D CG  
7566  C CD1 . TYR D  157 ? 1.7124 1.6976 1.4430 -0.1172 -0.0600 -0.0003 157 TYR D CD1 
7567  C CD2 . TYR D  157 ? 1.6710 1.6536 1.4047 -0.1180 -0.0627 0.0107  157 TYR D CD2 
7568  C CE1 . TYR D  157 ? 1.6488 1.6321 1.3764 -0.1186 -0.0557 -0.0027 157 TYR D CE1 
7569  C CE2 . TYR D  157 ? 1.7259 1.7064 1.4564 -0.1194 -0.0584 0.0083  157 TYR D CE2 
7570  C CZ  . TYR D  157 ? 1.6574 1.6383 1.3848 -0.1197 -0.0549 0.0015  157 TYR D CZ  
7571  O OH  . TYR D  157 ? 1.5287 1.5076 1.2532 -0.1211 -0.0506 -0.0010 157 TYR D OH  
7572  N N   . ASP D  158 ? 3.1560 3.1382 2.8721 -0.1253 -0.0742 0.0182  158 ASP D N   
7573  C CA  . ASP D  158 ? 3.3654 3.3456 3.0772 -0.1280 -0.0754 0.0240  158 ASP D CA  
7574  C C   . ASP D  158 ? 3.2967 3.2747 3.0109 -0.1272 -0.0706 0.0236  158 ASP D C   
7575  O O   . ASP D  158 ? 3.1395 3.1166 2.8520 -0.1271 -0.0662 0.0178  158 ASP D O   
7576  C CB  . ASP D  158 ? 3.4981 3.4767 3.1974 -0.1329 -0.0771 0.0236  158 ASP D CB  
7577  C CG  . ASP D  158 ? 3.1849 3.1614 2.8787 -0.1359 -0.0781 0.0292  158 ASP D CG  
7578  O OD1 . ASP D  158 ? 3.0853 3.0591 2.7721 -0.1383 -0.0748 0.0267  158 ASP D OD1 
7579  O OD2 . ASP D  158 ? 3.0288 3.0063 2.7254 -0.1359 -0.0820 0.0363  158 ASP D OD2 
7580  N N   . TYR D  159 ? 3.0468 3.0242 2.7654 -0.1266 -0.0715 0.0301  159 TYR D N   
7581  C CA  . TYR D  159 ? 2.9856 2.9609 2.7078 -0.1256 -0.0669 0.0303  159 TYR D CA  
7582  C C   . TYR D  159 ? 3.0505 3.0226 2.7646 -0.1291 -0.0654 0.0323  159 TYR D C   
7583  O O   . TYR D  159 ? 2.9997 2.9698 2.7163 -0.1284 -0.0611 0.0317  159 TYR D O   
7584  C CB  . TYR D  159 ? 2.8493 2.8251 2.5817 -0.1227 -0.0676 0.0363  159 TYR D CB  
7585  C CG  . TYR D  159 ? 2.7226 2.6963 2.4603 -0.1212 -0.0622 0.0355  159 TYR D CG  
7586  C CD1 . TYR D  159 ? 2.7912 2.7627 2.5302 -0.1218 -0.0616 0.0416  159 TYR D CD1 
7587  C CD2 . TYR D  159 ? 2.5440 2.5181 2.2854 -0.1193 -0.0577 0.0286  159 TYR D CD2 
7588  C CE1 . TYR D  159 ? 2.7348 2.7041 2.4786 -0.1206 -0.0563 0.0406  159 TYR D CE1 
7589  C CE2 . TYR D  159 ? 2.4873 2.4596 2.2334 -0.1182 -0.0526 0.0275  159 TYR D CE2 
7590  C CZ  . TYR D  159 ? 2.4786 2.4483 2.2259 -0.1189 -0.0518 0.0334  159 TYR D CZ  
7591  O OH  . TYR D  159 ? 2.1199 2.0876 1.8719 -0.1180 -0.0465 0.0322  159 TYR D OH  
7592  N N   . PRO D  160 ? 3.0850 3.0566 2.7893 -0.1329 -0.0688 0.0347  160 PRO D N   
7593  C CA  . PRO D  160 ? 2.9394 2.9078 2.6348 -0.1366 -0.0676 0.0364  160 PRO D CA  
7594  C C   . PRO D  160 ? 2.7645 2.7313 2.4534 -0.1381 -0.0632 0.0285  160 PRO D C   
7595  O O   . PRO D  160 ? 2.6601 2.6262 2.3392 -0.1415 -0.0644 0.0264  160 PRO D O   
7596  C CB  . PRO D  160 ? 2.5088 2.4780 2.1963 -0.1401 -0.0734 0.0411  160 PRO D CB  
7597  C CG  . PRO D  160 ? 2.4893 2.4616 2.1854 -0.1374 -0.0777 0.0462  160 PRO D CG  
7598  C CD  . PRO D  160 ? 2.9427 2.9165 2.6483 -0.1331 -0.0751 0.0411  160 PRO D CD  
7599  N N   . LYS D  161 ? 2.5046 2.4709 2.1991 -0.1358 -0.0581 0.0242  161 LYS D N   
7600  C CA  . LYS D  161 ? 2.2146 2.1797 1.9046 -0.1368 -0.0535 0.0167  161 LYS D CA  
7601  C C   . LYS D  161 ? 2.0942 2.0579 1.7892 -0.1353 -0.0479 0.0145  161 LYS D C   
7602  O O   . LYS D  161 ? 1.9470 1.9106 1.6412 -0.1352 -0.0438 0.0081  161 LYS D O   
7603  C CB  . LYS D  161 ? 2.1999 2.1677 1.8914 -0.1353 -0.0539 0.0108  161 LYS D CB  
7604  C CG  . LYS D  161 ? 2.0452 2.0131 1.7277 -0.1383 -0.0572 0.0100  161 LYS D CG  
7605  C CD  . LYS D  161 ? 1.9760 1.9404 1.6470 -0.1428 -0.0555 0.0091  161 LYS D CD  
7606  C CE  . LYS D  161 ? 1.6568 1.6211 1.3195 -0.1454 -0.0563 0.0048  161 LYS D CE  
7607  N NZ  . LYS D  161 ? 1.4321 1.3975 1.0979 -0.1433 -0.0523 -0.0027 161 LYS D NZ  
7608  N N   . TYR D  162 ? 2.2364 2.1991 1.9369 -0.1341 -0.0476 0.0199  162 TYR D N   
7609  C CA  . TYR D  162 ? 2.2273 2.1885 1.9329 -0.1329 -0.0423 0.0182  162 TYR D CA  
7610  C C   . TYR D  162 ? 2.2108 2.1690 1.9083 -0.1360 -0.0382 0.0149  162 TYR D C   
7611  O O   . TYR D  162 ? 2.3158 2.2717 2.0046 -0.1393 -0.0396 0.0181  162 TYR D O   
7612  C CB  . TYR D  162 ? 2.0967 2.0566 1.8086 -0.1316 -0.0428 0.0255  162 TYR D CB  
7613  C CG  . TYR D  162 ? 2.1072 2.0654 1.8254 -0.1302 -0.0371 0.0240  162 TYR D CG  
7614  C CD1 . TYR D  162 ? 2.2023 2.1624 1.9307 -0.1268 -0.0349 0.0213  162 TYR D CD1 
7615  C CD2 . TYR D  162 ? 1.9884 1.9431 1.7022 -0.1325 -0.0339 0.0252  162 TYR D CD2 
7616  C CE1 . TYR D  162 ? 2.2252 2.1836 1.9591 -0.1259 -0.0296 0.0197  162 TYR D CE1 
7617  C CE2 . TYR D  162 ? 1.9641 1.9171 1.6835 -0.1314 -0.0285 0.0237  162 TYR D CE2 
7618  C CZ  . TYR D  162 ? 2.1615 2.1164 1.8910 -0.1282 -0.0264 0.0209  162 TYR D CZ  
7619  O OH  . TYR D  162 ? 2.2083 2.1614 1.9432 -0.1275 -0.0209 0.0191  162 TYR D OH  
7620  N N   . ASP E  7   ? 1.9475 1.8688 1.8465 -0.1203 0.0915  -0.0300 7   ASP E N   
7621  C CA  . ASP E  7   ? 2.0141 1.9430 1.9072 -0.1217 0.0881  -0.0373 7   ASP E CA  
7622  C C   . ASP E  7   ? 1.9355 1.8692 1.8259 -0.1186 0.0798  -0.0342 7   ASP E C   
7623  O O   . ASP E  7   ? 1.8684 1.8077 1.7521 -0.1188 0.0747  -0.0367 7   ASP E O   
7624  C CB  . ASP E  7   ? 1.9925 1.9231 1.8788 -0.1244 0.0885  -0.0407 7   ASP E CB  
7625  C CG  . ASP E  7   ? 1.9999 1.9251 1.8890 -0.1274 0.0968  -0.0428 7   ASP E CG  
7626  O OD1 . ASP E  7   ? 1.8427 1.7617 1.7389 -0.1268 0.1017  -0.0395 7   ASP E OD1 
7627  O OD2 . ASP E  7   ? 1.9707 1.8978 1.8554 -0.1303 0.0986  -0.0478 7   ASP E OD2 
7628  N N   . THR E  8   ? 1.9432 1.8743 1.8393 -0.1157 0.0786  -0.0286 8   THR E N   
7629  C CA  . THR E  8   ? 1.9929 1.9279 1.8876 -0.1126 0.0711  -0.0253 8   THR E CA  
7630  C C   . THR E  8   ? 1.7734 1.7152 1.6656 -0.1130 0.0686  -0.0322 8   THR E C   
7631  O O   . THR E  8   ? 1.5847 1.5282 1.4777 -0.1156 0.0731  -0.0394 8   THR E O   
7632  C CB  . THR E  8   ? 1.8182 1.7490 1.7208 -0.1096 0.0714  -0.0185 8   THR E CB  
7633  O OG1 . THR E  8   ? 1.4895 1.4144 1.3993 -0.1108 0.0795  -0.0189 8   THR E OG1 
7634  C CG2 . THR E  8   ? 1.7729 1.7016 1.6744 -0.1073 0.0667  -0.0093 8   THR E CG2 
7635  N N   . LEU E  9   ? 1.9276 1.8738 1.8170 -0.1106 0.0615  -0.0301 9   LEU E N   
7636  C CA  . LEU E  9   ? 1.8293 1.7813 1.7183 -0.1101 0.0591  -0.0350 9   LEU E CA  
7637  C C   . LEU E  9   ? 1.6683 1.6195 1.5624 -0.1069 0.0563  -0.0303 9   LEU E C   
7638  O O   . LEU E  9   ? 1.6163 1.5689 1.5084 -0.1044 0.0501  -0.0253 9   LEU E O   
7639  C CB  . LEU E  9   ? 1.6230 1.5818 1.5040 -0.1105 0.0537  -0.0386 9   LEU E CB  
7640  C CG  . LEU E  9   ? 1.2797 1.2433 1.1599 -0.1131 0.0566  -0.0474 9   LEU E CG  
7641  C CD1 . LEU E  9   ? 1.2823 1.2536 1.1567 -0.1127 0.0512  -0.0511 9   LEU E CD1 
7642  C CD2 . LEU E  9   ? 1.2392 1.2014 1.1262 -0.1130 0.0607  -0.0493 9   LEU E CD2 
7643  N N   . CYS E  10  ? 1.4818 1.4308 1.3825 -0.1071 0.0613  -0.0324 10  CYS E N   
7644  C CA  . CYS E  10  ? 1.4256 1.3735 1.3324 -0.1044 0.0603  -0.0289 10  CYS E CA  
7645  C C   . CYS E  10  ? 1.3958 1.3503 1.3005 -0.1037 0.0564  -0.0334 10  CYS E C   
7646  O O   . CYS E  10  ? 1.1788 1.1367 1.0816 -0.1060 0.0589  -0.0407 10  CYS E O   
7647  C CB  . CYS E  10  ? 1.4282 1.3708 1.3429 -0.1054 0.0681  -0.0300 10  CYS E CB  
7648  S SG  . CYS E  10  ? 1.7942 1.7284 1.7163 -0.1034 0.0709  -0.0205 10  CYS E SG  
7649  N N   . ILE E  11  ? 1.5839 1.5401 1.4887 -0.1006 0.0505  -0.0289 11  ILE E N   
7650  C CA  . ILE E  11  ? 1.3672 1.3290 1.2710 -0.0996 0.0471  -0.0324 11  ILE E CA  
7651  C C   . ILE E  11  ? 1.2540 1.2133 1.1654 -0.0973 0.0483  -0.0296 11  ILE E C   
7652  O O   . ILE E  11  ? 1.3904 1.3444 1.3074 -0.0958 0.0495  -0.0232 11  ILE E O   
7653  C CB  . ILE E  11  ? 1.3055 1.2723 1.2028 -0.0979 0.0392  -0.0308 11  ILE E CB  
7654  C CG1 . ILE E  11  ? 1.4101 1.3824 1.3003 -0.1002 0.0384  -0.0375 11  ILE E CG1 
7655  C CG2 . ILE E  11  ? 1.2186 1.1881 1.1180 -0.0951 0.0351  -0.0293 11  ILE E CG2 
7656  C CD1 . ILE E  11  ? 1.2242 1.2029 1.1094 -0.0987 0.0318  -0.0385 11  ILE E CD1 
7657  N N   . GLY E  12  ? 1.5507 1.5138 1.4625 -0.0972 0.0479  -0.0341 12  GLY E N   
7658  C CA  . GLY E  12  ? 1.5190 1.4804 1.4374 -0.0949 0.0484  -0.0316 12  GLY E CA  
7659  C C   . GLY E  12  ? 1.4089 1.3748 1.3271 -0.0954 0.0487  -0.0376 12  GLY E C   
7660  O O   . GLY E  12  ? 1.2784 1.2501 1.1906 -0.0968 0.0468  -0.0431 12  GLY E O   
7661  N N   . TYR E  13  ? 1.2068 1.1699 1.1315 -0.0941 0.0513  -0.0364 13  TYR E N   
7662  C CA  . TYR E  13  ? 1.1085 1.0754 1.0334 -0.0943 0.0516  -0.0414 13  TYR E CA  
7663  C C   . TYR E  13  ? 1.0509 1.0139 0.9813 -0.0964 0.0595  -0.0450 13  TYR E C   
7664  O O   . TYR E  13  ? 1.0378 0.9956 0.9712 -0.0981 0.0652  -0.0448 13  TYR E O   
7665  C CB  . TYR E  13  ? 0.9417 0.9101 0.8688 -0.0906 0.0462  -0.0368 13  TYR E CB  
7666  C CG  . TYR E  13  ? 0.9128 0.8757 0.8460 -0.0879 0.0455  -0.0285 13  TYR E CG  
7667  C CD1 . TYR E  13  ? 0.8683 0.8263 0.8099 -0.0868 0.0498  -0.0261 13  TYR E CD1 
7668  C CD2 . TYR E  13  ? 0.7867 0.7494 0.7172 -0.0866 0.0407  -0.0229 13  TYR E CD2 
7669  C CE1 . TYR E  13  ? 0.8702 0.8237 0.8180 -0.0843 0.0491  -0.0181 13  TYR E CE1 
7670  C CE2 . TYR E  13  ? 0.8031 0.7613 0.7393 -0.0843 0.0398  -0.0150 13  TYR E CE2 
7671  C CZ  . TYR E  13  ? 0.9224 0.8762 0.8675 -0.0831 0.0440  -0.0125 13  TYR E CZ  
7672  O OH  . TYR E  13  ? 0.9331 0.8829 0.8844 -0.0807 0.0431  -0.0042 13  TYR E OH  
7673  N N   . HIS E  14  ? 1.1590 1.1245 1.0906 -0.0962 0.0600  -0.0484 14  HIS E N   
7674  C CA  . HIS E  14  ? 0.9507 0.9133 0.8863 -0.0986 0.0675  -0.0531 14  HIS E CA  
7675  C C   . HIS E  14  ? 1.1499 1.1060 1.0945 -0.0966 0.0710  -0.0484 14  HIS E C   
7676  O O   . HIS E  14  ? 1.2662 1.2214 1.2138 -0.0930 0.0667  -0.0420 14  HIS E O   
7677  C CB  . HIS E  14  ? 1.1441 1.1133 1.0757 -0.1001 0.0665  -0.0597 14  HIS E CB  
7678  C CG  . HIS E  14  ? 1.2519 1.2189 1.1861 -0.1033 0.0740  -0.0655 14  HIS E CG  
7679  N ND1 . HIS E  14  ? 1.3905 1.3588 1.3216 -0.1077 0.0786  -0.0720 14  HIS E ND1 
7680  C CD2 . HIS E  14  ? 1.3190 1.2829 1.2586 -0.1030 0.0779  -0.0659 14  HIS E CD2 
7681  C CE1 . HIS E  14  ? 1.4645 1.4304 1.3987 -0.1101 0.0849  -0.0762 14  HIS E CE1 
7682  N NE2 . HIS E  14  ? 1.3339 1.2970 1.2733 -0.1073 0.0848  -0.0727 14  HIS E NE2 
7683  N N   . ALA E  15  ? 1.0297 0.9812 0.9786 -0.0991 0.0790  -0.0518 15  ALA E N   
7684  C CA  . ALA E  15  ? 1.0477 0.9928 1.0056 -0.0976 0.0836  -0.0484 15  ALA E CA  
7685  C C   . ALA E  15  ? 1.0997 1.0427 1.0594 -0.1012 0.0917  -0.0554 15  ALA E C   
7686  O O   . ALA E  15  ? 1.2172 1.1623 1.1720 -0.1051 0.0944  -0.0619 15  ALA E O   
7687  C CB  . ALA E  15  ? 0.9852 0.9235 0.9490 -0.0961 0.0858  -0.0414 15  ALA E CB  
7688  N N   . ASN E  16  ? 1.1649 1.1036 1.1314 -0.1001 0.0956  -0.0542 16  ASN E N   
7689  C CA  . ASN E  16  ? 1.3356 1.2721 1.3038 -0.1037 0.1034  -0.0609 16  ASN E CA  
7690  C C   . ASN E  16  ? 1.3267 1.2564 1.3043 -0.1022 0.1088  -0.0580 16  ASN E C   
7691  O O   . ASN E  16  ? 1.2398 1.1660 1.2236 -0.0983 0.1069  -0.0502 16  ASN E O   
7692  C CB  . ASN E  16  ? 1.3547 1.2989 1.3155 -0.1057 0.1006  -0.0679 16  ASN E CB  
7693  C CG  . ASN E  16  ? 1.3126 1.2610 1.2728 -0.1019 0.0937  -0.0647 16  ASN E CG  
7694  O OD1 . ASN E  16  ? 1.3192 1.2642 1.2855 -0.0981 0.0920  -0.0579 16  ASN E OD1 
7695  N ND2 . ASN E  16  ? 1.1799 1.1360 1.1332 -0.1030 0.0897  -0.0696 16  ASN E ND2 
7696  N N   . ASN E  17  ? 1.3878 1.3157 1.3663 -0.1054 0.1155  -0.0642 17  ASN E N   
7697  C CA  . ASN E  17  ? 1.4339 1.3551 1.4212 -0.1043 0.1214  -0.0624 17  ASN E CA  
7698  C C   . ASN E  17  ? 1.6396 1.5641 1.6273 -0.1017 0.1173  -0.0614 17  ASN E C   
7699  O O   . ASN E  17  ? 1.7297 1.6502 1.7228 -0.1019 0.1225  -0.0623 17  ASN E O   
7700  C CB  . ASN E  17  ? 1.7236 1.6404 1.7123 -0.1092 0.1316  -0.0695 17  ASN E CB  
7701  C CG  . ASN E  17  ? 1.8587 1.7820 1.8388 -0.1134 0.1314  -0.0787 17  ASN E CG  
7702  O OD1 . ASN E  17  ? 1.9001 1.8300 1.8755 -0.1122 0.1252  -0.0797 17  ASN E OD1 
7703  N ND2 . ASN E  17  ? 1.9864 1.9079 1.9645 -0.1186 0.1382  -0.0854 17  ASN E ND2 
7704  N N   . SER E  18  ? 1.4799 1.4115 1.4621 -0.0993 0.1081  -0.0595 18  SER E N   
7705  C CA  . SER E  18  ? 1.2954 1.2308 1.2773 -0.0968 0.1036  -0.0587 18  SER E CA  
7706  C C   . SER E  18  ? 1.2113 1.1416 1.2027 -0.0924 0.1034  -0.0507 18  SER E C   
7707  O O   . SER E  18  ? 1.1070 1.0348 1.1023 -0.0898 0.1012  -0.0437 18  SER E O   
7708  C CB  . SER E  18  ? 1.2841 1.2281 1.2577 -0.0954 0.0940  -0.0586 18  SER E CB  
7709  O OG  . SER E  18  ? 1.1452 1.0931 1.1177 -0.0935 0.0902  -0.0589 18  SER E OG  
7710  N N   . THR E  19  ? 1.3426 1.2715 1.3376 -0.0918 0.1059  -0.0518 19  THR E N   
7711  C CA  . THR E  19  ? 1.3600 1.2847 1.3641 -0.0877 0.1056  -0.0446 19  THR E CA  
7712  C C   . THR E  19  ? 1.2238 1.1544 1.2253 -0.0847 0.0980  -0.0429 19  THR E C   
7713  O O   . THR E  19  ? 1.1991 1.1276 1.2075 -0.0811 0.0965  -0.0371 19  THR E O   
7714  C CB  . THR E  19  ? 1.3009 1.2183 1.3129 -0.0890 0.1153  -0.0463 19  THR E CB  
7715  O OG1 . THR E  19  ? 1.3697 1.2898 1.3764 -0.0923 0.1180  -0.0545 19  THR E OG1 
7716  C CG2 . THR E  19  ? 1.3836 1.2942 1.3998 -0.0913 0.1231  -0.0466 19  THR E CG2 
7717  N N   . ASP E  20  ? 1.1054 1.0434 1.0972 -0.0863 0.0933  -0.0480 20  ASP E N   
7718  C CA  . ASP E  20  ? 1.0304 0.9745 1.0188 -0.0837 0.0859  -0.0469 20  ASP E CA  
7719  C C   . ASP E  20  ? 1.0103 0.9545 1.0023 -0.0791 0.0792  -0.0383 20  ASP E C   
7720  O O   . ASP E  20  ? 1.1304 1.0746 1.1214 -0.0786 0.0765  -0.0349 20  ASP E O   
7721  C CB  . ASP E  20  ? 1.1238 1.0760 1.1013 -0.0858 0.0812  -0.0526 20  ASP E CB  
7722  C CG  . ASP E  20  ? 1.1789 1.1326 1.1522 -0.0902 0.0866  -0.0612 20  ASP E CG  
7723  O OD1 . ASP E  20  ? 1.0124 0.9726 0.9772 -0.0924 0.0837  -0.0661 20  ASP E OD1 
7724  O OD2 . ASP E  20  ? 1.2079 1.1563 1.1863 -0.0915 0.0937  -0.0630 20  ASP E OD2 
7725  N N   . THR E  21  ? 0.9331 0.8775 0.9294 -0.0760 0.0767  -0.0348 21  THR E N   
7726  C CA  . THR E  21  ? 0.9331 0.8783 0.9325 -0.0718 0.0700  -0.0268 21  THR E CA  
7727  C C   . THR E  21  ? 0.8096 0.7612 0.8046 -0.0698 0.0630  -0.0270 21  THR E C   
7728  O O   . THR E  21  ? 0.9666 0.9192 0.9614 -0.0702 0.0647  -0.0306 21  THR E O   
7729  C CB  . THR E  21  ? 1.0457 0.9843 1.0570 -0.0692 0.0735  -0.0202 21  THR E CB  
7730  O OG1 . THR E  21  ? 1.2460 1.1820 1.2614 -0.0697 0.0790  -0.0232 21  THR E OG1 
7731  C CG2 . THR E  21  ? 0.9971 0.9298 1.0132 -0.0704 0.0790  -0.0179 21  THR E CG2 
7732  N N   . VAL E  22  ? 0.8575 0.8131 0.8489 -0.0679 0.0552  -0.0232 22  VAL E N   
7733  C CA  . VAL E  22  ? 0.7478 0.7091 0.7354 -0.0657 0.0483  -0.0227 22  VAL E CA  
7734  C C   . VAL E  22  ? 0.7981 0.7588 0.7907 -0.0620 0.0429  -0.0144 22  VAL E C   
7735  O O   . VAL E  22  ? 0.8762 0.8331 0.8737 -0.0613 0.0436  -0.0092 22  VAL E O   
7736  C CB  . VAL E  22  ? 0.6612 0.6293 0.6382 -0.0672 0.0435  -0.0270 22  VAL E CB  
7737  C CG1 . VAL E  22  ? 0.7142 0.6831 0.6863 -0.0713 0.0487  -0.0348 22  VAL E CG1 
7738  C CG2 . VAL E  22  ? 0.5716 0.5404 0.5463 -0.0666 0.0388  -0.0228 22  VAL E CG2 
7739  N N   . ASP E  23  ? 0.7145 0.6791 0.7059 -0.0597 0.0374  -0.0131 23  ASP E N   
7740  C CA  . ASP E  23  ? 0.6825 0.6475 0.6776 -0.0565 0.0315  -0.0056 23  ASP E CA  
7741  C C   . ASP E  23  ? 0.6908 0.6619 0.6774 -0.0561 0.0237  -0.0058 23  ASP E C   
7742  O O   . ASP E  23  ? 0.7886 0.7642 0.7678 -0.0573 0.0224  -0.0114 23  ASP E O   
7743  C CB  . ASP E  23  ? 0.8713 0.8353 0.8733 -0.0539 0.0315  -0.0031 23  ASP E CB  
7744  C CG  . ASP E  23  ? 1.0004 0.9577 1.0126 -0.0537 0.0387  -0.0009 23  ASP E CG  
7745  O OD1 . ASP E  23  ? 1.1027 1.0560 1.1165 -0.0556 0.0439  -0.0017 23  ASP E OD1 
7746  O OD2 . ASP E  23  ? 1.0909 1.0467 1.1097 -0.0515 0.0393  0.0017  23  ASP E OD2 
7747  N N   . THR E  24  ? 0.6532 0.6244 0.6410 -0.0545 0.0187  0.0005  24  THR E N   
7748  C CA  . THR E  24  ? 0.7395 0.7159 0.7199 -0.0539 0.0113  0.0010  24  THR E CA  
7749  C C   . THR E  24  ? 0.7057 0.6829 0.6906 -0.0509 0.0061  0.0073  24  THR E C   
7750  O O   . THR E  24  ? 0.5994 0.5733 0.5931 -0.0493 0.0083  0.0109  24  THR E O   
7751  C CB  . THR E  24  ? 0.8805 0.8570 0.8565 -0.0554 0.0096  0.0024  24  THR E CB  
7752  O OG1 . THR E  24  ? 0.8635 0.8363 0.8462 -0.0541 0.0090  0.0098  24  THR E OG1 
7753  C CG2 . THR E  24  ? 0.7581 0.7331 0.7311 -0.0585 0.0154  -0.0032 24  THR E CG2 
7754  N N   . VAL E  25  ? 0.8310 0.8124 0.8101 -0.0503 -0.0007 0.0084  25  VAL E N   
7755  C CA  . VAL E  25  ? 0.8074 0.7899 0.7900 -0.0478 -0.0061 0.0142  25  VAL E CA  
7756  C C   . VAL E  25  ? 0.7992 0.7784 0.7881 -0.0471 -0.0067 0.0216  25  VAL E C   
7757  O O   . VAL E  25  ? 0.6650 0.6432 0.6613 -0.0450 -0.0082 0.0271  25  VAL E O   
7758  C CB  . VAL E  25  ? 0.7051 0.6928 0.6793 -0.0477 -0.0129 0.0133  25  VAL E CB  
7759  C CG1 . VAL E  25  ? 0.6797 0.6692 0.6570 -0.0453 -0.0175 0.0168  25  VAL E CG1 
7760  C CG2 . VAL E  25  ? 0.7815 0.7725 0.7477 -0.0492 -0.0118 0.0057  25  VAL E CG2 
7761  N N   . LEU E  26  ? 0.8016 0.7794 0.7877 -0.0489 -0.0054 0.0217  26  LEU E N   
7762  C CA  . LEU E  26  ? 0.7975 0.7729 0.7881 -0.0485 -0.0067 0.0289  26  LEU E CA  
7763  C C   . LEU E  26  ? 0.8162 0.7859 0.8155 -0.0485 0.0002  0.0310  26  LEU E C   
7764  O O   . LEU E  26  ? 0.8847 0.8521 0.8907 -0.0474 -0.0003 0.0380  26  LEU E O   
7765  C CB  . LEU E  26  ? 0.6925 0.6695 0.6747 -0.0504 -0.0098 0.0286  26  LEU E CB  
7766  C CG  . LEU E  26  ? 0.7834 0.7656 0.7560 -0.0508 -0.0156 0.0255  26  LEU E CG  
7767  C CD1 . LEU E  26  ? 0.5971 0.5803 0.5619 -0.0528 -0.0179 0.0253  26  LEU E CD1 
7768  C CD2 . LEU E  26  ? 0.8639 0.8486 0.8386 -0.0487 -0.0215 0.0298  26  LEU E CD2 
7769  N N   . GLU E  27  ? 0.9110 0.8786 0.9104 -0.0499 0.0067  0.0251  27  GLU E N   
7770  C CA  . GLU E  27  ? 0.8290 0.7910 0.8358 -0.0504 0.0140  0.0262  27  GLU E CA  
7771  C C   . GLU E  27  ? 0.8796 0.8393 0.8898 -0.0508 0.0206  0.0209  27  GLU E C   
7772  O O   . GLU E  27  ? 0.8213 0.7839 0.8251 -0.0520 0.0207  0.0143  27  GLU E O   
7773  C CB  . GLU E  27  ? 0.9293 0.8899 0.9312 -0.0529 0.0161  0.0245  27  GLU E CB  
7774  C CG  . GLU E  27  ? 1.1572 1.1119 1.1672 -0.0530 0.0219  0.0285  27  GLU E CG  
7775  C CD  . GLU E  27  ? 1.4011 1.3550 1.4061 -0.0551 0.0224  0.0284  27  GLU E CD  
7776  O OE1 . GLU E  27  ? 1.3350 1.2838 1.3451 -0.0559 0.0284  0.0297  27  GLU E OE1 
7777  O OE2 . GLU E  27  ? 1.3644 1.3223 1.3603 -0.0560 0.0171  0.0269  27  GLU E OE2 
7778  N N   . LYS E  28  ? 0.9183 0.8727 0.9385 -0.0500 0.0262  0.0240  28  LYS E N   
7779  C CA  . LYS E  28  ? 0.8804 0.8318 0.9045 -0.0506 0.0333  0.0194  28  LYS E CA  
7780  C C   . LYS E  28  ? 0.9757 0.9225 1.0007 -0.0532 0.0412  0.0159  28  LYS E C   
7781  O O   . LYS E  28  ? 1.0674 1.0119 1.0933 -0.0538 0.0419  0.0190  28  LYS E O   
7782  C CB  . LYS E  28  ? 0.8844 0.8328 0.9198 -0.0478 0.0348  0.0248  28  LYS E CB  
7783  C CG  . LYS E  28  ? 0.9401 0.8925 0.9748 -0.0459 0.0301  0.0245  28  LYS E CG  
7784  C CD  . LYS E  28  ? 1.0176 0.9669 1.0642 -0.0432 0.0321  0.0299  28  LYS E CD  
7785  C CE  . LYS E  28  ? 1.2139 1.1660 1.2598 -0.0419 0.0299  0.0277  28  LYS E CE  
7786  N NZ  . LYS E  28  ? 1.2008 1.1591 1.2390 -0.0412 0.0212  0.0281  28  LYS E NZ  
7787  N N   . ASN E  29  ? 1.0160 0.9613 1.0405 -0.0550 0.0471  0.0093  29  ASN E N   
7788  C CA  . ASN E  29  ? 0.9473 0.8881 0.9725 -0.0579 0.0553  0.0050  29  ASN E CA  
7789  C C   . ASN E  29  ? 1.0101 0.9511 1.0297 -0.0599 0.0547  0.0044  29  ASN E C   
7790  O O   . ASN E  29  ? 1.0928 1.0291 1.1178 -0.0600 0.0584  0.0081  29  ASN E O   
7791  C CB  . ASN E  29  ? 0.9714 0.9051 1.0087 -0.0568 0.0622  0.0089  29  ASN E CB  
7792  C CG  . ASN E  29  ? 1.3856 1.3178 1.4272 -0.0563 0.0661  0.0062  29  ASN E CG  
7793  O OD1 . ASN E  29  ? 1.3508 1.2827 1.3883 -0.0590 0.0708  -0.0013 29  ASN E OD1 
7794  N ND2 . ASN E  29  ? 1.3954 1.3268 1.4450 -0.0530 0.0642  0.0123  29  ASN E ND2 
7795  N N   . VAL E  30  ? 0.9332 0.8798 0.9423 -0.0614 0.0501  0.0000  30  VAL E N   
7796  C CA  . VAL E  30  ? 0.7569 0.7043 0.7599 -0.0635 0.0495  -0.0014 30  VAL E CA  
7797  C C   . VAL E  30  ? 0.8809 0.8276 0.8795 -0.0673 0.0557  -0.0098 30  VAL E C   
7798  O O   . VAL E  30  ? 0.8718 0.8224 0.8647 -0.0687 0.0554  -0.0160 30  VAL E O   
7799  C CB  . VAL E  30  ? 0.7899 0.7437 0.7840 -0.0630 0.0408  -0.0012 30  VAL E CB  
7800  C CG1 . VAL E  30  ? 0.6784 0.6332 0.6655 -0.0656 0.0409  -0.0038 30  VAL E CG1 
7801  C CG2 . VAL E  30  ? 0.8436 0.7980 0.8416 -0.0598 0.0346  0.0072  30  VAL E CG2 
7802  N N   . THR E  31  ? 1.0069 0.9486 1.0082 -0.0692 0.0616  -0.0098 31  THR E N   
7803  C CA  . THR E  31  ? 0.8949 0.8358 0.8923 -0.0731 0.0678  -0.0177 31  THR E CA  
7804  C C   . THR E  31  ? 0.8210 0.7679 0.8075 -0.0752 0.0636  -0.0223 31  THR E C   
7805  O O   . THR E  31  ? 0.8951 0.8436 0.8783 -0.0745 0.0588  -0.0189 31  THR E O   
7806  C CB  . THR E  31  ? 0.9807 0.9143 0.9845 -0.0746 0.0758  -0.0165 31  THR E CB  
7807  O OG1 . THR E  31  ? 0.9661 0.8943 0.9805 -0.0726 0.0802  -0.0124 31  THR E OG1 
7808  C CG2 . THR E  31  ? 0.8907 0.8236 0.8902 -0.0791 0.0824  -0.0252 31  THR E CG2 
7809  N N   . VAL E  32  ? 0.9439 0.8941 0.9248 -0.0779 0.0654  -0.0302 32  VAL E N   
7810  C CA  . VAL E  32  ? 0.9359 0.8929 0.9067 -0.0796 0.0609  -0.0349 32  VAL E CA  
7811  C C   . VAL E  32  ? 0.8687 0.8262 0.8355 -0.0841 0.0668  -0.0429 32  VAL E C   
7812  O O   . VAL E  32  ? 0.9399 0.8945 0.9099 -0.0858 0.0731  -0.0465 32  VAL E O   
7813  C CB  . VAL E  32  ? 0.8505 0.8135 0.8177 -0.0777 0.0551  -0.0358 32  VAL E CB  
7814  C CG1 . VAL E  32  ? 0.7969 0.7634 0.7596 -0.0806 0.0580  -0.0439 32  VAL E CG1 
7815  C CG2 . VAL E  32  ? 0.7609 0.7291 0.7219 -0.0761 0.0468  -0.0333 32  VAL E CG2 
7816  N N   . THR E  33  ? 0.9431 0.9043 0.9027 -0.0861 0.0647  -0.0459 33  THR E N   
7817  C CA  . THR E  33  ? 0.8621 0.8237 0.8182 -0.0906 0.0702  -0.0531 33  THR E CA  
7818  C C   . THR E  33  ? 0.9383 0.9044 0.8906 -0.0926 0.0714  -0.0600 33  THR E C   
7819  O O   . THR E  33  ? 1.0812 1.0453 1.0342 -0.0960 0.0781  -0.0653 33  THR E O   
7820  C CB  . THR E  33  ? 0.9684 0.9335 0.9176 -0.0922 0.0674  -0.0547 33  THR E CB  
7821  O OG1 . THR E  33  ? 1.0067 0.9792 0.9493 -0.0909 0.0599  -0.0552 33  THR E OG1 
7822  C CG2 . THR E  33  ? 0.9939 0.9542 0.9465 -0.0907 0.0670  -0.0482 33  THR E CG2 
7823  N N   . HIS E  34  ? 1.0253 0.9977 0.9735 -0.0906 0.0649  -0.0598 34  HIS E N   
7824  C CA  . HIS E  34  ? 0.9378 0.9154 0.8819 -0.0923 0.0651  -0.0658 34  HIS E CA  
7825  C C   . HIS E  34  ? 0.9484 0.9287 0.8932 -0.0886 0.0597  -0.0626 34  HIS E C   
7826  O O   . HIS E  34  ? 0.9413 0.9219 0.8870 -0.0852 0.0541  -0.0569 34  HIS E O   
7827  C CB  . HIS E  34  ? 0.9463 0.9312 0.8819 -0.0949 0.0625  -0.0710 34  HIS E CB  
7828  C CG  . HIS E  34  ? 1.1147 1.0976 1.0491 -0.0987 0.0674  -0.0745 34  HIS E CG  
7829  N ND1 . HIS E  34  ? 1.0402 1.0197 0.9756 -0.0982 0.0670  -0.0707 34  HIS E ND1 
7830  C CD2 . HIS E  34  ? 1.1575 1.1413 1.0896 -0.1033 0.0729  -0.0813 34  HIS E CD2 
7831  C CE1 . HIS E  34  ? 1.1549 1.1332 1.0890 -0.1021 0.0721  -0.0751 34  HIS E CE1 
7832  N NE2 . HIS E  34  ? 1.3007 1.2816 1.2328 -0.1053 0.0758  -0.0817 34  HIS E NE2 
7833  N N   . SER E  35  ? 0.9103 0.8925 0.8546 -0.0894 0.0616  -0.0665 35  SER E N   
7834  C CA  . SER E  35  ? 0.8122 0.7970 0.7571 -0.0861 0.0570  -0.0640 35  SER E CA  
7835  C C   . SER E  35  ? 0.7868 0.7753 0.7288 -0.0881 0.0591  -0.0697 35  SER E C   
7836  O O   . SER E  35  ? 0.8515 0.8394 0.7920 -0.0921 0.0648  -0.0754 35  SER E O   
7837  C CB  . SER E  35  ? 0.8536 0.8319 0.8072 -0.0828 0.0578  -0.0574 35  SER E CB  
7838  O OG  . SER E  35  ? 0.9899 0.9612 0.9495 -0.0846 0.0658  -0.0583 35  SER E OG  
7839  N N   . VAL E  36  ? 0.8864 0.8786 0.8275 -0.0854 0.0544  -0.0682 36  VAL E N   
7840  C CA  . VAL E  36  ? 0.8200 0.8159 0.7583 -0.0868 0.0558  -0.0729 36  VAL E CA  
7841  C C   . VAL E  36  ? 0.8032 0.7967 0.7465 -0.0833 0.0548  -0.0691 36  VAL E C   
7842  O O   . VAL E  36  ? 0.8491 0.8410 0.7960 -0.0795 0.0506  -0.0630 36  VAL E O   
7843  C CB  . VAL E  36  ? 0.7164 0.7216 0.6465 -0.0872 0.0503  -0.0760 36  VAL E CB  
7844  C CG1 . VAL E  36  ? 0.8354 0.8435 0.7608 -0.0906 0.0511  -0.0797 36  VAL E CG1 
7845  C CG2 . VAL E  36  ? 0.7610 0.7690 0.6906 -0.0828 0.0427  -0.0707 36  VAL E CG2 
7846  N N   . ASN E  37  ? 0.8599 0.8533 0.8034 -0.0848 0.0586  -0.0727 37  ASN E N   
7847  C CA  . ASN E  37  ? 0.8236 0.8149 0.7716 -0.0818 0.0580  -0.0695 37  ASN E CA  
7848  C C   . ASN E  37  ? 0.7472 0.7461 0.6897 -0.0804 0.0525  -0.0706 37  ASN E C   
7849  O O   . ASN E  37  ? 0.7933 0.7975 0.7298 -0.0832 0.0532  -0.0761 37  ASN E O   
7850  C CB  . ASN E  37  ? 0.7997 0.7854 0.7521 -0.0840 0.0660  -0.0722 37  ASN E CB  
7851  C CG  . ASN E  37  ? 0.9023 0.8835 0.8619 -0.0804 0.0663  -0.0675 37  ASN E CG  
7852  O OD1 . ASN E  37  ? 1.0532 1.0300 1.0167 -0.0816 0.0724  -0.0692 37  ASN E OD1 
7853  N ND2 . ASN E  37  ? 0.7494 0.7320 0.7110 -0.0761 0.0598  -0.0616 37  ASN E ND2 
7854  N N   . LEU E  38  ? 0.7310 0.7305 0.6758 -0.0761 0.0470  -0.0653 38  LEU E N   
7855  C CA  . LEU E  38  ? 0.5996 0.6057 0.5399 -0.0743 0.0417  -0.0657 38  LEU E CA  
7856  C C   . LEU E  38  ? 0.6367 0.6411 0.5798 -0.0735 0.0442  -0.0661 38  LEU E C   
7857  O O   . LEU E  38  ? 0.6709 0.6805 0.6105 -0.0724 0.0410  -0.0670 38  LEU E O   
7858  C CB  . LEU E  38  ? 0.4868 0.4946 0.4276 -0.0702 0.0344  -0.0600 38  LEU E CB  
7859  C CG  . LEU E  38  ? 0.5295 0.5403 0.4660 -0.0707 0.0307  -0.0597 38  LEU E CG  
7860  C CD1 . LEU E  38  ? 0.8374 0.8477 0.7757 -0.0669 0.0247  -0.0535 38  LEU E CD1 
7861  C CD2 . LEU E  38  ? 0.5895 0.6083 0.5179 -0.0726 0.0285  -0.0646 38  LEU E CD2 
7862  N N   . LEU E  39  ? 0.6385 0.6357 0.5882 -0.0741 0.0502  -0.0654 39  LEU E N   
7863  C CA  . LEU E  39  ? 0.6762 0.6708 0.6295 -0.0733 0.0533  -0.0655 39  LEU E CA  
7864  C C   . LEU E  39  ? 0.8118 0.8054 0.7628 -0.0778 0.0604  -0.0720 39  LEU E C   
7865  O O   . LEU E  39  ? 0.8802 0.8690 0.8335 -0.0806 0.0663  -0.0740 39  LEU E O   
7866  C CB  . LEU E  39  ? 0.5976 0.5845 0.5607 -0.0705 0.0552  -0.0597 39  LEU E CB  
7867  C CG  . LEU E  39  ? 0.6883 0.6714 0.6564 -0.0698 0.0593  -0.0596 39  LEU E CG  
7868  C CD1 . LEU E  39  ? 0.7264 0.7149 0.6910 -0.0676 0.0545  -0.0594 39  LEU E CD1 
7869  C CD2 . LEU E  39  ? 0.6982 0.6740 0.6768 -0.0670 0.0612  -0.0536 39  LEU E CD2 
7870  N N   . GLU E  40  ? 0.8414 0.8396 0.7878 -0.0786 0.0599  -0.0752 40  GLU E N   
7871  C CA  . GLU E  40  ? 0.7423 0.7399 0.6861 -0.0829 0.0664  -0.0814 40  GLU E CA  
7872  C C   . GLU E  40  ? 0.7785 0.7688 0.7294 -0.0821 0.0719  -0.0800 40  GLU E C   
7873  O O   . GLU E  40  ? 0.7488 0.7389 0.7027 -0.0786 0.0692  -0.0764 40  GLU E O   
7874  C CB  . GLU E  40  ? 0.6384 0.6447 0.5738 -0.0843 0.0634  -0.0854 40  GLU E CB  
7875  C CG  . GLU E  40  ? 0.8043 0.8108 0.7359 -0.0893 0.0697  -0.0919 40  GLU E CG  
7876  C CD  . GLU E  40  ? 1.0095 1.0147 0.9393 -0.0941 0.0746  -0.0966 40  GLU E CD  
7877  O OE1 . GLU E  40  ? 1.1125 1.1244 1.0348 -0.0977 0.0739  -0.1014 40  GLU E OE1 
7878  O OE2 . GLU E  40  ? 0.9737 0.9713 0.9097 -0.0944 0.0792  -0.0952 40  GLU E OE2 
7879  N N   . ASP E  41  ? 0.8441 0.8284 0.7979 -0.0855 0.0797  -0.0830 41  ASP E N   
7880  C CA  . ASP E  41  ? 0.8755 0.8521 0.8367 -0.0850 0.0859  -0.0819 41  ASP E CA  
7881  C C   . ASP E  41  ? 0.8904 0.8649 0.8488 -0.0905 0.0941  -0.0889 41  ASP E C   
7882  O O   . ASP E  41  ? 1.1277 1.0942 1.0924 -0.0917 0.1014  -0.0893 41  ASP E O   
7883  C CB  . ASP E  41  ? 1.0395 1.0084 1.0102 -0.0827 0.0880  -0.0766 41  ASP E CB  
7884  C CG  . ASP E  41  ? 1.2397 1.2068 1.2097 -0.0858 0.0909  -0.0786 41  ASP E CG  
7885  O OD1 . ASP E  41  ? 1.1201 1.0917 1.0824 -0.0898 0.0917  -0.0844 41  ASP E OD1 
7886  O OD2 . ASP E  41  ? 1.2420 1.2034 1.2194 -0.0841 0.0925  -0.0741 41  ASP E OD2 
7887  N N   . LYS E  42  ? 0.8781 0.8597 0.8272 -0.0938 0.0928  -0.0944 42  LYS E N   
7888  C CA  . LYS E  42  ? 1.0027 0.9834 0.9479 -0.0996 0.1000  -0.1016 42  LYS E CA  
7889  C C   . LYS E  42  ? 0.9915 0.9800 0.9279 -0.1017 0.0979  -0.1059 42  LYS E C   
7890  O O   . LYS E  42  ? 0.8439 0.8410 0.7733 -0.1021 0.0920  -0.1071 42  LYS E O   
7891  C CB  . LYS E  42  ? 1.0953 1.0763 1.0378 -0.1036 0.1023  -0.1051 42  LYS E CB  
7892  C CG  . LYS E  42  ? 1.4894 1.4627 1.4348 -0.1081 0.1124  -0.1094 42  LYS E CG  
7893  C CD  . LYS E  42  ? 1.6641 1.6356 1.6103 -0.1101 0.1142  -0.1103 42  LYS E CD  
7894  C CE  . LYS E  42  ? 1.4658 1.4343 1.4188 -0.1049 0.1099  -0.1027 42  LYS E CE  
7895  N NZ  . LYS E  42  ? 1.5181 1.4855 1.4713 -0.1066 0.1109  -0.1032 42  LYS E NZ  
7896  N N   . HIS E  43  ? 0.8363 0.8217 0.7733 -0.1031 0.1028  -0.1081 43  HIS E N   
7897  C CA  . HIS E  43  ? 0.7681 0.7603 0.6970 -0.1054 0.1017  -0.1122 43  HIS E CA  
7898  C C   . HIS E  43  ? 0.9235 0.9141 0.8482 -0.1122 0.1097  -0.1197 43  HIS E C   
7899  O O   . HIS E  43  ? 1.0660 1.0484 0.9958 -0.1144 0.1170  -0.1211 43  HIS E O   
7900  C CB  . HIS E  43  ? 0.7472 0.7377 0.6793 -0.1017 0.1008  -0.1089 43  HIS E CB  
7901  C CG  . HIS E  43  ? 0.8048 0.7850 0.7448 -0.1018 0.1086  -0.1083 43  HIS E CG  
7902  N ND1 . HIS E  43  ? 0.9405 0.9180 0.8785 -0.1056 0.1154  -0.1131 43  HIS E ND1 
7903  C CD2 . HIS E  43  ? 0.7984 0.7704 0.7486 -0.0987 0.1110  -0.1035 43  HIS E CD2 
7904  C CE1 . HIS E  43  ? 1.0184 0.9863 0.9652 -0.1046 0.1218  -0.1113 43  HIS E CE1 
7905  N NE2 . HIS E  43  ? 1.0073 0.9719 0.9619 -0.1004 0.1192  -0.1054 43  HIS E NE2 
7906  N N   . ASN E  44  ? 0.8532 0.8517 0.7687 -0.1158 0.1083  -0.1245 44  ASN E N   
7907  C CA  . ASN E  44  ? 0.8125 0.8106 0.7228 -0.1228 0.1154  -0.1320 44  ASN E CA  
7908  C C   . ASN E  44  ? 0.7844 0.7767 0.6963 -0.1243 0.1221  -0.1340 44  ASN E C   
7909  O O   . ASN E  44  ? 0.7884 0.7791 0.6964 -0.1303 0.1289  -0.1403 44  ASN E O   
7910  C CB  . ASN E  44  ? 0.7410 0.7506 0.6408 -0.1264 0.1112  -0.1364 44  ASN E CB  
7911  C CG  . ASN E  44  ? 0.8622 0.8790 0.7573 -0.1240 0.1055  -0.1347 44  ASN E CG  
7912  O OD1 . ASN E  44  ? 0.8706 0.8974 0.7578 -0.1261 0.1012  -0.1371 44  ASN E OD1 
7913  N ND2 . ASN E  44  ? 0.9274 0.9395 0.8278 -0.1197 0.1055  -0.1305 44  ASN E ND2 
7914  N N   . GLY E  45  ? 0.8423 0.8314 0.7598 -0.1190 0.1202  -0.1286 45  GLY E N   
7915  C CA  . GLY E  45  ? 0.8920 0.8751 0.8119 -0.1197 0.1263  -0.1297 45  GLY E CA  
7916  C C   . GLY E  45  ? 0.9042 0.8932 0.8145 -0.1242 0.1274  -0.1353 45  GLY E C   
7917  O O   . GLY E  45  ? 0.8831 0.8670 0.7931 -0.1278 0.1349  -0.1391 45  GLY E O   
7918  N N   . LYS E  46  ? 0.9495 0.9493 0.8520 -0.1242 0.1200  -0.1356 46  LYS E N   
7919  C CA  . LYS E  46  ? 0.8962 0.9031 0.7894 -0.1279 0.1196  -0.1399 46  LYS E CA  
7920  C C   . LYS E  46  ? 0.8063 0.8198 0.6978 -0.1227 0.1115  -0.1351 46  LYS E C   
7921  O O   . LYS E  46  ? 0.8454 0.8625 0.7391 -0.1180 0.1044  -0.1302 46  LYS E O   
7922  C CB  . LYS E  46  ? 0.9769 0.9920 0.8613 -0.1335 0.1185  -0.1454 46  LYS E CB  
7923  C CG  . LYS E  46  ? 1.0202 1.0297 0.9050 -0.1394 0.1266  -0.1510 46  LYS E CG  
7924  C CD  . LYS E  46  ? 1.3234 1.3417 1.2007 -0.1439 0.1239  -0.1551 46  LYS E CD  
7925  C CE  . LYS E  46  ? 1.4983 1.5116 1.3750 -0.1506 0.1323  -0.1615 46  LYS E CE  
7926  N NZ  . LYS E  46  ? 1.5070 1.5289 1.3771 -0.1546 0.1293  -0.1652 46  LYS E NZ  
7927  N N   . LEU E  47  ? 0.8407 0.8556 0.7285 -0.1235 0.1128  -0.1363 47  LEU E N   
7928  C CA  . LEU E  47  ? 0.8102 0.8327 0.6946 -0.1196 0.1052  -0.1327 47  LEU E CA  
7929  C C   . LEU E  47  ? 0.7252 0.7596 0.5994 -0.1232 0.1010  -0.1362 47  LEU E C   
7930  O O   . LEU E  47  ? 0.9116 0.9497 0.7785 -0.1280 0.1037  -0.1408 47  LEU E O   
7931  C CB  . LEU E  47  ? 0.7678 0.7871 0.6526 -0.1189 0.1084  -0.1324 47  LEU E CB  
7932  C CG  . LEU E  47  ? 0.6778 0.6901 0.5722 -0.1122 0.1074  -0.1259 47  LEU E CG  
7933  C CD1 . LEU E  47  ? 0.7174 0.7231 0.6210 -0.1094 0.1078  -0.1226 47  LEU E CD1 
7934  C CD2 . LEU E  47  ? 0.7126 0.7180 0.6090 -0.1133 0.1142  -0.1272 47  LEU E CD2 
7935  N N   . CYS E  48  ? 0.7933 0.8338 0.6671 -0.1209 0.0943  -0.1338 48  CYS E N   
7936  C CA  . CYS E  48  ? 0.8960 0.9477 0.7611 -0.1243 0.0902  -0.1368 48  CYS E CA  
7937  C C   . CYS E  48  ? 0.6799 0.7413 0.5407 -0.1210 0.0827  -0.1336 48  CYS E C   
7938  O O   . CYS E  48  ? 0.7264 0.7855 0.5909 -0.1158 0.0803  -0.1288 48  CYS E O   
7939  C CB  . CYS E  48  ? 0.7730 0.8263 0.6400 -0.1240 0.0875  -0.1363 48  CYS E CB  
7940  S SG  . CYS E  48  ? 0.8601 0.9020 0.7332 -0.1270 0.0958  -0.1391 48  CYS E SG  
7941  N N   . LYS E  49  ? 0.8135 0.8856 0.6666 -0.1241 0.0791  -0.1361 49  LYS E N   
7942  C CA  . LYS E  49  ? 0.8366 0.9188 0.6855 -0.1211 0.0719  -0.1330 49  LYS E CA  
7943  C C   . LYS E  49  ? 0.7750 0.8589 0.6285 -0.1150 0.0651  -0.1274 49  LYS E C   
7944  O O   . LYS E  49  ? 0.9269 1.0088 0.7834 -0.1150 0.0648  -0.1274 49  LYS E O   
7945  C CB  . LYS E  49  ? 0.8405 0.9340 0.6801 -0.1266 0.0705  -0.1375 49  LYS E CB  
7946  C CG  . LYS E  49  ? 0.9202 1.0121 0.7544 -0.1339 0.0777  -0.1440 49  LYS E CG  
7947  C CD  . LYS E  49  ? 1.0508 1.1549 0.8757 -0.1394 0.0755  -0.1481 49  LYS E CD  
7948  C CE  . LYS E  49  ? 1.2107 1.3138 1.0331 -0.1464 0.0806  -0.1545 49  LYS E CE  
7949  N NZ  . LYS E  49  ? 1.3562 1.4723 1.1713 -0.1504 0.0765  -0.1571 49  LYS E NZ  
7950  N N   . LEU E  50  ? 0.8355 0.9232 0.6894 -0.1099 0.0597  -0.1226 50  LEU E N   
7951  C CA  . LEU E  50  ? 0.8705 0.9581 0.7296 -0.1036 0.0538  -0.1169 50  LEU E CA  
7952  C C   . LEU E  50  ? 1.1086 1.2065 0.9643 -0.1027 0.0471  -0.1157 50  LEU E C   
7953  O O   . LEU E  50  ? 1.4397 1.5365 1.2987 -0.1006 0.0446  -0.1138 50  LEU E O   
7954  C CB  . LEU E  50  ? 0.8782 0.9635 0.7406 -0.0982 0.0516  -0.1119 50  LEU E CB  
7955  C CG  . LEU E  50  ? 0.8312 0.9143 0.6999 -0.0916 0.0463  -0.1058 50  LEU E CG  
7956  C CD1 . LEU E  50  ? 0.7268 0.8054 0.5998 -0.0915 0.0467  -0.1057 50  LEU E CD1 
7957  C CD2 . LEU E  50  ? 0.7319 0.8078 0.6062 -0.0872 0.0472  -0.1019 50  LEU E CD2 
7958  N N   . ARG E  51  ? 0.9089 1.0168 0.7579 -0.1042 0.0444  -0.1167 51  ARG E N   
7959  C CA  . ARG E  51  ? 1.2115 1.3300 1.0569 -0.1043 0.0389  -0.1164 51  ARG E CA  
7960  C C   . ARG E  51  ? 1.2140 1.3370 1.0535 -0.1116 0.0423  -0.1227 51  ARG E C   
7961  O O   . ARG E  51  ? 1.5573 1.6780 1.3979 -0.1142 0.0442  -0.1253 51  ARG E O   
7962  C CB  . ARG E  51  ? 1.4983 1.6258 1.3403 -0.1014 0.0336  -0.1132 51  ARG E CB  
7963  C CG  . ARG E  51  ? 1.6268 1.7495 1.4738 -0.0950 0.0315  -0.1077 51  ARG E CG  
7964  C CD  . ARG E  51  ? 2.0089 2.1407 1.8542 -0.0910 0.0249  -0.1036 51  ARG E CD  
7965  N NE  . ARG E  51  ? 2.1424 2.2781 1.9893 -0.0889 0.0204  -0.1018 51  ARG E NE  
7966  C CZ  . ARG E  51  ? 2.0359 2.1824 1.8787 -0.0898 0.0165  -0.1019 51  ARG E CZ  
7967  N NH1 . ARG E  51  ? 1.8692 2.0243 1.7060 -0.0928 0.0163  -0.1037 51  ARG E NH1 
7968  N NH2 . ARG E  51  ? 1.8792 2.0282 1.7241 -0.0877 0.0128  -0.1002 51  ARG E NH2 
7969  N N   . GLY E  52  ? 0.9968 1.1263 0.8298 -0.1150 0.0429  -0.1251 52  GLY E N   
7970  C CA  . GLY E  52  ? 1.2379 1.3710 1.0648 -0.1226 0.0470  -0.1315 52  GLY E CA  
7971  C C   . GLY E  52  ? 1.2474 1.3786 1.0710 -0.1247 0.0509  -0.1331 52  GLY E C   
7972  O O   . GLY E  52  ? 1.3091 1.4430 1.1267 -0.1311 0.0547  -0.1383 52  GLY E O   
7973  N N   . VAL E  53  ? 1.1893 1.3157 1.0168 -0.1193 0.0498  -0.1285 53  VAL E N   
7974  C CA  . VAL E  53  ? 1.0011 1.1253 0.8262 -0.1202 0.0530  -0.1291 53  VAL E CA  
7975  C C   . VAL E  53  ? 0.6568 0.7678 0.4866 -0.1211 0.0603  -0.1309 53  VAL E C   
7976  O O   . VAL E  53  ? 0.7455 0.8481 0.5828 -0.1175 0.0609  -0.1285 53  VAL E O   
7977  C CB  . VAL E  53  ? 0.8663 0.9930 0.6930 -0.1137 0.0479  -0.1230 53  VAL E CB  
7978  C CG1 . VAL E  53  ? 0.8717 0.9973 0.6949 -0.1150 0.0510  -0.1238 53  VAL E CG1 
7979  C CG2 . VAL E  53  ? 0.7254 0.8645 0.5489 -0.1118 0.0405  -0.1204 53  VAL E CG2 
7980  N N   . ALA E  54  ? 0.7253 0.8343 0.5506 -0.1260 0.0659  -0.1352 54  ALA E N   
7981  C CA  . ALA E  54  ? 0.7928 0.8894 0.6224 -0.1274 0.0736  -0.1374 54  ALA E CA  
7982  C C   . ALA E  54  ? 0.7918 0.8820 0.6265 -0.1220 0.0737  -0.1328 54  ALA E C   
7983  O O   . ALA E  54  ? 0.7926 0.8886 0.6249 -0.1189 0.0692  -0.1294 54  ALA E O   
7984  C CB  . ALA E  54  ? 0.9192 1.0160 0.7419 -0.1354 0.0801  -0.1443 54  ALA E CB  
7985  N N   . PRO E  55  ? 0.6236 0.7018 0.4655 -0.1207 0.0790  -0.1324 55  PRO E N   
7986  C CA  . PRO E  55  ? 0.6108 0.6820 0.4581 -0.1160 0.0801  -0.1285 55  PRO E CA  
7987  C C   . PRO E  55  ? 0.6657 0.7361 0.5078 -0.1198 0.0852  -0.1318 55  PRO E C   
7988  O O   . PRO E  55  ? 0.7627 0.8343 0.5987 -0.1266 0.0899  -0.1378 55  PRO E O   
7989  C CB  . PRO E  55  ? 0.5577 0.6170 0.4142 -0.1148 0.0849  -0.1280 55  PRO E CB  
7990  C CG  . PRO E  55  ? 0.6398 0.6984 0.4934 -0.1211 0.0895  -0.1339 55  PRO E CG  
7991  C CD  . PRO E  55  ? 0.6297 0.7005 0.4761 -0.1230 0.0837  -0.1351 55  PRO E CD  
7992  N N   . LEU E  56  ? 0.6726 0.7409 0.5169 -0.1156 0.0842  -0.1280 56  LEU E N   
7993  C CA  . LEU E  56  ? 0.5886 0.6549 0.4287 -0.1186 0.0893  -0.1306 56  LEU E CA  
7994  C C   . LEU E  56  ? 0.7304 0.7835 0.5776 -0.1188 0.0972  -0.1316 56  LEU E C   
7995  O O   . LEU E  56  ? 0.7747 0.8213 0.6302 -0.1132 0.0966  -0.1269 56  LEU E O   
7996  C CB  . LEU E  56  ? 0.7189 0.7900 0.5576 -0.1140 0.0844  -0.1259 56  LEU E CB  
7997  C CG  . LEU E  56  ? 0.7547 0.8242 0.5888 -0.1165 0.0889  -0.1278 56  LEU E CG  
7998  C CD1 . LEU E  56  ? 0.8304 0.9071 0.6535 -0.1241 0.0911  -0.1338 56  LEU E CD1 
7999  C CD2 . LEU E  56  ? 0.7054 0.7786 0.5398 -0.1108 0.0837  -0.1222 56  LEU E CD2 
8000  N N   . HIS E  57  ? 0.8020 0.8511 0.6462 -0.1254 0.1046  -0.1378 57  HIS E N   
8001  C CA  . HIS E  57  ? 0.7648 0.8012 0.6158 -0.1262 0.1129  -0.1392 57  HIS E CA  
8002  C C   . HIS E  57  ? 0.8969 0.9301 0.7447 -0.1283 0.1182  -0.1412 57  HIS E C   
8003  O O   . HIS E  57  ? 0.9789 1.0169 0.8171 -0.1343 0.1205  -0.1462 57  HIS E O   
8004  C CB  . HIS E  57  ? 0.8347 0.8672 0.6853 -0.1320 0.1188  -0.1449 57  HIS E CB  
8005  C CG  . HIS E  57  ? 0.9141 0.9334 0.7743 -0.1313 0.1263  -0.1449 57  HIS E CG  
8006  N ND1 . HIS E  57  ? 0.9777 0.9890 0.8386 -0.1343 0.1348  -0.1481 57  HIS E ND1 
8007  C CD2 . HIS E  57  ? 0.9162 0.9291 0.7860 -0.1279 0.1266  -0.1420 57  HIS E CD2 
8008  C CE1 . HIS E  57  ? 1.0550 1.0555 0.9258 -0.1327 0.1401  -0.1470 57  HIS E CE1 
8009  N NE2 . HIS E  57  ? 1.0139 1.0153 0.8903 -0.1288 0.1351  -0.1432 57  HIS E NE2 
8010  N N   . LEU E  58  ? 0.9087 0.9339 0.7644 -0.1236 0.1202  -0.1374 58  LEU E N   
8011  C CA  . LEU E  58  ? 0.9820 1.0039 0.8354 -0.1247 0.1247  -0.1384 58  LEU E CA  
8012  C C   . LEU E  58  ? 1.0597 1.0707 0.9157 -0.1292 0.1354  -0.1431 58  LEU E C   
8013  O O   . LEU E  58  ? 1.0732 1.0815 0.9256 -0.1319 0.1406  -0.1456 58  LEU E O   
8014  C CB  . LEU E  58  ? 0.8893 0.9089 0.7496 -0.1171 0.1209  -0.1315 58  LEU E CB  
8015  C CG  . LEU E  58  ? 0.7570 0.7865 0.6155 -0.1122 0.1107  -0.1264 58  LEU E CG  
8016  C CD1 . LEU E  58  ? 0.7462 0.7727 0.6114 -0.1053 0.1080  -0.1202 58  LEU E CD1 
8017  C CD2 . LEU E  58  ? 0.8829 0.9240 0.7292 -0.1160 0.1075  -0.1291 58  LEU E CD2 
8018  N N   . GLY E  59  ? 1.0661 1.0707 0.9285 -0.1300 0.1390  -0.1443 59  GLY E N   
8019  C CA  . GLY E  59  ? 1.0040 0.9979 0.8697 -0.1343 0.1495  -0.1488 59  GLY E CA  
8020  C C   . GLY E  59  ? 1.0652 1.0493 0.9392 -0.1306 0.1543  -0.1458 59  GLY E C   
8021  O O   . GLY E  59  ? 1.2036 1.1834 1.0879 -0.1242 0.1518  -0.1399 59  GLY E O   
8022  N N   . LYS E  60  ? 1.1790 1.1598 1.0483 -0.1349 0.1611  -0.1499 60  LYS E N   
8023  C CA  . LYS E  60  ? 1.3324 1.3033 1.2095 -0.1323 0.1669  -0.1480 60  LYS E CA  
8024  C C   . LYS E  60  ? 1.2557 1.2303 1.1337 -0.1264 0.1608  -0.1422 60  LYS E C   
8025  O O   . LYS E  60  ? 1.4017 1.3689 1.2868 -0.1231 0.1643  -0.1395 60  LYS E O   
8026  C CB  . LYS E  60  ? 1.3892 1.3547 1.2607 -0.1395 0.1771  -0.1549 60  LYS E CB  
8027  C CG  . LYS E  60  ? 1.8831 1.8366 1.7639 -0.1376 0.1851  -0.1537 60  LYS E CG  
8028  C CD  . LYS E  60  ? 2.0475 1.9915 1.9414 -0.1350 0.1891  -0.1516 60  LYS E CD  
8029  C CE  . LYS E  60  ? 2.2513 2.1925 2.1425 -0.1417 0.1954  -0.1581 60  LYS E CE  
8030  N NZ  . LYS E  60  ? 2.0702 2.0022 1.9744 -0.1391 0.1994  -0.1557 60  LYS E NZ  
8031  N N   . CYS E  61  ? 1.1539 1.1398 1.0249 -0.1248 0.1518  -0.1402 61  CYS E N   
8032  C CA  . CYS E  61  ? 1.0429 1.0330 0.9138 -0.1195 0.1459  -0.1350 61  CYS E CA  
8033  C C   . CYS E  61  ? 1.0621 1.0557 0.9398 -0.1122 0.1369  -0.1281 61  CYS E C   
8034  O O   . CYS E  61  ? 1.1414 1.1368 1.0210 -0.1119 0.1339  -0.1278 61  CYS E O   
8035  C CB  . CYS E  61  ? 0.9167 0.9172 0.7742 -0.1230 0.1427  -0.1375 61  CYS E CB  
8036  S SG  . CYS E  61  ? 1.2463 1.2438 1.0944 -0.1317 0.1525  -0.1454 61  CYS E SG  
8037  N N   . ASN E  62  ? 0.8575 0.8517 0.7385 -0.1066 0.1329  -0.1228 62  ASN E N   
8038  C CA  . ASN E  62  ? 0.8137 0.8123 0.6996 -0.0999 0.1240  -0.1164 62  ASN E CA  
8039  C C   . ASN E  62  ? 0.7497 0.7592 0.6271 -0.0986 0.1167  -0.1147 62  ASN E C   
8040  O O   . ASN E  62  ? 0.7666 0.7799 0.6349 -0.1026 0.1187  -0.1181 62  ASN E O   
8041  C CB  . ASN E  62  ? 0.9448 0.9353 0.8431 -0.0938 0.1246  -0.1109 62  ASN E CB  
8042  C CG  . ASN E  62  ? 0.9505 0.9377 0.8486 -0.0931 0.1282  -0.1104 62  ASN E CG  
8043  O OD1 . ASN E  62  ? 1.0151 1.0081 0.9036 -0.0954 0.1275  -0.1124 62  ASN E OD1 
8044  N ND2 . ASN E  62  ? 0.8905 0.8685 0.7993 -0.0897 0.1320  -0.1074 62  ASN E ND2 
8045  N N   . ILE E  63  ? 0.6853 0.7000 0.5656 -0.0932 0.1085  -0.1095 63  ILE E N   
8046  C CA  . ILE E  63  ? 0.7767 0.8018 0.6497 -0.0915 0.1013  -0.1074 63  ILE E CA  
8047  C C   . ILE E  63  ? 0.6983 0.7237 0.5674 -0.0915 0.1034  -0.1072 63  ILE E C   
8048  O O   . ILE E  63  ? 0.7968 0.8299 0.6558 -0.0946 0.1021  -0.1094 63  ILE E O   
8049  C CB  . ILE E  63  ? 0.6951 0.7231 0.5741 -0.0846 0.0932  -0.1010 63  ILE E CB  
8050  C CG1 . ILE E  63  ? 0.6710 0.6999 0.5528 -0.0848 0.0906  -0.1012 63  ILE E CG1 
8051  C CG2 . ILE E  63  ? 0.6904 0.7289 0.5626 -0.0827 0.0864  -0.0987 63  ILE E CG2 
8052  C CD1 . ILE E  63  ? 0.8041 0.8421 0.6762 -0.0894 0.0883  -0.1051 63  ILE E CD1 
8053  N N   . ALA E  64  ? 0.6623 0.6793 0.5394 -0.0882 0.1066  -0.1045 64  ALA E N   
8054  C CA  . ALA E  64  ? 0.7112 0.7273 0.5856 -0.0878 0.1090  -0.1040 64  ALA E CA  
8055  C C   . ALA E  64  ? 0.7936 0.8108 0.6578 -0.0950 0.1150  -0.1103 64  ALA E C   
8056  O O   . ALA E  64  ? 0.8069 0.8312 0.6623 -0.0964 0.1130  -0.1108 64  ALA E O   
8057  C CB  . ALA E  64  ? 0.7223 0.7278 0.6077 -0.0840 0.1132  -0.1011 64  ALA E CB  
8058  N N   . GLY E  65  ? 0.7399 0.7500 0.6055 -0.0997 0.1225  -0.1151 65  GLY E N   
8059  C CA  . GLY E  65  ? 0.7605 0.7705 0.6168 -0.1070 0.1290  -0.1216 65  GLY E CA  
8060  C C   . GLY E  65  ? 0.8532 0.8749 0.6975 -0.1115 0.1249  -0.1246 65  GLY E C   
8061  O O   . GLY E  65  ? 0.9855 1.0116 0.8199 -0.1157 0.1265  -0.1276 65  GLY E O   
8062  N N   . TRP E  66  ? 0.7699 0.7968 0.6151 -0.1105 0.1194  -0.1237 66  TRP E N   
8063  C CA  . TRP E  66  ? 0.8050 0.8430 0.6397 -0.1146 0.1153  -0.1265 66  TRP E CA  
8064  C C   . TRP E  66  ? 0.7498 0.7984 0.5775 -0.1126 0.1087  -0.1233 66  TRP E C   
8065  O O   . TRP E  66  ? 0.9361 0.9924 0.7532 -0.1176 0.1085  -0.1266 66  TRP E O   
8066  C CB  . TRP E  66  ? 0.8556 0.8962 0.6940 -0.1134 0.1109  -0.1257 66  TRP E CB  
8067  C CG  . TRP E  66  ? 0.9030 0.9564 0.7327 -0.1154 0.1045  -0.1264 66  TRP E CG  
8068  C CD1 . TRP E  66  ? 0.9307 0.9906 0.7499 -0.1225 0.1062  -0.1319 66  TRP E CD1 
8069  C CD2 . TRP E  66  ? 0.8469 0.9084 0.6777 -0.1104 0.0955  -0.1215 66  TRP E CD2 
8070  N NE1 . TRP E  66  ? 0.9284 1.0001 0.7425 -0.1221 0.0986  -0.1304 66  TRP E NE1 
8071  C CE2 . TRP E  66  ? 0.8621 0.9347 0.6832 -0.1147 0.0921  -0.1241 66  TRP E CE2 
8072  C CE3 . TRP E  66  ? 0.8417 0.9019 0.6808 -0.1030 0.0900  -0.1152 66  TRP E CE3 
8073  C CZ2 . TRP E  66  ? 0.8453 0.9278 0.6653 -0.1114 0.0837  -0.1205 66  TRP E CZ2 
8074  C CZ3 . TRP E  66  ? 0.8406 0.9103 0.6781 -0.1000 0.0819  -0.1120 66  TRP E CZ3 
8075  C CH2 . TRP E  66  ? 0.8210 0.9016 0.6492 -0.1041 0.0789  -0.1146 66  TRP E CH2 
8076  N N   . ILE E  67  ? 0.6940 0.7431 0.5279 -0.1053 0.1033  -0.1169 67  ILE E N   
8077  C CA  . ILE E  67  ? 0.9023 0.9611 0.7307 -0.1026 0.0968  -0.1132 67  ILE E CA  
8078  C C   . ILE E  67  ? 0.8982 0.9556 0.7221 -0.1037 0.1005  -0.1135 67  ILE E C   
8079  O O   . ILE E  67  ? 0.8521 0.9184 0.6669 -0.1056 0.0979  -0.1137 67  ILE E O   
8080  C CB  . ILE E  67  ? 0.7779 0.8378 0.6142 -0.0945 0.0897  -0.1063 67  ILE E CB  
8081  C CG1 . ILE E  67  ? 1.0312 1.0886 0.8745 -0.0929 0.0877  -0.1057 67  ILE E CG1 
8082  C CG2 . ILE E  67  ? 0.6737 0.7455 0.5036 -0.0925 0.0823  -0.1031 67  ILE E CG2 
8083  C CD1 . ILE E  67  ? 1.1219 1.1802 0.9727 -0.0855 0.0810  -0.0993 67  ILE E CD1 
8084  N N   . LEU E  68  ? 0.8444 0.8908 0.6749 -0.1024 0.1065  -0.1134 68  LEU E N   
8085  C CA  . LEU E  68  ? 0.8955 0.9394 0.7225 -0.1034 0.1107  -0.1138 68  LEU E CA  
8086  C C   . LEU E  68  ? 0.9639 1.0098 0.7798 -0.1118 0.1163  -0.1205 68  LEU E C   
8087  O O   . LEU E  68  ? 0.8063 0.8556 0.6146 -0.1137 0.1173  -0.1210 68  LEU E O   
8088  C CB  . LEU E  68  ? 0.7486 0.7798 0.5860 -0.1003 0.1163  -0.1124 68  LEU E CB  
8089  C CG  . LEU E  68  ? 0.8224 0.8519 0.6698 -0.0920 0.1112  -0.1053 68  LEU E CG  
8090  C CD1 . LEU E  68  ? 0.8004 0.8179 0.6572 -0.0897 0.1173  -0.1042 68  LEU E CD1 
8091  C CD2 . LEU E  68  ? 0.5948 0.6331 0.4368 -0.0889 0.1050  -0.1014 68  LEU E CD2 
8092  N N   . GLY E  69  ? 0.9217 0.9656 0.7366 -0.1169 0.1199  -0.1256 69  GLY E N   
8093  C CA  . GLY E  69  ? 0.9039 0.9494 0.7084 -0.1254 0.1254  -0.1325 69  GLY E CA  
8094  C C   . GLY E  69  ? 1.0598 1.0932 0.8670 -0.1289 0.1357  -0.1367 69  GLY E C   
8095  O O   . GLY E  69  ? 1.1471 1.1802 0.9460 -0.1342 0.1408  -0.1406 69  GLY E O   
8096  N N   . ASN E  70  ? 1.0278 1.0510 0.8465 -0.1259 0.1390  -0.1357 70  ASN E N   
8097  C CA  . ASN E  70  ? 1.1022 1.1133 0.9250 -0.1290 0.1493  -0.1396 70  ASN E CA  
8098  C C   . ASN E  70  ? 1.2309 1.2427 1.0439 -0.1383 0.1554  -0.1476 70  ASN E C   
8099  O O   . ASN E  70  ? 1.2537 1.2712 1.0628 -0.1415 0.1529  -0.1502 70  ASN E O   
8100  C CB  . ASN E  70  ? 1.1094 1.1112 0.9459 -0.1249 0.1510  -0.1374 70  ASN E CB  
8101  C CG  . ASN E  70  ? 1.1565 1.1451 0.9994 -0.1266 0.1614  -0.1400 70  ASN E CG  
8102  O OD1 . ASN E  70  ? 1.1806 1.1660 1.0173 -0.1336 0.1690  -0.1463 70  ASN E OD1 
8103  N ND2 . ASN E  70  ? 1.1471 1.1280 1.0026 -0.1204 0.1618  -0.1351 70  ASN E ND2 
8104  N N   . PRO E  71  ? 1.4100 1.4160 1.2187 -0.1429 0.1635  -0.1517 71  PRO E N   
8105  C CA  . PRO E  71  ? 1.3853 1.3916 1.1840 -0.1523 0.1701  -0.1597 71  PRO E CA  
8106  C C   . PRO E  71  ? 1.3241 1.3267 1.1264 -0.1556 0.1733  -0.1637 71  PRO E C   
8107  O O   . PRO E  71  ? 1.5376 1.5447 1.3306 -0.1629 0.1751  -0.1696 71  PRO E O   
8108  C CB  . PRO E  71  ? 1.3550 1.3508 1.1545 -0.1546 0.1798  -0.1623 71  PRO E CB  
8109  C CG  . PRO E  71  ? 1.3261 1.3223 1.1296 -0.1475 0.1757  -0.1557 71  PRO E CG  
8110  C CD  . PRO E  71  ? 1.3133 1.3126 1.1261 -0.1396 0.1670  -0.1490 71  PRO E CD  
8111  N N   . GLU E  72  ? 1.2743 1.2691 1.0897 -0.1503 0.1738  -0.1604 72  GLU E N   
8112  C CA  . GLU E  72  ? 1.4337 1.4237 1.2538 -0.1530 0.1775  -0.1637 72  GLU E CA  
8113  C C   . GLU E  72  ? 1.3756 1.3741 1.1962 -0.1506 0.1687  -0.1612 72  GLU E C   
8114  O O   . GLU E  72  ? 1.2703 1.2665 1.0936 -0.1529 0.1707  -0.1640 72  GLU E O   
8115  C CB  . GLU E  72  ? 1.2779 1.2542 1.1120 -0.1491 0.1837  -0.1617 72  GLU E CB  
8116  C CG  . GLU E  72  ? 1.5049 1.4716 1.3397 -0.1516 0.1935  -0.1645 72  GLU E CG  
8117  C CD  . GLU E  72  ? 1.7435 1.7070 1.5701 -0.1612 0.2027  -0.1732 72  GLU E CD  
8118  O OE1 . GLU E  72  ? 1.6646 1.6296 1.4894 -0.1651 0.2033  -0.1769 72  GLU E OE1 
8119  O OE2 . GLU E  72  ? 1.6821 1.6413 1.5041 -0.1649 0.2095  -0.1765 72  GLU E OE2 
8120  N N   . CYS E  73  ? 1.4572 1.4654 1.2757 -0.1458 0.1591  -0.1560 73  CYS E N   
8121  C CA  . CYS E  73  ? 1.4891 1.5061 1.3075 -0.1434 0.1504  -0.1534 73  CYS E CA  
8122  C C   . CYS E  73  ? 1.6458 1.6753 1.4506 -0.1490 0.1467  -0.1569 73  CYS E C   
8123  O O   . CYS E  73  ? 1.7325 1.7726 1.5347 -0.1460 0.1378  -0.1532 73  CYS E O   
8124  C CB  . CYS E  73  ? 1.2970 1.3166 1.1225 -0.1343 0.1422  -0.1452 73  CYS E CB  
8125  S SG  . CYS E  73  ? 1.2686 1.2746 1.1105 -0.1275 0.1456  -0.1405 73  CYS E SG  
8126  N N   . GLU E  74  ? 1.7783 1.8068 1.5749 -0.1572 0.1536  -0.1639 74  GLU E N   
8127  C CA  . GLU E  74  ? 2.0112 2.0512 1.7940 -0.1635 0.1512  -0.1677 74  GLU E CA  
8128  C C   . GLU E  74  ? 2.0857 2.1348 1.8659 -0.1652 0.1454  -0.1687 74  GLU E C   
8129  O O   . GLU E  74  ? 2.0680 2.1286 1.8446 -0.1627 0.1367  -0.1651 74  GLU E O   
8130  C CB  . GLU E  74  ? 2.0529 2.0880 1.8283 -0.1724 0.1610  -0.1755 74  GLU E CB  
8131  C CG  . GLU E  74  ? 2.1817 2.2262 1.9434 -0.1775 0.1598  -0.1778 74  GLU E CG  
8132  C CD  . GLU E  74  ? 2.2505 2.2868 2.0094 -0.1807 0.1684  -0.1808 74  GLU E CD  
8133  O OE1 . GLU E  74  ? 2.1714 2.1949 1.9400 -0.1780 0.1747  -0.1803 74  GLU E OE1 
8134  O OE2 . GLU E  74  ? 2.1882 2.2307 1.9353 -0.1860 0.1690  -0.1836 74  GLU E OE2 
8135  N N   . SER E  75  ? 2.1470 2.1907 1.9295 -0.1694 0.1507  -0.1735 75  SER E N   
8136  C CA  . SER E  75  ? 2.3150 2.3663 2.0942 -0.1726 0.1471  -0.1759 75  SER E CA  
8137  C C   . SER E  75  ? 2.3827 2.4412 2.1659 -0.1675 0.1379  -0.1712 75  SER E C   
8138  O O   . SER E  75  ? 2.4035 2.4677 2.1834 -0.1713 0.1363  -0.1743 75  SER E O   
8139  C CB  . SER E  75  ? 2.3691 2.4126 2.1481 -0.1798 0.1563  -0.1834 75  SER E CB  
8140  O OG  . SER E  75  ? 2.1745 2.2040 1.9649 -0.1763 0.1625  -0.1821 75  SER E OG  
8141  N N   . LEU E  76  ? 2.5666 2.6254 2.3566 -0.1590 0.1319  -0.1639 76  LEU E N   
8142  C CA  . LEU E  76  ? 2.5708 2.6354 2.3655 -0.1538 0.1237  -0.1592 76  LEU E CA  
8143  C C   . LEU E  76  ? 2.5562 2.6345 2.3466 -0.1508 0.1135  -0.1551 76  LEU E C   
8144  O O   . LEU E  76  ? 2.5467 2.6336 2.3321 -0.1543 0.1103  -0.1574 76  LEU E O   
8145  C CB  . LEU E  76  ? 2.4491 2.5035 2.2548 -0.1464 0.1247  -0.1539 76  LEU E CB  
8146  C CG  . LEU E  76  ? 2.3152 2.3608 2.1318 -0.1439 0.1269  -0.1531 76  LEU E CG  
8147  C CD1 . LEU E  76  ? 2.3728 2.4191 2.1859 -0.1506 0.1303  -0.1592 76  LEU E CD1 
8148  C CD2 . LEU E  76  ? 1.9186 1.9505 1.7441 -0.1415 0.1339  -0.1521 76  LEU E CD2 
8149  N N   . SER E  77  ? 2.1073 2.1877 1.9003 -0.1442 0.1083  -0.1488 77  SER E N   
8150  C CA  . SER E  77  ? 1.9466 2.0394 1.7367 -0.1407 0.0989  -0.1443 77  SER E CA  
8151  C C   . SER E  77  ? 2.2047 2.3095 1.9825 -0.1472 0.0972  -0.1479 77  SER E C   
8152  O O   . SER E  77  ? 2.2788 2.3860 2.0497 -0.1498 0.0991  -0.1490 77  SER E O   
8153  C CB  . SER E  77  ? 1.8167 1.9096 1.6107 -0.1332 0.0946  -0.1375 77  SER E CB  
8154  O OG  . SER E  77  ? 1.6085 1.7130 1.4002 -0.1297 0.0858  -0.1331 77  SER E OG  
8155  N N   . THR E  78  ? 2.8769 2.9893 2.6527 -0.1493 0.0935  -0.1493 78  THR E N   
8156  C CA  . THR E  78  ? 2.9061 3.0303 2.6717 -0.1559 0.0916  -0.1532 78  THR E CA  
8157  C C   . THR E  78  ? 2.8061 2.9374 2.5758 -0.1512 0.0836  -0.1490 78  THR E C   
8158  O O   . THR E  78  ? 2.7598 2.9027 2.5240 -0.1539 0.0790  -0.1498 78  THR E O   
8159  C CB  . THR E  78  ? 2.7317 2.8509 2.4946 -0.1639 0.0991  -0.1611 78  THR E CB  
8160  O OG1 . THR E  78  ? 2.7470 2.8624 2.5035 -0.1696 0.1061  -0.1656 78  THR E OG1 
8161  C CG2 . THR E  78  ? 2.5000 2.6298 2.2572 -0.1690 0.0959  -0.1643 78  THR E CG2 
8162  N N   . ALA E  79  ? 2.2236 2.3475 2.0033 -0.1439 0.0821  -0.1442 79  ALA E N   
8163  C CA  . ALA E  79  ? 1.9056 2.0326 1.6912 -0.1388 0.0757  -0.1402 79  ALA E CA  
8164  C C   . ALA E  79  ? 1.6943 1.8321 1.4785 -0.1338 0.0674  -0.1343 79  ALA E C   
8165  O O   . ALA E  79  ? 1.6790 1.8173 1.4624 -0.1306 0.0663  -0.1308 79  ALA E O   
8166  C CB  . ALA E  79  ? 1.8018 1.9164 1.5986 -0.1332 0.0777  -0.1374 79  ALA E CB  
8167  N N   . SER E  80  ? 1.2903 1.4365 1.0743 -0.1332 0.0618  -0.1332 80  SER E N   
8168  C CA  . SER E  80  ? 1.1551 1.3118 0.9385 -0.1284 0.0538  -0.1276 80  SER E CA  
8169  C C   . SER E  80  ? 0.9830 1.1348 0.7761 -0.1206 0.0501  -0.1223 80  SER E C   
8170  O O   . SER E  80  ? 0.9147 1.0709 0.7099 -0.1148 0.0447  -0.1166 80  SER E O   
8171  C CB  . SER E  80  ? 1.3540 1.5235 1.1312 -0.1328 0.0501  -0.1297 80  SER E CB  
8172  O OG  . SER E  80  ? 1.6120 1.7849 1.3805 -0.1410 0.0543  -0.1356 80  SER E OG  
8173  N N   . SER E  81  ? 0.9630 1.1055 0.7621 -0.1206 0.0533  -0.1241 81  SER E N   
8174  C CA  . SER E  81  ? 0.9215 1.0591 0.7296 -0.1139 0.0501  -0.1195 81  SER E CA  
8175  C C   . SER E  81  ? 0.8177 0.9433 0.6321 -0.1147 0.0554  -0.1219 81  SER E C   
8176  O O   . SER E  81  ? 0.7566 0.8790 0.5682 -0.1208 0.0610  -0.1276 81  SER E O   
8177  C CB  . SER E  81  ? 0.9050 1.0525 0.7127 -0.1123 0.0434  -0.1174 81  SER E CB  
8178  O OG  . SER E  81  ? 0.8636 1.0148 0.6675 -0.1184 0.0449  -0.1226 81  SER E OG  
8179  N N   . TRP E  82  ? 0.5992 0.7182 0.4222 -0.1085 0.0535  -0.1175 82  TRP E N   
8180  C CA  . TRP E  82  ? 0.7191 0.8272 0.5489 -0.1085 0.0576  -0.1188 82  TRP E CA  
8181  C C   . TRP E  82  ? 0.6828 0.7880 0.5207 -0.1017 0.0530  -0.1134 82  TRP E C   
8182  O O   . TRP E  82  ? 0.7149 0.8222 0.5550 -0.0963 0.0485  -0.1083 82  TRP E O   
8183  C CB  . TRP E  82  ? 0.6831 0.7805 0.5154 -0.1097 0.0649  -0.1205 82  TRP E CB  
8184  C CG  . TRP E  82  ? 0.6621 0.7570 0.4971 -0.1047 0.0637  -0.1160 82  TRP E CG  
8185  C CD1 . TRP E  82  ? 0.6112 0.6998 0.4546 -0.0982 0.0619  -0.1109 82  TRP E CD1 
8186  C CD2 . TRP E  82  ? 0.7141 0.8127 0.5432 -0.1059 0.0645  -0.1163 82  TRP E CD2 
8187  N NE1 . TRP E  82  ? 0.6311 0.7192 0.4745 -0.0953 0.0615  -0.1080 82  TRP E NE1 
8188  C CE2 . TRP E  82  ? 0.6662 0.7603 0.5008 -0.0998 0.0631  -0.1112 82  TRP E CE2 
8189  C CE3 . TRP E  82  ? 0.6786 0.7841 0.4981 -0.1117 0.0661  -0.1203 82  TRP E CE3 
8190  C CZ2 . TRP E  82  ? 0.6793 0.7753 0.5104 -0.0992 0.0635  -0.1100 82  TRP E CZ2 
8191  C CZ3 . TRP E  82  ? 0.7550 0.8626 0.5707 -0.1111 0.0664  -0.1190 82  TRP E CZ3 
8192  C CH2 . TRP E  82  ? 0.6052 0.7079 0.4267 -0.1048 0.0652  -0.1138 82  TRP E CH2 
8193  N N   . SER E  83  ? 0.6254 0.7259 0.4675 -0.1024 0.0543  -0.1145 83  SER E N   
8194  C CA  . SER E  83  ? 0.6829 0.7806 0.5322 -0.0967 0.0501  -0.1099 83  SER E CA  
8195  C C   . SER E  83  ? 0.6251 0.7121 0.4825 -0.0924 0.0523  -0.1065 83  SER E C   
8196  O O   . SER E  83  ? 0.7025 0.7884 0.5649 -0.0866 0.0478  -0.1013 83  SER E O   
8197  C CB  . SER E  83  ? 0.6160 0.7128 0.4665 -0.0992 0.0507  -0.1123 83  SER E CB  
8198  O OG  . SER E  83  ? 0.6559 0.7454 0.5070 -0.1040 0.0581  -0.1170 83  SER E OG  
8199  N N   . TYR E  84  ? 0.5778 0.6567 0.4365 -0.0953 0.0593  -0.1094 84  TYR E N   
8200  C CA  . TYR E  84  ? 0.5533 0.6222 0.4198 -0.0916 0.0620  -0.1064 84  TYR E CA  
8201  C C   . TYR E  84  ? 0.6381 0.7012 0.5032 -0.0957 0.0697  -0.1103 84  TYR E C   
8202  O O   . TYR E  84  ? 0.7374 0.8039 0.5955 -0.1016 0.0730  -0.1156 84  TYR E O   
8203  C CB  . TYR E  84  ? 0.6219 0.6834 0.4967 -0.0894 0.0624  -0.1045 84  TYR E CB  
8204  C CG  . TYR E  84  ? 0.6742 0.7315 0.5489 -0.0946 0.0681  -0.1094 84  TYR E CG  
8205  C CD1 . TYR E  84  ? 0.5393 0.5864 0.4188 -0.0963 0.0754  -0.1111 84  TYR E CD1 
8206  C CD2 . TYR E  84  ? 0.6662 0.7296 0.5363 -0.0979 0.0663  -0.1123 84  TYR E CD2 
8207  C CE1 . TYR E  84  ? 0.5383 0.5813 0.4181 -0.1011 0.0810  -0.1155 84  TYR E CE1 
8208  C CE2 . TYR E  84  ? 0.5249 0.5844 0.3950 -0.1028 0.0716  -0.1168 84  TYR E CE2 
8209  C CZ  . TYR E  84  ? 0.5295 0.5787 0.4044 -0.1043 0.0790  -0.1185 84  TYR E CZ  
8210  O OH  . TYR E  84  ? 0.5739 0.6188 0.4490 -0.1092 0.0848  -0.1230 84  TYR E OH  
8211  N N   . ILE E  85  ? 0.5431 0.5976 0.4149 -0.0926 0.0726  -0.1078 85  ILE E N   
8212  C CA  . ILE E  85  ? 0.6934 0.7418 0.5646 -0.0960 0.0801  -0.1110 85  ILE E CA  
8213  C C   . ILE E  85  ? 0.7072 0.7441 0.5864 -0.0966 0.0866  -0.1119 85  ILE E C   
8214  O O   . ILE E  85  ? 0.6669 0.6986 0.5547 -0.0920 0.0849  -0.1075 85  ILE E O   
8215  C CB  . ILE E  85  ? 0.6168 0.6646 0.4887 -0.0924 0.0793  -0.1078 85  ILE E CB  
8216  C CG1 . ILE E  85  ? 0.5932 0.6524 0.4567 -0.0923 0.0738  -0.1072 85  ILE E CG1 
8217  C CG2 . ILE E  85  ? 0.6596 0.6999 0.5317 -0.0957 0.0876  -0.1110 85  ILE E CG2 
8218  C CD1 . ILE E  85  ? 0.6707 0.7299 0.5346 -0.0886 0.0725  -0.1037 85  ILE E CD1 
8219  N N   . VAL E  86  ? 0.6500 0.6831 0.5263 -0.1025 0.0940  -0.1176 86  VAL E N   
8220  C CA  . VAL E  86  ? 0.6693 0.6913 0.5532 -0.1036 0.1011  -0.1188 86  VAL E CA  
8221  C C   . VAL E  86  ? 0.6716 0.6863 0.5573 -0.1047 0.1082  -0.1201 86  VAL E C   
8222  O O   . VAL E  86  ? 0.7975 0.8148 0.6755 -0.1092 0.1114  -0.1244 86  VAL E O   
8223  C CB  . VAL E  86  ? 0.6892 0.7109 0.5698 -0.1097 0.1054  -0.1245 86  VAL E CB  
8224  C CG1 . VAL E  86  ? 0.5610 0.5709 0.4503 -0.1104 0.1129  -0.1252 86  VAL E CG1 
8225  C CG2 . VAL E  86  ? 0.7140 0.7430 0.5927 -0.1088 0.0987  -0.1234 86  VAL E CG2 
8226  N N   . GLU E  87  ? 0.6873 0.6930 0.5834 -0.1006 0.1105  -0.1163 87  GLU E N   
8227  C CA  . GLU E  87  ? 0.7487 0.7463 0.6483 -0.1012 0.1176  -0.1170 87  GLU E CA  
8228  C C   . GLU E  87  ? 0.8566 0.8436 0.7648 -0.1024 0.1250  -0.1181 87  GLU E C   
8229  O O   . GLU E  87  ? 0.9162 0.9007 0.8318 -0.0992 0.1227  -0.1146 87  GLU E O   
8230  C CB  . GLU E  87  ? 0.8063 0.8028 0.7116 -0.0947 0.1138  -0.1109 87  GLU E CB  
8231  C CG  . GLU E  87  ? 0.8903 0.8877 0.7907 -0.0956 0.1159  -0.1120 87  GLU E CG  
8232  C CD  . GLU E  87  ? 0.9535 0.9506 0.8594 -0.0890 0.1115  -0.1058 87  GLU E CD  
8233  O OE1 . GLU E  87  ? 0.9991 1.0014 0.8990 -0.0885 0.1090  -0.1054 87  GLU E OE1 
8234  O OE2 . GLU E  87  ? 0.9151 0.9069 0.8313 -0.0844 0.1104  -0.1012 87  GLU E OE2 
8235  N N   . THR E  88  ? 1.0648 1.0456 0.9720 -0.1071 0.1339  -0.1229 88  THR E N   
8236  C CA  . THR E  88  ? 1.1066 1.0767 1.0225 -0.1082 0.1418  -0.1238 88  THR E CA  
8237  C C   . THR E  88  ? 1.0855 1.0476 1.0124 -0.1031 0.1439  -0.1187 88  THR E C   
8238  O O   . THR E  88  ? 1.2420 1.2047 1.1675 -0.1016 0.1437  -0.1176 88  THR E O   
8239  C CB  . THR E  88  ? 1.1299 1.0963 1.0403 -0.1158 0.1512  -0.1315 88  THR E CB  
8240  O OG1 . THR E  88  ? 1.2317 1.1960 1.1391 -0.1171 0.1553  -0.1331 88  THR E OG1 
8241  C CG2 . THR E  88  ? 1.0161 0.9913 0.9149 -0.1213 0.1488  -0.1367 88  THR E CG2 
8242  N N   . PRO E  89  ? 1.3833 1.3382 1.3213 -0.1003 0.1460  -0.1154 89  PRO E N   
8243  C CA  . PRO E  89  ? 1.3821 1.3293 1.3317 -0.0954 0.1480  -0.1102 89  PRO E CA  
8244  C C   . PRO E  89  ? 1.4887 1.4292 1.4389 -0.0981 0.1570  -0.1134 89  PRO E C   
8245  O O   . PRO E  89  ? 1.4604 1.3956 1.4188 -0.0943 0.1586  -0.1095 89  PRO E O   
8246  C CB  . PRO E  89  ? 1.2111 1.1518 1.1709 -0.0941 0.1504  -0.1078 89  PRO E CB  
8247  C CG  . PRO E  89  ? 1.3000 1.2473 1.2538 -0.0960 0.1457  -0.1096 89  PRO E CG  
8248  C CD  . PRO E  89  ? 1.4068 1.3604 1.3472 -0.1018 0.1465  -0.1162 89  PRO E CD  
8249  N N   . SER E  90  ? 1.4958 1.4365 1.4372 -0.1049 0.1628  -0.1206 90  SER E N   
8250  C CA  . SER E  90  ? 1.4807 1.4145 1.4217 -0.1085 0.1722  -0.1246 90  SER E CA  
8251  C C   . SER E  90  ? 1.6820 1.6223 1.6111 -0.1112 0.1708  -0.1278 90  SER E C   
8252  O O   . SER E  90  ? 1.8846 1.8215 1.8088 -0.1163 0.1784  -0.1333 90  SER E O   
8253  C CB  . SER E  90  ? 1.6321 1.5596 1.5727 -0.1147 0.1816  -0.1307 90  SER E CB  
8254  O OG  . SER E  90  ? 1.9416 1.8613 1.8830 -0.1180 0.1915  -0.1344 90  SER E OG  
8255  N N   . SER E  91  ? 1.6520 1.6017 1.5765 -0.1078 0.1611  -0.1245 91  SER E N   
8256  C CA  . SER E  91  ? 1.4831 1.4399 1.3966 -0.1097 0.1588  -0.1266 91  SER E CA  
8257  C C   . SER E  91  ? 1.5791 1.5337 1.4973 -0.1048 0.1578  -0.1220 91  SER E C   
8258  O O   . SER E  91  ? 1.5607 1.5170 1.4850 -0.0984 0.1511  -0.1157 91  SER E O   
8259  C CB  . SER E  91  ? 1.3090 1.2780 1.2141 -0.1092 0.1491  -0.1259 91  SER E CB  
8260  O OG  . SER E  91  ? 1.3510 1.3223 1.2629 -0.1022 0.1411  -0.1190 91  SER E OG  
8261  N N   . ASP E  92  ? 1.7461 1.6966 1.6611 -0.1079 0.1647  -0.1253 92  ASP E N   
8262  C CA  . ASP E  92  ? 1.7897 1.7372 1.7095 -0.1036 0.1649  -0.1214 92  ASP E CA  
8263  C C   . ASP E  92  ? 1.6696 1.6217 1.5783 -0.1066 0.1654  -0.1243 92  ASP E C   
8264  O O   . ASP E  92  ? 1.7611 1.7112 1.6725 -0.1034 0.1657  -0.1215 92  ASP E O   
8265  C CB  . ASP E  92  ? 2.0646 1.9997 1.9959 -0.1030 0.1739  -0.1209 92  ASP E CB  
8266  C CG  . ASP E  92  ? 2.0519 1.9822 1.9953 -0.0995 0.1734  -0.1171 92  ASP E CG  
8267  O OD1 . ASP E  92  ? 2.0349 1.9712 1.9790 -0.0963 0.1650  -0.1135 92  ASP E OD1 
8268  O OD2 . ASP E  92  ? 2.0558 1.9761 2.0081 -0.1001 0.1815  -0.1175 92  ASP E OD2 
8269  N N   . ASN E  93  ? 1.4747 1.4330 1.3711 -0.1127 0.1657  -0.1300 93  ASN E N   
8270  C CA  . ASN E  93  ? 1.4996 1.4635 1.3847 -0.1156 0.1654  -0.1325 93  ASN E CA  
8271  C C   . ASN E  93  ? 1.3577 1.3321 1.2389 -0.1110 0.1548  -0.1276 93  ASN E C   
8272  O O   . ASN E  93  ? 1.2500 1.2342 1.1223 -0.1131 0.1493  -0.1290 93  ASN E O   
8273  C CB  . ASN E  93  ? 1.4625 1.4296 1.3356 -0.1242 0.1697  -0.1403 93  ASN E CB  
8274  C CG  . ASN E  93  ? 1.5870 1.5434 1.4623 -0.1294 0.1816  -0.1457 93  ASN E CG  
8275  O OD1 . ASN E  93  ? 1.5970 1.5504 1.4725 -0.1336 0.1858  -0.1498 93  ASN E OD1 
8276  N ND2 . ASN E  93  ? 1.5986 1.5488 1.4751 -0.1294 0.1873  -0.1460 93  ASN E ND2 
8277  N N   . GLY E  94  ? 1.3791 1.3513 1.2676 -0.1047 0.1521  -0.1218 94  GLY E N   
8278  C CA  . GLY E  94  ? 1.2433 1.2242 1.1294 -0.0998 0.1428  -0.1169 94  GLY E CA  
8279  C C   . GLY E  94  ? 1.2237 1.2054 1.1053 -0.0994 0.1440  -0.1163 94  GLY E C   
8280  O O   . GLY E  94  ? 1.1349 1.1199 1.0056 -0.1048 0.1468  -0.1208 94  GLY E O   
8281  N N   . THR E  95  ? 1.0387 1.0173 0.9284 -0.0932 0.1419  -0.1107 95  THR E N   
8282  C CA  . THR E  95  ? 1.0667 1.0453 0.9533 -0.0923 0.1432  -0.1097 95  THR E CA  
8283  C C   . THR E  95  ? 1.0582 1.0262 0.9479 -0.0953 0.1537  -0.1129 95  THR E C   
8284  O O   . THR E  95  ? 1.0979 1.0575 0.9993 -0.0916 0.1568  -0.1099 95  THR E O   
8285  C CB  . THR E  95  ? 0.8122 0.7917 0.7061 -0.0846 0.1369  -0.1024 95  THR E CB  
8286  O OG1 . THR E  95  ? 0.8274 0.8006 0.7344 -0.0804 0.1366  -0.0989 95  THR E OG1 
8287  N N   . CYS E  96  ? 1.0118 0.9805 0.8912 -0.1021 0.1592  -0.1190 96  CYS E N   
8288  C CA  . CYS E  96  ? 1.0681 1.0269 0.9490 -0.1058 0.1698  -0.1229 96  CYS E CA  
8289  C C   . CYS E  96  ? 1.0722 1.0269 0.9572 -0.1020 0.1716  -0.1195 96  CYS E C   
8290  O O   . CYS E  96  ? 1.0595 1.0040 0.9522 -0.1019 0.1793  -0.1199 96  CYS E O   
8291  C CB  . CYS E  96  ? 1.0101 0.9716 0.8776 -0.1143 0.1748  -0.1303 96  CYS E CB  
8292  S SG  . CYS E  96  ? 1.2655 1.2417 1.1172 -0.1163 0.1668  -0.1306 96  CYS E SG  
8293  N N   . TYR E  97  ? 0.9486 0.9110 0.8285 -0.0989 0.1647  -0.1159 97  TYR E N   
8294  C CA  . TYR E  97  ? 0.9319 0.8910 0.8164 -0.0946 0.1653  -0.1119 97  TYR E CA  
8295  C C   . TYR E  97  ? 0.9407 0.8991 0.8376 -0.0867 0.1591  -0.1049 97  TYR E C   
8296  O O   . TYR E  97  ? 0.9818 0.9481 0.8773 -0.0837 0.1504  -0.1018 97  TYR E O   
8297  C CB  . TYR E  97  ? 0.9648 0.9321 0.8375 -0.0954 0.1619  -0.1118 97  TYR E CB  
8298  C CG  . TYR E  97  ? 0.9533 0.9157 0.8286 -0.0931 0.1655  -0.1097 97  TYR E CG  
8299  C CD1 . TYR E  97  ? 1.0276 0.9867 0.8955 -0.0984 0.1732  -0.1143 97  TYR E CD1 
8300  C CD2 . TYR E  97  ? 0.9693 0.9303 0.8544 -0.0858 0.1613  -0.1032 97  TYR E CD2 
8301  C CE1 . TYR E  97  ? 1.0490 1.0033 0.9191 -0.0964 0.1767  -0.1124 97  TYR E CE1 
8302  C CE2 . TYR E  97  ? 0.9700 0.9263 0.8576 -0.0837 0.1647  -0.1012 97  TYR E CE2 
8303  C CZ  . TYR E  97  ? 1.0116 0.9646 0.8918 -0.0889 0.1724  -0.1058 97  TYR E CZ  
8304  O OH  . TYR E  97  ? 0.9279 0.8762 0.8106 -0.0869 0.1760  -0.1040 97  TYR E OH  
8305  N N   . PRO E  98  ? 0.9164 0.8654 0.8254 -0.0834 0.1636  -0.1024 98  PRO E N   
8306  C CA  . PRO E  98  ? 0.8057 0.7531 0.7273 -0.0763 0.1584  -0.0959 98  PRO E CA  
8307  C C   . PRO E  98  ? 0.9276 0.8832 0.8464 -0.0715 0.1493  -0.0910 98  PRO E C   
8308  O O   . PRO E  98  ? 0.8869 0.8460 0.7980 -0.0722 0.1493  -0.0914 98  PRO E O   
8309  C CB  . PRO E  98  ? 0.7898 0.7266 0.7219 -0.0745 0.1657  -0.0946 98  PRO E CB  
8310  C CG  . PRO E  98  ? 0.9945 0.9256 0.9218 -0.0812 0.1757  -0.1011 98  PRO E CG  
8311  C CD  . PRO E  98  ? 0.9990 0.9384 0.9102 -0.0864 0.1739  -0.1056 98  PRO E CD  
8312  N N   . GLY E  99  ? 0.9696 0.9282 0.8949 -0.0667 0.1420  -0.0864 99  GLY E N   
8313  C CA  . GLY E  99  ? 0.8813 0.8472 0.8053 -0.0618 0.1333  -0.0816 99  GLY E CA  
8314  C C   . GLY E  99  ? 0.8747 0.8449 0.8025 -0.0590 0.1260  -0.0788 99  GLY E C   
8315  O O   . GLY E  99  ? 0.8768 0.8444 0.8073 -0.0611 0.1278  -0.0808 99  GLY E O   
8316  N N   . ASP E  100 ? 0.8484 0.8247 0.7765 -0.0543 0.1180  -0.0742 100 ASP E N   
8317  C CA  . ASP E  100 ? 0.8310 0.8117 0.7618 -0.0519 0.1109  -0.0717 100 ASP E CA  
8318  C C   . ASP E  100 ? 0.7880 0.7795 0.7082 -0.0524 0.1040  -0.0720 100 ASP E C   
8319  O O   . ASP E  100 ? 0.7694 0.7660 0.6833 -0.0516 0.1018  -0.0710 100 ASP E O   
8320  C CB  . ASP E  100 ? 0.8536 0.8309 0.7970 -0.0458 0.1073  -0.0658 100 ASP E CB  
8321  C CG  . ASP E  100 ? 1.1322 1.1142 1.0749 -0.0411 0.1012  -0.0614 100 ASP E CG  
8322  O OD1 . ASP E  100 ? 1.2318 1.2114 1.1748 -0.0401 0.1041  -0.0606 100 ASP E OD1 
8323  O OD2 . ASP E  100 ? 1.1845 1.1724 1.1269 -0.0383 0.0938  -0.0586 100 ASP E OD2 
8324  N N   . PHE E  101 ? 0.6617 0.6567 0.5807 -0.0537 0.1009  -0.0731 101 PHE E N   
8325  C CA  . PHE E  101 ? 0.7074 0.7125 0.6169 -0.0549 0.0950  -0.0740 101 PHE E CA  
8326  C C   . PHE E  101 ? 0.6768 0.6861 0.5906 -0.0492 0.0867  -0.0686 101 PHE E C   
8327  O O   . PHE E  101 ? 0.7800 0.7876 0.7001 -0.0474 0.0842  -0.0670 101 PHE E O   
8328  C CB  . PHE E  101 ? 0.5986 0.6042 0.5051 -0.0595 0.0966  -0.0783 101 PHE E CB  
8329  C CG  . PHE E  101 ? 0.6489 0.6642 0.5433 -0.0633 0.0938  -0.0814 101 PHE E CG  
8330  C CD1 . PHE E  101 ? 0.6439 0.6593 0.5306 -0.0698 0.0993  -0.0873 101 PHE E CD1 
8331  C CD2 . PHE E  101 ? 0.6971 0.7213 0.5880 -0.0605 0.0859  -0.0785 101 PHE E CD2 
8332  C CE1 . PHE E  101 ? 0.6161 0.6408 0.4918 -0.0735 0.0966  -0.0901 101 PHE E CE1 
8333  C CE2 . PHE E  101 ? 0.5791 0.6125 0.4594 -0.0639 0.0833  -0.0811 101 PHE E CE2 
8334  C CZ  . PHE E  101 ? 0.5584 0.5923 0.4311 -0.0705 0.0885  -0.0868 101 PHE E CZ  
8335  N N   . ILE E  102 ? 0.5032 0.5178 0.4134 -0.0464 0.0828  -0.0658 102 ILE E N   
8336  C CA  . ILE E  102 ? 0.5310 0.5490 0.4454 -0.0409 0.0755  -0.0607 102 ILE E CA  
8337  C C   . ILE E  102 ? 0.5786 0.6034 0.4898 -0.0413 0.0698  -0.0609 102 ILE E C   
8338  O O   . ILE E  102 ? 0.5416 0.5730 0.4435 -0.0448 0.0691  -0.0639 102 ILE E O   
8339  C CB  . ILE E  102 ? 0.7217 0.7444 0.6322 -0.0382 0.0728  -0.0579 102 ILE E CB  
8340  C CG1 . ILE E  102 ? 0.7662 0.7827 0.6783 -0.0386 0.0791  -0.0584 102 ILE E CG1 
8341  C CG2 . ILE E  102 ? 0.5679 0.5925 0.4842 -0.0323 0.0662  -0.0526 102 ILE E CG2 
8342  C CD1 . ILE E  102 ? 0.7003 0.7074 0.6246 -0.0358 0.0818  -0.0561 102 ILE E CD1 
8343  N N   . ASP E  103 ? 0.6287 0.6518 0.5476 -0.0378 0.0658  -0.0577 103 ASP E N   
8344  C CA  . ASP E  103 ? 0.5299 0.5586 0.4466 -0.0378 0.0605  -0.0576 103 ASP E CA  
8345  C C   . ASP E  103 ? 0.5775 0.6072 0.4887 -0.0434 0.0636  -0.0628 103 ASP E C   
8346  O O   . ASP E  103 ? 0.6927 0.7301 0.5965 -0.0453 0.0604  -0.0645 103 ASP E O   
8347  C CB  . ASP E  103 ? 0.6383 0.6763 0.5487 -0.0357 0.0544  -0.0556 103 ASP E CB  
8348  C CG  . ASP E  103 ? 0.7347 0.7718 0.6507 -0.0302 0.0510  -0.0505 103 ASP E CG  
8349  O OD1 . ASP E  103 ? 0.7564 0.7873 0.6816 -0.0274 0.0509  -0.0479 103 ASP E OD1 
8350  O OD2 . ASP E  103 ? 0.7278 0.7706 0.6389 -0.0286 0.0486  -0.0489 103 ASP E OD2 
8351  N N   . TYR E  104 ? 0.6017 0.6237 0.5170 -0.0460 0.0700  -0.0653 104 TYR E N   
8352  C CA  . TYR E  104 ? 0.6036 0.6253 0.5143 -0.0516 0.0741  -0.0706 104 TYR E CA  
8353  C C   . TYR E  104 ? 0.6506 0.6747 0.5624 -0.0518 0.0703  -0.0706 104 TYR E C   
8354  O O   . TYR E  104 ? 0.5185 0.5486 0.4227 -0.0553 0.0691  -0.0738 104 TYR E O   
8355  C CB  . TYR E  104 ? 0.6285 0.6403 0.5445 -0.0539 0.0823  -0.0728 104 TYR E CB  
8356  C CG  . TYR E  104 ? 0.6175 0.6278 0.5294 -0.0598 0.0874  -0.0784 104 TYR E CG  
8357  C CD1 . TYR E  104 ? 0.5430 0.5598 0.4437 -0.0647 0.0881  -0.0829 104 TYR E CD1 
8358  C CD2 . TYR E  104 ? 0.5421 0.5446 0.4617 -0.0607 0.0916  -0.0792 104 TYR E CD2 
8359  C CE1 . TYR E  104 ? 0.6123 0.6277 0.5092 -0.0704 0.0929  -0.0882 104 TYR E CE1 
8360  C CE2 . TYR E  104 ? 0.6930 0.6939 0.6092 -0.0662 0.0967  -0.0845 104 TYR E CE2 
8361  C CZ  . TYR E  104 ? 0.5995 0.6067 0.5041 -0.0712 0.0974  -0.0891 104 TYR E CZ  
8362  O OH  . TYR E  104 ? 0.7444 0.7499 0.6455 -0.0769 0.1025  -0.0946 104 TYR E OH  
8363  N N   . GLU E  105 ? 0.6166 0.6361 0.5378 -0.0482 0.0683  -0.0670 105 GLU E N   
8364  C CA  . GLU E  105 ? 0.6459 0.6669 0.5689 -0.0480 0.0647  -0.0666 105 GLU E CA  
8365  C C   . GLU E  105 ? 0.6751 0.7059 0.5910 -0.0473 0.0579  -0.0660 105 GLU E C   
8366  O O   . GLU E  105 ? 0.6319 0.6664 0.5443 -0.0495 0.0562  -0.0681 105 GLU E O   
8367  C CB  . GLU E  105 ? 0.5598 0.5750 0.4939 -0.0437 0.0629  -0.0620 105 GLU E CB  
8368  C CG  . GLU E  105 ? 0.6246 0.6301 0.5671 -0.0440 0.0694  -0.0620 105 GLU E CG  
8369  C CD  . GLU E  105 ? 0.8999 0.9027 0.8437 -0.0426 0.0724  -0.0610 105 GLU E CD  
8370  O OE1 . GLU E  105 ? 0.9235 0.9305 0.8657 -0.0394 0.0679  -0.0581 105 GLU E OE1 
8371  O OE2 . GLU E  105 ? 0.8135 0.8098 0.7600 -0.0448 0.0794  -0.0631 105 GLU E OE2 
8372  N N   . GLU E  106 ? 0.5802 0.6152 0.4945 -0.0440 0.0542  -0.0630 106 GLU E N   
8373  C CA  . GLU E  106 ? 0.4742 0.5187 0.3820 -0.0430 0.0481  -0.0621 106 GLU E CA  
8374  C C   . GLU E  106 ? 0.5299 0.5809 0.4275 -0.0480 0.0496  -0.0667 106 GLU E C   
8375  O O   . GLU E  106 ? 0.4870 0.5443 0.3804 -0.0494 0.0462  -0.0679 106 GLU E O   
8376  C CB  . GLU E  106 ? 0.4742 0.5213 0.3826 -0.0386 0.0447  -0.0581 106 GLU E CB  
8377  C CG  . GLU E  106 ? 0.7043 0.7491 0.6206 -0.0334 0.0402  -0.0532 106 GLU E CG  
8378  C CD  . GLU E  106 ? 0.6481 0.6985 0.5627 -0.0324 0.0344  -0.0522 106 GLU E CD  
8379  O OE1 . GLU E  106 ? 0.7371 0.7955 0.6441 -0.0338 0.0320  -0.0536 106 GLU E OE1 
8380  O OE2 . GLU E  106 ? 0.6052 0.6522 0.5262 -0.0304 0.0321  -0.0500 106 GLU E OE2 
8381  N N   . LEU E  107 ? 0.6292 0.6788 0.5229 -0.0509 0.0547  -0.0694 107 LEU E N   
8382  C CA  . LEU E  107 ? 0.6446 0.7004 0.5283 -0.0562 0.0564  -0.0739 107 LEU E CA  
8383  C C   . LEU E  107 ? 0.6070 0.6626 0.4892 -0.0605 0.0580  -0.0779 107 LEU E C   
8384  O O   . LEU E  107 ? 0.6380 0.7015 0.5133 -0.0632 0.0556  -0.0800 107 LEU E O   
8385  C CB  . LEU E  107 ? 0.5901 0.6422 0.4709 -0.0591 0.0628  -0.0765 107 LEU E CB  
8386  C CG  . LEU E  107 ? 0.5831 0.6417 0.4529 -0.0648 0.0648  -0.0811 107 LEU E CG  
8387  C CD1 . LEU E  107 ? 0.5380 0.6079 0.4011 -0.0635 0.0584  -0.0791 107 LEU E CD1 
8388  C CD2 . LEU E  107 ? 0.6527 0.7067 0.5200 -0.0677 0.0715  -0.0836 107 LEU E CD2 
8389  N N   . ARG E  108 ? 0.4666 0.5133 0.3558 -0.0610 0.0622  -0.0787 108 ARG E N   
8390  C CA  . ARG E  108 ? 0.5798 0.6249 0.4688 -0.0649 0.0646  -0.0824 108 ARG E CA  
8391  C C   . ARG E  108 ? 0.6391 0.6896 0.5281 -0.0632 0.0582  -0.0807 108 ARG E C   
8392  O O   . ARG E  108 ? 0.6467 0.7015 0.5307 -0.0670 0.0580  -0.0841 108 ARG E O   
8393  C CB  . ARG E  108 ? 0.5334 0.5675 0.4315 -0.0647 0.0700  -0.0824 108 ARG E CB  
8394  C CG  . ARG E  108 ? 0.6183 0.6457 0.5185 -0.0653 0.0762  -0.0831 108 ARG E CG  
8395  C CD  . ARG E  108 ? 0.6338 0.6508 0.5452 -0.0632 0.0799  -0.0812 108 ARG E CD  
8396  N NE  . ARG E  108 ? 0.5901 0.6039 0.5037 -0.0661 0.0824  -0.0837 108 ARG E NE  
8397  C CZ  . ARG E  108 ? 0.6957 0.7048 0.6080 -0.0711 0.0898  -0.0885 108 ARG E CZ  
8398  N NH1 . ARG E  108 ? 0.7167 0.7238 0.6252 -0.0739 0.0952  -0.0915 108 ARG E NH1 
8399  N NH2 . ARG E  108 ? 0.6229 0.6292 0.5376 -0.0734 0.0919  -0.0905 108 ARG E NH2 
8400  N N   . GLU E  109 ? 0.6162 0.6665 0.5109 -0.0577 0.0532  -0.0756 109 GLU E N   
8401  C CA  . GLU E  109 ? 0.5278 0.5829 0.4229 -0.0556 0.0470  -0.0736 109 GLU E CA  
8402  C C   . GLU E  109 ? 0.5844 0.6505 0.4706 -0.0570 0.0431  -0.0747 109 GLU E C   
8403  O O   . GLU E  109 ? 0.5970 0.6678 0.4803 -0.0585 0.0404  -0.0760 109 GLU E O   
8404  C CB  . GLU E  109 ? 0.5380 0.5908 0.4404 -0.0496 0.0426  -0.0679 109 GLU E CB  
8405  C CG  . GLU E  109 ? 0.7631 0.8201 0.6663 -0.0473 0.0364  -0.0657 109 GLU E CG  
8406  C CD  . GLU E  109 ? 0.9342 0.9872 0.8408 -0.0491 0.0377  -0.0671 109 GLU E CD  
8407  O OE1 . GLU E  109 ? 0.9518 0.9994 0.8597 -0.0525 0.0435  -0.0701 109 GLU E OE1 
8408  O OE2 . GLU E  109 ? 1.0134 1.0685 0.9214 -0.0472 0.0330  -0.0651 109 GLU E OE2 
8409  N N   . GLN E  110 ? 0.5719 0.6419 0.4537 -0.0564 0.0427  -0.0740 110 GLN E N   
8410  C CA  . GLN E  110 ? 0.5487 0.6296 0.4224 -0.0574 0.0390  -0.0744 110 GLN E CA  
8411  C C   . GLN E  110 ? 0.6469 0.7316 0.5129 -0.0640 0.0422  -0.0800 110 GLN E C   
8412  O O   . GLN E  110 ? 0.8236 0.9171 0.6840 -0.0657 0.0389  -0.0811 110 GLN E O   
8413  C CB  . GLN E  110 ? 0.7103 0.7938 0.5818 -0.0549 0.0380  -0.0718 110 GLN E CB  
8414  C CG  . GLN E  110 ? 0.7392 0.8171 0.6186 -0.0491 0.0365  -0.0669 110 GLN E CG  
8415  C CD  . GLN E  110 ? 0.7624 0.8469 0.6413 -0.0445 0.0304  -0.0625 110 GLN E CD  
8416  O OE1 . GLN E  110 ? 0.8770 0.9704 0.7500 -0.0454 0.0270  -0.0628 110 GLN E OE1 
8417  N NE2 . GLN E  110 ? 0.6303 0.7103 0.5155 -0.0397 0.0290  -0.0584 110 GLN E NE2 
8418  N N   . LEU E  111 ? 0.6219 0.7002 0.4879 -0.0677 0.0488  -0.0836 111 LEU E N   
8419  C CA  . LEU E  111 ? 0.6016 0.6825 0.4604 -0.0744 0.0527  -0.0894 111 LEU E CA  
8420  C C   . LEU E  111 ? 0.6282 0.7068 0.4890 -0.0771 0.0539  -0.0923 111 LEU E C   
8421  O O   . LEU E  111 ? 0.6556 0.7374 0.5104 -0.0827 0.0563  -0.0971 111 LEU E O   
8422  C CB  . LEU E  111 ? 0.6192 0.6938 0.4769 -0.0776 0.0600  -0.0924 111 LEU E CB  
8423  C CG  . LEU E  111 ? 0.6152 0.6958 0.4642 -0.0803 0.0609  -0.0940 111 LEU E CG  
8424  C CD1 . LEU E  111 ? 0.8064 0.8994 0.6491 -0.0796 0.0543  -0.0923 111 LEU E CD1 
8425  C CD2 . LEU E  111 ? 0.6444 0.7199 0.4966 -0.0770 0.0628  -0.0911 111 LEU E CD2 
8426  N N   . SER E  112 ? 0.6956 0.7687 0.5646 -0.0733 0.0523  -0.0893 112 SER E N   
8427  C CA  . SER E  112 ? 0.5266 0.5959 0.3985 -0.0754 0.0540  -0.0914 112 SER E CA  
8428  C C   . SER E  112 ? 0.5699 0.6480 0.4349 -0.0792 0.0516  -0.0946 112 SER E C   
8429  O O   . SER E  112 ? 0.6554 0.7314 0.5196 -0.0835 0.0551  -0.0986 112 SER E O   
8430  C CB  . SER E  112 ? 0.5912 0.6557 0.4721 -0.0702 0.0507  -0.0868 112 SER E CB  
8431  O OG  . SER E  112 ? 0.7049 0.7765 0.5847 -0.0666 0.0435  -0.0834 112 SER E OG  
8432  N N   . SER E  113 ? 0.6743 0.7621 0.5346 -0.0776 0.0459  -0.0926 113 SER E N   
8433  C CA  . SER E  113 ? 0.7265 0.8236 0.5805 -0.0809 0.0431  -0.0951 113 SER E CA  
8434  C C   . SER E  113 ? 0.7291 0.8367 0.5762 -0.0807 0.0393  -0.0940 113 SER E C   
8435  O O   . SER E  113 ? 0.6585 0.7694 0.5074 -0.0756 0.0345  -0.0893 113 SER E O   
8436  C CB  . SER E  113 ? 0.7050 0.8032 0.5630 -0.0780 0.0385  -0.0928 113 SER E CB  
8437  O OG  . SER E  113 ? 0.6949 0.8009 0.5474 -0.0818 0.0369  -0.0959 113 SER E OG  
8438  N N   . VAL E  114 ? 0.6529 0.7660 0.4922 -0.0863 0.0417  -0.0984 114 VAL E N   
8439  C CA  . VAL E  114 ? 0.8136 0.9378 0.6461 -0.0866 0.0379  -0.0973 114 VAL E CA  
8440  C C   . VAL E  114 ? 0.8485 0.9826 0.6755 -0.0905 0.0354  -0.0999 114 VAL E C   
8441  O O   . VAL E  114 ? 0.7872 0.9194 0.6131 -0.0952 0.0385  -0.1045 114 VAL E O   
8442  C CB  . VAL E  114 ? 0.8581 0.9823 0.6851 -0.0897 0.0420  -0.0993 114 VAL E CB  
8443  C CG1 . VAL E  114 ? 0.6999 0.8141 0.5328 -0.0860 0.0449  -0.0969 114 VAL E CG1 
8444  C CG2 . VAL E  114 ? 0.8606 0.9844 0.6822 -0.0975 0.0476  -0.1061 114 VAL E CG2 
8445  N N   . SER E  115 ? 0.9328 1.0773 0.7567 -0.0884 0.0297  -0.0969 115 SER E N   
8446  C CA  . SER E  115 ? 1.0136 1.1688 0.8325 -0.0915 0.0266  -0.0987 115 SER E CA  
8447  C C   . SER E  115 ? 1.0877 1.2501 0.8977 -0.0975 0.0286  -0.1022 115 SER E C   
8448  O O   . SER E  115 ? 1.1459 1.3121 0.9514 -0.1034 0.0303  -0.1070 115 SER E O   
8449  C CB  . SER E  115 ? 0.9934 1.1563 0.8143 -0.0861 0.0196  -0.0933 115 SER E CB  
8450  O OG  . SER E  115 ? 1.1991 1.3689 1.0188 -0.0878 0.0166  -0.0945 115 SER E OG  
8451  N N   . SER E  116 ? 1.0901 1.2543 0.8976 -0.0960 0.0285  -0.1000 116 SER E N   
8452  C CA  . SER E  116 ? 1.0901 1.2591 0.8891 -0.1018 0.0314  -0.1034 116 SER E CA  
8453  C C   . SER E  116 ? 0.9988 1.1604 0.7979 -0.1010 0.0356  -0.1030 116 SER E C   
8454  O O   . SER E  116 ? 1.0692 1.2263 0.8735 -0.0950 0.0341  -0.0983 116 SER E O   
8455  C CB  . SER E  116 ? 1.2517 1.4351 1.0447 -0.1021 0.0261  -0.1012 116 SER E CB  
8456  O OG  . SER E  116 ? 1.4552 1.6405 1.2505 -0.0960 0.0226  -0.0952 116 SER E OG  
8457  N N   . PHE E  117 ? 0.9516 1.1120 0.7445 -0.1074 0.0409  -0.1081 117 PHE E N   
8458  C CA  . PHE E  117 ? 0.8438 0.9956 0.6370 -0.1076 0.0462  -0.1087 117 PHE E CA  
8459  C C   . PHE E  117 ? 0.8452 1.0016 0.6285 -0.1147 0.0498  -0.1133 117 PHE E C   
8460  O O   . PHE E  117 ? 0.9413 1.0956 0.7211 -0.1212 0.0545  -0.1192 117 PHE E O   
8461  C CB  . PHE E  117 ? 0.7679 0.9062 0.5680 -0.1076 0.0516  -0.1111 117 PHE E CB  
8462  C CG  . PHE E  117 ? 0.8067 0.9348 0.6102 -0.1057 0.0563  -0.1103 117 PHE E CG  
8463  C CD1 . PHE E  117 ? 0.7603 0.8841 0.5590 -0.1112 0.0631  -0.1150 117 PHE E CD1 
8464  C CD2 . PHE E  117 ? 0.7940 0.9166 0.6054 -0.0984 0.0542  -0.1048 117 PHE E CD2 
8465  C CE1 . PHE E  117 ? 0.7424 0.8568 0.5446 -0.1094 0.0677  -0.1143 117 PHE E CE1 
8466  C CE2 . PHE E  117 ? 0.7627 0.8761 0.5777 -0.0967 0.0585  -0.1040 117 PHE E CE2 
8467  C CZ  . PHE E  117 ? 0.7499 0.8591 0.5603 -0.1021 0.0653  -0.1086 117 PHE E CZ  
8468  N N   . GLU E  118 ? 0.9514 1.1139 0.7300 -0.1136 0.0477  -0.1104 118 GLU E N   
8469  C CA  . GLU E  118 ? 1.0600 1.2272 0.8286 -0.1202 0.0509  -0.1142 118 GLU E CA  
8470  C C   . GLU E  118 ? 0.9306 1.0921 0.6986 -0.1186 0.0542  -0.1126 118 GLU E C   
8471  O O   . GLU E  118 ? 0.8841 1.0460 0.6557 -0.1122 0.0508  -0.1068 118 GLU E O   
8472  C CB  . GLU E  118 ? 1.0634 1.2463 0.8247 -0.1222 0.0451  -0.1129 118 GLU E CB  
8473  C CG  . GLU E  118 ? 1.1896 1.3789 0.9503 -0.1169 0.0404  -0.1063 118 GLU E CG  
8474  C CD  . GLU E  118 ? 1.6448 1.8477 1.3954 -0.1212 0.0378  -0.1065 118 GLU E CD  
8475  O OE1 . GLU E  118 ? 1.7878 1.9959 1.5320 -0.1285 0.0393  -0.1117 118 GLU E OE1 
8476  O OE2 . GLU E  118 ? 1.6482 1.8570 1.3975 -0.1175 0.0344  -0.1013 118 GLU E OE2 
8477  N N   . ARG E  119 ? 0.9376 1.0935 0.7009 -0.1246 0.0612  -0.1180 119 ARG E N   
8478  C CA  . ARG E  119 ? 0.8845 1.0335 0.6473 -0.1238 0.0656  -0.1174 119 ARG E CA  
8479  C C   . ARG E  119 ? 0.9426 1.1010 0.6945 -0.1279 0.0651  -0.1179 119 ARG E C   
8480  O O   . ARG E  119 ? 1.1243 1.2866 0.8678 -0.1356 0.0681  -0.1233 119 ARG E O   
8481  C CB  . ARG E  119 ? 0.7636 0.8996 0.5286 -0.1277 0.0742  -0.1230 119 ARG E CB  
8482  C CG  . ARG E  119 ? 0.8246 0.9541 0.5867 -0.1295 0.0803  -0.1243 119 ARG E CG  
8483  C CD  . ARG E  119 ? 1.0859 1.2034 0.8499 -0.1341 0.0891  -0.1304 119 ARG E CD  
8484  N NE  . ARG E  119 ? 1.2706 1.3835 1.0293 -0.1380 0.0956  -0.1333 119 ARG E NE  
8485  C CZ  . ARG E  119 ? 1.4357 1.5543 1.1831 -0.1455 0.0982  -0.1380 119 ARG E CZ  
8486  N NH1 . ARG E  119 ? 1.4685 1.5980 1.2088 -0.1502 0.0947  -0.1403 119 ARG E NH1 
8487  N NH2 . ARG E  119 ? 1.3332 1.4465 1.0764 -0.1486 0.1043  -0.1403 119 ARG E NH2 
8488  N N   . PHE E  120 ? 0.9452 1.1071 0.6973 -0.1227 0.0615  -0.1120 120 PHE E N   
8489  C CA  . PHE E  120 ? 0.9579 1.1293 0.7001 -0.1257 0.0603  -0.1114 120 PHE E CA  
8490  C C   . PHE E  120 ? 0.9373 1.1019 0.6793 -0.1238 0.0641  -0.1097 120 PHE E C   
8491  O O   . PHE E  120 ? 0.9447 1.0997 0.6954 -0.1178 0.0652  -0.1067 120 PHE E O   
8492  C CB  . PHE E  120 ? 0.9042 1.0891 0.6455 -0.1218 0.0517  -0.1055 120 PHE E CB  
8493  C CG  . PHE E  120 ? 0.8799 1.0621 0.6296 -0.1125 0.0479  -0.0984 120 PHE E CG  
8494  C CD1 . PHE E  120 ? 0.9759 1.1606 0.7233 -0.1094 0.0467  -0.0938 120 PHE E CD1 
8495  C CD2 . PHE E  120 ? 1.0139 1.1910 0.7735 -0.1072 0.0457  -0.0962 120 PHE E CD2 
8496  C CE1 . PHE E  120 ? 0.9839 1.1660 0.7392 -0.1011 0.0435  -0.0874 120 PHE E CE1 
8497  C CE2 . PHE E  120 ? 0.9341 1.1087 0.7011 -0.0990 0.0423  -0.0899 120 PHE E CE2 
8498  C CZ  . PHE E  120 ? 0.9438 1.1209 0.7088 -0.0960 0.0413  -0.0856 120 PHE E CZ  
8499  N N   . GLU E  121 ? 1.0147 1.1842 0.7465 -0.1289 0.0662  -0.1116 121 GLU E N   
8500  C CA  . GLU E  121 ? 0.9697 1.1337 0.7002 -0.1277 0.0699  -0.1101 121 GLU E CA  
8501  C C   . GLU E  121 ? 0.9836 1.1537 0.7161 -0.1204 0.0637  -0.1021 121 GLU E C   
8502  O O   . GLU E  121 ? 1.1364 1.3189 0.8619 -0.1214 0.0591  -0.0997 121 GLU E O   
8503  C CB  . GLU E  121 ? 1.0734 1.2407 0.7916 -0.1362 0.0743  -0.1151 121 GLU E CB  
8504  C CG  . GLU E  121 ? 1.2394 1.3975 0.9564 -0.1364 0.0806  -0.1157 121 GLU E CG  
8505  C CD  . GLU E  121 ? 1.3765 1.5368 1.0812 -0.1456 0.0858  -0.1216 121 GLU E CD  
8506  O OE1 . GLU E  121 ? 1.4610 1.6328 1.1570 -0.1511 0.0829  -0.1236 121 GLU E OE1 
8507  O OE2 . GLU E  121 ? 1.3800 1.5307 1.0837 -0.1475 0.0928  -0.1241 121 GLU E OE2 
8508  N N   . ILE E  122 ? 0.9652 1.1266 0.7076 -0.1131 0.0636  -0.0981 122 ILE E N   
8509  C CA  . ILE E  122 ? 0.8934 1.0591 0.6391 -0.1058 0.0582  -0.0905 122 ILE E CA  
8510  C C   . ILE E  122 ? 0.9531 1.1195 0.6925 -0.1065 0.0606  -0.0890 122 ILE E C   
8511  O O   . ILE E  122 ? 1.1042 1.2802 0.8400 -0.1041 0.0559  -0.0841 122 ILE E O   
8512  C CB  . ILE E  122 ? 0.9871 1.1430 0.7454 -0.0980 0.0575  -0.0869 122 ILE E CB  
8513  C CG1 . ILE E  122 ? 0.8481 1.0078 0.6095 -0.0907 0.0527  -0.0794 122 ILE E CG1 
8514  C CG2 . ILE E  122 ? 0.9403 1.0817 0.7030 -0.0988 0.0650  -0.0902 122 ILE E CG2 
8515  C CD1 . ILE E  122 ? 0.6833 0.8344 0.4567 -0.0832 0.0514  -0.0757 122 ILE E CD1 
8516  N N   . PHE E  123 ? 1.1338 1.2900 0.8720 -0.1097 0.0680  -0.0931 123 PHE E N   
8517  C CA  . PHE E  123 ? 0.9870 1.1432 0.7185 -0.1115 0.0712  -0.0925 123 PHE E CA  
8518  C C   . PHE E  123 ? 1.0652 1.2195 0.7873 -0.1208 0.0778  -0.1000 123 PHE E C   
8519  O O   . PHE E  123 ? 1.0950 1.2372 0.8201 -0.1227 0.0848  -0.1042 123 PHE E O   
8520  C CB  . PHE E  123 ? 0.9650 1.1096 0.7046 -0.1056 0.0742  -0.0895 123 PHE E CB  
8521  C CG  . PHE E  123 ? 1.0233 1.1697 0.7713 -0.0966 0.0681  -0.0821 123 PHE E CG  
8522  C CD1 . PHE E  123 ? 0.9204 1.0570 0.6803 -0.0911 0.0684  -0.0806 123 PHE E CD1 
8523  C CD2 . PHE E  123 ? 1.0393 1.1971 0.7835 -0.0939 0.0622  -0.0767 123 PHE E CD2 
8524  C CE1 . PHE E  123 ? 0.9196 1.0578 0.6870 -0.0833 0.0630  -0.0741 123 PHE E CE1 
8525  C CE2 . PHE E  123 ? 0.9915 1.1506 0.7435 -0.0859 0.0570  -0.0702 123 PHE E CE2 
8526  C CZ  . PHE E  123 ? 0.9371 1.0863 0.7006 -0.0807 0.0574  -0.0691 123 PHE E CZ  
8527  N N   . PRO E  124 ? 1.2848 1.4510 0.9958 -0.1266 0.0757  -0.1016 124 PRO E N   
8528  C CA  . PRO E  124 ? 1.3280 1.4935 1.0288 -0.1361 0.0818  -0.1088 124 PRO E CA  
8529  C C   . PRO E  124 ? 1.3219 1.4776 1.0208 -0.1370 0.0889  -0.1100 124 PRO E C   
8530  O O   . PRO E  124 ? 1.2912 1.4488 0.9895 -0.1329 0.0871  -0.1048 124 PRO E O   
8531  C CB  . PRO E  124 ? 1.4334 1.6150 1.1229 -0.1401 0.0767  -0.1076 124 PRO E CB  
8532  C CG  . PRO E  124 ? 1.3518 1.5424 1.0470 -0.1339 0.0681  -0.1016 124 PRO E CG  
8533  C CD  . PRO E  124 ? 1.2846 1.4659 0.9919 -0.1247 0.0675  -0.0966 124 PRO E CD  
8534  N N   . LYS E  125 ? 1.2850 1.4303 0.9832 -0.1423 0.0969  -0.1168 125 LYS E N   
8535  C CA  . LYS E  125 ? 1.4588 1.5940 1.1556 -0.1437 0.1045  -0.1186 125 LYS E CA  
8536  C C   . LYS E  125 ? 1.6409 1.7838 1.3266 -0.1462 0.1039  -0.1168 125 LYS E C   
8537  O O   . LYS E  125 ? 1.6519 1.7910 1.3397 -0.1416 0.1046  -0.1125 125 LYS E O   
8538  C CB  . LYS E  125 ? 1.4022 1.5284 1.0966 -0.1514 0.1133  -0.1272 125 LYS E CB  
8539  C CG  . LYS E  125 ? 1.2819 1.3928 0.9888 -0.1478 0.1185  -0.1283 125 LYS E CG  
8540  C CD  . LYS E  125 ? 1.3360 1.4381 1.0409 -0.1554 0.1274  -0.1367 125 LYS E CD  
8541  C CE  . LYS E  125 ? 1.3581 1.4564 1.0535 -0.1617 0.1350  -0.1409 125 LYS E CE  
8542  N NZ  . LYS E  125 ? 1.3263 1.4147 1.0208 -0.1688 0.1444  -0.1491 125 LYS E NZ  
8543  N N   . THR E  126 ? 2.3373 2.4913 2.0112 -0.1534 0.1023  -0.1197 126 THR E N   
8544  C CA  . THR E  126 ? 2.3477 2.5075 2.0090 -0.1584 0.1039  -0.1202 126 THR E CA  
8545  C C   . THR E  126 ? 2.3839 2.5563 2.0415 -0.1542 0.0963  -0.1125 126 THR E C   
8546  O O   . THR E  126 ? 2.6036 2.7837 2.2494 -0.1591 0.0963  -0.1128 126 THR E O   
8547  C CB  . THR E  126 ? 1.9052 2.0715 1.5543 -0.1691 0.1060  -0.1273 126 THR E CB  
8548  O OG1 . THR E  126 ? 1.7975 1.9709 1.4493 -0.1695 0.1008  -0.1280 126 THR E OG1 
8549  N N   . SER E  127 ? 1.6123 1.7869 1.2795 -0.1453 0.0899  -0.1057 127 SER E N   
8550  C CA  . SER E  127 ? 1.4822 1.6683 1.1470 -0.1409 0.0829  -0.0981 127 SER E CA  
8551  C C   . SER E  127 ? 1.3909 1.5713 1.0677 -0.1304 0.0803  -0.0911 127 SER E C   
8552  O O   . SER E  127 ? 1.5356 1.7223 1.2116 -0.1258 0.0762  -0.0845 127 SER E O   
8553  C CB  . SER E  127 ? 1.6100 1.8113 1.2708 -0.1427 0.0754  -0.0968 127 SER E CB  
8554  O OG  . SER E  127 ? 1.4419 1.6410 1.1125 -0.1394 0.0729  -0.0972 127 SER E OG  
8555  N N   . SER E  128 ? 1.3981 1.5665 1.0860 -0.1268 0.0830  -0.0926 128 SER E N   
8556  C CA  . SER E  128 ? 1.2771 1.4403 0.9772 -0.1171 0.0802  -0.0864 128 SER E CA  
8557  C C   . SER E  128 ? 1.3093 1.4608 1.0127 -0.1144 0.0860  -0.0855 128 SER E C   
8558  O O   . SER E  128 ? 1.3248 1.4746 1.0350 -0.1070 0.0835  -0.0794 128 SER E O   
8559  C CB  . SER E  128 ? 1.2605 1.4178 0.9712 -0.1144 0.0794  -0.0880 128 SER E CB  
8560  O OG  . SER E  128 ? 1.1427 1.3104 0.8503 -0.1173 0.0745  -0.0892 128 SER E OG  
8561  N N   . TRP E  129 ? 1.3333 1.4770 1.0319 -0.1206 0.0939  -0.0916 129 TRP E N   
8562  C CA  . TRP E  129 ? 1.3579 1.4894 1.0603 -0.1186 0.1003  -0.0916 129 TRP E CA  
8563  C C   . TRP E  129 ? 1.4133 1.5456 1.1034 -0.1252 0.1055  -0.0945 129 TRP E C   
8564  O O   . TRP E  129 ? 1.4202 1.5448 1.1069 -0.1314 0.1130  -0.1011 129 TRP E O   
8565  C CB  . TRP E  129 ? 1.4059 1.5236 1.1177 -0.1186 0.1061  -0.0961 129 TRP E CB  
8566  C CG  . TRP E  129 ? 1.2210 1.3395 0.9420 -0.1148 0.1012  -0.0950 129 TRP E CG  
8567  C CD1 . TRP E  129 ? 1.1460 1.2641 0.8673 -0.1191 0.1021  -0.1001 129 TRP E CD1 
8568  C CD2 . TRP E  129 ? 1.1822 1.3023 0.9129 -0.1062 0.0947  -0.0883 129 TRP E CD2 
8569  N NE1 . TRP E  129 ? 1.1481 1.2673 0.8787 -0.1136 0.0965  -0.0970 129 TRP E NE1 
8570  C CE2 . TRP E  129 ? 1.1811 1.3016 0.9175 -0.1057 0.0919  -0.0898 129 TRP E CE2 
8571  C CE3 . TRP E  129 ? 1.1103 1.2314 0.8455 -0.0989 0.0912  -0.0813 129 TRP E CE3 
8572  C CZ2 . TRP E  129 ? 1.1857 1.3075 0.9318 -0.0983 0.0858  -0.0847 129 TRP E CZ2 
8573  C CZ3 . TRP E  129 ? 1.0770 1.1993 0.8220 -0.0917 0.0852  -0.0764 129 TRP E CZ3 
8574  C CH2 . TRP E  129 ? 1.1666 1.2893 0.9168 -0.0915 0.0826  -0.0781 129 TRP E CH2 
8575  N N   . PRO E  130 ? 1.5580 1.6996 1.2414 -0.1238 0.1016  -0.0895 130 PRO E N   
8576  C CA  . PRO E  130 ? 1.4654 1.6100 1.1361 -0.1297 0.1053  -0.0912 130 PRO E CA  
8577  C C   . PRO E  130 ? 1.5782 1.7119 1.2517 -0.1268 0.1111  -0.0897 130 PRO E C   
8578  O O   . PRO E  130 ? 1.6051 1.7381 1.2688 -0.1320 0.1159  -0.0921 130 PRO E O   
8579  C CB  . PRO E  130 ? 1.4711 1.6315 1.1354 -0.1280 0.0972  -0.0849 130 PRO E CB  
8580  C CG  . PRO E  130 ? 1.4026 1.5678 1.0767 -0.1214 0.0896  -0.0806 130 PRO E CG  
8581  C CD  . PRO E  130 ? 1.6079 1.7591 1.2952 -0.1167 0.0929  -0.0817 130 PRO E CD  
8582  N N   . ASN E  131 ? 1.5726 1.6982 1.2593 -0.1187 0.1106  -0.0858 131 ASN E N   
8583  C CA  . ASN E  131 ? 1.5382 1.6534 1.2292 -0.1152 0.1156  -0.0840 131 ASN E CA  
8584  C C   . ASN E  131 ? 1.4377 1.5376 1.1387 -0.1147 0.1225  -0.0882 131 ASN E C   
8585  O O   . ASN E  131 ? 1.4364 1.5264 1.1434 -0.1112 0.1269  -0.0867 131 ASN E O   
8586  C CB  . ASN E  131 ? 1.5806 1.6987 1.2787 -0.1059 0.1097  -0.0754 131 ASN E CB  
8587  C CG  . ASN E  131 ? 1.7993 1.9319 1.4879 -0.1060 0.1037  -0.0705 131 ASN E CG  
8588  O OD1 . ASN E  131 ? 1.7957 1.9350 1.4715 -0.1129 0.1049  -0.0732 131 ASN E OD1 
8589  N ND2 . ASN E  131 ? 1.8723 2.0099 1.5673 -0.0982 0.0972  -0.0632 131 ASN E ND2 
8590  N N   . HIS E  132 ? 1.3098 1.4078 1.0127 -0.1182 0.1235  -0.0933 132 HIS E N   
8591  C CA  . HIS E  132 ? 1.2507 1.3349 0.9636 -0.1179 0.1298  -0.0972 132 HIS E CA  
8592  C C   . HIS E  132 ? 1.3090 1.3913 1.0158 -0.1267 0.1349  -0.1054 132 HIS E C   
8593  O O   . HIS E  132 ? 1.2866 1.3793 0.9843 -0.1317 0.1316  -0.1075 132 HIS E O   
8594  C CB  . HIS E  132 ? 1.2341 1.3163 0.9607 -0.1104 0.1246  -0.0933 132 HIS E CB  
8595  C CG  . HIS E  132 ? 1.1593 1.2452 0.8914 -0.1020 0.1185  -0.0852 132 HIS E CG  
8596  N ND1 . HIS E  132 ? 1.1248 1.2012 0.8675 -0.0957 0.1205  -0.0819 132 HIS E ND1 
8597  C CD2 . HIS E  132 ? 1.0488 1.1467 0.7773 -0.0990 0.1107  -0.0799 132 HIS E CD2 
8598  C CE1 . HIS E  132 ? 1.1941 1.2763 0.9393 -0.0893 0.1143  -0.0750 132 HIS E CE1 
8599  N NE2 . HIS E  132 ? 1.0221 1.1173 0.7591 -0.0910 0.1083  -0.0736 132 HIS E NE2 
8600  N N   . ASP E  133 ? 1.1253 1.1944 0.8376 -0.1285 0.1432  -0.1099 133 ASP E N   
8601  C CA  . ASP E  133 ? 1.1675 1.2332 0.8753 -0.1366 0.1491  -0.1180 133 ASP E CA  
8602  C C   . ASP E  133 ? 1.2580 1.3230 0.9744 -0.1350 0.1461  -0.1190 133 ASP E C   
8603  O O   . ASP E  133 ? 1.2226 1.2794 0.9522 -0.1291 0.1464  -0.1167 133 ASP E O   
8604  C CB  . ASP E  133 ? 1.2639 1.3154 0.9738 -0.1395 0.1599  -0.1225 133 ASP E CB  
8605  C CG  . ASP E  133 ? 1.5137 1.5624 1.2159 -0.1492 0.1669  -0.1312 133 ASP E CG  
8606  O OD1 . ASP E  133 ? 1.5570 1.6081 1.2604 -0.1514 0.1651  -0.1341 133 ASP E OD1 
8607  O OD2 . ASP E  133 ? 1.6477 1.6914 1.3426 -0.1547 0.1745  -0.1352 133 ASP E OD2 
8608  N N   . SER E  134 ? 1.2629 1.3368 0.9716 -0.1404 0.1433  -0.1223 134 SER E N   
8609  C CA  . SER E  134 ? 1.2275 1.3019 0.9430 -0.1394 0.1402  -0.1235 134 SER E CA  
8610  C C   . SER E  134 ? 1.2090 1.2771 0.9218 -0.1473 0.1477  -0.1318 134 SER E C   
8611  O O   . SER E  134 ? 1.3534 1.4256 1.0658 -0.1500 0.1454  -0.1345 134 SER E O   
8612  C CB  . SER E  134 ? 1.1704 1.2599 0.8807 -0.1388 0.1306  -0.1204 134 SER E CB  
8613  O OG  . SER E  134 ? 1.2090 1.3082 0.9046 -0.1463 0.1306  -0.1234 134 SER E OG  
8614  N N   . ASN E  135 ? 1.1988 1.2568 0.9101 -0.1511 0.1570  -0.1360 135 ASN E N   
8615  C CA  . ASN E  135 ? 1.3572 1.4085 1.0654 -0.1591 0.1653  -0.1442 135 ASN E CA  
8616  C C   . ASN E  135 ? 1.3748 1.4097 1.0937 -0.1576 0.1743  -0.1462 135 ASN E C   
8617  O O   . ASN E  135 ? 1.5460 1.5738 1.2679 -0.1616 0.1802  -0.1517 135 ASN E O   
8618  C CB  . ASN E  135 ? 1.5127 1.5690 1.2046 -0.1683 0.1691  -0.1493 135 ASN E CB  
8619  C CG  . ASN E  135 ? 1.4811 1.5538 1.1623 -0.1712 0.1609  -0.1484 135 ASN E CG  
8620  O OD1 . ASN E  135 ? 1.2272 1.3056 0.9104 -0.1712 0.1561  -0.1487 135 ASN E OD1 
8621  N ND2 . ASN E  135 ? 1.3969 1.4775 1.0667 -0.1737 0.1593  -0.1470 135 ASN E ND2 
8622  N N   . LYS E  136 ? 1.3114 1.3406 1.0365 -0.1518 0.1754  -0.1417 136 LYS E N   
8623  C CA  . LYS E  136 ? 1.4146 1.4287 1.1499 -0.1502 0.1840  -0.1431 136 LYS E CA  
8624  C C   . LYS E  136 ? 1.4497 1.4580 1.2013 -0.1428 0.1815  -0.1393 136 LYS E C   
8625  O O   . LYS E  136 ? 1.4832 1.4794 1.2453 -0.1404 0.1876  -0.1394 136 LYS E O   
8626  C CB  . LYS E  136 ? 1.5884 1.5985 1.3230 -0.1477 0.1869  -0.1401 136 LYS E CB  
8627  C CG  . LYS E  136 ? 1.6558 1.6709 1.3743 -0.1550 0.1898  -0.1437 136 LYS E CG  
8628  C CD  . LYS E  136 ? 1.6911 1.6943 1.4093 -0.1579 0.2006  -0.1471 136 LYS E CD  
8629  C CE  . LYS E  136 ? 1.8743 1.8811 1.5759 -0.1678 0.2054  -0.1533 136 LYS E CE  
8630  N NZ  . LYS E  136 ? 1.9955 2.0056 1.6913 -0.1751 0.2064  -0.1597 136 LYS E NZ  
8631  N N   . GLY E  137 ? 1.2851 1.3021 1.0388 -0.1394 0.1725  -0.1360 137 GLY E N   
8632  C CA  . GLY E  137 ? 1.2292 1.2422 0.9973 -0.1322 0.1690  -0.1319 137 GLY E CA  
8633  C C   . GLY E  137 ? 1.2022 1.2089 0.9761 -0.1351 0.1731  -0.1364 137 GLY E C   
8634  O O   . GLY E  137 ? 1.1682 1.1804 0.9437 -0.1343 0.1675  -0.1359 137 GLY E O   
8635  N N   . VAL E  138 ? 1.1693 1.1641 0.9466 -0.1383 0.1831  -0.1408 138 VAL E N   
8636  C CA  . VAL E  138 ? 1.2308 1.2182 1.0148 -0.1407 0.1881  -0.1449 138 VAL E CA  
8637  C C   . VAL E  138 ? 1.1861 1.1598 0.9846 -0.1364 0.1943  -0.1432 138 VAL E C   
8638  O O   . VAL E  138 ? 1.1698 1.1396 0.9720 -0.1324 0.1956  -0.1397 138 VAL E O   
8639  C CB  . VAL E  138 ? 1.2406 1.2269 1.0137 -0.1509 0.1956  -0.1534 138 VAL E CB  
8640  C CG1 . VAL E  138 ? 1.2390 1.2395 0.9978 -0.1555 0.1893  -0.1550 138 VAL E CG1 
8641  C CG2 . VAL E  138 ? 1.2059 1.1838 0.9756 -0.1546 0.2052  -0.1568 138 VAL E CG2 
8642  N N   . THR E  139 ? 1.0150 0.9816 0.8219 -0.1370 0.1982  -0.1455 139 THR E N   
8643  C CA  . THR E  139 ? 1.1774 1.1316 0.9992 -0.1327 0.2037  -0.1435 139 THR E CA  
8644  C C   . THR E  139 ? 1.2419 1.1880 1.0690 -0.1366 0.2109  -0.1484 139 THR E C   
8645  O O   . THR E  139 ? 1.1597 1.1106 0.9820 -0.1405 0.2090  -0.1517 139 THR E O   
8646  C CB  . THR E  139 ? 1.2020 1.1578 1.0357 -0.1233 0.1955  -0.1355 139 THR E CB  
8647  O OG1 . THR E  139 ? 1.1616 1.1058 1.0103 -0.1196 0.2007  -0.1337 139 THR E OG1 
8648  C CG2 . THR E  139 ? 1.2691 1.2335 1.1023 -0.1221 0.1870  -0.1342 139 THR E CG2 
8649  N N   . ALA E  140 ? 1.3843 1.3179 1.2218 -0.1355 0.2193  -0.1487 140 ALA E N   
8650  C CA  . ALA E  140 ? 1.3221 1.2468 1.1665 -0.1385 0.2268  -0.1527 140 ALA E CA  
8651  C C   . ALA E  140 ? 1.4119 1.3376 1.2674 -0.1330 0.2207  -0.1484 140 ALA E C   
8652  O O   . ALA E  140 ? 1.4230 1.3435 1.2836 -0.1352 0.2250  -0.1512 140 ALA E O   
8653  C CB  . ALA E  140 ? 1.4522 1.3636 1.3055 -0.1382 0.2374  -0.1536 140 ALA E CB  
8654  N N   . ALA E  141 ? 1.3471 1.2794 1.2061 -0.1260 0.2108  -0.1416 141 ALA E N   
8655  C CA  . ALA E  141 ? 1.2982 1.2322 1.1671 -0.1205 0.2041  -0.1370 141 ALA E CA  
8656  C C   . ALA E  141 ? 1.2526 1.1951 1.1136 -0.1241 0.1992  -0.1398 141 ALA E C   
8657  O O   . ALA E  141 ? 1.2757 1.2167 1.1437 -0.1229 0.1980  -0.1392 141 ALA E O   
8658  C CB  . ALA E  141 ? 1.2859 1.2244 1.1603 -0.1124 0.1954  -0.1292 141 ALA E CB  
8659  N N   . CYS E  142 ? 1.1867 1.1386 1.0333 -0.1285 0.1963  -0.1426 142 CYS E N   
8660  C CA  . CYS E  142 ? 1.1577 1.1185 0.9959 -0.1324 0.1916  -0.1455 142 CYS E CA  
8661  C C   . CYS E  142 ? 1.2108 1.1710 1.0376 -0.1420 0.1991  -0.1539 142 CYS E C   
8662  O O   . CYS E  142 ? 1.1371 1.1058 0.9507 -0.1462 0.1969  -0.1562 142 CYS E O   
8663  C CB  . CYS E  142 ? 1.3566 1.3306 1.1875 -0.1295 0.1808  -0.1415 142 CYS E CB  
8664  S SG  . CYS E  142 ? 1.3690 1.3443 1.2120 -0.1186 0.1717  -0.1319 142 CYS E SG  
8665  N N   . PRO E  143 ? 1.2355 1.1856 1.0674 -0.1456 0.2081  -0.1583 143 PRO E N   
8666  C CA  . PRO E  143 ? 1.3149 1.2622 1.1372 -0.1549 0.2170  -0.1667 143 PRO E CA  
8667  C C   . PRO E  143 ? 1.4491 1.4044 1.2624 -0.1607 0.2142  -0.1712 143 PRO E C   
8668  O O   . PRO E  143 ? 1.5207 1.4770 1.3402 -0.1584 0.2106  -0.1697 143 PRO E O   
8669  C CB  . PRO E  143 ? 1.4680 1.4009 1.3021 -0.1552 0.2273  -0.1686 143 PRO E CB  
8670  C CG  . PRO E  143 ? 1.4195 1.3482 1.2691 -0.1457 0.2235  -0.1607 143 PRO E CG  
8671  C CD  . PRO E  143 ? 1.3331 1.2735 1.1808 -0.1409 0.2109  -0.1554 143 PRO E CD  
8672  N N   . HIS E  144 ? 1.6021 1.5632 1.4008 -0.1682 0.2159  -0.1767 144 HIS E N   
8673  C CA  . HIS E  144 ? 1.6513 1.6190 1.4409 -0.1751 0.2152  -0.1823 144 HIS E CA  
8674  C C   . HIS E  144 ? 1.7964 1.7561 1.5805 -0.1842 0.2272  -0.1909 144 HIS E C   
8675  O O   . HIS E  144 ? 1.7383 1.6999 1.5113 -0.1897 0.2306  -0.1947 144 HIS E O   
8676  C CB  . HIS E  144 ? 1.5280 1.5108 1.3044 -0.1768 0.2063  -0.1815 144 HIS E CB  
8677  C CG  . HIS E  144 ? 1.6274 1.6192 1.3984 -0.1805 0.2015  -0.1841 144 HIS E CG  
8678  N ND1 . HIS E  144 ? 1.7095 1.7121 1.4659 -0.1874 0.1992  -0.1883 144 HIS E ND1 
8679  C CD2 . HIS E  144 ? 1.6544 1.6461 1.4328 -0.1782 0.1986  -0.1831 144 HIS E CD2 
8680  C CE1 . HIS E  144 ? 1.7347 1.7434 1.4900 -0.1892 0.1951  -0.1897 144 HIS E CE1 
8681  N NE2 . HIS E  144 ? 1.6758 1.6779 1.4441 -0.1837 0.1947  -0.1867 144 HIS E NE2 
8682  N N   . ALA E  145 ? 1.8545 1.8051 1.6468 -0.1855 0.2336  -0.1937 145 ALA E N   
8683  C CA  . ALA E  145 ? 1.8248 1.7662 1.6141 -0.1937 0.2459  -0.2018 145 ALA E CA  
8684  C C   . ALA E  145 ? 1.9469 1.8805 1.7355 -0.1946 0.2536  -0.2028 145 ALA E C   
8685  O O   . ALA E  145 ? 1.8030 1.7392 1.5787 -0.2015 0.2571  -0.2078 145 ALA E O   
8686  C CB  . ALA E  145 ? 1.6187 1.5683 1.3929 -0.2032 0.2461  -0.2090 145 ALA E CB  
8687  N N   . GLY E  146 ? 2.6172 2.5413 2.4196 -0.1877 0.2562  -0.1978 146 GLY E N   
8688  C CA  . GLY E  146 ? 2.6486 2.5642 2.4523 -0.1878 0.2638  -0.1983 146 GLY E CA  
8689  C C   . GLY E  146 ? 2.6312 2.5543 2.4282 -0.1848 0.2573  -0.1941 146 GLY E C   
8690  O O   . GLY E  146 ? 2.5920 2.5101 2.3972 -0.1787 0.2577  -0.1891 146 GLY E O   
8691  N N   . ALA E  147 ? 1.9115 1.8470 1.6939 -0.1890 0.2512  -0.1960 147 ALA E N   
8692  C CA  . ALA E  147 ? 1.9402 1.8837 1.7148 -0.1868 0.2452  -0.1923 147 ALA E CA  
8693  C C   . ALA E  147 ? 1.7742 1.7220 1.5583 -0.1764 0.2351  -0.1829 147 ALA E C   
8694  O O   . ALA E  147 ? 1.7158 1.6660 1.5076 -0.1720 0.2293  -0.1797 147 ALA E O   
8695  C CB  . ALA E  147 ? 1.8545 1.8112 1.6121 -0.1936 0.2404  -0.1960 147 ALA E CB  
8696  N N   . LYS E  148 ? 1.5741 1.5227 1.3574 -0.1726 0.2332  -0.1788 148 LYS E N   
8697  C CA  . LYS E  148 ? 1.5132 1.4660 1.3045 -0.1630 0.2239  -0.1701 148 LYS E CA  
8698  C C   . LYS E  148 ? 1.5015 1.4696 1.2838 -0.1623 0.2125  -0.1676 148 LYS E C   
8699  O O   . LYS E  148 ? 1.3409 1.3169 1.1101 -0.1662 0.2107  -0.1691 148 LYS E O   
8700  C CB  . LYS E  148 ? 1.4037 1.3522 1.1969 -0.1594 0.2262  -0.1668 148 LYS E CB  
8701  C CG  . LYS E  148 ? 1.5540 1.4874 1.3572 -0.1593 0.2372  -0.1684 148 LYS E CG  
8702  C CD  . LYS E  148 ? 1.5944 1.5245 1.4000 -0.1552 0.2385  -0.1645 148 LYS E CD  
8703  C CE  . LYS E  148 ? 1.5941 1.5312 1.3834 -0.1603 0.2382  -0.1671 148 LYS E CE  
8704  N NZ  . LYS E  148 ? 1.5860 1.5202 1.3773 -0.1561 0.2390  -0.1629 148 LYS E NZ  
8705  N N   . SER E  149 ? 1.4653 1.4375 1.2546 -0.1573 0.2050  -0.1636 149 SER E N   
8706  C CA  . SER E  149 ? 1.4052 1.3917 1.1873 -0.1563 0.1943  -0.1611 149 SER E CA  
8707  C C   . SER E  149 ? 1.3254 1.3154 1.1163 -0.1465 0.1851  -0.1524 149 SER E C   
8708  O O   . SER E  149 ? 1.1410 1.1242 0.9405 -0.1411 0.1867  -0.1484 149 SER E O   
8709  C CB  . SER E  149 ? 1.3232 1.3134 1.1031 -0.1605 0.1931  -0.1650 149 SER E CB  
8710  O OG  . SER E  149 ? 1.5077 1.5122 1.2783 -0.1614 0.1840  -0.1639 149 SER E OG  
8711  N N   . PHE E  150 ? 1.3479 1.3486 1.1366 -0.1445 0.1758  -0.1498 150 PHE E N   
8712  C CA  . PHE E  150 ? 1.1444 1.1494 0.9404 -0.1357 0.1668  -0.1420 150 PHE E CA  
8713  C C   . PHE E  150 ? 1.1153 1.1299 0.9102 -0.1349 0.1586  -0.1408 150 PHE E C   
8714  O O   . PHE E  150 ? 1.1217 1.1398 0.9097 -0.1412 0.1598  -0.1460 150 PHE E O   
8715  C CB  . PHE E  150 ? 0.9810 0.9921 0.7709 -0.1334 0.1629  -0.1382 150 PHE E CB  
8716  C CG  . PHE E  150 ? 0.9204 0.9331 0.7193 -0.1241 0.1557  -0.1302 150 PHE E CG  
8717  C CD1 . PHE E  150 ? 0.8667 0.8689 0.6787 -0.1186 0.1585  -0.1270 150 PHE E CD1 
8718  C CD2 . PHE E  150 ? 0.9141 0.9386 0.7085 -0.1210 0.1462  -0.1258 150 PHE E CD2 
8719  C CE1 . PHE E  150 ? 0.8076 0.8113 0.6277 -0.1104 0.1519  -0.1199 150 PHE E CE1 
8720  C CE2 . PHE E  150 ? 0.9824 1.0080 0.7849 -0.1127 0.1399  -0.1188 150 PHE E CE2 
8721  C CZ  . PHE E  150 ? 0.8532 0.8683 0.6684 -0.1076 0.1427  -0.1159 150 PHE E CZ  
8722  N N   . TYR E  151 ? 1.1859 1.2043 0.9875 -0.1273 0.1504  -0.1341 151 TYR E N   
8723  C CA  . TYR E  151 ? 1.0129 1.0407 0.8137 -0.1259 0.1422  -0.1324 151 TYR E CA  
8724  C C   . TYR E  151 ? 0.9745 1.0150 0.7612 -0.1307 0.1383  -0.1344 151 TYR E C   
8725  O O   . TYR E  151 ? 1.0624 1.1070 0.8421 -0.1312 0.1377  -0.1333 151 TYR E O   
8726  C CB  . TYR E  151 ? 1.0082 1.0378 0.8180 -0.1169 0.1344  -0.1247 151 TYR E CB  
8727  C CG  . TYR E  151 ? 0.8024 0.8203 0.6262 -0.1117 0.1375  -0.1219 151 TYR E CG  
8728  C CD1 . TYR E  151 ? 0.8941 0.9068 0.7263 -0.1111 0.1386  -0.1226 151 TYR E CD1 
8729  C CD2 . TYR E  151 ? 0.7792 0.7916 0.6081 -0.1074 0.1393  -0.1183 151 TYR E CD2 
8730  C CE1 . TYR E  151 ? 0.8742 0.8767 0.7194 -0.1063 0.1412  -0.1197 151 TYR E CE1 
8731  C CE2 . TYR E  151 ? 0.7204 0.7227 0.5625 -0.1028 0.1419  -0.1155 151 TYR E CE2 
8732  C CZ  . TYR E  151 ? 0.8976 0.8952 0.7478 -0.1022 0.1428  -0.1161 151 TYR E CZ  
8733  O OH  . TYR E  151 ? 0.8728 0.8608 0.7363 -0.0977 0.1452  -0.1130 151 TYR E OH  
8734  N N   . LYS E  152 ? 0.9059 0.9529 0.6885 -0.1344 0.1356  -0.1373 152 LYS E N   
8735  C CA  . LYS E  152 ? 1.0198 1.0794 0.7894 -0.1394 0.1318  -0.1394 152 LYS E CA  
8736  C C   . LYS E  152 ? 1.0295 1.1002 0.7979 -0.1337 0.1219  -0.1327 152 LYS E C   
8737  O O   . LYS E  152 ? 1.1485 1.2282 0.9072 -0.1358 0.1193  -0.1322 152 LYS E O   
8738  C CB  . LYS E  152 ? 1.0528 1.1159 0.8192 -0.1449 0.1319  -0.1444 152 LYS E CB  
8739  C CG  . LYS E  152 ? 1.3628 1.4157 1.1295 -0.1513 0.1420  -0.1514 152 LYS E CG  
8740  C CD  . LYS E  152 ? 1.6947 1.7465 1.4511 -0.1581 0.1486  -0.1562 152 LYS E CD  
8741  C CE  . LYS E  152 ? 1.8062 1.8476 1.5629 -0.1647 0.1590  -0.1636 152 LYS E CE  
8742  N NZ  . LYS E  152 ? 1.7888 1.8286 1.5353 -0.1716 0.1659  -0.1685 152 LYS E NZ  
8743  N N   . ASN E  153 ? 0.9189 0.9887 0.6973 -0.1266 0.1166  -0.1276 153 ASN E N   
8744  C CA  . ASN E  153 ? 0.8831 0.9630 0.6614 -0.1210 0.1073  -0.1213 153 ASN E CA  
8745  C C   . ASN E  153 ? 0.8496 0.9279 0.6307 -0.1151 0.1058  -0.1158 153 ASN E C   
8746  O O   . ASN E  153 ? 0.8572 0.9429 0.6389 -0.1100 0.0986  -0.1103 153 ASN E O   
8747  C CB  . ASN E  153 ? 0.7995 0.8797 0.5866 -0.1163 0.1020  -0.1185 153 ASN E CB  
8748  C CG  . ASN E  153 ? 0.9338 1.0171 0.7177 -0.1218 0.1025  -0.1235 153 ASN E CG  
8749  O OD1 . ASN E  153 ? 1.0670 1.1561 0.8407 -0.1287 0.1043  -0.1282 153 ASN E OD1 
8750  N ND2 . ASN E  153 ? 1.0056 1.0852 0.7981 -0.1188 0.1009  -0.1225 153 ASN E ND2 
8751  N N   . LEU E  154 ? 0.8807 0.9491 0.6636 -0.1160 0.1130  -0.1173 154 LEU E N   
8752  C CA  . LEU E  154 ? 1.0478 1.1140 0.8332 -0.1110 0.1127  -0.1126 154 LEU E CA  
8753  C C   . LEU E  154 ? 1.0038 1.0672 0.7811 -0.1162 0.1195  -0.1162 154 LEU E C   
8754  O O   . LEU E  154 ? 1.1255 1.1843 0.8990 -0.1228 0.1264  -0.1225 154 LEU E O   
8755  C CB  . LEU E  154 ? 0.9182 0.9734 0.7174 -0.1046 0.1141  -0.1093 154 LEU E CB  
8756  C CG  . LEU E  154 ? 0.8179 0.8747 0.6260 -0.0988 0.1074  -0.1051 154 LEU E CG  
8757  C CD1 . LEU E  154 ? 0.8508 0.8960 0.6722 -0.0939 0.1101  -0.1028 154 LEU E CD1 
8758  C CD2 . LEU E  154 ? 0.9340 1.0010 0.7402 -0.0939 0.0988  -0.0993 154 LEU E CD2 
8759  N N   . ILE E  155 ? 1.0454 1.1114 0.8201 -0.1132 0.1178  -0.1122 155 ILE E N   
8760  C CA  . ILE E  155 ? 1.1663 1.2296 0.9335 -0.1176 0.1241  -0.1150 155 ILE E CA  
8761  C C   . ILE E  155 ? 1.0499 1.1046 0.8248 -0.1120 0.1267  -0.1110 155 ILE E C   
8762  O O   . ILE E  155 ? 0.9929 1.0510 0.7716 -0.1054 0.1209  -0.1048 155 ILE E O   
8763  C CB  . ILE E  155 ? 1.1508 1.2267 0.9049 -0.1206 0.1201  -0.1143 155 ILE E CB  
8764  C CG1 . ILE E  155 ? 1.1759 1.2610 0.9218 -0.1268 0.1178  -0.1184 155 ILE E CG1 
8765  C CG2 . ILE E  155 ? 0.9700 1.0424 0.7165 -0.1248 0.1267  -0.1168 155 ILE E CG2 
8766  C CD1 . ILE E  155 ? 1.3496 1.4491 1.0846 -0.1285 0.1118  -0.1163 155 ILE E CD1 
8767  N N   . TRP E  156 ? 1.0107 1.0542 0.7880 -0.1147 0.1355  -0.1147 156 TRP E N   
8768  C CA  . TRP E  156 ? 1.0711 1.1057 0.8558 -0.1100 0.1389  -0.1115 156 TRP E CA  
8769  C C   . TRP E  156 ? 1.1456 1.1833 0.9207 -0.1120 0.1406  -0.1112 156 TRP E C   
8770  O O   . TRP E  156 ? 1.2951 1.3281 1.0642 -0.1178 0.1483  -0.1161 156 TRP E O   
8771  C CB  . TRP E  156 ? 1.0452 1.0661 0.8378 -0.1117 0.1478  -0.1154 156 TRP E CB  
8772  C CG  . TRP E  156 ? 1.0972 1.1088 0.9001 -0.1061 0.1508  -0.1117 156 TRP E CG  
8773  C CD1 . TRP E  156 ? 1.0299 1.0437 0.8347 -0.1004 0.1468  -0.1058 156 TRP E CD1 
8774  C CD2 . TRP E  156 ? 1.0832 1.0817 0.8962 -0.1058 0.1585  -0.1134 156 TRP E CD2 
8775  N NE1 . TRP E  156 ? 1.1988 1.2019 1.0142 -0.0966 0.1514  -0.1040 156 TRP E NE1 
8776  C CE2 . TRP E  156 ? 1.0895 1.0832 0.9103 -0.0997 0.1586  -0.1084 156 TRP E CE2 
8777  C CE3 . TRP E  156 ? 1.1070 1.0974 0.9236 -0.1099 0.1655  -0.1185 156 TRP E CE3 
8778  C CZ2 . TRP E  156 ? 1.2005 1.1820 1.0325 -0.0977 0.1652  -0.1083 156 TRP E CZ2 
8779  C CZ3 . TRP E  156 ? 1.1789 1.1571 1.0068 -0.1078 0.1722  -0.1183 156 TRP E CZ3 
8780  C CH2 . TRP E  156 ? 1.2443 1.2183 1.0799 -0.1017 0.1719  -0.1131 156 TRP E CH2 
8781  N N   . LEU E  157 ? 0.9384 0.9839 0.7120 -0.1071 0.1337  -0.1053 157 LEU E N   
8782  C CA  . LEU E  157 ? 0.8715 0.9209 0.6359 -0.1084 0.1345  -0.1041 157 LEU E CA  
8783  C C   . LEU E  157 ? 1.0029 1.0411 0.7728 -0.1064 0.1413  -0.1034 157 LEU E C   
8784  O O   . LEU E  157 ? 1.0176 1.0492 0.7997 -0.0999 0.1407  -0.0996 157 LEU E O   
8785  C CB  . LEU E  157 ? 0.9266 0.9871 0.6892 -0.1031 0.1254  -0.0974 157 LEU E CB  
8786  C CG  . LEU E  157 ? 1.0614 1.1353 0.8162 -0.1056 0.1186  -0.0976 157 LEU E CG  
8787  C CD1 . LEU E  157 ? 1.0206 1.1047 0.7733 -0.1005 0.1108  -0.0907 157 LEU E CD1 
8788  C CD2 . LEU E  157 ? 1.0602 1.1383 0.8017 -0.1150 0.1225  -0.1039 157 LEU E CD2 
8789  N N   . VAL E  158 ? 1.1395 1.1758 0.9001 -0.1121 0.1477  -0.1072 158 VAL E N   
8790  C CA  . VAL E  158 ? 1.0937 1.1201 0.8579 -0.1108 0.1544  -0.1068 158 VAL E CA  
8791  C C   . VAL E  158 ? 1.1624 1.1950 0.9158 -0.1119 0.1537  -0.1048 158 VAL E C   
8792  O O   . VAL E  158 ? 1.1934 1.2376 0.9360 -0.1147 0.1489  -0.1046 158 VAL E O   
8793  C CB  . VAL E  158 ? 1.0592 1.0747 0.8235 -0.1169 0.1649  -0.1138 158 VAL E CB  
8794  C CG1 . VAL E  158 ? 1.0621 1.0706 0.8381 -0.1154 0.1661  -0.1152 158 VAL E CG1 
8795  C CG2 . VAL E  158 ? 1.1787 1.1996 0.9278 -0.1263 0.1678  -0.1200 158 VAL E CG2 
8796  N N   . LYS E  159 ? 1.3444 1.3693 1.1010 -0.1096 0.1584  -0.1031 159 LYS E N   
8797  C CA  . LYS E  159 ? 1.4212 1.4510 1.1683 -0.1101 0.1581  -0.1008 159 LYS E CA  
8798  C C   . LYS E  159 ? 1.3442 1.3780 1.0758 -0.1194 0.1623  -0.1066 159 LYS E C   
8799  O O   . LYS E  159 ? 1.2292 1.2559 0.9591 -0.1254 0.1698  -0.1132 159 LYS E O   
8800  C CB  . LYS E  159 ? 1.3865 1.4061 1.1408 -0.1061 0.1633  -0.0984 159 LYS E CB  
8801  C CG  . LYS E  159 ? 1.3052 1.3125 1.0606 -0.1110 0.1742  -0.1044 159 LYS E CG  
8802  C CD  . LYS E  159 ? 1.4307 1.4289 1.1922 -0.1072 0.1792  -0.1018 159 LYS E CD  
8803  C CE  . LYS E  159 ? 1.4340 1.4206 1.1954 -0.1126 0.1905  -0.1080 159 LYS E CE  
8804  N NZ  . LYS E  159 ? 1.5494 1.5271 1.3172 -0.1090 0.1956  -0.1054 159 LYS E NZ  
8805  N N   . LYS E  160 ? 1.4837 1.5290 1.2040 -0.1207 0.1575  -0.1042 160 LYS E N   
8806  C CA  . LYS E  160 ? 1.6199 1.6702 1.3245 -0.1296 0.1609  -0.1092 160 LYS E CA  
8807  C C   . LYS E  160 ? 1.7139 1.7586 1.4133 -0.1313 0.1675  -0.1095 160 LYS E C   
8808  O O   . LYS E  160 ? 1.6776 1.7282 1.3726 -0.1285 0.1639  -0.1044 160 LYS E O   
8809  C CB  . LYS E  160 ? 1.5424 1.6089 1.2370 -0.1307 0.1522  -0.1063 160 LYS E CB  
8810  C CG  . LYS E  160 ? 1.5151 1.5882 1.1928 -0.1397 0.1548  -0.1107 160 LYS E CG  
8811  C CD  . LYS E  160 ? 1.6030 1.6926 1.2718 -0.1404 0.1458  -0.1073 160 LYS E CD  
8812  C CE  . LYS E  160 ? 1.6716 1.7665 1.3456 -0.1394 0.1400  -0.1077 160 LYS E CE  
8813  N NZ  . LYS E  160 ? 1.7266 1.8378 1.3907 -0.1419 0.1323  -0.1058 160 LYS E NZ  
8814  N N   . GLY E  161 ? 1.7551 1.7882 1.4553 -0.1358 0.1773  -0.1154 161 GLY E N   
8815  C CA  . GLY E  161 ? 1.7051 1.7316 1.4005 -0.1380 0.1846  -0.1165 161 GLY E CA  
8816  C C   . GLY E  161 ? 1.7758 1.7997 1.4782 -0.1301 0.1830  -0.1096 161 GLY E C   
8817  O O   . GLY E  161 ? 1.7287 1.7576 1.4223 -0.1305 0.1821  -0.1069 161 GLY E O   
8818  N N   . ASN E  162 ? 1.7277 1.7437 1.4458 -0.1229 0.1826  -0.1066 162 ASN E N   
8819  C CA  . ASN E  162 ? 1.7989 1.8109 1.5253 -0.1153 0.1818  -0.1003 162 ASN E CA  
8820  C C   . ASN E  162 ? 1.7525 1.7759 1.4792 -0.1091 0.1713  -0.0929 162 ASN E C   
8821  O O   . ASN E  162 ? 1.7638 1.7875 1.4916 -0.1044 0.1700  -0.0877 162 ASN E O   
8822  C CB  . ASN E  162 ? 1.9609 1.9678 1.6805 -0.1181 0.1891  -0.1014 162 ASN E CB  
8823  C CG  . ASN E  162 ? 2.0804 2.0721 1.8105 -0.1172 0.1982  -0.1037 162 ASN E CG  
8824  O OD1 . ASN E  162 ? 2.3524 2.3382 2.0788 -0.1191 0.2049  -0.1048 162 ASN E OD1 
8825  N ND2 . ASN E  162 ? 1.9053 1.8905 1.6487 -0.1142 0.1986  -0.1044 162 ASN E ND2 
8826  N N   . SER E  163 ? 1.7345 1.7669 1.4603 -0.1089 0.1642  -0.0923 163 SER E N   
8827  C CA  . SER E  163 ? 1.7351 1.7784 1.4616 -0.1031 0.1544  -0.0854 163 SER E CA  
8828  C C   . SER E  163 ? 1.5322 1.5795 1.2662 -0.1000 0.1477  -0.0843 163 SER E C   
8829  O O   . SER E  163 ? 1.4585 1.5099 1.1876 -0.1051 0.1470  -0.0887 163 SER E O   
8830  C CB  . SER E  163 ? 1.6704 1.7262 1.3812 -0.1073 0.1511  -0.0846 163 SER E CB  
8831  O OG  . SER E  163 ? 1.5024 1.5676 1.2144 -0.1011 0.1426  -0.0772 163 SER E OG  
8832  N N   . TYR E  164 ? 1.2493 1.2953 0.9950 -0.0917 0.1429  -0.0786 164 TYR E N   
8833  C CA  . TYR E  164 ? 1.2882 1.3390 1.0408 -0.0880 0.1358  -0.0765 164 TYR E CA  
8834  C C   . TYR E  164 ? 1.2297 1.2881 0.9851 -0.0808 0.1278  -0.0688 164 TYR E C   
8835  O O   . TYR E  164 ? 0.9603 1.0133 0.7271 -0.0740 0.1266  -0.0647 164 TYR E O   
8836  C CB  . TYR E  164 ? 1.3616 1.4013 1.1284 -0.0852 0.1386  -0.0779 164 TYR E CB  
8837  C CG  . TYR E  164 ? 1.2362 1.2799 1.0080 -0.0838 0.1329  -0.0780 164 TYR E CG  
8838  C CD1 . TYR E  164 ? 1.1439 1.1830 0.9172 -0.0883 0.1364  -0.0837 164 TYR E CD1 
8839  C CD2 . TYR E  164 ? 1.1783 1.2301 0.9533 -0.0781 0.1241  -0.0724 164 TYR E CD2 
8840  C CE1 . TYR E  164 ? 1.1025 1.1451 0.8803 -0.0871 0.1313  -0.0838 164 TYR E CE1 
8841  C CE2 . TYR E  164 ? 1.1603 1.2156 0.9396 -0.0770 0.1191  -0.0725 164 TYR E CE2 
8842  C CZ  . TYR E  164 ? 1.1923 1.2431 0.9729 -0.0815 0.1226  -0.0782 164 TYR E CZ  
8843  O OH  . TYR E  164 ? 1.1469 1.2010 0.9317 -0.0804 0.1177  -0.0783 164 TYR E OH  
8844  N N   . PRO E  165 ? 1.0935 1.1645 0.8385 -0.0825 0.1226  -0.0669 165 PRO E N   
8845  C CA  . PRO E  165 ? 1.2050 1.2845 0.9513 -0.0762 0.1151  -0.0595 165 PRO E CA  
8846  C C   . PRO E  165 ? 1.1964 1.2789 0.9516 -0.0715 0.1084  -0.0571 165 PRO E C   
8847  O O   . PRO E  165 ? 1.0726 1.1555 0.8282 -0.0748 0.1081  -0.0613 165 PRO E O   
8848  C CB  . PRO E  165 ? 1.0706 1.1628 0.8022 -0.0810 0.1124  -0.0594 165 PRO E CB  
8849  C CG  . PRO E  165 ? 1.2968 1.3856 1.0190 -0.0898 0.1195  -0.0666 165 PRO E CG  
8850  C CD  . PRO E  165 ? 1.0238 1.1018 0.7548 -0.0908 0.1239  -0.0716 165 PRO E CD  
8851  N N   . LYS E  166 ? 0.9658 1.0504 0.7281 -0.0640 0.1033  -0.0507 166 LYS E N   
8852  C CA  . LYS E  166 ? 1.0829 1.1712 0.8529 -0.0595 0.0967  -0.0481 166 LYS E CA  
8853  C C   . LYS E  166 ? 1.2065 1.3061 0.9683 -0.0638 0.0922  -0.0500 166 LYS E C   
8854  O O   . LYS E  166 ? 1.0979 1.2079 0.8502 -0.0655 0.0893  -0.0479 166 LYS E O   
8855  C CB  . LYS E  166 ? 1.0412 1.1327 0.8168 -0.0518 0.0915  -0.0406 166 LYS E CB  
8856  C CG  . LYS E  166 ? 1.1645 1.2633 0.9443 -0.0481 0.0838  -0.0377 166 LYS E CG  
8857  C CD  . LYS E  166 ? 1.2056 1.3089 0.9894 -0.0411 0.0789  -0.0304 166 LYS E CD  
8858  C CE  . LYS E  166 ? 1.3368 1.4296 1.1329 -0.0351 0.0804  -0.0280 166 LYS E CE  
8859  N NZ  . LYS E  166 ? 1.5097 1.6068 1.3102 -0.0282 0.0755  -0.0211 166 LYS E NZ  
8860  N N   . LEU E  167 ? 1.2567 1.3543 1.0223 -0.0656 0.0917  -0.0537 167 LEU E N   
8861  C CA  . LEU E  167 ? 1.1396 1.2476 0.8985 -0.0696 0.0875  -0.0557 167 LEU E CA  
8862  C C   . LEU E  167 ? 0.9918 1.1058 0.7574 -0.0637 0.0797  -0.0509 167 LEU E C   
8863  O O   . LEU E  167 ? 0.9167 1.0243 0.6934 -0.0578 0.0786  -0.0482 167 LEU E O   
8864  C CB  . LEU E  167 ? 0.9953 1.0981 0.7530 -0.0759 0.0921  -0.0631 167 LEU E CB  
8865  C CG  . LEU E  167 ? 1.0202 1.1207 0.7853 -0.0755 0.0902  -0.0654 167 LEU E CG  
8866  C CD1 . LEU E  167 ? 1.0430 1.1345 0.8079 -0.0814 0.0975  -0.0725 167 LEU E CD1 
8867  C CD2 . LEU E  167 ? 1.0808 1.1766 0.8592 -0.0676 0.0867  -0.0609 167 LEU E CD2 
8868  N N   . SER E  168 ? 1.0173 1.1437 0.7762 -0.0653 0.0743  -0.0498 168 SER E N   
8869  C CA  . SER E  168 ? 1.0355 1.1684 0.8001 -0.0598 0.0670  -0.0451 168 SER E CA  
8870  C C   . SER E  168 ? 1.1140 1.2583 0.8722 -0.0637 0.0625  -0.0468 168 SER E C   
8871  O O   . SER E  168 ? 1.3231 1.4790 1.0746 -0.0641 0.0585  -0.0436 168 SER E O   
8872  C CB  . SER E  168 ? 1.1434 1.2808 0.9089 -0.0539 0.0637  -0.0379 168 SER E CB  
8873  O OG  . SER E  168 ? 1.2801 1.4191 1.0544 -0.0474 0.0582  -0.0335 168 SER E OG  
8874  N N   . LYS E  169 ? 1.0648 1.2059 0.8257 -0.0666 0.0634  -0.0516 169 LYS E N   
8875  C CA  . LYS E  169 ? 1.0104 1.1613 0.7666 -0.0703 0.0594  -0.0535 169 LYS E CA  
8876  C C   . LYS E  169 ? 1.0549 1.2069 0.8203 -0.0648 0.0539  -0.0506 169 LYS E C   
8877  O O   . LYS E  169 ? 1.1130 1.2557 0.8884 -0.0602 0.0547  -0.0496 169 LYS E O   
8878  C CB  . LYS E  169 ? 0.9609 1.1076 0.7129 -0.0779 0.0644  -0.0613 169 LYS E CB  
8879  C CG  . LYS E  169 ? 1.1342 1.2890 0.8727 -0.0855 0.0658  -0.0647 169 LYS E CG  
8880  C CD  . LYS E  169 ? 1.1676 1.3369 0.9011 -0.0869 0.0591  -0.0631 169 LYS E CD  
8881  C CE  . LYS E  169 ? 1.2706 1.4474 0.9912 -0.0957 0.0609  -0.0678 169 LYS E CE  
8882  N NZ  . LYS E  169 ? 1.3706 1.5487 1.0830 -0.0978 0.0638  -0.0667 169 LYS E NZ  
8883  N N   . SER E  170 ? 1.0792 1.2429 0.8412 -0.0654 0.0482  -0.0493 170 SER E N   
8884  C CA  . SER E  170 ? 1.0489 1.2144 0.8188 -0.0608 0.0430  -0.0468 170 SER E CA  
8885  C C   . SER E  170 ? 0.9425 1.1190 0.7072 -0.0648 0.0391  -0.0487 170 SER E C   
8886  O O   . SER E  170 ? 0.9848 1.1726 0.7414 -0.0672 0.0366  -0.0473 170 SER E O   
8887  C CB  . SER E  170 ? 1.1141 1.2825 0.8893 -0.0531 0.0387  -0.0394 170 SER E CB  
8888  O OG  . SER E  170 ? 1.3359 1.5152 1.1034 -0.0536 0.0363  -0.0358 170 SER E OG  
8889  N N   . TYR E  171 ? 0.9912 1.1643 0.7607 -0.0655 0.0387  -0.0519 171 TYR E N   
8890  C CA  . TYR E  171 ? 0.9561 1.1385 0.7217 -0.0694 0.0353  -0.0542 171 TYR E CA  
8891  C C   . TYR E  171 ? 0.9037 1.0905 0.6762 -0.0637 0.0291  -0.0499 171 TYR E C   
8892  O O   . TYR E  171 ? 0.9061 1.0852 0.6879 -0.0582 0.0287  -0.0477 171 TYR E O   
8893  C CB  . TYR E  171 ? 0.9877 1.1634 0.7527 -0.0751 0.0397  -0.0614 171 TYR E CB  
8894  C CG  . TYR E  171 ? 0.8982 1.0800 0.6633 -0.0773 0.0362  -0.0635 171 TYR E CG  
8895  C CD1 . TYR E  171 ? 0.8844 1.0769 0.6404 -0.0835 0.0350  -0.0663 171 TYR E CD1 
8896  C CD2 . TYR E  171 ? 0.9418 1.1189 0.7161 -0.0732 0.0341  -0.0627 171 TYR E CD2 
8897  C CE1 . TYR E  171 ? 0.9901 1.1882 0.7465 -0.0854 0.0319  -0.0682 171 TYR E CE1 
8898  C CE2 . TYR E  171 ? 0.9418 1.1243 0.7163 -0.0751 0.0311  -0.0646 171 TYR E CE2 
8899  C CZ  . TYR E  171 ? 1.0398 1.2326 0.8054 -0.0812 0.0300  -0.0674 171 TYR E CZ  
8900  O OH  . TYR E  171 ? 1.0309 1.2291 0.7969 -0.0831 0.0271  -0.0694 171 TYR E OH  
8901  N N   . ILE E  172 ? 0.8871 1.0866 0.6552 -0.0651 0.0244  -0.0486 172 ILE E N   
8902  C CA  . ILE E  172 ? 0.9519 1.1564 0.7260 -0.0603 0.0187  -0.0448 172 ILE E CA  
8903  C C   . ILE E  172 ? 0.9685 1.1765 0.7419 -0.0644 0.0173  -0.0491 172 ILE E C   
8904  O O   . ILE E  172 ? 0.9515 1.1665 0.7168 -0.0707 0.0177  -0.0526 172 ILE E O   
8905  C CB  . ILE E  172 ? 0.8847 1.1014 0.6564 -0.0571 0.0137  -0.0384 172 ILE E CB  
8906  C CG1 . ILE E  172 ? 0.9928 1.2133 0.7717 -0.0515 0.0084  -0.0344 172 ILE E CG1 
8907  C CG2 . ILE E  172 ? 1.1595 1.3884 0.9206 -0.0634 0.0127  -0.0400 172 ILE E CG2 
8908  C CD1 . ILE E  172 ? 1.0500 1.2724 0.8334 -0.0444 0.0057  -0.0271 172 ILE E CD1 
8909  N N   . ASN E  173 ? 0.9238 1.1268 0.7055 -0.0608 0.0157  -0.0488 173 ASN E N   
8910  C CA  . ASN E  173 ? 0.8562 1.0608 0.6381 -0.0642 0.0147  -0.0529 173 ASN E CA  
8911  C C   . ASN E  173 ? 1.0580 1.2771 0.8360 -0.0655 0.0095  -0.0512 173 ASN E C   
8912  O O   . ASN E  173 ? 1.0016 1.2250 0.7845 -0.0606 0.0049  -0.0469 173 ASN E O   
8913  C CB  . ASN E  173 ? 0.9272 1.1228 0.7191 -0.0598 0.0141  -0.0525 173 ASN E CB  
8914  C CG  . ASN E  173 ? 1.0304 1.2253 0.8227 -0.0637 0.0143  -0.0573 173 ASN E CG  
8915  O OD1 . ASN E  173 ? 1.0353 1.2369 0.8208 -0.0697 0.0148  -0.0610 173 ASN E OD1 
8916  N ND2 . ASN E  173 ? 0.9249 1.1119 0.7253 -0.0604 0.0140  -0.0572 173 ASN E ND2 
8917  N N   . ASP E  174 ? 1.1820 1.4085 0.9509 -0.0723 0.0104  -0.0547 174 ASP E N   
8918  C CA  . ASP E  174 ? 1.1684 1.4093 0.9329 -0.0744 0.0057  -0.0536 174 ASP E CA  
8919  C C   . ASP E  174 ? 1.1782 1.4197 0.9432 -0.0784 0.0055  -0.0585 174 ASP E C   
8920  O O   . ASP E  174 ? 1.3909 1.6438 1.1513 -0.0821 0.0026  -0.0594 174 ASP E O   
8921  C CB  . ASP E  174 ? 1.2981 1.5478 1.0521 -0.0800 0.0065  -0.0545 174 ASP E CB  
8922  C CG  . ASP E  174 ? 1.5059 1.7500 1.2539 -0.0877 0.0123  -0.0619 174 ASP E CG  
8923  O OD1 . ASP E  174 ? 1.5897 1.8393 1.3331 -0.0937 0.0121  -0.0664 174 ASP E OD1 
8924  O OD2 . ASP E  174 ? 1.5258 1.7596 1.2738 -0.0877 0.0172  -0.0634 174 ASP E OD2 
8925  N N   . LYS E  175 ? 1.1450 1.3744 0.9158 -0.0777 0.0085  -0.0616 175 LYS E N   
8926  C CA  . LYS E  175 ? 1.0910 1.3198 0.8636 -0.0806 0.0083  -0.0658 175 LYS E CA  
8927  C C   . LYS E  175 ? 1.1459 1.3765 0.9263 -0.0744 0.0034  -0.0615 175 LYS E C   
8928  O O   . LYS E  175 ? 1.1604 1.3911 0.9451 -0.0681 0.0009  -0.0558 175 LYS E O   
8929  C CB  . LYS E  175 ? 0.9810 1.1959 0.7563 -0.0829 0.0141  -0.0711 175 LYS E CB  
8930  C CG  . LYS E  175 ? 1.0104 1.2212 0.7790 -0.0885 0.0199  -0.0754 175 LYS E CG  
8931  C CD  . LYS E  175 ? 0.9030 1.1226 0.6623 -0.0967 0.0206  -0.0803 175 LYS E CD  
8932  C CE  . LYS E  175 ? 0.8828 1.0969 0.6357 -0.1026 0.0271  -0.0853 175 LYS E CE  
8933  N NZ  . LYS E  175 ? 1.1914 1.4131 0.9351 -0.1112 0.0283  -0.0907 175 LYS E NZ  
8934  N N   . GLY E  176 ? 0.9203 1.1522 0.7023 -0.0764 0.0022  -0.0643 176 GLY E N   
8935  C CA  . GLY E  176 ? 1.1458 1.3786 0.9351 -0.0710 -0.0020 -0.0609 176 GLY E CA  
8936  C C   . GLY E  176 ? 1.1446 1.3641 0.9410 -0.0689 0.0004  -0.0627 176 GLY E C   
8937  O O   . GLY E  176 ? 1.1723 1.3910 0.9742 -0.0659 -0.0022 -0.0615 176 GLY E O   
8938  N N   . LYS E  177 ? 1.1039 1.3131 0.9003 -0.0705 0.0055  -0.0656 177 LYS E N   
8939  C CA  . LYS E  177 ? 0.9332 1.1295 0.7362 -0.0690 0.0083  -0.0674 177 LYS E CA  
8940  C C   . LYS E  177 ? 0.8614 1.0479 0.6667 -0.0667 0.0120  -0.0663 177 LYS E C   
8941  O O   . LYS E  177 ? 0.9560 1.1450 0.7562 -0.0682 0.0136  -0.0660 177 LYS E O   
8942  C CB  . LYS E  177 ? 0.8682 1.0615 0.6687 -0.0754 0.0119  -0.0739 177 LYS E CB  
8943  C CG  . LYS E  177 ? 0.8965 1.0918 0.6886 -0.0822 0.0160  -0.0783 177 LYS E CG  
8944  C CD  . LYS E  177 ? 0.9632 1.1578 0.7524 -0.0889 0.0190  -0.0848 177 LYS E CD  
8945  C CE  . LYS E  177 ? 1.1879 1.3937 0.9752 -0.0904 0.0143  -0.0849 177 LYS E CE  
8946  N NZ  . LYS E  177 ? 1.2207 1.4400 1.0007 -0.0924 0.0112  -0.0832 177 LYS E NZ  
8947  N N   . GLU E  178 ? 0.8262 1.0019 0.6392 -0.0632 0.0133  -0.0657 178 GLU E N   
8948  C CA  . GLU E  178 ? 0.7899 0.9558 0.6061 -0.0610 0.0170  -0.0648 178 GLU E CA  
8949  C C   . GLU E  178 ? 0.8220 0.9848 0.6324 -0.0671 0.0228  -0.0697 178 GLU E C   
8950  O O   . GLU E  178 ? 0.8433 1.0078 0.6495 -0.0729 0.0247  -0.0747 178 GLU E O   
8951  C CB  . GLU E  178 ? 0.7567 0.9116 0.5819 -0.0575 0.0178  -0.0643 178 GLU E CB  
8952  C CG  . GLU E  178 ? 1.1255 1.2823 0.9565 -0.0517 0.0125  -0.0597 178 GLU E CG  
8953  C CD  . GLU E  178 ? 1.1638 1.3103 1.0028 -0.0493 0.0132  -0.0597 178 GLU E CD  
8954  O OE1 . GLU E  178 ? 1.1440 1.2862 0.9834 -0.0530 0.0159  -0.0639 178 GLU E OE1 
8955  O OE2 . GLU E  178 ? 1.2196 1.3626 1.0646 -0.0437 0.0111  -0.0556 178 GLU E OE2 
8956  N N   . VAL E  179 ? 0.6786 0.8366 0.4887 -0.0659 0.0257  -0.0685 179 VAL E N   
8957  C CA  . VAL E  179 ? 0.7932 0.9469 0.5984 -0.0714 0.0318  -0.0732 179 VAL E CA  
8958  C C   . VAL E  179 ? 0.7966 0.9368 0.6085 -0.0692 0.0364  -0.0733 179 VAL E C   
8959  O O   . VAL E  179 ? 0.7056 0.8427 0.5218 -0.0640 0.0356  -0.0689 179 VAL E O   
8960  C CB  . VAL E  179 ? 0.7434 0.9047 0.5402 -0.0734 0.0319  -0.0723 179 VAL E CB  
8961  C CG1 . VAL E  179 ? 0.7660 0.9204 0.5589 -0.0781 0.0388  -0.0765 179 VAL E CG1 
8962  C CG2 . VAL E  179 ? 0.8111 0.9857 0.6004 -0.0772 0.0283  -0.0732 179 VAL E CG2 
8963  N N   . LEU E  180 ? 0.7012 0.8338 0.5144 -0.0731 0.0414  -0.0781 180 LEU E N   
8964  C CA  . LEU E  180 ? 0.6066 0.7266 0.4263 -0.0716 0.0463  -0.0786 180 LEU E CA  
8965  C C   . LEU E  180 ? 0.6479 0.7653 0.4627 -0.0744 0.0515  -0.0802 180 LEU E C   
8966  O O   . LEU E  180 ? 0.8156 0.9342 0.6233 -0.0808 0.0554  -0.0852 180 LEU E O   
8967  C CB  . LEU E  180 ? 0.6049 0.7176 0.4282 -0.0748 0.0500  -0.0830 180 LEU E CB  
8968  C CG  . LEU E  180 ? 0.6204 0.7199 0.4510 -0.0737 0.0557  -0.0836 180 LEU E CG  
8969  C CD1 . LEU E  180 ? 0.5682 0.6630 0.4085 -0.0665 0.0524  -0.0782 180 LEU E CD1 
8970  C CD2 . LEU E  180 ? 0.6088 0.7022 0.4408 -0.0783 0.0604  -0.0888 180 LEU E CD2 
8971  N N   . VAL E  181 ? 0.6663 0.7802 0.4845 -0.0698 0.0515  -0.0762 181 VAL E N   
8972  C CA  . VAL E  181 ? 0.6420 0.7527 0.4562 -0.0719 0.0565  -0.0773 181 VAL E CA  
8973  C C   . VAL E  181 ? 0.7136 0.8110 0.5358 -0.0702 0.0619  -0.0778 181 VAL E C   
8974  O O   . VAL E  181 ? 0.7264 0.8189 0.5575 -0.0645 0.0599  -0.0739 181 VAL E O   
8975  C CB  . VAL E  181 ? 0.5787 0.6957 0.3901 -0.0682 0.0531  -0.0724 181 VAL E CB  
8976  C CG1 . VAL E  181 ? 0.7321 0.8468 0.5377 -0.0713 0.0583  -0.0740 181 VAL E CG1 
8977  C CG2 . VAL E  181 ? 0.6067 0.7371 0.4118 -0.0687 0.0471  -0.0708 181 VAL E CG2 
8978  N N   . LEU E  182 ? 0.7370 0.8287 0.5562 -0.0755 0.0688  -0.0827 182 LEU E N   
8979  C CA  . LEU E  182 ? 0.7435 0.8227 0.5702 -0.0744 0.0746  -0.0833 182 LEU E CA  
8980  C C   . LEU E  182 ? 0.6916 0.7681 0.5144 -0.0756 0.0793  -0.0837 182 LEU E C   
8981  O O   . LEU E  182 ? 0.8133 0.8957 0.6259 -0.0803 0.0806  -0.0863 182 LEU E O   
8982  C CB  . LEU E  182 ? 0.5584 0.6311 0.3871 -0.0790 0.0798  -0.0887 182 LEU E CB  
8983  C CG  . LEU E  182 ? 0.7103 0.7833 0.5443 -0.0777 0.0762  -0.0885 182 LEU E CG  
8984  C CD1 . LEU E  182 ? 0.8656 0.9458 0.6916 -0.0836 0.0757  -0.0930 182 LEU E CD1 
8985  C CD2 . LEU E  182 ? 0.6928 0.7539 0.5368 -0.0766 0.0807  -0.0892 182 LEU E CD2 
8986  N N   . TRP E  183 ? 0.7179 0.7856 0.5486 -0.0715 0.0817  -0.0811 183 TRP E N   
8987  C CA  . TRP E  183 ? 0.7686 0.8323 0.5968 -0.0724 0.0867  -0.0814 183 TRP E CA  
8988  C C   . TRP E  183 ? 0.6031 0.6542 0.4416 -0.0701 0.0920  -0.0811 183 TRP E C   
8989  O O   . TRP E  183 ? 0.6720 0.7185 0.5200 -0.0668 0.0905  -0.0795 183 TRP E O   
8990  C CB  . TRP E  183 ? 0.7791 0.8495 0.6044 -0.0683 0.0821  -0.0763 183 TRP E CB  
8991  C CG  . TRP E  183 ? 0.6627 0.7302 0.4981 -0.0607 0.0781  -0.0705 183 TRP E CG  
8992  C CD1 . TRP E  183 ? 0.6617 0.7212 0.5042 -0.0569 0.0808  -0.0679 183 TRP E CD1 
8993  C CD2 . TRP E  183 ? 0.7166 0.7892 0.5560 -0.0562 0.0709  -0.0667 183 TRP E CD2 
8994  N NE1 . TRP E  183 ? 0.6567 0.7162 0.5073 -0.0505 0.0756  -0.0628 183 TRP E NE1 
8995  C CE2 . TRP E  183 ? 0.7619 0.8292 0.6106 -0.0500 0.0695  -0.0620 183 TRP E CE2 
8996  C CE3 . TRP E  183 ? 0.7385 0.8197 0.5746 -0.0570 0.0656  -0.0669 183 TRP E CE3 
8997  C CZ2 . TRP E  183 ? 0.7360 0.8061 0.5904 -0.0447 0.0632  -0.0577 183 TRP E CZ2 
8998  C CZ3 . TRP E  183 ? 0.7657 0.8495 0.6077 -0.0516 0.0594  -0.0626 183 TRP E CZ3 
8999  C CH2 . TRP E  183 ? 0.7288 0.8070 0.5797 -0.0456 0.0583  -0.0581 183 TRP E CH2 
9000  N N   . GLY E  184 ? 0.6592 0.7049 0.4960 -0.0718 0.0980  -0.0824 184 GLY E N   
9001  C CA  . GLY E  184 ? 0.6535 0.6872 0.5001 -0.0699 0.1036  -0.0823 184 GLY E CA  
9002  C C   . GLY E  184 ? 0.7398 0.7704 0.5881 -0.0667 0.1053  -0.0791 184 GLY E C   
9003  O O   . GLY E  184 ? 0.6864 0.7222 0.5257 -0.0683 0.1053  -0.0790 184 GLY E O   
9004  N N   . ILE E  185 ? 0.7631 0.7853 0.6229 -0.0621 0.1068  -0.0762 185 ILE E N   
9005  C CA  . ILE E  185 ? 0.5983 0.6160 0.4612 -0.0591 0.1094  -0.0734 185 ILE E CA  
9006  C C   . ILE E  185 ? 0.7155 0.7216 0.5841 -0.0613 0.1181  -0.0764 185 ILE E C   
9007  O O   . ILE E  185 ? 0.7377 0.7372 0.6167 -0.0595 0.1193  -0.0759 185 ILE E O   
9008  C CB  . ILE E  185 ? 0.6669 0.6844 0.5392 -0.0516 0.1037  -0.0671 185 ILE E CB  
9009  C CG1 . ILE E  185 ? 0.6697 0.6979 0.5375 -0.0493 0.0952  -0.0642 185 ILE E CG1 
9010  C CG2 . ILE E  185 ? 0.7003 0.7137 0.5751 -0.0487 0.1063  -0.0643 185 ILE E CG2 
9011  C CD1 . ILE E  185 ? 0.6770 0.7138 0.5330 -0.0513 0.0938  -0.0642 185 ILE E CD1 
9012  N N   . HIS E  186 ? 0.7526 0.7565 0.6145 -0.0652 0.1242  -0.0794 186 HIS E N   
9013  C CA  . HIS E  186 ? 0.8437 0.8366 0.7104 -0.0677 0.1333  -0.0826 186 HIS E CA  
9014  C C   . HIS E  186 ? 0.7848 0.7707 0.6610 -0.0627 0.1354  -0.0786 186 HIS E C   
9015  O O   . HIS E  186 ? 0.8685 0.8574 0.7415 -0.0604 0.1335  -0.0757 186 HIS E O   
9016  C CB  . HIS E  186 ? 0.8435 0.8366 0.6985 -0.0750 0.1397  -0.0883 186 HIS E CB  
9017  C CG  . HIS E  186 ? 0.9476 0.9293 0.8071 -0.0777 0.1496  -0.0917 186 HIS E CG  
9018  N ND1 . HIS E  186 ? 0.9329 0.9105 0.7898 -0.0786 0.1550  -0.0921 186 HIS E ND1 
9019  C CD2 . HIS E  186 ? 0.8867 0.8600 0.7535 -0.0796 0.1552  -0.0947 186 HIS E CD2 
9020  C CE1 . HIS E  186 ? 1.0216 0.9888 0.8841 -0.0809 0.1637  -0.0954 186 HIS E CE1 
9021  N NE2 . HIS E  186 ? 0.8919 0.8562 0.7605 -0.0815 0.1640  -0.0969 186 HIS E NE2 
9022  N N   . HIS E  187 ? 0.8255 0.8021 0.7136 -0.0612 0.1393  -0.0784 187 HIS E N   
9023  C CA  . HIS E  187 ? 0.8392 0.8083 0.7373 -0.0568 0.1421  -0.0749 187 HIS E CA  
9024  C C   . HIS E  187 ? 0.9965 0.9556 0.8969 -0.0606 0.1524  -0.0789 187 HIS E C   
9025  O O   . HIS E  187 ? 0.9851 0.9375 0.8935 -0.0615 0.1564  -0.0805 187 HIS E O   
9026  C CB  . HIS E  187 ? 0.8952 0.8619 0.8069 -0.0511 0.1376  -0.0703 187 HIS E CB  
9027  C CG  . HIS E  187 ? 0.8424 0.8181 0.7525 -0.0475 0.1279  -0.0666 187 HIS E CG  
9028  N ND1 . HIS E  187 ? 0.8474 0.8272 0.7579 -0.0427 0.1227  -0.0619 187 HIS E ND1 
9029  C CD2 . HIS E  187 ? 0.8582 0.8394 0.7664 -0.0480 0.1226  -0.0671 187 HIS E CD2 
9030  C CE1 . HIS E  187 ? 0.9559 0.9432 0.8649 -0.0405 0.1148  -0.0596 187 HIS E CE1 
9031  N NE2 . HIS E  187 ? 0.9556 0.9440 0.8632 -0.0436 0.1145  -0.0627 187 HIS E NE2 
9032  N N   . PRO E  188 ? 0.9705 0.9286 0.8638 -0.0630 0.1571  -0.0805 188 PRO E N   
9033  C CA  . PRO E  188 ? 0.9853 0.9339 0.8796 -0.0669 0.1675  -0.0846 188 PRO E CA  
9034  C C   . PRO E  188 ? 0.9895 0.9282 0.8997 -0.0629 0.1713  -0.0819 188 PRO E C   
9035  O O   . PRO E  188 ? 0.9623 0.9016 0.8816 -0.0568 0.1659  -0.0764 188 PRO E O   
9036  C CB  . PRO E  188 ? 0.9674 0.9183 0.8521 -0.0682 0.1693  -0.0848 188 PRO E CB  
9037  C CG  . PRO E  188 ? 0.9014 0.8644 0.7760 -0.0677 0.1608  -0.0830 188 PRO E CG  
9038  C CD  . PRO E  188 ? 0.8574 0.8236 0.7408 -0.0622 0.1528  -0.0786 188 PRO E CD  
9039  N N   . SER E  189 ? 1.0389 0.9684 0.9524 -0.0665 0.1807  -0.0858 189 SER E N   
9040  C CA  . SER E  189 ? 1.0091 0.9289 0.9381 -0.0631 0.1852  -0.0835 189 SER E CA  
9041  C C   . SER E  189 ? 1.0401 0.9556 0.9731 -0.0601 0.1882  -0.0807 189 SER E C   
9042  O O   . SER E  189 ? 1.0606 0.9723 1.0064 -0.0548 0.1869  -0.0760 189 SER E O   
9043  C CB  . SER E  189 ? 1.0324 0.9438 0.9642 -0.0680 0.1945  -0.0886 189 SER E CB  
9044  O OG  . SER E  189 ? 1.1710 1.0805 1.0917 -0.0742 0.2018  -0.0942 189 SER E OG  
9045  N N   . THR E  190 ? 1.1659 1.0822 1.0876 -0.0638 0.1921  -0.0837 190 THR E N   
9046  C CA  . THR E  190 ? 1.1800 1.0921 1.1041 -0.0617 0.1958  -0.0816 190 THR E CA  
9047  C C   . THR E  190 ? 1.1273 1.0474 1.0386 -0.0618 0.1915  -0.0806 190 THR E C   
9048  O O   . THR E  190 ? 1.1567 1.0845 1.0552 -0.0656 0.1885  -0.0832 190 THR E O   
9049  C CB  . THR E  190 ? 1.2018 1.1038 1.1267 -0.0662 0.2076  -0.0863 190 THR E CB  
9050  O OG1 . THR E  190 ? 1.4233 1.3243 1.3419 -0.0669 0.2110  -0.0863 190 THR E OG1 
9051  C CG2 . THR E  190 ? 1.1366 1.0388 1.0516 -0.0736 0.2120  -0.0930 190 THR E CG2 
9052  N N   . SER E  191 ? 1.2064 1.1250 1.1218 -0.0576 0.1912  -0.0766 191 SER E N   
9053  C CA  . SER E  191 ? 1.2301 1.1557 1.1345 -0.0572 0.1876  -0.0750 191 SER E CA  
9054  C C   . SER E  191 ? 1.1834 1.1089 1.0737 -0.0642 0.1941  -0.0805 191 SER E C   
9055  O O   . SER E  191 ? 1.1530 1.0863 1.0308 -0.0656 0.1908  -0.0804 191 SER E O   
9056  C CB  . SER E  191 ? 1.0885 1.0110 1.0010 -0.0515 0.1872  -0.0699 191 SER E CB  
9057  O OG  . SER E  191 ? 1.3220 1.2342 1.2403 -0.0528 0.1967  -0.0716 191 SER E OG  
9058  N N   . ALA E  192 ? 1.2779 1.1945 1.1702 -0.0685 0.2035  -0.0852 192 ALA E N   
9059  C CA  . ALA E  192 ? 1.3869 1.3027 1.2659 -0.0759 0.2104  -0.0912 192 ALA E CA  
9060  C C   . ALA E  192 ? 1.3772 1.3007 1.2449 -0.0809 0.2070  -0.0951 192 ALA E C   
9061  O O   . ALA E  192 ? 1.2554 1.1847 1.1084 -0.0857 0.2071  -0.0979 192 ALA E O   
9062  C CB  . ALA E  192 ? 1.4737 1.3772 1.3591 -0.0790 0.2217  -0.0952 192 ALA E CB  
9063  N N   . ASP E  193 ? 1.4291 1.3530 1.3038 -0.0799 0.2040  -0.0951 193 ASP E N   
9064  C CA  . ASP E  193 ? 1.2310 1.1624 1.0965 -0.0840 0.2001  -0.0983 193 ASP E CA  
9065  C C   . ASP E  193 ? 1.1551 1.0990 1.0123 -0.0817 0.1899  -0.0947 193 ASP E C   
9066  O O   . ASP E  193 ? 1.0578 1.0096 0.9025 -0.0862 0.1874  -0.0976 193 ASP E O   
9067  C CB  . ASP E  193 ? 1.1958 1.1244 1.0719 -0.0826 0.1988  -0.0984 193 ASP E CB  
9068  C CG  . ASP E  193 ? 1.5527 1.4735 1.4288 -0.0888 0.2081  -0.1048 193 ASP E CG  
9069  O OD1 . ASP E  193 ? 1.5811 1.4938 1.4576 -0.0915 0.2172  -0.1076 193 ASP E OD1 
9070  O OD2 . ASP E  193 ? 1.7988 1.7217 1.6747 -0.0909 0.2064  -0.1071 193 ASP E OD2 
9071  N N   . GLN E  194 ? 1.1164 1.0619 0.9809 -0.0746 0.1842  -0.0884 194 GLN E N   
9072  C CA  . GLN E  194 ? 1.0634 1.0201 0.9218 -0.0715 0.1747  -0.0843 194 GLN E CA  
9073  C C   . GLN E  194 ? 1.1903 1.1528 1.0337 -0.0753 0.1755  -0.0856 194 GLN E C   
9074  O O   . GLN E  194 ? 1.2008 1.1730 1.0332 -0.0781 0.1709  -0.0867 194 GLN E O   
9075  C CB  . GLN E  194 ? 1.1363 1.0921 1.0061 -0.0634 0.1698  -0.0774 194 GLN E CB  
9076  C CG  . GLN E  194 ? 1.1095 1.0758 0.9734 -0.0599 0.1613  -0.0729 194 GLN E CG  
9077  C CD  . GLN E  194 ? 1.0891 1.0645 0.9501 -0.0596 0.1531  -0.0722 194 GLN E CD  
9078  O OE1 . GLN E  194 ? 1.0181 1.0030 0.8722 -0.0581 0.1466  -0.0695 194 GLN E OE1 
9079  N NE2 . GLN E  194 ? 0.9722 0.9448 0.8387 -0.0608 0.1536  -0.0746 194 GLN E NE2 
9080  N N   . GLN E  195 ? 1.4668 1.4236 1.3102 -0.0752 0.1813  -0.0853 195 GLN E N   
9081  C CA  . GLN E  195 ? 1.5487 1.5103 1.3781 -0.0787 0.1826  -0.0863 195 GLN E CA  
9082  C C   . GLN E  195 ? 1.5160 1.4781 1.3332 -0.0875 0.1882  -0.0934 195 GLN E C   
9083  O O   . GLN E  195 ? 1.4885 1.4580 1.2917 -0.0915 0.1870  -0.0947 195 GLN E O   
9084  C CB  . GLN E  195 ? 1.5771 1.5316 1.4101 -0.0763 0.1879  -0.0842 195 GLN E CB  
9085  C CG  . GLN E  195 ? 1.8161 1.7576 1.6581 -0.0778 0.1977  -0.0874 195 GLN E CG  
9086  C CD  . GLN E  195 ? 2.0854 2.0201 1.9329 -0.0744 0.2020  -0.0845 195 GLN E CD  
9087  O OE1 . GLN E  195 ? 1.9882 1.9124 1.8435 -0.0751 0.2101  -0.0865 195 GLN E OE1 
9088  N NE2 . GLN E  195 ? 2.1878 2.1286 2.0317 -0.0707 0.1968  -0.0798 195 GLN E NE2 
9089  N N   . SER E  196 ? 1.2947 1.2489 1.1172 -0.0907 0.1943  -0.0980 196 SER E N   
9090  C CA  . SER E  196 ? 1.1997 1.1535 1.0116 -0.0993 0.2000  -0.1052 196 SER E CA  
9091  C C   . SER E  196 ? 1.3827 1.3480 1.1857 -0.1019 0.1927  -0.1063 196 SER E C   
9092  O O   . SER E  196 ? 1.3617 1.3320 1.1511 -0.1087 0.1943  -0.1108 196 SER E O   
9093  C CB  . SER E  196 ? 1.1563 1.0987 0.9778 -0.1013 0.2080  -0.1093 196 SER E CB  
9094  O OG  . SER E  196 ? 1.3259 1.2683 1.1377 -0.1096 0.2131  -0.1165 196 SER E OG  
9095  N N   . LEU E  197 ? 1.3322 1.3018 1.1429 -0.0964 0.1847  -0.1021 197 LEU E N   
9096  C CA  . LEU E  197 ? 1.2101 1.1903 1.0143 -0.0982 0.1776  -0.1028 197 LEU E CA  
9097  C C   . LEU E  197 ? 1.2215 1.2138 1.0181 -0.0954 0.1688  -0.0980 197 LEU E C   
9098  O O   . LEU E  197 ? 1.0918 1.0938 0.8767 -0.0997 0.1656  -0.0999 197 LEU E O   
9099  C CB  . LEU E  197 ? 1.2489 1.2272 1.0652 -0.0945 0.1740  -0.1014 197 LEU E CB  
9100  C CG  . LEU E  197 ? 1.1213 1.0912 0.9420 -0.0988 0.1810  -0.1070 197 LEU E CG  
9101  C CD1 . LEU E  197 ? 1.0006 0.9674 0.8355 -0.0935 0.1776  -0.1040 197 LEU E CD1 
9102  C CD2 . LEU E  197 ? 1.0380 1.0138 0.8459 -0.1066 0.1819  -0.1129 197 LEU E CD2 
9103  N N   . TYR E  198 ? 1.2201 1.2122 1.0237 -0.0883 0.1652  -0.0917 198 TYR E N   
9104  C CA  . TYR E  198 ? 1.3339 1.3373 1.1321 -0.0849 0.1567  -0.0866 198 TYR E CA  
9105  C C   . TYR E  198 ? 1.4471 1.4424 1.2497 -0.0821 0.1619  -0.0845 198 TYR E C   
9106  O O   . TYR E  198 ? 1.3045 1.2909 1.1201 -0.0780 0.1643  -0.0829 198 TYR E O   
9107  C CB  . TYR E  198 ? 1.4134 1.4188 1.2229 -0.0773 0.1490  -0.0811 198 TYR E CB  
9108  C CG  . TYR E  198 ? 1.2155 1.2193 1.0314 -0.0779 0.1477  -0.0834 198 TYR E CG  
9109  C CD1 . TYR E  198 ? 1.1985 1.1931 1.0286 -0.0741 0.1497  -0.0823 198 TYR E CD1 
9110  C CD2 . TYR E  198 ? 1.1843 1.1959 0.9921 -0.0824 0.1447  -0.0866 198 TYR E CD2 
9111  C CE1 . TYR E  198 ? 1.1980 1.1910 1.0339 -0.0747 0.1486  -0.0842 198 TYR E CE1 
9112  C CE2 . TYR E  198 ? 1.1199 1.1297 0.9335 -0.0830 0.1438  -0.0887 198 TYR E CE2 
9113  C CZ  . TYR E  198 ? 1.2295 1.2299 1.0570 -0.0791 0.1458  -0.0874 198 TYR E CZ  
9114  O OH  . TYR E  198 ? 1.1571 1.1558 0.9905 -0.0795 0.1449  -0.0892 198 TYR E OH  
9115  N N   . GLN E  199 ? 1.3777 1.3763 1.1697 -0.0845 0.1635  -0.0843 199 GLN E N   
9116  C CA  . GLN E  199 ? 1.3849 1.3769 1.1797 -0.0820 0.1682  -0.0821 199 GLN E CA  
9117  C C   . GLN E  199 ? 1.3806 1.3721 1.1851 -0.0735 0.1637  -0.0750 199 GLN E C   
9118  O O   . GLN E  199 ? 1.4215 1.4069 1.2287 -0.0716 0.1680  -0.0733 199 GLN E O   
9119  C CB  . GLN E  199 ? 1.5439 1.5460 1.3219 -0.0869 0.1665  -0.0832 199 GLN E CB  
9120  C CG  . GLN E  199 ? 1.6371 1.6343 1.4061 -0.0931 0.1753  -0.0876 199 GLN E CG  
9121  C CD  . GLN E  199 ? 1.6887 1.6762 1.4654 -0.0893 0.1806  -0.0852 199 GLN E CD  
9122  O OE1 . GLN E  199 ? 1.7346 1.7240 1.5159 -0.0828 0.1762  -0.0791 199 GLN E OE1 
9123  N NE2 . GLN E  199 ? 1.5809 1.5576 1.3593 -0.0931 0.1902  -0.0900 199 GLN E NE2 
9124  N N   . ASN E  200 ? 1.4773 1.4748 1.2870 -0.0687 0.1554  -0.0710 200 ASN E N   
9125  C CA  . ASN E  200 ? 1.3861 1.3831 1.2060 -0.0607 0.1508  -0.0645 200 ASN E CA  
9126  C C   . ASN E  200 ? 1.3455 1.3331 1.1812 -0.0570 0.1523  -0.0640 200 ASN E C   
9127  O O   . ASN E  200 ? 1.3369 1.3225 1.1759 -0.0591 0.1530  -0.0673 200 ASN E O   
9128  C CB  . ASN E  200 ? 1.3609 1.3696 1.1779 -0.0573 0.1410  -0.0602 200 ASN E CB  
9129  C CG  . ASN E  200 ? 1.3546 1.3737 1.1561 -0.0618 0.1390  -0.0611 200 ASN E CG  
9130  O OD1 . ASN E  200 ? 1.4151 1.4326 1.2076 -0.0668 0.1448  -0.0642 200 ASN E OD1 
9131  N ND2 . ASN E  200 ? 1.3209 1.3507 1.1190 -0.0601 0.1310  -0.0583 200 ASN E ND2 
9132  N N   . ALA E  201 ? 1.3398 1.3219 1.1852 -0.0515 0.1531  -0.0599 201 ALA E N   
9133  C CA  . ALA E  201 ? 1.2999 1.2733 1.1606 -0.0479 0.1546  -0.0590 201 ALA E CA  
9134  C C   . ALA E  201 ? 1.3246 1.3026 1.1930 -0.0422 0.1459  -0.0546 201 ALA E C   
9135  O O   . ALA E  201 ? 1.3232 1.2982 1.2001 -0.0414 0.1449  -0.0553 201 ALA E O   
9136  C CB  . ALA E  201 ? 1.4706 1.4354 1.3386 -0.0451 0.1600  -0.0570 201 ALA E CB  
9137  N N   . ASP E  202 ? 1.4495 1.4349 1.3150 -0.0384 0.1397  -0.0499 202 ASP E N   
9138  C CA  . ASP E  202 ? 1.4407 1.4307 1.3126 -0.0331 0.1316  -0.0456 202 ASP E CA  
9139  C C   . ASP E  202 ? 1.3455 1.3469 1.2073 -0.0348 0.1252  -0.0458 202 ASP E C   
9140  O O   . ASP E  202 ? 1.4181 1.4268 1.2722 -0.0339 0.1220  -0.0431 202 ASP E O   
9141  C CB  . ASP E  202 ? 1.5782 1.5678 1.4559 -0.0270 0.1292  -0.0399 202 ASP E CB  
9142  C CG  . ASP E  202 ? 1.6415 1.6321 1.5298 -0.0213 0.1227  -0.0359 202 ASP E CG  
9143  O OD1 . ASP E  202 ? 1.5633 1.5491 1.4603 -0.0211 0.1230  -0.0372 202 ASP E OD1 
9144  O OD2 . ASP E  202 ? 1.6694 1.6653 1.5574 -0.0171 0.1174  -0.0315 202 ASP E OD2 
9145  N N   . THR E  203 ? 1.1479 1.1507 1.0100 -0.0373 0.1236  -0.0487 203 THR E N   
9146  C CA  . THR E  203 ? 1.0509 1.0643 0.9038 -0.0395 0.1181  -0.0495 203 THR E CA  
9147  C C   . THR E  203 ? 0.9424 0.9594 0.8020 -0.0355 0.1108  -0.0468 203 THR E C   
9148  O O   . THR E  203 ? 1.0083 1.0194 0.8798 -0.0315 0.1102  -0.0448 203 THR E O   
9149  C CB  . THR E  203 ? 1.0401 1.0534 0.8851 -0.0469 0.1223  -0.0559 203 THR E CB  
9150  O OG1 . THR E  203 ? 0.9650 0.9709 0.8192 -0.0474 0.1249  -0.0584 203 THR E OG1 
9151  C CG2 . THR E  203 ? 1.1090 1.1189 0.9462 -0.0515 0.1298  -0.0590 203 THR E CG2 
9152  N N   . TYR E  204 ? 0.9519 0.9788 0.8040 -0.0368 0.1053  -0.0468 204 TYR E N   
9153  C CA  . TYR E  204 ? 0.9850 1.0163 0.8420 -0.0336 0.0984  -0.0446 204 TYR E CA  
9154  C C   . TYR E  204 ? 1.0157 1.0563 0.8628 -0.0378 0.0952  -0.0472 204 TYR E C   
9155  O O   . TYR E  204 ? 0.9451 0.9912 0.7812 -0.0417 0.0964  -0.0488 204 TYR E O   
9156  C CB  . TYR E  204 ? 0.9220 0.9572 0.7827 -0.0272 0.0928  -0.0385 204 TYR E CB  
9157  C CG  . TYR E  204 ? 0.9106 0.9562 0.7608 -0.0274 0.0892  -0.0363 204 TYR E CG  
9158  C CD1 . TYR E  204 ? 0.9679 1.0231 0.8142 -0.0271 0.0828  -0.0352 204 TYR E CD1 
9159  C CD2 . TYR E  204 ? 0.9695 1.0155 0.8138 -0.0279 0.0923  -0.0351 204 TYR E CD2 
9160  C CE1 . TYR E  204 ? 1.0423 1.1074 0.8796 -0.0272 0.0795  -0.0328 204 TYR E CE1 
9161  C CE2 . TYR E  204 ? 1.0628 1.1187 0.8977 -0.0281 0.0890  -0.0327 204 TYR E CE2 
9162  C CZ  . TYR E  204 ? 1.1881 1.2536 1.0197 -0.0276 0.0826  -0.0315 204 TYR E CZ  
9163  O OH  . TYR E  204 ? 1.2401 1.3157 1.0629 -0.0277 0.0793  -0.0287 204 TYR E OH  
9164  N N   . VAL E  205 ? 0.8153 0.8578 0.6664 -0.0371 0.0911  -0.0476 205 VAL E N   
9165  C CA  . VAL E  205 ? 0.7859 0.8381 0.6289 -0.0402 0.0869  -0.0491 205 VAL E CA  
9166  C C   . VAL E  205 ? 0.8441 0.9012 0.6923 -0.0354 0.0794  -0.0453 205 VAL E C   
9167  O O   . VAL E  205 ? 0.8232 0.8745 0.6818 -0.0317 0.0783  -0.0437 205 VAL E O   
9168  C CB  . VAL E  205 ? 0.8375 0.8875 0.6775 -0.0464 0.0907  -0.0553 205 VAL E CB  
9169  C CG1 . VAL E  205 ? 0.8504 0.8880 0.6984 -0.0471 0.0975  -0.0578 205 VAL E CG1 
9170  C CG2 . VAL E  205 ? 0.8461 0.9011 0.6874 -0.0462 0.0852  -0.0557 205 VAL E CG2 
9171  N N   . PHE E  206 ? 0.8047 0.8725 0.6456 -0.0356 0.0742  -0.0439 206 PHE E N   
9172  C CA  . PHE E  206 ? 0.8172 0.8905 0.6621 -0.0311 0.0672  -0.0400 206 PHE E CA  
9173  C C   . PHE E  206 ? 0.9097 0.9922 0.7480 -0.0343 0.0633  -0.0420 206 PHE E C   
9174  O O   . PHE E  206 ? 0.7874 0.8774 0.6156 -0.0380 0.0633  -0.0432 206 PHE E O   
9175  C CB  . PHE E  206 ? 0.7791 0.8566 0.6238 -0.0262 0.0641  -0.0344 206 PHE E CB  
9176  C CG  . PHE E  206 ? 0.8795 0.9645 0.7261 -0.0221 0.0570  -0.0306 206 PHE E CG  
9177  C CD1 . PHE E  206 ? 0.8981 0.9943 0.7363 -0.0234 0.0532  -0.0296 206 PHE E CD1 
9178  C CD2 . PHE E  206 ? 0.9570 1.0378 0.8137 -0.0172 0.0541  -0.0279 206 PHE E CD2 
9179  C CE1 . PHE E  206 ? 0.9541 1.0569 0.7944 -0.0197 0.0470  -0.0260 206 PHE E CE1 
9180  C CE2 . PHE E  206 ? 0.8223 0.9096 0.6806 -0.0137 0.0480  -0.0246 206 PHE E CE2 
9181  C CZ  . PHE E  206 ? 1.0207 1.1188 0.8709 -0.0148 0.0445  -0.0236 206 PHE E CZ  
9182  N N   . VAL E  207 ? 0.8847 0.9667 0.7286 -0.0330 0.0600  -0.0422 207 VAL E N   
9183  C CA  . VAL E  207 ? 0.8087 0.8991 0.6476 -0.0357 0.0562  -0.0440 207 VAL E CA  
9184  C C   . VAL E  207 ? 0.8424 0.9379 0.6857 -0.0305 0.0494  -0.0395 207 VAL E C   
9185  O O   . VAL E  207 ? 0.8139 0.9037 0.6664 -0.0266 0.0480  -0.0378 207 VAL E O   
9186  C CB  . VAL E  207 ? 0.7241 0.8095 0.5649 -0.0398 0.0589  -0.0491 207 VAL E CB  
9187  C CG1 . VAL E  207 ? 0.6547 0.7489 0.4901 -0.0426 0.0550  -0.0509 207 VAL E CG1 
9188  C CG2 . VAL E  207 ? 0.7336 0.8131 0.5705 -0.0450 0.0663  -0.0537 207 VAL E CG2 
9189  N N   . GLY E  208 ? 0.8523 0.9587 0.6892 -0.0305 0.0451  -0.0376 208 GLY E N   
9190  C CA  . GLY E  208 ? 0.8403 0.9519 0.6809 -0.0256 0.0390  -0.0333 208 GLY E CA  
9191  C C   . GLY E  208 ? 0.8622 0.9849 0.6967 -0.0277 0.0346  -0.0337 208 GLY E C   
9192  O O   . GLY E  208 ? 0.8694 0.9989 0.6949 -0.0319 0.0353  -0.0354 208 GLY E O   
9193  N N   . SER E  209 ? 0.8655 0.9900 0.7049 -0.0248 0.0301  -0.0321 209 SER E N   
9194  C CA  . SER E  209 ? 0.8541 0.9894 0.6893 -0.0256 0.0254  -0.0315 209 SER E CA  
9195  C C   . SER E  209 ? 0.8978 1.0357 0.7387 -0.0194 0.0206  -0.0262 209 SER E C   
9196  O O   . SER E  209 ? 0.9393 1.0723 0.7854 -0.0149 0.0210  -0.0229 209 SER E O   
9197  C CB  . SER E  209 ? 0.9250 1.0598 0.7600 -0.0296 0.0254  -0.0361 209 SER E CB  
9198  O OG  . SER E  209 ? 0.8081 0.9362 0.6519 -0.0264 0.0241  -0.0356 209 SER E OG  
9199  N N   . SER E  210 ? 0.8940 1.0395 0.7340 -0.0191 0.0162  -0.0256 210 SER E N   
9200  C CA  . SER E  210 ? 0.9674 1.1153 0.8129 -0.0135 0.0118  -0.0209 210 SER E CA  
9201  C C   . SER E  210 ? 1.0415 1.1794 0.8961 -0.0104 0.0119  -0.0208 210 SER E C   
9202  O O   . SER E  210 ? 0.8561 0.9926 0.7164 -0.0053 0.0097  -0.0169 210 SER E O   
9203  C CB  . SER E  210 ? 1.0575 1.2154 0.9001 -0.0143 0.0074  -0.0206 210 SER E CB  
9204  O OG  . SER E  210 ? 1.4359 1.6042 1.2708 -0.0162 0.0064  -0.0194 210 SER E OG  
9205  N N   . ARG E  211 ? 0.9300 1.0611 0.7863 -0.0136 0.0146  -0.0251 211 ARG E N   
9206  C CA  . ARG E  211 ? 1.1277 1.2498 0.9925 -0.0113 0.0146  -0.0252 211 ARG E CA  
9207  C C   . ARG E  211 ? 1.1111 1.2229 0.9793 -0.0122 0.0196  -0.0270 211 ARG E C   
9208  O O   . ARG E  211 ? 1.3974 1.5019 1.2731 -0.0087 0.0198  -0.0251 211 ARG E O   
9209  C CB  . ARG E  211 ? 1.2188 1.3418 1.0840 -0.0138 0.0129  -0.0283 211 ARG E CB  
9210  C CG  . ARG E  211 ? 1.4180 1.5401 1.2784 -0.0199 0.0164  -0.0336 211 ARG E CG  
9211  C CD  . ARG E  211 ? 1.4549 1.5816 1.3133 -0.0226 0.0140  -0.0361 211 ARG E CD  
9212  N NE  . ARG E  211 ? 1.5897 1.7133 1.4552 -0.0193 0.0109  -0.0346 211 ARG E NE  
9213  C CZ  . ARG E  211 ? 1.6657 1.7901 1.5316 -0.0212 0.0094  -0.0369 211 ARG E CZ  
9214  N NH1 . ARG E  211 ? 1.6220 1.7503 1.4821 -0.0264 0.0108  -0.0409 211 ARG E NH1 
9215  N NH2 . ARG E  211 ? 1.5094 1.6307 1.3814 -0.0181 0.0067  -0.0352 211 ARG E NH2 
9216  N N   . TYR E  212 ? 0.9146 1.0259 0.7773 -0.0169 0.0237  -0.0307 212 TYR E N   
9217  C CA  . TYR E  212 ? 0.8370 0.9386 0.7026 -0.0183 0.0290  -0.0327 212 TYR E CA  
9218  C C   . TYR E  212 ? 0.8735 0.9738 0.7380 -0.0165 0.0314  -0.0303 212 TYR E C   
9219  O O   . TYR E  212 ? 0.9481 1.0560 0.8062 -0.0166 0.0302  -0.0286 212 TYR E O   
9220  C CB  . TYR E  212 ? 0.7658 0.8667 0.6262 -0.0247 0.0329  -0.0383 212 TYR E CB  
9221  C CG  . TYR E  212 ? 0.8790 0.9692 0.7436 -0.0263 0.0386  -0.0408 212 TYR E CG  
9222  C CD1 . TYR E  212 ? 0.8301 0.9136 0.7011 -0.0267 0.0395  -0.0427 212 TYR E CD1 
9223  C CD2 . TYR E  212 ? 0.8225 0.9093 0.6849 -0.0273 0.0432  -0.0412 212 TYR E CD2 
9224  C CE1 . TYR E  212 ? 0.7707 0.8445 0.6463 -0.0280 0.0449  -0.0447 212 TYR E CE1 
9225  C CE2 . TYR E  212 ? 0.8074 0.8843 0.6742 -0.0287 0.0487  -0.0435 212 TYR E CE2 
9226  C CZ  . TYR E  212 ? 0.8095 0.8801 0.6832 -0.0290 0.0495  -0.0451 212 TYR E CZ  
9227  O OH  . TYR E  212 ? 0.7452 0.8060 0.6238 -0.0302 0.0551  -0.0471 212 TYR E OH  
9228  N N   . SER E  213 ? 0.7374 0.8283 0.6083 -0.0148 0.0346  -0.0298 213 SER E N   
9229  C CA  . SER E  213 ? 0.7974 0.8860 0.6680 -0.0130 0.0373  -0.0276 213 SER E CA  
9230  C C   . SER E  213 ? 0.7977 0.8751 0.6759 -0.0124 0.0417  -0.0285 213 SER E C   
9231  O O   . SER E  213 ? 1.0461 1.1183 0.9329 -0.0091 0.0402  -0.0268 213 SER E O   
9232  C CB  . SER E  213 ? 0.8154 0.9084 0.6878 -0.0076 0.0332  -0.0223 213 SER E CB  
9233  O OG  . SER E  213 ? 0.7631 0.8542 0.6347 -0.0060 0.0359  -0.0201 213 SER E OG  
9234  N N   . LYS E  214 ? 0.7188 0.7924 0.5938 -0.0157 0.0473  -0.0311 214 LYS E N   
9235  C CA  . LYS E  214 ? 0.8372 0.9002 0.7195 -0.0151 0.0520  -0.0317 214 LYS E CA  
9236  C C   . LYS E  214 ? 0.9998 1.0604 0.8773 -0.0178 0.0577  -0.0334 214 LYS E C   
9237  O O   . LYS E  214 ? 0.8537 0.9185 0.7220 -0.0224 0.0596  -0.0364 214 LYS E O   
9238  C CB  . LYS E  214 ? 0.7889 0.8458 0.6764 -0.0173 0.0537  -0.0350 214 LYS E CB  
9239  C CG  . LYS E  214 ? 0.9393 0.9856 0.8360 -0.0159 0.0579  -0.0347 214 LYS E CG  
9240  C CD  . LYS E  214 ? 1.1046 1.1465 1.0104 -0.0143 0.0558  -0.0342 214 LYS E CD  
9241  C CE  . LYS E  214 ? 1.1188 1.1557 1.0257 -0.0186 0.0600  -0.0386 214 LYS E CE  
9242  N NZ  . LYS E  214 ? 1.1674 1.1957 1.0784 -0.0196 0.0667  -0.0397 214 LYS E NZ  
9243  N N   . LYS E  215 ? 0.9616 1.0152 0.8451 -0.0149 0.0605  -0.0313 215 LYS E N   
9244  C CA  . LYS E  215 ? 0.7900 0.8399 0.6701 -0.0170 0.0664  -0.0326 215 LYS E CA  
9245  C C   . LYS E  215 ? 0.8413 0.8809 0.7281 -0.0188 0.0721  -0.0355 215 LYS E C   
9246  O O   . LYS E  215 ? 0.8968 0.9304 0.7937 -0.0157 0.0715  -0.0338 215 LYS E O   
9247  C CB  . LYS E  215 ? 0.9452 0.9949 0.8275 -0.0125 0.0658  -0.0280 215 LYS E CB  
9248  C CG  . LYS E  215 ? 1.0410 1.0878 0.9187 -0.0144 0.0716  -0.0290 215 LYS E CG  
9249  C CD  . LYS E  215 ? 1.1491 1.1965 1.0286 -0.0096 0.0704  -0.0241 215 LYS E CD  
9250  C CE  . LYS E  215 ? 1.1871 1.2337 1.0600 -0.0118 0.0755  -0.0247 215 LYS E CE  
9251  N NZ  . LYS E  215 ? 1.2231 1.2716 1.0966 -0.0073 0.0741  -0.0198 215 LYS E NZ  
9252  N N   . PHE E  216 ? 0.8732 0.9107 0.7541 -0.0240 0.0777  -0.0399 216 PHE E N   
9253  C CA  . PHE E  216 ? 0.8376 0.8655 0.7243 -0.0263 0.0837  -0.0430 216 PHE E CA  
9254  C C   . PHE E  216 ? 0.8385 0.8599 0.7261 -0.0265 0.0900  -0.0432 216 PHE E C   
9255  O O   . PHE E  216 ? 0.8532 0.8779 0.7320 -0.0287 0.0920  -0.0439 216 PHE E O   
9256  C CB  . PHE E  216 ? 0.8709 0.9000 0.7515 -0.0324 0.0863  -0.0485 216 PHE E CB  
9257  C CG  . PHE E  216 ? 0.9476 0.9828 0.8272 -0.0326 0.0806  -0.0487 216 PHE E CG  
9258  C CD1 . PHE E  216 ? 0.8096 0.8551 0.6797 -0.0339 0.0763  -0.0487 216 PHE E CD1 
9259  C CD2 . PHE E  216 ? 0.8358 0.8665 0.7240 -0.0314 0.0796  -0.0489 216 PHE E CD2 
9260  C CE1 . PHE E  216 ? 0.8471 0.8983 0.7166 -0.0340 0.0712  -0.0489 216 PHE E CE1 
9261  C CE2 . PHE E  216 ? 0.8630 0.8992 0.7501 -0.0317 0.0745  -0.0492 216 PHE E CE2 
9262  C CZ  . PHE E  216 ? 0.8873 0.9335 0.7650 -0.0330 0.0704  -0.0493 216 PHE E CZ  
9263  N N   . LYS E  217 ? 0.9224 0.9347 0.8207 -0.0244 0.0931  -0.0424 217 LYS E N   
9264  C CA  . LYS E  217 ? 0.9259 0.9309 0.8266 -0.0249 0.0998  -0.0429 217 LYS E CA  
9265  C C   . LYS E  217 ? 0.9172 0.9142 0.8214 -0.0288 0.1064  -0.0472 217 LYS E C   
9266  O O   . LYS E  217 ? 1.0189 1.0113 0.9326 -0.0274 0.1061  -0.0469 217 LYS E O   
9267  C CB  . LYS E  217 ? 1.0289 1.0297 0.9399 -0.0190 0.0984  -0.0380 217 LYS E CB  
9268  C CG  . LYS E  217 ? 1.0090 1.0139 0.9155 -0.0163 0.0968  -0.0347 217 LYS E CG  
9269  C CD  . LYS E  217 ? 1.0836 1.0862 0.9831 -0.0198 0.1035  -0.0371 217 LYS E CD  
9270  C CE  . LYS E  217 ? 1.2602 1.2664 1.1555 -0.0169 0.1020  -0.0334 217 LYS E CE  
9271  N NZ  . LYS E  217 ? 1.4306 1.4343 1.3191 -0.0203 0.1086  -0.0356 217 LYS E NZ  
9272  N N   . PRO E  218 ? 0.9822 0.9775 0.8787 -0.0337 0.1127  -0.0513 218 PRO E N   
9273  C CA  . PRO E  218 ? 0.9770 0.9644 0.8763 -0.0379 0.1200  -0.0558 218 PRO E CA  
9274  C C   . PRO E  218 ? 0.9780 0.9555 0.8909 -0.0346 0.1236  -0.0537 218 PRO E C   
9275  O O   . PRO E  218 ? 1.0161 0.9907 0.9324 -0.0317 0.1252  -0.0511 218 PRO E O   
9276  C CB  . PRO E  218 ? 0.9045 0.8920 0.7930 -0.0428 0.1259  -0.0593 218 PRO E CB  
9277  C CG  . PRO E  218 ? 0.9376 0.9356 0.8153 -0.0426 0.1203  -0.0577 218 PRO E CG  
9278  C CD  . PRO E  218 ? 0.9245 0.9255 0.8092 -0.0358 0.1133  -0.0518 218 PRO E CD  
9279  N N   . GLU E  219 ? 0.9696 0.9424 0.8906 -0.0350 0.1248  -0.0549 219 GLU E N   
9280  C CA  . GLU E  219 ? 0.9337 0.8973 0.8683 -0.0323 0.1284  -0.0530 219 GLU E CA  
9281  C C   . GLU E  219 ? 0.9327 0.8883 0.8676 -0.0369 0.1380  -0.0576 219 GLU E C   
9282  O O   . GLU E  219 ? 0.8395 0.7930 0.7745 -0.0404 0.1408  -0.0611 219 GLU E O   
9283  C CB  . GLU E  219 ? 0.9870 0.9502 0.9312 -0.0296 0.1237  -0.0509 219 GLU E CB  
9284  C CG  . GLU E  219 ? 0.9998 0.9711 0.9430 -0.0256 0.1144  -0.0470 219 GLU E CG  
9285  C CD  . GLU E  219 ? 1.2102 1.1810 1.1622 -0.0234 0.1099  -0.0450 219 GLU E CD  
9286  O OE1 . GLU E  219 ? 1.1271 1.0922 1.0851 -0.0251 0.1138  -0.0468 219 GLU E OE1 
9287  O OE2 . GLU E  219 ? 1.1616 1.1379 1.1144 -0.0198 0.1026  -0.0416 219 GLU E OE2 
9288  N N   . ILE E  220 ? 1.0769 1.0280 1.0118 -0.0368 0.1433  -0.0575 220 ILE E N   
9289  C CA  . ILE E  220 ? 1.0722 1.0155 1.0068 -0.0413 0.1531  -0.0619 220 ILE E CA  
9290  C C   . ILE E  220 ? 0.8499 0.7834 0.7997 -0.0390 0.1577  -0.0604 220 ILE E C   
9291  O O   . ILE E  220 ? 0.9100 0.8405 0.8684 -0.0346 0.1573  -0.0563 220 ILE E O   
9292  C CB  . ILE E  220 ? 0.9364 0.8795 0.8626 -0.0430 0.1572  -0.0629 220 ILE E CB  
9293  C CG1 . ILE E  220 ? 0.8660 0.8192 0.7769 -0.0455 0.1528  -0.0642 220 ILE E CG1 
9294  C CG2 . ILE E  220 ? 0.9829 0.9174 0.9088 -0.0477 0.1678  -0.0677 220 ILE E CG2 
9295  C CD1 . ILE E  220 ? 1.0820 1.0369 0.9848 -0.0459 0.1547  -0.0637 220 ILE E CD1 
9296  N N   . ALA E  221 ? 0.7623 0.6910 0.7157 -0.0422 0.1623  -0.0637 221 ALA E N   
9297  C CA  . ALA E  221 ? 0.8720 0.7914 0.8399 -0.0404 0.1673  -0.0624 221 ALA E CA  
9298  C C   . ALA E  221 ? 0.9792 0.8933 0.9478 -0.0453 0.1740  -0.0672 221 ALA E C   
9299  O O   . ALA E  221 ? 0.9718 0.8899 0.9298 -0.0498 0.1738  -0.0714 221 ALA E O   
9300  C CB  . ALA E  221 ? 0.8145 0.7354 0.7941 -0.0346 0.1601  -0.0568 221 ALA E CB  
9301  N N   . ILE E  222 ? 1.0428 0.9480 1.0242 -0.0443 0.1799  -0.0665 222 ILE E N   
9302  C CA  . ILE E  222 ? 1.0745 0.9737 1.0584 -0.0484 0.1869  -0.0706 222 ILE E CA  
9303  C C   . ILE E  222 ? 1.0969 0.9968 1.0898 -0.0462 0.1824  -0.0682 222 ILE E C   
9304  O O   . ILE E  222 ? 1.0803 0.9768 1.0870 -0.0417 0.1812  -0.0635 222 ILE E O   
9305  C CB  . ILE E  222 ? 1.2300 1.1184 1.2231 -0.0490 0.1971  -0.0714 222 ILE E CB  
9306  C CG1 . ILE E  222 ? 1.2535 1.1406 1.2374 -0.0516 0.2022  -0.0741 222 ILE E CG1 
9307  C CG2 . ILE E  222 ? 1.0070 0.8891 1.0033 -0.0532 0.2045  -0.0756 222 ILE E CG2 
9308  C CD1 . ILE E  222 ? 1.2069 1.0976 1.1742 -0.0582 0.2046  -0.0803 222 ILE E CD1 
9309  N N   . ARG E  223 ? 0.9715 0.8761 0.9564 -0.0495 0.1798  -0.0713 223 ARG E N   
9310  C CA  . ARG E  223 ? 1.0825 0.9874 1.0749 -0.0482 0.1764  -0.0697 223 ARG E CA  
9311  C C   . ARG E  223 ? 1.0699 0.9670 1.0659 -0.0524 0.1853  -0.0738 223 ARG E C   
9312  O O   . ARG E  223 ? 1.1626 1.0576 1.1498 -0.0579 0.1920  -0.0795 223 ARG E O   
9313  C CB  . ARG E  223 ? 1.0255 0.9400 1.0077 -0.0491 0.1682  -0.0704 223 ARG E CB  
9314  C CG  . ARG E  223 ? 0.8833 0.8059 0.8621 -0.0449 0.1589  -0.0663 223 ARG E CG  
9315  C CD  . ARG E  223 ? 0.8443 0.7734 0.8076 -0.0480 0.1579  -0.0694 223 ARG E CD  
9316  N NE  . ARG E  223 ? 0.8027 0.7383 0.7641 -0.0435 0.1502  -0.0650 223 ARG E NE  
9317  C CZ  . ARG E  223 ? 0.8867 0.8282 0.8366 -0.0446 0.1482  -0.0658 223 ARG E CZ  
9318  N NH1 . ARG E  223 ? 0.9491 0.8913 0.8879 -0.0502 0.1532  -0.0710 223 ARG E NH1 
9319  N NH2 . ARG E  223 ? 0.9442 0.8911 0.8940 -0.0401 0.1414  -0.0614 223 ARG E NH2 
9320  N N   . PRO E  224 ? 1.0026 0.8957 1.0116 -0.0499 0.1853  -0.0709 224 PRO E N   
9321  C CA  . PRO E  224 ? 1.0772 0.9632 1.0909 -0.0534 0.1933  -0.0742 224 PRO E CA  
9322  C C   . PRO E  224 ? 1.0157 0.9044 1.0152 -0.0599 0.1957  -0.0810 224 PRO E C   
9323  O O   . PRO E  224 ? 1.0763 0.9735 1.0666 -0.0605 0.1883  -0.0815 224 PRO E O   
9324  C CB  . PRO E  224 ? 0.9620 0.8487 0.9865 -0.0497 0.1879  -0.0696 224 PRO E CB  
9325  C CG  . PRO E  224 ? 1.0594 0.9490 1.0912 -0.0435 0.1810  -0.0631 224 PRO E CG  
9326  C CD  . PRO E  224 ? 1.0000 0.8957 1.0196 -0.0438 0.1774  -0.0642 224 PRO E CD  
9327  N N   . LYS E  225 ? 1.1581 1.0397 1.1558 -0.0649 0.2059  -0.0862 225 LYS E N   
9328  C CA  . LYS E  225 ? 1.1767 1.0606 1.1606 -0.0718 0.2089  -0.0931 225 LYS E CA  
9329  C C   . LYS E  225 ? 1.1520 1.0389 1.1353 -0.0732 0.2056  -0.0943 225 LYS E C   
9330  O O   . LYS E  225 ? 1.1236 1.0051 1.1183 -0.0719 0.2082  -0.0926 225 LYS E O   
9331  C CB  . LYS E  225 ? 1.3854 1.2603 1.3682 -0.0770 0.2213  -0.0987 225 LYS E CB  
9332  C CG  . LYS E  225 ? 1.5144 1.3908 1.4856 -0.0798 0.2237  -0.1016 225 LYS E CG  
9333  C CD  . LYS E  225 ? 1.6996 1.5657 1.6729 -0.0835 0.2362  -0.1057 225 LYS E CD  
9334  C CE  . LYS E  225 ? 1.9392 1.8062 1.9051 -0.0839 0.2375  -0.1061 225 LYS E CE  
9335  N NZ  . LYS E  225 ? 1.9244 1.7812 1.8923 -0.0873 0.2496  -0.1098 225 LYS E NZ  
9336  N N   . VAL E  226 ? 1.0317 0.9275 1.0017 -0.0758 0.1999  -0.0968 226 VAL E N   
9337  C CA  . VAL E  226 ? 0.9998 0.8989 0.9666 -0.0783 0.1974  -0.0990 226 VAL E CA  
9338  C C   . VAL E  226 ? 1.1106 1.0130 1.0617 -0.0856 0.2008  -0.1063 226 VAL E C   
9339  O O   . VAL E  226 ? 1.1498 1.0601 1.0894 -0.0866 0.1959  -0.1070 226 VAL E O   
9340  C CB  . VAL E  226 ? 0.9889 0.8973 0.9552 -0.0739 0.1854  -0.0943 226 VAL E CB  
9341  C CG1 . VAL E  226 ? 0.9206 0.8325 0.8830 -0.0767 0.1831  -0.0969 226 VAL E CG1 
9342  C CG2 . VAL E  226 ? 0.9485 0.8544 0.9297 -0.0668 0.1817  -0.0871 226 VAL E CG2 
9343  N N   . ARG E  227 ? 1.2005 1.0967 1.1513 -0.0910 0.2093  -0.1116 227 ARG E N   
9344  C CA  . ARG E  227 ? 1.1377 1.0360 1.0739 -0.0986 0.2137  -0.1190 227 ARG E CA  
9345  C C   . ARG E  227 ? 1.2250 1.1219 1.1543 -0.1007 0.2181  -0.1210 227 ARG E C   
9346  O O   . ARG E  227 ? 1.2852 1.1891 1.2004 -0.1045 0.2161  -0.1243 227 ARG E O   
9347  C CB  . ARG E  227 ? 1.0902 1.0002 1.0149 -0.1001 0.2048  -0.1200 227 ARG E CB  
9348  C CG  . ARG E  227 ? 1.0985 1.0098 1.0277 -0.0996 0.2016  -0.1195 227 ARG E CG  
9349  C CD  . ARG E  227 ? 1.1189 1.0423 1.0378 -0.1000 0.1918  -0.1193 227 ARG E CD  
9350  N NE  . ARG E  227 ? 0.9935 0.9185 0.9070 -0.1053 0.1933  -0.1244 227 ARG E NE  
9351  C CZ  . ARG E  227 ? 1.1180 1.0439 1.0201 -0.1128 0.1986  -0.1314 227 ARG E CZ  
9352  N NH1 . ARG E  227 ? 1.2636 1.1888 1.1583 -0.1158 0.2029  -0.1340 227 ARG E NH1 
9353  N NH2 . ARG E  227 ? 1.1461 1.0735 1.0440 -0.1174 0.1997  -0.1357 227 ARG E NH2 
9354  N N   . ASP E  228 ? 1.3246 1.2128 1.2642 -0.0980 0.2241  -0.1189 228 ASP E N   
9355  C CA  . ASP E  228 ? 1.4985 1.3834 1.4330 -0.1001 0.2299  -0.1209 228 ASP E CA  
9356  C C   . ASP E  228 ? 1.4305 1.3229 1.3600 -0.0962 0.2223  -0.1168 228 ASP E C   
9357  O O   . ASP E  228 ? 1.6127 1.5024 1.5393 -0.0969 0.2265  -0.1175 228 ASP E O   
9358  C CB  . ASP E  228 ? 1.8797 1.7640 1.8006 -0.1089 0.2371  -0.1293 228 ASP E CB  
9359  C CG  . ASP E  228 ? 2.1177 1.9897 2.0449 -0.1126 0.2498  -0.1335 228 ASP E CG  
9360  O OD1 . ASP E  228 ? 2.1694 2.0338 2.1034 -0.1110 0.2560  -0.1323 228 ASP E OD1 
9361  O OD2 . ASP E  228 ? 2.1971 2.0670 2.1228 -0.1173 0.2538  -0.1381 228 ASP E OD2 
9362  N N   . GLN E  229 ? 1.2316 1.1330 1.1603 -0.0921 0.2114  -0.1126 229 GLN E N   
9363  C CA  . GLN E  229 ? 1.2772 1.1861 1.2010 -0.0884 0.2039  -0.1086 229 GLN E CA  
9364  C C   . GLN E  229 ? 1.1794 1.0860 1.1171 -0.0804 0.1998  -0.1012 229 GLN E C   
9365  O O   . GLN E  229 ? 1.2355 1.1424 1.1827 -0.0766 0.1953  -0.0976 229 GLN E O   
9366  C CB  . GLN E  229 ? 1.0932 1.0141 1.0064 -0.0890 0.1944  -0.1086 229 GLN E CB  
9367  C CG  . GLN E  229 ? 1.1317 1.0555 1.0324 -0.0968 0.1974  -0.1156 229 GLN E CG  
9368  C CD  . GLN E  229 ? 1.1834 1.1054 1.0735 -0.1027 0.2048  -0.1208 229 GLN E CD  
9369  O OE1 . GLN E  229 ? 1.1966 1.1198 1.0834 -0.1011 0.2042  -0.1189 229 GLN E OE1 
9370  N NE2 . GLN E  229 ? 1.2050 1.1239 1.0892 -0.1099 0.2119  -0.1276 229 GLN E NE2 
9371  N N   . GLU E  230 ? 1.1162 1.0207 1.0551 -0.0782 0.2015  -0.0991 230 GLU E N   
9372  C CA  . GLU E  230 ? 1.0850 0.9882 1.0360 -0.0709 0.1973  -0.0922 230 GLU E CA  
9373  C C   . GLU E  230 ? 1.1291 1.0427 1.0741 -0.0673 0.1867  -0.0884 230 GLU E C   
9374  O O   . GLU E  230 ? 1.1131 1.0278 1.0668 -0.0612 0.1812  -0.0825 230 GLU E O   
9375  C CB  . GLU E  230 ? 1.3118 1.2070 1.2682 -0.0701 0.2048  -0.0917 230 GLU E CB  
9376  C CG  . GLU E  230 ? 1.4933 1.3815 1.4443 -0.0767 0.2160  -0.0983 230 GLU E CG  
9377  C CD  . GLU E  230 ? 1.4047 1.2851 1.3609 -0.0758 0.2233  -0.0977 230 GLU E CD  
9378  O OE1 . GLU E  230 ? 1.4160 1.2960 1.3614 -0.0801 0.2280  -0.1017 230 GLU E OE1 
9379  O OE2 . GLU E  230 ? 1.5461 1.4210 1.5172 -0.0708 0.2242  -0.0932 230 GLU E OE2 
9380  N N   . GLY E  231 ? 0.9377 0.8590 0.8678 -0.0712 0.1842  -0.0917 231 GLY E N   
9381  C CA  . GLY E  231 ? 0.9554 0.8871 0.8789 -0.0683 0.1744  -0.0884 231 GLY E CA  
9382  C C   . GLY E  231 ? 0.9878 0.9260 0.9102 -0.0680 0.1674  -0.0880 231 GLY E C   
9383  O O   . GLY E  231 ? 0.9535 0.8888 0.8773 -0.0713 0.1706  -0.0913 231 GLY E O   
9384  N N   . ARG E  232 ? 0.8597 0.8064 0.7796 -0.0642 0.1580  -0.0840 232 ARG E N   
9385  C CA  . ARG E  232 ? 0.7947 0.7480 0.7135 -0.0635 0.1509  -0.0832 232 ARG E CA  
9386  C C   . ARG E  232 ? 0.8700 0.8343 0.7747 -0.0657 0.1453  -0.0846 232 ARG E C   
9387  O O   . ARG E  232 ? 0.8112 0.7784 0.7075 -0.0672 0.1463  -0.0853 232 ARG E O   
9388  C CB  . ARG E  232 ? 0.8612 0.8150 0.7913 -0.0565 0.1440  -0.0768 232 ARG E CB  
9389  C CG  . ARG E  232 ? 0.8076 0.7520 0.7525 -0.0542 0.1481  -0.0749 232 ARG E CG  
9390  C CD  . ARG E  232 ? 0.8086 0.7506 0.7560 -0.0571 0.1502  -0.0778 232 ARG E CD  
9391  N NE  . ARG E  232 ? 1.0122 0.9439 0.9721 -0.0565 0.1570  -0.0773 232 ARG E NE  
9392  C CZ  . ARG E  232 ? 1.0259 0.9503 0.9857 -0.0607 0.1666  -0.0816 232 ARG E CZ  
9393  N NH1 . ARG E  232 ? 0.9412 0.8674 0.8884 -0.0661 0.1705  -0.0869 232 ARG E NH1 
9394  N NH2 . ARG E  232 ? 1.0159 0.9313 0.9882 -0.0596 0.1725  -0.0805 232 ARG E NH2 
9395  N N   . MET E  233 ? 0.9487 0.9192 0.8512 -0.0660 0.1396  -0.0847 233 MET E N   
9396  C CA  . MET E  233 ? 0.8476 0.8292 0.7382 -0.0675 0.1334  -0.0852 233 MET E CA  
9397  C C   . MET E  233 ? 0.8839 0.8712 0.7778 -0.0640 0.1250  -0.0820 233 MET E C   
9398  O O   . MET E  233 ? 0.8481 0.8347 0.7436 -0.0660 0.1251  -0.0842 233 MET E O   
9399  C CB  . MET E  233 ? 0.7818 0.7657 0.6609 -0.0751 0.1378  -0.0918 233 MET E CB  
9400  C CG  . MET E  233 ? 0.8577 0.8535 0.7238 -0.0772 0.1321  -0.0925 233 MET E CG  
9401  S SD  . MET E  233 ? 1.1638 1.1622 1.0159 -0.0868 0.1378  -0.1004 233 MET E SD  
9402  C CE  . MET E  233 ? 1.0028 0.9932 0.8531 -0.0891 0.1470  -0.1024 233 MET E CE  
9403  N N   . ASN E  234 ? 0.8284 0.8211 0.7234 -0.0588 0.1179  -0.0770 234 ASN E N   
9404  C CA  . ASN E  234 ? 0.8324 0.8308 0.7300 -0.0553 0.1098  -0.0738 234 ASN E CA  
9405  C C   . ASN E  234 ? 0.7188 0.7277 0.6048 -0.0584 0.1054  -0.0758 234 ASN E C   
9406  O O   . ASN E  234 ? 0.7432 0.7576 0.6196 -0.0603 0.1051  -0.0767 234 ASN E O   
9407  C CB  . ASN E  234 ? 0.7946 0.7941 0.6983 -0.0486 0.1044  -0.0676 234 ASN E CB  
9408  C CG  . ASN E  234 ? 0.7382 0.7284 0.6552 -0.0450 0.1071  -0.0648 234 ASN E CG  
9409  O OD1 . ASN E  234 ? 0.8093 0.7921 0.7317 -0.0471 0.1128  -0.0671 234 ASN E OD1 
9410  N ND2 . ASN E  234 ? 0.7606 0.7512 0.6832 -0.0395 0.1030  -0.0597 234 ASN E ND2 
9411  N N   . TYR E  235 ? 0.7001 0.7118 0.5871 -0.0589 0.1018  -0.0765 235 TYR E N   
9412  C CA  . TYR E  235 ? 0.5943 0.6158 0.4711 -0.0619 0.0976  -0.0785 235 TYR E CA  
9413  C C   . TYR E  235 ? 0.6368 0.6656 0.5152 -0.0570 0.0887  -0.0738 235 TYR E C   
9414  O O   . TYR E  235 ? 0.7556 0.7814 0.6429 -0.0533 0.0859  -0.0710 235 TYR E O   
9415  C CB  . TYR E  235 ? 0.6999 0.7199 0.5751 -0.0671 0.1009  -0.0836 235 TYR E CB  
9416  C CG  . TYR E  235 ? 0.9223 0.9343 0.7969 -0.0720 0.1103  -0.0884 235 TYR E CG  
9417  C CD1 . TYR E  235 ? 0.7323 0.7336 0.6175 -0.0709 0.1154  -0.0883 235 TYR E CD1 
9418  C CD2 . TYR E  235 ? 0.7961 0.8110 0.6596 -0.0777 0.1141  -0.0928 235 TYR E CD2 
9419  C CE1 . TYR E  235 ? 0.7109 0.7046 0.5961 -0.0752 0.1244  -0.0926 235 TYR E CE1 
9420  C CE2 . TYR E  235 ? 0.8114 0.8186 0.6741 -0.0823 0.1231  -0.0974 235 TYR E CE2 
9421  C CZ  . TYR E  235 ? 0.7836 0.7800 0.6574 -0.0810 0.1283  -0.0973 235 TYR E CZ  
9422  O OH  . TYR E  235 ? 0.9061 0.8944 0.7795 -0.0856 0.1377  -0.1019 235 TYR E OH  
9423  N N   . TYR E  236 ? 0.5718 0.6101 0.4415 -0.0571 0.0844  -0.0730 236 TYR E N   
9424  C CA  . TYR E  236 ? 0.6261 0.6716 0.4966 -0.0526 0.0763  -0.0686 236 TYR E CA  
9425  C C   . TYR E  236 ? 0.7214 0.7771 0.5828 -0.0558 0.0725  -0.0706 236 TYR E C   
9426  O O   . TYR E  236 ? 0.7914 0.8502 0.6442 -0.0614 0.0756  -0.0749 236 TYR E O   
9427  C CB  . TYR E  236 ? 0.5090 0.5567 0.3794 -0.0483 0.0740  -0.0641 236 TYR E CB  
9428  C CG  . TYR E  236 ? 0.7087 0.7472 0.5888 -0.0445 0.0769  -0.0615 236 TYR E CG  
9429  C CD1 . TYR E  236 ? 0.7427 0.7743 0.6227 -0.0468 0.0840  -0.0636 236 TYR E CD1 
9430  C CD2 . TYR E  236 ? 0.7135 0.7499 0.6027 -0.0388 0.0726  -0.0569 236 TYR E CD2 
9431  C CE1 . TYR E  236 ? 0.7825 0.8058 0.6718 -0.0433 0.0867  -0.0611 236 TYR E CE1 
9432  C CE2 . TYR E  236 ? 0.8487 0.8770 0.7470 -0.0355 0.0751  -0.0544 236 TYR E CE2 
9433  C CZ  . TYR E  236 ? 0.9186 0.9405 0.8172 -0.0376 0.0821  -0.0564 236 TYR E CZ  
9434  O OH  . TYR E  236 ? 0.7994 0.8134 0.7075 -0.0343 0.0847  -0.0539 236 TYR E OH  
9435  N N   . TRP E  237 ? 0.7157 0.7768 0.5792 -0.0525 0.0658  -0.0676 237 TRP E N   
9436  C CA  . TRP E  237 ? 0.6313 0.7024 0.4873 -0.0549 0.0617  -0.0690 237 TRP E CA  
9437  C C   . TRP E  237 ? 0.6449 0.7227 0.5025 -0.0497 0.0541  -0.0640 237 TRP E C   
9438  O O   . TRP E  237 ? 0.7281 0.8019 0.5935 -0.0444 0.0521  -0.0600 237 TRP E O   
9439  C CB  . TRP E  237 ? 0.6246 0.6937 0.4816 -0.0586 0.0630  -0.0730 237 TRP E CB  
9440  C CG  . TRP E  237 ? 0.6571 0.7210 0.5241 -0.0546 0.0607  -0.0705 237 TRP E CG  
9441  C CD1 . TRP E  237 ? 0.6144 0.6680 0.4904 -0.0533 0.0645  -0.0702 237 TRP E CD1 
9442  C CD2 . TRP E  237 ? 0.6230 0.6918 0.4921 -0.0514 0.0541  -0.0677 237 TRP E CD2 
9443  N NE1 . TRP E  237 ? 0.5398 0.5919 0.4230 -0.0496 0.0604  -0.0674 237 TRP E NE1 
9444  C CE2 . TRP E  237 ? 0.6607 0.7218 0.5397 -0.0485 0.0541  -0.0660 237 TRP E CE2 
9445  C CE3 . TRP E  237 ? 0.5955 0.6747 0.4594 -0.0509 0.0483  -0.0665 237 TRP E CE3 
9446  C CZ2 . TRP E  237 ? 0.7686 0.8319 0.6517 -0.0453 0.0486  -0.0633 237 TRP E CZ2 
9447  C CZ3 . TRP E  237 ? 0.6175 0.6984 0.4858 -0.0475 0.0430  -0.0639 237 TRP E CZ3 
9448  C CH2 . TRP E  237 ? 0.6464 0.7193 0.5240 -0.0449 0.0432  -0.0624 237 TRP E CH2 
9449  N N   . THR E  238 ? 0.6213 0.7094 0.4717 -0.0513 0.0501  -0.0644 238 THR E N   
9450  C CA  . THR E  238 ? 0.6045 0.6996 0.4560 -0.0467 0.0432  -0.0599 238 THR E CA  
9451  C C   . THR E  238 ? 0.6469 0.7527 0.4908 -0.0498 0.0398  -0.0615 238 THR E C   
9452  O O   . THR E  238 ? 0.7324 0.8415 0.5688 -0.0554 0.0425  -0.0656 238 THR E O   
9453  C CB  . THR E  238 ? 0.6905 0.7877 0.5415 -0.0427 0.0418  -0.0555 238 THR E CB  
9454  O OG1 . THR E  238 ? 0.6382 0.7402 0.4922 -0.0376 0.0356  -0.0509 238 THR E OG1 
9455  C CG2 . THR E  238 ? 0.6362 0.7407 0.4770 -0.0464 0.0430  -0.0569 238 THR E CG2 
9456  N N   . LEU E  239 ? 0.6790 0.7902 0.5251 -0.0463 0.0339  -0.0583 239 LEU E N   
9457  C CA  . LEU E  239 ? 0.7429 0.8645 0.5829 -0.0486 0.0302  -0.0593 239 LEU E CA  
9458  C C   . LEU E  239 ? 0.8569 0.9882 0.6932 -0.0458 0.0257  -0.0551 239 LEU E C   
9459  O O   . LEU E  239 ? 0.9517 1.0839 0.7929 -0.0404 0.0217  -0.0506 239 LEU E O   
9460  C CB  . LEU E  239 ? 0.7765 0.8973 0.6214 -0.0475 0.0272  -0.0595 239 LEU E CB  
9461  C CG  . LEU E  239 ? 0.6288 0.7419 0.4764 -0.0511 0.0313  -0.0639 239 LEU E CG  
9462  C CD1 . LEU E  239 ? 0.7718 0.8840 0.6246 -0.0492 0.0278  -0.0632 239 LEU E CD1 
9463  C CD2 . LEU E  239 ? 0.6599 0.7766 0.4994 -0.0581 0.0347  -0.0693 239 LEU E CD2 
9464  N N   . VAL E  240 ? 0.8154 0.9540 0.6432 -0.0495 0.0266  -0.0565 240 VAL E N   
9465  C CA  . VAL E  240 ? 0.8282 0.9767 0.6519 -0.0473 0.0226  -0.0524 240 VAL E CA  
9466  C C   . VAL E  240 ? 0.6718 0.8302 0.4941 -0.0471 0.0173  -0.0515 240 VAL E C   
9467  O O   . VAL E  240 ? 0.6921 0.8551 0.5097 -0.0521 0.0175  -0.0553 240 VAL E O   
9468  C CB  . VAL E  240 ? 0.8369 0.9902 0.6515 -0.0517 0.0253  -0.0541 240 VAL E CB  
9469  C CG1 . VAL E  240 ? 0.7924 0.9552 0.6039 -0.0485 0.0214  -0.0490 240 VAL E CG1 
9470  C CG2 . VAL E  240 ? 0.6940 0.8370 0.5097 -0.0528 0.0314  -0.0560 240 VAL E CG2 
9471  N N   . GLU E  241 ? 0.8281 0.9895 0.6547 -0.0414 0.0128  -0.0464 241 GLU E N   
9472  C CA  . GLU E  241 ? 0.8702 1.0408 0.6962 -0.0406 0.0078  -0.0449 241 GLU E CA  
9473  C C   . GLU E  241 ? 0.9678 1.1507 0.7852 -0.0440 0.0063  -0.0449 241 GLU E C   
9474  O O   . GLU E  241 ? 0.9708 1.1557 0.7836 -0.0449 0.0080  -0.0440 241 GLU E O   
9475  C CB  . GLU E  241 ? 0.9563 1.1272 0.7888 -0.0336 0.0039  -0.0392 241 GLU E CB  
9476  C CG  . GLU E  241 ? 1.2202 1.3800 1.0612 -0.0302 0.0046  -0.0388 241 GLU E CG  
9477  C CD  . GLU E  241 ? 1.5232 1.6809 1.3667 -0.0319 0.0037  -0.0418 241 GLU E CD  
9478  O OE1 . GLU E  241 ? 1.4778 1.6257 1.3265 -0.0316 0.0058  -0.0433 241 GLU E OE1 
9479  O OE2 . GLU E  241 ? 1.6215 1.7875 1.4619 -0.0337 0.0009  -0.0425 241 GLU E OE2 
9480  N N   . PRO E  242 ? 1.0266 1.2179 0.8419 -0.0460 0.0032  -0.0459 242 PRO E N   
9481  C CA  . PRO E  242 ? 1.0001 1.2044 0.8079 -0.0490 0.0010  -0.0454 242 PRO E CA  
9482  C C   . PRO E  242 ? 1.0194 1.2298 0.8274 -0.0441 -0.0019 -0.0391 242 PRO E C   
9483  O O   . PRO E  242 ? 0.9285 1.1380 0.7428 -0.0383 -0.0047 -0.0348 242 PRO E O   
9484  C CB  . PRO E  242 ? 0.8597 1.0703 0.6682 -0.0501 -0.0025 -0.0464 242 PRO E CB  
9485  C CG  . PRO E  242 ? 0.9294 1.1295 0.7429 -0.0507 -0.0003 -0.0501 242 PRO E CG  
9486  C CD  . PRO E  242 ? 0.8433 1.0323 0.6628 -0.0461 0.0017  -0.0479 242 PRO E CD  
9487  N N   . GLY E  243 ? 0.9562 1.1725 0.7574 -0.0464 -0.0010 -0.0384 243 GLY E N   
9488  C CA  . GLY E  243 ? 0.8856 1.1078 0.6865 -0.0420 -0.0034 -0.0323 243 GLY E CA  
9489  C C   . GLY E  243 ? 0.9682 1.1808 0.7726 -0.0382 -0.0005 -0.0301 243 GLY E C   
9490  O O   . GLY E  243 ? 1.0956 1.3116 0.9000 -0.0345 -0.0017 -0.0251 243 GLY E O   
9491  N N   . ASP E  244 ? 0.9897 1.1904 0.7974 -0.0391 0.0034  -0.0338 244 ASP E N   
9492  C CA  . ASP E  244 ? 0.8353 1.0260 0.6467 -0.0360 0.0065  -0.0323 244 ASP E CA  
9493  C C   . ASP E  244 ? 0.8650 1.0532 0.6696 -0.0410 0.0114  -0.0357 244 ASP E C   
9494  O O   . ASP E  244 ? 0.9883 1.1795 0.7868 -0.0472 0.0130  -0.0404 244 ASP E O   
9495  C CB  . ASP E  244 ? 0.8482 1.0272 0.6679 -0.0337 0.0078  -0.0338 244 ASP E CB  
9496  C CG  . ASP E  244 ? 1.1264 1.2957 0.9515 -0.0295 0.0103  -0.0314 244 ASP E CG  
9497  O OD1 . ASP E  244 ? 1.1873 1.3472 1.0194 -0.0275 0.0113  -0.0322 244 ASP E OD1 
9498  O OD2 . ASP E  244 ? 1.0564 1.2278 0.8789 -0.0282 0.0111  -0.0286 244 ASP E OD2 
9499  N N   . LYS E  245 ? 0.7745 0.9574 0.5801 -0.0385 0.0139  -0.0335 245 LYS E N   
9500  C CA  . LYS E  245 ? 0.8969 1.0764 0.6966 -0.0430 0.0190  -0.0367 245 LYS E CA  
9501  C C   . LYS E  245 ? 0.8689 1.0347 0.6746 -0.0411 0.0235  -0.0376 245 LYS E C   
9502  O O   . LYS E  245 ? 0.8901 1.0506 0.7038 -0.0353 0.0223  -0.0342 245 LYS E O   
9503  C CB  . LYS E  245 ? 0.9694 1.1573 0.7623 -0.0430 0.0182  -0.0332 245 LYS E CB  
9504  C CG  . LYS E  245 ? 1.0144 1.1991 0.8119 -0.0367 0.0180  -0.0275 245 LYS E CG  
9505  C CD  . LYS E  245 ? 1.1382 1.3316 0.9285 -0.0371 0.0174  -0.0241 245 LYS E CD  
9506  C CE  . LYS E  245 ? 1.2941 1.4836 1.0890 -0.0308 0.0176  -0.0185 245 LYS E CE  
9507  N NZ  . LYS E  245 ? 1.0267 1.2253 0.8149 -0.0308 0.0167  -0.0145 245 LYS E NZ  
9508  N N   . ILE E  246 ? 0.7494 0.9095 0.5514 -0.0461 0.0289  -0.0425 246 ILE E N   
9509  C CA  . ILE E  246 ? 0.7924 0.9397 0.5998 -0.0449 0.0338  -0.0437 246 ILE E CA  
9510  C C   . ILE E  246 ? 0.8519 0.9978 0.6533 -0.0473 0.0382  -0.0442 246 ILE E C   
9511  O O   . ILE E  246 ? 0.8299 0.9810 0.6222 -0.0531 0.0400  -0.0474 246 ILE E O   
9512  C CB  . ILE E  246 ? 0.7238 0.8632 0.5340 -0.0485 0.0372  -0.0492 246 ILE E CB  
9513  C CG1 . ILE E  246 ? 0.7789 0.9053 0.5956 -0.0471 0.0423  -0.0500 246 ILE E CG1 
9514  C CG2 . ILE E  246 ? 0.6566 0.8004 0.4577 -0.0562 0.0397  -0.0547 246 ILE E CG2 
9515  C CD1 . ILE E  246 ? 0.7242 0.8425 0.5439 -0.0507 0.0462  -0.0553 246 ILE E CD1 
9516  N N   . THR E  247 ? 1.0610 1.2001 0.8674 -0.0430 0.0401  -0.0412 247 THR E N   
9517  C CA  . THR E  247 ? 1.0820 1.2196 0.8831 -0.0445 0.0441  -0.0410 247 THR E CA  
9518  C C   . THR E  247 ? 1.0365 1.1613 0.8415 -0.0458 0.0507  -0.0443 247 THR E C   
9519  O O   . THR E  247 ? 1.1214 1.2376 0.9360 -0.0420 0.0512  -0.0434 247 THR E O   
9520  C CB  . THR E  247 ? 0.9292 1.0701 0.7319 -0.0387 0.0414  -0.0344 247 THR E CB  
9521  O OG1 . THR E  247 ? 1.0378 1.1910 0.8368 -0.0376 0.0357  -0.0311 247 THR E OG1 
9522  C CG2 . THR E  247 ? 0.7167 0.8560 0.5135 -0.0404 0.0457  -0.0342 247 THR E CG2 
9523  N N   . PHE E  248 ? 0.9268 1.0505 0.7243 -0.0512 0.0557  -0.0479 248 PHE E N   
9524  C CA  . PHE E  248 ? 0.9820 1.0939 0.7824 -0.0527 0.0626  -0.0510 248 PHE E CA  
9525  C C   . PHE E  248 ? 0.9416 1.0522 0.7388 -0.0516 0.0653  -0.0485 248 PHE E C   
9526  O O   . PHE E  248 ? 1.0166 1.1357 0.8045 -0.0539 0.0644  -0.0476 248 PHE E O   
9527  C CB  . PHE E  248 ? 0.7614 0.8711 0.5563 -0.0602 0.0673  -0.0579 248 PHE E CB  
9528  C CG  . PHE E  248 ? 0.8005 0.9083 0.6001 -0.0612 0.0660  -0.0607 248 PHE E CG  
9529  C CD1 . PHE E  248 ? 0.8343 0.9521 0.6304 -0.0625 0.0608  -0.0608 248 PHE E CD1 
9530  C CD2 . PHE E  248 ? 0.7928 0.8893 0.6008 -0.0608 0.0701  -0.0631 248 PHE E CD2 
9531  C CE1 . PHE E  248 ? 0.7991 0.9151 0.5994 -0.0634 0.0597  -0.0634 248 PHE E CE1 
9532  C CE2 . PHE E  248 ? 0.7720 0.8669 0.5843 -0.0617 0.0689  -0.0654 248 PHE E CE2 
9533  C CZ  . PHE E  248 ? 0.7247 0.8293 0.5330 -0.0630 0.0638  -0.0657 248 PHE E CZ  
9534  N N   . GLU E  249 ? 0.8609 0.9611 0.6659 -0.0482 0.0688  -0.0473 249 GLU E N   
9535  C CA  . GLU E  249 ? 0.9203 1.0181 0.7237 -0.0466 0.0717  -0.0448 249 GLU E CA  
9536  C C   . GLU E  249 ? 0.8896 0.9743 0.6990 -0.0470 0.0785  -0.0474 249 GLU E C   
9537  O O   . GLU E  249 ? 1.0158 1.0931 0.8359 -0.0430 0.0784  -0.0462 249 GLU E O   
9538  C CB  . GLU E  249 ? 1.0242 1.1250 0.8327 -0.0393 0.0667  -0.0380 249 GLU E CB  
9539  C CG  . GLU E  249 ? 1.2407 1.3394 1.0480 -0.0370 0.0693  -0.0347 249 GLU E CG  
9540  C CD  . GLU E  249 ? 1.4391 1.5413 1.2512 -0.0300 0.0643  -0.0280 249 GLU E CD  
9541  O OE1 . GLU E  249 ? 1.4714 1.5688 1.2867 -0.0266 0.0665  -0.0250 249 GLU E OE1 
9542  O OE2 . GLU E  249 ? 1.3035 1.4131 1.1165 -0.0279 0.0585  -0.0258 249 GLU E OE2 
9543  N N   . ALA E  250 ? 0.8874 0.9693 0.6900 -0.0519 0.0845  -0.0509 250 ALA E N   
9544  C CA  . ALA E  250 ? 0.9780 1.0474 0.7859 -0.0531 0.0917  -0.0539 250 ALA E CA  
9545  C C   . ALA E  250 ? 1.0043 1.0708 0.8062 -0.0554 0.0975  -0.0546 250 ALA E C   
9546  O O   . ALA E  250 ? 0.9988 1.0725 0.7893 -0.0594 0.0976  -0.0555 250 ALA E O   
9547  C CB  . ALA E  250 ? 1.0085 1.0742 0.8160 -0.0585 0.0951  -0.0601 250 ALA E CB  
9548  N N   . THR E  251 ? 0.9913 1.0472 0.8012 -0.0528 0.1021  -0.0540 251 THR E N   
9549  C CA  . THR E  251 ? 1.0249 1.0758 0.8304 -0.0553 0.1088  -0.0554 251 THR E CA  
9550  C C   . THR E  251 ? 1.0435 1.0846 0.8510 -0.0601 0.1164  -0.0614 251 THR E C   
9551  O O   . THR E  251 ? 1.0935 1.1272 0.9009 -0.0616 0.1232  -0.0630 251 THR E O   
9552  C CB  . THR E  251 ? 0.9597 1.0054 0.7729 -0.0490 0.1092  -0.0503 251 THR E CB  
9553  O OG1 . THR E  251 ? 1.0309 1.0701 0.8577 -0.0441 0.1078  -0.0486 251 THR E OG1 
9554  N N   . GLY E  252 ? 0.9710 1.0121 0.7805 -0.0623 0.1155  -0.0647 252 GLY E N   
9555  C CA  . GLY E  252 ? 0.9774 1.0095 0.7893 -0.0669 0.1225  -0.0704 252 GLY E CA  
9556  C C   . GLY E  252 ? 0.9959 1.0242 0.8184 -0.0647 0.1206  -0.0708 252 GLY E C   
9557  O O   . GLY E  252 ? 1.0009 1.0326 0.8297 -0.0593 0.1140  -0.0664 252 GLY E O   
9558  N N   . ASN E  253 ? 0.9334 0.9547 0.7578 -0.0691 0.1266  -0.0760 253 ASN E N   
9559  C CA  . ASN E  253 ? 0.8745 0.8904 0.7095 -0.0673 0.1261  -0.0765 253 ASN E CA  
9560  C C   . ASN E  253 ? 0.8730 0.8972 0.7059 -0.0678 0.1196  -0.0768 253 ASN E C   
9561  O O   . ASN E  253 ? 0.8704 0.8915 0.7120 -0.0657 0.1178  -0.0763 253 ASN E O   
9562  C CB  . ASN E  253 ? 0.9231 0.9329 0.7716 -0.0601 0.1247  -0.0714 253 ASN E CB  
9563  C CG  . ASN E  253 ? 0.9376 0.9387 0.7895 -0.0595 0.1315  -0.0711 253 ASN E CG  
9564  O OD1 . ASN E  253 ? 1.0102 1.0016 0.8715 -0.0591 0.1367  -0.0723 253 ASN E OD1 
9565  N ND2 . ASN E  253 ? 0.8229 0.8277 0.6674 -0.0594 0.1315  -0.0695 253 ASN E ND2 
9566  N N   . LEU E  254 ? 0.9344 0.9691 0.7556 -0.0708 0.1160  -0.0774 254 LEU E N   
9567  C CA  . LEU E  254 ? 0.8496 0.8931 0.6683 -0.0712 0.1095  -0.0774 254 LEU E CA  
9568  C C   . LEU E  254 ? 0.7898 0.8352 0.6007 -0.0788 0.1125  -0.0838 254 LEU E C   
9569  O O   . LEU E  254 ? 0.9124 0.9630 0.7117 -0.0841 0.1142  -0.0867 254 LEU E O   
9570  C CB  . LEU E  254 ? 0.8444 0.8994 0.6567 -0.0686 0.1024  -0.0730 254 LEU E CB  
9571  C CG  . LEU E  254 ? 0.8046 0.8698 0.6135 -0.0692 0.0955  -0.0728 254 LEU E CG  
9572  C CD1 . LEU E  254 ? 0.8224 0.8841 0.6425 -0.0650 0.0923  -0.0711 254 LEU E CD1 
9573  C CD2 . LEU E  254 ? 0.7906 0.8669 0.5936 -0.0666 0.0892  -0.0681 254 LEU E CD2 
9574  N N   . VAL E  255 ? 0.7885 0.8297 0.6056 -0.0794 0.1132  -0.0861 255 VAL E N   
9575  C CA  . VAL E  255 ? 0.7330 0.7770 0.5437 -0.0861 0.1149  -0.0918 255 VAL E CA  
9576  C C   . VAL E  255 ? 0.7765 0.8330 0.5818 -0.0857 0.1067  -0.0901 255 VAL E C   
9577  O O   . VAL E  255 ? 0.8550 0.9128 0.6668 -0.0822 0.1019  -0.0880 255 VAL E O   
9578  C CB  . VAL E  255 ? 0.7655 0.8004 0.5854 -0.0866 0.1187  -0.0945 255 VAL E CB  
9579  C CG1 . VAL E  255 ? 0.7944 0.8320 0.6073 -0.0937 0.1207  -0.1006 255 VAL E CG1 
9580  C CG2 . VAL E  255 ? 0.6723 0.6947 0.4989 -0.0865 0.1268  -0.0957 255 VAL E CG2 
9581  N N   . VAL E  256 ? 0.8180 0.8838 0.6115 -0.0892 0.1051  -0.0908 256 VAL E N   
9582  C CA  . VAL E  256 ? 0.7756 0.8541 0.5639 -0.0884 0.0972  -0.0884 256 VAL E CA  
9583  C C   . VAL E  256 ? 0.8751 0.9577 0.6609 -0.0927 0.0958  -0.0924 256 VAL E C   
9584  O O   . VAL E  256 ? 0.8550 0.9327 0.6385 -0.0986 0.1017  -0.0984 256 VAL E O   
9585  C CB  . VAL E  256 ? 0.9283 1.0162 0.7047 -0.0911 0.0959  -0.0876 256 VAL E CB  
9586  C CG1 . VAL E  256 ? 0.9739 1.0580 0.7525 -0.0867 0.0972  -0.0833 256 VAL E CG1 
9587  C CG2 . VAL E  256 ? 1.0129 1.1012 0.7788 -0.1000 0.1018  -0.0944 256 VAL E CG2 
9588  N N   . PRO E  257 ? 0.9389 1.0304 0.7254 -0.0899 0.0882  -0.0893 257 PRO E N   
9589  C CA  . PRO E  257 ? 0.7548 0.8517 0.5384 -0.0937 0.0860  -0.0927 257 PRO E CA  
9590  C C   . PRO E  257 ? 0.9101 1.0152 0.6805 -0.1014 0.0874  -0.0971 257 PRO E C   
9591  O O   . PRO E  257 ? 0.9801 1.0918 0.7432 -0.1019 0.0859  -0.0951 257 PRO E O   
9592  C CB  . PRO E  257 ? 0.7512 0.8565 0.5381 -0.0881 0.0772  -0.0872 257 PRO E CB  
9593  C CG  . PRO E  257 ? 0.8500 0.9505 0.6448 -0.0807 0.0758  -0.0814 257 PRO E CG  
9594  C CD  . PRO E  257 ? 0.7957 0.8917 0.5867 -0.0825 0.0814  -0.0823 257 PRO E CD  
9595  N N   . ARG E  258 ? 0.9864 1.0909 0.7538 -0.1075 0.0903  -0.1030 258 ARG E N   
9596  C CA  . ARG E  258 ? 0.9695 1.0828 0.7245 -0.1152 0.0909  -0.1073 258 ARG E CA  
9597  C C   . ARG E  258 ? 0.8385 0.9610 0.5923 -0.1163 0.0851  -0.1078 258 ARG E C   
9598  O O   . ARG E  258 ? 0.8973 1.0322 0.6434 -0.1180 0.0802  -0.1065 258 ARG E O   
9599  C CB  . ARG E  258 ? 0.9447 1.0498 0.6959 -0.1226 0.1000  -0.1147 258 ARG E CB  
9600  C CG  . ARG E  258 ? 0.9761 1.0898 0.7142 -0.1314 0.1011  -0.1199 258 ARG E CG  
9601  C CD  . ARG E  258 ? 0.9974 1.1018 0.7323 -0.1386 0.1108  -0.1274 258 ARG E CD  
9602  N NE  . ARG E  258 ? 1.1808 1.2920 0.9061 -0.1470 0.1116  -0.1334 258 ARG E NE  
9603  C CZ  . ARG E  258 ? 1.2729 1.3924 0.9856 -0.1534 0.1121  -0.1360 258 ARG E CZ  
9604  N NH1 . ARG E  258 ? 1.3209 1.4426 1.0286 -0.1523 0.1119  -0.1330 258 ARG E NH1 
9605  N NH2 . ARG E  258 ? 1.2932 1.4187 0.9980 -0.1611 0.1128  -0.1415 258 ARG E NH2 
9606  N N   . TYR E  259 ? 0.8809 0.9974 0.6427 -0.1151 0.0857  -0.1092 259 TYR E N   
9607  C CA  . TYR E  259 ? 0.8491 0.9731 0.6113 -0.1154 0.0804  -0.1094 259 TYR E CA  
9608  C C   . TYR E  259 ? 0.8284 0.9507 0.6015 -0.1072 0.0750  -0.1037 259 TYR E C   
9609  O O   . TYR E  259 ? 0.8085 0.9201 0.5907 -0.1031 0.0775  -0.1023 259 TYR E O   
9610  C CB  . TYR E  259 ? 0.9018 1.0212 0.6633 -0.1217 0.0854  -0.1163 259 TYR E CB  
9611  C CG  . TYR E  259 ? 1.0849 1.2085 0.8345 -0.1308 0.0896  -0.1224 259 TYR E CG  
9612  C CD1 . TYR E  259 ? 1.0709 1.1863 0.8174 -0.1349 0.0976  -0.1264 259 TYR E CD1 
9613  C CD2 . TYR E  259 ? 1.1594 1.2952 0.9010 -0.1354 0.0856  -0.1243 259 TYR E CD2 
9614  C CE1 . TYR E  259 ? 1.2089 1.3281 0.9441 -0.1436 0.1016  -0.1322 259 TYR E CE1 
9615  C CE2 . TYR E  259 ? 1.1731 1.3132 0.9036 -0.1440 0.0893  -0.1300 259 TYR E CE2 
9616  C CZ  . TYR E  259 ? 1.1955 1.3271 0.9226 -0.1482 0.0973  -0.1340 259 TYR E CZ  
9617  O OH  . TYR E  259 ? 1.2933 1.4290 1.0089 -0.1572 0.1012  -0.1400 259 TYR E OH  
9618  N N   . ALA E  260 ? 0.8106 0.9436 0.5825 -0.1049 0.0676  -0.1004 260 ALA E N   
9619  C CA  . ALA E  260 ? 0.7682 0.9005 0.5495 -0.0979 0.0623  -0.0957 260 ALA E CA  
9620  C C   . ALA E  260 ? 0.8462 0.9824 0.6280 -0.1004 0.0600  -0.0983 260 ALA E C   
9621  O O   . ALA E  260 ? 0.8144 0.9528 0.5898 -0.1073 0.0630  -0.1039 260 ALA E O   
9622  C CB  . ALA E  260 ? 0.7605 0.9014 0.5413 -0.0925 0.0558  -0.0892 260 ALA E CB  
9623  N N   . PHE E  261 ? 0.8236 0.9606 0.6126 -0.0948 0.0549  -0.0945 261 PHE E N   
9624  C CA  . PHE E  261 ? 0.7069 0.8467 0.4970 -0.0967 0.0528  -0.0967 261 PHE E CA  
9625  C C   . PHE E  261 ? 0.7585 0.9077 0.5504 -0.0921 0.0448  -0.0919 261 PHE E C   
9626  O O   . PHE E  261 ? 0.7744 0.9202 0.5741 -0.0856 0.0418  -0.0873 261 PHE E O   
9627  C CB  . PHE E  261 ? 0.5617 0.6893 0.3605 -0.0957 0.0565  -0.0985 261 PHE E CB  
9628  C CG  . PHE E  261 ? 0.6446 0.7625 0.4425 -0.1003 0.0648  -0.1035 261 PHE E CG  
9629  C CD1 . PHE E  261 ? 0.7697 0.8785 0.5721 -0.0975 0.0686  -0.1018 261 PHE E CD1 
9630  C CD2 . PHE E  261 ? 0.7323 0.8503 0.5251 -0.1076 0.0691  -0.1099 261 PHE E CD2 
9631  C CE1 . PHE E  261 ? 0.7672 0.8670 0.5692 -0.1017 0.0765  -0.1063 261 PHE E CE1 
9632  C CE2 . PHE E  261 ? 0.6709 0.7796 0.4630 -0.1120 0.0771  -0.1146 261 PHE E CE2 
9633  C CZ  . PHE E  261 ? 0.7178 0.8174 0.5146 -0.1089 0.0809  -0.1128 261 PHE E CZ  
9634  N N   . ALA E  262 ? 0.8605 1.0216 0.6452 -0.0957 0.0416  -0.0929 262 ALA E N   
9635  C CA  . ALA E  262 ? 0.7211 0.8913 0.5076 -0.0922 0.0346  -0.0892 262 ALA E CA  
9636  C C   . ALA E  262 ? 0.8506 1.0153 0.6437 -0.0915 0.0345  -0.0908 262 ALA E C   
9637  O O   . ALA E  262 ? 0.9055 1.0677 0.6966 -0.0969 0.0381  -0.0963 262 ALA E O   
9638  C CB  . ALA E  262 ? 0.9635 1.1474 0.7410 -0.0969 0.0318  -0.0905 262 ALA E CB  
9639  N N   . MET E  263 ? 0.8157 0.9784 0.6164 -0.0849 0.0305  -0.0862 263 MET E N   
9640  C CA  . MET E  263 ? 0.8196 0.9748 0.6275 -0.0835 0.0310  -0.0872 263 MET E CA  
9641  C C   . MET E  263 ? 0.7729 0.9322 0.5858 -0.0782 0.0248  -0.0828 263 MET E C   
9642  O O   . MET E  263 ? 0.8988 1.0598 0.7145 -0.0726 0.0212  -0.0775 263 MET E O   
9643  C CB  . MET E  263 ? 0.7833 0.9251 0.5979 -0.0810 0.0355  -0.0868 263 MET E CB  
9644  C CG  . MET E  263 ? 0.8691 1.0023 0.6910 -0.0801 0.0368  -0.0881 263 MET E CG  
9645  S SD  . MET E  263 ? 0.8762 0.9948 0.7068 -0.0764 0.0413  -0.0865 263 MET E SD  
9646  C CE  . MET E  263 ? 0.8898 1.0108 0.7248 -0.0683 0.0354  -0.0791 263 MET E CE  
9647  N N   . GLU E  264 ? 0.8061 0.9667 0.6199 -0.0801 0.0237  -0.0851 264 GLU E N   
9648  C CA  . GLU E  264 ? 0.8812 1.0440 0.7003 -0.0755 0.0186  -0.0817 264 GLU E CA  
9649  C C   . GLU E  264 ? 0.8788 1.0314 0.7044 -0.0751 0.0208  -0.0834 264 GLU E C   
9650  O O   . GLU E  264 ? 0.9479 1.0991 0.7718 -0.0800 0.0236  -0.0881 264 GLU E O   
9651  C CB  . GLU E  264 ? 0.9429 1.1180 0.7572 -0.0780 0.0146  -0.0824 264 GLU E CB  
9652  C CG  . GLU E  264 ? 1.2054 1.3898 1.0197 -0.0733 0.0089  -0.0768 264 GLU E CG  
9653  C CD  . GLU E  264 ? 1.4509 1.6487 1.2587 -0.0769 0.0060  -0.0777 264 GLU E CD  
9654  O OE1 . GLU E  264 ? 1.4242 1.6292 1.2338 -0.0737 0.0011  -0.0744 264 GLU E OE1 
9655  O OE2 . GLU E  264 ? 1.5929 1.7940 1.3939 -0.0830 0.0088  -0.0818 264 GLU E OE2 
9656  N N   . ARG E  265 ? 0.8825 1.0282 0.7155 -0.0694 0.0196  -0.0795 265 ARG E N   
9657  C CA  . ARG E  265 ? 0.9644 1.0997 0.8040 -0.0686 0.0218  -0.0804 265 ARG E CA  
9658  C C   . ARG E  265 ? 1.0249 1.1611 0.8693 -0.0649 0.0172  -0.0778 265 ARG E C   
9659  O O   . ARG E  265 ? 0.9725 1.1136 0.8181 -0.0605 0.0124  -0.0735 265 ARG E O   
9660  C CB  . ARG E  265 ? 0.8275 0.9528 0.6725 -0.0655 0.0248  -0.0785 265 ARG E CB  
9661  C CG  . ARG E  265 ? 0.9588 1.0869 0.8038 -0.0610 0.0222  -0.0738 265 ARG E CG  
9662  C CD  . ARG E  265 ? 1.0095 1.1276 0.8600 -0.0582 0.0254  -0.0721 265 ARG E CD  
9663  N NE  . ARG E  265 ? 0.9467 1.0606 0.8049 -0.0523 0.0221  -0.0676 265 ARG E NE  
9664  C CZ  . ARG E  265 ? 0.9565 1.0730 0.8162 -0.0474 0.0185  -0.0630 265 ARG E CZ  
9665  N NH1 . ARG E  265 ? 0.9398 1.0632 0.7941 -0.0475 0.0177  -0.0620 265 ARG E NH1 
9666  N NH2 . ARG E  265 ? 1.1075 1.2198 0.9741 -0.0426 0.0159  -0.0593 265 ARG E NH2 
9667  N N   . ASN E  266 ? 1.0356 1.1670 0.8827 -0.0669 0.0188  -0.0803 266 ASN E N   
9668  C CA  . ASN E  266 ? 1.1805 1.3109 1.0324 -0.0637 0.0151  -0.0781 266 ASN E CA  
9669  C C   . ASN E  266 ? 1.1245 1.2432 0.9841 -0.0611 0.0172  -0.0767 266 ASN E C   
9670  O O   . ASN E  266 ? 1.1596 1.2712 1.0206 -0.0640 0.0222  -0.0797 266 ASN E O   
9671  C CB  . ASN E  266 ? 1.2587 1.3937 1.1077 -0.0678 0.0147  -0.0816 266 ASN E CB  
9672  C CG  . ASN E  266 ? 1.1170 1.2514 0.9612 -0.0745 0.0200  -0.0873 266 ASN E CG  
9673  O OD1 . ASN E  266 ? 1.0211 1.1641 0.8591 -0.0785 0.0194  -0.0901 266 ASN E OD1 
9674  N ND2 . ASN E  266 ? 1.0453 1.1696 0.8925 -0.0757 0.0252  -0.0891 266 ASN E ND2 
9675  N N   . ALA E  267 ? 1.0845 1.2015 0.9492 -0.0557 0.0133  -0.0722 267 ALA E N   
9676  C CA  . ALA E  267 ? 1.1596 1.2664 1.0319 -0.0529 0.0146  -0.0702 267 ALA E CA  
9677  C C   . ALA E  267 ? 1.1430 1.2447 1.0185 -0.0547 0.0160  -0.0721 267 ALA E C   
9678  O O   . ALA E  267 ? 1.0940 1.2006 0.9667 -0.0567 0.0142  -0.0738 267 ALA E O   
9679  C CB  . ALA E  267 ? 1.2277 1.3346 1.1041 -0.0469 0.0100  -0.0649 267 ALA E CB  
9680  N N   . GLY E  268 ? 1.1816 1.2736 1.0630 -0.0540 0.0192  -0.0717 268 GLY E N   
9681  C CA  . GLY E  268 ? 1.2297 1.3161 1.1154 -0.0545 0.0198  -0.0721 268 GLY E CA  
9682  C C   . GLY E  268 ? 1.2012 1.2828 1.0868 -0.0594 0.0255  -0.0765 268 GLY E C   
9683  O O   . GLY E  268 ? 1.1937 1.2740 1.0805 -0.0609 0.0256  -0.0777 268 GLY E O   
9684  N N   . SER E  269 ? 0.9078 0.9865 0.7921 -0.0620 0.0306  -0.0789 269 SER E N   
9685  C CA  . SER E  269 ? 0.7961 0.8689 0.6811 -0.0665 0.0368  -0.0831 269 SER E CA  
9686  C C   . SER E  269 ? 0.8075 0.8701 0.6995 -0.0650 0.0411  -0.0816 269 SER E C   
9687  O O   . SER E  269 ? 0.9195 0.9790 0.8171 -0.0602 0.0386  -0.0771 269 SER E O   
9688  C CB  . SER E  269 ? 0.8446 0.9224 0.7216 -0.0720 0.0402  -0.0882 269 SER E CB  
9689  O OG  . SER E  269 ? 0.6538 0.7260 0.5314 -0.0767 0.0462  -0.0926 269 SER E OG  
9690  N N   . GLY E  270 ? 0.6551 0.7125 0.5471 -0.0691 0.0478  -0.0855 270 GLY E N   
9691  C CA  . GLY E  270 ? 0.6796 0.7272 0.5788 -0.0680 0.0526  -0.0844 270 GLY E CA  
9692  C C   . GLY E  270 ? 0.5468 0.5903 0.4437 -0.0730 0.0603  -0.0893 270 GLY E C   
9693  O O   . GLY E  270 ? 0.6384 0.6873 0.5275 -0.0775 0.0618  -0.0937 270 GLY E O   
9694  N N   . ILE E  271 ? 0.5496 0.5836 0.4539 -0.0723 0.0652  -0.0884 271 ILE E N   
9695  C CA  . ILE E  271 ? 0.5178 0.5464 0.4212 -0.0767 0.0733  -0.0928 271 ILE E CA  
9696  C C   . ILE E  271 ? 0.6334 0.6528 0.5448 -0.0774 0.0783  -0.0930 271 ILE E C   
9697  O O   . ILE E  271 ? 0.7431 0.7564 0.6634 -0.0732 0.0779  -0.0886 271 ILE E O   
9698  C CB  . ILE E  271 ? 0.5557 0.5815 0.4603 -0.0751 0.0757  -0.0915 271 ILE E CB  
9699  C CG1 . ILE E  271 ? 0.6467 0.6818 0.5435 -0.0744 0.0709  -0.0910 271 ILE E CG1 
9700  C CG2 . ILE E  271 ? 0.7012 0.7206 0.6052 -0.0798 0.0846  -0.0962 271 ILE E CG2 
9701  C CD1 . ILE E  271 ? 0.7484 0.7814 0.6479 -0.0706 0.0706  -0.0876 271 ILE E CD1 
9702  N N   . ILE E  272 ? 0.6685 0.6868 0.5768 -0.0827 0.0830  -0.0981 272 ILE E N   
9703  C CA  . ILE E  272 ? 0.7383 0.7478 0.6538 -0.0837 0.0882  -0.0986 272 ILE E CA  
9704  C C   . ILE E  272 ? 0.7664 0.7681 0.6840 -0.0868 0.0972  -0.1017 272 ILE E C   
9705  O O   . ILE E  272 ? 0.8112 0.8150 0.7214 -0.0919 0.1012  -0.1071 272 ILE E O   
9706  C CB  . ILE E  272 ? 0.6805 0.6927 0.5924 -0.0876 0.0884  -0.1021 272 ILE E CB  
9707  C CG1 . ILE E  272 ? 0.6879 0.7069 0.5988 -0.0843 0.0799  -0.0987 272 ILE E CG1 
9708  C CG2 . ILE E  272 ? 0.7049 0.7077 0.6243 -0.0890 0.0947  -0.1028 272 ILE E CG2 
9709  C CD1 . ILE E  272 ? 0.6445 0.6656 0.5528 -0.0876 0.0798  -0.1015 272 ILE E CD1 
9710  N N   . ILE E  273 ? 0.7239 0.7167 0.6517 -0.0839 0.1005  -0.0984 273 ILE E N   
9711  C CA  . ILE E  273 ? 0.8709 0.8552 0.8024 -0.0866 0.1096  -0.1011 273 ILE E CA  
9712  C C   . ILE E  273 ? 0.9319 0.9098 0.8679 -0.0894 0.1151  -0.1032 273 ILE E C   
9713  O O   . ILE E  273 ? 0.9032 0.8761 0.8486 -0.0860 0.1147  -0.0989 273 ILE E O   
9714  C CB  . ILE E  273 ? 0.7897 0.7677 0.7304 -0.0818 0.1107  -0.0962 273 ILE E CB  
9715  C CG1 . ILE E  273 ? 0.8125 0.7964 0.7489 -0.0791 0.1057  -0.0941 273 ILE E CG1 
9716  C CG2 . ILE E  273 ? 0.9195 0.8883 0.8645 -0.0847 0.1207  -0.0990 273 ILE E CG2 
9717  C CD1 . ILE E  273 ? 1.0794 1.0698 1.0159 -0.0742 0.0960  -0.0892 273 ILE E CD1 
9718  N N   . SER E  274 ? 0.9740 0.9525 0.9032 -0.0956 0.1203  -0.1097 274 SER E N   
9719  C CA  . SER E  274 ? 0.8918 0.8651 0.8240 -0.0988 0.1255  -0.1123 274 SER E CA  
9720  C C   . SER E  274 ? 1.0475 1.0178 0.9745 -0.1059 0.1344  -0.1198 274 SER E C   
9721  O O   . SER E  274 ? 1.0496 1.0248 0.9675 -0.1092 0.1348  -0.1237 274 SER E O   
9722  C CB  . SER E  274 ? 0.9177 0.8978 0.8462 -0.0990 0.1193  -0.1122 274 SER E CB  
9723  O OG  . SER E  274 ? 1.0207 0.9975 0.9489 -0.1037 0.1248  -0.1165 274 SER E OG  
9724  N N   . ASP E  275 ? 1.4389 1.4010 1.3716 -0.1082 0.1416  -0.1216 275 ASP E N   
9725  C CA  . ASP E  275 ? 1.4399 1.3983 1.3681 -0.1152 0.1507  -0.1289 275 ASP E CA  
9726  C C   . ASP E  275 ? 1.3011 1.2655 1.2215 -0.1200 0.1494  -0.1336 275 ASP E C   
9727  O O   . ASP E  275 ? 1.5686 1.5340 1.4814 -0.1266 0.1545  -0.1405 275 ASP E O   
9728  C CB  . ASP E  275 ? 1.6474 1.5936 1.5863 -0.1154 0.1598  -0.1286 275 ASP E CB  
9729  C CG  . ASP E  275 ? 1.9746 1.9146 1.9221 -0.1108 0.1616  -0.1239 275 ASP E CG  
9730  O OD1 . ASP E  275 ? 2.0814 2.0183 2.0390 -0.1050 0.1586  -0.1173 275 ASP E OD1 
9731  O OD2 . ASP E  275 ? 1.9141 1.8525 1.8584 -0.1130 0.1661  -0.1269 275 ASP E OD2 
9732  N N   . THR E  276 ? 0.9151 0.8834 0.8374 -0.1169 0.1426  -0.1300 276 THR E N   
9733  C CA  . THR E  276 ? 0.9769 0.9508 0.8930 -0.1207 0.1407  -0.1336 276 THR E CA  
9734  C C   . THR E  276 ? 1.0475 1.0296 0.9508 -0.1266 0.1405  -0.1400 276 THR E C   
9735  O O   . THR E  276 ? 0.9982 0.9865 0.8962 -0.1255 0.1363  -0.1392 276 THR E O   
9736  C CB  . THR E  276 ? 0.8899 0.8699 0.8074 -0.1157 0.1311  -0.1283 276 THR E CB  
9737  O OG1 . THR E  276 ? 0.8019 0.7746 0.7309 -0.1105 0.1310  -0.1222 276 THR E OG1 
9738  C CG2 . THR E  276 ? 0.8606 0.8458 0.7724 -0.1196 0.1296  -0.1319 276 THR E CG2 
9739  N N   . PRO E  277 ? 1.0680 1.0504 0.9667 -0.1330 0.1452  -0.1462 277 PRO E N   
9740  C CA  . PRO E  277 ? 1.0914 1.0817 0.9780 -0.1395 0.1456  -0.1527 277 PRO E CA  
9741  C C   . PRO E  277 ? 1.0262 1.0292 0.9057 -0.1379 0.1354  -0.1510 277 PRO E C   
9742  O O   . PRO E  277 ? 0.9739 0.9798 0.8561 -0.1346 0.1297  -0.1476 277 PRO E O   
9743  C CB  . PRO E  277 ? 1.2395 1.2264 1.1252 -0.1455 0.1520  -0.1585 277 PRO E CB  
9744  C CG  . PRO E  277 ? 1.2774 1.2520 1.1748 -0.1430 0.1581  -0.1559 277 PRO E CG  
9745  C CD  . PRO E  277 ? 1.0488 1.0231 0.9540 -0.1346 0.1513  -0.1474 277 PRO E CD  
9746  N N   . VAL E  278 ? 1.0628 1.0734 0.9333 -0.1403 0.1334  -0.1533 278 VAL E N   
9747  C CA  . VAL E  278 ? 1.0850 1.1084 0.9479 -0.1399 0.1247  -0.1526 278 VAL E CA  
9748  C C   . VAL E  278 ? 1.0412 1.0696 0.8980 -0.1463 0.1258  -0.1584 278 VAL E C   
9749  O O   . VAL E  278 ? 1.0868 1.1112 0.9408 -0.1527 0.1336  -0.1646 278 VAL E O   
9750  C CB  . VAL E  278 ? 0.9956 1.0257 0.8510 -0.1406 0.1225  -0.1531 278 VAL E CB  
9751  C CG1 . VAL E  278 ? 1.2090 1.2363 1.0584 -0.1481 0.1309  -0.1601 278 VAL E CG1 
9752  C CG2 . VAL E  278 ? 0.8503 0.8939 0.6981 -0.1405 0.1138  -0.1523 278 VAL E CG2 
9753  N N   . HIS E  279 ? 0.9703 1.0071 0.8249 -0.1446 0.1184  -0.1565 279 HIS E N   
9754  C CA  . HIS E  279 ? 1.0396 1.0811 0.8896 -0.1502 0.1191  -0.1614 279 HIS E CA  
9755  C C   . HIS E  279 ? 1.1319 1.1873 0.9741 -0.1507 0.1109  -0.1613 279 HIS E C   
9756  O O   . HIS E  279 ? 1.2725 1.3336 1.1149 -0.1452 0.1036  -0.1560 279 HIS E O   
9757  C CB  . HIS E  279 ? 1.2638 1.2987 1.1217 -0.1481 0.1203  -0.1597 279 HIS E CB  
9758  C CG  . HIS E  279 ? 1.4269 1.4520 1.2875 -0.1531 0.1302  -0.1646 279 HIS E CG  
9759  N ND1 . HIS E  279 ? 1.3475 1.3744 1.2045 -0.1592 0.1333  -0.1702 279 HIS E ND1 
9760  C CD2 . HIS E  279 ? 1.4116 1.4252 1.2785 -0.1530 0.1380  -0.1649 279 HIS E CD2 
9761  C CE1 . HIS E  279 ? 1.5819 1.5984 1.4427 -0.1626 0.1427  -0.1737 279 HIS E CE1 
9762  N NE2 . HIS E  279 ? 1.4946 1.5029 1.3616 -0.1589 0.1457  -0.1705 279 HIS E NE2 
9763  N N   . ASP E  280 ? 1.2181 1.2790 1.0537 -0.1573 0.1125  -0.1671 280 ASP E N   
9764  C CA  . ASP E  280 ? 1.4154 1.4897 1.2446 -0.1583 0.1052  -0.1672 280 ASP E CA  
9765  C C   . ASP E  280 ? 1.4023 1.4771 1.2360 -0.1555 0.1015  -0.1648 280 ASP E C   
9766  O O   . ASP E  280 ? 1.6660 1.7422 1.4978 -0.1603 0.1037  -0.1692 280 ASP E O   
9767  C CB  . ASP E  280 ? 1.5408 1.6215 1.3605 -0.1671 0.1085  -0.1747 280 ASP E CB  
9768  C CG  . ASP E  280 ? 1.7057 1.8005 1.5193 -0.1685 0.1012  -0.1749 280 ASP E CG  
9769  O OD1 . ASP E  280 ? 1.6396 1.7399 1.4550 -0.1624 0.0934  -0.1692 280 ASP E OD1 
9770  O OD2 . ASP E  280 ? 1.7976 1.8977 1.6045 -0.1757 0.1035  -0.1809 280 ASP E OD2 
9771  N N   . CYS E  281 ? 1.2597 1.3333 1.0995 -0.1479 0.0959  -0.1580 281 CYS E N   
9772  C CA  . CYS E  281 ? 1.2573 1.3313 1.1016 -0.1446 0.0918  -0.1549 281 CYS E CA  
9773  C C   . CYS E  281 ? 1.0132 1.0926 0.8592 -0.1374 0.0830  -0.1480 281 CYS E C   
9774  O O   . CYS E  281 ? 1.0195 1.0990 0.8659 -0.1339 0.0812  -0.1449 281 CYS E O   
9775  C CB  . CYS E  281 ? 1.0844 1.1455 0.9374 -0.1431 0.0973  -0.1539 281 CYS E CB  
9776  S SG  . CYS E  281 ? 1.5432 1.5937 1.4043 -0.1371 0.0993  -0.1486 281 CYS E SG  
9777  N N   . ASN E  282 ? 1.0705 1.1544 0.9177 -0.1352 0.0778  -0.1459 282 ASN E N   
9778  C CA  . ASN E  282 ? 0.9873 1.0761 0.8362 -0.1286 0.0696  -0.1396 282 ASN E CA  
9779  C C   . ASN E  282 ? 0.9751 1.0549 0.8328 -0.1230 0.0690  -0.1346 282 ASN E C   
9780  O O   . ASN E  282 ? 1.0425 1.1158 0.9039 -0.1245 0.0728  -0.1360 282 ASN E O   
9781  C CB  . ASN E  282 ? 1.0764 1.1765 0.9207 -0.1299 0.0642  -0.1405 282 ASN E CB  
9782  C CG  . ASN E  282 ? 1.2581 1.3654 1.1024 -0.1241 0.0560  -0.1349 282 ASN E CG  
9783  O OD1 . ASN E  282 ? 1.1962 1.3027 1.0415 -0.1202 0.0541  -0.1313 282 ASN E OD1 
9784  N ND2 . ASN E  282 ? 1.5811 1.6955 1.4243 -0.1235 0.0512  -0.1341 282 ASN E ND2 
9785  N N   . THR E  283 ? 0.8873 0.9669 0.7483 -0.1167 0.0642  -0.1288 283 THR E N   
9786  C CA  . THR E  283 ? 0.8437 0.9158 0.7128 -0.1112 0.0627  -0.1236 283 THR E CA  
9787  C C   . THR E  283 ? 0.7322 0.8094 0.6020 -0.1052 0.0549  -0.1179 283 THR E C   
9788  O O   . THR E  283 ? 0.7796 0.8640 0.6448 -0.1047 0.0519  -0.1176 283 THR E O   
9789  C CB  . THR E  283 ? 0.8293 0.8901 0.7046 -0.1100 0.0684  -0.1225 283 THR E CB  
9790  O OG1 . THR E  283 ? 0.6785 0.7323 0.5617 -0.1054 0.0671  -0.1176 283 THR E OG1 
9791  C CG2 . THR E  283 ? 0.6894 0.7512 0.5638 -0.1076 0.0673  -0.1205 283 THR E CG2 
9792  N N   . THR E  284 ? 0.8021 0.8756 0.6775 -0.1007 0.0518  -0.1133 284 THR E N   
9793  C CA  . THR E  284 ? 0.8434 0.9207 0.7199 -0.0949 0.0448  -0.1079 284 THR E CA  
9794  C C   . THR E  284 ? 0.7101 0.7793 0.5934 -0.0902 0.0452  -0.1033 284 THR E C   
9795  O O   . THR E  284 ? 0.5608 0.6321 0.4455 -0.0855 0.0402  -0.0989 284 THR E O   
9796  C CB  . THR E  284 ? 0.7911 0.8710 0.6687 -0.0930 0.0402  -0.1059 284 THR E CB  
9797  O OG1 . THR E  284 ? 0.7793 0.8640 0.6568 -0.0880 0.0336  -0.1013 284 THR E OG1 
9798  C CG2 . THR E  284 ? 0.7896 0.8597 0.6740 -0.0917 0.0426  -0.1039 284 THR E CG2 
9799  N N   . CYS E  285 ? 0.6118 0.6718 0.4997 -0.0916 0.0512  -0.1043 285 CYS E N   
9800  C CA  . CYS E  285 ? 0.5172 0.5690 0.4126 -0.0874 0.0521  -0.0999 285 CYS E CA  
9801  C C   . CYS E  285 ? 0.5605 0.6049 0.4582 -0.0905 0.0599  -0.1028 285 CYS E C   
9802  O O   . CYS E  285 ? 0.6255 0.6663 0.5232 -0.0947 0.0652  -0.1066 285 CYS E O   
9803  C CB  . CYS E  285 ? 0.5746 0.6214 0.4761 -0.0846 0.0503  -0.0961 285 CYS E CB  
9804  S SG  . CYS E  285 ? 0.7840 0.8209 0.6954 -0.0797 0.0512  -0.0903 285 CYS E SG  
9805  N N   . GLN E  286 ? 0.5003 0.5424 0.3998 -0.0884 0.0608  -0.1011 286 GLN E N   
9806  C CA  . GLN E  286 ? 0.5711 0.6064 0.4723 -0.0912 0.0684  -0.1039 286 GLN E CA  
9807  C C   . GLN E  286 ? 0.6086 0.6350 0.5190 -0.0870 0.0701  -0.0993 286 GLN E C   
9808  O O   . GLN E  286 ? 0.7102 0.7377 0.6230 -0.0822 0.0654  -0.0946 286 GLN E O   
9809  C CB  . GLN E  286 ? 0.4634 0.5042 0.3575 -0.0937 0.0692  -0.1071 286 GLN E CB  
9810  C CG  . GLN E  286 ? 0.5980 0.6325 0.4925 -0.0976 0.0775  -0.1110 286 GLN E CG  
9811  C CD  . GLN E  286 ? 0.7483 0.7798 0.6415 -0.1033 0.0835  -0.1163 286 GLN E CD  
9812  O OE1 . GLN E  286 ? 0.7210 0.7594 0.6074 -0.1073 0.0826  -0.1204 286 GLN E OE1 
9813  N NE2 . GLN E  286 ? 0.6149 0.6363 0.5153 -0.1036 0.0897  -0.1163 286 GLN E NE2 
9814  N N   . THR E  287 ? 0.5003 0.5180 0.4160 -0.0889 0.0769  -0.1005 287 THR E N   
9815  C CA  . THR E  287 ? 0.5652 0.5742 0.4902 -0.0854 0.0795  -0.0964 287 THR E CA  
9816  C C   . THR E  287 ? 0.6456 0.6490 0.5711 -0.0889 0.0878  -0.1002 287 THR E C   
9817  O O   . THR E  287 ? 0.7753 0.7802 0.6948 -0.0943 0.0921  -0.1062 287 THR E O   
9818  C CB  . THR E  287 ? 0.6455 0.6481 0.5783 -0.0839 0.0804  -0.0934 287 THR E CB  
9819  O OG1 . THR E  287 ? 0.5252 0.5211 0.4604 -0.0880 0.0888  -0.0971 287 THR E OG1 
9820  C CG2 . THR E  287 ? 0.4837 0.4921 0.4132 -0.0835 0.0746  -0.0926 287 THR E CG2 
9821  N N   . PRO E  288 ? 0.6817 0.6785 0.6144 -0.0858 0.0901  -0.0969 288 PRO E N   
9822  C CA  . PRO E  288 ? 0.7866 0.7772 0.7209 -0.0887 0.0985  -0.1001 288 PRO E CA  
9823  C C   . PRO E  288 ? 0.7352 0.7194 0.6717 -0.0932 0.1063  -0.1041 288 PRO E C   
9824  O O   . PRO E  288 ? 0.7518 0.7325 0.6862 -0.0975 0.1135  -0.1089 288 PRO E O   
9825  C CB  . PRO E  288 ? 0.7967 0.7810 0.7406 -0.0836 0.0986  -0.0944 288 PRO E CB  
9826  C CG  . PRO E  288 ? 0.6086 0.5989 0.5523 -0.0785 0.0893  -0.0893 288 PRO E CG  
9827  C CD  . PRO E  288 ? 0.6479 0.6437 0.5872 -0.0795 0.0848  -0.0900 288 PRO E CD  
9828  N N   . LYS E  289 ? 0.6967 0.6791 0.6371 -0.0924 0.1051  -0.1022 289 LYS E N   
9829  C CA  . LYS E  289 ? 0.8293 0.8050 0.7729 -0.0962 0.1126  -0.1053 289 LYS E CA  
9830  C C   . LYS E  289 ? 0.8308 0.8120 0.7654 -0.1017 0.1132  -0.1114 289 LYS E C   
9831  O O   . LYS E  289 ? 0.9028 0.8794 0.8371 -0.1065 0.1205  -0.1161 289 LYS E O   
9832  C CB  . LYS E  289 ? 0.7312 0.7016 0.6844 -0.0924 0.1115  -0.0997 289 LYS E CB  
9833  C CG  . LYS E  289 ? 0.9600 0.9259 0.9225 -0.0867 0.1099  -0.0931 289 LYS E CG  
9834  C CD  . LYS E  289 ? 0.9485 0.9112 0.9194 -0.0828 0.1070  -0.0870 289 LYS E CD  
9835  C CE  . LYS E  289 ? 0.9782 0.9330 0.9550 -0.0853 0.1145  -0.0882 289 LYS E CE  
9836  N NZ  . LYS E  289 ? 1.0971 1.0448 1.0861 -0.0809 0.1154  -0.0814 289 LYS E NZ  
9837  N N   . GLY E  290 ? 0.7039 0.6948 0.6312 -0.1012 0.1056  -0.1114 290 GLY E N   
9838  C CA  . GLY E  290 ? 0.7694 0.7665 0.6885 -0.1060 0.1051  -0.1166 290 GLY E CA  
9839  C C   . GLY E  290 ? 0.8000 0.8063 0.7149 -0.1034 0.0958  -0.1141 290 GLY E C   
9840  O O   . GLY E  290 ? 0.8391 0.8459 0.7581 -0.0978 0.0901  -0.1081 290 GLY E O   
9841  N N   . ALA E  291 ? 0.8211 0.8349 0.7279 -0.1075 0.0944  -0.1186 291 ALA E N   
9842  C CA  . ALA E  291 ? 0.7135 0.7366 0.6158 -0.1055 0.0860  -0.1167 291 ALA E CA  
9843  C C   . ALA E  291 ? 0.7780 0.7994 0.6844 -0.1036 0.0835  -0.1139 291 ALA E C   
9844  O O   . ALA E  291 ? 0.7753 0.7895 0.6863 -0.1053 0.0888  -0.1148 291 ALA E O   
9845  C CB  . ALA E  291 ? 0.5691 0.6014 0.4613 -0.1107 0.0854  -0.1224 291 ALA E CB  
9846  N N   . ILE E  292 ? 0.7609 0.7888 0.6656 -0.1001 0.0756  -0.1105 292 ILE E N   
9847  C CA  . ILE E  292 ? 0.7355 0.7626 0.6432 -0.0981 0.0724  -0.1076 292 ILE E CA  
9848  C C   . ILE E  292 ? 0.8771 0.9137 0.7776 -0.1001 0.0679  -0.1100 292 ILE E C   
9849  O O   . ILE E  292 ? 0.8888 0.9330 0.7857 -0.0977 0.0615  -0.1082 292 ILE E O   
9850  C CB  . ILE E  292 ? 0.6818 0.7068 0.5954 -0.0915 0.0670  -0.1004 292 ILE E CB  
9851  C CG1 . ILE E  292 ? 0.5571 0.5723 0.4793 -0.0895 0.0716  -0.0975 292 ILE E CG1 
9852  C CG2 . ILE E  292 ? 0.8186 0.8448 0.7335 -0.0896 0.0625  -0.0975 292 ILE E CG2 
9853  C CD1 . ILE E  292 ? 0.7615 0.7717 0.6914 -0.0850 0.0689  -0.0913 292 ILE E CD1 
9854  N N   . ASN E  293 ? 1.1017 1.1379 1.0005 -0.1045 0.0714  -0.1141 293 ASN E N   
9855  C CA  . ASN E  293 ? 1.2646 1.3088 1.1579 -0.1064 0.0676  -0.1161 293 ASN E CA  
9856  C C   . ASN E  293 ? 1.2943 1.3358 1.1919 -0.1034 0.0647  -0.1121 293 ASN E C   
9857  O O   . ASN E  293 ? 1.4801 1.5166 1.3800 -0.1058 0.0688  -0.1137 293 ASN E O   
9858  C CB  . ASN E  293 ? 1.4220 1.4678 1.3104 -0.1134 0.0731  -0.1232 293 ASN E CB  
9859  C CG  . ASN E  293 ? 1.6454 1.6928 1.5330 -0.1154 0.0726  -0.1247 293 ASN E CG  
9860  O OD1 . ASN E  293 ? 1.5031 1.5590 1.3863 -0.1153 0.0672  -0.1248 293 ASN E OD1 
9861  N ND2 . ASN E  293 ? 1.6501 1.6892 1.5423 -0.1172 0.0783  -0.1257 293 ASN E ND2 
9862  N N   . THR E  294 ? 1.0969 1.1412 0.9956 -0.0983 0.0578  -0.1070 294 THR E N   
9863  C CA  . THR E  294 ? 1.2996 1.3410 1.2021 -0.0956 0.0550  -0.1031 294 THR E CA  
9864  C C   . THR E  294 ? 1.1737 1.2219 1.0739 -0.0919 0.0470  -0.0997 294 THR E C   
9865  O O   . THR E  294 ? 0.9838 1.0370 0.8818 -0.0894 0.0428  -0.0980 294 THR E O   
9866  C CB  . THR E  294 ? 1.1545 1.1859 1.0656 -0.0924 0.0573  -0.0985 294 THR E CB  
9867  O OG1 . THR E  294 ? 1.0176 1.0445 0.9320 -0.0926 0.0584  -0.0972 294 THR E OG1 
9868  C CG2 . THR E  294 ? 0.9897 1.0217 0.9035 -0.0867 0.0516  -0.0927 294 THR E CG2 
9869  N N   . SER E  295 ? 0.9502 0.9982 0.8508 -0.0919 0.0453  -0.0988 295 SER E N   
9870  C CA  . SER E  295 ? 1.0112 1.0643 0.9101 -0.0886 0.0384  -0.0955 295 SER E CA  
9871  C C   . SER E  295 ? 0.9267 0.9736 0.8317 -0.0839 0.0359  -0.0893 295 SER E C   
9872  O O   . SER E  295 ? 0.9107 0.9606 0.8151 -0.0804 0.0300  -0.0858 295 SER E O   
9873  C CB  . SER E  295 ? 1.0068 1.0634 0.9024 -0.0915 0.0380  -0.0982 295 SER E CB  
9874  O OG  . SER E  295 ? 1.3970 1.4636 1.2864 -0.0930 0.0350  -0.1010 295 SER E OG  
9875  N N   . LEU E  296 ? 0.6791 0.7173 0.5900 -0.0839 0.0405  -0.0880 296 LEU E N   
9876  C CA  . LEU E  296 ? 0.6810 0.7131 0.5983 -0.0799 0.0386  -0.0820 296 LEU E CA  
9877  C C   . LEU E  296 ? 0.6518 0.6853 0.5705 -0.0754 0.0340  -0.0780 296 LEU E C   
9878  O O   . LEU E  296 ? 0.5666 0.6023 0.4838 -0.0756 0.0348  -0.0796 296 LEU E O   
9879  C CB  . LEU E  296 ? 0.6860 0.7088 0.6098 -0.0809 0.0450  -0.0815 296 LEU E CB  
9880  C CG  . LEU E  296 ? 0.6972 0.7175 0.6205 -0.0853 0.0503  -0.0853 296 LEU E CG  
9881  C CD1 . LEU E  296 ? 0.7512 0.7619 0.6820 -0.0856 0.0565  -0.0839 296 LEU E CD1 
9882  C CD2 . LEU E  296 ? 0.6522 0.6751 0.5731 -0.0851 0.0465  -0.0843 296 LEU E CD2 
9883  N N   . PRO E  297 ? 0.6631 0.6952 0.5846 -0.0717 0.0293  -0.0727 297 PRO E N   
9884  C CA  . PRO E  297 ? 0.5238 0.5574 0.4465 -0.0674 0.0244  -0.0687 297 PRO E CA  
9885  C C   . PRO E  297 ? 0.6096 0.6372 0.5387 -0.0655 0.0270  -0.0661 297 PRO E C   
9886  O O   . PRO E  297 ? 0.5925 0.6219 0.5220 -0.0628 0.0242  -0.0641 297 PRO E O   
9887  C CB  . PRO E  297 ? 0.6254 0.6583 0.5495 -0.0648 0.0195  -0.0642 297 PRO E CB  
9888  C CG  . PRO E  297 ? 0.7935 0.8267 0.7150 -0.0679 0.0211  -0.0667 297 PRO E CG  
9889  C CD  . PRO E  297 ? 0.7132 0.7428 0.6361 -0.0715 0.0282  -0.0706 297 PRO E CD  
9890  N N   . PHE E  298 ? 0.5685 0.5891 0.5028 -0.0670 0.0325  -0.0661 298 PHE E N   
9891  C CA  . PHE E  298 ? 0.6333 0.6477 0.5747 -0.0650 0.0351  -0.0630 298 PHE E CA  
9892  C C   . PHE E  298 ? 0.6369 0.6464 0.5806 -0.0682 0.0430  -0.0666 298 PHE E C   
9893  O O   . PHE E  298 ? 0.6794 0.6876 0.6217 -0.0718 0.0470  -0.0700 298 PHE E O   
9894  C CB  . PHE E  298 ? 0.6524 0.6617 0.6005 -0.0621 0.0330  -0.0570 298 PHE E CB  
9895  C CG  . PHE E  298 ? 0.5507 0.5641 0.4960 -0.0597 0.0259  -0.0539 298 PHE E CG  
9896  C CD1 . PHE E  298 ? 0.5324 0.5492 0.4769 -0.0565 0.0206  -0.0514 298 PHE E CD1 
9897  C CD2 . PHE E  298 ? 0.5634 0.5770 0.5070 -0.0609 0.0247  -0.0537 298 PHE E CD2 
9898  C CE1 . PHE E  298 ? 0.6860 0.7063 0.6279 -0.0546 0.0144  -0.0488 298 PHE E CE1 
9899  C CE2 . PHE E  298 ? 0.5808 0.5979 0.5216 -0.0589 0.0184  -0.0511 298 PHE E CE2 
9900  C CZ  . PHE E  298 ? 0.5716 0.5920 0.5115 -0.0558 0.0133  -0.0487 298 PHE E CZ  
9901  N N   . GLN E  299 ? 0.6280 0.6346 0.5754 -0.0671 0.0454  -0.0659 299 GLN E N   
9902  C CA  . GLN E  299 ? 0.6282 0.6294 0.5785 -0.0699 0.0533  -0.0689 299 GLN E CA  
9903  C C   . GLN E  299 ? 0.5869 0.5813 0.5463 -0.0669 0.0554  -0.0644 299 GLN E C   
9904  O O   . GLN E  299 ? 0.9102 0.9059 0.8716 -0.0632 0.0509  -0.0605 299 GLN E O   
9905  C CB  . GLN E  299 ? 0.5518 0.5576 0.4954 -0.0729 0.0554  -0.0746 299 GLN E CB  
9906  C CG  . GLN E  299 ? 0.5410 0.5511 0.4825 -0.0700 0.0511  -0.0731 299 GLN E CG  
9907  C CD  . GLN E  299 ? 0.5671 0.5716 0.5147 -0.0685 0.0548  -0.0713 299 GLN E CD  
9908  O OE1 . GLN E  299 ? 0.6266 0.6242 0.5793 -0.0701 0.0612  -0.0721 299 GLN E OE1 
9909  N NE2 . GLN E  299 ? 0.4868 0.4941 0.4342 -0.0653 0.0509  -0.0690 299 GLN E NE2 
9910  N N   . ASN E  300 ? 0.6043 0.5915 0.5695 -0.0686 0.0623  -0.0649 300 ASN E N   
9911  C CA  . ASN E  300 ? 0.5884 0.5688 0.5631 -0.0659 0.0650  -0.0606 300 ASN E CA  
9912  C C   . ASN E  300 ? 0.4920 0.4682 0.4680 -0.0685 0.0728  -0.0646 300 ASN E C   
9913  O O   . ASN E  300 ? 0.5834 0.5526 0.5679 -0.0675 0.0776  -0.0622 300 ASN E O   
9914  C CB  . ASN E  300 ? 0.4804 0.4550 0.4628 -0.0648 0.0663  -0.0561 300 ASN E CB  
9915  C CG  . ASN E  300 ? 0.6145 0.5848 0.5972 -0.0689 0.0734  -0.0600 300 ASN E CG  
9916  O OD1 . ASN E  300 ? 0.8057 0.7784 0.7818 -0.0729 0.0766  -0.0664 300 ASN E OD1 
9917  N ND2 . ASN E  300 ? 0.6026 0.5668 0.5931 -0.0680 0.0759  -0.0561 300 ASN E ND2 
9918  N N   . ILE E  301 ? 0.5217 0.5026 0.4895 -0.0719 0.0742  -0.0706 301 ILE E N   
9919  C CA  . ILE E  301 ? 0.5762 0.5538 0.5436 -0.0752 0.0816  -0.0753 301 ILE E CA  
9920  C C   . ILE E  301 ? 0.6073 0.5839 0.5776 -0.0725 0.0815  -0.0732 301 ILE E C   
9921  O O   . ILE E  301 ? 0.7724 0.7420 0.7496 -0.0723 0.0874  -0.0724 301 ILE E O   
9922  C CB  . ILE E  301 ? 0.7138 0.6973 0.6709 -0.0800 0.0828  -0.0824 301 ILE E CB  
9923  C CG1 . ILE E  301 ? 0.6403 0.6236 0.5952 -0.0833 0.0845  -0.0850 301 ILE E CG1 
9924  C CG2 . ILE E  301 ? 0.6325 0.6131 0.5883 -0.0834 0.0900  -0.0872 301 ILE E CG2 
9925  C CD1 . ILE E  301 ? 0.8167 0.8058 0.7620 -0.0885 0.0859  -0.0921 301 ILE E CD1 
9926  N N   . HIS E  302 ? 0.5184 0.5017 0.4836 -0.0704 0.0750  -0.0724 302 HIS E N   
9927  C CA  . HIS E  302 ? 0.6271 0.6101 0.5941 -0.0680 0.0746  -0.0708 302 HIS E CA  
9928  C C   . HIS E  302 ? 0.6008 0.5905 0.5651 -0.0641 0.0659  -0.0673 302 HIS E C   
9929  O O   . HIS E  302 ? 0.6059 0.6024 0.5628 -0.0648 0.0612  -0.0688 302 HIS E O   
9930  C CB  . HIS E  302 ? 0.6319 0.6161 0.5929 -0.0720 0.0797  -0.0769 302 HIS E CB  
9931  C CG  . HIS E  302 ? 0.7031 0.6837 0.6682 -0.0704 0.0826  -0.0757 302 HIS E CG  
9932  N ND1 . HIS E  302 ? 0.6119 0.5967 0.5752 -0.0673 0.0776  -0.0735 302 HIS E ND1 
9933  C CD2 . HIS E  302 ? 0.7303 0.7032 0.7012 -0.0715 0.0902  -0.0766 302 HIS E CD2 
9934  C CE1 . HIS E  302 ? 0.6562 0.6363 0.6240 -0.0666 0.0819  -0.0730 302 HIS E CE1 
9935  N NE2 . HIS E  302 ? 0.6158 0.5886 0.5883 -0.0691 0.0897  -0.0748 302 HIS E NE2 
9936  N N   . PRO E  303 ? 0.5633 0.5507 0.5336 -0.0601 0.0641  -0.0626 303 PRO E N   
9937  C CA  . PRO E  303 ? 0.4870 0.4797 0.4556 -0.0562 0.0564  -0.0590 303 PRO E CA  
9938  C C   . PRO E  303 ? 0.6368 0.6360 0.5971 -0.0572 0.0548  -0.0625 303 PRO E C   
9939  O O   . PRO E  303 ? 0.5123 0.5182 0.4670 -0.0561 0.0488  -0.0621 303 PRO E O   
9940  C CB  . PRO E  303 ? 0.5001 0.4874 0.4784 -0.0525 0.0568  -0.0537 303 PRO E CB  
9941  C CG  . PRO E  303 ? 0.7542 0.7335 0.7400 -0.0538 0.0635  -0.0533 303 PRO E CG  
9942  C CD  . PRO E  303 ? 0.6841 0.6633 0.6641 -0.0589 0.0694  -0.0600 303 PRO E CD  
9943  N N   . ILE E  304 ? 0.6157 0.6127 0.5753 -0.0592 0.0604  -0.0656 304 ILE E N   
9944  C CA  . ILE E  304 ? 0.5663 0.5692 0.5178 -0.0604 0.0595  -0.0689 304 ILE E CA  
9945  C C   . ILE E  304 ? 0.5098 0.5182 0.4524 -0.0650 0.0601  -0.0744 304 ILE E C   
9946  O O   . ILE E  304 ? 0.7243 0.7295 0.6664 -0.0690 0.0659  -0.0783 304 ILE E O   
9947  C CB  . ILE E  304 ? 0.4779 0.4767 0.4313 -0.0613 0.0654  -0.0705 304 ILE E CB  
9948  C CG1 . ILE E  304 ? 0.4546 0.4506 0.4151 -0.0565 0.0631  -0.0651 304 ILE E CG1 
9949  C CG2 . ILE E  304 ? 0.6770 0.6819 0.6207 -0.0642 0.0658  -0.0752 304 ILE E CG2 
9950  C CD1 . ILE E  304 ? 0.6647 0.6545 0.6355 -0.0537 0.0630  -0.0600 304 ILE E CD1 
9951  N N   . THR E  305 ? 0.5330 0.5497 0.4687 -0.0643 0.0542  -0.0747 305 THR E N   
9952  C CA  . THR E  305 ? 0.4628 0.4858 0.3906 -0.0681 0.0535  -0.0792 305 THR E CA  
9953  C C   . THR E  305 ? 0.6590 0.6909 0.5788 -0.0681 0.0496  -0.0806 305 THR E C   
9954  O O   . THR E  305 ? 0.6867 0.7207 0.6072 -0.0642 0.0454  -0.0770 305 THR E O   
9955  C CB  . THR E  305 ? 0.5390 0.5632 0.4677 -0.0671 0.0495  -0.0772 305 THR E CB  
9956  O OG1 . THR E  305 ? 0.8062 0.8302 0.7320 -0.0718 0.0532  -0.0817 305 THR E OG1 
9957  C CG2 . THR E  305 ? 0.5533 0.5858 0.4770 -0.0648 0.0419  -0.0756 305 THR E CG2 
9958  N N   . ILE E  306 ? 0.6177 0.6550 0.5300 -0.0726 0.0510  -0.0857 306 ILE E N   
9959  C CA  . ILE E  306 ? 0.5406 0.5873 0.4452 -0.0729 0.0472  -0.0869 306 ILE E CA  
9960  C C   . ILE E  306 ? 0.5817 0.6356 0.4803 -0.0755 0.0445  -0.0896 306 ILE E C   
9961  O O   . ILE E  306 ? 0.6099 0.6623 0.5072 -0.0797 0.0483  -0.0934 306 ILE E O   
9962  C CB  . ILE E  306 ? 0.4725 0.5201 0.3726 -0.0762 0.0517  -0.0907 306 ILE E CB  
9963  C CG1 . ILE E  306 ? 0.5510 0.5909 0.4573 -0.0739 0.0551  -0.0884 306 ILE E CG1 
9964  C CG2 . ILE E  306 ? 0.4856 0.5431 0.3783 -0.0759 0.0472  -0.0911 306 ILE E CG2 
9965  C CD1 . ILE E  306 ? 0.5194 0.5602 0.4211 -0.0766 0.0592  -0.0916 306 ILE E CD1 
9966  N N   . GLY E  307 ? 0.6262 0.6878 0.5215 -0.0730 0.0381  -0.0875 307 GLY E N   
9967  C CA  . GLY E  307 ? 0.6730 0.7421 0.5630 -0.0750 0.0350  -0.0895 307 GLY E CA  
9968  C C   . GLY E  307 ? 0.6203 0.6895 0.5135 -0.0715 0.0300  -0.0857 307 GLY E C   
9969  O O   . GLY E  307 ? 0.7274 0.7936 0.6252 -0.0669 0.0271  -0.0810 307 GLY E O   
9970  N N   . LYS E  308 ? 0.5813 0.6540 0.4717 -0.0738 0.0290  -0.0878 308 LYS E N   
9971  C CA  . LYS E  308 ? 0.6600 0.7322 0.5530 -0.0711 0.0249  -0.0847 308 LYS E CA  
9972  C C   . LYS E  308 ? 0.5253 0.5895 0.4229 -0.0727 0.0288  -0.0852 308 LYS E C   
9973  O O   . LYS E  308 ? 0.7086 0.7737 0.6038 -0.0767 0.0313  -0.0889 308 LYS E O   
9974  C CB  . LYS E  308 ? 0.7127 0.7941 0.6001 -0.0723 0.0210  -0.0862 308 LYS E CB  
9975  C CG  . LYS E  308 ? 0.9365 1.0176 0.8261 -0.0698 0.0169  -0.0832 308 LYS E CG  
9976  C CD  . LYS E  308 ? 1.0855 1.1757 0.9698 -0.0710 0.0135  -0.0849 308 LYS E CD  
9977  C CE  . LYS E  308 ? 1.1082 1.2063 0.9892 -0.0687 0.0094  -0.0834 308 LYS E CE  
9978  N NZ  . LYS E  308 ? 1.2199 1.3248 1.0987 -0.0674 0.0046  -0.0824 308 LYS E NZ  
9979  N N   . CYS E  309 ? 0.6712 0.7278 0.5757 -0.0696 0.0293  -0.0814 309 CYS E N   
9980  C CA  . CYS E  309 ? 0.7019 0.7501 0.6116 -0.0710 0.0339  -0.0815 309 CYS E CA  
9981  C C   . CYS E  309 ? 0.5648 0.6096 0.4791 -0.0681 0.0307  -0.0772 309 CYS E C   
9982  O O   . CYS E  309 ? 0.6435 0.6905 0.5584 -0.0642 0.0252  -0.0733 309 CYS E O   
9983  C CB  . CYS E  309 ? 0.5088 0.5500 0.4234 -0.0706 0.0387  -0.0809 309 CYS E CB  
9984  S SG  . CYS E  309 ? 0.8259 0.8703 0.7349 -0.0742 0.0429  -0.0859 309 CYS E SG  
9985  N N   . PRO E  310 ? 0.5593 0.5985 0.4768 -0.0700 0.0343  -0.0778 310 PRO E N   
9986  C CA  . PRO E  310 ? 0.6361 0.6709 0.5588 -0.0674 0.0319  -0.0734 310 PRO E CA  
9987  C C   . PRO E  310 ? 0.6173 0.6469 0.5467 -0.0633 0.0310  -0.0683 310 PRO E C   
9988  O O   . PRO E  310 ? 0.5347 0.5622 0.4659 -0.0632 0.0340  -0.0688 310 PRO E O   
9989  C CB  . PRO E  310 ? 0.5829 0.6120 0.5080 -0.0708 0.0377  -0.0756 310 PRO E CB  
9990  C CG  . PRO E  310 ? 0.5851 0.6182 0.5041 -0.0756 0.0414  -0.0819 310 PRO E CG  
9991  C CD  . PRO E  310 ? 0.5214 0.5584 0.4376 -0.0750 0.0408  -0.0829 310 PRO E CD  
9992  N N   . LYS E  311 ? 0.5770 0.6047 0.5102 -0.0601 0.0270  -0.0635 311 LYS E N   
9993  C CA  . LYS E  311 ? 0.4670 0.4902 0.4069 -0.0564 0.0257  -0.0584 311 LYS E CA  
9994  C C   . LYS E  311 ? 0.6141 0.6291 0.5615 -0.0570 0.0315  -0.0574 311 LYS E C   
9995  O O   . LYS E  311 ? 0.6100 0.6214 0.5590 -0.0591 0.0347  -0.0583 311 LYS E O   
9996  C CB  . LYS E  311 ? 0.4930 0.5169 0.4344 -0.0532 0.0195  -0.0536 311 LYS E CB  
9997  C CG  . LYS E  311 ? 0.5355 0.5645 0.4742 -0.0501 0.0139  -0.0518 311 LYS E CG  
9998  C CD  . LYS E  311 ? 0.5370 0.5726 0.4689 -0.0517 0.0142  -0.0561 311 LYS E CD  
9999  C CE  . LYS E  311 ? 0.5292 0.5713 0.4566 -0.0494 0.0080  -0.0550 311 LYS E CE  
10000 N NZ  . LYS E  311 ? 0.4265 0.4722 0.3523 -0.0478 0.0071  -0.0551 311 LYS E NZ  
10001 N N   . TYR E  312 ? 0.4914 0.5031 0.4434 -0.0551 0.0330  -0.0555 312 TYR E N   
10002 C CA  . TYR E  312 ? 0.5445 0.5483 0.5046 -0.0552 0.0385  -0.0539 312 TYR E CA  
10003 C C   . TYR E  312 ? 0.5995 0.5992 0.5666 -0.0524 0.0359  -0.0480 312 TYR E C   
10004 O O   . TYR E  312 ? 0.6339 0.6353 0.6025 -0.0490 0.0304  -0.0437 312 TYR E O   
10005 C CB  . TYR E  312 ? 0.4435 0.4450 0.4065 -0.0541 0.0413  -0.0538 312 TYR E CB  
10006 C CG  . TYR E  312 ? 0.5262 0.5195 0.4982 -0.0541 0.0472  -0.0521 312 TYR E CG  
10007 C CD1 . TYR E  312 ? 0.5288 0.5179 0.5014 -0.0578 0.0541  -0.0557 312 TYR E CD1 
10008 C CD2 . TYR E  312 ? 0.5711 0.5606 0.5512 -0.0505 0.0462  -0.0467 312 TYR E CD2 
10009 C CE1 . TYR E  312 ? 0.4944 0.4758 0.4756 -0.0578 0.0600  -0.0540 312 TYR E CE1 
10010 C CE2 . TYR E  312 ? 0.5291 0.5111 0.5180 -0.0503 0.0517  -0.0448 312 TYR E CE2 
10011 C CZ  . TYR E  312 ? 0.5328 0.5106 0.5223 -0.0539 0.0587  -0.0484 312 TYR E CZ  
10012 O OH  . TYR E  312 ? 0.7339 0.7041 0.7326 -0.0537 0.0647  -0.0465 312 TYR E OH  
10013 N N   . VAL E  313 ? 0.6275 0.6222 0.5988 -0.0539 0.0399  -0.0476 313 VAL E N   
10014 C CA  . VAL E  313 ? 0.5683 0.5592 0.5463 -0.0517 0.0378  -0.0418 313 VAL E CA  
10015 C C   . VAL E  313 ? 0.5572 0.5402 0.5442 -0.0520 0.0443  -0.0402 313 VAL E C   
10016 O O   . VAL E  313 ? 0.6448 0.6250 0.6315 -0.0550 0.0510  -0.0444 313 VAL E O   
10017 C CB  . VAL E  313 ? 0.5790 0.5720 0.5530 -0.0530 0.0353  -0.0422 313 VAL E CB  
10018 C CG1 . VAL E  313 ? 0.7958 0.7846 0.7767 -0.0510 0.0336  -0.0361 313 VAL E CG1 
10019 C CG2 . VAL E  313 ? 0.5506 0.5511 0.5164 -0.0524 0.0288  -0.0433 313 VAL E CG2 
10020 N N   . LYS E  314 ? 0.6143 0.5938 0.6094 -0.0488 0.0425  -0.0339 314 LYS E N   
10021 C CA  . LYS E  314 ? 0.6512 0.6234 0.6562 -0.0485 0.0483  -0.0313 314 LYS E CA  
10022 C C   . LYS E  314 ? 0.6021 0.5707 0.6098 -0.0500 0.0509  -0.0303 314 LYS E C   
10023 O O   . LYS E  314 ? 0.8142 0.7766 0.8305 -0.0498 0.0559  -0.0276 314 LYS E O   
10024 C CB  . LYS E  314 ? 0.6032 0.5738 0.6162 -0.0444 0.0449  -0.0246 314 LYS E CB  
10025 C CG  . LYS E  314 ? 0.9200 0.8839 0.9434 -0.0436 0.0511  -0.0223 314 LYS E CG  
10026 C CD  . LYS E  314 ? 1.2333 1.1968 1.2639 -0.0395 0.0469  -0.0159 314 LYS E CD  
10027 C CE  . LYS E  314 ? 1.2237 1.1930 1.2484 -0.0381 0.0414  -0.0170 314 LYS E CE  
10028 N NZ  . LYS E  314 ? 1.0590 1.0294 1.0891 -0.0344 0.0356  -0.0106 314 LYS E NZ  
10029 N N   . SER E  315 ? 0.6990 0.6715 0.6994 -0.0516 0.0478  -0.0323 315 SER E N   
10030 C CA  . SER E  315 ? 0.7661 0.7358 0.7681 -0.0531 0.0498  -0.0314 315 SER E CA  
10031 C C   . SER E  315 ? 0.6568 0.6214 0.6606 -0.0566 0.0587  -0.0357 315 SER E C   
10032 O O   . SER E  315 ? 0.6102 0.5757 0.6100 -0.0589 0.0625  -0.0413 315 SER E O   
10033 C CB  . SER E  315 ? 0.6805 0.6557 0.6735 -0.0544 0.0448  -0.0334 315 SER E CB  
10034 O OG  . SER E  315 ? 0.8627 0.8419 0.8546 -0.0513 0.0369  -0.0291 315 SER E OG  
10035 N N   . THR E  316 ? 0.7120 0.6714 0.7217 -0.0569 0.0621  -0.0330 316 THR E N   
10036 C CA  . THR E  316 ? 0.7424 0.6967 0.7539 -0.0603 0.0707  -0.0370 316 THR E CA  
10037 C C   . THR E  316 ? 0.7674 0.7244 0.7712 -0.0636 0.0705  -0.0411 316 THR E C   
10038 O O   . THR E  316 ? 0.8650 0.8212 0.8652 -0.0675 0.0761  -0.0473 316 THR E O   
10039 C CB  . THR E  316 ? 0.8874 0.8341 0.9105 -0.0589 0.0752  -0.0316 316 THR E CB  
10040 O OG1 . THR E  316 ? 1.1713 1.1132 1.1951 -0.0624 0.0830  -0.0354 316 THR E OG1 
10041 C CG2 . THR E  316 ? 0.9731 0.9207 0.9991 -0.0560 0.0690  -0.0246 316 THR E CG2 
10042 N N   . LYS E  317 ? 0.8206 0.7809 0.8220 -0.0621 0.0640  -0.0378 317 LYS E N   
10043 C CA  . LYS E  317 ? 0.7779 0.7412 0.7720 -0.0649 0.0630  -0.0412 317 LYS E CA  
10044 C C   . LYS E  317 ? 0.7679 0.7375 0.7563 -0.0630 0.0541  -0.0389 317 LYS E C   
10045 O O   . LYS E  317 ? 0.9713 0.9410 0.9634 -0.0595 0.0491  -0.0328 317 LYS E O   
10046 C CB  . LYS E  317 ? 0.9134 0.8707 0.9125 -0.0662 0.0679  -0.0396 317 LYS E CB  
10047 C CG  . LYS E  317 ? 0.9973 0.9508 1.0053 -0.0626 0.0659  -0.0312 317 LYS E CG  
10048 C CD  . LYS E  317 ? 1.3208 1.2690 1.3330 -0.0640 0.0706  -0.0297 317 LYS E CD  
10049 C CE  . LYS E  317 ? 1.2614 1.2134 1.2655 -0.0661 0.0677  -0.0321 317 LYS E CE  
10050 N NZ  . LYS E  317 ? 0.9583 0.9050 0.9666 -0.0673 0.0720  -0.0301 317 LYS E NZ  
10051 N N   . LEU E  318 ? 0.7293 0.7042 0.7086 -0.0655 0.0524  -0.0439 318 LEU E N   
10052 C CA  . LEU E  318 ? 0.6945 0.6755 0.6677 -0.0643 0.0447  -0.0427 318 LEU E CA  
10053 C C   . LEU E  318 ? 0.6905 0.6732 0.6579 -0.0674 0.0455  -0.0462 318 LEU E C   
10054 O O   . LEU E  318 ? 0.7032 0.6921 0.6627 -0.0688 0.0426  -0.0501 318 LEU E O   
10055 C CB  . LEU E  318 ? 0.6573 0.6447 0.6246 -0.0636 0.0408  -0.0454 318 LEU E CB  
10056 C CG  . LEU E  318 ? 0.6879 0.6750 0.6593 -0.0600 0.0381  -0.0416 318 LEU E CG  
10057 C CD1 . LEU E  318 ? 0.6848 0.6782 0.6497 -0.0600 0.0353  -0.0452 318 LEU E CD1 
10058 C CD2 . LEU E  318 ? 0.5387 0.5255 0.5135 -0.0566 0.0322  -0.0348 318 LEU E CD2 
10059 N N   . ARG E  319 ? 0.7391 0.7164 0.7109 -0.0684 0.0494  -0.0445 319 ARG E N   
10060 C CA  . ARG E  319 ? 0.7624 0.7404 0.7298 -0.0715 0.0511  -0.0477 319 ARG E CA  
10061 C C   . ARG E  319 ? 0.6254 0.6075 0.5880 -0.0703 0.0442  -0.0452 319 ARG E C   
10062 O O   . ARG E  319 ? 0.6280 0.6081 0.5944 -0.0676 0.0408  -0.0390 319 ARG E O   
10063 C CB  . ARG E  319 ? 0.8987 0.8690 0.8728 -0.0729 0.0580  -0.0465 319 ARG E CB  
10064 C CG  . ARG E  319 ? 0.8779 0.8483 0.8479 -0.0764 0.0607  -0.0501 319 ARG E CG  
10065 C CD  . ARG E  319 ? 0.9017 0.8652 0.8767 -0.0792 0.0699  -0.0524 319 ARG E CD  
10066 N NE  . ARG E  319 ? 1.0212 0.9861 0.9927 -0.0828 0.0748  -0.0598 319 ARG E NE  
10067 C CZ  . ARG E  319 ? 1.0815 1.0502 1.0457 -0.0867 0.0761  -0.0662 319 ARG E CZ  
10068 N NH1 . ARG E  319 ? 1.0699 1.0414 1.0298 -0.0875 0.0730  -0.0663 319 ARG E NH1 
10069 N NH2 . ARG E  319 ? 1.1173 1.0873 1.0786 -0.0901 0.0805  -0.0726 319 ARG E NH2 
10070 N N   . LEU E  320 ? 0.6357 0.6237 0.5901 -0.0724 0.0422  -0.0500 320 LEU E N   
10071 C CA  . LEU E  320 ? 0.5856 0.5782 0.5348 -0.0715 0.0358  -0.0485 320 LEU E CA  
10072 C C   . LEU E  320 ? 0.7348 0.7262 0.6818 -0.0741 0.0378  -0.0499 320 LEU E C   
10073 O O   . LEU E  320 ? 0.8046 0.7971 0.7483 -0.0776 0.0419  -0.0556 320 LEU E O   
10074 C CB  . LEU E  320 ? 0.6019 0.6023 0.5436 -0.0717 0.0319  -0.0525 320 LEU E CB  
10075 C CG  . LEU E  320 ? 0.6735 0.6791 0.6097 -0.0703 0.0248  -0.0510 320 LEU E CG  
10076 C CD1 . LEU E  320 ? 0.6133 0.6181 0.5528 -0.0663 0.0196  -0.0447 320 LEU E CD1 
10077 C CD2 . LEU E  320 ? 0.4862 0.4994 0.4155 -0.0714 0.0229  -0.0560 320 LEU E CD2 
10078 N N   . ALA E  321 ? 0.8113 0.8004 0.7600 -0.0725 0.0350  -0.0447 321 ALA E N   
10079 C CA  . ALA E  321 ? 0.7283 0.7158 0.6751 -0.0747 0.0367  -0.0452 321 ALA E CA  
10080 C C   . ALA E  321 ? 0.7327 0.7268 0.6709 -0.0767 0.0340  -0.0499 321 ALA E C   
10081 O O   . ALA E  321 ? 0.7500 0.7491 0.6838 -0.0750 0.0279  -0.0491 321 ALA E O   
10082 C CB  . ALA E  321 ? 0.6139 0.5981 0.5643 -0.0724 0.0336  -0.0381 321 ALA E CB  
10083 N N   . THR E  322 ? 0.6327 0.6267 0.5686 -0.0804 0.0387  -0.0549 322 THR E N   
10084 C CA  . THR E  322 ? 0.7536 0.7537 0.6819 -0.0826 0.0368  -0.0594 322 THR E CA  
10085 C C   . THR E  322 ? 0.7806 0.7782 0.7079 -0.0841 0.0379  -0.0586 322 THR E C   
10086 O O   . THR E  322 ? 0.7741 0.7757 0.6961 -0.0843 0.0340  -0.0590 322 THR E O   
10087 C CB  . THR E  322 ? 0.7527 0.7559 0.6781 -0.0861 0.0411  -0.0667 322 THR E CB  
10088 O OG1 . THR E  322 ? 0.8839 0.8812 0.8133 -0.0888 0.0485  -0.0685 322 THR E OG1 
10089 C CG2 . THR E  322 ? 0.8122 0.8183 0.7378 -0.0848 0.0399  -0.0677 322 THR E CG2 
10090 N N   . GLY E  323 ? 0.8177 0.8085 0.7504 -0.0852 0.0435  -0.0573 323 GLY E N   
10091 C CA  . GLY E  323 ? 0.8245 0.8121 0.7572 -0.0865 0.0451  -0.0559 323 GLY E CA  
10092 C C   . GLY E  323 ? 0.8315 0.8157 0.7673 -0.0833 0.0412  -0.0482 323 GLY E C   
10093 O O   . GLY E  323 ? 0.8637 0.8500 0.7994 -0.0802 0.0357  -0.0445 323 GLY E O   
10094 N N   . LEU E  324 ? 0.8925 0.8714 0.8311 -0.0841 0.0443  -0.0456 324 LEU E N   
10095 C CA  . LEU E  324 ? 0.8956 0.8714 0.8369 -0.0815 0.0409  -0.0381 324 LEU E CA  
10096 C C   . LEU E  324 ? 0.8806 0.8489 0.8310 -0.0805 0.0457  -0.0335 324 LEU E C   
10097 O O   . LEU E  324 ? 0.9583 0.9232 0.9126 -0.0823 0.0524  -0.0366 324 LEU E O   
10098 C CB  . LEU E  324 ? 0.8604 0.8371 0.7966 -0.0829 0.0393  -0.0380 324 LEU E CB  
10099 C CG  . LEU E  324 ? 0.8335 0.8086 0.7685 -0.0868 0.0457  -0.0432 324 LEU E CG  
10100 C CD1 . LEU E  324 ? 0.9461 0.9187 0.8796 -0.0875 0.0455  -0.0403 324 LEU E CD1 
10101 C CD2 . LEU E  324 ? 0.7247 0.7061 0.6531 -0.0893 0.0455  -0.0508 324 LEU E CD2 
10102 N N   . ARG E  325 ? 0.9306 0.8965 0.8844 -0.0779 0.0423  -0.0260 325 ARG E N   
10103 C CA  . ARG E  325 ? 0.8707 0.8298 0.8336 -0.0766 0.0462  -0.0205 325 ARG E CA  
10104 C C   . ARG E  325 ? 0.9948 0.9492 0.9596 -0.0796 0.0538  -0.0232 325 ARG E C   
10105 O O   . ARG E  325 ? 0.9873 0.9432 0.9461 -0.0820 0.0542  -0.0266 325 ARG E O   
10106 C CB  . ARG E  325 ? 0.7648 0.7230 0.7295 -0.0739 0.0408  -0.0122 325 ARG E CB  
10107 C CG  . ARG E  325 ? 0.8978 0.8506 0.8728 -0.0715 0.0429  -0.0052 325 ARG E CG  
10108 C CD  . ARG E  325 ? 1.1357 1.0880 1.1118 -0.0694 0.0376  0.0030  325 ARG E CD  
10109 N NE  . ARG E  325 ? 1.2113 1.1687 1.1835 -0.0674 0.0295  0.0052  325 ARG E NE  
10110 C CZ  . ARG E  325 ? 1.2821 1.2398 1.2597 -0.0645 0.0265  0.0099  325 ARG E CZ  
10111 N NH1 . ARG E  325 ? 1.1005 1.0536 1.0879 -0.0632 0.0310  0.0131  325 ARG E NH1 
10112 N NH2 . ARG E  325 ? 1.2609 1.2233 1.2344 -0.0631 0.0193  0.0113  325 ARG E NH2 
10113 N N   . ASN E  326 ? 1.1100 1.0584 1.0831 -0.0794 0.0601  -0.0216 326 ASN E N   
10114 C CA  . ASN E  326 ? 1.2054 1.1490 1.1808 -0.0824 0.0683  -0.0250 326 ASN E CA  
10115 C C   . ASN E  326 ? 1.2105 1.1474 1.1932 -0.0813 0.0714  -0.0182 326 ASN E C   
10116 O O   . ASN E  326 ? 1.2114 1.1455 1.2015 -0.0782 0.0706  -0.0116 326 ASN E O   
10117 C CB  . ASN E  326 ? 1.3165 1.2583 1.2952 -0.0840 0.0746  -0.0303 326 ASN E CB  
10118 C CG  . ASN E  326 ? 1.3363 1.2745 1.3151 -0.0880 0.0828  -0.0359 326 ASN E CG  
10119 O OD1 . ASN E  326 ? 1.4155 1.3556 1.3883 -0.0905 0.0827  -0.0392 326 ASN E OD1 
10120 N ND2 . ASN E  326 ? 1.2903 1.2231 1.2757 -0.0889 0.0902  -0.0373 326 ASN E ND2 
10121 N N   . ILE E  327 ? 1.2876 1.2222 1.2685 -0.0838 0.0749  -0.0197 327 ILE E N   
10122 C CA  . ILE E  327 ? 1.2711 1.1996 1.2585 -0.0828 0.0780  -0.0131 327 ILE E CA  
10123 C C   . ILE E  327 ? 1.1839 1.1069 1.1739 -0.0861 0.0873  -0.0173 327 ILE E C   
10124 O O   . ILE E  327 ? 1.0805 1.0052 1.0656 -0.0895 0.0906  -0.0254 327 ILE E O   
10125 C CB  . ILE E  327 ? 1.1345 1.0652 1.1170 -0.0819 0.0717  -0.0084 327 ILE E CB  
10126 C CG1 . ILE E  327 ? 1.0078 0.9443 0.9865 -0.0792 0.0624  -0.0054 327 ILE E CG1 
10127 C CG2 . ILE E  327 ? 1.2026 1.1273 1.1924 -0.0804 0.0741  -0.0005 327 ILE E CG2 
10128 C CD1 . ILE E  327 ? 0.9298 0.8643 0.9168 -0.0755 0.0604  0.0022  327 ILE E CD1 
10129 N N   . LEU F  2   ? 0.8877 0.8688 0.8198 -0.0659 -0.0091 0.0107  2   LEU F N   
10130 C CA  . LEU F  2   ? 0.9667 0.9517 0.8922 -0.0656 -0.0157 0.0116  2   LEU F CA  
10131 C C   . LEU F  2   ? 0.8960 0.8815 0.8137 -0.0678 -0.0170 0.0108  2   LEU F C   
10132 O O   . LEU F  2   ? 0.8466 0.8333 0.7601 -0.0678 -0.0221 0.0142  2   LEU F O   
10133 C CB  . LEU F  2   ? 0.8554 0.8449 0.7775 -0.0650 -0.0172 0.0060  2   LEU F CB  
10134 C CG  . LEU F  2   ? 0.7446 0.7363 0.6684 -0.0627 -0.0222 0.0088  2   LEU F CG  
10135 C CD1 . LEU F  2   ? 0.4614 0.4580 0.3779 -0.0628 -0.0258 0.0045  2   LEU F CD1 
10136 C CD2 . LEU F  2   ? 0.8989 0.8890 0.8254 -0.0618 -0.0262 0.0166  2   LEU F CD2 
10137 N N   . PHE F  3   ? 0.8367 0.8211 0.7524 -0.0698 -0.0121 0.0062  3   PHE F N   
10138 C CA  . PHE F  3   ? 0.9525 0.9373 0.8610 -0.0720 -0.0125 0.0048  3   PHE F CA  
10139 C C   . PHE F  3   ? 1.0285 1.0084 0.9395 -0.0731 -0.0094 0.0088  3   PHE F C   
10140 O O   . PHE F  3   ? 1.0958 1.0754 1.0015 -0.0751 -0.0090 0.0079  3   PHE F O   
10141 C CB  . PHE F  3   ? 0.9877 0.9753 0.8913 -0.0738 -0.0097 -0.0033 3   PHE F CB  
10142 C CG  . PHE F  3   ? 0.9629 0.9558 0.8625 -0.0729 -0.0134 -0.0070 3   PHE F CG  
10143 C CD1 . PHE F  3   ? 0.8954 0.8900 0.7990 -0.0714 -0.0125 -0.0092 3   PHE F CD1 
10144 C CD2 . PHE F  3   ? 0.9685 0.9645 0.8605 -0.0736 -0.0174 -0.0081 3   PHE F CD2 
10145 C CE1 . PHE F  3   ? 0.8769 0.8762 0.7768 -0.0705 -0.0158 -0.0122 3   PHE F CE1 
10146 C CE2 . PHE F  3   ? 0.8736 0.8742 0.7623 -0.0726 -0.0205 -0.0113 3   PHE F CE2 
10147 C CZ  . PHE F  3   ? 0.8799 0.8822 0.7726 -0.0711 -0.0197 -0.0132 3   PHE F CZ  
10148 N N   . GLY F  4   ? 0.9862 0.9625 0.9059 -0.0717 -0.0071 0.0134  4   GLY F N   
10149 C CA  . GLY F  4   ? 0.9356 0.9073 0.8588 -0.0723 -0.0045 0.0185  4   GLY F CA  
10150 C C   . GLY F  4   ? 1.0323 1.0011 0.9559 -0.0744 0.0023  0.0145  4   GLY F C   
10151 O O   . GLY F  4   ? 1.0764 1.0409 1.0029 -0.0749 0.0052  0.0184  4   GLY F O   
10152 N N   . ALA F  5   ? 0.9899 0.9609 0.9105 -0.0757 0.0050  0.0068  5   ALA F N   
10153 C CA  . ALA F  5   ? 0.8813 0.8501 0.8017 -0.0781 0.0115  0.0021  5   ALA F CA  
10154 C C   . ALA F  5   ? 0.9702 0.9348 0.8995 -0.0778 0.0178  0.0020  5   ALA F C   
10155 O O   . ALA F  5   ? 0.8915 0.8511 0.8256 -0.0780 0.0218  0.0057  5   ALA F O   
10156 C CB  . ALA F  5   ? 0.9201 0.8935 0.8336 -0.0799 0.0116  -0.0060 5   ALA F CB  
10157 N N   . ILE F  6   ? 1.0291 0.9957 0.9604 -0.0772 0.0191  -0.0022 6   ILE F N   
10158 C CA  . ILE F  6   ? 0.8200 0.7828 0.7593 -0.0771 0.0254  -0.0032 6   ILE F CA  
10159 C C   . ILE F  6   ? 0.9821 0.9412 0.9301 -0.0744 0.0250  0.0047  6   ILE F C   
10160 O O   . ILE F  6   ? 1.0393 1.0006 0.9881 -0.0721 0.0196  0.0084  6   ILE F O   
10161 C CB  . ILE F  6   ? 0.7109 0.6771 0.6497 -0.0773 0.0264  -0.0096 6   ILE F CB  
10162 C CG1 . ILE F  6   ? 0.7215 0.6919 0.6523 -0.0800 0.0270  -0.0172 6   ILE F CG1 
10163 C CG2 . ILE F  6   ? 0.6225 0.5844 0.5694 -0.0774 0.0332  -0.0106 6   ILE F CG2 
10164 C CD1 . ILE F  6   ? 0.7766 0.7504 0.7069 -0.0807 0.0290  -0.0238 6   ILE F CD1 
10165 N N   . ALA F  7   ? 0.8485 0.8019 0.8031 -0.0748 0.0308  0.0073  7   ALA F N   
10166 C CA  . ALA F  7   ? 0.8576 0.8071 0.8211 -0.0722 0.0310  0.0154  7   ALA F CA  
10167 C C   . ALA F  7   ? 1.0127 0.9634 0.9739 -0.0710 0.0243  0.0226  7   ALA F C   
10168 O O   . ALA F  7   ? 0.9685 0.9186 0.9355 -0.0686 0.0215  0.0296  7   ALA F O   
10169 C CB  . ALA F  7   ? 0.9621 0.9123 0.9314 -0.0700 0.0306  0.0157  7   ALA F CB  
10170 N N   . GLY F  8   ? 1.0608 1.0135 1.0135 -0.0729 0.0220  0.0209  8   GLY F N   
10171 C CA  . GLY F  8   ? 1.0437 0.9975 0.9926 -0.0724 0.0160  0.0270  8   GLY F CA  
10172 C C   . GLY F  8   ? 1.1725 1.1232 1.1190 -0.0743 0.0187  0.0285  8   GLY F C   
10173 O O   . GLY F  8   ? 1.1267 1.0725 1.0802 -0.0741 0.0236  0.0321  8   GLY F O   
10174 N N   . PHE F  9   ? 1.0059 0.9594 0.9429 -0.0761 0.0157  0.0257  9   PHE F N   
10175 C CA  . PHE F  9   ? 0.9124 0.8631 0.8461 -0.0782 0.0181  0.0265  9   PHE F CA  
10176 C C   . PHE F  9   ? 1.0814 1.0296 1.0159 -0.0804 0.0259  0.0199  9   PHE F C   
10177 O O   . PHE F  9   ? 1.3393 1.2846 1.2720 -0.0823 0.0291  0.0200  9   PHE F O   
10178 C CB  . PHE F  9   ? 1.1105 1.0648 1.0339 -0.0794 0.0123  0.0262  9   PHE F CB  
10179 C CG  . PHE F  9   ? 1.0204 0.9790 0.9361 -0.0811 0.0118  0.0176  9   PHE F CG  
10180 C CD1 . PHE F  9   ? 1.0652 1.0229 0.9799 -0.0833 0.0177  0.0108  9   PHE F CD1 
10181 C CD2 . PHE F  9   ? 1.1709 1.1344 1.0803 -0.0806 0.0054  0.0164  9   PHE F CD2 
10182 C CE1 . PHE F  9   ? 1.0648 1.0268 0.9727 -0.0848 0.0170  0.0033  9   PHE F CE1 
10183 C CE2 . PHE F  9   ? 1.2230 1.1904 1.1257 -0.0820 0.0050  0.0090  9   PHE F CE2 
10184 C CZ  . PHE F  9   ? 1.2025 1.1695 1.1047 -0.0841 0.0106  0.0026  9   PHE F CZ  
10185 N N   . ILE F  10  ? 0.9763 0.9256 0.9133 -0.0805 0.0288  0.0141  10  ILE F N   
10186 C CA  . ILE F  10  ? 0.9466 0.8930 0.8863 -0.0825 0.0367  0.0083  10  ILE F CA  
10187 C C   . ILE F  10  ? 0.9505 0.8937 0.9000 -0.0809 0.0408  0.0098  10  ILE F C   
10188 O O   . ILE F  10  ? 1.0724 1.0181 1.0226 -0.0805 0.0407  0.0056  10  ILE F O   
10189 C CB  . ILE F  10  ? 0.8609 0.8120 0.7938 -0.0847 0.0371  -0.0011 10  ILE F CB  
10190 C CG1 . ILE F  10  ? 0.9058 0.8615 0.8289 -0.0854 0.0311  -0.0022 10  ILE F CG1 
10191 C CG2 . ILE F  10  ? 0.8132 0.7614 0.7471 -0.0877 0.0450  -0.0068 10  ILE F CG2 
10192 C CD1 . ILE F  10  ? 0.8224 0.7821 0.7390 -0.0880 0.0324  -0.0108 10  ILE F CD1 
10193 N N   . GLU F  11  ? 1.1278 1.0654 1.0851 -0.0799 0.0446  0.0158  11  GLU F N   
10194 C CA  . GLU F  11  ? 1.2147 1.1491 1.1823 -0.0778 0.0475  0.0191  11  GLU F CA  
10195 C C   . GLU F  11  ? 1.1412 1.0745 1.1118 -0.0790 0.0538  0.0119  11  GLU F C   
10196 O O   . GLU F  11  ? 1.2047 1.1381 1.1807 -0.0772 0.0539  0.0125  11  GLU F O   
10197 C CB  . GLU F  11  ? 1.4100 1.3384 1.3854 -0.0768 0.0511  0.0268  11  GLU F CB  
10198 C CG  . GLU F  11  ? 1.6204 1.5499 1.5923 -0.0759 0.0451  0.0340  11  GLU F CG  
10199 C CD  . GLU F  11  ? 2.0373 1.9612 2.0163 -0.0752 0.0490  0.0414  11  GLU F CD  
10200 O OE1 . GLU F  11  ? 2.1024 2.0269 2.0791 -0.0746 0.0444  0.0480  11  GLU F OE1 
10201 O OE2 . GLU F  11  ? 1.9919 1.9106 1.9786 -0.0754 0.0568  0.0406  11  GLU F OE2 
10202 N N   . GLY F  12  ? 1.0352 0.9676 1.0023 -0.0822 0.0590  0.0051  12  GLY F N   
10203 C CA  . GLY F  12  ? 0.9603 0.8912 0.9305 -0.0839 0.0657  -0.0017 12  GLY F CA  
10204 C C   . GLY F  12  ? 1.0277 0.9632 0.9898 -0.0870 0.0662  -0.0112 12  GLY F C   
10205 O O   . GLY F  12  ? 1.0827 1.0221 1.0367 -0.0882 0.0623  -0.0132 12  GLY F O   
10206 N N   . GLY F  13  ? 0.9452 0.8802 0.9097 -0.0884 0.0711  -0.0170 13  GLY F N   
10207 C CA  . GLY F  13  ? 0.9658 0.9051 0.9237 -0.0916 0.0724  -0.0261 13  GLY F CA  
10208 C C   . GLY F  13  ? 0.9854 0.9207 0.9445 -0.0953 0.0808  -0.0309 13  GLY F C   
10209 O O   . GLY F  13  ? 0.9972 0.9258 0.9629 -0.0952 0.0861  -0.0272 13  GLY F O   
10210 N N   . TRP F  14  ? 0.9306 0.8700 0.8833 -0.0987 0.0820  -0.0391 14  TRP F N   
10211 C CA  . TRP F  14  ? 0.9668 0.9031 0.9198 -0.1027 0.0897  -0.0444 14  TRP F CA  
10212 C C   . TRP F  14  ? 1.0998 1.0369 1.0536 -0.1054 0.0949  -0.0520 14  TRP F C   
10213 O O   . TRP F  14  ? 1.1495 1.0931 1.0971 -0.1071 0.0924  -0.0580 14  TRP F O   
10214 C CB  . TRP F  14  ? 1.0400 0.9803 0.9849 -0.1050 0.0876  -0.0478 14  TRP F CB  
10215 C CG  . TRP F  14  ? 1.1217 1.0608 1.0651 -0.1031 0.0833  -0.0411 14  TRP F CG  
10216 C CD1 . TRP F  14  ? 1.0236 0.9570 0.9730 -0.1005 0.0838  -0.0330 14  TRP F CD1 
10217 C CD2 . TRP F  14  ? 1.0083 0.9522 0.9437 -0.1036 0.0781  -0.0418 14  TRP F CD2 
10218 N NE1 . TRP F  14  ? 0.8460 0.7803 0.7910 -0.0996 0.0790  -0.0286 14  TRP F NE1 
10219 C CE2 . TRP F  14  ? 1.0055 0.9460 0.9419 -0.1015 0.0755  -0.0340 14  TRP F CE2 
10220 C CE3 . TRP F  14  ? 0.9263 0.8770 0.8538 -0.1057 0.0753  -0.0480 14  TRP F CE3 
10221 C CZ2 . TRP F  14  ? 1.0523 0.9958 0.9818 -0.1016 0.0706  -0.0327 14  TRP F CZ2 
10222 C CZ3 . TRP F  14  ? 1.1054 1.0590 1.0267 -0.1056 0.0705  -0.0466 14  TRP F CZ3 
10223 C CH2 . TRP F  14  ? 1.1521 1.1019 1.0742 -0.1036 0.0683  -0.0391 14  TRP F CH2 
10224 N N   . THR F  15  ? 1.1890 1.1193 1.1505 -0.1059 0.1023  -0.0515 15  THR F N   
10225 C CA  . THR F  15  ? 1.2559 1.1859 1.2182 -0.1092 0.1085  -0.0590 15  THR F CA  
10226 C C   . THR F  15  ? 1.3340 1.2668 1.2902 -0.1140 0.1115  -0.0667 15  THR F C   
10227 O O   . THR F  15  ? 1.3341 1.2704 1.2872 -0.1172 0.1137  -0.0741 15  THR F O   
10228 C CB  . THR F  15  ? 1.2361 1.1572 1.2081 -0.1093 0.1171  -0.0570 15  THR F CB  
10229 O OG1 . THR F  15  ? 1.4164 1.3318 1.3909 -0.1107 0.1221  -0.0554 15  THR F OG1 
10230 C CG2 . THR F  15  ? 1.1536 1.0719 1.1326 -0.1044 0.1143  -0.0489 15  THR F CG2 
10231 N N   . GLY F  16  ? 1.2118 1.1431 1.1662 -0.1146 0.1115  -0.0648 16  GLY F N   
10232 C CA  . GLY F  16  ? 1.2558 1.1891 1.2051 -0.1191 0.1146  -0.0715 16  GLY F CA  
10233 C C   . GLY F  16  ? 1.2872 1.2301 1.2277 -0.1206 0.1088  -0.0770 16  GLY F C   
10234 O O   . GLY F  16  ? 1.3277 1.2737 1.2649 -0.1249 0.1122  -0.0846 16  GLY F O   
10235 N N   . MET F  17  ? 1.2871 1.2350 1.2243 -0.1172 0.1003  -0.0731 17  MET F N   
10236 C CA  . MET F  17  ? 1.2339 1.1911 1.1633 -0.1180 0.0946  -0.0775 17  MET F CA  
10237 C C   . MET F  17  ? 1.3320 1.2934 1.2610 -0.1181 0.0937  -0.0813 17  MET F C   
10238 O O   . MET F  17  ? 1.3954 1.3566 1.3268 -0.1146 0.0901  -0.0771 17  MET F O   
10239 C CB  . MET F  17  ? 0.9917 0.9521 0.9174 -0.1145 0.0862  -0.0720 17  MET F CB  
10240 C CG  . MET F  17  ? 1.1729 1.1425 1.0908 -0.1151 0.0803  -0.0761 17  MET F CG  
10241 S SD  . MET F  17  ? 1.3304 1.3030 1.2439 -0.1113 0.0713  -0.0699 17  MET F SD  
10242 C CE  . MET F  17  ? 1.1878 1.1566 1.1072 -0.1065 0.0683  -0.0622 17  MET F CE  
10243 N N   . VAL F  18  ? 1.3747 1.3400 1.3005 -0.1224 0.0969  -0.0892 18  VAL F N   
10244 C CA  . VAL F  18  ? 1.4699 1.4390 1.3952 -0.1232 0.0971  -0.0933 18  VAL F CA  
10245 C C   . VAL F  18  ? 1.4376 1.4169 1.3554 -0.1248 0.0923  -0.0985 18  VAL F C   
10246 O O   . VAL F  18  ? 1.4404 1.4240 1.3565 -0.1266 0.0930  -0.1034 18  VAL F O   
10247 C CB  . VAL F  18  ? 1.5140 1.4784 1.4429 -0.1272 0.1062  -0.0984 18  VAL F CB  
10248 C CG1 . VAL F  18  ? 1.3350 1.2892 1.2722 -0.1254 0.1114  -0.0931 18  VAL F CG1 
10249 C CG2 . VAL F  18  ? 1.4655 1.4317 1.3908 -0.1324 0.1103  -0.1049 18  VAL F CG2 
10250 N N   . ASP F  19  ? 1.4864 1.4695 1.3996 -0.1241 0.0875  -0.0973 19  ASP F N   
10251 C CA  . ASP F  19  ? 1.5727 1.5656 1.4793 -0.1255 0.0830  -0.1018 19  ASP F CA  
10252 C C   . ASP F  19  ? 1.4997 1.4977 1.4041 -0.1213 0.0750  -0.0983 19  ASP F C   
10253 O O   . ASP F  19  ? 1.4647 1.4706 1.3651 -0.1219 0.0719  -0.1019 19  ASP F O   
10254 C CB  . ASP F  19  ? 1.7335 1.7281 1.6365 -0.1273 0.0826  -0.1029 19  ASP F CB  
10255 C CG  . ASP F  19  ? 1.8654 1.8540 1.7711 -0.1310 0.0904  -0.1054 19  ASP F CG  
10256 O OD1 . ASP F  19  ? 1.9086 1.8942 1.8172 -0.1338 0.0965  -0.1091 19  ASP F OD1 
10257 O OD2 . ASP F  19  ? 1.8084 1.7949 1.7131 -0.1314 0.0907  -0.1038 19  ASP F OD2 
10258 N N   . GLY F  20  ? 1.3758 1.3695 1.2828 -0.1171 0.0718  -0.0912 20  GLY F N   
10259 C CA  . GLY F  20  ? 1.1485 1.1462 1.0537 -0.1130 0.0644  -0.0874 20  GLY F CA  
10260 C C   . GLY F  20  ? 1.0949 1.0864 1.0049 -0.1089 0.0627  -0.0799 20  GLY F C   
10261 O O   . GLY F  20  ? 0.9964 0.9805 0.9119 -0.1090 0.0676  -0.0775 20  GLY F O   
10262 N N   . TRP F  21  ? 0.9490 0.9437 0.8573 -0.1053 0.0559  -0.0760 21  TRP F N   
10263 C CA  . TRP F  21  ? 1.0029 0.9927 0.9155 -0.1013 0.0534  -0.0687 21  TRP F CA  
10264 C C   . TRP F  21  ? 0.9554 0.9417 0.8676 -0.1002 0.0515  -0.0634 21  TRP F C   
10265 O O   . TRP F  21  ? 0.8644 0.8444 0.7818 -0.0984 0.0527  -0.0579 21  TRP F O   
10266 C CB  . TRP F  21  ? 1.0672 1.0618 0.9783 -0.0981 0.0470  -0.0669 21  TRP F CB  
10267 C CG  . TRP F  21  ? 0.9961 0.9912 0.9102 -0.0980 0.0491  -0.0691 21  TRP F CG  
10268 C CD1 . TRP F  21  ? 0.8732 0.8630 0.7927 -0.0994 0.0555  -0.0702 21  TRP F CD1 
10269 C CD2 . TRP F  21  ? 0.8907 0.8918 0.8025 -0.0965 0.0450  -0.0705 21  TRP F CD2 
10270 N NE1 . TRP F  21  ? 0.8813 0.8734 0.8017 -0.0989 0.0557  -0.0723 21  TRP F NE1 
10271 C CE2 . TRP F  21  ? 0.8265 0.8255 0.7422 -0.0971 0.0492  -0.0725 21  TRP F CE2 
10272 C CE3 . TRP F  21  ? 0.8114 0.8190 0.7182 -0.0947 0.0385  -0.0703 21  TRP F CE3 
10273 C CZ2 . TRP F  21  ? 0.9368 0.9403 0.8514 -0.0960 0.0468  -0.0741 21  TRP F CZ2 
10274 C CZ3 . TRP F  21  ? 0.8042 0.8163 0.7103 -0.0935 0.0362  -0.0718 21  TRP F CZ3 
10275 C CH2 . TRP F  21  ? 0.9004 0.9105 0.8103 -0.0941 0.0403  -0.0736 21  TRP F CH2 
10276 N N   . TYR F  22  ? 1.0224 1.0129 0.9286 -0.1011 0.0485  -0.0650 22  TYR F N   
10277 C CA  . TYR F  22  ? 1.0093 0.9969 0.9142 -0.1005 0.0468  -0.0606 22  TYR F CA  
10278 C C   . TYR F  22  ? 1.1093 1.0976 1.0107 -0.1042 0.0502  -0.0651 22  TYR F C   
10279 O O   . TYR F  22  ? 1.1992 1.1932 1.0972 -0.1065 0.0509  -0.0713 22  TYR F O   
10280 C CB  . TYR F  22  ? 1.0549 1.0465 0.9554 -0.0977 0.0391  -0.0573 22  TYR F CB  
10281 C CG  . TYR F  22  ? 0.9967 0.9918 0.8977 -0.0951 0.0351  -0.0568 22  TYR F CG  
10282 C CD1 . TYR F  22  ? 0.9420 0.9444 0.8387 -0.0957 0.0327  -0.0616 22  TYR F CD1 
10283 C CD2 . TYR F  22  ? 0.9294 0.9208 0.8355 -0.0922 0.0337  -0.0514 22  TYR F CD2 
10284 C CE1 . TYR F  22  ? 0.9038 0.9095 0.8011 -0.0933 0.0292  -0.0611 22  TYR F CE1 
10285 C CE2 . TYR F  22  ? 0.8728 0.8675 0.7795 -0.0899 0.0302  -0.0510 22  TYR F CE2 
10286 C CZ  . TYR F  22  ? 0.9100 0.9117 0.8121 -0.0905 0.0281  -0.0559 22  TYR F CZ  
10287 O OH  . TYR F  22  ? 0.8431 0.8479 0.7458 -0.0881 0.0247  -0.0554 22  TYR F OH  
10288 N N   . GLY F  23  ? 1.4186 1.4015 1.3211 -0.1046 0.0524  -0.0619 23  GLY F N   
10289 C CA  . GLY F  23  ? 1.5378 1.5208 1.4376 -0.1081 0.0560  -0.0658 23  GLY F CA  
10290 C C   . GLY F  23  ? 1.5982 1.5751 1.4989 -0.1079 0.0574  -0.0608 23  GLY F C   
10291 O O   . GLY F  23  ? 1.4272 1.4010 1.3294 -0.1050 0.0541  -0.0541 23  GLY F O   
10292 N N   . TYR F  24  ? 1.2912 1.2665 1.1908 -0.1112 0.0622  -0.0642 24  TYR F N   
10293 C CA  . TYR F  24  ? 1.2001 1.1699 1.1000 -0.1114 0.0637  -0.0600 24  TYR F CA  
10294 C C   . TYR F  24  ? 1.2979 1.2613 1.2032 -0.1137 0.0719  -0.0610 24  TYR F C   
10295 O O   . TYR F  24  ? 1.2296 1.1931 1.1374 -0.1158 0.0766  -0.0661 24  TYR F O   
10296 C CB  . TYR F  24  ? 1.0793 1.0530 0.9724 -0.1131 0.0617  -0.0625 24  TYR F CB  
10297 C CG  . TYR F  24  ? 1.1117 1.0928 0.9991 -0.1118 0.0548  -0.0637 24  TYR F CG  
10298 C CD1 . TYR F  24  ? 1.1021 1.0901 0.9875 -0.1132 0.0545  -0.0702 24  TYR F CD1 
10299 C CD2 . TYR F  24  ? 1.1205 1.1020 1.0047 -0.1092 0.0489  -0.0585 24  TYR F CD2 
10300 C CE1 . TYR F  24  ? 1.1129 1.1077 0.9936 -0.1118 0.0485  -0.0711 24  TYR F CE1 
10301 C CE2 . TYR F  24  ? 1.1173 1.1052 0.9965 -0.1080 0.0431  -0.0597 24  TYR F CE2 
10302 C CZ  . TYR F  24  ? 1.1846 1.1790 1.0623 -0.1092 0.0430  -0.0659 24  TYR F CZ  
10303 O OH  . TYR F  24  ? 1.1734 1.1742 1.0468 -0.1078 0.0375  -0.0669 24  TYR F OH  
10304 N N   . HIS F  25  ? 1.3233 1.2808 1.2300 -0.1134 0.0737  -0.0562 25  HIS F N   
10305 C CA  . HIS F  25  ? 1.3163 1.2676 1.2275 -0.1159 0.0818  -0.0573 25  HIS F CA  
10306 C C   . HIS F  25  ? 1.4343 1.3831 1.3424 -0.1171 0.0825  -0.0553 25  HIS F C   
10307 O O   . HIS F  25  ? 1.3976 1.3420 1.3072 -0.1149 0.0811  -0.0481 25  HIS F O   
10308 C CB  . HIS F  25  ? 1.4041 1.3484 1.3235 -0.1138 0.0851  -0.0519 25  HIS F CB  
10309 C CG  . HIS F  25  ? 1.4352 1.3720 1.3593 -0.1157 0.0928  -0.0511 25  HIS F CG  
10310 N ND1 . HIS F  25  ? 1.3257 1.2571 1.2519 -0.1141 0.0931  -0.0438 25  HIS F ND1 
10311 C CD2 . HIS F  25  ? 1.3758 1.3098 1.3029 -0.1191 0.1008  -0.0566 25  HIS F CD2 
10312 C CE1 . HIS F  25  ? 1.3627 1.2881 1.2934 -0.1163 0.1009  -0.0448 25  HIS F CE1 
10313 N NE2 . HIS F  25  ? 1.4099 1.3365 1.3410 -0.1194 0.1058  -0.0526 25  HIS F NE2 
10314 N N   . HIS F  26  ? 1.6793 1.6311 1.5831 -0.1205 0.0847  -0.0617 26  HIS F N   
10315 C CA  . HIS F  26  ? 1.6266 1.5766 1.5269 -0.1220 0.0856  -0.0607 26  HIS F CA  
10316 C C   . HIS F  26  ? 1.6769 1.6186 1.5829 -0.1232 0.0930  -0.0585 26  HIS F C   
10317 O O   . HIS F  26  ? 1.6924 1.6304 1.6046 -0.1237 0.0983  -0.0596 26  HIS F O   
10318 C CB  . HIS F  26  ? 1.5650 1.5210 1.4599 -0.1255 0.0861  -0.0685 26  HIS F CB  
10319 C CG  . HIS F  26  ? 1.5986 1.5536 1.4965 -0.1294 0.0937  -0.0751 26  HIS F CG  
10320 N ND1 . HIS F  26  ? 1.5974 1.5548 1.4977 -0.1306 0.0957  -0.0799 26  HIS F ND1 
10321 C CD2 . HIS F  26  ? 1.7907 1.7422 1.6891 -0.1328 0.1000  -0.0779 26  HIS F CD2 
10322 C CE1 . HIS F  26  ? 1.7240 1.6797 1.6262 -0.1346 0.1029  -0.0855 26  HIS F CE1 
10323 N NE2 . HIS F  26  ? 1.8734 1.8254 1.7747 -0.1360 0.1056  -0.0844 26  HIS F NE2 
10324 N N   . GLN F  27  ? 2.0628 2.0014 1.9666 -0.1237 0.0937  -0.0555 27  GLN F N   
10325 C CA  . GLN F  27  ? 2.1376 2.0680 2.0465 -0.1245 0.1005  -0.0525 27  GLN F CA  
10326 C C   . GLN F  27  ? 2.0985 2.0285 2.0021 -0.1263 0.1007  -0.0525 27  GLN F C   
10327 O O   . GLN F  27  ? 2.0724 2.0001 1.9743 -0.1243 0.0975  -0.0458 27  GLN F O   
10328 C CB  . GLN F  27  ? 2.1281 2.0533 2.0423 -0.1207 0.0990  -0.0433 27  GLN F CB  
10329 C CG  . GLN F  27  ? 2.1393 2.0561 2.0588 -0.1209 0.1051  -0.0385 27  GLN F CG  
10330 C CD  . GLN F  27  ? 2.2418 2.1539 2.1682 -0.1231 0.1141  -0.0426 27  GLN F CD  
10331 O OE1 . GLN F  27  ? 2.1992 2.1072 2.1329 -0.1212 0.1166  -0.0390 27  GLN F OE1 
10332 N NE2 . GLN F  27  ? 2.3165 2.2293 2.2408 -0.1273 0.1192  -0.0501 27  GLN F NE2 
10333 N N   . ASN F  28  ? 1.9634 1.8958 1.8645 -0.1302 0.1045  -0.0600 28  ASN F N   
10334 C CA  . ASN F  28  ? 2.0147 1.9470 1.9106 -0.1321 0.1048  -0.0606 28  ASN F CA  
10335 C C   . ASN F  28  ? 2.0871 2.0137 1.9867 -0.1355 0.1138  -0.0635 28  ASN F C   
10336 O O   . ASN F  28  ? 2.0901 2.0104 1.9966 -0.1351 0.1191  -0.0610 28  ASN F O   
10337 C CB  . ASN F  28  ? 1.7837 1.7243 1.6722 -0.1335 0.1003  -0.0660 28  ASN F CB  
10338 C CG  . ASN F  28  ? 1.7541 1.6999 1.6427 -0.1367 0.1030  -0.0751 28  ASN F CG  
10339 O OD1 . ASN F  28  ? 1.6804 1.6333 1.5639 -0.1381 0.1000  -0.0798 28  ASN F OD1 
10340 N ND2 . ASN F  28  ? 1.7764 1.7190 1.6710 -0.1380 0.1089  -0.0774 28  ASN F ND2 
10341 N N   . GLU F  29  ? 1.9429 1.8720 1.8383 -0.1388 0.1158  -0.0689 29  GLU F N   
10342 C CA  . GLU F  29  ? 1.9937 1.9176 1.8920 -0.1423 0.1242  -0.0717 29  GLU F CA  
10343 C C   . GLU F  29  ? 1.9261 1.8529 1.8262 -0.1463 0.1293  -0.0809 29  GLU F C   
10344 O O   . GLU F  29  ? 1.8442 1.7665 1.7477 -0.1494 0.1370  -0.0840 29  GLU F O   
10345 C CB  . GLU F  29  ? 2.1099 2.0339 2.0027 -0.1438 0.1239  -0.0717 29  GLU F CB  
10346 C CG  . GLU F  29  ? 2.1106 2.0318 2.0007 -0.1404 0.1190  -0.0629 29  GLU F CG  
10347 C CD  . GLU F  29  ? 2.2194 2.1435 2.1021 -0.1416 0.1162  -0.0638 29  GLU F CD  
10348 O OE1 . GLU F  29  ? 2.1233 2.0539 2.0022 -0.1440 0.1154  -0.0709 29  GLU F OE1 
10349 O OE2 . GLU F  29  ? 2.2186 2.1387 2.0992 -0.1403 0.1149  -0.0574 29  GLU F OE2 
10350 N N   . GLN F  30  ? 1.9423 1.8767 1.8400 -0.1462 0.1249  -0.0852 30  GLN F N   
10351 C CA  . GLN F  30  ? 1.8342 1.7725 1.7329 -0.1501 0.1289  -0.0939 30  GLN F CA  
10352 C C   . GLN F  30  ? 1.9318 1.8684 1.8360 -0.1492 0.1308  -0.0941 30  GLN F C   
10353 O O   . GLN F  30  ? 1.9107 1.8510 1.8155 -0.1522 0.1334  -0.1010 30  GLN F O   
10354 C CB  . GLN F  30  ? 1.6515 1.6002 1.5441 -0.1513 0.1235  -0.0993 30  GLN F CB  
10355 C CG  . GLN F  30  ? 1.5872 1.5381 1.4748 -0.1533 0.1232  -0.1011 30  GLN F CG  
10356 C CD  . GLN F  30  ? 1.6208 1.5775 1.5026 -0.1505 0.1147  -0.0984 30  GLN F CD  
10357 O OE1 . GLN F  30  ? 1.4936 1.4586 1.3718 -0.1513 0.1110  -0.1030 30  GLN F OE1 
10358 N NE2 . GLN F  30  ? 1.7776 1.7297 1.6581 -0.1473 0.1118  -0.0909 30  GLN F NE2 
10359 N N   . GLY F  31  ? 2.4030 2.3342 2.3111 -0.1452 0.1295  -0.0865 31  GLY F N   
10360 C CA  . GLY F  31  ? 2.3500 2.2786 2.2639 -0.1441 0.1318  -0.0859 31  GLY F CA  
10361 C C   . GLY F  31  ? 2.2491 2.1796 2.1632 -0.1393 0.1245  -0.0800 31  GLY F C   
10362 O O   . GLY F  31  ? 2.1387 2.0717 2.0486 -0.1366 0.1178  -0.0754 31  GLY F O   
10363 N N   . SER F  32  ? 1.9706 1.8997 1.8894 -0.1383 0.1260  -0.0801 32  SER F N   
10364 C CA  . SER F  32  ? 1.8938 1.8245 1.8137 -0.1339 0.1198  -0.0748 32  SER F CA  
10365 C C   . SER F  32  ? 1.7949 1.7316 1.7139 -0.1347 0.1182  -0.0805 32  SER F C   
10366 O O   . SER F  32  ? 1.8059 1.7475 1.7218 -0.1384 0.1200  -0.0882 32  SER F O   
10367 C CB  . SER F  32  ? 1.7747 1.6970 1.7025 -0.1311 0.1230  -0.0676 32  SER F CB  
10368 O OG  . SER F  32  ? 1.9382 1.8547 1.8671 -0.1306 0.1252  -0.0624 32  SER F OG  
10369 N N   . GLY F  33  ? 1.8666 1.8032 1.7885 -0.1311 0.1148  -0.0764 33  GLY F N   
10370 C CA  . GLY F  33  ? 1.8464 1.7880 1.7679 -0.1315 0.1135  -0.0810 33  GLY F CA  
10371 C C   . GLY F  33  ? 1.5797 1.5270 1.4981 -0.1277 0.1045  -0.0777 33  GLY F C   
10372 O O   . GLY F  33  ? 1.4755 1.4239 1.3908 -0.1252 0.0989  -0.0727 33  GLY F O   
10373 N N   . TYR F  34  ? 1.4267 1.3777 1.3457 -0.1275 0.1034  -0.0807 34  TYR F N   
10374 C CA  . TYR F  34  ? 1.2372 1.1938 1.1535 -0.1240 0.0954  -0.0782 34  TYR F CA  
10375 C C   . TYR F  34  ? 1.1990 1.1649 1.1089 -0.1261 0.0920  -0.0849 34  TYR F C   
10376 O O   . TYR F  34  ? 1.2412 1.2095 1.1505 -0.1300 0.0964  -0.0919 34  TYR F O   
10377 C CB  . TYR F  34  ? 1.1125 1.0664 1.0344 -0.1217 0.0960  -0.0757 34  TYR F CB  
10378 C CG  . TYR F  34  ? 1.1752 1.1200 1.1047 -0.1197 0.1000  -0.0692 34  TYR F CG  
10379 C CD1 . TYR F  34  ? 1.1985 1.1369 1.1335 -0.1222 0.1088  -0.0714 34  TYR F CD1 
10380 C CD2 . TYR F  34  ? 1.1493 1.0920 1.0805 -0.1154 0.0951  -0.0608 34  TYR F CD2 
10381 C CE1 . TYR F  34  ? 1.2825 1.2126 1.2250 -0.1203 0.1127  -0.0652 34  TYR F CE1 
10382 C CE2 . TYR F  34  ? 0.9791 0.9140 0.9177 -0.1135 0.0985  -0.0544 34  TYR F CE2 
10383 C CZ  . TYR F  34  ? 1.0667 0.9953 1.0111 -0.1158 0.1074  -0.0565 34  TYR F CZ  
10384 O OH  . TYR F  34  ? 0.9303 0.8511 0.8826 -0.1138 0.1111  -0.0499 34  TYR F OH  
10385 N N   . ALA F  35  ? 1.1106 1.0821 1.0160 -0.1234 0.0842  -0.0827 35  ALA F N   
10386 C CA  . ALA F  35  ? 1.2658 1.2466 1.1656 -0.1247 0.0804  -0.0881 35  ALA F CA  
10387 C C   . ALA F  35  ? 1.3114 1.2965 1.2095 -0.1207 0.0729  -0.0847 35  ALA F C   
10388 O O   . ALA F  35  ? 1.3219 1.3066 1.2180 -0.1178 0.0679  -0.0795 35  ALA F O   
10389 C CB  . ALA F  35  ? 1.3296 1.3137 1.2243 -0.1267 0.0795  -0.0904 35  ALA F CB  
10390 N N   . ALA F  36  ? 1.1340 1.1230 1.0327 -0.1207 0.0723  -0.0877 36  ALA F N   
10391 C CA  . ALA F  36  ? 1.2189 1.2118 1.1163 -0.1170 0.0657  -0.0849 36  ALA F CA  
10392 C C   . ALA F  36  ? 1.1753 1.1761 1.0664 -0.1165 0.0597  -0.0863 36  ALA F C   
10393 O O   . ALA F  36  ? 1.3312 1.3372 1.2189 -0.1196 0.0608  -0.0919 36  ALA F O   
10394 C CB  . ALA F  36  ? 1.2701 1.2649 1.1699 -0.1173 0.0672  -0.0879 36  ALA F CB  
10395 N N   . ASP F  37  ? 1.0714 1.0729 0.9610 -0.1127 0.0535  -0.0812 37  ASP F N   
10396 C CA  . ASP F  37  ? 1.0824 1.0910 0.9664 -0.1119 0.0478  -0.0820 37  ASP F CA  
10397 C C   . ASP F  37  ? 1.2136 1.2300 1.0959 -0.1125 0.0462  -0.0869 37  ASP F C   
10398 O O   . ASP F  37  ? 1.1951 1.2121 1.0795 -0.1106 0.0449  -0.0859 37  ASP F O   
10399 C CB  . ASP F  37  ? 0.9753 0.9824 0.8583 -0.1079 0.0419  -0.0754 37  ASP F CB  
10400 C CG  . ASP F  37  ? 1.2657 1.2791 1.1429 -0.1071 0.0366  -0.0762 37  ASP F CG  
10401 O OD1 . ASP F  37  ? 1.3961 1.4091 1.2718 -0.1041 0.0315  -0.0715 37  ASP F OD1 
10402 O OD2 . ASP F  37  ? 1.4090 1.4278 1.2832 -0.1096 0.0375  -0.0814 37  ASP F OD2 
10403 N N   . LEU F  38  ? 1.3662 1.3889 1.2448 -0.1151 0.0464  -0.0919 38  LEU F N   
10404 C CA  . LEU F  38  ? 1.5048 1.5357 1.3816 -0.1162 0.0453  -0.0969 38  LEU F CA  
10405 C C   . LEU F  38  ? 1.3041 1.3398 1.1792 -0.1125 0.0388  -0.0944 38  LEU F C   
10406 O O   . LEU F  38  ? 1.1211 1.1585 0.9978 -0.1114 0.0381  -0.0948 38  LEU F O   
10407 C CB  . LEU F  38  ? 1.7788 1.8155 1.6523 -0.1197 0.0465  -0.1021 38  LEU F CB  
10408 C CG  . LEU F  38  ? 1.9291 1.9748 1.8009 -0.1220 0.0464  -0.1080 38  LEU F CG  
10409 C CD1 . LEU F  38  ? 1.8822 1.9283 1.7564 -0.1217 0.0474  -0.1090 38  LEU F CD1 
10410 C CD2 . LEU F  38  ? 1.8226 1.8704 1.6936 -0.1268 0.0510  -0.1135 38  LEU F CD2 
10411 N N   . LYS F  39  ? 1.6582 1.6958 1.5300 -0.1106 0.0344  -0.0920 39  LYS F N   
10412 C CA  . LYS F  39  ? 1.6839 1.7263 1.5537 -0.1073 0.0284  -0.0901 39  LYS F CA  
10413 C C   . LYS F  39  ? 1.6085 1.6464 1.4811 -0.1038 0.0261  -0.0850 39  LYS F C   
10414 O O   . LYS F  39  ? 1.4362 1.4779 1.3089 -0.1018 0.0231  -0.0847 39  LYS F O   
10415 C CB  . LYS F  39  ? 1.7798 1.8243 1.6455 -0.1064 0.0248  -0.0886 39  LYS F CB  
10416 C CG  . LYS F  39  ? 2.0253 2.0751 1.8888 -0.1033 0.0190  -0.0871 39  LYS F CG  
10417 C CD  . LYS F  39  ? 2.2859 2.3380 2.1453 -0.1029 0.0163  -0.0865 39  LYS F CD  
10418 C CE  . LYS F  39  ? 2.3109 2.3686 2.1684 -0.1000 0.0112  -0.0856 39  LYS F CE  
10419 N NZ  . LYS F  39  ? 2.1270 2.1871 1.9806 -0.0998 0.0090  -0.0855 39  LYS F NZ  
10420 N N   . SER F  40  ? 1.3018 1.3318 1.1769 -0.1031 0.0276  -0.0807 40  SER F N   
10421 C CA  . SER F  40  ? 1.1514 1.1771 1.0296 -0.0997 0.0253  -0.0753 40  SER F CA  
10422 C C   . SER F  40  ? 1.1078 1.1327 0.9902 -0.0997 0.0278  -0.0765 40  SER F C   
10423 O O   . SER F  40  ? 1.1634 1.1903 1.0465 -0.0971 0.0246  -0.0750 40  SER F O   
10424 C CB  . SER F  40  ? 1.0942 1.1120 0.9743 -0.0991 0.0263  -0.0702 40  SER F CB  
10425 O OG  . SER F  40  ? 1.2237 1.2378 1.1070 -0.0960 0.0238  -0.0647 40  SER F OG  
10426 N N   . THR F  41  ? 1.0639 1.0858 0.9490 -0.1026 0.0338  -0.0794 41  THR F N   
10427 C CA  . THR F  41  ? 0.9621 0.9826 0.8512 -0.1030 0.0371  -0.0810 41  THR F CA  
10428 C C   . THR F  41  ? 1.0827 1.1111 0.9695 -0.1033 0.0352  -0.0851 41  THR F C   
10429 O O   . THR F  41  ? 0.9671 0.9955 0.8562 -0.1018 0.0348  -0.0845 41  THR F O   
10430 C CB  . THR F  41  ? 0.8565 0.8729 0.7482 -0.1068 0.0444  -0.0844 41  THR F CB  
10431 O OG1 . THR F  41  ? 1.0152 1.0237 0.9101 -0.1062 0.0465  -0.0799 41  THR F OG1 
10432 C CG2 . THR F  41  ? 0.8807 0.8961 0.7760 -0.1076 0.0481  -0.0868 41  THR F CG2 
10433 N N   . GLN F  42  ? 1.1670 1.2023 1.0493 -0.1051 0.0340  -0.0891 42  GLN F N   
10434 C CA  . GLN F  42  ? 1.1806 1.2241 1.0606 -0.1055 0.0321  -0.0930 42  GLN F CA  
10435 C C   . GLN F  42  ? 1.1008 1.1468 0.9801 -0.1013 0.0262  -0.0893 42  GLN F C   
10436 O O   . GLN F  42  ? 1.0927 1.1415 0.9730 -0.1005 0.0256  -0.0902 42  GLN F O   
10437 C CB  . GLN F  42  ? 1.2372 1.2877 1.1130 -0.1082 0.0317  -0.0974 42  GLN F CB  
10438 C CG  . GLN F  42  ? 1.3053 1.3649 1.1790 -0.1091 0.0303  -0.1015 42  GLN F CG  
10439 C CD  . GLN F  42  ? 1.3943 1.4535 1.2701 -0.1116 0.0347  -0.1050 42  GLN F CD  
10440 O OE1 . GLN F  42  ? 1.4216 1.4751 1.2997 -0.1142 0.0400  -0.1064 42  GLN F OE1 
10441 N NE2 . GLN F  42  ? 1.4099 1.4751 1.2848 -0.1110 0.0326  -0.1064 42  GLN F NE2 
10442 N N   . ASN F  43  ? 1.0420 1.0872 0.9197 -0.0988 0.0221  -0.0853 43  ASN F N   
10443 C CA  . ASN F  43  ? 1.0236 1.0707 0.9007 -0.0949 0.0166  -0.0817 43  ASN F CA  
10444 C C   . ASN F  43  ? 1.0062 1.0483 0.8877 -0.0926 0.0166  -0.0781 43  ASN F C   
10445 O O   . ASN F  43  ? 0.9183 0.9634 0.8001 -0.0906 0.0142  -0.0777 43  ASN F O   
10446 C CB  . ASN F  43  ? 1.0601 1.1061 0.9345 -0.0932 0.0127  -0.0782 43  ASN F CB  
10447 C CG  . ASN F  43  ? 1.1957 1.2493 1.0657 -0.0934 0.0099  -0.0807 43  ASN F CG  
10448 O OD1 . ASN F  43  ? 1.2636 1.3208 1.1318 -0.0963 0.0122  -0.0848 43  ASN F OD1 
10449 N ND2 . ASN F  43  ? 1.2529 1.3090 1.1214 -0.0903 0.0050  -0.0782 43  ASN F ND2 
10450 N N   . ALA F  44  ? 0.9283 0.9627 0.8133 -0.0928 0.0196  -0.0754 44  ALA F N   
10451 C CA  . ALA F  44  ? 0.8652 0.8944 0.7551 -0.0907 0.0201  -0.0717 44  ALA F CA  
10452 C C   . ALA F  44  ? 0.9057 0.9371 0.7975 -0.0916 0.0227  -0.0752 44  ALA F C   
10453 O O   . ALA F  44  ? 0.9254 0.9573 0.8187 -0.0890 0.0204  -0.0733 44  ALA F O   
10454 C CB  . ALA F  44  ? 0.7462 0.7673 0.6401 -0.0913 0.0238  -0.0687 44  ALA F CB  
10455 N N   . ILE F  45  ? 0.8879 0.9204 0.7792 -0.0953 0.0276  -0.0804 45  ILE F N   
10456 C CA  . ILE F  45  ? 0.9370 0.9718 0.8293 -0.0969 0.0305  -0.0844 45  ILE F CA  
10457 C C   . ILE F  45  ? 0.9305 0.9731 0.8197 -0.0953 0.0260  -0.0855 45  ILE F C   
10458 O O   . ILE F  45  ? 0.8532 0.8959 0.7442 -0.0939 0.0258  -0.0850 45  ILE F O   
10459 C CB  . ILE F  45  ? 0.9323 0.9685 0.8233 -0.1017 0.0359  -0.0904 45  ILE F CB  
10460 C CG1 . ILE F  45  ? 0.8184 0.8459 0.7137 -0.1034 0.0417  -0.0896 45  ILE F CG1 
10461 C CG2 . ILE F  45  ? 0.9981 1.0391 0.8882 -0.1037 0.0377  -0.0951 45  ILE F CG2 
10462 C CD1 . ILE F  45  ? 1.0769 1.1049 0.9714 -0.1084 0.0477  -0.0956 45  ILE F CD1 
10463 N N   . ASP F  46  ? 0.9339 0.9828 0.8187 -0.0954 0.0226  -0.0869 46  ASP F N   
10464 C CA  . ASP F  46  ? 0.9506 1.0073 0.8326 -0.0938 0.0183  -0.0876 46  ASP F CA  
10465 C C   . ASP F  46  ? 0.9682 1.0229 0.8519 -0.0893 0.0141  -0.0826 46  ASP F C   
10466 O O   . ASP F  46  ? 0.7814 0.8391 0.6654 -0.0880 0.0129  -0.0829 46  ASP F O   
10467 C CB  . ASP F  46  ? 0.8842 0.9470 0.7618 -0.0943 0.0154  -0.0891 46  ASP F CB  
10468 C CG  . ASP F  46  ? 1.2830 1.3503 1.1586 -0.0987 0.0189  -0.0948 46  ASP F CG  
10469 O OD1 . ASP F  46  ? 1.3567 1.4239 1.2334 -0.1014 0.0229  -0.0981 46  ASP F OD1 
10470 O OD2 . ASP F  46  ? 1.3580 1.4290 1.2308 -0.0997 0.0177  -0.0960 46  ASP F OD2 
10471 N N   . GLU F  47  ? 0.9505 1.0003 0.8351 -0.0872 0.0119  -0.0779 47  GLU F N   
10472 C CA  . GLU F  47  ? 0.7713 0.8194 0.6573 -0.0832 0.0076  -0.0730 47  GLU F CA  
10473 C C   . GLU F  47  ? 0.7152 0.7581 0.6063 -0.0820 0.0096  -0.0707 47  GLU F C   
10474 O O   . GLU F  47  ? 0.7011 0.7451 0.5934 -0.0793 0.0069  -0.0687 47  GLU F O   
10475 C CB  . GLU F  47  ? 0.6994 0.7443 0.5844 -0.0817 0.0046  -0.0688 47  GLU F CB  
10476 C CG  . GLU F  47  ? 0.9000 0.9503 0.7799 -0.0822 0.0020  -0.0705 47  GLU F CG  
10477 C CD  . GLU F  47  ? 1.0376 1.0849 0.9161 -0.0806 -0.0014 -0.0663 47  GLU F CD  
10478 O OE1 . GLU F  47  ? 0.9210 0.9619 0.8023 -0.0798 -0.0011 -0.0623 47  GLU F OE1 
10479 O OE2 . GLU F  47  ? 1.0857 1.1373 0.9602 -0.0802 -0.0044 -0.0669 47  GLU F OE2 
10480 N N   . ILE F  48  ? 0.7115 0.7486 0.6060 -0.0839 0.0145  -0.0710 48  ILE F N   
10481 C CA  . ILE F  48  ? 0.5924 0.6243 0.4922 -0.0831 0.0173  -0.0693 48  ILE F CA  
10482 C C   . ILE F  48  ? 0.7496 0.7856 0.6490 -0.0841 0.0190  -0.0734 48  ILE F C   
10483 O O   . ILE F  48  ? 0.8106 0.8454 0.7129 -0.0821 0.0186  -0.0716 48  ILE F O   
10484 C CB  . ILE F  48  ? 0.6434 0.6682 0.5473 -0.0851 0.0228  -0.0689 48  ILE F CB  
10485 C CG1 . ILE F  48  ? 0.7818 0.8018 0.6871 -0.0834 0.0207  -0.0634 48  ILE F CG1 
10486 C CG2 . ILE F  48  ? 0.6035 0.6237 0.5129 -0.0848 0.0267  -0.0684 48  ILE F CG2 
10487 C CD1 . ILE F  48  ? 0.6766 0.6946 0.5846 -0.0795 0.0163  -0.0576 48  ILE F CD1 
10488 N N   . THR F  49  ? 0.7082 0.7494 0.6039 -0.0874 0.0210  -0.0788 49  THR F N   
10489 C CA  . THR F  49  ? 0.6495 0.6958 0.5437 -0.0887 0.0223  -0.0830 49  THR F CA  
10490 C C   . THR F  49  ? 0.7265 0.7778 0.6191 -0.0854 0.0169  -0.0811 49  THR F C   
10491 O O   . THR F  49  ? 0.7738 0.8252 0.6681 -0.0842 0.0171  -0.0809 49  THR F O   
10492 C CB  . THR F  49  ? 0.8693 0.9217 0.7592 -0.0928 0.0242  -0.0888 49  THR F CB  
10493 O OG1 . THR F  49  ? 0.9791 1.0266 0.8707 -0.0963 0.0300  -0.0913 49  THR F OG1 
10494 C CG2 . THR F  49  ? 0.6494 0.7084 0.5370 -0.0940 0.0243  -0.0926 49  THR F CG2 
10495 N N   . ASN F  50  ? 0.6413 0.6966 0.5306 -0.0838 0.0122  -0.0798 50  ASN F N   
10496 C CA  . ASN F  50  ? 0.7048 0.7647 0.5926 -0.0806 0.0071  -0.0778 50  ASN F CA  
10497 C C   . ASN F  50  ? 0.7704 0.8252 0.6624 -0.0771 0.0056  -0.0730 50  ASN F C   
10498 O O   . ASN F  50  ? 0.7055 0.7628 0.5977 -0.0751 0.0036  -0.0723 50  ASN F O   
10499 C CB  . ASN F  50  ? 0.6955 0.7589 0.5800 -0.0795 0.0029  -0.0766 50  ASN F CB  
10500 C CG  . ASN F  50  ? 0.8204 0.8896 0.7028 -0.0766 -0.0018 -0.0755 50  ASN F CG  
10501 O OD1 . ASN F  50  ? 0.9480 1.0246 0.8276 -0.0775 -0.0024 -0.0786 50  ASN F OD1 
10502 N ND2 . ASN F  50  ? 0.6836 0.7498 0.5677 -0.0731 -0.0051 -0.0710 50  ASN F ND2 
10503 N N   . LYS F  51  ? 0.6847 0.7323 0.5800 -0.0766 0.0065  -0.0696 51  LYS F N   
10504 C CA  . LYS F  51  ? 0.6426 0.6850 0.5425 -0.0735 0.0053  -0.0647 51  LYS F CA  
10505 C C   . LYS F  51  ? 0.6977 0.7385 0.6009 -0.0737 0.0086  -0.0659 51  LYS F C   
10506 O O   . LYS F  51  ? 0.6813 0.7227 0.5861 -0.0711 0.0064  -0.0638 51  LYS F O   
10507 C CB  . LYS F  51  ? 0.6988 0.7341 0.6020 -0.0735 0.0064  -0.0610 51  LYS F CB  
10508 C CG  . LYS F  51  ? 0.6323 0.6623 0.5408 -0.0704 0.0049  -0.0555 51  LYS F CG  
10509 C CD  . LYS F  51  ? 0.7017 0.7261 0.6124 -0.0703 0.0048  -0.0513 51  LYS F CD  
10510 C CE  . LYS F  51  ? 0.7042 0.7242 0.6200 -0.0672 0.0026  -0.0454 51  LYS F CE  
10511 N NZ  . LYS F  51  ? 0.6443 0.6608 0.5609 -0.0667 0.0006  -0.0408 51  LYS F NZ  
10512 N N   . VAL F  52  ? 0.6105 0.6493 0.5148 -0.0770 0.0142  -0.0694 52  VAL F N   
10513 C CA  . VAL F  52  ? 0.5893 0.6262 0.4965 -0.0777 0.0182  -0.0711 52  VAL F CA  
10514 C C   . VAL F  52  ? 0.7411 0.7850 0.6447 -0.0776 0.0166  -0.0740 52  VAL F C   
10515 O O   . VAL F  52  ? 0.8364 0.8795 0.7423 -0.0761 0.0169  -0.0732 52  VAL F O   
10516 C CB  . VAL F  52  ? 0.5474 0.5811 0.4557 -0.0818 0.0249  -0.0750 52  VAL F CB  
10517 C CG1 . VAL F  52  ? 0.5484 0.5793 0.4598 -0.0827 0.0294  -0.0767 52  VAL F CG1 
10518 C CG2 . VAL F  52  ? 0.6354 0.6622 0.5473 -0.0819 0.0267  -0.0720 52  VAL F CG2 
10519 N N   . ASN F  53  ? 0.6336 0.6846 0.5319 -0.0792 0.0148  -0.0773 53  ASN F N   
10520 C CA  . ASN F  53  ? 0.7215 0.7801 0.6162 -0.0791 0.0130  -0.0798 53  ASN F CA  
10521 C C   . ASN F  53  ? 0.8363 0.8965 0.7316 -0.0748 0.0079  -0.0758 53  ASN F C   
10522 O O   . ASN F  53  ? 0.8925 0.9557 0.7874 -0.0739 0.0075  -0.0765 53  ASN F O   
10523 C CB  . ASN F  53  ? 0.8194 0.8856 0.7090 -0.0814 0.0118  -0.0835 53  ASN F CB  
10524 C CG  . ASN F  53  ? 0.9155 0.9828 0.8036 -0.0863 0.0170  -0.0889 53  ASN F CG  
10525 O OD1 . ASN F  53  ? 0.7260 0.7887 0.6166 -0.0880 0.0216  -0.0903 53  ASN F OD1 
10526 N ND2 . ASN F  53  ? 0.9717 1.0450 0.8558 -0.0887 0.0164  -0.0921 53  ASN F ND2 
10527 N N   . SER F  54  ? 0.7075 0.7656 0.6036 -0.0721 0.0042  -0.0717 54  SER F N   
10528 C CA  . SER F  54  ? 0.6529 0.7121 0.5495 -0.0682 -0.0006 -0.0679 54  SER F CA  
10529 C C   . SER F  54  ? 0.6728 0.7273 0.5742 -0.0662 0.0004  -0.0653 54  SER F C   
10530 O O   . SER F  54  ? 0.6801 0.7375 0.5812 -0.0644 -0.0011 -0.0650 54  SER F O   
10531 C CB  . SER F  54  ? 0.6710 0.7283 0.5674 -0.0663 -0.0044 -0.0642 54  SER F CB  
10532 O OG  . SER F  54  ? 0.7859 0.8480 0.6777 -0.0678 -0.0056 -0.0665 54  SER F OG  
10533 N N   . VAL F  55  ? 0.6328 0.6799 0.5387 -0.0665 0.0032  -0.0633 55  VAL F N   
10534 C CA  . VAL F  55  ? 0.6216 0.6637 0.5330 -0.0647 0.0047  -0.0606 55  VAL F CA  
10535 C C   . VAL F  55  ? 0.6500 0.6943 0.5609 -0.0659 0.0078  -0.0641 55  VAL F C   
10536 O O   . VAL F  55  ? 0.6736 0.7165 0.5873 -0.0638 0.0076  -0.0623 55  VAL F O   
10537 C CB  . VAL F  55  ? 0.6517 0.6860 0.5684 -0.0655 0.0083  -0.0586 55  VAL F CB  
10538 C CG1 . VAL F  55  ? 0.7464 0.7757 0.6691 -0.0639 0.0105  -0.0562 55  VAL F CG1 
10539 C CG2 . VAL F  55  ? 0.5326 0.5645 0.4499 -0.0641 0.0049  -0.0544 55  VAL F CG2 
10540 N N   . ILE F  56  ? 0.6121 0.6600 0.5192 -0.0695 0.0107  -0.0692 56  ILE F N   
10541 C CA  . ILE F  56  ? 0.5971 0.6475 0.5030 -0.0714 0.0140  -0.0731 56  ILE F CA  
10542 C C   . ILE F  56  ? 0.6058 0.6646 0.5068 -0.0706 0.0104  -0.0745 56  ILE F C   
10543 O O   . ILE F  56  ? 0.6769 0.7370 0.5784 -0.0693 0.0102  -0.0743 56  ILE F O   
10544 C CB  . ILE F  56  ? 0.6702 0.7205 0.5745 -0.0762 0.0194  -0.0782 56  ILE F CB  
10545 C CG1 . ILE F  56  ? 0.6739 0.7152 0.5836 -0.0772 0.0241  -0.0769 56  ILE F CG1 
10546 C CG2 . ILE F  56  ? 0.6351 0.6894 0.5365 -0.0787 0.0221  -0.0826 56  ILE F CG2 
10547 C CD1 . ILE F  56  ? 0.5553 0.5957 0.4638 -0.0819 0.0297  -0.0819 56  ILE F CD1 
10548 N N   . GLU F  57  ? 0.5624 0.6271 0.4592 -0.0712 0.0075  -0.0758 57  GLU F N   
10549 C CA  . GLU F  57  ? 0.6223 0.6957 0.5145 -0.0708 0.0046  -0.0774 57  GLU F CA  
10550 C C   . GLU F  57  ? 0.6786 0.7532 0.5717 -0.0664 0.0002  -0.0735 57  GLU F C   
10551 O O   . GLU F  57  ? 0.7877 0.8681 0.6785 -0.0657 -0.0012 -0.0744 57  GLU F O   
10552 C CB  . GLU F  57  ? 0.8426 0.9215 0.7309 -0.0722 0.0025  -0.0791 57  GLU F CB  
10553 C CG  . GLU F  57  ? 1.3516 1.4402 1.2353 -0.0731 0.0009  -0.0819 57  GLU F CG  
10554 C CD  . GLU F  57  ? 1.4314 1.5246 1.3138 -0.0694 -0.0045 -0.0790 57  GLU F CD  
10555 O OE1 . GLU F  57  ? 1.2364 1.3263 1.1200 -0.0673 -0.0070 -0.0759 57  GLU F OE1 
10556 O OE2 . GLU F  57  ? 1.2895 1.3896 1.1696 -0.0688 -0.0062 -0.0797 57  GLU F OE2 
10557 N N   . LYS F  58  ? 0.6109 0.6802 0.5075 -0.0635 -0.0020 -0.0691 58  LYS F N   
10558 C CA  . LYS F  58  ? 0.5806 0.6505 0.4783 -0.0594 -0.0062 -0.0653 58  LYS F CA  
10559 C C   . LYS F  58  ? 0.6929 0.7602 0.5938 -0.0581 -0.0045 -0.0643 58  LYS F C   
10560 O O   . LYS F  58  ? 0.6864 0.7535 0.5889 -0.0548 -0.0075 -0.0612 58  LYS F O   
10561 C CB  . LYS F  58  ? 0.6401 0.7055 0.5402 -0.0572 -0.0091 -0.0611 58  LYS F CB  
10562 C CG  . LYS F  58  ? 0.6443 0.7126 0.5408 -0.0579 -0.0114 -0.0616 58  LYS F CG  
10563 C CD  . LYS F  58  ? 0.6866 0.7630 0.5789 -0.0569 -0.0145 -0.0628 58  LYS F CD  
10564 C CE  . LYS F  58  ? 0.6867 0.7659 0.5759 -0.0577 -0.0165 -0.0634 58  LYS F CE  
10565 N NZ  . LYS F  58  ? 0.6675 0.7546 0.5533 -0.0566 -0.0192 -0.0643 58  LYS F NZ  
10566 N N   . MET F  59  ? 0.6587 0.7237 0.5606 -0.0608 0.0004  -0.0671 59  MET F N   
10567 C CA  . MET F  59  ? 0.5938 0.6560 0.4988 -0.0599 0.0026  -0.0665 59  MET F CA  
10568 C C   . MET F  59  ? 0.7557 0.8242 0.6565 -0.0612 0.0034  -0.0699 59  MET F C   
10569 O O   . MET F  59  ? 0.9257 0.9942 0.8255 -0.0646 0.0079  -0.0736 59  MET F O   
10570 C CB  . MET F  59  ? 0.7210 0.7756 0.6303 -0.0619 0.0079  -0.0671 59  MET F CB  
10571 C CG  . MET F  59  ? 0.7110 0.7616 0.6245 -0.0607 0.0104  -0.0659 59  MET F CG  
10572 S SD  . MET F  59  ? 0.7801 0.8298 0.6968 -0.0554 0.0052  -0.0602 59  MET F SD  
10573 C CE  . MET F  59  ? 0.6515 0.6915 0.5765 -0.0542 0.0074  -0.0561 59  MET F CE  
10574 N N   . ASN F  60  ? 0.6542 0.7283 0.5528 -0.0586 -0.0007 -0.0684 60  ASN F N   
10575 C CA  . ASN F  60  ? 0.8432 0.9237 0.7382 -0.0593 -0.0004 -0.0708 60  ASN F CA  
10576 C C   . ASN F  60  ? 0.8053 0.8834 0.7031 -0.0566 -0.0004 -0.0684 60  ASN F C   
10577 O O   . ASN F  60  ? 0.7801 0.8594 0.6788 -0.0530 -0.0043 -0.0651 60  ASN F O   
10578 C CB  . ASN F  60  ? 1.1514 1.2406 1.0418 -0.0586 -0.0045 -0.0712 60  ASN F CB  
10579 C CG  . ASN F  60  ? 1.4963 1.5862 1.3880 -0.0541 -0.0093 -0.0669 60  ASN F CG  
10580 O OD1 . ASN F  60  ? 1.5030 1.5963 1.3940 -0.0521 -0.0106 -0.0659 60  ASN F OD1 
10581 N ND2 . ASN F  60  ? 1.4085 1.4954 1.3019 -0.0524 -0.0117 -0.0643 60  ASN F ND2 
10582 N N   . THR F  61  ? 0.8656 0.9401 0.7648 -0.0586 0.0042  -0.0703 61  THR F N   
10583 C CA  . THR F  61  ? 0.8269 0.8980 0.7294 -0.0562 0.0050  -0.0681 61  THR F CA  
10584 C C   . THR F  61  ? 0.8574 0.9350 0.7558 -0.0559 0.0041  -0.0693 61  THR F C   
10585 O O   . THR F  61  ? 0.7500 0.8343 0.6432 -0.0586 0.0044  -0.0726 61  THR F O   
10586 C CB  . THR F  61  ? 0.7928 0.8565 0.6992 -0.0583 0.0107  -0.0694 61  THR F CB  
10587 O OG1 . THR F  61  ? 0.8405 0.9066 0.7429 -0.0629 0.0149  -0.0745 61  THR F OG1 
10588 C CG2 . THR F  61  ? 0.7798 0.8364 0.6912 -0.0579 0.0114  -0.0671 61  THR F CG2 
10589 N N   . GLN F  62  ? 0.8519 0.9277 0.7529 -0.0527 0.0030  -0.0663 62  GLN F N   
10590 C CA  . GLN F  62  ? 0.8214 0.9027 0.7193 -0.0520 0.0024  -0.0668 62  GLN F CA  
10591 C C   . GLN F  62  ? 0.7974 0.8770 0.6943 -0.0553 0.0078  -0.0702 62  GLN F C   
10592 O O   . GLN F  62  ? 0.8228 0.8952 0.7234 -0.0567 0.0119  -0.0709 62  GLN F O   
10593 C CB  . GLN F  62  ? 0.7288 0.8084 0.6300 -0.0474 -0.0005 -0.0624 62  GLN F CB  
10594 C CG  . GLN F  62  ? 0.6497 0.7314 0.5512 -0.0442 -0.0058 -0.0592 62  GLN F CG  
10595 C CD  . GLN F  62  ? 0.7874 0.8783 0.6835 -0.0443 -0.0086 -0.0604 62  GLN F CD  
10596 O OE1 . GLN F  62  ? 0.9496 1.0442 0.8425 -0.0470 -0.0085 -0.0630 62  GLN F OE1 
10597 N NE2 . GLN F  62  ? 0.6475 0.7423 0.5429 -0.0414 -0.0111 -0.0583 62  GLN F NE2 
10598 N N   . PHE F  63  ? 0.6828 0.7689 0.5748 -0.0565 0.0079  -0.0722 63  PHE F N   
10599 C CA  . PHE F  63  ? 0.7391 0.8236 0.6297 -0.0594 0.0129  -0.0752 63  PHE F CA  
10600 C C   . PHE F  63  ? 0.6798 0.7592 0.5747 -0.0562 0.0136  -0.0721 63  PHE F C   
10601 O O   . PHE F  63  ? 0.8291 0.9123 0.7229 -0.0534 0.0108  -0.0699 63  PHE F O   
10602 C CB  . PHE F  63  ? 0.7348 0.8285 0.6184 -0.0621 0.0126  -0.0782 63  PHE F CB  
10603 C CG  . PHE F  63  ? 0.7729 0.8653 0.6541 -0.0659 0.0180  -0.0819 63  PHE F CG  
10604 C CD1 . PHE F  63  ? 0.6498 0.7432 0.5276 -0.0713 0.0218  -0.0868 63  PHE F CD1 
10605 C CD2 . PHE F  63  ? 0.7250 0.8149 0.6073 -0.0643 0.0195  -0.0806 63  PHE F CD2 
10606 C CE1 . PHE F  63  ? 0.7929 0.8848 0.6682 -0.0751 0.0270  -0.0905 63  PHE F CE1 
10607 C CE2 . PHE F  63  ? 0.7738 0.8622 0.6537 -0.0680 0.0247  -0.0841 63  PHE F CE2 
10608 C CZ  . PHE F  63  ? 0.8510 0.9404 0.7273 -0.0735 0.0284  -0.0891 63  PHE F CZ  
10609 N N   . THR F  64  ? 0.5805 0.6513 0.4807 -0.0566 0.0176  -0.0719 64  THR F N   
10610 C CA  . THR F  64  ? 0.7978 0.8631 0.7029 -0.0537 0.0187  -0.0690 64  THR F CA  
10611 C C   . THR F  64  ? 0.5847 0.6437 0.4918 -0.0566 0.0254  -0.0716 64  THR F C   
10612 O O   . THR F  64  ? 0.4946 0.5504 0.4023 -0.0599 0.0290  -0.0743 64  THR F O   
10613 C CB  . THR F  64  ? 0.9175 0.9776 0.8294 -0.0497 0.0157  -0.0642 64  THR F CB  
10614 O OG1 . THR F  64  ? 0.6891 0.7457 0.6032 -0.0512 0.0166  -0.0647 64  THR F OG1 
10615 C CG2 . THR F  64  ? 0.8469 0.9124 0.7572 -0.0461 0.0095  -0.0611 64  THR F CG2 
10616 N N   . ALA F  65  ? 0.5568 0.6139 0.4652 -0.0554 0.0272  -0.0708 65  ALA F N   
10617 C CA  . ALA F  65  ? 0.6035 0.6537 0.5148 -0.0576 0.0337  -0.0727 65  ALA F CA  
10618 C C   . ALA F  65  ? 0.6357 0.6783 0.5557 -0.0537 0.0339  -0.0682 65  ALA F C   
10619 O O   . ALA F  65  ? 0.6137 0.6552 0.5355 -0.0514 0.0340  -0.0663 65  ALA F O   
10620 C CB  . ALA F  65  ? 0.4791 0.5325 0.3850 -0.0596 0.0362  -0.0755 65  ALA F CB  
10621 N N   . VAL F  66  ? 0.4857 0.5232 0.4113 -0.0530 0.0339  -0.0664 66  VAL F N   
10622 C CA  . VAL F  66  ? 0.5764 0.6065 0.5109 -0.0499 0.0346  -0.0622 66  VAL F CA  
10623 C C   . VAL F  66  ? 0.6690 0.6936 0.6062 -0.0514 0.0412  -0.0638 66  VAL F C   
10624 O O   . VAL F  66  ? 0.8689 0.8936 0.8021 -0.0556 0.0460  -0.0685 66  VAL F O   
10625 C CB  . VAL F  66  ? 0.5184 0.5440 0.4582 -0.0497 0.0344  -0.0603 66  VAL F CB  
10626 C CG1 . VAL F  66  ? 0.5873 0.6143 0.5227 -0.0541 0.0371  -0.0648 66  VAL F CG1 
10627 C CG2 . VAL F  66  ? 0.5110 0.5280 0.4601 -0.0484 0.0383  -0.0577 66  VAL F CG2 
10628 N N   . GLY F  67  ? 0.5136 0.5334 0.4577 -0.0481 0.0415  -0.0601 67  GLY F N   
10629 C CA  . GLY F  67  ? 0.7809 0.7953 0.7281 -0.0491 0.0477  -0.0613 67  GLY F CA  
10630 C C   . GLY F  67  ? 0.6515 0.6696 0.5946 -0.0481 0.0468  -0.0616 67  GLY F C   
10631 O O   . GLY F  67  ? 0.4797 0.5045 0.4145 -0.0501 0.0456  -0.0646 67  GLY F O   
10632 N N   . LYS F  68  ? 0.7196 0.7336 0.6689 -0.0450 0.0473  -0.0582 68  LYS F N   
10633 C CA  . LYS F  68  ? 0.5077 0.5245 0.4541 -0.0436 0.0467  -0.0579 68  LYS F CA  
10634 C C   . LYS F  68  ? 0.6300 0.6398 0.5815 -0.0439 0.0530  -0.0581 68  LYS F C   
10635 O O   . LYS F  68  ? 0.6348 0.6376 0.5933 -0.0444 0.0571  -0.0576 68  LYS F O   
10636 C CB  . LYS F  68  ? 0.6605 0.6800 0.6091 -0.0387 0.0400  -0.0530 68  LYS F CB  
10637 C CG  . LYS F  68  ? 0.5503 0.5764 0.4942 -0.0381 0.0338  -0.0525 68  LYS F CG  
10638 C CD  . LYS F  68  ? 0.6765 0.7108 0.6116 -0.0386 0.0313  -0.0544 68  LYS F CD  
10639 C CE  . LYS F  68  ? 0.8259 0.8667 0.7558 -0.0393 0.0267  -0.0552 68  LYS F CE  
10640 N NZ  . LYS F  68  ? 0.7957 0.8382 0.7203 -0.0442 0.0301  -0.0601 68  LYS F NZ  
10641 N N   . GLU F  69  ? 0.7645 0.7761 0.7127 -0.0435 0.0539  -0.0588 69  GLU F N   
10642 C CA  . GLU F  69  ? 0.6335 0.6388 0.5859 -0.0439 0.0600  -0.0592 69  GLU F CA  
10643 C C   . GLU F  69  ? 0.6018 0.6065 0.5585 -0.0394 0.0574  -0.0548 69  GLU F C   
10644 O O   . GLU F  69  ? 0.6544 0.6652 0.6060 -0.0377 0.0530  -0.0540 69  GLU F O   
10645 C CB  . GLU F  69  ? 0.6543 0.6612 0.5985 -0.0484 0.0650  -0.0646 69  GLU F CB  
10646 C CG  . GLU F  69  ? 0.7830 0.7899 0.7233 -0.0534 0.0686  -0.0694 69  GLU F CG  
10647 C CD  . GLU F  69  ? 0.8431 0.8529 0.7741 -0.0582 0.0728  -0.0749 69  GLU F CD  
10648 O OE1 . GLU F  69  ? 0.8827 0.8975 0.8083 -0.0575 0.0707  -0.0747 69  GLU F OE1 
10649 O OE2 . GLU F  69  ? 0.7778 0.7850 0.7070 -0.0628 0.0782  -0.0793 69  GLU F OE2 
10650 N N   . PHE F  70  ? 0.5516 0.5492 0.5180 -0.0374 0.0601  -0.0520 70  PHE F N   
10651 C CA  . PHE F  70  ? 0.5950 0.5914 0.5665 -0.0332 0.0580  -0.0478 70  PHE F CA  
10652 C C   . PHE F  70  ? 0.6179 0.6070 0.5951 -0.0336 0.0650  -0.0481 70  PHE F C   
10653 O O   . PHE F  70  ? 0.6270 0.6103 0.6093 -0.0355 0.0703  -0.0493 70  PHE F O   
10654 C CB  . PHE F  70  ? 0.6252 0.6206 0.6043 -0.0293 0.0527  -0.0426 70  PHE F CB  
10655 C CG  . PHE F  70  ? 0.6405 0.6422 0.6148 -0.0290 0.0463  -0.0422 70  PHE F CG  
10656 C CD1 . PHE F  70  ? 0.5346 0.5428 0.5034 -0.0270 0.0408  -0.0412 70  PHE F CD1 
10657 C CD2 . PHE F  70  ? 0.5050 0.5058 0.4804 -0.0306 0.0460  -0.0428 70  PHE F CD2 
10658 C CE1 . PHE F  70  ? 0.4950 0.5086 0.4595 -0.0267 0.0352  -0.0409 70  PHE F CE1 
10659 C CE2 . PHE F  70  ? 0.4536 0.4598 0.4244 -0.0303 0.0403  -0.0425 70  PHE F CE2 
10660 C CZ  . PHE F  70  ? 0.4905 0.5031 0.4560 -0.0284 0.0350  -0.0416 70  PHE F CZ  
10661 N N   . ASN F  71  ? 0.6300 0.6197 0.6068 -0.0318 0.0651  -0.0471 71  ASN F N   
10662 C CA  . ASN F  71  ? 0.6185 0.6014 0.6009 -0.0319 0.0716  -0.0471 71  ASN F CA  
10663 C C   . ASN F  71  ? 0.6145 0.5919 0.6096 -0.0282 0.0710  -0.0420 71  ASN F C   
10664 O O   . ASN F  71  ? 0.5028 0.4819 0.5017 -0.0256 0.0654  -0.0384 71  ASN F O   
10665 C CB  . ASN F  71  ? 0.6186 0.6040 0.5955 -0.0316 0.0723  -0.0481 71  ASN F CB  
10666 C CG  . ASN F  71  ? 0.6575 0.6472 0.6350 -0.0271 0.0655  -0.0438 71  ASN F CG  
10667 O OD1 . ASN F  71  ? 0.7345 0.7214 0.7209 -0.0236 0.0632  -0.0394 71  ASN F OD1 
10668 N ND2 . ASN F  71  ? 0.8431 0.8396 0.8112 -0.0274 0.0625  -0.0451 71  ASN F ND2 
10669 N N   . HIS F  72  ? 0.6298 0.6007 0.6314 -0.0281 0.0771  -0.0417 72  HIS F N   
10670 C CA  . HIS F  72  ? 0.6913 0.6565 0.7057 -0.0250 0.0776  -0.0369 72  HIS F CA  
10671 C C   . HIS F  72  ? 0.7139 0.6821 0.7320 -0.0204 0.0706  -0.0319 72  HIS F C   
10672 O O   . HIS F  72  ? 0.8311 0.7967 0.8590 -0.0178 0.0687  -0.0274 72  HIS F O   
10673 C CB  . HIS F  72  ? 0.7942 0.7524 0.8143 -0.0258 0.0856  -0.0378 72  HIS F CB  
10674 C CG  . HIS F  72  ? 0.9806 0.9400 0.9956 -0.0255 0.0870  -0.0391 72  HIS F CG  
10675 N ND1 . HIS F  72  ? 1.0477 1.0097 1.0517 -0.0291 0.0899  -0.0442 72  HIS F ND1 
10676 C CD2 . HIS F  72  ? 1.0610 1.0197 1.0805 -0.0222 0.0858  -0.0359 72  HIS F CD2 
10677 C CE1 . HIS F  72  ? 1.1609 1.1236 1.1626 -0.0279 0.0904  -0.0439 72  HIS F CE1 
10678 N NE2 . HIS F  72  ? 1.1110 1.0716 1.1221 -0.0237 0.0881  -0.0389 72  HIS F NE2 
10679 N N   . LEU F  73  ? 0.5131 0.4869 0.5235 -0.0196 0.0670  -0.0325 73  LEU F N   
10680 C CA  . LEU F  73  ? 0.6565 0.6332 0.6695 -0.0154 0.0607  -0.0281 73  LEU F CA  
10681 C C   . LEU F  73  ? 0.6112 0.5944 0.6190 -0.0147 0.0532  -0.0273 73  LEU F C   
10682 O O   . LEU F  73  ? 0.5627 0.5500 0.5689 -0.0120 0.0480  -0.0251 73  LEU F O   
10683 C CB  . LEU F  73  ? 0.6817 0.6599 0.6908 -0.0144 0.0615  -0.0286 73  LEU F CB  
10684 C CG  . LEU F  73  ? 0.6643 0.6360 0.6800 -0.0142 0.0680  -0.0283 73  LEU F CG  
10685 C CD1 . LEU F  73  ? 0.6353 0.6091 0.6450 -0.0137 0.0689  -0.0294 73  LEU F CD1 
10686 C CD2 . LEU F  73  ? 0.6039 0.5715 0.6325 -0.0108 0.0667  -0.0231 73  LEU F CD2 
10687 N N   . GLU F  74  ? 0.5257 0.5097 0.5309 -0.0171 0.0531  -0.0293 74  GLU F N   
10688 C CA  . GLU F  74  ? 0.5063 0.4960 0.5068 -0.0167 0.0466  -0.0287 74  GLU F CA  
10689 C C   . GLU F  74  ? 0.5928 0.5800 0.5990 -0.0172 0.0459  -0.0272 74  GLU F C   
10690 O O   . GLU F  74  ? 0.5029 0.4935 0.5040 -0.0187 0.0432  -0.0287 74  GLU F O   
10691 C CB  . GLU F  74  ? 0.4236 0.4190 0.4122 -0.0196 0.0465  -0.0333 74  GLU F CB  
10692 C CG  . GLU F  74  ? 0.5046 0.5039 0.4868 -0.0189 0.0459  -0.0342 74  GLU F CG  
10693 C CD  . GLU F  74  ? 0.8197 0.8249 0.7906 -0.0221 0.0462  -0.0386 74  GLU F CD  
10694 O OE1 . GLU F  74  ? 0.7554 0.7589 0.7236 -0.0259 0.0509  -0.0424 74  GLU F OE1 
10695 O OE2 . GLU F  74  ? 0.5817 0.5931 0.5464 -0.0208 0.0418  -0.0382 74  GLU F OE2 
10696 N N   . LYS F  75  ? 0.5311 0.5123 0.5479 -0.0158 0.0482  -0.0241 75  LYS F N   
10697 C CA  . LYS F  75  ? 0.6174 0.5957 0.6407 -0.0161 0.0480  -0.0221 75  LYS F CA  
10698 C C   . LYS F  75  ? 0.5307 0.5133 0.5535 -0.0142 0.0402  -0.0190 75  LYS F C   
10699 O O   . LYS F  75  ? 0.4973 0.4798 0.5207 -0.0153 0.0389  -0.0187 75  LYS F O   
10700 C CB  . LYS F  75  ? 0.5958 0.5674 0.6315 -0.0146 0.0517  -0.0186 75  LYS F CB  
10701 C CG  . LYS F  75  ? 0.7005 0.6692 0.7440 -0.0144 0.0512  -0.0156 75  LYS F CG  
10702 C CD  . LYS F  75  ? 0.7703 0.7377 0.8099 -0.0180 0.0552  -0.0194 75  LYS F CD  
10703 C CE  . LYS F  75  ? 1.0386 1.0000 1.0815 -0.0202 0.0641  -0.0221 75  LYS F CE  
10704 N NZ  . LYS F  75  ? 1.2508 1.2105 1.2901 -0.0239 0.0682  -0.0259 75  LYS F NZ  
10705 N N   . ARG F  76  ? 0.5939 0.5800 0.6154 -0.0116 0.0352  -0.0169 76  ARG F N   
10706 C CA  . ARG F  76  ? 0.4886 0.4786 0.5095 -0.0099 0.0280  -0.0141 76  ARG F CA  
10707 C C   . ARG F  76  ? 0.4899 0.4850 0.5009 -0.0118 0.0253  -0.0172 76  ARG F C   
10708 O O   . ARG F  76  ? 0.5172 0.5130 0.5287 -0.0123 0.0224  -0.0161 76  ARG F O   
10709 C CB  . ARG F  76  ? 0.3960 0.3883 0.4177 -0.0067 0.0239  -0.0114 76  ARG F CB  
10710 C CG  . ARG F  76  ? 0.4221 0.4100 0.4550 -0.0044 0.0246  -0.0071 76  ARG F CG  
10711 C CD  . ARG F  76  ? 0.4754 0.4655 0.5083 -0.0016 0.0210  -0.0051 76  ARG F CD  
10712 N NE  . ARG F  76  ? 0.5225 0.5144 0.5487 -0.0019 0.0236  -0.0083 76  ARG F NE  
10713 C CZ  . ARG F  76  ? 0.4763 0.4725 0.4972 -0.0004 0.0201  -0.0083 76  ARG F CZ  
10714 N NH1 . ARG F  76  ? 0.5408 0.5396 0.5623 0.0015  0.0141  -0.0056 76  ARG F NH1 
10715 N NH2 . ARG F  76  ? 0.4170 0.4147 0.4319 -0.0008 0.0227  -0.0109 76  ARG F NH2 
10716 N N   . ILE F  77  ? 0.5243 0.5232 0.5265 -0.0130 0.0262  -0.0209 77  ILE F N   
10717 C CA  . ILE F  77  ? 0.5135 0.5177 0.5065 -0.0150 0.0240  -0.0240 77  ILE F CA  
10718 C C   . ILE F  77  ? 0.4812 0.4831 0.4736 -0.0184 0.0280  -0.0268 77  ILE F C   
10719 O O   . ILE F  77  ? 0.4639 0.4688 0.4518 -0.0199 0.0256  -0.0281 77  ILE F O   
10720 C CB  . ILE F  77  ? 0.4081 0.4174 0.3921 -0.0156 0.0241  -0.0270 77  ILE F CB  
10721 C CG1 . ILE F  77  ? 0.6681 0.6740 0.6528 -0.0165 0.0302  -0.0288 77  ILE F CG1 
10722 C CG2 . ILE F  77  ? 0.5050 0.5184 0.4874 -0.0124 0.0185  -0.0244 77  ILE F CG2 
10723 C CD1 . ILE F  77  ? 0.6890 0.7000 0.6652 -0.0170 0.0303  -0.0314 77  ILE F CD1 
10724 N N   . GLU F  78  ? 0.4582 0.4545 0.4552 -0.0198 0.0343  -0.0278 78  GLU F N   
10725 C CA  . GLU F  78  ? 0.4943 0.4874 0.4919 -0.0229 0.0388  -0.0303 78  GLU F CA  
10726 C C   . GLU F  78  ? 0.5142 0.5055 0.5178 -0.0220 0.0360  -0.0269 78  GLU F C   
10727 O O   . GLU F  78  ? 0.5114 0.5032 0.5124 -0.0243 0.0364  -0.0287 78  GLU F O   
10728 C CB  . GLU F  78  ? 0.5310 0.5177 0.5338 -0.0241 0.0464  -0.0314 78  GLU F CB  
10729 C CG  . GLU F  78  ? 0.5763 0.5590 0.5804 -0.0275 0.0519  -0.0341 78  GLU F CG  
10730 C CD  . GLU F  78  ? 0.9903 0.9660 1.0006 -0.0285 0.0597  -0.0349 78  GLU F CD  
10731 O OE1 . GLU F  78  ? 1.1907 1.1658 1.2007 -0.0278 0.0617  -0.0354 78  GLU F OE1 
10732 O OE2 . GLU F  78  ? 1.0842 1.0549 1.1000 -0.0299 0.0639  -0.0350 78  GLU F OE2 
10733 N N   . ASN F  79  ? 0.4870 0.4764 0.4985 -0.0188 0.0331  -0.0219 79  ASN F N   
10734 C CA  . ASN F  79  ? 0.4774 0.4655 0.4948 -0.0178 0.0298  -0.0180 79  ASN F CA  
10735 C C   . ASN F  79  ? 0.5109 0.5047 0.5222 -0.0172 0.0229  -0.0174 79  ASN F C   
10736 O O   . ASN F  79  ? 0.6134 0.6072 0.6253 -0.0179 0.0209  -0.0163 79  ASN F O   
10737 C CB  . ASN F  79  ? 0.4323 0.4167 0.4606 -0.0148 0.0291  -0.0127 79  ASN F CB  
10738 C CG  . ASN F  79  ? 0.5846 0.5624 0.6211 -0.0155 0.0362  -0.0124 79  ASN F CG  
10739 O OD1 . ASN F  79  ? 0.5845 0.5596 0.6205 -0.0181 0.0409  -0.0149 79  ASN F OD1 
10740 N ND2 . ASN F  79  ? 0.6365 0.6115 0.6807 -0.0132 0.0372  -0.0093 79  ASN F ND2 
10741 N N   . LEU F  80  ? 0.3296 0.3281 0.3352 -0.0160 0.0194  -0.0181 80  LEU F N   
10742 C CA  . LEU F  80  ? 0.4037 0.4078 0.4028 -0.0156 0.0135  -0.0182 80  LEU F CA  
10743 C C   . LEU F  80  ? 0.5285 0.5347 0.5206 -0.0189 0.0150  -0.0223 80  LEU F C   
10744 O O   . LEU F  80  ? 0.4708 0.4783 0.4614 -0.0195 0.0120  -0.0217 80  LEU F O   
10745 C CB  . LEU F  80  ? 0.4614 0.4700 0.4551 -0.0140 0.0108  -0.0188 80  LEU F CB  
10746 C CG  . LEU F  80  ? 0.5069 0.5203 0.4970 -0.0123 0.0041  -0.0172 80  LEU F CG  
10747 C CD1 . LEU F  80  ? 0.3132 0.3319 0.2957 -0.0118 0.0030  -0.0194 80  LEU F CD1 
10748 C CD2 . LEU F  80  ? 0.4984 0.5135 0.4857 -0.0138 0.0016  -0.0176 80  LEU F CD2 
10749 N N   . ASN F  81  ? 0.5037 0.5101 0.4915 -0.0212 0.0198  -0.0265 81  ASN F N   
10750 C CA  . ASN F  81  ? 0.4122 0.4205 0.3935 -0.0247 0.0220  -0.0309 81  ASN F CA  
10751 C C   . ASN F  81  ? 0.6915 0.6953 0.6776 -0.0262 0.0243  -0.0303 81  ASN F C   
10752 O O   . ASN F  81  ? 0.5038 0.5098 0.4859 -0.0279 0.0228  -0.0317 81  ASN F O   
10753 C CB  . ASN F  81  ? 0.4703 0.4787 0.4472 -0.0271 0.0275  -0.0353 81  ASN F CB  
10754 C CG  . ASN F  81  ? 0.5573 0.5675 0.5277 -0.0311 0.0301  -0.0400 81  ASN F CG  
10755 O OD1 . ASN F  81  ? 0.5679 0.5839 0.5315 -0.0319 0.0266  -0.0416 81  ASN F OD1 
10756 N ND2 . ASN F  81  ? 0.5455 0.5509 0.5183 -0.0338 0.0366  -0.0425 81  ASN F ND2 
10757 N N   . LYS F  82  ? 0.4439 0.4414 0.4387 -0.0256 0.0281  -0.0281 82  LYS F N   
10758 C CA  . LYS F  82  ? 0.5109 0.5038 0.5115 -0.0267 0.0305  -0.0268 82  LYS F CA  
10759 C C   . LYS F  82  ? 0.5259 0.5204 0.5282 -0.0251 0.0244  -0.0229 82  LYS F C   
10760 O O   . LYS F  82  ? 0.5770 0.5705 0.5796 -0.0267 0.0248  -0.0231 82  LYS F O   
10761 C CB  . LYS F  82  ? 0.5858 0.5720 0.5966 -0.0258 0.0354  -0.0244 82  LYS F CB  
10762 C CG  . LYS F  82  ? 0.7265 0.7080 0.7450 -0.0261 0.0371  -0.0216 82  LYS F CG  
10763 C CD  . LYS F  82  ? 0.8641 0.8390 0.8932 -0.0250 0.0421  -0.0190 82  LYS F CD  
10764 C CE  . LYS F  82  ? 1.1529 1.1238 1.1906 -0.0246 0.0427  -0.0149 82  LYS F CE  
10765 N NZ  . LYS F  82  ? 1.0164 0.9866 1.0504 -0.0277 0.0455  -0.0181 82  LYS F NZ  
10766 N N   . LYS F  83  ? 0.5449 0.5418 0.5483 -0.0221 0.0190  -0.0196 83  LYS F N   
10767 C CA  . LYS F  83  ? 0.5112 0.5098 0.5159 -0.0207 0.0130  -0.0159 83  LYS F CA  
10768 C C   . LYS F  83  ? 0.4828 0.4863 0.4785 -0.0224 0.0099  -0.0187 83  LYS F C   
10769 O O   . LYS F  83  ? 0.5943 0.5975 0.5904 -0.0231 0.0080  -0.0173 83  LYS F O   
10770 C CB  . LYS F  83  ? 0.3308 0.3309 0.3381 -0.0175 0.0081  -0.0121 83  LYS F CB  
10771 C CG  . LYS F  83  ? 0.3994 0.4015 0.4070 -0.0164 0.0018  -0.0087 83  LYS F CG  
10772 C CD  . LYS F  83  ? 0.3926 0.3950 0.4050 -0.0135 -0.0023 -0.0044 83  LYS F CD  
10773 C CE  . LYS F  83  ? 0.4725 0.4792 0.4789 -0.0123 -0.0048 -0.0061 83  LYS F CE  
10774 N NZ  . LYS F  83  ? 0.5465 0.5537 0.5567 -0.0097 -0.0095 -0.0021 83  LYS F NZ  
10775 N N   . VAL F  84  ? 0.5178 0.5259 0.5055 -0.0231 0.0096  -0.0224 84  VAL F N   
10776 C CA  . VAL F  84  ? 0.5400 0.5533 0.5193 -0.0246 0.0068  -0.0250 84  VAL F CA  
10777 C C   . VAL F  84  ? 0.4817 0.4936 0.4589 -0.0280 0.0107  -0.0283 84  VAL F C   
10778 O O   . VAL F  84  ? 0.5947 0.6092 0.5678 -0.0292 0.0084  -0.0292 84  VAL F O   
10779 C CB  . VAL F  84  ? 0.4136 0.4326 0.3853 -0.0244 0.0055  -0.0279 84  VAL F CB  
10780 C CG1 . VAL F  84  ? 0.6271 0.6455 0.5962 -0.0267 0.0113  -0.0320 84  VAL F CG1 
10781 C CG2 . VAL F  84  ? 0.5035 0.5281 0.4677 -0.0253 0.0016  -0.0296 84  VAL F CG2 
10782 N N   . ASP F  85  ? 0.4657 0.4734 0.4460 -0.0296 0.0169  -0.0301 85  ASP F N   
10783 C CA  . ASP F  85  ? 0.4463 0.4517 0.4256 -0.0330 0.0215  -0.0332 85  ASP F CA  
10784 C C   . ASP F  85  ? 0.4137 0.4148 0.3997 -0.0326 0.0212  -0.0296 85  ASP F C   
10785 O O   . ASP F  85  ? 0.5237 0.5253 0.5072 -0.0346 0.0213  -0.0309 85  ASP F O   
10786 C CB  . ASP F  85  ? 0.3841 0.3859 0.3649 -0.0349 0.0287  -0.0362 85  ASP F CB  
10787 C CG  . ASP F  85  ? 0.6101 0.6168 0.5824 -0.0368 0.0298  -0.0410 85  ASP F CG  
10788 O OD1 . ASP F  85  ? 0.5912 0.6042 0.5564 -0.0369 0.0255  -0.0423 85  ASP F OD1 
10789 O OD2 . ASP F  85  ? 0.8083 0.8126 0.7810 -0.0381 0.0351  -0.0434 85  ASP F OD2 
10790 N N   . ASP F  86  ? 0.4467 0.4439 0.4414 -0.0300 0.0209  -0.0249 86  ASP F N   
10791 C CA  . ASP F  86  ? 0.4079 0.4011 0.4097 -0.0294 0.0204  -0.0206 86  ASP F CA  
10792 C C   . ASP F  86  ? 0.4861 0.4830 0.4851 -0.0284 0.0135  -0.0181 86  ASP F C   
10793 O O   . ASP F  86  ? 0.4784 0.4734 0.4802 -0.0289 0.0129  -0.0159 86  ASP F O   
10794 C CB  . ASP F  86  ? 0.5696 0.5582 0.5818 -0.0269 0.0216  -0.0160 86  ASP F CB  
10795 C CG  . ASP F  86  ? 0.8181 0.8015 0.8350 -0.0282 0.0294  -0.0179 86  ASP F CG  
10796 O OD1 . ASP F  86  ? 0.8851 0.8676 0.8978 -0.0313 0.0340  -0.0224 86  ASP F OD1 
10797 O OD2 . ASP F  86  ? 0.8823 0.8623 0.9070 -0.0263 0.0311  -0.0149 86  ASP F OD2 
10798 N N   . GLY F  87  ? 0.5031 0.5050 0.4967 -0.0271 0.0087  -0.0185 87  GLY F N   
10799 C CA  . GLY F  87  ? 0.3892 0.3947 0.3793 -0.0263 0.0024  -0.0166 87  GLY F CA  
10800 C C   . GLY F  87  ? 0.4799 0.4880 0.4628 -0.0289 0.0024  -0.0202 87  GLY F C   
10801 O O   . GLY F  87  ? 0.4687 0.4764 0.4519 -0.0294 0.0003  -0.0184 87  GLY F O   
10802 N N   . PHE F  88  ? 0.4086 0.4198 0.3850 -0.0307 0.0048  -0.0252 88  PHE F N   
10803 C CA  . PHE F  88  ? 0.4666 0.4808 0.4362 -0.0335 0.0052  -0.0290 88  PHE F CA  
10804 C C   . PHE F  88  ? 0.4473 0.4567 0.4204 -0.0357 0.0096  -0.0293 88  PHE F C   
10805 O O   . PHE F  88  ? 0.5583 0.5687 0.5285 -0.0372 0.0085  -0.0300 88  PHE F O   
10806 C CB  . PHE F  88  ? 0.4533 0.4715 0.4161 -0.0352 0.0075  -0.0342 88  PHE F CB  
10807 C CG  . PHE F  88  ? 0.4029 0.4266 0.3612 -0.0332 0.0032  -0.0341 88  PHE F CG  
10808 C CD1 . PHE F  88  ? 0.3834 0.4102 0.3376 -0.0338 0.0051  -0.0373 88  PHE F CD1 
10809 C CD2 . PHE F  88  ? 0.4833 0.5090 0.4414 -0.0309 -0.0026 -0.0309 88  PHE F CD2 
10810 C CE1 . PHE F  88  ? 0.4135 0.4453 0.3639 -0.0318 0.0013  -0.0369 88  PHE F CE1 
10811 C CE2 . PHE F  88  ? 0.3921 0.4226 0.3464 -0.0290 -0.0062 -0.0308 88  PHE F CE2 
10812 C CZ  . PHE F  88  ? 0.3945 0.4280 0.3452 -0.0293 -0.0042 -0.0337 88  PHE F CZ  
10813 N N   . LEU F  89  ? 0.3913 0.3954 0.3710 -0.0358 0.0146  -0.0287 89  LEU F N   
10814 C CA  . LEU F  89  ? 0.4314 0.4303 0.4157 -0.0377 0.0194  -0.0286 89  LEU F CA  
10815 C C   . LEU F  89  ? 0.5036 0.5005 0.4922 -0.0365 0.0161  -0.0237 89  LEU F C   
10816 O O   . LEU F  89  ? 0.5511 0.5467 0.5391 -0.0384 0.0175  -0.0243 89  LEU F O   
10817 C CB  . LEU F  89  ? 0.4399 0.4332 0.4314 -0.0376 0.0254  -0.0282 89  LEU F CB  
10818 C CG  . LEU F  89  ? 0.4968 0.4838 0.4946 -0.0391 0.0309  -0.0274 89  LEU F CG  
10819 C CD1 . LEU F  89  ? 0.5399 0.5278 0.5317 -0.0428 0.0338  -0.0323 89  LEU F CD1 
10820 C CD2 . LEU F  89  ? 0.4972 0.4789 0.5019 -0.0390 0.0371  -0.0275 89  LEU F CD2 
10821 N N   . ASP F  90  ? 0.4562 0.4532 0.4492 -0.0334 0.0117  -0.0187 90  ASP F N   
10822 C CA  . ASP F  90  ? 0.4093 0.4047 0.4064 -0.0322 0.0080  -0.0135 90  ASP F CA  
10823 C C   . ASP F  90  ? 0.3991 0.3990 0.3889 -0.0330 0.0031  -0.0142 90  ASP F C   
10824 O O   . ASP F  90  ? 0.5073 0.5057 0.4981 -0.0337 0.0023  -0.0122 90  ASP F O   
10825 C CB  . ASP F  90  ? 0.3985 0.3931 0.4022 -0.0290 0.0046  -0.0082 90  ASP F CB  
10826 C CG  . ASP F  90  ? 0.7952 0.7844 0.8087 -0.0282 0.0096  -0.0059 90  ASP F CG  
10827 O OD1 . ASP F  90  ? 0.8645 0.8497 0.8809 -0.0300 0.0152  -0.0072 90  ASP F OD1 
10828 O OD2 . ASP F  90  ? 0.8893 0.8780 0.9079 -0.0258 0.0080  -0.0028 90  ASP F OD2 
10829 N N   . ILE F  91  ? 0.4064 0.4115 0.3890 -0.0327 -0.0001 -0.0169 91  ILE F N   
10830 C CA  . ILE F  91  ? 0.4947 0.5041 0.4701 -0.0334 -0.0046 -0.0179 91  ILE F CA  
10831 C C   . ILE F  91  ? 0.5413 0.5509 0.5123 -0.0365 -0.0014 -0.0218 91  ILE F C   
10832 O O   . ILE F  91  ? 0.5362 0.5456 0.5061 -0.0373 -0.0032 -0.0205 91  ILE F O   
10833 C CB  . ILE F  91  ? 0.4495 0.4646 0.4184 -0.0324 -0.0078 -0.0203 91  ILE F CB  
10834 C CG1 . ILE F  91  ? 0.3780 0.3931 0.3507 -0.0294 -0.0114 -0.0164 91  ILE F CG1 
10835 C CG2 . ILE F  91  ? 0.4978 0.5171 0.4592 -0.0334 -0.0115 -0.0218 91  ILE F CG2 
10836 C CD1 . ILE F  91  ? 0.5787 0.5988 0.5458 -0.0282 -0.0142 -0.0183 91  ILE F CD1 
10837 N N   . TRP F  92  ? 0.4105 0.4206 0.3791 -0.0384 0.0033  -0.0265 92  TRP F N   
10838 C CA  . TRP F  92  ? 0.3872 0.3979 0.3513 -0.0417 0.0065  -0.0308 92  TRP F CA  
10839 C C   . TRP F  92  ? 0.4892 0.4943 0.4587 -0.0430 0.0102  -0.0292 92  TRP F C   
10840 O O   . TRP F  92  ? 0.5325 0.5380 0.4990 -0.0449 0.0102  -0.0303 92  TRP F O   
10841 C CB  . TRP F  92  ? 0.3912 0.4039 0.3515 -0.0437 0.0107  -0.0362 92  TRP F CB  
10842 C CG  . TRP F  92  ? 0.4765 0.4961 0.4296 -0.0433 0.0071  -0.0386 92  TRP F CG  
10843 C CD1 . TRP F  92  ? 0.4137 0.4358 0.3657 -0.0418 0.0065  -0.0392 92  TRP F CD1 
10844 C CD2 . TRP F  92  ? 0.4608 0.4858 0.4069 -0.0442 0.0037  -0.0405 92  TRP F CD2 
10845 N NE1 . TRP F  92  ? 0.5259 0.5546 0.4709 -0.0417 0.0029  -0.0412 92  TRP F NE1 
10846 C CE2 . TRP F  92  ? 0.4408 0.4714 0.3822 -0.0431 0.0011  -0.0420 92  TRP F CE2 
10847 C CE3 . TRP F  92  ? 0.4791 0.5046 0.4227 -0.0458 0.0026  -0.0409 92  TRP F CE3 
10848 C CZ2 . TRP F  92  ? 0.4295 0.4663 0.3642 -0.0435 -0.0023 -0.0439 92  TRP F CZ2 
10849 C CZ3 . TRP F  92  ? 0.5737 0.6053 0.5104 -0.0463 -0.0008 -0.0430 92  TRP F CZ3 
10850 C CH2 . TRP F  92  ? 0.5353 0.5724 0.4678 -0.0451 -0.0032 -0.0444 92  TRP F CH2 
10851 N N   . THR F  93  ? 0.4924 0.4922 0.4701 -0.0420 0.0134  -0.0264 93  THR F N   
10852 C CA  . THR F  93  ? 0.5275 0.5216 0.5114 -0.0428 0.0171  -0.0241 93  THR F CA  
10853 C C   . THR F  93  ? 0.5182 0.5124 0.5028 -0.0417 0.0122  -0.0195 93  THR F C   
10854 O O   . THR F  93  ? 0.5208 0.5138 0.5045 -0.0435 0.0135  -0.0199 93  THR F O   
10855 C CB  . THR F  93  ? 0.4832 0.4718 0.4766 -0.0413 0.0209  -0.0210 93  THR F CB  
10856 O OG1 . THR F  93  ? 0.4993 0.4871 0.4918 -0.0427 0.0263  -0.0256 93  THR F OG1 
10857 C CG2 . THR F  93  ? 0.4336 0.4165 0.4342 -0.0418 0.0244  -0.0179 93  THR F CG2 
10858 N N   . TYR F  94  ? 0.5185 0.5144 0.5048 -0.0390 0.0066  -0.0153 94  TYR F N   
10859 C CA  . TYR F  94  ? 0.4817 0.4778 0.4686 -0.0380 0.0017  -0.0106 94  TYR F CA  
10860 C C   . TYR F  94  ? 0.4940 0.4941 0.4722 -0.0398 -0.0011 -0.0135 94  TYR F C   
10861 O O   . TYR F  94  ? 0.5233 0.5219 0.5014 -0.0408 -0.0014 -0.0119 94  TYR F O   
10862 C CB  . TYR F  94  ? 0.4458 0.4434 0.4352 -0.0351 -0.0038 -0.0063 94  TYR F CB  
10863 C CG  . TYR F  94  ? 0.4965 0.4939 0.4877 -0.0343 -0.0087 -0.0009 94  TYR F CG  
10864 C CD1 . TYR F  94  ? 0.4933 0.4864 0.4928 -0.0337 -0.0074 0.0042  94  TYR F CD1 
10865 C CD2 . TYR F  94  ? 0.4323 0.4339 0.4169 -0.0341 -0.0145 -0.0008 94  TYR F CD2 
10866 C CE1 . TYR F  94  ? 0.5220 0.5153 0.5228 -0.0331 -0.0120 0.0093  94  TYR F CE1 
10867 C CE2 . TYR F  94  ? 0.4524 0.4538 0.4380 -0.0337 -0.0190 0.0040  94  TYR F CE2 
10868 C CZ  . TYR F  94  ? 0.5870 0.5844 0.5806 -0.0332 -0.0178 0.0091  94  TYR F CZ  
10869 O OH  . TYR F  94  ? 0.7052 0.7029 0.6997 -0.0330 -0.0224 0.0140  94  TYR F OH  
10870 N N   . ASN F  95  ? 0.4716 0.4767 0.4427 -0.0401 -0.0029 -0.0175 95  ASN F N   
10871 C CA  . ASN F  95  ? 0.4876 0.4968 0.4504 -0.0416 -0.0054 -0.0203 95  ASN F CA  
10872 C C   . ASN F  95  ? 0.5155 0.5236 0.4762 -0.0447 -0.0009 -0.0239 95  ASN F C   
10873 O O   . ASN F  95  ? 0.5041 0.5127 0.4617 -0.0459 -0.0023 -0.0237 95  ASN F O   
10874 C CB  . ASN F  95  ? 0.5424 0.5574 0.4989 -0.0411 -0.0078 -0.0237 95  ASN F CB  
10875 C CG  . ASN F  95  ? 0.7040 0.7207 0.6611 -0.0382 -0.0133 -0.0202 95  ASN F CG  
10876 O OD1 . ASN F  95  ? 0.6076 0.6211 0.5707 -0.0366 -0.0148 -0.0154 95  ASN F OD1 
10877 N ND2 . ASN F  95  ? 0.6728 0.6946 0.6240 -0.0377 -0.0161 -0.0225 95  ASN F ND2 
10878 N N   . ALA F  96  ? 0.5018 0.5082 0.4639 -0.0462 0.0048  -0.0274 96  ALA F N   
10879 C CA  . ALA F  96  ? 0.5621 0.5671 0.5223 -0.0495 0.0098  -0.0313 96  ALA F CA  
10880 C C   . ALA F  96  ? 0.6067 0.6064 0.5722 -0.0499 0.0116  -0.0277 96  ALA F C   
10881 O O   . ALA F  96  ? 0.6012 0.6010 0.5636 -0.0520 0.0124  -0.0292 96  ALA F O   
10882 C CB  . ALA F  96  ? 0.5253 0.5292 0.4864 -0.0511 0.0157  -0.0355 96  ALA F CB  
10883 N N   . GLU F  97  ? 0.5144 0.5095 0.4882 -0.0479 0.0124  -0.0229 97  GLU F N   
10884 C CA  . GLU F  97  ? 0.5589 0.5490 0.5388 -0.0479 0.0141  -0.0186 97  GLU F CA  
10885 C C   . GLU F  97  ? 0.5653 0.5572 0.5420 -0.0475 0.0085  -0.0155 97  GLU F C   
10886 O O   . GLU F  97  ? 0.6476 0.6376 0.6239 -0.0491 0.0101  -0.0152 97  GLU F O   
10887 C CB  . GLU F  97  ? 0.6658 0.6517 0.6555 -0.0453 0.0150  -0.0134 97  GLU F CB  
10888 C CG  . GLU F  97  ? 0.5630 0.5454 0.5571 -0.0459 0.0216  -0.0159 97  GLU F CG  
10889 C CD  . GLU F  97  ? 0.7393 0.7164 0.7370 -0.0482 0.0287  -0.0173 97  GLU F CD  
10890 O OE1 . GLU F  97  ? 0.7667 0.7396 0.7703 -0.0484 0.0345  -0.0179 97  GLU F OE1 
10891 O OE2 . GLU F  97  ? 1.0135 0.9906 1.0084 -0.0499 0.0287  -0.0177 97  GLU F OE2 
10892 N N   . LEU F  98  ? 0.4505 0.4461 0.4248 -0.0454 0.0023  -0.0132 98  LEU F N   
10893 C CA  . LEU F  98  ? 0.4785 0.4761 0.4492 -0.0451 -0.0032 -0.0104 98  LEU F CA  
10894 C C   . LEU F  98  ? 0.5902 0.5913 0.5522 -0.0475 -0.0036 -0.0152 98  LEU F C   
10895 O O   . LEU F  98  ? 0.5249 0.5256 0.4847 -0.0485 -0.0052 -0.0137 98  LEU F O   
10896 C CB  . LEU F  98  ? 0.4724 0.4729 0.4424 -0.0426 -0.0094 -0.0075 98  LEU F CB  
10897 C CG  . LEU F  98  ? 0.5831 0.5810 0.5606 -0.0405 -0.0121 -0.0006 98  LEU F CG  
10898 C CD1 . LEU F  98  ? 0.7841 0.7816 0.7605 -0.0409 -0.0156 0.0034  98  LEU F CD1 
10899 C CD2 . LEU F  98  ? 0.6501 0.6429 0.6369 -0.0399 -0.0068 0.0015  98  LEU F CD2 
10900 N N   . LEU F  99  ? 0.5288 0.5334 0.4859 -0.0485 -0.0023 -0.0207 99  LEU F N   
10901 C CA  . LEU F  99  ? 0.6042 0.6128 0.5533 -0.0507 -0.0026 -0.0254 99  LEU F CA  
10902 C C   . LEU F  99  ? 0.5522 0.5578 0.5017 -0.0534 0.0019  -0.0269 99  LEU F C   
10903 O O   . LEU F  99  ? 0.5957 0.6025 0.5408 -0.0547 0.0003  -0.0274 99  LEU F O   
10904 C CB  . LEU F  99  ? 0.6359 0.6489 0.5808 -0.0514 -0.0012 -0.0308 99  LEU F CB  
10905 C CG  . LEU F  99  ? 0.5928 0.6107 0.5298 -0.0537 -0.0015 -0.0357 99  LEU F CG  
10906 C CD1 . LEU F  99  ? 0.6211 0.6425 0.5536 -0.0526 -0.0075 -0.0340 99  LEU F CD1 
10907 C CD2 . LEU F  99  ? 0.6421 0.6643 0.5758 -0.0546 0.0003  -0.0408 99  LEU F CD2 
10908 N N   . VAL F  100 ? 0.4607 0.4620 0.4155 -0.0543 0.0077  -0.0276 100 VAL F N   
10909 C CA  . VAL F  100 ? 0.5666 0.5642 0.5225 -0.0569 0.0128  -0.0291 100 VAL F CA  
10910 C C   . VAL F  100 ? 0.6138 0.6081 0.5729 -0.0562 0.0111  -0.0236 100 VAL F C   
10911 O O   . VAL F  100 ? 0.6796 0.6738 0.6354 -0.0581 0.0115  -0.0246 100 VAL F O   
10912 C CB  . VAL F  100 ? 0.5878 0.5808 0.5495 -0.0579 0.0198  -0.0307 100 VAL F CB  
10913 C CG1 . VAL F  100 ? 0.6375 0.6257 0.6018 -0.0602 0.0250  -0.0310 100 VAL F CG1 
10914 C CG2 . VAL F  100 ? 0.5271 0.5237 0.4845 -0.0596 0.0221  -0.0369 100 VAL F CG2 
10915 N N   . LEU F  101 ? 0.5927 0.5842 0.5581 -0.0536 0.0090  -0.0176 101 LEU F N   
10916 C CA  . LEU F  101 ? 0.6094 0.5981 0.5781 -0.0528 0.0069  -0.0117 101 LEU F CA  
10917 C C   . LEU F  101 ? 0.6061 0.5987 0.5673 -0.0532 0.0014  -0.0116 101 LEU F C   
10918 O O   . LEU F  101 ? 0.6933 0.6845 0.6529 -0.0548 0.0021  -0.0109 101 LEU F O   
10919 C CB  . LEU F  101 ? 0.5514 0.5382 0.5274 -0.0498 0.0043  -0.0053 101 LEU F CB  
10920 C CG  . LEU F  101 ? 0.5736 0.5560 0.5587 -0.0489 0.0096  -0.0041 101 LEU F CG  
10921 C CD1 . LEU F  101 ? 0.6000 0.5808 0.5926 -0.0459 0.0063  0.0030  101 LEU F CD1 
10922 C CD2 . LEU F  101 ? 0.5333 0.5107 0.5220 -0.0509 0.0163  -0.0048 101 LEU F CD2 
10923 N N   . LEU F  102 ? 0.5766 0.5738 0.5334 -0.0519 -0.0037 -0.0121 102 LEU F N   
10924 C CA  . LEU F  102 ? 0.6300 0.6309 0.5796 -0.0523 -0.0088 -0.0123 102 LEU F CA  
10925 C C   . LEU F  102 ? 0.6440 0.6465 0.5874 -0.0552 -0.0064 -0.0174 102 LEU F C   
10926 O O   . LEU F  102 ? 0.6232 0.6253 0.5636 -0.0562 -0.0078 -0.0162 102 LEU F O   
10927 C CB  . LEU F  102 ? 0.5804 0.5860 0.5264 -0.0506 -0.0134 -0.0132 102 LEU F CB  
10928 C CG  . LEU F  102 ? 0.8031 0.8087 0.7512 -0.0483 -0.0190 -0.0076 102 LEU F CG  
10929 C CD1 . LEU F  102 ? 0.7385 0.7394 0.6955 -0.0471 -0.0178 -0.0019 102 LEU F CD1 
10930 C CD2 . LEU F  102 ? 1.1399 1.1492 1.0861 -0.0465 -0.0220 -0.0089 102 LEU F CD2 
10931 N N   . GLU F  103 ? 0.5431 0.5476 0.4846 -0.0565 -0.0028 -0.0230 103 GLU F N   
10932 C CA  . GLU F  103 ? 0.6062 0.6130 0.5417 -0.0593 -0.0006 -0.0283 103 GLU F CA  
10933 C C   . GLU F  103 ? 0.6236 0.6259 0.5614 -0.0615 0.0040  -0.0281 103 GLU F C   
10934 O O   . GLU F  103 ? 0.7516 0.7550 0.6848 -0.0634 0.0040  -0.0300 103 GLU F O   
10935 C CB  . GLU F  103 ? 0.5501 0.5605 0.4831 -0.0604 0.0020  -0.0342 103 GLU F CB  
10936 C CG  . GLU F  103 ? 0.7884 0.8047 0.7170 -0.0588 -0.0027 -0.0354 103 GLU F CG  
10937 C CD  . GLU F  103 ? 0.9577 0.9772 0.8805 -0.0587 -0.0075 -0.0347 103 GLU F CD  
10938 O OE1 . GLU F  103 ? 0.9417 0.9642 0.8595 -0.0608 -0.0067 -0.0386 103 GLU F OE1 
10939 O OE2 . GLU F  103 ? 1.0200 1.0390 0.9435 -0.0565 -0.0121 -0.0304 103 GLU F OE2 
10940 N N   . ASN F  104 ? 0.5068 0.5039 0.4520 -0.0612 0.0082  -0.0259 104 ASN F N   
10941 C CA  . ASN F  104 ? 0.6075 0.5996 0.5558 -0.0630 0.0129  -0.0252 104 ASN F CA  
10942 C C   . ASN F  104 ? 0.7052 0.6960 0.6527 -0.0625 0.0095  -0.0203 104 ASN F C   
10943 O O   . ASN F  104 ? 0.7434 0.7330 0.6887 -0.0647 0.0115  -0.0215 104 ASN F O   
10944 C CB  . ASN F  104 ? 0.4861 0.4726 0.4434 -0.0623 0.0179  -0.0229 104 ASN F CB  
10945 C CG  . ASN F  104 ? 0.5848 0.5714 0.5424 -0.0640 0.0234  -0.0287 104 ASN F CG  
10946 O OD1 . ASN F  104 ? 0.5194 0.5102 0.4705 -0.0660 0.0237  -0.0345 104 ASN F OD1 
10947 N ND2 . ASN F  104 ? 0.6827 0.6646 0.6477 -0.0632 0.0277  -0.0271 104 ASN F ND2 
10948 N N   . GLU F  105 ? 0.6343 0.6254 0.5836 -0.0600 0.0042  -0.0149 105 GLU F N   
10949 C CA  . GLU F  105 ? 0.6002 0.5906 0.5481 -0.0596 0.0003  -0.0100 105 GLU F CA  
10950 C C   . GLU F  105 ? 0.6416 0.6359 0.5804 -0.0613 -0.0022 -0.0136 105 GLU F C   
10951 O O   . GLU F  105 ? 0.8822 0.8751 0.8189 -0.0626 -0.0023 -0.0122 105 GLU F O   
10952 C CB  . GLU F  105 ? 0.6643 0.6556 0.6147 -0.0568 -0.0054 -0.0044 105 GLU F CB  
10953 C CG  . GLU F  105 ? 0.8030 0.7938 0.7515 -0.0566 -0.0099 0.0008  105 GLU F CG  
10954 C CD  . GLU F  105 ? 1.3667 1.3526 1.3195 -0.0575 -0.0064 0.0042  105 GLU F CD  
10955 O OE1 . GLU F  105 ? 1.2913 1.2733 1.2518 -0.0571 -0.0017 0.0055  105 GLU F OE1 
10956 O OE2 . GLU F  105 ? 1.4511 1.4369 1.3997 -0.0588 -0.0081 0.0055  105 GLU F OE2 
10957 N N   . ARG F  106 ? 0.6500 0.6494 0.5839 -0.0613 -0.0040 -0.0181 106 ARG F N   
10958 C CA  . ARG F  106 ? 0.6342 0.6380 0.5598 -0.0627 -0.0063 -0.0217 106 ARG F CA  
10959 C C   . ARG F  106 ? 0.6981 0.7015 0.6214 -0.0658 -0.0014 -0.0264 106 ARG F C   
10960 O O   . ARG F  106 ? 0.7684 0.7726 0.6870 -0.0673 -0.0023 -0.0272 106 ARG F O   
10961 C CB  . ARG F  106 ? 0.6443 0.6536 0.5662 -0.0618 -0.0089 -0.0252 106 ARG F CB  
10962 C CG  . ARG F  106 ? 0.7696 0.7792 0.6946 -0.0588 -0.0128 -0.0215 106 ARG F CG  
10963 C CD  . ARG F  106 ? 0.9636 0.9770 0.8831 -0.0578 -0.0187 -0.0206 106 ARG F CD  
10964 N NE  . ARG F  106 ? 0.9787 0.9945 0.8914 -0.0598 -0.0191 -0.0237 106 ARG F NE  
10965 C CZ  . ARG F  106 ? 1.0904 1.1065 0.9990 -0.0600 -0.0228 -0.0216 106 ARG F CZ  
10966 N NH1 . ARG F  106 ? 1.1441 1.1585 1.0543 -0.0585 -0.0267 -0.0163 106 ARG F NH1 
10967 N NH2 . ARG F  106 ? 1.0748 1.0931 0.9776 -0.0619 -0.0225 -0.0248 106 ARG F NH2 
10968 N N   . THR F  107 ? 0.6836 0.6857 0.6102 -0.0668 0.0039  -0.0297 107 THR F N   
10969 C CA  . THR F  107 ? 0.7465 0.7483 0.6712 -0.0700 0.0090  -0.0347 107 THR F CA  
10970 C C   . THR F  107 ? 0.8144 0.8113 0.7410 -0.0713 0.0115  -0.0320 107 THR F C   
10971 O O   . THR F  107 ? 0.7700 0.7677 0.6924 -0.0737 0.0130  -0.0349 107 THR F O   
10972 C CB  . THR F  107 ? 0.7486 0.7494 0.6769 -0.0711 0.0146  -0.0385 107 THR F CB  
10973 O OG1 . THR F  107 ? 0.6696 0.6754 0.5955 -0.0701 0.0123  -0.0412 107 THR F OG1 
10974 C CG2 . THR F  107 ? 0.7037 0.7042 0.6299 -0.0747 0.0200  -0.0438 107 THR F CG2 
10975 N N   . LEU F  108 ? 0.6663 0.6581 0.5995 -0.0696 0.0121  -0.0263 108 LEU F N   
10976 C CA  . LEU F  108 ? 0.6439 0.6308 0.5796 -0.0705 0.0142  -0.0227 108 LEU F CA  
10977 C C   . LEU F  108 ? 0.7160 0.7046 0.6461 -0.0704 0.0092  -0.0202 108 LEU F C   
10978 O O   . LEU F  108 ? 0.7520 0.7391 0.6799 -0.0724 0.0110  -0.0207 108 LEU F O   
10979 C CB  . LEU F  108 ? 0.6435 0.6251 0.5881 -0.0684 0.0156  -0.0166 108 LEU F CB  
10980 C CG  . LEU F  108 ? 0.6391 0.6178 0.5900 -0.0686 0.0216  -0.0187 108 LEU F CG  
10981 C CD1 . LEU F  108 ? 0.5855 0.5586 0.5458 -0.0665 0.0232  -0.0120 108 LEU F CD1 
10982 C CD2 . LEU F  108 ? 0.6877 0.6649 0.6371 -0.0720 0.0281  -0.0246 108 LEU F CD2 
10983 N N   . ASP F  109 ? 0.6614 0.6531 0.5892 -0.0684 0.0030  -0.0177 109 ASP F N   
10984 C CA  . ASP F  109 ? 0.6945 0.6880 0.6164 -0.0685 -0.0020 -0.0157 109 ASP F CA  
10985 C C   . ASP F  109 ? 0.7448 0.7424 0.6591 -0.0707 -0.0016 -0.0217 109 ASP F C   
10986 O O   . ASP F  109 ? 0.7929 0.7905 0.7026 -0.0719 -0.0030 -0.0212 109 ASP F O   
10987 C CB  . ASP F  109 ? 0.7895 0.7856 0.7105 -0.0660 -0.0083 -0.0123 109 ASP F CB  
10988 C CG  . ASP F  109 ? 1.0315 1.0239 0.9593 -0.0640 -0.0097 -0.0052 109 ASP F CG  
10989 O OD1 . ASP F  109 ? 0.9807 0.9686 0.9134 -0.0645 -0.0063 -0.0021 109 ASP F OD1 
10990 O OD2 . ASP F  109 ? 1.0738 1.0680 1.0024 -0.0620 -0.0142 -0.0025 109 ASP F OD2 
10991 N N   . TYR F  110 ? 0.6762 0.6773 0.5893 -0.0713 0.0002  -0.0273 110 TYR F N   
10992 C CA  . TYR F  110 ? 0.6465 0.6520 0.5533 -0.0735 0.0009  -0.0332 110 TYR F CA  
10993 C C   . TYR F  110 ? 0.7665 0.7693 0.6730 -0.0763 0.0058  -0.0353 110 TYR F C   
10994 O O   . TYR F  110 ? 0.6339 0.6382 0.5352 -0.0779 0.0051  -0.0368 110 TYR F O   
10995 C CB  . TYR F  110 ? 0.5773 0.5872 0.4836 -0.0735 0.0020  -0.0383 110 TYR F CB  
10996 C CG  . TYR F  110 ? 0.5506 0.5653 0.4514 -0.0760 0.0034  -0.0446 110 TYR F CG  
10997 C CD1 . TYR F  110 ? 0.5221 0.5420 0.4170 -0.0757 -0.0007 -0.0461 110 TYR F CD1 
10998 C CD2 . TYR F  110 ? 0.6277 0.6416 0.5294 -0.0788 0.0091  -0.0489 110 TYR F CD2 
10999 C CE1 . TYR F  110 ? 0.6199 0.6446 0.5104 -0.0779 0.0006  -0.0515 110 TYR F CE1 
11000 C CE2 . TYR F  110 ? 0.7294 0.7482 0.6264 -0.0813 0.0103  -0.0545 110 TYR F CE2 
11001 C CZ  . TYR F  110 ? 0.7385 0.7628 0.6301 -0.0807 0.0059  -0.0556 110 TYR F CZ  
11002 O OH  . TYR F  110 ? 0.8344 0.8639 0.7218 -0.0830 0.0071  -0.0609 110 TYR F OH  
11003 N N   . HIS F  111 ? 0.6460 0.6445 0.5582 -0.0771 0.0111  -0.0354 111 HIS F N   
11004 C CA  . HIS F  111 ? 0.6972 0.6923 0.6100 -0.0798 0.0165  -0.0372 111 HIS F CA  
11005 C C   . HIS F  111 ? 0.8108 0.8022 0.7235 -0.0796 0.0151  -0.0319 111 HIS F C   
11006 O O   . HIS F  111 ? 0.7172 0.7085 0.6261 -0.0818 0.0164  -0.0336 111 HIS F O   
11007 C CB  . HIS F  111 ? 0.6384 0.6292 0.5580 -0.0805 0.0227  -0.0380 111 HIS F CB  
11008 C CG  . HIS F  111 ? 0.7591 0.7534 0.6780 -0.0818 0.0253  -0.0442 111 HIS F CG  
11009 N ND1 . HIS F  111 ? 0.8265 0.8245 0.7407 -0.0849 0.0276  -0.0506 111 HIS F ND1 
11010 C CD2 . HIS F  111 ? 0.8556 0.8504 0.7778 -0.0806 0.0260  -0.0450 111 HIS F CD2 
11011 C CE1 . HIS F  111 ? 0.8896 0.8905 0.8041 -0.0856 0.0295  -0.0550 111 HIS F CE1 
11012 N NE2 . HIS F  111 ? 0.8559 0.8548 0.7750 -0.0831 0.0286  -0.0517 111 HIS F NE2 
11013 N N   . ASP F  112 ? 0.7236 0.7119 0.6404 -0.0772 0.0125  -0.0254 112 ASP F N   
11014 C CA  . ASP F  112 ? 0.6210 0.6062 0.5377 -0.0768 0.0105  -0.0196 112 ASP F CA  
11015 C C   . ASP F  112 ? 0.6825 0.6713 0.5908 -0.0777 0.0064  -0.0209 112 ASP F C   
11016 O O   . ASP F  112 ? 0.7721 0.7589 0.6780 -0.0792 0.0070  -0.0196 112 ASP F O   
11017 C CB  . ASP F  112 ? 0.8331 0.8165 0.7546 -0.0738 0.0067  -0.0126 112 ASP F CB  
11018 C CG  . ASP F  112 ? 0.9410 0.9208 0.8635 -0.0736 0.0052  -0.0060 112 ASP F CG  
11019 O OD1 . ASP F  112 ? 0.9909 0.9705 0.9152 -0.0715 0.0006  -0.0002 112 ASP F OD1 
11020 O OD2 . ASP F  112 ? 0.9598 0.9370 0.8811 -0.0755 0.0086  -0.0065 112 ASP F OD2 
11021 N N   . SER F  113 ? 0.7720 0.7661 0.6761 -0.0769 0.0023  -0.0234 113 SER F N   
11022 C CA  . SER F  113 ? 0.6940 0.6919 0.5905 -0.0776 -0.0015 -0.0249 113 SER F CA  
11023 C C   . SER F  113 ? 0.7964 0.7955 0.6888 -0.0805 0.0020  -0.0302 113 SER F C   
11024 O O   . SER F  113 ? 0.8480 0.8465 0.7359 -0.0817 0.0011  -0.0295 113 SER F O   
11025 C CB  . SER F  113 ? 0.6369 0.6401 0.5306 -0.0760 -0.0057 -0.0270 113 SER F CB  
11026 O OG  . SER F  113 ? 0.8846 0.8917 0.7711 -0.0769 -0.0083 -0.0297 113 SER F OG  
11027 N N   . ASN F  114 ? 0.7444 0.7453 0.6381 -0.0818 0.0061  -0.0357 114 ASN F N   
11028 C CA  . ASN F  114 ? 0.8878 0.8906 0.7780 -0.0848 0.0095  -0.0411 114 ASN F CA  
11029 C C   . ASN F  114 ? 0.8839 0.8814 0.7750 -0.0867 0.0132  -0.0395 114 ASN F C   
11030 O O   . ASN F  114 ? 0.7778 0.7765 0.6644 -0.0887 0.0140  -0.0418 114 ASN F O   
11031 C CB  . ASN F  114 ? 0.7881 0.7934 0.6801 -0.0860 0.0135  -0.0469 114 ASN F CB  
11032 C CG  . ASN F  114 ? 0.8629 0.8742 0.7530 -0.0845 0.0099  -0.0491 114 ASN F CG  
11033 O OD1 . ASN F  114 ? 1.0178 1.0322 0.9040 -0.0831 0.0049  -0.0479 114 ASN F OD1 
11034 N ND2 . ASN F  114 ? 0.8655 0.8785 0.7583 -0.0849 0.0126  -0.0525 114 ASN F ND2 
11035 N N   . VAL F  115 ? 0.8085 0.8004 0.7058 -0.0859 0.0157  -0.0352 115 VAL F N   
11036 C CA  . VAL F  115 ? 0.8295 0.8160 0.7284 -0.0873 0.0192  -0.0326 115 VAL F CA  
11037 C C   . VAL F  115 ? 0.8108 0.7968 0.7050 -0.0869 0.0148  -0.0283 115 VAL F C   
11038 O O   . VAL F  115 ? 0.8256 0.8112 0.7160 -0.0889 0.0162  -0.0298 115 VAL F O   
11039 C CB  . VAL F  115 ? 0.7657 0.7462 0.6728 -0.0860 0.0222  -0.0279 115 VAL F CB  
11040 C CG1 . VAL F  115 ? 0.8877 0.8627 0.7965 -0.0870 0.0251  -0.0241 115 VAL F CG1 
11041 C CG2 . VAL F  115 ? 0.6876 0.6678 0.5992 -0.0869 0.0276  -0.0325 115 VAL F CG2 
11042 N N   . LYS F  116 ? 0.8084 0.7946 0.7030 -0.0843 0.0095  -0.0232 116 LYS F N   
11043 C CA  . LYS F  116 ? 0.8748 0.8609 0.7645 -0.0840 0.0048  -0.0190 116 LYS F CA  
11044 C C   . LYS F  116 ? 0.8291 0.8193 0.7109 -0.0858 0.0034  -0.0237 116 LYS F C   
11045 O O   . LYS F  116 ? 0.9618 0.9506 0.8394 -0.0871 0.0030  -0.0224 116 LYS F O   
11046 C CB  . LYS F  116 ? 0.8449 0.8323 0.7354 -0.0813 -0.0010 -0.0145 116 LYS F CB  
11047 C CG  . LYS F  116 ? 0.7980 0.7867 0.6822 -0.0812 -0.0065 -0.0115 116 LYS F CG  
11048 C CD  . LYS F  116 ? 1.0154 0.9996 0.9016 -0.0808 -0.0078 -0.0040 116 LYS F CD  
11049 C CE  . LYS F  116 ? 1.1366 1.1224 1.0166 -0.0807 -0.0139 -0.0008 116 LYS F CE  
11050 N NZ  . LYS F  116 ? 1.3351 1.3173 1.2174 -0.0801 -0.0160 0.0071  116 LYS F NZ  
11051 N N   . ASN F  117 ? 0.6579 0.6533 0.5377 -0.0857 0.0028  -0.0291 117 ASN F N   
11052 C CA  . ASN F  117 ? 0.8273 0.8271 0.7003 -0.0872 0.0017  -0.0337 117 ASN F CA  
11053 C C   . ASN F  117 ? 0.9382 0.9372 0.8100 -0.0902 0.0067  -0.0376 117 ASN F C   
11054 O O   . ASN F  117 ? 0.9934 0.9934 0.8598 -0.0916 0.0060  -0.0388 117 ASN F O   
11055 C CB  . ASN F  117 ? 0.8108 0.8166 0.6830 -0.0863 0.0001  -0.0382 117 ASN F CB  
11056 C CG  . ASN F  117 ? 0.8680 0.8756 0.7393 -0.0836 -0.0056 -0.0351 117 ASN F CG  
11057 O OD1 . ASN F  117 ? 0.8874 0.8925 0.7574 -0.0828 -0.0088 -0.0300 117 ASN F OD1 
11058 N ND2 . ASN F  117 ? 1.0551 1.0672 0.9268 -0.0824 -0.0068 -0.0380 117 ASN F ND2 
11059 N N   . LEU F  118 ? 0.8775 0.8745 0.7542 -0.0912 0.0119  -0.0396 118 LEU F N   
11060 C CA  . LEU F  118 ? 0.8800 0.8758 0.7561 -0.0943 0.0171  -0.0434 118 LEU F CA  
11061 C C   . LEU F  118 ? 0.9397 0.9302 0.8148 -0.0949 0.0178  -0.0389 118 LEU F C   
11062 O O   . LEU F  118 ? 1.1241 1.1149 0.9951 -0.0971 0.0191  -0.0410 118 LEU F O   
11063 C CB  . LEU F  118 ? 0.9239 0.9178 0.8060 -0.0953 0.0228  -0.0460 118 LEU F CB  
11064 C CG  . LEU F  118 ? 1.0246 1.0207 0.9052 -0.0986 0.0276  -0.0529 118 LEU F CG  
11065 C CD1 . LEU F  118 ? 0.9088 0.9126 0.7842 -0.0990 0.0246  -0.0576 118 LEU F CD1 
11066 C CD2 . LEU F  118 ? 1.0745 1.0689 0.9608 -0.0997 0.0330  -0.0556 118 LEU F CD2 
11067 N N   . TYR F  119 ? 0.9143 0.9002 0.7933 -0.0931 0.0167  -0.0324 119 TYR F N   
11068 C CA  . TYR F  119 ? 0.9147 0.8958 0.7931 -0.0935 0.0168  -0.0271 119 TYR F CA  
11069 C C   . TYR F  119 ? 0.9371 0.9203 0.8079 -0.0938 0.0121  -0.0261 119 TYR F C   
11070 O O   . TYR F  119 ? 1.0399 1.0214 0.9070 -0.0957 0.0137  -0.0263 119 TYR F O   
11071 C CB  . TYR F  119 ? 0.9862 0.9632 0.8704 -0.0911 0.0155  -0.0199 119 TYR F CB  
11072 C CG  . TYR F  119 ? 1.0795 1.0520 0.9632 -0.0912 0.0149  -0.0135 119 TYR F CG  
11073 C CD1 . TYR F  119 ? 1.0786 1.0457 0.9667 -0.0922 0.0203  -0.0116 119 TYR F CD1 
11074 C CD2 . TYR F  119 ? 1.0515 1.0250 0.9302 -0.0904 0.0090  -0.0093 119 TYR F CD2 
11075 C CE1 . TYR F  119 ? 1.1904 1.1536 1.0782 -0.0923 0.0197  -0.0053 119 TYR F CE1 
11076 C CE2 . TYR F  119 ? 1.3127 1.2824 1.1905 -0.0907 0.0083  -0.0033 119 TYR F CE2 
11077 C CZ  . TYR F  119 ? 1.3498 1.3144 1.2322 -0.0916 0.0135  -0.0012 119 TYR F CZ  
11078 O OH  . TYR F  119 ? 1.4508 1.4118 1.3324 -0.0918 0.0128  0.0052  119 TYR F OH  
11079 N N   . GLU F  120 ? 0.9727 0.9594 0.8410 -0.0919 0.0066  -0.0251 120 GLU F N   
11080 C CA  . GLU F  120 ? 1.0322 1.0209 0.8931 -0.0922 0.0022  -0.0244 120 GLU F CA  
11081 C C   . GLU F  120 ? 1.0111 1.0029 0.8668 -0.0946 0.0041  -0.0306 120 GLU F C   
11082 O O   . GLU F  120 ? 1.1873 1.1781 1.0378 -0.0960 0.0036  -0.0299 120 GLU F O   
11083 C CB  . GLU F  120 ? 1.2219 1.2141 1.0815 -0.0900 -0.0034 -0.0233 120 GLU F CB  
11084 C CG  . GLU F  120 ? 1.4018 1.3913 1.2636 -0.0881 -0.0072 -0.0160 120 GLU F CG  
11085 C CD  . GLU F  120 ? 1.6774 1.6644 1.5340 -0.0892 -0.0096 -0.0117 120 GLU F CD  
11086 O OE1 . GLU F  120 ? 1.6090 1.5975 1.4590 -0.0909 -0.0098 -0.0148 120 GLU F OE1 
11087 O OE2 . GLU F  120 ? 1.6516 1.6353 1.5107 -0.0884 -0.0112 -0.0052 120 GLU F OE2 
11088 N N   . LYS F  121 ? 1.0293 1.0251 0.8865 -0.0950 0.0064  -0.0365 121 LYS F N   
11089 C CA  . LYS F  121 ? 1.1842 1.1840 1.0371 -0.0971 0.0080  -0.0424 121 LYS F CA  
11090 C C   . LYS F  121 ? 1.3047 1.3009 1.1563 -0.0997 0.0122  -0.0430 121 LYS F C   
11091 O O   . LYS F  121 ? 1.3909 1.3885 1.2371 -0.1012 0.0119  -0.0448 121 LYS F O   
11092 C CB  . LYS F  121 ? 1.1216 1.1260 0.9772 -0.0974 0.0102  -0.0482 121 LYS F CB  
11093 C CG  . LYS F  121 ? 1.3231 1.3338 1.1742 -0.0986 0.0096  -0.0537 121 LYS F CG  
11094 C CD  . LYS F  121 ? 1.4565 1.4719 1.3104 -0.0993 0.0122  -0.0594 121 LYS F CD  
11095 C CE  . LYS F  121 ? 1.4794 1.5008 1.3294 -0.1011 0.0128  -0.0648 121 LYS F CE  
11096 N NZ  . LYS F  121 ? 1.4807 1.5079 1.3329 -0.1018 0.0144  -0.0701 121 LYS F NZ  
11097 N N   . VAL F  122 ? 1.2302 1.2218 1.0869 -0.1003 0.0164  -0.0413 122 VAL F N   
11098 C CA  . VAL F  122 ? 1.1602 1.1479 1.0166 -0.1028 0.0211  -0.0418 122 VAL F CA  
11099 C C   . VAL F  122 ? 1.2554 1.2390 1.1082 -0.1028 0.0191  -0.0361 122 VAL F C   
11100 O O   . VAL F  122 ? 1.5178 1.5001 1.3670 -0.1049 0.0212  -0.0372 122 VAL F O   
11101 C CB  . VAL F  122 ? 1.0653 1.0489 0.9287 -0.1034 0.0267  -0.0417 122 VAL F CB  
11102 C CG1 . VAL F  122 ? 1.0775 1.0647 0.9448 -0.1028 0.0277  -0.0458 122 VAL F CG1 
11103 C CG2 . VAL F  122 ? 1.1485 1.1261 1.0159 -0.1017 0.0262  -0.0341 122 VAL F CG2 
11104 N N   . ARG F  123 ? 1.1436 1.1253 0.9974 -0.1005 0.0150  -0.0299 123 ARG F N   
11105 C CA  . ARG F  123 ? 1.2807 1.2589 1.1308 -0.1006 0.0124  -0.0241 123 ARG F CA  
11106 C C   . ARG F  123 ? 1.2687 1.2501 1.1105 -0.1015 0.0090  -0.0260 123 ARG F C   
11107 O O   . ARG F  123 ? 1.5088 1.4882 1.3462 -0.1033 0.0100  -0.0254 123 ARG F O   
11108 C CB  . ARG F  123 ? 1.2515 1.2280 1.1046 -0.0980 0.0084  -0.0174 123 ARG F CB  
11109 C CG  . ARG F  123 ? 1.3024 1.2815 1.1495 -0.0971 0.0019  -0.0153 123 ARG F CG  
11110 C CD  . ARG F  123 ? 1.3786 1.3558 1.2287 -0.0950 -0.0020 -0.0081 123 ARG F CD  
11111 N NE  . ARG F  123 ? 1.5483 1.5203 1.4006 -0.0955 -0.0003 -0.0022 123 ARG F NE  
11112 C CZ  . ARG F  123 ? 1.6367 1.6063 1.4940 -0.0937 -0.0020 0.0046  123 ARG F CZ  
11113 N NH1 . ARG F  123 ? 1.5476 1.5194 1.4081 -0.0915 -0.0054 0.0059  123 ARG F NH1 
11114 N NH2 . ARG F  123 ? 1.7362 1.7012 1.5955 -0.0942 -0.0002 0.0100  123 ARG F NH2 
11115 N N   . SER F  124 ? 1.2925 1.2788 1.1325 -0.1001 0.0051  -0.0281 124 SER F N   
11116 C CA  . SER F  124 ? 1.5185 1.5075 1.3510 -0.1007 0.0016  -0.0295 124 SER F CA  
11117 C C   . SER F  124 ? 1.6170 1.6067 1.4462 -0.1033 0.0054  -0.0342 124 SER F C   
11118 O O   . SER F  124 ? 1.7440 1.7339 1.5669 -0.1045 0.0041  -0.0346 124 SER F O   
11119 C CB  . SER F  124 ? 1.6108 1.6054 1.4431 -0.0990 -0.0016 -0.0326 124 SER F CB  
11120 O OG  . SER F  124 ? 1.5645 1.5636 1.3958 -0.1001 0.0008  -0.0393 124 SER F OG  
11121 N N   . GLN F  125 ? 1.3908 1.3806 1.2245 -0.1043 0.0103  -0.0378 125 GLN F N   
11122 C CA  . GLN F  125 ? 1.3740 1.3660 1.2056 -0.1067 0.0140  -0.0436 125 GLN F CA  
11123 C C   . GLN F  125 ? 1.4910 1.4778 1.3236 -0.1089 0.0189  -0.0426 125 GLN F C   
11124 O O   . GLN F  125 ? 1.4984 1.4860 1.3287 -0.1112 0.0221  -0.0465 125 GLN F O   
11125 C CB  . GLN F  125 ? 1.2373 1.2347 1.0724 -0.1065 0.0154  -0.0494 125 GLN F CB  
11126 C CG  . GLN F  125 ? 1.3351 1.3361 1.1691 -0.1089 0.0190  -0.0558 125 GLN F CG  
11127 C CD  . GLN F  125 ? 1.5382 1.5371 1.3772 -0.1107 0.0248  -0.0580 125 GLN F CD  
11128 O OE1 . GLN F  125 ? 1.4323 1.4342 1.2752 -0.1107 0.0264  -0.0615 125 GLN F OE1 
11129 N NE2 . GLN F  125 ? 1.7268 1.7201 1.5655 -0.1124 0.0282  -0.0560 125 GLN F NE2 
11130 N N   . LEU F  126 ? 1.5307 1.5122 1.3669 -0.1080 0.0196  -0.0369 126 LEU F N   
11131 C CA  . LEU F  126 ? 1.3056 1.2814 1.1407 -0.1095 0.0221  -0.0333 126 LEU F CA  
11132 C C   . LEU F  126 ? 1.5560 1.5290 1.3883 -0.1081 0.0174  -0.0260 126 LEU F C   
11133 O O   . LEU F  126 ? 1.6890 1.6604 1.5256 -0.1061 0.0155  -0.0213 126 LEU F O   
11134 C CB  . LEU F  126 ? 1.3703 1.3417 1.2124 -0.1099 0.0275  -0.0322 126 LEU F CB  
11135 C CG  . LEU F  126 ? 1.3252 1.2985 1.1735 -0.1101 0.0314  -0.0372 126 LEU F CG  
11136 C CD1 . LEU F  126 ? 1.4025 1.3702 1.2579 -0.1094 0.0350  -0.0333 126 LEU F CD1 
11137 C CD2 . LEU F  126 ? 1.3301 1.3064 1.1773 -0.1129 0.0357  -0.0447 126 LEU F CD2 
11138 N N   . LYS F  127 ? 1.4989 1.4714 1.3241 -0.1094 0.0155  -0.0249 127 LYS F N   
11139 C CA  . LYS F  127 ? 1.4902 1.4606 1.3118 -0.1085 0.0107  -0.0183 127 LYS F CA  
11140 C C   . LYS F  127 ? 1.7933 1.7578 1.6144 -0.1096 0.0126  -0.0127 127 LYS F C   
11141 O O   . LYS F  127 ? 1.6470 1.6084 1.4733 -0.1083 0.0127  -0.0070 127 LYS F O   
11142 C CB  . LYS F  127 ? 1.4601 1.4337 1.2737 -0.1091 0.0067  -0.0201 127 LYS F CB  
11143 C CG  . LYS F  127 ? 1.4804 1.4599 1.2947 -0.1080 0.0051  -0.0256 127 LYS F CG  
11144 C CD  . LYS F  127 ? 1.4028 1.3854 1.2113 -0.1098 0.0060  -0.0312 127 LYS F CD  
11145 C CE  . LYS F  127 ? 1.5285 1.5172 1.3383 -0.1085 0.0046  -0.0363 127 LYS F CE  
11146 N NZ  . LYS F  127 ? 1.5810 1.5734 1.3861 -0.1099 0.0054  -0.0417 127 LYS F NZ  
11147 N N   . ASN F  128 ? 2.5081 2.4714 2.3234 -0.1120 0.0144  -0.0141 128 ASN F N   
11148 C CA  . ASN F  128 ? 2.4844 2.4422 2.2990 -0.1133 0.0168  -0.0093 128 ASN F CA  
11149 C C   . ASN F  128 ? 2.5168 2.4719 2.3371 -0.1143 0.0238  -0.0117 128 ASN F C   
11150 O O   . ASN F  128 ? 2.3534 2.3036 2.1765 -0.1145 0.0263  -0.0069 128 ASN F O   
11151 C CB  . ASN F  128 ? 2.3599 2.3173 2.1652 -0.1155 0.0156  -0.0095 128 ASN F CB  
11152 C CG  . ASN F  128 ? 2.4511 2.4097 2.2506 -0.1149 0.0091  -0.0055 128 ASN F CG  
11153 O OD1 . ASN F  128 ? 2.4026 2.3598 2.2043 -0.1134 0.0058  0.0008  128 ASN F OD1 
11154 N ND2 . ASN F  128 ? 2.5398 2.5009 2.3320 -0.1162 0.0072  -0.0092 128 ASN F ND2 
11155 N N   . ASN F  129 ? 2.4446 2.4030 2.2666 -0.1151 0.0268  -0.0191 129 ASN F N   
11156 C CA  . ASN F  129 ? 2.4278 2.3842 2.2542 -0.1167 0.0336  -0.0227 129 ASN F CA  
11157 C C   . ASN F  129 ? 2.3767 2.3297 2.2119 -0.1154 0.0367  -0.0198 129 ASN F C   
11158 O O   . ASN F  129 ? 2.2743 2.2254 2.1138 -0.1168 0.0427  -0.0230 129 ASN F O   
11159 C CB  . ASN F  129 ? 2.3123 2.2739 2.1383 -0.1180 0.0355  -0.0313 129 ASN F CB  
11160 C CG  . ASN F  129 ? 2.2621 2.2266 2.0801 -0.1195 0.0337  -0.0345 129 ASN F CG  
11161 O OD1 . ASN F  129 ? 2.2274 2.1963 2.0446 -0.1207 0.0352  -0.0410 129 ASN F OD1 
11162 N ND2 . ASN F  129 ? 2.3343 2.2966 2.1465 -0.1196 0.0305  -0.0297 129 ASN F ND2 
11163 N N   . ALA F  130 ? 2.0381 1.9901 1.8760 -0.1129 0.0329  -0.0139 130 ALA F N   
11164 C CA  . ALA F  130 ? 1.9076 1.8566 1.7543 -0.1113 0.0355  -0.0108 130 ALA F CA  
11165 C C   . ALA F  130 ? 1.7561 1.7045 1.6043 -0.1086 0.0301  -0.0033 130 ALA F C   
11166 O O   . ALA F  130 ? 1.7201 1.6712 1.5625 -0.1081 0.0243  -0.0017 130 ALA F O   
11167 C CB  . ALA F  130 ? 1.8870 1.8392 1.7385 -0.1111 0.0379  -0.0173 130 ALA F CB  
11168 N N   . LYS F  131 ? 2.1566 2.1015 2.0127 -0.1070 0.0321  0.0014  131 LYS F N   
11169 C CA  . LYS F  131 ? 2.2896 2.2340 2.1481 -0.1045 0.0272  0.0090  131 LYS F CA  
11170 C C   . LYS F  131 ? 2.3922 2.3369 2.2593 -0.1022 0.0280  0.0091  131 LYS F C   
11171 O O   . LYS F  131 ? 2.3243 2.2673 2.1972 -0.1026 0.0338  0.0056  131 LYS F O   
11172 C CB  . LYS F  131 ? 2.2515 2.1908 2.1112 -0.1044 0.0280  0.0171  131 LYS F CB  
11173 C CG  . LYS F  131 ? 2.3635 2.2976 2.2320 -0.1042 0.0350  0.0187  131 LYS F CG  
11174 C CD  . LYS F  131 ? 2.3561 2.2858 2.2275 -0.1032 0.0346  0.0283  131 LYS F CD  
11175 C CE  . LYS F  131 ? 2.2605 2.1850 2.1419 -0.1026 0.0415  0.0303  131 LYS F CE  
11176 N NZ  . LYS F  131 ? 2.1769 2.0975 2.0622 -0.1011 0.0409  0.0405  131 LYS F NZ  
11177 N N   . GLU F  132 ? 2.1050 2.0519 1.9730 -0.0999 0.0223  0.0132  132 GLU F N   
11178 C CA  . GLU F  132 ? 1.9350 1.8821 1.8112 -0.0975 0.0227  0.0142  132 GLU F CA  
11179 C C   . GLU F  132 ? 1.9604 1.9021 1.8448 -0.0963 0.0258  0.0213  132 GLU F C   
11180 O O   . GLU F  132 ? 2.0560 1.9953 1.9391 -0.0962 0.0240  0.0283  132 GLU F O   
11181 C CB  . GLU F  132 ? 2.0412 1.9925 1.9154 -0.0956 0.0155  0.0163  132 GLU F CB  
11182 C CG  . GLU F  132 ? 2.0545 2.0061 1.9372 -0.0930 0.0154  0.0178  132 GLU F CG  
11183 C CD  . GLU F  132 ? 2.1123 2.0679 1.9930 -0.0912 0.0082  0.0201  132 GLU F CD  
11184 O OE1 . GLU F  132 ? 1.9850 1.9428 1.8580 -0.0919 0.0033  0.0211  132 GLU F OE1 
11185 O OE2 . GLU F  132 ? 2.1172 2.0736 2.0041 -0.0891 0.0077  0.0208  132 GLU F OE2 
11186 N N   . ILE F  133 ? 1.8069 1.7466 1.6996 -0.0955 0.0307  0.0197  133 ILE F N   
11187 C CA  . ILE F  133 ? 1.8844 1.8190 1.7862 -0.0940 0.0342  0.0263  133 ILE F CA  
11188 C C   . ILE F  133 ? 1.8701 1.8061 1.7770 -0.0909 0.0296  0.0319  133 ILE F C   
11189 O O   . ILE F  133 ? 1.8958 1.8291 1.8077 -0.0893 0.0288  0.0402  133 ILE F O   
11190 C CB  . ILE F  133 ? 1.8960 1.8271 1.8047 -0.0948 0.0426  0.0217  133 ILE F CB  
11191 C CG1 . ILE F  133 ? 1.9126 1.8422 1.8169 -0.0980 0.0475  0.0164  133 ILE F CG1 
11192 C CG2 . ILE F  133 ? 1.7616 1.6873 1.6804 -0.0930 0.0463  0.0288  133 ILE F CG2 
11193 C CD1 . ILE F  133 ? 1.9933 1.9184 1.8968 -0.0987 0.0490  0.0223  133 ILE F CD1 
11194 N N   . GLY F  134 ? 1.8944 1.8348 1.8001 -0.0901 0.0265  0.0276  134 GLY F N   
11195 C CA  . GLY F  134 ? 1.8664 1.8086 1.7769 -0.0873 0.0222  0.0319  134 GLY F CA  
11196 C C   . GLY F  134 ? 1.6265 1.5681 1.5446 -0.0862 0.0263  0.0283  134 GLY F C   
11197 O O   . GLY F  134 ? 1.4221 1.3661 1.3432 -0.0841 0.0230  0.0294  134 GLY F O   
11198 N N   . ASN F  135 ? 1.5246 1.4630 1.4458 -0.0878 0.0337  0.0238  135 ASN F N   
11199 C CA  . ASN F  135 ? 1.3301 1.2675 1.2583 -0.0873 0.0386  0.0198  135 ASN F CA  
11200 C C   . ASN F  135 ? 1.3270 1.2686 1.2499 -0.0891 0.0393  0.0101  135 ASN F C   
11201 O O   . ASN F  135 ? 1.1583 1.0988 1.0848 -0.0901 0.0449  0.0047  135 ASN F O   
11202 C CB  . ASN F  135 ? 1.4012 1.3321 1.3369 -0.0879 0.0468  0.0210  135 ASN F CB  
11203 C CG  . ASN F  135 ? 1.5556 1.4846 1.4999 -0.0871 0.0517  0.0188  135 ASN F CG  
11204 O OD1 . ASN F  135 ? 1.4762 1.4085 1.4214 -0.0856 0.0486  0.0174  135 ASN F OD1 
11205 N ND2 . ASN F  135 ? 1.7766 1.7000 1.7271 -0.0880 0.0596  0.0184  135 ASN F ND2 
11206 N N   . GLY F  136 ? 1.3167 1.2633 1.2309 -0.0897 0.0336  0.0079  136 GLY F N   
11207 C CA  . GLY F  136 ? 1.1898 1.1410 1.0985 -0.0914 0.0337  -0.0008 136 GLY F CA  
11208 C C   . GLY F  136 ? 1.3657 1.3163 1.2698 -0.0946 0.0377  -0.0057 136 GLY F C   
11209 O O   . GLY F  136 ? 1.3749 1.3297 1.2738 -0.0963 0.0376  -0.0127 136 GLY F O   
11210 N N   . CYS F  137 ? 1.6353 1.5807 1.5414 -0.0953 0.0413  -0.0019 137 CYS F N   
11211 C CA  . CYS F  137 ? 1.6864 1.6303 1.5894 -0.0985 0.0462  -0.0065 137 CYS F CA  
11212 C C   . CYS F  137 ? 1.6988 1.6428 1.5944 -0.0993 0.0429  -0.0036 137 CYS F C   
11213 O O   . CYS F  137 ? 1.7202 1.6629 1.6156 -0.0977 0.0389  0.0038  137 CYS F O   
11214 C CB  . CYS F  137 ? 1.4715 1.4089 1.3821 -0.0993 0.0542  -0.0055 137 CYS F CB  
11215 S SG  . CYS F  137 ? 1.9620 1.8994 1.8748 -0.1024 0.0623  -0.0156 137 CYS F SG  
11216 N N   . PHE F  138 ? 1.6030 1.5488 1.4928 -0.1021 0.0448  -0.0096 138 PHE F N   
11217 C CA  . PHE F  138 ? 1.7021 1.6483 1.5843 -0.1034 0.0423  -0.0084 138 PHE F CA  
11218 C C   . PHE F  138 ? 1.9312 1.8732 1.8137 -0.1060 0.0488  -0.0101 138 PHE F C   
11219 O O   . PHE F  138 ? 2.0202 1.9619 1.9055 -0.1078 0.0544  -0.0161 138 PHE F O   
11220 C CB  . PHE F  138 ? 1.6279 1.5805 1.5025 -0.1043 0.0383  -0.0142 138 PHE F CB  
11221 C CG  . PHE F  138 ? 1.5093 1.4662 1.3832 -0.1019 0.0321  -0.0132 138 PHE F CG  
11222 C CD1 . PHE F  138 ? 1.3547 1.3173 1.2258 -0.1021 0.0304  -0.0196 138 PHE F CD1 
11223 C CD2 . PHE F  138 ? 1.4953 1.4505 1.3715 -0.0994 0.0280  -0.0057 138 PHE F CD2 
11224 C CE1 . PHE F  138 ? 1.3700 1.3364 1.2407 -0.0998 0.0249  -0.0185 138 PHE F CE1 
11225 C CE2 . PHE F  138 ? 1.4293 1.3884 1.3050 -0.0973 0.0225  -0.0048 138 PHE F CE2 
11226 C CZ  . PHE F  138 ? 1.4465 1.4109 1.3194 -0.0975 0.0210  -0.0113 138 PHE F CZ  
11227 N N   . GLU F  139 ? 2.0321 1.9710 1.9116 -0.1064 0.0481  -0.0050 139 GLU F N   
11228 C CA  . GLU F  139 ? 1.8914 1.8261 1.7711 -0.1088 0.0542  -0.0060 139 GLU F CA  
11229 C C   . GLU F  139 ? 1.8023 1.7395 1.6729 -0.1111 0.0528  -0.0097 139 GLU F C   
11230 O O   . GLU F  139 ? 1.7766 1.7152 1.6410 -0.1106 0.0473  -0.0062 139 GLU F O   
11231 C CB  . GLU F  139 ? 1.8727 1.8013 1.7564 -0.1076 0.0555  0.0029  139 GLU F CB  
11232 C CG  . GLU F  139 ? 2.1435 2.0671 2.0275 -0.1099 0.0619  0.0025  139 GLU F CG  
11233 C CD  . GLU F  139 ? 2.2653 2.1828 2.1555 -0.1085 0.0643  0.0112  139 GLU F CD  
11234 O OE1 . GLU F  139 ? 2.0805 1.9977 1.9750 -0.1056 0.0609  0.0174  139 GLU F OE1 
11235 O OE2 . GLU F  139 ? 2.3048 2.2177 2.1957 -0.1101 0.0696  0.0119  139 GLU F OE2 
11236 N N   . PHE F  140 ? 2.0169 1.9547 1.8867 -0.1139 0.0578  -0.0169 140 PHE F N   
11237 C CA  . PHE F  140 ? 2.1169 2.0573 1.9787 -0.1162 0.0572  -0.0211 140 PHE F CA  
11238 C C   . PHE F  140 ? 2.2232 2.1587 2.0822 -0.1174 0.0590  -0.0167 140 PHE F C   
11239 O O   . PHE F  140 ? 2.1800 2.1099 2.0441 -0.1178 0.0643  -0.0140 140 PHE F O   
11240 C CB  . PHE F  140 ? 2.1039 2.0469 1.9664 -0.1189 0.0621  -0.0301 140 PHE F CB  
11241 C CG  . PHE F  140 ? 2.0226 1.9717 1.8859 -0.1182 0.0598  -0.0353 140 PHE F CG  
11242 C CD1 . PHE F  140 ? 2.1200 2.0686 1.9903 -0.1177 0.0628  -0.0370 140 PHE F CD1 
11243 C CD2 . PHE F  140 ? 1.9643 1.9197 1.8214 -0.1181 0.0547  -0.0385 140 PHE F CD2 
11244 C CE1 . PHE F  140 ? 2.0971 2.0513 1.9679 -0.1171 0.0607  -0.0417 140 PHE F CE1 
11245 C CE2 . PHE F  140 ? 1.8821 1.8432 1.7401 -0.1174 0.0526  -0.0429 140 PHE F CE2 
11246 C CZ  . PHE F  140 ? 1.9483 1.9089 1.8130 -0.1169 0.0555  -0.0445 140 PHE F CZ  
11247 N N   . TYR F  141 ? 2.0560 1.9935 1.9068 -0.1180 0.0548  -0.0160 141 TYR F N   
11248 C CA  . TYR F  141 ? 1.9239 1.8575 1.7707 -0.1197 0.0567  -0.0132 141 TYR F CA  
11249 C C   . TYR F  141 ? 1.8395 1.7744 1.6835 -0.1229 0.0613  -0.0209 141 TYR F C   
11250 O O   . TYR F  141 ? 1.9092 1.8403 1.7514 -0.1248 0.0651  -0.0202 141 TYR F O   
11251 C CB  . TYR F  141 ? 1.9475 1.8824 1.7864 -0.1191 0.0501  -0.0087 141 TYR F CB  
11252 C CG  . TYR F  141 ? 1.8361 1.7699 1.6770 -0.1163 0.0452  -0.0006 141 TYR F CG  
11253 C CD1 . TYR F  141 ? 1.7475 1.6855 1.5838 -0.1150 0.0381  0.0006  141 TYR F CD1 
11254 C CD2 . TYR F  141 ? 1.7430 1.6717 1.5905 -0.1151 0.0477  0.0060  141 TYR F CD2 
11255 C CE1 . TYR F  141 ? 1.7857 1.7231 1.6239 -0.1126 0.0335  0.0080  141 TYR F CE1 
11256 C CE2 . TYR F  141 ? 1.7630 1.6912 1.6128 -0.1125 0.0430  0.0137  141 TYR F CE2 
11257 C CZ  . TYR F  141 ? 1.8147 1.7474 1.6598 -0.1114 0.0358  0.0146  141 TYR F CZ  
11258 O OH  . TYR F  141 ? 1.6458 1.5783 1.4931 -0.1091 0.0311  0.0221  141 TYR F OH  
11259 N N   . HIS F  142 ? 1.9442 1.8847 1.7880 -0.1234 0.0609  -0.0282 142 HIS F N   
11260 C CA  . HIS F  142 ? 1.9274 1.8704 1.7688 -0.1264 0.0646  -0.0358 142 HIS F CA  
11261 C C   . HIS F  142 ? 1.9743 1.9182 1.8224 -0.1276 0.0700  -0.0416 142 HIS F C   
11262 O O   . HIS F  142 ? 2.1055 2.0530 1.9566 -0.1263 0.0682  -0.0437 142 HIS F O   
11263 C CB  . HIS F  142 ? 1.9259 1.8755 1.7606 -0.1266 0.0597  -0.0397 142 HIS F CB  
11264 C CG  . HIS F  142 ? 1.9795 1.9354 1.8162 -0.1270 0.0599  -0.0470 142 HIS F CG  
11265 N ND1 . HIS F  142 ? 1.9618 1.9210 1.7974 -0.1298 0.0634  -0.0542 142 HIS F ND1 
11266 C CD2 . HIS F  142 ? 1.9503 1.9102 1.7899 -0.1251 0.0569  -0.0482 142 HIS F CD2 
11267 C CE1 . HIS F  142 ? 1.9096 1.8746 1.7473 -0.1296 0.0624  -0.0592 142 HIS F CE1 
11268 N NE2 . HIS F  142 ? 2.0049 1.9703 1.8449 -0.1267 0.0586  -0.0558 142 HIS F NE2 
11269 N N   . LYS F  143 ? 1.8164 1.7567 1.6666 -0.1302 0.0767  -0.0440 143 LYS F N   
11270 C CA  . LYS F  143 ? 1.8452 1.7855 1.7015 -0.1319 0.0826  -0.0495 143 LYS F CA  
11271 C C   . LYS F  143 ? 1.8381 1.7862 1.6940 -0.1322 0.0803  -0.0562 143 LYS F C   
11272 O O   . LYS F  143 ? 1.7548 1.7081 1.6060 -0.1337 0.0789  -0.0612 143 LYS F O   
11273 C CB  . LYS F  143 ? 1.8340 1.7714 1.6902 -0.1354 0.0893  -0.0532 143 LYS F CB  
11274 C CG  . LYS F  143 ? 1.8525 1.7816 1.7113 -0.1354 0.0935  -0.0471 143 LYS F CG  
11275 C CD  . LYS F  143 ? 1.9135 1.8378 1.7809 -0.1352 0.0992  -0.0464 143 LYS F CD  
11276 C CE  . LYS F  143 ? 1.9407 1.8641 1.8121 -0.1315 0.0953  -0.0403 143 LYS F CE  
11277 N NZ  . LYS F  143 ? 1.8288 1.7469 1.7090 -0.1313 0.1013  -0.0393 143 LYS F NZ  
11278 N N   . CYS F  144 ? 2.3148 2.2635 2.1758 -0.1306 0.0799  -0.0562 144 CYS F N   
11279 C CA  . CYS F  144 ? 2.3777 2.3336 2.2386 -0.1306 0.0775  -0.0619 144 CYS F CA  
11280 C C   . CYS F  144 ? 2.2030 2.1590 2.0696 -0.1328 0.0835  -0.0674 144 CYS F C   
11281 O O   . CYS F  144 ? 2.0845 2.0374 1.9567 -0.1315 0.0852  -0.0654 144 CYS F O   
11282 C CB  . CYS F  144 ? 2.3809 2.3388 2.2420 -0.1269 0.0711  -0.0576 144 CYS F CB  
11283 S SG  . CYS F  144 ? 2.4844 2.4517 2.3440 -0.1264 0.0669  -0.0637 144 CYS F SG  
11284 N N   . ASP F  145 ? 2.2648 2.2244 2.1299 -0.1362 0.0867  -0.0744 145 ASP F N   
11285 C CA  . ASP F  145 ? 2.3247 2.2852 2.1943 -0.1389 0.0923  -0.0806 145 ASP F CA  
11286 C C   . ASP F  145 ? 2.2543 2.2218 2.1244 -0.1382 0.0890  -0.0843 145 ASP F C   
11287 O O   . ASP F  145 ? 2.2441 2.2143 2.1125 -0.1350 0.0828  -0.0811 145 ASP F O   
11288 C CB  . ASP F  145 ? 2.4850 2.4471 2.3530 -0.1432 0.0971  -0.0868 145 ASP F CB  
11289 C CG  . ASP F  145 ? 2.5128 2.4810 2.3742 -0.1436 0.0927  -0.0888 145 ASP F CG  
11290 O OD1 . ASP F  145 ? 2.4428 2.4146 2.3031 -0.1470 0.0956  -0.0948 145 ASP F OD1 
11291 O OD2 . ASP F  145 ? 2.4709 2.4405 2.3287 -0.1406 0.0865  -0.0844 145 ASP F OD2 
11292 N N   . ASN F  146 ? 1.9023 1.8728 1.7749 -0.1412 0.0932  -0.0911 146 ASN F N   
11293 C CA  . ASN F  146 ? 1.7901 1.7668 1.6635 -0.1409 0.0909  -0.0947 146 ASN F CA  
11294 C C   . ASN F  146 ? 1.8852 1.8706 1.7535 -0.1397 0.0841  -0.0964 146 ASN F C   
11295 O O   . ASN F  146 ? 2.0671 2.0559 1.9354 -0.1371 0.0795  -0.0951 146 ASN F O   
11296 C CB  . ASN F  146 ? 1.5681 1.5465 1.4445 -0.1451 0.0970  -0.1020 146 ASN F CB  
11297 C CG  . ASN F  146 ? 1.5724 1.5425 1.4548 -0.1458 0.1035  -0.1007 146 ASN F CG  
11298 O OD1 . ASN F  146 ? 1.5858 1.5555 1.4708 -0.1495 0.1095  -0.1062 146 ASN F OD1 
11299 N ND2 . ASN F  146 ? 1.5500 1.5135 1.4349 -0.1423 0.1025  -0.0933 146 ASN F ND2 
11300 N N   . THR F  147 ? 2.0825 2.0714 1.9468 -0.1416 0.0838  -0.0991 147 THR F N   
11301 C CA  . THR F  147 ? 2.1566 2.1538 2.0164 -0.1407 0.0780  -0.1009 147 THR F CA  
11302 C C   . THR F  147 ? 2.2125 2.2080 2.0687 -0.1369 0.0723  -0.0945 147 THR F C   
11303 O O   . THR F  147 ? 2.1894 2.1908 2.0422 -0.1353 0.0670  -0.0948 147 THR F O   
11304 C CB  . THR F  147 ? 2.1108 2.1130 1.9681 -0.1442 0.0801  -0.1066 147 THR F CB  
11305 O OG1 . THR F  147 ? 2.2837 2.2807 2.1389 -0.1448 0.0820  -0.1041 147 THR F OG1 
11306 C CG2 . THR F  147 ? 1.5062 1.5102 1.3669 -0.1483 0.0859  -0.1131 147 THR F CG2 
11307 N N   . CYS F  148 ? 2.1269 2.1144 1.9840 -0.1357 0.0734  -0.0887 148 CYS F N   
11308 C CA  . CYS F  148 ? 2.1768 2.1621 2.0309 -0.1322 0.0680  -0.0821 148 CYS F CA  
11309 C C   . CYS F  148 ? 2.2751 2.2606 2.1321 -0.1291 0.0646  -0.0791 148 CYS F C   
11310 O O   . CYS F  148 ? 2.2913 2.2804 2.1455 -0.1265 0.0587  -0.0772 148 CYS F O   
11311 C CB  . CYS F  148 ? 2.1398 2.1166 1.9939 -0.1321 0.0704  -0.0766 148 CYS F CB  
11312 S SG  . CYS F  148 ? 2.1046 2.0783 1.9554 -0.1282 0.0638  -0.0679 148 CYS F SG  
11313 N N   . MET F  149 ? 2.0791 2.0607 1.9417 -0.1294 0.0687  -0.0789 149 MET F N   
11314 C CA  . MET F  149 ? 1.9271 1.9085 1.7933 -0.1268 0.0665  -0.0766 149 MET F CA  
11315 C C   . MET F  149 ? 1.8396 1.8294 1.7042 -0.1261 0.0624  -0.0806 149 MET F C   
11316 O O   . MET F  149 ? 1.7611 1.7520 1.6267 -0.1232 0.0584  -0.0778 149 MET F O   
11317 C CB  . MET F  149 ? 1.8257 1.8023 1.6983 -0.1281 0.0729  -0.0776 149 MET F CB  
11318 C CG  . MET F  149 ? 1.8057 1.7733 1.6814 -0.1279 0.0767  -0.0723 149 MET F CG  
11319 S SD  . MET F  149 ? 1.7619 1.7253 1.6389 -0.1232 0.0714  -0.0625 149 MET F SD  
11320 C CE  . MET F  149 ? 1.8006 1.7539 1.6829 -0.1237 0.0778  -0.0576 149 MET F CE  
11321 N N   . GLU F  150 ? 2.4544 2.4503 2.3167 -0.1288 0.0636  -0.0869 150 GLU F N   
11322 C CA  . GLU F  150 ? 2.4846 2.4889 2.3457 -0.1285 0.0603  -0.0910 150 GLU F CA  
11323 C C   . GLU F  150 ? 2.5376 2.5459 2.3940 -0.1258 0.0535  -0.0885 150 GLU F C   
11324 O O   . GLU F  150 ? 2.5226 2.5351 2.3790 -0.1235 0.0493  -0.0881 150 GLU F O   
11325 C CB  . GLU F  150 ? 2.5537 2.5635 2.4143 -0.1325 0.0638  -0.0984 150 GLU F CB  
11326 C CG  . GLU F  150 ? 2.5803 2.5956 2.4434 -0.1337 0.0646  -0.1031 150 GLU F CG  
11327 C CD  . GLU F  150 ? 2.6229 2.6332 2.4907 -0.1361 0.0711  -0.1051 150 GLU F CD  
11328 O OE1 . GLU F  150 ? 2.6843 2.6990 2.5534 -0.1385 0.0733  -0.1104 150 GLU F OE1 
11329 O OE2 . GLU F  150 ? 2.4979 2.4998 2.3681 -0.1356 0.0741  -0.1012 150 GLU F OE2 
11330 N N   . SER F  151 ? 2.1992 2.2063 2.0517 -0.1262 0.0528  -0.0871 151 SER F N   
11331 C CA  . SER F  151 ? 2.1110 2.1210 1.9587 -0.1240 0.0471  -0.0848 151 SER F CA  
11332 C C   . SER F  151 ? 2.0596 2.0672 1.9079 -0.1203 0.0425  -0.0791 151 SER F C   
11333 O O   . SER F  151 ? 2.0871 2.0985 1.9325 -0.1181 0.0374  -0.0780 151 SER F O   
11334 C CB  . SER F  151 ? 2.0425 2.0492 1.8862 -0.1251 0.0478  -0.0832 151 SER F CB  
11335 O OG  . SER F  151 ? 2.0172 2.0157 1.8619 -0.1245 0.0492  -0.0777 151 SER F OG  
11336 N N   . VAL F  152 ? 1.7425 1.7437 1.5947 -0.1195 0.0445  -0.0753 152 VAL F N   
11337 C CA  . VAL F  152 ? 1.6049 1.6035 1.4584 -0.1161 0.0405  -0.0696 152 VAL F CA  
11338 C C   . VAL F  152 ? 1.6673 1.6704 1.5238 -0.1148 0.0390  -0.0718 152 VAL F C   
11339 O O   . VAL F  152 ? 1.6108 1.6164 1.4661 -0.1121 0.0339  -0.0696 152 VAL F O   
11340 C CB  . VAL F  152 ? 1.3994 1.3898 1.2568 -0.1157 0.0433  -0.0644 152 VAL F CB  
11341 C CG1 . VAL F  152 ? 1.2391 1.2271 1.0971 -0.1122 0.0385  -0.0578 152 VAL F CG1 
11342 C CG2 . VAL F  152 ? 1.5508 1.5367 1.4058 -0.1176 0.0461  -0.0631 152 VAL F CG2 
11343 N N   . LYS F  153 ? 1.5706 1.5745 1.4309 -0.1168 0.0436  -0.0761 153 LYS F N   
11344 C CA  . LYS F  153 ? 1.5254 1.5335 1.3883 -0.1160 0.0428  -0.0787 153 LYS F CA  
11345 C C   . LYS F  153 ? 1.7857 1.8025 1.6449 -0.1156 0.0388  -0.0821 153 LYS F C   
11346 O O   . LYS F  153 ? 1.9275 1.9470 1.7864 -0.1129 0.0344  -0.0805 153 LYS F O   
11347 C CB  . LYS F  153 ? 1.4161 1.4233 1.2830 -0.1190 0.0491  -0.0832 153 LYS F CB  
11348 C CG  . LYS F  153 ? 1.2026 1.2013 1.0744 -0.1190 0.0534  -0.0797 153 LYS F CG  
11349 C CD  . LYS F  153 ? 1.3194 1.3176 1.1954 -0.1217 0.0594  -0.0845 153 LYS F CD  
11350 C CE  . LYS F  153 ? 1.2551 1.2444 1.1363 -0.1219 0.0645  -0.0812 153 LYS F CE  
11351 N NZ  . LYS F  153 ? 1.4618 1.4462 1.3421 -0.1233 0.0673  -0.0794 153 LYS F NZ  
11352 N N   . ASN F  154 ? 2.3650 2.3860 2.2217 -0.1183 0.0404  -0.0868 154 ASN F N   
11353 C CA  . ASN F  154 ? 2.4396 2.4690 2.2931 -0.1180 0.0369  -0.0899 154 ASN F CA  
11354 C C   . ASN F  154 ? 2.4935 2.5232 2.3434 -0.1148 0.0312  -0.0857 154 ASN F C   
11355 O O   . ASN F  154 ? 2.5525 2.5886 2.4004 -0.1137 0.0277  -0.0872 154 ASN F O   
11356 C CB  . ASN F  154 ? 2.5636 2.5969 2.4152 -0.1214 0.0398  -0.0949 154 ASN F CB  
11357 C CG  . ASN F  154 ? 2.5655 2.6021 2.4199 -0.1247 0.0442  -0.1006 154 ASN F CG  
11358 O OD1 . ASN F  154 ? 2.5798 2.6116 2.4365 -0.1271 0.0493  -0.1018 154 ASN F OD1 
11359 N ND2 . ASN F  154 ? 2.5697 2.6146 2.4241 -0.1248 0.0423  -0.1042 154 ASN F ND2 
11360 N N   . GLY F  155 ? 2.3530 2.3758 2.2023 -0.1136 0.0304  -0.0803 155 GLY F N   
11361 C CA  . GLY F  155 ? 2.3199 2.3422 2.1655 -0.1111 0.0254  -0.0762 155 GLY F CA  
11362 C C   . GLY F  155 ? 2.3992 2.4234 2.2399 -0.1125 0.0251  -0.0778 155 GLY F C   
11363 O O   . GLY F  155 ? 2.2996 2.3238 2.1365 -0.1109 0.0212  -0.0751 155 GLY F O   
11364 N N   . THR F  156 ? 2.3228 2.3486 2.1638 -0.1156 0.0293  -0.0822 156 THR F N   
11365 C CA  . THR F  156 ? 2.3525 2.3802 2.1894 -0.1172 0.0298  -0.0842 156 THR F CA  
11366 C C   . THR F  156 ? 2.1716 2.1926 2.0074 -0.1192 0.0334  -0.0826 156 THR F C   
11367 O O   . THR F  156 ? 2.0988 2.1197 1.9360 -0.1222 0.0381  -0.0861 156 THR F O   
11368 C CB  . THR F  156 ? 2.4342 2.4695 2.2719 -0.1195 0.0319  -0.0907 156 THR F CB  
11369 O OG1 . THR F  156 ? 2.3450 2.3792 2.1866 -0.1220 0.0367  -0.0935 156 THR F OG1 
11370 C CG2 . THR F  156 ? 2.4407 2.4834 2.2788 -0.1175 0.0281  -0.0922 156 THR F CG2 
11371 N N   . TYR F  157 ? 1.9898 2.0053 1.8230 -0.1177 0.0310  -0.0771 157 TYR F N   
11372 C CA  . TYR F  157 ? 1.8909 1.8995 1.7225 -0.1190 0.0335  -0.0740 157 TYR F CA  
11373 C C   . TYR F  157 ? 2.0640 2.0735 1.8895 -0.1182 0.0296  -0.0723 157 TYR F C   
11374 O O   . TYR F  157 ? 1.9739 1.9783 1.7965 -0.1174 0.0277  -0.0672 157 TYR F O   
11375 C CB  . TYR F  157 ? 1.7965 1.7987 1.6313 -0.1174 0.0333  -0.0685 157 TYR F CB  
11376 C CG  . TYR F  157 ? 1.6470 1.6415 1.4813 -0.1183 0.0358  -0.0641 157 TYR F CG  
11377 C CD1 . TYR F  157 ? 1.6392 1.6292 1.4784 -0.1196 0.0409  -0.0639 157 TYR F CD1 
11378 C CD2 . TYR F  157 ? 1.6306 1.6222 1.4597 -0.1179 0.0331  -0.0599 157 TYR F CD2 
11379 C CE1 . TYR F  157 ? 1.5514 1.5344 1.3905 -0.1202 0.0432  -0.0594 157 TYR F CE1 
11380 C CE2 . TYR F  157 ? 1.7117 1.6966 1.5403 -0.1186 0.0351  -0.0555 157 TYR F CE2 
11381 C CZ  . TYR F  157 ? 1.5635 1.5442 1.3973 -0.1197 0.0402  -0.0551 157 TYR F CZ  
11382 O OH  . TYR F  157 ? 1.4611 1.4351 1.2948 -0.1203 0.0423  -0.0504 157 TYR F OH  
11383 N N   . ASP F  158 ? 2.4484 2.4647 2.2723 -0.1183 0.0282  -0.0765 158 ASP F N   
11384 C CA  . ASP F  158 ? 2.5791 2.5974 2.3978 -0.1173 0.0245  -0.0756 158 ASP F CA  
11385 C C   . ASP F  158 ? 2.8176 2.8335 2.6319 -0.1196 0.0268  -0.0763 158 ASP F C   
11386 O O   . ASP F  158 ? 2.8732 2.8876 2.6825 -0.1191 0.0244  -0.0740 158 ASP F O   
11387 C CB  . ASP F  158 ? 2.2842 2.3108 2.1034 -0.1164 0.0227  -0.0798 158 ASP F CB  
11388 C CG  . ASP F  158 ? 2.1515 2.1800 1.9716 -0.1132 0.0180  -0.0775 158 ASP F CG  
11389 O OD1 . ASP F  158 ? 1.9099 1.9430 1.7280 -0.1119 0.0151  -0.0785 158 ASP F OD1 
11390 O OD2 . ASP F  158 ? 2.2104 2.2357 2.0335 -0.1120 0.0175  -0.0747 158 ASP F OD2 
11391 N N   . TYR F  159 ? 2.9045 2.9203 2.7208 -0.1223 0.0317  -0.0796 159 TYR F N   
11392 C CA  . TYR F  159 ? 3.0091 3.0226 2.8219 -0.1247 0.0345  -0.0806 159 TYR F CA  
11393 C C   . TYR F  159 ? 2.8946 2.9010 2.7088 -0.1262 0.0384  -0.0781 159 TYR F C   
11394 O O   . TYR F  159 ? 2.8122 2.8186 2.6289 -0.1287 0.0432  -0.0816 159 TYR F O   
11395 C CB  . TYR F  159 ? 3.1758 3.1959 2.9897 -0.1268 0.0372  -0.0869 159 TYR F CB  
11396 C CG  . TYR F  159 ? 3.2818 3.3010 3.0915 -0.1288 0.0391  -0.0881 159 TYR F CG  
11397 C CD1 . TYR F  159 ? 3.2918 3.3073 3.1018 -0.1316 0.0440  -0.0893 159 TYR F CD1 
11398 C CD2 . TYR F  159 ? 3.1994 3.2211 3.0048 -0.1279 0.0363  -0.0882 159 TYR F CD2 
11399 C CE1 . TYR F  159 ? 3.1687 3.1833 2.9749 -0.1335 0.0460  -0.0905 159 TYR F CE1 
11400 C CE2 . TYR F  159 ? 3.2970 3.3177 3.0986 -0.1298 0.0384  -0.0895 159 TYR F CE2 
11401 C CZ  . TYR F  159 ? 3.2400 3.2571 3.0419 -0.1326 0.0431  -0.0906 159 TYR F CZ  
11402 O OH  . TYR F  159 ? 3.0480 3.0640 2.8460 -0.1346 0.0453  -0.0918 159 TYR F OH  
11403 N N   . PRO F  160 ? 2.8741 2.8743 2.6868 -0.1248 0.0364  -0.0721 160 PRO F N   
11404 C CA  . PRO F  160 ? 2.7240 2.7172 2.5389 -0.1257 0.0397  -0.0687 160 PRO F CA  
11405 C C   . PRO F  160 ? 2.6452 2.6348 2.4572 -0.1284 0.0437  -0.0692 160 PRO F C   
11406 O O   . PRO F  160 ? 2.5109 2.5016 2.3176 -0.1292 0.0427  -0.0701 160 PRO F O   
11407 C CB  . PRO F  160 ? 2.2860 2.2750 2.0991 -0.1233 0.0354  -0.0617 160 PRO F CB  
11408 C CG  . PRO F  160 ? 2.5024 2.4965 2.3141 -0.1210 0.0302  -0.0622 160 PRO F CG  
11409 C CD  . PRO F  160 ? 2.8578 2.8576 2.6671 -0.1223 0.0309  -0.0679 160 PRO F CD  
11410 N N   . LYS F  161 ? 2.4124 2.3976 2.2280 -0.1299 0.0485  -0.0688 161 LYS F N   
11411 C CA  . LYS F  161 ? 1.9671 1.9478 1.7805 -0.1324 0.0527  -0.0686 161 LYS F CA  
11412 C C   . LYS F  161 ? 1.9940 1.9673 1.8106 -0.1324 0.0556  -0.0638 161 LYS F C   
11413 O O   . LYS F  161 ? 1.8670 1.8391 1.6891 -0.1334 0.0600  -0.0659 161 LYS F O   
11414 C CB  . LYS F  161 ? 1.7171 1.7016 1.5319 -0.1353 0.0573  -0.0756 161 LYS F CB  
11415 C CG  . LYS F  161 ? 1.9735 1.9642 1.7843 -0.1358 0.0552  -0.0796 161 LYS F CG  
11416 C CD  . LYS F  161 ? 1.9781 1.9653 1.7821 -0.1360 0.0537  -0.0763 161 LYS F CD  
11417 C CE  . LYS F  161 ? 1.8778 1.8709 1.6781 -0.1363 0.0518  -0.0800 161 LYS F CE  
11418 N NZ  . LYS F  161 ? 1.5287 1.5180 1.3219 -0.1367 0.0506  -0.0770 161 LYS F NZ  
11419 N N   . TYR F  162 ? 2.0192 1.9874 1.8323 -0.1313 0.0532  -0.0573 162 TYR F N   
11420 C CA  . TYR F  162 ? 1.9798 1.9412 1.7961 -0.1307 0.0552  -0.0515 162 TYR F CA  
11421 C C   . TYR F  162 ? 1.9824 1.9385 1.7974 -0.1332 0.0603  -0.0507 162 TYR F C   
11422 O O   . TYR F  162 ? 1.8537 1.8106 1.6635 -0.1351 0.0610  -0.0531 162 TYR F O   
11423 C CB  . TYR F  162 ? 1.7182 1.6774 1.5320 -0.1282 0.0495  -0.0443 162 TYR F CB  
11424 C CG  . TYR F  162 ? 1.9354 1.8947 1.7409 -0.1286 0.0460  -0.0424 162 TYR F CG  
11425 C CD1 . TYR F  162 ? 1.7293 1.6941 1.5305 -0.1284 0.0425  -0.0461 162 TYR F CD1 
11426 C CD2 . TYR F  162 ? 1.9824 1.9359 1.7841 -0.1293 0.0463  -0.0368 162 TYR F CD2 
11427 C CE1 . TYR F  162 ? 1.6594 1.6239 1.4529 -0.1290 0.0397  -0.0446 162 TYR F CE1 
11428 C CE2 . TYR F  162 ? 1.9854 1.9388 1.7790 -0.1301 0.0433  -0.0352 162 TYR F CE2 
11429 C CZ  . TYR F  162 ? 2.0368 1.9955 1.8263 -0.1300 0.0401  -0.0393 162 TYR F CZ  
11430 O OH  . TYR F  162 ? 2.0710 2.0292 1.8523 -0.1309 0.0374  -0.0380 162 TYR F OH  
11431 N N   . ASP G  7   ? 1.6785 1.6326 1.2466 -0.2567 -0.1004 -0.0853 7   ASP G N   
11432 C CA  . ASP G  7   ? 1.7227 1.6766 1.2973 -0.2483 -0.0981 -0.0831 7   ASP G CA  
11433 C C   . ASP G  7   ? 1.7472 1.7038 1.3379 -0.2385 -0.0984 -0.0802 7   ASP G C   
11434 O O   . ASP G  7   ? 1.9593 1.9212 1.5574 -0.2331 -0.1033 -0.0739 7   ASP G O   
11435 C CB  . ASP G  7   ? 1.6339 1.5798 1.2029 -0.2483 -0.0887 -0.0897 7   ASP G CB  
11436 C CG  . ASP G  7   ? 1.8842 1.8301 1.4496 -0.2464 -0.0884 -0.0875 7   ASP G CG  
11437 O OD1 . ASP G  7   ? 1.7081 1.6591 1.2704 -0.2483 -0.0954 -0.0819 7   ASP G OD1 
11438 O OD2 . ASP G  7   ? 1.6027 1.5436 1.1686 -0.2430 -0.0811 -0.0914 7   ASP G OD2 
11439 N N   . THR G  8   ? 1.6533 1.6062 1.2492 -0.2364 -0.0930 -0.0847 8   THR G N   
11440 C CA  . THR G  8   ? 1.6930 1.6478 1.3038 -0.2271 -0.0922 -0.0827 8   THR G CA  
11441 C C   . THR G  8   ? 1.5915 1.5508 1.2089 -0.2276 -0.0975 -0.0799 8   THR G C   
11442 O O   . THR G  8   ? 1.6833 1.6420 1.2945 -0.2349 -0.0987 -0.0824 8   THR G O   
11443 C CB  . THR G  8   ? 1.5067 1.4550 1.1213 -0.2230 -0.0826 -0.0887 8   THR G CB  
11444 O OG1 . THR G  8   ? 1.6802 1.6254 1.2939 -0.2270 -0.0799 -0.0932 8   THR G OG1 
11445 C CG2 . THR G  8   ? 1.6396 1.5823 1.2450 -0.2252 -0.0766 -0.0930 8   THR G CG2 
11446 N N   . LEU G  9   ? 1.7169 1.6807 1.3469 -0.2198 -0.1007 -0.0749 9   LEU G N   
11447 C CA  . LEU G  9   ? 1.5098 1.4773 1.1480 -0.2188 -0.1046 -0.0726 9   LEU G CA  
11448 C C   . LEU G  9   ? 1.6597 1.6248 1.3092 -0.2108 -0.0989 -0.0747 9   LEU G C   
11449 O O   . LEU G  9   ? 1.6559 1.6176 1.3074 -0.2057 -0.0932 -0.0767 9   LEU G O   
11450 C CB  . LEU G  9   ? 1.3513 1.3267 0.9953 -0.2166 -0.1134 -0.0645 9   LEU G CB  
11451 C CG  . LEU G  9   ? 1.3166 1.2968 0.9626 -0.2207 -0.1198 -0.0617 9   LEU G CG  
11452 C CD1 . LEU G  9   ? 1.1824 1.1681 0.8424 -0.2134 -0.1242 -0.0555 9   LEU G CD1 
11453 C CD2 . LEU G  9   ? 1.1974 1.1733 0.8410 -0.2250 -0.1155 -0.0679 9   LEU G CD2 
11454 N N   . CYS G  10  ? 1.6175 1.5843 1.2746 -0.2096 -0.1003 -0.0741 10  CYS G N   
11455 C CA  . CYS G  10  ? 1.4134 1.3779 1.0812 -0.2020 -0.0951 -0.0758 10  CYS G CA  
11456 C C   . CYS G  10  ? 1.3923 1.3610 1.0705 -0.1993 -0.0990 -0.0726 10  CYS G C   
11457 O O   . CYS G  10  ? 1.4109 1.3848 1.0890 -0.2028 -0.1063 -0.0685 10  CYS G O   
11458 C CB  . CYS G  10  ? 1.5225 1.4795 1.1859 -0.2044 -0.0864 -0.0834 10  CYS G CB  
11459 S SG  . CYS G  10  ? 1.8139 1.7653 1.4694 -0.2041 -0.0794 -0.0875 10  CYS G SG  
11460 N N   . ILE G  11  ? 1.5085 1.4748 1.1958 -0.1930 -0.0940 -0.0744 11  ILE G N   
11461 C CA  . ILE G  11  ? 1.3338 1.3040 1.0330 -0.1881 -0.0970 -0.0708 11  ILE G CA  
11462 C C   . ILE G  11  ? 1.3885 1.3541 1.0943 -0.1833 -0.0896 -0.0749 11  ILE G C   
11463 O O   . ILE G  11  ? 1.4481 1.4103 1.1553 -0.1787 -0.0836 -0.0771 11  ILE G O   
11464 C CB  . ILE G  11  ? 1.3289 1.3046 1.0363 -0.1811 -0.1015 -0.0642 11  ILE G CB  
11465 C CG1 . ILE G  11  ? 1.4204 1.3936 1.1302 -0.1743 -0.0962 -0.0651 11  ILE G CG1 
11466 C CG2 . ILE G  11  ? 1.2487 1.2293 0.9508 -0.1855 -0.1092 -0.0594 11  ILE G CG2 
11467 C CD1 . ILE G  11  ? 1.2952 1.2622 0.9963 -0.1771 -0.0892 -0.0712 11  ILE G CD1 
11468 N N   . GLY G  12  ? 1.7974 1.7633 1.5078 -0.1845 -0.0900 -0.0756 12  GLY G N   
11469 C CA  . GLY G  12  ? 1.6441 1.6056 1.3608 -0.1803 -0.0831 -0.0793 12  GLY G CA  
11470 C C   . GLY G  12  ? 1.4994 1.4627 1.2241 -0.1795 -0.0850 -0.0782 12  GLY G C   
11471 O O   . GLY G  12  ? 1.4830 1.4520 1.2112 -0.1802 -0.0921 -0.0735 12  GLY G O   
11472 N N   . TYR G  13  ? 1.2282 1.1866 0.9561 -0.1781 -0.0783 -0.0825 13  TYR G N   
11473 C CA  . TYR G  13  ? 1.2994 1.2589 1.0363 -0.1759 -0.0787 -0.0817 13  TYR G CA  
11474 C C   . TYR G  13  ? 1.2184 1.1715 0.9530 -0.1793 -0.0718 -0.0881 13  TYR G C   
11475 O O   . TYR G  13  ? 1.1912 1.1389 0.9182 -0.1825 -0.0661 -0.0930 13  TYR G O   
11476 C CB  . TYR G  13  ? 1.0878 1.0493 0.8368 -0.1657 -0.0777 -0.0781 13  TYR G CB  
11477 C CG  . TYR G  13  ? 1.0851 1.0443 0.8343 -0.1601 -0.0727 -0.0789 13  TYR G CG  
11478 C CD1 . TYR G  13  ? 1.0181 0.9722 0.7703 -0.1563 -0.0645 -0.0828 13  TYR G CD1 
11479 C CD2 . TYR G  13  ? 0.8571 0.8195 0.6041 -0.1584 -0.0761 -0.0756 13  TYR G CD2 
11480 C CE1 . TYR G  13  ? 0.8628 0.8153 0.6156 -0.1512 -0.0601 -0.0833 13  TYR G CE1 
11481 C CE2 . TYR G  13  ? 0.8888 0.8494 0.6362 -0.1535 -0.0716 -0.0764 13  TYR G CE2 
11482 C CZ  . TYR G  13  ? 0.9199 0.8758 0.6703 -0.1499 -0.0637 -0.0802 13  TYR G CZ  
11483 O OH  . TYR G  13  ? 0.8962 0.8507 0.6473 -0.1450 -0.0593 -0.0808 13  TYR G OH  
11484 N N   . HIS G  14  ? 1.4162 1.3698 1.1577 -0.1787 -0.0721 -0.0879 14  HIS G N   
11485 C CA  . HIS G  14  ? 1.3410 1.2889 1.0807 -0.1827 -0.0662 -0.0936 14  HIS G CA  
11486 C C   . HIS G  14  ? 1.5227 1.4646 1.2667 -0.1768 -0.0568 -0.0970 14  HIS G C   
11487 O O   . HIS G  14  ? 1.6202 1.5633 1.3702 -0.1688 -0.0555 -0.0943 14  HIS G O   
11488 C CB  . HIS G  14  ? 1.4739 1.4245 1.2203 -0.1837 -0.0696 -0.0920 14  HIS G CB  
11489 C CG  . HIS G  14  ? 1.7022 1.6472 1.4463 -0.1887 -0.0641 -0.0979 14  HIS G CG  
11490 N ND1 . HIS G  14  ? 1.8203 1.7643 1.5547 -0.1988 -0.0657 -0.1014 14  HIS G ND1 
11491 C CD2 . HIS G  14  ? 1.8264 1.7665 1.5765 -0.1852 -0.0568 -0.1011 14  HIS G CD2 
11492 C CE1 . HIS G  14  ? 1.9745 1.9129 1.7090 -0.2014 -0.0595 -0.1066 14  HIS G CE1 
11493 N NE2 . HIS G  14  ? 1.9449 1.8807 1.6891 -0.1932 -0.0539 -0.1065 14  HIS G NE2 
11494 N N   . ALA G  15  ? 1.2180 1.1537 0.9588 -0.1808 -0.0503 -0.1028 15  ALA G N   
11495 C CA  . ALA G  15  ? 1.3015 1.2310 1.0464 -0.1760 -0.0408 -0.1063 15  ALA G CA  
11496 C C   . ALA G  15  ? 1.2608 1.1845 1.0033 -0.1817 -0.0355 -0.1120 15  ALA G C   
11497 O O   . ALA G  15  ? 1.3677 1.2910 1.1019 -0.1907 -0.0380 -0.1146 15  ALA G O   
11498 C CB  . ALA G  15  ? 1.0274 0.9537 0.7664 -0.1753 -0.0364 -0.1084 15  ALA G CB  
11499 N N   . ASN G  16  ? 1.3828 1.3020 1.1325 -0.1767 -0.0279 -0.1141 16  ASN G N   
11500 C CA  . ASN G  16  ? 1.5212 1.4346 1.2700 -0.1814 -0.0223 -0.1193 16  ASN G CA  
11501 C C   . ASN G  16  ? 1.5684 1.4755 1.3235 -0.1756 -0.0122 -0.1220 16  ASN G C   
11502 O O   . ASN G  16  ? 1.5458 1.4528 1.3048 -0.1686 -0.0091 -0.1203 16  ASN G O   
11503 C CB  . ASN G  16  ? 1.6066 1.5238 1.3604 -0.1831 -0.0277 -0.1172 16  ASN G CB  
11504 C CG  . ASN G  16  ? 1.6415 1.5634 1.4080 -0.1736 -0.0304 -0.1114 16  ASN G CG  
11505 O OD1 . ASN G  16  ? 1.4400 1.3614 1.2122 -0.1656 -0.0269 -0.1096 16  ASN G OD1 
11506 N ND2 . ASN G  16  ? 1.5379 1.4645 1.3088 -0.1747 -0.0366 -0.1084 16  ASN G ND2 
11507 N N   . ASN G  17  ? 1.3809 1.2831 1.1373 -0.1787 -0.0071 -0.1261 17  ASN G N   
11508 C CA  . ASN G  17  ? 1.5136 1.4095 1.2764 -0.1738 0.0028  -0.1287 17  ASN G CA  
11509 C C   . ASN G  17  ? 1.7024 1.6011 1.4783 -0.1651 0.0025  -0.1243 17  ASN G C   
11510 O O   . ASN G  17  ? 1.7790 1.6729 1.5611 -0.1618 0.0099  -0.1262 17  ASN G O   
11511 C CB  . ASN G  17  ? 1.7812 1.6696 1.5389 -0.1815 0.0093  -0.1356 17  ASN G CB  
11512 C CG  . ASN G  17  ? 1.9022 1.7926 1.6612 -0.1864 0.0049  -0.1358 17  ASN G CG  
11513 O OD1 . ASN G  17  ? 1.9828 1.8789 1.7495 -0.1821 -0.0009 -0.1308 17  ASN G OD1 
11514 N ND2 . ASN G  17  ? 1.9947 1.8803 1.7460 -0.1957 0.0079  -0.1416 17  ASN G ND2 
11515 N N   . SER G  18  ? 1.5269 1.4332 1.3071 -0.1612 -0.0058 -0.1184 18  SER G N   
11516 C CA  . SER G  18  ? 1.4471 1.3565 1.2393 -0.1534 -0.0069 -0.1140 18  SER G CA  
11517 C C   . SER G  18  ? 1.3716 1.2799 1.1710 -0.1439 -0.0013 -0.1122 18  SER G C   
11518 O O   . SER G  18  ? 1.2154 1.1249 1.0121 -0.1414 -0.0012 -0.1111 18  SER G O   
11519 C CB  . SER G  18  ? 1.3185 1.2362 1.1129 -0.1523 -0.0173 -0.1083 18  SER G CB  
11520 O OG  . SER G  18  ? 1.3412 1.2617 1.1468 -0.1457 -0.0184 -0.1044 18  SER G OG  
11521 N N   . THR G  19  ? 1.4247 1.3308 1.2332 -0.1387 0.0035  -0.1118 19  THR G N   
11522 C CA  . THR G  19  ? 1.2858 1.1915 1.1022 -0.1294 0.0087  -0.1095 19  THR G CA  
11523 C C   . THR G  19  ? 1.2201 1.1318 1.0463 -0.1221 0.0039  -0.1035 19  THR G C   
11524 O O   . THR G  19  ? 1.2520 1.1646 1.0855 -0.1140 0.0069  -0.1008 19  THR G O   
11525 C CB  . THR G  19  ? 1.4042 1.3023 1.2240 -0.1284 0.0190  -0.1134 19  THR G CB  
11526 O OG1 . THR G  19  ? 1.5539 1.4502 1.3770 -0.1310 0.0194  -0.1147 19  THR G OG1 
11527 C CG2 . THR G  19  ? 1.4413 1.3331 1.2518 -0.1347 0.0248  -0.1193 19  THR G CG2 
11528 N N   . ASP G  20  ? 1.1894 1.1052 1.0158 -0.1252 -0.0035 -0.1015 20  ASP G N   
11529 C CA  . ASP G  20  ? 1.1771 1.0987 1.0123 -0.1191 -0.0085 -0.0960 20  ASP G CA  
11530 C C   . ASP G  20  ? 1.1712 1.0973 1.0088 -0.1122 -0.0107 -0.0917 20  ASP G C   
11531 O O   . ASP G  20  ? 1.0017 0.9298 0.8326 -0.1144 -0.0138 -0.0915 20  ASP G O   
11532 C CB  . ASP G  20  ? 1.0635 0.9896 0.8969 -0.1243 -0.0171 -0.0943 20  ASP G CB  
11533 C CG  . ASP G  20  ? 1.2395 1.1621 1.0726 -0.1303 -0.0155 -0.0977 20  ASP G CG  
11534 O OD1 . ASP G  20  ? 1.2510 1.1771 1.0820 -0.1356 -0.0221 -0.0970 20  ASP G OD1 
11535 O OD2 . ASP G  20  ? 1.2881 1.2047 1.1234 -0.1296 -0.0076 -0.1012 20  ASP G OD2 
11536 N N   . THR G  21  ? 1.2044 1.1323 1.0513 -0.1040 -0.0090 -0.0882 21  THR G N   
11537 C CA  . THR G  21  ? 1.0857 1.0183 0.9357 -0.0972 -0.0110 -0.0840 21  THR G CA  
11538 C C   . THR G  21  ? 1.0176 0.9556 0.8758 -0.0921 -0.0161 -0.0789 21  THR G C   
11539 O O   . THR G  21  ? 1.1602 1.0970 1.0252 -0.0896 -0.0139 -0.0783 21  THR G O   
11540 C CB  . THR G  21  ? 1.0227 0.9524 0.8760 -0.0913 -0.0032 -0.0847 21  THR G CB  
11541 O OG1 . THR G  21  ? 1.2492 1.1722 1.1033 -0.0931 0.0043  -0.0887 21  THR G OG1 
11542 C CG2 . THR G  21  ? 1.0023 0.9320 0.8488 -0.0924 -0.0025 -0.0860 21  THR G CG2 
11543 N N   . VAL G  22  ? 0.9239 0.8675 0.7814 -0.0906 -0.0225 -0.0753 22  VAL G N   
11544 C CA  . VAL G  22  ? 0.8746 0.8235 0.7397 -0.0856 -0.0272 -0.0703 22  VAL G CA  
11545 C C   . VAL G  22  ? 0.9288 0.8812 0.7964 -0.0788 -0.0273 -0.0671 22  VAL G C   
11546 O O   . VAL G  22  ? 0.8917 0.8433 0.7546 -0.0788 -0.0251 -0.0685 22  VAL G O   
11547 C CB  . VAL G  22  ? 0.7579 0.7108 0.6206 -0.0902 -0.0356 -0.0683 22  VAL G CB  
11548 C CG1 . VAL G  22  ? 0.8321 0.7819 0.6905 -0.0982 -0.0359 -0.0719 22  VAL G CG1 
11549 C CG2 . VAL G  22  ? 0.6963 0.6525 0.5529 -0.0917 -0.0400 -0.0671 22  VAL G CG2 
11550 N N   . ASP G  23  ? 0.8156 0.7721 0.6906 -0.0732 -0.0298 -0.0628 23  ASP G N   
11551 C CA  . ASP G  23  ? 0.8228 0.7834 0.7005 -0.0670 -0.0307 -0.0596 23  ASP G CA  
11552 C C   . ASP G  23  ? 0.7645 0.7305 0.6422 -0.0675 -0.0384 -0.0560 23  ASP G C   
11553 O O   . ASP G  23  ? 0.7961 0.7634 0.6757 -0.0699 -0.0427 -0.0547 23  ASP G O   
11554 C CB  . ASP G  23  ? 0.9579 0.9188 0.8442 -0.0596 -0.0266 -0.0574 23  ASP G CB  
11555 C CG  . ASP G  23  ? 0.9810 0.9373 0.8679 -0.0578 -0.0185 -0.0602 23  ASP G CG  
11556 O OD1 . ASP G  23  ? 1.1064 1.0587 0.9870 -0.0625 -0.0157 -0.0641 23  ASP G OD1 
11557 O OD2 . ASP G  23  ? 1.1011 1.0577 0.9948 -0.0517 -0.0147 -0.0584 23  ASP G OD2 
11558 N N   . THR G  24  ? 0.6543 0.6235 0.5301 -0.0651 -0.0401 -0.0543 24  THR G N   
11559 C CA  . THR G  24  ? 0.7163 0.6906 0.5930 -0.0645 -0.0467 -0.0506 24  THR G CA  
11560 C C   . THR G  24  ? 0.7392 0.7170 0.6215 -0.0571 -0.0459 -0.0475 24  THR G C   
11561 O O   . THR G  24  ? 0.6499 0.6264 0.5354 -0.0527 -0.0405 -0.0480 24  THR G O   
11562 C CB  . THR G  24  ? 0.8602 0.8354 0.7285 -0.0693 -0.0503 -0.0515 24  THR G CB  
11563 O OG1 . THR G  24  ? 0.9455 0.9206 0.8112 -0.0668 -0.0469 -0.0524 24  THR G OG1 
11564 C CG2 . THR G  24  ? 0.7095 0.6810 0.5711 -0.0770 -0.0503 -0.0551 24  THR G CG2 
11565 N N   . VAL G  25  ? 0.7866 0.7688 0.6702 -0.0559 -0.0511 -0.0442 25  VAL G N   
11566 C CA  . VAL G  25  ? 0.7725 0.7584 0.6609 -0.0494 -0.0507 -0.0413 25  VAL G CA  
11567 C C   . VAL G  25  ? 0.8064 0.7925 0.6907 -0.0480 -0.0479 -0.0427 25  VAL G C   
11568 O O   . VAL G  25  ? 0.6517 0.6393 0.5396 -0.0426 -0.0448 -0.0417 25  VAL G O   
11569 C CB  . VAL G  25  ? 0.7569 0.7472 0.6472 -0.0490 -0.0569 -0.0377 25  VAL G CB  
11570 C CG1 . VAL G  25  ? 0.7804 0.7738 0.6776 -0.0424 -0.0561 -0.0347 25  VAL G CG1 
11571 C CG2 . VAL G  25  ? 0.8268 0.8168 0.7183 -0.0531 -0.0610 -0.0368 25  VAL G CG2 
11572 N N   . LEU G  26  ? 0.8220 0.8066 0.6987 -0.0531 -0.0489 -0.0449 26  LEU G N   
11573 C CA  . LEU G  26  ? 0.7752 0.7603 0.6476 -0.0524 -0.0469 -0.0461 26  LEU G CA  
11574 C C   . LEU G  26  ? 0.8489 0.8296 0.7181 -0.0535 -0.0408 -0.0500 26  LEU G C   
11575 O O   . LEU G  26  ? 0.8225 0.8035 0.6901 -0.0515 -0.0377 -0.0508 26  LEU G O   
11576 C CB  . LEU G  26  ? 0.7303 0.7168 0.5963 -0.0569 -0.0519 -0.0459 26  LEU G CB  
11577 C CG  . LEU G  26  ? 0.8512 0.8417 0.7198 -0.0569 -0.0582 -0.0422 26  LEU G CG  
11578 C CD1 . LEU G  26  ? 0.6177 0.6094 0.4797 -0.0613 -0.0625 -0.0419 26  LEU G CD1 
11579 C CD2 . LEU G  26  ? 0.8372 0.8315 0.7126 -0.0503 -0.0582 -0.0390 26  LEU G CD2 
11580 N N   . GLU G  27  ? 0.9584 0.9348 0.8270 -0.0568 -0.0388 -0.0523 27  GLU G N   
11581 C CA  . GLU G  27  ? 0.8542 0.8257 0.7192 -0.0588 -0.0328 -0.0563 27  GLU G CA  
11582 C C   . GLU G  27  ? 0.8870 0.8544 0.7556 -0.0589 -0.0287 -0.0579 27  GLU G C   
11583 O O   . GLU G  27  ? 0.9266 0.8940 0.7975 -0.0606 -0.0316 -0.0571 27  GLU G O   
11584 C CB  . GLU G  27  ? 1.0146 0.9839 0.8702 -0.0660 -0.0346 -0.0592 27  GLU G CB  
11585 C CG  . GLU G  27  ? 1.1678 1.1329 1.0186 -0.0676 -0.0286 -0.0631 27  GLU G CG  
11586 C CD  . GLU G  27  ? 1.3625 1.3264 1.2038 -0.0740 -0.0308 -0.0653 27  GLU G CD  
11587 O OE1 . GLU G  27  ? 1.3115 1.2710 1.1478 -0.0770 -0.0261 -0.0691 27  GLU G OE1 
11588 O OE2 . GLU G  27  ? 1.3783 1.3457 1.2172 -0.0761 -0.0372 -0.0632 27  GLU G OE2 
11589 N N   . LYS G  28  ? 0.8423 0.8064 0.7119 -0.0570 -0.0218 -0.0601 28  LYS G N   
11590 C CA  . LYS G  28  ? 0.9320 0.8916 0.8051 -0.0569 -0.0169 -0.0619 28  LYS G CA  
11591 C C   . LYS G  28  ? 0.9357 0.8890 0.8033 -0.0622 -0.0120 -0.0668 28  LYS G C   
11592 O O   . LYS G  28  ? 0.9277 0.8795 0.7906 -0.0635 -0.0092 -0.0690 28  LYS G O   
11593 C CB  . LYS G  28  ? 0.9159 0.8759 0.7961 -0.0497 -0.0112 -0.0604 28  LYS G CB  
11594 C CG  . LYS G  28  ? 0.9769 0.9409 0.8650 -0.0440 -0.0133 -0.0562 28  LYS G CG  
11595 C CD  . LYS G  28  ? 1.2482 1.2125 1.1427 -0.0372 -0.0075 -0.0547 28  LYS G CD  
11596 C CE  . LYS G  28  ? 1.3663 1.3328 1.2685 -0.0324 -0.0083 -0.0513 28  LYS G CE  
11597 N NZ  . LYS G  28  ? 1.2989 1.2709 1.2021 -0.0313 -0.0151 -0.0480 28  LYS G NZ  
11598 N N   . ASN G  29  ? 1.1830 1.1327 1.0514 -0.0655 -0.0109 -0.0686 29  ASN G N   
11599 C CA  . ASN G  29  ? 1.1029 1.0464 0.9659 -0.0714 -0.0065 -0.0736 29  ASN G CA  
11600 C C   . ASN G  29  ? 1.0985 1.0417 0.9516 -0.0782 -0.0101 -0.0758 29  ASN G C   
11601 O O   . ASN G  29  ? 1.1604 1.1008 1.0084 -0.0801 -0.0063 -0.0787 29  ASN G O   
11602 C CB  . ASN G  29  ? 1.0709 1.0096 0.9357 -0.0689 0.0025  -0.0761 29  ASN G CB  
11603 C CG  . ASN G  29  ? 1.5119 1.4492 1.3857 -0.0639 0.0069  -0.0747 29  ASN G CG  
11604 O OD1 . ASN G  29  ? 1.5954 1.5285 1.4699 -0.0669 0.0091  -0.0769 29  ASN G OD1 
11605 N ND2 . ASN G  29  ? 1.4992 1.4401 1.3796 -0.0563 0.0079  -0.0710 29  ASN G ND2 
11606 N N   . VAL G  30  ? 0.9650 0.9114 0.8157 -0.0819 -0.0175 -0.0743 30  VAL G N   
11607 C CA  . VAL G  30  ? 0.7747 0.7211 0.6160 -0.0888 -0.0215 -0.0761 30  VAL G CA  
11608 C C   . VAL G  30  ? 0.9156 0.8579 0.7522 -0.0965 -0.0213 -0.0798 30  VAL G C   
11609 O O   . VAL G  30  ? 0.9750 0.9183 0.8152 -0.0976 -0.0241 -0.0787 30  VAL G O   
11610 C CB  . VAL G  30  ? 0.8718 0.8245 0.7130 -0.0886 -0.0299 -0.0719 30  VAL G CB  
11611 C CG1 . VAL G  30  ? 0.6965 0.6491 0.5279 -0.0963 -0.0342 -0.0735 30  VAL G CG1 
11612 C CG2 . VAL G  30  ? 0.8679 0.8246 0.7126 -0.0819 -0.0302 -0.0687 30  VAL G CG2 
11613 N N   . THR G  31  ? 0.9211 0.8590 0.7497 -0.1019 -0.0178 -0.0842 31  THR G N   
11614 C CA  . THR G  31  ? 1.0026 0.9363 0.8257 -0.1098 -0.0171 -0.0883 31  THR G CA  
11615 C C   . THR G  31  ? 0.9592 0.8966 0.7769 -0.1159 -0.0255 -0.0871 31  THR G C   
11616 O O   . THR G  31  ? 1.0092 0.9492 0.8212 -0.1177 -0.0295 -0.0860 31  THR G O   
11617 C CB  . THR G  31  ? 1.0705 0.9980 0.8862 -0.1141 -0.0105 -0.0937 31  THR G CB  
11618 O OG1 . THR G  31  ? 1.0201 0.9441 0.8414 -0.1083 -0.0023 -0.0946 31  THR G OG1 
11619 C CG2 . THR G  31  ? 1.1104 1.0334 0.9203 -0.1226 -0.0095 -0.0982 31  THR G CG2 
11620 N N   . VAL G  32  ? 1.0554 0.9931 0.8751 -0.1191 -0.0282 -0.0870 32  VAL G N   
11621 C CA  . VAL G  32  ? 0.9247 0.8664 0.7402 -0.1249 -0.0364 -0.0854 32  VAL G CA  
11622 C C   . VAL G  32  ? 0.9733 0.9112 0.7821 -0.1339 -0.0356 -0.0900 32  VAL G C   
11623 O O   . VAL G  32  ? 1.1076 1.0401 0.9173 -0.1349 -0.0291 -0.0939 32  VAL G O   
11624 C CB  . VAL G  32  ? 0.9519 0.8989 0.7761 -0.1210 -0.0420 -0.0803 32  VAL G CB  
11625 C CG1 . VAL G  32  ? 0.9144 0.8660 0.7436 -0.1135 -0.0442 -0.0756 32  VAL G CG1 
11626 C CG2 . VAL G  32  ? 0.8957 0.8400 0.7276 -0.1185 -0.0377 -0.0813 32  VAL G CG2 
11627 N N   . THR G  33  ? 1.0898 1.0307 0.8918 -0.1405 -0.0423 -0.0894 33  THR G N   
11628 C CA  . THR G  33  ? 1.0735 1.0117 0.8681 -0.1499 -0.0425 -0.0936 33  THR G CA  
11629 C C   . THR G  33  ? 1.1720 1.1106 0.9727 -0.1510 -0.0434 -0.0935 33  THR G C   
11630 O O   . THR G  33  ? 1.2699 1.2037 1.0678 -0.1562 -0.0393 -0.0982 33  THR G O   
11631 C CB  . THR G  33  ? 1.0426 0.9849 0.8285 -0.1565 -0.0501 -0.0923 33  THR G CB  
11632 O OG1 . THR G  33  ? 1.0652 1.0146 0.8569 -0.1539 -0.0581 -0.0863 33  THR G OG1 
11633 C CG2 . THR G  33  ? 1.0318 0.9733 0.8109 -0.1561 -0.0488 -0.0929 33  THR G CG2 
11634 N N   . HIS G  34  ? 1.0345 0.9785 0.8436 -0.1463 -0.0486 -0.0882 34  HIS G N   
11635 C CA  . HIS G  34  ? 1.1049 1.0498 0.9205 -0.1471 -0.0501 -0.0875 34  HIS G CA  
11636 C C   . HIS G  34  ? 1.1076 1.0556 0.9350 -0.1380 -0.0507 -0.0827 34  HIS G C   
11637 O O   . HIS G  34  ? 1.0736 1.0252 0.9035 -0.1325 -0.0532 -0.0788 34  HIS G O   
11638 C CB  . HIS G  34  ? 1.0184 0.9682 0.8302 -0.1544 -0.0583 -0.0860 34  HIS G CB  
11639 C CG  . HIS G  34  ? 1.1967 1.1441 0.9963 -0.1638 -0.0584 -0.0904 34  HIS G CG  
11640 N ND1 . HIS G  34  ? 1.0731 1.0209 0.8643 -0.1658 -0.0597 -0.0906 34  HIS G ND1 
11641 C CD2 . HIS G  34  ? 1.3662 1.3109 1.1605 -0.1721 -0.0574 -0.0948 34  HIS G CD2 
11642 C CE1 . HIS G  34  ? 1.1909 1.1362 0.9719 -0.1748 -0.0593 -0.0950 34  HIS G CE1 
11643 N NE2 . HIS G  34  ? 1.4787 1.4221 1.2612 -0.1789 -0.0580 -0.0977 34  HIS G NE2 
11644 N N   . SER G  35  ? 1.0121 0.9586 0.8465 -0.1367 -0.0484 -0.0832 35  SER G N   
11645 C CA  . SER G  35  ? 0.9875 0.9366 0.8331 -0.1284 -0.0486 -0.0789 35  SER G CA  
11646 C C   . SER G  35  ? 0.9632 0.9112 0.8152 -0.1293 -0.0477 -0.0794 35  SER G C   
11647 O O   . SER G  35  ? 1.1183 1.0627 0.9664 -0.1358 -0.0454 -0.0838 35  SER G O   
11648 C CB  . SER G  35  ? 0.9651 0.9112 0.8140 -0.1207 -0.0419 -0.0791 35  SER G CB  
11649 O OG  . SER G  35  ? 1.0426 0.9818 0.8898 -0.1221 -0.0337 -0.0841 35  SER G OG  
11650 N N   . VAL G  36  ? 0.9008 0.8520 0.7626 -0.1229 -0.0494 -0.0751 36  VAL G N   
11651 C CA  . VAL G  36  ? 0.9775 0.9279 0.8466 -0.1226 -0.0483 -0.0751 36  VAL G CA  
11652 C C   . VAL G  36  ? 1.0025 0.9518 0.8809 -0.1134 -0.0438 -0.0729 36  VAL G C   
11653 O O   . VAL G  36  ? 0.9096 0.8612 0.7900 -0.1072 -0.0442 -0.0698 36  VAL G O   
11654 C CB  . VAL G  36  ? 0.8619 0.8184 0.7342 -0.1253 -0.0567 -0.0714 36  VAL G CB  
11655 C CG1 . VAL G  36  ? 0.9403 0.8986 0.8034 -0.1346 -0.0617 -0.0731 36  VAL G CG1 
11656 C CG2 . VAL G  36  ? 0.7951 0.7572 0.6729 -0.1187 -0.0613 -0.0654 36  VAL G CG2 
11657 N N   . ASN G  37  ? 1.0639 1.0099 0.9479 -0.1125 -0.0394 -0.0744 37  ASN G N   
11658 C CA  . ASN G  37  ? 1.0241 0.9693 0.9172 -0.1040 -0.0351 -0.0721 37  ASN G CA  
11659 C C   . ASN G  37  ? 1.0043 0.9539 0.9059 -0.1013 -0.0399 -0.0677 37  ASN G C   
11660 O O   . ASN G  37  ? 1.0969 1.0469 1.0001 -0.1060 -0.0421 -0.0684 37  ASN G O   
11661 C CB  . ASN G  37  ? 0.9515 0.8897 0.8461 -0.1037 -0.0263 -0.0762 37  ASN G CB  
11662 C CG  . ASN G  37  ? 1.1759 1.1127 1.0778 -0.0945 -0.0209 -0.0740 37  ASN G CG  
11663 O OD1 . ASN G  37  ? 1.3417 1.2734 1.2467 -0.0928 -0.0138 -0.0763 37  ASN G OD1 
11664 N ND2 . ASN G  37  ? 1.0126 0.9542 0.9174 -0.0885 -0.0242 -0.0695 37  ASN G ND2 
11665 N N   . LEU G  38  ? 0.8808 0.8339 0.7878 -0.0940 -0.0414 -0.0631 38  LEU G N   
11666 C CA  . LEU G  38  ? 0.7902 0.7474 0.7056 -0.0909 -0.0456 -0.0587 38  LEU G CA  
11667 C C   . LEU G  38  ? 0.7642 0.7184 0.6878 -0.0855 -0.0398 -0.0585 38  LEU G C   
11668 O O   . LEU G  38  ? 0.7573 0.7139 0.6885 -0.0829 -0.0419 -0.0554 38  LEU G O   
11669 C CB  . LEU G  38  ? 0.6350 0.5976 0.5520 -0.0862 -0.0503 -0.0540 38  LEU G CB  
11670 C CG  . LEU G  38  ? 0.6369 0.6036 0.5474 -0.0909 -0.0572 -0.0529 38  LEU G CG  
11671 C CD1 . LEU G  38  ? 0.8116 0.7823 0.7232 -0.0855 -0.0598 -0.0490 38  LEU G CD1 
11672 C CD2 . LEU G  38  ? 0.7305 0.7007 0.6430 -0.0961 -0.0635 -0.0514 38  LEU G CD2 
11673 N N   . LEU G  39  ? 0.7385 0.6874 0.6607 -0.0838 -0.0323 -0.0617 39  LEU G N   
11674 C CA  . LEU G  39  ? 0.7834 0.7290 0.7128 -0.0782 -0.0261 -0.0613 39  LEU G CA  
11675 C C   . LEU G  39  ? 0.8739 0.8142 0.8036 -0.0830 -0.0216 -0.0656 39  LEU G C   
11676 O O   . LEU G  39  ? 0.9428 0.8788 0.8662 -0.0875 -0.0179 -0.0701 39  LEU G O   
11677 C CB  . LEU G  39  ? 0.7365 0.6799 0.6653 -0.0723 -0.0203 -0.0614 39  LEU G CB  
11678 C CG  . LEU G  39  ? 0.7125 0.6555 0.6495 -0.0640 -0.0159 -0.0586 39  LEU G CG  
11679 C CD1 . LEU G  39  ? 0.7567 0.6948 0.6928 -0.0611 -0.0077 -0.0609 39  LEU G CD1 
11680 C CD2 . LEU G  39  ? 0.7025 0.6449 0.6470 -0.0635 -0.0157 -0.0575 39  LEU G CD2 
11681 N N   . GLU G  40  ? 0.8598 0.8003 0.7968 -0.0821 -0.0218 -0.0643 40  GLU G N   
11682 C CA  . GLU G  40  ? 0.8384 0.7737 0.7767 -0.0859 -0.0169 -0.0682 40  GLU G CA  
11683 C C   . GLU G  40  ? 0.8295 0.7597 0.7723 -0.0799 -0.0082 -0.0688 40  GLU G C   
11684 O O   . GLU G  40  ? 0.8089 0.7407 0.7585 -0.0725 -0.0073 -0.0649 40  GLU G O   
11685 C CB  . GLU G  40  ? 0.7621 0.6999 0.7062 -0.0882 -0.0210 -0.0667 40  GLU G CB  
11686 C CG  . GLU G  40  ? 0.9407 0.8733 0.8866 -0.0925 -0.0162 -0.0707 40  GLU G CG  
11687 C CD  . GLU G  40  ? 1.0828 1.0121 1.0197 -0.1011 -0.0150 -0.0763 40  GLU G CD  
11688 O OE1 . GLU G  40  ? 1.1863 1.1165 1.1220 -0.1082 -0.0183 -0.0782 40  GLU G OE1 
11689 O OE2 . GLU G  40  ? 1.0204 0.9463 0.9515 -0.1010 -0.0108 -0.0788 40  GLU G OE2 
11690 N N   . ASP G  41  ? 0.8063 0.7304 0.7453 -0.0830 -0.0017 -0.0735 41  ASP G N   
11691 C CA  . ASP G  41  ? 0.9412 0.8602 0.8842 -0.0776 0.0071  -0.0742 41  ASP G CA  
11692 C C   . ASP G  41  ? 0.9944 0.9067 0.9375 -0.0823 0.0133  -0.0791 41  ASP G C   
11693 O O   . ASP G  41  ? 1.2177 1.1243 1.1600 -0.0812 0.0211  -0.0818 41  ASP G O   
11694 C CB  . ASP G  41  ? 0.9992 0.9171 0.9375 -0.0748 0.0103  -0.0747 41  ASP G CB  
11695 C CG  . ASP G  41  ? 1.3822 1.2980 1.3106 -0.0825 0.0098  -0.0794 41  ASP G CG  
11696 O OD1 . ASP G  41  ? 1.3407 1.2559 1.2657 -0.0901 0.0071  -0.0823 41  ASP G OD1 
11697 O OD2 . ASP G  41  ? 1.4244 1.3393 1.3484 -0.0810 0.0122  -0.0801 41  ASP G OD2 
11698 N N   . LYS G  42  ? 1.0152 0.9282 0.9595 -0.0877 0.0099  -0.0802 42  LYS G N   
11699 C CA  . LYS G  42  ? 1.0619 0.9689 1.0056 -0.0935 0.0151  -0.0852 42  LYS G CA  
11700 C C   . LYS G  42  ? 1.0470 0.9551 0.9975 -0.0948 0.0130  -0.0843 42  LYS G C   
11701 O O   . LYS G  42  ? 0.9736 0.8869 0.9236 -0.0988 0.0054  -0.0831 42  LYS G O   
11702 C CB  . LYS G  42  ? 1.1187 1.0246 1.0524 -0.1028 0.0132  -0.0901 42  LYS G CB  
11703 C CG  . LYS G  42  ? 1.4238 1.3216 1.3537 -0.1066 0.0220  -0.0960 42  LYS G CG  
11704 C CD  . LYS G  42  ? 1.6651 1.5622 1.5840 -0.1138 0.0204  -0.1000 42  LYS G CD  
11705 C CE  . LYS G  42  ? 1.5244 1.4254 1.4399 -0.1095 0.0173  -0.0969 42  LYS G CE  
11706 N NZ  . LYS G  42  ? 1.5997 1.5005 1.5042 -0.1166 0.0150  -0.1003 42  LYS G NZ  
11707 N N   . HIS G  43  ? 0.7877 0.6912 0.7449 -0.0913 0.0200  -0.0847 43  HIS G N   
11708 C CA  . HIS G  43  ? 0.9118 0.8154 0.8760 -0.0923 0.0193  -0.0842 43  HIS G CA  
11709 C C   . HIS G  43  ? 0.9805 0.8774 0.9430 -0.0990 0.0253  -0.0901 43  HIS G C   
11710 O O   . HIS G  43  ? 0.9506 0.8417 0.9088 -0.1003 0.0319  -0.0940 43  HIS G O   
11711 C CB  . HIS G  43  ? 0.8977 0.8011 0.8713 -0.0830 0.0227  -0.0797 43  HIS G CB  
11712 C CG  . HIS G  43  ? 0.8618 0.7589 0.8372 -0.0782 0.0324  -0.0809 43  HIS G CG  
11713 N ND1 . HIS G  43  ? 0.8740 0.7649 0.8542 -0.0782 0.0399  -0.0831 43  HIS G ND1 
11714 C CD2 . HIS G  43  ? 0.8655 0.7616 0.8388 -0.0732 0.0359  -0.0799 43  HIS G CD2 
11715 C CE1 . HIS G  43  ? 0.9632 0.8496 0.9443 -0.0733 0.0476  -0.0833 43  HIS G CE1 
11716 N NE2 . HIS G  43  ? 0.9484 0.8379 0.9254 -0.0702 0.0453  -0.0813 43  HIS G NE2 
11717 N N   . ASN G  44  ? 0.9010 0.7986 0.8672 -0.1032 0.0231  -0.0910 44  ASN G N   
11718 C CA  . ASN G  44  ? 0.9129 0.8045 0.8777 -0.1102 0.0284  -0.0968 44  ASN G CA  
11719 C C   . ASN G  44  ? 0.9851 0.8700 0.9572 -0.1054 0.0380  -0.0975 44  ASN G C   
11720 O O   . ASN G  44  ? 0.9584 0.8375 0.9302 -0.1104 0.0437  -0.1024 44  ASN G O   
11721 C CB  . ASN G  44  ? 0.7830 0.6785 0.7481 -0.1177 0.0218  -0.0978 44  ASN G CB  
11722 C CG  . ASN G  44  ? 0.9468 0.8461 0.9219 -0.1131 0.0187  -0.0930 44  ASN G CG  
11723 O OD1 . ASN G  44  ? 1.1001 1.0034 1.0770 -0.1180 0.0131  -0.0929 44  ASN G OD1 
11724 N ND2 . ASN G  44  ? 1.0228 0.9212 1.0045 -0.1037 0.0223  -0.0891 44  ASN G ND2 
11725 N N   . GLY G  45  ? 0.9151 0.8009 0.8936 -0.0958 0.0398  -0.0925 45  GLY G N   
11726 C CA  . GLY G  45  ? 1.0127 0.8927 0.9984 -0.0903 0.0488  -0.0923 45  GLY G CA  
11727 C C   . GLY G  45  ? 1.0067 0.8849 0.9989 -0.0926 0.0501  -0.0932 45  GLY G C   
11728 O O   . GLY G  45  ? 0.9074 0.7790 0.9037 -0.0915 0.0585  -0.0952 45  GLY G O   
11729 N N   . LYS G  46  ? 0.9863 0.8705 0.9798 -0.0958 0.0419  -0.0916 46  LYS G N   
11730 C CA  . LYS G  46  ? 0.9160 0.7996 0.9162 -0.0981 0.0420  -0.0920 46  LYS G CA  
11731 C C   . LYS G  46  ? 0.8705 0.7604 0.8780 -0.0924 0.0362  -0.0858 46  LYS G C   
11732 O O   . LYS G  46  ? 0.9791 0.8756 0.9844 -0.0912 0.0286  -0.0824 46  LYS G O   
11733 C CB  . LYS G  46  ? 1.0695 0.9545 1.0648 -0.1090 0.0376  -0.0965 46  LYS G CB  
11734 C CG  . LYS G  46  ? 1.0849 0.9637 1.0724 -0.1162 0.0430  -0.1033 46  LYS G CG  
11735 C CD  . LYS G  46  ? 1.4202 1.3023 1.4014 -0.1269 0.0365  -0.1068 46  LYS G CD  
11736 C CE  . LYS G  46  ? 1.6109 1.4865 1.5844 -0.1349 0.0423  -0.1142 46  LYS G CE  
11737 N NZ  . LYS G  46  ? 1.5082 1.3878 1.4746 -0.1456 0.0353  -0.1173 46  LYS G NZ  
11738 N N   . LEU G  47  ? 0.9572 0.8449 0.9734 -0.0889 0.0400  -0.0844 47  LEU G N   
11739 C CA  . LEU G  47  ? 1.0045 0.8978 1.0279 -0.0849 0.0345  -0.0792 47  LEU G CA  
11740 C C   . LEU G  47  ? 0.8987 0.7955 0.9229 -0.0929 0.0286  -0.0809 47  LEU G C   
11741 O O   . LEU G  47  ? 0.8984 0.7920 0.9272 -0.0958 0.0319  -0.0832 47  LEU G O   
11742 C CB  . LEU G  47  ? 0.7995 0.6891 0.8318 -0.0776 0.0412  -0.0767 47  LEU G CB  
11743 C CG  . LEU G  47  ? 0.7802 0.6670 0.8128 -0.0691 0.0471  -0.0742 47  LEU G CG  
11744 C CD1 . LEU G  47  ? 0.7538 0.6388 0.7956 -0.0615 0.0517  -0.0704 47  LEU G CD1 
11745 C CD2 . LEU G  47  ? 0.7716 0.6641 0.7994 -0.0659 0.0412  -0.0709 47  LEU G CD2 
11746 N N   . CYS G  48  ? 0.9690 0.8725 0.9887 -0.0965 0.0197  -0.0796 48  CYS G N   
11747 C CA  . CYS G  48  ? 1.0965 1.0041 1.1156 -0.1048 0.0132  -0.0812 48  CYS G CA  
11748 C C   . CYS G  48  ? 1.0527 0.9664 1.0802 -0.1021 0.0072  -0.0761 48  CYS G C   
11749 O O   . CYS G  48  ? 1.0411 0.9563 1.0738 -0.0939 0.0074  -0.0713 48  CYS G O   
11750 C CB  . CYS G  48  ? 1.0278 0.9395 1.0373 -0.1107 0.0067  -0.0825 48  CYS G CB  
11751 S SG  . CYS G  48  ? 1.5388 1.4442 1.5377 -0.1133 0.0128  -0.0878 48  CYS G SG  
11752 N N   . LYS G  49  ? 0.8444 0.7618 0.8732 -0.1092 0.0019  -0.0771 49  LYS G N   
11753 C CA  . LYS G  49  ? 0.9115 0.8351 0.9485 -0.1073 -0.0041 -0.0724 49  LYS G CA  
11754 C C   . LYS G  49  ? 0.8815 0.8120 0.9162 -0.1045 -0.0118 -0.0677 49  LYS G C   
11755 O O   . LYS G  49  ? 1.0786 1.0101 1.1047 -0.1071 -0.0142 -0.0689 49  LYS G O   
11756 C CB  . LYS G  49  ? 0.9800 0.9062 1.0191 -0.1159 -0.0079 -0.0746 49  LYS G CB  
11757 C CG  . LYS G  49  ? 1.0737 0.9929 1.1122 -0.1210 -0.0006 -0.0807 49  LYS G CG  
11758 C CD  . LYS G  49  ? 1.1872 1.1098 1.2282 -0.1296 -0.0047 -0.0828 49  LYS G CD  
11759 C CE  . LYS G  49  ? 1.2401 1.1590 1.2727 -0.1392 -0.0023 -0.0897 49  LYS G CE  
11760 N NZ  . LYS G  49  ? 1.2421 1.1659 1.2759 -0.1484 -0.0080 -0.0914 49  LYS G NZ  
11761 N N   . LEU G  50  ? 1.0695 1.0043 1.1119 -0.0994 -0.0153 -0.0623 50  LEU G N   
11762 C CA  . LEU G  50  ? 1.1493 1.0896 1.1904 -0.0952 -0.0212 -0.0576 50  LEU G CA  
11763 C C   . LEU G  50  ? 1.2469 1.1952 1.2884 -0.1001 -0.0309 -0.0552 50  LEU G C   
11764 O O   . LEU G  50  ? 1.3975 1.3495 1.4327 -0.1014 -0.0358 -0.0542 50  LEU G O   
11765 C CB  . LEU G  50  ? 1.0774 1.0175 1.1259 -0.0855 -0.0188 -0.0529 50  LEU G CB  
11766 C CG  . LEU G  50  ? 0.9610 0.9026 1.0064 -0.0787 -0.0195 -0.0496 50  LEU G CG  
11767 C CD1 . LEU G  50  ? 0.8519 0.7948 0.9055 -0.0704 -0.0188 -0.0445 50  LEU G CD1 
11768 C CD2 . LEU G  50  ? 0.9727 0.9202 1.0122 -0.0823 -0.0275 -0.0484 50  LEU G CD2 
11769 N N   . ARG G  51  ? 1.0714 1.0225 1.1203 -0.1028 -0.0336 -0.0541 51  ARG G N   
11770 C CA  . ARG G  51  ? 1.2480 1.2066 1.2974 -0.1087 -0.0425 -0.0523 51  ARG G CA  
11771 C C   . ARG G  51  ? 1.3181 1.2756 1.3634 -0.1185 -0.0425 -0.0576 51  ARG G C   
11772 O O   . ARG G  51  ? 1.5099 1.4676 1.5458 -0.1241 -0.0442 -0.0606 51  ARG G O   
11773 C CB  . ARG G  51  ? 1.3824 1.3456 1.4431 -0.1061 -0.0459 -0.0475 51  ARG G CB  
11774 C CG  . ARG G  51  ? 1.5351 1.4976 1.6012 -0.0962 -0.0437 -0.0430 51  ARG G CG  
11775 C CD  . ARG G  51  ? 1.8980 1.8669 1.9731 -0.0944 -0.0496 -0.0376 51  ARG G CD  
11776 N NE  . ARG G  51  ? 2.0811 2.0568 2.1528 -0.0973 -0.0578 -0.0350 51  ARG G NE  
11777 C CZ  . ARG G  51  ? 1.9558 1.9378 2.0312 -0.1027 -0.0647 -0.0331 51  ARG G CZ  
11778 N NH1 . ARG G  51  ? 1.7759 1.7585 1.8585 -0.1059 -0.0644 -0.0338 51  ARG G NH1 
11779 N NH2 . ARG G  51  ? 1.7714 1.7594 1.8435 -0.1048 -0.0718 -0.0304 51  ARG G NH2 
11780 N N   . GLY G  52  ? 1.1644 1.1207 1.2168 -0.1206 -0.0403 -0.0588 52  GLY G N   
11781 C CA  . GLY G  52  ? 1.2768 1.2303 1.3264 -0.1289 -0.0379 -0.0646 52  GLY G CA  
11782 C C   . GLY G  52  ? 1.3401 1.2872 1.3969 -0.1253 -0.0298 -0.0661 52  GLY G C   
11783 O O   . GLY G  52  ? 1.3342 1.2777 1.3912 -0.1308 -0.0261 -0.0707 52  GLY G O   
11784 N N   . VAL G  53  ? 1.2135 1.1593 1.2762 -0.1159 -0.0270 -0.0620 53  VAL G N   
11785 C CA  . VAL G  53  ? 0.9364 0.8766 1.0066 -0.1112 -0.0195 -0.0624 53  VAL G CA  
11786 C C   . VAL G  53  ? 0.9222 0.8542 0.9878 -0.1070 -0.0106 -0.0653 53  VAL G C   
11787 O O   . VAL G  53  ? 0.9105 0.8422 0.9702 -0.1033 -0.0105 -0.0643 53  VAL G O   
11788 C CB  . VAL G  53  ? 0.8840 0.8272 0.9636 -0.1032 -0.0211 -0.0562 53  VAL G CB  
11789 C CG1 . VAL G  53  ? 0.8400 0.7776 0.9276 -0.0991 -0.0136 -0.0566 53  VAL G CG1 
11790 C CG2 . VAL G  53  ? 0.6749 0.6266 0.7594 -0.1067 -0.0302 -0.0527 53  VAL G CG2 
11791 N N   . ALA G  54  ? 0.8950 0.8205 0.9635 -0.1077 -0.0030 -0.0687 54  ALA G N   
11792 C CA  . ALA G  54  ? 0.8502 0.7677 0.9153 -0.1040 0.0060  -0.0715 54  ALA G CA  
11793 C C   . ALA G  54  ? 0.8700 0.7854 0.9411 -0.0935 0.0103  -0.0671 54  ALA G C   
11794 O O   . ALA G  54  ? 0.8715 0.7897 0.9508 -0.0899 0.0084  -0.0631 54  ALA G O   
11795 C CB  . ALA G  54  ? 0.9471 0.8583 1.0128 -0.1095 0.0127  -0.0772 54  ALA G CB  
11796 N N   . PRO G  55  ? 0.7711 0.6816 0.8380 -0.0886 0.0162  -0.0676 55  PRO G N   
11797 C CA  . PRO G  55  ? 0.6737 0.5817 0.7455 -0.0788 0.0212  -0.0638 55  PRO G CA  
11798 C C   . PRO G  55  ? 0.8346 0.7367 0.9137 -0.0771 0.0289  -0.0650 55  PRO G C   
11799 O O   . PRO G  55  ? 0.9578 0.8558 1.0362 -0.0832 0.0325  -0.0699 55  PRO G O   
11800 C CB  . PRO G  55  ? 0.7127 0.6173 0.7770 -0.0760 0.0252  -0.0650 55  PRO G CB  
11801 C CG  . PRO G  55  ? 0.7206 0.6224 0.7779 -0.0845 0.0264  -0.0711 55  PRO G CG  
11802 C CD  . PRO G  55  ? 0.7111 0.6189 0.7680 -0.0921 0.0180  -0.0716 55  PRO G CD  
11803 N N   . LEU G  56  ? 0.8754 0.7770 0.9613 -0.0690 0.0315  -0.0606 56  LEU G N   
11804 C CA  . LEU G  56  ? 0.6902 0.5858 0.7829 -0.0664 0.0394  -0.0612 56  LEU G CA  
11805 C C   . LEU G  56  ? 0.7707 0.6597 0.8608 -0.0613 0.0480  -0.0619 56  LEU G C   
11806 O O   . LEU G  56  ? 0.8957 0.7855 0.9860 -0.0536 0.0490  -0.0579 56  LEU G O   
11807 C CB  . LEU G  56  ? 0.7288 0.6271 0.8303 -0.0604 0.0380  -0.0559 56  LEU G CB  
11808 C CG  . LEU G  56  ? 0.7239 0.6165 0.8332 -0.0569 0.0459  -0.0557 56  LEU G CG  
11809 C CD1 . LEU G  56  ? 0.8304 0.7204 0.9423 -0.0647 0.0476  -0.0604 56  LEU G CD1 
11810 C CD2 . LEU G  56  ? 0.8376 0.7334 0.9546 -0.0505 0.0440  -0.0501 56  LEU G CD2 
11811 N N   . HIS G  57  ? 0.7979 0.6807 0.8856 -0.0657 0.0542  -0.0671 57  HIS G N   
11812 C CA  . HIS G  57  ? 0.8138 0.6902 0.8993 -0.0613 0.0628  -0.0680 57  HIS G CA  
11813 C C   . HIS G  57  ? 0.9316 0.8022 1.0251 -0.0565 0.0711  -0.0670 57  HIS G C   
11814 O O   . HIS G  57  ? 0.9893 0.8563 1.0867 -0.0609 0.0743  -0.0701 57  HIS G O   
11815 C CB  . HIS G  57  ? 0.8353 0.7075 0.9134 -0.0684 0.0657  -0.0743 57  HIS G CB  
11816 C CG  . HIS G  57  ? 0.9410 0.8081 1.0153 -0.0640 0.0727  -0.0747 57  HIS G CG  
11817 N ND1 . HIS G  57  ? 0.9682 0.8279 1.0466 -0.0605 0.0827  -0.0755 57  HIS G ND1 
11818 C CD2 . HIS G  57  ? 0.9840 0.8526 1.0514 -0.0624 0.0712  -0.0743 57  HIS G CD2 
11819 C CE1 . HIS G  57  ? 1.0551 0.9121 1.1293 -0.0569 0.0870  -0.0754 57  HIS G CE1 
11820 N NE2 . HIS G  57  ? 1.1034 0.9658 1.1710 -0.0580 0.0801  -0.0748 57  HIS G NE2 
11821 N N   . LEU G  58  ? 1.0721 0.9418 1.1680 -0.0475 0.0747  -0.0625 58  LEU G N   
11822 C CA  . LEU G  58  ? 0.9866 0.8514 1.0901 -0.0420 0.0822  -0.0605 58  LEU G CA  
11823 C C   . LEU G  58  ? 1.0453 0.9018 1.1484 -0.0411 0.0925  -0.0634 58  LEU G C   
11824 O O   . LEU G  58  ? 1.0810 0.9324 1.1905 -0.0383 0.0995  -0.0629 58  LEU G O   
11825 C CB  . LEU G  58  ? 0.8273 0.6956 0.9342 -0.0328 0.0810  -0.0539 58  LEU G CB  
11826 C CG  . LEU G  58  ? 0.7226 0.5959 0.8355 -0.0315 0.0755  -0.0503 58  LEU G CG  
11827 C CD1 . LEU G  58  ? 0.8756 0.7528 0.9878 -0.0399 0.0682  -0.0532 58  LEU G CD1 
11828 C CD2 . LEU G  58  ? 0.8374 0.7161 0.9494 -0.0245 0.0712  -0.0447 58  LEU G CD2 
11829 N N   . GLY G  59  ? 1.0153 0.8704 1.1111 -0.0434 0.0936  -0.0662 59  GLY G N   
11830 C CA  . GLY G  59  ? 0.9824 0.8295 1.0775 -0.0428 0.1034  -0.0691 59  GLY G CA  
11831 C C   . GLY G  59  ? 1.0853 0.9299 1.1849 -0.0330 0.1099  -0.0642 59  GLY G C   
11832 O O   . GLY G  59  ? 1.1258 0.9743 1.2231 -0.0272 0.1075  -0.0601 59  GLY G O   
11833 N N   . LYS G  60  ? 1.2611 1.0992 1.3670 -0.0312 0.1183  -0.0646 60  LYS G N   
11834 C CA  . LYS G  60  ? 1.3159 1.1508 1.4263 -0.0222 0.1255  -0.0601 60  LYS G CA  
11835 C C   . LYS G  60  ? 1.1529 0.9925 1.2687 -0.0152 0.1223  -0.0537 60  LYS G C   
11836 O O   . LYS G  60  ? 1.2658 1.1042 1.3851 -0.0073 0.1271  -0.0492 60  LYS G O   
11837 C CB  . LYS G  60  ? 1.3776 1.2035 1.4929 -0.0229 0.1361  -0.0629 60  LYS G CB  
11838 C CG  . LYS G  60  ? 1.7794 1.6013 1.8987 -0.0142 0.1446  -0.0588 60  LYS G CG  
11839 C CD  . LYS G  60  ? 1.9175 1.7394 2.0309 -0.0122 0.1461  -0.0587 60  LYS G CD  
11840 C CE  . LYS G  60  ? 2.0183 1.8347 2.1271 -0.0200 0.1500  -0.0658 60  LYS G CE  
11841 N NZ  . LYS G  60  ? 1.9076 1.7238 2.0110 -0.0181 0.1518  -0.0658 60  LYS G NZ  
11842 N N   . CYS G  61  ? 1.1142 0.9593 1.2306 -0.0182 0.1142  -0.0533 61  CYS G N   
11843 C CA  . CYS G  61  ? 0.9756 0.8247 1.0975 -0.0125 0.1113  -0.0478 61  CYS G CA  
11844 C C   . CYS G  61  ? 0.9697 0.8273 1.0876 -0.0112 0.1017  -0.0447 61  CYS G C   
11845 O O   . CYS G  61  ? 1.1121 0.9729 1.2240 -0.0167 0.0957  -0.0474 61  CYS G O   
11846 C CB  . CYS G  61  ? 0.9609 0.8086 1.0892 -0.0162 0.1113  -0.0492 61  CYS G CB  
11847 S SG  . CYS G  61  ? 1.5011 1.3388 1.6344 -0.0186 0.1225  -0.0533 61  CYS G SG  
11848 N N   . ASN G  62  ? 0.8039 0.6648 0.9251 -0.0042 0.1004  -0.0390 62  ASN G N   
11849 C CA  . ASN G  62  ? 0.9181 0.7868 1.0365 -0.0026 0.0917  -0.0358 62  ASN G CA  
11850 C C   . ASN G  62  ? 0.8724 0.7445 0.9959 -0.0040 0.0866  -0.0344 62  ASN G C   
11851 O O   . ASN G  62  ? 0.8432 0.7117 0.9727 -0.0055 0.0900  -0.0355 62  ASN G O   
11852 C CB  . ASN G  62  ? 0.9487 0.8194 1.0663 0.0061  0.0931  -0.0304 62  ASN G CB  
11853 C CG  . ASN G  62  ? 0.8831 0.7508 1.0076 0.0125  0.0993  -0.0265 62  ASN G CG  
11854 O OD1 . ASN G  62  ? 0.9107 0.7766 1.0411 0.0112  0.1004  -0.0268 62  ASN G OD1 
11855 N ND2 . ASN G  62  ? 0.8867 0.7541 1.0108 0.0195  0.1035  -0.0227 62  ASN G ND2 
11856 N N   . ILE G  63  ? 0.7446 0.6235 0.8659 -0.0035 0.0785  -0.0319 63  ILE G N   
11857 C CA  . ILE G  63  ? 0.6968 0.5796 0.8230 -0.0049 0.0732  -0.0304 63  ILE G CA  
11858 C C   . ILE G  63  ? 0.7067 0.5864 0.8410 -0.0003 0.0785  -0.0276 63  ILE G C   
11859 O O   . ILE G  63  ? 0.7171 0.5956 0.8569 -0.0038 0.0784  -0.0290 63  ILE G O   
11860 C CB  . ILE G  63  ? 0.6955 0.5856 0.8191 -0.0025 0.0654  -0.0268 63  ILE G CB  
11861 C CG1 . ILE G  63  ? 0.6971 0.5905 0.8128 -0.0074 0.0598  -0.0295 63  ILE G CG1 
11862 C CG2 . ILE G  63  ? 0.6508 0.5445 0.7801 -0.0036 0.0605  -0.0249 63  ILE G CG2 
11863 C CD1 . ILE G  63  ? 0.8001 0.6944 0.9156 -0.0161 0.0555  -0.0336 63  ILE G CD1 
11864 N N   . ALA G  64  ? 0.7096 0.5881 0.8446 0.0073  0.0830  -0.0237 64  ALA G N   
11865 C CA  . ALA G  64  ? 0.7876 0.6631 0.9296 0.0123  0.0883  -0.0206 64  ALA G CA  
11866 C C   . ALA G  64  ? 0.7878 0.6567 0.9348 0.0088  0.0946  -0.0241 64  ALA G C   
11867 O O   . ALA G  64  ? 0.8237 0.6918 0.9769 0.0076  0.0947  -0.0239 64  ALA G O   
11868 C CB  . ALA G  64  ? 0.7161 0.5908 0.8571 0.0204  0.0931  -0.0163 64  ALA G CB  
11869 N N   . GLY G  65  ? 0.8375 0.7015 0.9818 0.0072  0.1001  -0.0272 65  GLY G N   
11870 C CA  . GLY G  65  ? 0.8028 0.6599 0.9513 0.0038  0.1068  -0.0309 65  GLY G CA  
11871 C C   . GLY G  65  ? 0.8299 0.6878 0.9801 -0.0045 0.1026  -0.0352 65  GLY G C   
11872 O O   . GLY G  65  ? 0.9454 0.7999 1.1019 -0.0063 0.1061  -0.0364 65  GLY G O   
11873 N N   . TRP G  66  ? 0.6695 0.5323 0.8141 -0.0097 0.0950  -0.0373 66  TRP G N   
11874 C CA  . TRP G  66  ? 0.8608 0.7253 1.0064 -0.0182 0.0903  -0.0414 66  TRP G CA  
11875 C C   . TRP G  66  ? 0.8329 0.7008 0.9856 -0.0181 0.0864  -0.0389 66  TRP G C   
11876 O O   . TRP G  66  ? 0.9396 0.8057 1.0970 -0.0231 0.0872  -0.0417 66  TRP G O   
11877 C CB  . TRP G  66  ? 0.8522 0.7217 0.9899 -0.0232 0.0827  -0.0435 66  TRP G CB  
11878 C CG  . TRP G  66  ? 0.8762 0.7500 1.0151 -0.0308 0.0756  -0.0458 66  TRP G CG  
11879 C CD1 . TRP G  66  ? 0.8923 0.7634 1.0333 -0.0382 0.0769  -0.0505 66  TRP G CD1 
11880 C CD2 . TRP G  66  ? 0.8969 0.7784 1.0350 -0.0320 0.0662  -0.0435 66  TRP G CD2 
11881 N NE1 . TRP G  66  ? 0.9418 0.8190 1.0835 -0.0438 0.0685  -0.0510 66  TRP G NE1 
11882 C CE2 . TRP G  66  ? 0.8340 0.7175 0.9741 -0.0400 0.0620  -0.0466 66  TRP G CE2 
11883 C CE3 . TRP G  66  ? 0.8950 0.7820 1.0310 -0.0271 0.0610  -0.0390 66  TRP G CE3 
11884 C CZ2 . TRP G  66  ? 0.7622 0.6532 0.9027 -0.0429 0.0528  -0.0451 66  TRP G CZ2 
11885 C CZ3 . TRP G  66  ? 0.8889 0.7827 1.0252 -0.0301 0.0522  -0.0377 66  TRP G CZ3 
11886 C CH2 . TRP G  66  ? 0.8171 0.7129 0.9558 -0.0378 0.0482  -0.0406 66  TRP G CH2 
11887 N N   . ILE G  67  ? 0.8356 0.7083 0.9892 -0.0126 0.0824  -0.0338 67  ILE G N   
11888 C CA  . ILE G  67  ? 0.8339 0.7101 0.9942 -0.0122 0.0786  -0.0313 67  ILE G CA  
11889 C C   . ILE G  67  ? 0.9004 0.7718 1.0683 -0.0077 0.0856  -0.0292 67  ILE G C   
11890 O O   . ILE G  67  ? 0.8583 0.7297 1.0330 -0.0102 0.0852  -0.0296 67  ILE G O   
11891 C CB  . ILE G  67  ? 0.7468 0.6296 0.9053 -0.0081 0.0720  -0.0267 67  ILE G CB  
11892 C CG1 . ILE G  67  ? 1.0305 0.9171 1.1803 -0.0104 0.0667  -0.0280 67  ILE G CG1 
11893 C CG2 . ILE G  67  ? 0.7033 0.5906 0.8678 -0.0103 0.0663  -0.0252 67  ILE G CG2 
11894 C CD1 . ILE G  67  ? 1.1711 1.0639 1.3189 -0.0063 0.0608  -0.0237 67  ILE G CD1 
11895 N N   . LEU G  68  ? 0.8078 0.6755 0.9750 -0.0011 0.0922  -0.0268 68  LEU G N   
11896 C CA  . LEU G  68  ? 0.7928 0.6557 0.9668 0.0037  0.0994  -0.0245 68  LEU G CA  
11897 C C   . LEU G  68  ? 0.8871 0.7437 1.0651 -0.0012 0.1052  -0.0290 68  LEU G C   
11898 O O   . LEU G  68  ? 0.9420 0.7957 1.1272 -0.0002 0.1091  -0.0282 68  LEU G O   
11899 C CB  . LEU G  68  ? 0.7065 0.5671 0.8784 0.0117  0.1050  -0.0208 68  LEU G CB  
11900 C CG  . LEU G  68  ? 0.7577 0.6237 0.9276 0.0179  0.1008  -0.0154 68  LEU G CG  
11901 C CD1 . LEU G  68  ? 0.7315 0.5949 0.9003 0.0256  0.1072  -0.0116 68  LEU G CD1 
11902 C CD2 . LEU G  68  ? 0.5509 0.4195 0.7272 0.0187  0.0979  -0.0129 68  LEU G CD2 
11903 N N   . GLY G  69  ? 0.8732 0.7276 1.0464 -0.0065 0.1062  -0.0338 69  GLY G N   
11904 C CA  . GLY G  69  ? 0.8829 0.7312 1.0590 -0.0119 0.1118  -0.0387 69  GLY G CA  
11905 C C   . GLY G  69  ? 0.9859 0.8266 1.1622 -0.0080 0.1219  -0.0390 69  GLY G C   
11906 O O   . GLY G  69  ? 0.9934 0.8283 1.1755 -0.0083 0.1288  -0.0402 69  GLY G O   
11907 N N   . ASN G  70  ? 1.0379 0.8787 1.2082 -0.0042 0.1230  -0.0376 70  ASN G N   
11908 C CA  . ASN G  70  ? 1.0981 0.9320 1.2682 -0.0006 0.1324  -0.0378 70  ASN G CA  
11909 C C   . ASN G  70  ? 1.2302 1.0576 1.4013 -0.0076 0.1378  -0.0441 70  ASN G C   
11910 O O   . ASN G  70  ? 1.2577 1.0866 1.4247 -0.0153 0.1335  -0.0489 70  ASN G O   
11911 C CB  . ASN G  70  ? 1.0730 0.9089 1.2358 0.0025  0.1314  -0.0364 70  ASN G CB  
11912 C CG  . ASN G  70  ? 1.1347 0.9645 1.2982 0.0080  0.1410  -0.0350 70  ASN G CG  
11913 O OD1 . ASN G  70  ? 1.2080 1.0308 1.3741 0.0056  0.1484  -0.0383 70  ASN G OD1 
11914 N ND2 . ASN G  70  ? 0.9775 0.8100 1.1387 0.0152  0.1408  -0.0299 70  ASN G ND2 
11915 N N   . PRO G  71  ? 1.3460 1.1662 1.5225 -0.0050 0.1473  -0.0440 71  PRO G N   
11916 C CA  . PRO G  71  ? 1.2776 1.0908 1.4558 -0.0113 0.1537  -0.0500 71  PRO G CA  
11917 C C   . PRO G  71  ? 1.2826 1.0944 1.4531 -0.0165 0.1537  -0.0549 71  PRO G C   
11918 O O   . PRO G  71  ? 1.5078 1.3173 1.6772 -0.0248 0.1539  -0.0609 71  PRO G O   
11919 C CB  . PRO G  71  ? 1.2563 1.0622 1.4401 -0.0048 0.1645  -0.0474 71  PRO G CB  
11920 C CG  . PRO G  71  ? 1.2247 1.0344 1.4121 0.0030  0.1624  -0.0405 71  PRO G CG  
11921 C CD  . PRO G  71  ? 1.2519 1.0701 1.4333 0.0041  0.1527  -0.0381 71  PRO G CD  
11922 N N   . GLU G  72  ? 1.2855 1.0989 1.4509 -0.0118 0.1535  -0.0524 72  GLU G N   
11923 C CA  . GLU G  72  ? 1.3830 1.1951 1.5410 -0.0161 0.1538  -0.0566 72  GLU G CA  
11924 C C   . GLU G  72  ? 1.2292 1.0489 1.3804 -0.0210 0.1429  -0.0580 72  GLU G C   
11925 O O   . GLU G  72  ? 1.2797 1.0999 1.4239 -0.0239 0.1415  -0.0607 72  GLU G O   
11926 C CB  . GLU G  72  ? 1.2914 1.1011 1.4476 -0.0087 0.1595  -0.0533 72  GLU G CB  
11927 C CG  . GLU G  72  ? 1.5008 1.3018 1.6631 -0.0052 0.1712  -0.0529 72  GLU G CG  
11928 C CD  . GLU G  72  ? 1.7418 1.5356 1.9043 -0.0131 0.1771  -0.0601 72  GLU G CD  
11929 O OE1 . GLU G  72  ? 1.6508 1.4436 1.8070 -0.0181 0.1767  -0.0645 72  GLU G OE1 
11930 O OE2 . GLU G  72  ? 1.6802 1.4692 1.8492 -0.0144 0.1822  -0.0614 72  GLU G OE2 
11931 N N   . CYS G  73  ? 1.4623 1.2880 1.6160 -0.0219 0.1354  -0.0562 73  CYS G N   
11932 C CA  . CYS G  73  ? 1.4918 1.3249 1.6401 -0.0268 0.1249  -0.0572 73  CYS G CA  
11933 C C   . CYS G  73  ? 1.7084 1.5432 1.8596 -0.0350 0.1208  -0.0609 73  CYS G C   
11934 O O   . CYS G  73  ? 1.6999 1.5417 1.8499 -0.0377 0.1117  -0.0601 73  CYS G O   
11935 C CB  . CYS G  73  ? 1.2903 1.1306 1.4381 -0.0204 0.1183  -0.0510 73  CYS G CB  
11936 S SG  . CYS G  73  ? 1.3424 1.1829 1.4852 -0.0122 0.1210  -0.0470 73  CYS G SG  
11937 N N   . GLU G  74  ? 1.7663 1.5945 1.9214 -0.0388 0.1276  -0.0649 74  GLU G N   
11938 C CA  . GLU G  74  ? 1.9324 1.7613 2.0888 -0.0481 0.1245  -0.0698 74  GLU G CA  
11939 C C   . GLU G  74  ? 2.0742 1.9040 2.2218 -0.0555 0.1215  -0.0750 74  GLU G C   
11940 O O   . GLU G  74  ? 2.0694 1.8978 2.2110 -0.0530 0.1234  -0.0749 74  GLU G O   
11941 C CB  . GLU G  74  ? 1.9345 1.7557 2.0977 -0.0497 0.1336  -0.0726 74  GLU G CB  
11942 C CG  . GLU G  74  ? 2.0520 1.8749 2.2193 -0.0576 0.1303  -0.0761 74  GLU G CG  
11943 C CD  . GLU G  74  ? 2.1902 2.0060 2.3656 -0.0574 0.1390  -0.0775 74  GLU G CD  
11944 O OE1 . GLU G  74  ? 2.1430 1.9530 2.3212 -0.0504 0.1473  -0.0750 74  GLU G OE1 
11945 O OE2 . GLU G  74  ? 2.0860 1.9022 2.2651 -0.0642 0.1377  -0.0809 74  GLU G OE2 
11946 N N   . SER G  75  ? 2.2374 2.0698 2.3840 -0.0646 0.1165  -0.0793 75  SER G N   
11947 C CA  . SER G  75  ? 2.4020 2.2348 2.5402 -0.0729 0.1140  -0.0848 75  SER G CA  
11948 C C   . SER G  75  ? 2.4723 2.3134 2.6036 -0.0740 0.1037  -0.0831 75  SER G C   
11949 O O   . SER G  75  ? 2.4120 2.2534 2.5353 -0.0798 0.1017  -0.0870 75  SER G O   
11950 C CB  . SER G  75  ? 2.3470 2.1714 2.4816 -0.0722 0.1236  -0.0881 75  SER G CB  
11951 O OG  . SER G  75  ? 2.1810 2.0045 2.3079 -0.0811 0.1225  -0.0943 75  SER G OG  
11952 N N   . LEU G  76  ? 2.7174 2.5649 2.8516 -0.0686 0.0974  -0.0772 76  LEU G N   
11953 C CA  . LEU G  76  ? 2.6642 2.5196 2.7926 -0.0690 0.0878  -0.0751 76  LEU G CA  
11954 C C   . LEU G  76  ? 2.6683 2.5314 2.8014 -0.0674 0.0795  -0.0705 76  LEU G C   
11955 O O   . LEU G  76  ? 2.6025 2.4689 2.7367 -0.0601 0.0772  -0.0651 76  LEU G O   
11956 C CB  . LEU G  76  ? 2.5684 2.4232 2.6921 -0.0617 0.0897  -0.0720 76  LEU G CB  
11957 C CG  . LEU G  76  ? 2.4170 2.2779 2.5328 -0.0617 0.0821  -0.0706 76  LEU G CG  
11958 C CD1 . LEU G  76  ? 1.9439 1.8053 2.0603 -0.0517 0.0839  -0.0651 76  LEU G CD1 
11959 C CD2 . LEU G  76  ? 2.4164 2.2858 2.5321 -0.0659 0.0714  -0.0693 76  LEU G CD2 
11960 N N   . SER G  77  ? 2.4118 2.2780 2.5480 -0.0746 0.0752  -0.0727 77  SER G N   
11961 C CA  . SER G  77  ? 2.4027 2.2756 2.5451 -0.0734 0.0683  -0.0685 77  SER G CA  
11962 C C   . SER G  77  ? 2.4142 2.2936 2.5555 -0.0824 0.0597  -0.0707 77  SER G C   
11963 O O   . SER G  77  ? 2.2568 2.1431 2.4020 -0.0816 0.0525  -0.0669 77  SER G O   
11964 C CB  . SER G  77  ? 2.3743 2.2431 2.5265 -0.0701 0.0745  -0.0673 77  SER G CB  
11965 O OG  . SER G  77  ? 2.2087 2.0747 2.3637 -0.0778 0.0768  -0.0723 77  SER G OG  
11966 N N   . THR G  78  ? 3.3591 3.2365 3.4952 -0.0909 0.0605  -0.0767 78  THR G N   
11967 C CA  . THR G  78  ? 3.3887 3.2721 3.5232 -0.1003 0.0527  -0.0792 78  THR G CA  
11968 C C   . THR G  78  ? 3.1301 3.0209 3.2585 -0.1000 0.0436  -0.0763 78  THR G C   
11969 O O   . THR G  78  ? 2.9652 2.8573 3.0851 -0.1057 0.0407  -0.0795 78  THR G O   
11970 C CB  . THR G  78  ? 2.9236 2.8026 3.0524 -0.1096 0.0562  -0.0866 78  THR G CB  
11971 O OG1 . THR G  78  ? 2.8996 2.7747 3.0192 -0.1088 0.0594  -0.0888 78  THR G OG1 
11972 C CG2 . THR G  78  ? 1.8473 1.7188 1.9824 -0.1104 0.0652  -0.0897 78  THR G CG2 
11973 N N   . ALA G  79  ? 2.2545 2.1500 2.3876 -0.0934 0.0395  -0.0702 79  ALA G N   
11974 C CA  . ALA G  79  ? 1.9138 1.8160 2.0422 -0.0915 0.0317  -0.0667 79  ALA G CA  
11975 C C   . ALA G  79  ? 1.6887 1.5981 1.8247 -0.0903 0.0246  -0.0618 79  ALA G C   
11976 O O   . ALA G  79  ? 1.6275 1.5360 1.7714 -0.0841 0.0272  -0.0583 79  ALA G O   
11977 C CB  . ALA G  79  ? 1.8162 1.7158 1.9409 -0.0828 0.0351  -0.0638 79  ALA G CB  
11978 N N   . SER G  80  ? 1.2262 1.1429 1.3599 -0.0962 0.0158  -0.0616 80  SER G N   
11979 C CA  . SER G  80  ? 1.1150 1.0393 1.2558 -0.0953 0.0085  -0.0567 80  SER G CA  
11980 C C   . SER G  80  ? 1.0307 0.9594 1.1679 -0.0900 0.0034  -0.0521 80  SER G C   
11981 O O   . SER G  80  ? 1.0020 0.9354 1.1454 -0.0861 -0.0006 -0.0471 80  SER G O   
11982 C CB  . SER G  80  ? 1.3354 1.2655 1.4766 -0.1051 0.0017  -0.0588 80  SER G CB  
11983 O OG  . SER G  80  ? 1.4325 1.3582 1.5748 -0.1112 0.0065  -0.0641 80  SER G OG  
11984 N N   . SER G  81  ? 0.9957 0.9228 1.1231 -0.0901 0.0039  -0.0540 81  SER G N   
11985 C CA  . SER G  81  ? 0.9606 0.8917 1.0835 -0.0858 -0.0007 -0.0502 81  SER G CA  
11986 C C   . SER G  81  ? 0.8894 0.8163 1.0020 -0.0850 0.0028  -0.0530 81  SER G C   
11987 O O   . SER G  81  ? 0.8117 0.7338 0.9199 -0.0896 0.0072  -0.0581 81  SER G O   
11988 C CB  . SER G  81  ? 0.9391 0.8788 1.0613 -0.0911 -0.0107 -0.0485 81  SER G CB  
11989 O OG  . SER G  81  ? 0.9245 0.8649 1.0407 -0.1003 -0.0129 -0.0532 81  SER G OG  
11990 N N   . TRP G  82  ? 0.7877 0.7164 0.8968 -0.0792 0.0009  -0.0496 82  TRP G N   
11991 C CA  . TRP G  82  ? 0.7315 0.6572 0.8312 -0.0781 0.0036  -0.0517 82  TRP G CA  
11992 C C   . TRP G  82  ? 0.6886 0.6189 0.7845 -0.0736 -0.0015 -0.0476 82  TRP G C   
11993 O O   . TRP G  82  ? 0.7326 0.6652 0.8336 -0.0672 -0.0026 -0.0429 82  TRP G O   
11994 C CB  . TRP G  82  ? 0.7098 0.6274 0.8099 -0.0728 0.0135  -0.0530 82  TRP G CB  
11995 C CG  . TRP G  82  ? 0.7249 0.6419 0.8322 -0.0640 0.0163  -0.0483 82  TRP G CG  
11996 C CD1 . TRP G  82  ? 0.7949 0.7135 0.9010 -0.0566 0.0158  -0.0442 82  TRP G CD1 
11997 C CD2 . TRP G  82  ? 0.7430 0.6575 0.8594 -0.0618 0.0203  -0.0473 82  TRP G CD2 
11998 N NE1 . TRP G  82  ? 0.7812 0.6984 0.8949 -0.0501 0.0191  -0.0407 82  TRP G NE1 
11999 C CE2 . TRP G  82  ? 0.7801 0.6947 0.9003 -0.0531 0.0220  -0.0425 82  TRP G CE2 
12000 C CE3 . TRP G  82  ? 0.7797 0.6919 0.9015 -0.0666 0.0227  -0.0501 82  TRP G CE3 
12001 C CZ2 . TRP G  82  ? 0.7555 0.6680 0.8844 -0.0489 0.0260  -0.0403 82  TRP G CZ2 
12002 C CZ3 . TRP G  82  ? 0.7805 0.6905 0.9113 -0.0624 0.0267  -0.0479 82  TRP G CZ3 
12003 C CH2 . TRP G  82  ? 0.5726 0.4826 0.7068 -0.0536 0.0284  -0.0430 82  TRP G CH2 
12004 N N   . SER G  83  ? 0.7790 0.7105 0.8657 -0.0772 -0.0042 -0.0497 83  SER G N   
12005 C CA  . SER G  83  ? 0.7713 0.7072 0.8536 -0.0739 -0.0090 -0.0464 83  SER G CA  
12006 C C   . SER G  83  ? 0.6755 0.6080 0.7570 -0.0651 -0.0037 -0.0443 83  SER G C   
12007 O O   . SER G  83  ? 0.8174 0.7535 0.8999 -0.0598 -0.0068 -0.0400 83  SER G O   
12008 C CB  . SER G  83  ? 0.7718 0.7092 0.8442 -0.0803 -0.0128 -0.0496 83  SER G CB  
12009 O OG  . SER G  83  ? 0.7778 0.7087 0.8446 -0.0827 -0.0062 -0.0547 83  SER G OG  
12010 N N   . TYR G  84  ? 0.5520 0.4777 0.6319 -0.0635 0.0043  -0.0472 84  TYR G N   
12011 C CA  . TYR G  84  ? 0.7010 0.6235 0.7803 -0.0553 0.0098  -0.0452 84  TYR G CA  
12012 C C   . TYR G  84  ? 0.7681 0.6832 0.8503 -0.0534 0.0191  -0.0475 84  TYR G C   
12013 O O   . TYR G  84  ? 0.7743 0.6862 0.8575 -0.0591 0.0214  -0.0514 84  TYR G O   
12014 C CB  . TYR G  84  ? 0.6403 0.5635 0.7104 -0.0549 0.0085  -0.0459 84  TYR G CB  
12015 C CG  . TYR G  84  ? 0.6328 0.5527 0.6957 -0.0616 0.0105  -0.0514 84  TYR G CG  
12016 C CD1 . TYR G  84  ? 0.6609 0.5747 0.7205 -0.0595 0.0182  -0.0539 84  TYR G CD1 
12017 C CD2 . TYR G  84  ? 0.7027 0.6256 0.7620 -0.0700 0.0048  -0.0540 84  TYR G CD2 
12018 C CE1 . TYR G  84  ? 0.6413 0.5516 0.6943 -0.0656 0.0204  -0.0591 84  TYR G CE1 
12019 C CE2 . TYR G  84  ? 0.6612 0.5809 0.7134 -0.0764 0.0068  -0.0593 84  TYR G CE2 
12020 C CZ  . TYR G  84  ? 0.7043 0.6175 0.7533 -0.0741 0.0148  -0.0619 84  TYR G CZ  
12021 O OH  . TYR G  84  ? 0.7318 0.6412 0.7738 -0.0804 0.0174  -0.0673 84  TYR G OH  
12022 N N   . ILE G  85  ? 0.6088 0.5211 0.6924 -0.0456 0.0244  -0.0451 85  ILE G N   
12023 C CA  . ILE G  85  ? 0.7025 0.6078 0.7893 -0.0430 0.0336  -0.0466 85  ILE G CA  
12024 C C   . ILE G  85  ? 0.8193 0.7204 0.8998 -0.0410 0.0390  -0.0484 85  ILE G C   
12025 O O   . ILE G  85  ? 0.8375 0.7411 0.9141 -0.0367 0.0375  -0.0460 85  ILE G O   
12026 C CB  . ILE G  85  ? 0.6676 0.5724 0.7624 -0.0355 0.0365  -0.0420 85  ILE G CB  
12027 C CG1 . ILE G  85  ? 0.6307 0.5389 0.7325 -0.0378 0.0320  -0.0406 85  ILE G CG1 
12028 C CG2 . ILE G  85  ? 0.6389 0.5364 0.7367 -0.0324 0.0462  -0.0432 85  ILE G CG2 
12029 C CD1 . ILE G  85  ? 0.6581 0.5659 0.7676 -0.0309 0.0347  -0.0362 85  ILE G CD1 
12030 N N   . VAL G  86  ? 0.7326 0.6274 0.8123 -0.0443 0.0455  -0.0528 86  VAL G N   
12031 C CA  . VAL G  86  ? 0.7563 0.6464 0.8311 -0.0424 0.0517  -0.0547 86  VAL G CA  
12032 C C   . VAL G  86  ? 0.7553 0.6393 0.8355 -0.0366 0.0611  -0.0537 86  VAL G C   
12033 O O   . VAL G  86  ? 0.7737 0.6536 0.8591 -0.0386 0.0653  -0.0555 86  VAL G O   
12034 C CB  . VAL G  86  ? 0.6962 0.5833 0.7647 -0.0508 0.0527  -0.0608 86  VAL G CB  
12035 C CG1 . VAL G  86  ? 0.5968 0.4785 0.6611 -0.0485 0.0600  -0.0627 86  VAL G CG1 
12036 C CG2 . VAL G  86  ? 0.8267 0.7199 0.8891 -0.0564 0.0436  -0.0616 86  VAL G CG2 
12037 N N   . GLU G  87  ? 0.8613 0.7449 0.9405 -0.0294 0.0642  -0.0506 87  GLU G N   
12038 C CA  . GLU G  87  ? 0.7198 0.5979 0.8037 -0.0234 0.0731  -0.0490 87  GLU G CA  
12039 C C   . GLU G  87  ? 0.8820 0.7562 0.9609 -0.0226 0.0787  -0.0511 87  GLU G C   
12040 O O   . GLU G  87  ? 0.9943 0.8719 1.0671 -0.0223 0.0752  -0.0507 87  GLU G O   
12041 C CB  . GLU G  87  ? 0.8122 0.6940 0.9002 -0.0149 0.0722  -0.0427 87  GLU G CB  
12042 C CG  . GLU G  87  ? 0.8554 0.7341 0.9519 -0.0112 0.0770  -0.0405 87  GLU G CG  
12043 C CD  . GLU G  87  ? 1.0004 0.8832 1.1001 -0.0035 0.0752  -0.0344 87  GLU G CD  
12044 O OE1 . GLU G  87  ? 0.9887 0.8719 1.0947 -0.0021 0.0749  -0.0324 87  GLU G OE1 
12045 O OE2 . GLU G  87  ? 0.9255 0.8112 1.0214 0.0010  0.0741  -0.0317 87  GLU G OE2 
12046 N N   . THR G  88  ? 0.9949 0.8620 1.0766 -0.0222 0.0876  -0.0532 88  THR G N   
12047 C CA  . THR G  88  ? 1.0764 0.9392 1.1544 -0.0210 0.0938  -0.0548 88  THR G CA  
12048 C C   . THR G  88  ? 1.1589 1.0222 1.2400 -0.0113 0.0977  -0.0493 88  THR G C   
12049 O O   . THR G  88  ? 1.1609 1.0241 1.2485 -0.0062 0.0998  -0.0455 88  THR G O   
12050 C CB  . THR G  88  ? 1.1650 1.0195 1.2447 -0.0252 0.1022  -0.0599 88  THR G CB  
12051 O OG1 . THR G  88  ? 1.3068 1.1573 1.3946 -0.0206 0.1085  -0.0575 88  THR G OG1 
12052 C CG2 . THR G  88  ? 0.9122 0.7665 0.9892 -0.0351 0.0983  -0.0653 88  THR G CG2 
12053 N N   . PRO G  89  ? 1.5582 1.4224 1.6345 -0.0088 0.0986  -0.0486 89  PRO G N   
12054 C CA  . PRO G  89  ? 1.5295 1.3950 1.6083 0.0002  0.1020  -0.0432 89  PRO G CA  
12055 C C   . PRO G  89  ? 1.6846 1.5436 1.7701 0.0044  0.1117  -0.0420 89  PRO G C   
12056 O O   . PRO G  89  ? 1.7062 1.5663 1.7951 0.0121  0.1147  -0.0369 89  PRO G O   
12057 C CB  . PRO G  89  ? 1.3817 1.2476 1.4540 -0.0001 0.1025  -0.0446 89  PRO G CB  
12058 C CG  . PRO G  89  ? 1.4812 1.3490 1.5468 -0.0085 0.0959  -0.0492 89  PRO G CG  
12059 C CD  . PRO G  89  ? 1.5283 1.3925 1.5967 -0.0145 0.0965  -0.0529 89  PRO G CD  
12060 N N   . SER G  90  ? 1.4762 1.3288 1.5637 -0.0008 0.1166  -0.0466 90  SER G N   
12061 C CA  . SER G  90  ? 1.5251 1.3708 1.6191 0.0025  0.1265  -0.0461 90  SER G CA  
12062 C C   . SER G  90  ? 1.6710 1.5150 1.7713 0.0018  0.1271  -0.0457 90  SER G C   
12063 O O   . SER G  90  ? 1.8051 1.6423 1.9103 0.0014  0.1348  -0.0473 90  SER G O   
12064 C CB  . SER G  90  ? 1.5959 1.4342 1.6876 -0.0024 0.1335  -0.0517 90  SER G CB  
12065 O OG  . SER G  90  ? 1.8935 1.7250 1.9916 0.0014  0.1437  -0.0508 90  SER G OG  
12066 N N   . SER G  91  ? 1.5994 1.4495 1.7001 0.0015  0.1190  -0.0436 91  SER G N   
12067 C CA  . SER G  91  ? 1.4483 1.2976 1.5552 0.0009  0.1188  -0.0430 91  SER G CA  
12068 C C   . SER G  91  ? 1.4540 1.3051 1.5665 0.0097  0.1204  -0.0364 91  SER G C   
12069 O O   . SER G  91  ? 1.4418 1.2994 1.5526 0.0136  0.1147  -0.0323 91  SER G O   
12070 C CB  . SER G  91  ? 1.3046 1.1591 1.4092 -0.0051 0.1092  -0.0448 91  SER G CB  
12071 O OG  . SER G  91  ? 1.2873 1.1494 1.3887 -0.0020 0.1017  -0.0411 91  SER G OG  
12072 N N   . ASP G  92  ? 1.7147 1.5602 1.8337 0.0125  0.1283  -0.0355 92  ASP G N   
12073 C CA  . ASP G  92  ? 1.7512 1.5977 1.8754 0.0209  0.1309  -0.0291 92  ASP G CA  
12074 C C   . ASP G  92  ? 1.6885 1.5319 1.8200 0.0210  0.1336  -0.0286 92  ASP G C   
12075 O O   . ASP G  92  ? 1.7193 1.5635 1.8554 0.0275  0.1357  -0.0235 92  ASP G O   
12076 C CB  . ASP G  92  ? 2.0407 1.8836 2.1661 0.0269  0.1392  -0.0266 92  ASP G CB  
12077 C CG  . ASP G  92  ? 2.1058 1.9528 2.2248 0.0287  0.1363  -0.0256 92  ASP G CG  
12078 O OD1 . ASP G  92  ? 2.0723 1.9261 2.1869 0.0276  0.1277  -0.0249 92  ASP G OD1 
12079 O OD2 . ASP G  92  ? 2.1781 2.0217 2.2970 0.0312  0.1427  -0.0254 92  ASP G OD2 
12080 N N   . ASN G  93  ? 1.6015 1.4417 1.7340 0.0136  0.1335  -0.0339 93  ASN G N   
12081 C CA  . ASN G  93  ? 1.5806 1.4183 1.7201 0.0129  0.1355  -0.0338 93  ASN G CA  
12082 C C   . ASN G  93  ? 1.3899 1.2343 1.5305 0.0131  0.1270  -0.0312 93  ASN G C   
12083 O O   . ASN G  93  ? 1.2101 1.0565 1.3503 0.0066  0.1216  -0.0345 93  ASN G O   
12084 C CB  . ASN G  93  ? 1.5280 1.3601 1.6683 0.0047  0.1384  -0.0405 93  ASN G CB  
12085 C CG  . ASN G  93  ? 1.7565 1.5803 1.8986 0.0053  0.1490  -0.0425 93  ASN G CG  
12086 O OD1 . ASN G  93  ? 1.7311 1.5515 1.8693 -0.0003 0.1510  -0.0478 93  ASN G OD1 
12087 N ND2 . ASN G  93  ? 1.6781 1.4984 1.8261 0.0123  0.1561  -0.0383 93  ASN G ND2 
12088 N N   . GLY G  94  ? 1.3666 1.2145 1.5086 0.0205  0.1261  -0.0252 94  GLY G N   
12089 C CA  . GLY G  94  ? 1.2043 1.0583 1.3479 0.0215  0.1189  -0.0223 94  GLY G CA  
12090 C C   . GLY G  94  ? 1.2060 1.0578 1.3571 0.0260  0.1231  -0.0188 94  GLY G C   
12091 O O   . GLY G  94  ? 1.1517 0.9986 1.3078 0.0231  0.1271  -0.0212 94  GLY G O   
12092 N N   . THR G  95  ? 0.9763 0.8315 1.1278 0.0331  0.1223  -0.0130 95  THR G N   
12093 C CA  . THR G  95  ? 1.0062 0.8595 1.1643 0.0380  0.1264  -0.0091 95  THR G CA  
12094 C C   . THR G  95  ? 0.9844 0.8315 1.1456 0.0426  0.1363  -0.0075 95  THR G C   
12095 O O   . THR G  95  ? 0.9522 0.8006 1.1117 0.0488  0.1386  -0.0033 95  THR G O   
12096 C CB  . THR G  95  ? 0.8670 0.7266 1.0243 0.0435  0.1217  -0.0037 95  THR G CB  
12097 O OG1 . THR G  95  ? 0.8460 0.7093 0.9972 0.0469  0.1200  -0.0015 95  THR G OG1 
12098 C CG2 . THR G  95  ? 0.8260 0.6906 0.9831 0.0392  0.1132  -0.0048 95  THR G CG2 
12099 N N   . CYS G  96  ? 1.0225 0.8630 1.1884 0.0394  0.1422  -0.0107 96  CYS G N   
12100 C CA  . CYS G  96  ? 0.9446 0.7784 1.1143 0.0433  0.1523  -0.0096 96  CYS G CA  
12101 C C   . CYS G  96  ? 0.9509 0.7847 1.1249 0.0513  0.1559  -0.0031 96  CYS G C   
12102 O O   . CYS G  96  ? 0.9170 0.7481 1.0921 0.0568  0.1625  0.0002  96  CYS G O   
12103 C CB  . CYS G  96  ? 0.8945 0.7211 1.0685 0.0375  0.1576  -0.0148 96  CYS G CB  
12104 S SG  . CYS G  96  ? 1.0688 0.8967 1.2474 0.0319  0.1527  -0.0173 96  CYS G SG  
12105 N N   . TYR G  97  ? 0.8363 0.6734 1.0128 0.0519  0.1517  -0.0010 97  TYR G N   
12106 C CA  . TYR G  97  ? 0.7535 0.5916 0.9331 0.0593  0.1541  0.0053  97  TYR G CA  
12107 C C   . TYR G  97  ? 0.7788 0.6247 0.9529 0.0630  0.1475  0.0092  97  TYR G C   
12108 O O   . TYR G  97  ? 0.9769 0.8279 1.1480 0.0597  0.1395  0.0077  97  TYR G O   
12109 C CB  . TYR G  97  ? 0.8773 0.7141 1.0631 0.0583  0.1542  0.0055  97  TYR G CB  
12110 C CG  . TYR G  97  ? 0.7667 0.6020 0.9568 0.0656  0.1595  0.0114  97  TYR G CG  
12111 C CD1 . TYR G  97  ? 0.8625 0.6906 1.0589 0.0668  0.1682  0.0115  97  TYR G CD1 
12112 C CD2 . TYR G  97  ? 0.8197 0.6605 1.0073 0.0711  0.1561  0.0167  97  TYR G CD2 
12113 C CE1 . TYR G  97  ? 1.0429 0.8696 1.2431 0.0735  0.1731  0.0171  97  TYR G CE1 
12114 C CE2 . TYR G  97  ? 0.8212 0.6607 1.0122 0.0775  0.1609  0.0222  97  TYR G CE2 
12115 C CZ  . TYR G  97  ? 0.9098 0.7423 1.1070 0.0788  0.1694  0.0224  97  TYR G CZ  
12116 O OH  . TYR G  97  ? 0.8032 0.6345 1.0037 0.0852  0.1742  0.0280  97  TYR G OH  
12117 N N   . PRO G  98  ? 0.7310 0.5779 0.9039 0.0699  0.1510  0.0142  98  PRO G N   
12118 C CA  . PRO G  98  ? 0.7282 0.5823 0.8955 0.0737  0.1455  0.0180  98  PRO G CA  
12119 C C   . PRO G  98  ? 0.8795 0.7385 1.0469 0.0738  0.1391  0.0198  98  PRO G C   
12120 O O   . PRO G  98  ? 0.7957 0.6525 0.9684 0.0749  0.1415  0.0212  98  PRO G O   
12121 C CB  . PRO G  98  ? 0.6951 0.5483 0.8637 0.0814  0.1520  0.0238  98  PRO G CB  
12122 C CG  . PRO G  98  ? 0.9152 0.7605 1.0881 0.0807  0.1605  0.0218  98  PRO G CG  
12123 C CD  . PRO G  98  ? 0.9946 0.8358 1.1716 0.0746  0.1606  0.0168  98  PRO G CD  
12124 N N   . GLY G  99  ? 0.9282 0.7938 1.0900 0.0728  0.1315  0.0198  99  GLY G N   
12125 C CA  . GLY G  99  ? 0.8470 0.7173 1.0085 0.0729  0.1254  0.0214  99  GLY G CA  
12126 C C   . GLY G  99  ? 0.9135 0.7900 1.0690 0.0698  0.1169  0.0197  99  GLY G C   
12127 O O   . GLY G  99  ? 0.7834 0.6604 0.9346 0.0673  0.1155  0.0170  99  GLY G O   
12128 N N   . ASP G  100 ? 0.9381 0.8190 1.0933 0.0698  0.1114  0.0212  100 ASP G N   
12129 C CA  . ASP G  100 ? 0.7307 0.6176 0.8806 0.0672  0.1033  0.0200  100 ASP G CA  
12130 C C   . ASP G  100 ? 0.6367 0.5238 0.7888 0.0606  0.0983  0.0159  100 ASP G C   
12131 O O   . ASP G  100 ? 0.7043 0.5897 0.8620 0.0597  0.0989  0.0160  100 ASP G O   
12132 C CB  . ASP G  100 ? 0.7667 0.6589 0.9144 0.0718  0.1004  0.0246  100 ASP G CB  
12133 C CG  . ASP G  100 ? 1.1885 1.0869 1.3298 0.0702  0.0931  0.0240  100 ASP G CG  
12134 O OD1 . ASP G  100 ? 1.3528 1.2515 1.4905 0.0669  0.0912  0.0207  100 ASP G OD1 
12135 O OD2 . ASP G  100 ? 1.0862 0.9889 1.2259 0.0723  0.0895  0.0266  100 ASP G OD2 
12136 N N   . PHE G  101 ? 0.5752 0.4647 0.7229 0.0559  0.0933  0.0125  101 PHE G N   
12137 C CA  . PHE G  101 ? 0.6357 0.5266 0.7848 0.0494  0.0876  0.0090  101 PHE G CA  
12138 C C   . PHE G  101 ? 0.5914 0.4888 0.7375 0.0497  0.0802  0.0107  101 PHE G C   
12139 O O   . PHE G  101 ? 0.5986 0.4997 0.7386 0.0488  0.0760  0.0101  101 PHE G O   
12140 C CB  . PHE G  101 ? 0.5626 0.4520 0.7086 0.0436  0.0865  0.0041  101 PHE G CB  
12141 C CG  . PHE G  101 ? 0.5234 0.4120 0.6728 0.0367  0.0834  0.0002  101 PHE G CG  
12142 C CD1 . PHE G  101 ? 0.6530 0.5362 0.8049 0.0327  0.0877  -0.0037 101 PHE G CD1 
12143 C CD2 . PHE G  101 ? 0.6345 0.5278 0.7848 0.0341  0.0764  0.0004  101 PHE G CD2 
12144 C CE1 . PHE G  101 ? 0.5561 0.4391 0.7111 0.0261  0.0846  -0.0072 101 PHE G CE1 
12145 C CE2 . PHE G  101 ? 0.5433 0.4365 0.6971 0.0278  0.0733  -0.0028 101 PHE G CE2 
12146 C CZ  . PHE G  101 ? 0.4137 0.3019 0.5697 0.0237  0.0773  -0.0067 101 PHE G CZ  
12147 N N   . ILE G  102 ? 0.5346 0.4332 0.6850 0.0509  0.0789  0.0129  102 ILE G N   
12148 C CA  . ILE G  102 ? 0.5697 0.4740 0.7180 0.0517  0.0728  0.0150  102 ILE G CA  
12149 C C   . ILE G  102 ? 0.6094 0.5173 0.7554 0.0458  0.0655  0.0119  102 ILE G C   
12150 O O   . ILE G  102 ? 0.5805 0.4870 0.7302 0.0406  0.0640  0.0090  102 ILE G O   
12151 C CB  . ILE G  102 ? 0.7619 0.6661 0.9162 0.0537  0.0734  0.0176  102 ILE G CB  
12152 C CG1 . ILE G  102 ? 0.7128 0.6129 0.8700 0.0591  0.0811  0.0205  102 ILE G CG1 
12153 C CG2 . ILE G  102 ? 0.5909 0.5006 0.7427 0.0554  0.0682  0.0201  102 ILE G CG2 
12154 C CD1 . ILE G  102 ? 0.6076 0.5093 0.7592 0.0647  0.0833  0.0237  102 ILE G CD1 
12155 N N   . ASP G  103 ? 0.6314 0.5440 0.7715 0.0465  0.0609  0.0128  103 ASP G N   
12156 C CA  . ASP G  103 ? 0.4697 0.3861 0.6071 0.0413  0.0538  0.0104  103 ASP G CA  
12157 C C   . ASP G  103 ? 0.5527 0.4665 0.6890 0.0358  0.0540  0.0059  103 ASP G C   
12158 O O   . ASP G  103 ? 0.5478 0.4627 0.6859 0.0303  0.0498  0.0035  103 ASP G O   
12159 C CB  . ASP G  103 ? 0.5972 0.5160 0.7397 0.0392  0.0494  0.0111  103 ASP G CB  
12160 C CG  . ASP G  103 ? 0.6882 0.6097 0.8311 0.0440  0.0489  0.0151  103 ASP G CG  
12161 O OD1 . ASP G  103 ? 0.7790 0.7027 0.9162 0.0476  0.0488  0.0168  103 ASP G OD1 
12162 O OD2 . ASP G  103 ? 0.6386 0.5601 0.7876 0.0441  0.0486  0.0164  103 ASP G OD2 
12163 N N   . TYR G  104 ? 0.6208 0.5313 0.7542 0.0374  0.0589  0.0050  104 TYR G N   
12164 C CA  . TYR G  104 ? 0.5463 0.4535 0.6784 0.0324  0.0603  0.0006  104 TYR G CA  
12165 C C   . TYR G  104 ? 0.5906 0.5015 0.7168 0.0276  0.0540  -0.0020 104 TYR G C   
12166 O O   . TYR G  104 ? 0.5197 0.4302 0.6465 0.0214  0.0513  -0.0054 104 TYR G O   
12167 C CB  . TYR G  104 ? 0.5404 0.4431 0.6711 0.0358  0.0677  0.0007  104 TYR G CB  
12168 C CG  . TYR G  104 ? 0.5895 0.4883 0.7187 0.0309  0.0700  -0.0039 104 TYR G CG  
12169 C CD1 . TYR G  104 ? 0.5363 0.4322 0.6696 0.0254  0.0703  -0.0074 104 TYR G CD1 
12170 C CD2 . TYR G  104 ? 0.5340 0.4320 0.6576 0.0317  0.0721  -0.0050 104 TYR G CD2 
12171 C CE1 . TYR G  104 ? 0.5533 0.4454 0.6847 0.0205  0.0726  -0.0119 104 TYR G CE1 
12172 C CE2 . TYR G  104 ? 0.6736 0.5676 0.7955 0.0270  0.0747  -0.0094 104 TYR G CE2 
12173 C CZ  . TYR G  104 ? 0.5787 0.4697 0.7044 0.0213  0.0749  -0.0130 104 TYR G CZ  
12174 O OH  . TYR G  104 ? 0.6749 0.5618 0.7986 0.0163  0.0776  -0.0177 104 TYR G OH  
12175 N N   . GLU G  105 ? 0.6729 0.5874 0.7932 0.0303  0.0518  -0.0004 105 GLU G N   
12176 C CA  . GLU G  105 ? 0.5073 0.4252 0.6216 0.0263  0.0460  -0.0026 105 GLU G CA  
12177 C C   . GLU G  105 ? 0.5143 0.4358 0.6307 0.0217  0.0391  -0.0031 105 GLU G C   
12178 O O   . GLU G  105 ? 0.5515 0.4744 0.6651 0.0161  0.0349  -0.0061 105 GLU G O   
12179 C CB  . GLU G  105 ? 0.5713 0.4929 0.6797 0.0305  0.0446  -0.0001 105 GLU G CB  
12180 C CG  . GLU G  105 ? 0.5430 0.4620 0.6496 0.0354  0.0511  0.0011  105 GLU G CG  
12181 C CD  . GLU G  105 ? 0.7156 0.6323 0.8275 0.0408  0.0564  0.0045  105 GLU G CD  
12182 O OE1 . GLU G  105 ? 0.7576 0.6764 0.8726 0.0424  0.0543  0.0069  105 GLU G OE1 
12183 O OE2 . GLU G  105 ? 0.7310 0.6435 0.8440 0.0434  0.0630  0.0047  105 GLU G OE2 
12184 N N   . GLU G  106 ? 0.5161 0.4393 0.6376 0.0242  0.0381  -0.0001 106 GLU G N   
12185 C CA  . GLU G  106 ? 0.5832 0.5097 0.7081 0.0205  0.0320  -0.0001 106 GLU G CA  
12186 C C   . GLU G  106 ? 0.5500 0.4740 0.6791 0.0146  0.0321  -0.0033 106 GLU G C   
12187 O O   . GLU G  106 ? 0.4848 0.4114 0.6132 0.0091  0.0266  -0.0052 106 GLU G O   
12188 C CB  . GLU G  106 ? 0.5390 0.4670 0.6690 0.0247  0.0320  0.0038  106 GLU G CB  
12189 C CG  . GLU G  106 ? 0.8210 0.7535 0.9467 0.0281  0.0287  0.0066  106 GLU G CG  
12190 C CD  . GLU G  106 ? 0.6830 0.6201 0.8066 0.0238  0.0212  0.0058  106 GLU G CD  
12191 O OE1 . GLU G  106 ? 0.6677 0.6057 0.7960 0.0194  0.0181  0.0048  106 GLU G OE1 
12192 O OE2 . GLU G  106 ? 0.5926 0.5329 0.7101 0.0248  0.0185  0.0063  106 GLU G OE2 
12193 N N   . LEU G  107 ? 0.6442 0.5632 0.7778 0.0159  0.0384  -0.0038 107 LEU G N   
12194 C CA  . LEU G  107 ? 0.6151 0.5313 0.7529 0.0104  0.0393  -0.0070 107 LEU G CA  
12195 C C   . LEU G  107 ? 0.5568 0.4729 0.6888 0.0044  0.0371  -0.0113 107 LEU G C   
12196 O O   . LEU G  107 ? 0.4824 0.4003 0.6155 -0.0018 0.0327  -0.0135 107 LEU G O   
12197 C CB  . LEU G  107 ? 0.6053 0.5154 0.7473 0.0132  0.0475  -0.0072 107 LEU G CB  
12198 C CG  . LEU G  107 ? 0.6471 0.5547 0.7971 0.0103  0.0492  -0.0083 107 LEU G CG  
12199 C CD1 . LEU G  107 ? 0.5687 0.4697 0.7199 0.0097  0.0567  -0.0110 107 LEU G CD1 
12200 C CD2 . LEU G  107 ? 0.5254 0.4367 0.6771 0.0034  0.0424  -0.0103 107 LEU G CD2 
12201 N N   . ARG G  108 ? 0.4840 0.3981 0.6098 0.0063  0.0402  -0.0122 108 ARG G N   
12202 C CA  . ARG G  108 ? 0.6304 0.5439 0.7500 0.0011  0.0389  -0.0163 108 ARG G CA  
12203 C C   . ARG G  108 ? 0.6625 0.5819 0.7783 -0.0032 0.0305  -0.0167 108 ARG G C   
12204 O O   . ARG G  108 ? 0.5492 0.4689 0.6632 -0.0099 0.0275  -0.0201 108 ARG G O   
12205 C CB  . ARG G  108 ? 0.5296 0.4409 0.6436 0.0050  0.0435  -0.0163 108 ARG G CB  
12206 C CG  . ARG G  108 ? 0.5653 0.4708 0.6827 0.0093  0.0522  -0.0157 108 ARG G CG  
12207 C CD  . ARG G  108 ? 0.6609 0.5655 0.7734 0.0143  0.0560  -0.0144 108 ARG G CD  
12208 N NE  . ARG G  108 ? 0.6782 0.5825 0.7839 0.0103  0.0549  -0.0179 108 ARG G NE  
12209 C CZ  . ARG G  108 ? 0.6886 0.5877 0.7932 0.0082  0.0604  -0.0213 108 ARG G CZ  
12210 N NH1 . ARG G  108 ? 0.5636 0.4572 0.6734 0.0097  0.0674  -0.0215 108 ARG G NH1 
12211 N NH2 . ARG G  108 ? 0.6326 0.5316 0.7306 0.0045  0.0592  -0.0244 108 ARG G NH2 
12212 N N   . GLU G  109 ? 0.6114 0.5352 0.7259 0.0006  0.0267  -0.0132 109 GLU G N   
12213 C CA  . GLU G  109 ? 0.5871 0.5165 0.6984 -0.0028 0.0189  -0.0130 109 GLU G CA  
12214 C C   . GLU G  109 ? 0.6184 0.5501 0.7352 -0.0080 0.0142  -0.0135 109 GLU G C   
12215 O O   . GLU G  109 ? 0.6070 0.5416 0.7210 -0.0137 0.0088  -0.0153 109 GLU G O   
12216 C CB  . GLU G  109 ? 0.5887 0.5221 0.6990 0.0027  0.0165  -0.0089 109 GLU G CB  
12217 C CG  . GLU G  109 ? 0.7594 0.6983 0.8662 -0.0002 0.0088  -0.0084 109 GLU G CG  
12218 C CD  . GLU G  109 ? 0.9484 0.8878 1.0467 -0.0031 0.0072  -0.0111 109 GLU G CD  
12219 O OE1 . GLU G  109 ? 0.9515 0.8867 1.0470 -0.0037 0.0119  -0.0138 109 GLU G OE1 
12220 O OE2 . GLU G  109 ? 1.0493 0.9931 1.1439 -0.0047 0.0014  -0.0105 109 GLU G OE2 
12221 N N   . GLN G  110 ? 0.5251 0.4556 0.6498 -0.0061 0.0164  -0.0117 110 GLN G N   
12222 C CA  . GLN G  110 ? 0.6181 0.5510 0.7492 -0.0105 0.0123  -0.0117 110 GLN G CA  
12223 C C   . GLN G  110 ? 0.7461 0.6766 0.8774 -0.0173 0.0130  -0.0161 110 GLN G C   
12224 O O   . GLN G  110 ? 0.8014 0.7351 0.9349 -0.0230 0.0078  -0.0170 110 GLN G O   
12225 C CB  . GLN G  110 ? 0.6311 0.5629 0.7707 -0.0063 0.0151  -0.0087 110 GLN G CB  
12226 C CG  . GLN G  110 ? 0.6445 0.5773 0.7835 0.0009  0.0164  -0.0047 110 GLN G CG  
12227 C CD  . GLN G  110 ? 0.8069 0.7440 0.9513 0.0020  0.0120  -0.0013 110 GLN G CD  
12228 O OE1 . GLN G  110 ? 0.9084 0.8483 1.0572 -0.0026 0.0075  -0.0016 110 GLN G OE1 
12229 N NE2 . GLN G  110 ? 0.7341 0.6718 0.8784 0.0080  0.0134  0.0020  110 GLN G NE2 
12230 N N   . LEU G  111 ? 0.8137 0.7386 0.9430 -0.0168 0.0196  -0.0187 111 LEU G N   
12231 C CA  . LEU G  111 ? 0.6772 0.5989 0.8067 -0.0231 0.0214  -0.0232 111 LEU G CA  
12232 C C   . LEU G  111 ? 0.7383 0.6603 0.8590 -0.0280 0.0194  -0.0268 111 LEU G C   
12233 O O   . LEU G  111 ? 0.7106 0.6307 0.8302 -0.0343 0.0199  -0.0309 111 LEU G O   
12234 C CB  . LEU G  111 ? 0.6347 0.5496 0.7674 -0.0204 0.0303  -0.0243 111 LEU G CB  
12235 C CG  . LEU G  111 ? 0.6906 0.6045 0.8328 -0.0183 0.0323  -0.0222 111 LEU G CG  
12236 C CD1 . LEU G  111 ? 0.6065 0.5140 0.7514 -0.0136 0.0413  -0.0221 111 LEU G CD1 
12237 C CD2 . LEU G  111 ? 0.8162 0.7316 0.9632 -0.0254 0.0290  -0.0245 111 LEU G CD2 
12238 N N   . SER G  112 ? 0.6630 0.5874 0.7775 -0.0252 0.0171  -0.0253 112 SER G N   
12239 C CA  . SER G  112 ? 0.6154 0.5402 0.7212 -0.0292 0.0152  -0.0284 112 SER G CA  
12240 C C   . SER G  112 ? 0.6889 0.6163 0.7934 -0.0379 0.0097  -0.0314 112 SER G C   
12241 O O   . SER G  112 ? 0.7743 0.6999 0.8729 -0.0429 0.0103  -0.0354 112 SER G O   
12242 C CB  . SER G  112 ? 0.6820 0.6106 0.7823 -0.0253 0.0117  -0.0257 112 SER G CB  
12243 O OG  . SER G  112 ? 0.6382 0.5729 0.7408 -0.0261 0.0045  -0.0228 112 SER G OG  
12244 N N   . SER G  113 ? 0.6931 0.6251 0.8034 -0.0397 0.0043  -0.0292 113 SER G N   
12245 C CA  . SER G  113 ? 0.6736 0.6092 0.7837 -0.0479 -0.0017 -0.0312 113 SER G CA  
12246 C C   . SER G  113 ? 0.7921 0.7303 0.9118 -0.0491 -0.0041 -0.0292 113 SER G C   
12247 O O   . SER G  113 ? 0.8445 0.7864 0.9690 -0.0452 -0.0071 -0.0249 113 SER G O   
12248 C CB  . SER G  113 ? 0.8236 0.7648 0.9276 -0.0499 -0.0090 -0.0301 113 SER G CB  
12249 O OG  . SER G  113 ? 0.7753 0.7198 0.8777 -0.0582 -0.0144 -0.0324 113 SER G OG  
12250 N N   . VAL G  114 ? 0.7077 0.6441 0.8304 -0.0548 -0.0028 -0.0325 114 VAL G N   
12251 C CA  . VAL G  114 ? 0.8511 0.7901 0.9832 -0.0567 -0.0051 -0.0308 114 VAL G CA  
12252 C C   . VAL G  114 ? 0.8510 0.7944 0.9826 -0.0658 -0.0113 -0.0331 114 VAL G C   
12253 O O   . VAL G  114 ? 0.8052 0.7466 0.9304 -0.0715 -0.0106 -0.0376 114 VAL G O   
12254 C CB  . VAL G  114 ? 0.8784 0.8115 1.0169 -0.0548 0.0025  -0.0321 114 VAL G CB  
12255 C CG1 . VAL G  114 ? 0.7724 0.7013 0.9113 -0.0459 0.0088  -0.0297 114 VAL G CG1 
12256 C CG2 . VAL G  114 ? 0.8317 0.7602 0.9667 -0.0610 0.0064  -0.0379 114 VAL G CG2 
12257 N N   . SER G  115 ? 0.9247 0.8741 1.0630 -0.0671 -0.0173 -0.0298 115 SER G N   
12258 C CA  . SER G  115 ? 1.1300 1.0845 1.2691 -0.0755 -0.0237 -0.0311 115 SER G CA  
12259 C C   . SER G  115 ? 1.1691 1.1208 1.3135 -0.0801 -0.0202 -0.0344 115 SER G C   
12260 O O   . SER G  115 ? 1.2374 1.1889 1.3776 -0.0876 -0.0211 -0.0387 115 SER G O   
12261 C CB  . SER G  115 ? 1.1250 1.0871 1.2704 -0.0748 -0.0311 -0.0259 115 SER G CB  
12262 O OG  . SER G  115 ? 1.2392 1.2074 1.3825 -0.0825 -0.0386 -0.0264 115 SER G OG  
12263 N N   . SER G  116 ? 1.0346 0.9841 1.1880 -0.0757 -0.0162 -0.0325 116 SER G N   
12264 C CA  . SER G  116 ? 1.0817 1.0277 1.2407 -0.0791 -0.0118 -0.0355 116 SER G CA  
12265 C C   . SER G  116 ? 1.1112 1.0501 1.2739 -0.0719 -0.0030 -0.0350 116 SER G C   
12266 O O   . SER G  116 ? 1.0913 1.0305 1.2571 -0.0645 -0.0021 -0.0308 116 SER G O   
12267 C CB  . SER G  116 ? 1.1336 1.0856 1.3021 -0.0830 -0.0171 -0.0334 116 SER G CB  
12268 O OG  . SER G  116 ? 1.3052 1.2585 1.4824 -0.0763 -0.0169 -0.0284 116 SER G OG  
12269 N N   . PHE G  117 ? 0.9378 0.8705 1.1003 -0.0741 0.0036  -0.0394 117 PHE G N   
12270 C CA  . PHE G  117 ? 0.8877 0.8132 1.0524 -0.0675 0.0126  -0.0393 117 PHE G CA  
12271 C C   . PHE G  117 ? 0.8579 0.7784 1.0276 -0.0710 0.0184  -0.0430 117 PHE G C   
12272 O O   . PHE G  117 ? 0.9898 0.9058 1.1544 -0.0754 0.0223  -0.0479 117 PHE G O   
12273 C CB  . PHE G  117 ? 0.8434 0.7644 0.9986 -0.0645 0.0166  -0.0409 117 PHE G CB  
12274 C CG  . PHE G  117 ? 0.8377 0.7525 0.9947 -0.0564 0.0249  -0.0394 117 PHE G CG  
12275 C CD1 . PHE G  117 ? 0.7690 0.6765 0.9274 -0.0567 0.0331  -0.0427 117 PHE G CD1 
12276 C CD2 . PHE G  117 ? 0.8268 0.7430 0.9839 -0.0485 0.0245  -0.0347 117 PHE G CD2 
12277 C CE1 . PHE G  117 ? 0.6823 0.5844 0.8424 -0.0491 0.0406  -0.0409 117 PHE G CE1 
12278 C CE2 . PHE G  117 ? 0.8243 0.7352 0.9828 -0.0412 0.0318  -0.0331 117 PHE G CE2 
12279 C CZ  . PHE G  117 ? 0.7613 0.6652 0.9214 -0.0414 0.0398  -0.0360 117 PHE G CZ  
12280 N N   . GLU G  118 ? 0.8109 0.7318 0.9906 -0.0692 0.0194  -0.0407 118 GLU G N   
12281 C CA  . GLU G  118 ? 0.9860 0.9020 1.1712 -0.0721 0.0253  -0.0440 118 GLU G CA  
12282 C C   . GLU G  118 ? 0.9223 0.8323 1.1130 -0.0642 0.0333  -0.0418 118 GLU G C   
12283 O O   . GLU G  118 ? 0.8846 0.7965 1.0795 -0.0577 0.0324  -0.0369 118 GLU G O   
12284 C CB  . GLU G  118 ? 1.0763 0.9977 1.2690 -0.0786 0.0201  -0.0441 118 GLU G CB  
12285 C CG  . GLU G  118 ? 1.2134 1.1378 1.4166 -0.0739 0.0187  -0.0390 118 GLU G CG  
12286 C CD  . GLU G  118 ? 1.5695 1.4959 1.7819 -0.0795 0.0177  -0.0402 118 GLU G CD  
12287 O OE1 . GLU G  118 ? 1.6823 1.6084 1.8924 -0.0874 0.0174  -0.0450 118 GLU G OE1 
12288 O OE2 . GLU G  118 ? 1.5041 1.4325 1.7258 -0.0761 0.0172  -0.0365 118 GLU G OE2 
12289 N N   . ARG G  119 ? 0.8447 0.7474 1.0354 -0.0650 0.0414  -0.0455 119 ARG G N   
12290 C CA  . ARG G  119 ? 0.8874 0.7838 1.0828 -0.0579 0.0498  -0.0438 119 ARG G CA  
12291 C C   . ARG G  119 ? 0.8642 0.7588 1.0695 -0.0602 0.0527  -0.0446 119 ARG G C   
12292 O O   . ARG G  119 ? 1.1126 1.0044 1.3185 -0.0665 0.0554  -0.0494 119 ARG G O   
12293 C CB  . ARG G  119 ? 0.8900 0.7788 1.0788 -0.0564 0.0575  -0.0470 119 ARG G CB  
12294 C CG  . ARG G  119 ? 0.9052 0.7865 1.0991 -0.0510 0.0672  -0.0465 119 ARG G CG  
12295 C CD  . ARG G  119 ? 1.0404 0.9145 1.2281 -0.0507 0.0747  -0.0500 119 ARG G CD  
12296 N NE  . ARG G  119 ? 1.0504 0.9169 1.2435 -0.0474 0.0843  -0.0504 119 ARG G NE  
12297 C CZ  . ARG G  119 ? 1.2528 1.1150 1.4497 -0.0528 0.0887  -0.0547 119 ARG G CZ  
12298 N NH1 . ARG G  119 ? 1.3934 1.2583 1.5891 -0.0620 0.0843  -0.0591 119 ARG G NH1 
12299 N NH2 . ARG G  119 ? 1.0526 0.9078 1.2545 -0.0490 0.0977  -0.0546 119 ARG G NH2 
12300 N N   . PHE G  120 ? 0.8331 0.7294 1.0462 -0.0551 0.0523  -0.0401 120 PHE G N   
12301 C CA  . PHE G  120 ? 0.8757 0.7710 1.0990 -0.0568 0.0547  -0.0403 120 PHE G CA  
12302 C C   . PHE G  120 ? 0.8566 0.7459 1.0849 -0.0488 0.0628  -0.0376 120 PHE G C   
12303 O O   . PHE G  120 ? 0.8853 0.7737 1.1107 -0.0414 0.0642  -0.0340 120 PHE G O   
12304 C CB  . PHE G  120 ? 0.8794 0.7829 1.1093 -0.0592 0.0465  -0.0374 120 PHE G CB  
12305 C CG  . PHE G  120 ? 0.8981 0.8047 1.1301 -0.0517 0.0440  -0.0314 120 PHE G CG  
12306 C CD1 . PHE G  120 ? 0.9197 0.8251 1.1608 -0.0468 0.0471  -0.0281 120 PHE G CD1 
12307 C CD2 . PHE G  120 ? 0.9521 0.8628 1.1772 -0.0497 0.0386  -0.0293 120 PHE G CD2 
12308 C CE1 . PHE G  120 ? 0.8457 0.7536 1.0884 -0.0402 0.0451  -0.0228 120 PHE G CE1 
12309 C CE2 . PHE G  120 ? 0.8965 0.8099 1.1234 -0.0431 0.0366  -0.0241 120 PHE G CE2 
12310 C CZ  . PHE G  120 ? 0.8918 0.8039 1.1275 -0.0384 0.0398  -0.0209 120 PHE G CZ  
12311 N N   . GLU G  121 ? 0.9634 0.8487 1.1990 -0.0505 0.0679  -0.0393 121 GLU G N   
12312 C CA  . GLU G  121 ? 0.9598 0.8394 1.2009 -0.0434 0.0757  -0.0367 121 GLU G CA  
12313 C C   . GLU G  121 ? 0.9785 0.8625 1.2269 -0.0392 0.0723  -0.0315 121 GLU G C   
12314 O O   . GLU G  121 ? 1.0826 0.9697 1.3391 -0.0428 0.0697  -0.0314 121 GLU G O   
12315 C CB  . GLU G  121 ? 0.9877 0.8612 1.2341 -0.0470 0.0827  -0.0406 121 GLU G CB  
12316 C CG  . GLU G  121 ? 1.1197 0.9856 1.3693 -0.0398 0.0924  -0.0388 121 GLU G CG  
12317 C CD  . GLU G  121 ? 1.2018 1.0613 1.4563 -0.0437 0.0997  -0.0430 121 GLU G CD  
12318 O OE1 . GLU G  121 ? 1.2217 1.0834 1.4785 -0.0519 0.0967  -0.0469 121 GLU G OE1 
12319 O OE2 . GLU G  121 ? 1.2293 1.0816 1.4853 -0.0386 0.1084  -0.0423 121 GLU G OE2 
12320 N N   . ILE G  122 ? 0.9556 0.8400 1.2013 -0.0316 0.0725  -0.0271 122 ILE G N   
12321 C CA  . ILE G  122 ? 0.9440 0.8322 1.1957 -0.0271 0.0696  -0.0221 122 ILE G CA  
12322 C C   . ILE G  122 ? 0.9787 0.8619 1.2389 -0.0233 0.0767  -0.0205 122 ILE G C   
12323 O O   . ILE G  122 ? 0.9998 0.8858 1.2684 -0.0235 0.0747  -0.0184 122 ILE G O   
12324 C CB  . ILE G  122 ? 0.9162 0.8064 1.1616 -0.0205 0.0675  -0.0181 122 ILE G CB  
12325 C CG1 . ILE G  122 ? 0.8384 0.7317 1.0903 -0.0158 0.0656  -0.0131 122 ILE G CG1 
12326 C CG2 . ILE G  122 ? 0.8871 0.7709 1.1268 -0.0149 0.0750  -0.0180 122 ILE G CG2 
12327 C CD1 . ILE G  122 ? 0.7602 0.6557 1.0061 -0.0097 0.0635  -0.0093 122 ILE G CD1 
12328 N N   . PHE G  123 ? 1.1322 1.0080 1.3903 -0.0197 0.0851  -0.0214 123 PHE G N   
12329 C CA  . PHE G  123 ? 1.0417 0.9120 1.3073 -0.0164 0.0926  -0.0203 123 PHE G CA  
12330 C C   . PHE G  123 ? 1.1185 0.9821 1.3844 -0.0198 0.0996  -0.0250 123 PHE G C   
12331 O O   . PHE G  123 ? 1.0719 0.9300 1.3326 -0.0164 0.1056  -0.0255 123 PHE G O   
12332 C CB  . PHE G  123 ? 0.9583 0.8258 1.2221 -0.0071 0.0971  -0.0156 123 PHE G CB  
12333 C CG  . PHE G  123 ? 0.9909 0.8643 1.2552 -0.0034 0.0913  -0.0111 123 PHE G CG  
12334 C CD1 . PHE G  123 ? 0.9644 0.8395 1.2207 0.0013  0.0895  -0.0086 123 PHE G CD1 
12335 C CD2 . PHE G  123 ? 1.0323 0.9094 1.3051 -0.0047 0.0880  -0.0093 123 PHE G CD2 
12336 C CE1 . PHE G  123 ? 0.9077 0.7879 1.1644 0.0045  0.0845  -0.0046 123 PHE G CE1 
12337 C CE2 . PHE G  123 ? 0.9599 0.8419 1.2333 -0.0013 0.0831  -0.0052 123 PHE G CE2 
12338 C CZ  . PHE G  123 ? 0.8985 0.7820 1.1637 0.0032  0.0815  -0.0030 123 PHE G CZ  
12339 N N   . PRO G  124 ? 1.2570 1.1210 1.5292 -0.0266 0.0990  -0.0283 124 PRO G N   
12340 C CA  . PRO G  124 ? 1.2340 1.0914 1.5072 -0.0305 0.1059  -0.0331 124 PRO G CA  
12341 C C   . PRO G  124 ? 1.2600 1.1093 1.5357 -0.0238 0.1160  -0.0313 124 PRO G C   
12342 O O   . PRO G  124 ? 1.2289 1.0781 1.5108 -0.0189 0.1177  -0.0273 124 PRO G O   
12343 C CB  . PRO G  124 ? 1.2878 1.1481 1.5698 -0.0373 0.1032  -0.0352 124 PRO G CB  
12344 C CG  . PRO G  124 ? 1.2407 1.1102 1.5231 -0.0394 0.0930  -0.0330 124 PRO G CG  
12345 C CD  . PRO G  124 ? 1.1480 1.0188 1.4269 -0.0311 0.0918  -0.0277 124 PRO G CD  
12346 N N   . LYS G  125 ? 1.2342 1.0771 1.5054 -0.0236 0.1227  -0.0341 125 LYS G N   
12347 C CA  . LYS G  125 ? 1.3325 1.1677 1.6051 -0.0167 0.1324  -0.0320 125 LYS G CA  
12348 C C   . LYS G  125 ? 1.5302 1.3616 1.8129 -0.0165 0.1379  -0.0317 125 LYS G C   
12349 O O   . LYS G  125 ? 1.4138 1.2412 1.6995 -0.0095 0.1438  -0.0279 125 LYS G O   
12350 C CB  . LYS G  125 ? 1.3024 1.1314 1.5690 -0.0176 0.1386  -0.0355 125 LYS G CB  
12351 C CG  . LYS G  125 ? 1.2028 1.0243 1.4706 -0.0102 0.1486  -0.0329 125 LYS G CG  
12352 C CD  . LYS G  125 ? 1.1054 0.9220 1.3662 -0.0096 0.1536  -0.0351 125 LYS G CD  
12353 C CE  . LYS G  125 ? 1.2891 1.1013 1.5505 -0.0177 0.1571  -0.0418 125 LYS G CE  
12354 N NZ  . LYS G  125 ? 1.2740 1.0805 1.5293 -0.0167 0.1632  -0.0439 125 LYS G NZ  
12355 N N   . THR G  126 ? 2.1972 2.0298 2.4853 -0.0241 0.1361  -0.0357 126 THR G N   
12356 C CA  . THR G  126 ? 2.2084 2.0362 2.5058 -0.0250 0.1425  -0.0366 126 THR G CA  
12357 C C   . THR G  126 ? 2.1493 1.9816 2.4559 -0.0250 0.1387  -0.0339 126 THR G C   
12358 O O   . THR G  126 ? 2.3258 2.1552 2.6406 -0.0274 0.1428  -0.0354 126 THR G O   
12359 C CB  . THR G  126 ? 1.7400 1.5650 2.0385 -0.0339 0.1447  -0.0434 126 THR G CB  
12360 O OG1 . THR G  126 ? 1.6740 1.5059 1.9681 -0.0411 0.1357  -0.0463 126 THR G OG1 
12361 N N   . SER G  127 ? 1.3711 1.2103 1.6766 -0.0224 0.1313  -0.0300 127 SER G N   
12362 C CA  . SER G  127 ? 1.3076 1.1511 1.6218 -0.0222 0.1278  -0.0272 127 SER G CA  
12363 C C   . SER G  127 ? 1.2674 1.1140 1.5800 -0.0146 0.1251  -0.0212 127 SER G C   
12364 O O   . SER G  127 ? 1.3985 1.2471 1.7183 -0.0122 0.1242  -0.0179 127 SER G O   
12365 C CB  . SER G  127 ? 1.3952 1.2460 1.7122 -0.0308 0.1193  -0.0300 127 SER G CB  
12366 O OG  . SER G  127 ? 1.2721 1.1285 1.5808 -0.0325 0.1118  -0.0301 127 SER G OG  
12367 N N   . SER G  128 ? 1.2326 1.0793 1.5358 -0.0106 0.1243  -0.0198 128 SER G N   
12368 C CA  . SER G  128 ? 1.0977 0.9481 1.3979 -0.0042 0.1209  -0.0146 128 SER G CA  
12369 C C   . SER G  128 ? 1.1761 1.0206 1.4761 0.0042  0.1287  -0.0108 128 SER G C   
12370 O O   . SER G  128 ? 1.1804 1.0270 1.4815 0.0096  0.1276  -0.0062 128 SER G O   
12371 C CB  . SER G  128 ? 1.1802 1.0346 1.4703 -0.0048 0.1151  -0.0151 128 SER G CB  
12372 O OG  . SER G  128 ? 1.1534 1.0131 1.4432 -0.0129 0.1080  -0.0186 128 SER G OG  
12373 N N   . TRP G  129 ? 1.2748 1.1122 1.5735 0.0053  0.1367  -0.0126 129 TRP G N   
12374 C CA  . TRP G  129 ? 1.2313 1.0632 1.5290 0.0133  0.1443  -0.0088 129 TRP G CA  
12375 C C   . TRP G  129 ? 1.3600 1.1845 1.6649 0.0134  0.1532  -0.0099 129 TRP G C   
12376 O O   . TRP G  129 ? 1.2961 1.1147 1.5991 0.0134  0.1597  -0.0121 129 TRP G O   
12377 C CB  . TRP G  129 ? 1.3203 1.1505 1.6083 0.0163  0.1460  -0.0087 129 TRP G CB  
12378 C CG  . TRP G  129 ? 1.1172 0.9541 1.3980 0.0138  0.1372  -0.0094 129 TRP G CG  
12379 C CD1 . TRP G  129 ? 1.0861 0.9239 1.3613 0.0085  0.1345  -0.0137 129 TRP G CD1 
12380 C CD2 . TRP G  129 ? 1.0706 0.9141 1.3490 0.0162  0.1302  -0.0059 129 TRP G CD2 
12381 N NE1 . TRP G  129 ? 1.1608 1.0054 1.4304 0.0077  0.1262  -0.0129 129 TRP G NE1 
12382 C CE2 . TRP G  129 ? 1.0494 0.8976 1.3210 0.0124  0.1234  -0.0081 129 TRP G CE2 
12383 C CE3 . TRP G  129 ? 1.0853 0.9310 1.3668 0.0212  0.1292  -0.0012 129 TRP G CE3 
12384 C CZ2 . TRP G  129 ? 1.0432 0.8982 1.3111 0.0135  0.1158  -0.0057 129 TRP G CZ2 
12385 C CZ3 . TRP G  129 ? 0.9260 0.7783 1.2038 0.0222  0.1217  0.0010  129 TRP G CZ3 
12386 C CH2 . TRP G  129 ? 0.9442 0.8011 1.2154 0.0184  0.1151  -0.0012 129 TRP G CH2 
12387 N N   . PRO G  130 ? 1.4750 1.3000 1.7887 0.0135  0.1537  -0.0084 130 PRO G N   
12388 C CA  . PRO G  130 ? 1.3323 1.1509 1.6542 0.0132  0.1616  -0.0094 130 PRO G CA  
12389 C C   . PRO G  130 ? 1.4381 1.2514 1.7604 0.0217  0.1693  -0.0046 130 PRO G C   
12390 O O   . PRO G  130 ? 1.5629 1.3698 1.8907 0.0225  0.1771  -0.0050 130 PRO G O   
12391 C CB  . PRO G  130 ? 1.4310 1.2541 1.7618 0.0094  0.1570  -0.0094 130 PRO G CB  
12392 C CG  . PRO G  130 ? 1.3780 1.2098 1.7051 0.0076  0.1466  -0.0086 130 PRO G CG  
12393 C CD  . PRO G  130 ? 1.4893 1.3213 1.8062 0.0129  0.1462  -0.0062 130 PRO G CD  
12394 N N   . ASN G  131 ? 1.4045 1.2205 1.7210 0.0277  0.1670  -0.0001 131 ASN G N   
12395 C CA  . ASN G  131 ? 1.4363 1.2482 1.7525 0.0358  0.1735  0.0048  131 ASN G CA  
12396 C C   . ASN G  131 ? 1.3334 1.1432 1.6405 0.0404  0.1764  0.0064  131 ASN G C   
12397 O O   . ASN G  131 ? 1.2256 1.0331 1.5307 0.0474  0.1809  0.0110  131 ASN G O   
12398 C CB  . ASN G  131 ? 1.4915 1.3080 1.8089 0.0395  0.1695  0.0092  131 ASN G CB  
12399 C CG  . ASN G  131 ? 1.6196 1.4376 1.9470 0.0358  0.1678  0.0084  131 ASN G CG  
12400 O OD1 . ASN G  131 ? 1.6743 1.4887 2.0084 0.0318  0.1715  0.0053  131 ASN G OD1 
12401 N ND2 . ASN G  131 ? 1.6952 1.5186 2.0238 0.0370  0.1623  0.0111  131 ASN G ND2 
12402 N N   . HIS G  132 ? 1.3200 1.1309 1.6218 0.0365  0.1737  0.0028  132 HIS G N   
12403 C CA  . HIS G  132 ? 1.1105 0.9199 1.4039 0.0403  0.1759  0.0040  132 HIS G CA  
12404 C C   . HIS G  132 ? 1.1510 0.9566 1.4430 0.0354  0.1788  -0.0012 132 HIS G C   
12405 O O   . HIS G  132 ? 1.2974 1.1039 1.5924 0.0281  0.1760  -0.0060 132 HIS G O   
12406 C CB  . HIS G  132 ? 1.0635 0.8802 1.3493 0.0414  0.1676  0.0057  132 HIS G CB  
12407 C CG  . HIS G  132 ? 1.0010 0.8221 1.2882 0.0449  0.1637  0.0099  132 HIS G CG  
12408 N ND1 . HIS G  132 ? 0.9937 0.8152 1.2769 0.0522  0.1655  0.0151  132 HIS G ND1 
12409 C CD2 . HIS G  132 ? 0.9672 0.7925 1.2596 0.0419  0.1583  0.0096  132 HIS G CD2 
12410 C CE1 . HIS G  132 ? 1.0143 0.8397 1.2998 0.0534  0.1615  0.0176  132 HIS G CE1 
12411 N NE2 . HIS G  132 ? 0.9539 0.7816 1.2452 0.0474  0.1572  0.0145  132 HIS G NE2 
12412 N N   . ASP G  133 ? 0.9548 0.7562 1.2421 0.0394  0.1845  -0.0001 133 ASP G N   
12413 C CA  . ASP G  133 ? 1.1625 0.9596 1.4480 0.0352  0.1881  -0.0048 133 ASP G CA  
12414 C C   . ASP G  133 ? 1.1731 0.9754 1.4507 0.0318  0.1809  -0.0073 133 ASP G C   
12415 O O   . ASP G  133 ? 1.0479 0.8533 1.3188 0.0364  0.1784  -0.0040 133 ASP G O   
12416 C CB  . ASP G  133 ? 1.1356 0.9257 1.4205 0.0411  0.1979  -0.0024 133 ASP G CB  
12417 C CG  . ASP G  133 ? 1.3932 1.1772 1.6786 0.0366  0.2036  -0.0075 133 ASP G CG  
12418 O OD1 . ASP G  133 ? 1.3853 1.1716 1.6662 0.0310  0.1992  -0.0119 133 ASP G OD1 
12419 O OD2 . ASP G  133 ? 1.5283 1.3051 1.8185 0.0386  0.2128  -0.0071 133 ASP G OD2 
12420 N N   . SER G  134 ? 1.0824 0.8856 1.3605 0.0237  0.1775  -0.0130 134 SER G N   
12421 C CA  . SER G  134 ? 1.0180 0.8261 1.2887 0.0196  0.1706  -0.0158 134 SER G CA  
12422 C C   . SER G  134 ? 1.0731 0.8759 1.3405 0.0161  0.1754  -0.0204 134 SER G C   
12423 O O   . SER G  134 ? 1.2446 1.0500 1.5080 0.0097  0.1707  -0.0248 134 SER G O   
12424 C CB  . SER G  134 ? 1.1498 0.9641 1.4227 0.0125  0.1618  -0.0186 134 SER G CB  
12425 O OG  . SER G  134 ? 1.1804 0.9916 1.4606 0.0068  0.1647  -0.0225 134 SER G OG  
12426 N N   . ASN G  135 ? 1.1591 0.9546 1.4284 0.0203  0.1851  -0.0192 135 ASN G N   
12427 C CA  . ASN G  135 ? 1.2174 1.0069 1.4847 0.0173  0.1913  -0.0235 135 ASN G CA  
12428 C C   . ASN G  135 ? 1.2330 1.0187 1.4964 0.0245  0.1976  -0.0199 135 ASN G C   
12429 O O   . ASN G  135 ? 1.4302 1.2131 1.6893 0.0228  0.2003  -0.0228 135 ASN G O   
12430 C CB  . ASN G  135 ? 1.3439 1.1267 1.6190 0.0133  0.1983  -0.0271 135 ASN G CB  
12431 C CG  . ASN G  135 ? 1.3441 1.1306 1.6228 0.0049  0.1922  -0.0316 135 ASN G CG  
12432 O OD1 . ASN G  135 ? 1.1274 0.9187 1.4015 -0.0011 0.1851  -0.0351 135 ASN G OD1 
12433 N ND2 . ASN G  135 ? 1.2948 1.0791 1.5819 0.0042  0.1951  -0.0314 135 ASN G ND2 
12434 N N   . LYS G  136 ? 1.1747 0.9605 1.4396 0.0326  0.1999  -0.0136 136 LYS G N   
12435 C CA  . LYS G  136 ? 1.2873 1.0700 1.5494 0.0400  0.2060  -0.0093 136 LYS G CA  
12436 C C   . LYS G  136 ? 1.3616 1.1505 1.6152 0.0427  0.1997  -0.0070 136 LYS G C   
12437 O O   . LYS G  136 ? 1.3313 1.1191 1.5819 0.0490  0.2035  -0.0030 136 LYS G O   
12438 C CB  . LYS G  136 ? 1.4486 1.2292 1.7155 0.0474  0.2110  -0.0033 136 LYS G CB  
12439 C CG  . LYS G  136 ? 1.5563 1.3308 1.8318 0.0453  0.2174  -0.0051 136 LYS G CG  
12440 C CD  . LYS G  136 ? 1.6418 1.4088 1.9206 0.0513  0.2283  -0.0018 136 LYS G CD  
12441 C CE  . LYS G  136 ? 1.8111 1.5706 2.0967 0.0465  0.2355  -0.0064 136 LYS G CE  
12442 N NZ  . LYS G  136 ? 1.7842 1.5435 2.0675 0.0379  0.2329  -0.0138 136 LYS G NZ  
12443 N N   . GLY G  137 ? 1.2273 1.0229 1.4773 0.0379  0.1902  -0.0094 137 GLY G N   
12444 C CA  . GLY G  137 ? 1.1575 0.9595 1.3997 0.0402  0.1835  -0.0072 137 GLY G CA  
12445 C C   . GLY G  137 ? 1.1070 0.9081 1.3430 0.0377  0.1839  -0.0105 137 GLY G C   
12446 O O   . GLY G  137 ? 1.0600 0.8655 1.2913 0.0324  0.1768  -0.0139 137 GLY G O   
12447 N N   . VAL G  138 ? 1.0774 0.8727 1.3133 0.0416  0.1923  -0.0093 138 VAL G N   
12448 C CA  . VAL G  138 ? 1.0593 0.8533 1.2896 0.0399  0.1935  -0.0120 138 VAL G CA  
12449 C C   . VAL G  138 ? 0.9965 0.7905 1.2239 0.0482  0.1973  -0.0064 138 VAL G C   
12450 O O   . VAL G  138 ? 0.9227 0.7168 1.1529 0.0549  0.1999  -0.0006 138 VAL G O   
12451 C CB  . VAL G  138 ? 1.1467 0.9327 1.3801 0.0347  0.2010  -0.0176 138 VAL G CB  
12452 C CG1 . VAL G  138 ? 1.1683 0.9547 1.4046 0.0259  0.1973  -0.0234 138 VAL G CG1 
12453 C CG2 . VAL G  138 ? 1.0949 0.8734 1.3345 0.0400  0.2119  -0.0147 138 VAL G CG2 
12454 N N   . THR G  139 ? 0.9595 0.7535 1.1814 0.0475  0.1975  -0.0080 139 THR G N   
12455 C CA  . THR G  139 ? 1.1135 0.9083 1.3324 0.0549  0.2005  -0.0028 139 THR G CA  
12456 C C   . THR G  139 ? 1.2123 1.0037 1.4276 0.0531  0.2042  -0.0059 139 THR G C   
12457 O O   . THR G  139 ? 1.2043 0.9954 1.4166 0.0458  0.2014  -0.0121 139 THR G O   
12458 C CB  . THR G  139 ? 1.0898 0.8934 1.3032 0.0585  0.1918  0.0014  139 THR G CB  
12459 O OG1 . THR G  139 ? 1.0397 0.8444 1.2497 0.0648  0.1944  0.0058  139 THR G OG1 
12460 C CG2 . THR G  139 ? 1.0972 0.9061 1.3051 0.0517  0.1825  -0.0032 139 THR G CG2 
12461 N N   . ALA G  140 ? 1.2885 1.0776 1.5040 0.0597  0.2106  -0.0016 140 ALA G N   
12462 C CA  . ALA G  140 ? 1.3437 1.1298 1.5564 0.0590  0.2148  -0.0038 140 ALA G CA  
12463 C C   . ALA G  140 ? 1.3675 1.1606 1.5720 0.0575  0.2064  -0.0046 140 ALA G C   
12464 O O   . ALA G  140 ? 1.3213 1.1128 1.5222 0.0552  0.2079  -0.0076 140 ALA G O   
12465 C CB  . ALA G  140 ? 1.3859 1.1683 1.6018 0.0670  0.2237  0.0019  140 ALA G CB  
12466 N N   . ALA G  141 ? 1.3633 1.1640 1.5650 0.0589  0.1978  -0.0018 141 ALA G N   
12467 C CA  . ALA G  141 ? 1.2196 1.0274 1.4137 0.0574  0.1892  -0.0025 141 ALA G CA  
12468 C C   . ALA G  141 ? 1.1912 0.9994 1.3822 0.0480  0.1840  -0.0097 141 ALA G C   
12469 O O   . ALA G  141 ? 1.1696 0.9801 1.3546 0.0453  0.1806  -0.0123 141 ALA G O   
12470 C CB  . ALA G  141 ? 1.1052 0.9207 1.2976 0.0614  0.1820  0.0025  141 ALA G CB  
12471 N N   . CYS G  142 ? 1.1029 0.9091 1.2979 0.0430  0.1833  -0.0131 142 CYS G N   
12472 C CA  . CYS G  142 ? 1.0477 0.8544 1.2399 0.0338  0.1784  -0.0199 142 CYS G CA  
12473 C C   . CYS G  142 ? 1.0563 0.8548 1.2520 0.0286  0.1861  -0.0254 142 CYS G C   
12474 O O   . CYS G  142 ? 1.1539 0.9501 1.3541 0.0241  0.1865  -0.0284 142 CYS G O   
12475 C CB  . CYS G  142 ? 1.2565 1.0688 1.4497 0.0308  0.1700  -0.0200 142 CYS G CB  
12476 S SG  . CYS G  142 ? 1.2920 1.1138 1.4812 0.0367  0.1614  -0.0138 142 CYS G SG  
12477 N N   . PRO G  143 ? 1.1339 0.9276 1.3276 0.0291  0.1924  -0.0269 143 PRO G N   
12478 C CA  . PRO G  143 ? 1.2417 1.0266 1.4389 0.0249  0.2012  -0.0318 143 PRO G CA  
12479 C C   . PRO G  143 ? 1.4069 1.1913 1.6006 0.0146  0.1976  -0.0396 143 PRO G C   
12480 O O   . PRO G  143 ? 1.5285 1.3170 1.7152 0.0114  0.1918  -0.0418 143 PRO G O   
12481 C CB  . PRO G  143 ? 1.3659 1.1469 1.5617 0.0295  0.2084  -0.0301 143 PRO G CB  
12482 C CG  . PRO G  143 ? 1.2871 1.0754 1.4793 0.0367  0.2034  -0.0237 143 PRO G CG  
12483 C CD  . PRO G  143 ? 1.2857 1.0819 1.4741 0.0336  0.1921  -0.0241 143 PRO G CD  
12484 N N   . HIS G  144 ? 1.4719 1.2515 1.6705 0.0094  0.2011  -0.0438 144 HIS G N   
12485 C CA  . HIS G  144 ? 1.6057 1.3834 1.8013 -0.0007 0.1997  -0.0516 144 HIS G CA  
12486 C C   . HIS G  144 ? 1.7451 1.5128 1.9436 -0.0025 0.2112  -0.0554 144 HIS G C   
12487 O O   . HIS G  144 ? 1.7090 1.4713 1.9142 -0.0034 0.2173  -0.0566 144 HIS G O   
12488 C CB  . HIS G  144 ? 1.4623 1.2431 1.6610 -0.0066 0.1939  -0.0540 144 HIS G CB  
12489 C CG  . HIS G  144 ? 1.5887 1.3720 1.7821 -0.0166 0.1878  -0.0606 144 HIS G CG  
12490 N ND1 . HIS G  144 ? 1.7338 1.5156 1.9302 -0.0246 0.1873  -0.0658 144 HIS G ND1 
12491 C CD2 . HIS G  144 ? 1.6916 1.4790 1.8768 -0.0201 0.1818  -0.0628 144 HIS G CD2 
12492 C CE1 . HIS G  144 ? 1.7431 1.5281 1.9332 -0.0326 0.1812  -0.0707 144 HIS G CE1 
12493 N NE2 . HIS G  144 ? 1.7312 1.5195 1.9143 -0.0300 0.1778  -0.0691 144 HIS G NE2 
12494 N N   . ALA G  145 ? 1.7398 1.5050 1.9334 -0.0029 0.2145  -0.0573 145 ALA G N   
12495 C CA  . ALA G  145 ? 1.7097 1.4652 1.9055 -0.0046 0.2257  -0.0610 145 ALA G CA  
12496 C C   . ALA G  145 ? 1.7184 1.4682 1.9224 0.0033  0.2354  -0.0561 145 ALA G C   
12497 O O   . ALA G  145 ? 1.6284 1.3723 1.8385 0.0010  0.2414  -0.0583 145 ALA G O   
12498 C CB  . ALA G  145 ? 1.4756 1.2274 1.6715 -0.0152 0.2265  -0.0691 145 ALA G CB  
12499 N N   . GLY G  146 ? 1.9378 1.6896 2.1419 0.0124  0.2366  -0.0492 146 GLY G N   
12500 C CA  . GLY G  146 ? 1.9635 1.7108 2.1748 0.0207  0.2453  -0.0435 146 GLY G CA  
12501 C C   . GLY G  146 ? 1.9600 1.7103 2.1764 0.0241  0.2424  -0.0391 146 GLY G C   
12502 O O   . GLY G  146 ? 1.8417 1.5944 2.0605 0.0326  0.2430  -0.0319 146 GLY G O   
12503 N N   . ALA G  147 ? 1.6759 1.4263 1.8939 0.0172  0.2391  -0.0437 147 ALA G N   
12504 C CA  . ALA G  147 ? 1.6459 1.3985 1.8693 0.0188  0.2366  -0.0409 147 ALA G CA  
12505 C C   . ALA G  147 ? 1.5509 1.3132 1.7712 0.0233  0.2265  -0.0354 147 ALA G C   
12506 O O   . ALA G  147 ? 1.6294 1.3979 1.8429 0.0212  0.2186  -0.0363 147 ALA G O   
12507 C CB  . ALA G  147 ? 1.6713 1.4226 1.8962 0.0092  0.2344  -0.0478 147 ALA G CB  
12508 N N   . LYS G  148 ? 1.4061 1.1697 1.6316 0.0293  0.2271  -0.0297 148 LYS G N   
12509 C CA  . LYS G  148 ? 1.2720 1.0440 1.4952 0.0342  0.2188  -0.0241 148 LYS G CA  
12510 C C   . LYS G  148 ? 1.4012 1.1793 1.6236 0.0285  0.2090  -0.0266 148 LYS G C   
12511 O O   . LYS G  148 ? 1.3482 1.1253 1.5764 0.0276  0.2095  -0.0264 148 LYS G O   
12512 C CB  . LYS G  148 ? 1.2502 1.0209 1.4791 0.0427  0.2236  -0.0171 148 LYS G CB  
12513 C CG  . LYS G  148 ? 1.5172 1.2840 1.7472 0.0503  0.2320  -0.0124 148 LYS G CG  
12514 C CD  . LYS G  148 ? 1.5199 1.2871 1.7547 0.0583  0.2348  -0.0050 148 LYS G CD  
12515 C CE  . LYS G  148 ? 1.5253 1.2882 1.7673 0.0559  0.2381  -0.0066 148 LYS G CE  
12516 N NZ  . LYS G  148 ? 1.4227 1.1859 1.6692 0.0635  0.2407  0.0004  148 LYS G NZ  
12517 N N   . SER G  149 ? 1.4327 1.2171 1.6482 0.0249  0.2002  -0.0285 149 SER G N   
12518 C CA  . SER G  149 ? 1.2628 1.0529 1.4776 0.0188  0.1910  -0.0312 149 SER G CA  
12519 C C   . SER G  149 ? 1.2197 1.0184 1.4320 0.0230  0.1822  -0.0261 149 SER G C   
12520 O O   . SER G  149 ? 1.0149 0.8148 1.2280 0.0309  0.1839  -0.0200 149 SER G O   
12521 C CB  . SER G  149 ? 1.3167 1.1076 1.5260 0.0100  0.1871  -0.0380 149 SER G CB  
12522 O OG  . SER G  149 ? 1.4629 1.2578 1.6733 0.0032  0.1799  -0.0412 149 SER G OG  
12523 N N   . PHE G  150 ? 1.2609 1.0657 1.4703 0.0174  0.1729  -0.0286 150 PHE G N   
12524 C CA  . PHE G  150 ? 1.0227 0.8357 1.2297 0.0203  0.1642  -0.0245 150 PHE G CA  
12525 C C   . PHE G  150 ? 1.0750 0.8939 1.2773 0.0131  0.1546  -0.0283 150 PHE G C   
12526 O O   . PHE G  150 ? 1.1590 0.9757 1.3599 0.0058  0.1547  -0.0341 150 PHE G O   
12527 C CB  . PHE G  150 ? 0.9119 0.7256 1.1259 0.0233  0.1642  -0.0210 150 PHE G CB  
12528 C CG  . PHE G  150 ? 0.8786 0.6994 1.0907 0.0283  0.1576  -0.0157 150 PHE G CG  
12529 C CD1 . PHE G  150 ? 0.8317 0.6538 1.0403 0.0358  0.1591  -0.0106 150 PHE G CD1 
12530 C CD2 . PHE G  150 ? 0.8796 0.7058 1.0935 0.0254  0.1501  -0.0157 150 PHE G CD2 
12531 C CE1 . PHE G  150 ? 0.7583 0.5868 0.9649 0.0400  0.1532  -0.0060 150 PHE G CE1 
12532 C CE2 . PHE G  150 ? 0.8850 0.7173 1.0972 0.0298  0.1445  -0.0110 150 PHE G CE2 
12533 C CZ  . PHE G  150 ? 0.7623 0.5956 0.9706 0.0370  0.1461  -0.0063 150 PHE G CZ  
12534 N N   . TYR G  151 ? 1.0433 0.8696 1.2430 0.0152  0.1465  -0.0251 151 TYR G N   
12535 C CA  . TYR G  151 ? 0.8597 0.6922 1.0554 0.0089  0.1371  -0.0279 151 TYR G CA  
12536 C C   . TYR G  151 ? 0.8548 0.6871 1.0559 0.0019  0.1351  -0.0315 151 TYR G C   
12537 O O   . TYR G  151 ? 0.9263 0.7570 1.1346 0.0038  0.1378  -0.0297 151 TYR G O   
12538 C CB  . TYR G  151 ? 0.8867 0.7268 1.0799 0.0130  0.1295  -0.0232 151 TYR G CB  
12539 C CG  . TYR G  151 ? 0.7848 0.6258 0.9730 0.0201  0.1311  -0.0191 151 TYR G CG  
12540 C CD1 . TYR G  151 ? 0.8475 0.6901 1.0281 0.0188  0.1289  -0.0208 151 TYR G CD1 
12541 C CD2 . TYR G  151 ? 0.6925 0.5330 0.8834 0.0280  0.1346  -0.0135 151 TYR G CD2 
12542 C CE1 . TYR G  151 ? 0.8228 0.6667 0.9993 0.0252  0.1302  -0.0169 151 TYR G CE1 
12543 C CE2 . TYR G  151 ? 0.6483 0.4902 0.8348 0.0344  0.1358  -0.0096 151 TYR G CE2 
12544 C CZ  . TYR G  151 ? 0.7590 0.6027 0.9385 0.0329  0.1336  -0.0113 151 TYR G CZ  
12545 O OH  . TYR G  151 ? 0.7657 0.6112 0.9411 0.0391  0.1346  -0.0074 151 TYR G OH  
12546 N N   . LYS G  152 ? 0.8149 0.6491 1.0126 -0.0061 0.1305  -0.0366 152 LYS G N   
12547 C CA  . LYS G  152 ? 0.9440 0.7786 1.1465 -0.0135 0.1282  -0.0404 152 LYS G CA  
12548 C C   . LYS G  152 ? 0.9519 0.7935 1.1579 -0.0135 0.1202  -0.0374 152 LYS G C   
12549 O O   . LYS G  152 ? 1.0723 0.9136 1.2857 -0.0154 0.1207  -0.0376 152 LYS G O   
12550 C CB  . LYS G  152 ? 1.0242 0.8592 1.2212 -0.0224 0.1254  -0.0465 152 LYS G CB  
12551 C CG  . LYS G  152 ? 1.3639 1.1915 1.5577 -0.0235 0.1336  -0.0503 152 LYS G CG  
12552 C CD  . LYS G  152 ? 1.5792 1.3991 1.7803 -0.0233 0.1429  -0.0517 152 LYS G CD  
12553 C CE  . LYS G  152 ? 1.7542 1.5664 1.9524 -0.0247 0.1515  -0.0556 152 LYS G CE  
12554 N NZ  . LYS G  152 ? 1.7436 1.5478 1.9490 -0.0243 0.1611  -0.0569 152 LYS G NZ  
12555 N N   . ASN G  153 ? 0.9167 0.7648 1.1178 -0.0115 0.1131  -0.0347 153 ASN G N   
12556 C CA  . ASN G  153 ? 0.8190 0.6741 1.0228 -0.0119 0.1051  -0.0320 153 ASN G CA  
12557 C C   . ASN G  153 ? 0.7975 0.6528 1.0064 -0.0041 0.1070  -0.0263 153 ASN G C   
12558 O O   . ASN G  153 ? 0.7473 0.6081 0.9586 -0.0033 0.1010  -0.0235 153 ASN G O   
12559 C CB  . ASN G  153 ? 0.6964 0.5581 0.8927 -0.0132 0.0968  -0.0316 153 ASN G CB  
12560 C CG  . ASN G  153 ? 0.8997 0.7618 1.0907 -0.0214 0.0940  -0.0371 153 ASN G CG  
12561 O OD1 . ASN G  153 ? 1.0751 0.9344 1.2690 -0.0275 0.0961  -0.0414 153 ASN G OD1 
12562 N ND2 . ASN G  153 ? 0.9713 0.8370 1.1544 -0.0218 0.0893  -0.0372 153 ASN G ND2 
12563 N N   . LEU G  154 ? 0.8072 0.6565 1.0178 0.0015  0.1155  -0.0246 154 LEU G N   
12564 C CA  . LEU G  154 ? 0.8888 0.7377 1.1036 0.0090  0.1182  -0.0192 154 LEU G CA  
12565 C C   . LEU G  154 ? 0.9484 0.7899 1.1695 0.0111  0.1276  -0.0193 154 LEU G C   
12566 O O   . LEU G  154 ? 1.0845 0.9203 1.3047 0.0093  0.1336  -0.0224 154 LEU G O   
12567 C CB  . LEU G  154 ? 0.8864 0.7370 1.0949 0.0160  0.1183  -0.0151 154 LEU G CB  
12568 C CG  . LEU G  154 ? 0.7899 0.6478 0.9922 0.0158  0.1094  -0.0138 154 LEU G CG  
12569 C CD1 . LEU G  154 ? 0.8157 0.6745 1.0121 0.0226  0.1107  -0.0101 154 LEU G CD1 
12570 C CD2 . LEU G  154 ? 0.8448 0.7080 1.0516 0.0155  0.1034  -0.0115 154 LEU G CD2 
12571 N N   . ILE G  155 ? 0.9135 0.7548 1.1412 0.0147  0.1292  -0.0159 155 ILE G N   
12572 C CA  . ILE G  155 ? 1.0237 0.8580 1.2575 0.0176  0.1383  -0.0151 155 ILE G CA  
12573 C C   . ILE G  155 ? 0.8928 0.7262 1.1268 0.0266  0.1420  -0.0090 155 ILE G C   
12574 O O   . ILE G  155 ? 0.7630 0.6008 0.9980 0.0296  0.1378  -0.0054 155 ILE G O   
12575 C CB  . ILE G  155 ? 1.0112 0.8449 1.2539 0.0138  0.1383  -0.0164 155 ILE G CB  
12576 C CG1 . ILE G  155 ? 1.0082 0.8420 1.2517 0.0045  0.1358  -0.0226 155 ILE G CG1 
12577 C CG2 . ILE G  155 ? 0.8606 0.6871 1.1093 0.0179  0.1479  -0.0149 155 ILE G CG2 
12578 C CD1 . ILE G  155 ? 1.2955 1.1287 1.5482 0.0005  0.1361  -0.0240 155 ILE G CD1 
12579 N N   . TRP G  156 ? 0.7691 0.5968 1.0023 0.0308  0.1501  -0.0079 156 TRP G N   
12580 C CA  . TRP G  156 ? 0.7903 0.6169 1.0238 0.0394  0.1543  -0.0021 156 TRP G CA  
12581 C C   . TRP G  156 ? 0.9590 0.7812 1.2009 0.0413  0.1601  -0.0004 156 TRP G C   
12582 O O   . TRP G  156 ? 1.1205 0.9359 1.3658 0.0421  0.1683  -0.0012 156 TRP G O   
12583 C CB  . TRP G  156 ? 0.8398 0.6628 1.0688 0.0434  0.1602  -0.0010 156 TRP G CB  
12584 C CG  . TRP G  156 ? 0.8219 0.6450 1.0498 0.0521  0.1636  0.0054  156 TRP G CG  
12585 C CD1 . TRP G  156 ? 0.8225 0.6478 1.0530 0.0564  0.1626  0.0099  156 TRP G CD1 
12586 C CD2 . TRP G  156 ? 0.9257 0.7468 1.1497 0.0575  0.1685  0.0082  156 TRP G CD2 
12587 N NE1 . TRP G  156 ? 0.8398 0.6648 1.0678 0.0639  0.1664  0.0152  156 TRP G NE1 
12588 C CE2 . TRP G  156 ? 0.9244 0.7470 1.1487 0.0648  0.1700  0.0144  156 TRP G CE2 
12589 C CE3 . TRP G  156 ? 0.9490 0.7673 1.1696 0.0567  0.1719  0.0060  156 TRP G CE3 
12590 C CZ2 . TRP G  156 ? 0.9885 0.8104 1.2098 0.0713  0.1745  0.0187  156 TRP G CZ2 
12591 C CZ3 . TRP G  156 ? 1.0315 0.8488 1.2496 0.0634  0.1766  0.0103  156 TRP G CZ3 
12592 C CH2 . TRP G  156 ? 0.9900 0.8093 1.2084 0.0706  0.1777  0.0167  156 TRP G CH2 
12593 N N   . LEU G  157 ? 0.8645 0.6904 1.1098 0.0421  0.1561  0.0019  157 LEU G N   
12594 C CA  . LEU G  157 ? 0.8290 0.6513 1.0825 0.0437  0.1610  0.0035  157 LEU G CA  
12595 C C   . LEU G  157 ? 0.9323 0.7507 1.1859 0.0519  0.1683  0.0087  157 LEU G C   
12596 O O   . LEU G  157 ? 0.8835 0.7053 1.1321 0.0572  0.1665  0.0129  157 LEU G O   
12597 C CB  . LEU G  157 ? 0.7888 0.6162 1.0458 0.0425  0.1546  0.0048  157 LEU G CB  
12598 C CG  . LEU G  157 ? 0.8924 0.7234 1.1521 0.0343  0.1481  0.0001  157 LEU G CG  
12599 C CD1 . LEU G  157 ? 0.8740 0.7091 1.1391 0.0342  0.1435  0.0022  157 LEU G CD1 
12600 C CD2 . LEU G  157 ? 0.9067 0.7321 1.1711 0.0289  0.1529  -0.0048 157 LEU G CD2 
12601 N N   . VAL G  158 ? 1.0203 0.8319 1.2799 0.0526  0.1766  0.0084  158 VAL G N   
12602 C CA  . VAL G  158 ? 0.9471 0.7546 1.2079 0.0601  0.1840  0.0135  158 VAL G CA  
12603 C C   . VAL G  158 ? 0.9993 0.8036 1.2684 0.0607  0.1878  0.0147  158 VAL G C   
12604 O O   . VAL G  158 ? 1.0227 0.8273 1.2970 0.0551  0.1855  0.0110  158 VAL G O   
12605 C CB  . VAL G  158 ? 0.9265 0.7277 1.1865 0.0617  0.1921  0.0128  158 VAL G CB  
12606 C CG1 . VAL G  158 ? 1.0764 0.8807 1.3282 0.0618  0.1889  0.0121  158 VAL G CG1 
12607 C CG2 . VAL G  158 ? 1.0815 0.8769 1.3472 0.0556  0.1965  0.0072  158 VAL G CG2 
12608 N N   . LYS G  159 ? 1.1770 0.9787 1.4474 0.0676  0.1937  0.0198  159 LYS G N   
12609 C CA  . LYS G  159 ? 1.2304 1.0289 1.5083 0.0688  0.1977  0.0215  159 LYS G CA  
12610 C C   . LYS G  159 ? 1.2189 1.0106 1.5039 0.0646  0.2039  0.0173  159 LYS G C   
12611 O O   . LYS G  159 ? 1.0353 0.8223 1.3196 0.0642  0.2093  0.0155  159 LYS G O   
12612 C CB  . LYS G  159 ? 1.2764 1.0730 1.5534 0.0771  0.2031  0.0280  159 LYS G CB  
12613 C CG  . LYS G  159 ? 1.2710 1.0616 1.5475 0.0809  0.2118  0.0296  159 LYS G CG  
12614 C CD  . LYS G  159 ? 1.3770 1.1661 1.6533 0.0889  0.2171  0.0364  159 LYS G CD  
12615 C CE  . LYS G  159 ? 1.3869 1.1696 1.6642 0.0925  0.2264  0.0381  159 LYS G CE  
12616 N NZ  . LYS G  159 ? 1.3963 1.1779 1.6733 0.1003  0.2315  0.0452  159 LYS G NZ  
12617 N N   . LYS G  160 ? 1.4565 1.2477 1.7487 0.0613  0.2033  0.0157  160 LYS G N   
12618 C CA  . LYS G  160 ? 1.5464 1.3314 1.8459 0.0570  0.2091  0.0117  160 LYS G CA  
12619 C C   . LYS G  160 ? 1.6195 1.3980 1.9244 0.0622  0.2185  0.0153  160 LYS G C   
12620 O O   . LYS G  160 ? 1.4555 1.2339 1.7658 0.0631  0.2189  0.0171  160 LYS G O   
12621 C CB  . LYS G  160 ? 1.4188 1.2070 1.7238 0.0500  0.2035  0.0078  160 LYS G CB  
12622 C CG  . LYS G  160 ? 1.5211 1.3033 1.8344 0.0455  0.2094  0.0038  160 LYS G CG  
12623 C CD  . LYS G  160 ? 1.5416 1.3278 1.8605 0.0387  0.2033  0.0003  160 LYS G CD  
12624 C CE  . LYS G  160 ? 1.5565 1.3492 1.8702 0.0330  0.1942  -0.0032 160 LYS G CE  
12625 N NZ  . LYS G  160 ? 1.6353 1.4314 1.9549 0.0253  0.1890  -0.0073 160 LYS G NZ  
12626 N N   . GLY G  161 ? 1.6641 1.4370 1.9677 0.0656  0.2261  0.0165  161 GLY G N   
12627 C CA  . GLY G  161 ? 1.4870 1.2534 1.7954 0.0707  0.2355  0.0201  161 GLY G CA  
12628 C C   . GLY G  161 ? 1.5807 1.3498 1.8886 0.0770  0.2346  0.0264  161 GLY G C   
12629 O O   . GLY G  161 ? 1.7071 1.4746 2.0212 0.0770  0.2365  0.0272  161 GLY G O   
12630 N N   . ASN G  162 ? 1.4775 1.2508 1.7778 0.0820  0.2318  0.0306  162 ASN G N   
12631 C CA  . ASN G  162 ? 1.5893 1.3651 1.8879 0.0883  0.2315  0.0368  162 ASN G CA  
12632 C C   . ASN G  162 ? 1.6139 1.3953 1.9132 0.0862  0.2240  0.0366  162 ASN G C   
12633 O O   . ASN G  162 ? 1.6345 1.4162 1.9353 0.0901  0.2252  0.0407  162 ASN G O   
12634 C CB  . ASN G  162 ? 1.8334 1.6023 2.1375 0.0928  0.2412  0.0404  162 ASN G CB  
12635 C CG  . ASN G  162 ? 1.9721 1.7403 2.2712 0.1006  0.2456  0.0467  162 ASN G CG  
12636 O OD1 . ASN G  162 ? 2.1941 1.9576 2.4966 0.1052  0.2530  0.0507  162 ASN G OD1 
12637 N ND2 . ASN G  162 ? 1.8846 1.6578 2.1759 0.1021  0.2410  0.0479  162 ASN G ND2 
12638 N N   . SER G  163 ? 1.6009 1.3870 1.8993 0.0802  0.2163  0.0320  163 SER G N   
12639 C CA  . SER G  163 ? 1.5902 1.3817 1.8898 0.0779  0.2091  0.0318  163 SER G CA  
12640 C C   . SER G  163 ? 1.4974 1.2958 1.7913 0.0740  0.1997  0.0291  163 SER G C   
12641 O O   . SER G  163 ? 1.4464 1.2449 1.7404 0.0685  0.1975  0.0242  163 SER G O   
12642 C CB  . SER G  163 ? 1.5299 1.3188 1.8392 0.0731  0.2105  0.0285  163 SER G CB  
12643 O OG  . SER G  163 ? 1.3356 1.1294 1.6472 0.0721  0.2048  0.0294  163 SER G OG  
12644 N N   . TYR G  164 ? 1.2434 1.0476 1.5323 0.0770  0.1942  0.0323  164 TYR G N   
12645 C CA  . TYR G  164 ? 1.1589 0.9700 1.4430 0.0734  0.1850  0.0302  164 TYR G CA  
12646 C C   . TYR G  164 ? 1.0919 0.9078 1.3775 0.0737  0.1797  0.0321  164 TYR G C   
12647 O O   . TYR G  164 ? 0.9875 0.8067 1.2678 0.0781  0.1777  0.0360  164 TYR G O   
12648 C CB  . TYR G  164 ? 1.1988 1.0126 1.4735 0.0768  0.1833  0.0321  164 TYR G CB  
12649 C CG  . TYR G  164 ? 1.1775 0.9971 1.4471 0.0724  0.1748  0.0289  164 TYR G CG  
12650 C CD1 . TYR G  164 ? 1.1524 0.9712 1.4180 0.0700  0.1748  0.0259  164 TYR G CD1 
12651 C CD2 . TYR G  164 ? 1.0181 0.8438 1.2873 0.0704  0.1671  0.0289  164 TYR G CD2 
12652 C CE1 . TYR G  164 ? 1.1008 0.9248 1.3617 0.0659  0.1671  0.0230  164 TYR G CE1 
12653 C CE2 . TYR G  164 ? 0.9079 0.7389 1.1726 0.0663  0.1594  0.0261  164 TYR G CE2 
12654 C CZ  . TYR G  164 ? 1.0269 0.8571 1.2873 0.0641  0.1594  0.0232  164 TYR G CZ  
12655 O OH  . TYR G  164 ? 0.9571 0.7925 1.2129 0.0600  0.1518  0.0205  164 TYR G OH  
12656 N N   . PRO G  165 ? 0.9081 0.7243 1.2013 0.0688  0.1776  0.0293  165 PRO G N   
12657 C CA  . PRO G  165 ? 1.0706 0.8910 1.3669 0.0684  0.1729  0.0306  165 PRO G CA  
12658 C C   . PRO G  165 ? 1.0880 0.9157 1.3790 0.0659  0.1636  0.0296  165 PRO G C   
12659 O O   . PRO G  165 ? 0.9387 0.7680 1.2264 0.0621  0.1603  0.0263  165 PRO G O   
12660 C CB  . PRO G  165 ? 1.0178 0.8363 1.3243 0.0630  0.1737  0.0272  165 PRO G CB  
12661 C CG  . PRO G  165 ? 1.1782 0.9902 1.4868 0.0618  0.1805  0.0248  165 PRO G CG  
12662 C CD  . PRO G  165 ? 0.9886 0.8010 1.2883 0.0632  0.1801  0.0246  165 PRO G CD  
12663 N N   . LYS G  166 ? 0.8525 0.6844 1.1427 0.0679  0.1597  0.0323  166 LYS G N   
12664 C CA  . LYS G  166 ? 0.9778 0.8165 1.2638 0.0654  0.1510  0.0314  166 LYS G CA  
12665 C C   . LYS G  166 ? 1.1063 0.9472 1.3968 0.0580  0.1461  0.0267  166 LYS G C   
12666 O O   . LYS G  166 ? 1.0650 0.9054 1.3642 0.0548  0.1461  0.0255  166 LYS G O   
12667 C CB  . LYS G  166 ? 0.9314 0.7735 1.2186 0.0676  0.1482  0.0346  166 LYS G CB  
12668 C CG  . LYS G  166 ? 1.0627 0.9116 1.3491 0.0637  0.1393  0.0331  166 LYS G CG  
12669 C CD  . LYS G  166 ? 1.2641 1.1156 1.5539 0.0652  0.1373  0.0357  166 LYS G CD  
12670 C CE  . LYS G  166 ? 1.2893 1.1417 1.5712 0.0711  0.1382  0.0397  166 LYS G CE  
12671 N NZ  . LYS G  166 ? 1.4733 1.3285 1.7578 0.0720  0.1358  0.0418  166 LYS G NZ  
12672 N N   . LEU G  167 ? 0.9964 0.8399 1.2812 0.0551  0.1418  0.0241  167 LEU G N   
12673 C CA  . LEU G  167 ? 1.0398 0.8863 1.3277 0.0478  0.1363  0.0198  167 LEU G CA  
12674 C C   . LEU G  167 ? 1.1023 0.9560 1.3889 0.0460  0.1276  0.0204  167 LEU G C   
12675 O O   . LEU G  167 ? 0.9818 0.8382 1.2622 0.0500  0.1255  0.0233  167 LEU G O   
12676 C CB  . LEU G  167 ? 0.8558 0.7007 1.1387 0.0448  0.1367  0.0162  167 LEU G CB  
12677 C CG  . LEU G  167 ? 0.9258 0.7730 1.1982 0.0467  0.1341  0.0166  167 LEU G CG  
12678 C CD1 . LEU G  167 ? 0.8898 0.7445 1.1587 0.0447  0.1250  0.0167  167 LEU G CD1 
12679 C CD2 . LEU G  167 ? 0.9695 0.8137 1.2392 0.0432  0.1362  0.0126  167 LEU G CD2 
12680 N N   . SER G  168 ? 1.0230 0.8799 1.3153 0.0400  0.1227  0.0178  168 SER G N   
12681 C CA  . SER G  168 ? 0.8932 0.7570 1.1855 0.0380  0.1145  0.0185  168 SER G CA  
12682 C C   . SER G  168 ? 1.0188 0.8864 1.3145 0.0303  0.1086  0.0147  168 SER G C   
12683 O O   . SER G  168 ? 1.3306 1.1997 1.6352 0.0270  0.1069  0.0142  168 SER G O   
12684 C CB  . SER G  168 ? 1.0631 0.9277 1.3618 0.0408  0.1150  0.0219  168 SER G CB  
12685 O OG  . SER G  168 ? 1.1763 1.0468 1.4726 0.0411  0.1085  0.0236  168 SER G OG  
12686 N N   . LYS G  169 ? 0.9542 0.8233 1.2428 0.0275  0.1054  0.0120  169 LYS G N   
12687 C CA  . LYS G  169 ? 0.9765 0.8496 1.2665 0.0201  0.0993  0.0085  169 LYS G CA  
12688 C C   . LYS G  169 ? 0.9673 0.8474 1.2527 0.0193  0.0909  0.0096  169 LYS G C   
12689 O O   . LYS G  169 ? 0.8674 0.7483 1.1458 0.0238  0.0904  0.0119  169 LYS G O   
12690 C CB  . LYS G  169 ? 0.8875 0.7574 1.1726 0.0169  0.1016  0.0043  169 LYS G CB  
12691 C CG  . LYS G  169 ? 1.0933 0.9599 1.3856 0.0118  0.1049  0.0008  169 LYS G CG  
12692 C CD  . LYS G  169 ? 1.1899 1.0624 1.4873 0.0045  0.0977  -0.0014 169 LYS G CD  
12693 C CE  . LYS G  169 ? 1.2384 1.1079 1.5408 -0.0016 0.1005  -0.0058 169 LYS G CE  
12694 N NZ  . LYS G  169 ? 1.3118 1.1757 1.6222 0.0009  0.1081  -0.0050 169 LYS G NZ  
12695 N N   . SER G  170 ? 1.0470 0.9322 1.3367 0.0133  0.0844  0.0081  170 SER G N   
12696 C CA  . SER G  170 ? 0.9236 0.8156 1.2095 0.0119  0.0763  0.0091  170 SER G CA  
12697 C C   . SER G  170 ? 0.8769 0.7736 1.1651 0.0040  0.0698  0.0060  170 SER G C   
12698 O O   . SER G  170 ? 0.9793 0.8771 1.2764 0.0001  0.0691  0.0051  170 SER G O   
12699 C CB  . SER G  170 ? 0.9049 0.7998 1.1956 0.0155  0.0744  0.0133  170 SER G CB  
12700 O OG  . SER G  170 ? 1.3988 1.2939 1.7007 0.0135  0.0752  0.0137  170 SER G OG  
12701 N N   . TYR G  171 ? 0.8830 0.7826 1.1629 0.0016  0.0652  0.0043  171 TYR G N   
12702 C CA  . TYR G  171 ? 0.8768 0.7810 1.1570 -0.0060 0.0588  0.0014  171 TYR G CA  
12703 C C   . TYR G  171 ? 0.8564 0.7681 1.1362 -0.0071 0.0504  0.0037  171 TYR G C   
12704 O O   . TYR G  171 ? 0.7216 0.6344 0.9959 -0.0026 0.0492  0.0062  171 TYR G O   
12705 C CB  . TYR G  171 ? 0.8955 0.7973 1.1666 -0.0088 0.0598  -0.0026 171 TYR G CB  
12706 C CG  . TYR G  171 ? 0.8778 0.7853 1.1455 -0.0156 0.0521  -0.0050 171 TYR G CG  
12707 C CD1 . TYR G  171 ? 0.8277 0.7364 1.0996 -0.0231 0.0503  -0.0084 171 TYR G CD1 
12708 C CD2 . TYR G  171 ? 0.9437 0.8553 1.2038 -0.0149 0.0467  -0.0039 171 TYR G CD2 
12709 C CE1 . TYR G  171 ? 0.9123 0.8265 1.1808 -0.0296 0.0431  -0.0105 171 TYR G CE1 
12710 C CE2 . TYR G  171 ? 0.9722 0.8890 1.2290 -0.0212 0.0397  -0.0059 171 TYR G CE2 
12711 C CZ  . TYR G  171 ? 0.9811 0.8992 1.2419 -0.0285 0.0379  -0.0092 171 TYR G CZ  
12712 O OH  . TYR G  171 ? 1.0155 0.9389 1.2726 -0.0349 0.0308  -0.0111 171 TYR G OH  
12713 N N   . ILE G  172 ? 0.8464 0.7633 1.1322 -0.0131 0.0447  0.0030  172 ILE G N   
12714 C CA  . ILE G  172 ? 0.8888 0.8131 1.1751 -0.0147 0.0366  0.0053  172 ILE G CA  
12715 C C   . ILE G  172 ? 0.9106 0.8390 1.1914 -0.0215 0.0304  0.0023  172 ILE G C   
12716 O O   . ILE G  172 ? 0.9509 0.8792 1.2337 -0.0274 0.0302  -0.0011 172 ILE G O   
12717 C CB  . ILE G  172 ? 0.8382 0.7663 1.1368 -0.0157 0.0341  0.0081  172 ILE G CB  
12718 C CG1 . ILE G  172 ? 0.8703 0.8058 1.1694 -0.0166 0.0262  0.0111  172 ILE G CG1 
12719 C CG2 . ILE G  172 ? 1.0640 0.9929 1.3700 -0.0222 0.0338  0.0054  172 ILE G CG2 
12720 C CD1 . ILE G  172 ? 0.9909 0.9275 1.2974 -0.0117 0.0267  0.0156  172 ILE G CD1 
12721 N N   . ASN G  173 ? 0.9108 0.8427 1.1843 -0.0207 0.0255  0.0035  173 ASN G N   
12722 C CA  . ASN G  173 ? 0.8880 0.8238 1.1550 -0.0267 0.0197  0.0008  173 ASN G CA  
12723 C C   . ASN G  173 ? 1.0051 0.9477 1.2790 -0.0334 0.0127  0.0010  173 ASN G C   
12724 O O   . ASN G  173 ? 0.9041 0.8526 1.1808 -0.0332 0.0068  0.0044  173 ASN G O   
12725 C CB  . ASN G  173 ? 0.8260 0.7638 1.0837 -0.0237 0.0164  0.0024  173 ASN G CB  
12726 C CG  . ASN G  173 ? 0.9467 0.8870 1.1958 -0.0292 0.0118  -0.0008 173 ASN G CG  
12727 O OD1 . ASN G  173 ? 0.9915 0.9322 1.2414 -0.0356 0.0108  -0.0042 173 ASN G OD1 
12728 N ND2 . ASN G  173 ? 0.9214 0.8633 1.1623 -0.0269 0.0092  0.0002  173 ASN G ND2 
12729 N N   . ASP G  174 ? 1.1274 1.0694 1.4043 -0.0393 0.0134  -0.0025 174 ASP G N   
12730 C CA  . ASP G  174 ? 1.0863 1.0350 1.3698 -0.0463 0.0069  -0.0025 174 ASP G CA  
12731 C C   . ASP G  174 ? 1.1304 1.0834 1.4056 -0.0525 0.0006  -0.0050 174 ASP G C   
12732 O O   . ASP G  174 ? 1.3325 1.2919 1.6115 -0.0588 -0.0057 -0.0050 174 ASP G O   
12733 C CB  . ASP G  174 ? 1.2193 1.1658 1.5107 -0.0501 0.0107  -0.0050 174 ASP G CB  
12734 C CG  . ASP G  174 ? 1.3988 1.3386 1.6834 -0.0521 0.0164  -0.0103 174 ASP G CG  
12735 O OD1 . ASP G  174 ? 1.5085 1.4502 1.7901 -0.0595 0.0136  -0.0141 174 ASP G OD1 
12736 O OD2 . ASP G  174 ? 1.3427 1.2754 1.6250 -0.0465 0.0240  -0.0106 174 ASP G OD2 
12737 N N   . LYS G  175 ? 0.9904 0.9399 1.2543 -0.0506 0.0024  -0.0069 175 LYS G N   
12738 C CA  . LYS G  175 ? 1.0069 0.9598 1.2618 -0.0559 -0.0029 -0.0092 175 LYS G CA  
12739 C C   . LYS G  175 ? 1.0593 1.0193 1.3137 -0.0553 -0.0107 -0.0051 175 LYS G C   
12740 O O   . LYS G  175 ? 1.0844 1.0460 1.3447 -0.0502 -0.0111 -0.0008 175 LYS G O   
12741 C CB  . LYS G  175 ? 1.0049 0.9516 1.2483 -0.0536 0.0019  -0.0123 175 LYS G CB  
12742 C CG  . LYS G  175 ? 1.0144 0.9531 1.2580 -0.0529 0.0106  -0.0158 175 LYS G CG  
12743 C CD  . LYS G  175 ? 0.9271 0.8660 1.1715 -0.0614 0.0101  -0.0206 175 LYS G CD  
12744 C CE  . LYS G  175 ? 0.9053 0.8357 1.1491 -0.0607 0.0193  -0.0244 175 LYS G CE  
12745 N NZ  . LYS G  175 ? 1.1749 1.1049 1.4186 -0.0693 0.0193  -0.0295 175 LYS G NZ  
12746 N N   . GLY G  176 ? 0.8405 0.8048 1.0880 -0.0606 -0.0167 -0.0066 176 GLY G N   
12747 C CA  . GLY G  176 ? 1.1373 1.1082 1.3835 -0.0603 -0.0239 -0.0029 176 GLY G CA  
12748 C C   . GLY G  176 ? 1.0746 1.0432 1.3093 -0.0567 -0.0233 -0.0034 176 GLY G C   
12749 O O   . GLY G  176 ? 1.1292 1.1027 1.3595 -0.0578 -0.0293 -0.0018 176 GLY G O   
12750 N N   . LYS G  177 ? 1.0567 1.0179 1.2867 -0.0523 -0.0159 -0.0055 177 LYS G N   
12751 C CA  . LYS G  177 ? 0.9487 0.9072 1.1678 -0.0488 -0.0143 -0.0063 177 LYS G CA  
12752 C C   . LYS G  177 ? 0.8511 0.8028 1.0701 -0.0411 -0.0063 -0.0056 177 LYS G C   
12753 O O   . LYS G  177 ? 0.8927 0.8408 1.1184 -0.0398 -0.0012 -0.0059 177 LYS G O   
12754 C CB  . LYS G  177 ? 0.9558 0.9124 1.1659 -0.0546 -0.0141 -0.0115 177 LYS G CB  
12755 C CG  . LYS G  177 ? 0.8565 0.8076 1.0687 -0.0572 -0.0080 -0.0156 177 LYS G CG  
12756 C CD  . LYS G  177 ? 0.9226 0.8723 1.1263 -0.0638 -0.0083 -0.0208 177 LYS G CD  
12757 C CE  . LYS G  177 ? 1.0870 1.0441 1.2911 -0.0720 -0.0166 -0.0213 177 LYS G CE  
12758 N NZ  . LYS G  177 ? 1.1311 1.0911 1.3461 -0.0757 -0.0181 -0.0207 177 LYS G NZ  
12759 N N   . GLU G  178 ? 0.8275 0.7778 1.0389 -0.0362 -0.0052 -0.0047 178 GLU G N   
12760 C CA  . GLU G  178 ? 0.8145 0.7588 1.0248 -0.0289 0.0021  -0.0038 178 GLU G CA  
12761 C C   . GLU G  178 ? 0.8720 0.8098 1.0814 -0.0298 0.0091  -0.0076 178 GLU G C   
12762 O O   . GLU G  178 ? 0.8599 0.7970 1.0656 -0.0356 0.0086  -0.0116 178 GLU G O   
12763 C CB  . GLU G  178 ? 0.8316 0.7758 1.0326 -0.0247 0.0017  -0.0028 178 GLU G CB  
12764 C CG  . GLU G  178 ? 1.0486 0.9986 1.2500 -0.0232 -0.0044 0.0010  178 GLU G CG  
12765 C CD  . GLU G  178 ? 1.1551 1.1052 1.3466 -0.0201 -0.0050 0.0013  178 GLU G CD  
12766 O OE1 . GLU G  178 ? 1.0519 1.0007 1.2355 -0.0228 -0.0050 -0.0020 178 GLU G OE1 
12767 O OE2 . GLU G  178 ? 1.3066 1.2580 1.4983 -0.0150 -0.0055 0.0046  178 GLU G OE2 
12768 N N   . VAL G  179 ? 0.7008 0.6336 0.9135 -0.0240 0.0159  -0.0063 179 VAL G N   
12769 C CA  . VAL G  179 ? 0.7452 0.6713 0.9579 -0.0238 0.0234  -0.0094 179 VAL G CA  
12770 C C   . VAL G  179 ? 0.7188 0.6400 0.9258 -0.0168 0.0294  -0.0084 179 VAL G C   
12771 O O   . VAL G  179 ? 0.6286 0.5493 0.8381 -0.0106 0.0314  -0.0048 179 VAL G O   
12772 C CB  . VAL G  179 ? 0.7136 0.6381 0.9373 -0.0242 0.0264  -0.0088 179 VAL G CB  
12773 C CG1 . VAL G  179 ? 0.7485 0.6653 0.9730 -0.0208 0.0355  -0.0101 179 VAL G CG1 
12774 C CG2 . VAL G  179 ? 0.6950 0.6231 0.9231 -0.0325 0.0219  -0.0113 179 VAL G CG2 
12775 N N   . LEU G  180 ? 0.6813 0.5992 0.8805 -0.0178 0.0321  -0.0116 180 LEU G N   
12776 C CA  . LEU G  180 ? 0.6352 0.5485 0.8291 -0.0115 0.0381  -0.0108 180 LEU G CA  
12777 C C   . LEU G  180 ? 0.6086 0.5155 0.8076 -0.0086 0.0464  -0.0110 180 LEU G C   
12778 O O   . LEU G  180 ? 0.7472 0.6503 0.9471 -0.0123 0.0500  -0.0146 180 LEU G O   
12779 C CB  . LEU G  180 ? 0.6645 0.5766 0.8488 -0.0138 0.0383  -0.0141 180 LEU G CB  
12780 C CG  . LEU G  180 ? 0.6309 0.5388 0.8094 -0.0077 0.0441  -0.0134 180 LEU G CG  
12781 C CD1 . LEU G  180 ? 0.6379 0.5496 0.8121 -0.0027 0.0408  -0.0097 180 LEU G CD1 
12782 C CD2 . LEU G  180 ? 0.5768 0.4816 0.7483 -0.0113 0.0462  -0.0177 180 LEU G CD2 
12783 N N   . VAL G  181 ? 0.6443 0.5501 0.8466 -0.0019 0.0495  -0.0071 181 VAL G N   
12784 C CA  . VAL G  181 ? 0.6365 0.5363 0.8435 0.0016  0.0576  -0.0068 181 VAL G CA  
12785 C C   . VAL G  181 ? 0.6915 0.5876 0.8927 0.0080  0.0631  -0.0052 181 VAL G C   
12786 O O   . VAL G  181 ? 0.6926 0.5914 0.8903 0.0127  0.0614  -0.0020 181 VAL G O   
12787 C CB  . VAL G  181 ? 0.5859 0.4864 0.8017 0.0042  0.0580  -0.0034 181 VAL G CB  
12788 C CG1 . VAL G  181 ? 0.6913 0.5854 0.9124 0.0069  0.0664  -0.0034 181 VAL G CG1 
12789 C CG2 . VAL G  181 ? 0.6392 0.5445 0.8612 -0.0018 0.0518  -0.0042 181 VAL G CG2 
12790 N N   . LEU G  182 ? 0.7515 0.6417 0.9519 0.0082  0.0699  -0.0075 182 LEU G N   
12791 C CA  . LEU G  182 ? 0.7209 0.6075 0.9167 0.0144  0.0757  -0.0057 182 LEU G CA  
12792 C C   . LEU G  182 ? 0.6310 0.5121 0.8329 0.0186  0.0835  -0.0040 182 LEU G C   
12793 O O   . LEU G  182 ? 0.6416 0.5198 0.8499 0.0154  0.0861  -0.0060 182 LEU G O   
12794 C CB  . LEU G  182 ? 0.5529 0.4369 0.7421 0.0120  0.0777  -0.0093 182 LEU G CB  
12795 C CG  . LEU G  182 ? 0.6673 0.5562 0.8491 0.0085  0.0708  -0.0109 182 LEU G CG  
12796 C CD1 . LEU G  182 ? 0.7741 0.6630 0.9558 0.0001  0.0681  -0.0159 182 LEU G CD1 
12797 C CD2 . LEU G  182 ? 0.6295 0.5171 0.8036 0.0124  0.0734  -0.0104 182 LEU G CD2 
12798 N N   . TRP G  183 ? 0.6159 0.4958 0.8157 0.0257  0.0873  -0.0003 183 TRP G N   
12799 C CA  . TRP G  183 ? 0.5976 0.4725 0.8024 0.0303  0.0949  0.0019  183 TRP G CA  
12800 C C   . TRP G  183 ? 0.6808 0.5540 0.8803 0.0371  0.0993  0.0049  183 TRP G C   
12801 O O   . TRP G  183 ? 0.6917 0.5684 0.8843 0.0384  0.0959  0.0057  183 TRP G O   
12802 C CB  . TRP G  183 ? 0.7174 0.5940 0.9288 0.0321  0.0935  0.0048  183 TRP G CB  
12803 C CG  . TRP G  183 ? 0.5969 0.4780 0.8050 0.0368  0.0902  0.0089  183 TRP G CG  
12804 C CD1 . TRP G  183 ? 0.6461 0.5259 0.8525 0.0436  0.0942  0.0129  183 TRP G CD1 
12805 C CD2 . TRP G  183 ? 0.6970 0.5844 0.9030 0.0349  0.0821  0.0094  183 TRP G CD2 
12806 N NE1 . TRP G  183 ? 0.6011 0.4861 0.8043 0.0459  0.0893  0.0156  183 TRP G NE1 
12807 C CE2 . TRP G  183 ? 0.6768 0.5663 0.8798 0.0407  0.0820  0.0135  183 TRP G CE2 
12808 C CE3 . TRP G  183 ? 0.7261 0.6177 0.9323 0.0287  0.0751  0.0069  183 TRP G CE3 
12809 C CZ2 . TRP G  183 ? 0.6832 0.5784 0.8836 0.0406  0.0755  0.0150  183 TRP G CZ2 
12810 C CZ3 . TRP G  183 ? 0.6611 0.5584 0.8650 0.0289  0.0686  0.0087  183 TRP G CZ3 
12811 C CH2 . TRP G  183 ? 0.6383 0.5372 0.8394 0.0348  0.0689  0.0126  183 TRP G CH2 
12812 N N   . GLY G  184 ? 0.6521 0.5202 0.8551 0.0413  0.1070  0.0068  184 GLY G N   
12813 C CA  . GLY G  184 ? 0.4856 0.3521 0.6842 0.0477  0.1117  0.0099  184 GLY G CA  
12814 C C   . GLY G  184 ? 0.6228 0.4875 0.8249 0.0540  0.1164  0.0146  184 GLY G C   
12815 O O   . GLY G  184 ? 0.6907 0.5527 0.8998 0.0535  0.1191  0.0148  184 GLY G O   
12816 N N   . ILE G  185 ? 0.5298 0.3964 0.7271 0.0598  0.1173  0.0185  185 ILE G N   
12817 C CA  . ILE G  185 ? 0.5493 0.4143 0.7487 0.0662  0.1222  0.0233  185 ILE G CA  
12818 C C   . ILE G  185 ? 0.7118 0.5731 0.9091 0.0707  0.1291  0.0252  185 ILE G C   
12819 O O   . ILE G  185 ? 0.6998 0.5636 0.8908 0.0728  0.1280  0.0263  185 ILE G O   
12820 C CB  . ILE G  185 ? 0.6029 0.4736 0.7984 0.0696  0.1176  0.0270  185 ILE G CB  
12821 C CG1 . ILE G  185 ? 0.6639 0.5382 0.8621 0.0653  0.1110  0.0254  185 ILE G CG1 
12822 C CG2 . ILE G  185 ? 0.5445 0.4134 0.7420 0.0757  0.1228  0.0318  185 ILE G CG2 
12823 C CD1 . ILE G  185 ? 0.6180 0.4888 0.8248 0.0640  0.1138  0.0250  185 ILE G CD1 
12824 N N   . HIS G  186 ? 0.7722 0.6275 0.9751 0.0722  0.1364  0.0258  186 HIS G N   
12825 C CA  . HIS G  186 ? 0.7461 0.5975 0.9481 0.0765  0.1437  0.0278  186 HIS G CA  
12826 C C   . HIS G  186 ? 0.6308 0.4835 0.8313 0.0838  0.1465  0.0340  186 HIS G C   
12827 O O   . HIS G  186 ? 0.6875 0.5400 0.8914 0.0858  0.1473  0.0364  186 HIS G O   
12828 C CB  . HIS G  186 ? 0.7966 0.6406 1.0052 0.0746  0.1508  0.0254  186 HIS G CB  
12829 C CG  . HIS G  186 ? 0.8712 0.7106 1.0799 0.0793  0.1589  0.0278  186 HIS G CG  
12830 N ND1 . HIS G  186 ? 0.8410 0.6762 1.0543 0.0840  0.1660  0.0315  186 HIS G ND1 
12831 C CD2 . HIS G  186 ? 0.8872 0.7256 1.0921 0.0802  0.1612  0.0273  186 HIS G CD2 
12832 C CE1 . HIS G  186 ? 0.8733 0.7052 1.0859 0.0876  0.1723  0.0334  186 HIS G CE1 
12833 N NE2 . HIS G  186 ? 0.8144 0.6481 1.0220 0.0854  0.1696  0.0309  186 HIS G NE2 
12834 N N   . HIS G  187 ? 0.7626 0.6168 0.9579 0.0877  0.1479  0.0365  187 HIS G N   
12835 C CA  . HIS G  187 ? 0.7531 0.6089 0.9465 0.0947  0.1507  0.0426  187 HIS G CA  
12836 C C   . HIS G  187 ? 0.8864 0.7372 1.0817 0.0986  0.1592  0.0448  187 HIS G C   
12837 O O   . HIS G  187 ? 0.9102 0.7617 1.1020 0.0997  0.1601  0.0449  187 HIS G O   
12838 C CB  . HIS G  187 ? 0.7279 0.5908 0.9135 0.0965  0.1448  0.0445  187 HIS G CB  
12839 C CG  . HIS G  187 ? 0.8252 0.6930 1.0087 0.0927  0.1366  0.0423  187 HIS G CG  
12840 N ND1 . HIS G  187 ? 0.8034 0.6740 0.9872 0.0942  0.1342  0.0448  187 HIS G ND1 
12841 C CD2 . HIS G  187 ? 0.8065 0.6769 0.9876 0.0873  0.1304  0.0379  187 HIS G CD2 
12842 C CE1 . HIS G  187 ? 0.8570 0.7316 1.0391 0.0902  0.1270  0.0422  187 HIS G CE1 
12843 N NE2 . HIS G  187 ? 0.8678 0.7425 1.0482 0.0860  0.1245  0.0381  187 HIS G NE2 
12844 N N   . PRO G  188 ? 0.8132 0.6589 1.0145 0.1008  0.1656  0.0466  188 PRO G N   
12845 C CA  . PRO G  188 ? 0.8824 0.7226 1.0866 0.1046  0.1743  0.0490  188 PRO G CA  
12846 C C   . PRO G  188 ? 0.9283 0.7721 1.1277 0.1110  0.1757  0.0546  188 PRO G C   
12847 O O   . PRO G  188 ? 0.8082 0.6582 1.0027 0.1131  0.1707  0.0575  188 PRO G O   
12848 C CB  . PRO G  188 ? 0.9172 0.7530 1.1279 0.1063  0.1793  0.0510  188 PRO G CB  
12849 C CG  . PRO G  188 ? 0.8673 0.7043 1.0802 0.1010  0.1739  0.0471  188 PRO G CG  
12850 C CD  . PRO G  188 ? 0.7933 0.6378 0.9995 0.0995  0.1651  0.0465  188 PRO G CD  
12851 N N   . SER G  189 ? 1.0365 0.8764 1.2376 0.1138  0.1825  0.0563  189 SER G N   
12852 C CA  . SER G  189 ? 0.9768 0.8200 1.1741 0.1198  0.1843  0.0618  189 SER G CA  
12853 C C   . SER G  189 ? 0.8651 0.7086 1.0639 0.1260  0.1882  0.0684  189 SER G C   
12854 O O   . SER G  189 ? 0.8297 0.6789 1.0236 0.1302  0.1859  0.0732  189 SER G O   
12855 C CB  . SER G  189 ? 0.9347 0.7737 1.1337 0.1205  0.1903  0.0611  189 SER G CB  
12856 O OG  . SER G  189 ? 1.1316 0.9626 1.3378 0.1206  0.1983  0.0606  189 SER G OG  
12857 N N   . THR G  190 ? 1.0528 0.8901 1.2580 0.1263  0.1940  0.0686  190 THR G N   
12858 C CA  . THR G  190 ? 1.0775 0.9141 1.2845 0.1320  0.1986  0.0748  190 THR G CA  
12859 C C   . THR G  190 ? 1.0553 0.8893 1.2663 0.1300  0.1985  0.0736  190 THR G C   
12860 O O   . THR G  190 ? 1.0397 0.8702 1.2546 0.1246  0.1977  0.0681  190 THR G O   
12861 C CB  . THR G  190 ? 1.0634 0.8944 1.2750 0.1363  0.2081  0.0782  190 THR G CB  
12862 O OG1 . THR G  190 ? 1.3774 1.2047 1.5934 0.1394  0.2134  0.0819  190 THR G OG1 
12863 C CG2 . THR G  190 ? 1.0063 0.8309 1.2223 0.1319  0.2117  0.0726  190 THR G CG2 
12864 N N   . SER G  191 ? 1.2049 1.0409 1.4151 0.1344  0.1995  0.0789  191 SER G N   
12865 C CA  . SER G  191 ? 1.2153 1.0488 1.4294 0.1332  0.2000  0.0784  191 SER G CA  
12866 C C   . SER G  191 ? 1.0991 0.9240 1.3214 0.1322  0.2077  0.0767  191 SER G C   
12867 O O   . SER G  191 ? 1.0887 0.9106 1.3156 0.1291  0.2078  0.0740  191 SER G O   
12868 C CB  . SER G  191 ? 1.0462 0.8831 1.2574 0.1384  0.2005  0.0847  191 SER G CB  
12869 O OG  . SER G  191 ? 1.2245 1.0591 1.4368 0.1442  0.2077  0.0904  191 SER G OG  
12870 N N   . ALA G  192 ? 1.2156 1.0366 1.4400 0.1349  0.2142  0.0784  192 ALA G N   
12871 C CA  . ALA G  192 ? 1.2325 1.0451 1.4646 0.1338  0.2220  0.0765  192 ALA G CA  
12872 C C   . ALA G  192 ? 1.2406 1.0506 1.4751 0.1265  0.2196  0.0686  192 ALA G C   
12873 O O   . ALA G  192 ? 1.1346 0.9391 1.3752 0.1231  0.2225  0.0652  192 ALA G O   
12874 C CB  . ALA G  192 ? 1.2780 1.0875 1.5117 0.1388  0.2296  0.0806  192 ALA G CB  
12875 N N   . ASP G  193 ? 1.2347 1.0487 1.4643 0.1239  0.2142  0.0658  193 ASP G N   
12876 C CA  . ASP G  193 ? 1.2247 1.0373 1.4552 0.1167  0.2108  0.0584  193 ASP G CA  
12877 C C   . ASP G  193 ? 1.0956 0.9108 1.3268 0.1121  0.2043  0.0552  193 ASP G C   
12878 O O   . ASP G  193 ? 0.9069 0.7192 1.1419 0.1062  0.2034  0.0497  193 ASP G O   
12879 C CB  . ASP G  193 ? 1.1475 0.9644 1.3718 0.1153  0.2062  0.0566  193 ASP G CB  
12880 C CG  . ASP G  193 ? 1.4609 1.2725 1.6873 0.1151  0.2126  0.0550  193 ASP G CG  
12881 O OD1 . ASP G  193 ? 1.5806 1.3877 1.8108 0.1197  0.2207  0.0589  193 ASP G OD1 
12882 O OD2 . ASP G  193 ? 1.6858 1.4978 1.9100 0.1102  0.2096  0.0499  193 ASP G OD2 
12883 N N   . GLN G  194 ? 1.0212 0.8418 1.2487 0.1148  0.1998  0.0589  194 GLN G N   
12884 C CA  . GLN G  194 ? 0.9596 0.7830 1.1879 0.1112  0.1938  0.0566  194 GLN G CA  
12885 C C   . GLN G  194 ? 1.1312 0.9487 1.3676 0.1096  0.1985  0.0553  194 GLN G C   
12886 O O   . GLN G  194 ? 1.1165 0.9326 1.3567 0.1037  0.1961  0.0501  194 GLN G O   
12887 C CB  . GLN G  194 ? 1.0247 0.8544 1.2478 0.1151  0.1895  0.0612  194 GLN G CB  
12888 C CG  . GLN G  194 ? 1.0167 0.8485 1.2415 0.1123  0.1848  0.0598  194 GLN G CG  
12889 C CD  . GLN G  194 ? 1.0063 0.8416 1.2297 0.1061  0.1769  0.0544  194 GLN G CD  
12890 O OE1 . GLN G  194 ? 1.1196 0.9559 1.3459 0.1028  0.1733  0.0524  194 GLN G OE1 
12891 N NE2 . GLN G  194 ? 0.9110 0.7484 1.1300 0.1044  0.1741  0.0523  194 GLN G NE2 
12892 N N   . GLN G  195 ? 1.3670 1.1813 1.6060 0.1148  0.2050  0.0602  195 GLN G N   
12893 C CA  . GLN G  195 ? 1.5115 1.3201 1.7583 0.1139  0.2100  0.0595  195 GLN G CA  
12894 C C   . GLN G  195 ? 1.4071 1.2088 1.6597 0.1103  0.2154  0.0551  195 GLN G C   
12895 O O   . GLN G  195 ? 1.3892 1.1868 1.6485 0.1071  0.2177  0.0523  195 GLN G O   
12896 C CB  . GLN G  195 ? 1.4810 1.2878 1.7286 0.1206  0.2160  0.0661  195 GLN G CB  
12897 C CG  . GLN G  195 ? 1.8051 1.6102 2.0507 0.1261  0.2220  0.0706  195 GLN G CG  
12898 C CD  . GLN G  195 ? 2.0429 1.8478 2.2882 0.1327  0.2266  0.0777  195 GLN G CD  
12899 O OE1 . GLN G  195 ? 1.9961 1.7999 2.2402 0.1378  0.2316  0.0823  195 GLN G OE1 
12900 N NE2 . GLN G  195 ? 2.0791 1.8849 2.3255 0.1327  0.2250  0.0787  195 GLN G NE2 
12901 N N   . SER G  196 ? 1.1428 0.9434 1.3931 0.1107  0.2176  0.0544  196 SER G N   
12902 C CA  . SER G  196 ? 1.0250 0.8190 1.2801 0.1071  0.2229  0.0500  196 SER G CA  
12903 C C   . SER G  196 ? 1.2133 1.0081 1.4694 0.0989  0.2173  0.0427  196 SER G C   
12904 O O   . SER G  196 ? 1.1918 0.9813 1.4539 0.0946  0.2209  0.0384  196 SER G O   
12905 C CB  . SER G  196 ? 1.0523 0.8452 1.3042 0.1098  0.2265  0.0513  196 SER G CB  
12906 O OG  . SER G  196 ? 1.3137 1.1005 1.5696 0.1055  0.2310  0.0462  196 SER G OG  
12907 N N   . LEU G  197 ? 1.2880 1.0897 1.5383 0.0967  0.2084  0.0414  197 LEU G N   
12908 C CA  . LEU G  197 ? 1.1282 0.9320 1.3782 0.0892  0.2020  0.0351  197 LEU G CA  
12909 C C   . LEU G  197 ? 1.0338 0.8403 1.2871 0.0866  0.1971  0.0343  197 LEU G C   
12910 O O   . LEU G  197 ? 0.9939 0.7981 1.2525 0.0811  0.1968  0.0300  197 LEU G O   
12911 C CB  . LEU G  197 ? 1.0652 0.8753 1.3072 0.0886  0.1951  0.0346  197 LEU G CB  
12912 C CG  . LEU G  197 ? 0.8897 0.6975 1.1287 0.0883  0.1981  0.0329  197 LEU G CG  
12913 C CD1 . LEU G  197 ? 0.9759 0.7906 1.2068 0.0889  0.1913  0.0336  197 LEU G CD1 
12914 C CD2 . LEU G  197 ? 0.9416 0.7453 1.1842 0.0810  0.1991  0.0260  197 LEU G CD2 
12915 N N   . TYR G  198 ? 1.0031 0.8147 1.2530 0.0905  0.1933  0.0386  198 TYR G N   
12916 C CA  . TYR G  198 ? 1.1334 0.9473 1.3864 0.0895  0.1898  0.0391  198 TYR G CA  
12917 C C   . TYR G  198 ? 1.2543 1.0665 1.5081 0.0964  0.1951  0.0452  198 TYR G C   
12918 O O   . TYR G  198 ? 1.3489 1.1644 1.5968 0.1014  0.1944  0.0497  198 TYR G O   
12919 C CB  . TYR G  198 ? 1.1851 1.0066 1.4331 0.0870  0.1800  0.0380  198 TYR G CB  
12920 C CG  . TYR G  198 ? 1.0261 0.8500 1.2684 0.0843  0.1762  0.0351  198 TYR G CG  
12921 C CD1 . TYR G  198 ? 0.9287 0.7556 1.1639 0.0886  0.1757  0.0382  198 TYR G CD1 
12922 C CD2 . TYR G  198 ? 1.0492 0.8725 1.2933 0.0774  0.1736  0.0292  198 TYR G CD2 
12923 C CE1 . TYR G  198 ? 0.9309 0.7598 1.1610 0.0863  0.1726  0.0355  198 TYR G CE1 
12924 C CE2 . TYR G  198 ? 0.9751 0.8004 1.2137 0.0748  0.1704  0.0264  198 TYR G CE2 
12925 C CZ  . TYR G  198 ? 0.9199 0.7478 1.1515 0.0794  0.1701  0.0296  198 TYR G CZ  
12926 O OH  . TYR G  198 ? 0.8042 0.6340 1.0305 0.0769  0.1671  0.0269  198 TYR G OH  
12927 N N   . GLN G  199 ? 1.2504 1.0573 1.5115 0.0963  0.2007  0.0453  199 GLN G N   
12928 C CA  . GLN G  199 ? 1.3499 1.1544 1.6129 0.1022  0.2063  0.0507  199 GLN G CA  
12929 C C   . GLN G  199 ? 1.2783 1.0889 1.5350 0.1064  0.2020  0.0554  199 GLN G C   
12930 O O   . GLN G  199 ? 1.1985 1.0098 1.4507 0.1121  0.2047  0.0603  199 GLN G O   
12931 C CB  . GLN G  199 ? 1.4701 1.2709 1.7416 0.0996  0.2088  0.0490  199 GLN G CB  
12932 C CG  . GLN G  199 ? 1.6609 1.4535 1.9389 0.1009  0.2185  0.0494  199 GLN G CG  
12933 C CD  . GLN G  199 ? 1.6959 1.4864 1.9723 0.1085  0.2248  0.0560  199 GLN G CD  
12934 O OE1 . GLN G  199 ? 1.6797 1.4728 1.9543 0.1118  0.2236  0.0600  199 GLN G OE1 
12935 N NE2 . GLN G  199 ? 1.5031 1.2889 1.7800 0.1111  0.2317  0.0574  199 GLN G NE2 
12936 N N   . ASN G  200 ? 1.4078 1.2229 1.6643 0.1035  0.1952  0.0538  200 ASN G N   
12937 C CA  . ASN G  200 ? 1.3514 1.1717 1.6027 0.1068  0.1914  0.0577  200 ASN G CA  
12938 C C   . ASN G  200 ? 1.3168 1.1416 1.5591 0.1103  0.1890  0.0605  200 ASN G C   
12939 O O   . ASN G  200 ? 1.3362 1.1624 1.5756 0.1083  0.1867  0.0580  200 ASN G O   
12940 C CB  . ASN G  200 ? 1.3146 1.1391 1.5672 0.1023  0.1840  0.0548  200 ASN G CB  
12941 C CG  . ASN G  200 ? 1.2819 1.1027 1.5437 0.0974  0.1851  0.0508  200 ASN G CG  
12942 O OD1 . ASN G  200 ? 1.4784 1.2931 1.7458 0.0980  0.1921  0.0509  200 ASN G OD1 
12943 N ND2 . ASN G  200 ? 1.2879 1.1125 1.5514 0.0925  0.1783  0.0475  200 ASN G ND2 
12944 N N   . ALA G  201 ? 1.1349 0.9622 1.3729 0.1154  0.1897  0.0657  201 ALA G N   
12945 C CA  . ALA G  201 ? 1.1245 0.9565 1.3541 0.1191  0.1876  0.0689  201 ALA G CA  
12946 C C   . ALA G  201 ? 1.3302 1.1694 1.5541 0.1170  0.1789  0.0677  201 ALA G C   
12947 O O   . ALA G  201 ? 1.3291 1.1723 1.5473 0.1166  0.1750  0.0670  201 ALA G O   
12948 C CB  . ALA G  201 ? 1.1968 1.0282 1.4243 0.1256  0.1930  0.0754  201 ALA G CB  
12949 N N   . ASP G  202 ? 1.3822 1.2228 1.6078 0.1157  0.1762  0.0675  202 ASP G N   
12950 C CA  . ASP G  202 ? 1.2837 1.1305 1.5046 0.1136  0.1684  0.0663  202 ASP G CA  
12951 C C   . ASP G  202 ? 1.2399 1.0868 1.4659 0.1074  0.1637  0.0610  202 ASP G C   
12952 O O   . ASP G  202 ? 1.2941 1.1395 1.5258 0.1057  0.1639  0.0603  202 ASP G O   
12953 C CB  . ASP G  202 ? 1.4312 1.2800 1.6499 0.1167  0.1685  0.0701  202 ASP G CB  
12954 C CG  . ASP G  202 ? 1.5080 1.3637 1.7197 0.1162  0.1614  0.0702  202 ASP G CG  
12955 O OD1 . ASP G  202 ? 1.4969 1.3562 1.7025 0.1167  0.1585  0.0703  202 ASP G OD1 
12956 O OD2 . ASP G  202 ? 1.5454 1.4026 1.7578 0.1152  0.1590  0.0702  202 ASP G OD2 
12957 N N   . THR G  203 ? 1.0873 0.9363 1.3114 0.1038  0.1594  0.0574  203 THR G N   
12958 C CA  . THR G  203 ? 0.9881 0.8374 1.2168 0.0976  0.1550  0.0524  203 THR G CA  
12959 C C   . THR G  203 ? 0.9053 0.7611 1.1290 0.0949  0.1465  0.0507  203 THR G C   
12960 O O   . THR G  203 ? 0.9982 0.8581 1.2146 0.0976  0.1441  0.0530  203 THR G O   
12961 C CB  . THR G  203 ? 1.0239 0.8694 1.2555 0.0945  0.1573  0.0488  203 THR G CB  
12962 O OG1 . THR G  203 ? 0.8490 0.6967 1.0736 0.0955  0.1559  0.0488  203 THR G OG1 
12963 C CG2 . THR G  203 ? 0.9894 0.8280 1.2264 0.0969  0.1660  0.0501  203 THR G CG2 
12964 N N   . TYR G  204 ? 0.9262 0.7831 1.1542 0.0893  0.1419  0.0467  204 TYR G N   
12965 C CA  . TYR G  204 ? 0.8110 0.6738 1.0350 0.0863  0.1338  0.0449  204 TYR G CA  
12966 C C   . TYR G  204 ? 0.8620 0.7250 1.0901 0.0798  0.1298  0.0400  204 TYR G C   
12967 O O   . TYR G  204 ? 0.8772 0.7364 1.1127 0.0772  0.1325  0.0381  204 TYR G O   
12968 C CB  . TYR G  204 ? 0.7945 0.6605 1.0188 0.0873  0.1308  0.0470  204 TYR G CB  
12969 C CG  . TYR G  204 ? 0.9270 0.7914 1.1603 0.0841  0.1306  0.0455  204 TYR G CG  
12970 C CD1 . TYR G  204 ? 0.9412 0.8088 1.1775 0.0790  0.1242  0.0425  204 TYR G CD1 
12971 C CD2 . TYR G  204 ? 1.0148 0.8746 1.2538 0.0864  0.1368  0.0474  204 TYR G CD2 
12972 C CE1 . TYR G  204 ? 1.0400 0.9066 1.2851 0.0761  0.1239  0.0414  204 TYR G CE1 
12973 C CE2 . TYR G  204 ? 1.0465 0.9050 1.2942 0.0836  0.1367  0.0461  204 TYR G CE2 
12974 C CZ  . TYR G  204 ? 1.0893 0.9513 1.3402 0.0784  0.1302  0.0432  204 TYR G CZ  
12975 O OH  . TYR G  204 ? 1.1719 1.0331 1.4319 0.0756  0.1300  0.0422  204 TYR G OH  
12976 N N   . VAL G  205 ? 0.8444 0.7120 1.0676 0.0770  0.1234  0.0381  205 VAL G N   
12977 C CA  . VAL G  205 ? 0.8063 0.6752 1.0326 0.0706  0.1186  0.0337  205 VAL G CA  
12978 C C   . VAL G  205 ? 0.8220 0.6969 1.0467 0.0685  0.1109  0.0336  205 VAL G C   
12979 O O   . VAL G  205 ? 0.8033 0.6818 1.0215 0.0713  0.1084  0.0357  205 VAL G O   
12980 C CB  . VAL G  205 ? 0.6863 0.5546 0.9081 0.0683  0.1182  0.0308  205 VAL G CB  
12981 C CG1 . VAL G  205 ? 0.6370 0.5066 0.8619 0.0613  0.1134  0.0262  205 VAL G CG1 
12982 C CG2 . VAL G  205 ? 0.7971 0.6594 1.0202 0.0710  0.1264  0.0313  205 VAL G CG2 
12983 N N   . PHE G  206 ? 0.8330 0.7092 1.0640 0.0636  0.1071  0.0312  206 PHE G N   
12984 C CA  . PHE G  206 ? 0.6786 0.5603 0.9089 0.0614  0.0999  0.0312  206 PHE G CA  
12985 C C   . PHE G  206 ? 0.7738 0.6579 1.0073 0.0548  0.0944  0.0275  206 PHE G C   
12986 O O   . PHE G  206 ? 0.8901 0.7721 1.1310 0.0514  0.0957  0.0256  206 PHE G O   
12987 C CB  . PHE G  206 ? 0.7483 0.6302 0.9840 0.0635  0.1008  0.0339  206 PHE G CB  
12988 C CG  . PHE G  206 ? 0.7603 0.6477 0.9959 0.0617  0.0941  0.0343  206 PHE G CG  
12989 C CD1 . PHE G  206 ? 0.8477 0.7373 1.0901 0.0567  0.0896  0.0324  206 PHE G CD1 
12990 C CD2 . PHE G  206 ? 0.8591 0.7495 1.0882 0.0651  0.0924  0.0367  206 PHE G CD2 
12991 C CE1 . PHE G  206 ? 0.9231 0.8176 1.1659 0.0552  0.0837  0.0331  206 PHE G CE1 
12992 C CE2 . PHE G  206 ? 0.7175 0.6125 0.9467 0.0635  0.0866  0.0370  206 PHE G CE2 
12993 C CZ  . PHE G  206 ? 0.9552 0.8521 1.1914 0.0587  0.0823  0.0353  206 PHE G CZ  
12994 N N   . VAL G  207 ? 0.8180 0.7068 1.0457 0.0528  0.0883  0.0264  207 VAL G N   
12995 C CA  . VAL G  207 ? 0.7289 0.6207 0.9584 0.0464  0.0823  0.0231  207 VAL G CA  
12996 C C   . VAL G  207 ? 0.7812 0.6788 1.0106 0.0451  0.0754  0.0243  207 VAL G C   
12997 O O   . VAL G  207 ? 0.8114 0.7118 1.0341 0.0477  0.0732  0.0258  207 VAL G O   
12998 C CB  . VAL G  207 ? 0.6085 0.5003 0.8309 0.0443  0.0812  0.0203  207 VAL G CB  
12999 C CG1 . VAL G  207 ? 0.5755 0.4706 0.7993 0.0374  0.0750  0.0170  207 VAL G CG1 
13000 C CG2 . VAL G  207 ? 0.6980 0.5838 0.9208 0.0455  0.0885  0.0193  207 VAL G CG2 
13001 N N   . GLY G  208 ? 0.7822 0.6817 1.0192 0.0411  0.0721  0.0235  208 GLY G N   
13002 C CA  . GLY G  208 ? 0.6611 0.5658 0.8995 0.0399  0.0659  0.0249  208 GLY G CA  
13003 C C   . GLY G  208 ? 0.8266 0.7350 1.0703 0.0335  0.0600  0.0228  208 GLY G C   
13004 O O   . GLY G  208 ? 0.9292 0.8359 1.1793 0.0301  0.0613  0.0210  208 GLY G O   
13005 N N   . SER G  209 ? 0.7580 0.6717 0.9988 0.0318  0.0534  0.0232  209 SER G N   
13006 C CA  . SER G  209 ? 0.7540 0.6721 1.0000 0.0261  0.0471  0.0221  209 SER G CA  
13007 C C   . SER G  209 ? 0.8272 0.7496 1.0755 0.0273  0.0429  0.0251  209 SER G C   
13008 O O   . SER G  209 ? 0.7977 0.7187 1.0457 0.0322  0.0460  0.0277  209 SER G O   
13009 C CB  . SER G  209 ? 0.7890 0.7094 1.0284 0.0217  0.0426  0.0192  209 SER G CB  
13010 O OG  . SER G  209 ? 0.6953 0.6184 0.9263 0.0236  0.0395  0.0201  209 SER G OG  
13011 N N   . SER G  210 ? 0.9946 0.9222 1.2453 0.0228  0.0362  0.0248  210 SER G N   
13012 C CA  . SER G  210 ? 0.9613 0.8931 1.2144 0.0237  0.0321  0.0276  210 SER G CA  
13013 C C   . SER G  210 ? 1.0504 0.9830 1.2936 0.0273  0.0314  0.0285  210 SER G C   
13014 O O   . SER G  210 ? 0.8279 0.7621 1.0717 0.0300  0.0306  0.0311  210 SER G O   
13015 C CB  . SER G  210 ? 1.0919 1.0293 1.3495 0.0180  0.0248  0.0273  210 SER G CB  
13016 O OG  . SER G  210 ? 1.3062 1.2435 1.5742 0.0149  0.0252  0.0271  210 SER G OG  
13017 N N   . ARG G  211 ? 1.0424 0.9739 1.2765 0.0271  0.0317  0.0264  211 ARG G N   
13018 C CA  . ARG G  211 ? 1.0921 1.0249 1.3165 0.0298  0.0306  0.0269  211 ARG G CA  
13019 C C   . ARG G  211 ? 1.0836 1.0120 1.3013 0.0343  0.0366  0.0266  211 ARG G C   
13020 O O   . ARG G  211 ? 1.2664 1.1950 1.4783 0.0384  0.0378  0.0282  211 ARG G O   
13021 C CB  . ARG G  211 ? 1.1842 1.1207 1.4032 0.0254  0.0245  0.0248  211 ARG G CB  
13022 C CG  . ARG G  211 ? 1.3187 1.2529 1.5343 0.0225  0.0258  0.0214  211 ARG G CG  
13023 C CD  . ARG G  211 ? 1.5143 1.4524 1.7272 0.0167  0.0193  0.0193  211 ARG G CD  
13024 N NE  . ARG G  211 ? 1.6974 1.6396 1.9045 0.0173  0.0146  0.0205  211 ARG G NE  
13025 C CZ  . ARG G  211 ? 1.5643 1.5097 1.7663 0.0133  0.0094  0.0188  211 ARG G CZ  
13026 N NH1 . ARG G  211 ? 1.4409 1.3860 1.6426 0.0083  0.0082  0.0158  211 ARG G NH1 
13027 N NH2 . ARG G  211 ? 1.4109 1.3598 1.6079 0.0142  0.0055  0.0201  211 ARG G NH2 
13028 N N   . TYR G  212 ? 1.1129 1.0374 1.3316 0.0335  0.0406  0.0247  212 TYR G N   
13029 C CA  . TYR G  212 ? 0.7465 0.6668 0.9596 0.0375  0.0466  0.0245  212 TYR G CA  
13030 C C   . TYR G  212 ? 0.7504 0.6664 0.9683 0.0417  0.0533  0.0265  212 TYR G C   
13031 O O   . TYR G  212 ? 0.8362 0.7502 1.0622 0.0400  0.0552  0.0261  212 TYR G O   
13032 C CB  . TYR G  212 ? 0.6642 0.5820 0.8754 0.0345  0.0481  0.0212  212 TYR G CB  
13033 C CG  . TYR G  212 ? 0.8741 0.7881 1.0786 0.0384  0.0536  0.0211  212 TYR G CG  
13034 C CD1 . TYR G  212 ? 0.7709 0.6864 0.9665 0.0387  0.0518  0.0201  212 TYR G CD1 
13035 C CD2 . TYR G  212 ? 0.8964 0.8055 1.1039 0.0420  0.0606  0.0222  212 TYR G CD2 
13036 C CE1 . TYR G  212 ? 0.8319 0.7443 1.0220 0.0424  0.0568  0.0204  212 TYR G CE1 
13037 C CE2 . TYR G  212 ? 0.7474 0.6533 0.9493 0.0457  0.0656  0.0225  212 TYR G CE2 
13038 C CZ  . TYR G  212 ? 0.8029 0.7106 0.9963 0.0459  0.0637  0.0217  212 TYR G CZ  
13039 O OH  . TYR G  212 ? 0.7476 0.6525 0.9361 0.0498  0.0687  0.0223  212 TYR G OH  
13040 N N   . SER G  213 ? 0.6668 0.5814 0.8794 0.0470  0.0568  0.0287  213 SER G N   
13041 C CA  . SER G  213 ? 0.7617 0.6723 0.9778 0.0513  0.0633  0.0308  213 SER G CA  
13042 C C   . SER G  213 ? 0.7581 0.6668 0.9666 0.0565  0.0678  0.0323  213 SER G C   
13043 O O   . SER G  213 ? 0.8533 0.7647 1.0556 0.0589  0.0662  0.0339  213 SER G O   
13044 C CB  . SER G  213 ? 0.7401 0.6526 0.9610 0.0523  0.0619  0.0332  213 SER G CB  
13045 O OG  . SER G  213 ? 0.7089 0.6177 0.9334 0.0562  0.0680  0.0353  213 SER G OG  
13046 N N   . LYS G  214 ? 0.7930 0.6971 1.0020 0.0581  0.0736  0.0320  214 LYS G N   
13047 C CA  . LYS G  214 ? 0.8140 0.7162 1.0168 0.0632  0.0783  0.0340  214 LYS G CA  
13048 C C   . LYS G  214 ? 0.8735 0.7701 1.0803 0.0657  0.0857  0.0348  214 LYS G C   
13049 O O   . LYS G  214 ? 0.7801 0.6737 0.9921 0.0628  0.0875  0.0326  214 LYS G O   
13050 C CB  . LYS G  214 ? 0.7865 0.6903 0.9811 0.0628  0.0765  0.0325  214 LYS G CB  
13051 C CG  . LYS G  214 ? 0.8358 0.7388 1.0237 0.0682  0.0806  0.0350  214 LYS G CG  
13052 C CD  . LYS G  214 ? 1.0865 0.9939 1.2658 0.0684  0.0763  0.0348  214 LYS G CD  
13053 C CE  . LYS G  214 ? 1.0356 0.9418 1.2110 0.0676  0.0774  0.0328  214 LYS G CE  
13054 N NZ  . LYS G  214 ? 1.2053 1.1082 1.3790 0.0724  0.0841  0.0350  214 LYS G NZ  
13055 N N   . LYS G  215 ? 0.7897 0.6850 0.9938 0.0710  0.0901  0.0381  215 LYS G N   
13056 C CA  . LYS G  215 ? 0.7394 0.6295 0.9466 0.0741  0.0975  0.0395  215 LYS G CA  
13057 C C   . LYS G  215 ? 0.8081 0.6971 1.0086 0.0775  0.1009  0.0405  215 LYS G C   
13058 O O   . LYS G  215 ? 0.9038 0.7960 1.0970 0.0801  0.0994  0.0423  215 LYS G O   
13059 C CB  . LYS G  215 ? 0.9590 0.8482 1.1685 0.0777  0.1004  0.0428  215 LYS G CB  
13060 C CG  . LYS G  215 ? 0.9798 0.8635 1.1935 0.0806  0.1080  0.0445  215 LYS G CG  
13061 C CD  . LYS G  215 ? 1.0749 0.9581 1.2910 0.0836  0.1105  0.0475  215 LYS G CD  
13062 C CE  . LYS G  215 ? 1.1689 1.0464 1.3907 0.0857  0.1177  0.0488  215 LYS G CE  
13063 N NZ  . LYS G  215 ? 1.0899 0.9666 1.3149 0.0878  0.1198  0.0513  215 LYS G NZ  
13064 N N   . PHE G  216 ? 0.8347 0.7192 1.0379 0.0772  0.1056  0.0394  216 PHE G N   
13065 C CA  . PHE G  216 ? 0.7738 0.6569 0.9716 0.0802  0.1091  0.0403  216 PHE G CA  
13066 C C   . PHE G  216 ? 0.7156 0.5945 0.9148 0.0853  0.1167  0.0437  216 PHE G C   
13067 O O   . PHE G  216 ? 0.7765 0.6512 0.9827 0.0851  0.1209  0.0437  216 PHE G O   
13068 C CB  . PHE G  216 ? 0.8968 0.7778 1.0957 0.0761  0.1091  0.0363  216 PHE G CB  
13069 C CG  . PHE G  216 ? 0.8103 0.6952 1.0073 0.0708  0.1018  0.0329  216 PHE G CG  
13070 C CD1 . PHE G  216 ? 0.7129 0.5981 0.9160 0.0658  0.0985  0.0304  216 PHE G CD1 
13071 C CD2 . PHE G  216 ? 0.7014 0.5900 0.8908 0.0708  0.0981  0.0325  216 PHE G CD2 
13072 C CE1 . PHE G  216 ? 0.8082 0.6974 1.0097 0.0610  0.0916  0.0276  216 PHE G CE1 
13073 C CE2 . PHE G  216 ? 0.8521 0.7443 1.0397 0.0659  0.0914  0.0295  216 PHE G CE2 
13074 C CZ  . PHE G  216 ? 0.7695 0.6620 0.9630 0.0610  0.0881  0.0271  216 PHE G CZ  
13075 N N   . LYS G  217 ? 0.8338 0.7142 1.0266 0.0899  0.1185  0.0469  217 LYS G N   
13076 C CA  . LYS G  217 ? 0.9035 0.7804 1.0969 0.0950  0.1257  0.0506  217 LYS G CA  
13077 C C   . LYS G  217 ? 0.8795 0.7547 1.0701 0.0966  0.1291  0.0506  217 LYS G C   
13078 O O   . LYS G  217 ? 0.9050 0.7840 1.0892 0.0975  0.1263  0.0510  217 LYS G O   
13079 C CB  . LYS G  217 ? 0.9573 0.8376 1.1459 0.0995  0.1256  0.0549  217 LYS G CB  
13080 C CG  . LYS G  217 ? 1.0230 0.9014 1.2161 0.1005  0.1277  0.0566  217 LYS G CG  
13081 C CD  . LYS G  217 ? 1.1315 1.0038 1.3303 0.1027  0.1354  0.0581  217 LYS G CD  
13082 C CE  . LYS G  217 ? 1.3098 1.1802 1.5131 0.1038  0.1378  0.0598  217 LYS G CE  
13083 N NZ  . LYS G  217 ? 1.3953 1.2596 1.6040 0.1061  0.1454  0.0615  217 LYS G NZ  
13084 N N   . PRO G  218 ? 0.9393 0.8086 1.1352 0.0970  0.1353  0.0503  218 PRO G N   
13085 C CA  . PRO G  218 ? 0.8564 0.7232 1.0508 0.0986  0.1396  0.0504  218 PRO G CA  
13086 C C   . PRO G  218 ? 0.8716 0.7411 1.0600 0.1044  0.1415  0.0552  218 PRO G C   
13087 O O   . PRO G  218 ? 0.8201 0.6894 1.0085 0.1087  0.1445  0.0595  218 PRO G O   
13088 C CB  . PRO G  218 ? 0.8653 0.7251 1.0672 0.0989  0.1468  0.0502  218 PRO G CB  
13089 C CG  . PRO G  218 ? 0.9521 0.8111 1.1598 0.0950  0.1444  0.0478  218 PRO G CG  
13090 C CD  . PRO G  218 ? 0.9574 0.8220 1.1614 0.0958  0.1389  0.0496  218 PRO G CD  
13091 N N   . GLU G  219 ? 0.9462 0.8182 1.1294 0.1045  0.1397  0.0547  219 GLU G N   
13092 C CA  . GLU G  219 ? 0.8880 0.7631 1.0656 0.1098  0.1412  0.0593  219 GLU G CA  
13093 C C   . GLU G  219 ? 0.9042 0.7747 1.0841 0.1127  0.1484  0.0608  219 GLU G C   
13094 O O   . GLU G  219 ? 0.8132 0.6830 0.9921 0.1111  0.1486  0.0585  219 GLU G O   
13095 C CB  . GLU G  219 ? 0.8903 0.7715 1.0609 0.1085  0.1347  0.0581  219 GLU G CB  
13096 C CG  . GLU G  219 ? 1.0265 0.9122 1.1949 0.1055  0.1275  0.0564  219 GLU G CG  
13097 C CD  . GLU G  219 ? 1.1542 1.0457 1.3157 0.1042  0.1214  0.0552  219 GLU G CD  
13098 O OE1 . GLU G  219 ? 1.0370 0.9289 1.1957 0.1051  0.1225  0.0552  219 GLU G OE1 
13099 O OE2 . GLU G  219 ? 1.0654 0.9610 1.2245 0.1022  0.1156  0.0544  219 GLU G OE2 
13100 N N   . ILE G  220 ? 0.9876 0.8551 1.1707 0.1170  0.1546  0.0649  220 ILE G N   
13101 C CA  . ILE G  220 ? 0.9154 0.7778 1.1018 0.1200  0.1623  0.0668  220 ILE G CA  
13102 C C   . ILE G  220 ? 0.8543 0.7202 1.0358 0.1253  0.1640  0.0717  220 ILE G C   
13103 O O   . ILE G  220 ? 0.9057 0.7754 1.0841 0.1294  0.1638  0.0766  220 ILE G O   
13104 C CB  . ILE G  220 ? 0.8837 0.7408 1.0763 0.1221  0.1687  0.0690  220 ILE G CB  
13105 C CG1 . ILE G  220 ? 0.7990 0.6525 0.9971 0.1168  0.1673  0.0642  220 ILE G CG1 
13106 C CG2 . ILE G  220 ? 0.9333 0.7850 1.1296 0.1254  0.1770  0.0712  220 ILE G CG2 
13107 C CD1 . ILE G  220 ? 1.0834 0.9326 1.2871 0.1186  0.1723  0.0663  220 ILE G CD1 
13108 N N   . ALA G  221 ? 0.8123 0.6772 0.9933 0.1250  0.1656  0.0704  221 ALA G N   
13109 C CA  . ALA G  221 ? 0.7631 0.6314 0.9404 0.1298  0.1674  0.0749  221 ALA G CA  
13110 C C   . ALA G  221 ? 0.9146 0.7794 1.0935 0.1289  0.1708  0.0727  221 ALA G C   
13111 O O   . ALA G  221 ? 0.8311 0.6916 1.0131 0.1240  0.1710  0.0672  221 ALA G O   
13112 C CB  . ALA G  221 ? 0.6264 0.5030 0.7961 0.1301  0.1600  0.0760  221 ALA G CB  
13113 N N   . ILE G  222 ? 0.9654 0.8325 1.1424 0.1336  0.1735  0.0771  222 ILE G N   
13114 C CA  . ILE G  222 ? 1.0783 0.9422 1.2569 0.1333  0.1774  0.0756  222 ILE G CA  
13115 C C   . ILE G  222 ? 0.9863 0.8556 1.1590 0.1311  0.1715  0.0732  222 ILE G C   
13116 O O   . ILE G  222 ? 0.9288 0.8047 1.0968 0.1345  0.1687  0.0771  222 ILE G O   
13117 C CB  . ILE G  222 ? 1.1607 1.0234 1.3419 0.1399  0.1850  0.0820  222 ILE G CB  
13118 C CG1 . ILE G  222 ? 1.0906 0.9475 1.2779 0.1422  0.1915  0.0844  222 ILE G CG1 
13119 C CG2 . ILE G  222 ? 0.9724 0.8317 1.1556 0.1397  0.1892  0.0804  222 ILE G CG2 
13120 C CD1 . ILE G  222 ? 1.2125 1.0610 1.4059 0.1377  0.1953  0.0789  222 ILE G CD1 
13121 N N   . ARG G  223 ? 0.9328 0.7993 1.1059 0.1253  0.1695  0.0667  223 ARG G N   
13122 C CA  . ARG G  223 ? 1.0033 0.8739 1.1711 0.1228  0.1645  0.0640  223 ARG G CA  
13123 C C   . ARG G  223 ? 1.0350 0.9020 1.2048 0.1238  0.1703  0.0636  223 ARG G C   
13124 O O   . ARG G  223 ? 1.0156 0.8754 1.1912 0.1238  0.1773  0.0628  223 ARG G O   
13125 C CB  . ARG G  223 ? 0.9805 0.8509 1.1469 0.1156  0.1584  0.0572  223 ARG G CB  
13126 C CG  . ARG G  223 ? 0.8285 0.7035 0.9923 0.1142  0.1516  0.0572  223 ARG G CG  
13127 C CD  . ARG G  223 ? 0.7680 0.6386 0.9374 0.1138  0.1542  0.0572  223 ARG G CD  
13128 N NE  . ARG G  223 ? 0.7960 0.6700 0.9637 0.1107  0.1475  0.0555  223 ARG G NE  
13129 C CZ  . ARG G  223 ? 0.8284 0.6998 1.0003 0.1098  0.1482  0.0552  223 ARG G CZ  
13130 N NH1 . ARG G  223 ? 0.9559 0.8213 1.1339 0.1115  0.1553  0.0564  223 ARG G NH1 
13131 N NH2 . ARG G  223 ? 0.9064 0.7813 1.0769 0.1071  0.1420  0.0537  223 ARG G NH2 
13132 N N   . PRO G  224 ? 0.9776 0.8493 1.1427 0.1246  0.1675  0.0642  224 PRO G N   
13133 C CA  . PRO G  224 ? 0.8929 0.7615 1.0596 0.1252  0.1726  0.0635  224 PRO G CA  
13134 C C   . PRO G  224 ? 1.0229 0.8841 1.1927 0.1192  0.1751  0.0566  224 PRO G C   
13135 O O   . PRO G  224 ? 1.1085 0.9703 1.2756 0.1133  0.1693  0.0512  224 PRO G O   
13136 C CB  . PRO G  224 ? 0.7893 0.6650 0.9494 0.1248  0.1666  0.0633  224 PRO G CB  
13137 C CG  . PRO G  224 ? 0.9560 0.8391 1.1120 0.1274  0.1609  0.0672  224 PRO G CG  
13138 C CD  . PRO G  224 ? 0.9916 0.8720 1.1499 0.1252  0.1598  0.0657  224 PRO G CD  
13139 N N   . LYS G  225 ? 1.1400 0.9943 1.3153 0.1206  0.1837  0.0569  225 LYS G N   
13140 C CA  . LYS G  225 ? 1.0657 0.9123 1.2444 0.1149  0.1871  0.0505  225 LYS G CA  
13141 C C   . LYS G  225 ? 0.9642 0.8116 1.1383 0.1088  0.1824  0.0442  225 LYS G C   
13142 O O   . LYS G  225 ? 1.0864 0.9358 1.2577 0.1099  0.1827  0.0446  225 LYS G O   
13143 C CB  . LYS G  225 ? 1.3148 1.1541 1.4998 0.1179  0.1976  0.0522  225 LYS G CB  
13144 C CG  . LYS G  225 ? 1.5369 1.3731 1.7275 0.1225  0.2032  0.0569  225 LYS G CG  
13145 C CD  . LYS G  225 ? 1.7177 1.5463 1.9149 0.1251  0.2139  0.0583  225 LYS G CD  
13146 C CE  . LYS G  225 ? 1.9339 1.7593 2.1368 0.1296  0.2196  0.0631  225 LYS G CE  
13147 N NZ  . LYS G  225 ? 1.9965 1.8191 2.2011 0.1251  0.2175  0.0592  225 LYS G NZ  
13148 N N   . VAL G  226 ? 0.9673 0.8134 1.1407 0.1023  0.1780  0.0385  226 VAL G N   
13149 C CA  . VAL G  226 ? 0.9864 0.8319 1.1562 0.0955  0.1744  0.0319  226 VAL G CA  
13150 C C   . VAL G  226 ? 0.9853 0.8230 1.1597 0.0901  0.1785  0.0264  226 VAL G C   
13151 O O   . VAL G  226 ? 0.9732 0.8103 1.1496 0.0874  0.1760  0.0249  226 VAL G O   
13152 C CB  . VAL G  226 ? 0.9176 0.7700 1.0816 0.0920  0.1640  0.0300  226 VAL G CB  
13153 C CG1 . VAL G  226 ? 0.9703 0.8219 1.1304 0.0849  0.1604  0.0232  226 VAL G CG1 
13154 C CG2 . VAL G  226 ? 0.8336 0.6938 0.9929 0.0972  0.1599  0.0353  226 VAL G CG2 
13155 N N   . ARG G  227 ? 1.0444 0.8761 1.2206 0.0885  0.1850  0.0236  227 ARG G N   
13156 C CA  . ARG G  227 ? 1.0198 0.8435 1.2004 0.0833  0.1899  0.0183  227 ARG G CA  
13157 C C   . ARG G  227 ? 1.1051 0.9238 1.2930 0.0870  0.1969  0.0215  227 ARG G C   
13158 O O   . ARG G  227 ? 1.1883 1.0024 1.3800 0.0827  0.1985  0.0178  227 ARG G O   
13159 C CB  . ARG G  227 ? 0.9444 0.7696 1.1223 0.0754  0.1824  0.0123  227 ARG G CB  
13160 C CG  . ARG G  227 ? 0.9648 0.7915 1.1366 0.0697  0.1782  0.0070  227 ARG G CG  
13161 C CD  . ARG G  227 ? 1.0331 0.8629 1.2020 0.0626  0.1697  0.0023  227 ARG G CD  
13162 N NE  . ARG G  227 ? 0.8934 0.7185 1.0613 0.0549  0.1710  -0.0048 227 ARG G NE  
13163 C CZ  . ARG G  227 ? 1.0906 0.9087 1.2635 0.0513  0.1766  -0.0084 227 ARG G CZ  
13164 N NH1 . ARG G  227 ? 1.2451 1.0600 1.4246 0.0548  0.1816  -0.0055 227 ARG G NH1 
13165 N NH2 . ARG G  227 ? 1.0853 0.8998 1.2564 0.0440  0.1773  -0.0150 227 ARG G NH2 
13166 N N   . ASP G  228 ? 1.1888 1.0087 1.3787 0.0948  0.2010  0.0285  228 ASP G N   
13167 C CA  . ASP G  228 ? 1.4261 1.2413 1.6229 0.0991  0.2083  0.0323  228 ASP G CA  
13168 C C   . ASP G  228 ? 1.4043 1.2231 1.6019 0.1005  0.2039  0.0351  228 ASP G C   
13169 O O   . ASP G  228 ? 1.5680 1.3839 1.7707 0.1047  0.2091  0.0391  228 ASP G O   
13170 C CB  . ASP G  228 ? 1.7417 1.5475 1.9441 0.0948  0.2158  0.0274  228 ASP G CB  
13171 C CG  . ASP G  228 ? 2.0319 1.8320 2.2376 0.0981  0.2255  0.0288  228 ASP G CG  
13172 O OD1 . ASP G  228 ? 2.0282 1.8276 2.2377 0.1052  0.2310  0.0354  228 ASP G OD1 
13173 O OD2 . ASP G  228 ? 2.2176 2.0138 2.4224 0.0934  0.2277  0.0235  228 ASP G OD2 
13174 N N   . GLN G  229 ? 1.2257 1.0506 1.4184 0.0972  0.1945  0.0331  229 GLN G N   
13175 C CA  . GLN G  229 ? 1.1329 0.9612 1.3262 0.0979  0.1900  0.0352  229 GLN G CA  
13176 C C   . GLN G  229 ? 1.0003 0.8362 1.1894 0.1038  0.1858  0.0414  229 GLN G C   
13177 O O   . GLN G  229 ? 1.0347 0.8763 1.2178 0.1033  0.1800  0.0412  229 GLN G O   
13178 C CB  . GLN G  229 ? 1.0132 0.8432 1.2044 0.0905  0.1824  0.0293  229 GLN G CB  
13179 C CG  . GLN G  229 ? 0.9539 0.7776 1.1478 0.0837  0.1852  0.0224  229 GLN G CG  
13180 C CD  . GLN G  229 ? 1.1036 0.9195 1.3052 0.0844  0.1939  0.0225  229 GLN G CD  
13181 O OE1 . GLN G  229 ? 1.1535 0.9692 1.3587 0.0882  0.1956  0.0265  229 GLN G OE1 
13182 N NE2 . GLN G  229 ? 1.2785 1.0877 1.4824 0.0808  0.1997  0.0181  229 GLN G NE2 
13183 N N   . GLU G  230 ? 1.0207 0.8566 1.2128 0.1091  0.1888  0.0469  230 GLU G N   
13184 C CA  . GLU G  230 ? 0.9412 0.7844 1.1294 0.1143  0.1849  0.0528  230 GLU G CA  
13185 C C   . GLU G  230 ? 0.9722 0.8193 1.1585 0.1118  0.1777  0.0517  230 GLU G C   
13186 O O   . GLU G  230 ? 0.9086 0.7621 1.0908 0.1146  0.1730  0.0554  230 GLU G O   
13187 C CB  . GLU G  230 ? 1.2194 1.0609 1.4113 0.1215  0.1920  0.0597  230 GLU G CB  
13188 N N   . GLY G  231 ? 0.8477 0.6908 1.0374 0.1063  0.1770  0.0467  231 GLY G N   
13189 C CA  . GLY G  231 ? 0.8848 0.7313 1.0737 0.1032  0.1702  0.0451  231 GLY G CA  
13190 C C   . GLY G  231 ? 0.9187 0.7689 1.1029 0.0973  0.1625  0.0400  231 GLY G C   
13191 O O   . GLY G  231 ? 0.9059 0.7550 1.0881 0.0949  0.1630  0.0370  231 GLY G O   
13192 N N   . ARG G  232 ? 0.8751 0.7296 1.0576 0.0949  0.1555  0.0391  232 ARG G N   
13193 C CA  . ARG G  232 ? 0.7517 0.6102 0.9299 0.0894  0.1477  0.0347  232 ARG G CA  
13194 C C   . ARG G  232 ? 0.7405 0.5979 0.9223 0.0837  0.1442  0.0307  232 ARG G C   
13195 O O   . ARG G  232 ? 0.7262 0.5809 0.9133 0.0846  0.1469  0.0319  232 ARG G O   
13196 C CB  . ARG G  232 ? 0.7802 0.6465 0.9520 0.0920  0.1413  0.0377  232 ARG G CB  
13197 C CG  . ARG G  232 ? 0.7971 0.6657 0.9643 0.0961  0.1430  0.0405  232 ARG G CG  
13198 C CD  . ARG G  232 ? 0.8084 0.6749 0.9740 0.0921  0.1433  0.0360  232 ARG G CD  
13199 N NE  . ARG G  232 ? 0.9393 0.8076 1.1015 0.0961  0.1456  0.0387  232 ARG G NE  
13200 C CZ  . ARG G  232 ? 0.9392 0.8035 1.1044 0.1002  0.1533  0.0415  232 ARG G CZ  
13201 N NH1 . ARG G  232 ? 0.7986 0.6567 0.9702 0.1009  0.1598  0.0417  232 ARG G NH1 
13202 N NH2 . ARG G  232 ? 0.8532 0.7198 1.0154 0.1037  0.1548  0.0441  232 ARG G NH2 
13203 N N   . MET G  233 ? 0.7484 0.6078 0.9274 0.0778  0.1384  0.0260  233 MET G N   
13204 C CA  . MET G  233 ? 0.7640 0.6236 0.9463 0.0720  0.1341  0.0223  233 MET G CA  
13205 C C   . MET G  233 ? 0.8432 0.7090 1.0202 0.0683  0.1251  0.0203  233 MET G C   
13206 O O   . MET G  233 ? 0.7586 0.6251 0.9316 0.0648  0.1228  0.0170  233 MET G O   
13207 C CB  . MET G  233 ? 0.7229 0.5763 0.9095 0.0669  0.1381  0.0174  233 MET G CB  
13208 C CG  . MET G  233 ? 0.7573 0.6107 0.9482 0.0610  0.1344  0.0139  233 MET G CG  
13209 S SD  . MET G  233 ? 0.9331 0.7792 1.1291 0.0550  0.1395  0.0082  233 MET G SD  
13210 C CE  . MET G  233 ? 0.9165 0.7558 1.1185 0.0611  0.1503  0.0119  233 MET G CE  
13211 N N   . ASN G  234 ? 0.7942 0.6644 0.9712 0.0691  0.1202  0.0223  234 ASN G N   
13212 C CA  . ASN G  234 ? 0.6954 0.5716 0.8680 0.0659  0.1117  0.0209  234 ASN G CA  
13213 C C   . ASN G  234 ? 0.6491 0.5251 0.8251 0.0589  0.1075  0.0164  234 ASN G C   
13214 O O   . ASN G  234 ? 0.7073 0.5806 0.8898 0.0576  0.1094  0.0160  234 ASN G O   
13215 C CB  . ASN G  234 ? 0.6383 0.5194 0.8092 0.0699  0.1084  0.0251  234 ASN G CB  
13216 C CG  . ASN G  234 ? 0.7463 0.6292 0.9124 0.0761  0.1108  0.0293  234 ASN G CG  
13217 O OD1 . ASN G  234 ? 0.7202 0.6010 0.8843 0.0776  0.1147  0.0293  234 ASN G OD1 
13218 N ND2 . ASN G  234 ? 0.8087 0.6956 0.9731 0.0797  0.1087  0.0330  234 ASN G ND2 
13219 N N   . TYR G  235 ? 0.5893 0.4683 0.7609 0.0543  0.1019  0.0132  235 TYR G N   
13220 C CA  . TYR G  235 ? 0.5340 0.4135 0.7081 0.0473  0.0975  0.0090  235 TYR G CA  
13221 C C   . TYR G  235 ? 0.6671 0.5530 0.8396 0.0456  0.0892  0.0097  235 TYR G C   
13222 O O   . TYR G  235 ? 0.6293 0.5195 0.7957 0.0469  0.0852  0.0108  235 TYR G O   
13223 C CB  . TYR G  235 ? 0.5102 0.3878 0.6808 0.0424  0.0976  0.0044  235 TYR G CB  
13224 C CG  . TYR G  235 ? 0.7616 0.6328 0.9335 0.0443  0.1061  0.0038  235 TYR G CG  
13225 C CD1 . TYR G  235 ? 0.7828 0.6534 0.9501 0.0487  0.1095  0.0057  235 TYR G CD1 
13226 C CD2 . TYR G  235 ? 0.7320 0.5977 0.9101 0.0417  0.1110  0.0014  235 TYR G CD2 
13227 C CE1 . TYR G  235 ? 0.7455 0.6102 0.9145 0.0507  0.1176  0.0054  235 TYR G CE1 
13228 C CE2 . TYR G  235 ? 0.7918 0.6513 0.9714 0.0434  0.1192  0.0009  235 TYR G CE2 
13229 C CZ  . TYR G  235 ? 0.7358 0.5948 0.9109 0.0480  0.1226  0.0030  235 TYR G CZ  
13230 O OH  . TYR G  235 ? 0.7863 0.6390 0.9634 0.0499  0.1310  0.0027  235 TYR G OH  
13231 N N   . TYR G  236 ? 0.6399 0.5264 0.8184 0.0426  0.0868  0.0091  236 TYR G N   
13232 C CA  . TYR G  236 ? 0.5534 0.4456 0.7318 0.0410  0.0794  0.0100  236 TYR G CA  
13233 C C   . TYR G  236 ? 0.6042 0.4978 0.7855 0.0336  0.0745  0.0062  236 TYR G C   
13234 O O   . TYR G  236 ? 0.7184 0.6082 0.9034 0.0300  0.0774  0.0032  236 TYR G O   
13235 C CB  . TYR G  236 ? 0.4734 0.3660 0.6567 0.0451  0.0807  0.0138  236 TYR G CB  
13236 C CG  . TYR G  236 ? 0.6934 0.5857 0.8734 0.0522  0.0846  0.0179  236 TYR G CG  
13237 C CD1 . TYR G  236 ? 0.6946 0.5818 0.8763 0.0560  0.0923  0.0192  236 TYR G CD1 
13238 C CD2 . TYR G  236 ? 0.6359 0.5330 0.8111 0.0549  0.0807  0.0205  236 TYR G CD2 
13239 C CE1 . TYR G  236 ? 0.6854 0.5728 0.8641 0.0624  0.0956  0.0233  236 TYR G CE1 
13240 C CE2 . TYR G  236 ? 0.7405 0.6378 0.9125 0.0611  0.0840  0.0242  236 TYR G CE2 
13241 C CZ  . TYR G  236 ? 0.7771 0.6697 0.9508 0.0648  0.0914  0.0257  236 TYR G CZ  
13242 O OH  . TYR G  236 ? 0.6644 0.5577 0.8348 0.0708  0.0945  0.0298  236 TYR G OH  
13243 N N   . TRP G  237 ? 0.6436 0.5427 0.8230 0.0313  0.0672  0.0064  237 TRP G N   
13244 C CA  . TRP G  237 ? 0.5787 0.4802 0.7606 0.0244  0.0617  0.0034  237 TRP G CA  
13245 C C   . TRP G  237 ? 0.5544 0.4617 0.7380 0.0240  0.0549  0.0056  237 TRP G C   
13246 O O   . TRP G  237 ? 0.6621 0.5717 0.8428 0.0284  0.0539  0.0087  237 TRP G O   
13247 C CB  . TRP G  237 ? 0.4917 0.3938 0.6672 0.0199  0.0593  -0.0003 237 TRP G CB  
13248 C CG  . TRP G  237 ? 0.6642 0.5703 0.8317 0.0217  0.0554  0.0009  237 TRP G CG  
13249 C CD1 . TRP G  237 ? 0.6275 0.5324 0.7890 0.0262  0.0586  0.0020  237 TRP G CD1 
13250 C CD2 . TRP G  237 ? 0.6158 0.5278 0.7808 0.0191  0.0476  0.0012  237 TRP G CD2 
13251 N NE1 . TRP G  237 ? 0.6551 0.5648 0.8105 0.0264  0.0532  0.0027  237 TRP G NE1 
13252 C CE2 . TRP G  237 ? 0.6517 0.5657 0.8090 0.0222  0.0465  0.0022  237 TRP G CE2 
13253 C CE3 . TRP G  237 ? 0.5650 0.4809 0.7338 0.0146  0.0414  0.0008  237 TRP G CE3 
13254 C CZ2 . TRP G  237 ? 0.7046 0.6239 0.8576 0.0207  0.0397  0.0027  237 TRP G CZ2 
13255 C CZ3 . TRP G  237 ? 0.6885 0.6098 0.8532 0.0133  0.0346  0.0016  237 TRP G CZ3 
13256 C CH2 . TRP G  237 ? 0.6266 0.5494 0.7835 0.0163  0.0339  0.0024  237 TRP G CH2 
13257 N N   . THR G  238 ? 0.5669 0.4765 0.7553 0.0184  0.0505  0.0040  238 THR G N   
13258 C CA  . THR G  238 ? 0.6440 0.5591 0.8350 0.0174  0.0440  0.0061  238 THR G CA  
13259 C C   . THR G  238 ? 0.6892 0.6070 0.8840 0.0102  0.0388  0.0036  238 THR G C   
13260 O O   . THR G  238 ? 0.7118 0.6268 0.9102 0.0065  0.0411  0.0009  238 THR G O   
13261 C CB  . THR G  238 ? 0.5877 0.5022 0.7856 0.0217  0.0464  0.0096  238 THR G CB  
13262 O OG1 . THR G  238 ? 0.6852 0.6049 0.8852 0.0210  0.0404  0.0117  238 THR G OG1 
13263 C CG2 . THR G  238 ? 0.6206 0.5317 0.8271 0.0195  0.0500  0.0084  238 THR G CG2 
13264 N N   . LEU G  239 ? 0.6651 0.5886 0.8592 0.0081  0.0317  0.0047  239 LEU G N   
13265 C CA  . LEU G  239 ? 0.6577 0.5849 0.8554 0.0013  0.0259  0.0030  239 LEU G CA  
13266 C C   . LEU G  239 ? 0.7979 0.7277 1.0053 0.0014  0.0238  0.0058  239 LEU G C   
13267 O O   . LEU G  239 ? 0.9782 0.9117 1.1863 0.0037  0.0204  0.0088  239 LEU G O   
13268 C CB  . LEU G  239 ? 0.7295 0.6615 0.9203 -0.0016 0.0192  0.0024  239 LEU G CB  
13269 C CG  . LEU G  239 ? 0.5782 0.5081 0.7594 -0.0026 0.0206  -0.0007 239 LEU G CG  
13270 C CD1 . LEU G  239 ? 0.8770 0.8117 1.0514 -0.0045 0.0142  -0.0006 239 LEU G CD1 
13271 C CD2 . LEU G  239 ? 0.6544 0.5813 0.8364 -0.0082 0.0225  -0.0049 239 LEU G CD2 
13272 N N   . VAL G  240 ? 0.7418 0.6697 0.9570 -0.0011 0.0261  0.0047  240 VAL G N   
13273 C CA  . VAL G  240 ? 0.7588 0.6892 0.9839 -0.0015 0.0242  0.0072  240 VAL G CA  
13274 C C   . VAL G  240 ? 0.7846 0.7211 1.0127 -0.0078 0.0165  0.0068  240 VAL G C   
13275 O O   . VAL G  240 ? 0.7978 0.7348 1.0252 -0.0137 0.0147  0.0036  240 VAL G O   
13276 C CB  . VAL G  240 ? 0.7922 0.7180 1.0252 -0.0009 0.0303  0.0067  240 VAL G CB  
13277 C CG1 . VAL G  240 ? 0.6763 0.5965 0.9050 -0.0017 0.0359  0.0031  240 VAL G CG1 
13278 C CG2 . VAL G  240 ? 0.8775 0.8067 1.1201 -0.0062 0.0265  0.0066  240 VAL G CG2 
13279 N N   . GLU G  241 ? 0.8859 0.8270 1.1174 -0.0065 0.0120  0.0103  241 GLU G N   
13280 C CA  . GLU G  241 ? 0.7699 0.7175 1.0043 -0.0117 0.0043  0.0109  241 GLU G CA  
13281 C C   . GLU G  241 ? 0.8574 0.8065 1.1013 -0.0168 0.0031  0.0100  241 GLU G C   
13282 O O   . GLU G  241 ? 0.8539 0.7993 1.1044 -0.0152 0.0082  0.0101  241 GLU G O   
13283 C CB  . GLU G  241 ? 0.9857 0.9371 1.2230 -0.0083 0.0010  0.0152  241 GLU G CB  
13284 C CG  . GLU G  241 ? 1.1867 1.1374 1.4150 -0.0035 0.0017  0.0162  241 GLU G CG  
13285 C CD  . GLU G  241 ? 1.4957 1.4496 1.7153 -0.0069 -0.0036 0.0146  241 GLU G CD  
13286 O OE1 . GLU G  241 ? 1.5710 1.5231 1.7815 -0.0040 -0.0019 0.0138  241 GLU G OE1 
13287 O OE2 . GLU G  241 ? 1.6560 1.6146 1.8779 -0.0125 -0.0094 0.0142  241 GLU G OE2 
13288 N N   . PRO G  242 ? 1.0055 0.9601 1.2501 -0.0231 -0.0037 0.0093  242 PRO G N   
13289 C CA  . PRO G  242 ? 0.9778 0.9350 1.2319 -0.0284 -0.0058 0.0089  242 PRO G CA  
13290 C C   . PRO G  242 ? 0.9546 0.9131 1.2200 -0.0253 -0.0051 0.0129  242 PRO G C   
13291 O O   . PRO G  242 ? 0.8634 0.8252 1.1303 -0.0224 -0.0080 0.0165  242 PRO G O   
13292 C CB  . PRO G  242 ? 0.7367 0.7009 0.9886 -0.0345 -0.0142 0.0088  242 PRO G CB  
13293 C CG  . PRO G  242 ? 0.7574 0.7203 0.9967 -0.0339 -0.0148 0.0069  242 PRO G CG  
13294 C CD  . PRO G  242 ? 0.8128 0.7714 1.0491 -0.0259 -0.0097 0.0087  242 PRO G CD  
13295 N N   . GLY G  243 ? 0.8661 0.8220 1.1396 -0.0259 -0.0010 0.0122  243 GLY G N   
13296 C CA  . GLY G  243 ? 0.8962 0.8529 1.1810 -0.0230 0.0002  0.0157  243 GLY G CA  
13297 C C   . GLY G  243 ? 0.8505 0.8014 1.1345 -0.0154 0.0072  0.0173  243 GLY G C   
13298 O O   . GLY G  243 ? 1.0440 0.9944 1.3367 -0.0124 0.0096  0.0201  243 GLY G O   
13299 N N   . ASP G  244 ? 0.8623 0.8089 1.1358 -0.0123 0.0106  0.0156  244 ASP G N   
13300 C CA  . ASP G  244 ? 0.8070 0.7482 1.0786 -0.0052 0.0174  0.0169  244 ASP G CA  
13301 C C   . ASP G  244 ? 0.8421 0.7769 1.1140 -0.0047 0.0245  0.0143  244 ASP G C   
13302 O O   . ASP G  244 ? 0.9891 0.9231 1.2595 -0.0096 0.0244  0.0107  244 ASP G O   
13303 C CB  . ASP G  244 ? 0.8821 0.8229 1.1423 -0.0018 0.0168  0.0172  244 ASP G CB  
13304 C CG  . ASP G  244 ? 1.0861 1.0228 1.3445 0.0055  0.0226  0.0194  244 ASP G CG  
13305 O OD1 . ASP G  244 ? 1.1134 1.0501 1.3633 0.0087  0.0223  0.0199  244 ASP G OD1 
13306 O OD2 . ASP G  244 ? 0.9622 0.8959 1.2278 0.0080  0.0273  0.0207  244 ASP G OD2 
13307 N N   . LYS G  245 ? 0.7584 0.6884 1.0322 0.0011  0.0310  0.0159  245 LYS G N   
13308 C CA  . LYS G  245 ? 0.8891 0.8126 1.1632 0.0023  0.0383  0.0139  245 LYS G CA  
13309 C C   . LYS G  245 ? 0.8967 0.8154 1.1631 0.0089  0.0440  0.0148  245 LYS G C   
13310 O O   . LYS G  245 ? 0.8781 0.7979 1.1421 0.0133  0.0435  0.0177  245 LYS G O   
13311 C CB  . LYS G  245 ? 1.0206 0.9426 1.3064 0.0024  0.0416  0.0150  245 LYS G CB  
13312 C CG  . LYS G  245 ? 1.0001 0.9205 1.2896 0.0087  0.0451  0.0189  245 LYS G CG  
13313 C CD  . LYS G  245 ? 1.0030 0.9215 1.3041 0.0084  0.0486  0.0197  245 LYS G CD  
13314 C CE  . LYS G  245 ? 1.1513 1.0677 1.4557 0.0146  0.0526  0.0233  245 LYS G CE  
13315 N NZ  . LYS G  245 ? 1.1273 1.0423 1.4436 0.0142  0.0557  0.0243  245 LYS G NZ  
13316 N N   . ILE G  246 ? 0.8198 0.7332 1.0827 0.0093  0.0495  0.0123  246 ILE G N   
13317 C CA  . ILE G  246 ? 0.7779 0.6868 1.0341 0.0153  0.0552  0.0132  246 ILE G CA  
13318 C C   . ILE G  246 ? 0.8466 0.7493 1.1078 0.0181  0.0633  0.0133  246 ILE G C   
13319 O O   . ILE G  246 ? 0.8576 0.7578 1.1231 0.0144  0.0655  0.0106  246 ILE G O   
13320 C CB  . ILE G  246 ? 0.7536 0.6615 0.9996 0.0142  0.0550  0.0105  246 ILE G CB  
13321 C CG1 . ILE G  246 ? 0.6870 0.5906 0.9266 0.0207  0.0609  0.0119  246 ILE G CG1 
13322 C CG2 . ILE G  246 ? 0.7298 0.6354 0.9772 0.0086  0.0563  0.0062  246 ILE G CG2 
13323 C CD1 . ILE G  246 ? 0.6494 0.5517 0.8797 0.0199  0.0614  0.0094  246 ILE G CD1 
13324 N N   . THR G  247 ? 0.8830 0.7832 1.1436 0.0244  0.0676  0.0165  247 THR G N   
13325 C CA  . THR G  247 ? 0.9402 0.8346 1.2057 0.0276  0.0753  0.0173  247 THR G CA  
13326 C C   . THR G  247 ? 0.8105 0.7000 1.0687 0.0323  0.0815  0.0175  247 THR G C   
13327 O O   . THR G  247 ? 0.7733 0.6641 1.0237 0.0358  0.0806  0.0191  247 THR G O   
13328 C CB  . THR G  247 ? 0.9289 0.8237 1.2005 0.0313  0.0765  0.0210  247 THR G CB  
13329 O OG1 . THR G  247 ? 1.0783 0.9766 1.3592 0.0269  0.0724  0.0208  247 THR G OG1 
13330 C CG2 . THR G  247 ? 0.8803 0.7689 1.1549 0.0356  0.0849  0.0222  247 THR G CG2 
13331 N N   . PHE G  248 ? 0.9194 0.8034 1.1806 0.0322  0.0878  0.0160  248 PHE G N   
13332 C CA  . PHE G  248 ? 0.9035 0.7824 1.1596 0.0370  0.0946  0.0168  248 PHE G CA  
13333 C C   . PHE G  248 ? 0.8464 0.7208 1.1083 0.0413  0.1014  0.0194  248 PHE G C   
13334 O O   . PHE G  248 ? 0.9632 0.8361 1.2338 0.0390  0.1030  0.0186  248 PHE G O   
13335 C CB  . PHE G  248 ? 0.7116 0.5872 0.9654 0.0336  0.0970  0.0129  248 PHE G CB  
13336 C CG  . PHE G  248 ? 0.6753 0.5545 0.9216 0.0303  0.0915  0.0105  248 PHE G CG  
13337 C CD1 . PHE G  248 ? 0.7599 0.6436 1.0079 0.0239  0.0847  0.0080  248 PHE G CD1 
13338 C CD2 . PHE G  248 ? 0.7238 0.6020 0.9613 0.0335  0.0931  0.0110  248 PHE G CD2 
13339 C CE1 . PHE G  248 ? 0.7694 0.6563 1.0102 0.0207  0.0797  0.0059  248 PHE G CE1 
13340 C CE2 . PHE G  248 ? 0.7484 0.6298 0.9791 0.0305  0.0882  0.0087  248 PHE G CE2 
13341 C CZ  . PHE G  248 ? 0.5672 0.4528 0.7993 0.0240  0.0815  0.0062  248 PHE G CZ  
13342 N N   . GLU G  249 ? 0.7348 0.6074 0.9919 0.0476  0.1053  0.0226  249 GLU G N   
13343 C CA  . GLU G  249 ? 0.8445 0.7130 1.1058 0.0522  0.1118  0.0255  249 GLU G CA  
13344 C C   . GLU G  249 ? 0.9033 0.7682 1.1581 0.0578  0.1176  0.0275  249 GLU G C   
13345 O O   . GLU G  249 ? 1.0108 0.8783 1.2581 0.0610  0.1158  0.0296  249 GLU G O   
13346 C CB  . GLU G  249 ? 0.9524 0.8242 1.2158 0.0544  0.1091  0.0286  249 GLU G CB  
13347 C CG  . GLU G  249 ? 1.1514 1.0192 1.4190 0.0591  0.1156  0.0317  249 GLU G CG  
13348 C CD  . GLU G  249 ? 1.2920 1.1630 1.5619 0.0606  0.1129  0.0344  249 GLU G CD  
13349 O OE1 . GLU G  249 ? 1.3850 1.2535 1.6547 0.0653  0.1176  0.0375  249 GLU G OE1 
13350 O OE2 . GLU G  249 ? 1.1160 0.9917 1.3878 0.0570  0.1064  0.0334  249 GLU G OE2 
13351 N N   . ALA G  250 ? 0.8628 0.7218 1.1208 0.0588  0.1247  0.0271  250 ALA G N   
13352 C CA  . ALA G  250 ? 0.8147 0.6703 1.0671 0.0638  0.1304  0.0290  250 ALA G CA  
13353 C C   . ALA G  250 ? 0.9583 0.8077 1.2157 0.0673  0.1389  0.0310  250 ALA G C   
13354 O O   . ALA G  250 ? 0.9415 0.7877 1.2067 0.0644  0.1415  0.0291  250 ALA G O   
13355 C CB  . ALA G  250 ? 0.8526 0.7074 1.1006 0.0611  0.1301  0.0257  250 ALA G CB  
13356 N N   . THR G  251 ? 0.8443 0.6923 1.0972 0.0734  0.1432  0.0349  251 THR G N   
13357 C CA  . THR G  251 ? 0.9102 0.7522 1.1665 0.0773  0.1517  0.0371  251 THR G CA  
13358 C C   . THR G  251 ? 0.9988 0.8375 1.2511 0.0790  0.1562  0.0369  251 THR G C   
13359 O O   . THR G  251 ? 0.8782 0.7123 1.1311 0.0834  0.1634  0.0396  251 THR G O   
13360 C CB  . THR G  251 ? 0.8688 0.7113 1.1231 0.0832  0.1539  0.0422  251 THR G CB  
13361 O OG1 . THR G  251 ? 0.8606 0.7078 1.1059 0.0859  0.1502  0.0443  251 THR G OG1 
13362 C CG2 . THR G  251 ? 0.8751 0.7192 1.1350 0.0817  0.1514  0.0425  251 THR G CG2 
13363 N N   . GLY G  252 ? 1.0169 0.8578 1.2651 0.0755  0.1521  0.0336  252 GLY G N   
13364 C CA  . GLY G  252 ? 0.9468 0.7848 1.1914 0.0765  0.1560  0.0329  252 GLY G CA  
13365 C C   . GLY G  252 ? 0.8893 0.7320 1.1256 0.0758  0.1505  0.0320  252 GLY G C   
13366 O O   . GLY G  252 ? 0.9174 0.7658 1.1502 0.0752  0.1438  0.0326  252 GLY G O   
13367 N N   . ASN G  253 ? 0.9206 0.7608 1.1540 0.0757  0.1535  0.0306  253 ASN G N   
13368 C CA  . ASN G  253 ? 0.8315 0.6757 1.0570 0.0757  0.1494  0.0302  253 ASN G CA  
13369 C C   . ASN G  253 ? 0.7565 0.6049 0.9803 0.0692  0.1416  0.0257  253 ASN G C   
13370 O O   . ASN G  253 ? 0.8432 0.6957 1.0603 0.0690  0.1370  0.0253  253 ASN G O   
13371 C CB  . ASN G  253 ? 0.8228 0.6715 1.0425 0.0815  0.1476  0.0351  253 ASN G CB  
13372 C CG  . ASN G  253 ? 0.7574 0.6027 0.9780 0.0880  0.1550  0.0400  253 ASN G CG  
13373 O OD1 . ASN G  253 ? 0.8256 0.6709 1.0418 0.0921  0.1578  0.0427  253 ASN G OD1 
13374 N ND2 . ASN G  253 ? 0.8486 0.6910 1.0751 0.0890  0.1583  0.0415  253 ASN G ND2 
13375 N N   . LEU G  254 ? 0.7835 0.6310 1.0134 0.0640  0.1399  0.0224  254 LEU G N   
13376 C CA  . LEU G  254 ? 0.7538 0.6055 0.9826 0.0576  0.1322  0.0185  254 LEU G CA  
13377 C C   . LEU G  254 ? 0.7194 0.5681 0.9490 0.0518  0.1333  0.0133  254 LEU G C   
13378 O O   . LEU G  254 ? 0.9418 0.7863 1.1778 0.0488  0.1369  0.0109  254 LEU G O   
13379 C CB  . LEU G  254 ? 0.7940 0.6483 1.0289 0.0551  0.1281  0.0185  254 LEU G CB  
13380 C CG  . LEU G  254 ? 0.6986 0.5574 0.9337 0.0482  0.1203  0.0147  254 LEU G CG  
13381 C CD1 . LEU G  254 ? 0.7707 0.6351 0.9975 0.0484  0.1139  0.0151  254 LEU G CD1 
13382 C CD2 . LEU G  254 ? 0.6781 0.5392 0.9204 0.0463  0.1171  0.0153  254 LEU G CD2 
13383 N N   . VAL G  255 ? 0.6310 0.4818 0.8537 0.0501  0.1302  0.0114  255 VAL G N   
13384 C CA  . VAL G  255 ? 0.6502 0.4991 0.8723 0.0439  0.1300  0.0061  255 VAL G CA  
13385 C C   . VAL G  255 ? 0.6668 0.5204 0.8906 0.0373  0.1221  0.0031  255 VAL G C   
13386 O O   . VAL G  255 ? 0.7758 0.6348 0.9943 0.0356  0.1152  0.0027  255 VAL G O   
13387 C CB  . VAL G  255 ? 0.6087 0.4582 0.8227 0.0450  0.1299  0.0055  255 VAL G CB  
13388 C CG1 . VAL G  255 ? 0.7478 0.5950 0.9606 0.0384  0.1301  -0.0002 255 VAL G CG1 
13389 C CG2 . VAL G  255 ? 0.5914 0.4369 0.8044 0.0519  0.1376  0.0092  255 VAL G CG2 
13390 N N   . VAL G  256 ? 0.7187 0.5704 0.9501 0.0336  0.1231  0.0012  256 VAL G N   
13391 C CA  . VAL G  256 ? 0.7293 0.5858 0.9639 0.0279  0.1158  -0.0007 256 VAL G CA  
13392 C C   . VAL G  256 ? 0.7088 0.5673 0.9399 0.0206  0.1112  -0.0056 256 VAL G C   
13393 O O   . VAL G  256 ? 0.8544 0.7087 1.0832 0.0185  0.1153  -0.0088 256 VAL G O   
13394 C CB  . VAL G  256 ? 0.8439 0.6980 1.0884 0.0260  0.1184  -0.0011 256 VAL G CB  
13395 C CG1 . VAL G  256 ? 0.8073 0.6595 1.0554 0.0329  0.1229  0.0037  256 VAL G CG1 
13396 C CG2 . VAL G  256 ? 0.9680 0.8161 1.2154 0.0220  0.1243  -0.0054 256 VAL G CG2 
13397 N N   . PRO G  257 ? 0.7294 0.5943 0.9601 0.0167  0.1027  -0.0062 257 PRO G N   
13398 C CA  . PRO G  257 ? 0.7456 0.6132 0.9731 0.0092  0.0975  -0.0106 257 PRO G CA  
13399 C C   . PRO G  257 ? 0.7976 0.6620 1.0309 0.0029  0.1000  -0.0149 257 PRO G C   
13400 O O   . PRO G  257 ? 0.8735 0.7365 1.1149 0.0030  0.1021  -0.0141 257 PRO G O   
13401 C CB  . PRO G  257 ? 0.6731 0.5482 0.9011 0.0075  0.0885  -0.0090 257 PRO G CB  
13402 C CG  . PRO G  257 ? 0.7475 0.6239 0.9757 0.0149  0.0890  -0.0038 257 PRO G CG  
13403 C CD  . PRO G  257 ? 0.6793 0.5494 0.9120 0.0193  0.0977  -0.0023 257 PRO G CD  
13404 N N   . ARG G  258 ? 0.9418 0.8049 1.1709 -0.0027 0.0997  -0.0196 258 ARG G N   
13405 C CA  . ARG G  258 ? 0.8929 0.7538 1.1268 -0.0097 0.1012  -0.0241 258 ARG G CA  
13406 C C   . ARG G  258 ? 0.7786 0.6455 1.0100 -0.0174 0.0926  -0.0271 258 ARG G C   
13407 O O   . ARG G  258 ? 0.8526 0.7226 1.0900 -0.0223 0.0888  -0.0281 258 ARG G O   
13408 C CB  . ARG G  258 ? 0.9261 0.7796 1.1574 -0.0106 0.1091  -0.0277 258 ARG G CB  
13409 C CG  . ARG G  258 ? 0.9287 0.7759 1.1679 -0.0106 0.1169  -0.0287 258 ARG G CG  
13410 C CD  . ARG G  258 ? 1.0708 0.9122 1.3084 -0.0157 0.1223  -0.0342 258 ARG G CD  
13411 N NE  . ARG G  258 ? 1.1427 0.9869 1.3817 -0.0251 0.1176  -0.0390 258 ARG G NE  
13412 C CZ  . ARG G  258 ? 1.1962 1.0356 1.4378 -0.0308 0.1223  -0.0439 258 ARG G CZ  
13413 N NH1 . ARG G  258 ? 1.1093 0.9406 1.3528 -0.0278 0.1321  -0.0446 258 ARG G NH1 
13414 N NH2 . ARG G  258 ? 1.1766 1.0194 1.4191 -0.0395 0.1173  -0.0481 258 ARG G NH2 
13415 N N   . TYR G  259 ? 0.8347 0.7035 1.0573 -0.0184 0.0895  -0.0283 259 TYR G N   
13416 C CA  . TYR G  259 ? 0.7562 0.6309 0.9751 -0.0253 0.0811  -0.0307 259 TYR G CA  
13417 C C   . TYR G  259 ? 0.7769 0.6579 0.9916 -0.0218 0.0743  -0.0268 259 TYR G C   
13418 O O   . TYR G  259 ? 0.8266 0.7064 1.0366 -0.0155 0.0765  -0.0242 259 TYR G O   
13419 C CB  . TYR G  259 ? 0.8232 0.6950 1.0350 -0.0303 0.0829  -0.0358 259 TYR G CB  
13420 C CG  . TYR G  259 ? 1.1077 0.9743 1.3233 -0.0359 0.0882  -0.0407 259 TYR G CG  
13421 C CD1 . TYR G  259 ? 1.0140 0.8725 1.2315 -0.0325 0.0981  -0.0414 259 TYR G CD1 
13422 C CD2 . TYR G  259 ? 1.0993 0.9691 1.3167 -0.0447 0.0835  -0.0444 259 TYR G CD2 
13423 C CE1 . TYR G  259 ? 1.0648 0.9182 1.2859 -0.0378 0.1033  -0.0460 259 TYR G CE1 
13424 C CE2 . TYR G  259 ? 1.0812 0.9464 1.3020 -0.0502 0.0885  -0.0490 259 TYR G CE2 
13425 C CZ  . TYR G  259 ? 1.0850 0.9418 1.3076 -0.0467 0.0985  -0.0499 259 TYR G CZ  
13426 O OH  . TYR G  259 ? 1.2908 1.1427 1.5169 -0.0523 0.1037  -0.0547 259 TYR G OH  
13427 N N   . ALA G  260 ? 0.7784 0.6662 0.9952 -0.0259 0.0662  -0.0263 260 ALA G N   
13428 C CA  . ALA G  260 ? 0.7413 0.6353 0.9537 -0.0239 0.0591  -0.0232 260 ALA G CA  
13429 C C   . ALA G  260 ? 0.7740 0.6720 0.9803 -0.0311 0.0528  -0.0266 260 ALA G C   
13430 O O   . ALA G  260 ? 0.7432 0.6387 0.9482 -0.0371 0.0545  -0.0312 260 ALA G O   
13431 C CB  . ALA G  260 ? 0.6885 0.5873 0.9085 -0.0222 0.0548  -0.0192 260 ALA G CB  
13432 N N   . PHE G  261 ? 0.8954 0.7995 1.0979 -0.0307 0.0456  -0.0243 261 PHE G N   
13433 C CA  . PHE G  261 ? 0.6951 0.6033 0.8912 -0.0371 0.0393  -0.0270 261 PHE G CA  
13434 C C   . PHE G  261 ? 0.7553 0.6716 0.9536 -0.0394 0.0301  -0.0244 261 PHE G C   
13435 O O   . PHE G  261 ? 0.8594 0.7790 1.0550 -0.0351 0.0268  -0.0209 261 PHE G O   
13436 C CB  . PHE G  261 ? 0.5964 0.5028 0.7823 -0.0344 0.0407  -0.0276 261 PHE G CB  
13437 C CG  . PHE G  261 ? 0.6957 0.5944 0.8792 -0.0324 0.0495  -0.0302 261 PHE G CG  
13438 C CD1 . PHE G  261 ? 0.7406 0.6352 0.9253 -0.0245 0.0558  -0.0273 261 PHE G CD1 
13439 C CD2 . PHE G  261 ? 0.7282 0.6235 0.9082 -0.0387 0.0518  -0.0355 261 PHE G CD2 
13440 C CE1 . PHE G  261 ? 0.7868 0.6744 0.9698 -0.0225 0.0641  -0.0292 261 PHE G CE1 
13441 C CE2 . PHE G  261 ? 0.6284 0.5163 0.8067 -0.0368 0.0604  -0.0378 261 PHE G CE2 
13442 C CZ  . PHE G  261 ? 0.7305 0.6146 0.9105 -0.0286 0.0665  -0.0345 261 PHE G CZ  
13443 N N   . ALA G  262 ? 0.8327 0.7525 1.0360 -0.0461 0.0261  -0.0259 262 ALA G N   
13444 C CA  . ALA G  262 ? 0.6989 0.6267 0.9039 -0.0493 0.0171  -0.0236 262 ALA G CA  
13445 C C   . ALA G  262 ? 0.8056 0.7363 1.0004 -0.0514 0.0124  -0.0247 262 ALA G C   
13446 O O   . ALA G  262 ? 0.8839 0.8120 1.0719 -0.0558 0.0138  -0.0291 262 ALA G O   
13447 C CB  . ALA G  262 ? 0.9899 0.9209 1.2014 -0.0569 0.0139  -0.0256 262 ALA G CB  
13448 N N   . MET G  263 ? 0.7983 0.7339 0.9918 -0.0484 0.0070  -0.0208 263 MET G N   
13449 C CA  . MET G  263 ? 0.8727 0.8100 1.0560 -0.0486 0.0038  -0.0213 263 MET G CA  
13450 C C   . MET G  263 ? 0.8605 0.8055 1.0438 -0.0497 -0.0048 -0.0180 263 MET G C   
13451 O O   . MET G  263 ? 0.9575 0.9059 1.1483 -0.0471 -0.0073 -0.0140 263 MET G O   
13452 C CB  . MET G  263 ? 0.7804 0.7132 0.9592 -0.0407 0.0093  -0.0199 263 MET G CB  
13453 C CG  . MET G  263 ? 0.8316 0.7601 1.0008 -0.0415 0.0129  -0.0237 263 MET G CG  
13454 S SD  . MET G  263 ? 1.0965 1.0215 1.2612 -0.0319 0.0182  -0.0210 263 MET G SD  
13455 C CE  . MET G  263 ? 0.8592 0.7849 1.0340 -0.0258 0.0194  -0.0160 263 MET G CE  
13456 N N   . GLU G  264 ? 0.8530 0.8006 1.0279 -0.0535 -0.0092 -0.0197 264 GLU G N   
13457 C CA  . GLU G  264 ? 0.8863 0.8404 1.0592 -0.0536 -0.0167 -0.0165 264 GLU G CA  
13458 C C   . GLU G  264 ? 0.9174 0.8703 1.0791 -0.0526 -0.0166 -0.0180 264 GLU G C   
13459 O O   . GLU G  264 ? 0.9492 0.9010 1.1041 -0.0578 -0.0169 -0.0220 264 GLU G O   
13460 C CB  . GLU G  264 ? 0.9299 0.8904 1.1054 -0.0614 -0.0241 -0.0168 264 GLU G CB  
13461 C CG  . GLU G  264 ? 1.1983 1.1642 1.3842 -0.0604 -0.0284 -0.0121 264 GLU G CG  
13462 C CD  . GLU G  264 ? 1.3661 1.3371 1.5573 -0.0682 -0.0335 -0.0129 264 GLU G CD  
13463 O OE1 . GLU G  264 ? 1.3914 1.3693 1.5865 -0.0700 -0.0405 -0.0094 264 GLU G OE1 
13464 O OE2 . GLU G  264 ? 1.4152 1.3833 1.6069 -0.0728 -0.0306 -0.0169 264 GLU G OE2 
13465 N N   . ARG G  265 ? 0.8969 0.8497 1.0565 -0.0458 -0.0159 -0.0149 265 ARG G N   
13466 C CA  . ARG G  265 ? 0.9968 0.9483 1.1463 -0.0440 -0.0153 -0.0160 265 ARG G CA  
13467 C C   . ARG G  265 ? 1.0077 0.9655 1.1539 -0.0448 -0.0228 -0.0134 265 ARG G C   
13468 O O   . ARG G  265 ? 0.8902 0.8519 1.0421 -0.0425 -0.0263 -0.0094 265 ARG G O   
13469 C CB  . ARG G  265 ? 0.8452 0.7921 0.9939 -0.0359 -0.0087 -0.0146 265 ARG G CB  
13470 C CG  . ARG G  265 ? 0.8950 0.8425 1.0524 -0.0305 -0.0076 -0.0103 265 ARG G CG  
13471 C CD  . ARG G  265 ? 0.9709 0.9140 1.1268 -0.0228 -0.0011 -0.0089 265 ARG G CD  
13472 N NE  . ARG G  265 ? 1.0370 0.9832 1.1904 -0.0181 -0.0038 -0.0054 265 ARG G NE  
13473 C CZ  . ARG G  265 ? 0.9913 0.9395 1.1508 -0.0142 -0.0046 -0.0016 265 ARG G CZ  
13474 N NH1 . ARG G  265 ? 0.9572 0.9047 1.1258 -0.0144 -0.0032 -0.0006 265 ARG G NH1 
13475 N NH2 . ARG G  265 ? 0.9847 0.9355 1.1413 -0.0104 -0.0068 0.0012  265 ARG G NH2 
13476 N N   . ASN G  266 ? 1.0463 1.0047 1.1833 -0.0483 -0.0251 -0.0159 266 ASN G N   
13477 C CA  . ASN G  266 ? 1.1752 1.1383 1.3072 -0.0480 -0.0308 -0.0138 266 ASN G CA  
13478 C C   . ASN G  266 ? 1.1729 1.1331 1.3000 -0.0410 -0.0269 -0.0128 266 ASN G C   
13479 O O   . ASN G  266 ? 1.2093 1.1640 1.3354 -0.0376 -0.0201 -0.0143 266 ASN G O   
13480 C CB  . ASN G  266 ? 1.2351 1.2000 1.3590 -0.0551 -0.0348 -0.0171 266 ASN G CB  
13481 C CG  . ASN G  266 ? 1.1025 1.0633 1.2248 -0.0603 -0.0311 -0.0220 266 ASN G CG  
13482 O OD1 . ASN G  266 ? 0.9662 0.9295 1.0918 -0.0666 -0.0343 -0.0232 266 ASN G OD1 
13483 N ND2 . ASN G  266 ? 1.0256 0.9801 1.1431 -0.0578 -0.0243 -0.0249 266 ASN G ND2 
13484 N N   . ALA G  267 ? 1.0347 0.9987 1.1586 -0.0389 -0.0310 -0.0101 267 ALA G N   
13485 C CA  . ALA G  267 ? 1.2109 1.1729 1.3292 -0.0330 -0.0280 -0.0094 267 ALA G CA  
13486 C C   . ALA G  267 ? 1.1630 1.1231 1.2712 -0.0356 -0.0272 -0.0130 267 ALA G C   
13487 O O   . ALA G  267 ? 1.1114 1.0723 1.2134 -0.0330 -0.0279 -0.0124 267 ALA G O   
13488 C CB  . ALA G  267 ? 1.2012 1.1678 1.3203 -0.0298 -0.0324 -0.0053 267 ALA G CB  
13489 N N   . GLY G  268 ? 1.4511 1.4085 1.5577 -0.0408 -0.0254 -0.0170 268 GLY G N   
13490 C CA  . GLY G  268 ? 1.4811 1.4365 1.5784 -0.0442 -0.0246 -0.0209 268 GLY G CA  
13491 C C   . GLY G  268 ? 1.5650 1.5142 1.6585 -0.0407 -0.0168 -0.0233 268 GLY G C   
13492 O O   . GLY G  268 ? 1.5884 1.5334 1.6868 -0.0378 -0.0110 -0.0235 268 GLY G O   
13493 N N   . SER G  269 ? 1.0250 0.9738 1.1100 -0.0405 -0.0168 -0.0247 269 SER G N   
13494 C CA  . SER G  269 ? 0.8637 0.8069 0.9436 -0.0402 -0.0104 -0.0283 269 SER G CA  
13495 C C   . SER G  269 ? 0.8990 0.8385 0.9795 -0.0324 -0.0037 -0.0268 269 SER G C   
13496 O O   . SER G  269 ? 0.9739 0.9159 1.0548 -0.0270 -0.0049 -0.0232 269 SER G O   
13497 C CB  . SER G  269 ? 0.8397 0.7792 0.9217 -0.0457 -0.0075 -0.0322 269 SER G CB  
13498 O OG  . SER G  269 ? 0.8382 0.7725 0.9142 -0.0470 -0.0021 -0.0362 269 SER G OG  
13499 N N   . GLY G  270 ? 0.6929 0.6266 0.7730 -0.0322 0.0032  -0.0296 270 GLY G N   
13500 C CA  . GLY G  270 ? 0.7726 0.7027 0.8523 -0.0254 0.0098  -0.0285 270 GLY G CA  
13501 C C   . GLY G  270 ? 0.7082 0.6319 0.7864 -0.0276 0.0166  -0.0326 270 GLY G C   
13502 O O   . GLY G  270 ? 0.6889 0.6113 0.7656 -0.0345 0.0157  -0.0364 270 GLY G O   
13503 N N   . ILE G  271 ? 0.6431 0.5629 0.7216 -0.0219 0.0234  -0.0318 271 ILE G N   
13504 C CA  . ILE G  271 ? 0.5410 0.4541 0.6193 -0.0229 0.0310  -0.0353 271 ILE G CA  
13505 C C   . ILE G  271 ? 0.7029 0.6141 0.7741 -0.0220 0.0340  -0.0369 271 ILE G C   
13506 O O   . ILE G  271 ? 0.8618 0.7747 0.9313 -0.0161 0.0346  -0.0339 271 ILE G O   
13507 C CB  . ILE G  271 ? 0.5627 0.4722 0.6482 -0.0170 0.0375  -0.0329 271 ILE G CB  
13508 C CG1 . ILE G  271 ? 0.5473 0.4594 0.6401 -0.0169 0.0343  -0.0305 271 ILE G CG1 
13509 C CG2 . ILE G  271 ? 0.7192 0.6216 0.8058 -0.0189 0.0453  -0.0365 271 ILE G CG2 
13510 C CD1 . ILE G  271 ? 0.6788 0.5924 0.7760 -0.0091 0.0355  -0.0254 271 ILE G CD1 
13511 N N   . ILE G  272 ? 0.6956 0.6032 0.7626 -0.0279 0.0361  -0.0418 272 ILE G N   
13512 C CA  . ILE G  272 ? 0.8062 0.7113 0.8667 -0.0276 0.0395  -0.0439 272 ILE G CA  
13513 C C   . ILE G  272 ? 0.7777 0.6759 0.8409 -0.0248 0.0492  -0.0452 272 ILE G C   
13514 O O   . ILE G  272 ? 0.7426 0.6363 0.8090 -0.0283 0.0530  -0.0481 272 ILE G O   
13515 C CB  . ILE G  272 ? 0.7523 0.6576 0.8057 -0.0359 0.0361  -0.0486 272 ILE G CB  
13516 C CG1 . ILE G  272 ? 0.8060 0.7184 0.8562 -0.0382 0.0266  -0.0469 272 ILE G CG1 
13517 C CG2 . ILE G  272 ? 0.7901 0.6918 0.8373 -0.0357 0.0409  -0.0511 272 ILE G CG2 
13518 C CD1 . ILE G  272 ? 0.8141 0.7274 0.8570 -0.0464 0.0227  -0.0511 272 ILE G CD1 
13519 N N   . ILE G  273 ? 0.7744 0.6717 0.8366 -0.0185 0.0533  -0.0429 273 ILE G N   
13520 C CA  . ILE G  273 ? 0.8555 0.7463 0.9200 -0.0156 0.0627  -0.0438 273 ILE G CA  
13521 C C   . ILE G  273 ? 0.9455 0.8330 1.0034 -0.0192 0.0656  -0.0480 273 ILE G C   
13522 O O   . ILE G  273 ? 0.9381 0.8276 0.9916 -0.0163 0.0651  -0.0467 273 ILE G O   
13523 C CB  . ILE G  273 ? 0.8661 0.7576 0.9342 -0.0063 0.0663  -0.0385 273 ILE G CB  
13524 C CG1 . ILE G  273 ? 0.8433 0.7375 0.9179 -0.0027 0.0641  -0.0345 273 ILE G CG1 
13525 C CG2 . ILE G  273 ? 0.8974 0.7822 0.9680 -0.0034 0.0762  -0.0393 273 ILE G CG2 
13526 C CD1 . ILE G  273 ? 1.0850 0.9864 1.1577 -0.0024 0.0553  -0.0318 273 ILE G CD1 
13527 N N   . SER G  274 ? 0.9743 0.8567 1.0314 -0.0257 0.0688  -0.0531 274 SER G N   
13528 C CA  . SER G  274 ? 0.9694 0.8486 1.0198 -0.0304 0.0713  -0.0578 274 SER G CA  
13529 C C   . SER G  274 ? 1.0234 0.8946 1.0754 -0.0345 0.0791  -0.0626 274 SER G C   
13530 O O   . SER G  274 ? 1.0027 0.8719 1.0599 -0.0364 0.0804  -0.0634 274 SER G O   
13531 C CB  . SER G  274 ? 0.8852 0.7689 0.9287 -0.0373 0.0629  -0.0602 274 SER G CB  
13532 O OG  . SER G  274 ? 0.9717 0.8513 1.0090 -0.0438 0.0655  -0.0657 274 SER G OG  
13533 N N   . ASP G  275 ? 1.3202 1.1869 1.3679 -0.0360 0.0845  -0.0658 275 ASP G N   
13534 C CA  . ASP G  275 ? 1.2730 1.1318 1.3213 -0.0406 0.0923  -0.0709 275 ASP G CA  
13535 C C   . ASP G  275 ? 1.1112 0.9697 1.1529 -0.0509 0.0885  -0.0769 275 ASP G C   
13536 O O   . ASP G  275 ? 1.2094 1.0622 1.2514 -0.0566 0.0931  -0.0817 275 ASP G O   
13537 C CB  . ASP G  275 ? 1.5027 1.3563 1.5500 -0.0369 0.1008  -0.0714 275 ASP G CB  
13538 C CG  . ASP G  275 ? 1.6900 1.5440 1.7437 -0.0268 0.1050  -0.0654 275 ASP G CG  
13539 O OD1 . ASP G  275 ? 1.8695 1.7280 1.9213 -0.0217 0.1025  -0.0617 275 ASP G OD1 
13540 O OD2 . ASP G  275 ? 1.5741 1.4240 1.6348 -0.0240 0.1108  -0.0644 275 ASP G OD2 
13541 N N   . THR G  276 ? 1.0778 0.9426 1.1134 -0.0534 0.0800  -0.0764 276 THR G N   
13542 C CA  . THR G  276 ? 1.0284 0.8941 1.0568 -0.0631 0.0752  -0.0814 276 THR G CA  
13543 C C   . THR G  276 ? 1.1125 0.9766 1.1437 -0.0698 0.0746  -0.0846 276 THR G C   
13544 O O   . THR G  276 ? 1.0520 0.9183 1.0899 -0.0674 0.0726  -0.0817 276 THR G O   
13545 C CB  . THR G  276 ? 0.8773 0.7513 0.9010 -0.0636 0.0649  -0.0788 276 THR G CB  
13546 O OG1 . THR G  276 ? 0.9121 0.7876 0.9330 -0.0578 0.0655  -0.0760 276 THR G OG1 
13547 C CG2 . THR G  276 ? 0.9093 0.7846 0.9251 -0.0736 0.0598  -0.0835 276 THR G CG2 
13548 N N   . PRO G  277 ? 1.1465 1.0067 1.1722 -0.0785 0.0764  -0.0909 277 PRO G N   
13549 C CA  . PRO G  277 ? 1.0088 0.8674 1.0363 -0.0860 0.0761  -0.0948 277 PRO G CA  
13550 C C   . PRO G  277 ? 1.0075 0.8741 1.0356 -0.0894 0.0655  -0.0928 277 PRO G C   
13551 O O   . PRO G  277 ? 1.0941 0.9664 1.1164 -0.0911 0.0579  -0.0916 277 PRO G O   
13552 C CB  . PRO G  277 ? 1.1851 1.0393 1.2041 -0.0948 0.0788  -0.1017 277 PRO G CB  
13553 C CG  . PRO G  277 ? 1.3578 1.2085 1.3734 -0.0902 0.0844  -0.1015 277 PRO G CG  
13554 C CD  . PRO G  277 ? 1.1366 0.9937 1.1541 -0.0818 0.0793  -0.0948 277 PRO G CD  
13555 N N   . VAL G  278 ? 1.0294 0.8961 1.0645 -0.0903 0.0653  -0.0923 278 VAL G N   
13556 C CA  . VAL G  278 ? 1.0989 0.9726 1.1351 -0.0947 0.0559  -0.0910 278 VAL G CA  
13557 C C   . VAL G  278 ? 1.0781 0.9516 1.1074 -0.1059 0.0535  -0.0971 278 VAL G C   
13558 O O   . VAL G  278 ? 1.2024 1.0691 1.2298 -0.1105 0.0605  -0.1024 278 VAL G O   
13559 C CB  . VAL G  278 ? 0.9768 0.8507 1.0232 -0.0924 0.0568  -0.0888 278 VAL G CB  
13560 C CG1 . VAL G  278 ? 1.2042 1.0699 1.2535 -0.0954 0.0660  -0.0935 278 VAL G CG1 
13561 C CG2 . VAL G  278 ? 0.8820 0.7632 0.9299 -0.0974 0.0472  -0.0876 278 VAL G CG2 
13562 N N   . HIS G  279 ? 1.0673 0.9481 1.0926 -0.1104 0.0439  -0.0961 279 HIS G N   
13563 C CA  . HIS G  279 ? 1.1022 0.9835 1.1197 -0.1212 0.0409  -0.1015 279 HIS G CA  
13564 C C   . HIS G  279 ? 1.1639 1.0528 1.1829 -0.1269 0.0314  -0.1003 279 HIS G C   
13565 O O   . HIS G  279 ? 1.2850 1.1800 1.3094 -0.1223 0.0254  -0.0947 279 HIS G O   
13566 C CB  . HIS G  279 ? 1.3231 1.2048 1.3305 -0.1225 0.0394  -0.1028 279 HIS G CB  
13567 C CG  . HIS G  279 ? 1.3941 1.2674 1.3960 -0.1256 0.0483  -0.1087 279 HIS G CG  
13568 N ND1 . HIS G  279 ? 1.4096 1.2812 1.4034 -0.1358 0.0481  -0.1148 279 HIS G ND1 
13569 C CD2 . HIS G  279 ? 1.3930 1.2592 1.3966 -0.1200 0.0579  -0.1093 279 HIS G CD2 
13570 C CE1 . HIS G  279 ? 1.5402 1.4036 1.5308 -0.1362 0.0574  -0.1191 279 HIS G CE1 
13571 N NE2 . HIS G  279 ? 1.4862 1.3463 1.4829 -0.1267 0.0634  -0.1158 279 HIS G NE2 
13572 N N   . ASP G  280 ? 1.2420 1.1306 1.2563 -0.1371 0.0302  -0.1055 280 ASP G N   
13573 C CA  . ASP G  280 ? 1.3171 1.2134 1.3315 -0.1437 0.0207  -0.1047 280 ASP G CA  
13574 C C   . ASP G  280 ? 1.3779 1.2798 1.3832 -0.1470 0.0131  -0.1040 280 ASP G C   
13575 O O   . ASP G  280 ? 1.5863 1.4879 1.5832 -0.1558 0.0118  -0.1087 280 ASP G O   
13576 C CB  . ASP G  280 ? 1.4263 1.3200 1.4400 -0.1535 0.0228  -0.1107 280 ASP G CB  
13577 C CG  . ASP G  280 ? 1.7323 1.6345 1.7453 -0.1613 0.0128  -0.1101 280 ASP G CG  
13578 O OD1 . ASP G  280 ? 1.7822 1.6920 1.7983 -0.1578 0.0048  -0.1043 280 ASP G OD1 
13579 O OD2 . ASP G  280 ? 1.7632 1.6645 1.7728 -0.1709 0.0130  -0.1153 280 ASP G OD2 
13580 N N   . CYS G  281 ? 1.3525 1.2593 1.3592 -0.1399 0.0083  -0.0981 281 CYS G N   
13581 C CA  . CYS G  281 ? 1.3338 1.2460 1.3325 -0.1420 0.0011  -0.0967 281 CYS G CA  
13582 C C   . CYS G  281 ? 1.2777 1.1980 1.2814 -0.1366 -0.0070 -0.0896 281 CYS G C   
13583 O O   . CYS G  281 ? 1.2965 1.2172 1.3093 -0.1293 -0.0057 -0.0856 281 CYS G O   
13584 C CB  . CYS G  281 ? 1.1787 1.0859 1.1701 -0.1390 0.0064  -0.0986 281 CYS G CB  
13585 S SG  . CYS G  281 ? 1.6378 1.5411 1.6359 -0.1258 0.0132  -0.0944 281 CYS G SG  
13586 N N   . ASN G  282 ? 1.1541 1.0807 1.1520 -0.1402 -0.0151 -0.0881 282 ASN G N   
13587 C CA  . ASN G  282 ? 1.0585 0.9928 1.0602 -0.1356 -0.0230 -0.0815 282 ASN G CA  
13588 C C   . ASN G  282 ? 1.1147 1.0488 1.1125 -0.1288 -0.0226 -0.0789 282 ASN G C   
13589 O O   . ASN G  282 ? 1.1167 1.0480 1.1054 -0.1311 -0.0206 -0.0821 282 ASN G O   
13590 C CB  . ASN G  282 ? 1.1352 1.0772 1.1339 -0.1435 -0.0326 -0.0808 282 ASN G CB  
13591 C CG  . ASN G  282 ? 1.4021 1.3493 1.4106 -0.1447 -0.0372 -0.0777 282 ASN G CG  
13592 O OD1 . ASN G  282 ? 1.3948 1.3422 1.4124 -0.1374 -0.0359 -0.0738 282 ASN G OD1 
13593 N ND2 . ASN G  282 ? 1.7574 1.7090 1.7638 -0.1539 -0.0425 -0.0795 282 ASN G ND2 
13594 N N   . THR G  283 ? 1.0375 0.9745 1.0419 -0.1205 -0.0243 -0.0733 283 THR G N   
13595 C CA  . THR G  283 ? 0.9195 0.8576 0.9208 -0.1140 -0.0250 -0.0702 283 THR G CA  
13596 C C   . THR G  283 ? 0.8272 0.7719 0.8350 -0.1088 -0.0313 -0.0637 283 THR G C   
13597 O O   . THR G  283 ? 0.9580 0.9048 0.9744 -0.1077 -0.0327 -0.0614 283 THR G O   
13598 C CB  . THR G  283 ? 0.8373 0.7685 0.8395 -0.1068 -0.0159 -0.0711 283 THR G CB  
13599 O OG1 . THR G  283 ? 0.7709 0.7033 0.7683 -0.1022 -0.0167 -0.0691 283 THR G OG1 
13600 C CG2 . THR G  283 ? 0.8230 0.7534 0.8359 -0.0998 -0.0129 -0.0677 283 THR G CG2 
13601 N N   . THR G  284 ? 0.7777 0.7257 0.7816 -0.1056 -0.0349 -0.0608 284 THR G N   
13602 C CA  . THR G  284 ? 0.8307 0.7845 0.8402 -0.1003 -0.0403 -0.0548 284 THR G CA  
13603 C C   . THR G  284 ? 0.8763 0.8277 0.8880 -0.0908 -0.0357 -0.0523 284 THR G C   
13604 O O   . THR G  284 ? 0.7857 0.7407 0.8029 -0.0852 -0.0384 -0.0475 284 THR G O   
13605 C CB  . THR G  284 ? 0.7954 0.7556 0.7996 -0.1039 -0.0486 -0.0528 284 THR G CB  
13606 O OG1 . THR G  284 ? 0.8877 0.8536 0.8987 -0.0995 -0.0539 -0.0469 284 THR G OG1 
13607 N N   . CYS G  285 ? 0.7059 0.6514 0.7132 -0.0892 -0.0287 -0.0556 285 CYS G N   
13608 C CA  . CYS G  285 ? 0.7222 0.6652 0.7308 -0.0805 -0.0239 -0.0536 285 CYS G CA  
13609 C C   . CYS G  285 ? 0.6954 0.6310 0.7043 -0.0790 -0.0146 -0.0572 285 CYS G C   
13610 O O   . CYS G  285 ? 0.7174 0.6490 0.7200 -0.0840 -0.0115 -0.0619 285 CYS G O   
13611 C CB  . CYS G  285 ? 0.6561 0.6014 0.6573 -0.0793 -0.0264 -0.0528 285 CYS G CB  
13612 S SG  . CYS G  285 ? 0.9217 0.8647 0.9237 -0.0692 -0.0209 -0.0504 285 CYS G SG  
13613 N N   . GLN G  286 ? 0.6930 0.6265 0.7091 -0.0721 -0.0100 -0.0548 286 GLN G N   
13614 C CA  . GLN G  286 ? 0.6992 0.6256 0.7169 -0.0701 -0.0009 -0.0576 286 GLN G CA  
13615 C C   . GLN G  286 ? 0.7152 0.6397 0.7339 -0.0614 0.0041  -0.0551 286 GLN G C   
13616 O O   . GLN G  286 ? 0.8011 0.7290 0.8242 -0.0552 0.0021  -0.0505 286 GLN G O   
13617 C CB  . GLN G  286 ? 0.6338 0.5584 0.6598 -0.0705 0.0012  -0.0575 286 GLN G CB  
13618 C CG  . GLN G  286 ? 0.6950 0.6120 0.7228 -0.0695 0.0106  -0.0608 286 GLN G CG  
13619 C CD  . GLN G  286 ? 0.8402 0.7529 0.8608 -0.0769 0.0134  -0.0668 286 GLN G CD  
13620 O OE1 . GLN G  286 ? 0.8131 0.7271 0.8315 -0.0848 0.0098  -0.0696 286 GLN G OE1 
13621 N NE2 . GLN G  286 ? 0.5660 0.4739 0.5828 -0.0744 0.0199  -0.0686 286 GLN G NE2 
13622 N N   . THR G  287 ? 0.5939 0.5131 0.6084 -0.0611 0.0106  -0.0582 287 THR G N   
13623 C CA  . THR G  287 ? 0.6623 0.5794 0.6781 -0.0531 0.0161  -0.0561 287 THR G CA  
13624 C C   . THR G  287 ? 0.6648 0.5749 0.6843 -0.0516 0.0252  -0.0583 287 THR G C   
13625 O O   . THR G  287 ? 0.7963 0.7024 0.8152 -0.0576 0.0277  -0.0625 287 THR G O   
13626 C CB  . THR G  287 ? 0.7583 0.6758 0.7661 -0.0530 0.0160  -0.0571 287 THR G CB  
13627 O OG1 . THR G  287 ? 0.5542 0.4654 0.5583 -0.0560 0.0227  -0.0618 287 THR G OG1 
13628 C CG2 . THR G  287 ? 0.6479 0.5706 0.6497 -0.0584 0.0075  -0.0573 287 THR G CG2 
13629 N N   . PRO G  288 ? 0.6531 0.5616 0.6765 -0.0437 0.0304  -0.0553 288 PRO G N   
13630 C CA  . PRO G  288 ? 0.6851 0.5869 0.7125 -0.0414 0.0396  -0.0568 288 PRO G CA  
13631 C C   . PRO G  288 ? 0.7960 0.6922 0.8178 -0.0460 0.0449  -0.0621 288 PRO G C   
13632 O O   . PRO G  288 ? 0.7776 0.6676 0.8020 -0.0473 0.0518  -0.0649 288 PRO G O   
13633 C CB  . PRO G  288 ? 0.8292 0.7320 0.8597 -0.0320 0.0427  -0.0521 288 PRO G CB  
13634 C CG  . PRO G  288 ? 0.7333 0.6431 0.7646 -0.0295 0.0349  -0.0478 288 PRO G CG  
13635 C CD  . PRO G  288 ? 0.7123 0.6256 0.7373 -0.0364 0.0277  -0.0501 288 PRO G CD  
13636 N N   . LYS G  289 ? 0.8636 0.7616 0.8776 -0.0484 0.0420  -0.0635 289 LYS G N   
13637 C CA  . LYS G  289 ? 0.8387 0.7315 0.8469 -0.0527 0.0470  -0.0684 289 LYS G CA  
13638 C C   . LYS G  289 ? 0.7929 0.6845 0.7965 -0.0627 0.0444  -0.0736 289 LYS G C   
13639 O O   . LYS G  289 ? 0.7812 0.6668 0.7819 -0.0672 0.0501  -0.0785 289 LYS G O   
13640 C CB  . LYS G  289 ? 0.8304 0.7256 0.8325 -0.0505 0.0457  -0.0676 289 LYS G CB  
13641 C CG  . LYS G  289 ? 1.0087 0.9055 1.0149 -0.0409 0.0483  -0.0626 289 LYS G CG  
13642 C CD  . LYS G  289 ? 0.9993 0.8999 0.9996 -0.0391 0.0452  -0.0613 289 LYS G CD  
13643 C CE  . LYS G  289 ? 1.1143 1.0101 1.1092 -0.0417 0.0508  -0.0654 289 LYS G CE  
13644 N NZ  . LYS G  289 ? 1.1807 1.0801 1.1708 -0.0389 0.0485  -0.0637 289 LYS G NZ  
13645 N N   . GLY G  290 ? 0.7359 0.6332 0.7389 -0.0662 0.0358  -0.0724 290 GLY G N   
13646 C CA  . GLY G  290 ? 0.7525 0.6500 0.7510 -0.0758 0.0321  -0.0766 290 GLY G CA  
13647 C C   . GLY G  290 ? 0.8388 0.7442 0.8359 -0.0782 0.0217  -0.0739 290 GLY G C   
13648 O O   . GLY G  290 ? 0.9711 0.8813 0.9697 -0.0725 0.0177  -0.0692 290 GLY G O   
13649 N N   . ALA G  291 ? 0.7845 0.6913 0.7788 -0.0866 0.0174  -0.0769 291 ALA G N   
13650 C CA  . ALA G  291 ? 0.7105 0.6247 0.7038 -0.0895 0.0075  -0.0743 291 ALA G CA  
13651 C C   . ALA G  291 ? 0.8882 0.8054 0.8724 -0.0922 0.0030  -0.0748 291 ALA G C   
13652 O O   . ALA G  291 ? 0.8111 0.7241 0.7886 -0.0945 0.0072  -0.0786 291 ALA G O   
13653 C CB  . ALA G  291 ? 0.6269 0.5420 0.6216 -0.0973 0.0045  -0.0767 291 ALA G CB  
13654 N N   . ILE G  292 ? 0.8836 0.8079 0.8676 -0.0919 -0.0054 -0.0709 292 ILE G N   
13655 C CA  . ILE G  292 ? 0.8281 0.7557 0.8038 -0.0946 -0.0104 -0.0709 292 ILE G CA  
13656 C C   . ILE G  292 ? 0.9633 0.8961 0.9363 -0.1023 -0.0187 -0.0711 292 ILE G C   
13657 O O   . ILE G  292 ? 1.0618 1.0001 1.0403 -0.1011 -0.0246 -0.0670 292 ILE G O   
13658 C CB  . ILE G  292 ? 0.7480 0.6797 0.7252 -0.0868 -0.0130 -0.0658 292 ILE G CB  
13659 C CG1 . ILE G  292 ? 0.6738 0.6010 0.6530 -0.0793 -0.0051 -0.0655 292 ILE G CG1 
13660 C CG2 . ILE G  292 ? 0.9042 0.8396 0.8730 -0.0898 -0.0186 -0.0657 292 ILE G CG2 
13661 C CD1 . ILE G  292 ? 0.8161 0.7471 0.7962 -0.0718 -0.0072 -0.0608 292 ILE G CD1 
13662 N N   . ASN G  293 ? 1.1799 1.1111 1.1446 -0.1103 -0.0190 -0.0757 293 ASN G N   
13663 C CA  . ASN G  293 ? 1.4331 1.3697 1.3935 -0.1180 -0.0272 -0.0758 293 ASN G CA  
13664 C C   . ASN G  293 ? 1.4219 1.3616 1.3745 -0.1180 -0.0313 -0.0746 293 ASN G C   
13665 O O   . ASN G  293 ? 1.4347 1.3713 1.3786 -0.1222 -0.0290 -0.0786 293 ASN G O   
13666 C CB  . ASN G  293 ? 1.5966 1.5299 1.5522 -0.1275 -0.0253 -0.0817 293 ASN G CB  
13667 C CG  . ASN G  293 ? 1.6580 1.5965 1.6063 -0.1360 -0.0332 -0.0824 293 ASN G CG  
13668 O OD1 . ASN G  293 ? 1.6214 1.5659 1.5686 -0.1348 -0.0401 -0.0783 293 ASN G OD1 
13669 N ND2 . ASN G  293 ? 1.5575 1.4935 1.5008 -0.1449 -0.0320 -0.0876 293 ASN G ND2 
13670 N N   . THR G  294 ? 1.2437 1.1893 1.1996 -0.1133 -0.0370 -0.0691 294 THR G N   
13671 C CA  . THR G  294 ? 1.3710 1.3195 1.3199 -0.1131 -0.0409 -0.0677 294 THR G CA  
13672 C C   . THR G  294 ? 1.2466 1.2030 1.1969 -0.1138 -0.0502 -0.0628 294 THR G C   
13673 O O   . THR G  294 ? 1.1112 1.0713 1.0687 -0.1138 -0.0540 -0.0600 294 THR G O   
13674 C CB  . THR G  294 ? 1.2280 1.1739 1.1768 -0.1050 -0.0359 -0.0666 294 THR G CB  
13675 O OG1 . THR G  294 ? 0.9672 0.9101 0.9064 -0.1081 -0.0335 -0.0703 294 THR G OG1 
13676 N N   . SER G  295 ? 1.1106 1.0694 1.0542 -0.1143 -0.0536 -0.0619 295 SER G N   
13677 C CA  . SER G  295 ? 1.0712 1.0372 1.0144 -0.1158 -0.0623 -0.0577 295 SER G CA  
13678 C C   . SER G  295 ? 0.9477 0.9151 0.8903 -0.1089 -0.0626 -0.0545 295 SER G C   
13679 O O   . SER G  295 ? 0.9582 0.9311 0.9021 -0.1076 -0.0688 -0.0501 295 SER G O   
13680 C CB  . SER G  295 ? 1.0707 1.0380 1.0043 -0.1249 -0.0662 -0.0605 295 SER G CB  
13681 O OG  . SER G  295 ? 1.2752 1.2366 1.2040 -0.1301 -0.0605 -0.0666 295 SER G OG  
13682 N N   . LEU G  296 ? 0.8296 0.7918 0.7703 -0.1047 -0.0556 -0.0568 296 LEU G N   
13683 C CA  . LEU G  296 ? 0.7339 0.6968 0.6731 -0.0985 -0.0549 -0.0546 296 LEU G CA  
13684 C C   . LEU G  296 ? 0.8172 0.7824 0.7659 -0.0903 -0.0550 -0.0498 296 LEU G C   
13685 O O   . LEU G  296 ? 0.8141 0.7785 0.7702 -0.0887 -0.0534 -0.0491 296 LEU G O   
13686 C CB  . LEU G  296 ? 0.7576 0.7144 0.6918 -0.0971 -0.0472 -0.0587 296 LEU G CB  
13687 C CG  . LEU G  296 ? 0.7893 0.7426 0.7144 -0.1053 -0.0457 -0.0641 296 LEU G CG  
13688 C CD1 . LEU G  296 ? 0.7946 0.7423 0.7149 -0.1034 -0.0384 -0.0676 296 LEU G CD1 
13689 C CD2 . LEU G  296 ? 0.7439 0.7020 0.6623 -0.1112 -0.0532 -0.0633 296 LEU G CD2 
13690 N N   . PRO G  297 ? 0.6849 0.6529 0.6330 -0.0855 -0.0569 -0.0466 297 PRO G N   
13691 C CA  . PRO G  297 ? 0.6783 0.6489 0.6343 -0.0781 -0.0576 -0.0420 297 PRO G CA  
13692 C C   . PRO G  297 ? 0.7862 0.7529 0.7460 -0.0712 -0.0502 -0.0424 297 PRO G C   
13693 O O   . PRO G  297 ? 0.7852 0.7531 0.7526 -0.0657 -0.0497 -0.0392 297 PRO G O   
13694 C CB  . PRO G  297 ? 0.7109 0.6856 0.6631 -0.0766 -0.0619 -0.0393 297 PRO G CB  
13695 C CG  . PRO G  297 ? 0.8491 0.8241 0.7923 -0.0840 -0.0650 -0.0419 297 PRO G CG  
13696 C CD  . PRO G  297 ? 0.6891 0.6585 0.6287 -0.0877 -0.0595 -0.0472 297 PRO G CD  
13697 N N   . PHE G  298 ? 0.6732 0.6352 0.6279 -0.0714 -0.0445 -0.0461 298 PHE G N   
13698 C CA  . PHE G  298 ? 0.7441 0.7029 0.7021 -0.0646 -0.0377 -0.0460 298 PHE G CA  
13699 C C   . PHE G  298 ? 0.7665 0.7189 0.7234 -0.0663 -0.0305 -0.0504 298 PHE G C   
13700 O O   . PHE G  298 ? 0.8143 0.7642 0.7649 -0.0726 -0.0299 -0.0545 298 PHE G O   
13701 C CB  . PHE G  298 ? 0.6286 0.5887 0.5825 -0.0606 -0.0372 -0.0450 298 PHE G CB  
13702 C CG  . PHE G  298 ? 0.6952 0.6610 0.6482 -0.0602 -0.0442 -0.0414 298 PHE G CG  
13703 C CD1 . PHE G  298 ? 0.5995 0.5689 0.5592 -0.0551 -0.0465 -0.0370 298 PHE G CD1 
13704 C CD2 . PHE G  298 ? 0.6238 0.5914 0.5692 -0.0651 -0.0482 -0.0425 298 PHE G CD2 
13705 C CE1 . PHE G  298 ? 0.7216 0.6960 0.6809 -0.0548 -0.0525 -0.0339 298 PHE G CE1 
13706 C CE2 . PHE G  298 ? 0.6731 0.6457 0.6180 -0.0647 -0.0543 -0.0392 298 PHE G CE2 
13707 C CZ  . PHE G  298 ? 0.6692 0.6452 0.6212 -0.0596 -0.0564 -0.0349 298 PHE G CZ  
13708 N N   . GLN G  299 ? 0.6532 0.6029 0.6162 -0.0607 -0.0250 -0.0496 299 GLN G N   
13709 C CA  . GLN G  299 ? 0.5489 0.4924 0.5122 -0.0612 -0.0174 -0.0533 299 GLN G CA  
13710 C C   . GLN G  299 ? 0.6613 0.6029 0.6277 -0.0533 -0.0113 -0.0517 299 GLN G C   
13711 O O   . GLN G  299 ? 0.9971 0.9419 0.9685 -0.0472 -0.0125 -0.0476 299 GLN G O   
13712 C CB  . GLN G  299 ? 0.6742 0.6157 0.6429 -0.0638 -0.0165 -0.0542 299 GLN G CB  
13713 C CG  . GLN G  299 ? 0.6659 0.6101 0.6436 -0.0584 -0.0179 -0.0498 299 GLN G CG  
13714 C CD  . GLN G  299 ? 0.6682 0.6089 0.6513 -0.0515 -0.0107 -0.0488 299 GLN G CD  
13715 O OE1 . GLN G  299 ? 0.7112 0.6472 0.6922 -0.0509 -0.0042 -0.0516 299 GLN G OE1 
13716 N NE2 . GLN G  299 ? 0.6480 0.5911 0.6382 -0.0461 -0.0116 -0.0448 299 GLN G NE2 
13717 N N   . ASN G  300 ? 0.6750 0.6115 0.6386 -0.0534 -0.0046 -0.0550 300 ASN G N   
13718 C CA  . ASN G  300 ? 0.7408 0.6756 0.7074 -0.0461 0.0015  -0.0534 300 ASN G CA  
13719 C C   . ASN G  300 ? 0.6969 0.6257 0.6679 -0.0452 0.0093  -0.0554 300 ASN G C   
13720 O O   . ASN G  300 ? 0.7366 0.6625 0.7088 -0.0408 0.0157  -0.0554 300 ASN G O   
13721 C CB  . ASN G  300 ? 0.6282 0.5628 0.5884 -0.0456 0.0031  -0.0547 300 ASN G CB  
13722 C CG  . ASN G  300 ? 0.7237 0.6531 0.6779 -0.0518 0.0069  -0.0600 300 ASN G CG  
13723 O OD1 . ASN G  300 ? 0.8142 0.7407 0.7680 -0.0574 0.0072  -0.0630 300 ASN G OD1 
13724 N ND2 . ASN G  300 ? 0.6820 0.6101 0.6315 -0.0509 0.0099  -0.0614 300 ASN G ND2 
13725 N N   . ILE G  301 ? 0.6943 0.6213 0.6678 -0.0494 0.0087  -0.0570 301 ILE G N   
13726 C CA  . ILE G  301 ? 0.7095 0.6306 0.6872 -0.0495 0.0159  -0.0593 301 ILE G CA  
13727 C C   . ILE G  301 ? 0.6928 0.6139 0.6790 -0.0417 0.0192  -0.0553 301 ILE G C   
13728 O O   . ILE G  301 ? 0.8042 0.7214 0.7928 -0.0374 0.0264  -0.0553 301 ILE G O   
13729 C CB  . ILE G  301 ? 0.7926 0.7120 0.7702 -0.0570 0.0140  -0.0624 301 ILE G CB  
13730 C CG1 . ILE G  301 ? 0.6448 0.5633 0.6134 -0.0651 0.0118  -0.0669 301 ILE G CG1 
13731 C CG2 . ILE G  301 ? 0.7409 0.6541 0.7236 -0.0564 0.0215  -0.0644 301 ILE G CG2 
13732 C CD1 . ILE G  301 ? 0.7505 0.6683 0.7182 -0.0731 0.0090  -0.0699 301 ILE G CD1 
13733 N N   . HIS G  302 ? 0.6639 0.5893 0.6546 -0.0400 0.0140  -0.0518 302 HIS G N   
13734 C CA  . HIS G  302 ? 0.6967 0.6223 0.6954 -0.0331 0.0168  -0.0481 302 HIS G CA  
13735 C C   . HIS G  302 ? 0.6856 0.6174 0.6874 -0.0304 0.0101  -0.0436 302 HIS G C   
13736 O O   . HIS G  302 ? 0.6133 0.5481 0.6139 -0.0350 0.0038  -0.0438 302 HIS G O   
13737 C CB  . HIS G  302 ? 0.6276 0.5484 0.6314 -0.0351 0.0212  -0.0501 302 HIS G CB  
13738 C CG  . HIS G  302 ? 0.7374 0.6561 0.7484 -0.0281 0.0269  -0.0472 302 HIS G CG  
13739 N ND1 . HIS G  302 ? 0.7310 0.6530 0.7481 -0.0236 0.0245  -0.0429 302 HIS G ND1 
13740 C CD2 . HIS G  302 ? 0.8111 0.7248 0.8244 -0.0247 0.0352  -0.0478 302 HIS G CD2 
13741 C CE1 . HIS G  302 ? 0.7528 0.6720 0.7752 -0.0179 0.0308  -0.0411 302 HIS G CE1 
13742 N NE2 . HIS G  302 ? 0.7290 0.6432 0.7493 -0.0183 0.0373  -0.0438 302 HIS G NE2 
13743 N N   . PRO G  303 ? 0.6693 0.6030 0.6750 -0.0229 0.0117  -0.0396 303 PRO G N   
13744 C CA  . PRO G  303 ? 0.5356 0.4748 0.5446 -0.0196 0.0063  -0.0353 303 PRO G CA  
13745 C C   . PRO G  303 ? 0.6574 0.5965 0.6728 -0.0206 0.0049  -0.0342 303 PRO G C   
13746 O O   . PRO G  303 ? 0.6401 0.5833 0.6565 -0.0225 -0.0014 -0.0327 303 PRO G O   
13747 C CB  . PRO G  303 ? 0.5999 0.5398 0.6114 -0.0115 0.0104  -0.0319 303 PRO G CB  
13748 C CG  . PRO G  303 ? 0.8772 0.8134 0.8851 -0.0111 0.0162  -0.0343 303 PRO G CG  
13749 C CD  . PRO G  303 ? 0.7398 0.6708 0.7468 -0.0173 0.0188  -0.0388 303 PRO G CD  
13750 N N   . ILE G  304 ? 0.5816 0.5162 0.6019 -0.0192 0.0108  -0.0350 304 ILE G N   
13751 C CA  . ILE G  304 ? 0.6511 0.5851 0.6779 -0.0202 0.0102  -0.0342 304 ILE G CA  
13752 C C   . ILE G  304 ? 0.6540 0.5868 0.6789 -0.0285 0.0073  -0.0380 304 ILE G C   
13753 O O   . ILE G  304 ? 0.6997 0.6282 0.7212 -0.0325 0.0110  -0.0421 304 ILE G O   
13754 C CB  . ILE G  304 ? 0.5847 0.5140 0.6173 -0.0159 0.0177  -0.0337 304 ILE G CB  
13755 C CG1 . ILE G  304 ? 0.5780 0.5096 0.6140 -0.0077 0.0192  -0.0289 304 ILE G CG1 
13756 C CG2 . ILE G  304 ? 0.6866 0.6141 0.7251 -0.0188 0.0177  -0.0344 304 ILE G CG2 
13757 C CD1 . ILE G  304 ? 0.7168 0.6502 0.7479 -0.0042 0.0201  -0.0280 304 ILE G CD1 
13758 N N   . THR G  305 ? 0.5833 0.5201 0.6105 -0.0311 0.0010  -0.0366 305 THR G N   
13759 C CA  . THR G  305 ? 0.5784 0.5156 0.6033 -0.0392 -0.0030 -0.0396 305 THR G CA  
13760 C C   . THR G  305 ? 0.7158 0.6555 0.7476 -0.0406 -0.0068 -0.0377 305 THR G C   
13761 O O   . THR G  305 ? 0.7746 0.7170 0.8116 -0.0355 -0.0083 -0.0336 305 THR G O   
13762 C CB  . THR G  305 ? 0.7024 0.6435 0.7198 -0.0428 -0.0091 -0.0401 305 THR G CB  
13763 O OG1 . THR G  305 ? 0.7018 0.6404 0.7134 -0.0501 -0.0088 -0.0449 305 THR G OG1 
13764 C CG2 . THR G  305 ? 0.5771 0.5242 0.5969 -0.0439 -0.0169 -0.0369 305 THR G CG2 
13765 N N   . ILE G  306 ? 0.6133 0.5520 0.6453 -0.0474 -0.0083 -0.0407 306 ILE G N   
13766 C CA  . ILE G  306 ? 0.7172 0.6585 0.7559 -0.0495 -0.0121 -0.0390 306 ILE G CA  
13767 C C   . ILE G  306 ? 0.7173 0.6623 0.7526 -0.0576 -0.0189 -0.0406 306 ILE G C   
13768 O O   . ILE G  306 ? 0.6570 0.5997 0.6863 -0.0634 -0.0182 -0.0448 306 ILE G O   
13769 C CB  . ILE G  306 ? 0.5505 0.4872 0.5955 -0.0494 -0.0063 -0.0405 306 ILE G CB  
13770 C CG1 . ILE G  306 ? 0.6351 0.5682 0.6834 -0.0414 0.0006  -0.0387 306 ILE G CG1 
13771 C CG2 . ILE G  306 ? 0.5096 0.4493 0.5620 -0.0512 -0.0104 -0.0385 306 ILE G CG2 
13772 C CD1 . ILE G  306 ? 0.6684 0.5969 0.7236 -0.0406 0.0063  -0.0395 306 ILE G CD1 
13773 N N   . GLY G  307 ? 0.6200 0.5705 0.6593 -0.0579 -0.0254 -0.0372 307 GLY G N   
13774 C CA  . GLY G  307 ? 0.6483 0.6031 0.6852 -0.0652 -0.0325 -0.0378 307 GLY G CA  
13775 C C   . GLY G  307 ? 0.7278 0.6877 0.7603 -0.0646 -0.0386 -0.0351 307 GLY G C   
13776 O O   . GLY G  307 ? 0.8474 0.8087 0.8815 -0.0583 -0.0385 -0.0318 307 GLY G O   
13777 N N   . LYS G  308 ? 0.6909 0.6537 0.7179 -0.0715 -0.0438 -0.0366 308 LYS G N   
13778 C CA  . LYS G  308 ? 0.6653 0.6325 0.6872 -0.0717 -0.0493 -0.0345 308 LYS G CA  
13779 C C   . LYS G  308 ? 0.6750 0.6391 0.6870 -0.0733 -0.0467 -0.0382 308 LYS G C   
13780 O O   . LYS G  308 ? 0.7620 0.7254 0.7679 -0.0802 -0.0478 -0.0417 308 LYS G O   
13781 C CB  . LYS G  308 ? 0.7509 0.7237 0.7732 -0.0780 -0.0573 -0.0332 308 LYS G CB  
13782 C CG  . LYS G  308 ? 1.0418 1.0194 1.0594 -0.0782 -0.0631 -0.0306 308 LYS G CG  
13783 C CD  . LYS G  308 ? 1.1478 1.1311 1.1659 -0.0847 -0.0709 -0.0290 308 LYS G CD  
13784 C CE  . LYS G  308 ? 1.1611 1.1481 1.1901 -0.0827 -0.0738 -0.0248 308 LYS G CE  
13785 N NZ  . LYS G  308 ? 1.2870 1.2809 1.3171 -0.0858 -0.0820 -0.0210 308 LYS G NZ  
13786 N N   . CYS G  309 ? 0.7763 0.7386 0.7866 -0.0669 -0.0430 -0.0373 309 CYS G N   
13787 C CA  . CYS G  309 ? 0.7524 0.7109 0.7546 -0.0674 -0.0389 -0.0407 309 CYS G CA  
13788 C C   . CYS G  309 ? 0.6709 0.6324 0.6673 -0.0656 -0.0419 -0.0392 309 CYS G C   
13789 O O   . CYS G  309 ? 0.7072 0.6729 0.7067 -0.0618 -0.0457 -0.0350 309 CYS G O   
13790 C CB  . CYS G  309 ? 0.6265 0.5796 0.6315 -0.0617 -0.0306 -0.0417 309 CYS G CB  
13791 S SG  . CYS G  309 ? 1.1057 1.0548 1.1182 -0.0630 -0.0260 -0.0434 309 CYS G SG  
13792 N N   . PRO G  310 ? 0.6710 0.6300 0.6589 -0.0684 -0.0401 -0.0426 310 PRO G N   
13793 C CA  . PRO G  310 ? 0.6800 0.6410 0.6621 -0.0663 -0.0417 -0.0416 310 PRO G CA  
13794 C C   . PRO G  310 ? 0.7013 0.6616 0.6870 -0.0577 -0.0376 -0.0391 310 PRO G C   
13795 O O   . PRO G  310 ? 0.6476 0.6046 0.6384 -0.0540 -0.0323 -0.0392 310 PRO G O   
13796 C CB  . PRO G  310 ? 0.6062 0.5631 0.5798 -0.0708 -0.0383 -0.0466 310 PRO G CB  
13797 C CG  . PRO G  310 ? 0.6129 0.5675 0.5868 -0.0775 -0.0378 -0.0499 310 PRO G CG  
13798 C CD  . PRO G  310 ? 0.5575 0.5117 0.5410 -0.0740 -0.0361 -0.0479 310 PRO G CD  
13799 N N   . LYS G  311 ? 0.6019 0.5652 0.5846 -0.0547 -0.0399 -0.0370 311 LYS G N   
13800 C CA  . LYS G  311 ? 0.6039 0.5674 0.5896 -0.0468 -0.0366 -0.0344 311 LYS G CA  
13801 C C   . LYS G  311 ? 0.6473 0.6059 0.6298 -0.0446 -0.0295 -0.0372 311 LYS G C   
13802 O O   . LYS G  311 ? 0.6610 0.6175 0.6367 -0.0487 -0.0284 -0.0406 311 LYS G O   
13803 C CB  . LYS G  311 ? 0.5461 0.5143 0.5293 -0.0447 -0.0413 -0.0315 311 LYS G CB  
13804 C CG  . LYS G  311 ? 0.6460 0.6186 0.6291 -0.0491 -0.0489 -0.0297 311 LYS G CG  
13805 C CD  . LYS G  311 ? 0.5648 0.5388 0.5560 -0.0494 -0.0510 -0.0276 311 LYS G CD  
13806 C CE  . LYS G  311 ? 0.5344 0.5100 0.5326 -0.0424 -0.0500 -0.0237 311 LYS G CE  
13807 N NZ  . LYS G  311 ? 0.5406 0.5158 0.5471 -0.0418 -0.0496 -0.0223 311 LYS G NZ  
13808 N N   . TYR G  312 ? 0.6133 0.5703 0.6009 -0.0383 -0.0244 -0.0357 312 TYR G N   
13809 C CA  . TYR G  312 ? 0.6543 0.6072 0.6396 -0.0355 -0.0176 -0.0376 312 TYR G CA  
13810 C C   . TYR G  312 ? 0.6811 0.6367 0.6621 -0.0322 -0.0183 -0.0363 312 TYR G C   
13811 O O   . TYR G  312 ? 0.8039 0.7635 0.7872 -0.0278 -0.0209 -0.0327 312 TYR G O   
13812 C CB  . TYR G  312 ? 0.5445 0.4947 0.5367 -0.0300 -0.0117 -0.0363 312 TYR G CB  
13813 C CG  . TYR G  312 ? 0.6852 0.6311 0.6756 -0.0276 -0.0044 -0.0383 312 TYR G CG  
13814 C CD1 . TYR G  312 ? 0.6593 0.6006 0.6456 -0.0326 -0.0011 -0.0428 312 TYR G CD1 
13815 C CD2 . TYR G  312 ? 0.6749 0.6215 0.6676 -0.0204 -0.0008 -0.0355 312 TYR G CD2 
13816 C CE1 . TYR G  312 ? 0.5951 0.5322 0.5801 -0.0304 0.0058  -0.0445 312 TYR G CE1 
13817 C CE2 . TYR G  312 ? 0.5315 0.4745 0.5230 -0.0181 0.0058  -0.0370 312 TYR G CE2 
13818 C CZ  . TYR G  312 ? 0.6776 0.6157 0.6655 -0.0230 0.0092  -0.0414 312 TYR G CZ  
13819 O OH  . TYR G  312 ? 0.7503 0.6846 0.7375 -0.0207 0.0162  -0.0428 312 TYR G OH  
13820 N N   . VAL G  313 ? 0.5965 0.5498 0.5712 -0.0344 -0.0158 -0.0394 313 VAL G N   
13821 C CA  . VAL G  313 ? 0.6588 0.6143 0.6289 -0.0319 -0.0162 -0.0387 313 VAL G CA  
13822 C C   . VAL G  313 ? 0.6886 0.6400 0.6573 -0.0294 -0.0089 -0.0406 313 VAL G C   
13823 O O   . VAL G  313 ? 0.7135 0.6599 0.6816 -0.0323 -0.0044 -0.0439 313 VAL G O   
13824 C CB  . VAL G  313 ? 0.6385 0.5960 0.6012 -0.0378 -0.0216 -0.0403 313 VAL G CB  
13825 C CG1 . VAL G  313 ? 0.8240 0.7831 0.7818 -0.0355 -0.0212 -0.0400 313 VAL G CG1 
13826 C CG2 . VAL G  313 ? 0.6435 0.6054 0.6081 -0.0398 -0.0289 -0.0377 313 VAL G CG2 
13827 N N   . LYS G  314 ? 0.6697 0.6234 0.6381 -0.0240 -0.0074 -0.0385 314 LYS G N   
13828 C CA  . LYS G  314 ? 0.6438 0.5944 0.6119 -0.0208 -0.0005 -0.0395 314 LYS G CA  
13829 C C   . LYS G  314 ? 0.7017 0.6506 0.6622 -0.0250 0.0002  -0.0431 314 LYS G C   
13830 O O   . LYS G  314 ? 0.8338 0.7803 0.7933 -0.0229 0.0057  -0.0442 314 LYS G O   
13831 C CB  . LYS G  314 ? 0.5215 0.4759 0.4927 -0.0133 0.0005  -0.0355 314 LYS G CB  
13832 C CG  . LYS G  314 ? 0.9335 0.8851 0.9075 -0.0085 0.0080  -0.0352 314 LYS G CG  
13833 C CD  . LYS G  314 ? 1.2862 1.2424 1.2633 -0.0015 0.0081  -0.0309 314 LYS G CD  
13834 C CE  . LYS G  314 ? 1.2417 1.2010 1.2232 0.0005  0.0042  -0.0277 314 LYS G CE  
13835 N NZ  . LYS G  314 ? 0.9925 0.9575 0.9745 0.0053  0.0017  -0.0241 314 LYS G NZ  
13836 N N   . SER G  315 ? 0.7553 0.7055 0.7106 -0.0310 -0.0054 -0.0447 315 SER G N   
13837 C CA  . SER G  315 ? 0.8068 0.7557 0.7544 -0.0355 -0.0054 -0.0480 315 SER G CA  
13838 C C   . SER G  315 ? 0.8049 0.7473 0.7505 -0.0393 0.0006  -0.0525 315 SER G C   
13839 O O   . SER G  315 ? 0.6593 0.5985 0.6083 -0.0409 0.0028  -0.0537 315 SER G O   
13840 C CB  . SER G  315 ? 0.6832 0.6351 0.6259 -0.0413 -0.0130 -0.0484 315 SER G CB  
13841 O OG  . SER G  315 ? 0.9887 0.9462 0.9324 -0.0380 -0.0181 -0.0445 315 SER G OG  
13842 N N   . THR G  316 ? 0.8788 0.8192 0.8188 -0.0406 0.0036  -0.0550 316 THR G N   
13843 C CA  . THR G  316 ? 0.9077 0.8418 0.8448 -0.0449 0.0094  -0.0597 316 THR G CA  
13844 C C   . THR G  316 ? 0.8409 0.7741 0.7702 -0.0535 0.0053  -0.0633 316 THR G C   
13845 O O   . THR G  316 ? 0.8462 0.7747 0.7736 -0.0589 0.0079  -0.0672 316 THR G O   
13846 C CB  . THR G  316 ? 0.8395 0.7715 0.7751 -0.0417 0.0156  -0.0606 316 THR G CB  
13847 O OG1 . THR G  316 ? 1.1128 1.0387 1.0435 -0.0473 0.0202  -0.0657 316 THR G OG1 
13848 C CG2 . THR G  316 ? 0.9366 0.8735 0.8681 -0.0402 0.0115  -0.0588 316 THR G CG2 
13849 N N   . LYS G  317 ? 0.9205 0.8584 0.8453 -0.0549 -0.0010 -0.0620 317 LYS G N   
13850 C CA  . LYS G  317 ? 0.9267 0.8648 0.8440 -0.0629 -0.0058 -0.0647 317 LYS G CA  
13851 C C   . LYS G  317 ? 0.8573 0.8019 0.7734 -0.0629 -0.0142 -0.0612 317 LYS G C   
13852 O O   . LYS G  317 ? 0.9635 0.9118 0.8812 -0.0576 -0.0156 -0.0580 317 LYS G O   
13853 C CB  . LYS G  317 ? 0.9314 0.8660 0.8410 -0.0662 -0.0021 -0.0686 317 LYS G CB  
13854 C CG  . LYS G  317 ? 1.1240 1.0608 1.0328 -0.0610 -0.0009 -0.0667 317 LYS G CG  
13855 C CD  . LYS G  317 ? 1.3217 1.2553 1.2228 -0.0649 0.0023  -0.0707 317 LYS G CD  
13856 C CE  . LYS G  317 ? 1.2587 1.1938 1.1514 -0.0723 -0.0040 -0.0724 317 LYS G CE  
13857 N NZ  . LYS G  317 ? 1.0229 0.9548 0.9077 -0.0762 -0.0008 -0.0762 317 LYS G NZ  
13858 N N   . LEU G  318 ? 0.8031 0.7491 0.7164 -0.0691 -0.0198 -0.0619 318 LEU G N   
13859 C CA  . LEU G  318 ? 0.8137 0.7656 0.7257 -0.0700 -0.0278 -0.0587 318 LEU G CA  
13860 C C   . LEU G  318 ? 0.8021 0.7539 0.7055 -0.0783 -0.0318 -0.0614 318 LEU G C   
13861 O O   . LEU G  318 ? 0.7676 0.7220 0.6709 -0.0825 -0.0375 -0.0604 318 LEU G O   
13862 C CB  . LEU G  318 ? 0.5977 0.5527 0.5171 -0.0683 -0.0318 -0.0553 318 LEU G CB  
13863 C CG  . LEU G  318 ? 0.6813 0.6377 0.6089 -0.0600 -0.0296 -0.0516 318 LEU G CG  
13864 C CD1 . LEU G  318 ? 0.6664 0.6248 0.6011 -0.0594 -0.0327 -0.0490 318 LEU G CD1 
13865 C CD2 . LEU G  318 ? 0.7035 0.6642 0.6303 -0.0554 -0.0320 -0.0485 318 LEU G CD2 
13866 N N   . ARG G  319 ? 0.8266 0.7755 0.7229 -0.0807 -0.0286 -0.0647 319 ARG G N   
13867 C CA  . ARG G  319 ? 0.8308 0.7790 0.7181 -0.0888 -0.0315 -0.0677 319 ARG G CA  
13868 C C   . ARG G  319 ? 0.7659 0.7198 0.6499 -0.0900 -0.0392 -0.0646 319 ARG G C   
13869 O O   . ARG G  319 ? 0.7676 0.7236 0.6508 -0.0859 -0.0395 -0.0628 319 ARG G O   
13870 C CB  . ARG G  319 ? 0.9635 0.9065 0.8444 -0.0910 -0.0252 -0.0723 319 ARG G CB  
13871 C CG  . ARG G  319 ? 0.9553 0.8967 0.8264 -0.0999 -0.0273 -0.0760 319 ARG G CG  
13872 C CD  . ARG G  319 ? 1.0015 0.9358 0.8683 -0.1034 -0.0196 -0.0816 319 ARG G CD  
13873 N NE  . ARG G  319 ? 1.1042 1.0349 0.9753 -0.1050 -0.0162 -0.0836 319 ARG G NE  
13874 C CZ  . ARG G  319 ? 1.1448 1.0748 1.0129 -0.1125 -0.0186 -0.0861 319 ARG G CZ  
13875 N NH1 . ARG G  319 ? 1.1768 1.1095 1.0372 -0.1191 -0.0247 -0.0866 319 ARG G NH1 
13876 N NH2 . ARG G  319 ? 1.1881 1.1148 1.0606 -0.1135 -0.0151 -0.0879 319 ARG G NH2 
13877 N N   . LEU G  320 ? 0.7821 0.7386 0.6644 -0.0957 -0.0452 -0.0641 320 LEU G N   
13878 C CA  . LEU G  320 ? 0.6615 0.6236 0.5415 -0.0971 -0.0529 -0.0607 320 LEU G CA  
13879 C C   . LEU G  320 ? 0.7797 0.7410 0.6491 -0.1046 -0.0550 -0.0635 320 LEU G C   
13880 O O   . LEU G  320 ? 0.9907 0.9499 0.8559 -0.1115 -0.0552 -0.0667 320 LEU G O   
13881 C CB  . LEU G  320 ? 0.6955 0.6615 0.5815 -0.0981 -0.0586 -0.0574 320 LEU G CB  
13882 C CG  . LEU G  320 ? 0.8013 0.7737 0.6886 -0.0977 -0.0664 -0.0525 320 LEU G CG  
13883 C CD1 . LEU G  320 ? 0.7029 0.6776 0.5954 -0.0895 -0.0659 -0.0489 320 LEU G CD1 
13884 C CD2 . LEU G  320 ? 0.7328 0.7083 0.6252 -0.1004 -0.0714 -0.0502 320 LEU G CD2 
13885 N N   . ALA G  321 ? 0.7854 0.7486 0.6503 -0.1035 -0.0566 -0.0624 321 ALA G N   
13886 C CA  . ALA G  321 ? 0.7371 0.6996 0.5916 -0.1100 -0.0583 -0.0649 321 ALA G CA  
13887 C C   . ALA G  321 ? 0.7947 0.7613 0.6462 -0.1163 -0.0661 -0.0631 321 ALA G C   
13888 O O   . ALA G  321 ? 0.8667 0.8386 0.7217 -0.1141 -0.0719 -0.0583 321 ALA G O   
13889 C CB  . ALA G  321 ? 0.6687 0.6323 0.5202 -0.1064 -0.0577 -0.0639 321 ALA G CB  
13890 N N   . THR G  322 ? 0.9427 0.9070 0.7874 -0.1243 -0.0663 -0.0667 322 THR G N   
13891 C CA  . THR G  322 ? 0.8607 0.8292 0.7019 -0.1309 -0.0737 -0.0651 322 THR G CA  
13892 C C   . THR G  322 ? 0.9137 0.8823 0.7439 -0.1364 -0.0758 -0.0666 322 THR G C   
13893 O O   . THR G  322 ? 0.8999 0.8734 0.7278 -0.1389 -0.0826 -0.0632 322 THR G O   
13894 C CB  . THR G  322 ? 0.9384 0.9054 0.7799 -0.1368 -0.0736 -0.0678 322 THR G CB  
13895 O OG1 . THR G  322 ? 0.9967 0.9573 0.8314 -0.1410 -0.0672 -0.0739 322 THR G OG1 
13896 C CG2 . THR G  322 ? 0.9933 0.9605 0.8460 -0.1315 -0.0720 -0.0659 322 THR G CG2 
13897 N N   . GLY G  323 ? 0.9726 0.9357 0.7961 -0.1383 -0.0696 -0.0716 323 GLY G N   
13898 C CA  . GLY G  323 ? 1.0227 0.9851 0.8355 -0.1433 -0.0705 -0.0735 323 GLY G CA  
13899 C C   . GLY G  323 ? 1.0109 0.9745 0.8237 -0.1375 -0.0700 -0.0712 323 GLY G C   
13900 O O   . GLY G  323 ? 0.9824 0.9491 0.8033 -0.1304 -0.0713 -0.0671 323 GLY G O   
13901 N N   . LEU G  324 ? 0.9862 0.9473 0.7899 -0.1406 -0.0680 -0.0740 324 LEU G N   
13902 C CA  . LEU G  324 ? 0.9378 0.8998 0.7408 -0.1357 -0.0672 -0.0724 324 LEU G CA  
13903 C C   . LEU G  324 ? 1.0325 0.9886 0.8325 -0.1341 -0.0587 -0.0770 324 LEU G C   
13904 O O   . LEU G  324 ? 1.2004 1.1514 0.9969 -0.1382 -0.0538 -0.0818 324 LEU G O   
13905 C CB  . LEU G  324 ? 1.0339 0.9994 0.8293 -0.1401 -0.0733 -0.0704 324 LEU G CB  
13906 C CG  . LEU G  324 ? 0.9464 0.9096 0.7300 -0.1494 -0.0738 -0.0742 324 LEU G CG  
13907 C CD1 . LEU G  324 ? 1.0175 0.9748 0.7946 -0.1500 -0.0666 -0.0791 324 LEU G CD1 
13908 C CD2 . LEU G  324 ? 0.8525 0.8208 0.6311 -0.1531 -0.0816 -0.0705 324 LEU G CD2 
13909 N N   . ARG G  325 ? 0.9480 0.9048 0.7496 -0.1282 -0.0569 -0.0755 325 ARG G N   
13910 C CA  . ARG G  325 ? 1.0256 0.9775 0.8257 -0.1257 -0.0490 -0.0791 325 ARG G CA  
13911 C C   . ARG G  325 ? 1.1340 1.0804 0.9244 -0.1333 -0.0451 -0.0848 325 ARG G C   
13912 O O   . ARG G  325 ? 1.1694 1.1166 0.9517 -0.1404 -0.0494 -0.0855 325 ARG G O   
13913 C CB  . ARG G  325 ? 0.9213 0.8756 0.7211 -0.1211 -0.0494 -0.0769 325 ARG G CB  
13914 C CG  . ARG G  325 ? 1.0424 0.9936 0.8455 -0.1153 -0.0417 -0.0787 325 ARG G CG  
13915 C CD  . ARG G  325 ? 1.2050 1.1587 1.0070 -0.1115 -0.0422 -0.0768 325 ARG G CD  
13916 N NE  . ARG G  325 ? 1.2493 1.2089 1.0582 -0.1059 -0.0471 -0.0715 325 ARG G NE  
13917 C CZ  . ARG G  325 ? 1.3158 1.2770 1.1330 -0.0982 -0.0446 -0.0694 325 ARG G CZ  
13918 N NH1 . ARG G  325 ? 1.1530 1.1107 0.9730 -0.0950 -0.0375 -0.0718 325 ARG G NH1 
13919 N NH2 . ARG G  325 ? 1.1903 1.1567 1.0130 -0.0939 -0.0492 -0.0648 325 ARG G NH2 
13920 N N   . ASN G  326 ? 1.4063 1.3471 1.1975 -0.1320 -0.0370 -0.0888 326 ASN G N   
13921 C CA  . ASN G  326 ? 1.5350 1.4698 1.3176 -0.1393 -0.0325 -0.0946 326 ASN G CA  
13922 C C   . ASN G  326 ? 1.6139 1.5452 1.3911 -0.1389 -0.0270 -0.0974 326 ASN G C   
13923 O O   . ASN G  326 ? 1.6877 1.6182 1.4706 -0.1321 -0.0222 -0.0968 326 ASN G O   
13924 C CB  . ASN G  326 ? 1.6995 1.6296 1.4861 -0.1399 -0.0268 -0.0978 326 ASN G CB  
13925 C CG  . ASN G  326 ? 1.7880 1.7124 1.5652 -0.1489 -0.0235 -0.1038 326 ASN G CG  
13926 O OD1 . ASN G  326 ? 1.7599 1.6857 1.5284 -0.1561 -0.0283 -0.1045 326 ASN G OD1 
13927 N ND2 . ASN G  326 ? 1.7795 1.6976 1.5585 -0.1488 -0.0153 -0.1079 326 ASN G ND2 
13928 N N   . ILE G  327 ? 1.4306 1.3599 1.1970 -0.1464 -0.0277 -0.1003 327 ILE G N   
13929 C CA  . ILE G  327 ? 1.3707 1.2960 1.1314 -0.1468 -0.0221 -0.1035 327 ILE G CA  
13930 C C   . ILE G  327 ? 1.3338 1.2526 1.0850 -0.1552 -0.0173 -0.1098 327 ILE G C   
13931 O O   . ILE G  327 ? 1.3168 1.2344 1.0649 -0.1614 -0.0190 -0.1117 327 ILE G O   
13932 C CB  . ILE G  327 ? 1.2076 1.1370 0.9636 -0.1467 -0.0270 -0.1008 327 ILE G CB  
13933 C CG1 . ILE G  327 ? 1.1279 1.0642 0.8922 -0.1397 -0.0329 -0.0945 327 ILE G CG1 
13934 C CG2 . ILE G  327 ? 1.1688 1.0949 0.9227 -0.1443 -0.0205 -0.1031 327 ILE G CG2 
13935 C CD1 . ILE G  327 ? 1.0468 0.9835 0.8198 -0.1307 -0.0283 -0.0930 327 ILE G CD1 
13936 N N   . GLY H  1   ? 0.8010 0.7831 0.6171 -0.0984 -0.0730 -0.0521 1   GLY H N   
13937 C CA  . GLY H  1   ? 1.2420 1.2246 1.0555 -0.0960 -0.0713 -0.0523 1   GLY H CA  
13938 C C   . GLY H  1   ? 0.9444 0.9318 0.7617 -0.0926 -0.0758 -0.0477 1   GLY H C   
13939 O O   . GLY H  1   ? 1.0606 1.0491 0.8764 -0.0904 -0.0749 -0.0474 1   GLY H O   
13940 N N   . LEU H  2   ? 0.8989 0.8892 0.7213 -0.0923 -0.0805 -0.0442 2   LEU H N   
13941 C CA  . LEU H  2   ? 0.9240 0.9188 0.7510 -0.0890 -0.0846 -0.0397 2   LEU H CA  
13942 C C   . LEU H  2   ? 0.8935 0.8900 0.7143 -0.0934 -0.0894 -0.0379 2   LEU H C   
13943 O O   . LEU H  2   ? 0.8286 0.8280 0.6513 -0.0910 -0.0917 -0.0349 2   LEU H O   
13944 C CB  . LEU H  2   ? 0.8464 0.8436 0.6818 -0.0867 -0.0875 -0.0364 2   LEU H CB  
13945 C CG  . LEU H  2   ? 0.8785 0.8795 0.7213 -0.0810 -0.0892 -0.0325 2   LEU H CG  
13946 C CD1 . LEU H  2   ? 0.8878 0.8883 0.7336 -0.0751 -0.0840 -0.0339 2   LEU H CD1 
13947 C CD2 . LEU H  2   ? 0.4977 0.5007 0.3482 -0.0797 -0.0923 -0.0293 2   LEU H CD2 
13948 N N   . PHE H  3   ? 0.9117 0.9063 0.7252 -0.1001 -0.0909 -0.0396 3   PHE H N   
13949 C CA  . PHE H  3   ? 0.9196 0.9159 0.7267 -0.1047 -0.0955 -0.0378 3   PHE H CA  
13950 C C   . PHE H  3   ? 1.0260 1.0192 0.8235 -0.1079 -0.0924 -0.0414 3   PHE H C   
13951 O O   . PHE H  3   ? 1.0537 1.0475 0.8446 -0.1122 -0.0956 -0.0405 3   PHE H O   
13952 C CB  . PHE H  3   ? 0.9605 0.9580 0.7660 -0.1103 -0.1007 -0.0361 3   PHE H CB  
13953 C CG  . PHE H  3   ? 0.9582 0.9595 0.7731 -0.1075 -0.1047 -0.0315 3   PHE H CG  
13954 C CD1 . PHE H  3   ? 0.8706 0.8714 0.6924 -0.1048 -0.1029 -0.0321 3   PHE H CD1 
13955 C CD2 . PHE H  3   ? 1.0623 1.0676 0.8792 -0.1073 -0.1100 -0.0266 3   PHE H CD2 
13956 C CE1 . PHE H  3   ? 0.8175 0.8216 0.6479 -0.1022 -0.1064 -0.0279 3   PHE H CE1 
13957 C CE2 . PHE H  3   ? 0.9837 0.9924 0.8096 -0.1046 -0.1134 -0.0223 3   PHE H CE2 
13958 C CZ  . PHE H  3   ? 0.8492 0.8572 0.6818 -0.1021 -0.1116 -0.0231 3   PHE H CZ  
13959 N N   . GLY H  4   ? 1.0881 1.0779 0.8853 -0.1057 -0.0862 -0.0454 4   GLY H N   
13960 C CA  . GLY H  4   ? 1.0154 1.0022 0.8048 -0.1077 -0.0824 -0.0490 4   GLY H CA  
13961 C C   . GLY H  4   ? 1.0927 1.0760 0.8725 -0.1154 -0.0821 -0.0523 4   GLY H C   
13962 O O   . GLY H  4   ? 1.1224 1.1028 0.8951 -0.1177 -0.0788 -0.0555 4   GLY H O   
13963 N N   . ALA H  5   ? 1.1186 1.1023 0.8982 -0.1194 -0.0855 -0.0517 5   ALA H N   
13964 C CA  . ALA H  5   ? 0.9525 0.9334 0.7227 -0.1273 -0.0857 -0.0548 5   ALA H CA  
13965 C C   . ALA H  5   ? 1.0347 1.0103 0.8036 -0.1283 -0.0792 -0.0602 5   ALA H C   
13966 O O   . ALA H  5   ? 0.9822 0.9538 0.7446 -0.1303 -0.0745 -0.0641 5   ALA H O   
13967 C CB  . ALA H  5   ? 0.9168 0.9007 0.6871 -0.1317 -0.0923 -0.0518 5   ALA H CB  
13968 N N   . ILE H  6   ? 1.0747 1.0501 0.8498 -0.1270 -0.0787 -0.0602 6   ILE H N   
13969 C CA  . ILE H  6   ? 0.9323 0.9026 0.7070 -0.1278 -0.0724 -0.0651 6   ILE H CA  
13970 C C   . ILE H  6   ? 0.9878 0.9560 0.7665 -0.1214 -0.0657 -0.0668 6   ILE H C   
13971 O O   . ILE H  6   ? 0.9283 0.8995 0.7154 -0.1145 -0.0659 -0.0638 6   ILE H O   
13972 C CB  . ILE H  6   ? 0.8594 0.8302 0.6406 -0.1275 -0.0735 -0.0644 6   ILE H CB  
13973 C CG1 . ILE H  6   ? 0.8380 0.8113 0.6152 -0.1343 -0.0802 -0.0627 6   ILE H CG1 
13974 C CG2 . ILE H  6   ? 0.6825 0.6478 0.4636 -0.1281 -0.0665 -0.0694 6   ILE H CG2 
13975 C CD1 . ILE H  6   ? 0.8638 0.8373 0.6463 -0.1353 -0.0811 -0.0627 6   ILE H CD1 
13976 N N   . ALA H  7   ? 0.9512 0.9145 0.7242 -0.1237 -0.0598 -0.0715 7   ALA H N   
13977 C CA  . ALA H  7   ? 0.8996 0.8610 0.6756 -0.1182 -0.0533 -0.0732 7   ALA H CA  
13978 C C   . ALA H  7   ? 1.0335 0.9985 0.8097 -0.1147 -0.0554 -0.0704 7   ALA H C   
13979 O O   . ALA H  7   ? 1.0946 1.0604 0.8761 -0.1085 -0.0520 -0.0698 7   ALA H O   
13980 C CB  . ALA H  7   ? 0.9286 0.8902 0.7148 -0.1119 -0.0502 -0.0724 7   ALA H CB  
13981 N N   . GLY H  8   ? 1.0751 1.0423 0.8455 -0.1189 -0.0609 -0.0685 8   GLY H N   
13982 C CA  . GLY H  8   ? 1.0673 1.0377 0.8371 -0.1164 -0.0631 -0.0658 8   GLY H CA  
13983 C C   . GLY H  8   ? 1.1708 1.1389 0.9299 -0.1220 -0.0627 -0.0682 8   GLY H C   
13984 O O   . GLY H  8   ? 1.2009 1.1646 0.9558 -0.1233 -0.0568 -0.0724 8   GLY H O   
13985 N N   . PHE H  9   ? 0.9722 0.9431 0.7269 -0.1253 -0.0686 -0.0653 9   PHE H N   
13986 C CA  . PHE H  9   ? 1.0037 0.9726 0.7477 -0.1311 -0.0687 -0.0672 9   PHE H CA  
13987 C C   . PHE H  9   ? 1.1435 1.1085 0.8794 -0.1388 -0.0679 -0.0709 9   PHE H C   
13988 O O   . PHE H  9   ? 1.3914 1.3532 1.1179 -0.1439 -0.0660 -0.0739 9   PHE H O   
13989 C CB  . PHE H  9   ? 1.1096 1.0828 0.8516 -0.1320 -0.0751 -0.0627 9   PHE H CB  
13990 C CG  . PHE H  9   ? 1.0828 1.0597 0.8271 -0.1340 -0.0821 -0.0586 9   PHE H CG  
13991 C CD1 . PHE H  9   ? 1.2072 1.1832 0.9446 -0.1414 -0.0850 -0.0594 9   PHE H CD1 
13992 C CD2 . PHE H  9   ? 1.2117 1.1932 0.9653 -0.1285 -0.0856 -0.0539 9   PHE H CD2 
13993 C CE1 . PHE H  9   ? 1.2131 1.1930 0.9532 -0.1431 -0.0916 -0.0554 9   PHE H CE1 
13994 C CE2 . PHE H  9   ? 1.2464 1.2314 1.0028 -0.1302 -0.0919 -0.0499 9   PHE H CE2 
13995 C CZ  . PHE H  9   ? 1.2455 1.2298 0.9953 -0.1374 -0.0949 -0.0506 9   PHE H CZ  
13996 N N   . ILE H  10  ? 1.0538 1.0190 0.7934 -0.1398 -0.0694 -0.0707 10  ILE H N   
13997 C CA  . ILE H  10  ? 1.0491 1.0101 0.7824 -0.1464 -0.0674 -0.0749 10  ILE H CA  
13998 C C   . ILE H  10  ? 1.0385 0.9957 0.7774 -0.1428 -0.0603 -0.0783 10  ILE H C   
13999 O O   . ILE H  10  ? 1.0511 1.0094 0.7975 -0.1401 -0.0609 -0.0772 10  ILE H O   
14000 C CB  . ILE H  10  ? 0.8660 0.8299 0.5994 -0.1507 -0.0739 -0.0724 10  ILE H CB  
14001 C CG1 . ILE H  10  ? 1.0209 0.9898 0.7515 -0.1526 -0.0814 -0.0676 10  ILE H CG1 
14002 C CG2 . ILE H  10  ? 0.8553 0.8150 0.5805 -0.1587 -0.0721 -0.0771 10  ILE H CG2 
14003 C CD1 . ILE H  10  ? 0.9338 0.9068 0.6669 -0.1553 -0.0883 -0.0639 10  ILE H CD1 
14004 N N   . GLU H  11  ? 1.1842 1.1369 0.9196 -0.1426 -0.0536 -0.0824 11  GLU H N   
14005 C CA  . GLU H  11  ? 1.3196 1.2689 1.0610 -0.1379 -0.0462 -0.0852 11  GLU H CA  
14006 C C   . GLU H  11  ? 1.2763 1.2221 1.0183 -0.1411 -0.0439 -0.0881 11  GLU H C   
14007 O O   . GLU H  11  ? 1.1885 1.1334 0.9387 -0.1362 -0.0402 -0.0884 11  GLU H O   
14008 C CB  . GLU H  11  ? 1.4080 1.3530 1.1446 -0.1382 -0.0395 -0.0890 11  GLU H CB  
14009 C CG  . GLU H  11  ? 1.6404 1.5885 1.3756 -0.1358 -0.0414 -0.0866 11  GLU H CG  
14010 C CD  . GLU H  11  ? 2.0365 1.9803 1.7662 -0.1369 -0.0349 -0.0906 11  GLU H CD  
14011 O OE1 . GLU H  11  ? 2.0937 2.0395 1.8220 -0.1352 -0.0357 -0.0892 11  GLU H OE1 
14012 O OE2 . GLU H  11  ? 2.0272 1.9654 1.7543 -0.1396 -0.0288 -0.0952 11  GLU H OE2 
14013 N N   . GLY H  12  ? 1.2395 1.1834 0.9727 -0.1494 -0.0459 -0.0903 12  GLY H N   
14014 C CA  . GLY H  12  ? 1.0839 1.0234 0.8158 -0.1536 -0.0425 -0.0943 12  GLY H CA  
14015 C C   . GLY H  12  ? 1.1108 1.0523 0.8406 -0.1593 -0.0484 -0.0934 12  GLY H C   
14016 O O   . GLY H  12  ? 1.1218 1.0679 0.8486 -0.1621 -0.0557 -0.0899 12  GLY H O   
14017 N N   . GLY H  13  ? 1.1155 1.0535 0.8471 -0.1612 -0.0449 -0.0965 13  GLY H N   
14018 C CA  . GLY H  13  ? 1.1434 1.0827 0.8732 -0.1671 -0.0494 -0.0965 13  GLY H CA  
14019 C C   . GLY H  13  ? 1.1269 1.0612 0.8452 -0.1767 -0.0468 -0.1021 13  GLY H C   
14020 O O   . GLY H  13  ? 1.1463 1.0751 0.8592 -0.1781 -0.0402 -0.1064 13  GLY H O   
14021 N N   . TRP H  14  ? 1.1356 1.0718 0.8501 -0.1834 -0.0519 -0.1019 14  TRP H N   
14022 C CA  . TRP H  14  ? 1.1643 1.0964 0.8673 -0.1933 -0.0503 -0.1070 14  TRP H CA  
14023 C C   . TRP H  14  ? 1.3174 1.2466 1.0222 -0.1969 -0.0478 -0.1105 14  TRP H C   
14024 O O   . TRP H  14  ? 1.3344 1.2678 1.0414 -0.1993 -0.0539 -0.1080 14  TRP H O   
14025 C CB  . TRP H  14  ? 1.1878 1.1246 0.8822 -0.2000 -0.0586 -0.1044 14  TRP H CB  
14026 C CG  . TRP H  14  ? 1.1984 1.1375 0.8895 -0.1977 -0.0608 -0.1015 14  TRP H CG  
14027 C CD1 . TRP H  14  ? 1.1498 1.0855 0.8408 -0.1932 -0.0550 -0.1031 14  TRP H CD1 
14028 C CD2 . TRP H  14  ? 0.9609 0.9060 0.6483 -0.1999 -0.0693 -0.0966 14  TRP H CD2 
14029 N NE1 . TRP H  14  ? 1.1364 1.0757 0.8239 -0.1926 -0.0594 -0.0996 14  TRP H NE1 
14030 C CE2 . TRP H  14  ? 1.0910 1.0359 0.7762 -0.1966 -0.0681 -0.0955 14  TRP H CE2 
14031 C CE3 . TRP H  14  ? 1.0765 1.0275 0.7627 -0.2044 -0.0778 -0.0927 14  TRP H CE3 
14032 C CZ2 . TRP H  14  ? 1.1216 1.0716 0.8033 -0.1975 -0.0748 -0.0908 14  TRP H CZ2 
14033 C CZ3 . TRP H  14  ? 1.2956 1.2517 0.9786 -0.2052 -0.0846 -0.0878 14  TRP H CZ3 
14034 C CH2 . TRP H  14  ? 1.3423 1.2977 1.0229 -0.2018 -0.0830 -0.0870 14  TRP H CH2 
14035 N N   . THR H  15  ? 1.3371 1.2591 1.0411 -0.1973 -0.0388 -0.1161 15  THR H N   
14036 C CA  . THR H  15  ? 1.4177 1.3357 1.1218 -0.2018 -0.0353 -0.1204 15  THR H CA  
14037 C C   . THR H  15  ? 1.6399 1.5588 1.3329 -0.2128 -0.0400 -0.1223 15  THR H C   
14038 O O   . THR H  15  ? 1.6955 1.6146 1.3891 -0.2173 -0.0414 -0.1238 15  THR H O   
14039 C CB  . THR H  15  ? 1.4742 1.3836 1.1774 -0.2014 -0.0242 -0.1265 15  THR H CB  
14040 O OG1 . THR H  15  ? 1.7286 1.6341 1.4198 -0.2075 -0.0214 -0.1305 15  THR H OG1 
14041 C CG2 . THR H  15  ? 1.4377 1.3466 1.1514 -0.1907 -0.0196 -0.1244 15  THR H CG2 
14042 N N   . GLY H  16  ? 1.4077 1.3275 1.0906 -0.2173 -0.0426 -0.1223 16  GLY H N   
14043 C CA  . GLY H  16  ? 1.3777 1.2985 1.0487 -0.2280 -0.0470 -0.1242 16  GLY H CA  
14044 C C   . GLY H  16  ? 1.3772 1.3058 1.0504 -0.2305 -0.0570 -0.1191 16  GLY H C   
14045 O O   . GLY H  16  ? 1.4882 1.4172 1.1556 -0.2389 -0.0594 -0.1214 16  GLY H O   
14046 N N   . MET H  17  ? 1.3836 1.3186 1.0653 -0.2233 -0.0628 -0.1123 17  MET H N   
14047 C CA  . MET H  17  ? 1.4189 1.3618 1.1042 -0.2246 -0.0723 -0.1069 17  MET H CA  
14048 C C   . MET H  17  ? 1.5576 1.5010 1.2535 -0.2216 -0.0717 -0.1065 17  MET H C   
14049 O O   . MET H  17  ? 1.6161 1.5596 1.3230 -0.2126 -0.0694 -0.1043 17  MET H O   
14050 C CB  . MET H  17  ? 1.2255 1.1747 0.9154 -0.2184 -0.0786 -0.0997 17  MET H CB  
14051 C CG  . MET H  17  ? 1.4361 1.3936 1.1300 -0.2195 -0.0884 -0.0936 17  MET H CG  
14052 S SD  . MET H  17  ? 1.5525 1.5168 1.2515 -0.2125 -0.0950 -0.0854 17  MET H SD  
14053 C CE  . MET H  17  ? 1.2953 1.2565 1.0062 -0.2005 -0.0882 -0.0854 17  MET H CE  
14054 N N   . VAL H  18  ? 1.5592 1.5031 1.2517 -0.2293 -0.0738 -0.1087 18  VAL H N   
14055 C CA  . VAL H  18  ? 1.6254 1.5691 1.3270 -0.2276 -0.0726 -0.1092 18  VAL H CA  
14056 C C   . VAL H  18  ? 1.5345 1.4861 1.2389 -0.2309 -0.0820 -0.1045 18  VAL H C   
14057 O O   . VAL H  18  ? 1.6917 1.6436 1.4013 -0.2323 -0.0820 -0.1055 18  VAL H O   
14058 C CB  . VAL H  18  ? 1.6829 1.6190 1.3792 -0.2338 -0.0648 -0.1171 18  VAL H CB  
14059 C CG1 . VAL H  18  ? 1.5018 1.4300 1.1965 -0.2302 -0.0550 -0.1216 18  VAL H CG1 
14060 C CG2 . VAL H  18  ? 1.6555 1.5922 1.3387 -0.2458 -0.0682 -0.1201 18  VAL H CG2 
14061 N N   . ASP H  19  ? 1.7506 1.7086 1.4519 -0.2322 -0.0900 -0.0993 19  ASP H N   
14062 C CA  . ASP H  19  ? 1.8883 1.8543 1.5919 -0.2355 -0.0993 -0.0943 19  ASP H CA  
14063 C C   . ASP H  19  ? 1.8077 1.7792 1.5251 -0.2262 -0.1035 -0.0874 19  ASP H C   
14064 O O   . ASP H  19  ? 1.7718 1.7484 1.4959 -0.2268 -0.1086 -0.0841 19  ASP H O   
14065 C CB  . ASP H  19  ? 2.0859 2.0562 1.7786 -0.2425 -0.1059 -0.0921 19  ASP H CB  
14066 C CG  . ASP H  19  ? 2.2302 2.1948 1.9085 -0.2513 -0.1014 -0.0989 19  ASP H CG  
14067 O OD1 . ASP H  19  ? 2.2704 2.2291 1.9467 -0.2547 -0.0951 -0.1053 19  ASP H OD1 
14068 O OD2 . ASP H  19  ? 2.1186 2.0845 1.7876 -0.2548 -0.1041 -0.0979 19  ASP H OD2 
14069 N N   . GLY H  20  ? 1.5903 1.5608 1.3120 -0.2179 -0.1011 -0.0852 20  GLY H N   
14070 C CA  . GLY H  20  ? 1.3159 1.2911 1.0499 -0.2089 -0.1044 -0.0789 20  GLY H CA  
14071 C C   . GLY H  20  ? 1.2654 1.2370 1.0043 -0.1997 -0.0986 -0.0790 20  GLY H C   
14072 O O   . GLY H  20  ? 1.1148 1.0799 0.8487 -0.1998 -0.0913 -0.0842 20  GLY H O   
14073 N N   . TRP H  21  ? 1.0553 1.0312 0.8042 -0.1918 -0.1017 -0.0733 21  TRP H N   
14074 C CA  . TRP H  21  ? 1.0790 1.0525 0.8334 -0.1828 -0.0968 -0.0728 21  TRP H CA  
14075 C C   . TRP H  21  ? 1.0694 1.0437 0.8177 -0.1820 -0.0979 -0.0712 21  TRP H C   
14076 O O   . TRP H  21  ? 1.0323 1.0024 0.7794 -0.1781 -0.0921 -0.0737 21  TRP H O   
14077 C CB  . TRP H  21  ? 1.1518 1.1292 0.9196 -0.1747 -0.0991 -0.0677 21  TRP H CB  
14078 C CG  . TRP H  21  ? 1.1560 1.1305 0.9312 -0.1723 -0.0946 -0.0701 21  TRP H CG  
14079 C CD1 . TRP H  21  ? 0.9417 0.9096 0.7143 -0.1737 -0.0870 -0.0762 21  TRP H CD1 
14080 C CD2 . TRP H  21  ? 0.9788 0.9567 0.7654 -0.1678 -0.0971 -0.0664 21  TRP H CD2 
14081 N NE1 . TRP H  21  ? 1.0363 1.0033 0.8180 -0.1705 -0.0847 -0.0764 21  TRP H NE1 
14082 C CE2 . TRP H  21  ? 1.0016 0.9747 0.7918 -0.1668 -0.0908 -0.0705 21  TRP H CE2 
14083 C CE3 . TRP H  21  ? 0.9277 0.9122 0.7220 -0.1645 -0.1037 -0.0599 21  TRP H CE3 
14084 C CZ2 . TRP H  21  ? 1.0303 1.0050 0.8313 -0.1628 -0.0912 -0.0684 21  TRP H CZ2 
14085 C CZ3 . TRP H  21  ? 0.9050 0.8909 0.7100 -0.1605 -0.1040 -0.0580 21  TRP H CZ3 
14086 C CH2 . TRP H  21  ? 0.9982 0.9793 0.8064 -0.1597 -0.0978 -0.0622 21  TRP H CH2 
14087 N N   . TYR H  22  ? 1.1703 1.1500 0.9150 -0.1856 -0.1055 -0.0670 22  TYR H N   
14088 C CA  . TYR H  22  ? 1.0837 1.0642 0.8220 -0.1856 -0.1070 -0.0653 22  TYR H CA  
14089 C C   . TYR H  22  ? 1.2564 1.2383 0.9828 -0.1954 -0.1112 -0.0660 22  TYR H C   
14090 O O   . TYR H  22  ? 1.4408 1.4262 1.1666 -0.2009 -0.1162 -0.0647 22  TYR H O   
14091 C CB  . TYR H  22  ? 1.1852 1.1716 0.9318 -0.1791 -0.1121 -0.0583 22  TYR H CB  
14092 C CG  . TYR H  22  ? 1.1098 1.0978 0.8696 -0.1719 -0.1118 -0.0557 22  TYR H CG  
14093 C CD1 . TYR H  22  ? 1.0132 1.0062 0.7793 -0.1729 -0.1176 -0.0518 22  TYR H CD1 
14094 C CD2 . TYR H  22  ? 1.0869 1.0717 0.8530 -0.1641 -0.1057 -0.0572 22  TYR H CD2 
14095 C CE1 . TYR H  22  ? 1.0475 1.0419 0.8256 -0.1664 -0.1171 -0.0495 22  TYR H CE1 
14096 C CE2 . TYR H  22  ? 1.0147 1.0010 0.7925 -0.1577 -0.1054 -0.0548 22  TYR H CE2 
14097 C CZ  . TYR H  22  ? 1.0730 1.0639 0.8567 -0.1589 -0.1110 -0.0511 22  TYR H CZ  
14098 O OH  . TYR H  22  ? 0.7336 0.7258 0.5288 -0.1526 -0.1104 -0.0488 22  TYR H OH  
14099 N N   . GLY H  23  ? 1.4086 1.3878 1.1254 -0.1979 -0.1092 -0.0681 23  GLY H N   
14100 C CA  . GLY H  23  ? 1.5230 1.5032 1.2275 -0.2072 -0.1127 -0.0690 23  GLY H CA  
14101 C C   . GLY H  23  ? 1.6001 1.5776 1.2954 -0.2083 -0.1105 -0.0704 23  GLY H C   
14102 O O   . GLY H  23  ? 1.4122 1.3886 1.1115 -0.2013 -0.1077 -0.0694 23  GLY H O   
14103 N N   . TYR H  24  ? 1.4658 1.4423 1.1485 -0.2173 -0.1118 -0.0729 24  TYR H N   
14104 C CA  . TYR H  24  ? 1.2665 1.2408 0.9394 -0.2194 -0.1102 -0.0741 24  TYR H CA  
14105 C C   . TYR H  24  ? 1.4106 1.3777 1.0722 -0.2260 -0.1035 -0.0818 24  TYR H C   
14106 O O   . TYR H  24  ? 1.4814 1.4457 1.1419 -0.2301 -0.1008 -0.0862 24  TYR H O   
14107 C CB  . TYR H  24  ? 1.2666 1.2470 0.9337 -0.2242 -0.1187 -0.0687 24  TYR H CB  
14108 C CG  . TYR H  24  ? 1.2651 1.2532 0.9426 -0.2198 -0.1262 -0.0610 24  TYR H CG  
14109 C CD1 . TYR H  24  ? 1.2826 1.2749 0.9645 -0.2227 -0.1310 -0.0590 24  TYR H CD1 
14110 C CD2 . TYR H  24  ? 1.2564 1.2474 0.9395 -0.2131 -0.1284 -0.0557 24  TYR H CD2 
14111 C CE1 . TYR H  24  ? 1.3287 1.3279 1.0204 -0.2187 -0.1376 -0.0518 24  TYR H CE1 
14112 C CE2 . TYR H  24  ? 1.0969 1.0946 0.7897 -0.2092 -0.1348 -0.0487 24  TYR H CE2 
14113 C CZ  . TYR H  24  ? 1.3007 1.3024 0.9979 -0.2120 -0.1394 -0.0467 24  TYR H CZ  
14114 O OH  . TYR H  24  ? 1.2097 1.2180 0.9169 -0.2080 -0.1456 -0.0396 24  TYR H OH  
14115 N N   . HIS H  25  ? 1.3537 1.3178 1.0071 -0.2272 -0.1008 -0.0836 25  HIS H N   
14116 C CA  . HIS H  25  ? 1.4922 1.4497 1.1334 -0.2343 -0.0949 -0.0906 25  HIS H CA  
14117 C C   . HIS H  25  ? 1.6741 1.6322 1.3039 -0.2390 -0.0973 -0.0897 25  HIS H C   
14118 O O   . HIS H  25  ? 1.4406 1.3966 1.0699 -0.2347 -0.0941 -0.0896 25  HIS H O   
14119 C CB  . HIS H  25  ? 1.4861 1.4362 1.1307 -0.2293 -0.0848 -0.0960 25  HIS H CB  
14120 C CG  . HIS H  25  ? 1.6187 1.5618 1.2513 -0.2354 -0.0782 -0.1027 25  HIS H CG  
14121 N ND1 . HIS H  25  ? 1.5347 1.4752 1.1624 -0.2339 -0.0750 -0.1036 25  HIS H ND1 
14122 C CD2 . HIS H  25  ? 1.6214 1.5594 1.2458 -0.2433 -0.0740 -0.1090 25  HIS H CD2 
14123 C CE1 . HIS H  25  ? 1.6143 1.5483 1.2315 -0.2404 -0.0690 -0.1100 25  HIS H CE1 
14124 N NE2 . HIS H  25  ? 1.7988 1.7310 1.4136 -0.2462 -0.0683 -0.1135 25  HIS H NE2 
14125 N N   . HIS H  26  ? 1.9228 1.8839 1.5434 -0.2479 -0.1029 -0.0888 26  HIS H N   
14126 C CA  . HIS H  26  ? 1.7722 1.7346 1.3816 -0.2531 -0.1061 -0.0873 26  HIS H CA  
14127 C C   . HIS H  26  ? 1.8916 1.8461 1.4892 -0.2581 -0.0984 -0.0946 26  HIS H C   
14128 O O   . HIS H  26  ? 2.0083 1.9568 1.6050 -0.2597 -0.0915 -0.1009 26  HIS H O   
14129 C CB  . HIS H  26  ? 1.7676 1.7361 1.3711 -0.2612 -0.1147 -0.0839 26  HIS H CB  
14130 C CG  . HIS H  26  ? 1.8280 1.7931 1.4217 -0.2710 -0.1125 -0.0900 26  HIS H CG  
14131 N ND1 . HIS H  26  ? 1.8428 1.8069 1.4419 -0.2717 -0.1107 -0.0930 26  HIS H ND1 
14132 C CD2 . HIS H  26  ? 2.0195 1.9821 1.5983 -0.2808 -0.1119 -0.0939 26  HIS H CD2 
14133 C CE1 . HIS H  26  ? 2.0109 1.9718 1.5989 -0.2816 -0.1088 -0.0986 26  HIS H CE1 
14134 N NE2 . HIS H  26  ? 2.1262 2.0863 1.7016 -0.2873 -0.1095 -0.0992 26  HIS H NE2 
14135 N N   . GLN H  27  ? 2.2405 2.1947 1.8290 -0.2606 -0.0993 -0.0937 27  GLN H N   
14136 C CA  . GLN H  27  ? 2.3550 2.3017 1.9325 -0.2649 -0.0918 -0.1002 27  GLN H CA  
14137 C C   . GLN H  27  ? 2.2332 2.1817 1.7977 -0.2718 -0.0959 -0.0985 27  GLN H C   
14138 O O   . GLN H  27  ? 2.1267 2.0725 1.6873 -0.2699 -0.0929 -0.0989 27  GLN H O   
14139 C CB  . GLN H  27  ? 2.2583 2.2004 1.8427 -0.2560 -0.0843 -0.1021 27  GLN H CB  
14140 C CG  . GLN H  27  ? 2.2887 2.2231 1.8632 -0.2592 -0.0761 -0.1083 27  GLN H CG  
14141 C CD  . GLN H  27  ? 2.4329 2.3605 2.0011 -0.2657 -0.0695 -0.1161 27  GLN H CD  
14142 O OE1 . GLN H  27  ? 2.3118 2.2338 1.8855 -0.2616 -0.0614 -0.1205 27  GLN H OE1 
14143 N NE2 . GLN H  27  ? 2.5513 2.4794 2.1081 -0.2760 -0.0727 -0.1178 27  GLN H NE2 
14144 N N   . ASN H  28  ? 2.1370 2.0902 1.6949 -0.2797 -0.1030 -0.0963 28  ASN H N   
14145 C CA  . ASN H  28  ? 2.0489 2.0044 1.5942 -0.2868 -0.1076 -0.0942 28  ASN H CA  
14146 C C   . ASN H  28  ? 2.1487 2.0989 1.6785 -0.2978 -0.1038 -0.1011 28  ASN H C   
14147 O O   . ASN H  28  ? 2.1323 2.0760 1.6612 -0.2994 -0.0964 -0.1082 28  ASN H O   
14148 C CB  . ASN H  28  ? 1.8373 1.8025 1.3850 -0.2882 -0.1186 -0.0860 28  ASN H CB  
14149 C CG  . ASN H  28  ? 1.9589 1.9271 1.5048 -0.2953 -0.1227 -0.0868 28  ASN H CG  
14150 O OD1 . ASN H  28  ? 1.9365 1.9127 1.4832 -0.2979 -0.1315 -0.0806 28  ASN H OD1 
14151 N ND2 . ASN H  28  ? 2.0330 1.9953 1.5770 -0.2984 -0.1161 -0.0943 28  ASN H ND2 
14152 N N   . GLU H  29  ? 2.1342 2.0873 1.6519 -0.3054 -0.1089 -0.0991 29  GLU H N   
14153 C CA  . GLU H  29  ? 2.2245 2.1725 1.7260 -0.3162 -0.1053 -0.1054 29  GLU H CA  
14154 C C   . GLU H  29  ? 2.2079 2.1561 1.7050 -0.3245 -0.1062 -0.1093 29  GLU H C   
14155 O O   . GLU H  29  ? 2.1481 2.0911 1.6323 -0.3335 -0.1020 -0.1158 29  GLU H O   
14156 C CB  . GLU H  29  ? 2.3624 2.3141 1.8524 -0.3216 -0.1110 -0.1013 29  GLU H CB  
14157 C CG  . GLU H  29  ? 2.3370 2.2890 1.8311 -0.3137 -0.1107 -0.0970 29  GLU H CG  
14158 C CD  . GLU H  29  ? 2.4662 2.4252 1.9547 -0.3166 -0.1195 -0.0895 29  GLU H CD  
14159 O OE1 . GLU H  29  ? 2.4191 2.3851 1.9065 -0.3214 -0.1275 -0.0852 29  GLU H OE1 
14160 O OE2 . GLU H  29  ? 2.4324 2.3902 1.9189 -0.3138 -0.1180 -0.0874 29  GLU H OE2 
14161 N N   . GLN H  30  ? 2.2664 2.2203 1.7740 -0.3218 -0.1115 -0.1055 30  GLN H N   
14162 C CA  . GLN H  30  ? 2.2959 2.2505 1.8004 -0.3296 -0.1127 -0.1089 30  GLN H CA  
14163 C C   . GLN H  30  ? 2.3573 2.3063 1.8709 -0.3254 -0.1052 -0.1145 30  GLN H C   
14164 O O   . GLN H  30  ? 2.3672 2.3168 1.8809 -0.3303 -0.1058 -0.1171 30  GLN H O   
14165 C CB  . GLN H  30  ? 2.1319 2.0971 1.6406 -0.3312 -0.1239 -0.1013 30  GLN H CB  
14166 C CG  . GLN H  30  ? 1.9996 1.9707 1.4975 -0.3377 -0.1316 -0.0963 30  GLN H CG  
14167 C CD  . GLN H  30  ? 2.0221 2.0016 1.5299 -0.3306 -0.1399 -0.0862 30  GLN H CD  
14168 O OE1 . GLN H  30  ? 1.9423 1.9298 1.4560 -0.3313 -0.1478 -0.0806 30  GLN H OE1 
14169 N NE2 . GLN H  30  ? 2.0740 2.0518 1.5842 -0.3237 -0.1379 -0.0838 30  GLN H NE2 
14170 N N   . GLY H  31  ? 2.9097 2.8535 2.4311 -0.3163 -0.0981 -0.1161 31  GLY H N   
14171 C CA  . GLY H  31  ? 2.8976 2.8356 2.4275 -0.3120 -0.0903 -0.1213 31  GLY H CA  
14172 C C   . GLY H  31  ? 2.8350 2.7747 2.3815 -0.2993 -0.0899 -0.1170 31  GLY H C   
14173 O O   . GLY H  31  ? 2.7974 2.7422 2.3489 -0.2935 -0.0949 -0.1104 31  GLY H O   
14174 N N   . SER H  32  ? 2.4003 2.3357 1.9554 -0.2952 -0.0836 -0.1209 32  SER H N   
14175 C CA  . SER H  32  ? 2.2283 2.1649 1.7992 -0.2834 -0.0825 -0.1175 32  SER H CA  
14176 C C   . SER H  32  ? 2.1440 2.0831 1.7246 -0.2821 -0.0844 -0.1169 32  SER H C   
14177 O O   . SER H  32  ? 2.1319 2.0741 1.7079 -0.2897 -0.0890 -0.1171 32  SER H O   
14178 C CB  . SER H  32  ? 2.0675 1.9959 1.6408 -0.2779 -0.0719 -0.1226 32  SER H CB  
14179 O OG  . SER H  32  ? 2.1531 2.0784 1.7166 -0.2801 -0.0694 -0.1240 32  SER H OG  
14180 N N   . GLY H  33  ? 2.2316 2.1695 1.8255 -0.2724 -0.0807 -0.1162 33  GLY H N   
14181 C CA  . GLY H  33  ? 2.1305 2.0701 1.7343 -0.2703 -0.0815 -0.1159 33  GLY H CA  
14182 C C   . GLY H  33  ? 1.9551 1.9007 1.5734 -0.2604 -0.0863 -0.1087 33  GLY H C   
14183 O O   . GLY H  33  ? 1.8837 1.8333 1.5040 -0.2558 -0.0903 -0.1034 33  GLY H O   
14184 N N   . TYR H  34  ? 1.5938 1.5400 1.2222 -0.2571 -0.0856 -0.1087 34  TYR H N   
14185 C CA  . TYR H  34  ? 1.3616 1.3134 1.0042 -0.2480 -0.0898 -0.1023 34  TYR H CA  
14186 C C   . TYR H  34  ? 1.3747 1.3339 1.0202 -0.2515 -0.0987 -0.0979 34  TYR H C   
14187 O O   . TYR H  34  ? 1.4888 1.4475 1.1289 -0.2595 -0.0993 -0.1011 34  TYR H O   
14188 C CB  . TYR H  34  ? 1.2983 1.2454 0.9516 -0.2405 -0.0824 -0.1050 34  TYR H CB  
14189 C CG  . TYR H  34  ? 1.3055 1.2451 0.9568 -0.2371 -0.0731 -0.1097 34  TYR H CG  
14190 C CD1 . TYR H  34  ? 1.3066 1.2386 0.9503 -0.2428 -0.0653 -0.1173 34  TYR H CD1 
14191 C CD2 . TYR H  34  ? 1.2648 1.2050 0.9222 -0.2283 -0.0718 -0.1066 34  TYR H CD2 
14192 C CE1 . TYR H  34  ? 1.3589 1.2841 1.0014 -0.2395 -0.0566 -0.1214 34  TYR H CE1 
14193 C CE2 . TYR H  34  ? 1.1694 1.1033 0.8256 -0.2251 -0.0633 -0.1107 34  TYR H CE2 
14194 C CZ  . TYR H  34  ? 1.2920 1.2184 0.9409 -0.2307 -0.0557 -0.1179 34  TYR H CZ  
14195 O OH  . TYR H  34  ? 1.1395 1.0597 0.7878 -0.2274 -0.0471 -0.1218 34  TYR H OH  
14196 N N   . ALA H  35  ? 1.3655 1.3315 1.0197 -0.2455 -0.1053 -0.0904 35  ALA H N   
14197 C CA  . ALA H  35  ? 1.4153 1.3890 1.0743 -0.2476 -0.1137 -0.0853 35  ALA H CA  
14198 C C   . ALA H  35  ? 1.4925 1.4704 1.1666 -0.2375 -0.1162 -0.0794 35  ALA H C   
14199 O O   . ALA H  35  ? 1.5237 1.5043 1.2012 -0.2318 -0.1186 -0.0746 35  ALA H O   
14200 C CB  . ALA H  35  ? 1.5568 1.5362 1.2068 -0.2543 -0.1217 -0.0813 35  ALA H CB  
14201 N N   . ALA H  36  ? 1.4082 1.3864 1.0912 -0.2355 -0.1155 -0.0799 36  ALA H N   
14202 C CA  . ALA H  36  ? 1.4374 1.4190 1.1349 -0.2261 -0.1173 -0.0748 36  ALA H CA  
14203 C C   . ALA H  36  ? 1.2944 1.2849 0.9960 -0.2259 -0.1270 -0.0668 36  ALA H C   
14204 O O   . ALA H  36  ? 1.4920 1.4869 1.1890 -0.2335 -0.1329 -0.0655 36  ALA H O   
14205 C CB  . ALA H  36  ? 1.4135 1.3928 1.1189 -0.2244 -0.1135 -0.0777 36  ALA H CB  
14206 N N   . ASP H  37  ? 1.2098 1.2031 0.9204 -0.2174 -0.1287 -0.0616 37  ASP H N   
14207 C CA  . ASP H  37  ? 1.3212 1.3227 1.0373 -0.2161 -0.1373 -0.0537 37  ASP H CA  
14208 C C   . ASP H  37  ? 1.4466 1.4522 1.1715 -0.2166 -0.1411 -0.0514 37  ASP H C   
14209 O O   . ASP H  37  ? 1.4165 1.4202 1.1509 -0.2109 -0.1374 -0.0525 37  ASP H O   
14210 C CB  . ASP H  37  ? 1.2016 1.2043 0.9258 -0.2066 -0.1373 -0.0491 37  ASP H CB  
14211 C CG  . ASP H  37  ? 1.3433 1.3541 1.0729 -0.2054 -0.1457 -0.0409 37  ASP H CG  
14212 O OD1 . ASP H  37  ? 1.5689 1.5812 1.3059 -0.1978 -0.1461 -0.0368 37  ASP H OD1 
14213 O OD2 . ASP H  37  ? 1.5428 1.5584 1.2692 -0.2121 -0.1520 -0.0385 37  ASP H OD2 
14214 N N   . LEU H  38  ? 1.5100 1.5216 1.2317 -0.2234 -0.1484 -0.0482 38  LEU H N   
14215 C CA  . LEU H  38  ? 1.6376 1.6535 1.3663 -0.2255 -0.1524 -0.0464 38  LEU H CA  
14216 C C   . LEU H  38  ? 1.4900 1.5100 1.2339 -0.2167 -0.1548 -0.0403 38  LEU H C   
14217 O O   . LEU H  38  ? 1.4196 1.4378 1.1721 -0.2127 -0.1516 -0.0419 38  LEU H O   
14218 C CB  . LEU H  38  ? 1.9527 1.9750 1.6744 -0.2348 -0.1602 -0.0435 38  LEU H CB  
14219 C CG  . LEU H  38  ? 2.0879 2.1117 1.8094 -0.2417 -0.1618 -0.0461 38  LEU H CG  
14220 C CD1 . LEU H  38  ? 1.9791 2.0094 1.6921 -0.2514 -0.1696 -0.0434 38  LEU H CD1 
14221 C CD2 . LEU H  38  ? 2.0503 2.0772 1.7868 -0.2359 -0.1632 -0.0428 38  LEU H CD2 
14222 N N   . LYS H  39  ? 1.7510 1.7764 1.4980 -0.2138 -0.1604 -0.0334 39  LYS H N   
14223 C CA  . LYS H  39  ? 1.8017 1.8316 1.5627 -0.2062 -0.1634 -0.0272 39  LYS H CA  
14224 C C   . LYS H  39  ? 1.7391 1.7641 1.5082 -0.1966 -0.1567 -0.0289 39  LYS H C   
14225 O O   . LYS H  39  ? 1.6498 1.6763 1.4305 -0.1914 -0.1567 -0.0268 39  LYS H O   
14226 C CB  . LYS H  39  ? 2.0269 2.0629 1.7888 -0.2054 -0.1701 -0.0197 39  LYS H CB  
14227 C CG  . LYS H  39  ? 2.1994 2.2405 1.9756 -0.1984 -0.1737 -0.0128 39  LYS H CG  
14228 C CD  . LYS H  39  ? 2.3927 2.4401 2.1694 -0.1986 -0.1805 -0.0052 39  LYS H CD  
14229 C CE  . LYS H  39  ? 2.4398 2.4923 2.2312 -0.1923 -0.1841 0.0017  39  LYS H CE  
14230 N NZ  . LYS H  39  ? 2.3047 2.3636 2.0973 -0.1928 -0.1908 0.0094  39  LYS H NZ  
14231 N N   . SER H  40  ? 1.5035 1.5230 1.2668 -0.1944 -0.1511 -0.0326 40  SER H N   
14232 C CA  . SER H  40  ? 1.3010 1.3163 1.0712 -0.1854 -0.1450 -0.0340 40  SER H CA  
14233 C C   . SER H  40  ? 1.1697 1.1805 0.9440 -0.1840 -0.1392 -0.0391 40  SER H C   
14234 O O   . SER H  40  ? 1.2151 1.2262 1.0003 -0.1774 -0.1378 -0.0374 40  SER H O   
14235 C CB  . SER H  40  ? 1.2791 1.2901 1.0416 -0.1840 -0.1406 -0.0367 40  SER H CB  
14236 O OG  . SER H  40  ? 1.3603 1.3686 1.1302 -0.1750 -0.1358 -0.0368 40  SER H OG  
14237 N N   . THR H  41  ? 1.1682 1.1745 0.9335 -0.1904 -0.1355 -0.0453 41  THR H N   
14238 C CA  . THR H  41  ? 1.1564 1.1577 0.9246 -0.1898 -0.1294 -0.0505 41  THR H CA  
14239 C C   . THR H  41  ? 1.1619 1.1671 0.9395 -0.1897 -0.1330 -0.0480 41  THR H C   
14240 O O   . THR H  41  ? 1.0108 1.0136 0.7967 -0.1848 -0.1288 -0.0493 41  THR H O   
14241 C CB  . THR H  41  ? 1.0709 1.0671 0.8273 -0.1979 -0.1254 -0.0576 41  THR H CB  
14242 O OG1 . THR H  41  ? 1.1612 1.1528 0.9097 -0.1971 -0.1209 -0.0605 41  THR H OG1 
14243 C CG2 . THR H  41  ? 1.0683 1.0595 0.8285 -0.1974 -0.1192 -0.0627 41  THR H CG2 
14244 N N   . GLN H  42  ? 1.3837 1.3952 1.1603 -0.1953 -0.1406 -0.0441 42  GLN H N   
14245 C CA  . GLN H  42  ? 1.4159 1.4319 1.2012 -0.1960 -0.1446 -0.0413 42  GLN H CA  
14246 C C   . GLN H  42  ? 1.3181 1.3365 1.1172 -0.1866 -0.1452 -0.0362 42  GLN H C   
14247 O O   . GLN H  42  ? 1.3368 1.3544 1.1444 -0.1836 -0.1431 -0.0369 42  GLN H O   
14248 C CB  . GLN H  42  ? 1.4394 1.4625 1.2209 -0.2037 -0.1531 -0.0373 42  GLN H CB  
14249 C CG  . GLN H  42  ? 1.5496 1.5775 1.3395 -0.2055 -0.1573 -0.0349 42  GLN H CG  
14250 C CD  . GLN H  42  ? 1.7548 1.7778 1.5436 -0.2088 -0.1520 -0.0416 42  GLN H CD  
14251 O OE1 . GLN H  42  ? 1.7901 1.8074 1.5688 -0.2134 -0.1472 -0.0479 42  GLN H OE1 
14252 N NE2 . GLN H  42  ? 1.6823 1.7071 1.4817 -0.2065 -0.1526 -0.0402 42  GLN H NE2 
14253 N N   . ASN H  43  ? 1.1385 1.1598 0.9395 -0.1822 -0.1480 -0.0312 43  ASN H N   
14254 C CA  . ASN H  43  ? 1.1946 1.2182 1.0082 -0.1734 -0.1485 -0.0264 43  ASN H CA  
14255 C C   . ASN H  43  ? 1.1941 1.2118 1.0126 -0.1662 -0.1407 -0.0301 43  ASN H C   
14256 O O   . ASN H  43  ? 1.0344 1.0528 0.8634 -0.1611 -0.1399 -0.0284 43  ASN H O   
14257 C CB  . ASN H  43  ? 1.1752 1.2022 0.9888 -0.1704 -0.1522 -0.0210 43  ASN H CB  
14258 C CG  . ASN H  43  ? 1.3667 1.4016 1.1846 -0.1728 -0.1607 -0.0141 43  ASN H CG  
14259 O OD1 . ASN H  43  ? 1.5213 1.5593 1.3329 -0.1806 -0.1653 -0.0136 43  ASN H OD1 
14260 N ND2 . ASN H  43  ? 1.3360 1.3741 1.1647 -0.1662 -0.1626 -0.0085 43  ASN H ND2 
14261 N N   . ALA H  44  ? 1.0643 1.0764 0.8752 -0.1659 -0.1350 -0.0349 44  ALA H N   
14262 C CA  . ALA H  44  ? 0.9838 0.9903 0.7986 -0.1594 -0.1274 -0.0384 44  ALA H CA  
14263 C C   . ALA H  44  ? 0.9974 1.0016 0.8170 -0.1600 -0.1242 -0.0415 44  ALA H C   
14264 O O   . ALA H  44  ? 1.0558 1.0592 0.8850 -0.1534 -0.1216 -0.0405 44  ALA H O   
14265 C CB  . ALA H  44  ? 0.9019 0.9029 0.7068 -0.1604 -0.1219 -0.0435 44  ALA H CB  
14266 N N   . ILE H  45  ? 1.0507 1.0536 0.8635 -0.1680 -0.1245 -0.0452 45  ILE H N   
14267 C CA  . ILE H  45  ? 1.0518 1.0525 0.8685 -0.1697 -0.1216 -0.0485 45  ILE H CA  
14268 C C   . ILE H  45  ? 1.0292 1.0348 0.8579 -0.1664 -0.1257 -0.0435 45  ILE H C   
14269 O O   . ILE H  45  ? 0.9830 0.9863 0.8197 -0.1616 -0.1217 -0.0444 45  ILE H O   
14270 C CB  . ILE H  45  ? 1.1008 1.1006 0.9079 -0.1800 -0.1226 -0.0527 45  ILE H CB  
14271 C CG1 . ILE H  45  ? 1.0356 1.0285 0.8320 -0.1827 -0.1161 -0.0591 45  ILE H CG1 
14272 C CG2 . ILE H  45  ? 1.1178 1.1170 0.9304 -0.1821 -0.1216 -0.0545 45  ILE H CG2 
14273 C CD1 . ILE H  45  ? 1.2455 1.2366 1.0320 -0.1930 -0.1159 -0.0640 45  ILE H CD1 
14274 N N   . ASP H  46  ? 1.0106 1.0230 0.8406 -0.1690 -0.1336 -0.0381 46  ASP H N   
14275 C CA  . ASP H  46  ? 0.9825 1.0000 0.8241 -0.1662 -0.1379 -0.0329 46  ASP H CA  
14276 C C   . ASP H  46  ? 0.9740 0.9907 0.8256 -0.1561 -0.1351 -0.0302 46  ASP H C   
14277 O O   . ASP H  46  ? 1.0074 1.0239 0.8683 -0.1524 -0.1335 -0.0296 46  ASP H O   
14278 C CB  . ASP H  46  ? 1.1055 1.1306 0.9468 -0.1700 -0.1467 -0.0269 46  ASP H CB  
14279 C CG  . ASP H  46  ? 1.4191 1.4466 1.2529 -0.1801 -0.1506 -0.0287 46  ASP H CG  
14280 O OD1 . ASP H  46  ? 1.3551 1.3789 1.1864 -0.1840 -0.1469 -0.0340 46  ASP H OD1 
14281 O OD2 . ASP H  46  ? 1.5623 1.5953 1.3926 -0.1844 -0.1573 -0.0246 46  ASP H OD2 
14282 N N   . GLU H  47  ? 1.0323 1.0486 0.8818 -0.1519 -0.1343 -0.0287 47  GLU H N   
14283 C CA  . GLU H  47  ? 0.9104 0.9264 0.7686 -0.1427 -0.1321 -0.0260 47  GLU H CA  
14284 C C   . GLU H  47  ? 0.9006 0.9105 0.7610 -0.1378 -0.1240 -0.0305 47  GLU H C   
14285 O O   . GLU H  47  ? 0.8893 0.8992 0.7592 -0.1316 -0.1222 -0.0287 47  GLU H O   
14286 C CB  . GLU H  47  ? 0.7987 0.8161 0.6536 -0.1401 -0.1337 -0.0232 47  GLU H CB  
14287 C CG  . GLU H  47  ? 0.9916 1.0156 0.8472 -0.1430 -0.1416 -0.0173 47  GLU H CG  
14288 C CD  . GLU H  47  ? 1.0477 1.0731 0.9031 -0.1388 -0.1428 -0.0137 47  GLU H CD  
14289 O OE1 . GLU H  47  ? 0.8970 0.9184 0.7473 -0.1364 -0.1381 -0.0169 47  GLU H OE1 
14290 O OE2 . GLU H  47  ? 1.1367 1.1674 0.9975 -0.1378 -0.1482 -0.0078 47  GLU H OE2 
14291 N N   . ILE H  48  ? 0.8385 0.8433 0.6902 -0.1407 -0.1192 -0.0362 48  ILE H N   
14292 C CA  . ILE H  48  ? 0.6786 0.6775 0.5321 -0.1367 -0.1113 -0.0405 48  ILE H CA  
14293 C C   . ILE H  48  ? 0.7851 0.7832 0.6449 -0.1376 -0.1101 -0.0417 48  ILE H C   
14294 O O   . ILE H  48  ? 0.8655 0.8611 0.7324 -0.1317 -0.1056 -0.0422 48  ILE H O   
14295 C CB  . ILE H  48  ? 0.7683 0.7616 0.6110 -0.1402 -0.1062 -0.0464 48  ILE H CB  
14296 C CG1 . ILE H  48  ? 0.8895 0.8828 0.7275 -0.1375 -0.1059 -0.0455 48  ILE H CG1 
14297 C CG2 . ILE H  48  ? 0.6650 0.6523 0.5102 -0.1372 -0.0982 -0.0510 48  ILE H CG2 
14298 C CD1 . ILE H  48  ? 0.9154 0.9088 0.7611 -0.1282 -0.1033 -0.0430 48  ILE H CD1 
14299 N N   . THR H  49  ? 0.8424 0.8427 0.6994 -0.1451 -0.1142 -0.0422 49  THR H N   
14300 C CA  . THR H  49  ? 0.8758 0.8760 0.7389 -0.1468 -0.1138 -0.0431 49  THR H CA  
14301 C C   . THR H  49  ? 0.8995 0.9034 0.7751 -0.1403 -0.1160 -0.0378 49  THR H C   
14302 O O   . THR H  49  ? 0.9213 0.9226 0.8039 -0.1361 -0.1118 -0.0388 49  THR H O   
14303 C CB  . THR H  49  ? 0.9939 0.9973 0.8520 -0.1563 -0.1192 -0.0435 49  THR H CB  
14304 O OG1 . THR H  49  ? 1.0532 1.0523 0.9000 -0.1627 -0.1159 -0.0494 49  THR H OG1 
14305 C CG2 . THR H  49  ? 0.8265 0.8311 0.6926 -0.1575 -0.1198 -0.0433 49  THR H CG2 
14306 N N   . ASN H  50  ? 0.6879 0.6977 0.5661 -0.1396 -0.1225 -0.0321 50  ASN H N   
14307 C CA  . ASN H  50  ? 0.8417 0.8552 0.7316 -0.1336 -0.1248 -0.0268 50  ASN H CA  
14308 C C   . ASN H  50  ? 0.9011 0.9109 0.7959 -0.1249 -0.1189 -0.0272 50  ASN H C   
14309 O O   . ASN H  50  ? 0.7754 0.7855 0.6797 -0.1200 -0.1176 -0.0254 50  ASN H O   
14310 C CB  . ASN H  50  ? 0.7745 0.7942 0.6653 -0.1340 -0.1319 -0.0208 50  ASN H CB  
14311 C CG  . ASN H  50  ? 0.8451 0.8692 0.7482 -0.1295 -0.1352 -0.0151 50  ASN H CG  
14312 O OD1 . ASN H  50  ? 1.0767 1.1049 0.9842 -0.1332 -0.1397 -0.0127 50  ASN H OD1 
14313 N ND2 . ASN H  50  ? 0.7695 0.7928 0.6783 -0.1217 -0.1328 -0.0130 50  ASN H ND2 
14314 N N   . LYS H  51  ? 0.7974 0.8041 0.6856 -0.1230 -0.1154 -0.0295 51  LYS H N   
14315 C CA  . LYS H  51  ? 0.7567 0.7602 0.6485 -0.1151 -0.1097 -0.0301 51  LYS H CA  
14316 C C   . LYS H  51  ? 0.7948 0.7938 0.6906 -0.1131 -0.1037 -0.0335 51  LYS H C   
14317 O O   . LYS H  51  ? 0.8484 0.8472 0.7527 -0.1069 -0.1016 -0.0317 51  LYS H O   
14318 C CB  . LYS H  51  ? 0.9166 0.9173 0.7997 -0.1146 -0.1068 -0.0326 51  LYS H CB  
14319 C CG  . LYS H  51  ? 0.6833 0.6813 0.5696 -0.1067 -0.1012 -0.0331 51  LYS H CG  
14320 C CD  . LYS H  51  ? 0.8261 0.8231 0.7048 -0.1062 -0.1001 -0.0342 51  LYS H CD  
14321 C CE  . LYS H  51  ? 0.8201 0.8156 0.7025 -0.0983 -0.0953 -0.0340 51  LYS H CE  
14322 N NZ  . LYS H  51  ? 0.8533 0.8496 0.7303 -0.0971 -0.0959 -0.0333 51  LYS H NZ  
14323 N N   . VAL H  52  ? 0.7141 0.7093 0.6035 -0.1186 -0.1009 -0.0385 52  VAL H N   
14324 C CA  . VAL H  52  ? 0.7294 0.7199 0.6219 -0.1175 -0.0948 -0.0422 52  VAL H CA  
14325 C C   . VAL H  52  ? 0.8750 0.8679 0.7769 -0.1171 -0.0970 -0.0399 52  VAL H C   
14326 O O   . VAL H  52  ? 0.9761 0.9666 0.8849 -0.1122 -0.0927 -0.0401 52  VAL H O   
14327 C CB  . VAL H  52  ? 0.6512 0.6373 0.5347 -0.1246 -0.0917 -0.0481 52  VAL H CB  
14328 C CG1 . VAL H  52  ? 0.6841 0.6648 0.5710 -0.1231 -0.0848 -0.0520 52  VAL H CG1 
14329 C CG2 . VAL H  52  ? 0.7538 0.7376 0.6279 -0.1253 -0.0896 -0.0505 52  VAL H CG2 
14330 N N   . ASN H  53  ? 0.7286 0.7263 0.6307 -0.1224 -0.1037 -0.0373 53  ASN H N   
14331 C CA  . ASN H  53  ? 0.8455 0.8462 0.7568 -0.1225 -0.1064 -0.0347 53  ASN H CA  
14332 C C   . ASN H  53  ? 0.9205 0.9233 0.8422 -0.1144 -0.1067 -0.0300 53  ASN H C   
14333 O O   . ASN H  53  ? 0.8981 0.9004 0.8280 -0.1117 -0.1049 -0.0294 53  ASN H O   
14334 C CB  . ASN H  53  ? 0.9557 0.9620 0.8653 -0.1297 -0.1141 -0.0324 53  ASN H CB  
14335 C CG  . ASN H  53  ? 1.0256 1.0299 0.9280 -0.1383 -0.1136 -0.0373 53  ASN H CG  
14336 O OD1 . ASN H  53  ? 0.8010 0.7995 0.7008 -0.1388 -0.1072 -0.0424 53  ASN H OD1 
14337 N ND2 . ASN H  53  ? 1.0577 1.0670 0.9569 -0.1453 -0.1203 -0.0356 53  ASN H ND2 
14338 N N   . SER H  54  ? 0.7820 0.7871 0.7031 -0.1107 -0.1088 -0.0267 54  SER H N   
14339 C CA  . SER H  54  ? 0.7115 0.7187 0.6417 -0.1032 -0.1090 -0.0223 54  SER H CA  
14340 C C   . SER H  54  ? 0.7193 0.7218 0.6534 -0.0968 -0.1019 -0.0244 54  SER H C   
14341 O O   . SER H  54  ? 0.7290 0.7318 0.6720 -0.0930 -0.1008 -0.0225 54  SER H O   
14342 C CB  . SER H  54  ? 0.7211 0.7310 0.6488 -0.1009 -0.1120 -0.0191 54  SER H CB  
14343 O OG  . SER H  54  ? 0.8722 0.8870 0.7978 -0.1063 -0.1189 -0.0162 54  SER H OG  
14344 N N   . VAL H  55  ? 0.7014 0.6997 0.6289 -0.0956 -0.0969 -0.0280 55  VAL H N   
14345 C CA  . VAL H  55  ? 0.7116 0.7057 0.6421 -0.0896 -0.0900 -0.0299 55  VAL H CA  
14346 C C   . VAL H  55  ? 0.7928 0.7844 0.7286 -0.0902 -0.0869 -0.0317 55  VAL H C   
14347 O O   . VAL H  55  ? 0.8436 0.8332 0.7857 -0.0845 -0.0828 -0.0312 55  VAL H O   
14348 C CB  . VAL H  55  ? 0.6705 0.6604 0.5926 -0.0897 -0.0851 -0.0341 55  VAL H CB  
14349 C CG1 . VAL H  55  ? 0.7242 0.7098 0.6498 -0.0837 -0.0778 -0.0359 55  VAL H CG1 
14350 C CG2 . VAL H  55  ? 0.5833 0.5755 0.5007 -0.0883 -0.0876 -0.0323 55  VAL H CG2 
14351 N N   . ILE H  56  ? 0.7803 0.7718 0.7133 -0.0973 -0.0890 -0.0338 56  ILE H N   
14352 C CA  . ILE H  56  ? 0.7653 0.7543 0.7027 -0.0990 -0.0862 -0.0360 56  ILE H CA  
14353 C C   . ILE H  56  ? 0.7806 0.7739 0.7272 -0.0988 -0.0907 -0.0320 56  ILE H C   
14354 O O   . ILE H  56  ? 0.6178 0.6097 0.5722 -0.0949 -0.0877 -0.0313 56  ILE H O   
14355 C CB  . ILE H  56  ? 0.7769 0.7634 0.7065 -0.1072 -0.0856 -0.0409 56  ILE H CB  
14356 C CG1 . ILE H  56  ? 0.7446 0.7257 0.6662 -0.1071 -0.0797 -0.0454 56  ILE H CG1 
14357 C CG2 . ILE H  56  ? 0.6082 0.5929 0.5429 -0.1096 -0.0836 -0.0427 56  ILE H CG2 
14358 C CD1 . ILE H  56  ? 0.7188 0.6971 0.6319 -0.1155 -0.0787 -0.0505 56  ILE H CD1 
14359 N N   . GLU H  57  ? 0.6969 0.6955 0.6427 -0.1031 -0.0978 -0.0291 57  GLU H N   
14360 C CA  . GLU H  57  ? 0.7359 0.7390 0.6901 -0.1043 -0.1026 -0.0253 57  GLU H CA  
14361 C C   . GLU H  57  ? 0.7678 0.7725 0.7320 -0.0967 -0.1023 -0.0209 57  GLU H C   
14362 O O   . GLU H  57  ? 0.8329 0.8391 0.8056 -0.0960 -0.1031 -0.0189 57  GLU H O   
14363 C CB  . GLU H  57  ? 0.9558 0.9645 0.9066 -0.1103 -0.1103 -0.0227 57  GLU H CB  
14364 C CG  . GLU H  57  ? 1.3821 1.3956 1.3401 -0.1138 -0.1154 -0.0198 57  GLU H CG  
14365 C CD  . GLU H  57  ? 1.4316 1.4503 1.3983 -0.1096 -0.1199 -0.0133 57  GLU H CD  
14366 O OE1 . GLU H  57  ? 1.2870 1.3071 1.2516 -0.1066 -0.1213 -0.0109 57  GLU H OE1 
14367 O OE2 . GLU H  57  ? 1.2930 1.3143 1.2688 -0.1093 -0.1218 -0.0107 57  GLU H OE2 
14368 N N   . LYS H  58  ? 0.6891 0.6936 0.6523 -0.0911 -0.1009 -0.0194 58  LYS H N   
14369 C CA  . LYS H  58  ? 0.7048 0.7107 0.6767 -0.0840 -0.1005 -0.0153 58  LYS H CA  
14370 C C   . LYS H  58  ? 0.7815 0.7833 0.7589 -0.0791 -0.0942 -0.0169 58  LYS H C   
14371 O O   . LYS H  58  ? 0.7371 0.7398 0.7224 -0.0737 -0.0935 -0.0137 58  LYS H O   
14372 C CB  . LYS H  58  ? 0.7196 0.7262 0.6881 -0.0799 -0.1006 -0.0137 58  LYS H CB  
14373 C CG  . LYS H  58  ? 0.8063 0.8182 0.7741 -0.0824 -0.1074 -0.0097 58  LYS H CG  
14374 C CD  . LYS H  58  ? 0.7936 0.8091 0.7640 -0.0885 -0.1127 -0.0082 58  LYS H CD  
14375 C CE  . LYS H  58  ? 0.7131 0.7344 0.6879 -0.0886 -0.1191 -0.0026 58  LYS H CE  
14376 N NZ  . LYS H  58  ? 0.6752 0.7006 0.6543 -0.0939 -0.1241 -0.0005 58  LYS H NZ  
14377 N N   . MET H  59  ? 0.6706 0.6677 0.6437 -0.0810 -0.0894 -0.0216 59  MET H N   
14378 C CA  . MET H  59  ? 0.6638 0.6567 0.6417 -0.0765 -0.0830 -0.0232 59  MET H CA  
14379 C C   . MET H  59  ? 0.7697 0.7627 0.7548 -0.0787 -0.0833 -0.0230 59  MET H C   
14380 O O   . MET H  59  ? 0.8086 0.7983 0.7914 -0.0827 -0.0806 -0.0269 59  MET H O   
14381 C CB  . MET H  59  ? 0.8761 0.8635 0.8469 -0.0769 -0.0769 -0.0281 59  MET H CB  
14382 C CG  . MET H  59  ? 0.7814 0.7645 0.7570 -0.0716 -0.0700 -0.0294 59  MET H CG  
14383 S SD  . MET H  59  ? 0.9663 0.9512 0.9493 -0.0625 -0.0692 -0.0246 59  MET H SD  
14384 C CE  . MET H  59  ? 0.6915 0.6737 0.6678 -0.0582 -0.0643 -0.0265 59  MET H CE  
14385 N N   . ASN H  60  ? 0.8423 0.8388 0.8360 -0.0761 -0.0863 -0.0187 60  ASN H N   
14386 C CA  . ASN H  60  ? 0.9655 0.9622 0.9671 -0.0773 -0.0862 -0.0183 60  ASN H CA  
14387 C C   . ASN H  60  ? 0.9316 0.9255 0.9405 -0.0702 -0.0809 -0.0172 60  ASN H C   
14388 O O   . ASN H  60  ? 0.9779 0.9742 0.9928 -0.0654 -0.0822 -0.0132 60  ASN H O   
14389 C CB  . ASN H  60  ? 1.1213 1.1240 1.1281 -0.0804 -0.0933 -0.0142 60  ASN H CB  
14390 C CG  . ASN H  60  ? 1.3305 1.3337 1.3414 -0.0856 -0.0945 -0.0153 60  ASN H CG  
14391 O OD1 . ASN H  60  ? 1.4755 1.4743 1.4850 -0.0871 -0.0898 -0.0194 60  ASN H OD1 
14392 N ND2 . ASN H  60  ? 1.2760 1.2848 1.2922 -0.0884 -0.1007 -0.0116 60  ASN H ND2 
14393 N N   . THR H  61  ? 0.8410 0.8298 0.8493 -0.0698 -0.0749 -0.0209 61  THR H N   
14394 C CA  . THR H  61  ? 0.8651 0.8507 0.8790 -0.0631 -0.0691 -0.0204 61  THR H CA  
14395 C C   . THR H  61  ? 0.8759 0.8620 0.8995 -0.0627 -0.0692 -0.0187 61  THR H C   
14396 O O   . THR H  61  ? 0.8434 0.8313 0.8689 -0.0683 -0.0724 -0.0192 61  THR H O   
14397 C CB  . THR H  61  ? 0.9900 0.9696 0.9991 -0.0625 -0.0622 -0.0249 61  THR H CB  
14398 O OG1 . THR H  61  ? 0.9114 0.8890 0.9185 -0.0691 -0.0617 -0.0287 61  THR H OG1 
14399 C CG2 . THR H  61  ? 0.8226 0.8015 0.8230 -0.0617 -0.0613 -0.0263 61  THR H CG2 
14400 N N   . GLN H  62  ? 0.8797 0.8645 0.9095 -0.0560 -0.0656 -0.0166 62  GLN H N   
14401 C CA  . GLN H  62  ? 0.9156 0.9004 0.9549 -0.0548 -0.0647 -0.0150 62  GLN H CA  
14402 C C   . GLN H  62  ? 0.9244 0.9040 0.9639 -0.0562 -0.0590 -0.0189 62  GLN H C   
14403 O O   . GLN H  62  ? 0.7871 0.7626 0.8208 -0.0554 -0.0543 -0.0221 62  GLN H O   
14404 C CB  . GLN H  62  ? 0.7963 0.7813 0.8414 -0.0472 -0.0626 -0.0115 62  GLN H CB  
14405 C CG  . GLN H  62  ? 0.7241 0.7140 0.7707 -0.0457 -0.0678 -0.0074 62  GLN H CG  
14406 C CD  . GLN H  62  ? 0.8509 0.8452 0.9038 -0.0495 -0.0736 -0.0047 62  GLN H CD  
14407 O OE1 . GLN H  62  ? 1.0869 1.0835 1.1366 -0.0558 -0.0779 -0.0057 62  GLN H OE1 
14408 N NE2 . GLN H  62  ? 0.7462 0.7418 0.8080 -0.0459 -0.0736 -0.0013 62  GLN H NE2 
14409 N N   . PHE H  63  ? 0.8331 0.8129 0.8798 -0.0582 -0.0593 -0.0186 63  PHE H N   
14410 C CA  . PHE H  63  ? 0.7803 0.7549 0.8286 -0.0588 -0.0534 -0.0220 63  PHE H CA  
14411 C C   . PHE H  63  ? 0.7581 0.7295 0.8110 -0.0510 -0.0475 -0.0205 63  PHE H C   
14412 O O   . PHE H  63  ? 0.9152 0.8883 0.9759 -0.0476 -0.0481 -0.0171 63  PHE H O   
14413 C CB  . PHE H  63  ? 0.7875 0.7636 0.8421 -0.0637 -0.0556 -0.0222 63  PHE H CB  
14414 C CG  . PHE H  63  ? 0.8643 0.8349 0.9202 -0.0651 -0.0495 -0.0260 63  PHE H CG  
14415 C CD1 . PHE H  63  ? 0.6874 0.6563 0.7380 -0.0722 -0.0493 -0.0305 63  PHE H CD1 
14416 C CD2 . PHE H  63  ? 0.8172 0.7842 0.8793 -0.0594 -0.0437 -0.0252 63  PHE H CD2 
14417 C CE1 . PHE H  63  ? 0.7802 0.7437 0.8321 -0.0736 -0.0433 -0.0342 63  PHE H CE1 
14418 C CE2 . PHE H  63  ? 0.7712 0.7330 0.8347 -0.0606 -0.0379 -0.0286 63  PHE H CE2 
14419 C CZ  . PHE H  63  ? 0.8688 0.8288 0.9273 -0.0677 -0.0376 -0.0332 63  PHE H CZ  
14420 N N   . THR H  64  ? 0.6234 0.5904 0.6715 -0.0483 -0.0417 -0.0229 64  THR H N   
14421 C CA  . THR H  64  ? 0.8526 0.8169 0.9041 -0.0408 -0.0362 -0.0212 64  THR H CA  
14422 C C   . THR H  64  ? 0.6793 0.6375 0.7286 -0.0401 -0.0289 -0.0248 64  THR H C   
14423 O O   . THR H  64  ? 0.6426 0.5987 0.6855 -0.0443 -0.0278 -0.0285 64  THR H O   
14424 C CB  . THR H  64  ? 0.8791 0.8457 0.9270 -0.0359 -0.0374 -0.0187 64  THR H CB  
14425 O OG1 . THR H  64  ? 0.8562 0.8210 0.9080 -0.0287 -0.0325 -0.0167 64  THR H OG1 
14426 C CG2 . THR H  64  ? 0.6890 0.6543 0.7275 -0.0375 -0.0365 -0.0216 64  THR H CG2 
14427 N N   . ALA H  65  ? 0.6383 0.5936 0.6933 -0.0349 -0.0236 -0.0236 65  ALA H N   
14428 C CA  . ALA H  65  ? 0.6749 0.6244 0.7287 -0.0334 -0.0161 -0.0264 65  ALA H CA  
14429 C C   . ALA H  65  ? 0.6693 0.6177 0.7215 -0.0261 -0.0121 -0.0245 65  ALA H C   
14430 O O   . ALA H  65  ? 0.5938 0.5414 0.6514 -0.0206 -0.0089 -0.0219 65  ALA H O   
14431 C CB  . ALA H  65  ? 0.6328 0.5792 0.6941 -0.0335 -0.0125 -0.0268 65  ALA H CB  
14432 N N   . VAL H  66  ? 0.6377 0.5864 0.6825 -0.0262 -0.0122 -0.0257 66  VAL H N   
14433 C CA  . VAL H  66  ? 0.5875 0.5355 0.6303 -0.0198 -0.0083 -0.0242 66  VAL H CA  
14434 C C   . VAL H  66  ? 0.7107 0.6535 0.7575 -0.0164 -0.0005 -0.0248 66  VAL H C   
14435 O O   . VAL H  66  ? 0.8612 0.8003 0.9101 -0.0199 0.0021  -0.0274 66  VAL H O   
14436 C CB  . VAL H  66  ? 0.5225 0.4705 0.5567 -0.0214 -0.0086 -0.0264 66  VAL H CB  
14437 C CG1 . VAL H  66  ? 0.6174 0.5666 0.6499 -0.0147 -0.0063 -0.0239 66  VAL H CG1 
14438 C CG2 . VAL H  66  ? 0.5482 0.5003 0.5782 -0.0269 -0.0160 -0.0269 66  VAL H CG2 
14439 N N   . GLY H  67  ? 0.6376 0.5802 0.6855 -0.0095 0.0032  -0.0221 67  GLY H N   
14440 C CA  . GLY H  67  ? 0.8659 0.8038 0.9174 -0.0056 0.0106  -0.0221 67  GLY H CA  
14441 C C   . GLY H  67  ? 0.6745 0.6120 0.7340 -0.0031 0.0117  -0.0196 67  GLY H C   
14442 O O   . GLY H  67  ? 0.4188 0.3564 0.4819 -0.0072 0.0092  -0.0205 67  GLY H O   
14443 N N   . LYS H  68  ? 0.6951 0.6324 0.7575 0.0036  0.0154  -0.0164 68  LYS H N   
14444 C CA  . LYS H  68  ? 0.5628 0.4994 0.6325 0.0067  0.0172  -0.0138 68  LYS H CA  
14445 C C   . LYS H  68  ? 0.6914 0.6237 0.7636 0.0116  0.0251  -0.0130 68  LYS H C   
14446 O O   . LYS H  68  ? 0.6188 0.5496 0.6871 0.0134  0.0286  -0.0138 68  LYS H O   
14447 C CB  . LYS H  68  ? 0.6406 0.5821 0.7117 0.0104  0.0132  -0.0099 68  LYS H CB  
14448 C CG  . LYS H  68  ? 0.5929 0.5389 0.6621 0.0061  0.0055  -0.0101 68  LYS H CG  
14449 C CD  . LYS H  68  ? 0.6963 0.6427 0.7720 0.0034  0.0028  -0.0095 68  LYS H CD  
14450 C CE  . LYS H  68  ? 0.8249 0.7752 0.8989 -0.0022 -0.0045 -0.0103 68  LYS H CE  
14451 N NZ  . LYS H  68  ? 0.8108 0.7591 0.8826 -0.0088 -0.0051 -0.0143 68  LYS H NZ  
14452 N N   . GLU H  69  ? 0.6844 0.6146 0.7633 0.0139  0.0280  -0.0114 69  GLU H N   
14453 C CA  . GLU H  69  ? 0.6567 0.5827 0.7385 0.0186  0.0356  -0.0103 69  GLU H CA  
14454 C C   . GLU H  69  ? 0.5778 0.5059 0.6633 0.0250  0.0366  -0.0056 69  GLU H C   
14455 O O   . GLU H  69  ? 0.6446 0.5744 0.7343 0.0248  0.0337  -0.0040 69  GLU H O   
14456 C CB  . GLU H  69  ? 0.6487 0.5694 0.7353 0.0154  0.0396  -0.0129 69  GLU H CB  
14457 C CG  . GLU H  69  ? 0.8701 0.7881 0.9529 0.0089  0.0397  -0.0178 69  GLU H CG  
14458 C CD  . GLU H  69  ? 0.9996 0.9129 1.0872 0.0051  0.0429  -0.0206 69  GLU H CD  
14459 O OE1 . GLU H  69  ? 0.9772 0.8906 1.0711 0.0061  0.0427  -0.0188 69  GLU H OE1 
14460 O OE2 . GLU H  69  ? 0.9212 0.8306 1.0064 0.0009  0.0458  -0.0246 69  GLU H OE2 
14461 N N   . PHE H  70  ? 0.5194 0.4474 0.6033 0.0305  0.0406  -0.0033 70  PHE H N   
14462 C CA  . PHE H  70  ? 0.5694 0.4994 0.6560 0.0367  0.0420  0.0012  70  PHE H CA  
14463 C C   . PHE H  70  ? 0.6425 0.5686 0.7317 0.0415  0.0497  0.0029  70  PHE H C   
14464 O O   . PHE H  70  ? 0.7337 0.6571 0.8207 0.0413  0.0536  0.0012  70  PHE H O   
14465 C CB  . PHE H  70  ? 0.4995 0.4351 0.5810 0.0392  0.0380  0.0034  70  PHE H CB  
14466 C CG  . PHE H  70  ? 0.6494 0.5888 0.7279 0.0347  0.0306  0.0019  70  PHE H CG  
14467 C CD1 . PHE H  70  ? 0.5340 0.4758 0.6158 0.0342  0.0266  0.0034  70  PHE H CD1 
14468 C CD2 . PHE H  70  ? 0.5729 0.5134 0.6456 0.0312  0.0279  -0.0007 70  PHE H CD2 
14469 C CE1 . PHE H  70  ? 0.5442 0.4896 0.6238 0.0303  0.0200  0.0025  70  PHE H CE1 
14470 C CE2 . PHE H  70  ? 0.4612 0.4053 0.5312 0.0273  0.0211  -0.0017 70  PHE H CE2 
14471 C CZ  . PHE H  70  ? 0.5441 0.4907 0.6178 0.0268  0.0171  0.0000  70  PHE H CZ  
14472 N N   . ASN H  71  ? 0.4743 0.4000 0.5681 0.0456  0.0522  0.0062  71  ASN H N   
14473 C CA  . ASN H  71  ? 0.7178 0.6403 0.8143 0.0507  0.0595  0.0085  71  ASN H CA  
14474 C C   . ASN H  71  ? 0.6466 0.5729 0.7394 0.0562  0.0603  0.0120  71  ASN H C   
14475 O O   . ASN H  71  ? 0.5821 0.5135 0.6705 0.0561  0.0552  0.0126  71  ASN H O   
14476 C CB  . ASN H  71  ? 0.7680 0.6882 0.8712 0.0527  0.0623  0.0105  71  ASN H CB  
14477 C CG  . ASN H  71  ? 0.7269 0.6515 0.8306 0.0551  0.0584  0.0137  71  ASN H CG  
14478 O OD1 . ASN H  71  ? 0.6464 0.5750 0.7466 0.0589  0.0574  0.0165  71  ASN H OD1 
14479 N ND2 . ASN H  71  ? 0.8336 0.7576 0.9418 0.0527  0.0563  0.0132  71  ASN H ND2 
14480 N N   . HIS H  72  ? 0.6446 0.5685 0.7395 0.0609  0.0667  0.0145  72  HIS H N   
14481 C CA  . HIS H  72  ? 0.7496 0.6772 0.8415 0.0662  0.0681  0.0181  72  HIS H CA  
14482 C C   . HIS H  72  ? 0.6854 0.6186 0.7756 0.0691  0.0641  0.0215  72  HIS H C   
14483 O O   . HIS H  72  ? 0.7619 0.6996 0.8481 0.0721  0.0629  0.0238  72  HIS H O   
14484 C CB  . HIS H  72  ? 0.8316 0.7555 0.9272 0.0709  0.0759  0.0207  72  HIS H CB  
14485 C CG  . HIS H  72  ? 1.0741 0.9953 1.1754 0.0731  0.0790  0.0229  72  HIS H CG  
14486 N ND1 . HIS H  72  ? 1.1378 1.0536 1.2439 0.0698  0.0812  0.0202  72  HIS H ND1 
14487 C CD2 . HIS H  72  ? 0.9329 0.8563 1.0360 0.0780  0.0803  0.0274  72  HIS H CD2 
14488 C CE1 . HIS H  72  ? 1.2639 1.1785 1.3746 0.0728  0.0838  0.0231  72  HIS H CE1 
14489 N NE2 . HIS H  72  ? 1.1099 1.0289 1.2187 0.0778  0.0833  0.0275  72  HIS H NE2 
14490 N N   . LEU H  73  ? 0.6654 0.5985 0.7589 0.0681  0.0620  0.0218  73  LEU H N   
14491 C CA  . LEU H  73  ? 0.6588 0.5966 0.7510 0.0704  0.0586  0.0247  73  LEU H CA  
14492 C C   . LEU H  73  ? 0.7791 0.7203 0.8685 0.0660  0.0513  0.0225  73  LEU H C   
14493 O O   . LEU H  73  ? 0.7078 0.6519 0.7974 0.0666  0.0482  0.0240  73  LEU H O   
14494 C CB  . LEU H  73  ? 0.7080 0.6436 0.8057 0.0727  0.0614  0.0271  73  LEU H CB  
14495 C CG  . LEU H  73  ? 0.8170 0.7505 0.9172 0.0782  0.0682  0.0307  73  LEU H CG  
14496 C CD1 . LEU H  73  ? 0.6963 0.6269 0.8023 0.0796  0.0710  0.0324  73  LEU H CD1 
14497 C CD2 . LEU H  73  ? 0.5430 0.4817 0.6387 0.0828  0.0681  0.0344  73  LEU H CD2 
14498 N N   . GLU H  74  ? 0.6731 0.6138 0.7598 0.0616  0.0489  0.0188  74  GLU H N   
14499 C CA  . GLU H  74  ? 0.5425 0.4864 0.6263 0.0573  0.0420  0.0168  74  GLU H CA  
14500 C C   . GLU H  74  ? 0.6587 0.6052 0.7361 0.0560  0.0397  0.0151  74  GLU H C   
14501 O O   . GLU H  74  ? 0.6336 0.5809 0.7086 0.0512  0.0352  0.0122  74  GLU H O   
14502 C CB  . GLU H  74  ? 0.5707 0.5116 0.6581 0.0520  0.0401  0.0136  74  GLU H CB  
14503 C CG  . GLU H  74  ? 0.4959 0.4351 0.5896 0.0530  0.0414  0.0153  74  GLU H CG  
14504 C CD  . GLU H  74  ? 0.7286 0.6649 0.8265 0.0477  0.0400  0.0123  74  GLU H CD  
14505 O OE1 . GLU H  74  ? 0.7086 0.6413 0.8066 0.0449  0.0422  0.0094  74  GLU H OE1 
14506 O OE2 . GLU H  74  ? 0.5572 0.4948 0.6585 0.0464  0.0367  0.0129  74  GLU H OE2 
14507 N N   . LYS H  75  ? 0.5804 0.5283 0.6553 0.0602  0.0428  0.0173  75  LYS H N   
14508 C CA  . LYS H  75  ? 0.6418 0.5923 0.7110 0.0596  0.0412  0.0161  75  LYS H CA  
14509 C C   . LYS H  75  ? 0.6372 0.5930 0.7019 0.0579  0.0346  0.0159  75  LYS H C   
14510 O O   . LYS H  75  ? 0.6512 0.6084 0.7115 0.0550  0.0318  0.0136  75  LYS H O   
14511 C CB  . LYS H  75  ? 0.5853 0.5370 0.6536 0.0651  0.0458  0.0193  75  LYS H CB  
14512 C CG  . LYS H  75  ? 0.6905 0.6453 0.7533 0.0650  0.0446  0.0185  75  LYS H CG  
14513 C CD  . LYS H  75  ? 0.8138 0.7648 0.8754 0.0605  0.0452  0.0142  75  LYS H CD  
14514 C CE  . LYS H  75  ? 1.0341 0.9799 1.0991 0.0623  0.0524  0.0143  75  LYS H CE  
14515 N NZ  . LYS H  75  ? 1.1776 1.1195 1.2410 0.0576  0.0533  0.0098  75  LYS H NZ  
14516 N N   . ARG H  76  ? 0.6366 0.5951 0.7025 0.0595  0.0323  0.0182  76  ARG H N   
14517 C CA  . ARG H  76  ? 0.5108 0.4741 0.5729 0.0580  0.0265  0.0181  76  ARG H CA  
14518 C C   . ARG H  76  ? 0.5865 0.5491 0.6484 0.0521  0.0217  0.0148  76  ARG H C   
14519 O O   . ARG H  76  ? 0.5222 0.4871 0.5793 0.0496  0.0179  0.0131  76  ARG H O   
14520 C CB  . ARG H  76  ? 0.4607 0.4266 0.5245 0.0609  0.0257  0.0212  76  ARG H CB  
14521 C CG  . ARG H  76  ? 0.4410 0.4104 0.5020 0.0660  0.0278  0.0245  76  ARG H CG  
14522 C CD  . ARG H  76  ? 0.5267 0.4979 0.5896 0.0684  0.0276  0.0272  76  ARG H CD  
14523 N NE  . ARG H  76  ? 0.5640 0.5308 0.6330 0.0684  0.0302  0.0276  76  ARG H NE  
14524 C CZ  . ARG H  76  ? 0.5142 0.4810 0.5863 0.0682  0.0290  0.0285  76  ARG H CZ  
14525 N NH1 . ARG H  76  ? 0.5946 0.5653 0.6640 0.0679  0.0253  0.0291  76  ARG H NH1 
14526 N NH2 . ARG H  76  ? 0.5366 0.4993 0.6145 0.0682  0.0317  0.0287  76  ARG H NH2 
14527 N N   . ILE H  77  ? 0.5962 0.5556 0.6632 0.0498  0.0217  0.0139  77  ILE H N   
14528 C CA  . ILE H  77  ? 0.4708 0.4296 0.5380 0.0441  0.0172  0.0111  77  ILE H CA  
14529 C C   . ILE H  77  ? 0.4479 0.4044 0.5121 0.0406  0.0178  0.0077  77  ILE H C   
14530 O O   . ILE H  77  ? 0.4498 0.4073 0.5113 0.0359  0.0133  0.0053  77  ILE H O   
14531 C CB  . ILE H  77  ? 0.4677 0.4239 0.5416 0.0424  0.0172  0.0110  77  ILE H CB  
14532 C CG1 . ILE H  77  ? 0.7316 0.6834 0.8099 0.0451  0.0236  0.0118  77  ILE H CG1 
14533 C CG2 . ILE H  77  ? 0.4991 0.4584 0.5752 0.0437  0.0143  0.0135  77  ILE H CG2 
14534 C CD1 . ILE H  77  ? 0.7475 0.6968 0.8327 0.0437  0.0241  0.0119  77  ILE H CD1 
14535 N N   . GLU H  78  ? 0.4301 0.3834 0.4948 0.0427  0.0234  0.0075  78  GLU H N   
14536 C CA  . GLU H  78  ? 0.5343 0.4850 0.5959 0.0397  0.0248  0.0043  78  GLU H CA  
14537 C C   . GLU H  78  ? 0.5601 0.5147 0.6152 0.0394  0.0219  0.0038  78  GLU H C   
14538 O O   . GLU H  78  ? 0.5750 0.5290 0.6264 0.0349  0.0196  0.0007  78  GLU H O   
14539 C CB  . GLU H  78  ? 0.5665 0.5132 0.6304 0.0428  0.0321  0.0047  78  GLU H CB  
14540 C CG  . GLU H  78  ? 0.6000 0.5436 0.6608 0.0399  0.0343  0.0013  78  GLU H CG  
14541 C CD  . GLU H  78  ? 1.0220 0.9616 1.0852 0.0434  0.0418  0.0020  78  GLU H CD  
14542 O OE1 . GLU H  78  ? 1.1513 1.0891 1.2197 0.0467  0.0455  0.0044  78  GLU H OE1 
14543 O OE2 . GLU H  78  ? 1.0889 1.0271 1.1491 0.0429  0.0443  0.0004  78  GLU H OE2 
14544 N N   . ASN H  79  ? 0.4560 0.4144 0.5093 0.0439  0.0219  0.0068  79  ASN H N   
14545 C CA  . ASN H  79  ? 0.4633 0.4257 0.5106 0.0440  0.0191  0.0066  79  ASN H CA  
14546 C C   . ASN H  79  ? 0.5164 0.4823 0.5614 0.0405  0.0123  0.0058  79  ASN H C   
14547 O O   . ASN H  79  ? 0.5441 0.5117 0.5842 0.0379  0.0093  0.0040  79  ASN H O   
14548 C CB  . ASN H  79  ? 0.5641 0.5299 0.6105 0.0499  0.0214  0.0102  79  ASN H CB  
14549 C CG  . ASN H  79  ? 0.7739 0.7373 0.8210 0.0530  0.0276  0.0108  79  ASN H CG  
14550 O OD1 . ASN H  79  ? 0.7573 0.7174 0.8034 0.0505  0.0295  0.0081  79  ASN H OD1 
14551 N ND2 . ASN H  79  ? 0.6057 0.5708 0.6546 0.0584  0.0309  0.0145  79  ASN H ND2 
14552 N N   . LEU H  80  ? 0.4986 0.4652 0.5473 0.0406  0.0102  0.0073  80  LEU H N   
14553 C CA  . LEU H  80  ? 0.4182 0.3874 0.4659 0.0371  0.0041  0.0067  80  LEU H CA  
14554 C C   . LEU H  80  ? 0.4409 0.4080 0.4874 0.0312  0.0017  0.0032  80  LEU H C   
14555 O O   . LEU H  80  ? 0.4663 0.4357 0.5087 0.0280  -0.0027 0.0019  80  LEU H O   
14556 C CB  . LEU H  80  ? 0.3892 0.3586 0.4423 0.0380  0.0031  0.0088  80  LEU H CB  
14557 C CG  . LEU H  80  ? 0.4209 0.3925 0.4747 0.0342  -0.0028 0.0083  80  LEU H CG  
14558 C CD1 . LEU H  80  ? 0.3676 0.3433 0.4157 0.0334  -0.0069 0.0081  80  LEU H CD1 
14559 C CD2 . LEU H  80  ? 0.3383 0.3102 0.3978 0.0361  -0.0030 0.0108  80  LEU H CD2 
14560 N N   . ASN H  81  ? 0.3999 0.3627 0.4502 0.0296  0.0046  0.0018  81  ASN H N   
14561 C CA  . ASN H  81  ? 0.4198 0.3802 0.4690 0.0238  0.0030  -0.0017 81  ASN H CA  
14562 C C   . ASN H  81  ? 0.5562 0.5164 0.5990 0.0221  0.0034  -0.0040 81  ASN H C   
14563 O O   . ASN H  81  ? 0.6513 0.6124 0.6903 0.0174  -0.0006 -0.0063 81  ASN H O   
14564 C CB  . ASN H  81  ? 0.4249 0.3804 0.4791 0.0228  0.0071  -0.0028 81  ASN H CB  
14565 C CG  . ASN H  81  ? 0.6101 0.5632 0.6629 0.0165  0.0058  -0.0067 81  ASN H CG  
14566 O OD1 . ASN H  81  ? 0.6944 0.6493 0.7473 0.0121  0.0005  -0.0075 81  ASN H OD1 
14567 N ND2 . ASN H  81  ? 0.6283 0.5773 0.6798 0.0158  0.0106  -0.0090 81  ASN H ND2 
14568 N N   . LYS H  82  ? 0.4924 0.4515 0.5340 0.0261  0.0084  -0.0034 82  LYS H N   
14569 C CA  . LYS H  82  ? 0.5192 0.4782 0.5551 0.0252  0.0094  -0.0054 82  LYS H CA  
14570 C C   . LYS H  82  ? 0.5568 0.5208 0.5876 0.0245  0.0041  -0.0050 82  LYS H C   
14571 O O   . LYS H  82  ? 0.4549 0.4190 0.4806 0.0213  0.0027  -0.0074 82  LYS H O   
14572 C CB  . LYS H  82  ? 0.6111 0.5688 0.6475 0.0304  0.0157  -0.0039 82  LYS H CB  
14573 C CG  . LYS H  82  ? 0.7438 0.7023 0.7748 0.0304  0.0167  -0.0052 82  LYS H CG  
14574 C CD  . LYS H  82  ? 0.8183 0.7757 0.8507 0.0357  0.0231  -0.0033 82  LYS H CD  
14575 C CE  . LYS H  82  ? 1.1282 1.0875 1.1556 0.0363  0.0237  -0.0040 82  LYS H CE  
14576 N NZ  . LYS H  82  ? 1.0171 0.9735 1.0405 0.0306  0.0229  -0.0084 82  LYS H NZ  
14577 N N   . LYS H  83  ? 0.6351 0.6028 0.6672 0.0272  0.0015  -0.0021 83  LYS H N   
14578 C CA  . LYS H  83  ? 0.4969 0.4693 0.5246 0.0267  -0.0032 -0.0015 83  LYS H CA  
14579 C C   . LYS H  83  ? 0.4772 0.4502 0.5031 0.0210  -0.0089 -0.0035 83  LYS H C   
14580 O O   . LYS H  83  ? 0.4698 0.4448 0.4904 0.0187  -0.0117 -0.0047 83  LYS H O   
14581 C CB  . LYS H  83  ? 0.3587 0.3347 0.3883 0.0311  -0.0040 0.0020  83  LYS H CB  
14582 C CG  . LYS H  83  ? 0.3599 0.3405 0.3848 0.0308  -0.0083 0.0024  83  LYS H CG  
14583 C CD  . LYS H  83  ? 0.3704 0.3546 0.3961 0.0355  -0.0079 0.0056  83  LYS H CD  
14584 C CE  . LYS H  83  ? 0.4558 0.4400 0.4865 0.0357  -0.0095 0.0073  83  LYS H CE  
14585 N NZ  . LYS H  83  ? 0.5632 0.5512 0.5934 0.0391  -0.0101 0.0099  83  LYS H NZ  
14586 N N   . VAL H  84  ? 0.3330 0.3046 0.3634 0.0186  -0.0105 -0.0035 84  VAL H N   
14587 C CA  . VAL H  84  ? 0.4980 0.4706 0.5274 0.0130  -0.0159 -0.0050 84  VAL H CA  
14588 C C   . VAL H  84  ? 0.4703 0.4405 0.4949 0.0084  -0.0156 -0.0086 84  VAL H C   
14589 O O   . VAL H  84  ? 0.5604 0.5324 0.5802 0.0048  -0.0197 -0.0099 84  VAL H O   
14590 C CB  . VAL H  84  ? 0.4124 0.3838 0.4483 0.0111  -0.0172 -0.0044 84  VAL H CB  
14591 C CG1 . VAL H  84  ? 0.5615 0.5367 0.5992 0.0106  -0.0225 -0.0022 84  VAL H CG1 
14592 C CG2 . VAL H  84  ? 0.6136 0.5824 0.6548 0.0154  -0.0120 -0.0029 84  VAL H CG2 
14593 N N   . ASP H  85  ? 0.4182 0.3842 0.4438 0.0088  -0.0104 -0.0102 85  ASP H N   
14594 C CA  . ASP H  85  ? 0.4459 0.4089 0.4672 0.0046  -0.0090 -0.0140 85  ASP H CA  
14595 C C   . ASP H  85  ? 0.5149 0.4795 0.5297 0.0051  -0.0090 -0.0148 85  ASP H C   
14596 O O   . ASP H  85  ? 0.5242 0.4887 0.5339 0.0004  -0.0116 -0.0173 85  ASP H O   
14597 C CB  . ASP H  85  ? 0.4518 0.4097 0.4764 0.0055  -0.0026 -0.0153 85  ASP H CB  
14598 C CG  . ASP H  85  ? 0.6931 0.6489 0.7233 0.0029  -0.0031 -0.0156 85  ASP H CG  
14599 O OD1 . ASP H  85  ? 0.6182 0.5765 0.6492 -0.0005 -0.0086 -0.0153 85  ASP H OD1 
14600 O OD2 . ASP H  85  ? 0.8365 0.7883 0.8705 0.0041  0.0021  -0.0162 85  ASP H OD2 
14601 N N   . ASP H  86  ? 0.4399 0.4059 0.4547 0.0107  -0.0062 -0.0126 86  ASP H N   
14602 C CA  . ASP H  86  ? 0.4086 0.3767 0.4178 0.0118  -0.0060 -0.0130 86  ASP H CA  
14603 C C   . ASP H  86  ? 0.6081 0.5807 0.6137 0.0102  -0.0122 -0.0123 86  ASP H C   
14604 O O   . ASP H  86  ? 0.5593 0.5333 0.5594 0.0087  -0.0134 -0.0137 86  ASP H O   
14605 C CB  . ASP H  86  ? 0.6693 0.6382 0.6800 0.0183  -0.0013 -0.0106 86  ASP H CB  
14606 C CG  . ASP H  86  ? 0.9227 0.8868 0.9356 0.0196  0.0054  -0.0116 86  ASP H CG  
14607 O OD1 . ASP H  86  ? 0.9254 0.8855 0.9375 0.0151  0.0065  -0.0149 86  ASP H OD1 
14608 O OD2 . ASP H  86  ? 0.9896 0.9541 1.0052 0.0250  0.0096  -0.0092 86  ASP H OD2 
14609 N N   . GLY H  87  ? 0.5645 0.5395 0.5736 0.0106  -0.0157 -0.0101 87  GLY H N   
14610 C CA  . GLY H  87  ? 0.4213 0.4003 0.4278 0.0091  -0.0215 -0.0092 87  GLY H CA  
14611 C C   . GLY H  87  ? 0.4536 0.4321 0.4568 0.0026  -0.0256 -0.0117 87  GLY H C   
14612 O O   . GLY H  87  ? 0.5200 0.5004 0.5177 0.0006  -0.0282 -0.0127 87  GLY H O   
14613 N N   . PHE H  88  ? 0.4501 0.4262 0.4565 -0.0007 -0.0262 -0.0127 88  PHE H N   
14614 C CA  . PHE H  88  ? 0.4957 0.4714 0.4992 -0.0072 -0.0301 -0.0150 88  PHE H CA  
14615 C C   . PHE H  88  ? 0.5145 0.4879 0.5116 -0.0099 -0.0280 -0.0184 88  PHE H C   
14616 O O   . PHE H  88  ? 0.4614 0.4357 0.4534 -0.0145 -0.0315 -0.0200 88  PHE H O   
14617 C CB  . PHE H  88  ? 0.4023 0.3758 0.4109 -0.0102 -0.0304 -0.0155 88  PHE H CB  
14618 C CG  . PHE H  88  ? 0.4364 0.4123 0.4514 -0.0086 -0.0332 -0.0123 88  PHE H CG  
14619 C CD1 . PHE H  88  ? 0.4307 0.4047 0.4521 -0.0091 -0.0319 -0.0120 88  PHE H CD1 
14620 C CD2 . PHE H  88  ? 0.4468 0.4269 0.4617 -0.0069 -0.0370 -0.0097 88  PHE H CD2 
14621 C CE1 . PHE H  88  ? 0.4446 0.4206 0.4721 -0.0076 -0.0343 -0.0090 88  PHE H CE1 
14622 C CE2 . PHE H  88  ? 0.4483 0.4303 0.4693 -0.0055 -0.0392 -0.0068 88  PHE H CE2 
14623 C CZ  . PHE H  88  ? 0.4355 0.4156 0.4629 -0.0058 -0.0379 -0.0064 88  PHE H CZ  
14624 N N   . LEU H  89  ? 0.5029 0.4732 0.5003 -0.0070 -0.0219 -0.0194 89  LEU H N   
14625 C CA  . LEU H  89  ? 0.4829 0.4505 0.4749 -0.0090 -0.0188 -0.0226 89  LEU H CA  
14626 C C   . LEU H  89  ? 0.5557 0.5264 0.5418 -0.0083 -0.0208 -0.0224 89  LEU H C   
14627 O O   . LEU H  89  ? 0.5675 0.5374 0.5478 -0.0125 -0.0220 -0.0250 89  LEU H O   
14628 C CB  . LEU H  89  ? 0.4344 0.3983 0.4289 -0.0051 -0.0116 -0.0229 89  LEU H CB  
14629 C CG  . LEU H  89  ? 0.5342 0.4951 0.5240 -0.0062 -0.0073 -0.0259 89  LEU H CG  
14630 C CD1 . LEU H  89  ? 0.5758 0.5341 0.5611 -0.0136 -0.0090 -0.0299 89  LEU H CD1 
14631 C CD2 . LEU H  89  ? 0.5014 0.4586 0.4951 -0.0023 0.0000  -0.0258 89  LEU H CD2 
14632 N N   . ASP H  90  ? 0.5030 0.4771 0.4906 -0.0031 -0.0211 -0.0193 90  ASP H N   
14633 C CA  . ASP H  90  ? 0.4549 0.4324 0.4377 -0.0020 -0.0227 -0.0189 90  ASP H CA  
14634 C C   . ASP H  90  ? 0.4676 0.4479 0.4470 -0.0061 -0.0293 -0.0189 90  ASP H C   
14635 O O   . ASP H  90  ? 0.5131 0.4944 0.4868 -0.0083 -0.0308 -0.0203 90  ASP H O   
14636 C CB  . ASP H  90  ? 0.4609 0.4415 0.4463 0.0044  -0.0212 -0.0156 90  ASP H CB  
14637 C CG  . ASP H  90  ? 0.7459 0.7245 0.7328 0.0087  -0.0147 -0.0155 90  ASP H CG  
14638 O OD1 . ASP H  90  ? 0.8908 0.8660 0.8755 0.0067  -0.0115 -0.0182 90  ASP H OD1 
14639 O OD2 . ASP H  90  ? 0.8077 0.7883 0.7982 0.0139  -0.0129 -0.0127 90  ASP H OD2 
14640 N N   . ILE H  91  ? 0.4631 0.4447 0.4465 -0.0071 -0.0330 -0.0172 91  ILE H N   
14641 C CA  . ILE H  91  ? 0.4716 0.4561 0.4529 -0.0109 -0.0392 -0.0166 91  ILE H CA  
14642 C C   . ILE H  91  ? 0.5518 0.5344 0.5283 -0.0174 -0.0410 -0.0197 91  ILE H C   
14643 O O   . ILE H  91  ? 0.5536 0.5376 0.5244 -0.0201 -0.0439 -0.0206 91  ILE H O   
14644 C CB  . ILE H  91  ? 0.4139 0.3999 0.4015 -0.0108 -0.0423 -0.0140 91  ILE H CB  
14645 C CG1 . ILE H  91  ? 0.4941 0.4824 0.4859 -0.0048 -0.0410 -0.0109 91  ILE H CG1 
14646 C CG2 . ILE H  91  ? 0.5106 0.4992 0.4964 -0.0152 -0.0486 -0.0134 91  ILE H CG2 
14647 C CD1 . ILE H  91  ? 0.6365 0.6259 0.6348 -0.0043 -0.0434 -0.0083 91  ILE H CD1 
14648 N N   . TRP H  92  ? 0.4544 0.4336 0.4329 -0.0201 -0.0393 -0.0215 92  TRP H N   
14649 C CA  . TRP H  92  ? 0.3784 0.3557 0.3525 -0.0268 -0.0410 -0.0246 92  TRP H CA  
14650 C C   . TRP H  92  ? 0.4832 0.4583 0.4501 -0.0283 -0.0381 -0.0278 92  TRP H C   
14651 O O   . TRP H  92  ? 0.5622 0.5376 0.5232 -0.0333 -0.0411 -0.0296 92  TRP H O   
14652 C CB  . TRP H  92  ? 0.3921 0.3661 0.3702 -0.0293 -0.0393 -0.0260 92  TRP H CB  
14653 C CG  . TRP H  92  ? 0.5109 0.4874 0.4946 -0.0304 -0.0437 -0.0235 92  TRP H CG  
14654 C CD1 . TRP H  92  ? 0.4472 0.4234 0.4384 -0.0272 -0.0423 -0.0214 92  TRP H CD1 
14655 C CD2 . TRP H  92  ? 0.5131 0.4928 0.4955 -0.0350 -0.0503 -0.0225 92  TRP H CD2 
14656 N NE1 . TRP H  92  ? 0.5427 0.5218 0.5378 -0.0295 -0.0475 -0.0193 92  TRP H NE1 
14657 C CE2 . TRP H  92  ? 0.4386 0.4200 0.4285 -0.0342 -0.0525 -0.0198 92  TRP H CE2 
14658 C CE3 . TRP H  92  ? 0.5238 0.5053 0.4997 -0.0396 -0.0544 -0.0235 92  TRP H CE3 
14659 C CZ2 . TRP H  92  ? 0.4796 0.4644 0.4709 -0.0379 -0.0588 -0.0179 92  TRP H CZ2 
14660 C CZ3 . TRP H  92  ? 0.5854 0.5703 0.5624 -0.0432 -0.0607 -0.0216 92  TRP H CZ3 
14661 C CH2 . TRP H  92  ? 0.6398 0.6265 0.6247 -0.0423 -0.0628 -0.0187 92  TRP H CH2 
14662 N N   . THR H  93  ? 0.5759 0.5488 0.5435 -0.0240 -0.0323 -0.0283 93  THR H N   
14663 C CA  . THR H  93  ? 0.5346 0.5055 0.4963 -0.0248 -0.0289 -0.0310 93  THR H CA  
14664 C C   . THR H  93  ? 0.5228 0.4974 0.4794 -0.0248 -0.0325 -0.0303 93  THR H C   
14665 O O   . THR H  93  ? 0.5663 0.5403 0.5166 -0.0292 -0.0338 -0.0327 93  THR H O   
14666 C CB  . THR H  93  ? 0.5080 0.4768 0.4724 -0.0193 -0.0221 -0.0308 93  THR H CB  
14667 O OG1 . THR H  93  ? 0.4637 0.4284 0.4325 -0.0196 -0.0183 -0.0319 93  THR H OG1 
14668 C CG2 . THR H  93  ? 0.4666 0.4337 0.4254 -0.0199 -0.0187 -0.0334 93  THR H CG2 
14669 N N   . TYR H  94  ? 0.5756 0.5541 0.5350 -0.0200 -0.0340 -0.0269 94  TYR H N   
14670 C CA  . TYR H  94  ? 0.4904 0.4725 0.4455 -0.0195 -0.0370 -0.0260 94  TYR H CA  
14671 C C   . TYR H  94  ? 0.4981 0.4818 0.4497 -0.0251 -0.0431 -0.0263 94  TYR H C   
14672 O O   . TYR H  94  ? 0.4451 0.4293 0.3905 -0.0279 -0.0446 -0.0278 94  TYR H O   
14673 C CB  . TYR H  94  ? 0.4153 0.4012 0.3745 -0.0137 -0.0374 -0.0225 94  TYR H CB  
14674 C CG  . TYR H  94  ? 0.4887 0.4782 0.4438 -0.0127 -0.0396 -0.0217 94  TYR H CG  
14675 C CD1 . TYR H  94  ? 0.5019 0.4914 0.4537 -0.0107 -0.0361 -0.0229 94  TYR H CD1 
14676 C CD2 . TYR H  94  ? 0.5393 0.5322 0.4943 -0.0137 -0.0449 -0.0198 94  TYR H CD2 
14677 C CE1 . TYR H  94  ? 0.6284 0.6212 0.5765 -0.0099 -0.0380 -0.0223 94  TYR H CE1 
14678 C CE2 . TYR H  94  ? 0.5601 0.5561 0.5114 -0.0129 -0.0466 -0.0192 94  TYR H CE2 
14679 C CZ  . TYR H  94  ? 0.6818 0.6778 0.6295 -0.0110 -0.0432 -0.0206 94  TYR H CZ  
14680 O OH  . TYR H  94  ? 0.7119 0.7111 0.6561 -0.0103 -0.0449 -0.0201 94  TYR H OH  
14681 N N   . ASN H  95  ? 0.5612 0.5459 0.5170 -0.0266 -0.0467 -0.0246 95  ASN H N   
14682 C CA  . ASN H  95  ? 0.5514 0.5382 0.5048 -0.0316 -0.0528 -0.0242 95  ASN H CA  
14683 C C   . ASN H  95  ? 0.6134 0.5976 0.5608 -0.0381 -0.0533 -0.0277 95  ASN H C   
14684 O O   . ASN H  95  ? 0.6021 0.5878 0.5440 -0.0418 -0.0569 -0.0281 95  ASN H O   
14685 C CB  . ASN H  95  ? 0.4690 0.4574 0.4292 -0.0317 -0.0560 -0.0215 95  ASN H CB  
14686 C CG  . ASN H  95  ? 0.7108 0.7023 0.6758 -0.0264 -0.0569 -0.0179 95  ASN H CG  
14687 O OD1 . ASN H  95  ? 0.7059 0.6982 0.6700 -0.0220 -0.0542 -0.0174 95  ASN H OD1 
14688 N ND2 . ASN H  95  ? 0.7399 0.7334 0.7102 -0.0268 -0.0605 -0.0152 95  ASN H ND2 
14689 N N   . ALA H  96  ? 0.5487 0.5289 0.4970 -0.0396 -0.0494 -0.0302 96  ALA H N   
14690 C CA  . ALA H  96  ? 0.5337 0.5110 0.4762 -0.0460 -0.0492 -0.0339 96  ALA H CA  
14691 C C   . ALA H  96  ? 0.6536 0.6296 0.5887 -0.0468 -0.0470 -0.0364 96  ALA H C   
14692 O O   . ALA H  96  ? 0.6586 0.6345 0.5871 -0.0521 -0.0496 -0.0382 96  ALA H O   
14693 C CB  . ALA H  96  ? 0.5587 0.5316 0.5042 -0.0469 -0.0447 -0.0362 96  ALA H CB  
14694 N N   . GLU H  97  ? 0.5014 0.4765 0.4376 -0.0414 -0.0420 -0.0363 97  GLU H N   
14695 C CA  . GLU H  97  ? 0.5694 0.5435 0.4995 -0.0413 -0.0394 -0.0384 97  GLU H CA  
14696 C C   . GLU H  97  ? 0.5733 0.5514 0.4990 -0.0425 -0.0445 -0.0370 97  GLU H C   
14697 O O   . GLU H  97  ? 0.5539 0.5310 0.4726 -0.0467 -0.0452 -0.0394 97  GLU H O   
14698 C CB  . GLU H  97  ? 0.6999 0.6735 0.6333 -0.0347 -0.0337 -0.0376 97  GLU H CB  
14699 C CG  . GLU H  97  ? 0.6164 0.5855 0.5535 -0.0334 -0.0276 -0.0392 97  GLU H CG  
14700 C CD  . GLU H  97  ? 0.7960 0.7604 0.7279 -0.0373 -0.0234 -0.0436 97  GLU H CD  
14701 O OE1 . GLU H  97  ? 0.8369 0.7974 0.7714 -0.0355 -0.0173 -0.0449 97  GLU H OE1 
14702 O OE2 . GLU H  97  ? 1.0167 0.9810 0.9417 -0.0423 -0.0260 -0.0456 97  GLU H OE2 
14703 N N   . LEU H  98  ? 0.5600 0.5422 0.4897 -0.0389 -0.0478 -0.0333 98  LEU H N   
14704 C CA  . LEU H  98  ? 0.5382 0.5242 0.4646 -0.0396 -0.0524 -0.0317 98  LEU H CA  
14705 C C   . LEU H  98  ? 0.6171 0.6039 0.5400 -0.0460 -0.0580 -0.0319 98  LEU H C   
14706 O O   . LEU H  98  ? 0.5992 0.5872 0.5162 -0.0488 -0.0606 -0.0324 98  LEU H O   
14707 C CB  . LEU H  98  ? 0.5097 0.4996 0.4418 -0.0343 -0.0542 -0.0278 98  LEU H CB  
14708 C CG  . LEU H  98  ? 0.5877 0.5793 0.5201 -0.0287 -0.0511 -0.0269 98  LEU H CG  
14709 C CD1 . LEU H  98  ? 0.7880 0.7818 0.7146 -0.0300 -0.0535 -0.0271 98  LEU H CD1 
14710 C CD2 . LEU H  98  ? 0.6543 0.6427 0.5869 -0.0263 -0.0447 -0.0290 98  LEU H CD2 
14711 N N   . LEU H  99  ? 0.6332 0.6195 0.5598 -0.0484 -0.0598 -0.0314 99  LEU H N   
14712 C CA  . LEU H  99  ? 0.7380 0.7254 0.6619 -0.0546 -0.0653 -0.0312 99  LEU H CA  
14713 C C   . LEU H  99  ? 0.6138 0.5987 0.5290 -0.0604 -0.0648 -0.0350 99  LEU H C   
14714 O O   . LEU H  99  ? 0.7041 0.6909 0.6142 -0.0644 -0.0691 -0.0347 99  LEU H O   
14715 C CB  . LEU H  99  ? 0.6594 0.6466 0.5892 -0.0562 -0.0666 -0.0304 99  LEU H CB  
14716 C CG  . LEU H  99  ? 0.6745 0.6635 0.6023 -0.0627 -0.0726 -0.0298 99  LEU H CG  
14717 C CD1 . LEU H  99  ? 0.6768 0.6705 0.6056 -0.0620 -0.0782 -0.0259 99  LEU H CD1 
14718 C CD2 . LEU H  99  ? 0.6399 0.6284 0.5736 -0.0644 -0.0731 -0.0295 99  LEU H CD2 
14719 N N   . VAL H  100 ? 0.5029 0.4833 0.4166 -0.0609 -0.0592 -0.0386 100 VAL H N   
14720 C CA  . VAL H  100 ? 0.6391 0.6164 0.5447 -0.0664 -0.0577 -0.0427 100 VAL H CA  
14721 C C   . VAL H  100 ? 0.6565 0.6347 0.5562 -0.0657 -0.0575 -0.0431 100 VAL H C   
14722 O O   . VAL H  100 ? 0.8567 0.8351 0.7493 -0.0709 -0.0602 -0.0444 100 VAL H O   
14723 C CB  . VAL H  100 ? 0.6515 0.6234 0.5574 -0.0664 -0.0508 -0.0463 100 VAL H CB  
14724 C CG1 . VAL H  100 ? 0.5804 0.5489 0.4777 -0.0713 -0.0482 -0.0507 100 VAL H CG1 
14725 C CG2 . VAL H  100 ? 0.6473 0.6179 0.5577 -0.0688 -0.0511 -0.0467 100 VAL H CG2 
14726 N N   . LEU H  101 ? 0.6320 0.6109 0.5345 -0.0593 -0.0542 -0.0419 101 LEU H N   
14727 C CA  . LEU H  101 ? 0.6495 0.6296 0.5472 -0.0581 -0.0538 -0.0422 101 LEU H CA  
14728 C C   . LEU H  101 ? 0.6644 0.6484 0.5593 -0.0605 -0.0603 -0.0398 101 LEU H C   
14729 O O   . LEU H  101 ? 0.6974 0.6811 0.5850 -0.0646 -0.0618 -0.0414 101 LEU H O   
14730 C CB  . LEU H  101 ? 0.5486 0.5299 0.4508 -0.0507 -0.0501 -0.0405 101 LEU H CB  
14731 C CG  . LEU H  101 ? 0.5867 0.5644 0.4916 -0.0476 -0.0431 -0.0425 101 LEU H CG  
14732 C CD1 . LEU H  101 ? 0.6048 0.5847 0.5131 -0.0406 -0.0403 -0.0405 101 LEU H CD1 
14733 C CD2 . LEU H  101 ? 0.5450 0.5182 0.4434 -0.0519 -0.0394 -0.0469 101 LEU H CD2 
14734 N N   . LEU H  102 ? 0.6306 0.6182 0.5313 -0.0578 -0.0641 -0.0360 102 LEU H N   
14735 C CA  . LEU H  102 ? 0.6240 0.6155 0.5234 -0.0594 -0.0701 -0.0332 102 LEU H CA  
14736 C C   . LEU H  102 ? 0.6655 0.6568 0.5594 -0.0668 -0.0742 -0.0341 102 LEU H C   
14737 O O   . LEU H  102 ? 0.6535 0.6461 0.5417 -0.0696 -0.0771 -0.0339 102 LEU H O   
14738 C CB  . LEU H  102 ? 0.6652 0.6600 0.5726 -0.0557 -0.0729 -0.0290 102 LEU H CB  
14739 C CG  . LEU H  102 ? 0.8168 0.8128 0.7297 -0.0485 -0.0698 -0.0274 102 LEU H CG  
14740 C CD1 . LEU H  102 ? 1.0936 1.0931 1.0130 -0.0459 -0.0734 -0.0232 102 LEU H CD1 
14741 C CD2 . LEU H  102 ? 0.8006 0.7971 0.7091 -0.0462 -0.0675 -0.0283 102 LEU H CD2 
14742 N N   . GLU H  103 ? 0.6395 0.6291 0.5351 -0.0700 -0.0745 -0.0351 103 GLU H N   
14743 C CA  . GLU H  103 ? 0.6956 0.6855 0.5864 -0.0773 -0.0787 -0.0359 103 GLU H CA  
14744 C C   . GLU H  103 ? 0.5817 0.5684 0.4628 -0.0822 -0.0767 -0.0401 103 GLU H C   
14745 O O   . GLU H  103 ? 0.7851 0.7732 0.6602 -0.0874 -0.0808 -0.0400 103 GLU H O   
14746 C CB  . GLU H  103 ? 0.6089 0.5979 0.5042 -0.0796 -0.0793 -0.0361 103 GLU H CB  
14747 C CG  . GLU H  103 ? 0.9176 0.9104 0.8215 -0.0768 -0.0831 -0.0316 103 GLU H CG  
14748 C CD  . GLU H  103 ? 1.0215 1.0188 0.9246 -0.0778 -0.0893 -0.0278 103 GLU H CD  
14749 O OE1 . GLU H  103 ? 1.0072 1.0063 0.9072 -0.0836 -0.0940 -0.0272 103 GLU H OE1 
14750 O OE2 . GLU H  103 ? 1.0319 1.0312 0.9378 -0.0728 -0.0893 -0.0253 103 GLU H OE2 
14751 N N   . ASN H  104 ? 0.5022 0.4847 0.3819 -0.0805 -0.0702 -0.0436 104 ASN H N   
14752 C CA  . ASN H  104 ? 0.6462 0.6253 0.5171 -0.0847 -0.0674 -0.0477 104 ASN H CA  
14753 C C   . ASN H  104 ? 0.7476 0.7288 0.6133 -0.0845 -0.0694 -0.0468 104 ASN H C   
14754 O O   . ASN H  104 ? 0.7609 0.7413 0.6186 -0.0900 -0.0709 -0.0486 104 ASN H O   
14755 C CB  . ASN H  104 ? 0.5413 0.5157 0.4130 -0.0819 -0.0596 -0.0511 104 ASN H CB  
14756 C CG  . ASN H  104 ? 0.6698 0.6408 0.5437 -0.0846 -0.0570 -0.0535 104 ASN H CG  
14757 O OD1 . ASN H  104 ? 0.7452 0.7171 0.6186 -0.0894 -0.0611 -0.0532 104 ASN H OD1 
14758 N ND2 . ASN H  104 ? 0.6826 0.6496 0.5589 -0.0815 -0.0502 -0.0558 104 ASN H ND2 
14759 N N   . GLU H  105 ? 0.6505 0.6345 0.5208 -0.0782 -0.0693 -0.0439 105 GLU H N   
14760 C CA  . GLU H  105 ? 0.6970 0.6833 0.5633 -0.0776 -0.0713 -0.0427 105 GLU H CA  
14761 C C   . GLU H  105 ? 0.7276 0.7170 0.5909 -0.0823 -0.0782 -0.0403 105 GLU H C   
14762 O O   . GLU H  105 ? 0.8367 0.8263 0.6929 -0.0857 -0.0798 -0.0410 105 GLU H O   
14763 C CB  . GLU H  105 ? 0.7750 0.7640 0.6475 -0.0702 -0.0703 -0.0398 105 GLU H CB  
14764 C CG  . GLU H  105 ? 0.8459 0.8373 0.7147 -0.0693 -0.0721 -0.0386 105 GLU H CG  
14765 C CD  . GLU H  105 ? 1.3722 1.3608 1.2330 -0.0720 -0.0688 -0.0424 105 GLU H CD  
14766 O OE1 . GLU H  105 ? 1.3075 1.2926 1.1679 -0.0712 -0.0633 -0.0455 105 GLU H OE1 
14767 O OE2 . GLU H  105 ? 1.3837 1.3734 1.2387 -0.0749 -0.0716 -0.0421 105 GLU H OE2 
14768 N N   . ARG H  106 ? 0.6278 0.6196 0.4968 -0.0823 -0.0822 -0.0372 106 ARG H N   
14769 C CA  . ARG H  106 ? 0.7202 0.7155 0.5878 -0.0865 -0.0889 -0.0343 106 ARG H CA  
14770 C C   . ARG H  106 ? 0.8245 0.8182 0.6844 -0.0944 -0.0907 -0.0368 106 ARG H C   
14771 O O   . ARG H  106 ? 0.8979 0.8936 0.7525 -0.0986 -0.0951 -0.0356 106 ARG H O   
14772 C CB  . ARG H  106 ? 0.6575 0.6559 0.5341 -0.0843 -0.0924 -0.0303 106 ARG H CB  
14773 C CG  . ARG H  106 ? 0.8281 0.8287 0.7118 -0.0771 -0.0917 -0.0272 106 ARG H CG  
14774 C CD  . ARG H  106 ? 0.9586 0.9628 0.8502 -0.0761 -0.0962 -0.0227 106 ARG H CD  
14775 N NE  . ARG H  106 ? 1.0442 1.0513 0.9331 -0.0809 -0.1023 -0.0202 106 ARG H NE  
14776 C CZ  . ARG H  106 ? 1.1015 1.1110 0.9883 -0.0807 -0.1051 -0.0178 106 ARG H CZ  
14777 N NH1 . ARG H  106 ? 1.0573 1.0666 0.9440 -0.0761 -0.1024 -0.0180 106 ARG H NH1 
14778 N NH2 . ARG H  106 ? 1.1158 1.1280 1.0004 -0.0853 -0.1107 -0.0153 106 ARG H NH2 
14779 N N   . THR H  107 ? 0.7285 0.7185 0.5876 -0.0967 -0.0871 -0.0404 107 THR H N   
14780 C CA  . THR H  107 ? 0.6628 0.6510 0.5146 -0.1046 -0.0883 -0.0434 107 THR H CA  
14781 C C   . THR H  107 ? 0.7443 0.7303 0.5860 -0.1079 -0.0866 -0.0463 107 THR H C   
14782 O O   . THR H  107 ? 0.8012 0.7881 0.6359 -0.1142 -0.0904 -0.0466 107 THR H O   
14783 C CB  . THR H  107 ? 0.7534 0.7376 0.6068 -0.1060 -0.0839 -0.0470 107 THR H CB  
14784 O OG1 . THR H  107 ? 0.8577 0.8440 0.7201 -0.1035 -0.0857 -0.0442 107 THR H OG1 
14785 C CG2 . THR H  107 ? 0.6255 0.6077 0.4705 -0.1147 -0.0849 -0.0505 107 THR H CG2 
14786 N N   . LEU H  108 ? 0.8014 0.7847 0.6425 -0.1036 -0.0810 -0.0485 108 LEU H N   
14787 C CA  . LEU H  108 ? 0.7875 0.7685 0.6197 -0.1061 -0.0788 -0.0513 108 LEU H CA  
14788 C C   . LEU H  108 ? 0.8043 0.7892 0.6337 -0.1064 -0.0839 -0.0479 108 LEU H C   
14789 O O   . LEU H  108 ? 0.7853 0.7698 0.6062 -0.1118 -0.0856 -0.0492 108 LEU H O   
14790 C CB  . LEU H  108 ? 0.6931 0.6710 0.5268 -0.1009 -0.0716 -0.0538 108 LEU H CB  
14791 C CG  . LEU H  108 ? 0.7041 0.6773 0.5399 -0.1007 -0.0656 -0.0575 108 LEU H CG  
14792 C CD1 . LEU H  108 ? 0.5995 0.5698 0.4359 -0.0958 -0.0586 -0.0596 108 LEU H CD1 
14793 C CD2 . LEU H  108 ? 0.7637 0.7335 0.5919 -0.1089 -0.0653 -0.0614 108 LEU H CD2 
14794 N N   . ASP H  109 ? 0.7242 0.7129 0.5608 -0.1008 -0.0862 -0.0437 109 ASP H N   
14795 C CA  . ASP H  109 ? 0.7428 0.7354 0.5779 -0.1007 -0.0909 -0.0401 109 ASP H CA  
14796 C C   . ASP H  109 ? 0.7531 0.7483 0.5854 -0.1068 -0.0975 -0.0378 109 ASP H C   
14797 O O   . ASP H  109 ? 0.7513 0.7484 0.5785 -0.1095 -0.1010 -0.0362 109 ASP H O   
14798 C CB  . ASP H  109 ? 0.8527 0.8485 0.6967 -0.0935 -0.0917 -0.0362 109 ASP H CB  
14799 C CG  . ASP H  109 ? 1.0877 1.0821 0.9330 -0.0878 -0.0861 -0.0378 109 ASP H CG  
14800 O OD1 . ASP H  109 ? 1.1050 1.0961 0.9440 -0.0894 -0.0822 -0.0415 109 ASP H OD1 
14801 O OD2 . ASP H  109 ? 1.0874 1.0838 0.9400 -0.0819 -0.0857 -0.0353 109 ASP H OD2 
14802 N N   . TYR H  110 ? 0.7636 0.7592 0.5997 -0.1088 -0.0991 -0.0375 110 TYR H N   
14803 C CA  . TYR H  110 ? 0.7699 0.7684 0.6039 -0.1149 -0.1053 -0.0353 110 TYR H CA  
14804 C C   . TYR H  110 ? 0.8636 0.8599 0.6861 -0.1225 -0.1054 -0.0388 110 TYR H C   
14805 O O   . TYR H  110 ? 0.7836 0.7825 0.6011 -0.1268 -0.1104 -0.0366 110 TYR H O   
14806 C CB  . TYR H  110 ? 0.6711 0.6703 0.5118 -0.1154 -0.1064 -0.0346 110 TYR H CB  
14807 C CG  . TYR H  110 ? 0.6923 0.6944 0.5304 -0.1224 -0.1125 -0.0330 110 TYR H CG  
14808 C CD1 . TYR H  110 ? 0.6398 0.6473 0.4826 -0.1222 -0.1189 -0.0273 110 TYR H CD1 
14809 C CD2 . TYR H  110 ? 0.7320 0.7315 0.5631 -0.1293 -0.1116 -0.0370 110 TYR H CD2 
14810 C CE1 . TYR H  110 ? 0.7001 0.7108 0.5408 -0.1286 -0.1246 -0.0254 110 TYR H CE1 
14811 C CE2 . TYR H  110 ? 0.7469 0.7496 0.5754 -0.1361 -0.1173 -0.0355 110 TYR H CE2 
14812 C CZ  . TYR H  110 ? 0.7744 0.7829 0.6078 -0.1356 -0.1240 -0.0295 110 TYR H CZ  
14813 O OH  . TYR H  110 ? 0.8273 0.8395 0.6585 -0.1423 -0.1298 -0.0276 110 TYR H OH  
14814 N N   . HIS H  111 ? 0.6958 0.6870 0.5142 -0.1242 -0.0998 -0.0441 111 HIS H N   
14815 C CA  . HIS H  111 ? 0.7094 0.6978 0.5166 -0.1314 -0.0990 -0.0481 111 HIS H CA  
14816 C C   . HIS H  111 ? 0.8481 0.8363 0.6488 -0.1312 -0.0987 -0.0480 111 HIS H C   
14817 O O   . HIS H  111 ? 0.8096 0.7988 0.6024 -0.1370 -0.1021 -0.0478 111 HIS H O   
14818 C CB  . HIS H  111 ? 0.6917 0.6742 0.4966 -0.1328 -0.0921 -0.0539 111 HIS H CB  
14819 C CG  . HIS H  111 ? 0.8131 0.7953 0.6219 -0.1352 -0.0926 -0.0547 111 HIS H CG  
14820 N ND1 . HIS H  111 ? 0.9840 0.9678 0.7884 -0.1428 -0.0972 -0.0548 111 HIS H ND1 
14821 C CD2 . HIS H  111 ? 0.8674 0.8479 0.6842 -0.1312 -0.0890 -0.0555 111 HIS H CD2 
14822 C CE1 . HIS H  111 ? 0.9311 0.9143 0.7408 -0.1434 -0.0964 -0.0557 111 HIS H CE1 
14823 N NE2 . HIS H  111 ? 0.9173 0.8983 0.7344 -0.1364 -0.0914 -0.0561 111 HIS H NE2 
14824 N N   . ASP H  112 ? 0.8459 0.8330 0.6502 -0.1245 -0.0945 -0.0482 112 ASP H N   
14825 C CA  . ASP H  112 ? 0.7578 0.7449 0.5571 -0.1235 -0.0938 -0.0481 112 ASP H CA  
14826 C C   . ASP H  112 ? 0.7517 0.7436 0.5497 -0.1254 -0.1008 -0.0433 112 ASP H C   
14827 O O   . ASP H  112 ? 0.8869 0.8786 0.6767 -0.1291 -0.1021 -0.0437 112 ASP H O   
14828 C CB  . ASP H  112 ? 0.8897 0.8766 0.6955 -0.1153 -0.0896 -0.0477 112 ASP H CB  
14829 C CG  . ASP H  112 ? 0.8789 0.8651 0.6794 -0.1143 -0.0877 -0.0485 112 ASP H CG  
14830 O OD1 . ASP H  112 ? 0.9859 0.9734 0.7915 -0.1080 -0.0860 -0.0471 112 ASP H OD1 
14831 O OD2 . ASP H  112 ? 0.9976 0.9820 0.7887 -0.1200 -0.0880 -0.0507 112 ASP H OD2 
14832 N N   . SER H  113 ? 0.7938 0.7899 0.5999 -0.1228 -0.1052 -0.0386 113 SER H N   
14833 C CA  . SER H  113 ? 0.7238 0.7246 0.5304 -0.1238 -0.1117 -0.0334 113 SER H CA  
14834 C C   . SER H  113 ? 0.8621 0.8641 0.6609 -0.1321 -0.1165 -0.0331 113 SER H C   
14835 O O   . SER H  113 ? 0.8723 0.8762 0.6658 -0.1347 -0.1198 -0.0310 113 SER H O   
14836 C CB  . SER H  113 ? 0.6790 0.6837 0.4969 -0.1191 -0.1148 -0.0287 113 SER H CB  
14837 O OG  . SER H  113 ? 0.8863 0.8956 0.7049 -0.1215 -0.1215 -0.0236 113 SER H OG  
14838 N N   . ASN H  114 ? 0.8758 0.8769 0.6739 -0.1364 -0.1168 -0.0351 114 ASN H N   
14839 C CA  . ASN H  114 ? 0.9086 0.9112 0.6991 -0.1448 -0.1214 -0.0350 114 ASN H CA  
14840 C C   . ASN H  114 ? 0.9428 0.9423 0.7211 -0.1498 -0.1195 -0.0385 114 ASN H C   
14841 O O   . ASN H  114 ? 0.8648 0.8667 0.6364 -0.1553 -0.1243 -0.0366 114 ASN H O   
14842 C CB  . ASN H  114 ? 0.8312 0.8328 0.6229 -0.1486 -0.1210 -0.0374 114 ASN H CB  
14843 C CG  . ASN H  114 ? 0.9526 0.9578 0.7558 -0.1449 -0.1240 -0.0334 114 ASN H CG  
14844 O OD1 . ASN H  114 ? 1.0734 1.0829 0.8828 -0.1412 -0.1279 -0.0280 114 ASN H OD1 
14845 N ND2 . ASN H  114 ? 1.0061 1.0095 0.8124 -0.1459 -0.1219 -0.0360 114 ASN H ND2 
14846 N N   . VAL H  115 ? 0.8501 0.8444 0.6255 -0.1479 -0.1126 -0.0435 115 VAL H N   
14847 C CA  . VAL H  115 ? 0.8725 0.8634 0.6368 -0.1519 -0.1099 -0.0471 115 VAL H CA  
14848 C C   . VAL H  115 ? 0.8809 0.8745 0.6436 -0.1500 -0.1127 -0.0434 115 VAL H C   
14849 O O   . VAL H  115 ? 0.9419 0.9365 0.6962 -0.1555 -0.1160 -0.0426 115 VAL H O   
14850 C CB  . VAL H  115 ? 0.8063 0.7913 0.5697 -0.1491 -0.1015 -0.0527 115 VAL H CB  
14851 C CG1 . VAL H  115 ? 0.9647 0.9465 0.7176 -0.1523 -0.0986 -0.0559 115 VAL H CG1 
14852 C CG2 . VAL H  115 ? 0.7312 0.7129 0.4949 -0.1519 -0.0982 -0.0569 115 VAL H CG2 
14853 N N   . LYS H  116 ? 0.8394 0.8341 0.6100 -0.1423 -0.1112 -0.0412 116 LYS H N   
14854 C CA  . LYS H  116 ? 0.9038 0.9010 0.6742 -0.1397 -0.1135 -0.0375 116 LYS H CA  
14855 C C   . LYS H  116 ? 0.9368 0.9389 0.7060 -0.1436 -0.1212 -0.0323 116 LYS H C   
14856 O O   . LYS H  116 ? 0.9948 0.9978 0.7576 -0.1461 -0.1233 -0.0308 116 LYS H O   
14857 C CB  . LYS H  116 ? 0.9061 0.9048 0.6871 -0.1310 -0.1119 -0.0352 116 LYS H CB  
14858 C CG  . LYS H  116 ? 0.8069 0.8090 0.5899 -0.1281 -0.1150 -0.0306 116 LYS H CG  
14859 C CD  . LYS H  116 ? 0.9208 0.9205 0.6998 -0.1257 -0.1105 -0.0331 116 LYS H CD  
14860 C CE  . LYS H  116 ? 1.1966 1.1995 0.9795 -0.1216 -0.1129 -0.0287 116 LYS H CE  
14861 N NZ  . LYS H  116 ? 1.4275 1.4285 1.2083 -0.1184 -0.1082 -0.0311 116 LYS H NZ  
14862 N N   . ASN H  117 ? 0.8203 0.8256 0.5957 -0.1441 -0.1252 -0.0294 117 ASN H N   
14863 C CA  . ASN H  117 ? 1.0081 1.0186 0.7837 -0.1477 -0.1326 -0.0239 117 ASN H CA  
14864 C C   . ASN H  117 ? 1.0693 1.0795 0.8332 -0.1565 -0.1352 -0.0254 117 ASN H C   
14865 O O   . ASN H  117 ? 0.9831 0.9965 0.7432 -0.1595 -0.1401 -0.0215 117 ASN H O   
14866 C CB  . ASN H  117 ? 0.8564 0.8702 0.6417 -0.1462 -0.1359 -0.0208 117 ASN H CB  
14867 C CG  . ASN H  117 ? 0.8980 0.9138 0.6949 -0.1380 -0.1356 -0.0171 117 ASN H CG  
14868 O OD1 . ASN H  117 ? 0.9746 0.9903 0.7722 -0.1340 -0.1342 -0.0159 117 ASN H OD1 
14869 N ND2 . ASN H  117 ? 1.0264 1.0440 0.8324 -0.1358 -0.1367 -0.0154 117 ASN H ND2 
14870 N N   . LEU H  118 ? 1.0480 1.0543 0.8062 -0.1608 -0.1318 -0.0309 118 LEU H N   
14871 C CA  . LEU H  118 ? 0.9828 0.9883 0.7292 -0.1697 -0.1335 -0.0332 118 LEU H CA  
14872 C C   . LEU H  118 ? 1.0178 1.0211 0.7551 -0.1710 -0.1317 -0.0344 118 LEU H C   
14873 O O   . LEU H  118 ? 1.1764 1.1818 0.9059 -0.1766 -0.1359 -0.0325 118 LEU H O   
14874 C CB  . LEU H  118 ? 1.0124 1.0133 0.7550 -0.1735 -0.1289 -0.0396 118 LEU H CB  
14875 C CG  . LEU H  118 ? 1.0550 1.0570 0.7895 -0.1830 -0.1326 -0.0407 118 LEU H CG  
14876 C CD1 . LEU H  118 ? 1.0312 1.0403 0.7718 -0.1840 -0.1406 -0.0343 118 LEU H CD1 
14877 C CD2 . LEU H  118 ? 1.1756 1.1728 0.9080 -0.1859 -0.1275 -0.0471 118 LEU H CD2 
14878 N N   . TYR H  119 ? 0.9592 0.9586 0.6978 -0.1657 -0.1255 -0.0375 119 TYR H N   
14879 C CA  . TYR H  119 ? 0.9976 0.9947 0.7287 -0.1660 -0.1232 -0.0387 119 TYR H CA  
14880 C C   . TYR H  119 ? 1.0522 1.0541 0.7850 -0.1645 -0.1287 -0.0324 119 TYR H C   
14881 O O   . TYR H  119 ? 1.2032 1.2055 0.9273 -0.1692 -0.1309 -0.0316 119 TYR H O   
14882 C CB  . TYR H  119 ? 0.9141 0.9072 0.6487 -0.1596 -0.1159 -0.0424 119 TYR H CB  
14883 C CG  . TYR H  119 ? 1.1448 1.1358 0.8731 -0.1591 -0.1133 -0.0436 119 TYR H CG  
14884 C CD1 . TYR H  119 ? 1.2503 1.2364 0.9683 -0.1638 -0.1089 -0.0489 119 TYR H CD1 
14885 C CD2 . TYR H  119 ? 1.1392 1.1331 0.8721 -0.1540 -0.1149 -0.0394 119 TYR H CD2 
14886 C CE1 . TYR H  119 ? 1.3203 1.3046 1.0328 -0.1634 -0.1063 -0.0500 119 TYR H CE1 
14887 C CE2 . TYR H  119 ? 1.3302 1.3222 1.0575 -0.1537 -0.1125 -0.0405 119 TYR H CE2 
14888 C CZ  . TYR H  119 ? 1.3801 1.3675 1.0973 -0.1583 -0.1082 -0.0458 119 TYR H CZ  
14889 O OH  . TYR H  119 ? 1.4380 1.4235 1.1499 -0.1580 -0.1056 -0.0469 119 TYR H OH  
14890 N N   . GLU H  120 ? 1.1171 1.1224 0.8611 -0.1581 -0.1306 -0.0280 120 GLU H N   
14891 C CA  . GLU H  120 ? 1.1111 1.1206 0.8582 -0.1559 -0.1352 -0.0218 120 GLU H CA  
14892 C C   . GLU H  120 ? 1.0868 1.1007 0.8300 -0.1622 -0.1424 -0.0173 120 GLU H C   
14893 O O   . GLU H  120 ? 1.2065 1.2222 0.9453 -0.1639 -0.1453 -0.0141 120 GLU H O   
14894 C CB  . GLU H  120 ? 1.3367 1.3489 1.0971 -0.1481 -0.1356 -0.0182 120 GLU H CB  
14895 C CG  . GLU H  120 ? 1.4062 1.4158 1.1702 -0.1413 -0.1301 -0.0202 120 GLU H CG  
14896 C CD  . GLU H  120 ? 1.7394 1.7494 1.4994 -0.1407 -0.1305 -0.0182 120 GLU H CD  
14897 O OE1 . GLU H  120 ? 1.6338 1.6471 1.3918 -0.1437 -0.1359 -0.0136 120 GLU H OE1 
14898 O OE2 . GLU H  120 ? 1.8424 1.8497 1.6017 -0.1372 -0.1256 -0.0212 120 GLU H OE2 
14899 N N   . LYS H  121 ? 1.1500 1.1658 0.8949 -0.1657 -0.1453 -0.0171 121 LYS H N   
14900 C CA  . LYS H  121 ? 1.2523 1.2729 0.9941 -0.1717 -0.1525 -0.0126 121 LYS H CA  
14901 C C   . LYS H  121 ? 1.3034 1.3225 1.0312 -0.1792 -0.1532 -0.0145 121 LYS H C   
14902 O O   . LYS H  121 ? 1.4053 1.4285 1.1297 -0.1829 -0.1588 -0.0098 121 LYS H O   
14903 C CB  . LYS H  121 ? 1.1844 1.2068 0.9300 -0.1745 -0.1547 -0.0129 121 LYS H CB  
14904 C CG  . LYS H  121 ? 1.4048 1.4333 1.1491 -0.1803 -0.1626 -0.0076 121 LYS H CG  
14905 C CD  . LYS H  121 ? 1.5563 1.5867 1.3049 -0.1830 -0.1646 -0.0081 121 LYS H CD  
14906 C CE  . LYS H  121 ? 1.6073 1.6444 1.3550 -0.1887 -0.1728 -0.0024 121 LYS H CE  
14907 N NZ  . LYS H  121 ? 1.7722 1.8116 1.5240 -0.1917 -0.1749 -0.0030 121 LYS H NZ  
14908 N N   . VAL H  122 ? 1.2459 1.2593 0.9659 -0.1815 -0.1473 -0.0215 122 VAL H N   
14909 C CA  . VAL H  122 ? 1.2969 1.3080 1.0032 -0.1884 -0.1468 -0.0242 122 VAL H CA  
14910 C C   . VAL H  122 ? 1.3690 1.3795 1.0727 -0.1856 -0.1459 -0.0223 122 VAL H C   
14911 O O   . VAL H  122 ? 1.6399 1.6520 1.3358 -0.1903 -0.1493 -0.0199 122 VAL H O   
14912 C CB  . VAL H  122 ? 1.1604 1.1650 0.8596 -0.1914 -0.1400 -0.0324 122 VAL H CB  
14913 C CG1 . VAL H  122 ? 1.2466 1.2477 0.9326 -0.1965 -0.1378 -0.0355 122 VAL H CG1 
14914 C CG2 . VAL H  122 ? 1.3228 1.3278 1.0209 -0.1967 -0.1414 -0.0346 122 VAL H CG2 
14915 N N   . ARG H  123 ? 1.2376 1.2458 0.9481 -0.1780 -0.1412 -0.0234 123 ARG H N   
14916 C CA  . ARG H  123 ? 1.2978 1.3049 1.0065 -0.1749 -0.1392 -0.0226 123 ARG H CA  
14917 C C   . ARG H  123 ? 1.3325 1.3449 1.0450 -0.1734 -0.1452 -0.0150 123 ARG H C   
14918 O O   . ARG H  123 ? 1.4500 1.4623 1.1562 -0.1752 -0.1459 -0.0135 123 ARG H O   
14919 C CB  . ARG H  123 ? 1.2814 1.2854 0.9971 -0.1671 -0.1329 -0.0255 123 ARG H CB  
14920 C CG  . ARG H  123 ? 1.3774 1.3792 1.0896 -0.1647 -0.1296 -0.0264 123 ARG H CG  
14921 C CD  . ARG H  123 ? 1.5126 1.5150 1.2354 -0.1560 -0.1271 -0.0251 123 ARG H CD  
14922 N NE  . ARG H  123 ? 1.7670 1.7746 1.4988 -0.1528 -0.1324 -0.0185 123 ARG H NE  
14923 C CZ  . ARG H  123 ? 1.8909 1.9000 1.6307 -0.1463 -0.1318 -0.0157 123 ARG H CZ  
14924 N NH1 . ARG H  123 ? 1.7521 1.7583 1.4918 -0.1424 -0.1264 -0.0190 123 ARG H NH1 
14925 N NH2 . ARG H  123 ? 1.9146 1.9280 1.6623 -0.1439 -0.1364 -0.0098 123 ARG H NH2 
14926 N N   . SER H  124 ? 1.4336 1.4503 1.1566 -0.1700 -0.1491 -0.0102 124 SER H N   
14927 C CA  . SER H  124 ? 1.5580 1.5798 1.2858 -0.1685 -0.1547 -0.0026 124 SER H CA  
14928 C C   . SER H  124 ? 1.6539 1.6796 1.3752 -0.1761 -0.1612 0.0010  124 SER H C   
14929 O O   . SER H  124 ? 1.7647 1.7956 1.4910 -0.1757 -0.1668 0.0079  124 SER H O   
14930 C CB  . SER H  124 ? 1.6602 1.6852 1.4022 -0.1621 -0.1562 0.0013  124 SER H CB  
14931 O OG  . SER H  124 ? 1.7059 1.7326 1.4512 -0.1642 -0.1583 0.0010  124 SER H OG  
14932 N N   . GLN H  125 ? 1.5216 1.5448 1.2318 -0.1831 -0.1603 -0.0035 125 GLN H N   
14933 C CA  . GLN H  125 ? 1.4762 1.5031 1.1792 -0.1910 -0.1663 -0.0007 125 GLN H CA  
14934 C C   . GLN H  125 ? 1.6357 1.6595 1.3244 -0.1969 -0.1648 -0.0036 125 GLN H C   
14935 O O   . GLN H  125 ? 1.6448 1.6717 1.3283 -0.2008 -0.1693 0.0010  125 GLN H O   
14936 C CB  . GLN H  125 ? 1.3711 1.3988 1.0746 -0.1949 -0.1674 -0.0032 125 GLN H CB  
14937 C CG  . GLN H  125 ? 1.5103 1.5430 1.2081 -0.2029 -0.1744 0.0003  125 GLN H CG  
14938 C CD  . GLN H  125 ? 1.7225 1.7558 1.4212 -0.2067 -0.1752 -0.0025 125 GLN H CD  
14939 O OE1 . GLN H  125 ? 1.6399 1.6681 1.3379 -0.2060 -0.1694 -0.0092 125 GLN H OE1 
14940 N NE2 . GLN H  125 ? 1.7691 1.8087 1.4696 -0.2108 -0.1823 0.0026  125 GLN H NE2 
14941 N N   . LEU H  126 ? 1.6461 1.6636 1.3288 -0.1975 -0.1579 -0.0110 126 LEU H N   
14942 C CA  . LEU H  126 ? 1.4811 1.4947 1.1533 -0.2002 -0.1545 -0.0136 126 LEU H CA  
14943 C C   . LEU H  126 ? 1.5881 1.6002 1.2671 -0.1923 -0.1509 -0.0124 126 LEU H C   
14944 O O   . LEU H  126 ? 1.7988 1.8087 1.4853 -0.1862 -0.1465 -0.0153 126 LEU H O   
14945 C CB  . LEU H  126 ? 1.4103 1.4175 1.0737 -0.2039 -0.1482 -0.0222 126 LEU H CB  
14946 C CG  . LEU H  126 ? 1.4391 1.4454 1.1014 -0.2078 -0.1479 -0.0266 126 LEU H CG  
14947 C CD1 . LEU H  126 ? 1.4846 1.4836 1.1417 -0.2083 -0.1396 -0.0349 126 LEU H CD1 
14948 C CD2 . LEU H  126 ? 1.5104 1.5202 1.1648 -0.2168 -0.1539 -0.0249 126 LEU H CD2 
14949 N N   . LYS H  127 ? 1.5997 1.6132 1.2761 -0.1924 -0.1527 -0.0083 127 LYS H N   
14950 C CA  . LYS H  127 ? 1.6128 1.6248 1.2948 -0.1854 -0.1492 -0.0073 127 LYS H CA  
14951 C C   . LYS H  127 ? 1.8696 1.8770 1.5416 -0.1877 -0.1445 -0.0111 127 LYS H C   
14952 O O   . LYS H  127 ? 1.6363 1.6387 1.3065 -0.1861 -0.1380 -0.0172 127 LYS H O   
14953 C CB  . LYS H  127 ? 1.5557 1.5731 1.2451 -0.1823 -0.1547 0.0008  127 LYS H CB  
14954 C CG  . LYS H  127 ? 1.6687 1.6910 1.3679 -0.1806 -0.1597 0.0047  127 LYS H CG  
14955 C CD  . LYS H  127 ? 1.6385 1.6670 1.3380 -0.1838 -0.1676 0.0125  127 LYS H CD  
14956 C CE  . LYS H  127 ? 1.7047 1.7380 1.4140 -0.1823 -0.1723 0.0161  127 LYS H CE  
14957 N NZ  . LYS H  127 ? 1.6024 1.6422 1.3133 -0.1853 -0.1801 0.0242  127 LYS H NZ  
14958 N N   . ASN H  128 ? 2.2714 2.2804 1.9366 -0.1916 -0.1479 -0.0072 128 ASN H N   
14959 C CA  . ASN H  128 ? 2.2269 2.2316 1.8814 -0.1948 -0.1440 -0.0105 128 ASN H CA  
14960 C C   . ASN H  128 ? 2.2288 2.2305 1.8708 -0.2031 -0.1428 -0.0156 128 ASN H C   
14961 O O   . ASN H  128 ? 2.1110 2.1076 1.7452 -0.2050 -0.1373 -0.0209 128 ASN H O   
14962 C CB  . ASN H  128 ? 2.1749 2.1824 1.8268 -0.1958 -0.1479 -0.0044 128 ASN H CB  
14963 C CG  . ASN H  128 ? 2.2664 2.2754 1.9293 -0.1877 -0.1474 -0.0006 128 ASN H CG  
14964 O OD1 . ASN H  128 ? 2.1785 2.1844 1.8462 -0.1822 -0.1417 -0.0043 128 ASN H OD1 
14965 N ND2 . ASN H  128 ? 2.4303 2.4443 2.0973 -0.1870 -0.1534 0.0068  128 ASN H ND2 
14966 N N   . ASN H  129 ? 2.2322 2.2372 1.8725 -0.2080 -0.1478 -0.0141 129 ASN H N   
14967 C CA  . ASN H  129 ? 2.3302 2.3330 1.9579 -0.2168 -0.1475 -0.0184 129 ASN H CA  
14968 C C   . ASN H  129 ? 2.3050 2.3015 1.9300 -0.2170 -0.1402 -0.0271 129 ASN H C   
14969 O O   . ASN H  129 ? 2.3652 2.3591 1.9799 -0.2242 -0.1390 -0.0316 129 ASN H O   
14970 C CB  . ASN H  129 ? 2.2569 2.2652 1.8844 -0.2218 -0.1548 -0.0147 129 ASN H CB  
14971 C CG  . ASN H  129 ? 2.2273 2.2417 1.8548 -0.2234 -0.1622 -0.0062 129 ASN H CG  
14972 O OD1 . ASN H  129 ? 2.2605 2.2802 1.8878 -0.2275 -0.1688 -0.0022 129 ASN H OD1 
14973 N ND2 . ASN H  129 ? 2.2109 2.2248 1.8387 -0.2201 -0.1612 -0.0035 129 ASN H ND2 
14974 N N   . ALA H  130 ? 2.1023 2.0966 1.7366 -0.2093 -0.1354 -0.0293 130 ALA H N   
14975 C CA  . ALA H  130 ? 1.9884 1.9769 1.6215 -0.2085 -0.1282 -0.0371 130 ALA H CA  
14976 C C   . ALA H  130 ? 1.8307 1.8175 1.4737 -0.1993 -0.1232 -0.0381 130 ALA H C   
14977 O O   . ALA H  130 ? 1.8415 1.8319 1.4932 -0.1937 -0.1257 -0.0328 130 ALA H O   
14978 C CB  . ALA H  130 ? 2.0021 1.9913 1.6370 -0.2109 -0.1295 -0.0394 130 ALA H CB  
14979 N N   . LYS H  131 ? 1.8391 1.8206 1.4808 -0.1980 -0.1162 -0.0448 131 LYS H N   
14980 C CA  . LYS H  131 ? 1.9470 1.9270 1.5976 -0.1897 -0.1112 -0.0461 131 LYS H CA  
14981 C C   . LYS H  131 ? 2.0601 2.0379 1.7163 -0.1866 -0.1074 -0.0506 131 LYS H C   
14982 O O   . LYS H  131 ? 2.0618 2.0368 1.7122 -0.1916 -0.1058 -0.0552 131 LYS H O   
14983 C CB  . LYS H  131 ? 1.9595 1.9352 1.6038 -0.1898 -0.1056 -0.0494 131 LYS H CB  
14984 C CG  . LYS H  131 ? 2.0765 2.0461 1.7117 -0.1945 -0.0996 -0.0570 131 LYS H CG  
14985 C CD  . LYS H  131 ? 2.0238 1.9892 1.6566 -0.1922 -0.0930 -0.0605 131 LYS H CD  
14986 C CE  . LYS H  131 ? 2.0223 1.9813 1.6474 -0.1959 -0.0863 -0.0683 131 LYS H CE  
14987 N NZ  . LYS H  131 ? 2.0052 1.9604 1.6295 -0.1929 -0.0795 -0.0718 131 LYS H NZ  
14988 N N   . GLU H  132 ? 2.1304 2.1096 1.7979 -0.1784 -0.1059 -0.0494 132 GLU H N   
14989 C CA  . GLU H  132 ? 2.0707 2.0479 1.7448 -0.1745 -0.1017 -0.0532 132 GLU H CA  
14990 C C   . GLU H  132 ? 2.0459 2.0173 1.7160 -0.1742 -0.0936 -0.0595 132 GLU H C   
14991 O O   . GLU H  132 ? 2.0904 2.0605 1.7577 -0.1727 -0.0911 -0.0600 132 GLU H O   
14992 C CB  . GLU H  132 ? 2.0543 2.0351 1.7417 -0.1659 -0.1026 -0.0495 132 GLU H CB  
14993 C CG  . GLU H  132 ? 2.0737 2.0602 1.7669 -0.1652 -0.1101 -0.0430 132 GLU H CG  
14994 C CD  . GLU H  132 ? 2.0817 2.0711 1.7875 -0.1568 -0.1102 -0.0398 132 GLU H CD  
14995 O OE1 . GLU H  132 ? 2.0279 2.0218 1.7392 -0.1553 -0.1157 -0.0341 132 GLU H OE1 
14996 O OE2 . GLU H  132 ? 2.0464 2.0336 1.7567 -0.1517 -0.1047 -0.0428 132 GLU H OE2 
14997 N N   . ILE H  133 ? 1.9604 1.9282 1.6303 -0.1754 -0.0893 -0.0642 133 ILE H N   
14998 C CA  . ILE H  133 ? 2.0141 1.9764 1.6819 -0.1744 -0.0811 -0.0701 133 ILE H CA  
14999 C C   . ILE H  133 ? 2.0227 1.9855 1.7024 -0.1656 -0.0775 -0.0701 133 ILE H C   
15000 O O   . ILE H  133 ? 2.0179 1.9784 1.6986 -0.1621 -0.0719 -0.0725 133 ILE H O   
15001 C CB  . ILE H  133 ? 2.0208 1.9783 1.6821 -0.1805 -0.0776 -0.0756 133 ILE H CB  
15002 C CG1 . ILE H  133 ? 2.0360 1.9927 1.6844 -0.1898 -0.0809 -0.0760 133 ILE H CG1 
15003 C CG2 . ILE H  133 ? 1.8949 1.8465 1.5554 -0.1788 -0.0686 -0.0814 133 ILE H CG2 
15004 C CD1 . ILE H  133 ? 2.0861 2.0400 1.7253 -0.1925 -0.0782 -0.0778 133 ILE H CD1 
15005 N N   . GLY H  134 ? 2.0571 2.0233 1.7459 -0.1620 -0.0806 -0.0671 134 GLY H N   
15006 C CA  . GLY H  134 ? 1.9594 1.9267 1.6596 -0.1539 -0.0777 -0.0667 134 GLY H CA  
15007 C C   . GLY H  134 ? 1.7415 1.7065 1.4458 -0.1534 -0.0745 -0.0697 134 GLY H C   
15008 O O   . GLY H  134 ? 1.5235 1.4901 1.2378 -0.1472 -0.0735 -0.0685 134 GLY H O   
15009 N N   . ASN H  135 ? 1.5547 1.5157 1.2509 -0.1602 -0.0728 -0.0737 135 ASN H N   
15010 C CA  . ASN H  135 ? 1.3014 1.2595 1.0003 -0.1608 -0.0694 -0.0770 135 ASN H CA  
15011 C C   . ASN H  135 ? 1.3228 1.2837 1.0223 -0.1645 -0.0755 -0.0746 135 ASN H C   
15012 O O   . ASN H  135 ? 1.1550 1.1132 0.8522 -0.1686 -0.0738 -0.0778 135 ASN H O   
15013 C CB  . ASN H  135 ? 1.4065 1.3581 1.0966 -0.1659 -0.0628 -0.0833 135 ASN H CB  
15014 C CG  . ASN H  135 ? 1.6439 1.5918 1.3384 -0.1649 -0.0574 -0.0872 135 ASN H CG  
15015 O OD1 . ASN H  135 ? 1.5225 1.4726 1.2269 -0.1597 -0.0581 -0.0851 135 ASN H OD1 
15016 N ND2 . ASN H  135 ? 1.8228 1.7646 1.5098 -0.1700 -0.0516 -0.0928 135 ASN H ND2 
15017 N N   . GLY H  136 ? 1.3997 1.3663 1.1026 -0.1630 -0.0825 -0.0688 136 GLY H N   
15018 C CA  . GLY H  136 ? 1.3175 1.2877 1.0214 -0.1664 -0.0890 -0.0656 136 GLY H CA  
15019 C C   . GLY H  136 ? 1.3512 1.3208 1.0432 -0.1757 -0.0922 -0.0665 136 GLY H C   
15020 O O   . GLY H  136 ? 1.4231 1.3951 1.1139 -0.1802 -0.0970 -0.0650 136 GLY H O   
15021 N N   . CYS H  137 ? 1.7865 1.7532 1.4695 -0.1786 -0.0895 -0.0690 137 CYS H N   
15022 C CA  . CYS H  137 ? 1.7830 1.7480 1.4532 -0.1879 -0.0911 -0.0709 137 CYS H CA  
15023 C C   . CYS H  137 ? 1.8022 1.7700 1.4666 -0.1897 -0.0954 -0.0672 137 CYS H C   
15024 O O   . CYS H  137 ? 1.8365 1.8041 1.5029 -0.1849 -0.0933 -0.0663 137 CYS H O   
15025 C CB  . CYS H  137 ? 1.6730 1.6309 1.3360 -0.1912 -0.0831 -0.0782 137 CYS H CB  
15026 S SG  . CYS H  137 ? 2.0495 2.0036 1.7166 -0.1919 -0.0784 -0.0830 137 CYS H SG  
15027 N N   . PHE H  138 ? 1.7591 1.7295 1.4163 -0.1966 -0.1014 -0.0649 138 PHE H N   
15028 C CA  . PHE H  138 ? 1.8688 1.8421 1.5202 -0.1988 -0.1060 -0.0608 138 PHE H CA  
15029 C C   . PHE H  138 ? 2.0518 2.0212 1.6886 -0.2071 -0.1041 -0.0647 138 PHE H C   
15030 O O   . PHE H  138 ? 2.0927 2.0587 1.7231 -0.2129 -0.1017 -0.0695 138 PHE H O   
15031 C CB  . PHE H  138 ? 1.8221 1.8022 1.4766 -0.2003 -0.1149 -0.0541 138 PHE H CB  
15032 C CG  . PHE H  138 ? 1.6585 1.6426 1.3271 -0.1924 -0.1172 -0.0497 138 PHE H CG  
15033 C CD1 . PHE H  138 ? 1.5580 1.5425 1.2339 -0.1907 -0.1168 -0.0507 138 PHE H CD1 
15034 C CD2 . PHE H  138 ? 1.6761 1.6636 1.3506 -0.1868 -0.1197 -0.0445 138 PHE H CD2 
15035 C CE1 . PHE H  138 ? 1.5786 1.5667 1.2673 -0.1836 -0.1188 -0.0467 138 PHE H CE1 
15036 C CE2 . PHE H  138 ? 1.5702 1.5613 1.2575 -0.1798 -0.1215 -0.0406 138 PHE H CE2 
15037 C CZ  . PHE H  138 ? 1.5329 1.5243 1.2272 -0.1782 -0.1211 -0.0417 138 PHE H CZ  
15038 N N   . GLU H  139 ? 2.1746 2.1443 1.8058 -0.2077 -0.1050 -0.0628 139 GLU H N   
15039 C CA  . GLU H  139 ? 2.0815 2.0481 1.6983 -0.2160 -0.1040 -0.0658 139 GLU H CA  
15040 C C   . GLU H  139 ? 1.9658 1.9374 1.5777 -0.2201 -0.1114 -0.0596 139 GLU H C   
15041 O O   . GLU H  139 ? 1.9703 1.9449 1.5870 -0.2156 -0.1136 -0.0544 139 GLU H O   
15042 C CB  . GLU H  139 ? 2.0790 2.0401 1.6919 -0.2142 -0.0966 -0.0702 139 GLU H CB  
15043 C CG  . GLU H  139 ? 2.3300 2.2873 1.9276 -0.2228 -0.0949 -0.0737 139 GLU H CG  
15044 C CD  . GLU H  139 ? 2.4448 2.3958 2.0389 -0.2214 -0.0864 -0.0791 139 GLU H CD  
15045 O OE1 . GLU H  139 ? 2.2710 2.2207 1.8746 -0.2138 -0.0818 -0.0803 139 GLU H OE1 
15046 O OE2 . GLU H  139 ? 2.5061 2.4535 2.0880 -0.2280 -0.0843 -0.0822 139 GLU H OE2 
15047 N N   . PHE H  140 ? 2.0199 1.9923 1.6225 -0.2287 -0.1149 -0.0601 140 PHE H N   
15048 C CA  . PHE H  140 ? 2.2024 2.1800 1.8002 -0.2333 -0.1222 -0.0539 140 PHE H CA  
15049 C C   . PHE H  140 ? 2.2854 2.2605 1.8732 -0.2363 -0.1204 -0.0540 140 PHE H C   
15050 O O   . PHE H  140 ? 2.2249 2.1941 1.8035 -0.2403 -0.1146 -0.0603 140 PHE H O   
15051 C CB  . PHE H  140 ? 2.2320 2.2115 1.8226 -0.2420 -0.1267 -0.0545 140 PHE H CB  
15052 C CG  . PHE H  140 ? 2.1298 2.1132 1.7303 -0.2397 -0.1304 -0.0528 140 PHE H CG  
15053 C CD1 . PHE H  140 ? 2.1456 2.1253 1.7477 -0.2402 -0.1259 -0.0588 140 PHE H CD1 
15054 C CD2 . PHE H  140 ? 2.0727 2.0634 1.6814 -0.2370 -0.1378 -0.0449 140 PHE H CD2 
15055 C CE1 . PHE H  140 ? 2.1400 2.1231 1.7518 -0.2381 -0.1288 -0.0569 140 PHE H CE1 
15056 C CE2 . PHE H  140 ? 2.0419 2.0362 1.6599 -0.2349 -0.1411 -0.0433 140 PHE H CE2 
15057 C CZ  . PHE H  140 ? 2.0825 2.0730 1.7022 -0.2354 -0.1365 -0.0492 140 PHE H CZ  
15058 N N   . TYR H  141 ? 2.2688 2.2485 1.8588 -0.2345 -0.1253 -0.0471 141 TYR H N   
15059 C CA  . TYR H  141 ? 2.1587 2.1370 1.7385 -0.2384 -0.1251 -0.0462 141 TYR H CA  
15060 C C   . TYR H  141 ? 2.0789 2.0603 1.6481 -0.2478 -0.1312 -0.0438 141 TYR H C   
15061 O O   . TYR H  141 ? 2.1529 2.1325 1.7103 -0.2537 -0.1308 -0.0445 141 TYR H O   
15062 C CB  . TYR H  141 ? 2.1501 2.1316 1.7373 -0.2319 -0.1272 -0.0399 141 TYR H CB  
15063 C CG  . TYR H  141 ? 2.0793 2.0582 1.6764 -0.2229 -0.1214 -0.0419 141 TYR H CG  
15064 C CD1 . TYR H  141 ? 2.0469 2.0298 1.6569 -0.2151 -0.1240 -0.0367 141 TYR H CD1 
15065 C CD2 . TYR H  141 ? 1.9723 1.9447 1.5656 -0.2224 -0.1134 -0.0489 141 TYR H CD2 
15066 C CE1 . TYR H  141 ? 1.9865 1.9675 1.6053 -0.2071 -0.1189 -0.0385 141 TYR H CE1 
15067 C CE2 . TYR H  141 ? 2.0095 1.9801 1.6119 -0.2142 -0.1084 -0.0505 141 TYR H CE2 
15068 C CZ  . TYR H  141 ? 1.9756 1.9506 1.5905 -0.2067 -0.1112 -0.0453 141 TYR H CZ  
15069 O OH  . TYR H  141 ? 1.7559 1.7295 1.3796 -0.1990 -0.1064 -0.0468 141 TYR H OH  
15070 N N   . HIS H  142 ? 2.0039 1.9902 1.5772 -0.2494 -0.1369 -0.0410 142 HIS H N   
15071 C CA  . HIS H  142 ? 2.0107 2.0013 1.5752 -0.2582 -0.1435 -0.0381 142 HIS H CA  
15072 C C   . HIS H  142 ? 2.0179 2.0066 1.5772 -0.2645 -0.1426 -0.0438 142 HIS H C   
15073 O O   . HIS H  142 ? 2.2014 2.1913 1.7698 -0.2612 -0.1428 -0.0447 142 HIS H O   
15074 C CB  . HIS H  142 ? 2.0326 2.0316 1.6058 -0.2555 -0.1522 -0.0288 142 HIS H CB  
15075 C CG  . HIS H  142 ? 2.1062 2.1098 1.6839 -0.2577 -0.1573 -0.0273 142 HIS H CG  
15076 N ND1 . HIS H  142 ? 2.0963 2.1047 1.6664 -0.2661 -0.1638 -0.0246 142 HIS H ND1 
15077 C CD2 . HIS H  142 ? 2.1368 2.1415 1.7260 -0.2526 -0.1570 -0.0279 142 HIS H CD2 
15078 C CE1 . HIS H  142 ? 2.1138 2.1258 1.6907 -0.2662 -0.1673 -0.0237 142 HIS H CE1 
15079 N NE2 . HIS H  142 ? 2.1861 2.1959 1.7746 -0.2580 -0.1632 -0.0258 142 HIS H NE2 
15080 N N   . LYS H  143 ? 1.9673 1.9530 1.5119 -0.2736 -0.1412 -0.0480 143 LYS H N   
15081 C CA  . LYS H  143 ? 2.0256 2.0089 1.5634 -0.2808 -0.1396 -0.0542 143 LYS H CA  
15082 C C   . LYS H  143 ? 2.0732 2.0625 1.6192 -0.2806 -0.1457 -0.0510 143 LYS H C   
15083 O O   . LYS H  143 ? 1.9861 1.9826 1.5318 -0.2838 -0.1538 -0.0445 143 LYS H O   
15084 C CB  . LYS H  143 ? 2.0937 2.0761 1.6144 -0.2919 -0.1409 -0.0560 143 LYS H CB  
15085 C CG  . LYS H  143 ? 2.0891 2.0639 1.5996 -0.2939 -0.1334 -0.0616 143 LYS H CG  
15086 C CD  . LYS H  143 ? 2.1817 2.1485 1.6879 -0.2962 -0.1249 -0.0715 143 LYS H CD  
15087 C CE  . LYS H  143 ? 2.1426 2.1061 1.6620 -0.2861 -0.1191 -0.0740 143 LYS H CE  
15088 N NZ  . LYS H  143 ? 2.0520 2.0075 1.5673 -0.2883 -0.1106 -0.0835 143 LYS H NZ  
15089 N N   . CYS H  144 ? 2.2062 2.1928 1.7599 -0.2768 -0.1417 -0.0555 144 CYS H N   
15090 C CA  . CYS H  144 ? 2.3184 2.3102 1.8809 -0.2759 -0.1468 -0.0529 144 CYS H CA  
15091 C C   . CYS H  144 ? 2.1984 2.1871 1.7550 -0.2830 -0.1443 -0.0599 144 CYS H C   
15092 O O   . CYS H  144 ? 2.2138 2.1966 1.7740 -0.2801 -0.1371 -0.0660 144 CYS H O   
15093 C CB  . CYS H  144 ? 2.2667 2.2590 1.8454 -0.2648 -0.1451 -0.0510 144 CYS H CB  
15094 S SG  . CYS H  144 ? 2.3047 2.3037 1.8963 -0.2626 -0.1513 -0.0468 144 CYS H SG  
15095 N N   . ASP H  145 ? 2.2904 2.2833 1.8384 -0.2922 -0.1501 -0.0585 145 ASP H N   
15096 C CA  . ASP H  145 ? 2.3936 2.3843 1.9359 -0.2998 -0.1484 -0.0645 145 ASP H CA  
15097 C C   . ASP H  145 ? 2.2898 2.2843 1.8450 -0.2963 -0.1509 -0.0629 145 ASP H C   
15098 O O   . ASP H  145 ? 2.2560 2.2531 1.8249 -0.2871 -0.1522 -0.0584 145 ASP H O   
15099 C CB  . ASP H  145 ? 2.5900 2.5841 2.1177 -0.3115 -0.1538 -0.0638 145 ASP H CB  
15100 C CG  . ASP H  145 ? 2.6108 2.6146 2.1410 -0.3116 -0.1640 -0.0539 145 ASP H CG  
15101 O OD1 . ASP H  145 ? 2.5091 2.5183 2.0324 -0.3200 -0.1704 -0.0517 145 ASP H OD1 
15102 O OD2 . ASP H  145 ? 2.5847 2.5908 2.1243 -0.3031 -0.1654 -0.0479 145 ASP H OD2 
15103 N N   . ASN H  146 ? 2.0656 2.0602 1.6163 -0.3039 -0.1515 -0.0666 146 ASN H N   
15104 C CA  . ASN H  146 ? 1.9293 1.9266 1.4914 -0.3014 -0.1530 -0.0662 146 ASN H CA  
15105 C C   . ASN H  146 ? 2.0155 2.0227 1.5881 -0.2979 -0.1625 -0.0567 146 ASN H C   
15106 O O   . ASN H  146 ? 2.2655 2.2743 1.8522 -0.2904 -0.1626 -0.0545 146 ASN H O   
15107 C CB  . ASN H  146 ? 1.8184 1.8141 1.3720 -0.3114 -0.1522 -0.0721 146 ASN H CB  
15108 C CG  . ASN H  146 ? 1.8177 1.8031 1.3648 -0.3134 -0.1416 -0.0820 146 ASN H CG  
15109 O OD1 . ASN H  146 ? 1.8441 1.8267 1.3824 -0.3221 -0.1395 -0.0879 146 ASN H OD1 
15110 N ND2 . ASN H  146 ? 1.6810 1.6606 1.2325 -0.3055 -0.1348 -0.0839 146 ASN H ND2 
15111 N N   . THR H  147 ? 2.3272 2.3410 1.8931 -0.3036 -0.1703 -0.0511 147 THR H N   
15112 C CA  . THR H  147 ? 2.4346 2.4580 2.0105 -0.3005 -0.1793 -0.0416 147 THR H CA  
15113 C C   . THR H  147 ? 2.3959 2.4205 1.9789 -0.2916 -0.1802 -0.0355 147 THR H C   
15114 O O   . THR H  147 ? 2.3277 2.3599 1.9176 -0.2891 -0.1875 -0.0271 147 THR H O   
15115 C CB  . THR H  147 ? 2.3727 2.4039 1.9400 -0.3105 -0.1881 -0.0373 147 THR H CB  
15116 O OG1 . THR H  147 ? 2.4547 2.4862 2.0110 -0.3139 -0.1899 -0.0350 147 THR H OG1 
15117 N N   . CYS H  148 ? 2.2827 2.2999 1.8641 -0.2870 -0.1726 -0.0399 148 CYS H N   
15118 C CA  . CYS H  148 ? 2.3472 2.3644 1.9365 -0.2777 -0.1719 -0.0356 148 CYS H CA  
15119 C C   . CYS H  148 ? 2.4612 2.4755 2.0644 -0.2685 -0.1670 -0.0376 148 CYS H C   
15120 O O   . CYS H  148 ? 2.3913 2.4097 2.0075 -0.2608 -0.1698 -0.0318 148 CYS H O   
15121 C CB  . CYS H  148 ? 2.2932 2.3039 1.8715 -0.2790 -0.1662 -0.0397 148 CYS H CB  
15122 S SG  . CYS H  148 ? 2.2590 2.2676 1.8452 -0.2681 -0.1626 -0.0366 148 CYS H SG  
15123 N N   . MET H  149 ? 2.4256 2.4329 2.0258 -0.2699 -0.1597 -0.0458 149 MET H N   
15124 C CA  . MET H  149 ? 2.2330 2.2369 1.8446 -0.2627 -0.1544 -0.0489 149 MET H CA  
15125 C C   . MET H  149 ? 2.2304 2.2408 1.8541 -0.2603 -0.1600 -0.0441 149 MET H C   
15126 O O   . MET H  149 ? 2.1391 2.1489 1.7753 -0.2520 -0.1577 -0.0434 149 MET H O   
15127 C CB  . MET H  149 ? 2.1743 2.1706 1.7788 -0.2673 -0.1467 -0.0583 149 MET H CB  
15128 C CG  . MET H  149 ? 2.1092 2.0980 1.7047 -0.2676 -0.1393 -0.0638 149 MET H CG  
15129 S SD  . MET H  149 ? 1.8560 1.8417 1.4624 -0.2551 -0.1338 -0.0629 149 MET H SD  
15130 C CE  . MET H  149 ? 1.8497 1.8259 1.4437 -0.2581 -0.1245 -0.0710 149 MET H CE  
15131 N N   . GLU H  150 ? 3.7232 3.7398 3.3432 -0.2675 -0.1673 -0.0408 150 GLU H N   
15132 C CA  . GLU H  150 ? 3.7267 3.7496 3.3576 -0.2662 -0.1728 -0.0364 150 GLU H CA  
15133 C C   . GLU H  150 ? 3.6978 3.7269 3.3404 -0.2586 -0.1781 -0.0275 150 GLU H C   
15134 O O   . GLU H  150 ? 3.6700 3.7011 3.3260 -0.2521 -0.1786 -0.0250 150 GLU H O   
15135 C CB  . GLU H  150 ? 3.7806 3.8088 3.4036 -0.2767 -0.1791 -0.0354 150 GLU H CB  
15136 C CG  . GLU H  150 ? 3.8466 3.8755 3.4746 -0.2791 -0.1791 -0.0383 150 GLU H CG  
15137 C CD  . GLU H  150 ? 3.8908 3.9115 3.5100 -0.2841 -0.1713 -0.0482 150 GLU H CD  
15138 O OE1 . GLU H  150 ? 3.8884 3.9100 3.5064 -0.2899 -0.1721 -0.0512 150 GLU H OE1 
15139 O OE2 . GLU H  150 ? 3.8153 3.8287 3.4290 -0.2823 -0.1642 -0.0531 150 GLU H OE2 
15140 N N   . SER H  151 ? 2.3811 2.4131 2.0186 -0.2597 -0.1819 -0.0226 151 SER H N   
15141 C CA  . SER H  151 ? 2.3222 2.3600 1.9699 -0.2532 -0.1870 -0.0139 151 SER H CA  
15142 C C   . SER H  151 ? 2.2031 2.2373 1.8627 -0.2423 -0.1817 -0.0145 151 SER H C   
15143 O O   . SER H  151 ? 2.2358 2.2745 1.9075 -0.2359 -0.1850 -0.0082 151 SER H O   
15144 C CB  . SER H  151 ? 2.2288 2.2682 1.8677 -0.2557 -0.1898 -0.0101 151 SER H CB  
15145 O OG  . SER H  151 ? 2.1233 2.1553 1.7560 -0.2535 -0.1827 -0.0152 151 SER H OG  
15146 N N   . VAL H  152 ? 2.0060 2.0323 1.6623 -0.2403 -0.1735 -0.0219 152 VAL H N   
15147 C CA  . VAL H  152 ? 1.8618 1.8845 1.5286 -0.2305 -0.1680 -0.0230 152 VAL H CA  
15148 C C   . VAL H  152 ? 1.8673 1.8904 1.5450 -0.2271 -0.1669 -0.0242 152 VAL H C   
15149 O O   . VAL H  152 ? 1.6542 1.6793 1.3444 -0.2192 -0.1675 -0.0205 152 VAL H O   
15150 C CB  . VAL H  152 ? 1.6312 1.6457 1.2909 -0.2295 -0.1595 -0.0303 152 VAL H CB  
15151 C CG1 . VAL H  152 ? 1.4381 1.4501 1.1083 -0.2192 -0.1548 -0.0302 152 VAL H CG1 
15152 C CG2 . VAL H  152 ? 1.7505 1.7640 1.3973 -0.2347 -0.1602 -0.0302 152 VAL H CG2 
15153 N N   . LYS H  153 ? 1.8706 1.8915 1.5433 -0.2331 -0.1652 -0.0296 153 LYS H N   
15154 C CA  . LYS H  153 ? 1.7578 1.7786 1.4401 -0.2306 -0.1639 -0.0312 153 LYS H CA  
15155 C C   . LYS H  153 ? 2.0994 2.1285 1.7913 -0.2297 -0.1719 -0.0236 153 LYS H C   
15156 O O   . LYS H  153 ? 2.0876 2.1182 1.7924 -0.2224 -0.1717 -0.0210 153 LYS H O   
15157 C CB  . LYS H  153 ? 1.6683 1.6851 1.3424 -0.2381 -0.1605 -0.0385 153 LYS H CB  
15158 C CG  . LYS H  153 ? 1.3946 1.4026 1.0608 -0.2384 -0.1516 -0.0464 153 LYS H CG  
15159 C CD  . LYS H  153 ? 1.4895 1.4927 1.1532 -0.2425 -0.1467 -0.0536 153 LYS H CD  
15160 C CE  . LYS H  153 ? 1.4560 1.4507 1.1094 -0.2451 -0.1384 -0.0614 153 LYS H CE  
15161 N NZ  . LYS H  153 ? 1.4501 1.4448 1.0904 -0.2511 -0.1402 -0.0612 153 LYS H NZ  
15162 N N   . ASN H  154 ? 3.4106 3.4453 3.0962 -0.2373 -0.1787 -0.0201 154 ASN H N   
15163 C CA  . ASN H  154 ? 3.4223 3.4656 3.1164 -0.2372 -0.1868 -0.0123 154 ASN H CA  
15164 C C   . ASN H  154 ? 3.3887 3.4351 3.0933 -0.2286 -0.1890 -0.0052 154 ASN H C   
15165 O O   . ASN H  154 ? 3.4271 3.4797 3.1420 -0.2262 -0.1944 0.0012  154 ASN H O   
15166 C CB  . ASN H  154 ? 3.4736 3.5223 3.1576 -0.2469 -0.1937 -0.0095 154 ASN H CB  
15167 C CG  . ASN H  154 ? 3.5591 3.6067 3.2354 -0.2557 -0.1933 -0.0152 154 ASN H CG  
15168 O OD1 . ASN H  154 ? 3.6034 3.6455 3.2672 -0.2613 -0.1890 -0.0217 154 ASN H OD1 
15169 N ND2 . ASN H  154 ? 3.5372 3.5900 3.2210 -0.2571 -0.1975 -0.0128 154 ASN H ND2 
15170 N N   . GLY H  155 ? 2.3998 2.4417 2.1019 -0.2242 -0.1846 -0.0065 155 GLY H N   
15171 C CA  . GLY H  155 ? 2.2648 2.3089 1.9759 -0.2163 -0.1858 -0.0005 155 GLY H CA  
15172 C C   . GLY H  155 ? 2.3852 2.4354 2.0930 -0.2195 -0.1929 0.0068  155 GLY H C   
15173 O O   . GLY H  155 ? 2.2221 2.2748 1.9370 -0.2138 -0.1947 0.0125  155 GLY H O   
15174 N N   . THR H  156 ? 2.8763 2.9290 2.5735 -0.2288 -0.1969 0.0066  156 THR H N   
15175 C CA  . THR H  156 ? 2.9286 2.9874 2.6215 -0.2328 -0.2038 0.0135  156 THR H CA  
15176 C C   . THR H  156 ? 2.7022 2.7568 2.3809 -0.2366 -0.2012 0.0104  156 THR H C   
15177 O O   . THR H  156 ? 2.7052 2.7596 2.3714 -0.2454 -0.2025 0.0076  156 THR H O   
15178 C CB  . THR H  156 ? 3.0308 3.0962 2.7208 -0.2410 -0.2108 0.0162  156 THR H CB  
15179 O OG1 . THR H  156 ? 2.9646 3.0259 2.6435 -0.2484 -0.2078 0.0083  156 THR H OG1 
15180 C CG2 . THR H  156 ? 3.0486 3.1190 2.7534 -0.2371 -0.2141 0.0203  156 THR H CG2 
15181 N N   . TYR H  157 ? 2.1060 2.1572 1.7869 -0.2302 -0.1976 0.0110  157 TYR H N   
15182 C CA  . TYR H  157 ? 2.0992 2.1458 1.7679 -0.2327 -0.1942 0.0078  157 TYR H CA  
15183 C C   . TYR H  157 ? 2.2606 2.3106 1.9307 -0.2300 -0.1977 0.0151  157 TYR H C   
15184 O O   . TYR H  157 ? 2.0594 2.1081 1.7383 -0.2218 -0.1952 0.0171  157 TYR H O   
15185 C CB  . TYR H  157 ? 1.9383 1.9767 1.6075 -0.2274 -0.1852 0.0005  157 TYR H CB  
15186 C CG  . TYR H  157 ? 1.7528 1.7858 1.4101 -0.2294 -0.1807 -0.0035 157 TYR H CG  
15187 C CD1 . TYR H  157 ? 1.8214 1.8485 1.4678 -0.2348 -0.1756 -0.0116 157 TYR H CD1 
15188 C CD2 . TYR H  157 ? 1.6130 1.6464 1.2707 -0.2258 -0.1810 0.0007  157 TYR H CD2 
15189 C CE1 . TYR H  157 ? 1.7907 1.8126 1.4270 -0.2365 -0.1709 -0.0152 157 TYR H CE1 
15190 C CE2 . TYR H  157 ? 1.7463 1.7745 1.3939 -0.2276 -0.1763 -0.0028 157 TYR H CE2 
15191 C CZ  . TYR H  157 ? 1.7457 1.7682 1.3826 -0.2329 -0.1713 -0.0107 157 TYR H CZ  
15192 O OH  . TYR H  157 ? 1.6463 1.6636 1.2734 -0.2348 -0.1665 -0.0144 157 TYR H OH  
15193 N N   . ASP H  158 ? 3.5325 3.5869 3.1942 -0.2367 -0.2034 0.0194  158 ASP H N   
15194 C CA  . ASP H  158 ? 3.6453 3.7015 3.3062 -0.2346 -0.2056 0.0253  158 ASP H CA  
15195 C C   . ASP H  158 ? 3.3899 3.4385 3.0416 -0.2343 -0.1985 0.0195  158 ASP H C   
15196 O O   . ASP H  158 ? 3.4310 3.4748 3.0718 -0.2397 -0.1946 0.0125  158 ASP H O   
15197 C CB  . ASP H  158 ? 3.8137 3.8774 3.4695 -0.2413 -0.2139 0.0326  158 ASP H CB  
15198 C CG  . ASP H  158 ? 4.0079 4.0717 3.6492 -0.2519 -0.2156 0.0287  158 ASP H CG  
15199 O OD1 . ASP H  158 ? 3.9093 3.9695 3.5377 -0.2565 -0.2133 0.0260  158 ASP H OD1 
15200 O OD2 . ASP H  158 ? 4.2802 4.3478 3.9234 -0.2558 -0.2190 0.0286  158 ASP H OD2 
15201 N N   . TYR H  159 ? 2.7023 2.7497 2.3585 -0.2280 -0.1966 0.0225  159 TYR H N   
15202 C CA  . TYR H  159 ? 2.4001 2.4404 2.0504 -0.2260 -0.1895 0.0174  159 TYR H CA  
15203 C C   . TYR H  159 ? 2.4403 2.4816 2.0812 -0.2298 -0.1918 0.0213  159 TYR H C   
15204 O O   . TYR H  159 ? 2.2300 2.2709 1.8748 -0.2246 -0.1907 0.0246  159 TYR H O   
15205 C CB  . TYR H  159 ? 2.2887 2.3265 1.9516 -0.2158 -0.1850 0.0170  159 TYR H CB  
15206 C CG  . TYR H  159 ? 2.1755 2.2084 1.8365 -0.2116 -0.1793 0.0151  159 TYR H CG  
15207 C CD1 . TYR H  159 ? 2.0782 2.1042 1.7359 -0.2101 -0.1715 0.0072  159 TYR H CD1 
15208 C CD2 . TYR H  159 ? 2.0853 2.1207 1.7488 -0.2089 -0.1818 0.0214  159 TYR H CD2 
15209 C CE1 . TYR H  159 ? 1.8162 1.8380 1.4726 -0.2063 -0.1665 0.0056  159 TYR H CE1 
15210 C CE2 . TYR H  159 ? 1.9074 1.9385 1.5694 -0.2052 -0.1768 0.0197  159 TYR H CE2 
15211 C CZ  . TYR H  159 ? 1.7677 1.7922 1.4262 -0.2040 -0.1692 0.0118  159 TYR H CZ  
15212 O OH  . TYR H  159 ? 1.8887 1.9093 1.5461 -0.2004 -0.1643 0.0102  159 TYR H OH  
15213 N N   . PRO H  160 ? 2.6701 2.7128 2.2984 -0.2390 -0.1949 0.0210  160 PRO H N   
15214 C CA  . PRO H  160 ? 2.3560 2.4004 1.9755 -0.2428 -0.1979 0.0255  160 PRO H CA  
15215 C C   . PRO H  160 ? 1.9138 1.9517 1.5188 -0.2475 -0.1924 0.0193  160 PRO H C   
15216 O O   . PRO H  160 ? 2.0305 2.0704 1.6263 -0.2526 -0.1958 0.0229  160 PRO H O   
15217 C CB  . PRO H  160 ? 2.2900 2.3419 1.9052 -0.2505 -0.2063 0.0305  160 PRO H CB  
15218 C CG  . PRO H  160 ? 2.5623 2.6161 2.1840 -0.2508 -0.2075 0.0282  160 PRO H CG  
15219 C CD  . PRO H  160 ? 2.7279 2.7740 2.3530 -0.2457 -0.1989 0.0199  160 PRO H CD  
15220 N N   . LYS H  161 ? 1.6631 1.6937 1.2662 -0.2458 -0.1845 0.0109  161 LYS H N   
15221 C CA  . LYS H  161 ? 1.7139 1.7389 1.3019 -0.2523 -0.1801 0.0048  161 LYS H CA  
15222 C C   . LYS H  161 ? 1.7393 1.7560 1.3269 -0.2479 -0.1706 -0.0027 161 LYS H C   
15223 O O   . LYS H  161 ? 1.8335 1.8463 1.4236 -0.2464 -0.1659 -0.0090 161 LYS H O   
15224 C CB  . LYS H  161 ? 2.0559 2.0812 1.6352 -0.2610 -0.1817 0.0008  161 LYS H CB  
15225 C CG  . LYS H  161 ? 2.2001 2.2194 1.7635 -0.2685 -0.1769 -0.0063 161 LYS H CG  
15226 C CD  . LYS H  161 ? 2.2733 2.2939 1.8296 -0.2769 -0.1791 -0.0097 161 LYS H CD  
15227 C CE  . LYS H  161 ? 1.9471 1.9616 1.4875 -0.2851 -0.1743 -0.0172 161 LYS H CE  
15228 N NZ  . LYS H  161 ? 1.6387 1.6548 1.1729 -0.2933 -0.1766 -0.0205 161 LYS H NZ  
15229 N N   . TYR H  162 ? 1.7813 1.7954 1.3655 -0.2461 -0.1680 -0.0019 162 TYR H N   
15230 C CA  . TYR H  162 ? 1.7155 1.7223 1.2988 -0.2422 -0.1593 -0.0083 162 TYR H CA  
15231 C C   . TYR H  162 ? 1.8179 1.8200 1.4038 -0.2406 -0.1534 -0.0161 162 TYR H C   
15232 O O   . TYR H  162 ? 1.8034 1.8008 1.3937 -0.2349 -0.1467 -0.0203 162 TYR H O   
15233 C CB  . TYR H  162 ? 1.7093 1.7121 1.2777 -0.2485 -0.1567 -0.0110 162 TYR H CB  
15234 C CG  . TYR H  162 ? 1.7344 1.7311 1.3027 -0.2438 -0.1492 -0.0150 162 TYR H CG  
15235 C CD1 . TYR H  162 ? 1.5099 1.5073 1.0779 -0.2415 -0.1499 -0.0107 162 TYR H CD1 
15236 C CD2 . TYR H  162 ? 1.6001 1.5906 1.1686 -0.2420 -0.1414 -0.0230 162 TYR H CD2 
15237 C CE1 . TYR H  162 ? 1.6589 1.6511 1.2268 -0.2375 -0.1431 -0.0143 162 TYR H CE1 
15238 C CE2 . TYR H  162 ? 1.5190 1.5046 1.0878 -0.2378 -0.1348 -0.0264 162 TYR H CE2 
15239 C CZ  . TYR H  162 ? 1.7237 1.7102 1.2922 -0.2357 -0.1357 -0.0221 162 TYR H CZ  
15240 O OH  . TYR H  162 ? 1.1828 1.1645 0.7516 -0.2317 -0.1291 -0.0256 162 TYR H OH  
15241 N N   . ASP I  7   ? 1.1661 1.1704 0.9242 -0.0940 -0.0621 -0.0431 7   ASP I N   
15242 C CA  . ASP I  7   ? 1.3121 1.3154 1.0682 -0.0966 -0.0669 -0.0393 7   ASP I CA  
15243 C C   . ASP I  7   ? 1.3846 1.3874 1.1418 -0.0968 -0.0693 -0.0385 7   ASP I C   
15244 O O   . ASP I  7   ? 1.5228 1.5236 1.2749 -0.1007 -0.0724 -0.0369 7   ASP I O   
15245 C CB  . ASP I  7   ? 1.3348 1.3408 1.0964 -0.0943 -0.0692 -0.0357 7   ASP I CB  
15246 C CG  . ASP I  7   ? 1.4127 1.4177 1.1698 -0.0967 -0.0692 -0.0348 7   ASP I CG  
15247 O OD1 . ASP I  7   ? 1.0589 1.0636 0.8148 -0.0983 -0.0729 -0.0311 7   ASP I OD1 
15248 O OD2 . ASP I  7   ? 1.4471 1.4517 1.2019 -0.0969 -0.0655 -0.0377 7   ASP I OD2 
15249 N N   . THR I  8   ? 1.3043 1.3091 1.0679 -0.0928 -0.0680 -0.0397 8   THR I N   
15250 C CA  . THR I  8   ? 1.5130 1.5179 1.2791 -0.0924 -0.0707 -0.0384 8   THR I CA  
15251 C C   . THR I  8   ? 1.2256 1.2307 0.9945 -0.0897 -0.0678 -0.0415 8   THR I C   
15252 O O   . THR I  8   ? 1.5354 1.5403 1.3033 -0.0887 -0.0637 -0.0449 8   THR I O   
15253 C CB  . THR I  8   ? 1.3973 1.4050 1.1706 -0.0895 -0.0742 -0.0343 8   THR I CB  
15254 O OG1 . THR I  8   ? 1.0168 1.0275 0.7959 -0.0854 -0.0719 -0.0347 8   THR I OG1 
15255 C CG2 . THR I  8   ? 1.5941 1.6012 1.3643 -0.0927 -0.0784 -0.0304 8   THR I CG2 
15256 N N   . LEU I  9   ? 0.8258 0.8315 0.5983 -0.0885 -0.0702 -0.0402 9   LEU I N   
15257 C CA  . LEU I  9   ? 1.0548 1.0608 0.8302 -0.0859 -0.0680 -0.0427 9   LEU I CA  
15258 C C   . LEU I  9   ? 1.1738 1.1812 0.9545 -0.0844 -0.0719 -0.0396 9   LEU I C   
15259 O O   . LEU I  9   ? 1.0242 1.0308 0.8028 -0.0874 -0.0757 -0.0369 9   LEU I O   
15260 C CB  . LEU I  9   ? 1.0114 1.0134 0.7793 -0.0899 -0.0665 -0.0459 9   LEU I CB  
15261 C CG  . LEU I  9   ? 0.9995 1.0010 0.7698 -0.0883 -0.0659 -0.0474 9   LEU I CG  
15262 C CD1 . LEU I  9   ? 0.9459 0.9489 0.7200 -0.0839 -0.0615 -0.0503 9   LEU I CD1 
15263 C CD2 . LEU I  9   ? 1.1432 1.1406 0.9059 -0.0933 -0.0660 -0.0497 9   LEU I CD2 
15264 N N   . CYS I  10  ? 1.4432 1.4528 1.2306 -0.0799 -0.0709 -0.0399 10  CYS I N   
15265 C CA  . CYS I  10  ? 1.2908 1.3020 1.0837 -0.0783 -0.0745 -0.0367 10  CYS I CA  
15266 C C   . CYS I  10  ? 1.2250 1.2366 1.0216 -0.0756 -0.0737 -0.0381 10  CYS I C   
15267 O O   . CYS I  10  ? 1.3220 1.3344 1.1202 -0.0728 -0.0701 -0.0408 10  CYS I O   
15268 C CB  . CYS I  10  ? 1.2008 1.2152 0.9999 -0.0752 -0.0758 -0.0338 10  CYS I CB  
15269 S SG  . CYS I  10  ? 1.5267 1.5409 1.3223 -0.0777 -0.0766 -0.0321 10  CYS I SG  
15270 N N   . ILE I  11  ? 1.2443 1.2555 1.0424 -0.0765 -0.0771 -0.0361 11  ILE I N   
15271 C CA  . ILE I  11  ? 1.3753 1.3866 1.1770 -0.0743 -0.0766 -0.0371 11  ILE I CA  
15272 C C   . ILE I  11  ? 1.2243 1.2388 1.0345 -0.0701 -0.0784 -0.0341 11  ILE I C   
15273 O O   . ILE I  11  ? 1.1461 1.1615 0.9580 -0.0709 -0.0822 -0.0307 11  ILE I O   
15274 C CB  . ILE I  11  ? 1.2999 1.3083 1.0978 -0.0786 -0.0790 -0.0369 11  ILE I CB  
15275 C CG1 . ILE I  11  ? 1.3584 1.3643 1.1470 -0.0842 -0.0797 -0.0380 11  ILE I CG1 
15276 C CG2 . ILE I  11  ? 1.1917 1.1986 0.9915 -0.0775 -0.0760 -0.0394 11  ILE I CG2 
15277 C CD1 . ILE I  11  ? 1.1331 1.1352 0.9157 -0.0882 -0.0780 -0.0411 11  ILE I CD1 
15278 N N   . GLY I  12  ? 1.6620 1.6781 1.4777 -0.0656 -0.0755 -0.0351 12  GLY I N   
15279 C CA  . GLY I  12  ? 1.5574 1.5765 1.3810 -0.0615 -0.0767 -0.0326 12  GLY I CA  
15280 C C   . GLY I  12  ? 1.4236 1.4429 1.2522 -0.0585 -0.0749 -0.0333 12  GLY I C   
15281 O O   . GLY I  12  ? 1.2433 1.2605 1.0698 -0.0592 -0.0724 -0.0358 12  GLY I O   
15282 N N   . TYR I  13  ? 1.0796 1.1013 0.9151 -0.0550 -0.0761 -0.0310 13  TYR I N   
15283 C CA  . TYR I  13  ? 1.0495 1.0719 0.8902 -0.0515 -0.0741 -0.0314 13  TYR I CA  
15284 C C   . TYR I  13  ? 1.0240 1.0500 0.8693 -0.0469 -0.0715 -0.0316 13  TYR I C   
15285 O O   . TYR I  13  ? 1.0125 1.0405 0.8572 -0.0465 -0.0716 -0.0313 13  TYR I O   
15286 C CB  . TYR I  13  ? 0.7041 0.7261 0.5491 -0.0514 -0.0771 -0.0288 13  TYR I CB  
15287 C CG  . TYR I  13  ? 0.7777 0.8008 0.6243 -0.0524 -0.0811 -0.0255 13  TYR I CG  
15288 C CD1 . TYR I  13  ? 0.7092 0.7350 0.5623 -0.0489 -0.0816 -0.0234 13  TYR I CD1 
15289 C CD2 . TYR I  13  ? 0.7477 0.7692 0.5894 -0.0569 -0.0843 -0.0244 13  TYR I CD2 
15290 C CE1 . TYR I  13  ? 0.6839 0.7104 0.5388 -0.0496 -0.0848 -0.0203 13  TYR I CE1 
15291 C CE2 . TYR I  13  ? 0.6365 0.6591 0.4802 -0.0576 -0.0878 -0.0210 13  TYR I CE2 
15292 C CZ  . TYR I  13  ? 0.7560 0.7810 0.6066 -0.0539 -0.0879 -0.0190 13  TYR I CZ  
15293 O OH  . TYR I  13  ? 0.8001 0.8260 0.6533 -0.0544 -0.0909 -0.0156 13  TYR I OH  
15294 N N   . HIS I  14  ? 1.0811 1.1080 0.9308 -0.0434 -0.0692 -0.0321 14  HIS I N   
15295 C CA  . HIS I  14  ? 0.8502 0.8808 0.7040 -0.0391 -0.0666 -0.0323 14  HIS I CA  
15296 C C   . HIS I  14  ? 0.9901 1.0233 0.8490 -0.0368 -0.0686 -0.0297 14  HIS I C   
15297 O O   . HIS I  14  ? 0.9729 1.0050 0.8340 -0.0375 -0.0715 -0.0276 14  HIS I O   
15298 C CB  . HIS I  14  ? 1.0480 1.0785 0.9047 -0.0363 -0.0634 -0.0334 14  HIS I CB  
15299 C CG  . HIS I  14  ? 1.1807 1.2154 1.0417 -0.0318 -0.0608 -0.0334 14  HIS I CG  
15300 N ND1 . HIS I  14  ? 1.2890 1.3253 1.1488 -0.0306 -0.0574 -0.0353 14  HIS I ND1 
15301 C CD2 . HIS I  14  ? 1.2022 1.2400 1.0688 -0.0283 -0.0611 -0.0316 14  HIS I CD2 
15302 C CE1 . HIS I  14  ? 1.3575 1.3981 1.2219 -0.0266 -0.0559 -0.0345 14  HIS I CE1 
15303 N NE2 . HIS I  14  ? 1.1800 1.2215 1.0483 -0.0252 -0.0581 -0.0324 14  HIS I NE2 
15304 N N   . ALA I  15  ? 0.8812 0.9181 0.7422 -0.0341 -0.0670 -0.0299 15  ALA I N   
15305 C CA  . ALA I  15  ? 0.9291 0.9688 0.7953 -0.0315 -0.0679 -0.0280 15  ALA I CA  
15306 C C   . ALA I  15  ? 0.8902 0.9339 0.7591 -0.0277 -0.0648 -0.0290 15  ALA I C   
15307 O O   . ALA I  15  ? 1.0307 1.0753 0.8971 -0.0276 -0.0623 -0.0310 15  ALA I O   
15308 C CB  . ALA I  15  ? 0.8578 0.8980 0.7228 -0.0333 -0.0700 -0.0269 15  ALA I CB  
15309 N N   . ASN I  16  ? 0.9704 1.0165 0.8444 -0.0247 -0.0647 -0.0275 16  ASN I N   
15310 C CA  . ASN I  16  ? 1.1951 1.2455 1.0717 -0.0212 -0.0620 -0.0282 16  ASN I CA  
15311 C C   . ASN I  16  ? 1.2064 1.2595 1.0874 -0.0190 -0.0626 -0.0266 16  ASN I C   
15312 O O   . ASN I  16  ? 1.1640 1.2156 1.0462 -0.0202 -0.0649 -0.0251 16  ASN I O   
15313 C CB  . ASN I  16  ? 1.2762 1.3264 1.1544 -0.0190 -0.0596 -0.0287 16  ASN I CB  
15314 C CG  . ASN I  16  ? 1.1926 1.2401 1.0739 -0.0183 -0.0607 -0.0271 16  ASN I CG  
15315 O OD1 . ASN I  16  ? 1.0159 1.0625 0.8991 -0.0189 -0.0632 -0.0255 16  ASN I OD1 
15316 N ND2 . ASN I  16  ? 1.1563 1.2025 1.0385 -0.0171 -0.0587 -0.0277 16  ASN I ND2 
15317 N N   . ASN I  17  ? 1.1982 1.2555 1.0818 -0.0158 -0.0604 -0.0268 17  ASN I N   
15318 C CA  . ASN I  17  ? 1.2000 1.2601 1.0873 -0.0138 -0.0606 -0.0256 17  ASN I CA  
15319 C C   . ASN I  17  ? 1.3262 1.3852 1.2178 -0.0117 -0.0609 -0.0238 17  ASN I C   
15320 O O   . ASN I  17  ? 1.3756 1.4373 1.2705 -0.0093 -0.0602 -0.0230 17  ASN I O   
15321 C CB  . ASN I  17  ? 1.4737 1.5395 1.3616 -0.0117 -0.0584 -0.0265 17  ASN I CB  
15322 C CG  . ASN I  17  ? 1.6287 1.6962 1.5177 -0.0091 -0.0560 -0.0268 17  ASN I CG  
15323 O OD1 . ASN I  17  ? 1.6611 1.7259 1.5516 -0.0082 -0.0558 -0.0260 17  ASN I OD1 
15324 N ND2 . ASN I  17  ? 1.7539 1.8261 1.6424 -0.0079 -0.0541 -0.0278 17  ASN I ND2 
15325 N N   . SER I  18  ? 1.3279 1.3828 1.2193 -0.0127 -0.0617 -0.0234 18  SER I N   
15326 C CA  . SER I  18  ? 1.2537 1.3072 1.1492 -0.0108 -0.0618 -0.0219 18  SER I CA  
15327 C C   . SER I  18  ? 1.0706 1.1232 0.9692 -0.0111 -0.0639 -0.0200 18  SER I C   
15328 O O   . SER I  18  ? 0.9489 0.9996 0.8462 -0.0137 -0.0661 -0.0195 18  SER I O   
15329 C CB  . SER I  18  ? 1.2455 1.2948 1.1396 -0.0123 -0.0622 -0.0222 18  SER I CB  
15330 O OG  . SER I  18  ? 1.0671 1.1152 0.9653 -0.0103 -0.0618 -0.0209 18  SER I OG  
15331 N N   . THR I  19  ? 1.2181 1.2722 1.1210 -0.0082 -0.0630 -0.0188 19  THR I N   
15332 C CA  . THR I  19  ? 1.1720 1.2251 1.0786 -0.0081 -0.0644 -0.0170 19  THR I CA  
15333 C C   . THR I  19  ? 1.1276 1.1778 1.0376 -0.0073 -0.0649 -0.0155 19  THR I C   
15334 O O   . THR I  19  ? 1.0271 1.0761 0.9408 -0.0070 -0.0660 -0.0138 19  THR I O   
15335 C CB  . THR I  19  ? 1.0821 1.1390 0.9910 -0.0058 -0.0628 -0.0168 19  THR I CB  
15336 O OG1 . THR I  19  ? 1.3431 1.4026 1.2531 -0.0027 -0.0605 -0.0170 19  THR I OG1 
15337 C CG2 . THR I  19  ? 1.1975 1.2570 1.1032 -0.0071 -0.0625 -0.0182 19  THR I CG2 
15338 N N   . ASP I  20  ? 1.0235 1.0725 0.9324 -0.0069 -0.0639 -0.0163 20  ASP I N   
15339 C CA  . ASP I  20  ? 0.9033 0.9494 0.8151 -0.0064 -0.0642 -0.0153 20  ASP I CA  
15340 C C   . ASP I  20  ? 0.9021 0.9450 0.8149 -0.0092 -0.0674 -0.0139 20  ASP I C   
15341 O O   . ASP I  20  ? 0.9932 1.0348 0.9026 -0.0123 -0.0693 -0.0143 20  ASP I O   
15342 C CB  . ASP I  20  ? 1.0079 1.0524 0.9173 -0.0067 -0.0628 -0.0167 20  ASP I CB  
15343 C CG  . ASP I  20  ? 1.1056 1.1533 1.0155 -0.0034 -0.0594 -0.0174 20  ASP I CG  
15344 O OD1 . ASP I  20  ? 0.9740 1.0207 0.8821 -0.0034 -0.0577 -0.0186 20  ASP I OD1 
15345 O OD2 . ASP I  20  ? 1.0073 1.0584 0.9194 -0.0009 -0.0585 -0.0166 20  ASP I OD2 
15346 N N   . THR I  21  ? 0.8931 0.9349 0.8108 -0.0080 -0.0679 -0.0121 21  THR I N   
15347 C CA  . THR I  21  ? 0.8504 0.8895 0.7700 -0.0104 -0.0710 -0.0103 21  THR I CA  
15348 C C   . THR I  21  ? 0.7417 0.7785 0.6644 -0.0100 -0.0711 -0.0096 21  THR I C   
15349 O O   . THR I  21  ? 0.8660 0.9033 0.7919 -0.0070 -0.0689 -0.0093 21  THR I O   
15350 C CB  . THR I  21  ? 0.7639 0.8039 0.6874 -0.0097 -0.0718 -0.0085 21  THR I CB  
15351 O OG1 . THR I  21  ? 1.0246 1.0664 0.9517 -0.0062 -0.0694 -0.0081 21  THR I OG1 
15352 C CG2 . THR I  21  ? 0.8356 0.8771 0.7559 -0.0111 -0.0722 -0.0091 21  THR I CG2 
15353 N N   . VAL I  22  ? 0.8426 0.8768 0.7641 -0.0132 -0.0736 -0.0092 22  VAL I N   
15354 C CA  . VAL I  22  ? 0.6844 0.7163 0.6088 -0.0136 -0.0741 -0.0086 22  VAL I CA  
15355 C C   . VAL I  22  ? 0.7281 0.7588 0.6556 -0.0159 -0.0777 -0.0062 22  VAL I C   
15356 O O   . VAL I  22  ? 0.7714 0.8028 0.6980 -0.0175 -0.0797 -0.0051 22  VAL I O   
15357 C CB  . VAL I  22  ? 0.5828 0.6127 0.5027 -0.0157 -0.0736 -0.0107 22  VAL I CB  
15358 C CG1 . VAL I  22  ? 0.5825 0.6137 0.4991 -0.0138 -0.0702 -0.0130 22  VAL I CG1 
15359 C CG2 . VAL I  22  ? 0.5751 0.6037 0.4907 -0.0203 -0.0768 -0.0108 22  VAL I CG2 
15360 N N   . ASP I  23  ? 0.6318 0.6608 0.5630 -0.0160 -0.0783 -0.0052 23  ASP I N   
15361 C CA  . ASP I  23  ? 0.6589 0.6870 0.5934 -0.0183 -0.0818 -0.0027 23  ASP I CA  
15362 C C   . ASP I  23  ? 0.6585 0.6847 0.5904 -0.0220 -0.0838 -0.0034 23  ASP I C   
15363 O O   . ASP I  23  ? 0.6518 0.6766 0.5817 -0.0219 -0.0818 -0.0055 23  ASP I O   
15364 C CB  . ASP I  23  ? 0.7822 0.8103 0.7242 -0.0158 -0.0813 -0.0006 23  ASP I CB  
15365 C CG  . ASP I  23  ? 0.9298 0.9596 0.8747 -0.0130 -0.0799 0.0005  23  ASP I CG  
15366 O OD1 . ASP I  23  ? 1.1155 1.1468 1.0568 -0.0130 -0.0794 -0.0005 23  ASP I OD1 
15367 O OD2 . ASP I  23  ? 0.8789 0.9086 0.8299 -0.0109 -0.0793 0.0022  23  ASP I OD2 
15368 N N   . THR I  24  ? 0.5685 0.5945 0.5002 -0.0254 -0.0876 -0.0016 24  THR I N   
15369 C CA  . THR I  24  ? 0.6170 0.6415 0.5466 -0.0294 -0.0900 -0.0018 24  THR I CA  
15370 C C   . THR I  24  ? 0.6440 0.6688 0.5802 -0.0302 -0.0929 0.0014  24  THR I C   
15371 O O   . THR I  24  ? 0.5193 0.5451 0.4615 -0.0274 -0.0925 0.0035  24  THR I O   
15372 C CB  . THR I  24  ? 0.7727 0.7973 0.6956 -0.0334 -0.0925 -0.0023 24  THR I CB  
15373 O OG1 . THR I  24  ? 0.8489 0.8750 0.7742 -0.0343 -0.0955 0.0008  24  THR I OG1 
15374 C CG2 . THR I  24  ? 0.6145 0.6392 0.5316 -0.0324 -0.0896 -0.0052 24  THR I CG2 
15375 N N   . VAL I  25  ? 0.7838 0.8078 0.7188 -0.0341 -0.0957 0.0017  25  VAL I N   
15376 C CA  . VAL I  25  ? 0.6873 0.7119 0.6285 -0.0353 -0.0989 0.0049  25  VAL I CA  
15377 C C   . VAL I  25  ? 0.6970 0.7235 0.6398 -0.0364 -0.1022 0.0083  25  VAL I C   
15378 O O   . VAL I  25  ? 0.6228 0.6504 0.5727 -0.0354 -0.1037 0.0116  25  VAL I O   
15379 C CB  . VAL I  25  ? 0.6512 0.6749 0.5901 -0.0398 -0.1013 0.0043  25  VAL I CB  
15380 C CG1 . VAL I  25  ? 0.6682 0.6923 0.6148 -0.0399 -0.1031 0.0069  25  VAL I CG1 
15381 C CG2 . VAL I  25  ? 0.7373 0.7586 0.6711 -0.0400 -0.0979 0.0001  25  VAL I CG2 
15382 N N   . LEU I  26  ? 0.7263 0.7531 0.6626 -0.0385 -0.1031 0.0075  26  LEU I N   
15383 C CA  . LEU I  26  ? 0.6519 0.6803 0.5888 -0.0401 -0.1063 0.0106  26  LEU I CA  
15384 C C   . LEU I  26  ? 0.6944 0.7235 0.6329 -0.0367 -0.1042 0.0112  26  LEU I C   
15385 O O   . LEU I  26  ? 0.7412 0.7714 0.6830 -0.0369 -0.1061 0.0144  26  LEU I O   
15386 C CB  . LEU I  26  ? 0.5678 0.5961 0.4966 -0.0446 -0.1087 0.0097  26  LEU I CB  
15387 C CG  . LEU I  26  ? 0.6720 0.7004 0.5993 -0.0494 -0.1125 0.0106  26  LEU I CG  
15388 C CD1 . LEU I  26  ? 0.7832 0.8112 0.7163 -0.0487 -0.1123 0.0108  26  LEU I CD1 
15389 C CD2 . LEU I  26  ? 0.5727 0.5998 0.4904 -0.0531 -0.1124 0.0072  26  LEU I CD2 
15390 N N   . GLU I  27  ? 0.8027 0.8312 0.7389 -0.0338 -0.1002 0.0081  27  GLU I N   
15391 C CA  . GLU I  27  ? 0.7569 0.7863 0.6931 -0.0313 -0.0981 0.0080  27  GLU I CA  
15392 C C   . GLU I  27  ? 0.8365 0.8659 0.7747 -0.0269 -0.0938 0.0060  27  GLU I C   
15393 O O   . GLU I  27  ? 0.8470 0.8756 0.7835 -0.0261 -0.0918 0.0037  27  GLU I O   
15394 C CB  . GLU I  27  ? 0.9118 0.9413 0.8401 -0.0335 -0.0983 0.0062  27  GLU I CB  
15395 C CG  . GLU I  27  ? 1.0862 1.1168 1.0146 -0.0323 -0.0976 0.0070  27  GLU I CG  
15396 C CD  . GLU I  27  ? 1.2605 1.2910 1.1814 -0.0352 -0.0987 0.0059  27  GLU I CD  
15397 O OE1 . GLU I  27  ? 1.0922 1.1234 1.0118 -0.0343 -0.0973 0.0055  27  GLU I OE1 
15398 O OE2 . GLU I  27  ? 1.2704 1.3002 1.1868 -0.0387 -0.1008 0.0053  27  GLU I OE2 
15399 N N   . LYS I  28  ? 0.8313 0.8617 0.7731 -0.0243 -0.0923 0.0071  28  LYS I N   
15400 C CA  . LYS I  28  ? 0.7892 0.8200 0.7327 -0.0203 -0.0884 0.0055  28  LYS I CA  
15401 C C   . LYS I  28  ? 0.9210 0.9530 0.8596 -0.0194 -0.0861 0.0032  28  LYS I C   
15402 O O   . LYS I  28  ? 1.0078 1.0402 0.9431 -0.0213 -0.0874 0.0034  28  LYS I O   
15403 C CB  . LYS I  28  ? 0.7988 0.8298 0.7501 -0.0180 -0.0878 0.0080  28  LYS I CB  
15404 C CG  . LYS I  28  ? 0.7932 0.8232 0.7500 -0.0171 -0.0880 0.0092  28  LYS I CG  
15405 C CD  . LYS I  28  ? 0.9733 1.0035 0.9378 -0.0147 -0.0869 0.0116  28  LYS I CD  
15406 C CE  . LYS I  28  ? 1.1345 1.1637 1.1039 -0.0128 -0.0857 0.0120  28  LYS I CE  
15407 N NZ  . LYS I  28  ? 1.2343 1.2627 1.2045 -0.0155 -0.0887 0.0128  28  LYS I NZ  
15408 N N   . ASN I  29  ? 0.9365 0.9693 0.8747 -0.0163 -0.0827 0.0012  29  ASN I N   
15409 C CA  . ASN I  29  ? 0.7658 0.8003 0.6999 -0.0152 -0.0804 -0.0010 29  ASN I CA  
15410 C C   . ASN I  29  ? 0.7650 0.7996 0.6925 -0.0181 -0.0817 -0.0023 29  ASN I C   
15411 O O   . ASN I  29  ? 0.8809 0.9163 0.8070 -0.0189 -0.0820 -0.0021 29  ASN I O   
15412 C CB  . ASN I  29  ? 0.8481 0.8839 0.7856 -0.0133 -0.0790 0.0000  29  ASN I CB  
15413 C CG  . ASN I  29  ? 1.2688 1.3052 1.2109 -0.0098 -0.0764 0.0001  29  ASN I CG  
15414 O OD1 . ASN I  29  ? 1.2754 1.3132 1.2154 -0.0077 -0.0738 -0.0018 29  ASN I OD1 
15415 N ND2 . ASN I  29  ? 1.2922 1.3275 1.2405 -0.0092 -0.0769 0.0026  29  ASN I ND2 
15416 N N   . VAL I  30  ? 0.6895 0.7230 0.6131 -0.0198 -0.0822 -0.0038 30  VAL I N   
15417 C CA  . VAL I  30  ? 0.6018 0.6351 0.5187 -0.0226 -0.0830 -0.0054 30  VAL I CA  
15418 C C   . VAL I  30  ? 0.6973 0.7319 0.6102 -0.0210 -0.0798 -0.0084 30  VAL I C   
15419 O O   . VAL I  30  ? 0.7510 0.7853 0.6642 -0.0193 -0.0777 -0.0096 30  VAL I O   
15420 C CB  . VAL I  30  ? 0.6246 0.6558 0.5389 -0.0261 -0.0854 -0.0054 30  VAL I CB  
15421 C CG1 . VAL I  30  ? 0.4921 0.5228 0.3989 -0.0289 -0.0856 -0.0074 30  VAL I CG1 
15422 C CG2 . VAL I  30  ? 0.6455 0.6760 0.5635 -0.0281 -0.0891 -0.0021 30  VAL I CG2 
15423 N N   . THR I  31  ? 0.6194 0.6555 0.5290 -0.0214 -0.0792 -0.0093 31  THR I N   
15424 C CA  . THR I  31  ? 0.7561 0.7939 0.6622 -0.0198 -0.0762 -0.0120 31  THR I CA  
15425 C C   . THR I  31  ? 0.7006 0.7369 0.6014 -0.0220 -0.0760 -0.0140 31  THR I C   
15426 O O   . THR I  31  ? 0.8269 0.8618 0.7237 -0.0254 -0.0780 -0.0141 31  THR I O   
15427 C CB  . THR I  31  ? 0.7565 0.7965 0.6608 -0.0198 -0.0756 -0.0125 31  THR I CB  
15428 O OG1 . THR I  31  ? 0.6510 0.6923 0.5602 -0.0179 -0.0753 -0.0109 31  THR I OG1 
15429 C CG2 . THR I  31  ? 0.8145 0.8570 0.7158 -0.0182 -0.0726 -0.0151 31  THR I CG2 
15430 N N   . VAL I  32  ? 0.6566 0.6931 0.5573 -0.0200 -0.0733 -0.0156 32  VAL I N   
15431 C CA  . VAL I  32  ? 0.7599 0.7947 0.6559 -0.0218 -0.0724 -0.0177 32  VAL I CA  
15432 C C   . VAL I  32  ? 0.8053 0.8423 0.6988 -0.0200 -0.0691 -0.0198 32  VAL I C   
15433 O O   . VAL I  32  ? 0.8845 0.9247 0.7808 -0.0168 -0.0674 -0.0196 32  VAL I O   
15434 C CB  . VAL I  32  ? 0.6844 0.7169 0.5824 -0.0215 -0.0718 -0.0178 32  VAL I CB  
15435 C CG1 . VAL I  32  ? 0.6808 0.7110 0.5802 -0.0243 -0.0753 -0.0160 32  VAL I CG1 
15436 C CG2 . VAL I  32  ? 0.6910 0.7252 0.5943 -0.0171 -0.0693 -0.0171 32  VAL I CG2 
15437 N N   . THR I  33  ? 0.7955 0.8312 0.6840 -0.0222 -0.0683 -0.0219 33  THR I N   
15438 C CA  . THR I  33  ? 0.6751 0.7128 0.5613 -0.0207 -0.0652 -0.0238 33  THR I CA  
15439 C C   . THR I  33  ? 0.8594 0.8982 0.7491 -0.0170 -0.0620 -0.0241 33  THR I C   
15440 O O   . THR I  33  ? 0.9913 1.0336 0.8819 -0.0143 -0.0597 -0.0245 33  THR I O   
15441 C CB  . THR I  33  ? 0.8261 0.8615 0.7063 -0.0241 -0.0648 -0.0260 33  THR I CB  
15442 O OG1 . THR I  33  ? 0.7975 0.8293 0.6769 -0.0257 -0.0645 -0.0267 33  THR I OG1 
15443 C CG2 . THR I  33  ? 0.9268 0.9615 0.8033 -0.0278 -0.0679 -0.0256 33  THR I CG2 
15444 N N   . HIS I  34  ? 0.9647 1.0008 0.8564 -0.0170 -0.0620 -0.0237 34  HIS I N   
15445 C CA  . HIS I  34  ? 0.8194 0.8560 0.7146 -0.0136 -0.0588 -0.0237 34  HIS I CA  
15446 C C   . HIS I  34  ? 0.8420 0.8765 0.7414 -0.0129 -0.0596 -0.0222 34  HIS I C   
15447 O O   . HIS I  34  ? 0.9097 0.9420 0.8090 -0.0156 -0.0627 -0.0213 34  HIS I O   
15448 C CB  . HIS I  34  ? 0.8270 0.8617 0.7190 -0.0143 -0.0558 -0.0260 34  HIS I CB  
15449 C CG  . HIS I  34  ? 0.9193 0.9560 0.8074 -0.0151 -0.0548 -0.0275 34  HIS I CG  
15450 N ND1 . HIS I  34  ? 0.9712 1.0069 0.8546 -0.0188 -0.0571 -0.0283 34  HIS I ND1 
15451 C CD2 . HIS I  34  ? 1.0282 1.0677 0.9165 -0.0126 -0.0516 -0.0283 34  HIS I CD2 
15452 C CE1 . HIS I  34  ? 1.0654 1.1032 0.9462 -0.0186 -0.0553 -0.0297 34  HIS I CE1 
15453 N NE2 . HIS I  34  ? 1.1253 1.1655 1.0091 -0.0149 -0.0520 -0.0297 34  HIS I NE2 
15454 N N   . SER I  35  ? 0.8442 0.8794 0.7474 -0.0094 -0.0568 -0.0218 35  SER I N   
15455 C CA  . SER I  35  ? 0.7944 0.8280 0.7022 -0.0082 -0.0573 -0.0202 35  SER I CA  
15456 C C   . SER I  35  ? 0.7304 0.7649 0.6418 -0.0041 -0.0535 -0.0198 35  SER I C   
15457 O O   . SER I  35  ? 0.8010 0.8388 0.7125 -0.0014 -0.0512 -0.0199 35  SER I O   
15458 C CB  . SER I  35  ? 0.6762 0.7116 0.5870 -0.0074 -0.0598 -0.0181 35  SER I CB  
15459 O OG  . SER I  35  ? 0.7943 0.8340 0.7063 -0.0044 -0.0584 -0.0176 35  SER I OG  
15460 N N   . VAL I  36  ? 0.7666 0.7984 0.6811 -0.0037 -0.0530 -0.0193 36  VAL I N   
15461 C CA  . VAL I  36  ? 0.7170 0.7494 0.6356 0.0003  -0.0495 -0.0185 36  VAL I CA  
15462 C C   . VAL I  36  ? 0.6734 0.7055 0.5969 0.0018  -0.0507 -0.0164 36  VAL I C   
15463 O O   . VAL I  36  ? 0.6078 0.6378 0.5317 -0.0009 -0.0537 -0.0159 36  VAL I O   
15464 C CB  . VAL I  36  ? 0.7131 0.7419 0.6309 -0.0004 -0.0465 -0.0201 36  VAL I CB  
15465 C CG1 . VAL I  36  ? 0.7847 0.8135 0.6976 -0.0020 -0.0451 -0.0223 36  VAL I CG1 
15466 C CG2 . VAL I  36  ? 0.6733 0.6975 0.5910 -0.0039 -0.0484 -0.0207 36  VAL I CG2 
15467 N N   . ASN I  37  ? 0.9191 0.9531 0.8464 0.0059  -0.0482 -0.0150 37  ASN I N   
15468 C CA  . ASN I  37  ? 0.8046 0.8382 0.7368 0.0076  -0.0488 -0.0130 37  ASN I CA  
15469 C C   . ASN I  37  ? 0.5603 0.5905 0.4953 0.0084  -0.0464 -0.0130 37  ASN I C   
15470 O O   . ASN I  37  ? 0.6826 0.7130 0.6181 0.0108  -0.0428 -0.0133 37  ASN I O   
15471 C CB  . ASN I  37  ? 0.7070 0.7450 0.6415 0.0114  -0.0478 -0.0113 37  ASN I CB  
15472 C CG  . ASN I  37  ? 0.8008 0.8385 0.7396 0.0123  -0.0490 -0.0094 37  ASN I CG  
15473 O OD1 . ASN I  37  ? 0.9404 0.9811 0.8814 0.0152  -0.0480 -0.0080 37  ASN I OD1 
15474 N ND2 . ASN I  37  ? 0.7244 0.7585 0.6644 0.0097  -0.0513 -0.0093 37  ASN I ND2 
15475 N N   . LEU I  38  ? 0.5100 0.5370 0.4470 0.0064  -0.0483 -0.0127 38  LEU I N   
15476 C CA  . LEU I  38  ? 0.5818 0.6053 0.5217 0.0068  -0.0462 -0.0128 38  LEU I CA  
15477 C C   . LEU I  38  ? 0.5427 0.5672 0.4881 0.0107  -0.0447 -0.0106 38  LEU I C   
15478 O O   . LEU I  38  ? 0.5666 0.5886 0.5151 0.0118  -0.0423 -0.0103 38  LEU I O   
15479 C CB  . LEU I  38  ? 0.4806 0.5005 0.4199 0.0023  -0.0490 -0.0136 38  LEU I CB  
15480 C CG  . LEU I  38  ? 0.4795 0.4975 0.4131 -0.0021 -0.0501 -0.0161 38  LEU I CG  
15481 C CD1 . LEU I  38  ? 0.7755 0.7912 0.7087 -0.0066 -0.0540 -0.0162 38  LEU I CD1 
15482 C CD2 . LEU I  38  ? 0.5448 0.5603 0.4771 -0.0018 -0.0460 -0.0181 38  LEU I CD2 
15483 N N   . LEU I  39  ? 0.6173 0.6453 0.5638 0.0125  -0.0458 -0.0090 39  LEU I N   
15484 C CA  . LEU I  39  ? 0.5695 0.5986 0.5208 0.0160  -0.0445 -0.0068 39  LEU I CA  
15485 C C   . LEU I  39  ? 0.6394 0.6724 0.5908 0.0201  -0.0415 -0.0059 39  LEU I C   
15486 O O   . LEU I  39  ? 0.7327 0.7693 0.6814 0.0205  -0.0422 -0.0060 39  LEU I O   
15487 C CB  . LEU I  39  ? 0.5134 0.5435 0.4664 0.0152  -0.0476 -0.0055 39  LEU I CB  
15488 C CG  . LEU I  39  ? 0.5246 0.5558 0.4821 0.0185  -0.0463 -0.0034 39  LEU I CG  
15489 C CD1 . LEU I  39  ? 0.5413 0.5693 0.5030 0.0196  -0.0444 -0.0027 39  LEU I CD1 
15490 C CD2 . LEU I  39  ? 0.5536 0.5857 0.5127 0.0174  -0.0491 -0.0023 39  LEU I CD2 
15491 N N   . GLU I  40  ? 0.6666 0.6988 0.6212 0.0232  -0.0382 -0.0048 40  GLU I N   
15492 C CA  . GLU I  40  ? 0.6356 0.6718 0.5910 0.0273  -0.0354 -0.0033 40  GLU I CA  
15493 C C   . GLU I  40  ? 0.6233 0.6618 0.5814 0.0295  -0.0359 -0.0013 40  GLU I C   
15494 O O   . GLU I  40  ? 0.5877 0.6236 0.5494 0.0298  -0.0359 -0.0003 40  GLU I O   
15495 C CB  . GLU I  40  ? 0.5144 0.5487 0.4721 0.0298  -0.0314 -0.0029 40  GLU I CB  
15496 C CG  . GLU I  40  ? 0.6644 0.7031 0.6233 0.0343  -0.0284 -0.0009 40  GLU I CG  
15497 C CD  . GLU I  40  ? 0.7979 0.8411 0.7531 0.0344  -0.0286 -0.0015 40  GLU I CD  
15498 O OE1 . GLU I  40  ? 0.9721 1.0159 0.9271 0.0359  -0.0257 -0.0015 40  GLU I OE1 
15499 O OE2 . GLU I  40  ? 0.8524 0.8984 0.8051 0.0330  -0.0314 -0.0019 40  GLU I OE2 
15500 N N   . ASP I  41  ? 0.7012 0.7445 0.6574 0.0308  -0.0362 -0.0007 41  ASP I N   
15501 C CA  . ASP I  41  ? 0.7462 0.7919 0.7041 0.0324  -0.0366 0.0010  41  ASP I CA  
15502 C C   . ASP I  41  ? 0.8149 0.8661 0.7721 0.0357  -0.0345 0.0023  41  ASP I C   
15503 O O   . ASP I  41  ? 1.0992 1.1540 1.0554 0.0361  -0.0354 0.0028  41  ASP I O   
15504 C CB  . ASP I  41  ? 0.8922 0.9384 0.8484 0.0295  -0.0400 0.0001  41  ASP I CB  
15505 C CG  . ASP I  41  ? 1.1397 1.1887 1.0912 0.0277  -0.0413 -0.0015 41  ASP I CG  
15506 O OD1 . ASP I  41  ? 1.1663 1.2171 1.1161 0.0289  -0.0395 -0.0019 41  ASP I OD1 
15507 O OD2 . ASP I  41  ? 1.1242 1.1735 1.0742 0.0253  -0.0438 -0.0023 41  ASP I OD2 
15508 N N   . LYS I  42  ? 0.7969 0.8488 0.7547 0.0381  -0.0317 0.0030  42  LYS I N   
15509 C CA  . LYS I  42  ? 0.8993 0.9569 0.8564 0.0412  -0.0298 0.0045  42  LYS I CA  
15510 C C   . LYS I  42  ? 0.8331 0.8904 0.7935 0.0448  -0.0262 0.0065  42  LYS I C   
15511 O O   . LYS I  42  ? 0.7976 0.8524 0.7585 0.0448  -0.0244 0.0059  42  LYS I O   
15512 C CB  . LYS I  42  ? 0.9031 0.9639 0.8565 0.0399  -0.0305 0.0030  42  LYS I CB  
15513 C CG  . LYS I  42  ? 1.2691 1.3365 1.2203 0.0409  -0.0311 0.0037  42  LYS I CG  
15514 C CD  . LYS I  42  ? 1.5126 1.5820 1.4598 0.0383  -0.0328 0.0016  42  LYS I CD  
15515 C CE  . LYS I  42  ? 1.4224 1.4874 1.3680 0.0343  -0.0358 -0.0006 42  LYS I CE  
15516 N NZ  . LYS I  42  ? 1.3412 1.4075 1.2829 0.0317  -0.0372 -0.0027 42  LYS I NZ  
15517 N N   . HIS I  43  ? 0.7060 0.7657 0.6684 0.0477  -0.0248 0.0089  43  HIS I N   
15518 C CA  . HIS I  43  ? 0.5802 0.6402 0.5459 0.0515  -0.0212 0.0114  43  HIS I CA  
15519 C C   . HIS I  43  ? 0.7259 0.7930 0.6906 0.0544  -0.0200 0.0135  43  HIS I C   
15520 O O   . HIS I  43  ? 0.8824 0.9541 0.8442 0.0535  -0.0220 0.0132  43  HIS I O   
15521 C CB  . HIS I  43  ? 0.4958 0.5530 0.4649 0.0528  -0.0203 0.0129  43  HIS I CB  
15522 C CG  . HIS I  43  ? 0.5468 0.6073 0.5150 0.0530  -0.0217 0.0138  43  HIS I CG  
15523 N ND1 . HIS I  43  ? 0.7082 0.7733 0.6769 0.0562  -0.0200 0.0165  43  HIS I ND1 
15524 C CD2 . HIS I  43  ? 0.7428 0.8026 0.7095 0.0503  -0.0245 0.0124  43  HIS I CD2 
15525 C CE1 . HIS I  43  ? 0.8631 0.9301 0.8304 0.0553  -0.0216 0.0164  43  HIS I CE1 
15526 N NE2 . HIS I  43  ? 0.8396 0.9033 0.8059 0.0518  -0.0242 0.0140  43  HIS I NE2 
15527 N N   . ASN I  44  ? 0.7343 0.8024 0.7014 0.0577  -0.0167 0.0157  44  ASN I N   
15528 C CA  . ASN I  44  ? 0.6358 0.7113 0.6026 0.0606  -0.0155 0.0182  44  ASN I CA  
15529 C C   . ASN I  44  ? 0.6242 0.7033 0.5919 0.0632  -0.0150 0.0211  44  ASN I C   
15530 O O   . ASN I  44  ? 0.7382 0.8240 0.7054 0.0655  -0.0143 0.0235  44  ASN I O   
15531 C CB  . ASN I  44  ? 0.5612 0.6367 0.5305 0.0632  -0.0121 0.0196  44  ASN I CB  
15532 C CG  . ASN I  44  ? 0.5878 0.6586 0.5616 0.0657  -0.0087 0.0213  44  ASN I CG  
15533 O OD1 . ASN I  44  ? 0.6939 0.7635 0.6703 0.0678  -0.0054 0.0224  44  ASN I OD1 
15534 N ND2 . ASN I  44  ? 0.5735 0.6414 0.5483 0.0654  -0.0093 0.0216  44  ASN I ND2 
15535 N N   . GLY I  45  ? 0.7187 0.7937 0.6878 0.0626  -0.0153 0.0209  45  GLY I N   
15536 C CA  . GLY I  45  ? 0.8445 0.9221 0.8141 0.0646  -0.0147 0.0234  45  GLY I CA  
15537 C C   . GLY I  45  ? 0.7497 0.8297 0.7223 0.0690  -0.0113 0.0272  45  GLY I C   
15538 O O   . GLY I  45  ? 0.7517 0.8366 0.7239 0.0710  -0.0108 0.0298  45  GLY I O   
15539 N N   . LYS I  46  ? 0.7097 0.7861 0.6854 0.0704  -0.0087 0.0276  46  LYS I N   
15540 C CA  . LYS I  46  ? 0.7364 0.8142 0.7156 0.0747  -0.0050 0.0314  46  LYS I CA  
15541 C C   . LYS I  46  ? 0.6752 0.7455 0.6585 0.0754  -0.0024 0.0313  46  LYS I C   
15542 O O   . LYS I  46  ? 0.5626 0.6270 0.5463 0.0729  -0.0028 0.0284  46  LYS I O   
15543 C CB  . LYS I  46  ? 0.7368 0.8182 0.7166 0.0763  -0.0035 0.0323  46  LYS I CB  
15544 C CG  . LYS I  46  ? 0.9425 1.0320 0.9187 0.0758  -0.0058 0.0326  46  LYS I CG  
15545 C CD  . LYS I  46  ? 1.1060 1.1974 1.0832 0.0767  -0.0043 0.0328  46  LYS I CD  
15546 C CE  . LYS I  46  ? 1.4270 1.5272 1.4014 0.0766  -0.0062 0.0335  46  LYS I CE  
15547 N NZ  . LYS I  46  ? 1.4096 1.5109 1.3851 0.0771  -0.0048 0.0332  46  LYS I NZ  
15548 N N   . LEU I  47  ? 0.7746 0.8450 0.7608 0.0787  0.0003  0.0347  47  LEU I N   
15549 C CA  . LEU I  47  ? 0.6752 0.7389 0.6659 0.0799  0.0034  0.0351  47  LEU I CA  
15550 C C   . LEU I  47  ? 0.6545 0.7183 0.6480 0.0826  0.0070  0.0367  47  LEU I C   
15551 O O   . LEU I  47  ? 0.8526 0.9203 0.8483 0.0865  0.0097  0.0407  47  LEU I O   
15552 C CB  . LEU I  47  ? 0.4642 0.5277 0.4570 0.0824  0.0051  0.0380  47  LEU I CB  
15553 C CG  . LEU I  47  ? 0.6216 0.6842 0.6123 0.0800  0.0021  0.0365  47  LEU I CG  
15554 C CD1 . LEU I  47  ? 0.6494 0.7098 0.6430 0.0822  0.0044  0.0389  47  LEU I CD1 
15555 C CD2 . LEU I  47  ? 0.6261 0.6832 0.6160 0.0756  -0.0004 0.0322  47  LEU I CD2 
15556 N N   . CYS I  48  ? 0.5902 0.6498 0.5836 0.0803  0.0073  0.0336  48  CYS I N   
15557 C CA  . CYS I  48  ? 0.7158 0.7755 0.7116 0.0823  0.0107  0.0347  48  CYS I CA  
15558 C C   . CYS I  48  ? 0.6081 0.6605 0.6085 0.0834  0.0150  0.0347  48  CYS I C   
15559 O O   . CYS I  48  ? 0.5666 0.6139 0.5684 0.0824  0.0152  0.0338  48  CYS I O   
15560 C CB  . CYS I  48  ? 0.6431 0.7032 0.6357 0.0792  0.0088  0.0313  48  CYS I CB  
15561 S SG  . CYS I  48  ? 1.1088 1.1789 1.0976 0.0795  0.0058  0.0324  48  CYS I SG  
15562 N N   . LYS I  49  ? 0.7091 0.7612 0.7120 0.0854  0.0187  0.0357  49  LYS I N   
15563 C CA  . LYS I  49  ? 0.7722 0.8177 0.7798 0.0867  0.0236  0.0360  49  LYS I CA  
15564 C C   . LYS I  49  ? 0.6878 0.7258 0.6943 0.0822  0.0234  0.0310  49  LYS I C   
15565 O O   . LYS I  49  ? 0.7993 0.8375 0.8027 0.0793  0.0215  0.0281  49  LYS I O   
15566 C CB  . LYS I  49  ? 0.8262 0.8743 0.8375 0.0908  0.0283  0.0394  49  LYS I CB  
15567 C CG  . LYS I  49  ? 0.8079 0.8648 0.8199 0.0950  0.0280  0.0445  49  LYS I CG  
15568 C CD  . LYS I  49  ? 0.9907 1.0500 1.0069 0.0990  0.0327  0.0479  49  LYS I CD  
15569 C CE  . LYS I  49  ? 1.0439 1.0966 1.0613 0.0969  0.0355  0.0444  49  LYS I CE  
15570 N NZ  . LYS I  49  ? 1.0988 1.1550 1.1183 0.0991  0.0383  0.0461  49  LYS I NZ  
15571 N N   . LEU I  50  ? 0.7577 0.7891 0.7669 0.0816  0.0253  0.0301  50  LEU I N   
15572 C CA  . LEU I  50  ? 0.8428 0.8674 0.8506 0.0768  0.0241  0.0254  50  LEU I CA  
15573 C C   . LEU I  50  ? 1.0670 1.0866 1.0754 0.0750  0.0273  0.0227  50  LEU I C   
15574 O O   . LEU I  50  ? 1.3272 1.3448 1.3320 0.0707  0.0248  0.0188  50  LEU I O   
15575 C CB  . LEU I  50  ? 0.7027 0.7223 0.7135 0.0765  0.0248  0.0255  50  LEU I CB  
15576 C CG  . LEU I  50  ? 0.7151 0.7288 0.7244 0.0713  0.0224  0.0210  50  LEU I CG  
15577 C CD1 . LEU I  50  ? 0.7580 0.7735 0.7620 0.0672  0.0177  0.0179  50  LEU I CD1 
15578 C CD2 . LEU I  50  ? 0.5888 0.6007 0.5997 0.0708  0.0206  0.0215  50  LEU I CD2 
15579 N N   . ARG I  51  ? 0.9041 0.9217 0.9170 0.0784  0.0330  0.0249  51  ARG I N   
15580 C CA  . ARG I  51  ? 1.1311 1.1447 1.1448 0.0773  0.0368  0.0227  51  ARG I CA  
15581 C C   . ARG I  51  ? 1.2045 1.2244 1.2191 0.0811  0.0386  0.0259  51  ARG I C   
15582 O O   . ARG I  51  ? 1.3873 1.4108 1.3982 0.0795  0.0360  0.0245  51  ARG I O   
15583 C CB  . ARG I  51  ? 1.2687 1.2753 1.2874 0.0784  0.0427  0.0228  51  ARG I CB  
15584 C CG  . ARG I  51  ? 1.4319 1.4338 1.4515 0.0763  0.0415  0.0214  51  ARG I CG  
15585 C CD  . ARG I  51  ? 1.8957 1.8895 1.9189 0.0755  0.0470  0.0196  51  ARG I CD  
15586 N NE  . ARG I  51  ? 2.0594 2.0487 2.0797 0.0708  0.0474  0.0148  51  ARG I NE  
15587 C CZ  . ARG I  51  ? 1.9316 1.9173 1.9539 0.0712  0.0529  0.0138  51  ARG I CZ  
15588 N NH1 . ARG I  51  ? 1.7438 1.7299 1.7714 0.0763  0.0586  0.0177  51  ARG I NH1 
15589 N NH2 . ARG I  51  ? 1.7081 1.6896 1.7270 0.0663  0.0529  0.0091  51  ARG I NH2 
15590 N N   . GLY I  52  ? 0.9900 1.0112 1.0098 0.0861  0.0432  0.0303  52  GLY I N   
15591 C CA  . GLY I  52  ? 1.1550 1.1832 1.1767 0.0906  0.0448  0.0346  52  GLY I CA  
15592 C C   . GLY I  52  ? 1.1195 1.1514 1.1448 0.0954  0.0460  0.0400  52  GLY I C   
15593 O O   . GLY I  52  ? 1.0856 1.1240 1.1131 0.0996  0.0473  0.0446  52  GLY I O   
15594 N N   . VAL I  53  ? 1.1355 1.1634 1.1614 0.0947  0.0455  0.0396  53  VAL I N   
15595 C CA  . VAL I  53  ? 0.9116 0.9421 0.9405 0.0988  0.0467  0.0444  53  VAL I CA  
15596 C C   . VAL I  53  ? 0.6545 0.6898 0.6794 0.0978  0.0411  0.0447  53  VAL I C   
15597 O O   . VAL I  53  ? 0.6265 0.6596 0.6476 0.0934  0.0369  0.0407  53  VAL I O   
15598 C CB  . VAL I  53  ? 0.6847 0.7074 0.7181 0.0995  0.0512  0.0443  53  VAL I CB  
15599 C CG1 . VAL I  53  ? 0.5322 0.5466 0.5649 0.0949  0.0523  0.0387  53  VAL I CG1 
15600 C CG2 . VAL I  53  ? 0.7581 0.7811 0.7912 0.0998  0.0489  0.0456  53  VAL I CG2 
15601 N N   . ALA I  54  ? 0.6421 0.6837 0.6680 0.1018  0.0411  0.0497  54  ALA I N   
15602 C CA  . ALA I  54  ? 0.6888 0.7359 0.7107 0.1012  0.0361  0.0504  54  ALA I CA  
15603 C C   . ALA I  54  ? 0.7155 0.7584 0.7379 0.1003  0.0355  0.0499  54  ALA I C   
15604 O O   . ALA I  54  ? 0.6723 0.7095 0.6989 0.1018  0.0395  0.0507  54  ALA I O   
15605 C CB  . ALA I  54  ? 0.8118 0.8679 0.8342 0.1055  0.0363  0.0558  54  ALA I CB  
15606 N N   . PRO I  55  ? 0.5026 0.5482 0.5208 0.0980  0.0306  0.0485  55  PRO I N   
15607 C CA  . PRO I  55  ? 0.4913 0.5338 0.5099 0.0975  0.0299  0.0485  55  PRO I CA  
15608 C C   . PRO I  55  ? 0.6893 0.7355 0.7101 0.1021  0.0323  0.0539  55  PRO I C   
15609 O O   . PRO I  55  ? 0.8150 0.8681 0.8355 0.1051  0.0328  0.0575  55  PRO I O   
15610 C CB  . PRO I  55  ? 0.4659 0.5114 0.4792 0.0939  0.0242  0.0459  55  PRO I CB  
15611 C CG  . PRO I  55  ? 0.5086 0.5614 0.5188 0.0944  0.0224  0.0468  55  PRO I CG  
15612 C CD  . PRO I  55  ? 0.4017 0.4527 0.4146 0.0955  0.0258  0.0467  55  PRO I CD  
15613 N N   . LEU I  56  ? 0.5784 0.6203 0.6016 0.1026  0.0338  0.0545  56  LEU I N   
15614 C CA  . LEU I  56  ? 0.4863 0.5313 0.5110 0.1066  0.0359  0.0594  56  LEU I CA  
15615 C C   . LEU I  56  ? 0.5753 0.6243 0.5956 0.1051  0.0317  0.0592  56  LEU I C   
15616 O O   . LEU I  56  ? 0.6762 0.7210 0.6960 0.1025  0.0301  0.0565  56  LEU I O   
15617 C CB  . LEU I  56  ? 0.5613 0.5991 0.5911 0.1080  0.0402  0.0602  56  LEU I CB  
15618 C CG  . LEU I  56  ? 0.6077 0.6475 0.6394 0.1121  0.0428  0.0652  56  LEU I CG  
15619 C CD1 . LEU I  56  ? 0.7233 0.7691 0.7565 0.1167  0.0455  0.0705  56  LEU I CD1 
15620 C CD2 . LEU I  56  ? 0.5499 0.5817 0.5864 0.1127  0.0466  0.0650  56  LEU I CD2 
15621 N N   . HIS I  57  ? 0.5604 0.6178 0.5777 0.1067  0.0301  0.0620  57  HIS I N   
15622 C CA  . HIS I  57  ? 0.5694 0.6311 0.5820 0.1051  0.0263  0.0618  57  HIS I CA  
15623 C C   . HIS I  57  ? 0.7784 0.8422 0.7919 0.1084  0.0285  0.0662  57  HIS I C   
15624 O O   . HIS I  57  ? 0.7940 0.8626 0.8087 0.1122  0.0308  0.0709  57  HIS I O   
15625 C CB  . HIS I  57  ? 0.6084 0.6783 0.6166 0.1043  0.0231  0.0618  57  HIS I CB  
15626 C CG  . HIS I  57  ? 0.6269 0.7000 0.6300 0.1014  0.0189  0.0599  57  HIS I CG  
15627 N ND1 . HIS I  57  ? 0.8046 0.8826 0.8053 0.1027  0.0186  0.0628  57  HIS I ND1 
15628 C CD2 . HIS I  57  ? 0.7707 0.8427 0.7705 0.0971  0.0151  0.0554  57  HIS I CD2 
15629 C CE1 . HIS I  57  ? 0.8847 0.9643 0.8810 0.0993  0.0149  0.0599  57  HIS I CE1 
15630 N NE2 . HIS I  57  ? 0.9194 0.9954 0.9152 0.0960  0.0128  0.0556  57  HIS I NE2 
15631 N N   . LEU I  58  ? 0.6811 0.7416 0.6940 0.1068  0.0277  0.0649  58  LEU I N   
15632 C CA  . LEU I  58  ? 0.7531 0.8143 0.7669 0.1096  0.0301  0.0688  58  LEU I CA  
15633 C C   . LEU I  58  ? 0.8965 0.9651 0.9050 0.1094  0.0276  0.0704  58  LEU I C   
15634 O O   . LEU I  58  ? 0.9939 1.0648 1.0023 0.1119  0.0294  0.0742  58  LEU I O   
15635 C CB  . LEU I  58  ? 0.7460 0.7989 0.7625 0.1083  0.0314  0.0667  58  LEU I CB  
15636 C CG  . LEU I  58  ? 0.5420 0.5871 0.5637 0.1081  0.0340  0.0648  58  LEU I CG  
15637 C CD1 . LEU I  58  ? 0.6980 0.7360 0.7226 0.1069  0.0352  0.0633  58  LEU I CD1 
15638 C CD2 . LEU I  58  ? 0.6926 0.7383 0.7183 0.1123  0.0385  0.0688  58  LEU I CD2 
15639 N N   . GLY I  59  ? 0.7554 0.8277 0.7594 0.1062  0.0235  0.0675  59  GLY I N   
15640 C CA  . GLY I  59  ? 0.7573 0.8368 0.7559 0.1054  0.0210  0.0685  59  GLY I CA  
15641 C C   . GLY I  59  ? 0.8631 0.9401 0.8603 0.1043  0.0210  0.0679  59  GLY I C   
15642 O O   . GLY I  59  ? 1.0623 1.1338 1.0597 0.1011  0.0197  0.0639  59  GLY I O   
15643 N N   . LYS I  60  ? 0.9470 1.0281 0.9429 0.1067  0.0227  0.0720  60  LYS I N   
15644 C CA  . LYS I  60  ? 1.1705 1.2498 1.1644 0.1057  0.0230  0.0718  60  LYS I CA  
15645 C C   . LYS I  60  ? 1.0462 1.1171 1.0453 0.1070  0.0264  0.0721  60  LYS I C   
15646 O O   . LYS I  60  ? 1.1895 1.2578 1.1880 0.1061  0.0271  0.0716  60  LYS I O   
15647 C CB  . LYS I  60  ? 1.2722 1.3594 1.2621 0.1076  0.0235  0.0761  60  LYS I CB  
15648 C CG  . LYS I  60  ? 1.6579 1.7447 1.6443 0.1057  0.0233  0.0754  60  LYS I CG  
15649 C CD  . LYS I  60  ? 1.7590 1.8462 1.7412 0.1011  0.0197  0.0705  60  LYS I CD  
15650 C CE  . LYS I  60  ? 1.8888 1.9849 1.8661 0.1001  0.0167  0.0707  60  LYS I CE  
15651 N NZ  . LYS I  60  ? 1.7319 1.8284 1.7053 0.0955  0.0134  0.0659  60  LYS I NZ  
15652 N N   . CYS I  61  ? 0.8908 0.9576 0.8950 0.1089  0.0287  0.0727  61  CYS I N   
15653 C CA  . CYS I  61  ? 0.8538 0.9129 0.8634 0.1102  0.0322  0.0731  61  CYS I CA  
15654 C C   . CYS I  61  ? 0.8101 0.8616 0.8230 0.1074  0.0314  0.0684  61  CYS I C   
15655 O O   . CYS I  61  ? 0.8930 0.9452 0.9048 0.1052  0.0287  0.0655  61  CYS I O   
15656 C CB  . CYS I  61  ? 0.8037 0.8632 0.8172 0.1149  0.0364  0.0778  61  CYS I CB  
15657 S SG  . CYS I  61  ? 1.3527 1.4208 1.3631 0.1186  0.0378  0.0843  61  CYS I SG  
15658 N N   . ASN I  62  ? 0.6456 0.6901 0.6626 0.1073  0.0336  0.0677  62  ASN I N   
15659 C CA  . ASN I  62  ? 0.6529 0.6902 0.6736 0.1049  0.0333  0.0638  62  ASN I CA  
15660 C C   . ASN I  62  ? 0.6706 0.7030 0.6971 0.1075  0.0376  0.0654  62  ASN I C   
15661 O O   . ASN I  62  ? 0.8096 0.8438 0.8374 0.1114  0.0410  0.0698  62  ASN I O   
15662 C CB  . ASN I  62  ? 0.8011 0.8339 0.8226 0.1020  0.0321  0.0611  62  ASN I CB  
15663 C CG  . ASN I  62  ? 0.8027 0.8333 0.8261 0.1043  0.0356  0.0639  62  ASN I CG  
15664 O OD1 . ASN I  62  ? 0.8095 0.8398 0.8354 0.1079  0.0393  0.0675  62  ASN I OD1 
15665 N ND2 . ASN I  62  ? 0.8668 0.8958 0.8893 0.1022  0.0345  0.0624  62  ASN I ND2 
15666 N N   . ILE I  63  ? 0.5420 0.5682 0.5718 0.1052  0.0375  0.0619  63  ILE I N   
15667 C CA  . ILE I  63  ? 0.5548 0.5756 0.5900 0.1070  0.0417  0.0627  63  ILE I CA  
15668 C C   . ILE I  63  ? 0.5427 0.5616 0.5810 0.1105  0.0460  0.0666  63  ILE I C   
15669 O O   . ILE I  63  ? 0.6801 0.6998 0.7205 0.1142  0.0498  0.0702  63  ILE I O   
15670 C CB  . ILE I  63  ? 0.7192 0.7331 0.7574 0.1032  0.0407  0.0581  63  ILE I CB  
15671 C CG1 . ILE I  63  ? 0.6314 0.6472 0.6666 0.1002  0.0369  0.0547  63  ILE I CG1 
15672 C CG2 . ILE I  63  ? 0.5851 0.5930 0.6290 0.1048  0.0454  0.0586  63  ILE I CG2 
15673 C CD1 . ILE I  63  ? 0.7016 0.7199 0.7366 0.1024  0.0388  0.0562  63  ILE I CD1 
15674 N N   . ALA I  64  ? 0.5363 0.5528 0.5751 0.1093  0.0457  0.0659  64  ALA I N   
15675 C CA  . ALA I  64  ? 0.5952 0.6097 0.6365 0.1124  0.0498  0.0695  64  ALA I CA  
15676 C C   . ALA I  64  ? 0.6542 0.6749 0.6933 0.1167  0.0519  0.0749  64  ALA I C   
15677 O O   . ALA I  64  ? 0.6363 0.6555 0.6791 0.1202  0.0563  0.0783  64  ALA I O   
15678 C CB  . ALA I  64  ? 0.5399 0.5528 0.5805 0.1104  0.0485  0.0682  64  ALA I CB  
15679 N N   . GLY I  65  ? 0.6544 0.6822 0.6878 0.1163  0.0488  0.0757  65  GLY I N   
15680 C CA  . GLY I  65  ? 0.6461 0.6807 0.6769 0.1199  0.0501  0.0808  65  GLY I CA  
15681 C C   . GLY I  65  ? 0.6300 0.6667 0.6631 0.1230  0.0522  0.0836  65  GLY I C   
15682 O O   . GLY I  65  ? 0.7760 0.8150 0.8105 0.1270  0.0556  0.0886  65  GLY I O   
15683 N N   . TRP I  66  ? 0.5661 0.6021 0.5997 0.1210  0.0504  0.0803  66  TRP I N   
15684 C CA  . TRP I  66  ? 0.7315 0.7697 0.7670 0.1235  0.0522  0.0825  66  TRP I CA  
15685 C C   . TRP I  66  ? 0.5582 0.5907 0.6002 0.1267  0.0579  0.0849  66  TRP I C   
15686 O O   . TRP I  66  ? 0.7952 0.8310 0.8390 0.1308  0.0609  0.0897  66  TRP I O   
15687 C CB  . TRP I  66  ? 0.6590 0.6972 0.6932 0.1203  0.0490  0.0781  66  TRP I CB  
15688 C CG  . TRP I  66  ? 0.7365 0.7740 0.7742 0.1224  0.0518  0.0792  66  TRP I CG  
15689 C CD1 . TRP I  66  ? 0.8834 0.9268 0.9216 0.1262  0.0536  0.0839  66  TRP I CD1 
15690 C CD2 . TRP I  66  ? 0.6408 0.6713 0.6822 0.1207  0.0535  0.0757  66  TRP I CD2 
15691 N NE1 . TRP I  66  ? 0.9092 0.9494 0.9515 0.1271  0.0565  0.0835  66  TRP I NE1 
15692 C CE2 . TRP I  66  ? 0.6639 0.6961 0.7080 0.1237  0.0565  0.0783  66  TRP I CE2 
15693 C CE3 . TRP I  66  ? 0.7530 0.7763 0.7959 0.1169  0.0526  0.0707  66  TRP I CE3 
15694 C CZ2 . TRP I  66  ? 0.6187 0.6451 0.6664 0.1228  0.0590  0.0757  66  TRP I CZ2 
15695 C CZ3 . TRP I  66  ? 0.7055 0.7235 0.7517 0.1159  0.0548  0.0682  66  TRP I CZ3 
15696 C CH2 . TRP I  66  ? 0.7317 0.7510 0.7801 0.1187  0.0580  0.0705  66  TRP I CH2 
15697 N N   . ILE I  67  ? 0.4756 0.4998 0.5213 0.1249  0.0594  0.0816  67  ILE I N   
15698 C CA  . ILE I  67  ? 0.7339 0.7520 0.7859 0.1274  0.0651  0.0833  67  ILE I CA  
15699 C C   . ILE I  67  ? 0.8526 0.8703 0.9063 0.1308  0.0686  0.0879  67  ILE I C   
15700 O O   . ILE I  67  ? 0.7646 0.7814 0.8222 0.1348  0.0734  0.0920  67  ILE I O   
15701 C CB  . ILE I  67  ? 0.5845 0.5938 0.6401 0.1239  0.0656  0.0781  67  ILE I CB  
15702 C CG1 . ILE I  67  ? 0.8796 0.8888 0.9315 0.1190  0.0601  0.0732  67  ILE I CG1 
15703 C CG2 . ILE I  67  ? 0.5716 0.5779 0.6302 0.1238  0.0678  0.0766  67  ILE I CG2 
15704 C CD1 . ILE I  67  ? 1.0240 1.0256 1.0794 0.1162  0.0606  0.0697  67  ILE I CD1 
15705 N N   . LEU I  68  ? 0.6981 0.7162 0.7490 0.1293  0.0665  0.0872  68  LEU I N   
15706 C CA  . LEU I  68  ? 0.6554 0.6730 0.7075 0.1322  0.0698  0.0913  68  LEU I CA  
15707 C C   . LEU I  68  ? 0.7633 0.7890 0.8126 0.1362  0.0706  0.0974  68  LEU I C   
15708 O O   . LEU I  68  ? 0.8052 0.8309 0.8558 0.1396  0.0741  0.1019  68  LEU I O   
15709 C CB  . LEU I  68  ? 0.6527 0.6684 0.7026 0.1294  0.0676  0.0888  68  LEU I CB  
15710 C CG  . LEU I  68  ? 0.6554 0.6622 0.7099 0.1267  0.0686  0.0845  68  LEU I CG  
15711 C CD1 . LEU I  68  ? 0.6232 0.6276 0.6773 0.1254  0.0685  0.0839  68  LEU I CD1 
15712 C CD2 . LEU I  68  ? 0.4351 0.4364 0.4960 0.1292  0.0740  0.0861  68  LEU I CD2 
15713 N N   . GLY I  69  ? 0.7373 0.7699 0.7828 0.1359  0.0673  0.0976  69  GLY I N   
15714 C CA  . GLY I  69  ? 0.7827 0.8238 0.8258 0.1394  0.0676  0.1033  69  GLY I CA  
15715 C C   . GLY I  69  ? 0.8864 0.9332 0.9235 0.1389  0.0651  0.1051  69  GLY I C   
15716 O O   . GLY I  69  ? 0.9995 1.0505 1.0360 0.1423  0.0672  0.1106  69  GLY I O   
15717 N N   . ASN I  70  ? 0.7657 0.8127 0.7985 0.1346  0.0608  0.1004  70  ASN I N   
15718 C CA  . ASN I  70  ? 0.9080 0.9606 0.9346 0.1334  0.0583  0.1012  70  ASN I CA  
15719 C C   . ASN I  70  ? 1.0190 1.0817 1.0418 0.1358  0.0572  0.1060  70  ASN I C   
15720 O O   . ASN I  70  ? 0.9290 0.9955 0.9519 0.1359  0.0555  0.1058  70  ASN I O   
15721 C CB  . ASN I  70  ? 0.9086 0.9603 0.9313 0.1283  0.0536  0.0952  70  ASN I CB  
15722 C CG  . ASN I  70  ? 1.0144 1.0701 1.0310 0.1267  0.0517  0.0954  70  ASN I CG  
15723 O OD1 . ASN I  70  ? 1.0871 1.1504 1.0996 0.1282  0.0513  0.0993  70  ASN I OD1 
15724 N ND2 . ASN I  70  ? 0.9059 0.9565 0.9221 0.1234  0.0506  0.0912  70  ASN I ND2 
15725 N N   . PRO I  71  ? 1.2037 1.2710 1.2234 0.1376  0.0581  0.1104  71  PRO I N   
15726 C CA  . PRO I  71  ? 1.1249 1.2026 1.1411 0.1399  0.0570  0.1155  71  PRO I CA  
15727 C C   . PRO I  71  ? 1.1210 1.2053 1.1325 0.1370  0.0520  0.1128  71  PRO I C   
15728 O O   . PRO I  71  ? 1.3684 1.4605 1.3792 0.1389  0.0511  0.1164  71  PRO I O   
15729 C CB  . PRO I  71  ? 1.0635 1.1438 1.0749 0.1400  0.0575  0.1182  71  PRO I CB  
15730 C CG  . PRO I  71  ? 1.2232 1.2940 1.2389 0.1405  0.0613  0.1172  71  PRO I CG  
15731 C CD  . PRO I  71  ? 1.1330 1.1960 1.1525 0.1377  0.0605  0.1110  71  PRO I CD  
15732 N N   . GLU I  72  ? 1.1469 1.2282 1.1556 0.1324  0.0488  0.1067  72  GLU I N   
15733 C CA  . GLU I  72  ? 1.2079 1.2952 1.2119 0.1293  0.0440  0.1038  72  GLU I CA  
15734 C C   . GLU I  72  ? 1.0630 1.1477 1.0704 0.1284  0.0429  0.1005  72  GLU I C   
15735 O O   . GLU I  72  ? 1.0325 1.1220 1.0367 0.1262  0.0393  0.0983  72  GLU I O   
15736 C CB  . GLU I  72  ? 1.0942 1.1803 1.0930 0.1248  0.0412  0.0991  72  GLU I CB  
15737 C CG  . GLU I  72  ? 1.3584 1.4473 1.3528 0.1250  0.0421  0.1018  72  GLU I CG  
15738 C CD  . GLU I  72  ? 1.5618 1.6619 1.5510 0.1261  0.0405  0.1061  72  GLU I CD  
15739 O OE1 . GLU I  72  ? 1.5395 1.6454 1.5271 0.1252  0.0375  0.1055  72  GLU I OE1 
15740 O OE2 . GLU I  72  ? 1.4814 1.5845 1.4680 0.1276  0.0422  0.1102  72  GLU I OE2 
15741 N N   . CYS I  73  ? 1.2620 1.3391 1.2758 0.1300  0.0462  0.1001  73  CYS I N   
15742 C CA  . CYS I  73  ? 1.2733 1.3474 1.2904 0.1292  0.0457  0.0971  73  CYS I CA  
15743 C C   . CYS I  73  ? 1.5336 1.6108 1.5548 0.1334  0.0486  0.1018  73  CYS I C   
15744 O O   . CYS I  73  ? 1.6033 1.6746 1.6299 0.1345  0.0514  0.1010  73  CYS I O   
15745 C CB  . CYS I  73  ? 1.1472 1.2106 1.1687 0.1275  0.0475  0.0930  73  CYS I CB  
15746 S SG  . CYS I  73  ? 1.0821 1.1412 1.1002 0.1224  0.0442  0.0872  73  CYS I SG  
15747 N N   . GLU I  74  ? 1.8100 1.8966 1.8285 0.1356  0.0478  0.1066  74  GLU I N   
15748 C CA  . GLU I  74  ? 1.9258 2.0163 1.9485 0.1405  0.0510  0.1126  74  GLU I CA  
15749 C C   . GLU I  74  ? 2.0385 2.1314 2.0631 0.1406  0.0501  0.1117  74  GLU I C   
15750 O O   . GLU I  74  ? 2.0003 2.0902 2.0309 0.1435  0.0539  0.1136  74  GLU I O   
15751 C CB  . GLU I  74  ? 1.8139 1.9144 1.8327 0.1426  0.0501  0.1184  74  GLU I CB  
15752 C CG  . GLU I  74  ? 2.0108 2.1131 2.0343 0.1481  0.0547  0.1258  74  GLU I CG  
15753 C CD  . GLU I  74  ? 2.0712 2.1776 2.0909 0.1493  0.0551  0.1300  74  GLU I CD  
15754 O OE1 . GLU I  74  ? 2.0431 2.1491 2.0571 0.1458  0.0524  0.1268  74  GLU I OE1 
15755 O OE2 . GLU I  74  ? 1.8997 2.0094 1.9221 0.1537  0.0582  0.1368  74  GLU I OE2 
15756 N N   . SER I  75  ? 2.0407 2.1388 2.0604 0.1373  0.0454  0.1087  75  SER I N   
15757 C CA  . SER I  75  ? 2.1911 2.2947 2.2117 0.1379  0.0442  0.1093  75  SER I CA  
15758 C C   . SER I  75  ? 2.2727 2.3694 2.2979 0.1372  0.0458  0.1057  75  SER I C   
15759 O O   . SER I  75  ? 2.3468 2.4465 2.3752 0.1395  0.0472  0.1080  75  SER I O   
15760 C CB  . SER I  75  ? 2.1782 2.2891 2.1919 0.1343  0.0387  0.1068  75  SER I CB  
15761 O OG  . SER I  75  ? 1.9748 2.0847 1.9835 0.1316  0.0367  0.1047  75  SER I OG  
15762 N N   . LEU I  76  ? 2.3384 2.4260 2.3639 0.1341  0.0458  0.1002  76  LEU I N   
15763 C CA  . LEU I  76  ? 2.4056 2.4867 2.4343 0.1326  0.0467  0.0960  76  LEU I CA  
15764 C C   . LEU I  76  ? 2.4255 2.4994 2.4614 0.1356  0.0526  0.0976  76  LEU I C   
15765 O O   . LEU I  76  ? 2.4294 2.4965 2.4676 0.1336  0.0536  0.0934  76  LEU I O   
15766 C CB  . LEU I  76  ? 2.3020 2.3772 2.3278 0.1274  0.0436  0.0892  76  LEU I CB  
15767 C CG  . LEU I  76  ? 2.1834 2.2629 2.2033 0.1234  0.0381  0.0853  76  LEU I CG  
15768 C CD1 . LEU I  76  ? 1.8001 1.8740 1.8177 0.1195  0.0360  0.0807  76  LEU I CD1 
15769 C CD2 . LEU I  76  ? 2.1529 2.2317 2.1739 0.1220  0.0375  0.0825  76  LEU I CD2 
15770 N N   . SER I  77  ? 2.0472 2.1224 2.0866 0.1401  0.0565  0.1035  77  SER I N   
15771 C CA  . SER I  77  ? 2.1395 2.2085 2.1860 0.1432  0.0624  0.1054  77  SER I CA  
15772 C C   . SER I  77  ? 2.4217 2.4920 2.4704 0.1435  0.0630  0.1047  77  SER I C   
15773 O O   . SER I  77  ? 2.3832 2.4602 2.4280 0.1420  0.0590  0.1039  77  SER I O   
15774 C CB  . SER I  77  ? 1.9596 2.0322 2.0094 0.1487  0.0663  0.1131  77  SER I CB  
15775 O OG  . SER I  77  ? 1.4231 1.4955 1.4702 0.1486  0.0657  0.1142  77  SER I OG  
15776 N N   . THR I  78  ? 3.0091 3.0729 3.0640 0.1454  0.0683  0.1050  78  THR I N   
15777 C CA  . THR I  78  ? 2.9288 2.9923 2.9868 0.1457  0.0701  0.1042  78  THR I CA  
15778 C C   . THR I  78  ? 2.7435 2.8039 2.7978 0.1404  0.0664  0.0969  78  THR I C   
15779 O O   . THR I  78  ? 2.7333 2.8000 2.7839 0.1389  0.0625  0.0960  78  THR I O   
15780 C CB  . THR I  78  ? 2.9121 2.9862 2.9704 0.1491  0.0695  0.1097  78  THR I CB  
15781 O OG1 . THR I  78  ? 2.8875 2.9697 2.9390 0.1468  0.0632  0.1090  78  THR I OG1 
15782 C CG2 . THR I  78  ? 2.6848 2.7621 2.7479 0.1549  0.0738  0.1176  78  THR I CG2 
15783 N N   . ALA I  79  ? 2.2076 2.2585 2.2627 0.1373  0.0674  0.0918  79  ALA I N   
15784 C CA  . ALA I  79  ? 1.8232 1.8700 1.8762 0.1327  0.0654  0.0854  79  ALA I CA  
15785 C C   . ALA I  79  ? 1.5808 1.6177 1.6389 0.1323  0.0706  0.0829  79  ALA I C   
15786 O O   . ALA I  79  ? 1.5080 1.5391 1.5690 0.1330  0.0736  0.0833  79  ALA I O   
15787 C CB  . ALA I  79  ? 1.7344 1.7805 1.7815 0.1278  0.0595  0.0804  79  ALA I CB  
15788 N N   . SER I  80  ? 1.1935 1.2284 1.2527 0.1310  0.0719  0.0804  80  SER I N   
15789 C CA  . SER I  80  ? 1.1136 1.1394 1.1776 0.1305  0.0774  0.0780  80  SER I CA  
15790 C C   . SER I  80  ? 0.8335 0.8520 0.8947 0.1246  0.0751  0.0707  80  SER I C   
15791 O O   . SER I  80  ? 0.7633 0.7733 0.8276 0.1234  0.0789  0.0684  80  SER I O   
15792 C CB  . SER I  80  ? 1.2816 1.3085 1.3491 0.1327  0.0813  0.0796  80  SER I CB  
15793 O OG  . SER I  80  ? 1.3824 1.4171 1.4525 0.1381  0.0828  0.0866  80  SER I OG  
15794 N N   . SER I  81  ? 0.8631 0.8848 0.9183 0.1208  0.0690  0.0672  81  SER I N   
15795 C CA  . SER I  81  ? 0.8421 0.8580 0.8943 0.1150  0.0662  0.0606  81  SER I CA  
15796 C C   . SER I  81  ? 0.7589 0.7802 0.8046 0.1119  0.0591  0.0584  81  SER I C   
15797 O O   . SER I  81  ? 0.6496 0.6790 0.6931 0.1137  0.0567  0.0613  81  SER I O   
15798 C CB  . SER I  81  ? 0.6764 0.6873 0.7299 0.1130  0.0691  0.0571  81  SER I CB  
15799 O OG  . SER I  81  ? 0.7362 0.7531 0.7884 0.1142  0.0685  0.0585  81  SER I OG  
15800 N N   . TRP I  82  ? 0.6041 0.6210 0.6469 0.1070  0.0557  0.0534  82  TRP I N   
15801 C CA  . TRP I  82  ? 0.6240 0.6451 0.6610 0.1036  0.0492  0.0508  82  TRP I CA  
15802 C C   . TRP I  82  ? 0.6185 0.6334 0.6533 0.0979  0.0467  0.0449  82  TRP I C   
15803 O O   . TRP I  82  ? 0.5708 0.5789 0.6085 0.0966  0.0489  0.0430  82  TRP I O   
15804 C CB  . TRP I  82  ? 0.6485 0.6742 0.6837 0.1049  0.0463  0.0535  82  TRP I CB  
15805 C CG  . TRP I  82  ? 0.5920 0.6124 0.6301 0.1052  0.0480  0.0538  82  TRP I CG  
15806 C CD1 . TRP I  82  ? 0.6418 0.6574 0.6791 0.1013  0.0456  0.0500  82  TRP I CD1 
15807 C CD2 . TRP I  82  ? 0.6472 0.6668 0.6897 0.1096  0.0526  0.0583  82  TRP I CD2 
15808 N NE1 . TRP I  82  ? 0.5518 0.5635 0.5928 0.1029  0.0485  0.0517  82  TRP I NE1 
15809 C CE2 . TRP I  82  ? 0.6074 0.6214 0.6515 0.1080  0.0528  0.0568  82  TRP I CE2 
15810 C CE3 . TRP I  82  ? 0.6862 0.7095 0.7318 0.1148  0.0566  0.0638  82  TRP I CE3 
15811 C CZ2 . TRP I  82  ? 0.6422 0.6538 0.6905 0.1114  0.0570  0.0602  82  TRP I CZ2 
15812 C CZ3 . TRP I  82  ? 0.6850 0.7059 0.7346 0.1181  0.0607  0.0674  82  TRP I CZ3 
15813 C CH2 . TRP I  82  ? 0.5347 0.5498 0.5856 0.1164  0.0609  0.0655  82  TRP I CH2 
15814 N N   . SER I  83  ? 0.7091 0.7269 0.7391 0.0946  0.0420  0.0419  83  SER I N   
15815 C CA  . SER I  83  ? 0.5779 0.5909 0.6055 0.0891  0.0391  0.0365  83  SER I CA  
15816 C C   . SER I  83  ? 0.5655 0.5775 0.5917 0.0869  0.0352  0.0353  83  SER I C   
15817 O O   . SER I  83  ? 0.5235 0.5299 0.5502 0.0833  0.0344  0.0320  83  SER I O   
15818 C CB  . SER I  83  ? 0.5518 0.5682 0.5746 0.0866  0.0357  0.0341  83  SER I CB  
15819 O OG  . SER I  83  ? 0.6153 0.6396 0.6352 0.0881  0.0324  0.0365  83  SER I OG  
15820 N N   . TYR I  84  ? 0.5171 0.5350 0.5417 0.0888  0.0329  0.0381  84  TYR I N   
15821 C CA  . TYR I  84  ? 0.5099 0.5272 0.5337 0.0872  0.0297  0.0376  84  TYR I CA  
15822 C C   . TYR I  84  ? 0.5266 0.5495 0.5502 0.0910  0.0298  0.0419  84  TYR I C   
15823 O O   . TYR I  84  ? 0.7182 0.7461 0.7418 0.0945  0.0316  0.0453  84  TYR I O   
15824 C CB  . TYR I  84  ? 0.5096 0.5279 0.5289 0.0825  0.0241  0.0338  84  TYR I CB  
15825 C CG  . TYR I  84  ? 0.5219 0.5473 0.5367 0.0828  0.0212  0.0343  84  TYR I CG  
15826 C CD1 . TYR I  84  ? 0.5339 0.5644 0.5460 0.0830  0.0180  0.0356  84  TYR I CD1 
15827 C CD2 . TYR I  84  ? 0.4272 0.4542 0.4404 0.0825  0.0217  0.0335  84  TYR I CD2 
15828 C CE1 . TYR I  84  ? 0.4749 0.5119 0.4829 0.0830  0.0153  0.0360  84  TYR I CE1 
15829 C CE2 . TYR I  84  ? 0.3588 0.3925 0.3681 0.0826  0.0189  0.0340  84  TYR I CE2 
15830 C CZ  . TYR I  84  ? 0.4424 0.4811 0.4491 0.0828  0.0157  0.0352  84  TYR I CZ  
15831 O OH  . TYR I  84  ? 0.5300 0.5755 0.5329 0.0827  0.0131  0.0355  84  TYR I OH  
15832 N N   . ILE I  85  ? 0.4016 0.4239 0.4250 0.0901  0.0279  0.0419  85  ILE I N   
15833 C CA  . ILE I  85  ? 0.5954 0.6224 0.6183 0.0933  0.0281  0.0458  85  ILE I CA  
15834 C C   . ILE I  85  ? 0.5237 0.5554 0.5418 0.0911  0.0231  0.0447  85  ILE I C   
15835 O O   . ILE I  85  ? 0.5396 0.5686 0.5566 0.0873  0.0200  0.0413  85  ILE I O   
15836 C CB  . ILE I  85  ? 0.5398 0.5624 0.5668 0.0948  0.0310  0.0474  85  ILE I CB  
15837 C CG1 . ILE I  85  ? 0.4600 0.4783 0.4920 0.0974  0.0365  0.0489  85  ILE I CG1 
15838 C CG2 . ILE I  85  ? 0.5095 0.5370 0.5353 0.0977  0.0310  0.0511  85  ILE I CG2 
15839 C CD1 . ILE I  85  ? 0.4270 0.4404 0.4634 0.0989  0.0397  0.0503  85  ILE I CD1 
15840 N N   . VAL I  86  ? 0.5175 0.5563 0.5330 0.0934  0.0225  0.0476  86  VAL I N   
15841 C CA  . VAL I  86  ? 0.5174 0.5609 0.5282 0.0914  0.0184  0.0467  86  VAL I CA  
15842 C C   . VAL I  86  ? 0.5371 0.5827 0.5477 0.0935  0.0192  0.0497  86  VAL I C   
15843 O O   . VAL I  86  ? 0.6248 0.6737 0.6362 0.0973  0.0219  0.0538  86  VAL I O   
15844 C CB  . VAL I  86  ? 0.4610 0.5115 0.4678 0.0916  0.0164  0.0472  86  VAL I CB  
15845 C CG1 . VAL I  86  ? 0.4577 0.5126 0.4598 0.0892  0.0123  0.0458  86  VAL I CG1 
15846 C CG2 . VAL I  86  ? 0.4154 0.4637 0.4224 0.0897  0.0160  0.0443  86  VAL I CG2 
15847 N N   . GLU I  87  ? 0.4848 0.5284 0.4943 0.0909  0.0169  0.0477  87  GLU I N   
15848 C CA  . GLU I  87  ? 0.5105 0.5559 0.5193 0.0922  0.0175  0.0499  87  GLU I CA  
15849 C C   . GLU I  87  ? 0.6304 0.6805 0.6341 0.0897  0.0136  0.0483  87  GLU I C   
15850 O O   . GLU I  87  ? 0.7445 0.7930 0.7469 0.0861  0.0106  0.0448  87  GLU I O   
15851 C CB  . GLU I  87  ? 0.6671 0.7056 0.6799 0.0914  0.0188  0.0489  87  GLU I CB  
15852 C CG  . GLU I  87  ? 0.7516 0.7894 0.7668 0.0949  0.0226  0.0527  87  GLU I CG  
15853 C CD  . GLU I  87  ? 0.8302 0.8608 0.8499 0.0940  0.0241  0.0515  87  GLU I CD  
15854 O OE1 . GLU I  87  ? 0.8088 0.8363 0.8324 0.0967  0.0281  0.0538  87  GLU I OE1 
15855 O OE2 . GLU I  87  ? 0.8183 0.8463 0.8379 0.0906  0.0214  0.0484  87  GLU I OE2 
15856 N N   . THR I  88  ? 0.7937 0.8498 0.7943 0.0914  0.0138  0.0510  88  THR I N   
15857 C CA  . THR I  88  ? 0.8965 0.9568 0.8921 0.0888  0.0106  0.0494  88  THR I CA  
15858 C C   . THR I  88  ? 1.0105 1.0667 1.0067 0.0870  0.0104  0.0480  88  THR I C   
15859 O O   . THR I  88  ? 1.1505 1.2037 1.1495 0.0889  0.0132  0.0499  88  THR I O   
15860 C CB  . THR I  88  ? 0.9022 0.9709 0.8938 0.0908  0.0107  0.0526  88  THR I CB  
15861 O OG1 . THR I  88  ? 1.0680 1.1366 1.0605 0.0934  0.0136  0.0559  88  THR I OG1 
15862 C CG2 . THR I  88  ? 0.6905 0.7635 0.6823 0.0931  0.0113  0.0546  88  THR I CG2 
15863 N N   . PRO I  89  ? 1.1359 1.1917 1.1298 0.0833  0.0072  0.0446  89  PRO I N   
15864 C CA  . PRO I  89  ? 1.2351 1.2897 1.2285 0.0823  0.0075  0.0444  89  PRO I CA  
15865 C C   . PRO I  89  ? 1.2888 1.3497 1.2789 0.0850  0.0092  0.0479  89  PRO I C   
15866 O O   . PRO I  89  ? 1.4416 1.5080 1.4295 0.0862  0.0086  0.0493  89  PRO I O   
15867 C CB  . PRO I  89  ? 1.1882 1.2438 1.1785 0.0784  0.0040  0.0410  89  PRO I CB  
15868 C CG  . PRO I  89  ? 1.1958 1.2522 1.1855 0.0772  0.0017  0.0392  89  PRO I CG  
15869 C CD  . PRO I  89  ? 1.1236 1.1812 1.1149 0.0803  0.0037  0.0416  89  PRO I CD  
15870 N N   . SER I  90  ? 1.3207 1.3809 1.3106 0.0858  0.0111  0.0494  90  SER I N   
15871 C CA  . SER I  90  ? 1.4802 1.5459 1.4673 0.0885  0.0131  0.0533  90  SER I CA  
15872 C C   . SER I  90  ? 1.5752 1.6405 1.5659 0.0927  0.0163  0.0572  90  SER I C   
15873 O O   . SER I  90  ? 1.5826 1.6539 1.5710 0.0952  0.0171  0.0606  90  SER I O   
15874 C CB  . SER I  90  ? 1.5318 1.6060 1.5131 0.0877  0.0107  0.0535  90  SER I CB  
15875 O OG  . SER I  90  ? 1.7939 1.8682 1.7735 0.0844  0.0074  0.0496  90  SER I OG  
15876 N N   . SER I  91  ? 1.5368 1.5950 1.5331 0.0935  0.0181  0.0568  91  SER I N   
15877 C CA  . SER I  91  ? 1.3060 1.3626 1.3061 0.0974  0.0219  0.0605  91  SER I CA  
15878 C C   . SER I  91  ? 1.4044 1.4553 1.4078 0.0981  0.0247  0.0611  91  SER I C   
15879 O O   . SER I  91  ? 1.4078 1.4519 1.4159 0.0972  0.0254  0.0592  91  SER I O   
15880 C CB  . SER I  91  ? 1.1225 1.1755 1.1268 0.0981  0.0224  0.0597  91  SER I CB  
15881 O OG  . SER I  91  ? 1.1541 1.2095 1.1562 0.0958  0.0191  0.0570  91  SER I OG  
15882 N N   . ASP I  92  ? 1.5612 1.6151 1.5620 0.0996  0.0264  0.0640  92  ASP I N   
15883 C CA  . ASP I  92  ? 1.7071 1.7561 1.7103 0.1001  0.0291  0.0646  92  ASP I CA  
15884 C C   . ASP I  92  ? 1.5825 1.6318 1.5876 0.1043  0.0332  0.0694  92  ASP I C   
15885 O O   . ASP I  92  ? 1.7159 1.7609 1.7235 0.1052  0.0360  0.0705  92  ASP I O   
15886 C CB  . ASP I  92  ? 2.0223 2.0734 2.0207 0.0977  0.0279  0.0634  92  ASP I CB  
15887 C CG  . ASP I  92  ? 2.0484 2.0996 2.0449 0.0936  0.0241  0.0589  92  ASP I CG  
15888 O OD1 . ASP I  92  ? 2.0430 2.0910 2.0426 0.0923  0.0224  0.0565  92  ASP I OD1 
15889 O OD2 . ASP I  92  ? 1.9813 2.0356 1.9731 0.0915  0.0229  0.0578  92  ASP I OD2 
15890 N N   . ASN I  93  ? 1.4180 1.4726 1.4220 0.1070  0.0335  0.0726  93  ASN I N   
15891 C CA  . ASN I  93  ? 1.3980 1.4529 1.4046 0.1113  0.0375  0.0775  93  ASN I CA  
15892 C C   . ASN I  93  ? 1.1727 1.2201 1.1863 0.1127  0.0402  0.0771  93  ASN I C   
15893 O O   . ASN I  93  ? 0.9767 1.0247 0.9927 0.1145  0.0410  0.0783  93  ASN I O   
15894 C CB  . ASN I  93  ? 1.3190 1.3822 1.3229 0.1138  0.0371  0.0812  93  ASN I CB  
15895 C CG  . ASN I  93  ? 1.4308 1.5018 1.4279 0.1132  0.0355  0.0830  93  ASN I CG  
15896 O OD1 . ASN I  93  ? 1.4362 1.5140 1.4293 0.1122  0.0325  0.0828  93  ASN I OD1 
15897 N ND2 . ASN I  93  ? 1.4287 1.4989 1.4244 0.1138  0.0375  0.0847  93  ASN I ND2 
15898 N N   . GLY I  94  ? 1.1948 1.2352 1.2118 0.1116  0.0417  0.0754  94  GLY I N   
15899 C CA  . GLY I  94  ? 1.0454 1.0785 1.0692 0.1126  0.0446  0.0749  94  GLY I CA  
15900 C C   . GLY I  94  ? 1.1011 1.1312 1.1277 0.1156  0.0491  0.0783  94  GLY I C   
15901 O O   . GLY I  94  ? 1.1229 1.1565 1.1488 0.1192  0.0516  0.0830  94  GLY I O   
15902 N N   . THR I  95  ? 0.8622 0.8858 0.8920 0.1140  0.0501  0.0762  95  THR I N   
15903 C CA  . THR I  95  ? 0.9661 0.9865 0.9985 0.1164  0.0544  0.0792  95  THR I CA  
15904 C C   . THR I  95  ? 0.8789 0.9040 0.9057 0.1168  0.0543  0.0814  95  THR I C   
15905 O O   . THR I  95  ? 0.9066 0.9312 0.9310 0.1138  0.0523  0.0786  95  THR I O   
15906 C CB  . THR I  95  ? 0.7117 0.7239 0.7495 0.1144  0.0555  0.0761  95  THR I CB  
15907 O OG1 . THR I  95  ? 0.4921 0.4999 0.5349 0.1140  0.0558  0.0742  95  THR I OG1 
15908 N N   . CYS I  96  ? 0.8196 0.8494 0.8443 0.1203  0.0565  0.0863  96  CYS I N   
15909 C CA  . CYS I  96  ? 0.8302 0.8646 0.8493 0.1207  0.0568  0.0888  96  CYS I CA  
15910 C C   . CYS I  96  ? 0.8923 0.9210 0.9139 0.1213  0.0605  0.0896  96  CYS I C   
15911 O O   . CYS I  96  ? 1.0032 1.0328 1.0210 0.1197  0.0603  0.0891  96  CYS I O   
15912 C CB  . CYS I  96  ? 0.8140 0.8561 0.8298 0.1241  0.0575  0.0941  96  CYS I CB  
15913 S SG  . CYS I  96  ? 1.1595 1.1997 1.1816 0.1290  0.0617  0.0985  96  CYS I SG  
15914 N N   . TYR I  97  ? 0.7870 0.8097 0.8151 0.1235  0.0641  0.0908  97  TYR I N   
15915 C CA  . TYR I  97  ? 0.7761 0.7925 0.8077 0.1239  0.0677  0.0910  97  TYR I CA  
15916 C C   . TYR I  97  ? 0.6868 0.6963 0.7232 0.1205  0.0665  0.0859  97  TYR I C   
15917 O O   . TYR I  97  ? 0.6926 0.6990 0.7334 0.1201  0.0659  0.0839  97  TYR I O   
15918 C CB  . TYR I  97  ? 0.8003 0.8139 0.8365 0.1281  0.0727  0.0954  97  TYR I CB  
15919 C CG  . TYR I  97  ? 0.7570 0.7661 0.7949 0.1292  0.0767  0.0971  97  TYR I CG  
15920 C CD1 . TYR I  97  ? 0.9063 0.9192 0.9405 0.1319  0.0792  0.1020  97  TYR I CD1 
15921 C CD2 . TYR I  97  ? 0.7059 0.7073 0.7492 0.1273  0.0780  0.0938  97  TYR I CD2 
15922 C CE1 . TYR I  97  ? 0.9709 0.9795 1.0064 0.1328  0.0831  0.1035  97  TYR I CE1 
15923 C CE2 . TYR I  97  ? 0.7722 0.7694 0.8173 0.1282  0.0818  0.0952  97  TYR I CE2 
15924 C CZ  . TYR I  97  ? 0.8026 0.8033 0.8437 0.1310  0.0844  0.1000  97  TYR I CZ  
15925 O OH  . TYR I  97  ? 0.6957 0.6921 0.7384 0.1318  0.0884  0.1015  97  TYR I OH  
15926 N N   . PRO I  98  ? 0.7305 0.7377 0.7661 0.1181  0.0662  0.0837  98  PRO I N   
15927 C CA  . PRO I  98  ? 0.6078 0.6093 0.6479 0.1147  0.0647  0.0790  98  PRO I CA  
15928 C C   . PRO I  98  ? 0.6786 0.6731 0.7266 0.1156  0.0673  0.0786  98  PRO I C   
15929 O O   . PRO I  98  ? 0.8552 0.8474 0.9059 0.1187  0.0717  0.0819  98  PRO I O   
15930 C CB  . PRO I  98  ? 0.6262 0.6261 0.6647 0.1134  0.0660  0.0787  98  PRO I CB  
15931 C CG  . PRO I  98  ? 0.7783 0.7849 0.8092 0.1147  0.0660  0.0817  98  PRO I CG  
15932 C CD  . PRO I  98  ? 0.8836 0.8936 0.9141 0.1185  0.0675  0.0859  98  PRO I CD  
15933 N N   . GLY I  99  ? 0.7822 0.7737 0.8340 0.1128  0.0648  0.0746  99  GLY I N   
15934 C CA  . GLY I  99  ? 0.7429 0.7280 0.8021 0.1130  0.0669  0.0737  99  GLY I CA  
15935 C C   . GLY I  99  ? 0.7201 0.7038 0.7815 0.1098  0.0632  0.0695  99  GLY I C   
15936 O O   . GLY I  99  ? 0.5799 0.5676 0.6372 0.1076  0.0590  0.0675  99  GLY I O   
15937 N N   . ASP I  100 ? 0.7384 0.7165 0.8063 0.1093  0.0649  0.0682  100 ASP I N   
15938 C CA  . ASP I  100 ? 0.6811 0.6573 0.7513 0.1060  0.0616  0.0643  100 ASP I CA  
15939 C C   . ASP I  100 ? 0.6243 0.6008 0.6950 0.1074  0.0625  0.0647  100 ASP I C   
15940 O O   . ASP I  100 ? 0.7063 0.6803 0.7799 0.1103  0.0670  0.0672  100 ASP I O   
15941 C CB  . ASP I  100 ? 0.7674 0.7373 0.8446 0.1038  0.0623  0.0619  100 ASP I CB  
15942 C CG  . ASP I  100 ? 1.0922 1.0612 1.1712 0.0995  0.0579  0.0577  100 ASP I CG  
15943 O OD1 . ASP I  100 ? 1.2834 1.2566 1.3576 0.0981  0.0540  0.0564  100 ASP I OD1 
15944 O OD2 . ASP I  100 ? 1.0585 1.0226 1.1434 0.0976  0.0584  0.0558  100 ASP I OD2 
15945 N N   . PHE I  101 ? 0.5228 0.5020 0.5907 0.1053  0.0586  0.0623  101 PHE I N   
15946 C CA  . PHE I  101 ? 0.4846 0.4636 0.5530 0.1060  0.0594  0.0622  101 PHE I CA  
15947 C C   . PHE I  101 ? 0.5249 0.4986 0.5981 0.1026  0.0584  0.0582  101 PHE I C   
15948 O O   . PHE I  101 ? 0.5991 0.5737 0.6709 0.0990  0.0540  0.0549  101 PHE I O   
15949 C CB  . PHE I  101 ? 0.4560 0.4413 0.5183 0.1057  0.0559  0.0620  101 PHE I CB  
15950 C CG  . PHE I  101 ? 0.5405 0.5271 0.6026 0.1083  0.0581  0.0638  101 PHE I CG  
15951 C CD1 . PHE I  101 ? 0.5883 0.5809 0.6463 0.1115  0.0587  0.0675  101 PHE I CD1 
15952 C CD2 . PHE I  101 ? 0.5561 0.5380 0.6223 0.1073  0.0596  0.0618  101 PHE I CD2 
15953 C CE1 . PHE I  101 ? 0.4539 0.4478 0.5122 0.1140  0.0609  0.0694  101 PHE I CE1 
15954 C CE2 . PHE I  101 ? 0.4372 0.4200 0.5035 0.1097  0.0621  0.0634  101 PHE I CE2 
15955 C CZ  . PHE I  101 ? 0.3828 0.3716 0.4455 0.1132  0.0627  0.0673  101 PHE I CZ  
15956 N N   . ILE I  102 ? 0.4480 0.4164 0.5269 0.1036  0.0626  0.0587  102 ILE I N   
15957 C CA  . ILE I  102 ? 0.4379 0.4010 0.5216 0.1001  0.0622  0.0550  102 ILE I CA  
15958 C C   . ILE I  102 ? 0.4851 0.4489 0.5671 0.0979  0.0598  0.0523  102 ILE I C   
15959 O O   . ILE I  102 ? 0.6154 0.5806 0.6957 0.1002  0.0619  0.0538  102 ILE I O   
15960 C CB  . ILE I  102 ? 0.5949 0.5522 0.6849 0.1018  0.0678  0.0561  102 ILE I CB  
15961 C CG1 . ILE I  102 ? 0.6143 0.5710 0.7056 0.1046  0.0706  0.0594  102 ILE I CG1 
15962 C CG2 . ILE I  102 ? 0.4441 0.3962 0.5392 0.0977  0.0669  0.0522  102 ILE I CG2 
15963 C CD1 . ILE I  102 ? 0.6538 0.6106 0.7455 0.1019  0.0675  0.0578  102 ILE I CD1 
15964 N N   . ASP I  103 ? 0.5693 0.5321 0.6518 0.0934  0.0557  0.0484  103 ASP I N   
15965 C CA  . ASP I  103 ? 0.5535 0.5167 0.6341 0.0906  0.0532  0.0455  103 ASP I CA  
15966 C C   . ASP I  103 ? 0.5020 0.4709 0.5764 0.0924  0.0517  0.0468  103 ASP I C   
15967 O O   . ASP I  103 ? 0.5281 0.4971 0.6014 0.0929  0.0528  0.0464  103 ASP I O   
15968 C CB  . ASP I  103 ? 0.5281 0.4861 0.6127 0.0905  0.0572  0.0444  103 ASP I CB  
15969 C CG  . ASP I  103 ? 0.6445 0.5971 0.7353 0.0880  0.0583  0.0426  103 ASP I CG  
15970 O OD1 . ASP I  103 ? 0.7894 0.7423 0.8811 0.0849  0.0544  0.0408  103 ASP I OD1 
15971 O OD2 . ASP I  103 ? 0.7538 0.7018 0.8488 0.0892  0.0631  0.0429  103 ASP I OD2 
15972 N N   . TYR I  104 ? 0.5589 0.5325 0.6295 0.0933  0.0493  0.0483  104 TYR I N   
15973 C CA  . TYR I  104 ? 0.4817 0.4613 0.5463 0.0950  0.0477  0.0498  104 TYR I CA  
15974 C C   . TYR I  104 ? 0.4900 0.4713 0.5515 0.0917  0.0436  0.0465  104 TYR I C   
15975 O O   . TYR I  104 ? 0.4530 0.4366 0.5121 0.0929  0.0442  0.0470  104 TYR I O   
15976 C CB  . TYR I  104 ? 0.4752 0.4592 0.5364 0.0959  0.0459  0.0516  104 TYR I CB  
15977 C CG  . TYR I  104 ? 0.5229 0.5137 0.5778 0.0973  0.0440  0.0531  104 TYR I CG  
15978 C CD1 . TYR I  104 ? 0.4938 0.4870 0.5476 0.1008  0.0468  0.0559  104 TYR I CD1 
15979 C CD2 . TYR I  104 ? 0.3776 0.3724 0.4281 0.0951  0.0396  0.0517  104 TYR I CD2 
15980 C CE1 . TYR I  104 ? 0.4985 0.4983 0.5469 0.1019  0.0450  0.0574  104 TYR I CE1 
15981 C CE2 . TYR I  104 ? 0.5070 0.5081 0.5519 0.0962  0.0379  0.0529  104 TYR I CE2 
15982 C CZ  . TYR I  104 ? 0.4849 0.4887 0.5288 0.0995  0.0405  0.0557  104 TYR I CZ  
15983 O OH  . TYR I  104 ? 0.5445 0.5550 0.5831 0.1005  0.0386  0.0570  104 TYR I OH  
15984 N N   . GLU I  105 ? 0.5778 0.5581 0.6397 0.0875  0.0395  0.0433  105 GLU I N   
15985 C CA  . GLU I  105 ? 0.5039 0.4857 0.5627 0.0840  0.0353  0.0401  105 GLU I CA  
15986 C C   . GLU I  105 ? 0.4627 0.4411 0.5230 0.0831  0.0373  0.0384  105 GLU I C   
15987 O O   . GLU I  105 ? 0.5268 0.5073 0.5837 0.0822  0.0358  0.0372  105 GLU I O   
15988 C CB  . GLU I  105 ? 0.5249 0.5056 0.5847 0.0798  0.0310  0.0374  105 GLU I CB  
15989 C CG  . GLU I  105 ? 0.5251 0.5087 0.5836 0.0803  0.0292  0.0387  105 GLU I CG  
15990 C CD  . GLU I  105 ? 0.7708 0.7518 0.8335 0.0826  0.0329  0.0410  105 GLU I CD  
15991 O OE1 . GLU I  105 ? 0.7599 0.7361 0.8278 0.0824  0.0355  0.0406  105 GLU I OE1 
15992 O OE2 . GLU I  105 ? 0.7194 0.7032 0.7800 0.0846  0.0333  0.0431  105 GLU I OE2 
15993 N N   . GLU I  106 ? 0.4930 0.4661 0.5586 0.0833  0.0408  0.0383  106 GLU I N   
15994 C CA  . GLU I  106 ? 0.4351 0.4043 0.5026 0.0824  0.0435  0.0366  106 GLU I CA  
15995 C C   . GLU I  106 ? 0.5258 0.4968 0.5917 0.0863  0.0472  0.0390  106 GLU I C   
15996 O O   . GLU I  106 ? 0.5439 0.5141 0.6085 0.0851  0.0477  0.0372  106 GLU I O   
15997 C CB  . GLU I  106 ? 0.4516 0.4147 0.5254 0.0819  0.0469  0.0361  106 GLU I CB  
15998 C CG  . GLU I  106 ? 0.8101 0.7705 0.8859 0.0766  0.0435  0.0323  106 GLU I CG  
15999 C CD  . GLU I  106 ? 0.7119 0.6709 0.7857 0.0733  0.0426  0.0289  106 GLU I CD  
16000 O OE1 . GLU I  106 ? 0.7461 0.7029 0.8205 0.0749  0.0469  0.0292  106 GLU I OE1 
16001 O OE2 . GLU I  106 ? 0.6184 0.5786 0.6903 0.0690  0.0377  0.0261  106 GLU I OE2 
16002 N N   . LEU I  107 ? 0.5931 0.5665 0.6588 0.0908  0.0498  0.0432  107 LEU I N   
16003 C CA  . LEU I  107 ? 0.5256 0.5015 0.5901 0.0949  0.0532  0.0463  107 LEU I CA  
16004 C C   . LEU I  107 ? 0.5617 0.5434 0.6206 0.0943  0.0496  0.0458  107 LEU I C   
16005 O O   . LEU I  107 ? 0.5662 0.5480 0.6243 0.0947  0.0509  0.0453  107 LEU I O   
16006 C CB  . LEU I  107 ? 0.5426 0.5207 0.6080 0.0996  0.0561  0.0511  107 LEU I CB  
16007 C CG  . LEU I  107 ? 0.5937 0.5749 0.6585 0.1044  0.0598  0.0552  107 LEU I CG  
16008 C CD1 . LEU I  107 ? 0.5403 0.5160 0.6099 0.1056  0.0653  0.0553  107 LEU I CD1 
16009 C CD2 . LEU I  107 ? 0.5209 0.5053 0.5852 0.1083  0.0614  0.0599  107 LEU I CD2 
16010 N N   . ARG I  108 ? 0.4507 0.4369 0.5059 0.0934  0.0452  0.0458  108 ARG I N   
16011 C CA  . ARG I  108 ? 0.5354 0.5271 0.5851 0.0923  0.0412  0.0450  108 ARG I CA  
16012 C C   . ARG I  108 ? 0.5362 0.5257 0.5851 0.0888  0.0397  0.0411  108 ARG I C   
16013 O O   . ARG I  108 ? 0.4764 0.4687 0.5226 0.0895  0.0397  0.0412  108 ARG I O   
16014 C CB  . ARG I  108 ? 0.5224 0.5172 0.5691 0.0903  0.0365  0.0441  108 ARG I CB  
16015 C CG  . ARG I  108 ? 0.5084 0.5059 0.5548 0.0934  0.0377  0.0477  108 ARG I CG  
16016 C CD  . ARG I  108 ? 0.5113 0.5106 0.5554 0.0908  0.0336  0.0463  108 ARG I CD  
16017 N NE  . ARG I  108 ? 0.4486 0.4525 0.4875 0.0888  0.0292  0.0446  108 ARG I NE  
16018 C CZ  . ARG I  108 ? 0.6208 0.6309 0.6552 0.0903  0.0280  0.0465  108 ARG I CZ  
16019 N NH1 . ARG I  108 ? 0.6004 0.6129 0.6344 0.0938  0.0307  0.0502  108 ARG I NH1 
16020 N NH2 . ARG I  108 ? 0.4486 0.4625 0.4786 0.0881  0.0242  0.0446  108 ARG I NH2 
16021 N N   . GLU I  109 ? 0.5081 0.4927 0.5593 0.0850  0.0385  0.0377  109 GLU I N   
16022 C CA  . GLU I  109 ? 0.5587 0.5408 0.6090 0.0810  0.0369  0.0338  109 GLU I CA  
16023 C C   . GLU I  109 ? 0.4726 0.4520 0.5246 0.0827  0.0418  0.0340  109 GLU I C   
16024 O O   . GLU I  109 ? 0.4703 0.4502 0.5198 0.0811  0.0412  0.0321  109 GLU I O   
16025 C CB  . GLU I  109 ? 0.5731 0.5506 0.6261 0.0767  0.0350  0.0307  109 GLU I CB  
16026 C CG  . GLU I  109 ? 0.6918 0.6669 0.7436 0.0721  0.0331  0.0265  109 GLU I CG  
16027 C CD  . GLU I  109 ? 0.8344 0.8138 0.8806 0.0696  0.0278  0.0249  109 GLU I CD  
16028 O OE1 . GLU I  109 ? 0.9466 0.9311 0.9900 0.0718  0.0261  0.0270  109 GLU I OE1 
16029 O OE2 . GLU I  109 ? 0.9347 0.9125 0.9794 0.0654  0.0255  0.0215  109 GLU I OE2 
16030 N N   . GLN I  110 ? 0.4462 0.4224 0.5027 0.0858  0.0470  0.0364  110 GLN I N   
16031 C CA  . GLN I  110 ? 0.6369 0.6100 0.6960 0.0877  0.0524  0.0369  110 GLN I CA  
16032 C C   . GLN I  110 ? 0.6962 0.6745 0.7530 0.0917  0.0539  0.0402  110 GLN I C   
16033 O O   . GLN I  110 ? 0.6773 0.6544 0.7344 0.0922  0.0567  0.0397  110 GLN I O   
16034 C CB  . GLN I  110 ? 0.7088 0.6770 0.7737 0.0899  0.0577  0.0387  110 GLN I CB  
16035 C CG  . GLN I  110 ? 0.6805 0.6447 0.7481 0.0867  0.0561  0.0365  110 GLN I CG  
16036 C CD  . GLN I  110 ? 0.7504 0.7074 0.8223 0.0843  0.0597  0.0337  110 GLN I CD  
16037 O OE1 . GLN I  110 ? 0.8530 0.8076 0.9256 0.0848  0.0634  0.0330  110 GLN I OE1 
16038 N NE2 . GLN I  110 ? 0.5812 0.5350 0.6562 0.0816  0.0586  0.0319  110 GLN I NE2 
16039 N N   . LEU I  111 ? 0.7262 0.7102 0.7808 0.0945  0.0522  0.0436  111 LEU I N   
16040 C CA  . LEU I  111 ? 0.5320 0.5220 0.5846 0.0984  0.0531  0.0472  111 LEU I CA  
16041 C C   . LEU I  111 ? 0.5875 0.5820 0.6348 0.0960  0.0485  0.0450  111 LEU I C   
16042 O O   . LEU I  111 ? 0.6104 0.6091 0.6563 0.0983  0.0494  0.0470  111 LEU I O   
16043 C CB  . LEU I  111 ? 0.5180 0.5126 0.5700 0.1019  0.0529  0.0515  111 LEU I CB  
16044 C CG  . LEU I  111 ? 0.5955 0.5893 0.6516 0.1069  0.0585  0.0563  111 LEU I CG  
16045 C CD1 . LEU I  111 ? 0.7586 0.7447 0.8201 0.1068  0.0635  0.0551  111 LEU I CD1 
16046 C CD2 . LEU I  111 ? 0.5535 0.5486 0.6095 0.1082  0.0578  0.0587  111 LEU I CD2 
16047 N N   . SER I  112 ? 0.5901 0.5838 0.6349 0.0914  0.0437  0.0411  112 SER I N   
16048 C CA  . SER I  112 ? 0.5499 0.5479 0.5895 0.0888  0.0389  0.0391  112 SER I CA  
16049 C C   . SER I  112 ? 0.5560 0.5553 0.5944 0.0895  0.0406  0.0388  112 SER I C   
16050 O O   . SER I  112 ? 0.6505 0.6555 0.6851 0.0900  0.0382  0.0395  112 SER I O   
16051 C CB  . SER I  112 ? 0.6281 0.6231 0.6663 0.0834  0.0346  0.0345  112 SER I CB  
16052 O OG  . SER I  112 ? 0.5933 0.5825 0.6334 0.0806  0.0364  0.0314  112 SER I OG  
16053 N N   . SER I  113 ? 0.5558 0.5496 0.5975 0.0893  0.0448  0.0376  113 SER I N   
16054 C CA  . SER I  113 ? 0.5800 0.5743 0.6213 0.0902  0.0474  0.0375  113 SER I CA  
16055 C C   . SER I  113 ? 0.7110 0.7011 0.7578 0.0934  0.0543  0.0396  113 SER I C   
16056 O O   . SER I  113 ? 0.6557 0.6392 0.7058 0.0919  0.0568  0.0378  113 SER I O   
16057 C CB  . SER I  113 ? 0.7655 0.7570 0.8039 0.0850  0.0448  0.0324  113 SER I CB  
16058 O OG  . SER I  113 ? 0.7721 0.7650 0.8094 0.0857  0.0468  0.0322  113 SER I OG  
16059 N N   . VAL I  114 ? 0.7925 0.7865 0.8404 0.0979  0.0573  0.0435  114 VAL I N   
16060 C CA  . VAL I  114 ? 0.7768 0.7675 0.8302 0.1018  0.0641  0.0465  114 VAL I CA  
16061 C C   . VAL I  114 ? 0.8077 0.7991 0.8619 0.1031  0.0674  0.0469  114 VAL I C   
16062 O O   . VAL I  114 ? 0.7966 0.7944 0.8479 0.1041  0.0650  0.0482  114 VAL I O   
16063 C CB  . VAL I  114 ? 0.7129 0.7078 0.7684 0.1070  0.0656  0.0523  114 VAL I CB  
16064 C CG1 . VAL I  114 ? 0.7777 0.7762 0.8357 0.1120  0.0699  0.0571  114 VAL I CG1 
16065 C CG2 . VAL I  114 ? 0.6928 0.6819 0.7524 0.1075  0.0686  0.0528  114 VAL I CG2 
16066 N N   . SER I  115 ? 0.8026 0.7872 0.8609 0.1031  0.0731  0.0457  115 SER I N   
16067 C CA  . SER I  115 ? 1.0359 1.0200 1.0956 0.1042  0.0770  0.0457  115 SER I CA  
16068 C C   . SER I  115 ? 0.9419 0.9300 1.0060 0.1107  0.0816  0.0522  115 SER I C   
16069 O O   . SER I  115 ? 1.0759 1.0696 1.1392 0.1129  0.0813  0.0545  115 SER I O   
16070 C CB  . SER I  115 ? 1.0694 1.0444 1.1316 0.1011  0.0814  0.0414  115 SER I CB  
16071 O OG  . SER I  115 ? 1.0768 1.0511 1.1387 0.1005  0.0840  0.0399  115 SER I OG  
16072 N N   . SER I  116 ? 0.9760 0.9611 1.0448 0.1138  0.0858  0.0552  116 SER I N   
16073 C CA  . SER I  116 ? 1.0194 1.0088 1.0923 0.1202  0.0896  0.0621  116 SER I CA  
16074 C C   . SER I  116 ? 0.9795 0.9701 1.0532 0.1223  0.0887  0.0652  116 SER I C   
16075 O O   . SER I  116 ? 0.9811 0.9657 1.0556 0.1199  0.0890  0.0626  116 SER I O   
16076 C CB  . SER I  116 ? 1.1418 1.1256 1.2211 0.1228  0.0977  0.0635  116 SER I CB  
16077 O OG  . SER I  116 ? 1.2657 1.2415 1.3486 0.1220  0.1016  0.0620  116 SER I OG  
16078 N N   . PHE I  117 ? 0.9231 0.9214 0.9963 0.1265  0.0875  0.0709  117 PHE I N   
16079 C CA  . PHE I  117 ? 0.8482 0.8487 0.9210 0.1283  0.0861  0.0739  117 PHE I CA  
16080 C C   . PHE I  117 ? 0.7956 0.8019 0.8713 0.1345  0.0891  0.0815  117 PHE I C   
16081 O O   . PHE I  117 ? 0.8998 0.9145 0.9730 0.1363  0.0863  0.0845  117 PHE I O   
16082 C CB  . PHE I  117 ? 0.7716 0.7771 0.8377 0.1251  0.0785  0.0717  117 PHE I CB  
16083 C CG  . PHE I  117 ? 0.7440 0.7499 0.8093 0.1255  0.0768  0.0732  117 PHE I CG  
16084 C CD1 . PHE I  117 ? 0.6166 0.6294 0.6809 0.1294  0.0762  0.0787  117 PHE I CD1 
16085 C CD2 . PHE I  117 ? 0.7178 0.7174 0.7831 0.1218  0.0757  0.0690  117 PHE I CD2 
16086 C CE1 . PHE I  117 ? 0.5367 0.5497 0.6000 0.1296  0.0749  0.0799  117 PHE I CE1 
16087 C CE2 . PHE I  117 ? 0.7402 0.7399 0.8050 0.1222  0.0744  0.0703  117 PHE I CE2 
16088 C CZ  . PHE I  117 ? 0.6638 0.6701 0.7275 0.1260  0.0741  0.0757  117 PHE I CZ  
16089 N N   . GLU I  118 ? 0.8796 0.8816 0.9608 0.1378  0.0948  0.0846  118 GLU I N   
16090 C CA  . GLU I  118 ? 0.8753 0.8826 0.9595 0.1438  0.0978  0.0922  118 GLU I CA  
16091 C C   . GLU I  118 ? 0.7395 0.7459 0.8241 0.1453  0.0982  0.0948  118 GLU I C   
16092 O O   . GLU I  118 ? 0.8571 0.8562 0.9427 0.1428  0.0991  0.0913  118 GLU I O   
16093 C CB  . GLU I  118 ? 1.0489 1.0529 1.1402 0.1475  0.1053  0.0952  118 GLU I CB  
16094 C CG  . GLU I  118 ? 1.2201 1.2151 1.3169 0.1486  0.1115  0.0953  118 GLU I CG  
16095 C CD  . GLU I  118 ? 1.5032 1.4998 1.6061 0.1550  0.1176  0.1029  118 GLU I CD  
16096 O OE1 . GLU I  118 ? 1.5193 1.5248 1.6212 0.1587  0.1159  0.1087  118 GLU I OE1 
16097 O OE2 . GLU I  118 ? 1.4524 1.4412 1.5611 0.1563  0.1241  0.1031  118 GLU I OE2 
16098 N N   . ARG I  119 ? 0.7672 0.7814 0.8509 0.1493  0.0974  0.1010  119 ARG I N   
16099 C CA  . ARG I  119 ? 0.7917 0.8060 0.8752 0.1509  0.0976  0.1040  119 ARG I CA  
16100 C C   . ARG I  119 ? 0.7878 0.8027 0.8770 0.1570  0.1038  0.1112  119 ARG I C   
16101 O O   . ARG I  119 ? 0.9237 0.9464 1.0132 0.1607  0.1040  0.1168  119 ARG I O   
16102 C CB  . ARG I  119 ? 0.7822 0.8051 0.8589 0.1500  0.0911  0.1049  119 ARG I CB  
16103 C CG  . ARG I  119 ? 0.7506 0.7752 0.8263 0.1521  0.0914  0.1089  119 ARG I CG  
16104 C CD  . ARG I  119 ? 0.9232 0.9578 0.9976 0.1564  0.0909  0.1159  119 ARG I CD  
16105 N NE  . ARG I  119 ? 0.9871 1.0274 1.0551 0.1551  0.0859  0.1165  119 ARG I NE  
16106 C CZ  . ARG I  119 ? 1.2094 1.2588 1.2747 0.1579  0.0846  0.1221  119 ARG I CZ  
16107 N NH1 . ARG I  119 ? 1.2566 1.3109 1.3254 0.1625  0.0875  0.1282  119 ARG I NH1 
16108 N NH2 . ARG I  119 ? 1.1198 1.1736 1.1790 0.1560  0.0803  0.1218  119 ARG I NH2 
16109 N N   . PHE I  120 ? 0.8250 0.8318 0.9191 0.1578  0.1090  0.1111  120 PHE I N   
16110 C CA  . PHE I  120 ? 0.8395 0.8455 0.9396 0.1635  0.1156  0.1177  120 PHE I CA  
16111 C C   . PHE I  120 ? 0.7554 0.7595 0.8559 0.1649  0.1169  0.1203  120 PHE I C   
16112 O O   . PHE I  120 ? 0.7355 0.7354 0.8336 0.1611  0.1145  0.1157  120 PHE I O   
16113 C CB  . PHE I  120 ? 0.8297 0.8271 0.9366 0.1638  0.1223  0.1159  120 PHE I CB  
16114 C CG  . PHE I  120 ? 0.8090 0.7961 0.9174 0.1600  0.1240  0.1100  120 PHE I CG  
16115 C CD1 . PHE I  120 ? 0.9175 0.8987 1.0308 0.1623  0.1295  0.1123  120 PHE I CD1 
16116 C CD2 . PHE I  120 ? 0.9232 0.9068 1.0281 0.1541  0.1201  0.1024  120 PHE I CD2 
16117 C CE1 . PHE I  120 ? 0.8832 0.8553 0.9981 0.1586  0.1311  0.1069  120 PHE I CE1 
16118 C CE2 . PHE I  120 ? 0.8474 0.8221 0.9539 0.1504  0.1215  0.0972  120 PHE I CE2 
16119 C CZ  . PHE I  120 ? 0.7633 0.7323 0.8749 0.1526  0.1269  0.0994  120 PHE I CZ  
16120 N N   . GLU I  121 ? 0.8457 0.8530 0.9494 0.1704  0.1208  0.1278  121 GLU I N   
16121 C CA  . GLU I  121 ? 0.7907 0.7961 0.8951 0.1722  0.1227  0.1309  121 GLU I CA  
16122 C C   . GLU I  121 ? 0.8491 0.8434 0.9598 0.1721  0.1291  0.1287  121 GLU I C   
16123 O O   . GLU I  121 ? 1.0584 1.0496 1.1756 0.1758  0.1355  0.1322  121 GLU I O   
16124 C CB  . GLU I  121 ? 0.8358 0.8490 0.9413 0.1781  0.1246  0.1399  121 GLU I CB  
16125 C CG  . GLU I  121 ? 1.0398 1.0538 1.1432 0.1794  0.1246  0.1433  121 GLU I CG  
16126 C CD  . GLU I  121 ? 1.2306 1.2535 1.3339 0.1847  0.1254  0.1523  121 GLU I CD  
16127 O OE1 . GLU I  121 ? 1.3833 1.4099 1.4905 0.1883  0.1280  0.1567  121 GLU I OE1 
16128 O OE2 . GLU I  121 ? 1.1451 1.1715 1.2445 0.1853  0.1237  0.1550  121 GLU I OE2 
16129 N N   . ILE I  122 ? 0.8849 0.8732 0.9940 0.1678  0.1274  0.1230  122 ILE I N   
16130 C CA  . ILE I  122 ? 0.8190 0.7967 0.9337 0.1669  0.1328  0.1203  122 ILE I CA  
16131 C C   . ILE I  122 ? 0.9790 0.9549 1.0974 0.1713  0.1379  0.1261  122 ILE I C   
16132 O O   . ILE I  122 ? 1.0585 1.0278 1.1835 0.1735  0.1448  0.1275  122 ILE I O   
16133 C CB  . ILE I  122 ? 0.8908 0.8631 1.0028 0.1608  0.1290  0.1125  122 ILE I CB  
16134 C CG1 . ILE I  122 ? 0.7839 0.7457 0.9018 0.1598  0.1346  0.1099  122 ILE I CG1 
16135 C CG2 . ILE I  122 ? 0.8322 0.8092 0.9383 0.1595  0.1234  0.1127  122 ILE I CG2 
16136 C CD1 . ILE I  122 ? 0.6695 0.6262 0.7855 0.1538  0.1311  0.1025  122 ILE I CD1 
16137 N N   . PHE I  123 ? 0.9628 0.9443 1.0768 0.1724  0.1346  0.1294  123 PHE I N   
16138 C CA  . PHE I  123 ? 0.8231 0.8042 0.9396 0.1767  0.1389  0.1355  123 PHE I CA  
16139 C C   . PHE I  123 ? 0.9957 0.9875 1.1086 0.1806  0.1367  0.1427  123 PHE I C   
16140 O O   . PHE I  123 ? 0.9316 0.9288 1.0380 0.1791  0.1315  0.1427  123 PHE I O   
16141 C CB  . PHE I  123 ? 0.8348 0.8111 0.9499 0.1740  0.1380  0.1324  123 PHE I CB  
16142 C CG  . PHE I  123 ? 0.9216 0.8874 1.0409 0.1703  0.1405  0.1259  123 PHE I CG  
16143 C CD1 . PHE I  123 ? 0.8766 0.8401 0.9926 0.1647  0.1356  0.1190  123 PHE I CD1 
16144 C CD2 . PHE I  123 ? 0.9806 0.9392 1.1072 0.1723  0.1478  0.1268  123 PHE I CD2 
16145 C CE1 . PHE I  123 ? 0.8937 0.8483 1.0135 0.1611  0.1376  0.1132  123 PHE I CE1 
16146 C CE2 . PHE I  123 ? 0.9310 0.8803 1.0613 0.1686  0.1501  0.1207  123 PHE I CE2 
16147 C CZ  . PHE I  123 ? 0.9281 0.8756 1.0549 0.1629  0.1448  0.1139  123 PHE I CZ  
16148 N N   . PRO I  124 ? 1.2422 1.2371 1.3592 0.1856  0.1408  0.1490  124 PRO I N   
16149 C CA  . PRO I  124 ? 1.2040 1.2096 1.3183 0.1896  0.1392  0.1567  124 PRO I CA  
16150 C C   . PRO I  124 ? 1.1934 1.2005 1.3048 0.1909  0.1390  0.1604  124 PRO I C   
16151 O O   . PRO I  124 ? 1.1276 1.1274 1.2431 0.1922  0.1441  0.1611  124 PRO I O   
16152 C CB  . PRO I  124 ? 1.2657 1.2710 1.3876 0.1951  0.1458  0.1629  124 PRO I CB  
16153 C CG  . PRO I  124 ? 1.2976 1.2945 1.4243 0.1928  0.1489  0.1570  124 PRO I CG  
16154 C CD  . PRO I  124 ? 1.1759 1.1646 1.3008 0.1876  0.1474  0.1493  124 PRO I CD  
16155 N N   . LYS I  125 ? 1.1047 1.1211 1.2089 0.1906  0.1334  0.1626  125 LYS I N   
16156 C CA  . LYS I  125 ? 1.2569 1.2750 1.3570 0.1909  0.1326  0.1651  125 LYS I CA  
16157 C C   . LYS I  125 ? 1.5779 1.5956 1.6825 0.1965  0.1388  0.1732  125 LYS I C   
16158 O O   . LYS I  125 ? 1.5408 1.5551 1.6447 0.1968  0.1406  0.1742  125 LYS I O   
16159 C CB  . LYS I  125 ? 1.1700 1.1989 1.2615 0.1894  0.1257  0.1662  125 LYS I CB  
16160 C CG  . LYS I  125 ? 1.2467 1.2772 1.3330 0.1891  0.1245  0.1681  125 LYS I CG  
16161 C CD  . LYS I  125 ? 1.1514 1.1905 1.2286 0.1858  0.1173  0.1665  125 LYS I CD  
16162 C CE  . LYS I  125 ? 1.2560 1.3069 1.3308 0.1886  0.1151  0.1726  125 LYS I CE  
16163 N NZ  . LYS I  125 ? 1.2082 1.2675 1.2738 0.1853  0.1084  0.1712  125 LYS I NZ  
16164 N N   . THR I  126 ? 2.2228 2.2440 2.3321 0.2011  0.1421  0.1792  126 THR I N   
16165 C CA  . THR I  126 ? 2.0949 2.1183 2.2075 0.2068  0.1471  0.1882  126 THR I CA  
16166 C C   . THR I  126 ? 2.1080 2.1220 2.2301 0.2102  0.1556  0.1902  126 THR I C   
16167 O O   . THR I  126 ? 2.3993 2.4154 2.5253 0.2155  0.1602  0.1982  126 THR I O   
16168 C CB  . THR I  126 ? 1.6428 1.6780 1.7549 0.2106  0.1454  0.1956  126 THR I CB  
16169 O OG1 . THR I  126 ? 1.6301 1.6663 1.7440 0.2092  0.1438  0.1921  126 THR I OG1 
16170 N N   . SER I  127 ? 1.3650 1.3690 1.4909 0.2071  0.1578  0.1830  127 SER I N   
16171 C CA  . SER I  127 ? 1.4052 1.3997 1.5399 0.2097  0.1660  0.1840  127 SER I CA  
16172 C C   . SER I  127 ? 1.3498 1.3332 1.4859 0.2054  0.1675  0.1762  127 SER I C   
16173 O O   . SER I  127 ? 1.3895 1.3643 1.5320 0.2070  0.1743  0.1768  127 SER I O   
16174 C CB  . SER I  127 ? 1.4828 1.4769 1.6235 0.2116  0.1691  0.1847  127 SER I CB  
16175 O OG  . SER I  127 ? 1.2216 1.2151 1.3595 0.2066  0.1645  0.1769  127 SER I OG  
16176 N N   . SER I  128 ? 1.3476 1.3313 1.4775 0.1999  0.1611  0.1693  128 SER I N   
16177 C CA  . SER I  128 ? 1.2526 1.2266 1.3836 0.1952  0.1615  0.1614  128 SER I CA  
16178 C C   . SER I  128 ? 1.2087 1.1802 1.3374 0.1945  0.1615  0.1617  128 SER I C   
16179 O O   . SER I  128 ? 1.1349 1.0974 1.2671 0.1925  0.1646  0.1577  128 SER I O   
16180 C CB  . SER I  128 ? 1.1164 1.0916 1.2426 0.1895  0.1547  0.1536  128 SER I CB  
16181 O OG  . SER I  128 ? 0.8770 0.8552 1.0046 0.1901  0.1544  0.1536  128 SER I OG  
16182 N N   . TRP I  129 ? 1.2151 1.1947 1.3380 0.1962  0.1583  0.1664  129 TRP I N   
16183 C CA  . TRP I  129 ? 1.2366 1.2148 1.3562 0.1952  0.1577  0.1665  129 TRP I CA  
16184 C C   . TRP I  129 ? 1.2947 1.2770 1.4141 0.2005  0.1611  0.1755  129 TRP I C   
16185 O O   . TRP I  129 ? 1.1841 1.1748 1.2968 0.2009  0.1570  0.1789  129 TRP I O   
16186 C CB  . TRP I  129 ? 1.3097 1.2931 1.4209 0.1906  0.1497  0.1620  129 TRP I CB  
16187 C CG  . TRP I  129 ? 1.2034 1.1856 1.3140 0.1861  0.1456  0.1546  129 TRP I CG  
16188 C CD1 . TRP I  129 ? 1.0864 1.0760 1.1923 0.1846  0.1401  0.1535  129 TRP I CD1 
16189 C CD2 . TRP I  129 ? 1.0966 1.0695 1.2113 0.1823  0.1468  0.1475  129 TRP I CD2 
16190 N NE1 . TRP I  129 ? 0.9565 0.9419 1.0632 0.1803  0.1378  0.1461  129 TRP I NE1 
16191 C CE2 . TRP I  129 ? 0.9829 0.9582 1.0949 0.1788  0.1418  0.1424  129 TRP I CE2 
16192 C CE3 . TRP I  129 ? 1.0264 0.9893 1.1467 0.1815  0.1516  0.1449  129 TRP I CE3 
16193 C CZ2 . TRP I  129 ? 1.0817 1.0500 1.1962 0.1744  0.1413  0.1350  129 TRP I CZ2 
16194 C CZ3 . TRP I  129 ? 0.9215 0.8778 1.0445 0.1771  0.1510  0.1375  129 TRP I CZ3 
16195 C CH2 . TRP I  129 ? 0.9738 0.9328 1.0937 0.1736  0.1458  0.1326  129 TRP I CH2 
16196 N N   . PRO I  130 ? 1.4362 1.4126 1.5630 0.2044  0.1686  0.1795  130 PRO I N   
16197 C CA  . PRO I  130 ? 1.3494 1.3292 1.4772 0.2099  0.1727  0.1887  130 PRO I CA  
16198 C C   . PRO I  130 ? 1.5167 1.4931 1.6422 0.2094  0.1740  0.1892  130 PRO I C   
16199 O O   . PRO I  130 ? 1.5254 1.5058 1.6496 0.2132  0.1760  0.1965  130 PRO I O   
16200 C CB  . PRO I  130 ? 1.3134 1.2866 1.4510 0.2138  0.1808  0.1915  130 PRO I CB  
16201 C CG  . PRO I  130 ? 1.2803 1.2474 1.4212 0.2099  0.1804  0.1835  130 PRO I CG  
16202 C CD  . PRO I  130 ? 1.4780 1.4443 1.6129 0.2038  0.1740  0.1756  130 PRO I CD  
16203 N N   . ASN I  131 ? 1.7229 1.6922 1.8481 0.2047  0.1728  0.1816  131 ASN I N   
16204 C CA  . ASN I  131 ? 1.6427 1.6078 1.7665 0.2038  0.1743  0.1813  131 ASN I CA  
16205 C C   . ASN I  131 ? 1.5643 1.5335 1.6798 0.1993  0.1673  0.1769  131 ASN I C   
16206 O O   . ASN I  131 ? 1.5395 1.5049 1.6534 0.1976  0.1677  0.1751  131 ASN I O   
16207 C CB  . ASN I  131 ? 1.6233 1.5765 1.7545 0.2023  0.1794  0.1765  131 ASN I CB  
16208 C CG  . ASN I  131 ? 1.7248 1.6730 1.8645 0.2069  0.1873  0.1809  131 ASN I CG  
16209 O OD1 . ASN I  131 ? 1.8470 1.8003 1.9873 0.2119  0.1898  0.1889  131 ASN I OD1 
16210 N ND2 . ASN I  131 ? 1.7005 1.6390 1.8470 0.2050  0.1914  0.1758  131 ASN I ND2 
16211 N N   . HIS I  132 ? 1.2568 1.2334 1.3671 0.1973  0.1610  0.1751  132 HIS I N   
16212 C CA  . HIS I  132 ? 1.0717 1.0520 1.1743 0.1927  0.1543  0.1704  132 HIS I CA  
16213 C C   . HIS I  132 ? 1.0476 1.0397 1.1432 0.1933  0.1490  0.1738  132 HIS I C   
16214 O O   . HIS I  132 ? 1.1729 1.1695 1.2704 0.1962  0.1495  0.1775  132 HIS I O   
16215 C CB  . HIS I  132 ? 1.0030 0.9780 1.1073 0.1876  0.1513  0.1614  132 HIS I CB  
16216 C CG  . HIS I  132 ? 0.9805 0.9443 1.0923 0.1866  0.1563  0.1578  132 HIS I CG  
16217 N ND1 . HIS I  132 ? 0.9047 0.8629 1.0166 0.1835  0.1562  0.1535  132 HIS I ND1 
16218 C CD2 . HIS I  132 ? 1.0534 1.0109 1.1731 0.1884  0.1617  0.1578  132 HIS I CD2 
16219 C CE1 . HIS I  132 ? 1.0419 0.9909 1.1613 0.1832  0.1611  0.1510  132 HIS I CE1 
16220 N NE2 . HIS I  132 ? 1.0673 1.0155 1.1913 0.1860  0.1646  0.1534  132 HIS I NE2 
16221 N N   . ASP I  133 ? 0.8935 0.8904 0.9811 0.1906  0.1442  0.1726  133 ASP I N   
16222 C CA  . ASP I  133 ? 1.0363 1.0446 1.1167 0.1906  0.1390  0.1753  133 ASP I CA  
16223 C C   . ASP I  133 ? 1.1260 1.1364 1.2044 0.1866  0.1332  0.1689  133 ASP I C   
16224 O O   . ASP I  133 ? 1.0499 1.0565 1.1263 0.1819  0.1302  0.1620  133 ASP I O   
16225 C CB  . ASP I  133 ? 1.0448 1.0574 1.1171 0.1893  0.1367  0.1768  133 ASP I CB  
16226 C CG  . ASP I  133 ? 1.2971 1.3219 1.3621 0.1901  0.1323  0.1813  133 ASP I CG  
16227 O OD1 . ASP I  133 ? 1.2748 1.3047 1.3383 0.1886  0.1280  0.1791  133 ASP I OD1 
16228 O OD2 . ASP I  133 ? 1.5083 1.5379 1.5690 0.1920  0.1332  0.1870  133 ASP I OD2 
16229 N N   . SER I  134 ? 1.0691 1.0854 1.1482 0.1884  0.1319  0.1714  134 SER I N   
16230 C CA  . SER I  134 ? 1.0031 1.0217 1.0805 0.1850  0.1268  0.1659  134 SER I CA  
16231 C C   . SER I  134 ? 0.9720 1.0022 1.0415 0.1842  0.1210  0.1679  134 SER I C   
16232 O O   . SER I  134 ? 1.1278 1.1626 1.1966 0.1834  0.1177  0.1665  134 SER I O   
16233 C CB  . SER I  134 ? 1.0524 1.0684 1.1371 0.1871  0.1298  0.1662  134 SER I CB  
16234 O OG  . SER I  134 ? 1.2312 1.2525 1.3182 0.1925  0.1329  0.1744  134 SER I OG  
16235 N N   . ASN I  135 ? 0.9511 0.9859 1.0144 0.1843  0.1199  0.1710  135 ASN I N   
16236 C CA  . ASN I  135 ? 1.1278 1.1740 1.1833 0.1835  0.1148  0.1734  135 ASN I CA  
16237 C C   . ASN I  135 ? 1.0873 1.1347 1.1347 0.1792  0.1110  0.1697  135 ASN I C   
16238 O O   . ASN I  135 ? 1.2544 1.3095 1.2951 0.1766  0.1057  0.1684  135 ASN I O   
16239 C CB  . ASN I  135 ? 1.3785 1.4322 1.4337 0.1887  0.1171  0.1830  135 ASN I CB  
16240 C CG  . ASN I  135 ? 1.3295 1.3836 1.3923 0.1930  0.1204  0.1872  135 ASN I CG  
16241 O OD1 . ASN I  135 ? 1.1088 1.1646 1.1732 0.1920  0.1180  0.1843  135 ASN I OD1 
16242 N ND2 . ASN I  135 ? 1.2502 1.3029 1.3178 0.1979  0.1260  0.1940  135 ASN I ND2 
16243 N N   . LYS I  136 ? 1.0708 1.1107 1.1191 0.1784  0.1139  0.1679  136 LYS I N   
16244 C CA  . LYS I  136 ? 1.2354 1.2757 1.2767 0.1745  0.1114  0.1648  136 LYS I CA  
16245 C C   . LYS I  136 ? 1.2791 1.3146 1.3200 0.1693  0.1078  0.1560  136 LYS I C   
16246 O O   . LYS I  136 ? 1.2157 1.2505 1.2517 0.1658  0.1058  0.1525  136 LYS I O   
16247 C CB  . LYS I  136 ? 1.3681 1.4026 1.4106 0.1761  0.1163  0.1672  136 LYS I CB  
16248 C CG  . LYS I  136 ? 1.4315 1.4704 1.4742 0.1812  0.1201  0.1763  136 LYS I CG  
16249 C CD  . LYS I  136 ? 1.4770 1.5186 1.5128 0.1807  0.1205  0.1790  136 LYS I CD  
16250 C CE  . LYS I  136 ? 1.7313 1.7818 1.7643 0.1849  0.1216  0.1881  136 LYS I CE  
16251 N NZ  . LYS I  136 ? 1.7744 1.8352 1.8047 0.1850  0.1169  0.1899  136 LYS I NZ  
16252 N N   . GLY I  137 ? 1.1573 1.1896 1.2033 0.1688  0.1071  0.1525  137 GLY I N   
16253 C CA  . GLY I  137 ? 1.0235 1.0511 1.0700 0.1640  0.1040  0.1445  137 GLY I CA  
16254 C C   . GLY I  137 ? 1.0302 1.0648 1.0702 0.1606  0.0976  0.1413  137 GLY I C   
16255 O O   . GLY I  137 ? 0.9666 1.0020 1.0082 0.1594  0.0952  0.1384  137 GLY I O   
16256 N N   . VAL I  138 ? 0.9731 1.0129 1.0056 0.1588  0.0952  0.1418  138 VAL I N   
16257 C CA  . VAL I  138 ? 0.8933 0.9396 0.9192 0.1551  0.0894  0.1385  138 VAL I CA  
16258 C C   . VAL I  138 ? 0.9389 0.9826 0.9603 0.1508  0.0877  0.1338  138 VAL I C   
16259 O O   . VAL I  138 ? 1.0858 1.1235 1.1087 0.1510  0.0910  0.1338  138 VAL I O   
16260 C CB  . VAL I  138 ? 0.9526 1.0102 0.9725 0.1569  0.0874  0.1440  138 VAL I CB  
16261 C CG1 . VAL I  138 ? 1.1175 1.1781 1.1426 0.1614  0.0893  0.1491  138 VAL I CG1 
16262 C CG2 . VAL I  138 ? 1.0793 1.1396 1.0943 0.1579  0.0893  0.1484  138 VAL I CG2 
16263 N N   . THR I  139 ? 0.7416 0.7896 0.7577 0.1470  0.0827  0.1298  139 THR I N   
16264 C CA  . THR I  139 ? 1.0349 1.0803 1.0471 0.1427  0.0810  0.1249  139 THR I CA  
16265 C C   . THR I  139 ? 1.1063 1.1594 1.1109 0.1393  0.0759  0.1227  139 THR I C   
16266 O O   . THR I  139 ? 1.0318 1.0903 1.0355 0.1394  0.0728  0.1228  139 THR I O   
16267 C CB  . THR I  139 ? 1.0816 1.1176 1.0999 0.1403  0.0812  0.1189  139 THR I CB  
16268 O OG1 . THR I  139 ? 0.8765 0.9109 0.8910 0.1359  0.0790  0.1142  139 THR I OG1 
16269 C CG2 . THR I  139 ? 0.9989 1.0351 1.0205 0.1396  0.0784  0.1162  139 THR I CG2 
16270 N N   . ALA I  140 ? 1.2043 1.2575 1.2034 0.1362  0.0751  0.1205  140 ALA I N   
16271 C CA  . ALA I  140 ? 1.1665 1.2260 1.1583 0.1324  0.0706  0.1177  140 ALA I CA  
16272 C C   . ALA I  140 ? 1.2015 1.2579 1.1957 0.1292  0.0672  0.1114  140 ALA I C   
16273 O O   . ALA I  140 ? 1.2062 1.2677 1.1956 0.1262  0.0632  0.1087  140 ALA I O   
16274 C CB  . ALA I  140 ? 1.2278 1.2873 1.2135 0.1298  0.0714  0.1167  140 ALA I CB  
16275 N N   . ALA I  141 ? 1.1556 1.2037 1.1575 0.1297  0.0689  0.1091  141 ALA I N   
16276 C CA  . ALA I  141 ? 1.1663 1.2106 1.1712 0.1266  0.0659  0.1033  141 ALA I CA  
16277 C C   . ALA I  141 ? 1.0913 1.1396 1.0973 0.1275  0.0634  0.1036  141 ALA I C   
16278 O O   . ALA I  141 ? 1.0098 1.0589 1.0150 0.1246  0.0597  0.0994  141 ALA I O   
16279 C CB  . ALA I  141 ? 1.0790 1.1133 1.0914 0.1266  0.0687  0.1009  141 ALA I CB  
16280 N N   . CYS I  142 ? 0.9942 1.0451 1.0024 0.1317  0.0656  0.1087  142 CYS I N   
16281 C CA  . CYS I  142 ? 0.9052 0.9608 0.9142 0.1329  0.0635  0.1096  142 CYS I CA  
16282 C C   . CYS I  142 ? 1.0571 1.1233 1.0604 0.1346  0.0623  0.1145  142 CYS I C   
16283 O O   . CYS I  142 ? 1.0994 1.1687 1.1047 0.1386  0.0644  0.1199  142 CYS I O   
16284 C CB  . CYS I  142 ? 1.1220 1.1723 1.1390 0.1361  0.0668  0.1111  142 CYS I CB  
16285 S SG  . CYS I  142 ? 1.2200 1.2586 1.2439 0.1337  0.0679  0.1051  142 CYS I SG  
16286 N N   . PRO I  143 ? 1.0705 1.1423 1.0665 0.1313  0.0587  0.1125  143 PRO I N   
16287 C CA  . PRO I  143 ? 1.1746 1.2570 1.1637 0.1317  0.0569  0.1163  143 PRO I CA  
16288 C C   . PRO I  143 ? 1.2358 1.3256 1.2248 0.1326  0.0540  0.1178  143 PRO I C   
16289 O O   . PRO I  143 ? 1.3191 1.4066 1.3105 0.1310  0.0519  0.1137  143 PRO I O   
16290 C CB  . PRO I  143 ? 1.1502 1.2339 1.1325 0.1268  0.0540  0.1119  143 PRO I CB  
16291 C CG  . PRO I  143 ? 1.0931 1.1682 1.0792 0.1239  0.0534  0.1056  143 PRO I CG  
16292 C CD  . PRO I  143 ? 1.0841 1.1524 1.0787 0.1266  0.0557  0.1058  143 PRO I CD  
16293 N N   . HIS I  144 ? 1.3931 1.4917 1.3791 0.1351  0.0540  0.1236  144 HIS I N   
16294 C CA  . HIS I  144 ? 1.4435 1.5501 1.4295 0.1364  0.0515  0.1258  144 HIS I CA  
16295 C C   . HIS I  144 ? 1.6675 1.7855 1.6469 0.1369  0.0499  0.1307  144 HIS I C   
16296 O O   . HIS I  144 ? 1.6185 1.7397 1.5989 0.1407  0.0525  0.1372  144 HIS I O   
16297 C CB  . HIS I  144 ? 1.3130 1.4169 1.3071 0.1410  0.0547  0.1294  144 HIS I CB  
16298 C CG  . HIS I  144 ? 1.4177 1.5262 1.4139 0.1416  0.0524  0.1294  144 HIS I CG  
16299 N ND1 . HIS I  144 ? 1.5435 1.6553 1.5445 0.1462  0.0545  0.1349  144 HIS I ND1 
16300 C CD2 . HIS I  144 ? 1.5120 1.6221 1.5063 0.1383  0.0484  0.1245  144 HIS I CD2 
16301 C CE1 . HIS I  144 ? 1.5694 1.6846 1.5714 0.1456  0.0520  0.1334  144 HIS I CE1 
16302 N NE2 . HIS I  144 ? 1.5552 1.6696 1.5531 0.1408  0.0482  0.1271  144 HIS I NE2 
16303 N N   . ALA I  145 ? 1.4881 1.6123 1.4610 0.1330  0.0457  0.1278  145 ALA I N   
16304 C CA  . ALA I  145 ? 1.4937 1.6292 1.4595 0.1325  0.0437  0.1317  145 ALA I CA  
16305 C C   . ALA I  145 ? 1.5773 1.7122 1.5386 0.1323  0.0460  0.1340  145 ALA I C   
16306 O O   . ALA I  145 ? 1.5260 1.6697 1.4823 0.1330  0.0454  0.1388  145 ALA I O   
16307 C CB  . ALA I  145 ? 1.3507 1.4943 1.3194 0.1368  0.0437  0.1385  145 ALA I CB  
16308 N N   . GLY I  146 ? 1.8132 1.9380 1.7764 0.1312  0.0486  0.1304  146 GLY I N   
16309 C CA  . GLY I  146 ? 1.7557 1.8785 1.7149 0.1308  0.0511  0.1318  146 GLY I CA  
16310 C C   . GLY I  146 ? 1.7939 1.9097 1.7594 0.1350  0.0562  0.1355  146 GLY I C   
16311 O O   . GLY I  146 ? 1.8764 1.9845 1.8422 0.1340  0.0588  0.1334  146 GLY I O   
16312 N N   . ALA I  147 ? 1.5216 1.6400 1.4923 0.1397  0.0576  0.1410  147 ALA I N   
16313 C CA  . ALA I  147 ? 1.6495 1.7619 1.6264 0.1441  0.0626  0.1451  147 ALA I CA  
16314 C C   . ALA I  147 ? 1.4954 1.5954 1.4791 0.1437  0.0649  0.1401  147 ALA I C   
16315 O O   . ALA I  147 ? 1.3367 1.4338 1.3227 0.1415  0.0626  0.1349  147 ALA I O   
16316 C CB  . ALA I  147 ? 1.5797 1.6975 1.5611 0.1491  0.0637  0.1518  147 ALA I CB  
16317 N N   . LYS I  148 ? 1.3757 1.4687 1.3625 0.1456  0.0694  0.1417  148 LYS I N   
16318 C CA  . LYS I  148 ? 1.1677 1.2492 1.1614 0.1454  0.0720  0.1376  148 LYS I CA  
16319 C C   . LYS I  148 ? 1.1974 1.2763 1.1994 0.1491  0.0738  0.1394  148 LYS I C   
16320 O O   . LYS I  148 ? 1.1926 1.2728 1.1978 0.1536  0.0772  0.1456  148 LYS I O   
16321 C CB  . LYS I  148 ? 1.1890 1.2641 1.1835 0.1463  0.0764  0.1389  148 LYS I CB  
16322 C CG  . LYS I  148 ? 1.3419 1.4183 1.3286 0.1426  0.0754  0.1368  148 LYS I CG  
16323 C CD  . LYS I  148 ? 1.3303 1.3994 1.3187 0.1436  0.0801  0.1378  148 LYS I CD  
16324 C CE  . LYS I  148 ? 1.3386 1.4096 1.3291 0.1487  0.0840  0.1455  148 LYS I CE  
16325 N NZ  . LYS I  148 ? 1.2685 1.3318 1.2611 0.1498  0.0890  0.1465  148 LYS I NZ  
16326 N N   . SER I  149 ? 1.1990 1.2741 1.2044 0.1471  0.0719  0.1342  149 SER I N   
16327 C CA  . SER I  149 ? 1.2132 1.2855 1.2260 0.1500  0.0736  0.1352  149 SER I CA  
16328 C C   . SER I  149 ? 1.1412 1.2022 1.1603 0.1488  0.0756  0.1301  149 SER I C   
16329 O O   . SER I  149 ? 1.0320 1.0870 1.0511 0.1471  0.0769  0.1277  149 SER I O   
16330 C CB  . SER I  149 ? 1.0793 1.1584 1.0908 0.1492  0.0695  0.1342  149 SER I CB  
16331 O OG  . SER I  149 ? 1.1705 1.2485 1.1887 0.1526  0.0717  0.1367  149 SER I OG  
16332 N N   . PHE I  150 ? 1.1454 1.2038 1.1699 0.1495  0.0757  0.1286  150 PHE I N   
16333 C CA  . PHE I  150 ? 0.9005 0.9488 0.9311 0.1482  0.0774  0.1239  150 PHE I CA  
16334 C C   . PHE I  150 ? 0.8645 0.9124 0.8984 0.1477  0.0759  0.1213  150 PHE I C   
16335 O O   . PHE I  150 ? 1.0757 1.1310 1.1076 0.1487  0.0738  0.1235  150 PHE I O   
16336 C CB  . PHE I  150 ? 0.8007 0.8426 0.8373 0.1517  0.0834  0.1273  150 PHE I CB  
16337 C CG  . PHE I  150 ? 0.7886 0.8200 0.8308 0.1498  0.0853  0.1224  150 PHE I CG  
16338 C CD1 . PHE I  150 ? 0.7069 0.7343 0.7473 0.1461  0.0837  0.1178  150 PHE I CD1 
16339 C CD2 . PHE I  150 ? 0.8243 0.8498 0.8737 0.1517  0.0888  0.1224  150 PHE I CD2 
16340 C CE1 . PHE I  150 ? 0.4576 0.4759 0.5034 0.1443  0.0852  0.1136  150 PHE I CE1 
16341 C CE2 . PHE I  150 ? 0.7640 0.7803 0.8184 0.1496  0.0903  0.1178  150 PHE I CE2 
16342 C CZ  . PHE I  150 ? 0.5928 0.6057 0.6455 0.1459  0.0884  0.1135  150 PHE I CZ  
16343 N N   . TYR I  151 ? 0.8476 0.8869 0.8865 0.1460  0.0770  0.1167  151 TYR I N   
16344 C CA  . TYR I  151 ? 0.7103 0.7482 0.7526 0.1453  0.0761  0.1141  151 TYR I CA  
16345 C C   . TYR I  151 ? 0.7829 0.8227 0.8294 0.1501  0.0799  0.1195  151 TYR I C   
16346 O O   . TYR I  151 ? 0.9642 1.0014 1.0144 0.1536  0.0846  0.1237  151 TYR I O   
16347 C CB  . TYR I  151 ? 0.8458 0.8738 0.8929 0.1427  0.0771  0.1086  151 TYR I CB  
16348 C CG  . TYR I  151 ? 0.6981 0.7235 0.7422 0.1383  0.0739  0.1036  151 TYR I CG  
16349 C CD1 . TYR I  151 ? 0.6465 0.6748 0.6865 0.1344  0.0686  0.0993  151 TYR I CD1 
16350 C CD2 . TYR I  151 ? 0.6998 0.7198 0.7457 0.1380  0.0762  0.1034  151 TYR I CD2 
16351 C CE1 . TYR I  151 ? 0.7144 0.7403 0.7523 0.1305  0.0659  0.0950  151 TYR I CE1 
16352 C CE2 . TYR I  151 ? 0.6220 0.6396 0.6658 0.1341  0.0735  0.0990  151 TYR I CE2 
16353 C CZ  . TYR I  151 ? 0.6977 0.7184 0.7377 0.1304  0.0684  0.0949  151 TYR I CZ  
16354 O OH  . TYR I  151 ? 0.6609 0.6791 0.6993 0.1266  0.0660  0.0908  151 TYR I OH  
16355 N N   . LYS I  152 ? 0.7306 0.7750 0.7768 0.1503  0.0779  0.1195  152 LYS I N   
16356 C CA  . LYS I  152 ? 0.8774 0.9241 0.9279 0.1548  0.0815  0.1246  152 LYS I CA  
16357 C C   . LYS I  152 ? 0.8348 0.8720 0.8930 0.1558  0.0863  0.1232  152 LYS I C   
16358 O O   . LYS I  152 ? 1.0424 1.0783 1.1055 0.1601  0.0914  0.1280  152 LYS I O   
16359 C CB  . LYS I  152 ? 0.8650 0.9191 0.9134 0.1544  0.0780  0.1246  152 LYS I CB  
16360 C CG  . LYS I  152 ? 1.1753 1.2394 1.2162 0.1533  0.0733  0.1261  152 LYS I CG  
16361 C CD  . LYS I  152 ? 1.5557 1.6256 1.5954 0.1573  0.0754  0.1335  152 LYS I CD  
16362 C CE  . LYS I  152 ? 1.6448 1.7250 1.6767 0.1558  0.0706  0.1349  152 LYS I CE  
16363 N NZ  . LYS I  152 ? 1.6229 1.7092 1.6532 0.1593  0.0724  0.1421  152 LYS I NZ  
16364 N N   . ASN I  153 ? 0.6910 0.7218 0.7502 0.1518  0.0848  0.1165  153 ASN I N   
16365 C CA  . ASN I  153 ? 0.7379 0.7599 0.8037 0.1518  0.0889  0.1142  153 ASN I CA  
16366 C C   . ASN I  153 ? 0.7240 0.7380 0.7938 0.1522  0.0929  0.1139  153 ASN I C   
16367 O O   . ASN I  153 ? 0.7262 0.7325 0.8016 0.1520  0.0966  0.1118  153 ASN I O   
16368 C CB  . ASN I  153 ? 0.6791 0.6983 0.7443 0.1472  0.0855  0.1073  153 ASN I CB  
16369 C CG  . ASN I  153 ? 0.8247 0.8508 0.8872 0.1473  0.0825  0.1077  153 ASN I CG  
16370 O OD1 . ASN I  153 ? 1.0468 1.0788 1.1101 0.1512  0.0842  0.1132  153 ASN I OD1 
16371 N ND2 . ASN I  153 ? 0.8134 0.8392 0.8731 0.1429  0.0782  0.1020  153 ASN I ND2 
16372 N N   . LEU I  154 ? 0.7286 0.7444 0.7955 0.1527  0.0925  0.1161  154 LEU I N   
16373 C CA  . LEU I  154 ? 0.8797 0.8885 0.9502 0.1533  0.0965  0.1164  154 LEU I CA  
16374 C C   . LEU I  154 ? 0.8091 0.8218 0.8782 0.1574  0.0990  0.1232  154 LEU I C   
16375 O O   . LEU I  154 ? 0.8011 0.8223 0.8647 0.1583  0.0962  0.1263  154 LEU I O   
16376 C CB  . LEU I  154 ? 0.8522 0.8571 0.9205 0.1485  0.0932  0.1106  154 LEU I CB  
16377 C CG  . LEU I  154 ? 0.6070 0.6075 0.6766 0.1441  0.0904  0.1039  154 LEU I CG  
16378 C CD1 . LEU I  154 ? 0.7309 0.7297 0.7978 0.1396  0.0865  0.0991  154 LEU I CD1 
16379 C CD2 . LEU I  154 ? 0.7402 0.7324 0.8170 0.1446  0.0952  0.1025  154 LEU I CD2 
16380 N N   . ILE I  155 ? 0.8548 0.8614 0.9288 0.1597  0.1044  0.1254  155 ILE I N   
16381 C CA  . ILE I  155 ? 1.0527 1.0621 1.1256 0.1634  0.1072  0.1317  155 ILE I CA  
16382 C C   . ILE I  155 ? 0.8680 0.8713 0.9413 0.1619  0.1087  0.1299  155 ILE I C   
16383 O O   . ILE I  155 ? 0.7889 0.7837 0.8680 0.1612  0.1121  0.1273  155 ILE I O   
16384 C CB  . ILE I  155 ? 1.0751 1.0836 1.1538 0.1687  0.1133  0.1377  155 ILE I CB  
16385 C CG1 . ILE I  155 ? 1.0492 1.0643 1.1277 0.1706  0.1120  0.1403  155 ILE I CG1 
16386 C CG2 . ILE I  155 ? 0.8315 0.8424 0.9091 0.1724  0.1162  0.1443  155 ILE I CG2 
16387 C CD1 . ILE I  155 ? 1.1453 1.1597 1.2301 0.1759  0.1181  0.1464  155 ILE I CD1 
16388 N N   . TRP I  156 ? 0.6415 0.6493 0.7088 0.1611  0.1063  0.1312  156 TRP I N   
16389 C CA  . TRP I  156 ? 0.7117 0.7144 0.7791 0.1598  0.1078  0.1297  156 TRP I CA  
16390 C C   . TRP I  156 ? 0.8762 0.8770 0.9463 0.1643  0.1137  0.1359  156 TRP I C   
16391 O O   . TRP I  156 ? 0.9931 0.9997 1.0586 0.1663  0.1137  0.1408  156 TRP I O   
16392 C CB  . TRP I  156 ? 0.6866 0.6944 0.7462 0.1568  0.1030  0.1281  156 TRP I CB  
16393 C CG  . TRP I  156 ? 0.7953 0.7973 0.8551 0.1546  0.1040  0.1255  156 TRP I CG  
16394 C CD1 . TRP I  156 ? 0.8852 0.8787 0.9512 0.1552  0.1086  0.1249  156 TRP I CD1 
16395 C CD2 . TRP I  156 ? 0.7381 0.7424 0.7918 0.1514  0.1007  0.1232  156 TRP I CD2 
16396 N NE1 . TRP I  156 ? 0.8477 0.8383 0.9122 0.1527  0.1081  0.1224  156 TRP I NE1 
16397 C CE2 . TRP I  156 ? 0.7690 0.7659 0.8259 0.1503  0.1035  0.1213  156 TRP I CE2 
16398 C CE3 . TRP I  156 ? 0.7802 0.7921 0.8263 0.1492  0.0958  0.1224  156 TRP I CE3 
16399 C CZ2 . TRP I  156 ? 0.8528 0.8494 0.9058 0.1473  0.1017  0.1188  156 TRP I CZ2 
16400 C CZ3 . TRP I  156 ? 0.8613 0.8727 0.9032 0.1461  0.0941  0.1197  156 TRP I CZ3 
16401 C CH2 . TRP I  156 ? 0.9628 0.9666 1.0083 0.1453  0.0971  0.1180  156 TRP I CH2 
16402 N N   . LEU I  157 ? 0.7180 0.7108 0.7956 0.1656  0.1187  0.1356  157 LEU I N   
16403 C CA  . LEU I  157 ? 0.7817 0.7719 0.8629 0.1700  0.1248  0.1413  157 LEU I CA  
16404 C C   . LEU I  157 ? 0.8747 0.8626 0.9536 0.1692  0.1258  0.1416  157 LEU I C   
16405 O O   . LEU I  157 ? 0.9845 0.9671 1.0641 0.1655  0.1246  0.1362  157 LEU I O   
16406 C CB  . LEU I  157 ? 0.7917 0.7732 0.8817 0.1712  0.1301  0.1403  157 LEU I CB  
16407 C CG  . LEU I  157 ? 0.8810 0.8639 0.9745 0.1733  0.1313  0.1416  157 LEU I CG  
16408 C CD1 . LEU I  157 ? 0.8405 0.8142 0.9426 0.1747  0.1376  0.1411  157 LEU I CD1 
16409 C CD2 . LEU I  157 ? 0.9065 0.8982 0.9973 0.1777  0.1316  0.1491  157 LEU I CD2 
16410 N N   . VAL I  158 ? 0.9570 0.9490 1.0332 0.1727  0.1281  0.1482  158 VAL I N   
16411 C CA  . VAL I  158 ? 0.9463 0.9360 1.0203 0.1725  0.1300  0.1492  158 VAL I CA  
16412 C C   . VAL I  158 ? 1.0221 1.0084 1.1006 0.1773  0.1368  0.1554  158 VAL I C   
16413 O O   . VAL I  158 ? 1.0260 1.0131 1.1086 0.1809  0.1397  0.1594  158 VAL I O   
16414 C CB  . VAL I  158 ? 0.8866 0.8849 0.9512 0.1715  0.1260  0.1512  158 VAL I CB  
16415 C CG1 . VAL I  158 ? 0.9438 0.9448 1.0038 0.1666  0.1196  0.1450  158 VAL I CG1 
16416 C CG2 . VAL I  158 ? 1.0843 1.0914 1.1461 0.1756  0.1262  0.1585  158 VAL I CG2 
16417 N N   . LYS I  159 ? 1.1615 1.1441 1.2395 0.1773  0.1395  0.1562  159 LYS I N   
16418 C CA  . LYS I  159 ? 1.3177 1.2963 1.4002 0.1815  0.1463  0.1617  159 LYS I CA  
16419 C C   . LYS I  159 ? 1.2872 1.2738 1.3666 0.1862  0.1475  0.1702  159 LYS I C   
16420 O O   . LYS I  159 ? 1.0324 1.0275 1.1039 0.1856  0.1434  0.1722  159 LYS I O   
16421 C CB  . LYS I  159 ? 1.2950 1.2683 1.3769 0.1802  0.1486  0.1606  159 LYS I CB  
16422 C CG  . LYS I  159 ? 1.1593 1.1391 1.2319 0.1792  0.1458  0.1626  159 LYS I CG  
16423 C CD  . LYS I  159 ? 1.3381 1.3119 1.4109 0.1784  0.1493  0.1620  159 LYS I CD  
16424 C CE  . LYS I  159 ? 1.3425 1.3226 1.4059 0.1776  0.1473  0.1646  159 LYS I CE  
16425 N NZ  . LYS I  159 ? 1.3322 1.3063 1.3957 0.1768  0.1510  0.1640  159 LYS I NZ  
16426 N N   . LYS I  160 ? 1.4202 1.4041 1.5058 0.1907  0.1531  0.1752  160 LYS I N   
16427 C CA  . LYS I  160 ? 1.5214 1.5129 1.6052 0.1955  0.1545  0.1839  160 LYS I CA  
16428 C C   . LYS I  160 ? 1.6037 1.5969 1.6832 0.1974  0.1569  0.1892  160 LYS I C   
16429 O O   . LYS I  160 ? 1.5586 1.5454 1.6427 0.1998  0.1628  0.1919  160 LYS I O   
16430 C CB  . LYS I  160 ? 1.3509 1.3393 1.4433 0.1999  0.1598  0.1876  160 LYS I CB  
16431 C CG  . LYS I  160 ? 1.4596 1.4426 1.5571 0.2042  0.1673  0.1932  160 LYS I CG  
16432 C CD  . LYS I  160 ? 1.5585 1.5450 1.6604 0.2099  0.1711  0.2012  160 LYS I CD  
16433 C CE  . LYS I  160 ? 1.5247 1.5226 1.6219 0.2106  0.1659  0.2040  160 LYS I CE  
16434 N NZ  . LYS I  160 ? 1.4748 1.4716 1.5771 0.2101  0.1651  0.2006  160 LYS I NZ  
16435 N N   . GLY I  161 ? 1.4704 1.4721 1.5407 0.1958  0.1523  0.1905  161 GLY I N   
16436 C CA  . GLY I  161 ? 1.4076 1.4115 1.4723 0.1968  0.1539  0.1950  161 GLY I CA  
16437 C C   . GLY I  161 ? 1.5725 1.5678 1.6375 0.1936  0.1556  0.1898  161 GLY I C   
16438 O O   . GLY I  161 ? 1.5850 1.5828 1.6428 0.1902  0.1525  0.1874  161 GLY I O   
16439 N N   . ASN I  162 ? 1.5484 1.5338 1.6220 0.1946  0.1607  0.1881  162 ASN I N   
16440 C CA  . ASN I  162 ? 1.5849 1.5614 1.6605 0.1921  0.1632  0.1837  162 ASN I CA  
16441 C C   . ASN I  162 ? 1.6080 1.5744 1.6935 0.1914  0.1663  0.1787  162 ASN I C   
16442 O O   . ASN I  162 ? 1.5997 1.5582 1.6885 0.1896  0.1689  0.1752  162 ASN I O   
16443 C CB  . ASN I  162 ? 1.8162 1.7914 1.8907 0.1953  0.1685  0.1899  162 ASN I CB  
16444 C CG  . ASN I  162 ? 1.9468 1.9160 2.0196 0.1921  0.1697  0.1859  162 ASN I CG  
16445 O OD1 . ASN I  162 ? 2.1688 2.1287 2.2485 0.1916  0.1735  0.1828  162 ASN I OD1 
16446 N ND2 . ASN I  162 ? 1.7785 1.7532 1.8421 0.1897  0.1663  0.1858  162 ASN I ND2 
16447 N N   . SER I  163 ? 1.5883 1.5550 1.6786 0.1926  0.1660  0.1783  163 SER I N   
16448 C CA  . SER I  163 ? 1.6687 1.6259 1.7683 0.1923  0.1698  0.1746  163 SER I CA  
16449 C C   . SER I  163 ? 1.4943 1.4507 1.5960 0.1888  0.1655  0.1677  163 SER I C   
16450 O O   . SER I  163 ? 1.3729 1.3367 1.4698 0.1877  0.1603  0.1672  163 SER I O   
16451 C CB  . SER I  163 ? 1.4771 1.4328 1.5826 0.1978  0.1760  0.1811  163 SER I CB  
16452 O OG  . SER I  163 ? 1.2422 1.1877 1.3565 0.1978  0.1813  0.1784  163 SER I OG  
16453 N N   . TYR I  164 ? 1.1716 1.1191 1.2803 0.1867  0.1677  0.1623  164 TYR I N   
16454 C CA  . TYR I  164 ? 1.0709 1.0171 1.1823 0.1835  0.1644  0.1561  164 TYR I CA  
16455 C C   . TYR I  164 ? 1.1297 1.0660 1.2504 0.1831  0.1694  0.1530  164 TYR I C   
16456 O O   . TYR I  164 ? 1.0512 0.9814 1.1746 0.1795  0.1691  0.1475  164 TYR I O   
16457 C CB  . TYR I  164 ? 1.2342 1.1820 1.3408 0.1781  0.1579  0.1497  164 TYR I CB  
16458 C CG  . TYR I  164 ? 1.1814 1.1309 1.2881 0.1751  0.1530  0.1445  164 TYR I CG  
16459 C CD1 . TYR I  164 ? 0.9850 0.9426 1.0844 0.1734  0.1467  0.1437  164 TYR I CD1 
16460 C CD2 . TYR I  164 ? 1.1225 1.0654 1.2361 0.1737  0.1549  0.1404  164 TYR I CD2 
16461 C CE1 . TYR I  164 ? 0.9311 0.8902 1.0304 0.1706  0.1424  0.1391  164 TYR I CE1 
16462 C CE2 . TYR I  164 ? 1.0071 0.9515 1.1204 0.1708  0.1505  0.1358  164 TYR I CE2 
16463 C CZ  . TYR I  164 ? 1.0116 0.9641 1.1178 0.1694  0.1443  0.1352  164 TYR I CZ  
16464 O OH  . TYR I  164 ? 0.9314 0.8854 1.0371 0.1665  0.1401  0.1307  164 TYR I OH  
16465 N N   . PRO I  165 ? 0.9534 0.8882 1.0792 0.1868  0.1739  0.1566  165 PRO I N   
16466 C CA  . PRO I  165 ? 1.0015 0.9271 1.1362 0.1867  0.1793  0.1540  165 PRO I CA  
16467 C C   . PRO I  165 ? 1.0349 0.9585 1.1714 0.1823  0.1757  0.1467  165 PRO I C   
16468 O O   . PRO I  165 ? 0.9785 0.9084 1.1104 0.1811  0.1704  0.1456  165 PRO I O   
16469 C CB  . PRO I  165 ? 1.0294 0.9559 1.1677 0.1923  0.1847  0.1609  165 PRO I CB  
16470 C CG  . PRO I  165 ? 1.2487 1.1849 1.3800 0.1956  0.1825  0.1679  165 PRO I CG  
16471 C CD  . PRO I  165 ? 0.9514 0.8935 1.0749 0.1914  0.1746  0.1638  165 PRO I CD  
16472 N N   . LYS I  166 ? 0.9180 0.8330 1.0610 0.1797  0.1785  0.1417  166 LYS I N   
16473 C CA  . LYS I  166 ? 1.0124 0.9250 1.1575 0.1755  0.1757  0.1350  166 LYS I CA  
16474 C C   . LYS I  166 ? 1.1916 1.1079 1.3366 0.1776  0.1757  0.1369  166 LYS I C   
16475 O O   . LYS I  166 ? 1.1249 1.0387 1.2745 0.1815  0.1818  0.1410  166 LYS I O   
16476 C CB  . LYS I  166 ? 0.8141 0.7167 0.9672 0.1734  0.1805  0.1308  166 LYS I CB  
16477 C CG  . LYS I  166 ? 1.0839 0.9836 1.2400 0.1700  0.1794  0.1251  166 LYS I CG  
16478 C CD  . LYS I  166 ? 1.1878 1.0777 1.3520 0.1684  0.1851  0.1216  166 LYS I CD  
16479 C CE  . LYS I  166 ? 1.3747 1.2609 1.5402 0.1637  0.1828  0.1164  166 LYS I CE  
16480 N NZ  . LYS I  166 ? 1.4481 1.3253 1.6214 0.1614  0.1876  0.1123  166 LYS I NZ  
16481 N N   . LEU I  167 ? 1.1738 1.0959 1.3137 0.1751  0.1692  0.1341  167 LEU I N   
16482 C CA  . LEU I  167 ? 1.0427 0.9681 1.1827 0.1765  0.1689  0.1352  167 LEU I CA  
16483 C C   . LEU I  167 ? 1.0061 0.9255 1.1504 0.1726  0.1692  0.1284  167 LEU I C   
16484 O O   . LEU I  167 ? 1.0129 0.9283 1.1577 0.1678  0.1668  0.1223  167 LEU I O   
16485 C CB  . LEU I  167 ? 0.7812 0.7167 0.9133 0.1763  0.1621  0.1364  167 LEU I CB  
16486 C CG  . LEU I  167 ? 0.9344 0.8729 1.0610 0.1709  0.1543  0.1302  167 LEU I CG  
16487 C CD1 . LEU I  167 ? 0.9815 0.9156 1.1109 0.1666  0.1527  0.1233  167 LEU I CD1 
16488 C CD2 . LEU I  167 ? 0.8744 0.8231 0.9936 0.1720  0.1491  0.1332  167 LEU I CD2 
16489 N N   . SER I  168 ? 0.9414 0.8602 1.0888 0.1745  0.1723  0.1296  168 SER I N   
16490 C CA  . SER I  168 ? 1.0458 0.9587 1.1971 0.1708  0.1732  0.1234  168 SER I CA  
16491 C C   . SER I  168 ? 1.0899 1.0058 1.2413 0.1724  0.1736  0.1246  168 SER I C   
16492 O O   . SER I  168 ? 1.3207 1.2330 1.4776 0.1755  0.1802  0.1273  168 SER I O   
16493 C CB  . SER I  168 ? 1.1554 1.0584 1.3145 0.1709  0.1806  0.1224  168 SER I CB  
16494 O OG  . SER I  168 ? 1.1994 1.0965 1.3612 0.1656  0.1801  0.1148  168 SER I OG  
16495 N N   . LYS I  169 ? 0.9205 0.8431 1.0659 0.1702  0.1668  0.1225  169 LYS I N   
16496 C CA  . LYS I  169 ? 0.9583 0.8842 1.1033 0.1711  0.1664  0.1229  169 LYS I CA  
16497 C C   . LYS I  169 ? 0.9456 0.8674 1.0909 0.1653  0.1640  0.1149  169 LYS I C   
16498 O O   . LYS I  169 ? 1.0825 1.0026 1.2256 0.1605  0.1597  0.1094  169 LYS I O   
16499 C CB  . LYS I  169 ? 0.8561 0.7927 0.9943 0.1726  0.1605  0.1264  169 LYS I CB  
16500 C CG  . LYS I  169 ? 1.1007 1.0425 1.2399 0.1790  0.1640  0.1349  169 LYS I CG  
16501 C CD  . LYS I  169 ? 1.1974 1.1380 1.3409 0.1805  0.1677  0.1352  169 LYS I CD  
16502 C CE  . LYS I  169 ? 1.1913 1.1392 1.3352 0.1865  0.1695  0.1437  169 LYS I CE  
16503 N NZ  . LYS I  169 ? 1.3049 1.2518 1.4520 0.1914  0.1749  0.1506  169 LYS I NZ  
16504 N N   . SER I  170 ? 1.0139 0.9342 1.1618 0.1658  0.1668  0.1142  170 SER I N   
16505 C CA  . SER I  170 ? 1.0320 0.9488 1.1796 0.1604  0.1646  0.1068  170 SER I CA  
16506 C C   . SER I  170 ? 0.9519 0.8714 1.0995 0.1617  0.1654  0.1076  170 SER I C   
16507 O O   . SER I  170 ? 1.0318 0.9496 1.1842 0.1659  0.1719  0.1118  170 SER I O   
16508 C CB  . SER I  170 ? 0.9761 0.8827 1.1297 0.1576  0.1698  0.1023  170 SER I CB  
16509 O OG  . SER I  170 ? 1.3243 1.2261 1.4845 0.1619  0.1784  0.1064  170 SER I OG  
16510 N N   . TYR I  171 ? 0.8838 0.8076 1.0261 0.1581  0.1589  0.1036  171 TYR I N   
16511 C CA  . TYR I  171 ? 0.8850 0.8117 1.0266 0.1587  0.1589  0.1037  171 TYR I CA  
16512 C C   . TYR I  171 ? 0.8576 0.7779 1.0003 0.1534  0.1595  0.0962  171 TYR I C   
16513 O O   . TYR I  171 ? 0.8427 0.7599 0.9836 0.1481  0.1559  0.0903  171 TYR I O   
16514 C CB  . TYR I  171 ? 0.9274 0.8641 1.0619 0.1587  0.1514  0.1050  171 TYR I CB  
16515 C CG  . TYR I  171 ? 0.9395 0.8787 1.0719 0.1570  0.1493  0.1024  171 TYR I CG  
16516 C CD1 . TYR I  171 ? 0.8807 0.8238 1.0151 0.1614  0.1523  0.1073  171 TYR I CD1 
16517 C CD2 . TYR I  171 ? 0.8965 0.8343 1.0253 0.1509  0.1443  0.0951  171 TYR I CD2 
16518 C CE1 . TYR I  171 ? 0.9738 0.9191 1.1065 0.1598  0.1506  0.1049  171 TYR I CE1 
16519 C CE2 . TYR I  171 ? 0.9298 0.8698 1.0565 0.1492  0.1425  0.0927  171 TYR I CE2 
16520 C CZ  . TYR I  171 ? 0.9991 0.9427 1.1278 0.1537  0.1457  0.0975  171 TYR I CZ  
16521 O OH  . TYR I  171 ? 1.0602 1.0058 1.1871 0.1521  0.1441  0.0950  171 TYR I OH  
16522 N N   . ILE I  172 ? 0.8866 0.8050 1.0324 0.1548  0.1640  0.0966  172 ILE I N   
16523 C CA  . ILE I  172 ? 0.9747 0.8871 1.1213 0.1497  0.1651  0.0897  172 ILE I CA  
16524 C C   . ILE I  172 ? 1.0225 0.9401 1.1652 0.1489  0.1616  0.0886  172 ILE I C   
16525 O O   . ILE I  172 ? 0.8832 0.8058 1.0268 0.1537  0.1633  0.0940  172 ILE I O   
16526 C CB  . ILE I  172 ? 0.8661 0.7697 1.0203 0.1511  0.1746  0.0898  172 ILE I CB  
16527 C CG1 . ILE I  172 ? 1.0353 0.9322 1.1898 0.1452  0.1756  0.0820  172 ILE I CG1 
16528 C CG2 . ILE I  172 ? 1.0348 0.9411 1.1928 0.1576  0.1800  0.0968  172 ILE I CG2 
16529 C CD1 . ILE I  172 ? 1.1226 1.0102 1.2812 0.1417  0.1796  0.0776  172 ILE I CD1 
16530 N N   . ASN I  173 ? 0.9947 0.9114 1.1332 0.1428  0.1566  0.0817  173 ASN I N   
16531 C CA  . ASN I  173 ? 0.8589 0.7806 0.9930 0.1413  0.1524  0.0800  173 ASN I CA  
16532 C C   . ASN I  173 ? 1.0084 0.9267 1.1464 0.1425  0.1587  0.0800  173 ASN I C   
16533 O O   . ASN I  173 ? 0.9399 0.8512 1.0790 0.1383  0.1613  0.0742  173 ASN I O   
16534 C CB  . ASN I  173 ? 0.8963 0.8173 1.0250 0.1342  0.1456  0.0726  173 ASN I CB  
16535 C CG  . ASN I  173 ? 0.9705 0.8978 1.0936 0.1327  0.1401  0.0712  173 ASN I CG  
16536 O OD1 . ASN I  173 ? 0.9931 0.9253 1.1164 0.1367  0.1414  0.0755  173 ASN I OD1 
16537 N ND2 . ASN I  173 ? 0.9252 0.8526 1.0434 0.1268  0.1340  0.0653  173 ASN I ND2 
16538 N N   . ASP I  174 ? 1.1328 1.0561 1.2726 0.1483  0.1612  0.0865  174 ASP I N   
16539 C CA  . ASP I  174 ? 1.1476 1.0685 1.2917 0.1502  0.1675  0.0873  174 ASP I CA  
16540 C C   . ASP I  174 ? 1.1746 1.1003 1.3139 0.1480  0.1629  0.0848  174 ASP I C   
16541 O O   . ASP I  174 ? 1.3328 1.2568 1.4748 0.1489  0.1673  0.0848  174 ASP I O   
16542 C CB  . ASP I  174 ? 1.2390 1.1628 1.3886 0.1579  0.1731  0.0961  174 ASP I CB  
16543 C CG  . ASP I  174 ? 1.4097 1.3447 1.5554 0.1616  0.1673  0.1021  174 ASP I CG  
16544 O OD1 . ASP I  174 ? 1.4968 1.4381 1.6415 0.1637  0.1660  0.1047  174 ASP I OD1 
16545 O OD2 . ASP I  174 ? 1.3677 1.3050 1.5113 0.1623  0.1642  0.1041  174 ASP I OD2 
16546 N N   . LYS I  175 ? 1.1269 1.0585 1.2591 0.1450  0.1542  0.0826  175 LYS I N   
16547 C CA  . LYS I  175 ? 1.0033 0.9396 1.1305 0.1423  0.1492  0.0798  175 LYS I CA  
16548 C C   . LYS I  175 ? 1.0596 0.9886 1.1855 0.1359  0.1498  0.0717  175 LYS I C   
16549 O O   . LYS I  175 ? 1.1145 1.0354 1.2431 0.1332  0.1531  0.0681  175 LYS I O   
16550 C CB  . LYS I  175 ? 0.9364 0.8807 1.0565 0.1409  0.1400  0.0797  175 LYS I CB  
16551 C CG  . LYS I  175 ? 0.8931 0.8446 1.0134 0.1463  0.1387  0.0871  175 LYS I CG  
16552 C CD  . LYS I  175 ? 0.8259 0.7843 0.9477 0.1516  0.1404  0.0933  175 LYS I CD  
16553 C CE  . LYS I  175 ? 0.8050 0.7716 0.9257 0.1562  0.1381  0.1003  175 LYS I CE  
16554 N NZ  . LYS I  175 ? 1.1636 1.1380 1.2858 0.1612  0.1391  0.1066  175 LYS I NZ  
16555 N N   . GLY I  176 ? 0.8509 0.7827 0.9728 0.1334  0.1465  0.0688  176 GLY I N   
16556 C CA  . GLY I  176 ? 1.1349 1.0606 1.2545 0.1270  0.1463  0.0610  176 GLY I CA  
16557 C C   . GLY I  176 ? 1.1852 1.1141 1.2974 0.1216  0.1372  0.0564  176 GLY I C   
16558 O O   . GLY I  176 ? 1.2643 1.1909 1.3728 0.1163  0.1349  0.0506  176 GLY I O   
16559 N N   . LYS I  177 ? 1.1113 1.0454 1.2214 0.1231  0.1322  0.0593  177 LYS I N   
16560 C CA  . LYS I  177 ? 0.9635 0.9014 1.0672 0.1188  0.1236  0.0558  177 LYS I CA  
16561 C C   . LYS I  177 ? 0.8194 0.7577 0.9236 0.1195  0.1216  0.0576  177 LYS I C   
16562 O O   . LYS I  177 ? 0.8376 0.7757 0.9462 0.1243  0.1258  0.0627  177 LYS I O   
16563 C CB  . LYS I  177 ? 1.0107 0.9578 1.1096 0.1204  0.1184  0.0583  177 LYS I CB  
16564 C CG  . LYS I  177 ? 0.8645 0.8181 0.9657 0.1272  0.1199  0.0661  177 LYS I CG  
16565 C CD  . LYS I  177 ? 0.9560 0.9187 1.0530 0.1286  0.1153  0.0682  177 LYS I CD  
16566 C CE  . LYS I  177 ? 1.0724 1.0341 1.1706 0.1285  0.1186  0.0670  177 LYS I CE  
16567 N NZ  . LYS I  177 ? 1.0566 1.0153 1.1621 0.1334  0.1271  0.0713  177 LYS I NZ  
16568 N N   . GLU I  178 ? 0.7600 0.6988 0.8600 0.1148  0.1152  0.0536  178 GLU I N   
16569 C CA  . GLU I  178 ? 0.8200 0.7592 0.9206 0.1153  0.1131  0.0550  178 GLU I CA  
16570 C C   . GLU I  178 ? 0.8431 0.7898 0.9428 0.1207  0.1118  0.0615  178 GLU I C   
16571 O O   . GLU I  178 ? 0.8131 0.7663 0.9099 0.1227  0.1096  0.0639  178 GLU I O   
16572 C CB  . GLU I  178 ? 0.8696 0.8095 0.9656 0.1096  0.1059  0.0501  178 GLU I CB  
16573 C CG  . GLU I  178 ? 1.0894 1.0223 1.1857 0.1036  0.1063  0.0437  178 GLU I CG  
16574 C CD  . GLU I  178 ? 1.1839 1.1194 1.2747 0.0983  0.0985  0.0394  178 GLU I CD  
16575 O OE1 . GLU I  178 ? 1.0973 1.0393 1.1835 0.0989  0.0940  0.0404  178 GLU I OE1 
16576 O OE2 . GLU I  178 ? 1.2159 1.1472 1.3072 0.0936  0.0969  0.0352  178 GLU I OE2 
16577 N N   . VAL I  179 ? 0.6574 0.6033 0.7594 0.1228  0.1129  0.0643  179 VAL I N   
16578 C CA  . VAL I  179 ? 0.7360 0.6887 0.8368 0.1276  0.1116  0.0704  179 VAL I CA  
16579 C C   . VAL I  179 ? 0.6540 0.6085 0.7520 0.1256  0.1064  0.0695  179 VAL I C   
16580 O O   . VAL I  179 ? 0.5903 0.5393 0.6910 0.1241  0.1079  0.0679  179 VAL I O   
16581 C CB  . VAL I  179 ? 0.7860 0.7368 0.8927 0.1333  0.1188  0.0761  179 VAL I CB  
16582 C CG1 . VAL I  179 ? 0.6899 0.6472 0.7950 0.1374  0.1171  0.0820  179 VAL I CG1 
16583 C CG2 . VAL I  179 ? 0.6887 0.6395 0.7982 0.1362  0.1237  0.0783  179 VAL I CG2 
16584 N N   . LEU I  180 ? 0.5888 0.5508 0.6812 0.1256  0.1005  0.0705  180 LEU I N   
16585 C CA  . LEU I  180 ? 0.5953 0.5595 0.6848 0.1240  0.0957  0.0700  180 LEU I CA  
16586 C C   . LEU I  180 ? 0.5834 0.5497 0.6746 0.1288  0.0984  0.0759  180 LEU I C   
16587 O O   . LEU I  180 ? 0.6699 0.6425 0.7595 0.1328  0.0986  0.0808  180 LEU I O   
16588 C CB  . LEU I  180 ? 0.5756 0.5469 0.6585 0.1220  0.0888  0.0688  180 LEU I CB  
16589 C CG  . LEU I  180 ? 0.4910 0.4653 0.5706 0.1205  0.0839  0.0685  180 LEU I CG  
16590 C CD1 . LEU I  180 ? 0.5508 0.5194 0.6315 0.1155  0.0818  0.0632  180 LEU I CD1 
16591 C CD2 . LEU I  180 ? 0.4750 0.4572 0.5484 0.1199  0.0782  0.0687  180 LEU I CD2 
16592 N N   . VAL I  181 ? 0.5377 0.4989 0.6322 0.1284  0.1005  0.0754  181 VAL I N   
16593 C CA  . VAL I  181 ? 0.5706 0.5331 0.6665 0.1326  0.1031  0.0807  181 VAL I CA  
16594 C C   . VAL I  181 ? 0.6539 0.6184 0.7464 0.1305  0.0983  0.0797  181 VAL I C   
16595 O O   . VAL I  181 ? 0.5685 0.5288 0.6618 0.1263  0.0963  0.0751  181 VAL I O   
16596 C CB  . VAL I  181 ? 0.5837 0.5386 0.6864 0.1343  0.1101  0.0818  181 VAL I CB  
16597 C CG1 . VAL I  181 ? 0.6189 0.5757 0.7228 0.1392  0.1131  0.0879  181 VAL I CG1 
16598 C CG2 . VAL I  181 ? 0.6227 0.5744 0.7292 0.1357  0.1151  0.0819  181 VAL I CG2 
16599 N N   . LEU I  182 ? 0.6932 0.6644 0.7821 0.1333  0.0966  0.0839  182 LEU I N   
16600 C CA  . LEU I  182 ? 0.6045 0.5776 0.6901 0.1317  0.0928  0.0834  182 LEU I CA  
16601 C C   . LEU I  182 ? 0.5425 0.5152 0.6300 0.1355  0.0967  0.0882  182 LEU I C   
16602 O O   . LEU I  182 ? 0.6492 0.6241 0.7380 0.1401  0.1005  0.0935  182 LEU I O   
16603 C CB  . LEU I  182 ? 0.4930 0.4743 0.5718 0.1308  0.0870  0.0835  182 LEU I CB  
16604 C CG  . LEU I  182 ? 0.5634 0.5457 0.6395 0.1266  0.0823  0.0785  182 LEU I CG  
16605 C CD1 . LEU I  182 ? 0.7659 0.7536 0.8399 0.1286  0.0821  0.0805  182 LEU I CD1 
16606 C CD2 . LEU I  182 ? 0.6146 0.6001 0.6859 0.1231  0.0763  0.0758  182 LEU I CD2 
16607 N N   . TRP I  183 ? 0.6484 0.6183 0.7362 0.1336  0.0957  0.0866  183 TRP I N   
16608 C CA  . TRP I  183 ? 0.6975 0.6668 0.7865 0.1367  0.0990  0.0909  183 TRP I CA  
16609 C C   . TRP I  183 ? 0.6777 0.6477 0.7639 0.1341  0.0954  0.0890  183 TRP I C   
16610 O O   . TRP I  183 ? 0.5945 0.5643 0.6791 0.1298  0.0908  0.0842  183 TRP I O   
16611 C CB  . TRP I  183 ? 0.6620 0.6235 0.7582 0.1382  0.1054  0.0914  183 TRP I CB  
16612 C CG  . TRP I  183 ? 0.4990 0.4537 0.5988 0.1339  0.1048  0.0861  183 TRP I CG  
16613 C CD1 . TRP I  183 ? 0.5532 0.5047 0.6547 0.1326  0.1051  0.0852  183 TRP I CD1 
16614 C CD2 . TRP I  183 ? 0.5908 0.5412 0.6931 0.1300  0.1040  0.0808  183 TRP I CD2 
16615 N NE1 . TRP I  183 ? 0.5874 0.5333 0.6926 0.1284  0.1043  0.0800  183 TRP I NE1 
16616 C CE2 . TRP I  183 ? 0.6321 0.5772 0.7376 0.1266  0.1035  0.0772  183 TRP I CE2 
16617 C CE3 . TRP I  183 ? 0.6638 0.6143 0.7659 0.1291  0.1037  0.0789  183 TRP I CE3 
16618 C CZ2 . TRP I  183 ? 0.5682 0.5086 0.6765 0.1222  0.1025  0.0719  183 TRP I CZ2 
16619 C CZ3 . TRP I  183 ? 0.6310 0.5764 0.7354 0.1246  0.1029  0.0734  183 TRP I CZ3 
16620 C CH2 . TRP I  183 ? 0.5905 0.5312 0.6980 0.1212  0.1022  0.0700  183 TRP I CH2 
16621 N N   . GLY I  184 ? 0.7098 0.6806 0.7955 0.1367  0.0976  0.0928  184 GLY I N   
16622 C CA  . GLY I  184 ? 0.5730 0.5444 0.6561 0.1345  0.0948  0.0914  184 GLY I CA  
16623 C C   . GLY I  184 ? 0.6431 0.6091 0.7302 0.1357  0.0991  0.0928  184 GLY I C   
16624 O O   . GLY I  184 ? 0.7223 0.6865 0.8124 0.1395  0.1044  0.0969  184 GLY I O   
16625 N N   . ILE I  185 ? 0.6825 0.6460 0.7701 0.1324  0.0971  0.0896  185 ILE I N   
16626 C CA  . ILE I  185 ? 0.5558 0.5147 0.6468 0.1332  0.1008  0.0908  185 ILE I CA  
16627 C C   . ILE I  185 ? 0.6397 0.6025 0.7255 0.1328  0.0986  0.0918  185 ILE I C   
16628 O O   . ILE I  185 ? 0.6313 0.5954 0.7148 0.1293  0.0941  0.0882  185 ILE I O   
16629 C CB  . ILE I  185 ? 0.5898 0.5417 0.6870 0.1296  0.1008  0.0860  185 ILE I CB  
16630 C CG1 . ILE I  185 ? 0.5650 0.5131 0.6667 0.1291  0.1025  0.0841  185 ILE I CG1 
16631 C CG2 . ILE I  185 ? 0.5538 0.5007 0.6551 0.1308  0.1052  0.0875  185 ILE I CG2 
16632 C CD1 . ILE I  185 ? 0.5948 0.5405 0.6997 0.1335  0.1088  0.0883  185 ILE I CD1 
16633 N N   . HIS I  186 ? 0.7652 0.7299 0.8490 0.1365  0.1019  0.0968  186 HIS I N   
16634 C CA  . HIS I  186 ? 0.7005 0.6690 0.7786 0.1361  0.1003  0.0980  186 HIS I CA  
16635 C C   . HIS I  186 ? 0.6713 0.6343 0.7528 0.1348  0.1024  0.0967  186 HIS I C   
16636 O O   . HIS I  186 ? 0.7566 0.7142 0.8433 0.1367  0.1073  0.0983  186 HIS I O   
16637 C CB  . HIS I  186 ? 0.6970 0.6710 0.7705 0.1403  0.1024  0.1041  186 HIS I CB  
16638 C CG  . HIS I  186 ? 0.7224 0.7001 0.7898 0.1398  0.1014  0.1055  186 HIS I CG  
16639 N ND1 . HIS I  186 ? 0.8690 0.8450 0.9363 0.1421  0.1056  0.1090  186 HIS I ND1 
16640 C CD2 . HIS I  186 ? 0.6394 0.6222 0.7004 0.1372  0.0968  0.1036  186 HIS I CD2 
16641 C CE1 . HIS I  186 ? 0.8761 0.8560 0.9371 0.1407  0.1037  0.1092  186 HIS I CE1 
16642 N NE2 . HIS I  186 ? 0.5965 0.5806 0.6536 0.1377  0.0984  0.1059  186 HIS I NE2 
16643 N N   . HIS I  187 ? 0.7433 0.7075 0.8218 0.1316  0.0989  0.0938  187 HIS I N   
16644 C CA  . HIS I  187 ? 0.6270 0.5865 0.7083 0.1302  0.1007  0.0926  187 HIS I CA  
16645 C C   . HIS I  187 ? 0.8128 0.7763 0.8875 0.1308  0.1008  0.0949  187 HIS I C   
16646 O O   . HIS I  187 ? 0.7977 0.7649 0.8677 0.1281  0.0968  0.0927  187 HIS I O   
16647 C CB  . HIS I  187 ? 0.6122 0.5690 0.6968 0.1256  0.0970  0.0870  187 HIS I CB  
16648 C CG  . HIS I  187 ? 0.7166 0.6700 0.8068 0.1244  0.0962  0.0843  187 HIS I CG  
16649 N ND1 . HIS I  187 ? 0.7283 0.6751 0.8262 0.1243  0.0997  0.0834  187 HIS I ND1 
16650 C CD2 . HIS I  187 ? 0.7868 0.7426 0.8759 0.1229  0.0926  0.0821  187 HIS I CD2 
16651 C CE1 . HIS I  187 ? 0.8355 0.7807 0.9365 0.1227  0.0982  0.0807  187 HIS I CE1 
16652 N NE2 . HIS I  187 ? 0.7532 0.7037 0.8489 0.1218  0.0939  0.0799  187 HIS I NE2 
16653 N N   . PRO I  188 ? 0.7974 0.7600 0.8717 0.1341  0.1056  0.0993  188 PRO I N   
16654 C CA  . PRO I  188 ? 0.7659 0.7322 0.8336 0.1347  0.1063  0.1019  188 PRO I CA  
16655 C C   . PRO I  188 ? 0.8645 0.8284 0.9320 0.1312  0.1051  0.0983  188 PRO I C   
16656 O O   . PRO I  188 ? 0.7731 0.7314 0.8471 0.1290  0.1051  0.0948  188 PRO I O   
16657 C CB  . PRO I  188 ? 0.8232 0.7866 0.8932 0.1386  0.1123  0.1068  188 PRO I CB  
16658 C CG  . PRO I  188 ? 0.8660 0.8273 0.9414 0.1409  0.1141  0.1079  188 PRO I CG  
16659 C CD  . PRO I  188 ? 0.7377 0.6960 0.8177 0.1374  0.1107  0.1023  188 PRO I CD  
16660 N N   . SER I  189 ? 0.9601 0.9283 1.0204 0.1305  0.1043  0.0993  189 SER I N   
16661 C CA  . SER I  189 ? 0.8020 0.7682 0.8615 0.1272  0.1035  0.0960  189 SER I CA  
16662 C C   . SER I  189 ? 0.8996 0.8598 0.9629 0.1280  0.1086  0.0971  189 SER I C   
16663 O O   . SER I  189 ? 0.8735 0.8290 0.9412 0.1255  0.1089  0.0938  189 SER I O   
16664 C CB  . SER I  189 ? 0.8219 0.7948 0.8718 0.1258  0.1008  0.0962  189 SER I CB  
16665 O OG  . SER I  189 ? 1.0941 1.0709 1.1383 0.1287  0.1034  0.1012  189 SER I OG  
16666 N N   . THR I  190 ? 0.9800 0.9404 1.0416 0.1315  0.1129  0.1019  190 THR I N   
16667 C CA  . THR I  190 ? 0.9407 0.8957 1.0053 0.1325  0.1181  0.1034  190 THR I CA  
16668 C C   . THR I  190 ? 0.9788 0.9305 1.0482 0.1365  0.1227  0.1073  190 THR I C   
16669 O O   . THR I  190 ? 1.0026 0.9577 1.0709 0.1391  0.1224  0.1101  190 THR I O   
16670 C CB  . THR I  190 ? 0.9748 0.9331 1.0311 0.1326  0.1196  0.1057  190 THR I CB  
16671 O OG1 . THR I  190 ? 1.4034 1.3588 1.4606 0.1357  0.1253  0.1100  190 THR I OG1 
16672 N N   . SER I  191 ? 1.0963 1.0413 1.1714 0.1370  0.1273  0.1074  191 SER I N   
16673 C CA  . SER I  191 ? 1.1678 1.1088 1.2479 0.1406  0.1323  0.1109  191 SER I CA  
16674 C C   . SER I  191 ? 1.1453 1.0907 1.2189 0.1443  0.1349  0.1170  191 SER I C   
16675 O O   . SER I  191 ? 1.1469 1.0913 1.2234 0.1478  0.1381  0.1208  191 SER I O   
16676 C CB  . SER I  191 ? 1.0066 0.9397 1.0937 0.1400  0.1367  0.1097  191 SER I CB  
16677 O OG  . SER I  191 ? 1.1106 1.0437 1.1930 0.1395  0.1387  0.1107  191 SER I OG  
16678 N N   . ALA I  192 ? 1.0965 1.0469 1.1615 0.1434  0.1335  0.1181  192 ALA I N   
16679 C CA  . ALA I  192 ? 1.2379 1.1939 1.2958 0.1465  0.1351  0.1239  192 ALA I CA  
16680 C C   . ALA I  192 ? 1.3110 1.2737 1.3662 0.1481  0.1316  0.1258  192 ALA I C   
16681 O O   . ALA I  192 ? 1.1655 1.1308 1.2197 0.1519  0.1338  0.1312  192 ALA I O   
16682 C CB  . ALA I  192 ? 1.2328 1.1923 1.2819 0.1445  0.1345  0.1240  192 ALA I CB  
16683 N N   . ASP I  193 ? 1.2655 1.2310 1.3196 0.1451  0.1263  0.1216  193 ASP I N   
16684 C CA  . ASP I  193 ? 1.1226 1.0940 1.1748 0.1462  0.1227  0.1226  193 ASP I CA  
16685 C C   . ASP I  193 ? 1.0333 1.0008 1.0937 0.1487  0.1249  0.1235  193 ASP I C   
16686 O O   . ASP I  193 ? 0.9708 0.9424 1.0305 0.1514  0.1246  0.1268  193 ASP I O   
16687 C CB  . ASP I  193 ? 1.0262 1.0006 1.0761 0.1421  0.1168  0.1174  193 ASP I CB  
16688 C CG  . ASP I  193 ? 1.3566 1.3392 1.3965 0.1409  0.1135  0.1183  193 ASP I CG  
16689 O OD1 . ASP I  193 ? 1.4337 1.4176 1.4683 0.1410  0.1156  0.1206  193 ASP I OD1 
16690 O OD2 . ASP I  193 ? 1.6234 1.6112 1.6605 0.1395  0.1088  0.1166  193 ASP I OD2 
16691 N N   . GLN I  194 ? 1.0054 0.9648 1.0736 0.1477  0.1272  0.1205  194 GLN I N   
16692 C CA  . GLN I  194 ? 0.9968 0.9515 1.0731 0.1495  0.1297  0.1206  194 GLN I CA  
16693 C C   . GLN I  194 ? 1.1085 1.0629 1.1860 0.1544  0.1350  0.1270  194 GLN I C   
16694 O O   . GLN I  194 ? 1.1060 1.0625 1.1848 0.1570  0.1354  0.1295  194 GLN I O   
16695 C CB  . GLN I  194 ? 1.0533 0.9997 1.1377 0.1472  0.1312  0.1162  194 GLN I CB  
16696 C CG  . GLN I  194 ? 1.0192 0.9597 1.1121 0.1489  0.1349  0.1164  194 GLN I CG  
16697 C CD  . GLN I  194 ? 0.9404 0.8825 1.0351 0.1481  0.1317  0.1141  194 GLN I CD  
16698 O OE1 . GLN I  194 ? 1.0604 0.9990 1.1608 0.1499  0.1346  0.1148  194 GLN I OE1 
16699 N NE2 . GLN I  194 ? 0.7798 0.7270 0.8698 0.1454  0.1258  0.1113  194 GLN I NE2 
16700 N N   . GLN I  195 ? 1.7266 1.6782 1.8036 0.1558  0.1393  0.1296  195 GLN I N   
16701 C CA  . GLN I  195 ? 1.8848 1.8358 1.9628 0.1604  0.1447  0.1360  195 GLN I CA  
16702 C C   . GLN I  195 ? 1.7391 1.6992 1.8092 0.1630  0.1431  0.1414  195 GLN I C   
16703 O O   . GLN I  195 ? 1.6517 1.6131 1.7229 0.1672  0.1464  0.1470  195 GLN I O   
16704 C CB  . GLN I  195 ? 1.8082 1.7538 1.8875 0.1609  0.1496  0.1372  195 GLN I CB  
16705 C CG  . GLN I  195 ? 2.0917 2.0401 2.1636 0.1583  0.1478  0.1362  195 GLN I CG  
16706 C CD  . GLN I  195 ? 2.3909 2.3329 2.4651 0.1583  0.1527  0.1366  195 GLN I CD  
16707 O OE1 . GLN I  195 ? 2.3626 2.3056 2.4315 0.1563  0.1524  0.1357  195 GLN I OE1 
16708 N NE2 . GLN I  195 ? 2.4483 2.3835 2.5306 0.1605  0.1577  0.1376  195 GLN I NE2 
16709 N N   . SER I  196 ? 1.1012 1.0675 1.1635 0.1603  0.1383  0.1398  196 SER I N   
16710 C CA  . SER I  196 ? 1.0263 1.0021 1.0808 0.1620  0.1360  0.1444  196 SER I CA  
16711 C C   . SER I  196 ? 1.2686 1.2481 1.3254 0.1638  0.1339  0.1454  196 SER I C   
16712 O O   . SER I  196 ? 1.3784 1.3639 1.4325 0.1672  0.1344  0.1512  196 SER I O   
16713 C CB  . SER I  196 ? 0.9572 0.9384 1.0032 0.1581  0.1311  0.1414  196 SER I CB  
16714 O OG  . SER I  196 ? 1.1261 1.1170 1.1648 0.1593  0.1283  0.1453  196 SER I OG  
16715 N N   . LEU I  197 ? 1.1216 1.0975 1.1835 0.1615  0.1317  0.1400  197 LEU I N   
16716 C CA  . LEU I  197 ? 0.9456 0.9245 1.0094 0.1624  0.1294  0.1400  197 LEU I CA  
16717 C C   . LEU I  197 ? 1.0485 1.0215 1.1211 0.1655  0.1342  0.1416  197 LEU I C   
16718 O O   . LEU I  197 ? 1.0703 1.0467 1.1439 0.1687  0.1351  0.1455  197 LEU I O   
16719 C CB  . LEU I  197 ? 1.0896 1.0688 1.1531 0.1579  0.1239  0.1332  197 LEU I CB  
16720 C CG  . LEU I  197 ? 0.9934 0.9805 1.0481 0.1553  0.1183  0.1319  197 LEU I CG  
16721 C CD1 . LEU I  197 ? 0.9155 0.9008 0.9709 0.1506  0.1138  0.1248  197 LEU I CD1 
16722 C CD2 . LEU I  197 ? 0.8547 0.8503 0.9056 0.1578  0.1164  0.1362  197 LEU I CD2 
16723 N N   . TYR I  198 ? 1.0671 1.0314 1.1462 0.1645  0.1374  0.1386  198 TYR I N   
16724 C CA  . TYR I  198 ? 1.1322 1.0902 1.2198 0.1666  0.1418  0.1390  198 TYR I CA  
16725 C C   . TYR I  198 ? 1.1506 1.1017 1.2428 0.1687  0.1483  0.1414  198 TYR I C   
16726 O O   . TYR I  198 ? 1.2123 1.1572 1.3121 0.1702  0.1526  0.1415  198 TYR I O   
16727 C CB  . TYR I  198 ? 1.2861 1.2396 1.3785 0.1628  0.1392  0.1321  198 TYR I CB  
16728 C CG  . TYR I  198 ? 0.9660 0.9255 1.0531 0.1595  0.1324  0.1284  198 TYR I CG  
16729 C CD1 . TYR I  198 ? 0.8380 0.7972 0.9226 0.1551  0.1283  0.1234  198 TYR I CD1 
16730 C CD2 . TYR I  198 ? 0.9598 0.9251 1.0447 0.1609  0.1301  0.1302  198 TYR I CD2 
16731 C CE1 . TYR I  198 ? 0.9673 0.9317 1.0472 0.1522  0.1223  0.1202  198 TYR I CE1 
16732 C CE2 . TYR I  198 ? 0.9445 0.9152 1.0246 0.1580  0.1240  0.1269  198 TYR I CE2 
16733 C CZ  . TYR I  198 ? 0.9976 0.9678 1.0752 0.1536  0.1201  0.1219  198 TYR I CZ  
16734 O OH  . TYR I  198 ? 0.8432 0.8185 0.9161 0.1507  0.1142  0.1186  198 TYR I OH  
16735 N N   . GLN I  199 ? 1.1566 1.1087 1.2444 0.1686  0.1490  0.1432  199 GLN I N   
16736 C CA  . GLN I  199 ? 1.3379 1.2842 1.4289 0.1708  0.1552  0.1462  199 GLN I CA  
16737 C C   . GLN I  199 ? 1.3004 1.2376 1.3988 0.1681  0.1572  0.1410  199 GLN I C   
16738 O O   . GLN I  199 ? 1.3233 1.2577 1.4208 0.1664  0.1581  0.1395  199 GLN I O   
16739 C CB  . GLN I  199 ? 1.5158 1.4619 1.6104 0.1760  0.1603  0.1526  199 GLN I CB  
16740 C CG  . GLN I  199 ? 1.5762 1.5265 1.6655 0.1795  0.1630  0.1598  199 GLN I CG  
16741 C CD  . GLN I  199 ? 1.6107 1.5562 1.6994 0.1786  0.1660  0.1595  199 GLN I CD  
16742 O OE1 . GLN I  199 ? 1.6574 1.5946 1.7532 0.1783  0.1701  0.1573  199 GLN I OE1 
16743 N NE2 . GLN I  199 ? 1.4155 1.3663 1.4958 0.1780  0.1643  0.1616  199 GLN I NE2 
16744 N N   . ASN I  200 ? 1.4626 1.3952 1.5682 0.1676  0.1581  0.1381  200 ASN I N   
16745 C CA  . ASN I  200 ? 1.4319 1.3562 1.5449 0.1649  0.1599  0.1331  200 ASN I CA  
16746 C C   . ASN I  200 ? 1.4461 1.3708 1.5572 0.1599  0.1547  0.1272  200 ASN I C   
16747 O O   . ASN I  200 ? 1.4274 1.3578 1.5331 0.1579  0.1490  0.1253  200 ASN I O   
16748 C CB  . ASN I  200 ? 1.3886 1.3088 1.5087 0.1649  0.1612  0.1310  200 ASN I CB  
16749 C CG  . ASN I  200 ? 1.4197 1.3412 1.5410 0.1699  0.1654  0.1368  200 ASN I CG  
16750 O OD1 . ASN I  200 ? 1.5269 1.4512 1.6449 0.1736  0.1681  0.1429  200 ASN I OD1 
16751 N ND2 . ASN I  200 ? 1.3659 1.2853 1.4919 0.1699  0.1660  0.1351  200 ASN I ND2 
16752 N N   . ALA I  201 ? 1.2087 1.1272 1.3243 0.1579  0.1567  0.1244  201 ALA I N   
16753 C CA  . ALA I  201 ? 1.1485 1.0669 1.2632 0.1533  0.1523  0.1192  201 ALA I CA  
16754 C C   . ALA I  201 ? 1.3336 1.2488 1.4543 0.1498  0.1495  0.1133  201 ALA I C   
16755 O O   . ALA I  201 ? 1.2558 1.1739 1.3742 0.1464  0.1439  0.1094  201 ALA I O   
16756 C CB  . ALA I  201 ? 1.2525 1.1664 1.3689 0.1529  0.1558  0.1193  201 ALA I CB  
16757 N N   . ASP I  202 ? 1.3313 1.2405 1.4598 0.1505  0.1535  0.1128  202 ASP I N   
16758 C CA  . ASP I  202 ? 1.3446 1.2504 1.4791 0.1470  0.1513  0.1074  202 ASP I CA  
16759 C C   . ASP I  202 ? 1.2791 1.1859 1.4142 0.1485  0.1515  0.1081  202 ASP I C   
16760 O O   . ASP I  202 ? 1.2983 1.2009 1.4383 0.1509  0.1568  0.1101  202 ASP I O   
16761 C CB  . ASP I  202 ? 1.5068 1.4047 1.6499 0.1459  0.1556  0.1055  202 ASP I CB  
16762 C CG  . ASP I  202 ? 1.6050 1.5003 1.7535 0.1411  0.1521  0.0993  202 ASP I CG  
16763 O OD1 . ASP I  202 ? 1.5436 1.4426 1.6890 0.1379  0.1463  0.0963  202 ASP I OD1 
16764 O OD2 . ASP I  202 ? 1.6233 1.5130 1.7791 0.1404  0.1552  0.0976  202 ASP I OD2 
16765 N N   . THR I  203 ? 1.1676 1.0800 1.2980 0.1470  0.1460  0.1064  203 THR I N   
16766 C CA  . THR I  203 ? 0.9622 0.8764 1.0925 0.1484  0.1459  0.1071  203 THR I CA  
16767 C C   . THR I  203 ? 0.8229 0.7359 0.9557 0.1442  0.1418  0.1013  203 THR I C   
16768 O O   . THR I  203 ? 0.9837 0.8955 1.1179 0.1401  0.1384  0.0968  203 THR I O   
16769 C CB  . THR I  203 ? 0.9437 0.8661 1.0658 0.1508  0.1431  0.1109  203 THR I CB  
16770 O OG1 . THR I  203 ? 0.7578 0.6849 0.8745 0.1474  0.1366  0.1077  203 THR I OG1 
16771 C CG2 . THR I  203 ? 1.0826 1.0067 1.2015 0.1549  0.1470  0.1171  203 THR I CG2 
16772 N N   . TYR I  204 ? 0.8433 0.7568 0.9768 0.1451  0.1424  0.1014  204 TYR I N   
16773 C CA  . TYR I  204 ? 0.9598 0.8725 1.0951 0.1412  0.1387  0.0961  204 TYR I CA  
16774 C C   . TYR I  204 ? 0.9033 0.8197 1.0358 0.1428  0.1380  0.0974  204 TYR I C   
16775 O O   . TYR I  204 ? 0.7828 0.7004 0.9146 0.1473  0.1419  0.1024  204 TYR I O   
16776 C CB  . TYR I  204 ? 0.8213 0.7262 0.9649 0.1391  0.1422  0.0928  204 TYR I CB  
16777 C CG  . TYR I  204 ? 0.9234 0.8242 1.0713 0.1423  0.1487  0.0953  204 TYR I CG  
16778 C CD1 . TYR I  204 ? 0.9815 0.8816 1.1305 0.1414  0.1487  0.0933  204 TYR I CD1 
16779 C CD2 . TYR I  204 ? 0.9877 0.8851 1.1385 0.1461  0.1551  0.0997  204 TYR I CD2 
16780 C CE1 . TYR I  204 ? 1.1179 1.0140 1.2711 0.1443  0.1551  0.0956  204 TYR I CE1 
16781 C CE2 . TYR I  204 ? 1.0675 0.9610 1.2226 0.1491  0.1613  0.1022  204 TYR I CE2 
16782 C CZ  . TYR I  204 ? 1.1690 1.0617 1.3254 0.1482  0.1614  0.1001  204 TYR I CZ  
16783 O OH  . TYR I  204 ? 1.2147 1.1032 1.3756 0.1512  0.1680  0.1025  204 TYR I OH  
16784 N N   . VAL I  205 ? 0.8099 0.7282 0.9408 0.1392  0.1329  0.0930  205 VAL I N   
16785 C CA  . VAL I  205 ? 0.7337 0.6549 0.8626 0.1401  0.1321  0.0934  205 VAL I CA  
16786 C C   . VAL I  205 ? 0.7581 0.6747 0.8912 0.1362  0.1315  0.0879  205 VAL I C   
16787 O O   . VAL I  205 ? 0.8270 0.7419 0.9613 0.1317  0.1280  0.0832  205 VAL I O   
16788 C CB  . VAL I  205 ? 0.7225 0.6518 0.8436 0.1396  0.1259  0.0936  205 VAL I CB  
16789 C CG1 . VAL I  205 ? 0.7005 0.6329 0.8198 0.1409  0.1256  0.0944  205 VAL I CG1 
16790 C CG2 . VAL I  205 ? 0.7238 0.6578 0.8401 0.1426  0.1260  0.0983  205 VAL I CG2 
16791 N N   . PHE I  206 ? 0.7404 0.6550 0.8759 0.1378  0.1352  0.0886  206 PHE I N   
16792 C CA  . PHE I  206 ? 0.8174 0.7277 0.9563 0.1339  0.1349  0.0833  206 PHE I CA  
16793 C C   . PHE I  206 ? 0.8553 0.7683 0.9918 0.1346  0.1345  0.0834  206 PHE I C   
16794 O O   . PHE I  206 ? 0.8739 0.7874 1.0110 0.1390  0.1389  0.0878  206 PHE I O   
16795 C CB  . PHE I  206 ? 0.6571 0.5592 0.8036 0.1338  0.1414  0.0825  206 PHE I CB  
16796 C CG  . PHE I  206 ? 0.8432 0.7408 0.9931 0.1301  0.1422  0.0776  206 PHE I CG  
16797 C CD1 . PHE I  206 ? 0.8260 0.7214 0.9777 0.1323  0.1470  0.0788  206 PHE I CD1 
16798 C CD2 . PHE I  206 ? 0.9417 0.8374 1.0928 0.1244  0.1381  0.0717  206 PHE I CD2 
16799 C CE1 . PHE I  206 ? 0.8864 0.7774 1.0408 0.1286  0.1480  0.0739  206 PHE I CE1 
16800 C CE2 . PHE I  206 ? 0.9080 0.7997 1.0616 0.1206  0.1388  0.0670  206 PHE I CE2 
16801 C CZ  . PHE I  206 ? 1.0346 0.9238 1.1897 0.1226  0.1438  0.0680  206 PHE I CZ  
16802 N N   . VAL I  207 ? 0.7260 0.6407 0.8599 0.1302  0.1292  0.0786  207 VAL I N   
16803 C CA  . VAL I  207 ? 0.6389 0.5558 0.7705 0.1302  0.1284  0.0779  207 VAL I CA  
16804 C C   . VAL I  207 ? 0.8264 0.7378 0.9612 0.1255  0.1286  0.0720  207 VAL I C   
16805 O O   . VAL I  207 ? 0.9457 0.8562 1.0804 0.1206  0.1243  0.0674  207 VAL I O   
16806 C CB  . VAL I  207 ? 0.6628 0.5875 0.7872 0.1293  0.1214  0.0776  207 VAL I CB  
16807 C CG1 . VAL I  207 ? 0.6306 0.5574 0.7529 0.1293  0.1208  0.0769  207 VAL I CG1 
16808 C CG2 . VAL I  207 ? 0.6581 0.5884 0.7787 0.1334  0.1209  0.0831  207 VAL I CG2 
16809 N N   . GLY I  208 ? 0.8360 0.7439 0.9738 0.1269  0.1338  0.0724  208 GLY I N   
16810 C CA  . GLY I  208 ? 0.8631 0.7655 1.0038 0.1224  0.1349  0.0668  208 GLY I CA  
16811 C C   . GLY I  208 ? 0.8964 0.7983 1.0367 0.1231  0.1375  0.0665  208 GLY I C   
16812 O O   . GLY I  208 ? 0.8943 0.7975 1.0353 0.1282  0.1417  0.0713  208 GLY I O   
16813 N N   . SER I  209 ? 0.8288 0.7290 0.9680 0.1179  0.1349  0.0608  209 SER I N   
16814 C CA  . SER I  209 ? 0.7518 0.6501 0.8912 0.1176  0.1379  0.0593  209 SER I CA  
16815 C C   . SER I  209 ? 0.7959 0.6871 0.9386 0.1121  0.1397  0.0532  209 SER I C   
16816 O O   . SER I  209 ? 0.8865 0.7738 1.0329 0.1100  0.1406  0.0515  209 SER I O   
16817 C CB  . SER I  209 ? 0.8792 0.7841 1.0121 0.1166  0.1319  0.0585  209 SER I CB  
16818 O OG  . SER I  209 ? 0.8194 0.7250 0.9493 0.1106  0.1254  0.0531  209 SER I OG  
16819 N N   . SER I  210 ? 0.9504 0.8401 1.0919 0.1096  0.1404  0.0499  210 SER I N   
16820 C CA  . SER I  210 ? 1.0922 0.9754 1.2359 0.1038  0.1419  0.0437  210 SER I CA  
16821 C C   . SER I  210 ? 1.1150 1.0001 1.2561 0.0978  0.1343  0.0391  210 SER I C   
16822 O O   . SER I  210 ? 0.8942 0.7745 1.0381 0.0929  0.1347  0.0346  210 SER I O   
16823 C CB  . SER I  210 ? 1.1481 1.0295 1.2905 0.1024  0.1443  0.0412  210 SER I CB  
16824 O OG  . SER I  210 ? 1.3230 1.2013 1.4693 0.1074  0.1524  0.0450  210 SER I OG  
16825 N N   . ARG I  211 ? 1.0091 0.9012 1.1449 0.0982  0.1274  0.0404  211 ARG I N   
16826 C CA  . ARG I  211 ? 1.2293 1.1238 1.3623 0.0928  0.1198  0.0365  211 ARG I CA  
16827 C C   . ARG I  211 ? 1.1258 1.0244 1.2585 0.0947  0.1160  0.0395  211 ARG I C   
16828 O O   . ARG I  211 ? 1.3544 1.2526 1.4885 0.0910  0.1124  0.0370  211 ARG I O   
16829 C CB  . ARG I  211 ? 1.3349 1.2338 1.4616 0.0903  0.1145  0.0342  211 ARG I CB  
16830 C CG  . ARG I  211 ? 1.3990 1.3048 1.5213 0.0950  0.1122  0.0387  211 ARG I CG  
16831 C CD  . ARG I  211 ? 1.5568 1.4654 1.6740 0.0934  0.1096  0.0368  211 ARG I CD  
16832 N NE  . ARG I  211 ? 1.7658 1.6739 1.8805 0.0867  0.1046  0.0310  211 ARG I NE  
16833 C CZ  . ARG I  211 ? 1.6333 1.5447 1.7427 0.0844  0.1005  0.0288  211 ARG I CZ  
16834 N NH1 . ARG I  211 ? 1.4304 1.3458 1.5367 0.0882  0.1008  0.0318  211 ARG I NH1 
16835 N NH2 . ARG I  211 ? 1.5665 1.4772 1.6737 0.0781  0.0960  0.0238  211 ARG I NH2 
16836 N N   . TYR I  212 ? 1.0199 0.9227 1.1509 0.1004  0.1168  0.0449  212 TYR I N   
16837 C CA  . TYR I  212 ? 0.7876 0.6945 0.9175 0.1024  0.1135  0.0479  212 TYR I CA  
16838 C C   . TYR I  212 ? 0.8782 0.7810 1.0137 0.1053  0.1189  0.0508  212 TYR I C   
16839 O O   . TYR I  212 ? 0.9402 0.8391 1.0794 0.1083  0.1257  0.0528  212 TYR I O   
16840 C CB  . TYR I  212 ? 0.7451 0.6590 0.8698 0.1066  0.1114  0.0522  212 TYR I CB  
16841 C CG  . TYR I  212 ? 0.8587 0.7774 0.9808 0.1076  0.1069  0.0544  212 TYR I CG  
16842 C CD1 . TYR I  212 ? 0.8203 0.7438 0.9376 0.1045  0.0998  0.0521  212 TYR I CD1 
16843 C CD2 . TYR I  212 ? 0.8822 0.8007 1.0065 0.1117  0.1101  0.0587  212 TYR I CD2 
16844 C CE1 . TYR I  212 ? 0.7867 0.7143 0.9018 0.1053  0.0961  0.0540  212 TYR I CE1 
16845 C CE2 . TYR I  212 ? 0.8289 0.7516 0.9507 0.1124  0.1064  0.0605  212 TYR I CE2 
16846 C CZ  . TYR I  212 ? 0.7973 0.7244 0.9145 0.1091  0.0995  0.0580  212 TYR I CZ  
16847 O OH  . TYR I  212 ? 0.7025 0.6334 0.8172 0.1097  0.0961  0.0596  212 TYR I OH  
16848 N N   . SER I  213 ? 0.8247 0.7285 0.9611 0.1044  0.1160  0.0510  213 SER I N   
16849 C CA  . SER I  213 ? 0.8457 0.7458 0.9873 0.1070  0.1208  0.0536  213 SER I CA  
16850 C C   . SER I  213 ? 0.8503 0.7535 0.9910 0.1062  0.1162  0.0541  213 SER I C   
16851 O O   . SER I  213 ? 1.0469 0.9504 1.1878 0.1014  0.1113  0.0503  213 SER I O   
16852 C CB  . SER I  213 ? 0.7954 0.6880 0.9433 0.1041  0.1254  0.0502  213 SER I CB  
16853 O OG  . SER I  213 ? 0.6593 0.5481 0.8124 0.1068  0.1304  0.0529  213 SER I OG  
16854 N N   . LYS I  214 ? 0.7354 0.6409 0.8753 0.1108  0.1178  0.0590  214 LYS I N   
16855 C CA  . LYS I  214 ? 0.8103 0.7181 0.9496 0.1104  0.1145  0.0598  214 LYS I CA  
16856 C C   . LYS I  214 ? 0.9156 0.8238 1.0554 0.1158  0.1187  0.0653  214 LYS I C   
16857 O O   . LYS I  214 ? 0.7257 0.6362 0.8629 0.1201  0.1213  0.0693  214 LYS I O   
16858 C CB  . LYS I  214 ? 0.7356 0.6498 0.8688 0.1084  0.1071  0.0586  214 LYS I CB  
16859 C CG  . LYS I  214 ? 0.8836 0.7993 1.0171 0.1073  0.1038  0.0586  214 LYS I CG  
16860 C CD  . LYS I  214 ? 1.1325 1.0510 1.2639 0.1023  0.0968  0.0546  214 LYS I CD  
16861 C CE  . LYS I  214 ? 1.1544 1.0796 1.2789 0.1033  0.0922  0.0561  214 LYS I CE  
16862 N NZ  . LYS I  214 ? 1.1127 1.0395 1.2367 0.1054  0.0923  0.0589  214 LYS I NZ  
16863 N N   . LYS I  215 ? 0.9296 0.8355 1.0729 0.1153  0.1194  0.0654  215 LYS I N   
16864 C CA  . LYS I  215 ? 0.8348 0.7407 0.9784 0.1198  0.1233  0.0703  215 LYS I CA  
16865 C C   . LYS I  215 ? 0.7591 0.6700 0.8984 0.1195  0.1185  0.0712  215 LYS I C   
16866 O O   . LYS I  215 ? 0.9445 0.8554 1.0848 0.1155  0.1143  0.0678  215 LYS I O   
16867 C CB  . LYS I  215 ? 0.9325 0.8316 1.0835 0.1196  0.1284  0.0700  215 LYS I CB  
16868 C CG  . LYS I  215 ? 0.9162 0.8144 1.0681 0.1244  0.1334  0.0752  215 LYS I CG  
16869 C CD  . LYS I  215 ? 1.1621 1.0532 1.3218 0.1240  0.1388  0.0745  215 LYS I CD  
16870 C CE  . LYS I  215 ? 1.2034 1.0929 1.3641 0.1292  0.1448  0.0801  215 LYS I CE  
16871 N NZ  . LYS I  215 ? 1.0780 0.9601 1.2464 0.1291  0.1508  0.0795  215 LYS I NZ  
16872 N N   . PHE I  216 ? 0.7309 0.6461 0.8654 0.1236  0.1192  0.0758  216 PHE I N   
16873 C CA  . PHE I  216 ? 0.6467 0.5669 0.7762 0.1234  0.1150  0.0766  216 PHE I CA  
16874 C C   . PHE I  216 ? 0.7140 0.6328 0.8446 0.1260  0.1185  0.0801  216 PHE I C   
16875 O O   . PHE I  216 ? 0.8244 0.7417 0.9560 0.1301  0.1238  0.0842  216 PHE I O   
16876 C CB  . PHE I  216 ? 0.7577 0.6848 0.8798 0.1254  0.1122  0.0789  216 PHE I CB  
16877 C CG  . PHE I  216 ? 0.9063 0.8351 1.0267 0.1230  0.1088  0.0758  216 PHE I CG  
16878 C CD1 . PHE I  216 ? 0.8075 0.7348 0.9294 0.1248  0.1121  0.0766  216 PHE I CD1 
16879 C CD2 . PHE I  216 ? 0.7802 0.7119 0.8976 0.1189  0.1024  0.0720  216 PHE I CD2 
16880 C CE1 . PHE I  216 ? 0.7605 0.6891 0.8806 0.1225  0.1092  0.0736  216 PHE I CE1 
16881 C CE2 . PHE I  216 ? 0.8072 0.7405 0.9229 0.1166  0.0993  0.0691  216 PHE I CE2 
16882 C CZ  . PHE I  216 ? 0.7850 0.7166 0.9019 0.1184  0.1027  0.0699  216 PHE I CZ  
16883 N N   . LYS I  217 ? 0.8632 0.7824 0.9939 0.1236  0.1157  0.0784  217 LYS I N   
16884 C CA  . LYS I  217 ? 0.8073 0.7256 0.9382 0.1257  0.1185  0.0813  217 LYS I CA  
16885 C C   . LYS I  217 ? 0.8220 0.7465 0.9456 0.1259  0.1146  0.0825  217 LYS I C   
16886 O O   . LYS I  217 ? 0.9484 0.8750 1.0704 0.1224  0.1095  0.0792  217 LYS I O   
16887 C CB  . LYS I  217 ? 0.9546 0.8676 1.0924 0.1229  0.1194  0.0785  217 LYS I CB  
16888 C CG  . LYS I  217 ? 1.0621 0.9687 1.2066 0.1247  0.1259  0.0798  217 LYS I CG  
16889 C CD  . LYS I  217 ? 1.1659 1.0725 1.3084 0.1294  0.1309  0.0852  217 LYS I CD  
16890 C CE  . LYS I  217 ? 1.2512 1.1512 1.4006 0.1313  0.1377  0.0866  217 LYS I CE  
16891 N NZ  . LYS I  217 ? 1.3719 1.2719 1.5193 0.1359  0.1426  0.0920  217 LYS I NZ  
16892 N N   . PRO I  218 ? 0.8390 0.7663 0.9580 0.1298  0.1171  0.0872  218 PRO I N   
16893 C CA  . PRO I  218 ? 0.8785 0.8119 0.9900 0.1300  0.1140  0.0886  218 PRO I CA  
16894 C C   . PRO I  218 ? 0.8412 0.7732 0.9536 0.1272  0.1123  0.0862  218 PRO I C   
16895 O O   . PRO I  218 ? 0.8325 0.7598 0.9496 0.1276  0.1160  0.0868  218 PRO I O   
16896 C CB  . PRO I  218 ? 0.7783 0.7132 0.8868 0.1348  0.1185  0.0944  218 PRO I CB  
16897 C CG  . PRO I  218 ? 0.8890 0.8208 1.0019 0.1373  0.1227  0.0962  218 PRO I CG  
16898 C CD  . PRO I  218 ? 0.9374 0.8627 1.0580 0.1343  0.1232  0.0917  218 PRO I CD  
16899 N N   . GLU I  219 ? 0.9887 0.9248 1.0969 0.1244  0.1069  0.0837  219 GLU I N   
16900 C CA  . GLU I  219 ? 0.9107 0.8460 1.0197 0.1216  0.1051  0.0815  219 GLU I CA  
16901 C C   . GLU I  219 ? 0.8282 0.7677 0.9299 0.1230  0.1052  0.0841  219 GLU I C   
16902 O O   . GLU I  219 ? 0.7644 0.7093 0.8598 0.1219  0.1012  0.0835  219 GLU I O   
16903 C CB  . GLU I  219 ? 0.7909 0.7275 0.9005 0.1174  0.0993  0.0769  219 GLU I CB  
16904 C CG  . GLU I  219 ? 0.9250 0.8579 1.0411 0.1155  0.0988  0.0742  219 GLU I CG  
16905 C CD  . GLU I  219 ? 1.0695 1.0041 1.1859 0.1113  0.0929  0.0700  219 GLU I CD  
16906 O OE1 . GLU I  219 ? 1.0834 1.0220 1.1950 0.1099  0.0892  0.0692  219 GLU I OE1 
16907 O OE2 . GLU I  219 ? 0.9803 0.9121 1.1016 0.1091  0.0920  0.0674  219 GLU I OE2 
16908 N N   . ILE I  220 ? 0.9015 0.8384 1.0040 0.1251  0.1100  0.0869  220 ILE I N   
16909 C CA  . ILE I  220 ? 0.9426 0.8832 1.0379 0.1265  0.1109  0.0897  220 ILE I CA  
16910 C C   . ILE I  220 ? 0.8619 0.8022 0.9563 0.1234  0.1091  0.0871  220 ILE I C   
16911 O O   . ILE I  220 ? 0.8957 0.8308 0.9961 0.1222  0.1112  0.0857  220 ILE I O   
16912 C CB  . ILE I  220 ? 0.8459 0.7840 0.9419 0.1303  0.1171  0.0942  220 ILE I CB  
16913 C CG1 . ILE I  220 ? 0.7641 0.7024 0.8611 0.1336  0.1192  0.0972  220 ILE I CG1 
16914 C CG2 . ILE I  220 ? 0.8406 0.7827 0.9285 0.1314  0.1179  0.0971  220 ILE I CG2 
16915 C CD1 . ILE I  220 ? 1.0122 0.9467 1.1120 0.1372  0.1257  0.1014  220 ILE I CD1 
16916 N N   . ALA I  221 ? 0.7613 0.7072 0.8485 0.1220  0.1053  0.0863  221 ALA I N   
16917 C CA  . ALA I  221 ? 0.7364 0.6824 0.8222 0.1191  0.1037  0.0839  221 ALA I CA  
16918 C C   . ALA I  221 ? 0.8347 0.7874 0.9110 0.1182  0.1003  0.0839  221 ALA I C   
16919 O O   . ALA I  221 ? 0.9671 0.9248 1.0387 0.1197  0.0986  0.0856  221 ALA I O   
16920 C CB  . ALA I  221 ? 0.7217 0.6646 0.8144 0.1156  0.1007  0.0795  221 ALA I CB  
16921 N N   . ILE I  222 ? 0.8433 0.7964 0.9173 0.1158  0.0995  0.0821  222 ILE I N   
16922 C CA  . ILE I  222 ? 0.9607 0.9199 1.0258 0.1145  0.0966  0.0817  222 ILE I CA  
16923 C C   . ILE I  222 ? 0.9305 0.8916 0.9960 0.1111  0.0912  0.0777  222 ILE I C   
16924 O O   . ILE I  222 ? 0.8882 0.8461 0.9580 0.1084  0.0904  0.0747  222 ILE I O   
16925 C CB  . ILE I  222 ? 1.1234 1.0819 1.1845 0.1136  0.0994  0.0821  222 ILE I CB  
16926 C CG1 . ILE I  222 ? 1.1464 1.1034 1.2063 0.1169  0.1048  0.0863  222 ILE I CG1 
16927 C CG2 . ILE I  222 ? 0.8761 0.8410 0.9279 0.1119  0.0964  0.0813  222 ILE I CG2 
16928 C CD1 . ILE I  222 ? 1.2106 1.1732 1.2641 0.1199  0.1047  0.0903  222 ILE I CD1 
16929 N N   . ARG I  223 ? 0.8834 0.8497 0.9446 0.1114  0.0876  0.0778  223 ARG I N   
16930 C CA  . ARG I  223 ? 0.8622 0.8309 0.9226 0.1083  0.0824  0.0742  223 ARG I CA  
16931 C C   . ARG I  223 ? 0.8889 0.8630 0.9405 0.1068  0.0805  0.0738  223 ARG I C   
16932 O O   . ARG I  223 ? 1.0813 1.0592 1.1263 0.1086  0.0821  0.0767  223 ARG I O   
16933 C CB  . ARG I  223 ? 0.8164 0.7873 0.8775 0.1091  0.0795  0.0742  223 ARG I CB  
16934 C CG  . ARG I  223 ? 0.7384 0.7040 0.8083 0.1096  0.0806  0.0736  223 ARG I CG  
16935 C CD  . ARG I  223 ? 0.7055 0.6689 0.7772 0.1134  0.0854  0.0773  223 ARG I CD  
16936 N NE  . ARG I  223 ? 0.6914 0.6509 0.7701 0.1138  0.0860  0.0766  223 ARG I NE  
16937 C CZ  . ARG I  223 ? 0.7777 0.7343 0.8597 0.1168  0.0902  0.0793  223 ARG I CZ  
16938 N NH1 . ARG I  223 ? 0.8522 0.8096 0.9311 0.1199  0.0941  0.0833  223 ARG I NH1 
16939 N NH2 . ARG I  223 ? 0.8317 0.7847 0.9199 0.1166  0.0905  0.0781  223 ARG I NH2 
16940 N N   . PRO I  224 ? 0.8171 0.7919 0.8687 0.1034  0.0770  0.0702  224 PRO I N   
16941 C CA  . PRO I  224 ? 0.9286 0.9085 0.9720 0.1016  0.0750  0.0693  224 PRO I CA  
16942 C C   . PRO I  224 ? 0.9079 0.8947 0.9442 0.1032  0.0730  0.0714  224 PRO I C   
16943 O O   . PRO I  224 ? 0.9323 0.9205 0.9703 0.1039  0.0705  0.0713  224 PRO I O   
16944 C CB  . PRO I  224 ? 0.8195 0.7986 0.8658 0.0981  0.0710  0.0652  224 PRO I CB  
16945 C CG  . PRO I  224 ? 0.8730 0.8455 0.9292 0.0978  0.0723  0.0641  224 PRO I CG  
16946 C CD  . PRO I  224 ? 0.8729 0.8435 0.9322 0.1011  0.0749  0.0670  224 PRO I CD  
16947 N N   . LYS I  225 ? 0.9602 0.9513 0.9886 0.1036  0.0742  0.0732  225 LYS I N   
16948 C CA  . LYS I  225 ? 1.0663 1.0645 1.0881 0.1054  0.0727  0.0759  225 LYS I CA  
16949 C C   . LYS I  225 ? 0.9761 0.9786 0.9960 0.1038  0.0676  0.0737  225 LYS I C   
16950 O O   . LYS I  225 ? 0.8617 0.8655 0.8792 0.1006  0.0649  0.0705  225 LYS I O   
16951 C CB  . LYS I  225 ? 1.2605 1.2631 1.2735 0.1051  0.0743  0.0777  225 LYS I CB  
16952 C CG  . LYS I  225 ? 1.4661 1.4660 1.4794 0.1075  0.0794  0.0811  225 LYS I CG  
16953 C CD  . LYS I  225 ? 1.6512 1.6559 1.6551 0.1068  0.0807  0.0828  225 LYS I CD  
16954 C CE  . LYS I  225 ? 1.8858 1.8877 1.8898 0.1092  0.0859  0.0863  225 LYS I CE  
16955 N NZ  . LYS I  225 ? 1.8604 1.8627 1.8673 0.1135  0.0873  0.0907  225 LYS I NZ  
16956 N N   . VAL I  226 ? 0.9090 0.9134 0.9304 0.1062  0.0665  0.0756  226 VAL I N   
16957 C CA  . VAL I  226 ? 0.8776 0.8870 0.8963 0.1053  0.0621  0.0743  226 VAL I CA  
16958 C C   . VAL I  226 ? 0.9464 0.9621 0.9604 0.1083  0.0625  0.0786  226 VAL I C   
16959 O O   . VAL I  226 ? 0.9299 0.9443 0.9474 0.1116  0.0647  0.0816  226 VAL I O   
16960 C CB  . VAL I  226 ? 0.8821 0.8878 0.9079 0.1049  0.0603  0.0722  226 VAL I CB  
16961 C CG1 . VAL I  226 ? 0.8376 0.8483 0.8602 0.1040  0.0559  0.0710  226 VAL I CG1 
16962 C CG2 . VAL I  226 ? 0.7902 0.7898 0.8213 0.1020  0.0598  0.0685  226 VAL I CG2 
16963 N N   . ARG I  227 ? 0.9437 0.9664 0.9499 0.1073  0.0606  0.0790  227 ARG I N   
16964 C CA  . ARG I  227 ? 0.9172 0.9468 0.9185 0.1100  0.0608  0.0834  227 ARG I CA  
16965 C C   . ARG I  227 ? 1.1037 1.1322 1.1047 0.1130  0.0655  0.0878  227 ARG I C   
16966 O O   . ARG I  227 ? 1.2101 1.2405 1.2122 0.1166  0.0671  0.0921  227 ARG I O   
16967 C CB  . ARG I  227 ? 0.8687 0.8998 0.8734 0.1122  0.0593  0.0846  227 ARG I CB  
16968 C CG  . ARG I  227 ? 0.9065 0.9398 0.9103 0.1095  0.0546  0.0808  227 ARG I CG  
16969 C CD  . ARG I  227 ? 0.8731 0.9064 0.8814 0.1116  0.0538  0.0816  227 ARG I CD  
16970 N NE  . ARG I  227 ? 0.8628 0.9034 0.8666 0.1112  0.0503  0.0818  227 ARG I NE  
16971 C CZ  . ARG I  227 ? 1.0549 1.1025 1.0545 0.1136  0.0506  0.0859  227 ARG I CZ  
16972 N NH1 . ARG I  227 ? 1.1375 1.1859 1.1366 0.1165  0.0541  0.0903  227 ARG I NH1 
16973 N NH2 . ARG I  227 ? 0.9347 0.9890 0.9308 0.1130  0.0473  0.0858  227 ARG I NH2 
16974 N N   . ASP I  228 ? 1.1447 1.1699 1.1445 0.1114  0.0677  0.0867  228 ASP I N   
16975 C CA  . ASP I  228 ? 1.2600 1.2842 1.2583 0.1136  0.0722  0.0906  228 ASP I CA  
16976 C C   . ASP I  228 ? 1.1767 1.1940 1.1831 0.1166  0.0760  0.0925  228 ASP I C   
16977 O O   . ASP I  228 ? 1.3613 1.3766 1.3674 0.1183  0.0801  0.0953  228 ASP I O   
16978 C CB  . ASP I  228 ? 1.6559 1.6887 1.6473 0.1157  0.0719  0.0953  228 ASP I CB  
16979 C CG  . ASP I  228 ? 1.9271 1.9650 1.9094 0.1128  0.0712  0.0947  228 ASP I CG  
16980 O OD1 . ASP I  228 ? 1.8987 1.9333 1.8793 0.1120  0.0744  0.0947  228 ASP I OD1 
16981 O OD2 . ASP I  228 ? 2.0538 2.0988 2.0305 0.1113  0.0676  0.0942  228 ASP I OD2 
16982 N N   . GLN I  229 ? 1.0310 1.0447 1.0442 0.1170  0.0749  0.0908  229 GLN I N   
16983 C CA  . GLN I  229 ? 1.1043 1.1115 1.1254 0.1196  0.0785  0.0922  229 GLN I CA  
16984 C C   . GLN I  229 ? 0.9857 0.9849 1.0129 0.1173  0.0795  0.0883  229 GLN I C   
16985 O O   . GLN I  229 ? 0.9225 0.9204 0.9519 0.1144  0.0762  0.0842  229 GLN I O   
16986 C CB  . GLN I  229 ? 0.8714 0.8791 0.8965 0.1216  0.0773  0.0930  229 GLN I CB  
16987 C CG  . GLN I  229 ? 0.9123 0.9283 0.9320 0.1235  0.0755  0.0963  229 GLN I CG  
16988 C CD  . GLN I  229 ? 1.0328 1.0524 1.0487 0.1267  0.0787  0.1019  229 GLN I CD  
16989 O OE1 . GLN I  229 ? 1.1354 1.1503 1.1547 0.1289  0.0831  0.1043  229 GLN I OE1 
16990 N NE2 . GLN I  229 ? 1.1235 1.1516 1.1321 0.1268  0.0766  0.1042  229 GLN I NE2 
16991 N N   . GLU I  230 ? 0.9814 0.9757 1.0115 0.1186  0.0840  0.0899  230 GLU I N   
16992 C CA  . GLU I  230 ? 0.9203 0.9070 0.9575 0.1168  0.0854  0.0868  230 GLU I CA  
16993 C C   . GLU I  230 ? 0.9136 0.8950 0.9592 0.1187  0.0871  0.0872  230 GLU I C   
16994 O O   . GLU I  230 ? 0.9860 0.9614 1.0385 0.1173  0.0878  0.0846  230 GLU I O   
16995 C CB  . GLU I  230 ? 1.1991 1.1829 1.2349 0.1167  0.0894  0.0877  230 GLU I CB  
16996 C CG  . GLU I  230 ? 1.2184 1.2040 1.2490 0.1131  0.0877  0.0848  230 GLU I CG  
16997 C CD  . GLU I  230 ? 1.6337 1.6183 1.6604 0.1131  0.0918  0.0864  230 GLU I CD  
16998 O OE1 . GLU I  230 ? 1.4410 1.4242 1.4660 0.1101  0.0918  0.0835  230 GLU I OE1 
16999 O OE2 . GLU I  230 ? 1.8100 1.7949 1.8353 0.1162  0.0952  0.0907  230 GLU I OE2 
17000 N N   . GLY I  231 ? 0.7477 0.7318 0.7930 0.1219  0.0878  0.0905  231 GLY I N   
17001 C CA  . GLY I  231 ? 0.7901 0.7697 0.8428 0.1235  0.0892  0.0906  231 GLY I CA  
17002 C C   . GLY I  231 ? 0.8365 0.8181 0.8902 0.1219  0.0848  0.0878  231 GLY I C   
17003 O O   . GLY I  231 ? 0.7818 0.7687 0.8299 0.1201  0.0808  0.0865  231 GLY I O   
17004 N N   . ARG I  232 ? 0.7534 0.7304 0.8139 0.1223  0.0856  0.0867  232 ARG I N   
17005 C CA  . ARG I  232 ? 0.7082 0.6864 0.7698 0.1206  0.0817  0.0839  232 ARG I CA  
17006 C C   . ARG I  232 ? 0.7414 0.7193 0.8057 0.1237  0.0839  0.0864  232 ARG I C   
17007 O O   . ARG I  232 ? 0.6513 0.6266 0.7183 0.1268  0.0885  0.0897  232 ARG I O   
17008 C CB  . ARG I  232 ? 0.7333 0.7063 0.8008 0.1171  0.0799  0.0792  232 ARG I CB  
17009 C CG  . ARG I  232 ? 0.6598 0.6337 0.7249 0.1136  0.0768  0.0763  232 ARG I CG  
17010 C CD  . ARG I  232 ? 0.6911 0.6715 0.7494 0.1122  0.0722  0.0752  232 ARG I CD  
17011 N NE  . ARG I  232 ? 0.7453 0.7265 0.8013 0.1090  0.0697  0.0725  232 ARG I NE  
17012 C CZ  . ARG I  232 ? 0.8548 0.8382 0.9058 0.1090  0.0709  0.0737  232 ARG I CZ  
17013 N NH1 . ARG I  232 ? 0.8220 0.8074 0.8696 0.1121  0.0742  0.0778  232 ARG I NH1 
17014 N NH2 . ARG I  232 ? 0.8262 0.8099 0.8757 0.1059  0.0689  0.0710  232 ARG I NH2 
17015 N N   . MET I  233 ? 0.8078 0.7881 0.8713 0.1227  0.0806  0.0846  233 MET I N   
17016 C CA  . MET I  233 ? 0.7012 0.6810 0.7675 0.1252  0.0826  0.0864  233 MET I CA  
17017 C C   . MET I  233 ? 0.6585 0.6365 0.7274 0.1223  0.0794  0.0820  233 MET I C   
17018 O O   . MET I  233 ? 0.5624 0.5448 0.6272 0.1204  0.0751  0.0802  233 MET I O   
17019 C CB  . MET I  233 ? 0.6150 0.6018 0.6757 0.1283  0.0826  0.0907  233 MET I CB  
17020 C CG  . MET I  233 ? 0.6709 0.6572 0.7350 0.1315  0.0855  0.0933  233 MET I CG  
17021 S SD  . MET I  233 ? 0.7605 0.7556 0.8188 0.1355  0.0858  0.0991  233 MET I SD  
17022 C CE  . MET I  233 ? 0.8027 0.7984 0.8589 0.1380  0.0894  0.1038  233 MET I CE  
17023 N N   . ASN I  234 ? 0.5963 0.5678 0.6721 0.1217  0.0817  0.0803  234 ASN I N   
17024 C CA  . ASN I  234 ? 0.6112 0.5806 0.6896 0.1187  0.0790  0.0762  234 ASN I CA  
17025 C C   . ASN I  234 ? 0.6349 0.6054 0.7135 0.1208  0.0804  0.0775  234 ASN I C   
17026 O O   . ASN I  234 ? 0.5931 0.5622 0.6739 0.1244  0.0851  0.0811  234 ASN I O   
17027 C CB  . ASN I  234 ? 0.5995 0.5616 0.6850 0.1166  0.0806  0.0734  234 ASN I CB  
17028 C CG  . ASN I  234 ? 0.6890 0.6501 0.7750 0.1138  0.0784  0.0714  234 ASN I CG  
17029 O OD1 . ASN I  234 ? 0.6799 0.6454 0.7608 0.1133  0.0758  0.0716  234 ASN I OD1 
17030 N ND2 . ASN I  234 ? 0.8165 0.7718 0.9090 0.1120  0.0797  0.0693  234 ASN I ND2 
17031 N N   . TYR I  235 ? 0.6006 0.5735 0.6770 0.1184  0.0764  0.0747  235 TYR I N   
17032 C CA  . TYR I  235 ? 0.5321 0.5064 0.6084 0.1201  0.0775  0.0757  235 TYR I CA  
17033 C C   . TYR I  235 ? 0.5797 0.5486 0.6606 0.1174  0.0776  0.0717  235 TYR I C   
17034 O O   . TYR I  235 ? 0.5610 0.5287 0.6419 0.1132  0.0736  0.0674  235 TYR I O   
17035 C CB  . TYR I  235 ? 0.4672 0.4489 0.5369 0.1198  0.0732  0.0759  235 TYR I CB  
17036 C CG  . TYR I  235 ? 0.6442 0.6317 0.7087 0.1217  0.0726  0.0793  235 TYR I CG  
17037 C CD1 . TYR I  235 ? 0.6295 0.6189 0.6905 0.1190  0.0689  0.0773  235 TYR I CD1 
17038 C CD2 . TYR I  235 ? 0.6066 0.5976 0.6698 0.1262  0.0758  0.0846  235 TYR I CD2 
17039 C CE1 . TYR I  235 ? 0.6178 0.6123 0.6738 0.1204  0.0686  0.0801  235 TYR I CE1 
17040 C CE2 . TYR I  235 ? 0.6174 0.6139 0.6754 0.1276  0.0751  0.0876  235 TYR I CE2 
17041 C CZ  . TYR I  235 ? 0.5547 0.5528 0.6089 0.1245  0.0715  0.0852  235 TYR I CZ  
17042 O OH  . TYR I  235 ? 0.6741 0.6775 0.7228 0.1255  0.0711  0.0879  235 TYR I OH  
17043 N N   . TYR I  236 ? 0.5648 0.5304 0.6496 0.1197  0.0822  0.0732  236 TYR I N   
17044 C CA  . TYR I  236 ? 0.5338 0.4939 0.6229 0.1172  0.0832  0.0695  236 TYR I CA  
17045 C C   . TYR I  236 ? 0.5907 0.5521 0.6792 0.1186  0.0846  0.0702  236 TYR I C   
17046 O O   . TYR I  236 ? 0.7075 0.6730 0.7939 0.1226  0.0864  0.0744  236 TYR I O   
17047 C CB  . TYR I  236 ? 0.4519 0.4050 0.5476 0.1179  0.0883  0.0699  236 TYR I CB  
17048 C CG  . TYR I  236 ? 0.5639 0.5150 0.6614 0.1161  0.0872  0.0688  236 TYR I CG  
17049 C CD1 . TYR I  236 ? 0.5784 0.5316 0.6743 0.1189  0.0885  0.0725  236 TYR I CD1 
17050 C CD2 . TYR I  236 ? 0.6577 0.6049 0.7585 0.1116  0.0849  0.0643  236 TYR I CD2 
17051 C CE1 . TYR I  236 ? 0.6365 0.5876 0.7342 0.1173  0.0878  0.0715  236 TYR I CE1 
17052 C CE2 . TYR I  236 ? 0.7171 0.6625 0.8200 0.1101  0.0841  0.0635  236 TYR I CE2 
17053 C CZ  . TYR I  236 ? 0.7553 0.7025 0.8568 0.1130  0.0856  0.0671  236 TYR I CZ  
17054 O OH  . TYR I  236 ? 0.6428 0.5880 0.7467 0.1115  0.0851  0.0663  236 TYR I OH  
17055 N N   . TRP I  237 ? 0.5718 0.5297 0.6621 0.1153  0.0838  0.0660  237 TRP I N   
17056 C CA  . TRP I  237 ? 0.4785 0.4368 0.5684 0.1162  0.0854  0.0659  237 TRP I CA  
17057 C C   . TRP I  237 ? 0.4851 0.4366 0.5794 0.1131  0.0875  0.0618  237 TRP I C   
17058 O O   . TRP I  237 ? 0.6377 0.5853 0.7343 0.1094  0.0861  0.0584  237 TRP I O   
17059 C CB  . TRP I  237 ? 0.5379 0.5025 0.6218 0.1147  0.0801  0.0647  237 TRP I CB  
17060 C CG  . TRP I  237 ? 0.5488 0.5128 0.6309 0.1093  0.0746  0.0595  237 TRP I CG  
17061 C CD1 . TRP I  237 ? 0.5557 0.5219 0.6355 0.1071  0.0701  0.0583  237 TRP I CD1 
17062 C CD2 . TRP I  237 ? 0.6021 0.5630 0.6848 0.1052  0.0732  0.0549  237 TRP I CD2 
17063 N NE1 . TRP I  237 ? 0.5765 0.5414 0.6556 0.1021  0.0659  0.0535  237 TRP I NE1 
17064 C CE2 . TRP I  237 ? 0.6621 0.6239 0.7428 0.1008  0.0676  0.0514  237 TRP I CE2 
17065 C CE3 . TRP I  237 ? 0.5735 0.5309 0.6582 0.1049  0.0764  0.0534  237 TRP I CE3 
17066 C CZ2 . TRP I  237 ? 0.6288 0.5884 0.7091 0.0961  0.0647  0.0466  237 TRP I CZ2 
17067 C CZ3 . TRP I  237 ? 0.6510 0.6061 0.7351 0.1000  0.0737  0.0484  237 TRP I CZ3 
17068 C CH2 . TRP I  237 ? 0.5825 0.5388 0.6643 0.0956  0.0678  0.0452  237 TRP I CH2 
17069 N N   . THR I  238 ? 0.5205 0.4707 0.6160 0.1144  0.0909  0.0621  238 THR I N   
17070 C CA  . THR I  238 ? 0.5903 0.5341 0.6893 0.1112  0.0932  0.0580  238 THR I CA  
17071 C C   . THR I  238 ? 0.6146 0.5588 0.7130 0.1126  0.0958  0.0584  238 THR I C   
17072 O O   . THR I  238 ? 0.6166 0.5653 0.7138 0.1171  0.0973  0.0629  238 THR I O   
17073 C CB  . THR I  238 ? 0.6353 0.5722 0.7408 0.1121  0.0989  0.0585  238 THR I CB  
17074 O OG1 . THR I  238 ? 0.6304 0.5613 0.7389 0.1083  0.1007  0.0539  238 THR I OG1 
17075 C CG2 . THR I  238 ? 0.6509 0.5878 0.7589 0.1181  0.1052  0.0641  238 THR I CG2 
17076 N N   . LEU I  239 ? 0.6468 0.5867 0.7463 0.1088  0.0963  0.0538  239 LEU I N   
17077 C CA  . LEU I  239 ? 0.7754 0.7149 0.8746 0.1096  0.0991  0.0535  239 LEU I CA  
17078 C C   . LEU I  239 ? 0.8621 0.7941 0.9673 0.1104  0.1066  0.0532  239 LEU I C   
17079 O O   . LEU I  239 ? 0.9612 0.8874 1.0686 0.1061  0.1074  0.0486  239 LEU I O   
17080 C CB  . LEU I  239 ? 0.7793 0.7197 0.8743 0.1044  0.0941  0.0484  239 LEU I CB  
17081 C CG  . LEU I  239 ? 0.5778 0.5258 0.6667 0.1038  0.0872  0.0487  239 LEU I CG  
17082 C CD1 . LEU I  239 ? 0.7938 0.7417 0.8789 0.0983  0.0826  0.0434  239 LEU I CD1 
17083 C CD2 . LEU I  239 ? 0.6368 0.5907 0.7238 0.1089  0.0884  0.0536  239 LEU I CD2 
17084 N N   . VAL I  240 ? 0.7843 0.7167 0.8922 0.1159  0.1121  0.0582  240 VAL I N   
17085 C CA  . VAL I  240 ? 0.8129 0.7384 0.9269 0.1173  0.1200  0.0585  240 VAL I CA  
17086 C C   . VAL I  240 ? 0.7279 0.6507 0.8418 0.1152  0.1222  0.0553  240 VAL I C   
17087 O O   . VAL I  240 ? 0.7004 0.6277 0.8119 0.1173  0.1216  0.0572  240 VAL I O   
17088 C CB  . VAL I  240 ? 0.8042 0.7312 0.9216 0.1242  0.1253  0.0656  240 VAL I CB  
17089 C CG1 . VAL I  240 ? 0.8389 0.7580 0.9631 0.1256  0.1337  0.0659  240 VAL I CG1 
17090 C CG2 . VAL I  240 ? 0.6914 0.6220 0.8076 0.1263  0.1227  0.0690  240 VAL I CG2 
17091 N N   . GLU I  241 ? 0.7476 0.6630 0.8641 0.1109  0.1248  0.0503  241 GLU I N   
17092 C CA  . GLU I  241 ? 0.8768 0.7887 0.9932 0.1084  0.1275  0.0466  241 GLU I CA  
17093 C C   . GLU I  241 ? 0.9457 0.8561 1.0663 0.1138  0.1352  0.0509  241 GLU I C   
17094 O O   . GLU I  241 ? 0.9869 0.8963 1.1120 0.1184  0.1397  0.0556  241 GLU I O   
17095 C CB  . GLU I  241 ? 1.0444 0.9485 1.1629 0.1025  0.1291  0.0405  241 GLU I CB  
17096 C CG  . GLU I  241 ? 1.3160 1.2214 1.4309 0.0968  0.1216  0.0361  241 GLU I CG  
17097 C CD  . GLU I  241 ? 1.5763 1.4860 1.6847 0.0933  0.1154  0.0331  241 GLU I CD  
17098 O OE1 . GLU I  241 ? 1.6271 1.5410 1.7318 0.0908  0.1083  0.0319  241 GLU I OE1 
17099 O OE2 . GLU I  241 ? 1.6616 1.5706 1.7689 0.0931  0.1178  0.0319  241 GLU I OE2 
17100 N N   . PRO I  242 ? 1.0726 0.9830 1.1920 0.1132  0.1367  0.0495  242 PRO I N   
17101 C CA  . PRO I  242 ? 1.0603 0.9686 1.1845 0.1179  0.1445  0.0532  242 PRO I CA  
17102 C C   . PRO I  242 ? 1.0705 0.9698 1.2013 0.1179  0.1525  0.0523  242 PRO I C   
17103 O O   . PRO I  242 ? 0.9571 0.8503 1.0880 0.1123  0.1530  0.0462  242 PRO I O   
17104 C CB  . PRO I  242 ? 0.7891 0.6974 0.9104 0.1151  0.1442  0.0495  242 PRO I CB  
17105 C CG  . PRO I  242 ? 0.9392 0.8531 1.0533 0.1112  0.1350  0.0467  242 PRO I CG  
17106 C CD  . PRO I  242 ? 0.9123 0.8250 1.0258 0.1083  0.1311  0.0447  242 PRO I CD  
17107 N N   . GLY I  243 ? 0.8882 0.7869 1.0243 0.1240  0.1585  0.0583  243 GLY I N   
17108 C CA  . GLY I  243 ? 0.9524 0.8426 1.0951 0.1245  0.1665  0.0580  243 GLY I CA  
17109 C C   . GLY I  243 ? 1.0007 0.8891 1.1448 0.1237  0.1651  0.0580  243 GLY I C   
17110 O O   . GLY I  243 ? 1.1752 1.0569 1.3249 0.1243  0.1714  0.0580  243 GLY I O   
17111 N N   . ASP I  244 ? 1.0861 0.9805 1.2252 0.1224  0.1570  0.0579  244 ASP I N   
17112 C CA  . ASP I  244 ? 1.0202 0.9138 1.1603 0.1217  0.1551  0.0581  244 ASP I CA  
17113 C C   . ASP I  244 ? 0.9735 0.8724 1.1144 0.1283  0.1554  0.0657  244 ASP I C   
17114 O O   . ASP I  244 ? 1.0840 0.9892 1.2228 0.1322  0.1543  0.0701  244 ASP I O   
17115 C CB  . ASP I  244 ? 0.9421 0.8387 1.0765 0.1161  0.1462  0.0533  244 ASP I CB  
17116 C CG  . ASP I  244 ? 1.1292 1.0237 1.2654 0.1143  0.1446  0.0524  244 ASP I CG  
17117 O OD1 . ASP I  244 ? 1.1580 1.0547 1.2905 0.1098  0.1377  0.0488  244 ASP I OD1 
17118 O OD2 . ASP I  244 ? 1.0316 0.9221 1.1730 0.1173  0.1502  0.0552  244 ASP I OD2 
17119 N N   . LYS I  245 ? 0.8245 0.7210 0.9683 0.1294  0.1569  0.0673  245 LYS I N   
17120 C CA  . LYS I  245 ? 0.8946 0.7960 1.0387 0.1351  0.1570  0.0743  245 LYS I CA  
17121 C C   . LYS I  245 ? 0.8625 0.7661 1.0040 0.1333  0.1515  0.0735  245 LYS I C   
17122 O O   . LYS I  245 ? 0.8741 0.7732 1.0165 0.1284  0.1500  0.0685  245 LYS I O   
17123 C CB  . LYS I  245 ? 1.0134 0.9098 1.1644 0.1400  0.1660  0.0789  245 LYS I CB  
17124 C CG  . LYS I  245 ? 1.0687 0.9576 1.2243 0.1380  0.1695  0.0765  245 LYS I CG  
17125 C CD  . LYS I  245 ? 1.1116 0.9958 1.2740 0.1432  0.1786  0.0815  245 LYS I CD  
17126 C CE  . LYS I  245 ? 1.1870 1.0639 1.3542 0.1412  0.1822  0.0793  245 LYS I CE  
17127 N NZ  . LYS I  245 ? 1.1017 0.9733 1.2758 0.1461  0.1916  0.0838  245 LYS I NZ  
17128 N N   . ILE I  246 ? 0.6939 0.6044 0.8323 0.1370  0.1484  0.0787  246 ILE I N   
17129 C CA  . ILE I  246 ? 0.7513 0.6643 0.8873 0.1358  0.1436  0.0786  246 ILE I CA  
17130 C C   . ILE I  246 ? 0.8779 0.7914 1.0164 0.1412  0.1476  0.0850  246 ILE I C   
17131 O O   . ILE I  246 ? 0.8601 0.7777 0.9985 0.1464  0.1499  0.0909  246 ILE I O   
17132 C CB  . ILE I  246 ? 0.7580 0.6792 0.8868 0.1344  0.1354  0.0781  246 ILE I CB  
17133 C CG1 . ILE I  246 ? 0.7949 0.7181 0.9215 0.1331  0.1309  0.0779  246 ILE I CG1 
17134 C CG2 . ILE I  246 ? 0.6198 0.5481 0.7461 0.1394  0.1355  0.0839  246 ILE I CG2 
17135 C CD1 . ILE I  246 ? 0.5857 0.5169 0.7053 0.1320  0.1233  0.0778  246 ILE I CD1 
17136 N N   . THR I  247 ? 0.9843 0.8938 1.1253 0.1399  0.1483  0.0839  247 THR I N   
17137 C CA  . THR I  247 ? 0.8845 0.7935 1.0282 0.1446  0.1525  0.0895  247 THR I CA  
17138 C C   . THR I  247 ? 0.7984 0.7125 0.9377 0.1446  0.1473  0.0910  247 THR I C   
17139 O O   . THR I  247 ? 0.9338 0.8479 1.0709 0.1400  0.1421  0.0865  247 THR I O   
17140 C CB  . THR I  247 ? 0.9890 0.8889 1.1397 0.1438  0.1588  0.0879  247 THR I CB  
17141 O OG1 . THR I  247 ? 1.1593 1.0544 1.3144 0.1451  0.1653  0.0881  247 THR I OG1 
17142 C CG2 . THR I  247 ? 0.8664 0.7658 1.0192 0.1479  0.1622  0.0932  247 THR I CG2 
17143 N N   . PHE I  248 ? 0.8223 0.7406 0.9604 0.1497  0.1488  0.0976  248 PHE I N   
17144 C CA  . PHE I  248 ? 0.9173 0.8398 1.0515 0.1502  0.1451  0.0996  248 PHE I CA  
17145 C C   . PHE I  248 ? 0.9131 0.8317 1.0515 0.1535  0.1509  0.1035  248 PHE I C   
17146 O O   . PHE I  248 ? 0.9452 0.8621 1.0872 0.1579  0.1570  0.1082  248 PHE I O   
17147 C CB  . PHE I  248 ? 0.7110 0.6429 0.8388 0.1529  0.1412  0.1038  248 PHE I CB  
17148 C CG  . PHE I  248 ? 0.7603 0.6968 0.8832 0.1493  0.1346  0.0998  248 PHE I CG  
17149 C CD1 . PHE I  248 ? 0.7544 0.6910 0.8779 0.1491  0.1353  0.0986  248 PHE I CD1 
17150 C CD2 . PHE I  248 ? 0.7827 0.7232 0.9003 0.1462  0.1280  0.0972  248 PHE I CD2 
17151 C CE1 . PHE I  248 ? 0.6723 0.6130 0.7912 0.1458  0.1294  0.0949  248 PHE I CE1 
17152 C CE2 . PHE I  248 ? 0.7562 0.7008 0.8693 0.1429  0.1221  0.0936  248 PHE I CE2 
17153 C CZ  . PHE I  248 ? 0.6599 0.6046 0.7735 0.1427  0.1227  0.0925  248 PHE I CZ  
17154 N N   . GLU I  249 ? 0.8822 0.7991 1.0204 0.1513  0.1490  0.1017  249 GLU I N   
17155 C CA  . GLU I  249 ? 0.8656 0.7783 1.0077 0.1538  0.1542  0.1048  249 GLU I CA  
17156 C C   . GLU I  249 ? 0.8104 0.7262 0.9485 0.1528  0.1503  0.1052  249 GLU I C   
17157 O O   . GLU I  249 ? 1.0262 0.9410 1.1637 0.1483  0.1460  0.1002  249 GLU I O   
17158 C CB  . GLU I  249 ? 0.9430 0.8466 1.0922 0.1510  0.1584  0.1006  249 GLU I CB  
17159 C CG  . GLU I  249 ? 1.1603 1.0587 1.3143 0.1532  0.1641  0.1032  249 GLU I CG  
17160 C CD  . GLU I  249 ? 1.3716 1.2611 1.5327 0.1503  0.1683  0.0988  249 GLU I CD  
17161 O OE1 . GLU I  249 ? 1.3915 1.2766 1.5564 0.1502  0.1712  0.0989  249 GLU I OE1 
17162 O OE2 . GLU I  249 ? 1.2570 1.1440 1.4198 0.1480  0.1687  0.0951  249 GLU I OE2 
17163 N N   . ALA I  250 ? 0.8005 0.7202 0.9360 0.1571  0.1518  0.1113  250 ALA I N   
17164 C CA  . ALA I  250 ? 0.8067 0.7299 0.9374 0.1564  0.1481  0.1119  250 ALA I CA  
17165 C C   . ALA I  250 ? 1.0474 0.9701 1.1787 0.1605  0.1528  0.1177  250 ALA I C   
17166 O O   . ALA I  250 ? 1.0150 0.9384 1.1475 0.1652  0.1574  0.1233  250 ALA I O   
17167 C CB  . ALA I  250 ? 0.7753 0.7074 0.8983 0.1558  0.1417  0.1123  250 ALA I CB  
17168 N N   . THR I  251 ? 0.9950 0.9163 1.1255 0.1588  0.1517  0.1165  251 THR I N   
17169 C CA  . THR I  251 ? 0.8625 0.7840 0.9920 0.1622  0.1552  0.1217  251 THR I CA  
17170 C C   . THR I  251 ? 0.8965 0.8257 1.0176 0.1618  0.1501  0.1231  251 THR I C   
17171 O O   . THR I  251 ? 0.9355 0.8654 1.0543 0.1633  0.1516  0.1262  251 THR I O   
17172 C CB  . THR I  251 ? 0.8097 0.7237 0.9446 0.1606  0.1586  0.1194  251 THR I CB  
17173 O OG1 . THR I  251 ? 1.0513 0.9642 1.1860 0.1553  0.1536  0.1131  251 THR I OG1 
17174 C CG2 . THR I  251 ? 0.8811 0.7875 1.0242 0.1616  0.1648  0.1191  251 THR I CG2 
17175 N N   . GLY I  252 ? 0.9068 0.8416 1.0233 0.1598  0.1443  0.1208  252 GLY I N   
17176 C CA  . GLY I  252 ? 0.8655 0.8078 0.9739 0.1590  0.1392  0.1217  252 GLY I CA  
17177 C C   . GLY I  252 ? 0.8678 0.8126 0.9734 0.1543  0.1325  0.1158  252 GLY I C   
17178 O O   . GLY I  252 ? 0.8934 0.8336 1.0033 0.1512  0.1316  0.1108  252 GLY I O   
17179 N N   . ASN I  253 ? 0.8048 0.7568 0.9029 0.1536  0.1279  0.1165  253 ASN I N   
17180 C CA  . ASN I  253 ? 0.7878 0.7424 0.8825 0.1491  0.1215  0.1112  253 ASN I CA  
17181 C C   . ASN I  253 ? 0.8513 0.8076 0.9464 0.1479  0.1186  0.1087  253 ASN I C   
17182 O O   . ASN I  253 ? 0.7946 0.7521 0.8880 0.1439  0.1136  0.1039  253 ASN I O   
17183 C CB  . ASN I  253 ? 0.8289 0.7774 0.9274 0.1452  0.1208  0.1061  253 ASN I CB  
17184 C CG  . ASN I  253 ? 0.7750 0.7215 0.8733 0.1460  0.1236  0.1081  253 ASN I CG  
17185 O OD1 . ASN I  253 ? 0.8309 0.7792 0.9254 0.1437  0.1207  0.1064  253 ASN I OD1 
17186 N ND2 . ASN I  253 ? 0.7859 0.7283 0.8883 0.1493  0.1296  0.1118  253 ASN I ND2 
17187 N N   . LEU I  254 ? 0.8970 0.8536 0.9943 0.1513  0.1219  0.1120  254 LEU I N   
17188 C CA  . LEU I  254 ? 0.7881 0.7458 0.8864 0.1503  0.1201  0.1098  254 LEU I CA  
17189 C C   . LEU I  254 ? 0.5909 0.5572 0.6835 0.1523  0.1173  0.1130  254 LEU I C   
17190 O O   . LEU I  254 ? 0.7931 0.7623 0.8858 0.1567  0.1206  0.1188  254 LEU I O   
17191 C CB  . LEU I  254 ? 0.7692 0.7204 0.8748 0.1522  0.1258  0.1104  254 LEU I CB  
17192 C CG  . LEU I  254 ? 0.7087 0.6606 0.8155 0.1517  0.1250  0.1085  254 LEU I CG  
17193 C CD1 . LEU I  254 ? 0.7965 0.7477 0.9019 0.1462  0.1195  0.1017  254 LEU I CD1 
17194 C CD2 . LEU I  254 ? 0.6887 0.6338 0.8028 0.1537  0.1315  0.1093  254 LEU I CD2 
17195 N N   . VAL I  255 ? 0.6487 0.6194 0.7366 0.1490  0.1113  0.1095  255 VAL I N   
17196 C CA  . VAL I  255 ? 0.5366 0.5153 0.6197 0.1502  0.1084  0.1116  255 VAL I CA  
17197 C C   . VAL I  255 ? 0.6846 0.6614 0.7717 0.1509  0.1099  0.1107  255 VAL I C   
17198 O O   . VAL I  255 ? 0.6620 0.6371 0.7494 0.1472  0.1068  0.1055  255 VAL I O   
17199 C CB  . VAL I  255 ? 0.5732 0.5568 0.6500 0.1463  0.1016  0.1079  255 VAL I CB  
17200 C CG1 . VAL I  255 ? 0.6198 0.6118 0.6918 0.1475  0.0987  0.1101  255 VAL I CG1 
17201 C CG2 . VAL I  255 ? 0.5620 0.5469 0.6348 0.1453  0.1004  0.1083  255 VAL I CG2 
17202 N N   . VAL I  256 ? 0.6983 0.6752 0.7885 0.1554  0.1148  0.1159  256 VAL I N   
17203 C CA  . VAL I  256 ? 0.6209 0.5947 0.7161 0.1564  0.1177  0.1153  256 VAL I CA  
17204 C C   . VAL I  256 ? 0.7194 0.6993 0.8113 0.1558  0.1139  0.1146  256 VAL I C   
17205 O O   . VAL I  256 ? 0.7324 0.7204 0.8185 0.1564  0.1102  0.1170  256 VAL I O   
17206 C CB  . VAL I  256 ? 0.7804 0.7525 0.8805 0.1618  0.1247  0.1216  256 VAL I CB  
17207 C CG1 . VAL I  256 ? 0.9012 0.8667 1.0050 0.1624  0.1289  0.1222  256 VAL I CG1 
17208 C CG2 . VAL I  256 ? 0.8710 0.8522 0.9671 0.1659  0.1241  0.1284  256 VAL I CG2 
17209 N N   . PRO I  257 ? 0.6461 0.6222 0.7415 0.1543  0.1148  0.1112  257 PRO I N   
17210 C CA  . PRO I  257 ? 0.6232 0.6043 0.7164 0.1539  0.1120  0.1105  257 PRO I CA  
17211 C C   . PRO I  257 ? 0.8219 0.8083 0.9159 0.1594  0.1151  0.1176  257 PRO I C   
17212 O O   . PRO I  257 ? 0.8884 0.8717 0.9874 0.1632  0.1211  0.1218  257 PRO I O   
17213 C CB  . PRO I  257 ? 0.5860 0.5597 0.6840 0.1514  0.1142  0.1056  257 PRO I CB  
17214 C CG  . PRO I  257 ? 0.6790 0.6448 0.7801 0.1489  0.1157  0.1021  257 PRO I CG  
17215 C CD  . PRO I  257 ? 0.6961 0.6626 0.7976 0.1524  0.1184  0.1072  257 PRO I CD  
17216 N N   . ARG I  258 ? 0.8713 0.8660 0.9609 0.1598  0.1112  0.1190  258 ARG I N   
17217 C CA  . ARG I  258 ? 0.7848 0.7853 0.8757 0.1647  0.1137  0.1256  258 ARG I CA  
17218 C C   . ARG I  258 ? 0.7393 0.7409 0.8313 0.1639  0.1129  0.1234  258 ARG I C   
17219 O O   . ARG I  258 ? 0.7939 0.7942 0.8911 0.1672  0.1178  0.1264  258 ARG I O   
17220 C CB  . ARG I  258 ? 0.7313 0.7417 0.8160 0.1664  0.1101  0.1303  258 ARG I CB  
17221 C CG  . ARG I  258 ? 0.8218 0.8400 0.9073 0.1710  0.1115  0.1371  258 ARG I CG  
17222 C CD  . ARG I  258 ? 0.8347 0.8633 0.9133 0.1717  0.1071  0.1409  258 ARG I CD  
17223 N NE  . ARG I  258 ? 0.9928 1.0302 1.0710 0.1745  0.1062  0.1456  258 ARG I NE  
17224 C CZ  . ARG I  258 ? 1.1324 1.1747 1.2130 0.1797  0.1094  0.1535  258 ARG I CZ  
17225 N NH1 . ARG I  258 ? 1.1829 1.2218 1.2661 0.1826  0.1139  0.1576  258 ARG I NH1 
17226 N NH2 . ARG I  258 ? 1.0887 1.1393 1.1692 0.1820  0.1082  0.1575  258 ARG I NH2 
17227 N N   . TYR I  259 ? 0.8281 0.8319 0.9154 0.1594  0.1071  0.1181  259 TYR I N   
17228 C CA  . TYR I  259 ? 0.7023 0.7064 0.7900 0.1579  0.1060  0.1151  259 TYR I CA  
17229 C C   . TYR I  259 ? 0.7026 0.6992 0.7908 0.1525  0.1045  0.1072  259 TYR I C   
17230 O O   . TYR I  259 ? 0.6162 0.6117 0.7010 0.1488  0.1006  0.1034  259 TYR I O   
17231 C CB  . TYR I  259 ? 0.7396 0.7537 0.8212 0.1572  0.1002  0.1158  259 TYR I CB  
17232 C CG  . TYR I  259 ? 0.9043 0.9269 0.9859 0.1623  0.1014  0.1235  259 TYR I CG  
17233 C CD1 . TYR I  259 ? 0.9449 0.9734 1.0229 0.1641  0.0999  0.1280  259 TYR I CD1 
17234 C CD2 . TYR I  259 ? 0.9361 0.9611 1.0213 0.1651  0.1039  0.1263  259 TYR I CD2 
17235 C CE1 . TYR I  259 ? 1.1022 1.1390 1.1800 0.1685  0.1007  0.1352  259 TYR I CE1 
17236 C CE2 . TYR I  259 ? 1.0482 1.0817 1.1338 0.1697  0.1047  0.1336  259 TYR I CE2 
17237 C CZ  . TYR I  259 ? 1.0996 1.1391 1.1814 0.1714  0.1030  0.1382  259 TYR I CZ  
17238 O OH  . TYR I  259 ? 1.1863 1.2347 1.2683 0.1758  0.1036  0.1457  259 TYR I OH  
17239 N N   . ALA I  260 ? 0.8060 0.7975 0.8983 0.1520  0.1078  0.1049  260 ALA I N   
17240 C CA  . ALA I  260 ? 0.6413 0.6265 0.7336 0.1467  0.1061  0.0975  260 ALA I CA  
17241 C C   . ALA I  260 ? 0.7175 0.7062 0.8072 0.1448  0.1031  0.0950  260 ALA I C   
17242 O O   . ALA I  260 ? 0.6851 0.6814 0.7729 0.1475  0.1019  0.0988  260 ALA I O   
17243 C CB  . ALA I  260 ? 0.6210 0.5966 0.7200 0.1468  0.1125  0.0960  260 ALA I CB  
17244 N N   . PHE I  261 ? 0.8180 0.8014 0.9075 0.1401  0.1018  0.0886  261 PHE I N   
17245 C CA  . PHE I  261 ? 0.6324 0.6186 0.7190 0.1378  0.0988  0.0857  261 PHE I CA  
17246 C C   . PHE I  261 ? 0.6331 0.6118 0.7232 0.1353  0.1023  0.0812  261 PHE I C   
17247 O O   . PHE I  261 ? 0.7144 0.6871 0.8043 0.1308  0.1012  0.0758  261 PHE I O   
17248 C CB  . PHE I  261 ? 0.5190 0.5090 0.5990 0.1334  0.0912  0.0817  261 PHE I CB  
17249 C CG  . PHE I  261 ? 0.5691 0.5667 0.6451 0.1353  0.0876  0.0855  261 PHE I CG  
17250 C CD1 . PHE I  261 ? 0.6234 0.6196 0.6989 0.1349  0.0868  0.0858  261 PHE I CD1 
17251 C CD2 . PHE I  261 ? 0.5485 0.5549 0.6212 0.1373  0.0852  0.0887  261 PHE I CD2 
17252 C CE1 . PHE I  261 ? 0.6125 0.6154 0.6838 0.1363  0.0838  0.0890  261 PHE I CE1 
17253 C CE2 . PHE I  261 ? 0.5563 0.5697 0.6248 0.1387  0.0820  0.0920  261 PHE I CE2 
17254 C CZ  . PHE I  261 ? 0.6585 0.6702 0.7263 0.1381  0.0813  0.0921  261 PHE I CZ  
17255 N N   . ALA I  262 ? 0.7998 0.7788 0.8930 0.1381  0.1066  0.0835  262 ALA I N   
17256 C CA  . ALA I  262 ? 0.7901 0.7627 0.8856 0.1354  0.1096  0.0790  262 ALA I CA  
17257 C C   . ALA I  262 ? 0.7791 0.7541 0.8686 0.1305  0.1033  0.0738  262 ALA I C   
17258 O O   . ALA I  262 ? 0.7741 0.7568 0.8598 0.1314  0.0994  0.0755  262 ALA I O   
17259 C CB  . ALA I  262 ? 0.8493 0.8224 0.9494 0.1398  0.1156  0.0831  262 ALA I CB  
17260 N N   . MET I  263 ? 0.6496 0.6183 0.7384 0.1251  0.1022  0.0675  263 MET I N   
17261 C CA  . MET I  263 ? 0.8116 0.7824 0.8944 0.1201  0.0955  0.0625  263 MET I CA  
17262 C C   . MET I  263 ? 0.8190 0.7831 0.9017 0.1149  0.0963  0.0562  263 MET I C   
17263 O O   . MET I  263 ? 0.9423 0.8990 1.0282 0.1129  0.0994  0.0536  263 MET I O   
17264 C CB  . MET I  263 ? 0.7653 0.7376 0.8450 0.1180  0.0902  0.0616  263 MET I CB  
17265 C CG  . MET I  263 ? 0.7777 0.7534 0.8513 0.1134  0.0829  0.0575  263 MET I CG  
17266 S SD  . MET I  263 ? 1.0746 1.0510 1.1458 0.1110  0.0776  0.0564  263 MET I SD  
17267 C CE  . MET I  263 ? 0.8698 0.8361 0.9458 0.1078  0.0810  0.0525  263 MET I CE  
17268 N N   . GLU I  264 ? 0.8161 0.7828 0.8950 0.1126  0.0934  0.0537  264 GLU I N   
17269 C CA  . GLU I  264 ? 0.9183 0.8795 0.9956 0.1071  0.0930  0.0473  264 GLU I CA  
17270 C C   . GLU I  264 ? 0.8137 0.7789 0.8845 0.1027  0.0850  0.0439  264 GLU I C   
17271 O O   . GLU I  264 ? 0.9343 0.9062 1.0015 0.1037  0.0817  0.0453  264 GLU I O   
17272 C CB  . GLU I  264 ? 0.9432 0.9030 1.0222 0.1081  0.0977  0.0472  264 GLU I CB  
17273 C CG  . GLU I  264 ? 1.2460 1.1965 1.3297 0.1068  0.1046  0.0446  264 GLU I CG  
17274 C CD  . GLU I  264 ? 1.4495 1.3989 1.5368 0.1099  0.1111  0.0466  264 GLU I CD  
17275 O OE1 . GLU I  264 ? 1.4115 1.3544 1.4997 0.1068  0.1149  0.0424  264 GLU I OE1 
17276 O OE2 . GLU I  264 ? 1.4287 1.3838 1.5179 0.1155  0.1124  0.0524  264 GLU I OE2 
17277 N N   . ARG I  265 ? 0.8965 0.8577 0.9660 0.0978  0.0821  0.0395  265 ARG I N   
17278 C CA  . ARG I  265 ? 1.0091 0.9739 1.0730 0.0938  0.0746  0.0367  265 ARG I CA  
17279 C C   . ARG I  265 ? 0.9761 0.9375 1.0369 0.0879  0.0725  0.0308  265 ARG I C   
17280 O O   . ARG I  265 ? 0.8434 0.7982 0.9064 0.0856  0.0764  0.0278  265 ARG I O   
17281 C CB  . ARG I  265 ? 0.7314 0.6957 0.7959 0.0930  0.0717  0.0369  265 ARG I CB  
17282 C CG  . ARG I  265 ? 0.7785 0.7354 0.8482 0.0922  0.0761  0.0358  265 ARG I CG  
17283 C CD  . ARG I  265 ? 0.9471 0.9046 1.0186 0.0934  0.0746  0.0378  265 ARG I CD  
17284 N NE  . ARG I  265 ? 0.9679 0.9206 1.0402 0.0884  0.0726  0.0337  265 ARG I NE  
17285 C CZ  . ARG I  265 ? 0.9946 0.9405 1.0715 0.0871  0.0768  0.0319  265 ARG I CZ  
17286 N NH1 . ARG I  265 ? 1.0423 0.9848 1.1232 0.0903  0.0837  0.0338  265 ARG I NH1 
17287 N NH2 . ARG I  265 ? 1.1040 1.0466 1.1815 0.0823  0.0743  0.0282  265 ARG I NH2 
17288 N N   . ASN I  266 ? 0.9005 0.8666 0.9558 0.0854  0.0664  0.0291  266 ASN I N   
17289 C CA  . ASN I  266 ? 1.0881 1.0517 1.1396 0.0794  0.0632  0.0237  266 ASN I CA  
17290 C C   . ASN I  266 ? 1.1800 1.1458 1.2284 0.0760  0.0563  0.0220  266 ASN I C   
17291 O O   . ASN I  266 ? 1.2664 1.2382 1.3124 0.0778  0.0525  0.0244  266 ASN I O   
17292 C CB  . ASN I  266 ? 1.1723 1.1392 1.2202 0.0793  0.0627  0.0230  266 ASN I CB  
17293 C CG  . ASN I  266 ? 1.1119 1.0860 1.1594 0.0846  0.0624  0.0280  266 ASN I CG  
17294 O OD1 . ASN I  266 ? 1.0068 0.9819 1.0561 0.0878  0.0667  0.0301  266 ASN I OD1 
17295 N ND2 . ASN I  266 ? 1.0620 1.0415 1.1073 0.0854  0.0576  0.0299  266 ASN I ND2 
17296 N N   . ALA I  267 ? 1.0581 1.0192 1.1066 0.0710  0.0549  0.0179  267 ALA I N   
17297 C CA  . ALA I  267 ? 1.2379 1.2004 1.2845 0.0677  0.0488  0.0166  267 ALA I CA  
17298 C C   . ALA I  267 ? 1.1462 1.1135 1.1869 0.0651  0.0429  0.0149  267 ALA I C   
17299 O O   . ALA I  267 ? 1.0300 0.9975 1.0677 0.0640  0.0434  0.0133  267 ALA I O   
17300 C CB  . ALA I  267 ? 1.2850 1.2415 1.3336 0.0629  0.0489  0.0128  267 ALA I CB  
17301 N N   . GLY I  268 ? 1.1825 1.1532 1.2216 0.0642  0.0376  0.0155  268 GLY I N   
17302 C CA  . GLY I  268 ? 1.2526 1.2270 1.2864 0.0610  0.0317  0.0136  268 GLY I CA  
17303 C C   . GLY I  268 ? 1.2301 1.2112 1.2605 0.0640  0.0297  0.0161  268 GLY I C   
17304 O O   . GLY I  268 ? 1.2185 1.2018 1.2449 0.0626  0.0281  0.0147  268 GLY I O   
17305 N N   . SER I  269 ? 0.9045 0.8890 0.9365 0.0678  0.0297  0.0198  269 SER I N   
17306 C CA  . SER I  269 ? 0.7852 0.7765 0.8137 0.0700  0.0269  0.0220  269 SER I CA  
17307 C C   . SER I  269 ? 0.7908 0.7843 0.8196 0.0701  0.0236  0.0233  269 SER I C   
17308 O O   . SER I  269 ? 0.9316 0.9217 0.9625 0.0675  0.0222  0.0218  269 SER I O   
17309 C CB  . SER I  269 ? 0.7399 0.7343 0.7695 0.0753  0.0311  0.0258  269 SER I CB  
17310 O OG  . SER I  269 ? 0.7370 0.7384 0.7628 0.0768  0.0281  0.0275  269 SER I OG  
17311 N N   . GLY I  270 ? 0.5217 0.5209 0.5485 0.0731  0.0226  0.0262  270 GLY I N   
17312 C CA  . GLY I  270 ? 0.6471 0.6485 0.6739 0.0732  0.0198  0.0274  270 GLY I CA  
17313 C C   . GLY I  270 ? 0.4571 0.4643 0.4825 0.0774  0.0204  0.0312  270 GLY I C   
17314 O O   . GLY I  270 ? 0.5107 0.5204 0.5361 0.0807  0.0234  0.0335  270 GLY I O   
17315 N N   . ILE I  271 ? 0.5598 0.5692 0.5841 0.0770  0.0177  0.0317  271 ILE I N   
17316 C CA  . ILE I  271 ? 0.4261 0.4411 0.4487 0.0803  0.0179  0.0351  271 ILE I CA  
17317 C C   . ILE I  271 ? 0.5116 0.5307 0.5297 0.0779  0.0132  0.0338  271 ILE I C   
17318 O O   . ILE I  271 ? 0.7682 0.7854 0.7868 0.0752  0.0106  0.0321  271 ILE I O   
17319 C CB  . ILE I  271 ? 0.4500 0.4631 0.4762 0.0827  0.0205  0.0376  271 ILE I CB  
17320 C CG1 . ILE I  271 ? 0.4628 0.4715 0.4936 0.0850  0.0256  0.0389  271 ILE I CG1 
17321 C CG2 . ILE I  271 ? 0.6176 0.6366 0.6413 0.0856  0.0206  0.0409  271 ILE I CG2 
17322 C CD1 . ILE I  271 ? 0.6347 0.6392 0.6700 0.0858  0.0279  0.0399  271 ILE I CD1 
17323 N N   . ILE I  272 ? 0.5417 0.5667 0.5559 0.0790  0.0121  0.0347  272 ILE I N   
17324 C CA  . ILE I  272 ? 0.5999 0.6291 0.6097 0.0768  0.0079  0.0334  272 ILE I CA  
17325 C C   . ILE I  272 ? 0.6007 0.6346 0.6089 0.0791  0.0081  0.0362  272 ILE I C   
17326 O O   . ILE I  272 ? 0.6436 0.6814 0.6512 0.0825  0.0104  0.0393  272 ILE I O   
17327 C CB  . ILE I  272 ? 0.5099 0.5429 0.5159 0.0759  0.0063  0.0323  272 ILE I CB  
17328 C CG1 . ILE I  272 ? 0.4931 0.5213 0.4998 0.0730  0.0058  0.0291  272 ILE I CG1 
17329 C CG2 . ILE I  272 ? 0.7238 0.7614 0.7253 0.0740  0.0023  0.0312  272 ILE I CG2 
17330 C CD1 . ILE I  272 ? 0.6926 0.7239 0.6954 0.0716  0.0039  0.0275  272 ILE I CD1 
17331 N N   . ILE I  273 ? 0.5354 0.5689 0.5429 0.0771  0.0058  0.0351  273 ILE I N   
17332 C CA  . ILE I  273 ? 0.6471 0.6850 0.6522 0.0785  0.0058  0.0371  273 ILE I CA  
17333 C C   . ILE I  273 ? 0.7259 0.7690 0.7258 0.0765  0.0024  0.0357  273 ILE I C   
17334 O O   . ILE I  273 ? 0.9703 1.0121 0.9692 0.0732  -0.0006 0.0331  273 ILE I O   
17335 C CB  . ILE I  273 ? 0.6157 0.6500 0.6233 0.0776  0.0060  0.0369  273 ILE I CB  
17336 C CG1 . ILE I  273 ? 0.7021 0.7311 0.7150 0.0796  0.0096  0.0384  273 ILE I CG1 
17337 C CG2 . ILE I  273 ? 0.7752 0.8139 0.7798 0.0786  0.0061  0.0386  273 ILE I CG2 
17338 C CD1 . ILE I  273 ? 0.9568 0.9801 0.9733 0.0774  0.0092  0.0359  273 ILE I CD1 
17339 N N   . SER I  274 ? 0.7746 0.8237 0.7715 0.0784  0.0028  0.0375  274 SER I N   
17340 C CA  . SER I  274 ? 0.7899 0.8443 0.7820 0.0766  -0.0002 0.0362  274 SER I CA  
17341 C C   . SER I  274 ? 0.9201 0.9819 0.9090 0.0792  0.0006  0.0391  274 SER I C   
17342 O O   . SER I  274 ? 0.8206 0.8840 0.8113 0.0827  0.0035  0.0424  274 SER I O   
17343 C CB  . SER I  274 ? 0.7163 0.7701 0.7079 0.0750  -0.0016 0.0340  274 SER I CB  
17344 O OG  . SER I  274 ? 0.8502 0.9100 0.8373 0.0743  -0.0037 0.0335  274 SER I OG  
17345 N N   . ASP I  275 ? 1.1298 1.1965 1.1142 0.0772  -0.0020 0.0379  275 ASP I N   
17346 C CA  . ASP I  275 ? 1.0414 1.1160 1.0223 0.0789  -0.0019 0.0404  275 ASP I CA  
17347 C C   . ASP I  275 ? 0.9140 0.9928 0.8937 0.0794  -0.0027 0.0404  275 ASP I C   
17348 O O   . ASP I  275 ? 1.2335 1.3188 1.2118 0.0817  -0.0019 0.0432  275 ASP I O   
17349 C CB  . ASP I  275 ? 1.3544 1.4322 1.3309 0.0763  -0.0041 0.0388  275 ASP I CB  
17350 C CG  . ASP I  275 ? 1.5754 1.6491 1.5531 0.0758  -0.0030 0.0388  275 ASP I CG  
17351 O OD1 . ASP I  275 ? 1.7074 1.7765 1.6861 0.0730  -0.0045 0.0359  275 ASP I OD1 
17352 O OD2 . ASP I  275 ? 1.4295 1.5049 1.4074 0.0783  -0.0007 0.0417  275 ASP I OD2 
17353 N N   . THR I  276 ? 0.7631 0.8381 0.7433 0.0771  -0.0042 0.0374  276 THR I N   
17354 C CA  . THR I  276 ? 0.8142 0.8924 0.7933 0.0769  -0.0050 0.0368  276 THR I CA  
17355 C C   . THR I  276 ? 0.8245 0.9064 0.8055 0.0809  -0.0022 0.0405  276 THR I C   
17356 O O   . THR I  276 ? 0.7923 0.8709 0.7771 0.0836  0.0009  0.0427  276 THR I O   
17357 C CB  . THR I  276 ? 0.7158 0.7877 0.6964 0.0745  -0.0059 0.0335  276 THR I CB  
17358 O OG1 . THR I  276 ? 0.7315 0.8005 0.7105 0.0707  -0.0088 0.0304  276 THR I OG1 
17359 C CG2 . THR I  276 ? 0.7172 0.7921 0.6964 0.0742  -0.0065 0.0327  276 THR I CG2 
17360 N N   . PRO I  277 ? 0.9640 1.0528 0.9426 0.0814  -0.0031 0.0414  277 PRO I N   
17361 C CA  . PRO I  277 ? 0.9161 1.0096 0.8966 0.0852  -0.0007 0.0452  277 PRO I CA  
17362 C C   . PRO I  277 ? 0.8249 0.9131 0.8098 0.0867  0.0020  0.0453  277 PRO I C   
17363 O O   . PRO I  277 ? 0.8546 0.9387 0.8393 0.0842  0.0010  0.0419  277 PRO I O   
17364 C CB  . PRO I  277 ? 0.9122 1.0131 0.8890 0.0841  -0.0031 0.0447  277 PRO I CB  
17365 C CG  . PRO I  277 ? 1.0912 1.1932 1.0636 0.0805  -0.0063 0.0419  277 PRO I CG  
17366 C CD  . PRO I  277 ? 0.9078 1.0010 0.8816 0.0783  -0.0066 0.0390  277 PRO I CD  
17367 N N   . VAL I  278 ? 0.8695 0.9579 0.8582 0.0907  0.0057  0.0492  278 VAL I N   
17368 C CA  . VAL I  278 ? 0.8235 0.9078 0.8165 0.0925  0.0089  0.0497  278 VAL I CA  
17369 C C   . VAL I  278 ? 0.8625 0.9527 0.8550 0.0934  0.0087  0.0506  278 VAL I C   
17370 O O   . VAL I  278 ? 1.0098 1.1083 1.0004 0.0947  0.0076  0.0532  278 VAL I O   
17371 C CB  . VAL I  278 ? 0.8374 0.9200 0.8351 0.0967  0.0132  0.0539  278 VAL I CB  
17372 C CG1 . VAL I  278 ? 1.0853 1.1765 1.0823 0.1000  0.0136  0.0588  278 VAL I CG1 
17373 C CG2 . VAL I  278 ? 0.6369 0.7154 0.6391 0.0985  0.0169  0.0543  278 VAL I CG2 
17374 N N   . HIS I  279 ? 0.9223 1.0085 0.9165 0.0925  0.0099  0.0484  279 HIS I N   
17375 C CA  . HIS I  279 ? 0.9306 1.0217 0.9243 0.0928  0.0097  0.0486  279 HIS I CA  
17376 C C   . HIS I  279 ? 0.9531 1.0405 0.9514 0.0949  0.0140  0.0495  279 HIS I C   
17377 O O   . HIS I  279 ? 1.1007 1.1804 1.1018 0.0948  0.0165  0.0483  279 HIS I O   
17378 C CB  . HIS I  279 ? 1.0499 1.1409 1.0390 0.0882  0.0057  0.0439  279 HIS I CB  
17379 C CG  . HIS I  279 ? 1.1283 1.2276 1.1131 0.0873  0.0023  0.0444  279 HIS I CG  
17380 N ND1 . HIS I  279 ? 1.1067 1.2123 1.0904 0.0873  0.0015  0.0447  279 HIS I ND1 
17381 C CD2 . HIS I  279 ? 1.2065 1.3089 1.1881 0.0861  -0.0003 0.0444  279 HIS I CD2 
17382 C CE1 . HIS I  279 ? 1.3657 1.4780 1.3455 0.0862  -0.0016 0.0450  279 HIS I CE1 
17383 N NE2 . HIS I  279 ? 1.2440 1.3545 1.2224 0.0854  -0.0026 0.0447  279 HIS I NE2 
17384 N N   . ASP I  280 ? 1.0338 1.1270 1.0332 0.0968  0.0149  0.0515  280 ASP I N   
17385 C CA  . ASP I  280 ? 1.2131 1.3034 1.2170 0.0988  0.0192  0.0523  280 ASP I CA  
17386 C C   . ASP I  280 ? 1.1367 1.2242 1.1384 0.0951  0.0180  0.0476  280 ASP I C   
17387 O O   . ASP I  280 ? 1.4079 1.5007 1.4090 0.0953  0.0175  0.0481  280 ASP I O   
17388 C CB  . ASP I  280 ? 1.4620 1.5604 1.4693 0.1034  0.0215  0.0580  280 ASP I CB  
17389 C CG  . ASP I  280 ? 1.5610 1.6586 1.5719 0.1048  0.0249  0.0582  280 ASP I CG  
17390 O OD1 . ASP I  280 ? 1.4155 1.5048 1.4287 0.1039  0.0280  0.0558  280 ASP I OD1 
17391 O OD2 . ASP I  280 ? 1.5797 1.6853 1.5915 0.1066  0.0247  0.0610  280 ASP I OD2 
17392 N N   . CYS I  281 ? 1.0352 1.1144 1.0354 0.0916  0.0174  0.0432  281 CYS I N   
17393 C CA  . CYS I  281 ? 1.0506 1.1260 1.0485 0.0879  0.0165  0.0386  281 CYS I CA  
17394 C C   . CYS I  281 ? 0.9283 0.9937 0.9275 0.0857  0.0185  0.0355  281 CYS I C   
17395 O O   . CYS I  281 ? 1.0409 1.1026 1.0435 0.0877  0.0212  0.0371  281 CYS I O   
17396 C CB  . CYS I  281 ? 0.9344 1.0130 0.9264 0.0840  0.0110  0.0356  281 CYS I CB  
17397 S SG  . CYS I  281 ? 1.4384 1.5102 1.4270 0.0793  0.0074  0.0313  281 CYS I SG  
17398 N N   . ASN I  282 ? 0.9058 0.9671 0.9020 0.0815  0.0170  0.0309  282 ASN I N   
17399 C CA  . ASN I  282 ? 0.8036 0.8558 0.8005 0.0789  0.0186  0.0276  282 ASN I CA  
17400 C C   . ASN I  282 ? 0.9389 0.9878 0.9313 0.0739  0.0139  0.0235  282 ASN I C   
17401 O O   . ASN I  282 ? 1.0125 1.0653 1.0007 0.0717  0.0099  0.0220  282 ASN I O   
17402 C CB  . ASN I  282 ? 0.9384 0.9871 0.9365 0.0783  0.0222  0.0258  282 ASN I CB  
17403 C CG  . ASN I  282 ? 1.1498 1.1924 1.1530 0.0804  0.0279  0.0268  282 ASN I CG  
17404 O OD1 . ASN I  282 ? 1.1853 1.2249 1.1907 0.0814  0.0287  0.0279  282 ASN I OD1 
17405 N ND2 . ASN I  282 ? 1.3802 1.4208 1.3855 0.0811  0.0321  0.0264  282 ASN I ND2 
17406 N N   . THR I  283 ? 0.8263 0.8682 0.8198 0.0722  0.0146  0.0217  283 THR I N   
17407 C CA  . THR I  283 ? 0.7529 0.7912 0.7430 0.0674  0.0104  0.0180  283 THR I CA  
17408 C C   . THR I  283 ? 0.6587 0.6888 0.6508 0.0653  0.0125  0.0156  283 THR I C   
17409 O O   . THR I  283 ? 0.6983 0.7255 0.6947 0.0679  0.0169  0.0173  283 THR I O   
17410 C CB  . THR I  283 ? 0.7325 0.7738 0.7216 0.0675  0.0068  0.0192  283 THR I CB  
17411 O OG1 . THR I  283 ? 0.5865 0.6253 0.5721 0.0628  0.0025  0.0158  283 THR I OG1 
17412 C CG2 . THR I  283 ? 0.6908 0.7293 0.6842 0.0700  0.0092  0.0215  283 THR I CG2 
17413 N N   . THR I  284 ? 0.6479 0.6743 0.6367 0.0604  0.0094  0.0118  284 THR I N   
17414 C CA  . THR I  284 ? 0.7280 0.7469 0.7180 0.0575  0.0106  0.0093  284 THR I CA  
17415 C C   . THR I  284 ? 0.6224 0.6398 0.6124 0.0555  0.0070  0.0088  284 THR I C   
17416 O O   . THR I  284 ? 0.4786 0.4905 0.4704 0.0536  0.0077  0.0073  284 THR I O   
17417 C CB  . THR I  284 ? 0.6504 0.6658 0.6368 0.0530  0.0100  0.0051  284 THR I CB  
17418 O OG1 . THR I  284 ? 0.6201 0.6284 0.6080 0.0504  0.0119  0.0028  284 THR I OG1 
17419 C CG2 . THR I  284 ? 0.7356 0.7532 0.7170 0.0492  0.0041  0.0031  284 THR I CG2 
17420 N N   . CYS I  285 ? 0.5612 0.5837 0.5493 0.0559  0.0032  0.0100  285 CYS I N   
17421 C CA  . CYS I  285 ? 0.4239 0.4456 0.4125 0.0544  -0.0001 0.0100  285 CYS I CA  
17422 C C   . CYS I  285 ? 0.4542 0.4815 0.4432 0.0578  -0.0010 0.0132  285 CYS I C   
17423 O O   . CYS I  285 ? 0.5503 0.5830 0.5365 0.0584  -0.0027 0.0138  285 CYS I O   
17424 C CB  . CYS I  285 ? 0.4648 0.4856 0.4493 0.0495  -0.0049 0.0068  285 CYS I CB  
17425 S SG  . CYS I  285 ? 0.7856 0.8057 0.7710 0.0475  -0.0091 0.0069  285 CYS I SG  
17426 N N   . GLN I  286 ? 0.4567 0.4826 0.4493 0.0597  0.0001  0.0151  286 GLN I N   
17427 C CA  . GLN I  286 ? 0.4754 0.5062 0.4683 0.0627  -0.0004 0.0181  286 GLN I CA  
17428 C C   . GLN I  286 ? 0.4927 0.5226 0.4857 0.0607  -0.0037 0.0176  286 GLN I C   
17429 O O   . GLN I  286 ? 0.4831 0.5080 0.4787 0.0591  -0.0036 0.0166  286 GLN I O   
17430 C CB  . GLN I  286 ? 0.4041 0.4349 0.4012 0.0672  0.0042  0.0215  286 GLN I CB  
17431 C CG  . GLN I  286 ? 0.3715 0.4086 0.3682 0.0708  0.0043  0.0250  286 GLN I CG  
17432 C CD  . GLN I  286 ? 0.5584 0.6019 0.5515 0.0712  0.0030  0.0254  286 GLN I CD  
17433 O OE1 . GLN I  286 ? 0.5769 0.6211 0.5704 0.0723  0.0051  0.0256  286 GLN I OE1 
17434 N NE2 . GLN I  286 ? 0.5033 0.5513 0.4932 0.0703  -0.0004 0.0254  286 GLN I NE2 
17435 N N   . THR I  287 ? 0.4765 0.5113 0.4668 0.0607  -0.0064 0.0183  287 THR I N   
17436 C CA  . THR I  287 ? 0.4296 0.4642 0.4204 0.0597  -0.0087 0.0185  287 THR I CA  
17437 C C   . THR I  287 ? 0.4318 0.4709 0.4229 0.0634  -0.0072 0.0217  287 THR I C   
17438 O O   . THR I  287 ? 0.6344 0.6776 0.6248 0.0663  -0.0053 0.0236  287 THR I O   
17439 C CB  . THR I  287 ? 0.5276 0.5636 0.5146 0.0560  -0.0132 0.0162  287 THR I CB  
17440 O OG1 . THR I  287 ? 0.4901 0.5324 0.4740 0.0572  -0.0141 0.0172  287 THR I OG1 
17441 C CG2 . THR I  287 ? 0.4219 0.4558 0.4069 0.0528  -0.0145 0.0133  287 THR I CG2 
17442 N N   . PRO I  288 ? 0.5065 0.5449 0.4989 0.0633  -0.0080 0.0223  288 PRO I N   
17443 C CA  . PRO I  288 ? 0.5774 0.6201 0.5694 0.0661  -0.0070 0.0250  288 PRO I CA  
17444 C C   . PRO I  288 ? 0.6205 0.6694 0.6078 0.0654  -0.0093 0.0248  288 PRO I C   
17445 O O   . PRO I  288 ? 0.6478 0.7014 0.6340 0.0678  -0.0083 0.0271  288 PRO I O   
17446 C CB  . PRO I  288 ? 0.6211 0.6604 0.6157 0.0651  -0.0075 0.0249  288 PRO I CB  
17447 C CG  . PRO I  288 ? 0.4880 0.5209 0.4859 0.0632  -0.0075 0.0232  288 PRO I CG  
17448 C CD  . PRO I  288 ? 0.5099 0.5428 0.5052 0.0608  -0.0091 0.0209  288 PRO I CD  
17449 N N   . LYS I  289 ? 0.5047 0.5538 0.4892 0.0622  -0.0124 0.0221  289 LYS I N   
17450 C CA  . LYS I  289 ? 0.5538 0.6087 0.5338 0.0613  -0.0145 0.0216  289 LYS I CA  
17451 C C   . LYS I  289 ? 0.5995 0.6586 0.5776 0.0626  -0.0138 0.0221  289 LYS I C   
17452 O O   . LYS I  289 ? 0.6839 0.7490 0.6589 0.0632  -0.0144 0.0228  289 LYS I O   
17453 C CB  . LYS I  289 ? 0.6425 0.6959 0.6205 0.0572  -0.0181 0.0187  289 LYS I CB  
17454 C CG  . LYS I  289 ? 0.8408 0.8887 0.8219 0.0554  -0.0190 0.0179  289 LYS I CG  
17455 C CD  . LYS I  289 ? 0.7408 0.7885 0.7199 0.0517  -0.0225 0.0157  289 LYS I CD  
17456 C CE  . LYS I  289 ? 0.9485 0.9990 0.9234 0.0500  -0.0243 0.0140  289 LYS I CE  
17457 N NZ  . LYS I  289 ? 1.0668 1.1173 1.0397 0.0466  -0.0276 0.0120  289 LYS I NZ  
17458 N N   . GLY I  290 ? 0.4707 0.5264 0.4506 0.0628  -0.0122 0.0216  290 GLY I N   
17459 C CA  . GLY I  290 ? 0.5472 0.6060 0.5258 0.0638  -0.0112 0.0218  290 GLY I CA  
17460 C C   . GLY I  290 ? 0.5740 0.6273 0.5539 0.0624  -0.0103 0.0198  290 GLY I C   
17461 O O   . GLY I  290 ? 0.5710 0.6187 0.5523 0.0601  -0.0111 0.0180  290 GLY I O   
17462 N N   . ALA I  291 ? 0.6493 0.7043 0.6290 0.0636  -0.0085 0.0201  291 ALA I N   
17463 C CA  . ALA I  291 ? 0.5339 0.5836 0.5146 0.0622  -0.0070 0.0181  291 ALA I CA  
17464 C C   . ALA I  291 ? 0.5956 0.6443 0.5725 0.0579  -0.0102 0.0146  291 ALA I C   
17465 O O   . ALA I  291 ? 0.6062 0.6591 0.5797 0.0567  -0.0130 0.0140  291 ALA I O   
17466 C CB  . ALA I  291 ? 0.4038 0.4555 0.3864 0.0655  -0.0031 0.0200  291 ALA I CB  
17467 N N   . ILE I  292 ? 0.5197 0.5626 0.4970 0.0555  -0.0097 0.0122  292 ILE I N   
17468 C CA  . ILE I  292 ? 0.6420 0.6835 0.6156 0.0512  -0.0125 0.0089  292 ILE I CA  
17469 C C   . ILE I  292 ? 0.7397 0.7795 0.7127 0.0509  -0.0100 0.0076  292 ILE I C   
17470 O O   . ILE I  292 ? 0.6527 0.6875 0.6281 0.0509  -0.0071 0.0070  292 ILE I O   
17471 C CB  . ILE I  292 ? 0.5859 0.6220 0.5596 0.0475  -0.0150 0.0068  292 ILE I CB  
17472 C CG1 . ILE I  292 ? 0.4653 0.5031 0.4397 0.0476  -0.0175 0.0080  292 ILE I CG1 
17473 C CG2 . ILE I  292 ? 0.6588 0.6935 0.6284 0.0431  -0.0178 0.0037  292 ILE I CG2 
17474 C CD1 . ILE I  292 ? 0.6382 0.6713 0.6133 0.0441  -0.0202 0.0064  292 ILE I CD1 
17475 N N   . ASN I  293 ? 1.0571 1.1009 1.0269 0.0505  -0.0108 0.0070  293 ASN I N   
17476 C CA  . ASN I  293 ? 1.2583 1.3007 1.2272 0.0498  -0.0086 0.0055  293 ASN I CA  
17477 C C   . ASN I  293 ? 1.2599 1.2996 1.2243 0.0448  -0.0117 0.0018  293 ASN I C   
17478 O O   . ASN I  293 ? 1.2961 1.3396 1.2571 0.0435  -0.0142 0.0010  293 ASN I O   
17479 C CB  . ASN I  293 ? 1.4842 1.5332 1.4529 0.0528  -0.0072 0.0074  293 ASN I CB  
17480 C CG  . ASN I  293 ? 1.5742 1.6219 1.5422 0.0524  -0.0045 0.0060  293 ASN I CG  
17481 O OD1 . ASN I  293 ? 1.4279 1.4695 1.3960 0.0501  -0.0029 0.0037  293 ASN I OD1 
17482 N ND2 . ASN I  293 ? 1.4975 1.5511 1.4651 0.0544  -0.0038 0.0074  293 ASN I ND2 
17483 N N   . THR I  294 ? 1.1174 1.1508 1.0819 0.0418  -0.0117 -0.0003 294 THR I N   
17484 C CA  . THR I  294 ? 1.2164 1.2474 1.1768 0.0369  -0.0153 -0.0034 294 THR I CA  
17485 C C   . THR I  294 ? 1.0577 1.0824 1.0171 0.0336  -0.0138 -0.0062 294 THR I C   
17486 O O   . THR I  294 ? 1.0547 1.0758 1.0174 0.0347  -0.0103 -0.0060 294 THR I O   
17487 C CB  . THR I  294 ? 1.1309 1.1615 1.0914 0.0351  -0.0193 -0.0032 294 THR I CB  
17488 O OG1 . THR I  294 ? 0.7874 0.8171 0.7437 0.0307  -0.0231 -0.0056 294 THR I OG1 
17489 C CG2 . THR I  294 ? 0.8802 0.9059 0.8444 0.0349  -0.0182 -0.0030 294 THR I CG2 
17490 N N   . SER I  295 ? 0.8845 0.9081 0.8393 0.0294  -0.0164 -0.0089 295 SER I N   
17491 C CA  . SER I  295 ? 0.9342 0.9520 0.8871 0.0253  -0.0158 -0.0119 295 SER I CA  
17492 C C   . SER I  295 ? 0.7663 0.7822 0.7175 0.0211  -0.0206 -0.0130 295 SER I C   
17493 O O   . SER I  295 ? 0.7750 0.7862 0.7252 0.0175  -0.0208 -0.0151 295 SER I O   
17494 C CB  . SER I  295 ? 0.8512 0.8690 0.7998 0.0234  -0.0148 -0.0141 295 SER I CB  
17495 O OG  . SER I  295 ? 1.3230 1.3374 1.2730 0.0242  -0.0097 -0.0150 295 SER I OG  
17496 N N   . LEU I  296 ? 0.6058 0.6256 0.5567 0.0216  -0.0243 -0.0115 296 LEU I N   
17497 C CA  . LEU I  296 ? 0.5704 0.5890 0.5202 0.0180  -0.0289 -0.0121 296 LEU I CA  
17498 C C   . LEU I  296 ? 0.6601 0.6750 0.6138 0.0174  -0.0289 -0.0116 296 LEU I C   
17499 O O   . LEU I  296 ? 0.6375 0.6521 0.5954 0.0209  -0.0259 -0.0100 296 LEU I O   
17500 C CB  . LEU I  296 ? 0.6143 0.6377 0.5637 0.0192  -0.0320 -0.0104 296 LEU I CB  
17501 C CG  . LEU I  296 ? 0.6534 0.6809 0.5991 0.0196  -0.0323 -0.0108 296 LEU I CG  
17502 C CD1 . LEU I  296 ? 0.6287 0.6604 0.5741 0.0202  -0.0354 -0.0094 296 LEU I CD1 
17503 C CD2 . LEU I  296 ? 0.5377 0.5630 0.4784 0.0154  -0.0334 -0.0136 296 LEU I CD2 
17504 N N   . PRO I  297 ? 0.6423 0.6545 0.5945 0.0130  -0.0322 -0.0130 297 PRO I N   
17505 C CA  . PRO I  297 ? 0.5070 0.5156 0.4628 0.0116  -0.0325 -0.0129 297 PRO I CA  
17506 C C   . PRO I  297 ? 0.5858 0.5963 0.5462 0.0139  -0.0341 -0.0102 297 PRO I C   
17507 O O   . PRO I  297 ? 0.4725 0.4805 0.4371 0.0143  -0.0332 -0.0096 297 PRO I O   
17508 C CB  . PRO I  297 ? 0.5493 0.5560 0.5015 0.0059  -0.0364 -0.0149 297 PRO I CB  
17509 C CG  . PRO I  297 ? 0.6615 0.6695 0.6079 0.0044  -0.0367 -0.0165 297 PRO I CG  
17510 C CD  . PRO I  297 ? 0.6259 0.6384 0.5730 0.0087  -0.0357 -0.0147 297 PRO I CD  
17511 N N   . PHE I  298 ? 0.5623 0.5769 0.5220 0.0153  -0.0363 -0.0088 298 PHE I N   
17512 C CA  . PHE I  298 ? 0.5902 0.6063 0.5539 0.0170  -0.0378 -0.0065 298 PHE I CA  
17513 C C   . PHE I  298 ? 0.5763 0.5968 0.5404 0.0211  -0.0367 -0.0046 298 PHE I C   
17514 O O   . PHE I  298 ? 0.6104 0.6338 0.5709 0.0216  -0.0366 -0.0051 298 PHE I O   
17515 C CB  . PHE I  298 ? 0.5105 0.5266 0.4734 0.0133  -0.0427 -0.0065 298 PHE I CB  
17516 C CG  . PHE I  298 ? 0.6050 0.6177 0.5660 0.0085  -0.0445 -0.0085 298 PHE I CG  
17517 C CD1 . PHE I  298 ? 0.4779 0.4873 0.4423 0.0072  -0.0442 -0.0086 298 PHE I CD1 
17518 C CD2 . PHE I  298 ? 0.5697 0.5827 0.5252 0.0052  -0.0466 -0.0103 298 PHE I CD2 
17519 C CE1 . PHE I  298 ? 0.5644 0.5710 0.5268 0.0024  -0.0461 -0.0105 298 PHE I CE1 
17520 C CE2 . PHE I  298 ? 0.5324 0.5425 0.4856 0.0005  -0.0483 -0.0120 298 PHE I CE2 
17521 C CZ  . PHE I  298 ? 0.5061 0.5131 0.4626 -0.0009 -0.0481 -0.0122 298 PHE I CZ  
17522 N N   . GLN I  299 ? 0.5358 0.5568 0.5043 0.0239  -0.0358 -0.0025 299 GLN I N   
17523 C CA  . GLN I  299 ? 0.5216 0.5469 0.4906 0.0275  -0.0349 -0.0006 299 GLN I CA  
17524 C C   . GLN I  299 ? 0.4669 0.4924 0.4392 0.0278  -0.0366 0.0010  299 GLN I C   
17525 O O   . GLN I  299 ? 2.7614 2.7838 2.7375 0.0270  -0.0369 0.0014  299 GLN I O   
17526 C CB  . GLN I  299 ? 0.4803 0.5062 0.4511 0.0317  -0.0304 0.0006  299 GLN I CB  
17527 C CG  . GLN I  299 ? 0.4509 0.4730 0.4265 0.0328  -0.0281 0.0014  299 GLN I CG  
17528 C CD  . GLN I  299 ? 0.5900 0.6131 0.5694 0.0352  -0.0278 0.0037  299 GLN I CD  
17529 O OE1 . GLN I  299 ? 0.6430 0.6699 0.6214 0.0365  -0.0289 0.0048  299 GLN I OE1 
17530 N NE2 . GLN I  299 ? 0.5908 0.6104 0.5746 0.0358  -0.0263 0.0044  299 GLN I NE2 
17531 N N   . ASN I  300 ? 0.5148 0.5441 0.4859 0.0289  -0.0376 0.0018  300 ASN I N   
17532 C CA  . ASN I  300 ? 0.4860 0.5157 0.4602 0.0293  -0.0388 0.0033  300 ASN I CA  
17533 C C   . ASN I  300 ? 0.4893 0.5221 0.4644 0.0332  -0.0363 0.0050  300 ASN I C   
17534 O O   . ASN I  300 ? 0.6084 0.6427 0.5846 0.0336  -0.0370 0.0060  300 ASN I O   
17535 C CB  . ASN I  300 ? 0.3533 0.3842 0.3253 0.0264  -0.0424 0.0026  300 ASN I CB  
17536 C CG  . ASN I  300 ? 0.4621 0.4973 0.4296 0.0270  -0.0424 0.0020  300 ASN I CG  
17537 O OD1 . ASN I  300 ? 0.6233 0.6607 0.5889 0.0292  -0.0401 0.0020  300 ASN I OD1 
17538 N ND2 . ASN I  300 ? 0.5247 0.5612 0.4907 0.0250  -0.0449 0.0017  300 ASN I ND2 
17539 N N   . ILE I  301 ? 0.3966 0.4304 0.3714 0.0360  -0.0332 0.0056  301 ILE I N   
17540 C CA  . ILE I  301 ? 0.5529 0.5903 0.5282 0.0397  -0.0307 0.0075  301 ILE I CA  
17541 C C   . ILE I  301 ? 0.5056 0.5409 0.4856 0.0416  -0.0291 0.0093  301 ILE I C   
17542 O O   . ILE I  301 ? 0.6538 0.6909 0.6345 0.0426  -0.0291 0.0104  301 ILE I O   
17543 C CB  . ILE I  301 ? 0.5627 0.6021 0.5366 0.0422  -0.0279 0.0079  301 ILE I CB  
17544 C CG1 . ILE I  301 ? 0.4433 0.4857 0.4126 0.0408  -0.0292 0.0064  301 ILE I CG1 
17545 C CG2 . ILE I  301 ? 0.5229 0.5658 0.4981 0.0462  -0.0252 0.0104  301 ILE I CG2 
17546 C CD1 . ILE I  301 ? 0.6791 0.7235 0.6474 0.0431  -0.0264 0.0068  301 ILE I CD1 
17547 N N   . HIS I  302 ? 0.4065 0.4379 0.3896 0.0420  -0.0274 0.0094  302 HIS I N   
17548 C CA  . HIS I  302 ? 0.5261 0.5552 0.5139 0.0439  -0.0255 0.0111  302 HIS I CA  
17549 C C   . HIS I  302 ? 0.5557 0.5796 0.5469 0.0424  -0.0251 0.0104  302 HIS I C   
17550 O O   . HIS I  302 ? 0.5305 0.5528 0.5206 0.0416  -0.0243 0.0091  302 HIS I O   
17551 C CB  . HIS I  302 ? 0.4979 0.5296 0.4861 0.0482  -0.0218 0.0133  302 HIS I CB  
17552 C CG  . HIS I  302 ? 0.5935 0.6244 0.5853 0.0504  -0.0200 0.0153  302 HIS I CG  
17553 N ND1 . HIS I  302 ? 0.3984 0.4251 0.3949 0.0512  -0.0180 0.0160  302 HIS I ND1 
17554 C CD2 . HIS I  302 ? 0.6863 0.7200 0.6778 0.0518  -0.0198 0.0167  302 HIS I CD2 
17555 C CE1 . HIS I  302 ? 0.4901 0.5170 0.4890 0.0532  -0.0167 0.0178  302 HIS I CE1 
17556 N NE2 . HIS I  302 ? 0.5949 0.6260 0.5907 0.0535  -0.0177 0.0182  302 HIS I NE2 
17557 N N   . PRO I  303 ? 0.4704 0.4916 0.4659 0.0419  -0.0256 0.0111  303 PRO I N   
17558 C CA  . PRO I  303 ? 0.3742 0.3908 0.3736 0.0403  -0.0254 0.0105  303 PRO I CA  
17559 C C   . PRO I  303 ? 0.5054 0.5200 0.5070 0.0430  -0.0211 0.0113  303 PRO I C   
17560 O O   . PRO I  303 ? 0.4148 0.4263 0.4169 0.0416  -0.0203 0.0099  303 PRO I O   
17561 C CB  . PRO I  303 ? 0.3573 0.3727 0.3610 0.0399  -0.0265 0.0117  303 PRO I CB  
17562 C CG  . PRO I  303 ? 0.6668 0.6859 0.6681 0.0400  -0.0282 0.0121  303 PRO I CG  
17563 C CD  . PRO I  303 ? 0.5132 0.5359 0.5101 0.0425  -0.0264 0.0124  303 PRO I CD  
17564 N N   . ILE I  304 ? 0.5487 0.5650 0.5515 0.0469  -0.0183 0.0135  304 ILE I N   
17565 C CA  . ILE I  304 ? 0.4714 0.4861 0.4766 0.0500  -0.0140 0.0148  304 ILE I CA  
17566 C C   . ILE I  304 ? 0.5275 0.5443 0.5293 0.0513  -0.0122 0.0145  304 ILE I C   
17567 O O   . ILE I  304 ? 0.6786 0.7000 0.6769 0.0527  -0.0127 0.0152  304 ILE I O   
17568 C CB  . ILE I  304 ? 0.3756 0.3916 0.3831 0.0537  -0.0115 0.0175  304 ILE I CB  
17569 C CG1 . ILE I  304 ? 0.4015 0.4141 0.4140 0.0528  -0.0119 0.0179  304 ILE I CG1 
17570 C CG2 . ILE I  304 ? 0.6564 0.6722 0.6651 0.0574  -0.0070 0.0192  304 ILE I CG2 
17571 C CD1 . ILE I  304 ? 0.7297 0.7427 0.7419 0.0496  -0.0160 0.0169  304 ILE I CD1 
17572 N N   . THR I  305 ? 0.4309 0.4442 0.4338 0.0508  -0.0101 0.0134  305 THR I N   
17573 C CA  . THR I  305 ? 0.3834 0.3979 0.3834 0.0515  -0.0084 0.0128  305 THR I CA  
17574 C C   . THR I  305 ? 0.6281 0.6391 0.6313 0.0535  -0.0037 0.0133  305 THR I C   
17575 O O   . THR I  305 ? 0.4949 0.5014 0.5018 0.0528  -0.0025 0.0129  305 THR I O   
17576 C CB  . THR I  305 ? 0.5263 0.5399 0.5227 0.0472  -0.0116 0.0097  305 THR I CB  
17577 O OG1 . THR I  305 ? 0.8272 0.8450 0.8193 0.0479  -0.0120 0.0095  305 THR I OG1 
17578 C CG2 . THR I  305 ? 0.5258 0.5343 0.5234 0.0451  -0.0097 0.0076  305 THR I CG2 
17579 N N   . ILE I  306 ? 0.6130 0.6260 0.6150 0.0561  -0.0009 0.0142  306 ILE I N   
17580 C CA  . ILE I  306 ? 0.5833 0.5929 0.5883 0.0580  0.0040  0.0146  306 ILE I CA  
17581 C C   . ILE I  306 ? 0.4991 0.5085 0.5015 0.0571  0.0053  0.0129  306 ILE I C   
17582 O O   . ILE I  306 ? 0.4846 0.4986 0.4837 0.0579  0.0043  0.0133  306 ILE I O   
17583 C CB  . ILE I  306 ? 0.4248 0.4367 0.4326 0.0633  0.0077  0.0186  306 ILE I CB  
17584 C CG1 . ILE I  306 ? 0.5376 0.5499 0.5475 0.0643  0.0066  0.0203  306 ILE I CG1 
17585 C CG2 . ILE I  306 ? 0.3200 0.3277 0.3316 0.0653  0.0131  0.0192  306 ILE I CG2 
17586 C CD1 . ILE I  306 ? 0.5290 0.5430 0.5418 0.0692  0.0104  0.0242  306 ILE I CD1 
17587 N N   . GLY I  307 ? 0.5563 0.5603 0.5602 0.0552  0.0078  0.0108  307 GLY I N   
17588 C CA  . GLY I  307 ? 0.5367 0.5395 0.5384 0.0541  0.0097  0.0089  307 GLY I CA  
17589 C C   . GLY I  307 ? 0.5687 0.5682 0.5672 0.0484  0.0068  0.0048  307 GLY I C   
17590 O O   . GLY I  307 ? 0.7008 0.6971 0.7003 0.0453  0.0048  0.0033  307 GLY I O   
17591 N N   . LYS I  308 ? 0.5930 0.5935 0.5877 0.0470  0.0067  0.0031  308 LYS I N   
17592 C CA  . LYS I  308 ? 0.5754 0.5735 0.5661 0.0415  0.0038  -0.0007 308 LYS I CA  
17593 C C   . LYS I  308 ? 0.5585 0.5612 0.5449 0.0400  -0.0016 -0.0009 308 LYS I C   
17594 O O   . LYS I  308 ? 0.7202 0.7261 0.7034 0.0404  -0.0018 -0.0011 308 LYS I O   
17595 C CB  . LYS I  308 ? 0.5821 0.5778 0.5710 0.0405  0.0073  -0.0028 308 LYS I CB  
17596 C CG  . LYS I  308 ? 0.7558 0.7446 0.7458 0.0373  0.0101  -0.0057 308 LYS I CG  
17597 C CD  . LYS I  308 ? 0.8631 0.8492 0.8573 0.0410  0.0168  -0.0045 308 LYS I CD  
17598 C CE  . LYS I  308 ? 0.9966 0.9757 0.9909 0.0373  0.0201  -0.0080 308 LYS I CE  
17599 N NZ  . LYS I  308 ? 1.2427 1.2186 1.2422 0.0409  0.0270  -0.0065 308 LYS I NZ  
17600 N N   . CYS I  309 ? 0.5235 0.5267 0.5103 0.0382  -0.0057 -0.0007 309 CYS I N   
17601 C CA  . CYS I  309 ? 0.6324 0.6402 0.6161 0.0374  -0.0102 -0.0003 309 CYS I CA  
17602 C C   . CYS I  309 ? 0.5849 0.5914 0.5652 0.0321  -0.0148 -0.0029 309 CYS I C   
17603 O O   . CYS I  309 ? 0.6394 0.6416 0.6205 0.0288  -0.0153 -0.0046 309 CYS I O   
17604 C CB  . CYS I  309 ? 0.5098 0.5202 0.4965 0.0403  -0.0112 0.0026  309 CYS I CB  
17605 S SG  . CYS I  309 ? 0.8604 0.8727 0.8510 0.0465  -0.0060 0.0061  309 CYS I SG  
17606 N N   . PRO I  310 ? 0.5221 0.5324 0.4985 0.0311  -0.0181 -0.0031 310 PRO I N   
17607 C CA  . PRO I  310 ? 0.6154 0.6252 0.5888 0.0264  -0.0229 -0.0049 310 PRO I CA  
17608 C C   . PRO I  310 ? 0.5993 0.6083 0.5763 0.0257  -0.0253 -0.0037 310 PRO I C   
17609 O O   . PRO I  310 ? 0.5907 0.6005 0.5715 0.0292  -0.0238 -0.0014 310 PRO I O   
17610 C CB  . PRO I  310 ? 0.4839 0.4988 0.4537 0.0271  -0.0251 -0.0044 310 PRO I CB  
17611 C CG  . PRO I  310 ? 0.5368 0.5541 0.5066 0.0310  -0.0212 -0.0034 310 PRO I CG  
17612 C CD  . PRO I  310 ? 0.5204 0.5359 0.4951 0.0344  -0.0175 -0.0016 310 PRO I CD  
17613 N N   . LYS I  311 ? 0.4490 0.4564 0.4248 0.0213  -0.0291 -0.0051 311 LYS I N   
17614 C CA  . LYS I  311 ? 0.4692 0.4757 0.4490 0.0204  -0.0315 -0.0039 311 LYS I CA  
17615 C C   . LYS I  311 ? 0.5021 0.5126 0.4824 0.0219  -0.0340 -0.0020 311 LYS I C   
17616 O O   . LYS I  311 ? 0.5302 0.5434 0.5065 0.0211  -0.0361 -0.0024 311 LYS I O   
17617 C CB  . LYS I  311 ? 0.3953 0.3991 0.3740 0.0151  -0.0348 -0.0058 311 LYS I CB  
17618 C CG  . LYS I  311 ? 0.5119 0.5123 0.4954 0.0141  -0.0340 -0.0057 311 LYS I CG  
17619 C CD  . LYS I  311 ? 0.4387 0.4364 0.4243 0.0167  -0.0286 -0.0060 311 LYS I CD  
17620 C CE  . LYS I  311 ? 0.5157 0.5098 0.4985 0.0133  -0.0271 -0.0090 311 LYS I CE  
17621 N NZ  . LYS I  311 ? 0.4725 0.4631 0.4589 0.0153  -0.0220 -0.0092 311 LYS I NZ  
17622 N N   . TYR I  312 ? 0.4122 0.4226 0.3972 0.0241  -0.0335 0.0001  312 TYR I N   
17623 C CA  . TYR I  312 ? 0.4357 0.4493 0.4214 0.0255  -0.0353 0.0018  312 TYR I CA  
17624 C C   . TYR I  312 ? 0.5632 0.5769 0.5489 0.0217  -0.0400 0.0016  312 TYR I C   
17625 O O   . TYR I  312 ? 0.6147 0.6257 0.6033 0.0193  -0.0415 0.0014  312 TYR I O   
17626 C CB  . TYR I  312 ? 0.3493 0.3628 0.3402 0.0290  -0.0330 0.0041  312 TYR I CB  
17627 C CG  . TYR I  312 ? 0.4285 0.4449 0.4201 0.0302  -0.0345 0.0057  312 TYR I CG  
17628 C CD1 . TYR I  312 ? 0.3956 0.4160 0.3836 0.0320  -0.0342 0.0060  312 TYR I CD1 
17629 C CD2 . TYR I  312 ? 0.4427 0.4579 0.4387 0.0294  -0.0361 0.0068  312 TYR I CD2 
17630 C CE1 . TYR I  312 ? 0.4226 0.4455 0.4111 0.0328  -0.0353 0.0072  312 TYR I CE1 
17631 C CE2 . TYR I  312 ? 0.3760 0.3935 0.3727 0.0304  -0.0370 0.0081  312 TYR I CE2 
17632 C CZ  . TYR I  312 ? 0.4876 0.5088 0.4804 0.0320  -0.0366 0.0082  312 TYR I CZ  
17633 O OH  . TYR I  312 ? 0.6173 0.6406 0.6106 0.0327  -0.0372 0.0092  312 TYR I OH  
17634 N N   . VAL I  313 ? 0.5931 0.6098 0.5755 0.0213  -0.0421 0.0016  313 VAL I N   
17635 C CA  . VAL I  313 ? 0.4264 0.4434 0.4086 0.0179  -0.0463 0.0016  313 VAL I CA  
17636 C C   . VAL I  313 ? 0.4681 0.4881 0.4511 0.0196  -0.0471 0.0031  313 VAL I C   
17637 O O   . VAL I  313 ? 0.5693 0.5919 0.5503 0.0224  -0.0451 0.0034  313 VAL I O   
17638 C CB  . VAL I  313 ? 0.4495 0.4669 0.4261 0.0146  -0.0485 -0.0004 313 VAL I CB  
17639 C CG1 . VAL I  313 ? 0.7331 0.7511 0.7094 0.0113  -0.0529 0.0001  313 VAL I CG1 
17640 C CG2 . VAL I  313 ? 0.5452 0.5593 0.5208 0.0124  -0.0477 -0.0022 313 VAL I CG2 
17641 N N   . LYS I  314 ? 0.5257 0.5453 0.5117 0.0178  -0.0499 0.0042  314 LYS I N   
17642 C CA  . LYS I  314 ? 0.4597 0.4813 0.4470 0.0190  -0.0504 0.0055  314 LYS I CA  
17643 C C   . LYS I  314 ? 0.4625 0.4865 0.4451 0.0172  -0.0526 0.0047  314 LYS I C   
17644 O O   . LYS I  314 ? 0.6904 0.7161 0.6735 0.0177  -0.0532 0.0055  314 LYS I O   
17645 C CB  . LYS I  314 ? 0.4659 0.4858 0.4592 0.0179  -0.0521 0.0072  314 LYS I CB  
17646 C CG  . LYS I  314 ? 0.7589 0.7800 0.7552 0.0201  -0.0510 0.0088  314 LYS I CG  
17647 C CD  . LYS I  314 ? 1.1332 1.1524 1.1363 0.0192  -0.0523 0.0106  314 LYS I CD  
17648 C CE  . LYS I  314 ? 1.1606 1.1771 1.1672 0.0194  -0.0511 0.0107  314 LYS I CE  
17649 N NZ  . LYS I  314 ? 0.9802 0.9950 0.9930 0.0174  -0.0533 0.0122  314 LYS I NZ  
17650 N N   . SER I  315 ? 0.5263 0.5502 0.5044 0.0151  -0.0537 0.0030  315 SER I N   
17651 C CA  . SER I  315 ? 0.6236 0.6494 0.5970 0.0131  -0.0559 0.0021  315 SER I CA  
17652 C C   . SER I  315 ? 0.5726 0.6018 0.5431 0.0156  -0.0539 0.0018  315 SER I C   
17653 O O   . SER I  315 ? 0.4106 0.4408 0.3810 0.0187  -0.0509 0.0019  315 SER I O   
17654 C CB  . SER I  315 ? 0.6257 0.6504 0.5945 0.0103  -0.0569 0.0002  315 SER I CB  
17655 O OG  . SER I  315 ? 0.8231 0.8451 0.7939 0.0073  -0.0592 0.0003  315 SER I OG  
17656 N N   . THR I  316 ? 0.7236 0.7547 0.6919 0.0143  -0.0557 0.0017  316 THR I N   
17657 C CA  . THR I  316 ? 0.6392 0.6737 0.6041 0.0160  -0.0543 0.0011  316 THR I CA  
17658 C C   . THR I  316 ? 0.5960 0.6318 0.5553 0.0147  -0.0546 -0.0008 316 THR I C   
17659 O O   . THR I  316 ? 0.6941 0.7326 0.6506 0.0167  -0.0525 -0.0015 316 THR I O   
17660 C CB  . THR I  316 ? 0.7514 0.7873 0.7169 0.0152  -0.0556 0.0017  316 THR I CB  
17661 O OG1 . THR I  316 ? 1.0210 1.0604 0.9822 0.0158  -0.0546 0.0006  316 THR I OG1 
17662 C CG2 . THR I  316 ? 0.8293 0.8634 0.7950 0.0116  -0.0590 0.0019  316 THR I CG2 
17663 N N   . LYS I  317 ? 0.6471 0.6809 0.6046 0.0114  -0.0571 -0.0016 317 LYS I N   
17664 C CA  . LYS I  317 ? 0.6232 0.6576 0.5754 0.0098  -0.0574 -0.0035 317 LYS I CA  
17665 C C   . LYS I  317 ? 0.6692 0.7003 0.6204 0.0065  -0.0592 -0.0043 317 LYS I C   
17666 O O   . LYS I  317 ? 0.8489 0.8781 0.8025 0.0043  -0.0617 -0.0033 317 LYS I O   
17667 C CB  . LYS I  317 ? 0.7412 0.7780 0.6899 0.0084  -0.0589 -0.0040 317 LYS I CB  
17668 C CG  . LYS I  317 ? 0.9256 0.9612 0.8761 0.0059  -0.0620 -0.0029 317 LYS I CG  
17669 C CD  . LYS I  317 ? 1.2206 1.2583 1.1675 0.0043  -0.0633 -0.0036 317 LYS I CD  
17670 C CE  . LYS I  317 ? 1.1737 1.2110 1.1151 0.0019  -0.0643 -0.0054 317 LYS I CE  
17671 N NZ  . LYS I  317 ? 0.8975 0.9366 0.8355 0.0002  -0.0655 -0.0060 317 LYS I NZ  
17672 N N   . LEU I  318 ? 0.6151 0.6456 0.5629 0.0062  -0.0577 -0.0060 318 LEU I N   
17673 C CA  . LEU I  318 ? 0.5436 0.5711 0.4892 0.0027  -0.0591 -0.0073 318 LEU I CA  
17674 C C   . LEU I  318 ? 0.5655 0.5938 0.5051 0.0011  -0.0589 -0.0093 318 LEU I C   
17675 O O   . LEU I  318 ? 0.7079 0.7352 0.6454 0.0015  -0.0565 -0.0109 318 LEU I O   
17676 C CB  . LEU I  318 ? 0.4183 0.4431 0.3663 0.0037  -0.0566 -0.0076 318 LEU I CB  
17677 C CG  . LEU I  318 ? 0.5336 0.5570 0.4876 0.0050  -0.0566 -0.0058 318 LEU I CG  
17678 C CD1 . LEU I  318 ? 0.5998 0.6205 0.5557 0.0060  -0.0537 -0.0065 318 LEU I CD1 
17679 C CD2 . LEU I  318 ? 0.5112 0.5333 0.4671 0.0017  -0.0605 -0.0048 318 LEU I CD2 
17680 N N   . ARG I  319 ? 0.5616 0.5915 0.4986 -0.0006 -0.0613 -0.0093 319 ARG I N   
17681 C CA  . ARG I  319 ? 0.6776 0.7085 0.6089 -0.0021 -0.0612 -0.0112 319 ARG I CA  
17682 C C   . ARG I  319 ? 0.6070 0.6350 0.5346 -0.0065 -0.0631 -0.0125 319 ARG I C   
17683 O O   . ARG I  319 ? 0.5417 0.5688 0.4691 -0.0095 -0.0665 -0.0117 319 ARG I O   
17684 C CB  . ARG I  319 ? 0.7387 0.7725 0.6687 -0.0022 -0.0627 -0.0106 319 ARG I CB  
17685 C CG  . ARG I  319 ? 0.7618 0.7989 0.6888 -0.0004 -0.0604 -0.0119 319 ARG I CG  
17686 C CD  . ARG I  319 ? 0.8043 0.8444 0.7345 0.0037  -0.0582 -0.0107 319 ARG I CD  
17687 N NE  . ARG I  319 ? 0.8683 0.9112 0.7969 0.0061  -0.0553 -0.0116 319 ARG I NE  
17688 C CZ  . ARG I  319 ? 0.8692 0.9130 0.7935 0.0049  -0.0547 -0.0133 319 ARG I CZ  
17689 N NH1 . ARG I  319 ? 1.0051 1.0471 0.9258 0.0013  -0.0570 -0.0144 319 ARG I NH1 
17690 N NH2 . ARG I  319 ? 0.9604 1.0070 0.8841 0.0075  -0.0519 -0.0137 319 ARG I NH2 
17691 N N   . LEU I  320 ? 0.5479 0.5745 0.4724 -0.0069 -0.0608 -0.0146 320 LEU I N   
17692 C CA  . LEU I  320 ? 0.4598 0.4834 0.3803 -0.0112 -0.0620 -0.0162 320 LEU I CA  
17693 C C   . LEU I  320 ? 0.6786 0.7030 0.5931 -0.0133 -0.0625 -0.0179 320 LEU I C   
17694 O O   . LEU I  320 ? 0.8441 0.8699 0.7568 -0.0114 -0.0596 -0.0191 320 LEU I O   
17695 C CB  . LEU I  320 ? 0.5172 0.5380 0.4382 -0.0108 -0.0588 -0.0177 320 LEU I CB  
17696 C CG  . LEU I  320 ? 0.5868 0.6039 0.5042 -0.0155 -0.0597 -0.0196 320 LEU I CG  
17697 C CD1 . LEU I  320 ? 0.6064 0.6221 0.5265 -0.0180 -0.0633 -0.0181 320 LEU I CD1 
17698 C CD2 . LEU I  320 ? 0.5655 0.5798 0.4829 -0.0147 -0.0554 -0.0215 320 LEU I CD2 
17699 N N   . ALA I  321 ? 0.6983 0.7220 0.6099 -0.0172 -0.0661 -0.0177 321 ALA I N   
17700 C CA  . ALA I  321 ? 0.5225 0.5468 0.4283 -0.0196 -0.0668 -0.0191 321 ALA I CA  
17701 C C   . ALA I  321 ? 0.5396 0.5613 0.4407 -0.0216 -0.0645 -0.0219 321 ALA I C   
17702 O O   . ALA I  321 ? 0.6945 0.7131 0.5948 -0.0241 -0.0646 -0.0228 321 ALA I O   
17703 C CB  . ALA I  321 ? 0.5527 0.5767 0.4569 -0.0233 -0.0712 -0.0178 321 ALA I CB  
17704 N N   . THR I  322 ? 0.5482 0.5714 0.4462 -0.0206 -0.0622 -0.0234 322 THR I N   
17705 C CA  . THR I  322 ? 0.7906 0.8116 0.6843 -0.0222 -0.0594 -0.0261 322 THR I CA  
17706 C C   . THR I  322 ? 0.7220 0.7433 0.6096 -0.0254 -0.0608 -0.0274 322 THR I C   
17707 O O   . THR I  322 ? 0.6780 0.6963 0.5607 -0.0292 -0.0608 -0.0293 322 THR I O   
17708 C CB  . THR I  322 ? 0.6978 0.7203 0.5936 -0.0179 -0.0548 -0.0267 322 THR I CB  
17709 O OG1 . THR I  322 ? 0.6527 0.6796 0.5492 -0.0153 -0.0549 -0.0257 322 THR I OG1 
17710 C CG2 . THR I  322 ? 0.8250 0.8470 0.7265 -0.0148 -0.0531 -0.0255 322 THR I CG2 
17711 N N   . GLY I  323 ? 0.6410 0.6657 0.5289 -0.0238 -0.0618 -0.0263 323 GLY I N   
17712 C CA  . GLY I  323 ? 0.7823 0.8075 0.6651 -0.0266 -0.0634 -0.0270 323 GLY I CA  
17713 C C   . GLY I  323 ? 0.7677 0.7922 0.6495 -0.0299 -0.0680 -0.0254 323 GLY I C   
17714 O O   . GLY I  323 ? 0.8738 0.8971 0.7587 -0.0304 -0.0699 -0.0239 323 GLY I O   
17715 N N   . LEU I  324 ? 0.6939 0.7191 0.5717 -0.0321 -0.0697 -0.0255 324 LEU I N   
17716 C CA  . LEU I  324 ? 0.8468 0.8714 0.7233 -0.0355 -0.0740 -0.0238 324 LEU I CA  
17717 C C   . LEU I  324 ? 0.7357 0.7632 0.6155 -0.0338 -0.0758 -0.0214 324 LEU I C   
17718 O O   . LEU I  324 ? 0.8328 0.8629 0.7151 -0.0303 -0.0737 -0.0215 324 LEU I O   
17719 C CB  . LEU I  324 ? 0.8549 0.8777 0.7240 -0.0400 -0.0749 -0.0253 324 LEU I CB  
17720 C CG  . LEU I  324 ? 0.7294 0.7537 0.5948 -0.0396 -0.0729 -0.0270 324 LEU I CG  
17721 C CD1 . LEU I  324 ? 0.8988 0.9223 0.7589 -0.0437 -0.0757 -0.0266 324 LEU I CD1 
17722 C CD2 . LEU I  324 ? 0.7025 0.7255 0.5653 -0.0391 -0.0688 -0.0300 324 LEU I CD2 
17723 N N   . ARG I  325 ? 0.8226 0.8495 0.7024 -0.0364 -0.0796 -0.0192 325 ARG I N   
17724 C CA  . ARG I  325 ? 0.8988 0.9279 0.7817 -0.0352 -0.0812 -0.0169 325 ARG I CA  
17725 C C   . ARG I  325 ? 0.9013 0.9323 0.7812 -0.0344 -0.0794 -0.0184 325 ARG I C   
17726 O O   . ARG I  325 ? 0.8538 0.8839 0.7280 -0.0366 -0.0786 -0.0204 325 ARG I O   
17727 C CB  . ARG I  325 ? 0.8487 0.8769 0.7311 -0.0387 -0.0855 -0.0144 325 ARG I CB  
17728 C CG  . ARG I  325 ? 0.8427 0.8726 0.7306 -0.0370 -0.0870 -0.0114 325 ARG I CG  
17729 C CD  . ARG I  325 ? 0.9948 1.0240 0.8822 -0.0404 -0.0911 -0.0085 325 ARG I CD  
17730 N NE  . ARG I  325 ? 1.1431 1.1709 1.0320 -0.0424 -0.0937 -0.0071 325 ARG I NE  
17731 C CZ  . ARG I  325 ? 1.1337 1.1620 1.0293 -0.0413 -0.0953 -0.0043 325 ARG I CZ  
17732 N NH1 . ARG I  325 ? 0.8654 0.8951 0.7666 -0.0380 -0.0944 -0.0027 325 ARG I NH1 
17733 N NH2 . ARG I  325 ? 1.0924 1.1197 0.9890 -0.0435 -0.0978 -0.0031 325 ARG I NH2 
17734 N N   . ASN I  326 ? 0.9611 0.9946 0.8449 -0.0314 -0.0786 -0.0174 326 ASN I N   
17735 C CA  . ASN I  326 ? 1.1144 1.1503 0.9962 -0.0303 -0.0765 -0.0189 326 ASN I CA  
17736 C C   . ASN I  326 ? 1.1319 1.1687 1.0139 -0.0313 -0.0782 -0.0174 326 ASN I C   
17737 O O   . ASN I  326 ? 1.0871 1.1243 0.9738 -0.0302 -0.0794 -0.0152 326 ASN I O   
17738 C CB  . ASN I  326 ? 1.2324 1.2709 1.1179 -0.0260 -0.0735 -0.0196 326 ASN I CB  
17739 C CG  . ASN I  326 ? 1.2059 1.2474 1.0893 -0.0249 -0.0711 -0.0214 326 ASN I CG  
17740 O OD1 . ASN I  326 ? 1.2755 1.3164 1.1540 -0.0267 -0.0703 -0.0232 326 ASN I OD1 
17741 N ND2 . ASN I  326 ? 1.1801 1.2246 1.0670 -0.0220 -0.0699 -0.0209 326 ASN I ND2 
17742 N N   . ILE I  327 ? 1.1537 1.1906 1.0307 -0.0333 -0.0780 -0.0187 327 ILE I N   
17743 C CA  . ILE I  327 ? 1.0790 1.1167 0.9559 -0.0343 -0.0791 -0.0176 327 ILE I CA  
17744 C C   . ILE I  327 ? 1.1442 1.1843 1.0186 -0.0335 -0.0765 -0.0198 327 ILE I C   
17745 O O   . ILE I  327 ? 1.1340 1.1740 1.0039 -0.0345 -0.0751 -0.0220 327 ILE I O   
17746 C CB  . ILE I  327 ? 0.9735 1.0087 0.8463 -0.0385 -0.0820 -0.0164 327 ILE I CB  
17747 C CG1 . ILE I  327 ? 0.8008 0.8342 0.6763 -0.0396 -0.0851 -0.0137 327 ILE I CG1 
17748 C CG2 . ILE I  327 ? 1.1746 1.2105 1.0468 -0.0394 -0.0825 -0.0154 327 ILE I CG2 
17749 C CD1 . ILE I  327 ? 0.8007 0.8351 0.6836 -0.0370 -0.0855 -0.0113 327 ILE I CD1 
17750 N N   . GLY J  1   ? 1.3623 1.3855 1.2316 -0.0609 -0.1047 -0.0061 1   GLY J N   
17751 C CA  . GLY J  1   ? 1.2982 1.3224 1.1741 -0.0607 -0.1076 -0.0029 1   GLY J CA  
17752 C C   . GLY J  1   ? 1.0061 1.0299 0.8788 -0.0659 -0.1114 -0.0019 1   GLY J C   
17753 O O   . GLY J  1   ? 1.3064 1.3313 1.1775 -0.0689 -0.1151 0.0010  1   GLY J O   
17754 N N   . LEU J  2   ? 0.8641 0.8864 0.7360 -0.0670 -0.1103 -0.0043 2   LEU J N   
17755 C CA  . LEU J  2   ? 0.9488 0.9709 0.8183 -0.0720 -0.1138 -0.0036 2   LEU J CA  
17756 C C   . LEU J  2   ? 0.8103 0.8313 0.6699 -0.0772 -0.1151 -0.0050 2   LEU J C   
17757 O O   . LEU J  2   ? 0.7392 0.7610 0.5963 -0.0819 -0.1192 -0.0032 2   LEU J O   
17758 C CB  . LEU J  2   ? 0.8377 0.8581 0.7088 -0.0717 -0.1118 -0.0062 2   LEU J CB  
17759 C CG  . LEU J  2   ? 0.8360 0.8571 0.7088 -0.0755 -0.1156 -0.0044 2   LEU J CG  
17760 C CD1 . LEU J  2   ? 0.7681 0.7921 0.6497 -0.0735 -0.1190 0.0007  2   LEU J CD1 
17761 C CD2 . LEU J  2   ? 0.5004 0.5192 0.3739 -0.0754 -0.1128 -0.0076 2   LEU J CD2 
17762 N N   . PHE J  3   ? 0.7794 0.7988 0.6336 -0.0766 -0.1116 -0.0083 3   PHE J N   
17763 C CA  . PHE J  3   ? 0.8360 0.8540 0.6805 -0.0814 -0.1122 -0.0101 3   PHE J CA  
17764 C C   . PHE J  3   ? 0.9341 0.9534 0.7765 -0.0813 -0.1134 -0.0080 3   PHE J C   
17765 O O   . PHE J  3   ? 0.9303 0.9485 0.7647 -0.0849 -0.1136 -0.0093 3   PHE J O   
17766 C CB  . PHE J  3   ? 0.9422 0.9571 0.7814 -0.0815 -0.1072 -0.0154 3   PHE J CB  
17767 C CG  . PHE J  3   ? 0.8618 0.8748 0.7012 -0.0830 -0.1061 -0.0178 3   PHE J CG  
17768 C CD1 . PHE J  3   ? 0.8960 0.9089 0.7425 -0.0787 -0.1036 -0.0182 3   PHE J CD1 
17769 C CD2 . PHE J  3   ? 0.9631 0.9743 0.7953 -0.0890 -0.1074 -0.0195 3   PHE J CD2 
17770 C CE1 . PHE J  3   ? 0.9059 0.9168 0.7527 -0.0801 -0.1024 -0.0204 3   PHE J CE1 
17771 C CE2 . PHE J  3   ? 0.9397 0.9490 0.7721 -0.0907 -0.1061 -0.0219 3   PHE J CE2 
17772 C CZ  . PHE J  3   ? 0.9419 0.9510 0.7818 -0.0861 -0.1035 -0.0223 3   PHE J CZ  
17773 N N   . GLY J  4   ? 0.9540 0.9753 0.8035 -0.0772 -0.1139 -0.0049 4   GLY J N   
17774 C CA  . GLY J  4   ? 0.9486 0.9713 0.7974 -0.0770 -0.1152 -0.0024 4   GLY J CA  
17775 C C   . GLY J  4   ? 1.0371 1.0587 0.8816 -0.0755 -0.1113 -0.0054 4   GLY J C   
17776 O O   . GLY J  4   ? 1.0592 1.0815 0.9027 -0.0754 -0.1120 -0.0037 4   GLY J O   
17777 N N   . ALA J  5   ? 0.9526 0.9724 0.7948 -0.0743 -0.1072 -0.0098 5   ALA J N   
17778 C CA  . ALA J  5   ? 0.7701 0.7890 0.6083 -0.0729 -0.1034 -0.0129 5   ALA J CA  
17779 C C   . ALA J  5   ? 0.8762 0.8969 0.7208 -0.0673 -0.1009 -0.0126 5   ALA J C   
17780 O O   . ALA J  5   ? 0.7993 0.8212 0.6444 -0.0664 -0.1011 -0.0111 5   ALA J O   
17781 C CB  . ALA J  5   ? 0.7460 0.7624 0.5791 -0.0741 -0.0999 -0.0176 5   ALA J CB  
17782 N N   . ILE J  6   ? 0.8912 0.9119 0.7406 -0.0638 -0.0984 -0.0139 6   ILE J N   
17783 C CA  . ILE J  6   ? 0.6278 0.6504 0.4831 -0.0587 -0.0959 -0.0138 6   ILE J CA  
17784 C C   . ILE J  6   ? 0.7535 0.7780 0.6156 -0.0571 -0.0986 -0.0096 6   ILE J C   
17785 O O   . ILE J  6   ? 0.9306 0.9552 0.7966 -0.0577 -0.1012 -0.0072 6   ILE J O   
17786 C CB  . ILE J  6   ? 0.7358 0.7581 0.5945 -0.0554 -0.0926 -0.0160 6   ILE J CB  
17787 C CG1 . ILE J  6   ? 0.6630 0.6833 0.5157 -0.0567 -0.0894 -0.0201 6   ILE J CG1 
17788 C CG2 . ILE J  6   ? 0.6448 0.6693 0.5093 -0.0504 -0.0903 -0.0157 6   ILE J CG2 
17789 C CD1 . ILE J  6   ? 0.6680 0.6882 0.5241 -0.0532 -0.0856 -0.0222 6   ILE J CD1 
17790 N N   . ALA J  7   ? 0.7191 0.7450 0.5825 -0.0552 -0.0978 -0.0088 7   ALA J N   
17791 C CA  . ALA J  7   ? 0.7622 0.7895 0.6317 -0.0540 -0.0999 -0.0049 7   ALA J CA  
17792 C C   . ALA J  7   ? 0.9429 0.9699 0.8107 -0.0580 -0.1043 -0.0015 7   ALA J C   
17793 O O   . ALA J  7   ? 1.0118 1.0398 0.8854 -0.0576 -0.1068 0.0023  7   ALA J O   
17794 C CB  . ALA J  7   ? 0.7771 0.8052 0.6544 -0.0506 -0.0994 -0.0037 7   ALA J CB  
17795 N N   . GLY J  8   ? 1.0082 1.0339 0.8682 -0.0620 -0.1052 -0.0029 8   GLY J N   
17796 C CA  . GLY J  8   ? 0.9002 0.9259 0.7574 -0.0663 -0.1095 0.0001  8   GLY J CA  
17797 C C   . GLY J  8   ? 1.0902 1.1155 0.9414 -0.0684 -0.1095 0.0001  8   GLY J C   
17798 O O   . GLY J  8   ? 1.1014 1.1275 0.9552 -0.0662 -0.1084 0.0012  8   GLY J O   
17799 N N   . PHE J  9   ? 0.8365 0.8604 0.6795 -0.0728 -0.1105 -0.0013 9   PHE J N   
17800 C CA  . PHE J  9   ? 0.8202 0.8435 0.6569 -0.0751 -0.1104 -0.0015 9   PHE J CA  
17801 C C   . PHE J  9   ? 1.0049 1.0274 0.8391 -0.0728 -0.1056 -0.0057 9   PHE J C   
17802 O O   . PHE J  9   ? 1.2639 1.2863 1.0948 -0.0734 -0.1047 -0.0060 9   PHE J O   
17803 C CB  . PHE J  9   ? 1.0677 1.0896 0.8960 -0.0807 -0.1130 -0.0017 9   PHE J CB  
17804 C CG  . PHE J  9   ? 0.9590 0.9790 0.7825 -0.0825 -0.1111 -0.0059 9   PHE J CG  
17805 C CD1 . PHE J  9   ? 1.0322 1.0505 0.8509 -0.0820 -0.1069 -0.0105 9   PHE J CD1 
17806 C CD2 . PHE J  9   ? 1.2118 1.2317 1.0358 -0.0847 -0.1136 -0.0053 9   PHE J CD2 
17807 C CE1 . PHE J  9   ? 1.0425 1.0588 0.8572 -0.0836 -0.1048 -0.0144 9   PHE J CE1 
17808 C CE2 . PHE J  9   ? 1.2225 1.2403 1.0422 -0.0865 -0.1116 -0.0094 9   PHE J CE2 
17809 C CZ  . PHE J  9   ? 1.1195 1.1353 0.9345 -0.0858 -0.1070 -0.0139 9   PHE J CZ  
17810 N N   . ILE J  10  ? 0.9654 0.9877 0.8015 -0.0702 -0.1026 -0.0089 10  ILE J N   
17811 C CA  . ILE J  10  ? 0.8533 0.8759 0.6895 -0.0670 -0.0982 -0.0122 10  ILE J CA  
17812 C C   . ILE J  10  ? 0.8374 0.8620 0.6823 -0.0623 -0.0973 -0.0108 10  ILE J C   
17813 O O   . ILE J  10  ? 0.9197 0.9447 0.7688 -0.0601 -0.0967 -0.0112 10  ILE J O   
17814 C CB  . ILE J  10  ? 0.6727 0.6938 0.5053 -0.0671 -0.0951 -0.0165 10  ILE J CB  
17815 C CG1 . ILE J  10  ? 0.7224 0.7411 0.5467 -0.0723 -0.0962 -0.0178 10  ILE J CG1 
17816 C CG2 . ILE J  10  ? 0.6964 0.7183 0.5286 -0.0642 -0.0908 -0.0196 10  ILE J CG2 
17817 C CD1 . ILE J  10  ? 0.7863 0.8030 0.6068 -0.0727 -0.0927 -0.0221 10  ILE J CD1 
17818 N N   . GLU J  11  ? 1.0331 1.0591 0.8806 -0.0609 -0.0972 -0.0091 11  GLU J N   
17819 C CA  . GLU J  11  ? 1.1379 1.1655 0.9936 -0.0571 -0.0969 -0.0071 11  GLU J CA  
17820 C C   . GLU J  11  ? 0.9979 1.0268 0.8567 -0.0530 -0.0931 -0.0099 11  GLU J C   
17821 O O   . GLU J  11  ? 1.0507 1.0805 0.9158 -0.0502 -0.0929 -0.0088 11  GLU J O   
17822 C CB  . GLU J  11  ? 1.3308 1.3591 1.1881 -0.0570 -0.0975 -0.0046 11  GLU J CB  
17823 C CG  . GLU J  11  ? 1.5121 1.5395 1.3671 -0.0608 -0.1013 -0.0011 11  GLU J CG  
17824 C CD  . GLU J  11  ? 1.9986 2.0264 1.8547 -0.0607 -0.1012 0.0010  11  GLU J CD  
17825 O OE1 . GLU J  11  ? 2.0752 2.1025 1.9297 -0.0635 -0.1041 0.0043  11  GLU J OE1 
17826 O OE2 . GLU J  11  ? 1.9961 2.0247 1.8548 -0.0579 -0.0981 -0.0005 11  GLU J OE2 
17827 N N   . GLY J  12  ? 0.9892 1.0183 0.8437 -0.0528 -0.0901 -0.0134 12  GLY J N   
17828 C CA  . GLY J  12  ? 0.8653 0.8962 0.7226 -0.0489 -0.0866 -0.0157 12  GLY J CA  
17829 C C   . GLY J  12  ? 0.8935 0.9240 0.7472 -0.0487 -0.0839 -0.0193 12  GLY J C   
17830 O O   . GLY J  12  ? 0.8646 0.8931 0.7125 -0.0518 -0.0843 -0.0206 12  GLY J O   
17831 N N   . GLY J  13  ? 0.8854 0.9180 0.7426 -0.0450 -0.0810 -0.0208 13  GLY J N   
17832 C CA  . GLY J  13  ? 0.8279 0.8605 0.6827 -0.0441 -0.0780 -0.0239 13  GLY J CA  
17833 C C   . GLY J  13  ? 0.8362 0.8709 0.6891 -0.0431 -0.0752 -0.0261 13  GLY J C   
17834 O O   . GLY J  13  ? 0.8898 0.9260 0.7435 -0.0429 -0.0755 -0.0253 13  GLY J O   
17835 N N   . TRP J  14  ? 0.8060 0.8409 0.6567 -0.0425 -0.0723 -0.0288 14  TRP J N   
17836 C CA  . TRP J  14  ? 0.8528 0.8900 0.7018 -0.0416 -0.0695 -0.0309 14  TRP J CA  
17837 C C   . TRP J  14  ? 0.9644 1.0050 0.8175 -0.0375 -0.0665 -0.0319 14  TRP J C   
17838 O O   . TRP J  14  ? 1.0320 1.0720 0.8850 -0.0365 -0.0645 -0.0332 14  TRP J O   
17839 C CB  . TRP J  14  ? 0.9006 0.9355 0.7430 -0.0447 -0.0683 -0.0332 14  TRP J CB  
17840 C CG  . TRP J  14  ? 0.9811 1.0129 0.8192 -0.0489 -0.0708 -0.0320 14  TRP J CG  
17841 C CD1 . TRP J  14  ? 0.9502 0.9821 0.7898 -0.0499 -0.0732 -0.0294 14  TRP J CD1 
17842 C CD2 . TRP J  14  ? 0.7950 0.8234 0.6266 -0.0528 -0.0710 -0.0334 14  TRP J CD2 
17843 N NE1 . TRP J  14  ? 0.8372 0.8661 0.6717 -0.0541 -0.0751 -0.0287 14  TRP J NE1 
17844 C CE2 . TRP J  14  ? 0.8907 0.9175 0.7201 -0.0560 -0.0737 -0.0312 14  TRP J CE2 
17845 C CE3 . TRP J  14  ? 0.7572 0.7836 0.5847 -0.0539 -0.0688 -0.0361 14  TRP J CE3 
17846 C CZ2 . TRP J  14  ? 0.9957 1.0192 0.8185 -0.0604 -0.0747 -0.0317 14  TRP J CZ2 
17847 C CZ3 . TRP J  14  ? 0.9695 0.9924 0.7902 -0.0584 -0.0696 -0.0370 14  TRP J CZ3 
17848 C CH2 . TRP J  14  ? 1.0904 1.1120 0.9089 -0.0617 -0.0726 -0.0347 14  TRP J CH2 
17849 N N   . THR J  15  ? 0.9543 0.9984 0.8110 -0.0352 -0.0662 -0.0313 15  THR J N   
17850 C CA  . THR J  15  ? 1.0299 1.0781 0.8902 -0.0315 -0.0634 -0.0322 15  THR J CA  
17851 C C   . THR J  15  ? 1.1888 1.2380 1.0459 -0.0317 -0.0606 -0.0346 15  THR J C   
17852 O O   . THR J  15  ? 1.2665 1.3180 1.1257 -0.0290 -0.0581 -0.0354 15  THR J O   
17853 C CB  . THR J  15  ? 1.0117 1.0636 0.8752 -0.0298 -0.0635 -0.0314 15  THR J CB  
17854 O OG1 . THR J  15  ? 1.4128 1.4652 1.2736 -0.0319 -0.0631 -0.0323 15  THR J OG1 
17855 C CG2 . THR J  15  ? 1.0568 1.1074 0.9238 -0.0296 -0.0660 -0.0290 15  THR J CG2 
17856 N N   . GLY J  16  ? 1.0658 1.1133 0.9180 -0.0349 -0.0609 -0.0357 16  GLY J N   
17857 C CA  . GLY J  16  ? 1.1321 1.1803 0.9810 -0.0355 -0.0582 -0.0381 16  GLY J CA  
17858 C C   . GLY J  16  ? 1.0483 1.0943 0.8959 -0.0355 -0.0561 -0.0394 16  GLY J C   
17859 O O   . GLY J  16  ? 1.2511 1.2991 1.0992 -0.0339 -0.0530 -0.0409 16  GLY J O   
17860 N N   . MET J  17  ? 1.0531 1.0948 0.8991 -0.0373 -0.0577 -0.0388 17  MET J N   
17861 C CA  . MET J  17  ? 1.1153 1.1542 0.9599 -0.0376 -0.0556 -0.0402 17  MET J CA  
17862 C C   . MET J  17  ? 1.2115 1.2521 1.0619 -0.0337 -0.0542 -0.0394 17  MET J C   
17863 O O   . MET J  17  ? 1.2815 1.3213 1.1346 -0.0330 -0.0563 -0.0376 17  MET J O   
17864 C CB  . MET J  17  ? 0.9826 1.0164 0.8227 -0.0418 -0.0578 -0.0401 17  MET J CB  
17865 C CG  . MET J  17  ? 1.1862 1.2165 1.0241 -0.0428 -0.0555 -0.0420 17  MET J CG  
17866 S SD  . MET J  17  ? 1.1473 1.1719 0.9790 -0.0483 -0.0583 -0.0421 17  MET J SD  
17867 C CE  . MET J  17  ? 1.1196 1.1451 0.9560 -0.0474 -0.0628 -0.0386 17  MET J CE  
17868 N N   . VAL J  18  ? 1.3028 1.3457 1.1551 -0.0311 -0.0506 -0.0406 18  VAL J N   
17869 C CA  . VAL J  18  ? 1.3610 1.4060 1.2189 -0.0271 -0.0489 -0.0396 18  VAL J CA  
17870 C C   . VAL J  18  ? 1.3401 1.3825 1.1978 -0.0266 -0.0455 -0.0410 18  VAL J C   
17871 O O   . VAL J  18  ? 1.3561 1.4006 1.2184 -0.0230 -0.0431 -0.0404 18  VAL J O   
17872 C CB  . VAL J  18  ? 1.4458 1.4971 1.3077 -0.0235 -0.0477 -0.0390 18  VAL J CB  
17873 C CG1 . VAL J  18  ? 1.2218 1.2755 1.0842 -0.0239 -0.0506 -0.0378 18  VAL J CG1 
17874 C CG2 . VAL J  18  ? 1.4450 1.4981 1.3051 -0.0236 -0.0446 -0.0409 18  VAL J CG2 
17875 N N   . ASP J  19  ? 1.4860 1.5239 1.3383 -0.0304 -0.0449 -0.0429 19  ASP J N   
17876 C CA  . ASP J  19  ? 1.5330 1.5678 1.3845 -0.0306 -0.0412 -0.0446 19  ASP J CA  
17877 C C   . ASP J  19  ? 1.3900 1.4204 1.2416 -0.0318 -0.0420 -0.0444 19  ASP J C   
17878 O O   . ASP J  19  ? 1.4187 1.4474 1.2724 -0.0304 -0.0388 -0.0451 19  ASP J O   
17879 C CB  . ASP J  19  ? 1.7535 1.7855 1.5988 -0.0342 -0.0395 -0.0472 19  ASP J CB  
17880 C CG  . ASP J  19  ? 1.8112 1.8446 1.6530 -0.0366 -0.0422 -0.0471 19  ASP J CG  
17881 O OD1 . ASP J  19  ? 1.7383 1.7725 1.5776 -0.0374 -0.0402 -0.0487 19  ASP J OD1 
17882 O OD2 . ASP J  19  ? 1.7594 1.7929 1.6009 -0.0376 -0.0462 -0.0455 19  ASP J OD2 
17883 N N   . GLY J  20  ? 1.2490 1.2776 1.0985 -0.0345 -0.0462 -0.0434 20  GLY J N   
17884 C CA  . GLY J  20  ? 1.0569 1.0815 0.9063 -0.0361 -0.0475 -0.0430 20  GLY J CA  
17885 C C   . GLY J  20  ? 0.9774 1.0023 0.8273 -0.0373 -0.0525 -0.0408 20  GLY J C   
17886 O O   . GLY J  20  ? 0.9536 0.9817 0.8046 -0.0365 -0.0546 -0.0393 20  GLY J O   
17887 N N   . TRP J  21  ? 0.9259 0.9473 0.7752 -0.0395 -0.0541 -0.0405 21  TRP J N   
17888 C CA  . TRP J  21  ? 0.8870 0.9086 0.7374 -0.0407 -0.0588 -0.0380 21  TRP J CA  
17889 C C   . TRP J  21  ? 0.7440 0.7638 0.5884 -0.0455 -0.0620 -0.0380 21  TRP J C   
17890 O O   . TRP J  21  ? 0.7068 0.7283 0.5522 -0.0459 -0.0655 -0.0358 21  TRP J O   
17891 C CB  . TRP J  21  ? 0.9821 1.0013 0.8352 -0.0408 -0.0594 -0.0374 21  TRP J CB  
17892 C CG  . TRP J  21  ? 0.9378 0.9595 0.7981 -0.0358 -0.0579 -0.0360 21  TRP J CG  
17893 C CD1 . TRP J  21  ? 0.8637 0.8897 0.7283 -0.0319 -0.0579 -0.0344 21  TRP J CD1 
17894 C CD2 . TRP J  21  ? 0.7825 0.8024 0.6464 -0.0343 -0.0563 -0.0359 21  TRP J CD2 
17895 N NE1 . TRP J  21  ? 0.7706 0.7977 0.6409 -0.0281 -0.0564 -0.0333 21  TRP J NE1 
17896 C CE2 . TRP J  21  ? 0.7940 0.8174 0.6642 -0.0294 -0.0554 -0.0341 21  TRP J CE2 
17897 C CE3 . TRP J  21  ? 0.7460 0.7616 0.6082 -0.0369 -0.0554 -0.0374 21  TRP J CE3 
17898 C CZ2 . TRP J  21  ? 0.8615 0.8842 0.7365 -0.0267 -0.0536 -0.0335 21  TRP J CZ2 
17899 C CZ3 . TRP J  21  ? 0.7674 0.7823 0.6346 -0.0343 -0.0536 -0.0369 21  TRP J CZ3 
17900 C CH2 . TRP J  21  ? 0.7960 0.8143 0.6695 -0.0292 -0.0527 -0.0349 21  TRP J CH2 
17901 N N   . TYR J  22  ? 0.8633 0.8798 0.7015 -0.0492 -0.0607 -0.0404 22  TYR J N   
17902 C CA  . TYR J  22  ? 0.8990 0.9139 0.7308 -0.0540 -0.0635 -0.0405 22  TYR J CA  
17903 C C   . TYR J  22  ? 0.9348 0.9489 0.7614 -0.0555 -0.0605 -0.0431 22  TYR J C   
17904 O O   . TYR J  22  ? 1.2027 1.2157 1.0293 -0.0543 -0.0562 -0.0455 22  TYR J O   
17905 C CB  . TYR J  22  ? 1.0726 1.0838 0.9010 -0.0585 -0.0656 -0.0407 22  TYR J CB  
17906 C CG  . TYR J  22  ? 0.9935 1.0043 0.8272 -0.0567 -0.0659 -0.0398 22  TYR J CG  
17907 C CD1 . TYR J  22  ? 0.8149 0.8232 0.6490 -0.0563 -0.0621 -0.0421 22  TYR J CD1 
17908 C CD2 . TYR J  22  ? 0.8519 0.8646 0.6904 -0.0554 -0.0696 -0.0365 22  TYR J CD2 
17909 C CE1 . TYR J  22  ? 0.8267 0.8344 0.6656 -0.0547 -0.0622 -0.0412 22  TYR J CE1 
17910 C CE2 . TYR J  22  ? 0.7990 0.8113 0.6424 -0.0538 -0.0697 -0.0357 22  TYR J CE2 
17911 C CZ  . TYR J  22  ? 0.8520 0.8619 0.6956 -0.0534 -0.0660 -0.0381 22  TYR J CZ  
17912 O OH  . TYR J  22  ? 0.7727 0.7819 0.6213 -0.0519 -0.0660 -0.0373 22  TYR J OH  
17913 N N   . GLY J  23  ? 1.2218 1.2364 1.0443 -0.0578 -0.0625 -0.0427 23  GLY J N   
17914 C CA  . GLY J  23  ? 1.4344 1.4482 1.2519 -0.0593 -0.0597 -0.0451 23  GLY J CA  
17915 C C   . GLY J  23  ? 1.4186 1.4324 1.2311 -0.0626 -0.0625 -0.0443 23  GLY J C   
17916 O O   . GLY J  23  ? 1.2076 1.2211 1.0194 -0.0647 -0.0667 -0.0419 23  GLY J O   
17917 N N   . TYR J  24  ? 1.2865 1.3006 1.0958 -0.0631 -0.0600 -0.0461 24  TYR J N   
17918 C CA  . TYR J  24  ? 1.0696 1.0832 0.8735 -0.0664 -0.0620 -0.0456 24  TYR J CA  
17919 C C   . TYR J  24  ? 1.1579 1.1753 0.9644 -0.0637 -0.0611 -0.0452 24  TYR J C   
17920 O O   . TYR J  24  ? 1.1741 1.1945 0.9857 -0.0595 -0.0585 -0.0457 24  TYR J O   
17921 C CB  . TYR J  24  ? 1.0344 1.0440 0.8302 -0.0709 -0.0600 -0.0485 24  TYR J CB  
17922 C CG  . TYR J  24  ? 1.0228 1.0286 0.8160 -0.0734 -0.0593 -0.0499 24  TYR J CG  
17923 C CD1 . TYR J  24  ? 1.0831 1.0879 0.8789 -0.0713 -0.0550 -0.0522 24  TYR J CD1 
17924 C CD2 . TYR J  24  ? 1.0385 1.0417 0.8267 -0.0782 -0.0630 -0.0490 24  TYR J CD2 
17925 C CE1 . TYR J  24  ? 1.1709 1.1719 0.9644 -0.0738 -0.0541 -0.0538 24  TYR J CE1 
17926 C CE2 . TYR J  24  ? 1.0942 1.0940 0.8798 -0.0809 -0.0623 -0.0506 24  TYR J CE2 
17927 C CZ  . TYR J  24  ? 1.1678 1.1664 0.9561 -0.0787 -0.0577 -0.0532 24  TYR J CZ  
17928 O OH  . TYR J  24  ? 1.0181 1.0129 0.8038 -0.0815 -0.0567 -0.0550 24  TYR J OH  
17929 N N   . HIS J  25  ? 1.2023 1.2195 1.0054 -0.0662 -0.0630 -0.0442 25  HIS J N   
17930 C CA  . HIS J  25  ? 1.3160 1.3361 1.1212 -0.0645 -0.0614 -0.0440 25  HIS J CA  
17931 C C   . HIS J  25  ? 1.4067 1.4244 1.2055 -0.0687 -0.0612 -0.0445 25  HIS J C   
17932 O O   . HIS J  25  ? 1.2277 1.2446 1.0252 -0.0710 -0.0641 -0.0420 25  HIS J O   
17933 C CB  . HIS J  25  ? 1.3165 1.3397 1.1280 -0.0620 -0.0638 -0.0407 25  HIS J CB  
17934 C CG  . HIS J  25  ? 1.4014 1.4269 1.2141 -0.0613 -0.0627 -0.0405 25  HIS J CG  
17935 N ND1 . HIS J  25  ? 1.2825 1.3069 1.0930 -0.0640 -0.0646 -0.0386 25  HIS J ND1 
17936 C CD2 . HIS J  25  ? 1.3124 1.3415 1.1282 -0.0585 -0.0598 -0.0419 25  HIS J CD2 
17937 C CE1 . HIS J  25  ? 1.3765 1.4034 1.1886 -0.0628 -0.0629 -0.0390 25  HIS J CE1 
17938 N NE2 . HIS J  25  ? 1.3985 1.4283 1.2138 -0.0596 -0.0600 -0.0410 25  HIS J NE2 
17939 N N   . HIS J  26  ? 1.6550 1.6715 1.4496 -0.0696 -0.0576 -0.0478 26  HIS J N   
17940 C CA  . HIS J  26  ? 1.5650 1.5790 1.3530 -0.0736 -0.0568 -0.0488 26  HIS J CA  
17941 C C   . HIS J  26  ? 1.5572 1.5739 1.3474 -0.0727 -0.0566 -0.0476 26  HIS J C   
17942 O O   . HIS J  26  ? 1.6566 1.6772 1.4529 -0.0688 -0.0559 -0.0471 26  HIS J O   
17943 C CB  . HIS J  26  ? 1.5771 1.5890 1.3604 -0.0746 -0.0526 -0.0529 26  HIS J CB  
17944 C CG  . HIS J  26  ? 1.5672 1.5825 1.3539 -0.0711 -0.0491 -0.0546 26  HIS J CG  
17945 N ND1 . HIS J  26  ? 1.5754 1.5941 1.3691 -0.0664 -0.0475 -0.0547 26  HIS J ND1 
17946 C CD2 . HIS J  26  ? 1.7571 1.7733 1.5422 -0.0715 -0.0465 -0.0561 26  HIS J CD2 
17947 C CE1 . HIS J  26  ? 1.7314 1.7532 1.5274 -0.0642 -0.0444 -0.0560 26  HIS J CE1 
17948 N NE2 . HIS J  26  ? 1.8906 1.9109 1.6812 -0.0673 -0.0438 -0.0571 26  HIS J NE2 
17949 N N   . GLN J  27  ? 1.8734 1.8878 1.6581 -0.0765 -0.0573 -0.0472 27  GLN J N   
17950 C CA  . GLN J  27  ? 1.9544 1.9706 1.7401 -0.0763 -0.0571 -0.0462 27  GLN J CA  
17951 C C   . GLN J  27  ? 1.9024 1.9154 1.6801 -0.0807 -0.0558 -0.0476 27  GLN J C   
17952 O O   . GLN J  27  ? 1.8752 1.8858 1.6486 -0.0842 -0.0585 -0.0456 27  GLN J O   
17953 C CB  . GLN J  27  ? 1.9457 1.9629 1.7347 -0.0760 -0.0610 -0.0422 27  GLN J CB  
17954 C CG  . GLN J  27  ? 1.9527 1.9712 1.7422 -0.0762 -0.0610 -0.0411 27  GLN J CG  
17955 C CD  . GLN J  27  ? 2.1233 2.1462 1.9189 -0.0722 -0.0585 -0.0422 27  GLN J CD  
17956 O OE1 . GLN J  27  ? 2.0952 2.1207 1.8967 -0.0696 -0.0598 -0.0403 27  GLN J OE1 
17957 N NE2 . GLN J  27  ? 2.2072 2.2310 2.0014 -0.0719 -0.0548 -0.0453 27  GLN J NE2 
17958 N N   . ASN J  28  ? 1.9116 1.9244 1.6872 -0.0806 -0.0517 -0.0511 28  ASN J N   
17959 C CA  . ASN J  28  ? 1.9432 1.9528 1.7111 -0.0847 -0.0500 -0.0528 28  ASN J CA  
17960 C C   . ASN J  28  ? 2.0472 2.0593 1.8166 -0.0833 -0.0471 -0.0542 28  ASN J C   
17961 O O   . ASN J  28  ? 2.0173 2.0330 1.7924 -0.0806 -0.0479 -0.0525 28  ASN J O   
17962 C CB  . ASN J  28  ? 1.7274 1.7332 1.4892 -0.0872 -0.0476 -0.0561 28  ASN J CB  
17963 C CG  . ASN J  28  ? 1.7709 1.7784 1.5359 -0.0838 -0.0435 -0.0593 28  ASN J CG  
17964 O OD1 . ASN J  28  ? 1.7497 1.7541 1.5102 -0.0853 -0.0408 -0.0623 28  ASN J OD1 
17965 N ND2 . ASN J  28  ? 1.8563 1.8687 1.6287 -0.0792 -0.0430 -0.0586 28  ASN J ND2 
17966 N N   . GLU J  29  ? 1.8459 1.8560 1.6102 -0.0853 -0.0436 -0.0573 29  GLU J N   
17967 C CA  . GLU J  29  ? 1.8122 1.8242 1.5768 -0.0848 -0.0408 -0.0587 29  GLU J CA  
17968 C C   . GLU J  29  ? 1.8318 1.8475 1.6012 -0.0810 -0.0372 -0.0613 29  GLU J C   
17969 O O   . GLU J  29  ? 1.7608 1.7798 1.5328 -0.0795 -0.0354 -0.0620 29  GLU J O   
17970 C CB  . GLU J  29  ? 1.9652 1.9728 1.7210 -0.0895 -0.0392 -0.0604 29  GLU J CB  
17971 C CG  . GLU J  29  ? 1.9804 1.9847 1.7308 -0.0936 -0.0429 -0.0576 29  GLU J CG  
17972 C CD  . GLU J  29  ? 2.1242 2.1235 1.8649 -0.0986 -0.0413 -0.0596 29  GLU J CD  
17973 O OE1 . GLU J  29  ? 2.0943 2.0918 1.8324 -0.0991 -0.0378 -0.0631 29  GLU J OE1 
17974 O OE2 . GLU J  29  ? 2.0814 2.0785 1.8168 -0.1022 -0.0435 -0.0578 29  GLU J OE2 
17975 N N   . GLN J  30  ? 2.0700 2.0852 1.8400 -0.0796 -0.0360 -0.0628 30  GLN J N   
17976 C CA  . GLN J  30  ? 1.9217 1.9408 1.6967 -0.0755 -0.0330 -0.0648 30  GLN J CA  
17977 C C   . GLN J  30  ? 1.8815 1.9057 1.6647 -0.0712 -0.0353 -0.0623 30  GLN J C   
17978 O O   . GLN J  30  ? 1.8833 1.9125 1.6716 -0.0679 -0.0337 -0.0629 30  GLN J O   
17979 C CB  . GLN J  30  ? 1.8257 1.8420 1.5996 -0.0754 -0.0300 -0.0669 30  GLN J CB  
17980 C CG  . GLN J  30  ? 1.6709 1.6833 1.4388 -0.0786 -0.0258 -0.0700 30  GLN J CG  
17981 C CD  . GLN J  30  ? 1.6428 1.6488 1.4025 -0.0834 -0.0267 -0.0707 30  GLN J CD  
17982 O OE1 . GLN J  30  ? 1.5642 1.5666 1.3217 -0.0846 -0.0233 -0.0730 30  GLN J OE1 
17983 N NE2 . GLN J  30  ? 1.8163 1.8207 1.5715 -0.0863 -0.0312 -0.0686 30  GLN J NE2 
17984 N N   . GLY J  31  ? 2.0616 2.0848 1.8463 -0.0713 -0.0390 -0.0596 31  GLY J N   
17985 C CA  . GLY J  31  ? 2.1030 2.1307 1.8953 -0.0674 -0.0409 -0.0574 31  GLY J CA  
17986 C C   . GLY J  31  ? 2.0834 2.1096 1.8772 -0.0672 -0.0444 -0.0549 31  GLY J C   
17987 O O   . GLY J  31  ? 2.0780 2.0998 1.8670 -0.0705 -0.0462 -0.0542 31  GLY J O   
17988 N N   . SER J  32  ? 1.9916 2.0218 1.7923 -0.0633 -0.0455 -0.0534 32  SER J N   
17989 C CA  . SER J  32  ? 1.8651 1.8946 1.6684 -0.0626 -0.0487 -0.0509 32  SER J CA  
17990 C C   . SER J  32  ? 1.7646 1.7969 1.5727 -0.0585 -0.0479 -0.0514 32  SER J C   
17991 O O   . SER J  32  ? 1.8654 1.9000 1.6743 -0.0565 -0.0448 -0.0536 32  SER J O   
17992 C CB  . SER J  32  ? 1.7505 1.7817 1.5574 -0.0621 -0.0514 -0.0480 32  SER J CB  
17993 O OG  . SER J  32  ? 1.8007 1.8324 1.6057 -0.0637 -0.0503 -0.0484 32  SER J OG  
17994 N N   . GLY J  33  ? 1.7733 1.8056 1.5848 -0.0572 -0.0505 -0.0492 33  GLY J N   
17995 C CA  . GLY J  33  ? 1.8523 1.8872 1.6683 -0.0534 -0.0500 -0.0493 33  GLY J CA  
17996 C C   . GLY J  33  ? 1.6051 1.6366 1.4203 -0.0541 -0.0519 -0.0485 33  GLY J C   
17997 O O   . GLY J  33  ? 1.4152 1.4426 1.2255 -0.0579 -0.0537 -0.0482 33  GLY J O   
17998 N N   . TYR J  34  ? 1.3379 1.3712 1.1586 -0.0506 -0.0512 -0.0479 34  TYR J N   
17999 C CA  . TYR J  34  ? 1.0677 1.0980 0.8887 -0.0511 -0.0526 -0.0470 34  TYR J CA  
18000 C C   . TYR J  34  ? 1.0005 1.0290 0.8215 -0.0505 -0.0489 -0.0491 34  TYR J C   
18001 O O   . TYR J  34  ? 1.2351 1.2662 1.0588 -0.0478 -0.0454 -0.0503 34  TYR J O   
18002 C CB  . TYR J  34  ? 1.0772 1.1105 0.9048 -0.0477 -0.0547 -0.0446 34  TYR J CB  
18003 C CG  . TYR J  34  ? 1.0782 1.1135 0.9070 -0.0478 -0.0577 -0.0425 34  TYR J CG  
18004 C CD1 . TYR J  34  ? 0.9856 1.0253 0.8175 -0.0455 -0.0565 -0.0426 34  TYR J CD1 
18005 C CD2 . TYR J  34  ? 0.9626 0.9955 0.7905 -0.0501 -0.0613 -0.0403 34  TYR J CD2 
18006 C CE1 . TYR J  34  ? 1.0576 1.0987 0.8924 -0.0455 -0.0582 -0.0405 34  TYR J CE1 
18007 C CE2 . TYR J  34  ? 0.9344 0.9688 0.7653 -0.0499 -0.0630 -0.0379 34  TYR J CE2 
18008 C CZ  . TYR J  34  ? 0.9454 0.9837 0.7796 -0.0476 -0.0614 -0.0382 34  TYR J CZ  
18009 O OH  . TYR J  34  ? 0.7614 0.8008 0.5982 -0.0476 -0.0628 -0.0362 34  TYR J OH  
18010 N N   . ALA J  35  ? 1.1175 1.1415 0.9353 -0.0531 -0.0496 -0.0495 35  ALA J N   
18011 C CA  . ALA J  35  ? 1.1779 1.1994 0.9957 -0.0528 -0.0460 -0.0515 35  ALA J CA  
18012 C C   . ALA J  35  ? 1.2588 1.2775 1.0773 -0.0536 -0.0478 -0.0506 35  ALA J C   
18013 O O   . ALA J  35  ? 1.3673 1.3826 1.1809 -0.0577 -0.0505 -0.0504 35  ALA J O   
18014 C CB  . ALA J  35  ? 1.3112 1.3290 1.1222 -0.0566 -0.0434 -0.0543 35  ALA J CB  
18015 N N   . ALA J  36  ? 1.1400 1.1602 0.9646 -0.0497 -0.0463 -0.0499 36  ALA J N   
18016 C CA  . ALA J  36  ? 1.1755 1.1932 1.0015 -0.0501 -0.0478 -0.0491 36  ALA J CA  
18017 C C   . ALA J  36  ? 1.1171 1.1295 0.9383 -0.0536 -0.0454 -0.0517 36  ALA J C   
18018 O O   . ALA J  36  ? 1.2947 1.3059 1.1148 -0.0534 -0.0410 -0.0541 36  ALA J O   
18019 C CB  . ALA J  36  ? 1.2251 1.2459 1.0589 -0.0449 -0.0465 -0.0477 36  ALA J CB  
18020 N N   . ASP J  37  ? 0.9979 1.0072 0.8166 -0.0569 -0.0484 -0.0512 37  ASP J N   
18021 C CA  . ASP J  37  ? 1.1195 1.1237 0.9334 -0.0607 -0.0464 -0.0538 37  ASP J CA  
18022 C C   . ASP J  37  ? 1.2992 1.3024 1.1178 -0.0577 -0.0422 -0.0548 37  ASP J C   
18023 O O   . ASP J  37  ? 1.2647 1.2694 1.0891 -0.0546 -0.0432 -0.0530 37  ASP J O   
18024 C CB  . ASP J  37  ? 1.0772 1.0791 0.8877 -0.0650 -0.0510 -0.0527 37  ASP J CB  
18025 C CG  . ASP J  37  ? 1.2054 1.2020 1.0098 -0.0698 -0.0493 -0.0556 37  ASP J CG  
18026 O OD1 . ASP J  37  ? 1.4194 1.4142 1.2211 -0.0735 -0.0528 -0.0549 37  ASP J OD1 
18027 O OD2 . ASP J  37  ? 1.2556 1.2499 1.0580 -0.0701 -0.0443 -0.0585 37  ASP J OD2 
18028 N N   . LEU J  38  ? 1.4151 1.4156 1.2314 -0.0584 -0.0372 -0.0578 38  LEU J N   
18029 C CA  . LEU J  38  ? 1.4465 1.4461 1.2677 -0.0552 -0.0323 -0.0588 38  LEU J CA  
18030 C C   . LEU J  38  ? 1.3226 1.3186 1.1443 -0.0568 -0.0326 -0.0591 38  LEU J C   
18031 O O   . LEU J  38  ? 1.2514 1.2491 1.0796 -0.0530 -0.0326 -0.0573 38  LEU J O   
18032 C CB  . LEU J  38  ? 1.8364 1.8334 1.6547 -0.0562 -0.0266 -0.0619 38  LEU J CB  
18033 C CG  . LEU J  38  ? 1.9018 1.9012 1.7270 -0.0507 -0.0216 -0.0618 38  LEU J CG  
18034 C CD1 . LEU J  38  ? 1.8106 1.8071 1.6326 -0.0523 -0.0160 -0.0649 38  LEU J CD1 
18035 C CD2 . LEU J  38  ? 1.9135 1.9122 1.7446 -0.0478 -0.0199 -0.0609 38  LEU J CD2 
18036 N N   . LYS J  39  ? 1.6116 1.6028 1.4263 -0.0625 -0.0329 -0.0613 39  LYS J N   
18037 C CA  . LYS J  39  ? 1.6711 1.6585 1.4857 -0.0647 -0.0328 -0.0622 39  LYS J CA  
18038 C C   . LYS J  39  ? 1.6159 1.6056 1.4340 -0.0639 -0.0381 -0.0591 39  LYS J C   
18039 O O   . LYS J  39  ? 1.5568 1.5455 1.3793 -0.0624 -0.0373 -0.0587 39  LYS J O   
18040 C CB  . LYS J  39  ? 1.8656 1.8477 1.6710 -0.0717 -0.0324 -0.0654 39  LYS J CB  
18041 C CG  . LYS J  39  ? 2.0923 2.0702 1.8970 -0.0745 -0.0315 -0.0670 39  LYS J CG  
18042 C CD  . LYS J  39  ? 2.2931 2.2658 2.0884 -0.0816 -0.0303 -0.0705 39  LYS J CD  
18043 C CE  . LYS J  39  ? 2.2824 2.2507 2.0770 -0.0845 -0.0288 -0.0726 39  LYS J CE  
18044 N NZ  . LYS J  39  ? 2.1552 2.1183 1.9403 -0.0917 -0.0271 -0.0765 39  LYS J NZ  
18045 N N   . SER J  40  ? 1.2764 1.2690 1.0930 -0.0649 -0.0434 -0.0568 40  SER J N   
18046 C CA  . SER J  40  ? 1.1654 1.1600 0.9852 -0.0645 -0.0486 -0.0537 40  SER J CA  
18047 C C   . SER J  40  ? 1.1003 1.0986 0.9291 -0.0582 -0.0480 -0.0513 40  SER J C   
18048 O O   . SER J  40  ? 1.1955 1.1935 1.0286 -0.0570 -0.0488 -0.0502 40  SER J O   
18049 C CB  . SER J  40  ? 1.1083 1.1050 0.9246 -0.0669 -0.0538 -0.0516 40  SER J CB  
18050 O OG  . SER J  40  ? 1.2048 1.2030 1.0239 -0.0674 -0.0587 -0.0487 40  SER J OG  
18051 N N   . THR J  41  ? 1.0906 1.0926 0.9223 -0.0542 -0.0468 -0.0504 41  THR J N   
18052 C CA  . THR J  41  ? 0.9748 0.9808 0.8144 -0.0483 -0.0463 -0.0481 41  THR J CA  
18053 C C   . THR J  41  ? 1.0212 1.0256 0.8652 -0.0455 -0.0419 -0.0490 41  THR J C   
18054 O O   . THR J  41  ? 0.9965 1.0025 0.8465 -0.0422 -0.0424 -0.0471 41  THR J O   
18055 C CB  . THR J  41  ? 0.8583 0.8686 0.6994 -0.0451 -0.0452 -0.0475 41  THR J CB  
18056 O OG1 . THR J  41  ? 0.9852 0.9972 0.8232 -0.0472 -0.0494 -0.0463 41  THR J OG1 
18057 C CG2 . THR J  41  ? 0.8708 0.8853 0.7198 -0.0392 -0.0444 -0.0453 41  THR J CG2 
18058 N N   . GLN J  42  ? 1.1594 1.1604 1.0005 -0.0469 -0.0373 -0.0520 42  GLN J N   
18059 C CA  . GLN J  42  ? 1.1769 1.1760 1.0222 -0.0444 -0.0324 -0.0529 42  GLN J CA  
18060 C C   . GLN J  42  ? 1.1169 1.1129 0.9633 -0.0461 -0.0336 -0.0528 42  GLN J C   
18061 O O   . GLN J  42  ? 1.1687 1.1654 1.0213 -0.0423 -0.0322 -0.0515 42  GLN J O   
18062 C CB  . GLN J  42  ? 1.3194 1.3150 1.1611 -0.0461 -0.0270 -0.0563 42  GLN J CB  
18063 C CG  . GLN J  42  ? 1.4304 1.4242 1.2771 -0.0429 -0.0212 -0.0570 42  GLN J CG  
18064 C CD  . GLN J  42  ? 1.5644 1.5635 1.4191 -0.0361 -0.0201 -0.0542 42  GLN J CD  
18065 O OE1 . GLN J  42  ? 1.6453 1.6492 1.5010 -0.0340 -0.0219 -0.0526 42  GLN J OE1 
18066 N NE2 . GLN J  42  ? 1.4568 1.4550 1.3171 -0.0330 -0.0170 -0.0535 42  GLN J NE2 
18067 N N   . ASN J  43  ? 1.0466 1.0392 0.8868 -0.0519 -0.0362 -0.0543 43  ASN J N   
18068 C CA  . ASN J  43  ? 1.0514 1.0413 0.8921 -0.0543 -0.0378 -0.0543 43  ASN J CA  
18069 C C   . ASN J  43  ? 1.0021 0.9956 0.8488 -0.0513 -0.0420 -0.0507 43  ASN J C   
18070 O O   . ASN J  43  ? 0.9497 0.9423 0.8011 -0.0496 -0.0411 -0.0501 43  ASN J O   
18071 C CB  . ASN J  43  ? 1.1041 1.0907 0.9367 -0.0614 -0.0405 -0.0561 43  ASN J CB  
18072 C CG  . ASN J  43  ? 1.2869 1.2679 1.1150 -0.0650 -0.0357 -0.0602 43  ASN J CG  
18073 O OD1 . ASN J  43  ? 1.3953 1.3749 1.2213 -0.0647 -0.0312 -0.0624 43  ASN J OD1 
18074 N ND2 . ASN J  43  ? 1.3759 1.3538 1.2027 -0.0687 -0.0365 -0.0613 43  ASN J ND2 
18075 N N   . ALA J  44  ? 0.9542 0.9515 0.8007 -0.0509 -0.0463 -0.0483 44  ALA J N   
18076 C CA  . ALA J  44  ? 0.8584 0.8590 0.7105 -0.0482 -0.0502 -0.0449 44  ALA J CA  
18077 C C   . ALA J  44  ? 0.9140 0.9167 0.7736 -0.0420 -0.0471 -0.0436 44  ALA J C   
18078 O O   . ALA J  44  ? 0.9263 0.9290 0.7907 -0.0404 -0.0479 -0.0421 44  ALA J O   
18079 C CB  . ALA J  44  ? 0.6720 0.6763 0.5228 -0.0482 -0.0542 -0.0428 44  ALA J CB  
18080 N N   . ILE J  45  ? 0.8238 0.8285 0.6845 -0.0387 -0.0436 -0.0441 45  ILE J N   
18081 C CA  . ILE J  45  ? 0.8506 0.8577 0.7181 -0.0329 -0.0405 -0.0427 45  ILE J CA  
18082 C C   . ILE J  45  ? 0.8752 0.8787 0.7455 -0.0324 -0.0371 -0.0437 45  ILE J C   
18083 O O   . ILE J  45  ? 0.8394 0.8440 0.7155 -0.0291 -0.0371 -0.0417 45  ILE J O   
18084 C CB  . ILE J  45  ? 0.9231 0.9327 0.7909 -0.0300 -0.0368 -0.0434 45  ILE J CB  
18085 C CG1 . ILE J  45  ? 0.8975 0.9117 0.7646 -0.0292 -0.0400 -0.0418 45  ILE J CG1 
18086 C CG2 . ILE J  45  ? 0.9493 0.9606 0.8237 -0.0246 -0.0328 -0.0423 45  ILE J CG2 
18087 C CD1 . ILE J  45  ? 1.0348 1.0524 0.9028 -0.0262 -0.0369 -0.0422 45  ILE J CD1 
18088 N N   . ASP J  46  ? 0.8859 0.8849 0.7521 -0.0357 -0.0340 -0.0468 46  ASP J N   
18089 C CA  . ASP J  46  ? 0.8977 0.8925 0.7660 -0.0358 -0.0303 -0.0481 46  ASP J CA  
18090 C C   . ASP J  46  ? 0.8448 0.8384 0.7148 -0.0374 -0.0337 -0.0470 46  ASP J C   
18091 O O   . ASP J  46  ? 0.7790 0.7722 0.6546 -0.0345 -0.0320 -0.0460 46  ASP J O   
18092 C CB  . ASP J  46  ? 0.9437 0.9334 0.8060 -0.0403 -0.0267 -0.0520 46  ASP J CB  
18093 C CG  . ASP J  46  ? 1.3041 1.2942 1.1664 -0.0378 -0.0217 -0.0532 46  ASP J CG  
18094 O OD1 . ASP J  46  ? 1.3502 1.3445 1.2182 -0.0323 -0.0203 -0.0510 46  ASP J OD1 
18095 O OD2 . ASP J  46  ? 1.4532 1.4398 1.3101 -0.0416 -0.0191 -0.0563 46  ASP J OD2 
18096 N N   . GLU J  47  ? 0.8708 0.8640 0.7362 -0.0422 -0.0386 -0.0471 47  GLU J N   
18097 C CA  . GLU J  47  ? 0.7687 0.7608 0.6355 -0.0444 -0.0422 -0.0461 47  GLU J CA  
18098 C C   . GLU J  47  ? 0.7405 0.7368 0.6139 -0.0402 -0.0452 -0.0423 47  GLU J C   
18099 O O   . GLU J  47  ? 0.7691 0.7645 0.6468 -0.0395 -0.0456 -0.0413 47  GLU J O   
18100 C CB  . GLU J  47  ? 0.7253 0.7162 0.5853 -0.0508 -0.0466 -0.0469 47  GLU J CB  
18101 C CG  . GLU J  47  ? 0.8886 0.8747 0.7417 -0.0559 -0.0437 -0.0509 47  GLU J CG  
18102 C CD  . GLU J  47  ? 1.0048 0.9897 0.8512 -0.0626 -0.0483 -0.0516 47  GLU J CD  
18103 O OE1 . GLU J  47  ? 0.9162 0.9044 0.7628 -0.0630 -0.0537 -0.0488 47  GLU J OE1 
18104 O OE2 . GLU J  47  ? 1.0962 1.0769 0.9372 -0.0674 -0.0465 -0.0548 47  GLU J OE2 
18105 N N   . ILE J  48  ? 0.6778 0.6782 0.5519 -0.0376 -0.0470 -0.0404 48  ILE J N   
18106 C CA  . ILE J  48  ? 0.5736 0.5779 0.4538 -0.0334 -0.0492 -0.0371 48  ILE J CA  
18107 C C   . ILE J  48  ? 0.6956 0.7005 0.5820 -0.0282 -0.0449 -0.0364 48  ILE J C   
18108 O O   . ILE J  48  ? 0.7018 0.7076 0.5935 -0.0257 -0.0457 -0.0344 48  ILE J O   
18109 C CB  . ILE J  48  ? 0.6888 0.6974 0.5683 -0.0320 -0.0515 -0.0355 48  ILE J CB  
18110 C CG1 . ILE J  48  ? 0.7363 0.7447 0.6111 -0.0367 -0.0565 -0.0352 48  ILE J CG1 
18111 C CG2 . ILE J  48  ? 0.5118 0.5242 0.3978 -0.0271 -0.0523 -0.0325 48  ILE J CG2 
18112 C CD1 . ILE J  48  ? 0.7072 0.7151 0.5845 -0.0385 -0.0605 -0.0332 48  ILE J CD1 
18113 N N   . THR J  49  ? 0.6831 0.6874 0.5687 -0.0265 -0.0402 -0.0380 49  THR J N   
18114 C CA  . THR J  49  ? 0.6609 0.6655 0.5521 -0.0216 -0.0356 -0.0374 49  THR J CA  
18115 C C   . THR J  49  ? 0.7460 0.7466 0.6396 -0.0226 -0.0342 -0.0380 49  THR J C   
18116 O O   . THR J  49  ? 0.7429 0.7444 0.6422 -0.0191 -0.0337 -0.0359 49  THR J O   
18117 C CB  . THR J  49  ? 0.7851 0.7892 0.6749 -0.0203 -0.0305 -0.0392 49  THR J CB  
18118 O OG1 . THR J  49  ? 0.8393 0.8479 0.7280 -0.0186 -0.0315 -0.0383 49  THR J OG1 
18119 C CG2 . THR J  49  ? 0.6910 0.6948 0.5867 -0.0157 -0.0255 -0.0384 49  THR J CG2 
18120 N N   . ASN J  50  ? 0.6455 0.6414 0.5345 -0.0275 -0.0335 -0.0408 50  ASN J N   
18121 C CA  . ASN J  50  ? 0.7774 0.7692 0.6680 -0.0293 -0.0322 -0.0419 50  ASN J CA  
18122 C C   . ASN J  50  ? 0.7649 0.7582 0.6590 -0.0294 -0.0367 -0.0394 50  ASN J C   
18123 O O   . ASN J  50  ? 0.7159 0.7077 0.6148 -0.0277 -0.0352 -0.0388 50  ASN J O   
18124 C CB  . ASN J  50  ? 0.7264 0.7135 0.6102 -0.0357 -0.0317 -0.0455 50  ASN J CB  
18125 C CG  . ASN J  50  ? 0.7991 0.7815 0.6845 -0.0376 -0.0290 -0.0473 50  ASN J CG  
18126 O OD1 . ASN J  50  ? 0.9175 0.8967 0.8038 -0.0364 -0.0232 -0.0491 50  ASN J OD1 
18127 N ND2 . ASN J  50  ? 0.7597 0.7416 0.6454 -0.0406 -0.0330 -0.0467 50  ASN J ND2 
18128 N N   . LYS J  51  ? 0.6040 0.6000 0.4960 -0.0312 -0.0420 -0.0380 51  LYS J N   
18129 C CA  . LYS J  51  ? 0.6388 0.6365 0.5343 -0.0312 -0.0465 -0.0354 51  LYS J CA  
18130 C C   . LYS J  51  ? 0.6347 0.6350 0.5374 -0.0252 -0.0453 -0.0327 51  LYS J C   
18131 O O   . LYS J  51  ? 0.7127 0.7122 0.6201 -0.0243 -0.0454 -0.0316 51  LYS J O   
18132 C CB  . LYS J  51  ? 0.7650 0.7655 0.6573 -0.0336 -0.0519 -0.0342 51  LYS J CB  
18133 C CG  . LYS J  51  ? 0.5788 0.5810 0.4749 -0.0338 -0.0566 -0.0313 51  LYS J CG  
18134 C CD  . LYS J  51  ? 0.7085 0.7126 0.6007 -0.0371 -0.0616 -0.0303 51  LYS J CD  
18135 C CE  . LYS J  51  ? 0.6785 0.6842 0.5748 -0.0377 -0.0662 -0.0273 51  LYS J CE  
18136 N NZ  . LYS J  51  ? 0.7775 0.7839 0.6696 -0.0424 -0.0710 -0.0266 51  LYS J NZ  
18137 N N   . VAL J  52  ? 0.5658 0.5695 0.4694 -0.0212 -0.0439 -0.0317 52  VAL J N   
18138 C CA  . VAL J  52  ? 0.6009 0.6077 0.5107 -0.0156 -0.0426 -0.0291 52  VAL J CA  
18139 C C   . VAL J  52  ? 0.6610 0.6654 0.5748 -0.0129 -0.0377 -0.0294 52  VAL J C   
18140 O O   . VAL J  52  ? 0.7942 0.7992 0.7134 -0.0099 -0.0374 -0.0274 52  VAL J O   
18141 C CB  . VAL J  52  ? 0.5366 0.5477 0.4459 -0.0123 -0.0418 -0.0283 52  VAL J CB  
18142 C CG1 . VAL J  52  ? 0.3942 0.4087 0.3094 -0.0069 -0.0408 -0.0255 52  VAL J CG1 
18143 C CG2 . VAL J  52  ? 0.5901 0.6033 0.4954 -0.0150 -0.0462 -0.0281 52  VAL J CG2 
18144 N N   . ASN J  53  ? 0.5691 0.5705 0.4804 -0.0140 -0.0337 -0.0320 53  ASN J N   
18145 C CA  . ASN J  53  ? 0.7208 0.7194 0.6358 -0.0116 -0.0285 -0.0324 53  ASN J CA  
18146 C C   . ASN J  53  ? 0.8063 0.8012 0.7235 -0.0138 -0.0291 -0.0328 53  ASN J C   
18147 O O   . ASN J  53  ? 0.7825 0.7766 0.7050 -0.0106 -0.0262 -0.0317 53  ASN J O   
18148 C CB  . ASN J  53  ? 0.7996 0.7953 0.7112 -0.0129 -0.0239 -0.0353 53  ASN J CB  
18149 C CG  . ASN J  53  ? 0.8162 0.8155 0.7286 -0.0087 -0.0213 -0.0343 53  ASN J CG  
18150 O OD1 . ASN J  53  ? 0.6214 0.6255 0.5371 -0.0047 -0.0225 -0.0315 53  ASN J OD1 
18151 N ND2 . ASN J  53  ? 0.8713 0.8686 0.7809 -0.0098 -0.0175 -0.0367 53  ASN J ND2 
18152 N N   . SER J  54  ? 0.7222 0.7153 0.6355 -0.0193 -0.0328 -0.0342 54  SER J N   
18153 C CA  . SER J  54  ? 0.6526 0.6426 0.5677 -0.0220 -0.0338 -0.0347 54  SER J CA  
18154 C C   . SER J  54  ? 0.6174 0.6099 0.5387 -0.0189 -0.0362 -0.0314 54  SER J C   
18155 O O   . SER J  54  ? 0.6939 0.6845 0.6199 -0.0172 -0.0338 -0.0309 54  SER J O   
18156 C CB  . SER J  54  ? 0.6858 0.6742 0.5951 -0.0287 -0.0379 -0.0365 54  SER J CB  
18157 O OG  . SER J  54  ? 0.7765 0.7618 0.6799 -0.0321 -0.0352 -0.0399 54  SER J OG  
18158 N N   . VAL J  55  ? 0.5235 0.5199 0.4447 -0.0183 -0.0406 -0.0292 55  VAL J N   
18159 C CA  . VAL J  55  ? 0.6181 0.6171 0.5451 -0.0154 -0.0429 -0.0261 55  VAL J CA  
18160 C C   . VAL J  55  ? 0.7007 0.7004 0.6330 -0.0096 -0.0385 -0.0246 55  VAL J C   
18161 O O   . VAL J  55  ? 0.6450 0.6448 0.5826 -0.0076 -0.0387 -0.0228 55  VAL J O   
18162 C CB  . VAL J  55  ? 0.5931 0.5963 0.5190 -0.0150 -0.0472 -0.0241 55  VAL J CB  
18163 C CG1 . VAL J  55  ? 0.6390 0.6446 0.5711 -0.0116 -0.0487 -0.0210 55  VAL J CG1 
18164 C CG2 . VAL J  55  ? 0.5379 0.5406 0.4592 -0.0207 -0.0518 -0.0250 55  VAL J CG2 
18165 N N   . ILE J  56  ? 0.5942 0.5944 0.5252 -0.0070 -0.0347 -0.0253 56  ILE J N   
18166 C CA  . ILE J  56  ? 0.5827 0.5842 0.5185 -0.0014 -0.0305 -0.0236 56  ILE J CA  
18167 C C   . ILE J  56  ? 0.6552 0.6523 0.5931 -0.0009 -0.0254 -0.0249 56  ILE J C   
18168 O O   . ILE J  56  ? 0.6139 0.6105 0.5571 0.0024  -0.0232 -0.0233 56  ILE J O   
18169 C CB  . ILE J  56  ? 0.6279 0.6331 0.5620 0.0016  -0.0289 -0.0231 56  ILE J CB  
18170 C CG1 . ILE J  56  ? 0.7221 0.7320 0.6552 0.0021  -0.0332 -0.0214 56  ILE J CG1 
18171 C CG2 . ILE J  56  ? 0.5369 0.5432 0.4757 0.0071  -0.0241 -0.0214 56  ILE J CG2 
18172 C CD1 . ILE J  56  ? 0.6337 0.6476 0.5649 0.0045  -0.0320 -0.0211 56  ILE J CD1 
18173 N N   . GLU J  57  ? 0.5668 0.5606 0.5007 -0.0042 -0.0233 -0.0280 57  GLU J N   
18174 C CA  . GLU J  57  ? 0.6965 0.6858 0.6321 -0.0038 -0.0177 -0.0295 57  GLU J CA  
18175 C C   . GLU J  57  ? 0.6628 0.6483 0.6013 -0.0059 -0.0178 -0.0301 57  GLU J C   
18176 O O   . GLU J  57  ? 0.8179 0.8006 0.7603 -0.0039 -0.0132 -0.0302 57  GLU J O   
18177 C CB  . GLU J  57  ? 0.9058 0.8921 0.8360 -0.0072 -0.0153 -0.0330 57  GLU J CB  
18178 C CG  . GLU J  57  ? 1.3477 1.3302 1.2801 -0.0054 -0.0083 -0.0342 57  GLU J CG  
18179 C CD  . GLU J  57  ? 1.5147 1.4911 1.4458 -0.0102 -0.0066 -0.0374 57  GLU J CD  
18180 O OE1 . GLU J  57  ? 1.3814 1.3566 1.3078 -0.0158 -0.0105 -0.0394 57  GLU J OE1 
18181 O OE2 . GLU J  57  ? 1.3606 1.3335 1.2954 -0.0084 -0.0012 -0.0379 57  GLU J OE2 
18182 N N   . LYS J  58  ? 0.6178 0.6037 0.5548 -0.0098 -0.0231 -0.0302 58  LYS J N   
18183 C CA  . LYS J  58  ? 0.5580 0.5407 0.4973 -0.0126 -0.0238 -0.0309 58  LYS J CA  
18184 C C   . LYS J  58  ? 0.6811 0.6649 0.6275 -0.0085 -0.0236 -0.0279 58  LYS J C   
18185 O O   . LYS J  58  ? 0.7395 0.7205 0.6889 -0.0100 -0.0231 -0.0283 58  LYS J O   
18186 C CB  . LYS J  58  ? 0.5981 0.5810 0.5333 -0.0185 -0.0297 -0.0319 58  LYS J CB  
18187 C CG  . LYS J  58  ? 0.7556 0.7358 0.6837 -0.0238 -0.0293 -0.0355 58  LYS J CG  
18188 C CD  . LYS J  58  ? 0.6815 0.6562 0.6095 -0.0254 -0.0238 -0.0385 58  LYS J CD  
18189 C CE  . LYS J  58  ? 0.7546 0.7266 0.6752 -0.0309 -0.0231 -0.0423 58  LYS J CE  
18190 N NZ  . LYS J  58  ? 0.5820 0.5482 0.5023 -0.0328 -0.0174 -0.0455 58  LYS J NZ  
18191 N N   . MET J  59  ? 0.6441 0.6321 0.5930 -0.0035 -0.0238 -0.0249 59  MET J N   
18192 C CA  . MET J  59  ? 0.6309 0.6197 0.5861 0.0011  -0.0223 -0.0222 59  MET J CA  
18193 C C   . MET J  59  ? 0.7756 0.7619 0.7334 0.0044  -0.0157 -0.0225 59  MET J C   
18194 O O   . MET J  59  ? 0.9991 0.9860 0.9550 0.0062  -0.0127 -0.0229 59  MET J O   
18195 C CB  . MET J  59  ? 0.7956 0.7899 0.7524 0.0051  -0.0246 -0.0190 59  MET J CB  
18196 C CG  . MET J  59  ? 0.7501 0.7453 0.7130 0.0087  -0.0243 -0.0162 59  MET J CG  
18197 S SD  . MET J  59  ? 0.7299 0.7228 0.6953 0.0046  -0.0282 -0.0164 59  MET J SD  
18198 C CE  . MET J  59  ? 0.6450 0.6427 0.6101 0.0046  -0.0340 -0.0141 59  MET J CE  
18199 N N   . ASN J  60  ? 0.7523 0.7355 0.7147 0.0050  -0.0133 -0.0222 60  ASN J N   
18200 C CA  . ASN J  60  ? 0.9114 0.8924 0.8774 0.0090  -0.0070 -0.0217 60  ASN J CA  
18201 C C   . ASN J  60  ? 0.8052 0.7856 0.7774 0.0114  -0.0064 -0.0195 60  ASN J C   
18202 O O   . ASN J  60  ? 0.9033 0.8798 0.8774 0.0087  -0.0058 -0.0209 60  ASN J O   
18203 C CB  . ASN J  60  ? 1.1021 1.0778 1.0659 0.0058  -0.0028 -0.0252 60  ASN J CB  
18204 C CG  . ASN J  60  ? 1.4071 1.3784 1.3718 0.0013  -0.0032 -0.0274 60  ASN J CG  
18205 O OD1 . ASN J  60  ? 1.5236 1.4920 1.4932 0.0031  0.0004  -0.0269 60  ASN J OD1 
18206 N ND2 . ASN J  60  ? 1.2040 1.1747 1.1641 -0.0046 -0.0075 -0.0297 60  ASN J ND2 
18207 N N   . THR J  61  ? 0.8217 0.8062 0.7968 0.0163  -0.0069 -0.0161 61  THR J N   
18208 C CA  . THR J  61  ? 0.7535 0.7382 0.7341 0.0186  -0.0071 -0.0137 61  THR J CA  
18209 C C   . THR J  61  ? 0.7646 0.7460 0.7500 0.0219  -0.0011 -0.0129 61  THR J C   
18210 O O   . THR J  61  ? 0.8336 0.8142 0.8188 0.0241  0.0035  -0.0131 61  THR J O   
18211 C CB  . THR J  61  ? 0.8702 0.8603 0.8517 0.0223  -0.0098 -0.0104 61  THR J CB  
18212 O OG1 . THR J  61  ? 0.8973 0.8904 0.8782 0.0265  -0.0069 -0.0089 61  THR J OG1 
18213 C CG2 . THR J  61  ? 0.7308 0.7237 0.7085 0.0189  -0.0158 -0.0110 61  THR J CG2 
18214 N N   . GLN J  62  ? 0.7702 0.7497 0.7601 0.0222  -0.0010 -0.0120 62  GLN J N   
18215 C CA  . GLN J  62  ? 0.8546 0.8310 0.8495 0.0254  0.0046  -0.0109 62  GLN J CA  
18216 C C   . GLN J  62  ? 0.8417 0.8220 0.8395 0.0317  0.0063  -0.0069 62  GLN J C   
18217 O O   . GLN J  62  ? 0.8295 0.8144 0.8265 0.0330  0.0025  -0.0050 62  GLN J O   
18218 C CB  . GLN J  62  ? 0.7375 0.7107 0.7364 0.0232  0.0039  -0.0114 62  GLN J CB  
18219 C CG  . GLN J  62  ? 0.6967 0.6658 0.6932 0.0168  0.0028  -0.0153 62  GLN J CG  
18220 C CD  . GLN J  62  ? 0.8928 0.8572 0.8885 0.0161  0.0086  -0.0178 62  GLN J CD  
18221 O OE1 . GLN J  62  ? 1.1118 1.0767 1.1037 0.0161  0.0101  -0.0189 62  GLN J OE1 
18222 N NE2 . GLN J  62  ? 0.8230 0.7827 0.8226 0.0153  0.0123  -0.0188 62  GLN J NE2 
18223 N N   . PHE J  63  ? 0.8117 0.7903 0.8130 0.0355  0.0121  -0.0055 63  PHE J N   
18224 C CA  . PHE J  63  ? 0.7616 0.7438 0.7660 0.0415  0.0139  -0.0014 63  PHE J CA  
18225 C C   . PHE J  63  ? 0.5477 0.5291 0.5564 0.0423  0.0129  0.0003  63  PHE J C   
18226 O O   . PHE J  63  ? 0.7655 0.7425 0.7782 0.0423  0.0162  0.0000  63  PHE J O   
18227 C CB  . PHE J  63  ? 0.6725 0.6531 0.6797 0.0454  0.0205  0.0000  63  PHE J CB  
18228 C CG  . PHE J  63  ? 0.7269 0.7120 0.7367 0.0515  0.0221  0.0045  63  PHE J CG  
18229 C CD1 . PHE J  63  ? 0.6553 0.6454 0.6630 0.0543  0.0223  0.0062  63  PHE J CD1 
18230 C CD2 . PHE J  63  ? 0.6459 0.6304 0.6602 0.0542  0.0234  0.0071  63  PHE J CD2 
18231 C CE1 . PHE J  63  ? 0.7140 0.7087 0.7240 0.0596  0.0236  0.0105  63  PHE J CE1 
18232 C CE2 . PHE J  63  ? 0.7138 0.7026 0.7302 0.0596  0.0248  0.0113  63  PHE J CE2 
18233 C CZ  . PHE J  63  ? 0.8125 0.8065 0.8266 0.0622  0.0248  0.0130  63  PHE J CZ  
18234 N N   . THR J  64  ? 0.5727 0.5584 0.5808 0.0429  0.0085  0.0019  64  THR J N   
18235 C CA  . THR J  64  ? 0.7398 0.7250 0.7518 0.0436  0.0074  0.0036  64  THR J CA  
18236 C C   . THR J  64  ? 0.5437 0.5340 0.5562 0.0479  0.0065  0.0071  64  THR J C   
18237 O O   . THR J  64  ? 0.5235 0.5183 0.5322 0.0484  0.0042  0.0076  64  THR J O   
18238 C CB  . THR J  64  ? 0.7295 0.7138 0.7407 0.0385  0.0022  0.0015  64  THR J CB  
18239 O OG1 . THR J  64  ? 0.6850 0.6728 0.6910 0.0363  -0.0022 0.0005  64  THR J OG1 
18240 C CG2 . THR J  64  ? 0.6658 0.6447 0.6777 0.0342  0.0033  -0.0017 64  THR J CG2 
18241 N N   . ALA J  65  ? 0.4788 0.4683 0.4958 0.0506  0.0084  0.0094  65  ALA J N   
18242 C CA  . ALA J  65  ? 0.5511 0.5451 0.5685 0.0541  0.0074  0.0126  65  ALA J CA  
18243 C C   . ALA J  65  ? 0.5382 0.5317 0.5575 0.0520  0.0039  0.0125  65  ALA J C   
18244 O O   . ALA J  65  ? 0.7429 0.7341 0.7667 0.0533  0.0057  0.0138  65  ALA J O   
18245 C CB  . ALA J  65  ? 0.5394 0.5332 0.5603 0.0592  0.0125  0.0158  65  ALA J CB  
18246 N N   . VAL J  66  ? 0.5161 0.5116 0.5322 0.0488  -0.0010 0.0110  66  VAL J N   
18247 C CA  . VAL J  66  ? 0.4893 0.4850 0.5073 0.0470  -0.0045 0.0113  66  VAL J CA  
18248 C C   . VAL J  66  ? 0.5890 0.5872 0.6088 0.0511  -0.0033 0.0144  66  VAL J C   
18249 O O   . VAL J  66  ? 0.7280 0.7296 0.7458 0.0545  -0.0015 0.0162  66  VAL J O   
18250 C CB  . VAL J  66  ? 0.3770 0.3750 0.3911 0.0434  -0.0098 0.0097  66  VAL J CB  
18251 C CG1 . VAL J  66  ? 0.5022 0.5037 0.5110 0.0441  -0.0100 0.0092  66  VAL J CG1 
18252 C CG2 . VAL J  66  ? 0.4864 0.4866 0.5019 0.0436  -0.0126 0.0111  66  VAL J CG2 
18253 N N   . GLY J  67  ? 0.5803 0.5771 0.6040 0.0507  -0.0041 0.0152  67  GLY J N   
18254 C CA  . GLY J  67  ? 0.7679 0.7666 0.7935 0.0542  -0.0026 0.0180  67  GLY J CA  
18255 C C   . GLY J  67  ? 0.5094 0.5049 0.5396 0.0570  0.0020  0.0196  67  GLY J C   
18256 O O   . GLY J  67  ? 0.4135 0.4081 0.4436 0.0590  0.0056  0.0200  67  GLY J O   
18257 N N   . LYS J  68  ? 0.6179 0.6115 0.6524 0.0571  0.0022  0.0205  68  LYS J N   
18258 C CA  . LYS J  68  ? 0.4558 0.4461 0.4951 0.0596  0.0066  0.0220  68  LYS J CA  
18259 C C   . LYS J  68  ? 0.5768 0.5688 0.6176 0.0627  0.0077  0.0248  68  LYS J C   
18260 O O   . LYS J  68  ? 0.5566 0.5519 0.5949 0.0623  0.0050  0.0252  68  LYS J O   
18261 C CB  . LYS J  68  ? 0.5934 0.5790 0.6373 0.0564  0.0062  0.0202  68  LYS J CB  
18262 C CG  . LYS J  68  ? 0.5672 0.5509 0.6093 0.0526  0.0047  0.0171  68  LYS J CG  
18263 C CD  . LYS J  68  ? 0.6531 0.6342 0.6953 0.0543  0.0094  0.0169  68  LYS J CD  
18264 C CE  . LYS J  68  ? 0.8244 0.8049 0.8628 0.0510  0.0081  0.0140  68  LYS J CE  
18265 N NZ  . LYS J  68  ? 0.6887 0.6703 0.7244 0.0541  0.0116  0.0147  68  LYS J NZ  
18266 N N   . GLU J  69  ? 0.5484 0.5379 0.5930 0.0655  0.0119  0.0267  69  GLU J N   
18267 C CA  . GLU J  69  ? 0.5332 0.5238 0.5795 0.0682  0.0134  0.0293  69  GLU J CA  
18268 C C   . GLU J  69  ? 0.4901 0.4760 0.5427 0.0677  0.0150  0.0294  69  GLU J C   
18269 O O   . GLU J  69  ? 0.5603 0.5423 0.6161 0.0678  0.0179  0.0290  69  GLU J O   
18270 C CB  . GLU J  69  ? 0.6707 0.6635 0.7152 0.0729  0.0173  0.0322  69  GLU J CB  
18271 C CG  . GLU J  69  ? 0.8014 0.7995 0.8399 0.0737  0.0158  0.0325  69  GLU J CG  
18272 C CD  . GLU J  69  ? 0.8466 0.8471 0.8839 0.0782  0.0197  0.0356  69  GLU J CD  
18273 O OE1 . GLU J  69  ? 0.8390 0.8363 0.8800 0.0804  0.0238  0.0371  69  GLU J OE1 
18274 O OE2 . GLU J  69  ? 0.7519 0.7577 0.7847 0.0795  0.0186  0.0367  69  GLU J OE2 
18275 N N   . PHE J  70  ? 0.4331 0.4193 0.4875 0.0669  0.0134  0.0298  70  PHE J N   
18276 C CA  . PHE J  70  ? 0.5103 0.4925 0.5711 0.0663  0.0147  0.0301  70  PHE J CA  
18277 C C   . PHE J  70  ? 0.5348 0.5179 0.5967 0.0689  0.0165  0.0325  70  PHE J C   
18278 O O   . PHE J  70  ? 0.6327 0.6194 0.6909 0.0692  0.0147  0.0330  70  PHE J O   
18279 C CB  . PHE J  70  ? 0.5273 0.5083 0.5907 0.0617  0.0105  0.0278  70  PHE J CB  
18280 C CG  . PHE J  70  ? 0.4968 0.4772 0.5583 0.0586  0.0083  0.0252  70  PHE J CG  
18281 C CD1 . PHE J  70  ? 0.4107 0.3873 0.4752 0.0576  0.0104  0.0240  70  PHE J CD1 
18282 C CD2 . PHE J  70  ? 0.4691 0.4527 0.5258 0.0564  0.0042  0.0238  70  PHE J CD2 
18283 C CE1 . PHE J  70  ? 0.4756 0.4514 0.5380 0.0544  0.0086  0.0214  70  PHE J CE1 
18284 C CE2 . PHE J  70  ? 0.4098 0.3928 0.4645 0.0534  0.0023  0.0214  70  PHE J CE2 
18285 C CZ  . PHE J  70  ? 0.4155 0.3945 0.4728 0.0523  0.0045  0.0201  70  PHE J CZ  
18286 N N   . ASN J  71  ? 0.4654 0.4450 0.5321 0.0707  0.0202  0.0339  71  ASN J N   
18287 C CA  . ASN J  71  ? 0.5470 0.5269 0.6150 0.0729  0.0222  0.0361  71  ASN J CA  
18288 C C   . ASN J  71  ? 0.6161 0.5950 0.6880 0.0702  0.0197  0.0352  71  ASN J C   
18289 O O   . ASN J  71  ? 0.6022 0.5803 0.6762 0.0667  0.0163  0.0331  71  ASN J O   
18290 C CB  . ASN J  71  ? 0.4992 0.4759 0.5708 0.0761  0.0275  0.0381  71  ASN J CB  
18291 C CG  . ASN J  71  ? 0.6154 0.5871 0.6936 0.0742  0.0284  0.0368  71  ASN J CG  
18292 O OD1 . ASN J  71  ? 0.7422 0.7124 0.8245 0.0715  0.0263  0.0357  71  ASN J OD1 
18293 N ND2 . ASN J  71  ? 0.7688 0.7380 0.8483 0.0756  0.0318  0.0371  71  ASN J ND2 
18294 N N   . HIS J  72  ? 0.5655 0.5446 0.6384 0.0719  0.0214  0.0369  72  HIS J N   
18295 C CA  . HIS J  72  ? 0.6105 0.5889 0.6870 0.0698  0.0194  0.0364  72  HIS J CA  
18296 C C   . HIS J  72  ? 0.6360 0.6104 0.7201 0.0674  0.0189  0.0354  72  HIS J C   
18297 O O   . HIS J  72  ? 0.7858 0.7601 0.8733 0.0648  0.0161  0.0347  72  HIS J O   
18298 C CB  . HIS J  72  ? 0.7415 0.7201 0.8178 0.0722  0.0225  0.0384  72  HIS J CB  
18299 C CG  . HIS J  72  ? 1.0030 0.9786 1.0825 0.0752  0.0274  0.0404  72  HIS J CG  
18300 N ND1 . HIS J  72  ? 1.0161 0.9927 1.0918 0.0784  0.0304  0.0421  72  HIS J ND1 
18301 C CD2 . HIS J  72  ? 0.9502 0.9218 1.0363 0.0754  0.0299  0.0410  72  HIS J CD2 
18302 C CE1 . HIS J  72  ? 1.0691 1.0423 1.1489 0.0805  0.0347  0.0437  72  HIS J CE1 
18303 N NE2 . HIS J  72  ? 0.9885 0.9586 1.0746 0.0787  0.0345  0.0430  72  HIS J NE2 
18304 N N   . LEU J  73  ? 0.4987 0.4701 0.5856 0.0682  0.0216  0.0355  73  LEU J N   
18305 C CA  . LEU J  73  ? 0.5525 0.5203 0.6466 0.0659  0.0214  0.0346  73  LEU J CA  
18306 C C   . LEU J  73  ? 0.4660 0.4336 0.5596 0.0626  0.0183  0.0321  73  LEU J C   
18307 O O   . LEU J  73  ? 0.4966 0.4613 0.5953 0.0607  0.0187  0.0311  73  LEU J O   
18308 C CB  . LEU J  73  ? 0.6591 0.6231 0.7574 0.0685  0.0266  0.0360  73  LEU J CB  
18309 C CG  . LEU J  73  ? 0.5954 0.5586 0.6959 0.0710  0.0297  0.0382  73  LEU J CG  
18310 C CD1 . LEU J  73  ? 0.7522 0.7118 0.8560 0.0738  0.0351  0.0398  73  LEU J CD1 
18311 C CD2 . LEU J  73  ? 0.5634 0.5259 0.6697 0.0684  0.0274  0.0377  73  LEU J CD2 
18312 N N   . GLU J  74  ? 0.4035 0.3743 0.4909 0.0618  0.0154  0.0311  74  GLU J N   
18313 C CA  . GLU J  74  ? 0.5013 0.4722 0.5872 0.0585  0.0125  0.0287  74  GLU J CA  
18314 C C   . GLU J  74  ? 0.5314 0.5058 0.6141 0.0558  0.0073  0.0277  74  GLU J C   
18315 O O   . GLU J  74  ? 0.5321 0.5080 0.6103 0.0540  0.0049  0.0260  74  GLU J O   
18316 C CB  . GLU J  74  ? 0.4703 0.4412 0.5517 0.0604  0.0150  0.0285  74  GLU J CB  
18317 C CG  . GLU J  74  ? 0.4127 0.3798 0.4975 0.0628  0.0202  0.0294  74  GLU J CG  
18318 C CD  . GLU J  74  ? 0.7203 0.6875 0.8009 0.0651  0.0231  0.0296  74  GLU J CD  
18319 O OE1 . GLU J  74  ? 0.6357 0.6065 0.7111 0.0675  0.0231  0.0309  74  GLU J OE1 
18320 O OE2 . GLU J  74  ? 0.4800 0.4439 0.5628 0.0644  0.0254  0.0285  74  GLU J OE2 
18321 N N   . LYS J  75  ? 0.4631 0.4385 0.5481 0.0554  0.0057  0.0286  75  LYS J N   
18322 C CA  . LYS J  75  ? 0.4939 0.4724 0.5766 0.0530  0.0011  0.0279  75  LYS J CA  
18323 C C   . LYS J  75  ? 0.4898 0.4680 0.5740 0.0486  -0.0030 0.0260  75  LYS J C   
18324 O O   . LYS J  75  ? 0.4993 0.4800 0.5798 0.0464  -0.0069 0.0250  75  LYS J O   
18325 C CB  . LYS J  75  ? 0.4790 0.4578 0.5653 0.0532  0.0008  0.0293  75  LYS J CB  
18326 C CG  . LYS J  75  ? 0.6029 0.5844 0.6880 0.0506  -0.0038 0.0287  75  LYS J CG  
18327 C CD  . LYS J  75  ? 0.6187 0.6036 0.6956 0.0513  -0.0049 0.0280  75  LYS J CD  
18328 C CE  . LYS J  75  ? 0.8282 0.8143 0.9020 0.0545  -0.0019 0.0294  75  LYS J CE  
18329 N NZ  . LYS J  75  ? 1.0274 1.0173 1.0934 0.0550  -0.0032 0.0288  75  LYS J NZ  
18330 N N   . ARG J  76  ? 0.5390 0.5142 0.6287 0.0472  -0.0021 0.0255  76  ARG J N   
18331 C CA  . ARG J  76  ? 0.3847 0.3597 0.4760 0.0427  -0.0059 0.0237  76  ARG J CA  
18332 C C   . ARG J  76  ? 0.4590 0.4346 0.5440 0.0414  -0.0069 0.0216  76  ARG J C   
18333 O O   . ARG J  76  ? 0.4445 0.4224 0.5263 0.0385  -0.0111 0.0205  76  ARG J O   
18334 C CB  . ARG J  76  ? 0.4610 0.4328 0.5598 0.0413  -0.0046 0.0236  76  ARG J CB  
18335 C CG  . ARG J  76  ? 0.3801 0.3520 0.4861 0.0407  -0.0058 0.0253  76  ARG J CG  
18336 C CD  . ARG J  76  ? 0.4817 0.4507 0.5954 0.0396  -0.0042 0.0253  76  ARG J CD  
18337 N NE  . ARG J  76  ? 0.3947 0.3605 0.5082 0.0427  0.0013  0.0254  76  ARG J NE  
18338 C CZ  . ARG J  76  ? 0.4755 0.4384 0.5921 0.0414  0.0032  0.0242  76  ARG J CZ  
18339 N NH1 . ARG J  76  ? 0.5749 0.5377 0.6946 0.0369  -0.0001 0.0227  76  ARG J NH1 
18340 N NH2 . ARG J  76  ? 0.5082 0.4681 0.6247 0.0446  0.0085  0.0246  76  ARG J NH2 
18341 N N   . ILE J  77  ? 0.5086 0.4822 0.5919 0.0434  -0.0029 0.0212  77  ILE J N   
18342 C CA  . ILE J  77  ? 0.4954 0.4693 0.5728 0.0425  -0.0031 0.0193  77  ILE J CA  
18343 C C   . ILE J  77  ? 0.4413 0.4188 0.5118 0.0438  -0.0047 0.0196  77  ILE J C   
18344 O O   . ILE J  77  ? 0.4827 0.4615 0.5484 0.0418  -0.0068 0.0178  77  ILE J O   
18345 C CB  . ILE J  77  ? 0.4146 0.3853 0.4920 0.0449  0.0022  0.0191  77  ILE J CB  
18346 C CG1 . ILE J  77  ? 0.6772 0.6475 0.7564 0.0498  0.0065  0.0218  77  ILE J CG1 
18347 C CG2 . ILE J  77  ? 0.4310 0.3980 0.5133 0.0420  0.0030  0.0175  77  ILE J CG2 
18348 C CD1 . ILE J  77  ? 0.7117 0.6788 0.7920 0.0525  0.0120  0.0222  77  ILE J CD1 
18349 N N   . GLU J  78  ? 0.3396 0.3190 0.4098 0.0469  -0.0037 0.0216  78  GLU J N   
18350 C CA  . GLU J  78  ? 0.4116 0.3948 0.4757 0.0479  -0.0054 0.0219  78  GLU J CA  
18351 C C   . GLU J  78  ? 0.4762 0.4615 0.5392 0.0440  -0.0107 0.0207  78  GLU J C   
18352 O O   . GLU J  78  ? 0.5639 0.5516 0.6212 0.0431  -0.0128 0.0197  78  GLU J O   
18353 C CB  . GLU J  78  ? 0.4315 0.4160 0.4958 0.0514  -0.0032 0.0242  78  GLU J CB  
18354 C CG  . GLU J  78  ? 0.4852 0.4739 0.5432 0.0524  -0.0047 0.0244  78  GLU J CG  
18355 C CD  . GLU J  78  ? 0.8549 0.8450 0.9131 0.0553  -0.0027 0.0264  78  GLU J CD  
18356 O OE1 . GLU J  78  ? 1.0637 1.0516 1.1253 0.0577  0.0010  0.0279  78  GLU J OE1 
18357 O OE2 . GLU J  78  ? 0.9969 0.9900 1.0514 0.0550  -0.0046 0.0264  78  GLU J OE2 
18358 N N   . ASN J  79  ? 0.4756 0.4600 0.5442 0.0418  -0.0128 0.0211  79  ASN J N   
18359 C CA  . ASN J  79  ? 0.4406 0.4269 0.5091 0.0381  -0.0179 0.0205  79  ASN J CA  
18360 C C   . ASN J  79  ? 0.5001 0.4858 0.5671 0.0342  -0.0206 0.0183  79  ASN J C   
18361 O O   . ASN J  79  ? 0.5093 0.4971 0.5728 0.0315  -0.0245 0.0174  79  ASN J O   
18362 C CB  . ASN J  79  ? 0.4153 0.4011 0.4910 0.0373  -0.0192 0.0220  79  ASN J CB  
18363 C CG  . ASN J  79  ? 0.6026 0.5897 0.6784 0.0401  -0.0177 0.0238  79  ASN J CG  
18364 O OD1 . ASN J  79  ? 0.6274 0.6169 0.6974 0.0415  -0.0178 0.0236  79  ASN J OD1 
18365 N ND2 . ASN J  79  ? 0.5171 0.5027 0.5995 0.0409  -0.0164 0.0253  79  ASN J ND2 
18366 N N   . LEU J  80  ? 0.3789 0.3616 0.4485 0.0336  -0.0183 0.0174  80  LEU J N   
18367 C CA  . LEU J  80  ? 0.3593 0.3410 0.4268 0.0299  -0.0201 0.0150  80  LEU J CA  
18368 C C   . LEU J  80  ? 0.4493 0.4325 0.5088 0.0305  -0.0199 0.0137  80  LEU J C   
18369 O O   . LEU J  80  ? 0.4910 0.4755 0.5466 0.0273  -0.0234 0.0122  80  LEU J O   
18370 C CB  . LEU J  80  ? 0.3828 0.3606 0.4537 0.0299  -0.0165 0.0142  80  LEU J CB  
18371 C CG  . LEU J  80  ? 0.3759 0.3522 0.4476 0.0249  -0.0184 0.0118  80  LEU J CG  
18372 C CD1 . LEU J  80  ? 0.3309 0.3032 0.4034 0.0258  -0.0136 0.0104  80  LEU J CD1 
18373 C CD2 . LEU J  80  ? 0.4000 0.3784 0.4653 0.0216  -0.0223 0.0100  80  LEU J CD2 
18374 N N   . ASN J  81  ? 0.4277 0.4107 0.4851 0.0348  -0.0158 0.0145  81  ASN J N   
18375 C CA  . ASN J  81  ? 0.4104 0.3952 0.4609 0.0360  -0.0151 0.0137  81  ASN J CA  
18376 C C   . ASN J  81  ? 0.5061 0.4946 0.5525 0.0351  -0.0190 0.0138  81  ASN J C   
18377 O O   . ASN J  81  ? 0.4727 0.4626 0.5138 0.0333  -0.0209 0.0123  81  ASN J O   
18378 C CB  . ASN J  81  ? 0.3858 0.3704 0.4357 0.0411  -0.0102 0.0154  81  ASN J CB  
18379 C CG  . ASN J  81  ? 0.4956 0.4825 0.5390 0.0427  -0.0094 0.0149  81  ASN J CG  
18380 O OD1 . ASN J  81  ? 0.4341 0.4199 0.4748 0.0412  -0.0089 0.0130  81  ASN J OD1 
18381 N ND2 . ASN J  81  ? 0.5326 0.5229 0.5735 0.0456  -0.0091 0.0166  81  ASN J ND2 
18382 N N   . LYS J  82  ? 0.4104 0.4006 0.4592 0.0362  -0.0201 0.0157  82  LYS J N   
18383 C CA  . LYS J  82  ? 0.4629 0.4564 0.5084 0.0352  -0.0236 0.0158  82  LYS J CA  
18384 C C   . LYS J  82  ? 0.5354 0.5292 0.5807 0.0304  -0.0284 0.0145  82  LYS J C   
18385 O O   . LYS J  82  ? 0.4320 0.4281 0.4725 0.0289  -0.0311 0.0137  82  LYS J O   
18386 C CB  . LYS J  82  ? 0.4618 0.4563 0.5108 0.0371  -0.0234 0.0179  82  LYS J CB  
18387 C CG  . LYS J  82  ? 0.6859 0.6832 0.7328 0.0355  -0.0270 0.0181  82  LYS J CG  
18388 C CD  . LYS J  82  ? 0.8387 0.8365 0.8892 0.0373  -0.0262 0.0200  82  LYS J CD  
18389 C CE  . LYS J  82  ? 1.0758 1.0758 1.1257 0.0352  -0.0298 0.0201  82  LYS J CE  
18390 N NZ  . LYS J  82  ? 0.9933 0.9960 1.0357 0.0349  -0.0311 0.0189  82  LYS J NZ  
18391 N N   . LYS J  83  ? 0.5617 0.5533 0.6121 0.0280  -0.0293 0.0143  83  LYS J N   
18392 C CA  . LYS J  83  ? 0.4600 0.4522 0.5106 0.0232  -0.0340 0.0134  83  LYS J CA  
18393 C C   . LYS J  83  ? 0.4528 0.4448 0.4972 0.0208  -0.0348 0.0108  83  LYS J C   
18394 O O   . LYS J  83  ? 0.5478 0.5416 0.5885 0.0179  -0.0386 0.0101  83  LYS J O   
18395 C CB  . LYS J  83  ? 0.3493 0.3396 0.4070 0.0210  -0.0348 0.0138  83  LYS J CB  
18396 C CG  . LYS J  83  ? 0.4550 0.4463 0.5128 0.0158  -0.0398 0.0130  83  LYS J CG  
18397 C CD  . LYS J  83  ? 0.4358 0.4262 0.5014 0.0136  -0.0411 0.0140  83  LYS J CD  
18398 C CE  . LYS J  83  ? 0.4388 0.4259 0.5063 0.0132  -0.0380 0.0125  83  LYS J CE  
18399 N NZ  . LYS J  83  ? 0.5022 0.4888 0.5761 0.0096  -0.0403 0.0128  83  LYS J NZ  
18400 N N   . VAL J  84  ? 0.3751 0.3647 0.4183 0.0221  -0.0309 0.0096  84  VAL J N   
18401 C CA  . VAL J  84  ? 0.5051 0.4939 0.5427 0.0199  -0.0309 0.0070  84  VAL J CA  
18402 C C   . VAL J  84  ? 0.4386 0.4301 0.4696 0.0214  -0.0312 0.0068  84  VAL J C   
18403 O O   . VAL J  84  ? 0.5689 0.5609 0.5949 0.0187  -0.0329 0.0049  84  VAL J O   
18404 C CB  . VAL J  84  ? 0.4071 0.3924 0.4456 0.0211  -0.0261 0.0058  84  VAL J CB  
18405 C CG1 . VAL J  84  ? 0.5706 0.5560 0.6086 0.0265  -0.0215 0.0073  84  VAL J CG1 
18406 C CG2 . VAL J  84  ? 0.6072 0.5911 0.6405 0.0178  -0.0263 0.0029  84  VAL J CG2 
18407 N N   . ASP J  85  ? 0.3852 0.3786 0.4164 0.0255  -0.0294 0.0087  85  ASP J N   
18408 C CA  . ASP J  85  ? 0.4222 0.4186 0.4476 0.0270  -0.0299 0.0086  85  ASP J CA  
18409 C C   . ASP J  85  ? 0.4550 0.4540 0.4789 0.0243  -0.0347 0.0087  85  ASP J C   
18410 O O   . ASP J  85  ? 0.5313 0.5319 0.5497 0.0228  -0.0366 0.0075  85  ASP J O   
18411 C CB  . ASP J  85  ? 0.4042 0.4021 0.4302 0.0319  -0.0266 0.0106  85  ASP J CB  
18412 C CG  . ASP J  85  ? 0.5856 0.5820 0.6111 0.0350  -0.0218 0.0106  85  ASP J CG  
18413 O OD1 . ASP J  85  ? 0.5802 0.5746 0.6042 0.0335  -0.0208 0.0088  85  ASP J OD1 
18414 O OD2 . ASP J  85  ? 0.7340 0.7312 0.7607 0.0390  -0.0188 0.0125  85  ASP J OD2 
18415 N N   . ASP J  86  ? 0.3777 0.3769 0.4066 0.0237  -0.0366 0.0103  86  ASP J N   
18416 C CA  . ASP J  86  ? 0.3785 0.3799 0.4069 0.0213  -0.0410 0.0109  86  ASP J CA  
18417 C C   . ASP J  86  ? 0.5324 0.5334 0.5594 0.0164  -0.0448 0.0095  86  ASP J C   
18418 O O   . ASP J  86  ? 0.5459 0.5489 0.5702 0.0142  -0.0483 0.0094  86  ASP J O   
18419 C CB  . ASP J  86  ? 0.5418 0.5433 0.5768 0.0221  -0.0415 0.0132  86  ASP J CB  
18420 C CG  . ASP J  86  ? 0.8553 0.8579 0.8904 0.0263  -0.0386 0.0145  86  ASP J CG  
18421 O OD1 . ASP J  86  ? 0.8958 0.9000 0.9253 0.0281  -0.0372 0.0139  86  ASP J OD1 
18422 O OD2 . ASP J  86  ? 0.9221 0.9241 0.9626 0.0276  -0.0378 0.0163  86  ASP J OD2 
18423 N N   . GLY J  87  ? 0.4339 0.4322 0.4626 0.0147  -0.0440 0.0083  87  GLY J N   
18424 C CA  . GLY J  87  ? 0.4167 0.4146 0.4435 0.0097  -0.0473 0.0067  87  GLY J CA  
18425 C C   . GLY J  87  ? 0.4503 0.4487 0.4693 0.0086  -0.0473 0.0045  87  GLY J C   
18426 O O   . GLY J  87  ? 0.4764 0.4765 0.4918 0.0056  -0.0510 0.0040  87  GLY J O   
18427 N N   . PHE J  88  ? 0.4318 0.4287 0.4483 0.0111  -0.0431 0.0033  88  PHE J N   
18428 C CA  . PHE J  88  ? 0.4427 0.4400 0.4523 0.0105  -0.0425 0.0012  88  PHE J CA  
18429 C C   . PHE J  88  ? 0.3554 0.3562 0.3613 0.0114  -0.0445 0.0020  88  PHE J C   
18430 O O   . PHE J  88  ? 0.4360 0.4377 0.4365 0.0090  -0.0464 0.0005  88  PHE J O   
18431 C CB  . PHE J  88  ? 0.4591 0.4546 0.4678 0.0139  -0.0371 0.0005  88  PHE J CB  
18432 C CG  . PHE J  88  ? 0.4225 0.4141 0.4340 0.0126  -0.0346 -0.0008 88  PHE J CG  
18433 C CD1 . PHE J  88  ? 0.3730 0.3626 0.3867 0.0163  -0.0294 -0.0005 88  PHE J CD1 
18434 C CD2 . PHE J  88  ? 0.5115 0.5016 0.5236 0.0076  -0.0374 -0.0023 88  PHE J CD2 
18435 C CE1 . PHE J  88  ? 0.4563 0.4421 0.4727 0.0150  -0.0268 -0.0018 88  PHE J CE1 
18436 C CE2 . PHE J  88  ? 0.4334 0.4199 0.4479 0.0060  -0.0350 -0.0037 88  PHE J CE2 
18437 C CZ  . PHE J  88  ? 0.5045 0.4886 0.5212 0.0098  -0.0296 -0.0036 88  PHE J CZ  
18438 N N   . LEU J  89  ? 0.3252 0.3278 0.3339 0.0147  -0.0440 0.0042  89  LEU J N   
18439 C CA  . LEU J  89  ? 0.3401 0.3459 0.3458 0.0156  -0.0457 0.0049  89  LEU J CA  
18440 C C   . LEU J  89  ? 0.4743 0.4813 0.4790 0.0115  -0.0507 0.0049  89  LEU J C   
18441 O O   . LEU J  89  ? 0.5532 0.5620 0.5528 0.0104  -0.0524 0.0041  89  LEU J O   
18442 C CB  . LEU J  89  ? 0.3861 0.3933 0.3955 0.0194  -0.0441 0.0071  89  LEU J CB  
18443 C CG  . LEU J  89  ? 0.4601 0.4704 0.4669 0.0201  -0.0456 0.0078  89  LEU J CG  
18444 C CD1 . LEU J  89  ? 0.4337 0.4459 0.4337 0.0205  -0.0450 0.0063  89  LEU J CD1 
18445 C CD2 . LEU J  89  ? 0.3617 0.3729 0.3717 0.0238  -0.0432 0.0097  89  LEU J CD2 
18446 N N   . ASP J  90  ? 0.3962 0.4023 0.4060 0.0094  -0.0530 0.0060  90  ASP J N   
18447 C CA  . ASP J  90  ? 0.3323 0.3396 0.3421 0.0056  -0.0578 0.0067  90  ASP J CA  
18448 C C   . ASP J  90  ? 0.3961 0.4030 0.4008 0.0013  -0.0600 0.0045  90  ASP J C   
18449 O O   . ASP J  90  ? 0.4976 0.5062 0.4987 -0.0012 -0.0633 0.0045  90  ASP J O   
18450 C CB  . ASP J  90  ? 0.4112 0.4181 0.4286 0.0046  -0.0595 0.0088  90  ASP J CB  
18451 C CG  . ASP J  90  ? 0.6735 0.6814 0.6956 0.0081  -0.0582 0.0111  90  ASP J CG  
18452 O OD1 . ASP J  90  ? 0.8051 0.8147 0.8241 0.0102  -0.0574 0.0112  90  ASP J OD1 
18453 O OD2 . ASP J  90  ? 0.8027 0.8096 0.8316 0.0086  -0.0580 0.0127  90  ASP J OD2 
18454 N N   . ILE J  91  ? 0.3177 0.3220 0.3218 0.0002  -0.0581 0.0027  91  ILE J N   
18455 C CA  . ILE J  91  ? 0.4244 0.4278 0.4233 -0.0041 -0.0596 0.0003  91  ILE J CA  
18456 C C   . ILE J  91  ? 0.4786 0.4829 0.4702 -0.0035 -0.0588 -0.0013 91  ILE J C   
18457 O O   . ILE J  91  ? 0.4488 0.4542 0.4360 -0.0068 -0.0619 -0.0020 91  ILE J O   
18458 C CB  . ILE J  91  ? 0.4715 0.4715 0.4712 -0.0050 -0.0567 -0.0017 91  ILE J CB  
18459 C CG1 . ILE J  91  ? 0.3860 0.3851 0.3926 -0.0065 -0.0580 -0.0003 91  ILE J CG1 
18460 C CG2 . ILE J  91  ? 0.5500 0.5488 0.5433 -0.0094 -0.0576 -0.0046 91  ILE J CG2 
18461 C CD1 . ILE J  91  ? 0.6038 0.5994 0.6118 -0.0074 -0.0549 -0.0023 91  ILE J CD1 
18462 N N   . TRP J  92  ? 0.4238 0.4279 0.4145 0.0006  -0.0545 -0.0017 92  TRP J N   
18463 C CA  . TRP J  92  ? 0.4127 0.4178 0.3971 0.0014  -0.0532 -0.0032 92  TRP J CA  
18464 C C   . TRP J  92  ? 0.4492 0.4575 0.4312 0.0016  -0.0559 -0.0022 92  TRP J C   
18465 O O   . TRP J  92  ? 0.4682 0.4774 0.4446 -0.0004 -0.0572 -0.0036 92  TRP J O   
18466 C CB  . TRP J  92  ? 0.3706 0.3752 0.3554 0.0060  -0.0481 -0.0034 92  TRP J CB  
18467 C CG  . TRP J  92  ? 0.3548 0.3558 0.3397 0.0053  -0.0449 -0.0053 92  TRP J CG  
18468 C CD1 . TRP J  92  ? 0.3796 0.3784 0.3693 0.0074  -0.0417 -0.0047 92  TRP J CD1 
18469 C CD2 . TRP J  92  ? 0.3560 0.3551 0.3359 0.0021  -0.0444 -0.0081 92  TRP J CD2 
18470 N NE1 . TRP J  92  ? 1.0549 1.0504 1.0431 0.0058  -0.0391 -0.0071 92  TRP J NE1 
18471 C CE2 . TRP J  92  ? 0.3957 0.3913 0.3779 0.0024  -0.0406 -0.0092 92  TRP J CE2 
18472 C CE3 . TRP J  92  ? 0.3681 0.3680 0.3419 -0.0011 -0.0465 -0.0098 92  TRP J CE3 
18473 C CZ2 . TRP J  92  ? 0.3925 0.3852 0.3710 -0.0004 -0.0388 -0.0121 92  TRP J CZ2 
18474 C CZ3 . TRP J  92  ? 0.4666 0.4636 0.4365 -0.0039 -0.0448 -0.0127 92  TRP J CZ3 
18475 C CH2 . TRP J  92  ? 0.5319 0.5254 0.5042 -0.0036 -0.0409 -0.0139 92  TRP J CH2 
18476 N N   . THR J  93  ? 0.3831 0.3931 0.3694 0.0038  -0.0566 0.0002  93  THR J N   
18477 C CA  . THR J  93  ? 0.3942 0.4070 0.3789 0.0039  -0.0590 0.0012  93  THR J CA  
18478 C C   . THR J  93  ? 0.4057 0.4189 0.3884 -0.0008 -0.0636 0.0012  93  THR J C   
18479 O O   . THR J  93  ? 0.4378 0.4523 0.4154 -0.0022 -0.0650 0.0003  93  THR J O   
18480 C CB  . THR J  93  ? 0.4196 0.4335 0.4098 0.0067  -0.0587 0.0037  93  THR J CB  
18481 O OG1 . THR J  93  ? 0.3883 0.4025 0.3794 0.0110  -0.0545 0.0039  93  THR J OG1 
18482 C CG2 . THR J  93  ? 0.3799 0.3964 0.3686 0.0062  -0.0611 0.0047  93  THR J CG2 
18483 N N   . TYR J  94  ? 0.4940 0.5061 0.4809 -0.0033 -0.0659 0.0021  94  TYR J N   
18484 C CA  . TYR J  94  ? 0.4126 0.4253 0.3983 -0.0078 -0.0705 0.0026  94  TYR J CA  
18485 C C   . TYR J  94  ? 0.4072 0.4191 0.3857 -0.0113 -0.0712 -0.0001 94  TYR J C   
18486 O O   . TYR J  94  ? 0.4633 0.4766 0.4376 -0.0137 -0.0739 -0.0002 94  TYR J O   
18487 C CB  . TYR J  94  ? 0.3212 0.3332 0.3131 -0.0099 -0.0727 0.0042  94  TYR J CB  
18488 C CG  . TYR J  94  ? 0.4902 0.5036 0.4820 -0.0143 -0.0778 0.0056  94  TYR J CG  
18489 C CD1 . TYR J  94  ? 0.5177 0.5334 0.5122 -0.0138 -0.0803 0.0082  94  TYR J CD1 
18490 C CD2 . TYR J  94  ? 0.4818 0.4944 0.4708 -0.0189 -0.0801 0.0042  94  TYR J CD2 
18491 C CE1 . TYR J  94  ? 0.5540 0.5712 0.5487 -0.0177 -0.0850 0.0099  94  TYR J CE1 
18492 C CE2 . TYR J  94  ? 0.4945 0.5089 0.4833 -0.0230 -0.0851 0.0058  94  TYR J CE2 
18493 C CZ  . TYR J  94  ? 0.6697 0.6864 0.6615 -0.0222 -0.0875 0.0088  94  TYR J CZ  
18494 O OH  . TYR J  94  ? 0.6470 0.6657 0.6389 -0.0262 -0.0924 0.0108  94  TYR J OH  
18495 N N   . ASN J  95  ? 0.3904 0.3998 0.3676 -0.0116 -0.0685 -0.0023 95  ASN J N   
18496 C CA  . ASN J  95  ? 0.4362 0.4442 0.4067 -0.0150 -0.0685 -0.0051 95  ASN J CA  
18497 C C   . ASN J  95  ? 0.5123 0.5216 0.4769 -0.0136 -0.0671 -0.0063 95  ASN J C   
18498 O O   . ASN J  95  ? 0.5687 0.5783 0.5277 -0.0168 -0.0691 -0.0076 95  ASN J O   
18499 C CB  . ASN J  95  ? 0.4742 0.4790 0.4450 -0.0152 -0.0650 -0.0072 95  ASN J CB  
18500 C CG  . ASN J  95  ? 0.6864 0.6900 0.6616 -0.0182 -0.0670 -0.0067 95  ASN J CG  
18501 O OD1 . ASN J  95  ? 0.6519 0.6572 0.6314 -0.0191 -0.0705 -0.0042 95  ASN J OD1 
18502 N ND2 . ASN J  95  ? 0.7670 0.7676 0.7415 -0.0199 -0.0645 -0.0090 95  ASN J ND2 
18503 N N   . ALA J  96  ? 0.3910 0.4010 0.3568 -0.0088 -0.0636 -0.0060 96  ALA J N   
18504 C CA  . ALA J  96  ? 0.4790 0.4907 0.4399 -0.0071 -0.0621 -0.0070 96  ALA J CA  
18505 C C   . ALA J  96  ? 0.5403 0.5546 0.4991 -0.0084 -0.0657 -0.0059 96  ALA J C   
18506 O O   . ALA J  96  ? 0.5598 0.5747 0.5129 -0.0101 -0.0663 -0.0073 96  ALA J O   
18507 C CB  . ALA J  96  ? 0.5241 0.5367 0.4874 -0.0018 -0.0581 -0.0063 96  ALA J CB  
18508 N N   . GLU J  97  ? 0.3678 0.3834 0.3314 -0.0076 -0.0678 -0.0033 97  GLU J N   
18509 C CA  . GLU J  97  ? 0.4710 0.4888 0.4337 -0.0088 -0.0709 -0.0019 97  GLU J CA  
18510 C C   . GLU J  97  ? 0.5237 0.5411 0.4826 -0.0138 -0.0748 -0.0024 97  GLU J C   
18511 O O   . GLU J  97  ? 0.5046 0.5233 0.4587 -0.0153 -0.0761 -0.0030 97  GLU J O   
18512 C CB  . GLU J  97  ? 0.5828 0.6016 0.5523 -0.0072 -0.0721 0.0010  97  GLU J CB  
18513 C CG  . GLU J  97  ? 0.4277 0.4473 0.4002 -0.0023 -0.0686 0.0016  97  GLU J CG  
18514 C CD  . GLU J  97  ? 0.6448 0.6669 0.6141 -0.0006 -0.0678 0.0014  97  GLU J CD  
18515 O OE1 . GLU J  97  ? 0.6076 0.6308 0.5795 0.0027  -0.0657 0.0023  97  GLU J OE1 
18516 O OE2 . GLU J  97  ? 0.9522 0.9750 0.9161 -0.0028 -0.0693 0.0002  97  GLU J OE2 
18517 N N   . LEU J  98  ? 0.4421 0.4579 0.4030 -0.0167 -0.0765 -0.0022 98  LEU J N   
18518 C CA  . LEU J  98  ? 0.4750 0.4907 0.4325 -0.0219 -0.0804 -0.0025 98  LEU J CA  
18519 C C   . LEU J  98  ? 0.6313 0.6456 0.5810 -0.0241 -0.0791 -0.0058 98  LEU J C   
18520 O O   . LEU J  98  ? 0.5341 0.5490 0.4788 -0.0275 -0.0817 -0.0062 98  LEU J O   
18521 C CB  . LEU J  98  ? 0.4128 0.4274 0.3746 -0.0244 -0.0823 -0.0016 98  LEU J CB  
18522 C CG  . LEU J  98  ? 0.4423 0.4588 0.4100 -0.0254 -0.0862 0.0020  98  LEU J CG  
18523 C CD1 . LEU J  98  ? 0.7652 0.7832 0.7292 -0.0298 -0.0908 0.0029  98  LEU J CD1 
18524 C CD2 . LEU J  98  ? 0.5972 0.6150 0.5698 -0.0208 -0.0849 0.0042  98  LEU J CD2 
18525 N N   . LEU J  99  ? 0.5327 0.5451 0.4815 -0.0221 -0.0749 -0.0080 99  LEU J N   
18526 C CA  . LEU J  99  ? 0.5850 0.5957 0.5270 -0.0239 -0.0729 -0.0112 99  LEU J CA  
18527 C C   . LEU J  99  ? 0.5367 0.5493 0.4738 -0.0233 -0.0729 -0.0116 99  LEU J C   
18528 O O   . LEU J  99  ? 0.5310 0.5431 0.4621 -0.0268 -0.0741 -0.0133 99  LEU J O   
18529 C CB  . LEU J  99  ? 0.4944 0.5030 0.4375 -0.0210 -0.0678 -0.0129 99  LEU J CB  
18530 C CG  . LEU J  99  ? 0.5437 0.5503 0.4806 -0.0225 -0.0649 -0.0162 99  LEU J CG  
18531 C CD1 . LEU J  99  ? 0.6408 0.6451 0.5738 -0.0284 -0.0670 -0.0181 99  LEU J CD1 
18532 C CD2 . LEU J  99  ? 0.6798 0.6847 0.6189 -0.0188 -0.0595 -0.0173 99  LEU J CD2 
18533 N N   . VAL J  100 ? 0.4278 0.4426 0.3675 -0.0190 -0.0716 -0.0103 100 VAL J N   
18534 C CA  . VAL J  100 ? 0.5711 0.5880 0.5067 -0.0181 -0.0715 -0.0106 100 VAL J CA  
18535 C C   . VAL J  100 ? 0.5401 0.5582 0.4736 -0.0216 -0.0760 -0.0094 100 VAL J C   
18536 O O   . VAL J  100 ? 0.6524 0.6707 0.5800 -0.0238 -0.0767 -0.0108 100 VAL J O   
18537 C CB  . VAL J  100 ? 0.5267 0.5460 0.4658 -0.0131 -0.0694 -0.0093 100 VAL J CB  
18538 C CG1 . VAL J  100 ? 0.5170 0.5388 0.4525 -0.0129 -0.0700 -0.0094 100 VAL J CG1 
18539 C CG2 . VAL J  100 ? 0.4660 0.4846 0.4063 -0.0096 -0.0648 -0.0104 100 VAL J CG2 
18540 N N   . LEU J  101 ? 0.4678 0.4866 0.4062 -0.0220 -0.0789 -0.0067 101 LEU J N   
18541 C CA  . LEU J  101 ? 0.5654 0.5855 0.5028 -0.0251 -0.0832 -0.0049 101 LEU J CA  
18542 C C   . LEU J  101 ? 0.5872 0.6059 0.5188 -0.0303 -0.0854 -0.0064 101 LEU J C   
18543 O O   . LEU J  101 ? 0.6236 0.6430 0.5499 -0.0324 -0.0868 -0.0070 101 LEU J O   
18544 C CB  . LEU J  101 ? 0.4882 0.5091 0.4328 -0.0249 -0.0857 -0.0016 101 LEU J CB  
18545 C CG  . LEU J  101 ? 0.4735 0.4956 0.4239 -0.0203 -0.0839 0.0001  101 LEU J CG  
18546 C CD1 . LEU J  101 ? 0.4678 0.4906 0.4250 -0.0208 -0.0867 0.0035  101 LEU J CD1 
18547 C CD2 . LEU J  101 ? 0.4183 0.4422 0.3658 -0.0186 -0.0828 -0.0002 101 LEU J CD2 
18548 N N   . LEU J  102 ? 0.5992 0.6161 0.5318 -0.0324 -0.0857 -0.0071 102 LEU J N   
18549 C CA  . LEU J  102 ? 0.5798 0.5953 0.5068 -0.0377 -0.0876 -0.0087 102 LEU J CA  
18550 C C   . LEU J  102 ? 0.5496 0.5639 0.4690 -0.0386 -0.0852 -0.0120 102 LEU J C   
18551 O O   . LEU J  102 ? 0.5854 0.5998 0.4990 -0.0424 -0.0875 -0.0125 102 LEU J O   
18552 C CB  . LEU J  102 ? 0.6580 0.6714 0.5874 -0.0393 -0.0871 -0.0096 102 LEU J CB  
18553 C CG  . LEU J  102 ? 0.7432 0.7575 0.6766 -0.0424 -0.0916 -0.0070 102 LEU J CG  
18554 C CD1 . LEU J  102 ? 0.7531 0.7702 0.6925 -0.0402 -0.0941 -0.0030 102 LEU J CD1 
18555 C CD2 . LEU J  102 ? 0.9927 1.0051 0.9302 -0.0425 -0.0900 -0.0078 102 LEU J CD2 
18556 N N   . GLU J  103 ? 0.4638 0.4770 0.3833 -0.0351 -0.0805 -0.0140 103 GLU J N   
18557 C CA  . GLU J  103 ? 0.5607 0.5726 0.4736 -0.0357 -0.0776 -0.0171 103 GLU J CA  
18558 C C   . GLU J  103 ? 0.5690 0.5831 0.4785 -0.0350 -0.0784 -0.0167 103 GLU J C   
18559 O O   . GLU J  103 ? 0.6997 0.7130 0.6028 -0.0377 -0.0783 -0.0187 103 GLU J O   
18560 C CB  . GLU J  103 ? 0.5848 0.5954 0.4996 -0.0318 -0.0724 -0.0188 103 GLU J CB  
18561 C CG  . GLU J  103 ? 0.8261 0.8335 0.7420 -0.0334 -0.0707 -0.0203 103 GLU J CG  
18562 C CD  . GLU J  103 ? 1.0617 1.0669 0.9715 -0.0394 -0.0724 -0.0225 103 GLU J CD  
18563 O OE1 . GLU J  103 ? 0.9839 0.9874 0.8881 -0.0407 -0.0698 -0.0253 103 GLU J OE1 
18564 O OE2 . GLU J  103 ? 1.0226 1.0278 0.9333 -0.0430 -0.0762 -0.0213 103 GLU J OE2 
18565 N N   . ASN J  104 ? 0.4964 0.5131 0.4102 -0.0316 -0.0789 -0.0144 104 ASN J N   
18566 C CA  . ASN J  104 ? 0.5379 0.5568 0.4489 -0.0310 -0.0796 -0.0140 104 ASN J CA  
18567 C C   . ASN J  104 ? 0.5893 0.6083 0.4963 -0.0357 -0.0838 -0.0132 104 ASN J C   
18568 O O   . ASN J  104 ? 0.6092 0.6284 0.5107 -0.0372 -0.0839 -0.0143 104 ASN J O   
18569 C CB  . ASN J  104 ? 0.4359 0.4573 0.3525 -0.0269 -0.0795 -0.0116 104 ASN J CB  
18570 C CG  . ASN J  104 ? 0.4900 0.5122 0.4087 -0.0222 -0.0752 -0.0125 104 ASN J CG  
18571 O OD1 . ASN J  104 ? 0.5577 0.5788 0.4737 -0.0217 -0.0721 -0.0148 104 ASN J OD1 
18572 N ND2 . ASN J  104 ? 0.5640 0.5881 0.4878 -0.0188 -0.0747 -0.0106 104 ASN J ND2 
18573 N N   . GLU J  105 ? 0.4943 0.5132 0.4042 -0.0380 -0.0873 -0.0110 105 GLU J N   
18574 C CA  . GLU J  105 ? 0.5531 0.5723 0.4596 -0.0427 -0.0916 -0.0097 105 GLU J CA  
18575 C C   . GLU J  105 ? 0.5961 0.6131 0.4946 -0.0469 -0.0912 -0.0128 105 GLU J C   
18576 O O   . GLU J  105 ? 0.6741 0.6914 0.5671 -0.0497 -0.0929 -0.0130 105 GLU J O   
18577 C CB  . GLU J  105 ? 0.6166 0.6363 0.5282 -0.0444 -0.0953 -0.0068 105 GLU J CB  
18578 C CG  . GLU J  105 ? 0.8858 0.9064 0.7943 -0.0493 -0.1001 -0.0050 105 GLU J CG  
18579 C CD  . GLU J  105 ? 1.3793 1.4016 1.2862 -0.0488 -0.1013 -0.0034 105 GLU J CD  
18580 O OE1 . GLU J  105 ? 1.3028 1.3263 1.2142 -0.0447 -0.0999 -0.0021 105 GLU J OE1 
18581 O OE2 . GLU J  105 ? 1.4472 1.4695 1.3481 -0.0526 -0.1035 -0.0035 105 GLU J OE2 
18582 N N   . ARG J  106 ? 0.6275 0.6422 0.5255 -0.0472 -0.0886 -0.0153 106 ARG J N   
18583 C CA  . ARG J  106 ? 0.6560 0.6682 0.5467 -0.0512 -0.0874 -0.0186 106 ARG J CA  
18584 C C   . ARG J  106 ? 0.7203 0.7320 0.6060 -0.0499 -0.0840 -0.0211 106 ARG J C   
18585 O O   . ARG J  106 ? 0.8196 0.8301 0.6984 -0.0536 -0.0843 -0.0230 106 ARG J O   
18586 C CB  . ARG J  106 ? 0.6706 0.6800 0.5627 -0.0517 -0.0849 -0.0207 106 ARG J CB  
18587 C CG  . ARG J  106 ? 0.6926 0.7022 0.5884 -0.0544 -0.0884 -0.0188 106 ARG J CG  
18588 C CD  . ARG J  106 ? 1.0469 1.0533 0.9418 -0.0565 -0.0860 -0.0217 106 ARG J CD  
18589 N NE  . ARG J  106 ? 1.1200 1.1238 1.0064 -0.0607 -0.0846 -0.0252 106 ARG J NE  
18590 C CZ  . ARG J  106 ? 1.0485 1.0523 0.9291 -0.0665 -0.0881 -0.0255 106 ARG J CZ  
18591 N NH1 . ARG J  106 ? 0.9839 0.9904 0.8667 -0.0687 -0.0935 -0.0221 106 ARG J NH1 
18592 N NH2 . ARG J  106 ? 1.0898 1.0910 0.9627 -0.0701 -0.0862 -0.0290 106 ARG J NH2 
18593 N N   . THR J  107 ? 0.6133 0.6262 0.5027 -0.0447 -0.0808 -0.0210 107 THR J N   
18594 C CA  . THR J  107 ? 0.6344 0.6476 0.5201 -0.0430 -0.0775 -0.0232 107 THR J CA  
18595 C C   . THR J  107 ? 0.6182 0.6330 0.4999 -0.0446 -0.0799 -0.0224 107 THR J C   
18596 O O   . THR J  107 ? 0.6156 0.6295 0.4912 -0.0464 -0.0786 -0.0246 107 THR J O   
18597 C CB  . THR J  107 ? 0.6017 0.6165 0.4925 -0.0370 -0.0740 -0.0228 107 THR J CB  
18598 O OG1 . THR J  107 ? 0.6659 0.6789 0.5601 -0.0354 -0.0713 -0.0236 107 THR J OG1 
18599 C CG2 . THR J  107 ? 0.5426 0.5582 0.4298 -0.0354 -0.0708 -0.0247 107 THR J CG2 
18600 N N   . LEU J  108 ? 0.5956 0.6127 0.4809 -0.0438 -0.0832 -0.0192 108 LEU J N   
18601 C CA  . LEU J  108 ? 0.6147 0.6334 0.4968 -0.0453 -0.0856 -0.0180 108 LEU J CA  
18602 C C   . LEU J  108 ? 0.6462 0.6634 0.5220 -0.0511 -0.0886 -0.0184 108 LEU J C   
18603 O O   . LEU J  108 ? 0.7074 0.7244 0.5774 -0.0530 -0.0886 -0.0195 108 LEU J O   
18604 C CB  . LEU J  108 ? 0.6026 0.6237 0.4907 -0.0433 -0.0881 -0.0144 108 LEU J CB  
18605 C CG  . LEU J  108 ? 0.4535 0.4764 0.3471 -0.0378 -0.0853 -0.0140 108 LEU J CG  
18606 C CD1 . LEU J  108 ? 0.5144 0.5393 0.4133 -0.0364 -0.0876 -0.0106 108 LEU J CD1 
18607 C CD2 . LEU J  108 ? 0.4391 0.4629 0.3293 -0.0359 -0.0820 -0.0163 108 LEU J CD2 
18608 N N   . ASP J  109 ? 0.5842 0.6004 0.4610 -0.0539 -0.0910 -0.0176 109 ASP J N   
18609 C CA  . ASP J  109 ? 0.5768 0.5917 0.4474 -0.0598 -0.0939 -0.0179 109 ASP J CA  
18610 C C   . ASP J  109 ? 0.6909 0.7030 0.5543 -0.0621 -0.0907 -0.0222 109 ASP J C   
18611 O O   . ASP J  109 ? 0.7244 0.7355 0.5808 -0.0665 -0.0920 -0.0231 109 ASP J O   
18612 C CB  . ASP J  109 ? 0.7312 0.7459 0.6049 -0.0623 -0.0971 -0.0163 109 ASP J CB  
18613 C CG  . ASP J  109 ? 1.0016 1.0191 0.8815 -0.0613 -0.1011 -0.0117 109 ASP J CG  
18614 O OD1 . ASP J  109 ? 0.9980 1.0173 0.8786 -0.0597 -0.1019 -0.0098 109 ASP J OD1 
18615 O OD2 . ASP J  109 ? 1.0232 1.0412 0.9075 -0.0623 -0.1034 -0.0099 109 ASP J OD2 
18616 N N   . TYR J  110 ? 0.6171 0.6277 0.4823 -0.0592 -0.0861 -0.0246 110 TYR J N   
18617 C CA  . TYR J  110 ? 0.6204 0.6281 0.4797 -0.0607 -0.0822 -0.0287 110 TYR J CA  
18618 C C   . TYR J  110 ? 0.7839 0.7923 0.6387 -0.0603 -0.0808 -0.0297 110 TYR J C   
18619 O O   . TYR J  110 ? 0.6821 0.6885 0.5296 -0.0641 -0.0803 -0.0320 110 TYR J O   
18620 C CB  . TYR J  110 ? 0.5852 0.5915 0.4486 -0.0569 -0.0774 -0.0305 110 TYR J CB  
18621 C CG  . TYR J  110 ? 0.5757 0.5793 0.4344 -0.0574 -0.0726 -0.0343 110 TYR J CG  
18622 C CD1 . TYR J  110 ? 0.5565 0.5564 0.4105 -0.0618 -0.0712 -0.0372 110 TYR J CD1 
18623 C CD2 . TYR J  110 ? 0.6317 0.6365 0.4906 -0.0536 -0.0691 -0.0352 110 TYR J CD2 
18624 C CE1 . TYR J  110 ? 0.6000 0.5970 0.4499 -0.0623 -0.0664 -0.0408 110 TYR J CE1 
18625 C CE2 . TYR J  110 ? 0.6918 0.6942 0.5470 -0.0539 -0.0645 -0.0385 110 TYR J CE2 
18626 C CZ  . TYR J  110 ? 0.7473 0.7457 0.5981 -0.0582 -0.0630 -0.0413 110 TYR J CZ  
18627 O OH  . TYR J  110 ? 0.8638 0.8595 0.7112 -0.0585 -0.0580 -0.0446 110 TYR J OH  
18628 N N   . HIS J  111 ? 0.7202 0.7313 0.5791 -0.0557 -0.0801 -0.0282 111 HIS J N   
18629 C CA  . HIS J  111 ? 0.6555 0.6678 0.5109 -0.0550 -0.0789 -0.0290 111 HIS J CA  
18630 C C   . HIS J  111 ? 0.7386 0.7514 0.5893 -0.0590 -0.0829 -0.0275 111 HIS J C   
18631 O O   . HIS J  111 ? 0.7106 0.7222 0.5548 -0.0616 -0.0821 -0.0294 111 HIS J O   
18632 C CB  . HIS J  111 ? 0.5720 0.5875 0.4332 -0.0495 -0.0776 -0.0275 111 HIS J CB  
18633 C CG  . HIS J  111 ? 0.6402 0.6558 0.5051 -0.0453 -0.0731 -0.0290 111 HIS J CG  
18634 N ND1 . HIS J  111 ? 0.7407 0.7551 0.6023 -0.0447 -0.0689 -0.0319 111 HIS J ND1 
18635 C CD2 . HIS J  111 ? 0.6357 0.6523 0.5072 -0.0413 -0.0720 -0.0277 111 HIS J CD2 
18636 C CE1 . HIS J  111 ? 0.7998 0.8149 0.6662 -0.0406 -0.0655 -0.0322 111 HIS J CE1 
18637 N NE2 . HIS J  111 ? 0.7141 0.7304 0.5863 -0.0384 -0.0673 -0.0298 111 HIS J NE2 
18638 N N   . ASP J  112 ? 0.5765 0.5909 0.4308 -0.0595 -0.0872 -0.0240 112 ASP J N   
18639 C CA  . ASP J  112 ? 0.6439 0.6589 0.4945 -0.0633 -0.0913 -0.0219 112 ASP J CA  
18640 C C   . ASP J  112 ? 0.6704 0.6828 0.5130 -0.0690 -0.0920 -0.0241 112 ASP J C   
18641 O O   . ASP J  112 ? 0.7769 0.7890 0.6134 -0.0719 -0.0931 -0.0243 112 ASP J O   
18642 C CB  . ASP J  112 ? 0.8400 0.8567 0.6964 -0.0633 -0.0956 -0.0179 112 ASP J CB  
18643 C CG  . ASP J  112 ? 0.7742 0.7922 0.6282 -0.0664 -0.0999 -0.0149 112 ASP J CG  
18644 O OD1 . ASP J  112 ? 0.9142 0.9333 0.7714 -0.0679 -0.1038 -0.0116 112 ASP J OD1 
18645 O OD2 . ASP J  112 ? 0.9232 0.9412 0.7723 -0.0673 -0.0992 -0.0158 112 ASP J OD2 
18646 N N   . SER J  113 ? 0.7057 0.7160 0.5479 -0.0706 -0.0910 -0.0258 113 SER J N   
18647 C CA  . SER J  113 ? 0.6881 0.6956 0.5226 -0.0763 -0.0913 -0.0282 113 SER J CA  
18648 C C   . SER J  113 ? 0.7606 0.7659 0.5884 -0.0772 -0.0873 -0.0320 113 SER J C   
18649 O O   . SER J  113 ? 0.8544 0.8585 0.6748 -0.0818 -0.0886 -0.0328 113 SER J O   
18650 C CB  . SER J  113 ? 0.6052 0.6107 0.4415 -0.0773 -0.0902 -0.0298 113 SER J CB  
18651 O OG  . SER J  113 ? 0.8971 0.8992 0.7257 -0.0822 -0.0885 -0.0334 113 SER J OG  
18652 N N   . ASN J  114 ? 0.7608 0.7656 0.5913 -0.0729 -0.0825 -0.0341 114 ASN J N   
18653 C CA  . ASN J  114 ? 0.8424 0.8453 0.6676 -0.0733 -0.0782 -0.0376 114 ASN J CA  
18654 C C   . ASN J  114 ? 0.8681 0.8724 0.6892 -0.0742 -0.0795 -0.0368 114 ASN J C   
18655 O O   . ASN J  114 ? 0.8664 0.8686 0.6804 -0.0774 -0.0779 -0.0393 114 ASN J O   
18656 C CB  . ASN J  114 ? 0.7260 0.7292 0.5563 -0.0679 -0.0732 -0.0391 114 ASN J CB  
18657 C CG  . ASN J  114 ? 0.7709 0.7719 0.6043 -0.0673 -0.0710 -0.0404 114 ASN J CG  
18658 O OD1 . ASN J  114 ? 1.0008 0.9992 0.8308 -0.0717 -0.0721 -0.0414 114 ASN J OD1 
18659 N ND2 . ASN J  114 ? 0.8383 0.8404 0.6781 -0.0619 -0.0678 -0.0403 114 ASN J ND2 
18660 N N   . VAL J  115 ? 0.7579 0.7655 0.5836 -0.0714 -0.0821 -0.0335 115 VAL J N   
18661 C CA  . VAL J  115 ? 0.7115 0.7206 0.5340 -0.0723 -0.0836 -0.0324 115 VAL J CA  
18662 C C   . VAL J  115 ? 0.7270 0.7347 0.5426 -0.0783 -0.0873 -0.0316 115 VAL J C   
18663 O O   . VAL J  115 ? 0.7168 0.7230 0.5253 -0.0813 -0.0864 -0.0334 115 VAL J O   
18664 C CB  . VAL J  115 ? 0.7215 0.7341 0.5506 -0.0684 -0.0858 -0.0288 115 VAL J CB  
18665 C CG1 . VAL J  115 ? 0.7728 0.7864 0.5984 -0.0699 -0.0876 -0.0274 115 VAL J CG1 
18666 C CG2 . VAL J  115 ? 0.6221 0.6364 0.4572 -0.0627 -0.0821 -0.0296 115 VAL J CG2 
18667 N N   . LYS J  116 ? 0.7277 0.7362 0.5455 -0.0802 -0.0916 -0.0288 116 LYS J N   
18668 C CA  . LYS J  116 ? 0.8408 0.8486 0.6525 -0.0860 -0.0957 -0.0275 116 LYS J CA  
18669 C C   . LYS J  116 ? 0.8867 0.8909 0.6896 -0.0907 -0.0934 -0.0316 116 LYS J C   
18670 O O   . LYS J  116 ? 0.8935 0.8969 0.6890 -0.0950 -0.0948 -0.0318 116 LYS J O   
18671 C CB  . LYS J  116 ? 0.8546 0.8637 0.6707 -0.0872 -0.0998 -0.0246 116 LYS J CB  
18672 C CG  . LYS J  116 ? 0.7758 0.7843 0.5856 -0.0937 -0.1039 -0.0236 116 LYS J CG  
18673 C CD  . LYS J  116 ? 1.0026 1.0139 0.8130 -0.0949 -0.1089 -0.0188 116 LYS J CD  
18674 C CE  . LYS J  116 ? 1.1279 1.1397 0.9337 -0.1011 -0.1136 -0.0171 116 LYS J CE  
18675 N NZ  . LYS J  116 ? 1.3667 1.3817 1.1747 -0.1018 -0.1187 -0.0116 116 LYS J NZ  
18676 N N   . ASN J  117 ? 0.7633 0.7652 0.5670 -0.0899 -0.0895 -0.0349 117 ASN J N   
18677 C CA  . ASN J  117 ? 0.8400 0.8381 0.6360 -0.0941 -0.0865 -0.0391 117 ASN J CA  
18678 C C   . ASN J  117 ? 0.9525 0.9493 0.7435 -0.0939 -0.0828 -0.0417 117 ASN J C   
18679 O O   . ASN J  117 ? 1.0322 1.0264 0.8147 -0.0989 -0.0822 -0.0439 117 ASN J O   
18680 C CB  . ASN J  117 ? 0.7789 0.7747 0.5780 -0.0927 -0.0828 -0.0419 117 ASN J CB  
18681 C CG  . ASN J  117 ? 0.7762 0.7721 0.5774 -0.0952 -0.0862 -0.0405 117 ASN J CG  
18682 O OD1 . ASN J  117 ? 0.8843 0.8818 0.6832 -0.0990 -0.0913 -0.0378 117 ASN J OD1 
18683 N ND2 . ASN J  117 ? 0.9127 0.9073 0.7185 -0.0931 -0.0833 -0.0420 117 ASN J ND2 
18684 N N   . LEU J  118 ? 0.9584 0.9570 0.7545 -0.0884 -0.0803 -0.0414 118 LEU J N   
18685 C CA  . LEU J  118 ? 0.8747 0.8726 0.6670 -0.0878 -0.0769 -0.0435 118 LEU J CA  
18686 C C   . LEU J  118 ? 0.8512 0.8499 0.6379 -0.0912 -0.0803 -0.0418 118 LEU J C   
18687 O O   . LEU J  118 ? 1.1205 1.1169 0.8998 -0.0944 -0.0785 -0.0441 118 LEU J O   
18688 C CB  . LEU J  118 ? 0.8910 0.8917 0.6906 -0.0812 -0.0742 -0.0430 118 LEU J CB  
18689 C CG  . LEU J  118 ? 0.8631 0.8626 0.6610 -0.0795 -0.0686 -0.0464 118 LEU J CG  
18690 C CD1 . LEU J  118 ? 0.9791 0.9746 0.7740 -0.0816 -0.0647 -0.0501 118 LEU J CD1 
18691 C CD2 . LEU J  118 ? 1.0295 1.0325 0.8352 -0.0730 -0.0665 -0.0456 118 LEU J CD2 
18692 N N   . TYR J  119 ? 0.7715 0.7731 0.5618 -0.0904 -0.0850 -0.0375 119 TYR J N   
18693 C CA  . TYR J  119 ? 0.8857 0.8883 0.6716 -0.0935 -0.0886 -0.0351 119 TYR J CA  
18694 C C   . TYR J  119 ? 0.9355 0.9356 0.7125 -0.1003 -0.0906 -0.0360 119 TYR J C   
18695 O O   . TYR J  119 ? 1.0685 1.0673 0.8382 -0.1036 -0.0903 -0.0369 119 TYR J O   
18696 C CB  . TYR J  119 ? 0.8852 0.8913 0.6777 -0.0914 -0.0932 -0.0301 119 TYR J CB  
18697 C CG  . TYR J  119 ? 1.0648 1.0720 0.8536 -0.0944 -0.0972 -0.0269 119 TYR J CG  
18698 C CD1 . TYR J  119 ? 1.1350 1.1435 0.9254 -0.0920 -0.0963 -0.0256 119 TYR J CD1 
18699 C CD2 . TYR J  119 ? 1.1358 1.1427 0.9202 -0.0996 -0.1016 -0.0249 119 TYR J CD2 
18700 C CE1 . TYR J  119 ? 1.2501 1.2593 1.0382 -0.0945 -0.0992 -0.0223 119 TYR J CE1 
18701 C CE2 . TYR J  119 ? 1.3242 1.3322 1.1061 -0.1021 -0.1048 -0.0214 119 TYR J CE2 
18702 C CZ  . TYR J  119 ? 1.3208 1.3297 1.1045 -0.0995 -0.1035 -0.0200 119 TYR J CZ  
18703 O OH  . TYR J  119 ? 1.3322 1.3420 1.1135 -0.1019 -0.1066 -0.0164 119 TYR J OH  
18704 N N   . GLU J  120 ? 1.0421 1.0416 0.8196 -0.1026 -0.0926 -0.0357 120 GLU J N   
18705 C CA  . GLU J  120 ? 1.0152 1.0127 0.7844 -0.1095 -0.0948 -0.0365 120 GLU J CA  
18706 C C   . GLU J  120 ? 0.9855 0.9788 0.7466 -0.1126 -0.0900 -0.0417 120 GLU J C   
18707 O O   . GLU J  120 ? 1.2431 1.2349 0.9954 -0.1179 -0.0911 -0.0424 120 GLU J O   
18708 C CB  . GLU J  120 ? 1.2596 1.2574 1.0318 -0.1110 -0.0973 -0.0357 120 GLU J CB  
18709 C CG  . GLU J  120 ? 1.3869 1.3885 1.1634 -0.1113 -0.1036 -0.0302 120 GLU J CG  
18710 C CD  . GLU J  120 ? 1.7529 1.7551 1.5218 -0.1172 -0.1079 -0.0280 120 GLU J CD  
18711 O OE1 . GLU J  120 ? 1.6492 1.6485 1.4088 -0.1222 -0.1065 -0.0312 120 GLU J OE1 
18712 O OE2 . GLU J  120 ? 1.8552 1.8607 1.6275 -0.1167 -0.1126 -0.0231 120 GLU J OE2 
18713 N N   . LYS J  121 ? 1.0231 1.0145 0.7871 -0.1093 -0.0846 -0.0451 121 LYS J N   
18714 C CA  . LYS J  121 ? 1.1503 1.1375 0.9077 -0.1118 -0.0794 -0.0501 121 LYS J CA  
18715 C C   . LYS J  121 ? 1.2676 1.2543 1.0193 -0.1127 -0.0781 -0.0508 121 LYS J C   
18716 O O   . LYS J  121 ? 1.4648 1.4481 1.2080 -0.1173 -0.0759 -0.0539 121 LYS J O   
18717 C CB  . LYS J  121 ? 1.1342 1.1201 0.8974 -0.1070 -0.0737 -0.0529 121 LYS J CB  
18718 C CG  . LYS J  121 ? 1.4270 1.4082 1.1841 -0.1096 -0.0679 -0.0580 121 LYS J CG  
18719 C CD  . LYS J  121 ? 1.4798 1.4600 1.2435 -0.1046 -0.0623 -0.0603 121 LYS J CD  
18720 C CE  . LYS J  121 ? 1.5562 1.5315 1.3142 -0.1072 -0.0562 -0.0653 121 LYS J CE  
18721 N NZ  . LYS J  121 ? 1.6783 1.6527 1.4430 -0.1022 -0.0505 -0.0671 121 LYS J NZ  
18722 N N   . VAL J  122 ? 1.2423 1.2323 0.9988 -0.1084 -0.0792 -0.0480 122 VAL J N   
18723 C CA  . VAL J  122 ? 1.1686 1.1586 0.9206 -0.1091 -0.0782 -0.0482 122 VAL J CA  
18724 C C   . VAL J  122 ? 1.2021 1.1923 0.9472 -0.1144 -0.0831 -0.0457 122 VAL J C   
18725 O O   . VAL J  122 ? 1.5246 1.5125 1.2618 -0.1183 -0.0818 -0.0473 122 VAL J O   
18726 C CB  . VAL J  122 ? 1.1053 1.0988 0.8648 -0.1030 -0.0779 -0.0461 122 VAL J CB  
18727 C CG1 . VAL J  122 ? 1.2696 1.2637 1.0253 -0.1043 -0.0785 -0.0448 122 VAL J CG1 
18728 C CG2 . VAL J  122 ? 1.1291 1.1224 0.8934 -0.0982 -0.0723 -0.0491 122 VAL J CG2 
18729 N N   . ARG J  123 ? 1.1685 1.1616 0.9175 -0.1145 -0.0885 -0.0413 123 ARG J N   
18730 C CA  . ARG J  123 ? 1.2754 1.2694 1.0203 -0.1188 -0.0932 -0.0375 123 ARG J CA  
18731 C C   . ARG J  123 ? 1.2928 1.2839 1.0274 -0.1261 -0.0940 -0.0397 123 ARG J C   
18732 O O   . ARG J  123 ? 1.4114 1.4015 1.1388 -0.1302 -0.0947 -0.0391 123 ARG J O   
18733 C CB  . ARG J  123 ? 1.2258 1.2236 0.9779 -0.1171 -0.0985 -0.0324 123 ARG J CB  
18734 C CG  . ARG J  123 ? 1.3033 1.3030 1.0532 -0.1201 -0.1034 -0.0276 123 ARG J CG  
18735 C CD  . ARG J  123 ? 1.4053 1.4077 1.1585 -0.1215 -0.1091 -0.0236 123 ARG J CD  
18736 N NE  . ARG J  123 ? 1.5812 1.5819 1.3289 -0.1264 -0.1098 -0.0262 123 ARG J NE  
18737 C CZ  . ARG J  123 ? 1.8112 1.8137 1.5580 -0.1302 -0.1150 -0.0234 123 ARG J CZ  
18738 N NH1 . ARG J  123 ? 1.7985 1.8047 1.5498 -0.1295 -0.1200 -0.0175 123 ARG J NH1 
18739 N NH2 . ARG J  123 ? 1.8440 1.8447 1.5855 -0.1349 -0.1152 -0.0264 123 ARG J NH2 
18740 N N   . SER J  124 ? 1.3874 1.3771 1.1212 -0.1279 -0.0937 -0.0423 124 SER J N   
18741 C CA  . SER J  124 ? 1.5658 1.5526 1.2900 -0.1351 -0.0942 -0.0447 124 SER J CA  
18742 C C   . SER J  124 ? 1.6072 1.5893 1.3241 -0.1371 -0.0881 -0.0501 124 SER J C   
18743 O O   . SER J  124 ? 1.7660 1.7447 1.4763 -0.1420 -0.0862 -0.0538 124 SER J O   
18744 C CB  . SER J  124 ? 1.6590 1.6456 1.3862 -0.1362 -0.0951 -0.0454 124 SER J CB  
18745 O OG  . SER J  124 ? 1.5790 1.5634 1.3112 -0.1320 -0.0895 -0.0490 124 SER J OG  
18746 N N   . GLN J  125 ? 1.5194 1.5014 1.2376 -0.1334 -0.0848 -0.0508 125 GLN J N   
18747 C CA  . GLN J  125 ? 1.5030 1.4809 1.2159 -0.1343 -0.0785 -0.0558 125 GLN J CA  
18748 C C   . GLN J  125 ? 1.5478 1.5260 1.2579 -0.1338 -0.0773 -0.0551 125 GLN J C   
18749 O O   . GLN J  125 ? 1.5162 1.4909 1.2198 -0.1360 -0.0729 -0.0590 125 GLN J O   
18750 C CB  . GLN J  125 ? 1.2961 1.2730 1.0161 -0.1291 -0.0731 -0.0588 125 GLN J CB  
18751 C CG  . GLN J  125 ? 1.4004 1.3774 1.1233 -0.1244 -0.0686 -0.0601 125 GLN J CG  
18752 C CD  . GLN J  125 ? 1.6428 1.6179 1.3703 -0.1208 -0.0623 -0.0638 125 GLN J CD  
18753 O OE1 . GLN J  125 ? 1.6013 1.5791 1.3381 -0.1148 -0.0615 -0.0625 125 GLN J OE1 
18754 N NE2 . GLN J  125 ? 1.7148 1.6852 1.4359 -0.1245 -0.0576 -0.0683 125 GLN J NE2 
18755 N N   . LEU J  126 ? 1.5732 1.5552 1.2889 -0.1307 -0.0807 -0.0502 126 LEU J N   
18756 C CA  . LEU J  126 ? 1.3659 1.3482 1.0776 -0.1325 -0.0816 -0.0480 126 LEU J CA  
18757 C C   . LEU J  126 ? 1.6882 1.6734 1.4000 -0.1350 -0.0883 -0.0426 126 LEU J C   
18758 O O   . LEU J  126 ? 1.9163 1.9051 1.6365 -0.1311 -0.0915 -0.0386 126 LEU J O   
18759 C CB  . LEU J  126 ? 1.3754 1.3597 1.0934 -0.1268 -0.0791 -0.0473 126 LEU J CB  
18760 C CG  . LEU J  126 ? 1.3948 1.3814 1.1231 -0.1201 -0.0776 -0.0475 126 LEU J CG  
18761 C CD1 . LEU J  126 ? 1.3956 1.3860 1.1315 -0.1155 -0.0794 -0.0434 126 LEU J CD1 
18762 C CD2 . LEU J  126 ? 1.3988 1.3833 1.1274 -0.1176 -0.0714 -0.0526 126 LEU J CD2 
18763 N N   . LYS J  127 ? 1.5631 1.5466 1.2654 -0.1416 -0.0903 -0.0426 127 LYS J N   
18764 C CA  . LYS J  127 ? 1.5989 1.5851 1.3001 -0.1448 -0.0969 -0.0375 127 LYS J CA  
18765 C C   . LYS J  127 ? 1.8705 1.8583 1.5702 -0.1450 -0.0989 -0.0335 127 LYS J C   
18766 O O   . LYS J  127 ? 1.7216 1.7126 1.4291 -0.1406 -0.1010 -0.0294 127 LYS J O   
18767 C CB  . LYS J  127 ? 1.6170 1.6012 1.3086 -0.1522 -0.0985 -0.0392 127 LYS J CB  
18768 C CG  . LYS J  127 ? 1.6335 1.6157 1.3261 -0.1523 -0.0961 -0.0437 127 LYS J CG  
18769 C CD  . LYS J  127 ? 1.5729 1.5499 1.2548 -0.1578 -0.0917 -0.0496 127 LYS J CD  
18770 C CE  . LYS J  127 ? 1.7337 1.7085 1.4163 -0.1583 -0.0893 -0.0540 127 LYS J CE  
18771 N NZ  . LYS J  127 ? 1.7255 1.6947 1.3983 -0.1632 -0.0841 -0.0605 127 LYS J NZ  
18772 N N   . ASN J  128 ? 2.2060 2.1912 1.8955 -0.1502 -0.0979 -0.0349 128 ASN J N   
18773 C CA  . ASN J  128 ? 2.1801 2.1661 1.8672 -0.1507 -0.0992 -0.0318 128 ASN J CA  
18774 C C   . ASN J  128 ? 2.2284 2.2135 1.9191 -0.1459 -0.0941 -0.0338 128 ASN J C   
18775 O O   . ASN J  128 ? 2.1754 2.1623 1.8686 -0.1439 -0.0953 -0.0305 128 ASN J O   
18776 C CB  . ASN J  128 ? 2.1234 2.1070 1.7978 -0.1583 -0.1002 -0.0324 128 ASN J CB  
18777 C CG  . ASN J  128 ? 2.2471 2.2329 1.9182 -0.1633 -0.1064 -0.0290 128 ASN J CG  
18778 O OD1 . ASN J  128 ? 2.2582 2.2481 1.9355 -0.1614 -0.1115 -0.0237 128 ASN J OD1 
18779 N ND2 . ASN J  128 ? 2.3952 2.3783 2.0564 -0.1698 -0.1059 -0.0322 128 ASN J ND2 
18780 N N   . ASN J  129 ? 2.3726 2.3551 2.0638 -0.1441 -0.0885 -0.0391 129 ASN J N   
18781 C CA  . ASN J  129 ? 2.3571 2.3387 2.0506 -0.1402 -0.0834 -0.0415 129 ASN J CA  
18782 C C   . ASN J  129 ? 2.2885 2.2739 1.9933 -0.1334 -0.0839 -0.0387 129 ASN J C   
18783 O O   . ASN J  129 ? 2.2862 2.2716 1.9940 -0.1299 -0.0800 -0.0404 129 ASN J O   
18784 C CB  . ASN J  129 ? 2.2931 2.2714 1.9849 -0.1399 -0.0775 -0.0477 129 ASN J CB  
18785 C CG  . ASN J  129 ? 2.2196 2.1937 1.8997 -0.1469 -0.0760 -0.0511 129 ASN J CG  
18786 O OD1 . ASN J  129 ? 2.1914 2.1620 1.8685 -0.1475 -0.0709 -0.0563 129 ASN J OD1 
18787 N ND2 . ASN J  129 ? 2.2929 2.2670 1.9659 -0.1523 -0.0803 -0.0483 129 ASN J ND2 
18788 N N   . ALA J  130 ? 2.0334 2.0219 1.7444 -0.1316 -0.0885 -0.0346 130 ALA J N   
18789 C CA  . ALA J  130 ? 1.8816 1.8736 1.6030 -0.1255 -0.0892 -0.0318 130 ALA J CA  
18790 C C   . ALA J  130 ? 1.6693 1.6643 1.3950 -0.1253 -0.0953 -0.0265 130 ALA J C   
18791 O O   . ALA J  130 ? 1.5855 1.5803 1.3071 -0.1296 -0.0988 -0.0253 130 ALA J O   
18792 C CB  . ALA J  130 ? 1.8448 1.8371 1.5732 -0.1204 -0.0853 -0.0351 130 ALA J CB  
18793 N N   . LYS J  131 ? 1.7289 1.7268 1.4631 -0.1206 -0.0964 -0.0233 131 LYS J N   
18794 C CA  . LYS J  131 ? 1.9467 1.9476 1.6858 -0.1200 -0.1019 -0.0181 131 LYS J CA  
18795 C C   . LYS J  131 ? 2.0592 2.0625 1.8092 -0.1140 -0.1015 -0.0175 131 LYS J C   
18796 O O   . LYS J  131 ? 1.9482 1.9516 1.7026 -0.1097 -0.0975 -0.0199 131 LYS J O   
18797 C CB  . LYS J  131 ? 1.9339 1.9361 1.6720 -0.1208 -0.1047 -0.0137 131 LYS J CB  
18798 C CG  . LYS J  131 ? 1.9403 1.9436 1.6844 -0.1158 -0.1020 -0.0136 131 LYS J CG  
18799 C CD  . LYS J  131 ? 1.9214 1.9264 1.6666 -0.1160 -0.1057 -0.0083 131 LYS J CD  
18800 C CE  . LYS J  131 ? 1.8494 1.8557 1.6012 -0.1110 -0.1032 -0.0083 131 LYS J CE  
18801 N NZ  . LYS J  131 ? 1.9019 1.9099 1.6555 -0.1108 -0.1068 -0.0030 131 LYS J NZ  
18802 N N   . GLU J  132 ? 2.1303 2.1357 1.8845 -0.1139 -0.1057 -0.0144 132 GLU J N   
18803 C CA  . GLU J  132 ? 1.9761 1.9837 1.7404 -0.1086 -0.1059 -0.0133 132 GLU J CA  
18804 C C   . GLU J  132 ? 1.9782 1.9881 1.7483 -0.1053 -0.1070 -0.0097 132 GLU J C   
18805 O O   . GLU J  132 ? 2.1913 2.2020 1.9590 -0.1076 -0.1103 -0.0059 132 GLU J O   
18806 C CB  . GLU J  132 ? 2.0546 2.0637 1.8214 -0.1098 -0.1102 -0.0110 132 GLU J CB  
18807 C CG  . GLU J  132 ? 2.0786 2.0855 1.8398 -0.1135 -0.1095 -0.0145 132 GLU J CG  
18808 C CD  . GLU J  132 ? 2.1540 2.1627 1.9176 -0.1151 -0.1142 -0.0119 132 GLU J CD  
18809 O OE1 . GLU J  132 ? 2.1299 2.1371 1.8881 -0.1192 -0.1146 -0.0142 132 GLU J OE1 
18810 O OE2 . GLU J  132 ? 2.1675 2.1792 1.9386 -0.1125 -0.1174 -0.0076 132 GLU J OE2 
18811 N N   . ILE J  133 ? 1.8109 1.8219 1.5884 -0.0999 -0.1042 -0.0108 133 ILE J N   
18812 C CA  . ILE J  133 ? 1.9544 1.9676 1.7380 -0.0966 -0.1050 -0.0077 133 ILE J CA  
18813 C C   . ILE J  133 ? 2.0225 2.0381 1.8135 -0.0946 -0.1089 -0.0039 133 ILE J C   
18814 O O   . ILE J  133 ? 2.0944 2.1118 1.8888 -0.0939 -0.1118 0.0004  133 ILE J O   
18815 C CB  . ILE J  133 ? 2.0162 2.0297 1.8039 -0.0921 -0.1001 -0.0109 133 ILE J CB  
18816 C CG1 . ILE J  133 ? 2.0149 2.0262 1.7957 -0.0940 -0.0963 -0.0144 133 ILE J CG1 
18817 C CG2 . ILE J  133 ? 1.8308 1.8464 1.6247 -0.0889 -0.1009 -0.0079 133 ILE J CG2 
18818 C CD1 . ILE J  133 ? 2.0655 2.0764 1.8418 -0.0965 -0.0976 -0.0122 133 ILE J CD1 
18819 N N   . GLY J  134 ? 1.7863 1.8020 1.5800 -0.0937 -0.1088 -0.0054 134 GLY J N   
18820 C CA  . GLY J  134 ? 1.7839 1.8018 1.5848 -0.0918 -0.1121 -0.0022 134 GLY J CA  
18821 C C   . GLY J  134 ? 1.5281 1.5469 1.3365 -0.0864 -0.1090 -0.0043 134 GLY J C   
18822 O O   . GLY J  134 ? 1.3473 1.3674 1.1615 -0.0846 -0.1106 -0.0029 134 GLY J O   
18823 N N   . ASN J  135 ? 1.4036 1.4219 1.2119 -0.0840 -0.1045 -0.0074 135 ASN J N   
18824 C CA  . ASN J  135 ? 1.2901 1.3095 1.1049 -0.0790 -0.1013 -0.0094 135 ASN J CA  
18825 C C   . ASN J  135 ? 1.2937 1.3118 1.1063 -0.0786 -0.0979 -0.0139 135 ASN J C   
18826 O O   . ASN J  135 ? 1.0748 1.0935 0.8904 -0.0750 -0.0942 -0.0165 135 ASN J O   
18827 C CB  . ASN J  135 ? 1.3163 1.3366 1.1331 -0.0764 -0.0986 -0.0099 135 ASN J CB  
18828 C CG  . ASN J  135 ? 1.5006 1.5228 1.3249 -0.0713 -0.0964 -0.0108 135 ASN J CG  
18829 O OD1 . ASN J  135 ? 1.3775 1.4005 1.2060 -0.0696 -0.0972 -0.0106 135 ASN J OD1 
18830 N ND2 . ASN J  135 ? 1.7186 1.7418 1.5444 -0.0691 -0.0936 -0.0119 135 ASN J ND2 
18831 N N   . GLY J  136 ? 1.2592 1.2755 1.0665 -0.0824 -0.0992 -0.0148 136 GLY J N   
18832 C CA  . GLY J  136 ? 1.0679 1.0825 0.8725 -0.0826 -0.0961 -0.0191 136 GLY J CA  
18833 C C   . GLY J  136 ? 1.2925 1.3053 1.0910 -0.0838 -0.0922 -0.0226 136 GLY J C   
18834 O O   . GLY J  136 ? 1.4005 1.4119 1.1970 -0.0834 -0.0888 -0.0265 136 GLY J O   
18835 N N   . CYS J  137 ? 1.6415 1.6542 1.4373 -0.0852 -0.0924 -0.0213 137 CYS J N   
18836 C CA  . CYS J  137 ? 1.6447 1.6558 1.4349 -0.0864 -0.0887 -0.0245 137 CYS J CA  
18837 C C   . CYS J  137 ? 1.6418 1.6509 1.4237 -0.0920 -0.0907 -0.0235 137 CYS J C   
18838 O O   . CYS J  137 ? 1.7070 1.7167 1.4885 -0.0941 -0.0951 -0.0196 137 CYS J O   
18839 C CB  . CYS J  137 ? 1.4269 1.4399 1.2209 -0.0829 -0.0862 -0.0246 137 CYS J CB  
18840 S SG  . CYS J  137 ? 1.9609 1.9761 1.7618 -0.0772 -0.0821 -0.0274 137 CYS J SG  
18841 N N   . PHE J  138 ? 1.4812 1.4879 1.2563 -0.0944 -0.0876 -0.0271 138 PHE J N   
18842 C CA  . PHE J  138 ? 1.7360 1.7403 1.5020 -0.1000 -0.0887 -0.0270 138 PHE J CA  
18843 C C   . PHE J  138 ? 1.8783 1.8816 1.6404 -0.1005 -0.0855 -0.0288 138 PHE J C   
18844 O O   . PHE J  138 ? 1.7960 1.7991 1.5592 -0.0981 -0.0810 -0.0323 138 PHE J O   
18845 C CB  . PHE J  138 ? 1.6539 1.6554 1.4138 -0.1035 -0.0876 -0.0304 138 PHE J CB  
18846 C CG  . PHE J  138 ? 1.5568 1.5589 1.3199 -0.1034 -0.0903 -0.0295 138 PHE J CG  
18847 C CD1 . PHE J  138 ? 1.4829 1.4861 1.2528 -0.0988 -0.0883 -0.0310 138 PHE J CD1 
18848 C CD2 . PHE J  138 ? 1.6195 1.6211 1.3784 -0.1080 -0.0946 -0.0274 138 PHE J CD2 
18849 C CE1 . PHE J  138 ? 1.5577 1.5613 1.3304 -0.0987 -0.0906 -0.0303 138 PHE J CE1 
18850 C CE2 . PHE J  138 ? 1.5366 1.5389 1.2986 -0.1080 -0.0970 -0.0268 138 PHE J CE2 
18851 C CZ  . PHE J  138 ? 1.5225 1.5257 1.2914 -0.1033 -0.0949 -0.0283 138 PHE J CZ  
18852 N N   . GLU J  139 ? 2.0556 2.0583 1.8129 -0.1038 -0.0877 -0.0264 139 GLU J N   
18853 C CA  . GLU J  139 ? 1.9026 1.9044 1.6560 -0.1046 -0.0849 -0.0278 139 GLU J CA  
18854 C C   . GLU J  139 ? 1.8555 1.8538 1.5986 -0.1099 -0.0835 -0.0304 139 GLU J C   
18855 O O   . GLU J  139 ? 1.8861 1.8832 1.6234 -0.1145 -0.0868 -0.0287 139 GLU J O   
18856 C CB  . GLU J  139 ? 1.9952 1.9985 1.7499 -0.1045 -0.0877 -0.0236 139 GLU J CB  
18857 C CG  . GLU J  139 ? 2.2023 2.2047 1.9533 -0.1052 -0.0849 -0.0249 139 GLU J CG  
18858 C CD  . GLU J  139 ? 2.2991 2.3031 2.0528 -0.1041 -0.0872 -0.0210 139 GLU J CD  
18859 O OE1 . GLU J  139 ? 2.2001 2.2061 1.9591 -0.1025 -0.0907 -0.0173 139 GLU J OE1 
18860 O OE2 . GLU J  139 ? 2.2885 2.2918 2.0391 -0.1048 -0.0852 -0.0217 139 GLU J OE2 
18861 N N   . PHE J  140 ? 2.1224 2.1192 1.8635 -0.1092 -0.0785 -0.0347 140 PHE J N   
18862 C CA  . PHE J  140 ? 2.2722 2.2653 2.0036 -0.1140 -0.0762 -0.0379 140 PHE J CA  
18863 C C   . PHE J  140 ? 2.2844 2.2764 2.0092 -0.1176 -0.0772 -0.0363 140 PHE J C   
18864 O O   . PHE J  140 ? 2.2397 2.2332 1.9675 -0.1154 -0.0766 -0.0350 140 PHE J O   
18865 C CB  . PHE J  140 ? 2.2172 2.2093 1.9491 -0.1119 -0.0704 -0.0428 140 PHE J CB  
18866 C CG  . PHE J  140 ? 2.1203 2.1127 1.8563 -0.1094 -0.0689 -0.0451 140 PHE J CG  
18867 C CD1 . PHE J  140 ? 2.0444 2.0400 1.7897 -0.1036 -0.0678 -0.0449 140 PHE J CD1 
18868 C CD2 . PHE J  140 ? 2.1366 2.1260 1.8670 -0.1129 -0.0685 -0.0475 140 PHE J CD2 
18869 C CE1 . PHE J  140 ? 2.0161 2.0119 1.7650 -0.1012 -0.0665 -0.0468 140 PHE J CE1 
18870 C CE2 . PHE J  140 ? 2.1215 2.1108 1.8555 -0.1106 -0.0670 -0.0496 140 PHE J CE2 
18871 C CZ  . PHE J  140 ? 2.0611 2.0537 1.8044 -0.1046 -0.0660 -0.0492 140 PHE J CZ  
18872 N N   . TYR J  141 ? 1.9754 1.9646 1.6909 -0.1234 -0.0785 -0.0366 141 TYR J N   
18873 C CA  . TYR J  141 ? 1.9767 1.9642 1.6844 -0.1273 -0.0787 -0.0358 141 TYR J CA  
18874 C C   . TYR J  141 ? 1.9239 1.9082 1.6260 -0.1288 -0.0730 -0.0410 141 TYR J C   
18875 O O   . TYR J  141 ? 1.9441 1.9269 1.6406 -0.1311 -0.0717 -0.0413 141 TYR J O   
18876 C CB  . TYR J  141 ? 2.0475 2.0338 1.7473 -0.1332 -0.0833 -0.0332 141 TYR J CB  
18877 C CG  . TYR J  141 ? 1.9828 1.9724 1.6874 -0.1324 -0.0893 -0.0277 141 TYR J CG  
18878 C CD1 . TYR J  141 ? 1.9291 1.9190 1.6321 -0.1353 -0.0931 -0.0263 141 TYR J CD1 
18879 C CD2 . TYR J  141 ? 1.8603 1.8526 1.5710 -0.1290 -0.0911 -0.0238 141 TYR J CD2 
18880 C CE1 . TYR J  141 ? 1.8995 1.8927 1.6072 -0.1345 -0.0986 -0.0210 141 TYR J CE1 
18881 C CE2 . TYR J  141 ? 1.8186 1.8137 1.5338 -0.1282 -0.0964 -0.0187 141 TYR J CE2 
18882 C CZ  . TYR J  141 ? 1.8610 1.8567 1.5749 -0.1309 -0.1002 -0.0172 141 TYR J CZ  
18883 O OH  . TYR J  141 ? 1.7464 1.7452 1.4652 -0.1301 -0.1055 -0.0119 141 TYR J OH  
18884 N N   . HIS J  142 ? 1.9377 1.9210 1.6413 -0.1274 -0.0696 -0.0450 142 HIS J N   
18885 C CA  . HIS J  142 ? 1.9000 1.8801 1.5985 -0.1288 -0.0641 -0.0501 142 HIS J CA  
18886 C C   . HIS J  142 ? 1.8839 1.8658 1.5902 -0.1231 -0.0597 -0.0527 142 HIS J C   
18887 O O   . HIS J  142 ? 1.9539 1.9375 1.6667 -0.1196 -0.0596 -0.0531 142 HIS J O   
18888 C CB  . HIS J  142 ? 1.9034 1.8800 1.5950 -0.1332 -0.0634 -0.0530 142 HIS J CB  
18889 C CG  . HIS J  142 ? 1.9701 1.9470 1.6672 -0.1299 -0.0612 -0.0558 142 HIS J CG  
18890 N ND1 . HIS J  142 ? 1.9565 1.9302 1.6503 -0.1307 -0.0559 -0.0610 142 HIS J ND1 
18891 C CD2 . HIS J  142 ? 1.9974 1.9772 1.7030 -0.1259 -0.0633 -0.0540 142 HIS J CD2 
18892 C CE1 . HIS J  142 ? 1.9846 1.9592 1.6844 -0.1272 -0.0550 -0.0622 142 HIS J CE1 
18893 N NE2 . HIS J  142 ? 2.0360 2.0144 1.7430 -0.1243 -0.0595 -0.0581 142 HIS J NE2 
18894 N N   . LYS J  143 ? 1.8839 1.8657 1.5898 -0.1221 -0.0562 -0.0543 143 LYS J N   
18895 C CA  . LYS J  143 ? 1.8681 1.8525 1.5818 -0.1166 -0.0525 -0.0563 143 LYS J CA  
18896 C C   . LYS J  143 ? 1.8859 1.8698 1.6022 -0.1146 -0.0499 -0.0595 143 LYS J C   
18897 O O   . LYS J  143 ? 1.8243 1.8045 1.5345 -0.1174 -0.0466 -0.0633 143 LYS J O   
18898 C CB  . LYS J  143 ? 1.9066 1.8900 1.6173 -0.1171 -0.0482 -0.0588 143 LYS J CB  
18899 C CG  . LYS J  143 ? 1.9338 1.9186 1.6444 -0.1174 -0.0501 -0.0558 143 LYS J CG  
18900 C CD  . LYS J  143 ? 2.0092 1.9989 1.7299 -0.1118 -0.0503 -0.0542 143 LYS J CD  
18901 C CE  . LYS J  143 ? 2.0038 1.9961 1.7307 -0.1095 -0.0549 -0.0502 143 LYS J CE  
18902 N NZ  . LYS J  143 ? 1.8912 1.8879 1.6272 -0.1044 -0.0548 -0.0489 143 LYS J NZ  
18903 N N   . CYS J  144 ? 2.0636 2.0511 1.7888 -0.1098 -0.0513 -0.0579 144 CYS J N   
18904 C CA  . CYS J  144 ? 2.1193 2.1067 1.8476 -0.1075 -0.0493 -0.0604 144 CYS J CA  
18905 C C   . CYS J  144 ? 1.9651 1.9560 1.7014 -0.1017 -0.0461 -0.0617 144 CYS J C   
18906 O O   . CYS J  144 ? 1.9286 1.9235 1.6728 -0.0975 -0.0480 -0.0592 144 CYS J O   
18907 C CB  . CYS J  144 ? 2.1019 2.0902 1.8333 -0.1071 -0.0537 -0.0577 144 CYS J CB  
18908 S SG  . CYS J  144 ? 2.1489 2.1357 1.8818 -0.1057 -0.0514 -0.0610 144 CYS J SG  
18909 N N   . ASP J  145 ? 2.1185 2.1079 1.8523 -0.1017 -0.0410 -0.0657 145 ASP J N   
18910 C CA  . ASP J  145 ? 2.1703 2.1632 1.9109 -0.0965 -0.0377 -0.0673 145 ASP J CA  
18911 C C   . ASP J  145 ? 2.0651 2.0588 1.8111 -0.0932 -0.0367 -0.0679 145 ASP J C   
18912 O O   . ASP J  145 ? 2.1020 2.0943 1.8473 -0.0944 -0.0395 -0.0669 145 ASP J O   
18913 C CB  . ASP J  145 ? 2.2994 2.2907 2.0363 -0.0975 -0.0324 -0.0709 145 ASP J CB  
18914 C CG  . ASP J  145 ? 2.3534 2.3387 2.0820 -0.1024 -0.0296 -0.0739 145 ASP J CG  
18915 O OD1 . ASP J  145 ? 2.2121 2.1957 1.9394 -0.1027 -0.0243 -0.0770 145 ASP J OD1 
18916 O OD2 . ASP J  145 ? 2.3797 2.3621 2.1031 -0.1061 -0.0327 -0.0732 145 ASP J OD2 
18917 N N   . ASN J  146 ? 1.9052 1.9014 1.6575 -0.0890 -0.0326 -0.0694 146 ASN J N   
18918 C CA  . ASN J  146 ? 1.7731 1.7708 1.5323 -0.0851 -0.0312 -0.0694 146 ASN J CA  
18919 C C   . ASN J  146 ? 1.8595 1.8522 1.6151 -0.0877 -0.0290 -0.0716 146 ASN J C   
18920 O O   . ASN J  146 ? 2.1062 2.0989 1.8649 -0.0865 -0.0307 -0.0706 146 ASN J O   
18921 C CB  . ASN J  146 ? 1.5481 1.5498 1.3144 -0.0803 -0.0270 -0.0704 146 ASN J CB  
18922 C CG  . ASN J  146 ? 1.5496 1.5572 1.3215 -0.0769 -0.0294 -0.0680 146 ASN J CG  
18923 O OD1 . ASN J  146 ? 1.6233 1.6349 1.4004 -0.0734 -0.0266 -0.0685 146 ASN J OD1 
18924 N ND2 . ASN J  146 ? 1.5610 1.5693 1.3319 -0.0778 -0.0345 -0.0653 146 ASN J ND2 
18925 N N   . THR J  147 ? 2.0482 2.0365 1.7973 -0.0914 -0.0252 -0.0748 147 THR J N   
18926 C CA  . THR J  147 ? 2.2291 2.2121 1.9742 -0.0944 -0.0225 -0.0773 147 THR J CA  
18927 C C   . THR J  147 ? 2.2992 2.2789 2.0366 -0.0997 -0.0270 -0.0765 147 THR J C   
18928 O O   . THR J  147 ? 2.3022 2.2779 2.0364 -0.1025 -0.0260 -0.0783 147 THR J O   
18929 C CB  . THR J  147 ? 2.2025 2.1817 1.9434 -0.0965 -0.0162 -0.0812 147 THR J CB  
18930 O OG1 . THR J  147 ? 2.3093 2.2865 2.0419 -0.1011 -0.0171 -0.0818 147 THR J OG1 
18931 N N   . CYS J  148 ? 2.1238 2.1053 1.8586 -0.1012 -0.0319 -0.0739 148 CYS J N   
18932 C CA  . CYS J  148 ? 2.1663 2.1461 1.8955 -0.1056 -0.0371 -0.0721 148 CYS J CA  
18933 C C   . CYS J  148 ? 2.2404 2.2231 1.9766 -0.1024 -0.0408 -0.0693 148 CYS J C   
18934 O O   . CYS J  148 ? 2.1887 2.1693 1.9231 -0.1047 -0.0426 -0.0692 148 CYS J O   
18935 C CB  . CYS J  148 ? 2.0815 2.0622 1.8060 -0.1080 -0.0408 -0.0698 148 CYS J CB  
18936 S SG  . CYS J  148 ? 2.0771 2.0569 1.7968 -0.1129 -0.0475 -0.0662 148 CYS J SG  
18937 N N   . MET J  149 ? 2.2327 2.2203 1.9770 -0.0970 -0.0418 -0.0670 149 MET J N   
18938 C CA  . MET J  149 ? 2.0314 2.0222 1.7834 -0.0932 -0.0448 -0.0644 149 MET J CA  
18939 C C   . MET J  149 ? 1.9677 1.9567 1.7226 -0.0920 -0.0421 -0.0661 149 MET J C   
18940 O O   . MET J  149 ? 1.9520 1.9419 1.7105 -0.0910 -0.0449 -0.0643 149 MET J O   
18941 C CB  . MET J  149 ? 1.8861 1.8823 1.6462 -0.0876 -0.0446 -0.0627 149 MET J CB  
18942 C CG  . MET J  149 ? 1.8543 1.8527 1.6131 -0.0882 -0.0476 -0.0605 149 MET J CG  
18943 S SD  . MET J  149 ? 1.6659 1.6647 1.4256 -0.0900 -0.0541 -0.0557 149 MET J SD  
18944 C CE  . MET J  149 ? 1.7036 1.7053 1.4655 -0.0891 -0.0553 -0.0529 149 MET J CE  
18945 N N   . GLU J  150 ? 2.5444 2.5309 2.2981 -0.0921 -0.0363 -0.0696 150 GLU J N   
18946 C CA  . GLU J  150 ? 2.5636 2.5482 2.3207 -0.0906 -0.0328 -0.0714 150 GLU J CA  
18947 C C   . GLU J  150 ? 2.5764 2.5561 2.3269 -0.0960 -0.0338 -0.0728 150 GLU J C   
18948 O O   . GLU J  150 ? 2.6013 2.5805 2.3550 -0.0951 -0.0344 -0.0724 150 GLU J O   
18949 C CB  . GLU J  150 ? 2.6742 2.6577 2.4326 -0.0889 -0.0260 -0.0745 150 GLU J CB  
18950 C CG  . GLU J  150 ? 2.7011 2.6873 2.4690 -0.0829 -0.0229 -0.0742 150 GLU J CG  
18951 C CD  . GLU J  150 ? 2.6750 2.6676 2.4500 -0.0776 -0.0240 -0.0717 150 GLU J CD  
18952 O OE1 . GLU J  150 ? 2.6631 2.6584 2.4452 -0.0729 -0.0205 -0.0718 150 GLU J OE1 
18953 O OE2 . GLU J  150 ? 2.5837 2.5788 2.3574 -0.0783 -0.0283 -0.0697 150 GLU J OE2 
18954 N N   . SER J  151 ? 2.1498 2.1260 1.8908 -0.1017 -0.0340 -0.0744 151 SER J N   
18955 C CA  . SER J  151 ? 2.1455 2.1171 1.8791 -0.1077 -0.0350 -0.0759 151 SER J CA  
18956 C C   . SER J  151 ? 2.1122 2.0857 1.8478 -0.1080 -0.0411 -0.0726 151 SER J C   
18957 O O   . SER J  151 ? 2.1463 2.1170 1.8793 -0.1112 -0.0416 -0.0737 151 SER J O   
18958 C CB  . SER J  151 ? 2.1260 2.0945 1.8489 -0.1137 -0.0354 -0.0772 151 SER J CB  
18959 O OG  . SER J  151 ? 2.1477 2.1194 1.8694 -0.1143 -0.0410 -0.0736 151 SER J OG  
18960 N N   . VAL J  152 ? 1.7777 1.7560 1.5183 -0.1047 -0.0454 -0.0687 152 VAL J N   
18961 C CA  . VAL J  152 ? 1.6014 1.5821 1.3451 -0.1045 -0.0512 -0.0652 152 VAL J CA  
18962 C C   . VAL J  152 ? 1.6696 1.6517 1.4221 -0.0997 -0.0499 -0.0649 152 VAL J C   
18963 O O   . VAL J  152 ? 1.6618 1.6429 1.4148 -0.1011 -0.0520 -0.0644 152 VAL J O   
18964 C CB  . VAL J  152 ? 1.3982 1.3832 1.1444 -0.1026 -0.0559 -0.0612 152 VAL J CB  
18965 C CG1 . VAL J  152 ? 1.2886 1.2752 1.0363 -0.1037 -0.0620 -0.0575 152 VAL J CG1 
18966 C CG2 . VAL J  152 ? 1.5259 1.5097 1.2644 -0.1063 -0.0560 -0.0616 152 VAL J CG2 
18967 N N   . LYS J  153 ? 1.6857 1.6703 1.4451 -0.0941 -0.0466 -0.0651 153 LYS J N   
18968 C CA  . LYS J  153 ? 1.5897 1.5758 1.3575 -0.0892 -0.0450 -0.0647 153 LYS J CA  
18969 C C   . LYS J  153 ? 1.8358 1.8174 1.6020 -0.0911 -0.0408 -0.0680 153 LYS J C   
18970 O O   . LYS J  153 ? 1.9650 1.9459 1.7337 -0.0911 -0.0421 -0.0674 153 LYS J O   
18971 C CB  . LYS J  153 ? 1.4760 1.4659 1.2508 -0.0832 -0.0420 -0.0643 153 LYS J CB  
18972 C CG  . LYS J  153 ? 1.2128 1.2075 0.9907 -0.0807 -0.0457 -0.0611 153 LYS J CG  
18973 C CD  . LYS J  153 ? 1.4189 1.4178 1.2045 -0.0747 -0.0429 -0.0607 153 LYS J CD  
18974 C CE  . LYS J  153 ? 1.3422 1.3456 1.1304 -0.0725 -0.0462 -0.0580 153 LYS J CE  
18975 N NZ  . LYS J  153 ? 1.4358 1.4384 1.2176 -0.0760 -0.0468 -0.0586 153 LYS J NZ  
18976 N N   . ASN J  154 ? 2.4891 2.4674 2.2513 -0.0927 -0.0355 -0.0715 154 ASN J N   
18977 C CA  . ASN J  154 ? 2.6116 2.5848 2.3714 -0.0950 -0.0308 -0.0751 154 ASN J CA  
18978 C C   . ASN J  154 ? 2.6662 2.6360 2.4193 -0.1012 -0.0339 -0.0757 154 ASN J C   
18979 O O   . ASN J  154 ? 2.7421 2.7079 2.4940 -0.1032 -0.0309 -0.0783 154 ASN J O   
18980 C CB  . ASN J  154 ? 2.7627 2.7326 2.5179 -0.0967 -0.0249 -0.0787 154 ASN J CB  
18981 C CG  . ASN J  154 ? 2.6409 2.6134 2.4039 -0.0905 -0.0202 -0.0788 154 ASN J CG  
18982 O OD1 . ASN J  154 ? 2.6587 2.6347 2.4231 -0.0882 -0.0206 -0.0776 154 ASN J OD1 
18983 N ND2 . ASN J  154 ? 2.4567 2.4277 2.2248 -0.0879 -0.0156 -0.0801 154 ASN J ND2 
18984 N N   . GLY J  155 ? 2.2147 2.1863 1.9637 -0.1042 -0.0399 -0.0732 155 GLY J N   
18985 C CA  . GLY J  155 ? 2.2049 2.1741 1.9473 -0.1103 -0.0436 -0.0733 155 GLY J CA  
18986 C C   . GLY J  155 ? 2.2587 2.2228 1.9904 -0.1168 -0.0410 -0.0770 155 GLY J C   
18987 O O   . GLY J  155 ? 2.1821 2.1440 1.9071 -0.1228 -0.0435 -0.0777 155 GLY J O   
18988 N N   . THR J  156 ? 2.4792 2.4418 2.2095 -0.1159 -0.0358 -0.0795 156 THR J N   
18989 C CA  . THR J  156 ? 2.5576 2.5152 2.2778 -0.1218 -0.0326 -0.0833 156 THR J CA  
18990 C C   . THR J  156 ? 2.4094 2.3685 2.1240 -0.1239 -0.0354 -0.0818 156 THR J C   
18991 O O   . THR J  156 ? 2.3322 2.2915 2.0473 -0.1218 -0.0319 -0.0828 156 THR J O   
18992 C CB  . THR J  156 ? 2.6056 2.5598 2.3276 -0.1199 -0.0243 -0.0872 156 THR J CB  
18993 O OG1 . THR J  156 ? 2.4572 2.4155 2.1869 -0.1133 -0.0227 -0.0856 156 THR J OG1 
18994 C CG2 . THR J  156 ? 2.6344 2.5861 2.3606 -0.1189 -0.0209 -0.0891 156 THR J CG2 
18995 N N   . TYR J  157 ? 2.0779 2.0381 1.7874 -0.1280 -0.0416 -0.0793 157 TYR J N   
18996 C CA  . TYR J  157 ? 2.0020 1.9641 1.7071 -0.1295 -0.0449 -0.0771 157 TYR J CA  
18997 C C   . TYR J  157 ? 2.1092 2.0676 1.8019 -0.1375 -0.0459 -0.0787 157 TYR J C   
18998 O O   . TYR J  157 ? 2.0685 2.0265 1.7569 -0.1421 -0.0501 -0.0777 157 TYR J O   
18999 C CB  . TYR J  157 ? 1.9264 1.8938 1.6368 -0.1268 -0.0518 -0.0717 157 TYR J CB  
19000 C CG  . TYR J  157 ? 1.7708 1.7404 1.4777 -0.1280 -0.0552 -0.0689 157 TYR J CG  
19001 C CD1 . TYR J  157 ? 1.7364 1.7092 1.4490 -0.1228 -0.0546 -0.0673 157 TYR J CD1 
19002 C CD2 . TYR J  157 ? 1.7818 1.7502 1.4795 -0.1343 -0.0591 -0.0679 157 TYR J CD2 
19003 C CE1 . TYR J  157 ? 1.6314 1.6060 1.3413 -0.1238 -0.0574 -0.0647 157 TYR J CE1 
19004 C CE2 . TYR J  157 ? 1.7872 1.7574 1.4827 -0.1352 -0.0618 -0.0648 157 TYR J CE2 
19005 C CZ  . TYR J  157 ? 1.5836 1.5567 1.2857 -0.1298 -0.0606 -0.0631 157 TYR J CZ  
19006 O OH  . TYR J  157 ? 1.4671 1.4417 1.1678 -0.1306 -0.0628 -0.0600 157 TYR J OH  
19007 N N   . ASP J  158 ? 1.9905 1.9465 1.6777 -0.1392 -0.0421 -0.0811 158 ASP J N   
19008 C CA  . ASP J  158 ? 2.0883 2.0409 1.7634 -0.1466 -0.0428 -0.0825 158 ASP J CA  
19009 C C   . ASP J  158 ? 2.0818 2.0381 1.7544 -0.1480 -0.0497 -0.0777 158 ASP J C   
19010 O O   . ASP J  158 ? 1.9463 1.9053 1.6220 -0.1445 -0.0502 -0.0756 158 ASP J O   
19011 C CB  . ASP J  158 ? 2.1262 2.0749 1.7968 -0.1476 -0.0361 -0.0866 158 ASP J CB  
19012 C CG  . ASP J  158 ? 2.1007 2.0465 1.7589 -0.1547 -0.0370 -0.0875 158 ASP J CG  
19013 O OD1 . ASP J  158 ? 1.9301 1.8716 1.5799 -0.1609 -0.0358 -0.0905 158 ASP J OD1 
19014 O OD2 . ASP J  158 ? 2.0439 1.9917 1.7007 -0.1541 -0.0387 -0.0854 158 ASP J OD2 
19015 N N   . TYR J  159 ? 2.2859 2.2424 1.9533 -0.1529 -0.0549 -0.0759 159 TYR J N   
19016 C CA  . TYR J  159 ? 2.2533 2.2136 1.9202 -0.1541 -0.0615 -0.0704 159 TYR J CA  
19017 C C   . TYR J  159 ? 2.3649 2.3237 2.0233 -0.1584 -0.0613 -0.0699 159 TYR J C   
19018 O O   . TYR J  159 ? 2.3615 2.3235 2.0222 -0.1569 -0.0648 -0.0654 159 TYR J O   
19019 C CB  . TYR J  159 ? 2.3269 2.2885 1.9923 -0.1578 -0.0671 -0.0680 159 TYR J CB  
19020 C CG  . TYR J  159 ? 2.6579 2.6152 2.3116 -0.1658 -0.0663 -0.0716 159 TYR J CG  
19021 C CD1 . TYR J  159 ? 2.6900 2.6469 2.3345 -0.1720 -0.0692 -0.0698 159 TYR J CD1 
19022 C CD2 . TYR J  159 ? 2.6767 2.6303 2.3291 -0.1674 -0.0621 -0.0765 159 TYR J CD2 
19023 C CE1 . TYR J  159 ? 2.7566 2.7097 2.3899 -0.1797 -0.0685 -0.0732 159 TYR J CE1 
19024 C CE2 . TYR J  159 ? 2.7461 2.6954 2.3877 -0.1751 -0.0609 -0.0800 159 TYR J CE2 
19025 C CZ  . TYR J  159 ? 2.7361 2.6854 2.3673 -0.1814 -0.0645 -0.0787 159 TYR J CZ  
19026 O OH  . TYR J  159 ? 2.6227 2.5679 2.2426 -0.1895 -0.0634 -0.0822 159 TYR J OH  
19027 N N   . PRO J  160 ? 2.3912 2.3449 2.0394 -0.1638 -0.0572 -0.0747 160 PRO J N   
19028 C CA  . PRO J  160 ? 2.2934 2.2455 1.9325 -0.1685 -0.0573 -0.0741 160 PRO J CA  
19029 C C   . PRO J  160 ? 1.9564 1.9090 1.5986 -0.1643 -0.0540 -0.0741 160 PRO J C   
19030 O O   . PRO J  160 ? 1.8614 1.8100 1.4986 -0.1658 -0.0483 -0.0785 160 PRO J O   
19031 C CB  . PRO J  160 ? 2.3134 2.2595 1.9413 -0.1752 -0.0531 -0.0800 160 PRO J CB  
19032 C CG  . PRO J  160 ? 2.3772 2.3222 2.0078 -0.1748 -0.0523 -0.0826 160 PRO J CG  
19033 C CD  . PRO J  160 ? 2.3554 2.3043 1.9993 -0.1665 -0.0525 -0.0806 160 PRO J CD  
19034 N N   . LYS J  161 ? 1.9005 1.8578 1.5511 -0.1593 -0.0573 -0.0693 161 LYS J N   
19035 C CA  . LYS J  161 ? 1.4942 1.4526 1.1476 -0.1559 -0.0550 -0.0686 161 LYS J CA  
19036 C C   . LYS J  161 ? 1.4364 1.3986 1.0916 -0.1556 -0.0608 -0.0625 161 LYS J C   
19037 O O   . LYS J  161 ? 1.3046 1.2704 0.9684 -0.1501 -0.0615 -0.0598 161 LYS J O   
19038 C CB  . LYS J  161 ? 1.2894 1.2498 0.9534 -0.1485 -0.0515 -0.0700 161 LYS J CB  
19039 C CG  . LYS J  161 ? 1.4348 1.3915 1.0976 -0.1483 -0.0454 -0.0759 161 LYS J CG  
19040 C CD  . LYS J  161 ? 1.3025 1.2544 0.9560 -0.1524 -0.0402 -0.0802 161 LYS J CD  
19041 C CE  . LYS J  161 ? 1.5106 1.4578 1.1617 -0.1535 -0.0342 -0.0859 161 LYS J CE  
19042 N NZ  . LYS J  161 ? 1.6436 1.5931 1.3065 -0.1464 -0.0309 -0.0866 161 LYS J NZ  
19043 N N   . TYR J  162 ? 1.5607 1.5221 1.2074 -0.1617 -0.0647 -0.0604 162 TYR J N   
19044 C CA  . TYR J  162 ? 1.6176 1.5826 1.2655 -0.1620 -0.0708 -0.0543 162 TYR J CA  
19045 C C   . TYR J  162 ? 1.6464 1.6123 1.2954 -0.1598 -0.0698 -0.0525 162 TYR J C   
19046 O O   . TYR J  162 ? 1.5066 1.4692 1.1489 -0.1621 -0.0658 -0.0555 162 TYR J O   
19047 C CB  . TYR J  162 ? 1.8489 1.8127 1.4861 -0.1696 -0.0749 -0.0528 162 TYR J CB  
19048 C CG  . TYR J  162 ? 2.2813 2.2495 1.9218 -0.1697 -0.0823 -0.0465 162 TYR J CG  
19049 C CD1 . TYR J  162 ? 2.3408 2.3117 1.9887 -0.1672 -0.0852 -0.0449 162 TYR J CD1 
19050 C CD2 . TYR J  162 ? 2.1416 2.1112 1.7775 -0.1724 -0.0863 -0.0419 162 TYR J CD2 
19051 C CE1 . TYR J  162 ? 2.2141 2.1892 1.8654 -0.1672 -0.0919 -0.0390 162 TYR J CE1 
19052 C CE2 . TYR J  162 ? 2.2806 2.2544 1.9198 -0.1724 -0.0930 -0.0359 162 TYR J CE2 
19053 C CZ  . TYR J  162 ? 2.2628 2.2394 1.9098 -0.1698 -0.0958 -0.0345 162 TYR J CZ  
19054 O OH  . TYR J  162 ? 1.7101 1.6910 1.3608 -0.1698 -0.1024 -0.0284 162 TYR J OH  
19055 N N   . ASP K  7   ? 1.6283 1.7057 1.4625 -0.1351 -0.2045 0.1150  7   ASP K N   
19056 C CA  . ASP K  7   ? 1.4834 1.5567 1.3037 -0.1387 -0.2021 0.1065  7   ASP K CA  
19057 C C   . ASP K  7   ? 1.3177 1.3913 1.1366 -0.1405 -0.2026 0.1011  7   ASP K C   
19058 O O   . ASP K  7   ? 1.3903 1.4620 1.1975 -0.1450 -0.2022 0.0953  7   ASP K O   
19059 C CB  . ASP K  7   ? 1.4590 1.5338 1.2667 -0.1452 -0.2056 0.1086  7   ASP K CB  
19060 C CG  . ASP K  7   ? 1.2984 1.3801 1.1061 -0.1502 -0.2132 0.1151  7   ASP K CG  
19061 O OD1 . ASP K  7   ? 1.2898 1.3727 1.0852 -0.1568 -0.2162 0.1145  7   ASP K OD1 
19062 O OD2 . ASP K  7   ? 1.4452 1.5313 1.2650 -0.1479 -0.2162 0.1209  7   ASP K OD2 
19063 N N   . THR K  8   ? 1.3735 1.4491 1.2046 -0.1367 -0.2030 0.1029  8   THR K N   
19064 C CA  . THR K  8   ? 1.3255 1.4023 1.1571 -0.1385 -0.2044 0.0994  8   THR K CA  
19065 C C   . THR K  8   ? 1.2315 1.3055 1.0732 -0.1319 -0.1996 0.0960  8   THR K C   
19066 O O   . THR K  8   ? 1.0611 1.1371 0.9155 -0.1275 -0.1999 0.1011  8   THR K O   
19067 C CB  . THR K  8   ? 1.4934 1.5774 1.3312 -0.1412 -0.2114 0.1071  8   THR K CB  
19068 O OG1 . THR K  8   ? 1.7977 1.8848 1.6417 -0.1396 -0.2137 0.1157  8   THR K OG1 
19069 C CG2 . THR K  8   ? 1.4743 1.5610 1.3001 -0.1492 -0.2161 0.1062  8   THR K CG2 
19070 N N   . LEU K  9   ? 1.3366 1.4059 1.1730 -0.1312 -0.1949 0.0875  9   LEU K N   
19071 C CA  . LEU K  9   ? 1.0450 1.1117 0.8902 -0.1254 -0.1905 0.0840  9   LEU K CA  
19072 C C   . LEU K  9   ? 1.0066 1.0731 0.8496 -0.1275 -0.1907 0.0788  9   LEU K C   
19073 O O   . LEU K  9   ? 1.4047 1.4693 1.2365 -0.1319 -0.1901 0.0735  9   LEU K O   
19074 C CB  . LEU K  9   ? 1.0940 1.1553 0.9373 -0.1213 -0.1839 0.0789  9   LEU K CB  
19075 C CG  . LEU K  9   ? 0.8037 0.8633 0.6583 -0.1146 -0.1799 0.0774  9   LEU K CG  
19076 C CD1 . LEU K  9   ? 0.9008 0.9647 0.7684 -0.1124 -0.1832 0.0850  9   LEU K CD1 
19077 C CD2 . LEU K  9   ? 0.7939 0.8493 0.6488 -0.1103 -0.1742 0.0748  9   LEU K CD2 
19078 N N   . CYS K  10  ? 1.3845 1.4528 1.2384 -0.1244 -0.1911 0.0803  10  CYS K N   
19079 C CA  . CYS K  10  ? 1.4007 1.4689 1.2536 -0.1262 -0.1912 0.0757  10  CYS K CA  
19080 C C   . CYS K  10  ? 1.3545 1.4213 1.2187 -0.1201 -0.1877 0.0742  10  CYS K C   
19081 O O   . CYS K  10  ? 1.2536 1.3218 1.1288 -0.1155 -0.1875 0.0790  10  CYS K O   
19082 C CB  . CYS K  10  ? 1.3881 1.4619 1.2403 -0.1319 -0.1980 0.0800  10  CYS K CB  
19083 S SG  . CYS K  10  ? 1.5779 1.6538 1.4162 -0.1397 -0.2025 0.0820  10  CYS K SG  
19084 N N   . ILE K  11  ? 1.4192 1.4832 1.2806 -0.1201 -0.1848 0.0675  11  ILE K N   
19085 C CA  . ILE K  11  ? 1.3481 1.4106 1.2188 -0.1147 -0.1813 0.0652  11  ILE K CA  
19086 C C   . ILE K  11  ? 1.2497 1.3141 1.1220 -0.1174 -0.1837 0.0641  11  ILE K C   
19087 O O   . ILE K  11  ? 1.3072 1.3697 1.1710 -0.1210 -0.1828 0.0586  11  ILE K O   
19088 C CB  . ILE K  11  ? 1.2916 1.3484 1.1579 -0.1115 -0.1746 0.0579  11  ILE K CB  
19089 C CG1 . ILE K  11  ? 1.3598 1.4141 1.2120 -0.1164 -0.1738 0.0526  11  ILE K CG1 
19090 C CG2 . ILE K  11  ? 1.2645 1.3196 1.1346 -0.1066 -0.1714 0.0594  11  ILE K CG2 
19091 C CD1 . ILE K  11  ? 1.2386 1.2901 1.0843 -0.1157 -0.1709 0.0512  11  ILE K CD1 
19092 N N   . GLY K  12  ? 2.1378 2.2061 2.0214 -0.1158 -0.1866 0.0694  12  GLY K N   
19093 C CA  . GLY K  12  ? 2.2125 2.2831 2.0994 -0.1179 -0.1890 0.0690  12  GLY K CA  
19094 C C   . GLY K  12  ? 2.1622 2.2319 2.0614 -0.1117 -0.1860 0.0692  12  GLY K C   
19095 O O   . GLY K  12  ? 1.9570 2.0272 1.8647 -0.1071 -0.1850 0.0733  12  GLY K O   
19096 N N   . TYR K  13  ? 1.2691 1.3374 1.1690 -0.1116 -0.1841 0.0647  13  TYR K N   
19097 C CA  . TYR K  13  ? 1.1408 1.2077 1.0513 -0.1058 -0.1807 0.0641  13  TYR K CA  
19098 C C   . TYR K  13  ? 1.0278 1.0997 0.9504 -0.1051 -0.1848 0.0710  13  TYR K C   
19099 O O   . TYR K  13  ? 1.0467 1.1231 0.9704 -0.1081 -0.1900 0.0770  13  TYR K O   
19100 C CB  . TYR K  13  ? 0.7261 0.7898 0.6334 -0.1062 -0.1775 0.0572  13  TYR K CB  
19101 C CG  . TYR K  13  ? 0.7246 0.7897 0.6235 -0.1131 -0.1808 0.0551  13  TYR K CG  
19102 C CD1 . TYR K  13  ? 0.7802 0.8490 0.6841 -0.1159 -0.1846 0.0573  13  TYR K CD1 
19103 C CD2 . TYR K  13  ? 0.6498 0.7125 0.5357 -0.1172 -0.1800 0.0509  13  TYR K CD2 
19104 C CE1 . TYR K  13  ? 0.7508 0.8208 0.6467 -0.1226 -0.1875 0.0551  13  TYR K CE1 
19105 C CE2 . TYR K  13  ? 0.8078 0.8715 0.6856 -0.1239 -0.1827 0.0488  13  TYR K CE2 
19106 C CZ  . TYR K  13  ? 0.8800 0.9474 0.7627 -0.1267 -0.1865 0.0508  13  TYR K CZ  
19107 O OH  . TYR K  13  ? 0.9329 1.0014 0.8074 -0.1337 -0.1891 0.0484  13  TYR K OH  
19108 N N   . HIS K  14  ? 1.1167 1.1878 1.0487 -0.1010 -0.1825 0.0704  14  HIS K N   
19109 C CA  . HIS K  14  ? 0.7380 0.8134 0.6830 -0.0992 -0.1854 0.0769  14  HIS K CA  
19110 C C   . HIS K  14  ? 1.1019 1.1811 1.0488 -0.1035 -0.1896 0.0777  14  HIS K C   
19111 O O   . HIS K  14  ? 1.1894 1.2669 1.1287 -0.1068 -0.1890 0.0723  14  HIS K O   
19112 C CB  . HIS K  14  ? 1.0531 1.1257 1.0080 -0.0923 -0.1803 0.0761  14  HIS K CB  
19113 C CG  . HIS K  14  ? 1.2290 1.3053 1.1978 -0.0899 -0.1825 0.0828  14  HIS K CG  
19114 N ND1 . HIS K  14  ? 1.3828 1.4606 1.3583 -0.0873 -0.1831 0.0887  14  HIS K ND1 
19115 C CD2 . HIS K  14  ? 1.2573 1.3360 1.2348 -0.0896 -0.1840 0.0845  14  HIS K CD2 
19116 C CE1 . HIS K  14  ? 1.4068 1.4877 1.3948 -0.0855 -0.1847 0.0939  14  HIS K CE1 
19117 N NE2 . HIS K  14  ? 1.2848 1.3664 1.2742 -0.0869 -0.1854 0.0914  14  HIS K NE2 
19118 N N   . ALA K  15  ? 0.9417 1.0260 0.8990 -0.1034 -0.1937 0.0847  15  ALA K N   
19119 C CA  . ALA K  15  ? 0.9835 1.0721 0.9448 -0.1070 -0.1979 0.0864  15  ALA K CA  
19120 C C   . ALA K  15  ? 0.9852 1.0778 0.9618 -0.1037 -0.1998 0.0935  15  ALA K C   
19121 O O   . ALA K  15  ? 0.9645 1.0574 0.9468 -0.1002 -0.1993 0.0982  15  ALA K O   
19122 C CB  . ALA K  15  ? 0.9617 1.0544 0.9142 -0.1145 -0.2038 0.0880  15  ALA K CB  
19123 N N   . ASN K  16  ? 1.1082 1.2035 1.0915 -0.1048 -0.2017 0.0943  16  ASN K N   
19124 C CA  . ASN K  16  ? 1.2073 1.3063 1.2058 -0.1016 -0.2031 0.1008  16  ASN K CA  
19125 C C   . ASN K  16  ? 1.2594 1.3629 1.2638 -0.1047 -0.2069 0.1023  16  ASN K C   
19126 O O   . ASN K  16  ? 1.1621 1.2666 1.1584 -0.1102 -0.2092 0.0989  16  ASN K O   
19127 C CB  . ASN K  16  ? 1.2234 1.3175 1.2295 -0.0942 -0.1967 0.0990  16  ASN K CB  
19128 C CG  . ASN K  16  ? 1.3075 1.3966 1.3099 -0.0928 -0.1918 0.0912  16  ASN K CG  
19129 O OD1 . ASN K  16  ? 1.2382 1.3277 1.2345 -0.0972 -0.1933 0.0875  16  ASN K OD1 
19130 N ND2 . ASN K  16  ? 1.1556 1.2398 1.1617 -0.0869 -0.1859 0.0886  16  ASN K ND2 
19131 N N   . ASN K  17  ? 1.3003 1.4064 1.3189 -0.1011 -0.2072 0.1074  17  ASN K N   
19132 C CA  . ASN K  17  ? 1.4244 1.5352 1.4505 -0.1036 -0.2108 0.1095  17  ASN K CA  
19133 C C   . ASN K  17  ? 1.5461 1.6527 1.5739 -0.1016 -0.2062 0.1033  17  ASN K C   
19134 O O   . ASN K  17  ? 1.6365 1.7460 1.6734 -0.1017 -0.2076 0.1051  17  ASN K O   
19135 C CB  . ASN K  17  ? 1.7087 1.8247 1.7502 -0.1010 -0.2134 0.1184  17  ASN K CB  
19136 C CG  . ASN K  17  ? 1.6791 1.7907 1.7305 -0.0933 -0.2074 0.1188  17  ASN K CG  
19137 O OD1 . ASN K  17  ? 1.7093 1.8148 1.7580 -0.0900 -0.2016 0.1124  17  ASN K OD1 
19138 N ND2 . ASN K  17  ? 1.8157 1.9307 1.8787 -0.0906 -0.2088 0.1265  17  ASN K ND2 
19139 N N   . SER K  18  ? 1.4040 1.5039 1.4230 -0.0996 -0.2007 0.0961  18  SER K N   
19140 C CA  . SER K  18  ? 1.2576 1.3530 1.2780 -0.0970 -0.1957 0.0902  18  SER K CA  
19141 C C   . SER K  18  ? 1.1554 1.2521 1.1711 -0.1026 -0.1980 0.0866  18  SER K C   
19142 O O   . SER K  18  ? 1.0130 1.1107 1.0178 -0.1083 -0.2008 0.0844  18  SER K O   
19143 C CB  . SER K  18  ? 1.2357 1.3239 1.2477 -0.0936 -0.1895 0.0838  18  SER K CB  
19144 O OG  . SER K  18  ? 1.1704 1.2543 1.1848 -0.0903 -0.1844 0.0788  18  SER K OG  
19145 N N   . THR K  19  ? 1.2382 1.3349 1.2623 -0.1010 -0.1966 0.0859  19  THR K N   
19146 C CA  . THR K  19  ? 1.2961 1.3935 1.3166 -0.1059 -0.1978 0.0819  19  THR K CA  
19147 C C   . THR K  19  ? 1.1942 1.2847 1.2117 -0.1028 -0.1911 0.0744  19  THR K C   
19148 O O   . THR K  19  ? 1.1700 1.2597 1.1849 -0.1059 -0.1907 0.0704  19  THR K O   
19149 C CB  . THR K  19  ? 1.2820 1.3855 1.3142 -0.1076 -0.2022 0.0870  19  THR K CB  
19150 O OG1 . THR K  19  ? 1.4065 1.5088 1.4517 -0.1011 -0.1988 0.0893  19  THR K OG1 
19151 C CG2 . THR K  19  ? 1.3538 1.4649 1.3882 -0.1115 -0.2093 0.0944  19  THR K CG2 
19152 N N   . ASP K  20  ? 1.1395 1.2250 1.1572 -0.0968 -0.1858 0.0727  20  ASP K N   
19153 C CA  . ASP K  20  ? 1.0124 1.0915 1.0270 -0.0934 -0.1792 0.0660  20  ASP K CA  
19154 C C   . ASP K  20  ? 0.9572 1.0335 0.9586 -0.0982 -0.1785 0.0595  20  ASP K C   
19155 O O   . ASP K  20  ? 1.0897 1.1663 1.0813 -0.1016 -0.1804 0.0588  20  ASP K O   
19156 C CB  . ASP K  20  ? 1.0262 1.1009 1.0408 -0.0871 -0.1743 0.0652  20  ASP K CB  
19157 C CG  . ASP K  20  ? 1.1391 1.2152 1.1670 -0.0819 -0.1735 0.0705  20  ASP K CG  
19158 O OD1 . ASP K  20  ? 0.9653 1.0387 0.9940 -0.0772 -0.1701 0.0708  20  ASP K OD1 
19159 O OD2 . ASP K  20  ? 1.1384 1.2182 1.1760 -0.0826 -0.1762 0.0743  20  ASP K OD2 
19160 N N   . THR K  21  ? 0.9439 1.0175 0.9452 -0.0985 -0.1755 0.0549  21  THR K N   
19161 C CA  . THR K  21  ? 0.9506 1.0208 0.9401 -0.1025 -0.1737 0.0483  21  THR K CA  
19162 C C   . THR K  21  ? 0.8409 0.9046 0.8292 -0.0978 -0.1665 0.0426  21  THR K C   
19163 O O   . THR K  21  ? 0.9308 0.9934 0.9280 -0.0937 -0.1638 0.0429  21  THR K O   
19164 C CB  . THR K  21  ? 0.9476 1.0209 0.9364 -0.1091 -0.1774 0.0475  21  THR K CB  
19165 O OG1 . THR K  21  ? 1.1411 1.2160 1.1418 -0.1070 -0.1772 0.0495  21  THR K OG1 
19166 C CG2 . THR K  21  ? 0.9451 1.0247 0.9315 -0.1150 -0.1846 0.0522  21  THR K CG2 
19167 N N   . VAL K  22  ? 0.7457 0.8052 0.7230 -0.0984 -0.1633 0.0376  22  VAL K N   
19168 C CA  . VAL K  22  ? 0.7632 0.8168 0.7384 -0.0944 -0.1566 0.0321  22  VAL K CA  
19169 C C   . VAL K  22  ? 0.8219 0.8726 0.7869 -0.0993 -0.1551 0.0261  22  VAL K C   
19170 O O   . VAL K  22  ? 0.8672 0.9201 0.8255 -0.1056 -0.1590 0.0259  22  VAL K O   
19171 C CB  . VAL K  22  ? 0.6872 0.7379 0.6595 -0.0893 -0.1530 0.0314  22  VAL K CB  
19172 C CG1 . VAL K  22  ? 0.6511 0.7048 0.6322 -0.0854 -0.1549 0.0375  22  VAL K CG1 
19173 C CG2 . VAL K  22  ? 0.6320 0.6816 0.5920 -0.0930 -0.1538 0.0290  22  VAL K CG2 
19174 N N   . ASP K  23  ? 0.6697 0.7153 0.6335 -0.0964 -0.1491 0.0212  23  ASP K N   
19175 C CA  . ASP K  23  ? 0.6979 0.7398 0.6522 -0.1004 -0.1465 0.0151  23  ASP K CA  
19176 C C   . ASP K  23  ? 0.6993 0.7367 0.6462 -0.0973 -0.1416 0.0113  23  ASP K C   
19177 O O   . ASP K  23  ? 0.6681 0.7041 0.6188 -0.0910 -0.1386 0.0123  23  ASP K O   
19178 C CB  . ASP K  23  ? 0.8211 0.8608 0.7799 -0.1003 -0.1434 0.0122  23  ASP K CB  
19179 C CG  . ASP K  23  ? 1.0369 1.0811 1.0009 -0.1051 -0.1484 0.0148  23  ASP K CG  
19180 O OD1 . ASP K  23  ? 1.1891 1.2384 1.1536 -0.1083 -0.1544 0.0192  23  ASP K OD1 
19181 O OD2 . ASP K  23  ? 1.1297 1.1723 1.0974 -0.1056 -0.1463 0.0126  23  ASP K OD2 
19182 N N   . THR K  24  ? 0.6962 0.7312 0.6324 -0.1018 -0.1407 0.0070  24  THR K N   
19183 C CA  . THR K  24  ? 0.7191 0.7496 0.6481 -0.0993 -0.1356 0.0029  24  THR K CA  
19184 C C   . THR K  24  ? 0.7451 0.7710 0.6694 -0.1015 -0.1310 -0.0030 24  THR K C   
19185 O O   . THR K  24  ? 0.6525 0.6786 0.5790 -0.1049 -0.1318 -0.0040 24  THR K O   
19186 C CB  . THR K  24  ? 0.8448 0.8763 0.7646 -0.1025 -0.1381 0.0032  24  THR K CB  
19187 O OG1 . THR K  24  ? 1.0472 1.0789 0.9591 -0.1102 -0.1405 0.0009  24  THR K OG1 
19188 C CG2 . THR K  24  ? 0.6794 0.7156 0.6038 -0.1014 -0.1431 0.0094  24  THR K CG2 
19189 N N   . VAL K  25  ? 0.8129 0.8345 0.7308 -0.0996 -0.1260 -0.0070 25  VAL K N   
19190 C CA  . VAL K  25  ? 0.8038 0.8206 0.7169 -0.1015 -0.1211 -0.0128 25  VAL K CA  
19191 C C   . VAL K  25  ? 0.8131 0.8302 0.7176 -0.1099 -0.1239 -0.0151 25  VAL K C   
19192 O O   . VAL K  25  ? 0.7191 0.7338 0.6218 -0.1135 -0.1219 -0.0187 25  VAL K O   
19193 C CB  . VAL K  25  ? 0.7804 0.7930 0.6888 -0.0974 -0.1153 -0.0161 25  VAL K CB  
19194 C CG1 . VAL K  25  ? 0.7043 0.7119 0.6128 -0.0964 -0.1090 -0.0208 25  VAL K CG1 
19195 C CG2 . VAL K  25  ? 0.8999 0.9138 0.8142 -0.0902 -0.1145 -0.0128 25  VAL K CG2 
19196 N N   . LEU K  26  ? 0.8573 0.8775 0.7565 -0.1132 -0.1285 -0.0128 26  LEU K N   
19197 C CA  . LEU K  26  ? 0.8476 0.8679 0.7369 -0.1212 -0.1310 -0.0152 26  LEU K CA  
19198 C C   . LEU K  26  ? 0.8656 0.8915 0.7569 -0.1268 -0.1381 -0.0114 26  LEU K C   
19199 O O   . LEU K  26  ? 0.8335 0.8599 0.7173 -0.1342 -0.1404 -0.0135 26  LEU K O   
19200 C CB  . LEU K  26  ? 0.7722 0.7919 0.6528 -0.1219 -0.1311 -0.0156 26  LEU K CB  
19201 C CG  . LEU K  26  ? 0.8167 0.8321 0.6955 -0.1162 -0.1249 -0.0183 26  LEU K CG  
19202 C CD1 . LEU K  26  ? 0.6011 0.6164 0.4710 -0.1179 -0.1258 -0.0186 26  LEU K CD1 
19203 C CD2 . LEU K  26  ? 0.9291 0.9388 0.8057 -0.1160 -0.1184 -0.0242 26  LEU K CD2 
19204 N N   . GLU K  27  ? 0.8990 0.9291 0.8002 -0.1235 -0.1416 -0.0059 27  GLU K N   
19205 C CA  . GLU K  27  ? 0.8235 0.8597 0.7276 -0.1283 -0.1487 -0.0015 27  GLU K CA  
19206 C C   . GLU K  27  ? 0.8385 0.8779 0.7557 -0.1245 -0.1504 0.0029  27  GLU K C   
19207 O O   . GLU K  27  ? 0.8557 0.8940 0.7799 -0.1173 -0.1478 0.0046  27  GLU K O   
19208 C CB  . GLU K  27  ? 0.9693 1.0092 0.8691 -0.1300 -0.1536 0.0024  27  GLU K CB  
19209 C CG  . GLU K  27  ? 1.2395 1.2851 1.1372 -0.1373 -0.1608 0.0056  27  GLU K CG  
19210 C CD  . GLU K  27  ? 1.3921 1.4402 1.2827 -0.1398 -0.1646 0.0083  27  GLU K CD  
19211 O OE1 . GLU K  27  ? 1.3159 1.3698 1.2069 -0.1443 -0.1711 0.0127  27  GLU K OE1 
19212 O OE2 . GLU K  27  ? 1.4288 1.4732 1.3135 -0.1373 -0.1611 0.0061  27  GLU K OE2 
19213 N N   . LYS K  28  ? 0.9397 0.9830 0.8601 -0.1294 -0.1548 0.0046  28  LYS K N   
19214 C CA  . LYS K  28  ? 1.0138 1.0606 0.9469 -0.1265 -0.1569 0.0089  28  LYS K CA  
19215 C C   . LYS K  28  ? 0.9703 1.0241 0.9081 -0.1278 -0.1641 0.0160  28  LYS K C   
19216 O O   . LYS K  28  ? 0.9459 1.0026 0.8765 -0.1329 -0.1684 0.0173  28  LYS K O   
19217 C CB  . LYS K  28  ? 1.0241 1.0705 0.9594 -0.1305 -0.1564 0.0061  28  LYS K CB  
19218 C CG  . LYS K  28  ? 0.9497 0.9901 0.8877 -0.1261 -0.1491 0.0016  28  LYS K CG  
19219 C CD  . LYS K  28  ? 1.2234 1.2636 1.1638 -0.1304 -0.1488 -0.0010 28  LYS K CD  
19220 C CE  . LYS K  28  ? 1.2965 1.3319 1.2434 -0.1248 -0.1423 -0.0036 28  LYS K CE  
19221 N NZ  . LYS K  28  ? 1.2660 1.2949 1.2066 -0.1211 -0.1355 -0.0082 28  LYS K NZ  
19222 N N   . ASN K  29  ? 1.0691 1.1256 1.0190 -0.1232 -0.1651 0.0207  29  ASN K N   
19223 C CA  . ASN K  29  ? 1.0442 1.1074 1.0007 -0.1236 -0.1715 0.0279  29  ASN K CA  
19224 C C   . ASN K  29  ? 0.9574 1.0225 0.9069 -0.1252 -0.1747 0.0304  29  ASN K C   
19225 O O   . ASN K  29  ? 1.0051 1.0750 0.9510 -0.1312 -0.1805 0.0330  29  ASN K O   
19226 C CB  . ASN K  29  ? 0.9745 1.0430 0.9349 -0.1296 -0.1767 0.0301  29  ASN K CB  
19227 C CG  . ASN K  29  ? 1.3450 1.4134 1.3170 -0.1264 -0.1749 0.0306  29  ASN K CG  
19228 O OD1 . ASN K  29  ? 1.3502 1.4208 1.3330 -0.1214 -0.1755 0.0354  29  ASN K OD1 
19229 N ND2 . ASN K  29  ? 1.3959 1.4615 1.3656 -0.1294 -0.1722 0.0255  29  ASN K ND2 
19230 N N   . VAL K  30  ? 0.8816 0.9432 0.8293 -0.1198 -0.1709 0.0297  30  VAL K N   
19231 C CA  . VAL K  30  ? 0.7644 0.8273 0.7063 -0.1203 -0.1733 0.0322  30  VAL K CA  
19232 C C   . VAL K  30  ? 0.7967 0.8632 0.7488 -0.1155 -0.1756 0.0391  30  VAL K C   
19233 O O   . VAL K  30  ? 0.7962 0.8604 0.7554 -0.1089 -0.1717 0.0395  30  VAL K O   
19234 C CB  . VAL K  30  ? 0.7539 0.8109 0.6872 -0.1176 -0.1677 0.0272  30  VAL K CB  
19235 C CG1 . VAL K  30  ? 0.6935 0.7518 0.6221 -0.1174 -0.1698 0.0301  30  VAL K CG1 
19236 C CG2 . VAL K  30  ? 0.8221 0.8754 0.7449 -0.1226 -0.1652 0.0204  30  VAL K CG2 
19237 N N   . THR K  31  ? 0.8598 0.9320 0.8125 -0.1190 -0.1818 0.0446  31  THR K N   
19238 C CA  . THR K  31  ? 0.8950 0.9709 0.8575 -0.1149 -0.1842 0.0516  31  THR K CA  
19239 C C   . THR K  31  ? 0.7489 0.8217 0.7085 -0.1103 -0.1812 0.0517  31  THR K C   
19240 O O   . THR K  31  ? 0.9652 1.0371 0.9145 -0.1131 -0.1817 0.0501  31  THR K O   
19241 C CB  . THR K  31  ? 0.9159 0.9990 0.8799 -0.1202 -0.1919 0.0579  31  THR K CB  
19242 O OG1 . THR K  31  ? 0.8230 0.9094 0.7900 -0.1247 -0.1949 0.0579  31  THR K OG1 
19243 C CG2 . THR K  31  ? 0.9133 1.0001 0.8887 -0.1156 -0.1939 0.0653  31  THR K CG2 
19244 N N   . VAL K  32  ? 0.7120 0.7834 0.6806 -0.1035 -0.1780 0.0534  32  VAL K N   
19245 C CA  . VAL K  32  ? 0.8095 0.8780 0.7763 -0.0988 -0.1748 0.0534  32  VAL K CA  
19246 C C   . VAL K  32  ? 0.7877 0.8597 0.7644 -0.0956 -0.1771 0.0605  32  VAL K C   
19247 O O   . VAL K  32  ? 0.9476 1.0232 0.9347 -0.0951 -0.1796 0.0650  32  VAL K O   
19248 C CB  . VAL K  32  ? 0.8201 0.8828 0.7874 -0.0932 -0.1677 0.0483  32  VAL K CB  
19249 C CG1 . VAL K  32  ? 0.7102 0.7688 0.6666 -0.0960 -0.1647 0.0412  32  VAL K CG1 
19250 C CG2 . VAL K  32  ? 0.7594 0.8223 0.7384 -0.0895 -0.1662 0.0496  32  VAL K CG2 
19251 N N   . THR K  33  ? 0.7871 0.8579 0.7607 -0.0934 -0.1760 0.0616  33  THR K N   
19252 C CA  . THR K  33  ? 0.8852 0.9587 0.8675 -0.0903 -0.1776 0.0682  33  THR K CA  
19253 C C   . THR K  33  ? 0.8341 0.9058 0.8276 -0.0838 -0.1735 0.0690  33  THR K C   
19254 O O   . THR K  33  ? 1.0017 1.0766 1.0062 -0.0820 -0.1754 0.0748  33  THR K O   
19255 C CB  . THR K  33  ? 0.9456 1.0177 0.9211 -0.0897 -0.1768 0.0685  33  THR K CB  
19256 O OG1 . THR K  33  ? 0.8301 0.8965 0.8008 -0.0859 -0.1707 0.0627  33  THR K OG1 
19257 C CG2 . THR K  33  ? 1.0056 1.0796 0.9701 -0.0962 -0.1810 0.0683  33  THR K CG2 
19258 N N   . HIS K  34  ? 0.9381 1.0047 0.9289 -0.0804 -0.1678 0.0633  34  HIS K N   
19259 C CA  . HIS K  34  ? 0.9640 1.0284 0.9641 -0.0743 -0.1634 0.0634  34  HIS K CA  
19260 C C   . HIS K  34  ? 0.8856 0.9461 0.8836 -0.0727 -0.1589 0.0574  34  HIS K C   
19261 O O   . HIS K  34  ? 0.7925 0.8506 0.7805 -0.0751 -0.1577 0.0522  34  HIS K O   
19262 C CB  . HIS K  34  ? 0.8606 0.9227 0.8607 -0.0699 -0.1601 0.0640  34  HIS K CB  
19263 C CG  . HIS K  34  ? 0.9386 1.0040 0.9409 -0.0710 -0.1639 0.0699  34  HIS K CG  
19264 N ND1 . HIS K  34  ? 0.9633 1.0303 0.9566 -0.0755 -0.1673 0.0704  34  HIS K ND1 
19265 C CD2 . HIS K  34  ? 1.0152 1.0826 1.0278 -0.0683 -0.1645 0.0758  34  HIS K CD2 
19266 C CE1 . HIS K  34  ? 1.1688 1.2386 1.1667 -0.0753 -0.1700 0.0765  34  HIS K CE1 
19267 N NE2 . HIS K  34  ? 1.2654 1.3356 1.2752 -0.0709 -0.1683 0.0798  34  HIS K NE2 
19268 N N   . SER K  35  ? 0.8480 0.9076 0.8555 -0.0687 -0.1563 0.0580  35  SER K N   
19269 C CA  . SER K  35  ? 0.7701 0.8261 0.7768 -0.0668 -0.1519 0.0528  35  SER K CA  
19270 C C   . SER K  35  ? 0.7071 0.7620 0.7247 -0.0613 -0.1484 0.0542  35  SER K C   
19271 O O   . SER K  35  ? 0.8118 0.8690 0.8385 -0.0595 -0.1499 0.0594  35  SER K O   
19272 C CB  . SER K  35  ? 0.8597 0.9169 0.8643 -0.0716 -0.1544 0.0511  35  SER K CB  
19273 O OG  . SER K  35  ? 0.8808 0.9425 0.8948 -0.0733 -0.1586 0.0562  35  SER K OG  
19274 N N   . VAL K  36  ? 0.7460 0.7971 0.7625 -0.0586 -0.1437 0.0497  36  VAL K N   
19275 C CA  . VAL K  36  ? 0.8197 0.8694 0.8456 -0.0536 -0.1400 0.0504  36  VAL K CA  
19276 C C   . VAL K  36  ? 0.8044 0.8524 0.8312 -0.0539 -0.1381 0.0470  36  VAL K C   
19277 O O   . VAL K  36  ? 0.6730 0.7194 0.6916 -0.0567 -0.1377 0.0428  36  VAL K O   
19278 C CB  . VAL K  36  ? 0.7011 0.7472 0.7251 -0.0486 -0.1348 0.0482  36  VAL K CB  
19279 C CG1 . VAL K  36  ? 0.9273 0.9747 0.9502 -0.0483 -0.1362 0.0511  36  VAL K CG1 
19280 C CG2 . VAL K  36  ? 0.6748 0.7175 0.6887 -0.0485 -0.1314 0.0421  36  VAL K CG2 
19281 N N   . ASN K  37  ? 0.8898 0.9378 0.9267 -0.0510 -0.1366 0.0489  37  ASN K N   
19282 C CA  . ASN K  37  ? 0.7668 0.8130 0.8055 -0.0509 -0.1343 0.0460  37  ASN K CA  
19283 C C   . ASN K  37  ? 0.7521 0.7939 0.7903 -0.0456 -0.1280 0.0425  37  ASN K C   
19284 O O   . ASN K  37  ? 0.8028 0.8439 0.8467 -0.0413 -0.1255 0.0444  37  ASN K O   
19285 C CB  . ASN K  37  ? 0.7607 0.8098 0.8107 -0.0514 -0.1367 0.0500  37  ASN K CB  
19286 C CG  . ASN K  37  ? 0.8859 0.9340 0.9364 -0.0533 -0.1359 0.0471  37  ASN K CG  
19287 O OD1 . ASN K  37  ? 1.0773 1.1272 1.1370 -0.0534 -0.1370 0.0496  37  ASN K OD1 
19288 N ND2 . ASN K  37  ? 0.7263 0.7715 0.7672 -0.0548 -0.1339 0.0418  37  ASN K ND2 
19289 N N   . LEU K  38  ? 0.6289 0.6678 0.6601 -0.0461 -0.1252 0.0375  38  LEU K N   
19290 C CA  . LEU K  38  ? 0.5713 0.6063 0.6014 -0.0413 -0.1193 0.0342  38  LEU K CA  
19291 C C   . LEU K  38  ? 0.6147 0.6485 0.6523 -0.0394 -0.1169 0.0341  38  LEU K C   
19292 O O   . LEU K  38  ? 0.5499 0.5809 0.5887 -0.0351 -0.1121 0.0322  38  LEU K O   
19293 C CB  . LEU K  38  ? 0.4247 0.4571 0.4438 -0.0425 -0.1172 0.0291  38  LEU K CB  
19294 C CG  . LEU K  38  ? 0.4737 0.5064 0.4845 -0.0434 -0.1181 0.0284  38  LEU K CG  
19295 C CD1 . LEU K  38  ? 0.7960 0.8265 0.7966 -0.0456 -0.1166 0.0236  38  LEU K CD1 
19296 C CD2 . LEU K  38  ? 0.4812 0.5130 0.4934 -0.0383 -0.1149 0.0290  38  LEU K CD2 
19297 N N   . LEU K  39  ? 0.6493 0.6854 0.6921 -0.0428 -0.1204 0.0361  39  LEU K N   
19298 C CA  . LEU K  39  ? 0.5814 0.6166 0.6316 -0.0415 -0.1185 0.0360  39  LEU K CA  
19299 C C   . LEU K  39  ? 0.6626 0.7000 0.7246 -0.0395 -0.1196 0.0410  39  LEU K C   
19300 O O   . LEU K  39  ? 0.8256 0.8669 0.8918 -0.0422 -0.1244 0.0450  39  LEU K O   
19301 C CB  . LEU K  39  ? 0.5047 0.5409 0.5532 -0.0468 -0.1211 0.0345  39  LEU K CB  
19302 C CG  . LEU K  39  ? 0.5788 0.6145 0.6354 -0.0463 -0.1198 0.0347  39  LEU K CG  
19303 C CD1 . LEU K  39  ? 0.6352 0.6663 0.6917 -0.0415 -0.1133 0.0315  39  LEU K CD1 
19304 C CD2 . LEU K  39  ? 0.5321 0.5690 0.5864 -0.0522 -0.1227 0.0330  39  LEU K CD2 
19305 N N   . GLU K  40  ? 0.6136 0.6486 0.6811 -0.0347 -0.1151 0.0409  40  GLU K N   
19306 C CA  . GLU K  40  ? 0.6367 0.6733 0.7161 -0.0326 -0.1153 0.0452  40  GLU K CA  
19307 C C   . GLU K  40  ? 0.6362 0.6736 0.7219 -0.0347 -0.1164 0.0456  40  GLU K C   
19308 O O   . GLU K  40  ? 0.5919 0.6268 0.6747 -0.0349 -0.1138 0.0420  40  GLU K O   
19309 C CB  . GLU K  40  ? 0.5842 0.6176 0.6665 -0.0268 -0.1097 0.0447  40  GLU K CB  
19310 C CG  . GLU K  40  ? 0.7555 0.7899 0.8497 -0.0243 -0.1093 0.0490  40  GLU K CG  
19311 C CD  . GLU K  40  ? 0.9125 0.9502 1.0104 -0.0252 -0.1128 0.0535  40  GLU K CD  
19312 O OE1 . GLU K  40  ? 0.9275 0.9639 1.0247 -0.0222 -0.1106 0.0541  40  GLU K OE1 
19313 O OE2 . GLU K  40  ? 0.9173 0.9587 1.0187 -0.0289 -0.1178 0.0566  40  GLU K OE2 
19314 N N   . ASP K  41  ? 0.8154 0.8567 0.9101 -0.0363 -0.1202 0.0503  41  ASP K N   
19315 C CA  . ASP K  41  ? 0.8292 0.8721 0.9311 -0.0385 -0.1218 0.0513  41  ASP K CA  
19316 C C   . ASP K  41  ? 0.6841 0.7295 0.7990 -0.0367 -0.1227 0.0567  41  ASP K C   
19317 O O   . ASP K  41  ? 0.9592 1.0084 1.0811 -0.0397 -0.1265 0.0596  41  ASP K O   
19318 C CB  . ASP K  41  ? 0.8436 0.8900 0.9411 -0.0450 -0.1273 0.0511  41  ASP K CB  
19319 C CG  . ASP K  41  ? 1.2055 1.2561 1.3021 -0.0474 -0.1325 0.0551  41  ASP K CG  
19320 O OD1 . ASP K  41  ? 1.2401 1.2909 1.3403 -0.0441 -0.1318 0.0581  41  ASP K OD1 
19321 O OD2 . ASP K  41  ? 1.2071 1.2608 1.2994 -0.0528 -0.1373 0.0552  41  ASP K OD2 
19322 N N   . LYS K  42  ? 0.7441 0.7875 0.8625 -0.0318 -0.1190 0.0579  42  LYS K N   
19323 C CA  . LYS K  42  ? 0.8482 0.8935 0.9788 -0.0297 -0.1193 0.0630  42  LYS K CA  
19324 C C   . LYS K  42  ? 0.7721 0.8133 0.9068 -0.0240 -0.1131 0.0623  42  LYS K C   
19325 O O   . LYS K  42  ? 0.7793 0.8180 0.9090 -0.0212 -0.1101 0.0609  42  LYS K O   
19326 C CB  . LYS K  42  ? 0.9817 1.0303 1.1130 -0.0308 -0.1232 0.0671  42  LYS K CB  
19327 C CG  . LYS K  42  ? 1.3292 1.3828 1.4720 -0.0327 -0.1276 0.0731  42  LYS K CG  
19328 C CD  . LYS K  42  ? 1.5770 1.6347 1.7177 -0.0354 -0.1327 0.0766  42  LYS K CD  
19329 C CE  . LYS K  42  ? 1.4078 1.4664 1.5362 -0.0401 -0.1361 0.0733  42  LYS K CE  
19330 N NZ  . LYS K  42  ? 1.3922 1.4543 1.5174 -0.0427 -0.1407 0.0765  42  LYS K NZ  
19331 N N   . HIS K  43  ? 0.6290 0.6696 0.7728 -0.0227 -0.1111 0.0633  43  HIS K N   
19332 C CA  . HIS K  43  ? 0.6710 0.7079 0.8198 -0.0176 -0.1053 0.0630  43  HIS K CA  
19333 C C   . HIS K  43  ? 0.7509 0.7899 0.9126 -0.0163 -0.1058 0.0684  43  HIS K C   
19334 O O   . HIS K  43  ? 0.8300 0.8734 0.9983 -0.0193 -0.1106 0.0722  43  HIS K O   
19335 C CB  . HIS K  43  ? 0.6754 0.7095 0.8246 -0.0167 -0.1019 0.0598  43  HIS K CB  
19336 C CG  . HIS K  43  ? 0.7687 0.8055 0.9257 -0.0197 -0.1048 0.0617  43  HIS K CG  
19337 N ND1 . HIS K  43  ? 0.8485 0.8856 1.0176 -0.0180 -0.1033 0.0645  43  HIS K ND1 
19338 C CD2 . HIS K  43  ? 0.7319 0.7715 0.8865 -0.0246 -0.1092 0.0610  43  HIS K CD2 
19339 C CE1 . HIS K  43  ? 0.8076 0.8477 0.9815 -0.0216 -0.1067 0.0656  43  HIS K CE1 
19340 N NE2 . HIS K  43  ? 0.7514 0.7931 0.9165 -0.0258 -0.1104 0.0634  43  HIS K NE2 
19341 N N   . ASN K  44  ? 0.6821 0.7181 0.8478 -0.0119 -0.1009 0.0689  44  ASN K N   
19342 C CA  . ASN K  44  ? 0.6219 0.6593 0.8001 -0.0102 -0.1006 0.0739  44  ASN K CA  
19343 C C   . ASN K  44  ? 0.7329 0.7702 0.9217 -0.0096 -0.0992 0.0753  44  ASN K C   
19344 O O   . ASN K  44  ? 0.8700 0.9084 1.0703 -0.0083 -0.0986 0.0795  44  ASN K O   
19345 C CB  . ASN K  44  ? 0.5486 0.5826 0.7267 -0.0061 -0.0958 0.0739  44  ASN K CB  
19346 C CG  . ASN K  44  ? 0.6996 0.7287 0.8741 -0.0026 -0.0895 0.0697  44  ASN K CG  
19347 O OD1 . ASN K  44  ? 0.8827 0.9089 1.0557 0.0005  -0.0852 0.0689  44  ASN K OD1 
19348 N ND2 . ASN K  44  ? 0.7527 0.7808 0.9257 -0.0032 -0.0888 0.0671  44  ASN K ND2 
19349 N N   . GLY K  45  ? 0.6812 0.7171 0.8663 -0.0106 -0.0984 0.0717  45  GLY K N   
19350 C CA  . GLY K  45  ? 0.7615 0.7974 0.9560 -0.0103 -0.0970 0.0726  45  GLY K CA  
19351 C C   . GLY K  45  ? 0.7043 0.7364 0.9056 -0.0055 -0.0909 0.0732  45  GLY K C   
19352 O O   . GLY K  45  ? 0.6769 0.7095 0.8892 -0.0049 -0.0900 0.0756  45  GLY K O   
19353 N N   . LYS K  46  ? 0.7087 0.7372 0.9036 -0.0024 -0.0867 0.0709  46  LYS K N   
19354 C CA  . LYS K  46  ? 0.8092 0.8336 1.0086 0.0020  -0.0805 0.0708  46  LYS K CA  
19355 C C   . LYS K  46  ? 0.7192 0.7393 0.9091 0.0043  -0.0758 0.0658  46  LYS K C   
19356 O O   . LYS K  46  ? 0.7637 0.7833 0.9424 0.0037  -0.0765 0.0627  46  LYS K O   
19357 C CB  . LYS K  46  ? 0.8244 0.8486 1.0260 0.0039  -0.0792 0.0732  46  LYS K CB  
19358 C CG  . LYS K  46  ? 0.8175 0.8458 1.0293 0.0022  -0.0832 0.0787  46  LYS K CG  
19359 C CD  . LYS K  46  ? 1.1596 1.1873 1.3708 0.0038  -0.0820 0.0804  46  LYS K CD  
19360 C CE  . LYS K  46  ? 1.3723 1.4038 1.5949 0.0027  -0.0853 0.0864  46  LYS K CE  
19361 N NZ  . LYS K  46  ? 1.3148 1.3456 1.5362 0.0039  -0.0842 0.0878  46  LYS K NZ  
19362 N N   . LEU K  47  ? 0.6124 0.6294 0.8070 0.0070  -0.0710 0.0651  47  LEU K N   
19363 C CA  . LEU K  47  ? 0.5861 0.5988 0.7727 0.0098  -0.0658 0.0610  47  LEU K CA  
19364 C C   . LEU K  47  ? 0.6399 0.6504 0.8252 0.0129  -0.0620 0.0612  47  LEU K C   
19365 O O   . LEU K  47  ? 0.8137 0.8226 1.0072 0.0151  -0.0585 0.0631  47  LEU K O   
19366 C CB  . LEU K  47  ? 0.6628 0.6730 0.8545 0.0114  -0.0622 0.0602  47  LEU K CB  
19367 C CG  . LEU K  47  ? 0.6529 0.6633 0.8407 0.0092  -0.0637 0.0577  47  LEU K CG  
19368 C CD1 . LEU K  47  ? 0.5773 0.5918 0.7620 0.0048  -0.0701 0.0581  47  LEU K CD1 
19369 C CD2 . LEU K  47  ? 0.5474 0.5569 0.7448 0.0095  -0.0619 0.0587  47  LEU K CD2 
19370 N N   . CYS K  48  ? 0.5776 0.5882 0.7527 0.0128  -0.0626 0.0591  48  CYS K N   
19371 C CA  . CYS K  48  ? 0.7324 0.7416 0.9054 0.0149  -0.0597 0.0591  48  CYS K CA  
19372 C C   . CYS K  48  ? 0.7638 0.7695 0.9287 0.0178  -0.0545 0.0554  48  CYS K C   
19373 O O   . CYS K  48  ? 0.6962 0.7008 0.8559 0.0181  -0.0535 0.0527  48  CYS K O   
19374 C CB  . CYS K  48  ? 0.6171 0.6288 0.7845 0.0128  -0.0639 0.0596  48  CYS K CB  
19375 S SG  . CYS K  48  ? 1.0795 1.0960 1.2555 0.0092  -0.0705 0.0643  48  CYS K SG  
19376 N N   . LYS K  49  ? 0.7613 0.7654 0.9253 0.0198  -0.0511 0.0553  49  LYS K N   
19377 C CA  . LYS K  49  ? 0.6919 0.6932 0.8479 0.0223  -0.0464 0.0521  49  LYS K CA  
19378 C C   . LYS K  49  ? 0.6136 0.6163 0.7576 0.0213  -0.0486 0.0492  49  LYS K C   
19379 O O   . LYS K  49  ? 0.7210 0.7261 0.8628 0.0190  -0.0528 0.0500  49  LYS K O   
19380 C CB  . LYS K  49  ? 0.7719 0.7712 0.9305 0.0242  -0.0422 0.0528  49  LYS K CB  
19381 C CG  . LYS K  49  ? 0.7401 0.7399 0.9111 0.0238  -0.0428 0.0569  49  LYS K CG  
19382 C CD  . LYS K  49  ? 0.9397 0.9373 1.1125 0.0253  -0.0385 0.0573  49  LYS K CD  
19383 C CE  . LYS K  49  ? 1.0655 1.0635 1.2513 0.0250  -0.0388 0.0617  49  LYS K CE  
19384 N NZ  . LYS K  49  ? 1.0887 1.0855 1.2846 0.0260  -0.0369 0.0635  49  LYS K NZ  
19385 N N   . LEU K  50  ? 0.6997 0.7008 0.8360 0.0230  -0.0456 0.0461  50  LEU K N   
19386 C CA  . LEU K  50  ? 0.8037 0.8060 0.9294 0.0221  -0.0476 0.0434  50  LEU K CA  
19387 C C   . LEU K  50  ? 0.9954 0.9982 1.1126 0.0227  -0.0466 0.0416  50  LEU K C   
19388 O O   . LEU K  50  ? 1.1659 1.1706 1.2767 0.0209  -0.0499 0.0406  50  LEU K O   
19389 C CB  . LEU K  50  ? 0.8309 0.8317 0.9528 0.0236  -0.0452 0.0411  50  LEU K CB  
19390 C CG  . LEU K  50  ? 0.8338 0.8357 0.9461 0.0226  -0.0470 0.0385  50  LEU K CG  
19391 C CD1 . LEU K  50  ? 0.7297 0.7343 0.8399 0.0192  -0.0525 0.0389  50  LEU K CD1 
19392 C CD2 . LEU K  50  ? 0.6694 0.6700 0.7822 0.0229  -0.0460 0.0374  50  LEU K CD2 
19393 N N   . ARG K  51  ? 0.9089 0.9098 1.0258 0.0251  -0.0420 0.0410  51  ARG K N   
19394 C CA  . ARG K  51  ? 1.0832 1.0845 1.1935 0.0255  -0.0408 0.0395  51  ARG K CA  
19395 C C   . ARG K  51  ? 1.0992 1.0999 1.2169 0.0252  -0.0401 0.0420  51  ARG K C   
19396 O O   . ARG K  51  ? 1.3753 1.3776 1.4947 0.0232  -0.0436 0.0436  51  ARG K O   
19397 C CB  . ARG K  51  ? 1.2597 1.2595 1.3641 0.0281  -0.0359 0.0372  51  ARG K CB  
19398 C CG  . ARG K  51  ? 1.4181 1.4178 1.5178 0.0291  -0.0355 0.0355  51  ARG K CG  
19399 C CD  . ARG K  51  ? 1.7889 1.7887 1.8800 0.0310  -0.0322 0.0331  51  ARG K CD  
19400 N NE  . ARG K  51  ? 1.9721 1.9743 2.0554 0.0298  -0.0343 0.0315  51  ARG K NE  
19401 C CZ  . ARG K  51  ? 1.8774 1.8801 1.9562 0.0303  -0.0324 0.0304  51  ARG K CZ  
19402 N NH1 . ARG K  51  ? 1.6951 1.6960 1.7762 0.0318  -0.0281 0.0306  51  ARG K NH1 
19403 N NH2 . ARG K  51  ? 1.7190 1.7240 1.7909 0.0290  -0.0345 0.0290  51  ARG K NH2 
19404 N N   . GLY K  52  ? 0.9150 0.9132 1.0369 0.0272  -0.0353 0.0423  52  GLY K N   
19405 C CA  . GLY K  52  ? 1.1590 1.1559 1.2900 0.0273  -0.0337 0.0448  52  GLY K CA  
19406 C C   . GLY K  52  ? 1.1137 1.1081 1.2519 0.0290  -0.0301 0.0458  52  GLY K C   
19407 O O   . GLY K  52  ? 1.1130 1.1057 1.2598 0.0296  -0.0275 0.0478  52  GLY K O   
19408 N N   . VAL K  53  ? 1.0791 1.0733 1.2139 0.0299  -0.0298 0.0443  53  VAL K N   
19409 C CA  . VAL K  53  ? 0.8189 0.8107 0.9592 0.0317  -0.0263 0.0448  53  VAL K CA  
19410 C C   . VAL K  53  ? 0.6926 0.6852 0.8414 0.0305  -0.0295 0.0472  53  VAL K C   
19411 O O   . VAL K  53  ? 0.7109 0.7058 0.8572 0.0286  -0.0340 0.0470  53  VAL K O   
19412 C CB  . VAL K  53  ? 0.6689 0.6599 0.8010 0.0335  -0.0236 0.0421  53  VAL K CB  
19413 C CG1 . VAL K  53  ? 0.7432 0.7313 0.8811 0.0354  -0.0194 0.0427  53  VAL K CG1 
19414 C CG2 . VAL K  53  ? 0.4877 0.4788 0.6105 0.0343  -0.0212 0.0397  53  VAL K CG2 
19415 N N   . ALA K  54  ? 0.6276 0.6184 0.7863 0.0314  -0.0269 0.0492  54  ALA K N   
19416 C CA  . ALA K  54  ? 0.5426 0.5342 0.7103 0.0303  -0.0296 0.0516  54  ALA K CA  
19417 C C   . ALA K  54  ? 0.6709 0.6617 0.8367 0.0310  -0.0288 0.0501  54  ALA K C   
19418 O O   . ALA K  54  ? 0.7136 0.7022 0.8739 0.0331  -0.0248 0.0480  54  ALA K O   
19419 C CB  . ALA K  54  ? 0.7053 0.6954 0.8852 0.0310  -0.0271 0.0546  54  ALA K CB  
19420 N N   . PRO K  55  ? 0.5603 0.5529 0.7306 0.0291  -0.0327 0.0513  55  PRO K N   
19421 C CA  . PRO K  55  ? 0.5443 0.5358 0.7143 0.0295  -0.0319 0.0501  55  PRO K CA  
19422 C C   . PRO K  55  ? 0.4765 0.4651 0.6552 0.0314  -0.0274 0.0514  55  PRO K C   
19423 O O   . PRO K  55  ? 0.6242 0.6125 0.8115 0.0317  -0.0263 0.0539  55  PRO K O   
19424 C CB  . PRO K  55  ? 0.4979 0.4924 0.6712 0.0262  -0.0377 0.0513  55  PRO K CB  
19425 C CG  . PRO K  55  ? 0.4583 0.4550 0.6386 0.0247  -0.0405 0.0545  55  PRO K CG  
19426 C CD  . PRO K  55  ? 0.5005 0.4964 0.6754 0.0261  -0.0384 0.0537  55  PRO K CD  
19427 N N   . LEU K  56  ? 0.5190 0.5057 0.6957 0.0328  -0.0246 0.0498  56  LEU K N   
19428 C CA  . LEU K  56  ? 0.5426 0.5266 0.7274 0.0346  -0.0205 0.0509  56  LEU K CA  
19429 C C   . LEU K  56  ? 0.5615 0.5466 0.7546 0.0326  -0.0234 0.0525  56  LEU K C   
19430 O O   . LEU K  56  ? 0.5932 0.5785 0.7829 0.0317  -0.0247 0.0509  56  LEU K O   
19431 C CB  . LEU K  56  ? 0.5794 0.5604 0.7576 0.0373  -0.0156 0.0486  56  LEU K CB  
19432 C CG  . LEU K  56  ? 0.5135 0.4912 0.6987 0.0392  -0.0107 0.0495  56  LEU K CG  
19433 C CD1 . LEU K  56  ? 0.6044 0.5805 0.7960 0.0404  -0.0074 0.0512  56  LEU K CD1 
19434 C CD2 . LEU K  56  ? 0.6598 0.6352 0.8374 0.0417  -0.0066 0.0473  56  LEU K CD2 
19435 N N   . HIS K  57  ? 0.5696 0.5556 0.7739 0.0318  -0.0243 0.0555  57  HIS K N   
19436 C CA  . HIS K  57  ? 0.5514 0.5392 0.7646 0.0296  -0.0274 0.0574  57  HIS K CA  
19437 C C   . HIS K  57  ? 0.7079 0.6928 0.9290 0.0314  -0.0229 0.0580  57  HIS K C   
19438 O O   . HIS K  57  ? 0.7655 0.7484 0.9927 0.0332  -0.0190 0.0595  57  HIS K O   
19439 C CB  . HIS K  57  ? 0.6475 0.6387 0.8691 0.0274  -0.0316 0.0608  57  HIS K CB  
19440 C CG  . HIS K  57  ? 0.6835 0.6782 0.9117 0.0243  -0.0366 0.0624  57  HIS K CG  
19441 N ND1 . HIS K  57  ? 0.7243 0.7187 0.9636 0.0242  -0.0356 0.0644  57  HIS K ND1 
19442 C CD2 . HIS K  57  ? 0.6933 0.6916 0.9182 0.0209  -0.0426 0.0624  57  HIS K CD2 
19443 C CE1 . HIS K  57  ? 0.8082 0.8064 1.0510 0.0207  -0.0409 0.0654  57  HIS K CE1 
19444 N NE2 . HIS K  57  ? 0.8023 0.8028 1.0363 0.0187  -0.0451 0.0642  57  HIS K NE2 
19445 N N   . LEU K  58  ? 0.7596 0.7440 0.9806 0.0307  -0.0231 0.0568  58  LEU K N   
19446 C CA  . LEU K  58  ? 0.7717 0.7530 0.9990 0.0325  -0.0184 0.0570  58  LEU K CA  
19447 C C   . LEU K  58  ? 0.9048 0.8879 1.1454 0.0306  -0.0204 0.0598  58  LEU K C   
19448 O O   . LEU K  58  ? 0.9442 0.9249 1.1922 0.0321  -0.0165 0.0606  58  LEU K O   
19449 C CB  . LEU K  58  ? 0.7735 0.7528 0.9936 0.0331  -0.0167 0.0541  58  LEU K CB  
19450 C CG  . LEU K  58  ? 0.5555 0.5333 0.7626 0.0351  -0.0146 0.0514  58  LEU K CG  
19451 C CD1 . LEU K  58  ? 0.6281 0.6039 0.8299 0.0359  -0.0124 0.0491  58  LEU K CD1 
19452 C CD2 . LEU K  58  ? 0.5897 0.5651 0.7956 0.0381  -0.0098 0.0517  58  LEU K CD2 
19453 N N   . GLY K  59  ? 0.8483 0.8358 1.0920 0.0274  -0.0264 0.0615  59  GLY K N   
19454 C CA  . GLY K  59  ? 0.7226 0.7127 0.9790 0.0253  -0.0291 0.0646  59  GLY K CA  
19455 C C   . GLY K  59  ? 0.8796 0.8690 1.1393 0.0243  -0.0285 0.0635  59  GLY K C   
19456 O O   . GLY K  59  ? 0.9967 0.9872 1.2500 0.0221  -0.0312 0.0612  59  GLY K O   
19457 N N   . LYS K  60  ? 1.0041 0.9916 1.2739 0.0257  -0.0248 0.0651  60  LYS K N   
19458 C CA  . LYS K  60  ? 1.1290 1.1159 1.4037 0.0246  -0.0241 0.0644  60  LYS K CA  
19459 C C   . LYS K  60  ? 1.1134 1.0956 1.3798 0.0269  -0.0192 0.0609  60  LYS K C   
19460 O O   . LYS K  60  ? 1.1215 1.1026 1.3902 0.0261  -0.0181 0.0598  60  LYS K O   
19461 C CB  . LYS K  60  ? 1.2538 1.2405 1.5431 0.0253  -0.0219 0.0676  60  LYS K CB  
19462 C CG  . LYS K  60  ? 1.7384 1.7257 2.0349 0.0233  -0.0224 0.0675  60  LYS K CG  
19463 C CD  . LYS K  60  ? 1.8019 1.7949 2.0998 0.0186  -0.0297 0.0681  60  LYS K CD  
19464 C CE  . LYS K  60  ? 1.8752 1.8731 2.1820 0.0170  -0.0341 0.0724  60  LYS K CE  
19465 N NZ  . LYS K  60  ? 1.7872 1.7910 2.0951 0.0121  -0.0415 0.0732  60  LYS K NZ  
19466 N N   . CYS K  61  ? 1.0035 0.9831 1.2603 0.0296  -0.0161 0.0593  61  CYS K N   
19467 C CA  . CYS K  61  ? 0.8520 0.8274 1.1009 0.0322  -0.0113 0.0564  61  CYS K CA  
19468 C C   . CYS K  61  ? 0.7975 0.7735 1.0334 0.0315  -0.0134 0.0536  61  CYS K C   
19469 O O   . CYS K  61  ? 0.9002 0.8794 1.1319 0.0296  -0.0179 0.0536  61  CYS K O   
19470 C CB  . CYS K  61  ? 0.8017 0.7734 1.0495 0.0361  -0.0052 0.0567  61  CYS K CB  
19471 S SG  . CYS K  61  ? 1.0792 1.0490 1.3418 0.0374  -0.0012 0.0597  61  CYS K SG  
19472 N N   . ASN K  62  ? 0.6583 0.6311 0.8881 0.0330  -0.0099 0.0512  62  ASN K N   
19473 C CA  . ASN K  62  ? 0.7993 0.7721 1.0168 0.0331  -0.0107 0.0485  62  ASN K CA  
19474 C C   . ASN K  62  ? 0.7234 0.6931 0.9333 0.0372  -0.0055 0.0476  62  ASN K C   
19475 O O   . ASN K  62  ? 0.6531 0.6203 0.8672 0.0397  -0.0011 0.0488  62  ASN K O   
19476 C CB  . ASN K  62  ? 0.7927 0.7648 1.0086 0.0314  -0.0112 0.0465  62  ASN K CB  
19477 C CG  . ASN K  62  ? 0.7423 0.7105 0.9629 0.0334  -0.0057 0.0464  62  ASN K CG  
19478 O OD1 . ASN K  62  ? 0.7744 0.7398 0.9956 0.0369  -0.0008 0.0471  62  ASN K OD1 
19479 N ND2 . ASN K  62  ? 0.7844 0.7524 1.0081 0.0312  -0.0064 0.0453  62  ASN K ND2 
19480 N N   . ILE K  63  ? 0.5701 0.5401 0.7690 0.0377  -0.0061 0.0455  63  ILE K N   
19481 C CA  . ILE K  63  ? 0.5337 0.5016 0.7246 0.0412  -0.0018 0.0447  63  ILE K CA  
19482 C C   . ILE K  63  ? 0.5509 0.5149 0.7449 0.0442  0.0043  0.0451  63  ILE K C   
19483 O O   . ILE K  63  ? 0.6024 0.5647 0.7961 0.0467  0.0081  0.0459  63  ILE K O   
19484 C CB  . ILE K  63  ? 0.6223 0.5910 0.8018 0.0413  -0.0029 0.0424  63  ILE K CB  
19485 C CG1 . ILE K  63  ? 0.4625 0.4349 0.6383 0.0385  -0.0087 0.0420  63  ILE K CG1 
19486 C CG2 . ILE K  63  ? 0.5020 0.4689 0.6737 0.0449  0.0015  0.0419  63  ILE K CG2 
19487 C CD1 . ILE K  63  ? 0.6271 0.6008 0.8015 0.0392  -0.0092 0.0431  63  ILE K CD1 
19488 N N   . ALA K  64  ? 0.5865 0.5488 0.7831 0.0437  0.0054  0.0444  64  ALA K N   
19489 C CA  . ALA K  64  ? 0.5609 0.5194 0.7605 0.0463  0.0112  0.0448  64  ALA K CA  
19490 C C   . ALA K  64  ? 0.6098 0.5669 0.8183 0.0474  0.0138  0.0469  64  ALA K C   
19491 O O   . ALA K  64  ? 0.7147 0.6693 0.9215 0.0504  0.0186  0.0473  64  ALA K O   
19492 C CB  . ALA K  64  ? 0.5104 0.4676 0.7135 0.0449  0.0113  0.0439  64  ALA K CB  
19493 N N   . GLY K  65  ? 0.6502 0.6092 0.8684 0.0448  0.0107  0.0483  65  GLY K N   
19494 C CA  . GLY K  65  ? 0.5868 0.5446 0.8148 0.0455  0.0130  0.0505  65  GLY K CA  
19495 C C   . GLY K  65  ? 0.5884 0.5462 0.8134 0.0473  0.0145  0.0512  65  GLY K C   
19496 O O   . GLY K  65  ? 0.6041 0.5591 0.8324 0.0495  0.0193  0.0521  65  GLY K O   
19497 N N   . TRP K  66  ? 0.5593 0.5199 0.7779 0.0461  0.0106  0.0506  66  TRP K N   
19498 C CA  . TRP K  66  ? 0.7187 0.6796 0.9344 0.0473  0.0116  0.0511  66  TRP K CA  
19499 C C   . TRP K  66  ? 0.5603 0.5182 0.7678 0.0505  0.0170  0.0500  66  TRP K C   
19500 O O   . TRP K  66  ? 0.6580 0.6142 0.8673 0.0520  0.0207  0.0508  66  TRP K O   
19501 C CB  . TRP K  66  ? 0.6427 0.6073 0.8528 0.0452  0.0061  0.0506  66  TRP K CB  
19502 C CG  . TRP K  66  ? 0.6896 0.6543 0.8934 0.0465  0.0074  0.0503  66  TRP K CG  
19503 C CD1 . TRP K  66  ? 0.7719 0.7356 0.9806 0.0472  0.0097  0.0517  66  TRP K CD1 
19504 C CD2 . TRP K  66  ? 0.6763 0.6421 0.8680 0.0471  0.0068  0.0483  66  TRP K CD2 
19505 N NE1 . TRP K  66  ? 0.7911 0.7551 0.9911 0.0480  0.0105  0.0505  66  TRP K NE1 
19506 C CE2 . TRP K  66  ? 0.7077 0.6732 0.8973 0.0480  0.0086  0.0485  66  TRP K CE2 
19507 C CE3 . TRP K  66  ? 0.6159 0.5828 0.7986 0.0469  0.0049  0.0464  66  TRP K CE3 
19508 C CZ2 . TRP K  66  ? 0.6857 0.6522 0.8643 0.0486  0.0085  0.0469  66  TRP K CZ2 
19509 C CZ3 . TRP K  66  ? 0.7082 0.6762 0.8804 0.0477  0.0048  0.0450  66  TRP K CZ3 
19510 C CH2 . TRP K  66  ? 0.6939 0.6619 0.8641 0.0485  0.0064  0.0452  66  TRP K CH2 
19511 N N   . ILE K  67  ? 0.6192 0.5768 0.8179 0.0515  0.0176  0.0483  67  ILE K N   
19512 C CA  . ILE K  67  ? 0.7168 0.6724 0.9070 0.0545  0.0222  0.0474  67  ILE K CA  
19513 C C   . ILE K  67  ? 0.6790 0.6307 0.8734 0.0568  0.0280  0.0482  67  ILE K C   
19514 O O   . ILE K  67  ? 0.6932 0.6429 0.8849 0.0589  0.0325  0.0484  67  ILE K O   
19515 C CB  . ILE K  67  ? 0.4854 0.4424 0.6650 0.0550  0.0209  0.0457  67  ILE K CB  
19516 C CG1 . ILE K  67  ? 0.8532 0.8138 1.0300 0.0522  0.0147  0.0448  67  ILE K CG1 
19517 C CG2 . ILE K  67  ? 0.5222 0.4786 0.6922 0.0575  0.0243  0.0451  67  ILE K CG2 
19518 C CD1 . ILE K  67  ? 1.0370 0.9989 1.2038 0.0526  0.0135  0.0431  67  ILE K CD1 
19519 N N   . LEU K  68  ? 0.5725 0.5230 0.7733 0.0562  0.0281  0.0485  68  LEU K N   
19520 C CA  . LEU K  68  ? 0.6098 0.5564 0.8152 0.0582  0.0337  0.0493  68  LEU K CA  
19521 C C   . LEU K  68  ? 0.6576 0.6025 0.8717 0.0585  0.0363  0.0509  68  LEU K C   
19522 O O   . LEU K  68  ? 0.6235 0.5650 0.8386 0.0607  0.0418  0.0514  68  LEU K O   
19523 C CB  . LEU K  68  ? 0.5984 0.5442 0.8093 0.0572  0.0330  0.0491  68  LEU K CB  
19524 C CG  . LEU K  68  ? 0.6393 0.5850 0.8420 0.0578  0.0329  0.0476  68  LEU K CG  
19525 C CD1 . LEU K  68  ? 0.5168 0.4609 0.7260 0.0568  0.0334  0.0473  68  LEU K CD1 
19526 C CD2 . LEU K  68  ? 0.4138 0.3575 0.6083 0.0614  0.0379  0.0475  68  LEU K CD2 
19527 N N   . GLY K  69  ? 0.7261 0.6734 0.9466 0.0562  0.0325  0.0518  69  GLY K N   
19528 C CA  . GLY K  69  ? 0.6477 0.5937 0.8774 0.0563  0.0347  0.0535  69  GLY K CA  
19529 C C   . GLY K  69  ? 0.7406 0.6859 0.9831 0.0551  0.0347  0.0550  69  GLY K C   
19530 O O   . GLY K  69  ? 0.6919 0.6343 0.9416 0.0563  0.0392  0.0562  69  GLY K O   
19531 N N   . ASN K  70  ? 0.7957 0.7439 1.0410 0.0527  0.0296  0.0549  70  ASN K N   
19532 C CA  . ASN K  70  ? 0.8702 0.8187 1.1279 0.0510  0.0286  0.0564  70  ASN K CA  
19533 C C   . ASN K  70  ? 1.0202 0.9691 1.2884 0.0507  0.0291  0.0588  70  ASN K C   
19534 O O   . ASN K  70  ? 0.9566 0.9078 1.2238 0.0499  0.0265  0.0594  70  ASN K O   
19535 C CB  . ASN K  70  ? 0.8179 0.7703 1.0760 0.0477  0.0222  0.0559  70  ASN K CB  
19536 C CG  . ASN K  70  ? 0.9296 0.8827 1.1996 0.0457  0.0211  0.0570  70  ASN K CG  
19537 O OD1 . ASN K  70  ? 1.0024 0.9556 1.2833 0.0455  0.0220  0.0592  70  ASN K OD1 
19538 N ND2 . ASN K  70  ? 0.9396 0.8931 1.2077 0.0441  0.0193  0.0555  70  ASN K ND2 
19539 N N   . PRO K  71  ? 1.1670 1.1135 1.4456 0.0513  0.0328  0.0602  71  PRO K N   
19540 C CA  . PRO K  71  ? 1.0240 0.9705 1.3138 0.0512  0.0341  0.0627  71  PRO K CA  
19541 C C   . PRO K  71  ? 1.0373 0.9888 1.3328 0.0485  0.0277  0.0645  71  PRO K C   
19542 O O   . PRO K  71  ? 1.3411 1.2929 1.6421 0.0487  0.0284  0.0663  71  PRO K O   
19543 C CB  . PRO K  71  ? 1.0661 1.0106 1.3668 0.0514  0.0370  0.0638  71  PRO K CB  
19544 C CG  . PRO K  71  ? 1.1239 1.0651 1.4166 0.0531  0.0404  0.0616  71  PRO K CG  
19545 C CD  . PRO K  71  ? 1.1415 1.0851 1.4221 0.0523  0.0363  0.0595  71  PRO K CD  
19546 N N   . GLU K  72  ? 1.0507 1.0060 1.3446 0.0459  0.0218  0.0639  72  GLU K N   
19547 C CA  . GLU K  72  ? 1.1132 1.0735 1.4125 0.0429  0.0154  0.0658  72  GLU K CA  
19548 C C   . GLU K  72  ? 0.9562 0.9188 1.2452 0.0424  0.0118  0.0649  72  GLU K C   
19549 O O   . GLU K  72  ? 1.0161 0.9828 1.3085 0.0402  0.0067  0.0666  72  GLU K O   
19550 C CB  . GLU K  72  ? 1.0860 1.0496 1.3899 0.0399  0.0107  0.0659  72  GLU K CB  
19551 C CG  . GLU K  72  ? 1.3205 1.2824 1.6355 0.0399  0.0136  0.0670  72  GLU K CG  
19552 C CD  . GLU K  72  ? 1.5567 1.5199 1.8859 0.0398  0.0141  0.0706  72  GLU K CD  
19553 O OE1 . GLU K  72  ? 1.6136 1.5803 1.9455 0.0386  0.0103  0.0726  72  GLU K OE1 
19554 O OE2 . GLU K  72  ? 1.3262 1.2868 1.6642 0.0410  0.0185  0.0715  72  GLU K OE2 
19555 N N   . CYS K  73  ? 1.1955 1.1556 1.4722 0.0444  0.0145  0.0623  73  CYS K N   
19556 C CA  . CYS K  73  ? 1.2131 1.1750 1.4795 0.0440  0.0117  0.0612  73  CYS K CA  
19557 C C   . CYS K  73  ? 1.4705 1.4302 1.7355 0.0461  0.0157  0.0616  73  CYS K C   
19558 O O   . CYS K  73  ? 1.5792 1.5380 1.8331 0.0473  0.0170  0.0597  73  CYS K O   
19559 C CB  . CYS K  73  ? 1.0295 0.9907 1.2830 0.0446  0.0116  0.0581  73  CYS K CB  
19560 S SG  . CYS K  73  ? 0.9912 0.9545 1.2452 0.0419  0.0073  0.0571  73  CYS K SG  
19561 N N   . GLU K  74  ? 1.5991 1.5579 1.8754 0.0464  0.0178  0.0641  74  GLU K N   
19562 C CA  . GLU K  74  ? 1.7688 1.7246 2.0455 0.0484  0.0230  0.0644  74  GLU K CA  
19563 C C   . GLU K  74  ? 1.9182 1.8760 2.1902 0.0477  0.0207  0.0645  74  GLU K C   
19564 O O   . GLU K  74  ? 1.8863 1.8423 2.1482 0.0490  0.0232  0.0625  74  GLU K O   
19565 C CB  . GLU K  74  ? 1.7934 1.7478 2.0848 0.0487  0.0260  0.0672  74  GLU K CB  
19566 C CG  . GLU K  74  ? 1.9269 1.8760 2.2188 0.0513  0.0338  0.0668  74  GLU K CG  
19567 C CD  . GLU K  74  ? 1.9629 1.9096 2.2654 0.0521  0.0375  0.0681  74  GLU K CD  
19568 O OE1 . GLU K  74  ? 1.9091 1.8581 2.2171 0.0508  0.0342  0.0689  74  GLU K OE1 
19569 O OE2 . GLU K  74  ? 1.8919 1.8344 2.1971 0.0540  0.0440  0.0682  74  GLU K OE2 
19570 N N   . SER K  75  ? 1.9461 1.9077 2.2252 0.0456  0.0157  0.0669  75  SER K N   
19571 C CA  . SER K  75  ? 2.1177 2.0804 2.3975 0.0452  0.0148  0.0681  75  SER K CA  
19572 C C   . SER K  75  ? 2.1911 2.1555 2.4585 0.0446  0.0120  0.0661  75  SER K C   
19573 O O   . SER K  75  ? 2.2476 2.2131 2.5167 0.0440  0.0109  0.0674  75  SER K O   
19574 C CB  . SER K  75  ? 2.0941 2.0605 2.3870 0.0433  0.0105  0.0719  75  SER K CB  
19575 O OG  . SER K  75  ? 1.9117 1.8815 2.2070 0.0413  0.0054  0.0723  75  SER K OG  
19576 N N   . LEU K  76  ? 2.3377 2.3019 2.5928 0.0449  0.0113  0.0631  76  LEU K N   
19577 C CA  . LEU K  76  ? 2.3474 2.3138 2.5918 0.0441  0.0081  0.0615  76  LEU K CA  
19578 C C   . LEU K  76  ? 2.3524 2.3166 2.5835 0.0458  0.0117  0.0582  76  LEU K C   
19579 O O   . LEU K  76  ? 2.2207 2.1869 2.4416 0.0452  0.0087  0.0564  76  LEU K O   
19580 C CB  . LEU K  76  ? 2.2400 2.2107 2.4824 0.0416  0.0011  0.0615  76  LEU K CB  
19581 C CG  . LEU K  76  ? 2.1266 2.1005 2.3607 0.0400  -0.0036 0.0607  76  LEU K CG  
19582 C CD1 . LEU K  76  ? 2.1559 2.1289 2.3897 0.0407  -0.0015 0.0612  76  LEU K CD1 
19583 C CD2 . LEU K  76  ? 1.7317 1.7100 1.9708 0.0370  -0.0104 0.0626  76  LEU K CD2 
19584 N N   . SER K  77  ? 2.1223 2.0824 2.3533 0.0480  0.0181  0.0576  77  SER K N   
19585 C CA  . SER K  77  ? 1.9491 1.9074 2.1679 0.0495  0.0216  0.0548  77  SER K CA  
19586 C C   . SER K  77  ? 1.9142 1.8741 2.1256 0.0487  0.0200  0.0538  77  SER K C   
19587 O O   . SER K  77  ? 1.7370 1.6975 1.9367 0.0492  0.0201  0.0514  77  SER K O   
19588 C CB  . SER K  77  ? 1.8830 1.8367 2.1038 0.0516  0.0289  0.0546  77  SER K CB  
19589 O OG  . SER K  77  ? 1.7436 1.6957 1.9623 0.0519  0.0323  0.0541  77  SER K OG  
19590 N N   . THR K  78  ? 2.6206 2.5816 2.8395 0.0474  0.0184  0.0557  78  THR K N   
19591 C CA  . THR K  78  ? 2.6177 2.5795 2.8313 0.0467  0.0178  0.0550  78  THR K CA  
19592 C C   . THR K  78  ? 2.5381 2.5038 2.7421 0.0453  0.0122  0.0535  78  THR K C   
19593 O O   . THR K  78  ? 2.5093 2.4780 2.7162 0.0435  0.0072  0.0550  78  THR K O   
19594 C CB  . THR K  78  ? 2.4103 2.3718 2.6354 0.0459  0.0182  0.0577  78  THR K CB  
19595 O OG1 . THR K  78  ? 2.3961 2.3533 2.6238 0.0473  0.0252  0.0574  78  THR K OG1 
19596 C CG2 . THR K  78  ? 1.7970 1.7611 2.0188 0.0443  0.0146  0.0578  78  THR K CG2 
19597 N N   . ALA K  79  ? 2.1893 2.1548 2.3817 0.0462  0.0133  0.0508  79  ALA K N   
19598 C CA  . ALA K  79  ? 1.7802 1.7490 1.9627 0.0453  0.0087  0.0492  79  ALA K CA  
19599 C C   . ALA K  79  ? 1.5067 1.4749 1.6769 0.0466  0.0117  0.0464  79  ALA K C   
19600 O O   . ALA K  79  ? 1.4287 1.3951 1.5961 0.0483  0.0151  0.0455  79  ALA K O   
19601 C CB  . ALA K  79  ? 1.6512 1.6219 1.8346 0.0446  0.0047  0.0495  79  ALA K CB  
19602 N N   . SER K  80  ? 1.0574 1.0272 1.2206 0.0457  0.0104  0.0451  80  SER K N   
19603 C CA  . SER K  80  ? 1.0597 1.0296 1.2112 0.0466  0.0127  0.0425  80  SER K CA  
19604 C C   . SER K  80  ? 0.8965 0.8698 1.0395 0.0461  0.0082  0.0412  80  SER K C   
19605 O O   . SER K  80  ? 0.8401 0.8142 0.9738 0.0472  0.0095  0.0394  80  SER K O   
19606 C CB  . SER K  80  ? 1.2530 1.2225 1.4020 0.0459  0.0148  0.0416  80  SER K CB  
19607 O OG  . SER K  80  ? 1.3810 1.3472 1.5387 0.0462  0.0190  0.0429  80  SER K OG  
19608 N N   . SER K  81  ? 0.7541 0.7297 0.9006 0.0444  0.0030  0.0423  81  SER K N   
19609 C CA  . SER K  81  ? 0.7441 0.7228 0.8833 0.0435  -0.0015 0.0411  81  SER K CA  
19610 C C   . SER K  81  ? 0.6467 0.6272 0.7920 0.0414  -0.0068 0.0427  81  SER K C   
19611 O O   . SER K  81  ? 0.6905 0.6706 0.8451 0.0405  -0.0076 0.0448  81  SER K O   
19612 C CB  . SER K  81  ? 0.7518 0.7324 0.8820 0.0428  -0.0023 0.0393  81  SER K CB  
19613 O OG  . SER K  81  ? 0.7597 0.7404 0.8945 0.0413  -0.0032 0.0403  81  SER K OG  
19614 N N   . TRP K  82  ? 0.4841 0.4666 0.6243 0.0407  -0.0104 0.0417  82  TRP K N   
19615 C CA  . TRP K  82  ? 0.5512 0.5358 0.6955 0.0383  -0.0157 0.0429  82  TRP K CA  
19616 C C   . TRP K  82  ? 0.5758 0.5628 0.7111 0.0372  -0.0193 0.0410  82  TRP K C   
19617 O O   . TRP K  82  ? 0.6076 0.5943 0.7358 0.0387  -0.0175 0.0392  82  TRP K O   
19618 C CB  . TRP K  82  ? 0.5590 0.5424 0.7125 0.0382  -0.0157 0.0445  82  TRP K CB  
19619 C CG  . TRP K  82  ? 0.6290 0.6105 0.7797 0.0400  -0.0127 0.0432  82  TRP K CG  
19620 C CD1 . TRP K  82  ? 0.6480 0.6304 0.7938 0.0396  -0.0145 0.0418  82  TRP K CD1 
19621 C CD2 . TRP K  82  ? 0.5672 0.5457 0.7202 0.0426  -0.0072 0.0434  82  TRP K CD2 
19622 N NE1 . TRP K  82  ? 0.5990 0.5790 0.7440 0.0419  -0.0104 0.0413  82  TRP K NE1 
19623 C CE2 . TRP K  82  ? 0.5649 0.5425 0.7140 0.0437  -0.0060 0.0422  82  TRP K CE2 
19624 C CE3 . TRP K  82  ? 0.5099 0.4860 0.6676 0.0439  -0.0029 0.0444  82  TRP K CE3 
19625 C CZ2 . TRP K  82  ? 0.5811 0.5558 0.7310 0.0462  -0.0008 0.0422  82  TRP K CZ2 
19626 C CZ3 . TRP K  82  ? 0.6025 0.5757 0.7607 0.0462  0.0022  0.0441  82  TRP K CZ3 
19627 C CH2 . TRP K  82  ? 0.5237 0.4963 0.6780 0.0474  0.0031  0.0432  82  TRP K CH2 
19628 N N   . SER K  83  ? 0.6113 0.6008 0.7472 0.0346  -0.0243 0.0416  83  SER K N   
19629 C CA  . SER K  83  ? 0.6201 0.6119 0.7477 0.0332  -0.0278 0.0399  83  SER K CA  
19630 C C   . SER K  83  ? 0.5345 0.5261 0.6627 0.0325  -0.0294 0.0394  83  SER K C   
19631 O O   . SER K  83  ? 0.6655 0.6578 0.7862 0.0325  -0.0299 0.0374  83  SER K O   
19632 C CB  . SER K  83  ? 0.6299 0.6242 0.7577 0.0306  -0.0325 0.0407  83  SER K CB  
19633 O OG  . SER K  83  ? 0.6185 0.6133 0.7563 0.0289  -0.0350 0.0434  83  SER K OG  
19634 N N   . TYR K  84  ? 0.4252 0.4162 0.5629 0.0317  -0.0299 0.0412  84  TYR K N   
19635 C CA  . TYR K  84  ? 0.4715 0.4620 0.6108 0.0309  -0.0308 0.0407  84  TYR K CA  
19636 C C   . TYR K  84  ? 0.5167 0.5057 0.6670 0.0311  -0.0293 0.0428  84  TYR K C   
19637 O O   . TYR K  84  ? 0.6377 0.6262 0.7946 0.0317  -0.0280 0.0448  84  TYR K O   
19638 C CB  . TYR K  84  ? 0.4645 0.4576 0.6014 0.0274  -0.0363 0.0403  84  TYR K CB  
19639 C CG  . TYR K  84  ? 0.5902 0.5856 0.7342 0.0248  -0.0406 0.0428  84  TYR K CG  
19640 C CD1 . TYR K  84  ? 0.5088 0.5050 0.6611 0.0227  -0.0429 0.0445  84  TYR K CD1 
19641 C CD2 . TYR K  84  ? 0.5709 0.5680 0.7136 0.0243  -0.0422 0.0437  84  TYR K CD2 
19642 C CE1 . TYR K  84  ? 0.5015 0.5003 0.6605 0.0203  -0.0470 0.0472  84  TYR K CE1 
19643 C CE2 . TYR K  84  ? 0.4567 0.4559 0.6060 0.0220  -0.0460 0.0465  84  TYR K CE2 
19644 C CZ  . TYR K  84  ? 0.5032 0.5034 0.6608 0.0201  -0.0484 0.0483  84  TYR K CZ  
19645 O OH  . TYR K  84  ? 0.6180 0.6209 0.7827 0.0178  -0.0524 0.0514  84  TYR K OH  
19646 N N   . ILE K  85  ? 0.4050 0.3931 0.5576 0.0306  -0.0293 0.0424  85  ILE K N   
19647 C CA  . ILE K  85  ? 0.5226 0.5093 0.6857 0.0308  -0.0277 0.0442  85  ILE K CA  
19648 C C   . ILE K  85  ? 0.5706 0.5596 0.7400 0.0272  -0.0326 0.0453  85  ILE K C   
19649 O O   . ILE K  85  ? 0.5040 0.4942 0.6686 0.0250  -0.0355 0.0437  85  ILE K O   
19650 C CB  . ILE K  85  ? 0.5120 0.4955 0.6743 0.0333  -0.0229 0.0430  85  ILE K CB  
19651 C CG1 . ILE K  85  ? 0.4621 0.4436 0.6190 0.0367  -0.0180 0.0423  85  ILE K CG1 
19652 C CG2 . ILE K  85  ? 0.4237 0.4058 0.5970 0.0332  -0.0215 0.0447  85  ILE K CG2 
19653 C CD1 . ILE K  85  ? 0.5311 0.5097 0.6863 0.0394  -0.0132 0.0413  85  ILE K CD1 
19654 N N   . VAL K  86  ? 0.5543 0.5439 0.7344 0.0265  -0.0333 0.0481  86  VAL K N   
19655 C CA  . VAL K  86  ? 0.5005 0.4928 0.6875 0.0230  -0.0379 0.0497  86  VAL K CA  
19656 C C   . VAL K  86  ? 0.4630 0.4537 0.6592 0.0233  -0.0356 0.0506  86  VAL K C   
19657 O O   . VAL K  86  ? 0.5204 0.5092 0.7234 0.0257  -0.0318 0.0522  86  VAL K O   
19658 C CB  . VAL K  86  ? 0.5314 0.5268 0.7244 0.0214  -0.0417 0.0528  86  VAL K CB  
19659 C CG1 . VAL K  86  ? 0.4760 0.4749 0.6757 0.0175  -0.0469 0.0546  86  VAL K CG1 
19660 C CG2 . VAL K  86  ? 0.5417 0.5386 0.7259 0.0210  -0.0437 0.0519  86  VAL K CG2 
19661 N N   . GLU K  87  ? 0.5535 0.5449 0.7499 0.0208  -0.0378 0.0495  87  GLU K N   
19662 C CA  . GLU K  87  ? 0.5906 0.5808 0.7956 0.0205  -0.0361 0.0501  87  GLU K CA  
19663 C C   . GLU K  87  ? 0.7567 0.7510 0.9683 0.0161  -0.0418 0.0517  87  GLU K C   
19664 O O   . GLU K  87  ? 0.8028 0.7996 1.0086 0.0130  -0.0463 0.0506  87  GLU K O   
19665 C CB  . GLU K  87  ? 0.5894 0.5765 0.7886 0.0215  -0.0328 0.0470  87  GLU K CB  
19666 C CG  . GLU K  87  ? 0.6553 0.6385 0.8591 0.0248  -0.0267 0.0472  87  GLU K CG  
19667 C CD  . GLU K  87  ? 0.7986 0.7786 0.9960 0.0260  -0.0233 0.0444  87  GLU K CD  
19668 O OE1 . GLU K  87  ? 0.8085 0.7852 1.0043 0.0297  -0.0179 0.0440  87  GLU K OE1 
19669 O OE2 . GLU K  87  ? 0.8218 0.8027 1.0156 0.0233  -0.0259 0.0425  87  GLU K OE2 
19670 N N   . THR K  88  ? 0.8230 0.8180 1.0464 0.0157  -0.0418 0.0544  88  THR K N   
19671 C CA  . THR K  88  ? 0.8459 0.8453 1.0765 0.0114  -0.0472 0.0563  88  THR K CA  
19672 C C   . THR K  88  ? 0.9179 0.9164 1.1486 0.0093  -0.0470 0.0540  88  THR K C   
19673 O O   . THR K  88  ? 1.0492 1.0438 1.2807 0.0117  -0.0419 0.0526  88  THR K O   
19674 C CB  . THR K  88  ? 0.9192 0.9202 1.1634 0.0119  -0.0473 0.0604  88  THR K CB  
19675 O OG1 . THR K  88  ? 1.1082 1.1058 1.3588 0.0141  -0.0421 0.0603  88  THR K OG1 
19676 C CG2 . THR K  88  ? 0.7715 0.7725 1.0160 0.0143  -0.0464 0.0625  88  THR K CG2 
19677 N N   . PRO K  89  ? 1.1633 1.1655 1.3929 0.0046  -0.0525 0.0535  89  PRO K N   
19678 C CA  . PRO K  89  ? 1.1522 1.1535 1.3813 0.0020  -0.0523 0.0510  89  PRO K CA  
19679 C C   . PRO K  89  ? 1.2957 1.2963 1.5367 0.0025  -0.0498 0.0526  89  PRO K C   
19680 O O   . PRO K  89  ? 1.2873 1.2856 1.5286 0.0017  -0.0475 0.0503  89  PRO K O   
19681 C CB  . PRO K  89  ? 1.0914 1.0977 1.3191 -0.0035 -0.0593 0.0512  89  PRO K CB  
19682 C CG  . PRO K  89  ? 1.1598 1.1684 1.3824 -0.0032 -0.0622 0.0525  89  PRO K CG  
19683 C CD  . PRO K  89  ? 1.2424 1.2495 1.4705 0.0013  -0.0589 0.0552  89  PRO K CD  
19684 N N   . SER K  90  ? 1.5036 1.5058 1.7544 0.0038  -0.0500 0.0564  90  SER K N   
19685 C CA  . SER K  90  ? 1.4742 1.4756 1.7370 0.0047  -0.0473 0.0582  90  SER K CA  
19686 C C   . SER K  90  ? 1.5719 1.5681 1.8353 0.0101  -0.0402 0.0582  90  SER K C   
19687 O O   . SER K  90  ? 1.7405 1.7364 2.0143 0.0119  -0.0380 0.0610  90  SER K O   
19688 C CB  . SER K  90  ? 1.5763 1.5831 1.8511 0.0025  -0.0517 0.0628  90  SER K CB  
19689 O OG  . SER K  90  ? 1.8424 1.8490 2.1292 0.0026  -0.0497 0.0644  90  SER K OG  
19690 N N   . SER K  91  ? 1.3211 1.3132 1.5736 0.0127  -0.0365 0.0550  91  SER K N   
19691 C CA  . SER K  91  ? 1.2531 1.2401 1.5053 0.0175  -0.0296 0.0546  91  SER K CA  
19692 C C   . SER K  91  ? 1.3545 1.3395 1.6130 0.0171  -0.0267 0.0539  91  SER K C   
19693 O O   . SER K  91  ? 1.3375 1.3254 1.6018 0.0133  -0.0303 0.0543  91  SER K O   
19694 C CB  . SER K  91  ? 1.1714 1.1552 1.4103 0.0200  -0.0267 0.0516  91  SER K CB  
19695 O OG  . SER K  91  ? 1.1877 1.1742 1.4178 0.0179  -0.0312 0.0504  91  SER K OG  
19696 N N   . ASP K  92  ? 1.5568 1.5368 1.8139 0.0208  -0.0203 0.0528  92  ASP K N   
19697 C CA  . ASP K  92  ? 1.6258 1.6034 1.8904 0.0211  -0.0168 0.0526  92  ASP K CA  
19698 C C   . ASP K  92  ? 1.4967 1.4697 1.7574 0.0224  -0.0119 0.0499  92  ASP K C   
19699 O O   . ASP K  92  ? 1.5956 1.5649 1.8606 0.0253  -0.0064 0.0503  92  ASP K O   
19700 C CB  . ASP K  92  ? 1.8105 1.7872 2.0862 0.0233  -0.0138 0.0557  92  ASP K CB  
19701 C CG  . ASP K  92  ? 1.7742 1.7463 2.0458 0.0283  -0.0076 0.0555  92  ASP K CG  
19702 O OD1 . ASP K  92  ? 1.7622 1.7308 2.0390 0.0305  -0.0023 0.0559  92  ASP K OD1 
19703 O OD2 . ASP K  92  ? 1.8054 1.7776 2.0688 0.0298  -0.0078 0.0551  92  ASP K OD2 
19704 N N   . ASN K  93  ? 1.3025 1.2757 1.5549 0.0204  -0.0138 0.0471  93  ASN K N   
19705 C CA  . ASN K  93  ? 1.2469 1.2159 1.4943 0.0216  -0.0094 0.0443  93  ASN K CA  
19706 C C   . ASN K  93  ? 1.2285 1.1934 1.4712 0.0268  -0.0036 0.0445  93  ASN K C   
19707 O O   . ASN K  93  ? 1.0929 1.0587 1.3301 0.0286  -0.0042 0.0450  93  ASN K O   
19708 C CB  . ASN K  93  ? 1.2458 1.2131 1.5001 0.0198  -0.0075 0.0435  93  ASN K CB  
19709 C CG  . ASN K  93  ? 1.3360 1.3034 1.5844 0.0164  -0.0093 0.0403  93  ASN K CG  
19710 O OD1 . ASN K  93  ? 1.3291 1.2933 1.5785 0.0163  -0.0057 0.0385  93  ASN K OD1 
19711 N ND2 . ASN K  93  ? 1.2939 1.2647 1.5359 0.0136  -0.0146 0.0394  93  ASN K ND2 
19712 N N   . GLY K  94  ? 1.5158 1.4764 1.7604 0.0292  0.0020  0.0439  94  GLY K N   
19713 C CA  . GLY K  94  ? 1.3260 1.2830 1.5634 0.0338  0.0074  0.0434  94  GLY K CA  
19714 C C   . GLY K  94  ? 1.4206 1.3754 1.6629 0.0373  0.0117  0.0457  94  GLY K C   
19715 O O   . GLY K  94  ? 1.2723 1.2287 1.5236 0.0364  0.0104  0.0478  94  GLY K O   
19716 N N   . THR K  95  ? 0.8797 0.8309 1.1159 0.0413  0.0170  0.0453  95  THR K N   
19717 C CA  . THR K  95  ? 0.9046 0.8530 1.1447 0.0447  0.0222  0.0470  95  THR K CA  
19718 C C   . THR K  95  ? 0.7982 0.7454 1.0507 0.0436  0.0237  0.0482  95  THR K C   
19719 O O   . THR K  95  ? 0.7771 0.7245 1.0332 0.0411  0.0224  0.0471  95  THR K O   
19720 C CB  . THR K  95  ? 0.7457 0.6900 0.9781 0.0486  0.0280  0.0462  95  THR K CB  
19721 O OG1 . THR K  95  ? 0.7643 0.7052 1.0018 0.0491  0.0320  0.0460  95  THR K OG1 
19722 C CG2 . THR K  95  ? 0.7192 0.6646 0.9401 0.0487  0.0263  0.0443  95  THR K CG2 
19723 N N   . CYS K  96  ? 0.6746 0.6207 0.9339 0.0453  0.0264  0.0503  96  CYS K N   
19724 C CA  . CYS K  96  ? 0.8157 0.7606 1.0873 0.0446  0.0282  0.0516  96  CYS K CA  
19725 C C   . CYS K  96  ? 0.7379 0.6783 1.0099 0.0462  0.0337  0.0506  96  CYS K C   
19726 O O   . CYS K  96  ? 0.7873 0.7274 1.0675 0.0443  0.0338  0.0506  96  CYS K O   
19727 C CB  . CYS K  96  ? 0.8463 0.7910 1.1252 0.0461  0.0302  0.0541  96  CYS K CB  
19728 S SG  . CYS K  96  ? 0.9882 0.9293 1.2587 0.0507  0.0359  0.0543  96  CYS K SG  
19729 N N   . TYR K  97  ? 0.7551 0.6922 1.0184 0.0498  0.0383  0.0500  97  TYR K N   
19730 C CA  . TYR K  97  ? 0.6907 0.6236 0.9530 0.0516  0.0435  0.0491  97  TYR K CA  
19731 C C   . TYR K  97  ? 0.6890 0.6221 0.9427 0.0507  0.0420  0.0468  97  TYR K C   
19732 O O   . TYR K  97  ? 0.7017 0.6357 0.9453 0.0520  0.0411  0.0462  97  TYR K O   
19733 C CB  . TYR K  97  ? 0.6801 0.6091 0.9386 0.0560  0.0499  0.0501  97  TYR K CB  
19734 C CG  . TYR K  97  ? 0.6818 0.6061 0.9430 0.0579  0.0558  0.0501  97  TYR K CG  
19735 C CD1 . TYR K  97  ? 0.8214 0.7431 1.0917 0.0589  0.0600  0.0516  97  TYR K CD1 
19736 C CD2 . TYR K  97  ? 0.7156 0.6382 0.9707 0.0586  0.0574  0.0486  97  TYR K CD2 
19737 C CE1 . TYR K  97  ? 0.8428 0.7601 1.1157 0.0606  0.0655  0.0516  97  TYR K CE1 
19738 C CE2 . TYR K  97  ? 0.7379 0.6561 0.9957 0.0603  0.0630  0.0487  97  TYR K CE2 
19739 C CZ  . TYR K  97  ? 0.7293 0.6449 0.9959 0.0613  0.0670  0.0502  97  TYR K CZ  
19740 O OH  . TYR K  97  ? 0.7391 0.6502 1.0085 0.0630  0.0727  0.0504  97  TYR K OH  
19741 N N   . PRO K  98  ? 0.6307 0.5629 0.8886 0.0485  0.0420  0.0456  98  PRO K N   
19742 C CA  . PRO K  98  ? 0.5969 0.5292 0.8478 0.0471  0.0406  0.0432  98  PRO K CA  
19743 C C   . PRO K  98  ? 0.7248 0.6545 0.9650 0.0510  0.0445  0.0428  98  PRO K C   
19744 O O   . PRO K  98  ? 0.6419 0.5682 0.8818 0.0547  0.0500  0.0441  98  PRO K O   
19745 C CB  . PRO K  98  ? 0.6530 0.5828 0.9113 0.0453  0.0428  0.0423  98  PRO K CB  
19746 C CG  . PRO K  98  ? 0.7368 0.6677 1.0070 0.0441  0.0423  0.0440  98  PRO K CG  
19747 C CD  . PRO K  98  ? 0.7547 0.6852 1.0242 0.0474  0.0442  0.0462  98  PRO K CD  
19748 N N   . GLY K  99  ? 0.6931 0.6245 0.9246 0.0502  0.0416  0.0412  99  GLY K N   
19749 C CA  . GLY K  99  ? 0.6498 0.5795 0.8712 0.0537  0.0448  0.0410  99  GLY K CA  
19750 C C   . GLY K  99  ? 0.6990 0.6319 0.9115 0.0524  0.0404  0.0395  99  GLY K C   
19751 O O   . GLY K  99  ? 0.6666 0.6029 0.8803 0.0487  0.0348  0.0387  99  GLY K O   
19752 N N   . ASP K  100 ? 0.7813 0.7131 0.9848 0.0555  0.0430  0.0394  100 ASP K N   
19753 C CA  . ASP K  100 ? 0.6022 0.5367 0.7969 0.0546  0.0395  0.0380  100 ASP K CA  
19754 C C   . ASP K  100 ? 0.5271 0.4642 0.7155 0.0567  0.0382  0.0393  100 ASP K C   
19755 O O   . ASP K  100 ? 0.5826 0.5183 0.7691 0.0604  0.0422  0.0409  100 ASP K O   
19756 C CB  . ASP K  100 ? 0.6540 0.5860 0.8431 0.0563  0.0430  0.0370  100 ASP K CB  
19757 C CG  . ASP K  100 ? 1.0783 1.0127 1.2600 0.0544  0.0392  0.0351  100 ASP K CG  
19758 O OD1 . ASP K  100 ? 1.2538 1.1916 1.4359 0.0509  0.0336  0.0342  100 ASP K OD1 
19759 O OD2 . ASP K  100 ? 1.1532 1.0862 1.3290 0.0564  0.0420  0.0346  100 ASP K OD2 
19760 N N   . PHE K  101 ? 0.3989 0.3399 0.5842 0.0543  0.0327  0.0384  101 PHE K N   
19761 C CA  . PHE K  101 ? 0.5043 0.4478 0.6828 0.0559  0.0313  0.0392  101 PHE K CA  
19762 C C   . PHE K  101 ? 0.5252 0.4697 0.6937 0.0570  0.0310  0.0381  101 PHE K C   
19763 O O   . PHE K  101 ? 0.5200 0.4666 0.6855 0.0543  0.0269  0.0364  101 PHE K O   
19764 C CB  . PHE K  101 ? 0.4613 0.4084 0.6424 0.0528  0.0256  0.0392  101 PHE K CB  
19765 C CG  . PHE K  101 ? 0.4045 0.3533 0.5825 0.0546  0.0255  0.0405  101 PHE K CG  
19766 C CD1 . PHE K  101 ? 0.5041 0.4532 0.6892 0.0540  0.0250  0.0419  101 PHE K CD1 
19767 C CD2 . PHE K  101 ? 0.5538 0.5038 0.7221 0.0567  0.0260  0.0403  101 PHE K CD2 
19768 C CE1 . PHE K  101 ? 0.4242 0.3744 0.6064 0.0555  0.0253  0.0429  101 PHE K CE1 
19769 C CE2 . PHE K  101 ? 0.4791 0.4306 0.6443 0.0580  0.0260  0.0412  101 PHE K CE2 
19770 C CZ  . PHE K  101 ? 0.3779 0.3293 0.5499 0.0574  0.0258  0.0424  101 PHE K CZ  
19771 N N   . ILE K  102 ? 0.3966 0.3397 0.5600 0.0610  0.0355  0.0391  102 ILE K N   
19772 C CA  . ILE K  102 ? 0.4300 0.3738 0.5848 0.0625  0.0361  0.0385  102 ILE K CA  
19773 C C   . ILE K  102 ? 0.4967 0.4447 0.6446 0.0614  0.0315  0.0377  102 ILE K C   
19774 O O   . ILE K  102 ? 0.5324 0.4824 0.6792 0.0619  0.0303  0.0387  102 ILE K O   
19775 C CB  . ILE K  102 ? 0.5562 0.4983 0.7073 0.0672  0.0417  0.0404  102 ILE K CB  
19776 C CG1 . ILE K  102 ? 0.6548 0.5929 0.8133 0.0686  0.0464  0.0416  102 ILE K CG1 
19777 C CG2 . ILE K  102 ? 0.5235 0.4654 0.6683 0.0688  0.0433  0.0399  102 ILE K CG2 
19778 C CD1 . ILE K  102 ? 0.5265 0.4616 0.6911 0.0666  0.0474  0.0404  102 ILE K CD1 
19779 N N   . ASP K  103 ? 0.5401 0.4893 0.6835 0.0598  0.0291  0.0360  103 ASP K N   
19780 C CA  . ASP K  103 ? 0.4747 0.4278 0.6116 0.0586  0.0247  0.0351  103 ASP K CA  
19781 C C   . ASP K  103 ? 0.4724 0.4278 0.6126 0.0561  0.0205  0.0353  103 ASP K C   
19782 O O   . ASP K  103 ? 0.4473 0.4051 0.5837 0.0570  0.0193  0.0360  103 ASP K O   
19783 C CB  . ASP K  103 ? 0.6137 0.5683 0.7425 0.0622  0.0269  0.0362  103 ASP K CB  
19784 C CG  . ASP K  103 ? 0.6532 0.6061 0.7786 0.0647  0.0307  0.0363  103 ASP K CG  
19785 O OD1 . ASP K  103 ? 0.6565 0.6080 0.7826 0.0628  0.0301  0.0346  103 ASP K OD1 
19786 O OD2 . ASP K  103 ? 0.5968 0.5497 0.7185 0.0685  0.0343  0.0381  103 ASP K OD2 
19787 N N   . TYR K  104 ? 0.5416 0.4963 0.6894 0.0530  0.0185  0.0348  104 TYR K N   
19788 C CA  . TYR K  104 ? 0.4924 0.4491 0.6451 0.0506  0.0147  0.0355  104 TYR K CA  
19789 C C   . TYR K  104 ? 0.5239 0.4843 0.6717 0.0480  0.0092  0.0344  104 TYR K C   
19790 O O   . TYR K  104 ? 0.4364 0.3991 0.5832 0.0480  0.0072  0.0352  104 TYR K O   
19791 C CB  . TYR K  104 ? 0.4578 0.4131 0.6204 0.0480  0.0140  0.0355  104 TYR K CB  
19792 C CG  . TYR K  104 ? 0.5354 0.4931 0.7041 0.0453  0.0099  0.0364  104 TYR K CG  
19793 C CD1 . TYR K  104 ? 0.4478 0.4061 0.6181 0.0471  0.0107  0.0382  104 TYR K CD1 
19794 C CD2 . TYR K  104 ? 0.3975 0.3569 0.5707 0.0410  0.0054  0.0357  104 TYR K CD2 
19795 C CE1 . TYR K  104 ? 0.5233 0.4837 0.6999 0.0449  0.0072  0.0393  104 TYR K CE1 
19796 C CE2 . TYR K  104 ? 0.4738 0.4357 0.6531 0.0388  0.0016  0.0370  104 TYR K CE2 
19797 C CZ  . TYR K  104 ? 0.4685 0.4308 0.6497 0.0408  0.0026  0.0389  104 TYR K CZ  
19798 O OH  . TYR K  104 ? 0.5565 0.5213 0.7444 0.0387  -0.0009 0.0405  104 TYR K OH  
19799 N N   . GLU K  105 ? 0.4465 0.4074 0.5915 0.0456  0.0070  0.0325  105 GLU K N   
19800 C CA  . GLU K  105 ? 0.4025 0.3666 0.5424 0.0429  0.0019  0.0313  105 GLU K CA  
19801 C C   . GLU K  105 ? 0.4870 0.4531 0.6188 0.0454  0.0022  0.0316  105 GLU K C   
19802 O O   . GLU K  105 ? 0.5037 0.4727 0.6330 0.0439  -0.0016 0.0315  105 GLU K O   
19803 C CB  . GLU K  105 ? 0.4750 0.4387 0.6121 0.0403  0.0006  0.0289  105 GLU K CB  
19804 C CG  . GLU K  105 ? 0.4089 0.3709 0.5535 0.0373  0.0003  0.0283  105 GLU K CG  
19805 C CD  . GLU K  105 ? 0.7871 0.7451 0.9359 0.0400  0.0060  0.0289  105 GLU K CD  
19806 O OE1 . GLU K  105 ? 0.8473 0.8036 0.9915 0.0436  0.0102  0.0290  105 GLU K OE1 
19807 O OE2 . GLU K  105 ? 0.6892 0.6460 0.8462 0.0385  0.0063  0.0293  105 GLU K OE2 
19808 N N   . GLU K  106 ? 0.5382 0.5028 0.6660 0.0491  0.0067  0.0319  106 GLU K N   
19809 C CA  . GLU K  106 ? 0.4519 0.4185 0.5722 0.0517  0.0074  0.0324  106 GLU K CA  
19810 C C   . GLU K  106 ? 0.4192 0.3869 0.5414 0.0524  0.0071  0.0339  106 GLU K C   
19811 O O   . GLU K  106 ? 0.4435 0.4140 0.5612 0.0519  0.0045  0.0337  106 GLU K O   
19812 C CB  . GLU K  106 ? 0.3856 0.3505 0.5021 0.0556  0.0125  0.0330  106 GLU K CB  
19813 C CG  . GLU K  106 ? 0.6059 0.5709 0.7171 0.0554  0.0125  0.0315  106 GLU K CG  
19814 C CD  . GLU K  106 ? 0.5977 0.5663 0.7011 0.0549  0.0094  0.0306  106 GLU K CD  
19815 O OE1 . GLU K  106 ? 0.5589 0.5298 0.6590 0.0565  0.0093  0.0316  106 GLU K OE1 
19816 O OE2 . GLU K  106 ? 0.5200 0.4893 0.6206 0.0527  0.0071  0.0288  106 GLU K OE2 
19817 N N   . LEU K  107 ? 0.5004 0.4658 0.6293 0.0535  0.0100  0.0353  107 LEU K N   
19818 C CA  . LEU K  107 ? 0.5632 0.5290 0.6947 0.0542  0.0104  0.0366  107 LEU K CA  
19819 C C   . LEU K  107 ? 0.4627 0.4311 0.5965 0.0509  0.0053  0.0364  107 LEU K C   
19820 O O   . LEU K  107 ? 0.4596 0.4297 0.5907 0.0512  0.0044  0.0368  107 LEU K O   
19821 C CB  . LEU K  107 ? 0.3564 0.3190 0.4962 0.0553  0.0141  0.0380  107 LEU K CB  
19822 C CG  . LEU K  107 ? 0.3725 0.3348 0.5155 0.0562  0.0155  0.0394  107 LEU K CG  
19823 C CD1 . LEU K  107 ? 0.4543 0.4178 0.5891 0.0587  0.0178  0.0396  107 LEU K CD1 
19824 C CD2 . LEU K  107 ? 0.4422 0.4011 0.5935 0.0572  0.0194  0.0407  107 LEU K CD2 
19825 N N   . ARG K  108 ? 0.3518 0.3204 0.4903 0.0478  0.0020  0.0359  108 ARG K N   
19826 C CA  . ARG K  108 ? 0.5187 0.4898 0.6600 0.0445  -0.0031 0.0360  108 ARG K CA  
19827 C C   . ARG K  108 ? 0.5850 0.5591 0.7177 0.0437  -0.0062 0.0349  108 ARG K C   
19828 O O   . ARG K  108 ? 0.4218 0.3980 0.5544 0.0427  -0.0088 0.0354  108 ARG K O   
19829 C CB  . ARG K  108 ? 0.4103 0.3814 0.5574 0.0411  -0.0060 0.0356  108 ARG K CB  
19830 C CG  . ARG K  108 ? 0.4250 0.3933 0.5807 0.0416  -0.0030 0.0365  108 ARG K CG  
19831 C CD  . ARG K  108 ? 0.4743 0.4426 0.6337 0.0381  -0.0056 0.0354  108 ARG K CD  
19832 N NE  . ARG K  108 ? 0.6047 0.5764 0.7662 0.0342  -0.0115 0.0356  108 ARG K NE  
19833 C CZ  . ARG K  108 ? 0.5566 0.5295 0.7273 0.0319  -0.0139 0.0372  108 ARG K CZ  
19834 N NH1 . ARG K  108 ? 0.4432 0.4139 0.6221 0.0331  -0.0107 0.0384  108 ARG K NH1 
19835 N NH2 . ARG K  108 ? 0.4966 0.4729 0.6685 0.0285  -0.0194 0.0376  108 ARG K NH2 
19836 N N   . GLU K  109 ? 0.5308 0.5050 0.6565 0.0442  -0.0059 0.0333  109 GLU K N   
19837 C CA  . GLU K  109 ? 0.4093 0.3862 0.5266 0.0436  -0.0084 0.0321  109 GLU K CA  
19838 C C   . GLU K  109 ? 0.4654 0.4435 0.5784 0.0460  -0.0068 0.0328  109 GLU K C   
19839 O O   . GLU K  109 ? 0.5491 0.5297 0.6588 0.0447  -0.0098 0.0325  109 GLU K O   
19840 C CB  . GLU K  109 ? 0.4958 0.4721 0.6071 0.0444  -0.0071 0.0305  109 GLU K CB  
19841 C CG  . GLU K  109 ? 0.7302 0.7074 0.8400 0.0407  -0.0110 0.0288  109 GLU K CG  
19842 C CD  . GLU K  109 ? 0.8125 0.7930 0.9167 0.0390  -0.0152 0.0281  109 GLU K CD  
19843 O OE1 . GLU K  109 ? 0.9629 0.9448 1.0697 0.0356  -0.0195 0.0281  109 GLU K OE1 
19844 O OE2 . GLU K  109 ? 0.8638 0.8455 0.9610 0.0410  -0.0141 0.0277  109 GLU K OE2 
19845 N N   . GLN K  110 ? 0.4398 0.4162 0.5529 0.0493  -0.0021 0.0337  110 GLN K N   
19846 C CA  . GLN K  110 ? 0.5519 0.5293 0.6607 0.0514  -0.0001 0.0342  110 GLN K CA  
19847 C C   . GLN K  110 ? 0.5344 0.5119 0.6482 0.0504  -0.0009 0.0352  110 GLN K C   
19848 O O   . GLN K  110 ? 0.7667 0.7459 0.8766 0.0506  -0.0012 0.0351  110 GLN K O   
19849 C CB  . GLN K  110 ? 0.5907 0.5661 0.6984 0.0550  0.0053  0.0351  110 GLN K CB  
19850 C CG  . GLN K  110 ? 0.6036 0.5780 0.7090 0.0562  0.0069  0.0346  110 GLN K CG  
19851 C CD  . GLN K  110 ? 0.7581 0.7341 0.8551 0.0590  0.0092  0.0346  110 GLN K CD  
19852 O OE1 . GLN K  110 ? 0.8256 0.8038 0.9178 0.0597  0.0091  0.0348  110 GLN K OE1 
19853 N NE2 . GLN K  110 ? 0.7053 0.6802 0.8006 0.0605  0.0112  0.0346  110 GLN K NE2 
19854 N N   . LEU K  111 ? 0.6172 0.5928 0.7401 0.0493  -0.0010 0.0363  111 LEU K N   
19855 C CA  . LEU K  111 ? 0.4949 0.4705 0.6242 0.0484  -0.0015 0.0375  111 LEU K CA  
19856 C C   . LEU K  111 ? 0.4802 0.4583 0.6109 0.0451  -0.0069 0.0375  111 LEU K C   
19857 O O   . LEU K  111 ? 0.6113 0.5899 0.7463 0.0444  -0.0076 0.0386  111 LEU K O   
19858 C CB  . LEU K  111 ? 0.4603 0.4331 0.5994 0.0487  0.0008  0.0390  111 LEU K CB  
19859 C CG  . LEU K  111 ? 0.4889 0.4590 0.6301 0.0514  0.0062  0.0400  111 LEU K CG  
19860 C CD1 . LEU K  111 ? 0.6753 0.6465 0.8082 0.0531  0.0081  0.0394  111 LEU K CD1 
19861 C CD2 . LEU K  111 ? 0.4819 0.4493 0.6246 0.0534  0.0100  0.0402  111 LEU K CD2 
19862 N N   . SER K  112 ? 0.4588 0.4385 0.5860 0.0433  -0.0104 0.0363  112 SER K N   
19863 C CA  . SER K  112 ? 0.4880 0.4701 0.6166 0.0399  -0.0158 0.0363  112 SER K CA  
19864 C C   . SER K  112 ? 0.5307 0.5147 0.6570 0.0396  -0.0171 0.0367  112 SER K C   
19865 O O   . SER K  112 ? 0.5955 0.5808 0.7269 0.0374  -0.0202 0.0380  112 SER K O   
19866 C CB  . SER K  112 ? 0.5219 0.5054 0.6445 0.0381  -0.0187 0.0345  112 SER K CB  
19867 O OG  . SER K  112 ? 0.6068 0.5914 0.7199 0.0396  -0.0179 0.0332  112 SER K OG  
19868 N N   . SER K  113 ? 0.5490 0.5333 0.6678 0.0416  -0.0147 0.0358  113 SER K N   
19869 C CA  . SER K  113 ? 0.4903 0.4760 0.6066 0.0414  -0.0153 0.0359  113 SER K CA  
19870 C C   . SER K  113 ? 0.6412 0.6258 0.7541 0.0443  -0.0103 0.0357  113 SER K C   
19871 O O   . SER K  113 ? 0.6943 0.6789 0.8009 0.0462  -0.0081 0.0347  113 SER K O   
19872 C CB  . SER K  113 ? 0.7048 0.6935 0.8134 0.0398  -0.0190 0.0344  113 SER K CB  
19873 O OG  . SER K  113 ? 0.6825 0.6725 0.7900 0.0391  -0.0199 0.0347  113 SER K OG  
19874 N N   . VAL K  114 ? 0.6196 0.6032 0.7368 0.0444  -0.0086 0.0367  114 VAL K N   
19875 C CA  . VAL K  114 ? 0.7209 0.7031 0.8356 0.0467  -0.0037 0.0365  114 VAL K CA  
19876 C C   . VAL K  114 ? 0.7055 0.6887 0.8179 0.0460  -0.0036 0.0361  114 VAL K C   
19877 O O   . VAL K  114 ? 0.6401 0.6234 0.7580 0.0442  -0.0057 0.0371  114 VAL K O   
19878 C CB  . VAL K  114 ? 0.7679 0.7468 0.8910 0.0480  0.0000  0.0380  114 VAL K CB  
19879 C CG1 . VAL K  114 ? 0.7913 0.7688 0.9173 0.0482  0.0030  0.0386  114 VAL K CG1 
19880 C CG2 . VAL K  114 ? 0.6436 0.6210 0.7636 0.0505  0.0037  0.0377  114 VAL K CG2 
19881 N N   . SER K  115 ? 0.8150 0.7990 0.9193 0.0472  -0.0012 0.0348  115 SER K N   
19882 C CA  . SER K  115 ? 0.9374 0.9224 1.0385 0.0464  -0.0007 0.0340  115 SER K CA  
19883 C C   . SER K  115 ? 0.8974 0.8794 1.0036 0.0470  0.0038  0.0348  115 SER K C   
19884 O O   . SER K  115 ? 1.0312 1.0125 1.1421 0.0456  0.0036  0.0353  115 SER K O   
19885 C CB  . SER K  115 ? 0.9956 0.9831 1.0856 0.0471  -0.0001 0.0322  115 SER K CB  
19886 O OG  . SER K  115 ? 1.1261 1.1150 1.2128 0.0456  -0.0008 0.0312  115 SER K OG  
19887 N N   . SER K  116 ? 1.0141 0.9943 1.1196 0.0491  0.0081  0.0348  116 SER K N   
19888 C CA  . SER K  116 ? 1.1100 1.0869 1.2210 0.0497  0.0127  0.0356  116 SER K CA  
19889 C C   . SER K  116 ? 1.1189 1.0933 1.2348 0.0515  0.0151  0.0368  116 SER K C   
19890 O O   . SER K  116 ? 1.1094 1.0845 1.2208 0.0529  0.0152  0.0366  116 SER K O   
19891 C CB  . SER K  116 ? 1.1298 1.1067 1.2334 0.0502  0.0166  0.0341  116 SER K CB  
19892 O OG  . SER K  116 ? 1.3167 1.2944 1.4133 0.0522  0.0187  0.0336  116 SER K OG  
19893 N N   . PHE K  117 ? 0.9147 0.8860 1.0401 0.0515  0.0173  0.0382  117 PHE K N   
19894 C CA  . PHE K  117 ? 0.7339 0.7028 0.8656 0.0528  0.0192  0.0396  117 PHE K CA  
19895 C C   . PHE K  117 ? 0.7570 0.7223 0.8959 0.0533  0.0240  0.0405  117 PHE K C   
19896 O O   . PHE K  117 ? 0.8626 0.8269 1.0102 0.0521  0.0233  0.0417  117 PHE K O   
19897 C CB  . PHE K  117 ? 0.6423 0.6121 0.7810 0.0515  0.0146  0.0407  117 PHE K CB  
19898 C CG  . PHE K  117 ? 0.6792 0.6471 0.8228 0.0527  0.0159  0.0417  117 PHE K CG  
19899 C CD1 . PHE K  117 ? 0.6614 0.6265 0.8152 0.0529  0.0184  0.0433  117 PHE K CD1 
19900 C CD2 . PHE K  117 ? 0.6776 0.6465 0.8160 0.0535  0.0147  0.0410  117 PHE K CD2 
19901 C CE1 . PHE K  117 ? 0.4974 0.4608 0.6560 0.0539  0.0196  0.0441  117 PHE K CE1 
19902 C CE2 . PHE K  117 ? 0.7375 0.7045 0.8805 0.0544  0.0161  0.0417  117 PHE K CE2 
19903 C CZ  . PHE K  117 ? 0.5516 0.5158 0.7046 0.0546  0.0185  0.0432  117 PHE K CZ  
19904 N N   . GLU K  118 ? 0.7894 0.7527 0.9246 0.0551  0.0290  0.0401  118 GLU K N   
19905 C CA  . GLU K  118 ? 0.8426 0.8020 0.9842 0.0557  0.0342  0.0409  118 GLU K CA  
19906 C C   . GLU K  118 ? 0.7312 0.6882 0.8753 0.0577  0.0374  0.0418  118 GLU K C   
19907 O O   . GLU K  118 ? 0.7658 0.7237 0.9027 0.0592  0.0378  0.0413  118 GLU K O   
19908 C CB  . GLU K  118 ? 1.0078 0.9664 1.1430 0.0555  0.0381  0.0394  118 GLU K CB  
19909 C CG  . GLU K  118 ? 1.1554 1.1141 1.2811 0.0572  0.0415  0.0384  118 GLU K CG  
19910 C CD  . GLU K  118 ? 1.4183 1.3746 1.5413 0.0571  0.0471  0.0374  118 GLU K CD  
19911 O OE1 . GLU K  118 ? 1.5154 1.4698 1.6438 0.0557  0.0485  0.0373  118 GLU K OE1 
19912 O OE2 . GLU K  118 ? 1.3859 1.3423 1.5014 0.0583  0.0502  0.0368  118 GLU K OE2 
19913 N N   . ARG K  119 ? 0.7541 0.7080 0.9088 0.0579  0.0396  0.0432  119 ARG K N   
19914 C CA  . ARG K  119 ? 0.7174 0.6686 0.8758 0.0596  0.0429  0.0442  119 ARG K CA  
19915 C C   . ARG K  119 ? 0.6913 0.6389 0.8495 0.0607  0.0495  0.0441  119 ARG K C   
19916 O O   . ARG K  119 ? 0.9114 0.8567 1.0761 0.0599  0.0519  0.0445  119 ARG K O   
19917 C CB  . ARG K  119 ? 0.6821 0.6325 0.8527 0.0589  0.0408  0.0460  119 ARG K CB  
19918 C CG  . ARG K  119 ? 0.6921 0.6387 0.8699 0.0604  0.0454  0.0472  119 ARG K CG  
19919 C CD  . ARG K  119 ? 0.8099 0.7543 0.9997 0.0595  0.0469  0.0487  119 ARG K CD  
19920 N NE  . ARG K  119 ? 0.8806 0.8235 1.0807 0.0598  0.0473  0.0503  119 ARG K NE  
19921 C CZ  . ARG K  119 ? 1.1032 1.0432 1.3138 0.0600  0.0506  0.0518  119 ARG K CZ  
19922 N NH1 . ARG K  119 ? 1.2059 1.1438 1.4182 0.0599  0.0543  0.0518  119 ARG K NH1 
19923 N NH2 . ARG K  119 ? 1.0037 0.9427 1.2233 0.0602  0.0506  0.0532  119 ARG K NH2 
19924 N N   . PHE K  120 ? 0.7358 0.6828 0.8863 0.0625  0.0527  0.0436  120 PHE K N   
19925 C CA  . PHE K  120 ? 0.7688 0.7125 0.9174 0.0634  0.0590  0.0433  120 PHE K CA  
19926 C C   . PHE K  120 ? 0.6970 0.6380 0.8482 0.0655  0.0625  0.0446  120 PHE K C   
19927 O O   . PHE K  120 ? 0.7391 0.6814 0.8896 0.0665  0.0601  0.0451  120 PHE K O   
19928 C CB  . PHE K  120 ? 0.7484 0.6942 0.8842 0.0634  0.0601  0.0417  120 PHE K CB  
19929 C CG  . PHE K  120 ? 0.6867 0.6353 0.8138 0.0649  0.0585  0.0417  120 PHE K CG  
19930 C CD1 . PHE K  120 ? 0.8574 0.8047 0.9798 0.0669  0.0627  0.0422  120 PHE K CD1 
19931 C CD2 . PHE K  120 ? 0.8222 0.7747 0.9459 0.0645  0.0529  0.0413  120 PHE K CD2 
19932 C CE1 . PHE K  120 ? 0.8361 0.7861 0.9510 0.0685  0.0614  0.0426  120 PHE K CE1 
19933 C CE2 . PHE K  120 ? 0.7857 0.7407 0.9019 0.0660  0.0518  0.0414  120 PHE K CE2 
19934 C CZ  . PHE K  120 ? 0.8386 0.7924 0.9507 0.0681  0.0560  0.0422  120 PHE K CZ  
19935 N N   . GLU K  121 ? 0.7587 0.6958 0.9129 0.0661  0.0682  0.0449  121 GLU K N   
19936 C CA  . GLU K  121 ? 0.7886 0.7228 0.9450 0.0681  0.0722  0.0460  121 GLU K CA  
19937 C C   . GLU K  121 ? 0.7616 0.6970 0.9059 0.0697  0.0740  0.0456  121 GLU K C   
19938 O O   . GLU K  121 ? 0.9186 0.8535 1.0559 0.0695  0.0775  0.0447  121 GLU K O   
19939 C CB  . GLU K  121 ? 0.8837 0.8130 1.0474 0.0681  0.0779  0.0465  121 GLU K CB  
19940 C CG  . GLU K  121 ? 0.9925 0.9185 1.1624 0.0698  0.0814  0.0480  121 GLU K CG  
19941 C CD  . GLU K  121 ? 1.1111 1.0324 1.2898 0.0696  0.0868  0.0485  121 GLU K CD  
19942 O OE1 . GLU K  121 ? 1.2749 1.1952 1.4522 0.0684  0.0891  0.0475  121 GLU K OE1 
19943 O OE2 . GLU K  121 ? 1.1338 1.0523 1.3207 0.0706  0.0889  0.0499  121 GLU K OE2 
19944 N N   . ILE K  122 ? 0.7732 0.7105 0.9151 0.0710  0.0715  0.0463  122 ILE K N   
19945 C CA  . ILE K  122 ? 0.7976 0.7366 0.9288 0.0728  0.0729  0.0465  122 ILE K CA  
19946 C C   . ILE K  122 ? 0.9335 0.8687 1.0649 0.0747  0.0790  0.0477  122 ILE K C   
19947 O O   . ILE K  122 ? 0.8882 0.8239 1.0108 0.0755  0.0821  0.0476  122 ILE K O   
19948 C CB  . ILE K  122 ? 0.7550 0.6970 0.8840 0.0737  0.0685  0.0469  122 ILE K CB  
19949 C CG1 . ILE K  122 ? 0.6838 0.6275 0.8026 0.0759  0.0703  0.0476  122 ILE K CG1 
19950 C CG2 . ILE K  122 ? 0.8343 0.7738 0.9735 0.0742  0.0680  0.0481  122 ILE K CG2 
19951 C CD1 . ILE K  122 ? 0.6482 0.5946 0.7646 0.0769  0.0667  0.0481  122 ILE K CD1 
19952 N N   . PHE K  123 ? 0.9642 0.8958 1.1058 0.0752  0.0807  0.0488  123 PHE K N   
19953 C CA  . PHE K  123 ? 0.8072 0.7347 0.9506 0.0769  0.0868  0.0499  123 PHE K CA  
19954 C C   . PHE K  123 ? 0.9575 0.8808 1.1122 0.0759  0.0897  0.0501  123 PHE K C   
19955 O O   . PHE K  123 ? 0.9542 0.8760 1.1191 0.0759  0.0887  0.0509  123 PHE K O   
19956 C CB  . PHE K  123 ? 0.8865 0.8134 1.0312 0.0791  0.0870  0.0515  123 PHE K CB  
19957 C CG  . PHE K  123 ? 0.8920 0.8226 1.0262 0.0805  0.0851  0.0518  123 PHE K CG  
19958 C CD1 . PHE K  123 ? 0.8352 0.7681 0.9702 0.0809  0.0808  0.0520  123 PHE K CD1 
19959 C CD2 . PHE K  123 ? 0.9232 0.8553 1.0468 0.0813  0.0877  0.0519  123 PHE K CD2 
19960 C CE1 . PHE K  123 ? 0.7817 0.7180 0.9077 0.0823  0.0794  0.0524  123 PHE K CE1 
19961 C CE2 . PHE K  123 ? 0.8435 0.7795 0.9581 0.0827  0.0859  0.0525  123 PHE K CE2 
19962 C CZ  . PHE K  123 ? 0.7956 0.7336 0.9115 0.0833  0.0818  0.0528  123 PHE K CZ  
19963 N N   . PRO K  124 ? 1.1022 1.0237 1.2552 0.0749  0.0934  0.0492  124 PRO K N   
19964 C CA  . PRO K  124 ? 1.1532 1.0704 1.3168 0.0741  0.0970  0.0494  124 PRO K CA  
19965 C C   . PRO K  124 ? 1.1752 1.0885 1.3460 0.0758  0.1009  0.0510  124 PRO K C   
19966 O O   . PRO K  124 ? 1.1787 1.0909 1.3433 0.0776  0.1042  0.0516  124 PRO K O   
19967 C CB  . PRO K  124 ? 1.2123 1.1280 1.3692 0.0732  0.1017  0.0481  124 PRO K CB  
19968 C CG  . PRO K  124 ? 1.1249 1.0453 1.2697 0.0726  0.0983  0.0468  124 PRO K CG  
19969 C CD  . PRO K  124 ? 1.0822 1.0056 1.2232 0.0744  0.0947  0.0479  124 PRO K CD  
19970 N N   . LYS K  125 ? 1.0925 1.0037 1.2762 0.0753  0.1005  0.0518  125 LYS K N   
19971 C CA  . LYS K  125 ? 1.1991 1.1070 1.3908 0.0767  0.1035  0.0533  125 LYS K CA  
19972 C C   . LYS K  125 ? 1.3551 1.2584 1.5452 0.0779  0.1111  0.0536  125 LYS K C   
19973 O O   . LYS K  125 ? 1.3366 1.2376 1.5277 0.0797  0.1140  0.0548  125 LYS K O   
19974 C CB  . LYS K  125 ? 1.1878 1.0949 1.3942 0.0755  0.1017  0.0541  125 LYS K CB  
19975 C CG  . LYS K  125 ? 1.1958 1.0997 1.4112 0.0768  0.1043  0.0555  125 LYS K CG  
19976 C CD  . LYS K  125 ? 1.0994 1.0042 1.3283 0.0754  0.1007  0.0564  125 LYS K CD  
19977 C CE  . LYS K  125 ? 1.1723 1.0757 1.4102 0.0740  0.1022  0.0567  125 LYS K CE  
19978 N NZ  . LYS K  125 ? 1.2439 1.1485 1.4956 0.0727  0.0987  0.0580  125 LYS K NZ  
19979 N N   . THR K  126 ? 1.9231 1.8248 2.1106 0.0768  0.1144  0.0525  126 THR K N   
19980 C CA  . THR K  126 ? 1.9910 1.8877 2.1791 0.0774  0.1219  0.0527  126 THR K CA  
19981 C C   . THR K  126 ? 2.0628 1.9594 2.2370 0.0781  0.1256  0.0521  126 THR K C   
19982 O O   . THR K  126 ? 2.2683 2.1608 2.4416 0.0781  0.1319  0.0520  126 THR K O   
19983 C CB  . THR K  126 ? 1.5404 1.4344 1.7356 0.0755  0.1247  0.0519  126 THR K CB  
19984 O OG1 . THR K  126 ? 1.6667 1.5643 1.8584 0.0737  0.1203  0.0505  126 THR K OG1 
19985 N N   . SER K  127 ? 1.4439 1.3449 1.6073 0.0785  0.1217  0.0519  127 SER K N   
19986 C CA  . SER K  127 ? 1.2638 1.1656 1.4139 0.0790  0.1246  0.0516  127 SER K CA  
19987 C C   . SER K  127 ? 1.1299 1.0353 1.2728 0.0811  0.1217  0.0530  127 SER K C   
19988 O O   . SER K  127 ? 1.3371 1.2431 1.4702 0.0822  0.1244  0.0536  127 SER K O   
19989 C CB  . SER K  127 ? 1.3335 1.2375 1.4757 0.0768  0.1239  0.0494  127 SER K CB  
19990 O OG  . SER K  127 ? 1.2318 1.1406 1.3734 0.0759  0.1171  0.0488  127 SER K OG  
19991 N N   . SER K  128 ? 1.1490 1.0566 1.2971 0.0816  0.1165  0.0535  128 SER K N   
19992 C CA  . SER K  128 ? 1.0888 1.0000 1.2306 0.0834  0.1133  0.0546  128 SER K CA  
19993 C C   . SER K  128 ? 1.0755 0.9838 1.2218 0.0858  0.1160  0.0566  128 SER K C   
19994 O O   . SER K  128 ? 1.1250 1.0349 1.2647 0.0877  0.1160  0.0580  128 SER K O   
19995 C CB  . SER K  128 ? 1.0632 0.9784 1.2072 0.0823  0.1062  0.0538  128 SER K CB  
19996 O OG  . SER K  128 ? 1.0437 0.9613 1.1841 0.0801  0.1039  0.0520  128 SER K OG  
19997 N N   . TRP K  129 ? 1.1232 1.0272 1.2811 0.0856  0.1184  0.0569  129 TRP K N   
19998 C CA  . TRP K  129 ? 1.1704 1.0715 1.3342 0.0875  0.1209  0.0587  129 TRP K CA  
19999 C C   . TRP K  129 ? 1.2871 1.1827 1.4560 0.0880  0.1278  0.0593  129 TRP K C   
20000 O O   . TRP K  129 ? 1.1430 1.0355 1.3236 0.0873  0.1289  0.0593  129 TRP K O   
20001 C CB  . TRP K  129 ? 1.1982 1.0999 1.3725 0.0869  0.1164  0.0586  129 TRP K CB  
20002 C CG  . TRP K  129 ? 0.9901 0.8969 1.1607 0.0856  0.1096  0.0574  129 TRP K CG  
20003 C CD1 . TRP K  129 ? 0.9838 0.8924 1.1598 0.0833  0.1053  0.0562  129 TRP K CD1 
20004 C CD2 . TRP K  129 ? 1.0038 0.9146 1.1646 0.0866  0.1064  0.0576  129 TRP K CD2 
20005 N NE1 . TRP K  129 ? 1.0617 0.9750 1.2315 0.0827  0.0997  0.0554  129 TRP K NE1 
20006 C CE2 . TRP K  129 ? 1.0004 0.9151 1.1610 0.0847  0.1003  0.0562  129 TRP K CE2 
20007 C CE3 . TRP K  129 ? 0.9741 0.8857 1.1266 0.0890  0.1082  0.0590  129 TRP K CE3 
20008 C CZ2 . TRP K  129 ? 1.0464 0.9656 1.1988 0.0850  0.0961  0.0559  129 TRP K CZ2 
20009 C CZ3 . TRP K  129 ? 0.8401 0.7563 0.9849 0.0894  0.1040  0.0589  129 TRP K CZ3 
20010 C CH2 . TRP K  129 ? 0.9091 0.8289 1.0538 0.0874  0.0981  0.0573  129 TRP K CH2 
20011 N N   . PRO K  130 ? 1.4012 1.2956 1.5610 0.0891  0.1325  0.0600  130 PRO K N   
20012 C CA  . PRO K  130 ? 1.2841 1.1731 1.4461 0.0894  0.1396  0.0605  130 PRO K CA  
20013 C C   . PRO K  130 ? 1.3892 1.2751 1.5549 0.0919  0.1431  0.0626  130 PRO K C   
20014 O O   . PRO K  130 ? 1.5261 1.4071 1.6962 0.0923  0.1489  0.0632  130 PRO K O   
20015 C CB  . PRO K  130 ? 1.3642 1.2547 1.5126 0.0892  0.1421  0.0601  130 PRO K CB  
20016 C CG  . PRO K  130 ? 1.2726 1.1693 1.4124 0.0887  0.1360  0.0594  130 PRO K CG  
20017 C CD  . PRO K  130 ? 1.3578 1.2564 1.5037 0.0897  0.1310  0.0601  130 PRO K CD  
20018 N N   . ASN K  131 ? 1.2871 1.1756 1.4511 0.0935  0.1398  0.0638  131 ASN K N   
20019 C CA  . ASN K  131 ? 1.3798 1.2653 1.5468 0.0959  0.1430  0.0659  131 ASN K CA  
20020 C C   . ASN K  131 ? 1.2716 1.1567 1.4502 0.0958  0.1400  0.0658  131 ASN K C   
20021 O O   . ASN K  131 ? 1.2909 1.1739 1.4728 0.0976  0.1419  0.0673  131 ASN K O   
20022 C CB  . ASN K  131 ? 1.4592 1.3475 1.6147 0.0982  0.1429  0.0676  131 ASN K CB  
20023 C CG  . ASN K  131 ? 1.5854 1.4743 1.7295 0.0983  0.1464  0.0681  131 ASN K CG  
20024 O OD1 . ASN K  131 ? 1.6315 1.5172 1.7766 0.0971  0.1506  0.0673  131 ASN K OD1 
20025 N ND2 . ASN K  131 ? 1.6355 1.5286 1.7686 0.0997  0.1449  0.0694  131 ASN K ND2 
20026 N N   . HIS K  132 ? 1.1218 1.0089 1.3063 0.0935  0.1352  0.0641  132 HIS K N   
20027 C CA  . HIS K  132 ? 1.0074 0.8947 1.2024 0.0928  0.1316  0.0638  132 HIS K CA  
20028 C C   . HIS K  132 ? 1.0127 0.8993 1.2183 0.0904  0.1302  0.0626  132 HIS K C   
20029 O O   . HIS K  132 ? 1.1237 1.0109 1.3270 0.0890  0.1302  0.0616  132 HIS K O   
20030 C CB  . HIS K  132 ? 0.9231 0.8153 1.1129 0.0927  0.1253  0.0633  132 HIS K CB  
20031 C CG  . HIS K  132 ? 1.0307 0.9245 1.2095 0.0951  0.1263  0.0646  132 HIS K CG  
20032 N ND1 . HIS K  132 ? 1.0163 0.9093 1.1959 0.0969  0.1268  0.0659  132 HIS K ND1 
20033 C CD2 . HIS K  132 ? 0.8998 0.7959 1.0664 0.0959  0.1269  0.0650  132 HIS K CD2 
20034 C CE1 . HIS K  132 ? 0.9388 0.8338 1.1078 0.0990  0.1277  0.0673  132 HIS K CE1 
20035 N NE2 . HIS K  132 ? 0.7825 0.6796 0.9433 0.0983  0.1276  0.0668  132 HIS K NE2 
20036 N N   . ASP K  133 ? 0.8149 0.7003 1.0323 0.0897  0.1290  0.0628  133 ASP K N   
20037 C CA  . ASP K  133 ? 1.0422 0.9275 1.2709 0.0875  0.1274  0.0621  133 ASP K CA  
20038 C C   . ASP K  133 ? 1.0006 0.8908 1.2293 0.0854  0.1199  0.0610  133 ASP K C   
20039 O O   . ASP K  133 ? 0.9167 0.8094 1.1458 0.0852  0.1157  0.0608  133 ASP K O   
20040 C CB  . ASP K  133 ? 1.0548 0.9369 1.2966 0.0874  0.1294  0.0629  133 ASP K CB  
20041 C CG  . ASP K  133 ? 1.1932 1.0745 1.4473 0.0855  0.1292  0.0628  133 ASP K CG  
20042 O OD1 . ASP K  133 ? 1.1226 1.0074 1.3781 0.0836  0.1243  0.0620  133 ASP K OD1 
20043 O OD2 . ASP K  133 ? 1.4494 1.3266 1.7120 0.0859  0.1342  0.0636  133 ASP K OD2 
20044 N N   . SER K  134 ? 0.9721 0.8638 1.2002 0.0839  0.1184  0.0601  134 SER K N   
20045 C CA  . SER K  134 ? 0.9997 0.8961 1.2274 0.0819  0.1116  0.0591  134 SER K CA  
20046 C C   . SER K  134 ? 0.9225 0.8191 1.1635 0.0798  0.1096  0.0593  134 SER K C   
20047 O O   . SER K  134 ? 1.0637 0.9632 1.3051 0.0781  0.1055  0.0587  134 SER K O   
20048 C CB  . SER K  134 ? 1.0086 0.9071 1.2249 0.0816  0.1109  0.0581  134 SER K CB  
20049 O OG  . SER K  134 ? 1.1216 1.0171 1.3385 0.0815  0.1160  0.0580  134 SER K OG  
20050 N N   . ASN K  135 ? 0.9944 0.8879 1.2465 0.0800  0.1124  0.0603  135 ASN K N   
20051 C CA  . ASN K  135 ? 1.0288 0.9225 1.2946 0.0782  0.1110  0.0610  135 ASN K CA  
20052 C C   . ASN K  135 ? 1.0623 0.9566 1.3386 0.0774  0.1087  0.0617  135 ASN K C   
20053 O O   . ASN K  135 ? 1.2860 1.1827 1.5724 0.0754  0.1048  0.0622  135 ASN K O   
20054 C CB  . ASN K  135 ? 1.1564 1.0456 1.4277 0.0787  0.1176  0.0616  135 ASN K CB  
20055 C CG  . ASN K  135 ? 1.1857 1.0746 1.4482 0.0787  0.1197  0.0606  135 ASN K CG  
20056 O OD1 . ASN K  135 ? 0.9884 0.8808 1.2477 0.0773  0.1153  0.0599  135 ASN K OD1 
20057 N ND2 . ASN K  135 ? 1.1427 1.0273 1.4011 0.0801  0.1265  0.0606  135 ASN K ND2 
20058 N N   . LYS K  136 ? 0.9764 0.8687 1.2504 0.0789  0.1110  0.0618  136 LYS K N   
20059 C CA  . LYS K  136 ? 1.1512 1.0433 1.4351 0.0782  0.1099  0.0623  136 LYS K CA  
20060 C C   . LYS K  136 ? 1.1248 1.0211 1.4061 0.0767  0.1032  0.0614  136 LYS K C   
20061 O O   . LYS K  136 ? 1.1384 1.0349 1.4263 0.0757  0.1018  0.0614  136 LYS K O   
20062 C CB  . LYS K  136 ? 1.3443 1.2317 1.6276 0.0804  0.1161  0.0628  136 LYS K CB  
20063 C CG  . LYS K  136 ? 1.3469 1.2297 1.6332 0.0817  0.1231  0.0637  136 LYS K CG  
20064 C CD  . LYS K  136 ? 1.4659 1.3452 1.7636 0.0820  0.1271  0.0646  136 LYS K CD  
20065 C CE  . LYS K  136 ? 1.7477 1.6233 2.0523 0.0824  0.1327  0.0654  136 LYS K CE  
20066 N NZ  . LYS K  136 ? 1.6833 1.5616 1.9938 0.0804  0.1294  0.0655  136 LYS K NZ  
20067 N N   . GLY K  137 ? 1.0517 0.9513 1.3232 0.0764  0.0992  0.0605  137 GLY K N   
20068 C CA  . GLY K  137 ? 0.9517 0.8551 1.2189 0.0751  0.0933  0.0595  137 GLY K CA  
20069 C C   . GLY K  137 ? 0.9353 0.8429 1.2100 0.0720  0.0868  0.0594  137 GLY K C   
20070 O O   . GLY K  137 ? 0.8658 0.7770 1.1352 0.0709  0.0823  0.0587  137 GLY K O   
20071 N N   . VAL K  138 ? 0.9383 0.8456 1.2254 0.0705  0.0864  0.0601  138 VAL K N   
20072 C CA  . VAL K  138 ? 0.8909 0.8025 1.1862 0.0673  0.0802  0.0604  138 VAL K CA  
20073 C C   . VAL K  138 ? 0.9109 0.8232 1.2119 0.0656  0.0781  0.0600  138 VAL K C   
20074 O O   . VAL K  138 ? 0.9034 0.8125 1.2035 0.0670  0.0821  0.0596  138 VAL K O   
20075 C CB  . VAL K  138 ? 1.0015 0.9128 1.3084 0.0667  0.0815  0.0621  138 VAL K CB  
20076 C CG1 . VAL K  138 ? 0.9540 0.8642 1.2552 0.0681  0.0840  0.0622  138 VAL K CG1 
20077 C CG2 . VAL K  138 ? 0.9519 0.8593 1.2687 0.0675  0.0869  0.0631  138 VAL K CG2 
20078 N N   . THR K  139 ? 0.7742 0.6909 1.0811 0.0625  0.0719  0.0600  139 THR K N   
20079 C CA  . THR K  139 ? 0.8826 0.8004 1.1942 0.0602  0.0694  0.0593  139 THR K CA  
20080 C C   . THR K  139 ? 1.0137 0.9362 1.3356 0.0566  0.0634  0.0602  139 THR K C   
20081 O O   . THR K  139 ? 0.9162 0.8420 1.2386 0.0556  0.0598  0.0611  139 THR K O   
20082 C CB  . THR K  139 ? 0.9243 0.8430 1.2244 0.0601  0.0670  0.0572  139 THR K CB  
20083 O OG1 . THR K  139 ? 0.8647 0.7850 1.1698 0.0572  0.0639  0.0563  139 THR K OG1 
20084 C CG2 . THR K  139 ? 0.9168 0.8392 1.2084 0.0594  0.0621  0.0567  139 THR K CG2 
20085 N N   . ALA K  140 ? 1.2475 1.1707 1.5777 0.0544  0.0625  0.0600  140 ALA K N   
20086 C CA  . ALA K  140 ? 1.1602 1.0884 1.5000 0.0506  0.0564  0.0609  140 ALA K CA  
20087 C C   . ALA K  140 ? 1.2995 1.2319 1.6320 0.0479  0.0498  0.0593  140 ALA K C   
20088 O O   . ALA K  140 ? 1.2696 1.2062 1.6084 0.0442  0.0446  0.0596  140 ALA K O   
20089 C CB  . ALA K  140 ? 1.2038 1.1312 1.5553 0.0490  0.0579  0.0613  140 ALA K CB  
20090 N N   . ALA K  141 ? 1.3341 1.2653 1.6532 0.0496  0.0502  0.0577  141 ALA K N   
20091 C CA  . ALA K  141 ? 1.2410 1.1758 1.5518 0.0474  0.0444  0.0561  141 ALA K CA  
20092 C C   . ALA K  141 ? 1.1124 1.0516 1.4237 0.0461  0.0394  0.0575  141 ALA K C   
20093 O O   . ALA K  141 ? 1.1408 1.0845 1.4583 0.0427  0.0338  0.0583  141 ALA K O   
20094 C CB  . ALA K  141 ? 1.1917 1.1238 1.4887 0.0499  0.0469  0.0542  141 ALA K CB  
20095 N N   . CYS K  142 ? 0.8598 0.7976 1.1642 0.0489  0.0415  0.0578  142 CYS K N   
20096 C CA  . CYS K  142 ? 1.0404 0.9816 1.3455 0.0482  0.0378  0.0592  142 CYS K CA  
20097 C C   . CYS K  142 ? 1.0191 0.9589 1.3343 0.0495  0.0413  0.0617  142 CYS K C   
20098 O O   . CYS K  142 ? 0.8145 0.7510 1.1257 0.0524  0.0460  0.0618  142 CYS K O   
20099 C CB  . CYS K  142 ? 1.2638 1.2047 1.5553 0.0500  0.0378  0.0579  142 CYS K CB  
20100 S SG  . CYS K  142 ? 0.9688 0.9045 1.2491 0.0538  0.0443  0.0561  142 CYS K SG  
20101 N N   . PRO K  143 ? 1.1293 1.0717 1.4577 0.0473  0.0389  0.0636  143 PRO K N   
20102 C CA  . PRO K  143 ? 1.1280 1.0694 1.4677 0.0482  0.0420  0.0662  143 PRO K CA  
20103 C C   . PRO K  143 ? 1.3417 1.2865 1.6836 0.0476  0.0386  0.0681  143 PRO K C   
20104 O O   . PRO K  143 ? 1.4145 1.3643 1.7567 0.0448  0.0319  0.0686  143 PRO K O   
20105 C CB  . PRO K  143 ? 1.1950 1.1387 1.5481 0.0456  0.0401  0.0675  143 PRO K CB  
20106 C CG  . PRO K  143 ? 1.1237 1.0703 1.4716 0.0426  0.0348  0.0656  143 PRO K CG  
20107 C CD  . PRO K  143 ? 1.1201 1.0672 1.4534 0.0433  0.0327  0.0637  143 PRO K CD  
20108 N N   . HIS K  144 ? 1.3161 1.2578 1.6601 0.0501  0.0435  0.0692  144 HIS K N   
20109 C CA  . HIS K  144 ? 1.4369 1.3800 1.7832 0.0503  0.0428  0.0710  144 HIS K CA  
20110 C C   . HIS K  144 ? 1.5492 1.4904 1.9096 0.0512  0.0472  0.0736  144 HIS K C   
20111 O O   . HIS K  144 ? 1.4756 1.4118 1.8376 0.0535  0.0539  0.0733  144 HIS K O   
20112 C CB  . HIS K  144 ? 1.2848 1.2253 1.6162 0.0524  0.0451  0.0688  144 HIS K CB  
20113 C CG  . HIS K  144 ? 1.4193 1.3598 1.7501 0.0532  0.0461  0.0698  144 HIS K CG  
20114 N ND1 . HIS K  144 ? 1.4969 1.4331 1.8312 0.0554  0.0527  0.0704  144 HIS K ND1 
20115 C CD2 . HIS K  144 ? 1.4449 1.3883 1.7701 0.0523  0.0419  0.0697  144 HIS K CD2 
20116 C CE1 . HIS K  144 ? 1.5331 1.4697 1.8651 0.0555  0.0525  0.0709  144 HIS K CE1 
20117 N NE2 . HIS K  144 ? 1.4131 1.3541 1.7397 0.0537  0.0460  0.0705  144 HIS K NE2 
20118 N N   . ALA K  145 ? 1.5132 1.4587 1.8842 0.0494  0.0431  0.0764  145 ALA K N   
20119 C CA  . ALA K  145 ? 1.4850 1.4299 1.8711 0.0498  0.0462  0.0794  145 ALA K CA  
20120 C C   . ALA K  145 ? 1.6183 1.5620 2.0130 0.0495  0.0484  0.0797  145 ALA K C   
20121 O O   . ALA K  145 ? 1.5461 1.4862 1.9490 0.0512  0.0542  0.0808  145 ALA K O   
20122 C CB  . ALA K  145 ? 1.3594 1.2992 1.7434 0.0527  0.0531  0.0792  145 ALA K CB  
20123 N N   . GLY K  146 ? 1.8512 1.7977 2.2440 0.0473  0.0439  0.0785  146 GLY K N   
20124 C CA  . GLY K  146 ? 1.7979 1.7431 2.1977 0.0468  0.0461  0.0783  146 GLY K CA  
20125 C C   . GLY K  146 ? 1.7876 1.7258 2.1817 0.0501  0.0540  0.0764  146 GLY K C   
20126 O O   . GLY K  146 ? 1.7115 1.6471 2.1107 0.0505  0.0576  0.0761  146 GLY K O   
20127 N N   . ALA K  147 ? 1.5986 1.5339 1.9816 0.0523  0.0567  0.0751  147 ALA K N   
20128 C CA  . ALA K  147 ? 1.5151 1.4441 1.8902 0.0554  0.0640  0.0733  147 ALA K CA  
20129 C C   . ALA K  147 ? 1.4090 1.3372 1.7698 0.0558  0.0629  0.0703  147 ALA K C   
20130 O O   . ALA K  147 ? 1.3089 1.2401 1.6610 0.0548  0.0581  0.0693  147 ALA K O   
20131 C CB  . ALA K  147 ? 1.3995 1.3261 1.7708 0.0574  0.0675  0.0735  147 ALA K CB  
20132 N N   . LYS K  148 ? 1.2411 1.1653 1.6000 0.0572  0.0676  0.0691  148 LYS K N   
20133 C CA  . LYS K  148 ? 1.1545 1.0768 1.5001 0.0582  0.0683  0.0665  148 LYS K CA  
20134 C C   . LYS K  148 ? 1.1396 1.0614 1.4722 0.0599  0.0687  0.0655  148 LYS K C   
20135 O O   . LYS K  148 ? 0.9304 0.8486 1.2610 0.0621  0.0740  0.0658  148 LYS K O   
20136 C CB  . LYS K  148 ? 1.0422 0.9591 1.3883 0.0605  0.0753  0.0660  148 LYS K CB  
20137 C CG  . LYS K  148 ? 1.3066 1.2231 1.6663 0.0593  0.0764  0.0671  148 LYS K CG  
20138 C CD  . LYS K  148 ? 1.2268 1.1412 1.5829 0.0594  0.0778  0.0654  148 LYS K CD  
20139 C CE  . LYS K  148 ? 1.2421 1.1515 1.5866 0.0628  0.0837  0.0642  148 LYS K CE  
20140 N NZ  . LYS K  148 ? 1.3236 1.2314 1.6631 0.0629  0.0844  0.0625  148 LYS K NZ  
20141 N N   . SER K  149 ? 1.1795 1.1046 1.5032 0.0586  0.0633  0.0642  149 SER K N   
20142 C CA  . SER K  149 ? 1.0872 1.0123 1.3986 0.0599  0.0633  0.0632  149 SER K CA  
20143 C C   . SER K  149 ? 1.0920 1.0172 1.3903 0.0605  0.0621  0.0610  149 SER K C   
20144 O O   . SER K  149 ? 1.0150 0.9389 1.3128 0.0607  0.0631  0.0602  149 SER K O   
20145 C CB  . SER K  149 ? 1.1693 1.0988 1.4826 0.0580  0.0579  0.0641  149 SER K CB  
20146 O OG  . SER K  149 ? 1.2353 1.1637 1.5402 0.0595  0.0597  0.0636  149 SER K OG  
20147 N N   . PHE K  150 ? 1.0729 0.9997 1.3607 0.0609  0.0601  0.0600  150 PHE K N   
20148 C CA  . PHE K  150 ? 0.8671 0.7942 1.1419 0.0617  0.0592  0.0581  150 PHE K CA  
20149 C C   . PHE K  150 ? 0.8431 0.7732 1.1094 0.0612  0.0555  0.0575  150 PHE K C   
20150 O O   . PHE K  150 ? 0.9609 0.8925 1.2315 0.0603  0.0541  0.0585  150 PHE K O   
20151 C CB  . PHE K  150 ? 0.8037 0.7262 1.0723 0.0649  0.0660  0.0577  150 PHE K CB  
20152 C CG  . PHE K  150 ? 0.7828 0.7053 1.0399 0.0660  0.0657  0.0562  150 PHE K CG  
20153 C CD1 . PHE K  150 ? 0.7500 0.6728 1.0085 0.0651  0.0640  0.0555  150 PHE K CD1 
20154 C CD2 . PHE K  150 ? 0.6912 0.6134 0.9364 0.0680  0.0673  0.0555  150 PHE K CD2 
20155 C CE1 . PHE K  150 ? 0.6003 0.5229 0.8487 0.0662  0.0641  0.0543  150 PHE K CE1 
20156 C CE2 . PHE K  150 ? 0.7432 0.6658 0.9785 0.0692  0.0671  0.0545  150 PHE K CE2 
20157 C CZ  . PHE K  150 ? 0.6887 0.6113 0.9257 0.0684  0.0656  0.0539  150 PHE K CZ  
20158 N N   . TYR K  151 ? 0.8078 0.7389 1.0625 0.0617  0.0539  0.0559  151 TYR K N   
20159 C CA  . TYR K  151 ? 0.6842 0.6183 0.9301 0.0612  0.0505  0.0551  151 TYR K CA  
20160 C C   . TYR K  151 ? 0.6413 0.5735 0.8838 0.0630  0.0545  0.0553  151 TYR K C   
20161 O O   . TYR K  151 ? 0.8346 0.7633 1.0745 0.0653  0.0602  0.0554  151 TYR K O   
20162 C CB  . TYR K  151 ? 0.6856 0.6206 0.9197 0.0618  0.0490  0.0533  151 TYR K CB  
20163 C CG  . TYR K  151 ? 0.6004 0.5365 0.8369 0.0601  0.0459  0.0527  151 TYR K CG  
20164 C CD1 . TYR K  151 ? 0.5035 0.4436 0.7418 0.0570  0.0395  0.0523  151 TYR K CD1 
20165 C CD2 . TYR K  151 ? 0.6013 0.5345 0.8380 0.0615  0.0495  0.0523  151 TYR K CD2 
20166 C CE1 . TYR K  151 ? 0.6237 0.5647 0.8637 0.0551  0.0368  0.0514  151 TYR K CE1 
20167 C CE2 . TYR K  151 ? 0.5233 0.4572 0.7620 0.0597  0.0470  0.0515  151 TYR K CE2 
20168 C CZ  . TYR K  151 ? 0.6218 0.5597 0.8621 0.0564  0.0407  0.0509  151 TYR K CZ  
20169 O OH  . TYR K  151 ? 0.6708 0.6094 0.9128 0.0542  0.0383  0.0498  151 TYR K OH  
20170 N N   . LYS K  152 ? 0.7091 0.6437 0.9513 0.0617  0.0517  0.0555  152 LYS K N   
20171 C CA  . LYS K  152 ? 0.8004 0.7333 1.0397 0.0629  0.0555  0.0556  152 LYS K CA  
20172 C C   . LYS K  152 ? 0.7092 0.6417 0.9344 0.0646  0.0575  0.0540  152 LYS K C   
20173 O O   . LYS K  152 ? 0.7364 0.6660 0.9582 0.0663  0.0628  0.0538  152 LYS K O   
20174 C CB  . LYS K  152 ? 0.8260 0.7617 1.0688 0.0609  0.0518  0.0562  152 LYS K CB  
20175 C CG  . LYS K  152 ? 1.1887 1.1253 1.4459 0.0592  0.0498  0.0583  152 LYS K CG  
20176 C CD  . LYS K  152 ? 1.5127 1.4452 1.7790 0.0606  0.0558  0.0596  152 LYS K CD  
20177 C CE  . LYS K  152 ? 1.5890 1.5229 1.8704 0.0589  0.0537  0.0619  152 LYS K CE  
20178 N NZ  . LYS K  152 ? 1.4897 1.4195 1.7806 0.0602  0.0598  0.0632  152 LYS K NZ  
20179 N N   . ASN K  153 ? 0.6770 0.6125 0.8942 0.0641  0.0532  0.0528  153 ASN K N   
20180 C CA  . ASN K  153 ? 0.7759 0.7120 0.9798 0.0656  0.0542  0.0515  153 ASN K CA  
20181 C C   . ASN K  153 ? 0.7298 0.6637 0.9288 0.0679  0.0581  0.0514  153 ASN K C   
20182 O O   . ASN K  153 ? 0.6226 0.5573 0.8109 0.0693  0.0590  0.0506  153 ASN K O   
20183 C CB  . ASN K  153 ? 0.6459 0.5863 0.8434 0.0640  0.0482  0.0504  153 ASN K CB  
20184 C CG  . ASN K  153 ? 0.7440 0.6867 0.9451 0.0618  0.0446  0.0506  153 ASN K CG  
20185 O OD1 . ASN K  153 ? 0.8822 0.8233 1.0878 0.0619  0.0473  0.0513  153 ASN K OD1 
20186 N ND2 . ASN K  153 ? 0.7435 0.6898 0.9426 0.0600  0.0387  0.0501  153 ASN K ND2 
20187 N N   . LEU K  154 ? 0.7445 0.6758 0.9516 0.0684  0.0603  0.0523  154 LEU K N   
20188 C CA  . LEU K  154 ? 0.7247 0.6534 0.9283 0.0707  0.0645  0.0525  154 LEU K CA  
20189 C C   . LEU K  154 ? 0.7712 0.6955 0.9829 0.0719  0.0701  0.0537  154 LEU K C   
20190 O O   . LEU K  154 ? 0.8812 0.8049 1.1035 0.0705  0.0698  0.0544  154 LEU K O   
20191 C CB  . LEU K  154 ? 0.7465 0.6763 0.9508 0.0702  0.0614  0.0521  154 LEU K CB  
20192 C CG  . LEU K  154 ? 0.5771 0.5108 0.7731 0.0692  0.0562  0.0508  154 LEU K CG  
20193 C CD1 . LEU K  154 ? 0.6783 0.6126 0.8769 0.0681  0.0535  0.0503  154 LEU K CD1 
20194 C CD2 . LEU K  154 ? 0.6537 0.5881 0.8376 0.0714  0.0583  0.0504  154 LEU K CD2 
20195 N N   . ILE K  155 ? 0.8010 0.7226 1.0079 0.0744  0.0752  0.0541  155 ILE K N   
20196 C CA  . ILE K  155 ? 0.9111 0.8283 1.1249 0.0756  0.0809  0.0552  155 ILE K CA  
20197 C C   . ILE K  155 ? 0.7485 0.6635 0.9627 0.0772  0.0833  0.0557  155 ILE K C   
20198 O O   . ILE K  155 ? 0.6273 0.5426 0.8323 0.0790  0.0845  0.0557  155 ILE K O   
20199 C CB  . ILE K  155 ? 0.9289 0.8439 1.1370 0.0771  0.0862  0.0554  155 ILE K CB  
20200 C CG1 . ILE K  155 ? 1.0057 0.9221 1.2142 0.0754  0.0846  0.0548  155 ILE K CG1 
20201 C CG2 . ILE K  155 ? 0.7713 0.6815 0.9861 0.0784  0.0924  0.0565  155 ILE K CG2 
20202 C CD1 . ILE K  155 ? 1.0986 1.0129 1.3012 0.0764  0.0898  0.0546  155 ILE K CD1 
20203 N N   . TRP K  156 ? 0.6612 0.5742 0.8865 0.0765  0.0841  0.0563  156 TRP K N   
20204 C CA  . TRP K  156 ? 0.7178 0.6284 0.9448 0.0778  0.0866  0.0567  156 TRP K CA  
20205 C C   . TRP K  156 ? 0.7699 0.6759 0.9967 0.0803  0.0939  0.0579  156 TRP K C   
20206 O O   . TRP K  156 ? 0.9201 0.8232 1.1564 0.0801  0.0970  0.0586  156 TRP K O   
20207 C CB  . TRP K  156 ? 0.7944 0.7050 1.0334 0.0756  0.0842  0.0566  156 TRP K CB  
20208 C CG  . TRP K  156 ? 0.7453 0.6538 0.9857 0.0764  0.0862  0.0566  156 TRP K CG  
20209 C CD1 . TRP K  156 ? 0.6945 0.6007 0.9277 0.0791  0.0902  0.0570  156 TRP K CD1 
20210 C CD2 . TRP K  156 ? 0.8149 0.7233 1.0648 0.0744  0.0843  0.0563  156 TRP K CD2 
20211 N NE1 . TRP K  156 ? 0.6256 0.5300 0.8633 0.0791  0.0912  0.0569  156 TRP K NE1 
20212 C CE2 . TRP K  156 ? 0.6600 0.5656 0.9078 0.0760  0.0876  0.0562  156 TRP K CE2 
20213 C CE3 . TRP K  156 ? 0.7687 0.6792 1.0287 0.0712  0.0801  0.0561  156 TRP K CE3 
20214 C CZ2 . TRP K  156 ? 0.7193 0.6240 0.9746 0.0744  0.0871  0.0557  156 TRP K CZ2 
20215 C CZ3 . TRP K  156 ? 0.8350 0.7451 1.1023 0.0695  0.0793  0.0557  156 TRP K CZ3 
20216 C CH2 . TRP K  156 ? 0.8793 0.7864 1.1441 0.0711  0.0828  0.0553  156 TRP K CH2 
20217 N N   . LEU K  157 ? 0.6502 0.5559 0.8662 0.0826  0.0965  0.0581  157 LEU K N   
20218 C CA  . LEU K  157 ? 0.6009 0.5026 0.8150 0.0851  0.1033  0.0594  157 LEU K CA  
20219 C C   . LEU K  157 ? 0.7949 0.6930 1.0153 0.0863  0.1069  0.0603  157 LEU K C   
20220 O O   . LEU K  157 ? 0.8189 0.7176 1.0379 0.0866  0.1053  0.0601  157 LEU K O   
20221 C CB  . LEU K  157 ? 0.6215 0.5244 0.8220 0.0871  0.1047  0.0597  157 LEU K CB  
20222 C CG  . LEU K  157 ? 0.7102 0.6159 0.9037 0.0862  0.1031  0.0589  157 LEU K CG  
20223 C CD1 . LEU K  157 ? 0.7186 0.6252 0.8993 0.0883  0.1055  0.0595  157 LEU K CD1 
20224 C CD2 . LEU K  157 ? 0.8641 0.7673 1.0641 0.0851  0.1058  0.0587  157 LEU K CD2 
20225 N N   . VAL K  158 ? 0.8683 0.7623 1.0955 0.0868  0.1119  0.0611  158 VAL K N   
20226 C CA  . VAL K  158 ? 0.8465 0.7367 1.0798 0.0880  0.1161  0.0621  158 VAL K CA  
20227 C C   . VAL K  158 ? 0.8780 0.7642 1.1070 0.0906  0.1232  0.0635  158 VAL K C   
20228 O O   . VAL K  158 ? 0.8252 0.7116 1.0481 0.0910  0.1247  0.0635  158 VAL K O   
20229 C CB  . VAL K  158 ? 0.8917 0.7805 1.1395 0.0860  0.1157  0.0619  158 VAL K CB  
20230 C CG1 . VAL K  158 ? 0.8639 0.7567 1.1158 0.0832  0.1087  0.0607  158 VAL K CG1 
20231 C CG2 . VAL K  158 ? 0.9615 0.8488 1.2141 0.0854  0.1181  0.0622  158 VAL K CG2 
20232 N N   . LYS K  159 ? 1.0372 0.9198 1.2692 0.0923  0.1275  0.0646  159 LYS K N   
20233 C CA  . LYS K  159 ? 1.1674 1.0462 1.3952 0.0949  0.1344  0.0662  159 LYS K CA  
20234 C C   . LYS K  159 ? 1.1386 1.0146 1.3719 0.0942  0.1381  0.0662  159 LYS K C   
20235 O O   . LYS K  159 ? 1.0537 0.9288 1.2985 0.0924  0.1373  0.0657  159 LYS K O   
20236 C CB  . LYS K  159 ? 1.1810 1.0561 1.4124 0.0967  0.1383  0.0673  159 LYS K CB  
20237 C CG  . LYS K  159 ? 1.1603 1.0325 1.4059 0.0952  0.1396  0.0670  159 LYS K CG  
20238 C CD  . LYS K  159 ? 1.2062 1.0744 1.4547 0.0971  0.1444  0.0682  159 LYS K CD  
20239 C CE  . LYS K  159 ? 1.1687 1.0339 1.4314 0.0956  0.1462  0.0679  159 LYS K CE  
20240 N NZ  . LYS K  159 ? 1.3573 1.2184 1.6232 0.0974  0.1510  0.0689  159 LYS K NZ  
20241 N N   . LYS K  160 ? 1.2372 1.1119 1.4622 0.0955  0.1421  0.0669  160 LYS K N   
20242 C CA  . LYS K  160 ? 1.4061 1.2776 1.6352 0.0949  0.1466  0.0669  160 LYS K CA  
20243 C C   . LYS K  160 ? 1.5444 1.4104 1.7779 0.0967  0.1536  0.0683  160 LYS K C   
20244 O O   . LYS K  160 ? 1.3690 1.2331 1.5940 0.0988  0.1580  0.0696  160 LYS K O   
20245 C CB  . LYS K  160 ? 1.2588 1.1316 1.4766 0.0950  0.1475  0.0665  160 LYS K CB  
20246 C CG  . LYS K  160 ? 1.3761 1.2450 1.5968 0.0944  0.1531  0.0664  160 LYS K CG  
20247 C CD  . LYS K  160 ? 1.4726 1.3429 1.6815 0.0940  0.1539  0.0657  160 LYS K CD  
20248 C CE  . LYS K  160 ? 1.4599 1.3354 1.6657 0.0922  0.1472  0.0641  160 LYS K CE  
20249 N NZ  . LYS K  160 ? 1.5414 1.4179 1.7379 0.0912  0.1484  0.0630  160 LYS K NZ  
20250 N N   . GLY K  161 ? 1.4745 1.3381 1.7213 0.0958  0.1545  0.0683  161 GLY K N   
20251 C CA  . GLY K  161 ? 1.4035 1.2618 1.6559 0.0972  0.1611  0.0695  161 GLY K CA  
20252 C C   . GLY K  161 ? 1.5074 1.3640 1.7530 0.0999  0.1641  0.0711  161 GLY K C   
20253 O O   . GLY K  161 ? 1.5067 1.3602 1.7465 0.1018  0.1699  0.0724  161 GLY K O   
20254 N N   . ASN K  162 ? 1.4744 1.3331 1.7208 0.1001  0.1605  0.0710  162 ASN K N   
20255 C CA  . ASN K  162 ? 1.5435 1.4005 1.7850 0.1027  0.1633  0.0726  162 ASN K CA  
20256 C C   . ASN K  162 ? 1.4070 1.2666 1.6336 0.1046  0.1629  0.0736  162 ASN K C   
20257 O O   . ASN K  162 ? 1.4659 1.3236 1.6869 0.1072  0.1671  0.0756  162 ASN K O   
20258 C CB  . ASN K  162 ? 1.6605 1.5116 1.9069 0.1043  0.1708  0.0741  162 ASN K CB  
20259 C CG  . ASN K  162 ? 1.7809 1.6296 2.0388 0.1039  0.1714  0.0739  162 ASN K CG  
20260 O OD1 . ASN K  162 ? 2.0082 1.8522 2.2713 0.1051  0.1773  0.0750  162 ASN K OD1 
20261 N ND2 . ASN K  162 ? 1.7154 1.5675 1.9772 0.1021  0.1655  0.0724  162 ASN K ND2 
20262 N N   . SER K  163 ? 1.5101 1.3743 1.7306 0.1032  0.1578  0.0724  163 SER K N   
20263 C CA  . SER K  163 ? 1.4995 1.3669 1.7061 0.1047  0.1569  0.0733  163 SER K CA  
20264 C C   . SER K  163 ? 1.3911 1.2642 1.5932 0.1032  0.1497  0.0718  163 SER K C   
20265 O O   . SER K  163 ? 1.3561 1.2311 1.5605 0.1008  0.1464  0.0700  163 SER K O   
20266 C CB  . SER K  163 ? 1.3865 1.2526 1.5863 0.1051  0.1612  0.0739  163 SER K CB  
20267 O OG  . SER K  163 ? 1.2189 1.0878 1.4053 0.1068  0.1611  0.0753  163 SER K OG  
20268 N N   . TYR K  164 ? 1.2290 1.1048 1.4249 0.1047  0.1474  0.0725  164 TYR K N   
20269 C CA  . TYR K  164 ? 1.0617 0.9429 1.2516 0.1036  0.1410  0.0713  164 TYR K CA  
20270 C C   . TYR K  164 ? 1.0148 0.8987 1.1920 0.1060  0.1415  0.0732  164 TYR K C   
20271 O O   . TYR K  164 ? 0.8260 0.7108 1.0014 0.1076  0.1408  0.0742  164 TYR K O   
20272 C CB  . TYR K  164 ? 1.0956 0.9780 1.2923 0.1023  0.1365  0.0700  164 TYR K CB  
20273 C CG  . TYR K  164 ? 1.0855 0.9731 1.2786 0.1003  0.1296  0.0682  164 TYR K CG  
20274 C CD1 . TYR K  164 ? 1.0520 0.9407 1.2531 0.0973  0.1253  0.0662  164 TYR K CD1 
20275 C CD2 . TYR K  164 ? 1.0162 0.9078 1.1980 0.1014  0.1273  0.0687  164 TYR K CD2 
20276 C CE1 . TYR K  164 ? 0.9821 0.8755 1.1799 0.0954  0.1190  0.0646  164 TYR K CE1 
20277 C CE2 . TYR K  164 ? 0.8865 0.7827 1.0650 0.0995  0.1212  0.0670  164 TYR K CE2 
20278 C CZ  . TYR K  164 ? 1.0019 0.8989 1.1883 0.0965  0.1171  0.0649  164 TYR K CZ  
20279 O OH  . TYR K  164 ? 0.8552 0.7567 1.0383 0.0947  0.1110  0.0633  164 TYR K OH  
20280 N N   . PRO K  165 ? 0.9007 0.7860 1.0693 0.1061  0.1428  0.0736  165 PRO K N   
20281 C CA  . PRO K  165 ? 1.0207 0.9092 1.1769 0.1082  0.1432  0.0755  165 PRO K CA  
20282 C C   . PRO K  165 ? 1.0558 0.9501 1.2065 0.1074  0.1367  0.0745  165 PRO K C   
20283 O O   . PRO K  165 ? 0.9518 0.8478 1.1059 0.1048  0.1323  0.0720  165 PRO K O   
20284 C CB  . PRO K  165 ? 0.8538 0.7421 1.0040 0.1074  0.1460  0.0754  165 PRO K CB  
20285 C CG  . PRO K  165 ? 1.0589 0.9425 1.2193 0.1057  0.1486  0.0740  165 PRO K CG  
20286 C CD  . PRO K  165 ? 0.8896 0.7735 1.0603 0.1042  0.1443  0.0722  165 PRO K CD  
20287 N N   . LYS K  166 ? 0.9308 0.8282 1.0734 0.1096  0.1363  0.0765  166 LYS K N   
20288 C CA  . LYS K  166 ? 0.9589 0.8619 1.0955 0.1090  0.1306  0.0756  166 LYS K CA  
20289 C C   . LYS K  166 ? 1.0718 0.9778 1.2040 0.1064  0.1276  0.0735  166 LYS K C   
20290 O O   . LYS K  166 ? 0.9545 0.8610 1.0799 0.1065  0.1301  0.0742  166 LYS K O   
20291 C CB  . LYS K  166 ? 0.8668 0.7729 0.9940 0.1120  0.1314  0.0786  166 LYS K CB  
20292 C CG  . LYS K  166 ? 1.0247 0.9373 1.1439 0.1112  0.1260  0.0778  166 LYS K CG  
20293 C CD  . LYS K  166 ? 1.2689 1.1852 1.3783 0.1140  0.1271  0.0811  166 LYS K CD  
20294 C CE  . LYS K  166 ? 1.3319 1.2476 1.4442 0.1167  0.1276  0.0831  166 LYS K CE  
20295 N NZ  . LYS K  166 ? 1.4116 1.3318 1.5146 0.1194  0.1280  0.0865  166 LYS K NZ  
20296 N N   . LEU K  167 ? 1.1014 1.0093 1.2373 0.1040  0.1224  0.0709  167 LEU K N   
20297 C CA  . LEU K  167 ? 1.0194 0.9302 1.1516 0.1015  0.1193  0.0689  167 LEU K CA  
20298 C C   . LEU K  167 ? 0.9288 0.8457 1.0516 0.1016  0.1148  0.0688  167 LEU K C   
20299 O O   . LEU K  167 ? 0.8586 0.7773 0.9809 0.1029  0.1126  0.0695  167 LEU K O   
20300 C CB  . LEU K  167 ? 0.8357 0.7449 0.9779 0.0987  0.1166  0.0663  167 LEU K CB  
20301 C CG  . LEU K  167 ? 0.8589 0.7716 1.0031 0.0965  0.1099  0.0642  167 LEU K CG  
20302 C CD1 . LEU K  167 ? 0.8414 0.7512 0.9980 0.0945  0.1089  0.0628  167 LEU K CD1 
20303 C CD2 . LEU K  167 ? 1.0081 0.9241 1.1485 0.0976  0.1065  0.0647  167 LEU K CD2 
20304 N N   . SER K  168 ? 0.8918 0.8117 1.0071 0.1002  0.1137  0.0678  168 SER K N   
20305 C CA  . SER K  168 ? 0.9886 0.9145 1.0945 0.1003  0.1097  0.0679  168 SER K CA  
20306 C C   . SER K  168 ? 1.0451 0.9738 1.1468 0.0975  0.1070  0.0654  168 SER K C   
20307 O O   . SER K  168 ? 1.2931 1.2234 1.3868 0.0972  0.1088  0.0657  168 SER K O   
20308 C CB  . SER K  168 ? 1.1028 1.0307 1.1997 0.1031  0.1127  0.0710  168 SER K CB  
20309 O OG  . SER K  168 ? 1.2918 1.2254 1.3820 0.1038  0.1088  0.0716  168 SER K OG  
20310 N N   . LYS K  169 ? 0.8083 0.7375 0.9154 0.0952  0.1027  0.0631  169 LYS K N   
20311 C CA  . LYS K  169 ? 0.9425 0.8742 1.0464 0.0925  0.0997  0.0607  169 LYS K CA  
20312 C C   . LYS K  169 ? 0.9495 0.8869 1.0477 0.0922  0.0942  0.0601  169 LYS K C   
20313 O O   . LYS K  169 ? 0.9599 0.8982 1.0601 0.0933  0.0919  0.0608  169 LYS K O   
20314 C CB  . LYS K  169 ? 0.8621 0.7907 0.9764 0.0902  0.0987  0.0588  169 LYS K CB  
20315 C CG  . LYS K  169 ? 1.0960 1.0213 1.2121 0.0888  0.1028  0.0580  169 LYS K CG  
20316 C CD  . LYS K  169 ? 1.1492 1.0777 1.2569 0.0869  0.1016  0.0563  169 LYS K CD  
20317 C CE  . LYS K  169 ? 1.2788 1.2036 1.3902 0.0850  0.1052  0.0550  169 LYS K CE  
20318 N NZ  . LYS K  169 ? 1.2820 1.2025 1.3936 0.0863  0.1117  0.0564  169 LYS K NZ  
20319 N N   . SER K  170 ? 1.0259 0.9669 1.1168 0.0905  0.0924  0.0588  170 SER K N   
20320 C CA  . SER K  170 ? 1.0087 0.9551 1.0940 0.0899  0.0872  0.0580  170 SER K CA  
20321 C C   . SER K  170 ? 0.8455 0.7941 0.9274 0.0869  0.0849  0.0554  170 SER K C   
20322 O O   . SER K  170 ? 0.8921 0.8408 0.9687 0.0860  0.0877  0.0550  170 SER K O   
20323 C CB  . SER K  170 ? 0.9810 0.9315 1.0572 0.0922  0.0876  0.0603  170 SER K CB  
20324 O OG  . SER K  170 ? 1.4338 1.3850 1.5027 0.0924  0.0913  0.0611  170 SER K OG  
20325 N N   . TYR K  171 ? 0.8126 0.7628 0.8975 0.0852  0.0800  0.0537  171 TYR K N   
20326 C CA  . TYR K  171 ? 0.8784 0.8306 0.9610 0.0824  0.0776  0.0513  171 TYR K CA  
20327 C C   . TYR K  171 ? 0.8678 0.8261 0.9418 0.0821  0.0734  0.0508  171 TYR K C   
20328 O O   . TYR K  171 ? 0.7767 0.7371 0.8502 0.0834  0.0706  0.0517  171 TYR K O   
20329 C CB  . TYR K  171 ? 0.9114 0.8610 1.0040 0.0805  0.0751  0.0498  171 TYR K CB  
20330 C CG  . TYR K  171 ? 0.8291 0.7816 0.9197 0.0778  0.0710  0.0477  171 TYR K CG  
20331 C CD1 . TYR K  171 ? 0.7626 0.7140 0.8531 0.0758  0.0727  0.0461  171 TYR K CD1 
20332 C CD2 . TYR K  171 ? 0.8578 0.8140 0.9470 0.0774  0.0657  0.0471  171 TYR K CD2 
20333 C CE1 . TYR K  171 ? 0.7859 0.7397 0.8748 0.0734  0.0692  0.0442  171 TYR K CE1 
20334 C CE2 . TYR K  171 ? 0.8567 0.8155 0.9441 0.0750  0.0620  0.0452  171 TYR K CE2 
20335 C CZ  . TYR K  171 ? 0.9015 0.8591 0.9888 0.0731  0.0638  0.0438  171 TYR K CZ  
20336 O OH  . TYR K  171 ? 0.9710 0.9309 1.0567 0.0707  0.0603  0.0420  171 TYR K OH  
20337 N N   . ILE K  172 ? 0.8333 0.7941 0.9005 0.0802  0.0731  0.0493  172 ILE K N   
20338 C CA  . ILE K  172 ? 0.8388 0.8055 0.8980 0.0796  0.0692  0.0486  172 ILE K CA  
20339 C C   . ILE K  172 ? 0.9131 0.8807 0.9739 0.0766  0.0655  0.0459  172 ILE K C   
20340 O O   . ILE K  172 ? 0.9098 0.8749 0.9729 0.0746  0.0673  0.0444  172 ILE K O   
20341 C CB  . ILE K  172 ? 0.8939 0.8642 0.9424 0.0798  0.0714  0.0492  172 ILE K CB  
20342 C CG1 . ILE K  172 ? 0.9505 0.9273 0.9910 0.0793  0.0672  0.0488  172 ILE K CG1 
20343 C CG2 . ILE K  172 ? 1.0806 1.0485 1.1276 0.0774  0.0748  0.0475  172 ILE K CG2 
20344 C CD1 . ILE K  172 ? 0.9835 0.9646 1.0162 0.0817  0.0681  0.0514  172 ILE K CD1 
20345 N N   . ASN K  173 ? 0.8865 0.8575 0.9464 0.0764  0.0607  0.0454  173 ASN K N   
20346 C CA  . ASN K  173 ? 0.8226 0.7944 0.8843 0.0737  0.0568  0.0432  173 ASN K CA  
20347 C C   . ASN K  173 ? 0.9649 0.9397 1.0191 0.0716  0.0568  0.0414  173 ASN K C   
20348 O O   . ASN K  173 ? 0.8344 0.8143 0.8808 0.0715  0.0545  0.0411  173 ASN K O   
20349 C CB  . ASN K  173 ? 0.7750 0.7497 0.8371 0.0740  0.0518  0.0431  173 ASN K CB  
20350 C CG  . ASN K  173 ? 0.9259 0.9008 0.9915 0.0713  0.0478  0.0411  173 ASN K CG  
20351 O OD1 . ASN K  173 ? 0.8704 0.8436 0.9383 0.0694  0.0487  0.0399  173 ASN K OD1 
20352 N ND2 . ASN K  173 ? 0.8689 0.8460 0.9350 0.0712  0.0435  0.0409  173 ASN K ND2 
20353 N N   . ASP K  174 ? 1.1122 1.0837 1.1688 0.0698  0.0597  0.0401  174 ASP K N   
20354 C CA  . ASP K  174 ? 0.9739 0.9475 1.0239 0.0674  0.0604  0.0381  174 ASP K CA  
20355 C C   . ASP K  174 ? 1.0388 1.0132 1.0913 0.0650  0.0565  0.0361  174 ASP K C   
20356 O O   . ASP K  174 ? 1.2379 1.2140 1.2855 0.0628  0.0565  0.0341  174 ASP K O   
20357 C CB  . ASP K  174 ? 1.0857 1.0551 1.1367 0.0666  0.0660  0.0376  174 ASP K CB  
20358 C CG  . ASP K  174 ? 1.3634 1.3270 1.4260 0.0663  0.0675  0.0376  174 ASP K CG  
20359 O OD1 . ASP K  174 ? 1.3705 1.3325 1.4365 0.0640  0.0673  0.0359  174 ASP K OD1 
20360 O OD2 . ASP K  174 ? 1.3708 1.3316 1.4395 0.0683  0.0688  0.0395  174 ASP K OD2 
20361 N N   . LYS K  175 ? 0.9729 0.9461 1.0329 0.0654  0.0532  0.0366  175 LYS K N   
20362 C CA  . LYS K  175 ? 1.0114 0.9855 1.0742 0.0633  0.0491  0.0351  175 LYS K CA  
20363 C C   . LYS K  175 ? 1.0854 1.0653 1.1402 0.0628  0.0450  0.0343  175 LYS K C   
20364 O O   . LYS K  175 ? 1.1107 1.0938 1.1586 0.0644  0.0452  0.0352  175 LYS K O   
20365 C CB  . LYS K  175 ? 0.8878 0.8594 0.9609 0.0636  0.0466  0.0361  175 LYS K CB  
20366 C CG  . LYS K  175 ? 0.8767 0.8431 0.9589 0.0642  0.0504  0.0372  175 LYS K CG  
20367 C CD  . LYS K  175 ? 0.7882 0.7517 0.8744 0.0622  0.0527  0.0360  175 LYS K CD  
20368 C CE  . LYS K  175 ? 0.8125 0.7709 0.9089 0.0628  0.0562  0.0373  175 LYS K CE  
20369 N NZ  . LYS K  175 ? 1.0954 1.0508 1.1968 0.0610  0.0587  0.0364  175 LYS K NZ  
20370 N N   . GLY K  176 ? 0.7332 0.7142 0.7890 0.0608  0.0414  0.0328  176 GLY K N   
20371 C CA  . GLY K  176 ? 1.0514 1.0375 1.1003 0.0602  0.0374  0.0319  176 GLY K CA  
20372 C C   . GLY K  176 ? 1.0852 1.0721 1.1381 0.0606  0.0328  0.0326  176 GLY K C   
20373 O O   . GLY K  176 ? 1.0716 1.0620 1.1207 0.0597  0.0290  0.0316  176 GLY K O   
20374 N N   . LYS K  177 ? 1.0067 0.9902 1.0672 0.0619  0.0334  0.0340  177 LYS K N   
20375 C CA  . LYS K  177 ? 0.8741 0.8575 0.9393 0.0620  0.0295  0.0345  177 LYS K CA  
20376 C C   . LYS K  177 ? 0.7567 0.7377 0.8261 0.0644  0.0314  0.0364  177 LYS K C   
20377 O O   . LYS K  177 ? 0.8955 0.8740 0.9663 0.0656  0.0357  0.0373  177 LYS K O   
20378 C CB  . LYS K  177 ? 0.8270 0.8082 0.9002 0.0598  0.0276  0.0340  177 LYS K CB  
20379 C CG  . LYS K  177 ? 0.8633 0.8400 0.9437 0.0598  0.0315  0.0346  177 LYS K CG  
20380 C CD  . LYS K  177 ? 0.8472 0.8222 0.9351 0.0576  0.0297  0.0343  177 LYS K CD  
20381 C CE  . LYS K  177 ? 0.9714 0.9483 1.0547 0.0555  0.0289  0.0326  177 LYS K CE  
20382 N NZ  . LYS K  177 ? 0.9863 0.9622 1.0650 0.0555  0.0338  0.0317  177 LYS K NZ  
20383 N N   . GLU K  178 ? 0.6659 0.6476 0.7371 0.0649  0.0285  0.0368  178 GLU K N   
20384 C CA  . GLU K  178 ? 0.7163 0.6954 0.7919 0.0669  0.0302  0.0384  178 GLU K CA  
20385 C C   . GLU K  178 ? 0.8049 0.7794 0.8897 0.0666  0.0326  0.0390  178 GLU K C   
20386 O O   . GLU K  178 ? 0.7574 0.7308 0.8470 0.0645  0.0314  0.0383  178 GLU K O   
20387 C CB  . GLU K  178 ? 0.6939 0.6739 0.7711 0.0666  0.0264  0.0382  178 GLU K CB  
20388 C CG  . GLU K  178 ? 1.0244 1.0089 1.0933 0.0671  0.0241  0.0377  178 GLU K CG  
20389 C CD  . GLU K  178 ? 1.1325 1.1175 1.2032 0.0662  0.0203  0.0371  178 GLU K CD  
20390 O OE1 . GLU K  178 ? 1.0751 1.0590 1.1508 0.0639  0.0175  0.0363  178 GLU K OE1 
20391 O OE2 . GLU K  178 ? 1.1798 1.1664 1.2468 0.0678  0.0204  0.0376  178 GLU K OE2 
20392 N N   . VAL K  179 ? 0.6409 0.6127 0.7286 0.0686  0.0361  0.0405  179 VAL K N   
20393 C CA  . VAL K  179 ? 0.6488 0.6162 0.7458 0.0685  0.0385  0.0412  179 VAL K CA  
20394 C C   . VAL K  179 ? 0.6542 0.6196 0.7572 0.0694  0.0380  0.0421  179 VAL K C   
20395 O O   . VAL K  179 ? 0.6232 0.5885 0.7234 0.0715  0.0398  0.0431  179 VAL K O   
20396 C CB  . VAL K  179 ? 0.6539 0.6189 0.7497 0.0699  0.0441  0.0420  179 VAL K CB  
20397 C CG1 . VAL K  179 ? 0.6392 0.5995 0.7450 0.0703  0.0469  0.0430  179 VAL K CG1 
20398 C CG2 . VAL K  179 ? 0.6671 0.6333 0.7588 0.0684  0.0449  0.0407  179 VAL K CG2 
20399 N N   . LEU K  180 ? 0.5056 0.4695 0.6170 0.0675  0.0357  0.0420  180 LEU K N   
20400 C CA  . LEU K  180 ? 0.5329 0.4948 0.6507 0.0678  0.0352  0.0426  180 LEU K CA  
20401 C C   . LEU K  180 ? 0.5681 0.5259 0.6922 0.0692  0.0400  0.0439  180 LEU K C   
20402 O O   . LEU K  180 ? 0.6637 0.6195 0.7943 0.0683  0.0412  0.0442  180 LEU K O   
20403 C CB  . LEU K  180 ? 0.5162 0.4786 0.6406 0.0650  0.0305  0.0420  180 LEU K CB  
20404 C CG  . LEU K  180 ? 0.5136 0.4741 0.6452 0.0645  0.0296  0.0424  180 LEU K CG  
20405 C CD1 . LEU K  180 ? 0.5580 0.5199 0.6843 0.0651  0.0282  0.0418  180 LEU K CD1 
20406 C CD2 . LEU K  180 ? 0.4370 0.3980 0.5762 0.0615  0.0255  0.0422  180 LEU K CD2 
20407 N N   . VAL K  181 ? 0.5674 0.5239 0.6900 0.0716  0.0429  0.0449  181 VAL K N   
20408 C CA  . VAL K  181 ? 0.6400 0.5925 0.7682 0.0731  0.0477  0.0462  181 VAL K CA  
20409 C C   . VAL K  181 ? 0.6352 0.5854 0.7708 0.0729  0.0472  0.0465  181 VAL K C   
20410 O O   . VAL K  181 ? 0.6371 0.5883 0.7700 0.0735  0.0461  0.0464  181 VAL K O   
20411 C CB  . VAL K  181 ? 0.5375 0.4897 0.6587 0.0760  0.0522  0.0473  181 VAL K CB  
20412 C CG1 . VAL K  181 ? 0.5442 0.4919 0.6712 0.0774  0.0574  0.0487  181 VAL K CG1 
20413 C CG2 . VAL K  181 ? 0.5118 0.4667 0.6247 0.0758  0.0524  0.0468  181 VAL K CG2 
20414 N N   . LEU K  182 ? 0.6055 0.5529 0.7508 0.0719  0.0482  0.0470  182 LEU K N   
20415 C CA  . LEU K  182 ? 0.5743 0.5196 0.7273 0.0715  0.0481  0.0472  182 LEU K CA  
20416 C C   . LEU K  182 ? 0.5362 0.4774 0.6938 0.0736  0.0538  0.0486  182 LEU K C   
20417 O O   . LEU K  182 ? 0.6416 0.5810 0.8005 0.0743  0.0571  0.0493  182 LEU K O   
20418 C CB  . LEU K  182 ? 0.3957 0.3416 0.5571 0.0684  0.0439  0.0467  182 LEU K CB  
20419 C CG  . LEU K  182 ? 0.5367 0.4865 0.6942 0.0661  0.0380  0.0454  182 LEU K CG  
20420 C CD1 . LEU K  182 ? 0.5615 0.5131 0.7194 0.0645  0.0358  0.0453  182 LEU K CD1 
20421 C CD2 . LEU K  182 ? 0.5230 0.4731 0.6861 0.0638  0.0343  0.0448  182 LEU K CD2 
20422 N N   . TRP K  183 ? 0.4720 0.4114 0.6317 0.0745  0.0550  0.0489  183 TRP K N   
20423 C CA  . TRP K  183 ? 0.5106 0.4458 0.6748 0.0764  0.0604  0.0502  183 TRP K CA  
20424 C C   . TRP K  183 ? 0.4879 0.4214 0.6587 0.0757  0.0600  0.0500  183 TRP K C   
20425 O O   . TRP K  183 ? 0.5049 0.4403 0.6744 0.0741  0.0561  0.0488  183 TRP K O   
20426 C CB  . TRP K  183 ? 0.6961 0.6309 0.8518 0.0797  0.0647  0.0514  183 TRP K CB  
20427 C CG  . TRP K  183 ? 0.5472 0.4832 0.6975 0.0811  0.0642  0.0515  183 TRP K CG  
20428 C CD1 . TRP K  183 ? 0.6014 0.5347 0.7547 0.0824  0.0668  0.0521  183 TRP K CD1 
20429 C CD2 . TRP K  183 ? 0.5945 0.5345 0.7357 0.0814  0.0613  0.0509  183 TRP K CD2 
20430 N NE1 . TRP K  183 ? 0.5345 0.4697 0.6813 0.0835  0.0658  0.0520  183 TRP K NE1 
20431 C CE2 . TRP K  183 ? 0.5876 0.5270 0.7270 0.0830  0.0624  0.0513  183 TRP K CE2 
20432 C CE3 . TRP K  183 ? 0.6260 0.5699 0.7606 0.0805  0.0582  0.0501  183 TRP K CE3 
20433 C CZ2 . TRP K  183 ? 0.5931 0.5358 0.7247 0.0837  0.0604  0.0511  183 TRP K CZ2 
20434 C CZ3 . TRP K  183 ? 0.5835 0.5308 0.7102 0.0811  0.0560  0.0498  183 TRP K CZ3 
20435 C CH2 . TRP K  183 ? 0.5610 0.5077 0.6863 0.0827  0.0571  0.0503  183 TRP K CH2 
20436 N N   . GLY K  184 ? 0.4718 0.4015 0.6493 0.0767  0.0643  0.0509  184 GLY K N   
20437 C CA  . GLY K  184 ? 0.5005 0.4281 0.6846 0.0758  0.0644  0.0506  184 GLY K CA  
20438 C C   . GLY K  184 ? 0.4955 0.4194 0.6799 0.0786  0.0702  0.0518  184 GLY K C   
20439 O O   . GLY K  184 ? 0.5255 0.4475 0.7083 0.0810  0.0747  0.0532  184 GLY K O   
20440 N N   . ILE K  185 ? 0.4910 0.4137 0.6774 0.0783  0.0702  0.0512  185 ILE K N   
20441 C CA  . ILE K  185 ? 0.4755 0.3942 0.6634 0.0807  0.0757  0.0523  185 ILE K CA  
20442 C C   . ILE K  185 ? 0.4866 0.4027 0.6855 0.0786  0.0762  0.0516  185 ILE K C   
20443 O O   . ILE K  185 ? 0.5810 0.4981 0.7826 0.0760  0.0728  0.0500  185 ILE K O   
20444 C CB  . ILE K  185 ? 0.5993 0.5184 0.7803 0.0824  0.0763  0.0522  185 ILE K CB  
20445 C CG1 . ILE K  185 ? 0.5490 0.4717 0.7193 0.0840  0.0750  0.0528  185 ILE K CG1 
20446 C CG2 . ILE K  185 ? 0.5248 0.4397 0.7075 0.0852  0.0825  0.0538  185 ILE K CG2 
20447 C CD1 . ILE K  185 ? 0.4970 0.4192 0.6636 0.0867  0.0788  0.0548  185 ILE K CD1 
20448 N N   . HIS K  186 ? 0.5481 0.4608 0.7532 0.0797  0.0805  0.0529  186 HIS K N   
20449 C CA  . HIS K  186 ? 0.6470 0.5574 0.8632 0.0776  0.0811  0.0524  186 HIS K CA  
20450 C C   . HIS K  186 ? 0.5416 0.4483 0.7593 0.0790  0.0853  0.0525  186 HIS K C   
20451 O O   . HIS K  186 ? 0.5892 0.4934 0.8030 0.0824  0.0904  0.0541  186 HIS K O   
20452 C CB  . HIS K  186 ? 0.5757 0.4842 0.7991 0.0779  0.0837  0.0536  186 HIS K CB  
20453 C CG  . HIS K  186 ? 0.6908 0.5969 0.9260 0.0760  0.0848  0.0533  186 HIS K CG  
20454 N ND1 . HIS K  186 ? 0.7118 0.6135 0.9519 0.0779  0.0908  0.0545  186 HIS K ND1 
20455 C CD2 . HIS K  186 ? 0.7177 0.6257 0.9609 0.0723  0.0805  0.0521  186 HIS K CD2 
20456 C CE1 . HIS K  186 ? 0.7860 0.6868 1.0366 0.0754  0.0902  0.0538  186 HIS K CE1 
20457 N NE2 . HIS K  186 ? 0.7164 0.6211 0.9691 0.0719  0.0840  0.0525  186 HIS K NE2 
20458 N N   . HIS K  187 ? 0.5764 0.4829 0.7996 0.0761  0.0832  0.0508  187 HIS K N   
20459 C CA  . HIS K  187 ? 0.5924 0.4952 0.8183 0.0768  0.0872  0.0505  187 HIS K CA  
20460 C C   . HIS K  187 ? 0.7112 0.6117 0.9490 0.0746  0.0884  0.0501  187 HIS K C   
20461 O O   . HIS K  187 ? 0.7172 0.6193 0.9605 0.0707  0.0843  0.0484  187 HIS K O   
20462 C CB  . HIS K  187 ? 0.5948 0.4989 0.8167 0.0750  0.0842  0.0485  187 HIS K CB  
20463 C CG  . HIS K  187 ? 0.6716 0.5785 0.8825 0.0768  0.0825  0.0487  187 HIS K CG  
20464 N ND1 . HIS K  187 ? 0.7382 0.6435 0.9423 0.0805  0.0866  0.0501  187 HIS K ND1 
20465 C CD2 . HIS K  187 ? 0.7070 0.6183 0.9126 0.0753  0.0770  0.0479  187 HIS K CD2 
20466 C CE1 . HIS K  187 ? 0.7961 0.7050 0.9915 0.0812  0.0837  0.0501  187 HIS K CE1 
20467 N NE2 . HIS K  187 ? 0.7399 0.6523 0.9359 0.0781  0.0779  0.0486  187 HIS K NE2 
20468 N N   . PRO K  188 ? 0.6058 0.5025 0.8475 0.0770  0.0941  0.0519  188 PRO K N   
20469 C CA  . PRO K  188 ? 0.7197 0.6139 0.9730 0.0754  0.0961  0.0518  188 PRO K CA  
20470 C C   . PRO K  188 ? 0.7725 0.6651 1.0305 0.0730  0.0962  0.0499  188 PRO K C   
20471 O O   . PRO K  188 ? 0.7059 0.5978 0.9580 0.0737  0.0968  0.0491  188 PRO K O   
20472 C CB  . PRO K  188 ? 0.7040 0.5940 0.9575 0.0793  0.1031  0.0540  188 PRO K CB  
20473 C CG  . PRO K  188 ? 0.7297 0.6213 0.9729 0.0822  0.1033  0.0554  188 PRO K CG  
20474 C CD  . PRO K  188 ? 0.6214 0.5163 0.8565 0.0814  0.0990  0.0541  188 PRO K CD  
20475 N N   . SER K  189 ? 0.8213 0.7133 1.0901 0.0702  0.0958  0.0492  189 SER K N   
20476 C CA  . SER K  189 ? 0.8041 0.6949 1.0782 0.0671  0.0956  0.0472  189 SER K CA  
20477 C C   . SER K  189 ? 0.8851 0.7702 1.1613 0.0696  0.1029  0.0477  189 SER K C   
20478 O O   . SER K  189 ? 0.9871 0.8703 1.2622 0.0688  0.1043  0.0462  189 SER K O   
20479 C CB  . SER K  189 ? 0.8487 0.7418 1.1337 0.0628  0.0918  0.0463  189 SER K CB  
20480 O OG  . SER K  189 ? 0.9292 0.8207 1.2218 0.0641  0.0949  0.0482  189 SER K OG  
20481 N N   . THR K  190 ? 1.0281 0.9104 1.3073 0.0725  0.1078  0.0499  190 THR K N   
20482 C CA  . THR K  190 ? 1.0511 0.9278 1.3330 0.0750  0.1150  0.0508  190 THR K CA  
20483 C C   . THR K  190 ? 0.9289 0.8031 1.2042 0.0801  0.1201  0.0536  190 THR K C   
20484 O O   . THR K  190 ? 0.8604 0.7369 1.1322 0.0813  0.1186  0.0549  190 THR K O   
20485 C CB  . THR K  190 ? 0.9565 0.8312 1.2510 0.0729  0.1169  0.0506  190 THR K CB  
20486 O OG1 . THR K  190 ? 1.2775 1.1470 1.5739 0.0764  0.1244  0.0525  190 THR K OG1 
20487 C CG2 . THR K  190 ? 0.9696 0.8481 1.2698 0.0708  0.1126  0.0510  190 THR K CG2 
20488 N N   . SER K  191 ? 1.0949 0.9647 1.3687 0.0830  0.1263  0.0546  191 SER K N   
20489 C CA  . SER K  191 ? 1.1539 1.0214 1.4216 0.0878  0.1314  0.0576  191 SER K CA  
20490 C C   . SER K  191 ? 0.9798 0.8457 1.2531 0.0885  0.1341  0.0591  191 SER K C   
20491 O O   . SER K  191 ? 0.9270 0.7924 1.1947 0.0917  0.1367  0.0613  191 SER K O   
20492 C CB  . SER K  191 ? 1.0046 0.8673 1.2710 0.0905  0.1377  0.0585  191 SER K CB  
20493 O OG  . SER K  191 ? 1.1268 0.9855 1.4034 0.0890  0.1413  0.0578  191 SER K OG  
20494 N N   . ALA K  192 ? 1.0577 0.9230 1.3421 0.0855  0.1335  0.0579  192 ALA K N   
20495 C CA  . ALA K  192 ? 1.2183 1.0823 1.5094 0.0858  0.1357  0.0591  192 ALA K CA  
20496 C C   . ALA K  192 ? 1.2309 1.0994 1.5195 0.0849  0.1308  0.0593  192 ALA K C   
20497 O O   . ALA K  192 ? 1.0807 0.9483 1.3684 0.0867  0.1333  0.0609  192 ALA K O   
20498 C CB  . ALA K  192 ? 1.2269 1.0896 1.5312 0.0826  0.1361  0.0578  192 ALA K CB  
20499 N N   . ASP K  193 ? 1.2023 1.0755 1.4899 0.0818  0.1240  0.0575  193 ASP K N   
20500 C CA  . ASP K  193 ? 1.0594 0.9370 1.3440 0.0809  0.1189  0.0575  193 ASP K CA  
20501 C C   . ASP K  193 ? 0.9297 0.8079 1.2018 0.0842  0.1199  0.0588  193 ASP K C   
20502 O O   . ASP K  193 ? 0.7770 0.6569 1.0465 0.0847  0.1188  0.0595  193 ASP K O   
20503 C CB  . ASP K  193 ? 1.0570 0.9393 1.3425 0.0769  0.1115  0.0553  193 ASP K CB  
20504 C CG  . ASP K  193 ? 1.3348 1.2192 1.6322 0.0732  0.1082  0.0548  193 ASP K CG  
20505 O OD1 . ASP K  193 ? 1.3897 1.2712 1.6966 0.0728  0.1118  0.0552  193 ASP K OD1 
20506 O OD2 . ASP K  193 ? 1.5687 1.4577 1.8660 0.0708  0.1021  0.0542  193 ASP K OD2 
20507 N N   . GLN K  194 ? 0.9385 0.8153 1.2031 0.0864  0.1221  0.0591  194 GLN K N   
20508 C CA  . GLN K  194 ? 0.8429 0.7208 1.0956 0.0896  0.1230  0.0605  194 GLN K CA  
20509 C C   . GLN K  194 ? 0.9652 0.8404 1.2162 0.0926  0.1284  0.0628  194 GLN K C   
20510 O O   . GLN K  194 ? 0.9258 0.8031 1.1713 0.0932  0.1272  0.0634  194 GLN K O   
20511 C CB  . GLN K  194 ? 0.9897 0.8663 1.2363 0.0915  0.1249  0.0607  194 GLN K CB  
20512 C CG  . GLN K  194 ? 0.9916 0.8689 1.2266 0.0953  0.1270  0.0629  194 GLN K CG  
20513 C CD  . GLN K  194 ? 0.8088 0.6914 1.0358 0.0946  0.1213  0.0622  194 GLN K CD  
20514 O OE1 . GLN K  194 ? 0.8570 0.7410 1.0751 0.0971  0.1222  0.0638  194 GLN K OE1 
20515 N NE2 . GLN K  194 ? 0.7542 0.6398 0.9842 0.0910  0.1154  0.0599  194 GLN K NE2 
20516 N N   . GLN K  195 ? 1.3555 1.2259 1.6112 0.0943  0.1345  0.0640  195 GLN K N   
20517 C CA  . GLN K  195 ? 1.4297 1.2969 1.6839 0.0970  0.1402  0.0662  195 GLN K CA  
20518 C C   . GLN K  195 ? 1.2658 1.1332 1.5272 0.0952  0.1397  0.0658  195 GLN K C   
20519 O O   . GLN K  195 ? 1.2195 1.0857 1.4777 0.0968  0.1428  0.0672  195 GLN K O   
20520 C CB  . GLN K  195 ? 1.5707 1.4326 1.8284 0.0992  0.1470  0.0676  195 GLN K CB  
20521 C CG  . GLN K  195 ? 1.8588 1.7183 2.1288 0.0967  0.1475  0.0661  195 GLN K CG  
20522 C CD  . GLN K  195 ? 2.0508 1.9051 2.3234 0.0989  0.1541  0.0673  195 GLN K CD  
20523 O OE1 . GLN K  195 ? 1.9795 1.8313 2.2617 0.0971  0.1554  0.0662  195 GLN K OE1 
20524 N NE2 . GLN K  195 ? 2.0638 1.9164 2.3278 0.1027  0.1584  0.0697  195 GLN K NE2 
20525 N N   . SER K  196 ? 1.0022 0.8710 1.2731 0.0918  0.1359  0.0641  196 SER K N   
20526 C CA  . SER K  196 ? 0.9592 0.8287 1.2380 0.0899  0.1348  0.0639  196 SER K CA  
20527 C C   . SER K  196 ? 1.1251 0.9985 1.3969 0.0895  0.1310  0.0638  196 SER K C   
20528 O O   . SER K  196 ? 1.2156 1.0884 1.4896 0.0896  0.1325  0.0644  196 SER K O   
20529 C CB  . SER K  196 ? 0.9503 0.8215 1.2406 0.0861  0.1308  0.0623  196 SER K CB  
20530 O OG  . SER K  196 ? 1.1064 0.9789 1.4044 0.0843  0.1292  0.0624  196 SER K OG  
20531 N N   . LEU K  197 ? 1.1192 0.9964 1.3829 0.0892  0.1262  0.0629  197 LEU K N   
20532 C CA  . LEU K  197 ? 0.9211 0.8023 1.1782 0.0885  0.1220  0.0625  197 LEU K CA  
20533 C C   . LEU K  197 ? 0.9767 0.8578 1.2213 0.0915  0.1245  0.0637  197 LEU K C   
20534 O O   . LEU K  197 ? 0.8849 0.7671 1.1260 0.0916  0.1246  0.0639  197 LEU K O   
20535 C CB  . LEU K  197 ? 0.8907 0.7764 1.1461 0.0860  0.1149  0.0607  197 LEU K CB  
20536 C CG  . LEU K  197 ? 0.8696 0.7576 1.1359 0.0822  0.1102  0.0595  197 LEU K CG  
20537 C CD1 . LEU K  197 ? 0.8686 0.7603 1.1323 0.0799  0.1040  0.0578  197 LEU K CD1 
20538 C CD2 . LEU K  197 ? 0.8259 0.7156 1.0949 0.0812  0.1085  0.0599  197 LEU K CD2 
20539 N N   . TYR K  198 ? 0.9962 0.8763 1.2342 0.0939  0.1268  0.0645  198 TYR K N   
20540 C CA  . TYR K  198 ? 1.0373 0.9183 1.2630 0.0966  0.1285  0.0659  198 TYR K CA  
20541 C C   . TYR K  198 ? 1.1820 1.0589 1.4052 0.0999  0.1353  0.0681  198 TYR K C   
20542 O O   . TYR K  198 ? 1.1369 1.0146 1.3501 0.1024  0.1371  0.0697  198 TYR K O   
20543 C CB  . TYR K  198 ? 1.1123 0.9977 1.3300 0.0964  0.1235  0.0651  198 TYR K CB  
20544 C CG  . TYR K  198 ? 0.9521 0.8411 1.1737 0.0929  0.1168  0.0629  198 TYR K CG  
20545 C CD1 . TYR K  198 ? 0.8591 0.7485 1.0855 0.0912  0.1140  0.0615  198 TYR K CD1 
20546 C CD2 . TYR K  198 ? 0.9570 0.8489 1.1775 0.0912  0.1132  0.0621  198 TYR K CD2 
20547 C CE1 . TYR K  198 ? 0.9023 0.7951 1.1319 0.0878  0.1077  0.0596  198 TYR K CE1 
20548 C CE2 . TYR K  198 ? 0.8516 0.7469 1.0757 0.0880  0.1070  0.0603  198 TYR K CE2 
20549 C CZ  . TYR K  198 ? 0.8014 0.6972 1.0299 0.0863  0.1042  0.0591  198 TYR K CZ  
20550 O OH  . TYR K  198 ? 0.7724 0.6718 1.0041 0.0831  0.0980  0.0575  198 TYR K OH  
20551 N N   . GLN K  199 ? 1.2122 1.0849 1.4448 0.0999  0.1391  0.0684  199 GLN K N   
20552 C CA  . GLN K  199 ? 1.2525 1.1207 1.4842 0.1029  0.1460  0.0706  199 GLN K CA  
20553 C C   . GLN K  199 ? 1.2164 1.0844 1.4422 0.1053  0.1472  0.0718  199 GLN K C   
20554 O O   . GLN K  199 ? 1.2647 1.1294 1.4961 0.1059  0.1502  0.0721  199 GLN K O   
20555 C CB  . GLN K  199 ? 1.2610 1.1283 1.4863 0.1046  0.1498  0.0722  199 GLN K CB  
20556 C CG  . GLN K  199 ? 1.3836 1.2460 1.6166 0.1049  0.1555  0.0729  199 GLN K CG  
20557 C CD  . GLN K  199 ? 1.4950 1.3528 1.7331 0.1066  0.1605  0.0741  199 GLN K CD  
20558 O OE1 . GLN K  199 ? 1.5034 1.3605 1.7348 0.1093  0.1631  0.0760  199 GLN K OE1 
20559 N NE2 . GLN K  199 ? 1.2974 1.1523 1.5475 0.1050  0.1619  0.0732  199 GLN K NE2 
20560 N N   . ASN K  200 ? 1.2689 1.1406 1.4838 0.1066  0.1450  0.0725  200 ASN K N   
20561 C CA  . ASN K  200 ? 1.2583 1.1305 1.4673 0.1091  0.1460  0.0740  200 ASN K CA  
20562 C C   . ASN K  200 ? 1.2505 1.1229 1.4646 0.1073  0.1428  0.0720  200 ASN K C   
20563 O O   . ASN K  200 ? 1.2096 1.0846 1.4275 0.1040  0.1375  0.0695  200 ASN K O   
20564 C CB  . ASN K  200 ? 1.2445 1.1214 1.4413 0.1104  0.1434  0.0750  200 ASN K CB  
20565 C CG  . ASN K  200 ? 1.1493 1.0269 1.3409 0.1108  0.1450  0.0759  200 ASN K CG  
20566 O OD1 . ASN K  200 ? 1.3756 1.2494 1.5719 0.1109  0.1492  0.0764  200 ASN K OD1 
20567 N ND2 . ASN K  200 ? 1.1565 1.0387 1.3385 0.1109  0.1417  0.0761  200 ASN K ND2 
20568 N N   . ALA K  201 ? 1.1694 1.0392 1.3838 0.1093  0.1463  0.0732  201 ALA K N   
20569 C CA  . ALA K  201 ? 1.0662 0.9357 1.2855 0.1075  0.1442  0.0712  201 ALA K CA  
20570 C C   . ALA K  201 ? 1.2907 1.1643 1.5018 0.1079  0.1402  0.0709  201 ALA K C   
20571 O O   . ALA K  201 ? 1.2316 1.1074 1.4446 0.1050  0.1353  0.0683  201 ALA K O   
20572 C CB  . ALA K  201 ? 1.2909 1.1550 1.5154 0.1093  0.1503  0.0724  201 ALA K CB  
20573 N N   . ASP K  202 ? 1.4139 1.2887 1.6160 0.1114  0.1423  0.0737  202 ASP K N   
20574 C CA  . ASP K  202 ? 1.3701 1.2491 1.5643 0.1122  0.1390  0.0739  202 ASP K CA  
20575 C C   . ASP K  202 ? 1.2625 1.1465 1.4484 0.1120  0.1351  0.0742  202 ASP K C   
20576 O O   . ASP K  202 ? 1.3206 1.2056 1.4997 0.1148  0.1376  0.0769  202 ASP K O   
20577 C CB  . ASP K  202 ? 1.5199 1.3972 1.7101 0.1162  0.1439  0.0771  202 ASP K CB  
20578 C CG  . ASP K  202 ? 1.6179 1.4982 1.8034 0.1166  0.1411  0.0768  202 ASP K CG  
20579 O OD1 . ASP K  202 ? 1.6113 1.4920 1.8005 0.1136  0.1374  0.0736  202 ASP K OD1 
20580 O OD2 . ASP K  202 ? 1.6618 1.5442 1.8399 0.1200  0.1426  0.0799  202 ASP K OD2 
20581 N N   . THR K  203 ? 1.1289 1.0163 1.3154 0.1087  0.1290  0.0713  203 THR K N   
20582 C CA  . THR K  203 ? 0.8833 0.7753 1.0628 0.1081  0.1252  0.0711  203 THR K CA  
20583 C C   . THR K  203 ? 0.8095 0.7063 0.9827 0.1073  0.1200  0.0700  203 THR K C   
20584 O O   . THR K  203 ? 0.9551 0.8515 1.1298 0.1069  0.1190  0.0691  203 THR K O   
20585 C CB  . THR K  203 ? 0.8988 0.7907 1.0842 0.1048  0.1226  0.0689  203 THR K CB  
20586 O OG1 . THR K  203 ? 0.8783 0.7708 1.0702 0.1015  0.1183  0.0660  203 THR K OG1 
20587 C CG2 . THR K  203 ? 1.0422 0.9294 1.2342 0.1054  0.1279  0.0699  203 THR K CG2 
20588 N N   . TYR K  204 ? 0.7909 0.6920 0.9570 0.1070  0.1168  0.0700  204 TYR K N   
20589 C CA  . TYR K  204 ? 0.8461 0.7522 1.0058 0.1062  0.1116  0.0689  204 TYR K CA  
20590 C C   . TYR K  204 ? 0.8320 0.7418 0.9877 0.1043  0.1078  0.0678  204 TYR K C   
20591 O O   . TYR K  204 ? 0.7665 0.6754 0.9213 0.1048  0.1101  0.0686  204 TYR K O   
20592 C CB  . TYR K  204 ? 0.8045 0.7126 0.9562 0.1098  0.1136  0.0717  204 TYR K CB  
20593 C CG  . TYR K  204 ? 0.8762 0.7867 1.0199 0.1119  0.1153  0.0742  204 TYR K CG  
20594 C CD1 . TYR K  204 ? 0.8209 0.7368 0.9567 0.1112  0.1112  0.0738  204 TYR K CD1 
20595 C CD2 . TYR K  204 ? 0.9627 0.8700 1.1066 0.1143  0.1211  0.0769  204 TYR K CD2 
20596 C CE1 . TYR K  204 ? 0.9125 0.8307 1.0407 0.1127  0.1128  0.0759  204 TYR K CE1 
20597 C CE2 . TYR K  204 ? 1.0598 0.9695 1.1960 0.1159  0.1226  0.0792  204 TYR K CE2 
20598 C CZ  . TYR K  204 ? 1.0770 0.9922 1.2052 0.1150  0.1184  0.0785  204 TYR K CZ  
20599 O OH  . TYR K  204 ? 1.0954 1.0131 1.2157 0.1162  0.1199  0.0806  204 TYR K OH  
20600 N N   . VAL K  205 ? 0.6914 0.6050 0.8444 0.1022  0.1022  0.0657  205 VAL K N   
20601 C CA  . VAL K  205 ? 0.7030 0.6206 0.8509 0.1007  0.0985  0.0648  205 VAL K CA  
20602 C C   . VAL K  205 ? 0.6986 0.6211 0.8382 0.1010  0.0947  0.0646  205 VAL K C   
20603 O O   . VAL K  205 ? 0.6866 0.6096 0.8271 0.1006  0.0928  0.0637  205 VAL K O   
20604 C CB  . VAL K  205 ? 0.6976 0.6149 0.8523 0.0970  0.0948  0.0621  205 VAL K CB  
20605 C CG1 . VAL K  205 ? 0.7741 0.6880 0.9388 0.0955  0.0950  0.0609  205 VAL K CG1 
20606 C CG2 . VAL K  205 ? 0.5200 0.4422 0.6700 0.0948  0.0888  0.0603  205 VAL K CG2 
20607 N N   . PHE K  206 ? 0.6273 0.5535 0.7589 0.1016  0.0938  0.0653  206 PHE K N   
20608 C CA  . PHE K  206 ? 0.6632 0.5945 0.7865 0.1021  0.0906  0.0655  206 PHE K CA  
20609 C C   . PHE K  206 ? 0.7600 0.6952 0.8789 0.0998  0.0864  0.0637  206 PHE K C   
20610 O O   . PHE K  206 ? 0.7877 0.7229 0.9046 0.0996  0.0879  0.0640  206 PHE K O   
20611 C CB  . PHE K  206 ? 0.7513 0.6839 0.8678 0.1058  0.0943  0.0689  206 PHE K CB  
20612 C CG  . PHE K  206 ? 0.8804 0.8191 0.9878 0.1065  0.0913  0.0694  206 PHE K CG  
20613 C CD1 . PHE K  206 ? 0.8211 0.7634 0.9214 0.1061  0.0905  0.0698  206 PHE K CD1 
20614 C CD2 . PHE K  206 ? 0.8625 0.8031 0.9685 0.1073  0.0895  0.0696  206 PHE K CD2 
20615 C CE1 . PHE K  206 ? 0.7889 0.7368 0.8809 0.1066  0.0877  0.0703  206 PHE K CE1 
20616 C CE2 . PHE K  206 ? 0.7551 0.7013 0.8530 0.1079  0.0868  0.0702  206 PHE K CE2 
20617 C CZ  . PHE K  206 ? 0.9043 0.8544 0.9954 0.1075  0.0857  0.0706  206 PHE K CZ  
20618 N N   . VAL K  207 ? 0.6538 0.5921 0.7710 0.0979  0.0814  0.0618  207 VAL K N   
20619 C CA  . VAL K  207 ? 0.7113 0.6534 0.8243 0.0957  0.0772  0.0601  207 VAL K CA  
20620 C C   . VAL K  207 ? 0.8087 0.7560 0.9130 0.0965  0.0746  0.0605  207 VAL K C   
20621 O O   . VAL K  207 ? 0.8992 0.8474 1.0036 0.0967  0.0729  0.0601  207 VAL K O   
20622 C CB  . VAL K  207 ? 0.6740 0.6154 0.7935 0.0921  0.0730  0.0573  207 VAL K CB  
20623 C CG1 . VAL K  207 ? 0.5974 0.5426 0.7125 0.0899  0.0689  0.0557  207 VAL K CG1 
20624 C CG2 . VAL K  207 ? 0.5207 0.4574 0.6495 0.0912  0.0754  0.0571  207 VAL K CG2 
20625 N N   . GLY K  208 ? 0.7731 0.7239 0.8699 0.0969  0.0745  0.0611  208 GLY K N   
20626 C CA  . GLY K  208 ? 0.7952 0.7514 0.8836 0.0977  0.0723  0.0617  208 GLY K CA  
20627 C C   . GLY K  208 ? 0.7977 0.7580 0.8799 0.0958  0.0694  0.0604  208 GLY K C   
20628 O O   . GLY K  208 ? 0.8437 0.8031 0.9254 0.0949  0.0710  0.0600  208 GLY K O   
20629 N N   . SER K  209 ? 0.6909 0.6556 0.7684 0.0951  0.0654  0.0594  209 SER K N   
20630 C CA  . SER K  209 ? 0.7349 0.7042 0.8054 0.0936  0.0627  0.0583  209 SER K CA  
20631 C C   . SER K  209 ? 0.8066 0.7813 0.8696 0.0954  0.0616  0.0599  209 SER K C   
20632 O O   . SER K  209 ? 0.8474 0.8220 0.9103 0.0983  0.0640  0.0624  209 SER K O   
20633 C CB  . SER K  209 ? 0.8442 0.8137 0.9175 0.0901  0.0581  0.0552  209 SER K CB  
20634 O OG  . SER K  209 ? 0.6719 0.6428 0.7457 0.0898  0.0549  0.0544  209 SER K OG  
20635 N N   . SER K  210 ? 0.9130 0.8925 0.9700 0.0938  0.0582  0.0586  210 SER K N   
20636 C CA  . SER K  210 ? 1.0506 1.0357 1.1008 0.0953  0.0567  0.0600  210 SER K CA  
20637 C C   . SER K  210 ? 1.0394 1.0242 1.0927 0.0960  0.0549  0.0598  210 SER K C   
20638 O O   . SER K  210 ? 0.8300 0.8180 0.8800 0.0982  0.0552  0.0618  210 SER K O   
20639 C CB  . SER K  210 ? 1.0480 1.0381 1.0917 0.0930  0.0533  0.0582  210 SER K CB  
20640 O OG  . SER K  210 ? 1.3186 1.3096 1.3581 0.0924  0.0554  0.0585  210 SER K OG  
20641 N N   . ARG K  211 ? 0.9744 0.9554 1.0342 0.0939  0.0532  0.0574  211 ARG K N   
20642 C CA  . ARG K  211 ? 1.0748 1.0551 1.1374 0.0938  0.0512  0.0566  211 ARG K CA  
20643 C C   . ARG K  211 ? 1.0877 1.0622 1.1584 0.0942  0.0537  0.0566  211 ARG K C   
20644 O O   . ARG K  211 ? 1.2077 1.1811 1.2804 0.0956  0.0546  0.0573  211 ARG K O   
20645 C CB  . ARG K  211 ? 1.0449 1.0268 1.1070 0.0903  0.0461  0.0534  211 ARG K CB  
20646 C CG  . ARG K  211 ? 1.2927 1.2711 1.3605 0.0874  0.0450  0.0512  211 ARG K CG  
20647 C CD  . ARG K  211 ? 1.4087 1.3898 1.4742 0.0843  0.0403  0.0486  211 ARG K CD  
20648 N NE  . ARG K  211 ? 1.6218 1.6057 1.6844 0.0838  0.0370  0.0477  211 ARG K NE  
20649 C CZ  . ARG K  211 ? 1.5423 1.5279 1.6040 0.0809  0.0327  0.0454  211 ARG K CZ  
20650 N NH1 . ARG K  211 ? 1.4342 1.4190 1.4979 0.0785  0.0311  0.0439  211 ARG K NH1 
20651 N NH2 . ARG K  211 ? 1.3686 1.3565 1.4276 0.0806  0.0302  0.0446  211 ARG K NH2 
20652 N N   . TYR K  212 ? 1.0435 1.0141 1.1193 0.0929  0.0549  0.0559  212 TYR K N   
20653 C CA  . TYR K  212 ? 0.8051 0.7702 0.8891 0.0929  0.0570  0.0558  212 TYR K CA  
20654 C C   . TYR K  212 ? 0.8316 0.7942 0.9167 0.0962  0.0625  0.0587  212 TYR K C   
20655 O O   . TYR K  212 ? 0.9354 0.8996 1.0164 0.0976  0.0646  0.0605  212 TYR K O   
20656 C CB  . TYR K  212 ? 0.6505 0.6130 0.7404 0.0899  0.0554  0.0536  212 TYR K CB  
20657 C CG  . TYR K  212 ? 0.7892 0.7467 0.8879 0.0890  0.0564  0.0529  212 TYR K CG  
20658 C CD1 . TYR K  212 ? 0.7494 0.7065 0.8517 0.0864  0.0528  0.0507  212 TYR K CD1 
20659 C CD2 . TYR K  212 ? 0.8614 0.8148 0.9650 0.0907  0.0610  0.0545  212 TYR K CD2 
20660 C CE1 . TYR K  212 ? 0.7864 0.7394 0.8966 0.0853  0.0535  0.0500  212 TYR K CE1 
20661 C CE2 . TYR K  212 ? 0.7581 0.7072 0.8700 0.0897  0.0620  0.0538  212 TYR K CE2 
20662 C CZ  . TYR K  212 ? 0.8135 0.7625 0.9287 0.0869  0.0581  0.0515  212 TYR K CZ  
20663 O OH  . TYR K  212 ? 0.7179 0.6629 0.8411 0.0856  0.0589  0.0507  212 TYR K OH  
20664 N N   . SER K  213 ? 0.8124 0.7712 0.9031 0.0973  0.0649  0.0593  213 SER K N   
20665 C CA  . SER K  213 ? 0.8021 0.7580 0.8946 0.1004  0.0703  0.0622  213 SER K CA  
20666 C C   . SER K  213 ? 0.7243 0.6752 0.8246 0.1003  0.0720  0.0615  213 SER K C   
20667 O O   . SER K  213 ? 0.8160 0.7671 0.9169 0.0999  0.0706  0.0606  213 SER K O   
20668 C CB  . SER K  213 ? 0.7991 0.7589 0.8846 0.1038  0.0721  0.0653  213 SER K CB  
20669 O OG  . SER K  213 ? 0.7654 0.7225 0.8523 0.1069  0.0774  0.0684  213 SER K OG  
20670 N N   . LYS K  214 ? 0.6639 0.6102 0.7702 0.1004  0.0753  0.0619  214 LYS K N   
20671 C CA  . LYS K  214 ? 0.6723 0.6138 0.7864 0.1001  0.0773  0.0613  214 LYS K CA  
20672 C C   . LYS K  214 ? 0.7849 0.7219 0.9044 0.1011  0.0819  0.0626  214 LYS K C   
20673 O O   . LYS K  214 ? 0.7409 0.6775 0.8614 0.1000  0.0818  0.0622  214 LYS K O   
20674 C CB  . LYS K  214 ? 0.7489 0.6895 0.8676 0.0962  0.0730  0.0578  214 LYS K CB  
20675 C CG  . LYS K  214 ? 0.8281 0.7640 0.9543 0.0955  0.0751  0.0569  214 LYS K CG  
20676 C CD  . LYS K  214 ? 1.1024 1.0392 1.2285 0.0932  0.0716  0.0545  214 LYS K CD  
20677 C CE  . LYS K  214 ? 1.0925 1.0279 1.2249 0.0889  0.0681  0.0515  214 LYS K CE  
20678 N NZ  . LYS K  214 ? 1.1903 1.1206 1.3310 0.0886  0.0715  0.0514  214 LYS K NZ  
20679 N N   . LYS K  215 ? 0.7963 0.7296 0.9195 0.1032  0.0862  0.0641  215 LYS K N   
20680 C CA  . LYS K  215 ? 0.8391 0.7677 0.9679 0.1043  0.0910  0.0654  215 LYS K CA  
20681 C C   . LYS K  215 ? 0.7418 0.6661 0.8798 0.1019  0.0910  0.0631  215 LYS K C   
20682 O O   . LYS K  215 ? 0.7738 0.6971 0.9134 0.1014  0.0905  0.0620  215 LYS K O   
20683 C CB  . LYS K  215 ? 0.9579 0.8854 1.0843 0.1086  0.0963  0.0691  215 LYS K CB  
20684 C CG  . LYS K  215 ? 0.9217 0.8446 1.0528 0.1101  0.1017  0.0709  215 LYS K CG  
20685 C CD  . LYS K  215 ? 0.9613 0.8839 1.0890 0.1145  0.1067  0.0749  215 LYS K CD  
20686 C CE  . LYS K  215 ? 1.1646 1.0831 1.2952 0.1161  0.1120  0.0770  215 LYS K CE  
20687 N NZ  . LYS K  215 ? 1.1336 1.0526 1.2598 0.1204  0.1165  0.0814  215 LYS K NZ  
20688 N N   . PHE K  216 ? 0.7301 0.6517 0.8741 0.1003  0.0916  0.0623  216 PHE K N   
20689 C CA  . PHE K  216 ? 0.7250 0.6431 0.8781 0.0975  0.0910  0.0600  216 PHE K CA  
20690 C C   . PHE K  216 ? 0.7125 0.6254 0.8721 0.0991  0.0969  0.0614  216 PHE K C   
20691 O O   . PHE K  216 ? 0.6735 0.5849 0.8329 0.1010  0.1004  0.0634  216 PHE K O   
20692 C CB  . PHE K  216 ? 0.7863 0.7056 0.9430 0.0940  0.0868  0.0579  216 PHE K CB  
20693 C CG  . PHE K  216 ? 0.8192 0.7435 0.9702 0.0922  0.0811  0.0564  216 PHE K CG  
20694 C CD1 . PHE K  216 ? 0.7050 0.6325 0.8493 0.0931  0.0803  0.0573  216 PHE K CD1 
20695 C CD2 . PHE K  216 ? 0.6509 0.5765 0.8029 0.0893  0.0768  0.0540  216 PHE K CD2 
20696 C CE1 . PHE K  216 ? 0.6674 0.5993 0.8065 0.0913  0.0752  0.0559  216 PHE K CE1 
20697 C CE2 . PHE K  216 ? 0.7017 0.6317 0.8484 0.0876  0.0716  0.0527  216 PHE K CE2 
20698 C CZ  . PHE K  216 ? 0.7201 0.6532 0.8605 0.0887  0.0709  0.0537  216 PHE K CZ  
20699 N N   . LYS K  217 ? 0.8412 0.7510 1.0062 0.0982  0.0980  0.0603  217 LYS K N   
20700 C CA  . LYS K  217 ? 0.7831 0.6876 0.9553 0.0992  0.1033  0.0611  217 LYS K CA  
20701 C C   . LYS K  217 ? 0.7348 0.6374 0.9163 0.0952  0.1012  0.0583  217 LYS K C   
20702 O O   . LYS K  217 ? 0.7919 0.6950 0.9751 0.0923  0.0980  0.0559  217 LYS K O   
20703 C CB  . LYS K  217 ? 0.9772 0.8793 1.1488 0.1016  0.1074  0.0623  217 LYS K CB  
20704 C CG  . LYS K  217 ? 0.9606 0.8619 1.1278 0.1064  0.1127  0.0663  217 LYS K CG  
20705 C CD  . LYS K  217 ? 1.0645 0.9618 1.2369 0.1073  0.1172  0.0677  217 LYS K CD  
20706 C CE  . LYS K  217 ? 1.3068 1.2033 1.4747 0.1120  0.1226  0.0719  217 LYS K CE  
20707 N NZ  . LYS K  217 ? 1.4160 1.3082 1.5889 0.1129  0.1273  0.0732  217 LYS K NZ  
20708 N N   . PRO K  218 ? 0.8099 0.7103 0.9972 0.0948  0.1030  0.0588  218 PRO K N   
20709 C CA  . PRO K  218 ? 0.8393 0.7382 1.0361 0.0910  0.1012  0.0566  218 PRO K CA  
20710 C C   . PRO K  218 ? 0.8255 0.7211 1.0280 0.0898  0.1030  0.0552  218 PRO K C   
20711 O O   . PRO K  218 ? 0.8114 0.7031 1.0150 0.0924  0.1086  0.0566  218 PRO K O   
20712 C CB  . PRO K  218 ? 0.8045 0.7006 1.0061 0.0923  0.1051  0.0582  218 PRO K CB  
20713 C CG  . PRO K  218 ? 0.8604 0.7584 1.0534 0.0954  0.1065  0.0605  218 PRO K CG  
20714 C CD  . PRO K  218 ? 0.8830 0.7825 1.0681 0.0977  0.1070  0.0615  218 PRO K CD  
20715 N N   . GLU K  219 ? 0.8959 0.7929 1.1016 0.0857  0.0983  0.0523  219 GLU K N   
20716 C CA  . GLU K  219 ? 0.7835 0.6776 0.9945 0.0836  0.0996  0.0504  219 GLU K CA  
20717 C C   . GLU K  219 ? 0.7643 0.6564 0.9860 0.0808  0.0998  0.0494  219 GLU K C   
20718 O O   . GLU K  219 ? 0.6966 0.5913 0.9222 0.0769  0.0947  0.0475  219 GLU K O   
20719 C CB  . GLU K  219 ? 0.8140 0.7111 1.0216 0.0806  0.0944  0.0477  219 GLU K CB  
20720 C CG  . GLU K  219 ? 0.9237 0.8232 1.1211 0.0831  0.0938  0.0487  219 GLU K CG  
20721 C CD  . GLU K  219 ? 1.0935 0.9957 1.2876 0.0799  0.0889  0.0459  219 GLU K CD  
20722 O OE1 . GLU K  219 ? 0.9793 0.8818 1.1785 0.0755  0.0854  0.0433  219 GLU K OE1 
20723 O OE2 . GLU K  219 ? 1.1054 1.0094 1.2918 0.0818  0.0885  0.0464  219 GLU K OE2 
20724 N N   . ILE K  220 ? 0.9623 0.8499 1.1889 0.0829  0.1058  0.0508  220 ILE K N   
20725 C CA  . ILE K  220 ? 0.9133 0.7987 1.1504 0.0807  0.1069  0.0502  220 ILE K CA  
20726 C C   . ILE K  220 ? 0.7942 0.6776 1.0377 0.0772  0.1069  0.0476  220 ILE K C   
20727 O O   . ILE K  220 ? 0.7796 0.6593 1.0229 0.0786  0.1115  0.0475  220 ILE K O   
20728 C CB  . ILE K  220 ? 0.7273 0.6086 0.9669 0.0844  0.1136  0.0529  220 ILE K CB  
20729 C CG1 . ILE K  220 ? 0.7869 0.6703 1.0201 0.0873  0.1136  0.0553  220 ILE K CG1 
20730 C CG2 . ILE K  220 ? 0.8281 0.7073 1.0791 0.0821  0.1148  0.0523  220 ILE K CG2 
20731 C CD1 . ILE K  220 ? 0.9907 0.8703 1.2236 0.0914  0.1204  0.0582  220 ILE K CD1 
20732 N N   . ALA K  221 ? 0.6606 0.5465 0.9101 0.0726  0.1019  0.0455  221 ALA K N   
20733 C CA  . ALA K  221 ? 0.6471 0.5317 0.9028 0.0685  0.1013  0.0428  221 ALA K CA  
20734 C C   . ALA K  221 ? 0.8231 0.7113 1.0862 0.0637  0.0956  0.0414  221 ALA K C   
20735 O O   . ALA K  221 ? 0.8801 0.7718 1.1430 0.0637  0.0919  0.0425  221 ALA K O   
20736 C CB  . ALA K  221 ? 0.8122 0.6973 1.0614 0.0674  0.0999  0.0407  221 ALA K CB  
20737 N N   . ILE K  222 ? 0.9076 0.7949 1.1774 0.0596  0.0949  0.0390  222 ILE K N   
20738 C CA  . ILE K  222 ? 0.9318 0.8228 1.2093 0.0548  0.0895  0.0378  222 ILE K CA  
20739 C C   . ILE K  222 ? 0.8905 0.7859 1.1640 0.0506  0.0828  0.0354  222 ILE K C   
20740 O O   . ILE K  222 ? 0.9805 0.8746 1.2525 0.0481  0.0830  0.0328  222 ILE K O   
20741 C CB  . ILE K  222 ? 1.0923 0.9806 1.3805 0.0522  0.0924  0.0367  222 ILE K CB  
20742 C CG1 . ILE K  222 ? 1.0153 0.8991 1.3081 0.0563  0.0991  0.0392  222 ILE K CG1 
20743 C CG2 . ILE K  222 ? 0.9287 0.8215 1.2251 0.0471  0.0863  0.0358  222 ILE K CG2 
20744 C CD1 . ILE K  222 ? 1.0567 0.9426 1.3520 0.0581  0.0980  0.0418  222 ILE K CD1 
20745 N N   . ARG K  223 ? 0.7794 0.6797 1.0511 0.0497  0.0770  0.0361  223 ARG K N   
20746 C CA  . ARG K  223 ? 0.9112 0.8160 1.1794 0.0455  0.0702  0.0341  223 ARG K CA  
20747 C C   . ARG K  223 ? 0.8602 0.7685 1.1380 0.0404  0.0654  0.0334  223 ARG K C   
20748 O O   . ARG K  223 ? 0.9478 0.8564 1.2338 0.0409  0.0661  0.0353  223 ARG K O   
20749 C CB  . ARG K  223 ? 0.8471 0.7555 1.1073 0.0474  0.0665  0.0354  223 ARG K CB  
20750 C CG  . ARG K  223 ? 0.7398 0.6462 0.9894 0.0516  0.0697  0.0358  223 ARG K CG  
20751 C CD  . ARG K  223 ? 0.7278 0.6311 0.9768 0.0570  0.0754  0.0387  223 ARG K CD  
20752 N NE  . ARG K  223 ? 0.6748 0.5781 0.9133 0.0608  0.0768  0.0396  223 ARG K NE  
20753 C CZ  . ARG K  223 ? 0.6788 0.5800 0.9143 0.0656  0.0815  0.0421  223 ARG K CZ  
20754 N NH1 . ARG K  223 ? 0.7751 0.6736 1.0172 0.0672  0.0855  0.0437  223 ARG K NH1 
20755 N NH2 . ARG K  223 ? 0.7969 0.6988 1.0228 0.0687  0.0822  0.0430  223 ARG K NH2 
20756 N N   . PRO K  224 ? 0.7815 0.6925 1.0583 0.0354  0.0606  0.0308  224 PRO K N   
20757 C CA  . PRO K  224 ? 0.7957 0.7110 1.0808 0.0302  0.0552  0.0303  224 PRO K CA  
20758 C C   . PRO K  224 ? 0.9482 0.8678 1.2363 0.0310  0.0513  0.0332  224 PRO K C   
20759 O O   . PRO K  224 ? 0.9896 0.9112 1.2702 0.0328  0.0488  0.0340  224 PRO K O   
20760 C CB  . PRO K  224 ? 0.8214 0.7396 1.1007 0.0256  0.0503  0.0274  224 PRO K CB  
20761 C CG  . PRO K  224 ? 0.9293 0.8427 1.2008 0.0277  0.0552  0.0256  224 PRO K CG  
20762 C CD  . PRO K  224 ? 0.9052 0.8156 1.1730 0.0343  0.0602  0.0283  224 PRO K CD  
20763 N N   . LYS K  225 ? 1.0963 1.0172 1.3955 0.0296  0.0508  0.0346  225 LYS K N   
20764 C CA  . LYS K  225 ? 0.9567 0.8810 1.2602 0.0308  0.0481  0.0376  225 LYS K CA  
20765 C C   . LYS K  225 ? 0.8528 0.7828 1.1523 0.0283  0.0407  0.0377  225 LYS K C   
20766 O O   . LYS K  225 ? 0.9179 0.8518 1.2193 0.0233  0.0354  0.0364  225 LYS K O   
20767 C CB  . LYS K  225 ? 1.1833 1.1087 1.5004 0.0287  0.0480  0.0388  225 LYS K CB  
20768 C CG  . LYS K  225 ? 1.3859 1.3059 1.7081 0.0319  0.0554  0.0396  225 LYS K CG  
20769 C CD  . LYS K  225 ? 1.5895 1.5113 1.9255 0.0298  0.0548  0.0411  225 LYS K CD  
20770 C CE  . LYS K  225 ? 1.7967 1.7131 2.1377 0.0336  0.0624  0.0423  225 LYS K CE  
20771 N NZ  . LYS K  225 ? 1.7487 1.6623 2.0827 0.0391  0.0660  0.0441  225 LYS K NZ  
20772 N N   . VAL K  226 ? 0.7532 0.6838 1.0472 0.0318  0.0404  0.0395  226 VAL K N   
20773 C CA  . VAL K  226 ? 0.8856 0.8215 1.1772 0.0301  0.0339  0.0403  226 VAL K CA  
20774 C C   . VAL K  226 ? 0.9683 0.9049 1.2654 0.0329  0.0347  0.0435  226 VAL K C   
20775 O O   . VAL K  226 ? 0.8416 0.7752 1.1342 0.0374  0.0390  0.0445  226 VAL K O   
20776 C CB  . VAL K  226 ? 0.8813 0.8172 1.1597 0.0316  0.0328  0.0390  226 VAL K CB  
20777 C CG1 . VAL K  226 ? 0.7819 0.7231 1.0579 0.0298  0.0262  0.0400  226 VAL K CG1 
20778 C CG2 . VAL K  226 ? 0.9063 0.8407 1.1794 0.0291  0.0330  0.0358  226 VAL K CG2 
20779 N N   . ARG K  227 ? 1.0937 1.0343 1.4008 0.0301  0.0308  0.0452  227 ARG K N   
20780 C CA  . ARG K  227 ? 0.9691 0.9102 1.2831 0.0323  0.0319  0.0483  227 ARG K CA  
20781 C C   . ARG K  227 ? 1.0691 1.0050 1.3885 0.0357  0.0393  0.0491  227 ARG K C   
20782 O O   . ARG K  227 ? 1.0963 1.0300 1.4149 0.0395  0.0429  0.0508  227 ARG K O   
20783 C CB  . ARG K  227 ? 0.7661 0.7079 1.0715 0.0351  0.0311  0.0492  227 ARG K CB  
20784 C CG  . ARG K  227 ? 0.8605 0.8077 1.1628 0.0320  0.0238  0.0492  227 ARG K CG  
20785 C CD  . ARG K  227 ? 0.8933 0.8405 1.1853 0.0349  0.0236  0.0493  227 ARG K CD  
20786 N NE  . ARG K  227 ? 0.8231 0.7749 1.1177 0.0335  0.0186  0.0513  227 ARG K NE  
20787 C CZ  . ARG K  227 ? 0.9735 0.9256 1.2760 0.0349  0.0197  0.0540  227 ARG K CZ  
20788 N NH1 . ARG K  227 ? 1.0491 0.9973 1.3574 0.0376  0.0257  0.0549  227 ARG K NH1 
20789 N NH2 . ARG K  227 ? 0.9604 0.9166 1.2653 0.0337  0.0152  0.0559  227 ARG K NH2 
20790 N N   . ASP K  228 ? 1.1258 1.0597 1.4502 0.0341  0.0415  0.0478  228 ASP K N   
20791 C CA  . ASP K  228 ? 1.2907 1.2199 1.6216 0.0367  0.0484  0.0486  228 ASP K CA  
20792 C C   . ASP K  228 ? 1.2448 1.1681 1.5667 0.0414  0.0549  0.0479  228 ASP K C   
20793 O O   . ASP K  228 ? 1.3889 1.3078 1.7148 0.0436  0.0610  0.0484  228 ASP K O   
20794 C CB  . ASP K  228 ? 1.6435 1.5736 1.9842 0.0379  0.0491  0.0517  228 ASP K CB  
20795 C CG  . ASP K  228 ? 1.8663 1.7996 2.2210 0.0342  0.0467  0.0526  228 ASP K CG  
20796 O OD1 . ASP K  228 ? 1.8372 1.7677 2.1974 0.0336  0.0503  0.0518  228 ASP K OD1 
20797 O OD2 . ASP K  228 ? 1.8833 1.8219 2.2437 0.0319  0.0413  0.0544  228 ASP K OD2 
20798 N N   . GLN K  229 ? 1.0218 0.9453 1.3316 0.0428  0.0537  0.0470  229 GLN K N   
20799 C CA  . GLN K  229 ? 0.9975 0.9163 1.2983 0.0473  0.0595  0.0468  229 GLN K CA  
20800 C C   . GLN K  229 ? 0.9483 0.8649 1.2434 0.0466  0.0609  0.0443  229 GLN K C   
20801 O O   . GLN K  229 ? 1.0413 0.9606 1.3314 0.0438  0.0564  0.0424  229 GLN K O   
20802 C CB  . GLN K  229 ? 0.8603 0.7805 1.1514 0.0497  0.0581  0.0475  229 GLN K CB  
20803 C CG  . GLN K  229 ? 0.7927 0.7156 1.0887 0.0498  0.0559  0.0497  229 GLN K CG  
20804 C CD  . GLN K  229 ? 0.9409 0.8607 1.2457 0.0519  0.0612  0.0516  229 GLN K CD  
20805 O OE1 . GLN K  229 ? 0.9668 0.8819 1.2699 0.0549  0.0673  0.0517  229 GLN K OE1 
20806 N NE2 . GLN K  229 ? 1.1135 1.0359 1.4279 0.0504  0.0589  0.0533  229 GLN K NE2 
20807 N N   . GLU K  230 ? 0.9110 0.8224 1.2070 0.0491  0.0674  0.0442  230 GLU K N   
20808 C CA  . GLU K  230 ? 0.9666 0.8750 1.2571 0.0491  0.0699  0.0421  230 GLU K CA  
20809 C C   . GLU K  230 ? 0.8582 0.7645 1.1372 0.0535  0.0730  0.0426  230 GLU K C   
20810 O O   . GLU K  230 ? 0.9057 0.8100 1.1785 0.0541  0.0748  0.0412  230 GLU K O   
20811 C CB  . GLU K  230 ? 1.2098 1.1139 1.5081 0.0492  0.0755  0.0419  230 GLU K CB  
20812 C CG  . GLU K  230 ? 1.5331 1.4393 1.8426 0.0444  0.0725  0.0410  230 GLU K CG  
20813 C CD  . GLU K  230 ? 1.7582 1.6599 2.0753 0.0446  0.0783  0.0406  230 GLU K CD  
20814 O OE1 . GLU K  230 ? 1.7878 1.6848 2.1033 0.0490  0.0847  0.0420  230 GLU K OE1 
20815 O OE2 . GLU K  230 ? 1.8539 1.7567 2.1783 0.0402  0.0765  0.0390  230 GLU K OE2 
20816 N N   . GLY K  231 ? 0.6626 0.5696 0.9390 0.0566  0.0737  0.0447  231 GLY K N   
20817 C CA  . GLY K  231 ? 0.6800 0.5861 0.9451 0.0605  0.0756  0.0454  231 GLY K CA  
20818 C C   . GLY K  231 ? 0.7374 0.6482 0.9954 0.0590  0.0695  0.0447  231 GLY K C   
20819 O O   . GLY K  231 ? 0.7488 0.6635 1.0110 0.0554  0.0639  0.0442  231 GLY K O   
20820 N N   . ARG K  232 ? 0.7264 0.6372 0.9738 0.0618  0.0704  0.0449  232 ARG K N   
20821 C CA  . ARG K  232 ? 0.5869 0.5019 0.8267 0.0608  0.0650  0.0442  232 ARG K CA  
20822 C C   . ARG K  232 ? 0.5958 0.5115 0.8289 0.0643  0.0661  0.0460  232 ARG K C   
20823 O O   . ARG K  232 ? 0.5681 0.4808 0.8006 0.0677  0.0715  0.0476  232 ARG K O   
20824 C CB  . ARG K  232 ? 0.6298 0.5449 0.8625 0.0601  0.0641  0.0423  232 ARG K CB  
20825 C CG  . ARG K  232 ? 0.6320 0.5474 0.8698 0.0556  0.0615  0.0399  232 ARG K CG  
20826 C CD  . ARG K  232 ? 0.7025 0.6227 0.9437 0.0514  0.0545  0.0393  232 ARG K CD  
20827 N NE  . ARG K  232 ? 0.8312 0.7521 1.0772 0.0466  0.0518  0.0371  232 ARG K NE  
20828 C CZ  . ARG K  232 ? 0.8108 0.7309 1.0670 0.0444  0.0525  0.0371  232 ARG K CZ  
20829 N NH1 . ARG K  232 ? 0.7175 0.6357 0.9804 0.0466  0.0560  0.0392  232 ARG K NH1 
20830 N NH2 . ARG K  232 ? 0.8232 0.7443 1.0829 0.0397  0.0498  0.0349  232 ARG K NH2 
20831 N N   . MET K  233 ? 0.6379 0.5577 0.8660 0.0631  0.0611  0.0456  233 MET K N   
20832 C CA  . MET K  233 ? 0.5970 0.5180 0.8179 0.0659  0.0617  0.0469  233 MET K CA  
20833 C C   . MET K  233 ? 0.7078 0.6324 0.9194 0.0651  0.0572  0.0457  233 MET K C   
20834 O O   . MET K  233 ? 0.6295 0.5576 0.8422 0.0620  0.0517  0.0448  233 MET K O   
20835 C CB  . MET K  233 ? 0.6123 0.5343 0.8391 0.0654  0.0608  0.0482  233 MET K CB  
20836 C CG  . MET K  233 ? 0.6532 0.5759 0.8732 0.0681  0.0623  0.0493  233 MET K CG  
20837 S SD  . MET K  233 ? 0.7693 0.6922 0.9969 0.0675  0.0624  0.0508  233 MET K SD  
20838 C CE  . MET K  233 ? 0.7526 0.6706 0.9899 0.0688  0.0686  0.0519  233 MET K CE  
20839 N N   . ASN K  234 ? 0.6749 0.5989 0.8777 0.0680  0.0597  0.0459  234 ASN K N   
20840 C CA  . ASN K  234 ? 0.6370 0.5642 0.8306 0.0676  0.0560  0.0449  234 ASN K CA  
20841 C C   . ASN K  234 ? 0.5540 0.4839 0.7422 0.0689  0.0546  0.0458  234 ASN K C   
20842 O O   . ASN K  234 ? 0.5416 0.4701 0.7287 0.0717  0.0585  0.0474  234 ASN K O   
20843 C CB  . ASN K  234 ? 0.5811 0.5068 0.7682 0.0701  0.0591  0.0447  234 ASN K CB  
20844 C CG  . ASN K  234 ? 0.5099 0.4333 0.7012 0.0682  0.0599  0.0432  234 ASN K CG  
20845 O OD1 . ASN K  234 ? 0.5880 0.5113 0.7869 0.0649  0.0576  0.0421  234 ASN K OD1 
20846 N ND2 . ASN K  234 ? 0.6503 0.5718 0.8369 0.0704  0.0631  0.0432  234 ASN K ND2 
20847 N N   . TYR K  235 ? 0.4648 0.3985 0.6496 0.0666  0.0492  0.0447  235 TYR K N   
20848 C CA  . TYR K  235 ? 0.4704 0.4068 0.6504 0.0672  0.0475  0.0453  235 TYR K CA  
20849 C C   . TYR K  235 ? 0.5139 0.4528 0.6830 0.0685  0.0463  0.0447  235 TYR K C   
20850 O O   . TYR K  235 ? 0.4637 0.4042 0.6299 0.0669  0.0432  0.0433  235 TYR K O   
20851 C CB  . TYR K  235 ? 0.5168 0.4559 0.7020 0.0638  0.0424  0.0448  235 TYR K CB  
20852 C CG  . TYR K  235 ? 0.6542 0.5914 0.8509 0.0622  0.0430  0.0455  235 TYR K CG  
20853 C CD1 . TYR K  235 ? 0.6374 0.5747 0.8402 0.0593  0.0407  0.0445  235 TYR K CD1 
20854 C CD2 . TYR K  235 ? 0.6067 0.5423 0.8084 0.0636  0.0462  0.0470  235 TYR K CD2 
20855 C CE1 . TYR K  235 ? 0.5419 0.4779 0.7555 0.0578  0.0412  0.0452  235 TYR K CE1 
20856 C CE2 . TYR K  235 ? 0.5351 0.4692 0.7479 0.0623  0.0469  0.0478  235 TYR K CE2 
20857 C CZ  . TYR K  235 ? 0.5205 0.4550 0.7394 0.0594  0.0443  0.0469  235 TYR K CZ  
20858 O OH  . TYR K  235 ? 0.6140 0.5474 0.8441 0.0580  0.0449  0.0478  235 TYR K OH  
20859 N N   . TYR K  236 ? 0.5217 0.4610 0.6848 0.0713  0.0488  0.0459  236 TYR K N   
20860 C CA  . TYR K  236 ? 0.5921 0.5341 0.7450 0.0728  0.0480  0.0457  236 TYR K CA  
20861 C C   . TYR K  236 ? 0.6091 0.5542 0.7576 0.0724  0.0458  0.0457  236 TYR K C   
20862 O O   . TYR K  236 ? 0.5855 0.5298 0.7384 0.0718  0.0462  0.0462  236 TYR K O   
20863 C CB  . TYR K  236 ? 0.4392 0.3794 0.5879 0.0766  0.0534  0.0473  236 TYR K CB  
20864 C CG  . TYR K  236 ? 0.5973 0.5343 0.7497 0.0772  0.0560  0.0473  236 TYR K CG  
20865 C CD1 . TYR K  236 ? 0.6019 0.5350 0.7626 0.0772  0.0592  0.0478  236 TYR K CD1 
20866 C CD2 . TYR K  236 ? 0.6187 0.5565 0.7665 0.0776  0.0554  0.0466  236 TYR K CD2 
20867 C CE1 . TYR K  236 ? 0.6114 0.5415 0.7756 0.0776  0.0618  0.0477  236 TYR K CE1 
20868 C CE2 . TYR K  236 ? 0.7337 0.6683 0.8850 0.0780  0.0581  0.0464  236 TYR K CE2 
20869 C CZ  . TYR K  236 ? 0.7671 0.6978 0.9265 0.0779  0.0613  0.0469  236 TYR K CZ  
20870 O OH  . TYR K  236 ? 0.7284 0.6557 0.8913 0.0782  0.0642  0.0466  236 TYR K OH  
20871 N N   . TRP K  237 ? 0.5381 0.4865 0.6781 0.0726  0.0434  0.0451  237 TRP K N   
20872 C CA  . TRP K  237 ? 0.5098 0.4612 0.6447 0.0721  0.0414  0.0449  237 TRP K CA  
20873 C C   . TRP K  237 ? 0.4856 0.4400 0.6102 0.0738  0.0411  0.0448  237 TRP K C   
20874 O O   . TRP K  237 ? 0.5345 0.4891 0.6564 0.0748  0.0413  0.0447  237 TRP K O   
20875 C CB  . TRP K  237 ? 0.5015 0.4549 0.6395 0.0686  0.0360  0.0435  237 TRP K CB  
20876 C CG  . TRP K  237 ? 0.4741 0.4294 0.6097 0.0668  0.0320  0.0420  237 TRP K CG  
20877 C CD1 . TRP K  237 ? 0.4468 0.4007 0.5874 0.0650  0.0306  0.0412  237 TRP K CD1 
20878 C CD2 . TRP K  237 ? 0.5074 0.4662 0.6347 0.0664  0.0290  0.0410  237 TRP K CD2 
20879 N NE1 . TRP K  237 ? 0.4047 0.3609 0.5404 0.0634  0.0271  0.0397  237 TRP K NE1 
20880 C CE2 . TRP K  237 ? 0.4948 0.4540 0.6224 0.0644  0.0260  0.0396  237 TRP K CE2 
20881 C CE3 . TRP K  237 ? 0.5657 0.5274 0.6852 0.0674  0.0285  0.0411  237 TRP K CE3 
20882 C CZ2 . TRP K  237 ? 0.5733 0.5355 0.6940 0.0635  0.0228  0.0384  237 TRP K CZ2 
20883 C CZ3 . TRP K  237 ? 0.5347 0.4996 0.6476 0.0666  0.0252  0.0399  237 TRP K CZ3 
20884 C CH2 . TRP K  237 ? 0.5129 0.4779 0.6265 0.0648  0.0225  0.0386  237 TRP K CH2 
20885 N N   . THR K  238 ? 0.4830 0.4399 0.6022 0.0742  0.0408  0.0449  238 THR K N   
20886 C CA  . THR K  238 ? 0.5054 0.4658 0.6149 0.0755  0.0402  0.0450  238 THR K CA  
20887 C C   . THR K  238 ? 0.6038 0.5671 0.7089 0.0744  0.0384  0.0443  238 THR K C   
20888 O O   . THR K  238 ? 0.6484 0.6103 0.7575 0.0733  0.0390  0.0443  238 THR K O   
20889 C CB  . THR K  238 ? 0.5426 0.5023 0.6481 0.0791  0.0450  0.0469  238 THR K CB  
20890 O OG1 . THR K  238 ? 0.5919 0.5557 0.6886 0.0803  0.0440  0.0471  238 THR K OG1 
20891 C CG2 . THR K  238 ? 0.5385 0.4966 0.6448 0.0802  0.0488  0.0481  238 THR K CG2 
20892 N N   . LEU K  239 ? 0.6569 0.6241 0.7539 0.0745  0.0363  0.0438  239 LEU K N   
20893 C CA  . LEU K  239 ? 0.7110 0.6811 0.8032 0.0733  0.0346  0.0429  239 LEU K CA  
20894 C C   . LEU K  239 ? 0.7738 0.7461 0.8581 0.0756  0.0375  0.0440  239 LEU K C   
20895 O O   . LEU K  239 ? 0.8364 0.8116 0.9145 0.0770  0.0371  0.0444  239 LEU K O   
20896 C CB  . LEU K  239 ? 0.7365 0.7098 0.8257 0.0712  0.0294  0.0413  239 LEU K CB  
20897 C CG  . LEU K  239 ? 0.5843 0.5563 0.6806 0.0683  0.0259  0.0402  239 LEU K CG  
20898 C CD1 . LEU K  239 ? 0.7077 0.6829 0.7999 0.0663  0.0211  0.0386  239 LEU K CD1 
20899 C CD2 . LEU K  239 ? 0.6942 0.6647 0.7958 0.0667  0.0260  0.0401  239 LEU K CD2 
20900 N N   . VAL K  240 ? 0.6847 0.6556 0.7693 0.0758  0.0405  0.0444  240 VAL K N   
20901 C CA  . VAL K  240 ? 0.6989 0.6719 0.7760 0.0775  0.0434  0.0454  240 VAL K CA  
20902 C C   . VAL K  240 ? 0.7435 0.7210 0.8134 0.0759  0.0407  0.0440  240 VAL K C   
20903 O O   . VAL K  240 ? 0.7646 0.7417 0.8363 0.0736  0.0392  0.0425  240 VAL K O   
20904 C CB  . VAL K  240 ? 0.6680 0.6377 0.7478 0.0780  0.0480  0.0462  240 VAL K CB  
20905 C CG1 . VAL K  240 ? 0.7782 0.7502 0.8497 0.0798  0.0512  0.0475  240 VAL K CG1 
20906 C CG2 . VAL K  240 ? 0.6131 0.5781 0.7012 0.0792  0.0505  0.0474  240 VAL K CG2 
20907 N N   . GLU K  241 ? 0.8601 0.8417 0.9223 0.0772  0.0401  0.0446  241 GLU K N   
20908 C CA  . GLU K  241 ? 0.8327 0.8190 0.8876 0.0758  0.0376  0.0433  241 GLU K CA  
20909 C C   . GLU K  241 ? 0.8652 0.8515 0.9169 0.0750  0.0402  0.0429  241 GLU K C   
20910 O O   . GLU K  241 ? 0.8676 0.8516 0.9201 0.0763  0.0443  0.0442  241 GLU K O   
20911 C CB  . GLU K  241 ? 0.9851 0.9760 1.0329 0.0777  0.0369  0.0444  241 GLU K CB  
20912 C CG  . GLU K  241 ? 1.1258 1.1167 1.1761 0.0784  0.0346  0.0446  241 GLU K CG  
20913 C CD  . GLU K  241 ? 1.4141 1.4061 1.4652 0.0757  0.0299  0.0423  241 GLU K CD  
20914 O OE1 . GLU K  241 ? 1.4874 1.4775 1.5430 0.0753  0.0281  0.0418  241 GLU K OE1 
20915 O OE2 . GLU K  241 ? 1.4599 1.4546 1.5070 0.0738  0.0280  0.0408  241 GLU K OE2 
20916 N N   . PRO K  242 ? 1.0002 0.9891 1.0482 0.0726  0.0380  0.0410  242 PRO K N   
20917 C CA  . PRO K  242 ? 0.9325 0.9218 0.9763 0.0714  0.0405  0.0402  242 PRO K CA  
20918 C C   . PRO K  242 ? 0.9986 0.9910 1.0348 0.0734  0.0432  0.0418  242 PRO K C   
20919 O O   . PRO K  242 ? 0.8595 0.8564 0.8902 0.0745  0.0414  0.0426  242 PRO K O   
20920 C CB  . PRO K  242 ? 0.7693 0.7618 0.8095 0.0688  0.0370  0.0379  242 PRO K CB  
20921 C CG  . PRO K  242 ? 0.7883 0.7800 0.8340 0.0681  0.0330  0.0374  242 PRO K CG  
20922 C CD  . PRO K  242 ? 0.8567 0.8477 0.9045 0.0706  0.0332  0.0392  242 PRO K CD  
20923 N N   . GLY K  243 ? 0.8975 0.8875 0.9334 0.0737  0.0476  0.0425  243 GLY K N   
20924 C CA  . GLY K  243 ? 0.8049 0.7978 0.8336 0.0754  0.0504  0.0443  243 GLY K CA  
20925 C C   . GLY K  243 ? 0.8545 0.8459 0.8858 0.0788  0.0524  0.0473  243 GLY K C   
20926 O O   . GLY K  243 ? 1.0371 1.0304 1.0633 0.0806  0.0550  0.0494  243 GLY K O   
20927 N N   . ASP K  244 ? 0.8334 0.8214 0.8726 0.0795  0.0512  0.0474  244 ASP K N   
20928 C CA  . ASP K  244 ? 0.7740 0.7597 0.8167 0.0825  0.0534  0.0500  244 ASP K CA  
20929 C C   . ASP K  244 ? 0.7530 0.7327 0.8026 0.0827  0.0573  0.0503  244 ASP K C   
20930 O O   . ASP K  244 ? 0.8445 0.8214 0.8981 0.0805  0.0574  0.0485  244 ASP K O   
20931 C CB  . ASP K  244 ? 0.7546 0.7402 0.8017 0.0830  0.0501  0.0498  244 ASP K CB  
20932 C CG  . ASP K  244 ? 1.0618 1.0461 1.1112 0.0862  0.0523  0.0525  244 ASP K CG  
20933 O OD1 . ASP K  244 ? 1.1872 1.1713 1.2396 0.0867  0.0501  0.0524  244 ASP K OD1 
20934 O OD2 . ASP K  244 ? 0.9983 0.9816 1.0463 0.0881  0.0563  0.0546  244 ASP K OD2 
20935 N N   . LYS K  245 ? 0.7915 0.7692 0.8427 0.0854  0.0607  0.0528  245 LYS K N   
20936 C CA  . LYS K  245 ? 0.8938 0.8657 0.9518 0.0858  0.0646  0.0533  245 LYS K CA  
20937 C C   . LYS K  245 ? 0.7534 0.7220 0.8185 0.0878  0.0653  0.0548  245 LYS K C   
20938 O O   . LYS K  245 ? 0.7211 0.6919 0.7842 0.0898  0.0644  0.0562  245 LYS K O   
20939 C CB  . LYS K  245 ? 0.9993 0.9709 1.0523 0.0869  0.0694  0.0549  245 LYS K CB  
20940 C CG  . LYS K  245 ? 0.9606 0.9339 1.0102 0.0903  0.0716  0.0582  245 LYS K CG  
20941 C CD  . LYS K  245 ? 0.9117 0.8845 0.9562 0.0909  0.0763  0.0598  245 LYS K CD  
20942 C CE  . LYS K  245 ? 1.2147 1.1892 1.2561 0.0944  0.0786  0.0636  245 LYS K CE  
20943 N NZ  . LYS K  245 ? 1.1569 1.1318 1.1923 0.0949  0.0828  0.0652  245 LYS K NZ  
20944 N N   . ILE K  246 ? 0.6639 0.6273 0.7377 0.0872  0.0670  0.0543  246 ILE K N   
20945 C CA  . ILE K  246 ? 0.6831 0.6429 0.7643 0.0887  0.0679  0.0553  246 ILE K CA  
20946 C C   . ILE K  246 ? 0.7660 0.7212 0.8510 0.0902  0.0734  0.0569  246 ILE K C   
20947 O O   . ILE K  246 ? 0.7305 0.6833 0.8177 0.0889  0.0755  0.0561  246 ILE K O   
20948 C CB  . ILE K  246 ? 0.6729 0.6308 0.7622 0.0864  0.0644  0.0532  246 ILE K CB  
20949 C CG1 . ILE K  246 ? 0.7821 0.7365 0.8789 0.0876  0.0655  0.0541  246 ILE K CG1 
20950 C CG2 . ILE K  246 ? 0.5671 0.5226 0.6611 0.0841  0.0649  0.0518  246 ILE K CG2 
20951 C CD1 . ILE K  246 ? 0.5972 0.5500 0.7020 0.0851  0.0620  0.0523  246 ILE K CD1 
20952 N N   . THR K  247 ? 0.9533 0.9072 1.0392 0.0930  0.0759  0.0592  247 THR K N   
20953 C CA  . THR K  247 ? 0.8896 0.8393 0.9785 0.0947  0.0814  0.0610  247 THR K CA  
20954 C C   . THR K  247 ? 0.7666 0.7114 0.8657 0.0950  0.0826  0.0610  247 THR K C   
20955 O O   . THR K  247 ? 0.7617 0.7068 0.8635 0.0954  0.0804  0.0609  247 THR K O   
20956 C CB  . THR K  247 ? 0.8183 0.7701 0.9002 0.0978  0.0844  0.0641  247 THR K CB  
20957 O OG1 . THR K  247 ? 0.9947 0.9506 1.0674 0.0973  0.0843  0.0642  247 THR K OG1 
20958 C CG2 . THR K  247 ? 1.0297 0.9766 1.1156 0.0998  0.0900  0.0662  247 THR K CG2 
20959 N N   . PHE K  248 ? 0.8369 0.7772 0.9419 0.0947  0.0861  0.0611  248 PHE K N   
20960 C CA  . PHE K  248 ? 0.8401 0.7756 0.9548 0.0951  0.0880  0.0614  248 PHE K CA  
20961 C C   . PHE K  248 ? 0.7831 0.7153 0.8980 0.0978  0.0940  0.0640  248 PHE K C   
20962 O O   . PHE K  248 ? 0.8287 0.7605 0.9395 0.0983  0.0972  0.0648  248 PHE K O   
20963 C CB  . PHE K  248 ? 0.6318 0.5646 0.7551 0.0924  0.0870  0.0594  248 PHE K CB  
20964 C CG  . PHE K  248 ? 0.7264 0.6619 0.8515 0.0897  0.0810  0.0572  248 PHE K CG  
20965 C CD1 . PHE K  248 ? 0.6942 0.6334 0.8134 0.0881  0.0781  0.0559  248 PHE K CD1 
20966 C CD2 . PHE K  248 ? 0.7686 0.7030 0.9011 0.0887  0.0785  0.0564  248 PHE K CD2 
20967 C CE1 . PHE K  248 ? 0.6261 0.5676 0.7468 0.0857  0.0727  0.0540  248 PHE K CE1 
20968 C CE2 . PHE K  248 ? 0.6501 0.5870 0.7838 0.0861  0.0730  0.0545  248 PHE K CE2 
20969 C CZ  . PHE K  248 ? 0.5452 0.4856 0.6731 0.0847  0.0701  0.0534  248 PHE K CZ  
20970 N N   . GLU K  249 ? 0.7458 0.6756 0.8652 0.0996  0.0957  0.0652  249 GLU K N   
20971 C CA  . GLU K  249 ? 0.8482 0.7747 0.9680 0.1024  0.1014  0.0678  249 GLU K CA  
20972 C C   . GLU K  249 ? 0.7702 0.6921 0.9000 0.1026  0.1030  0.0678  249 GLU K C   
20973 O O   . GLU K  249 ? 0.8579 0.7804 0.9896 0.1028  0.1010  0.0675  249 GLU K O   
20974 C CB  . GLU K  249 ? 0.9847 0.9146 1.0959 0.1053  0.1023  0.0705  249 GLU K CB  
20975 C CG  . GLU K  249 ? 1.1087 1.0357 1.2195 0.1084  0.1082  0.0737  249 GLU K CG  
20976 C CD  . GLU K  249 ? 1.3028 1.2338 1.4050 0.1113  0.1088  0.0767  249 GLU K CD  
20977 O OE1 . GLU K  249 ? 1.4615 1.3905 1.5645 0.1142  0.1129  0.0796  249 GLU K OE1 
20978 O OE2 . GLU K  249 ? 1.0610 0.9975 1.1561 0.1107  0.1051  0.0763  249 GLU K OE2 
20979 N N   . ALA K  250 ? 0.7533 0.6707 0.8897 0.1024  0.1068  0.0679  250 ALA K N   
20980 C CA  . ALA K  250 ? 0.7694 0.6823 0.9160 0.1022  0.1082  0.0675  250 ALA K CA  
20981 C C   . ALA K  250 ? 0.8550 0.7630 1.0058 0.1039  0.1146  0.0693  250 ALA K C   
20982 O O   . ALA K  250 ? 0.8704 0.7774 1.0191 0.1041  0.1174  0.0699  250 ALA K O   
20983 C CB  . ALA K  250 ? 0.7654 0.6782 0.9198 0.0987  0.1042  0.0648  250 ALA K CB  
20984 N N   . THR K  251 ? 0.8158 0.7205 0.9725 0.1050  0.1169  0.0701  251 THR K N   
20985 C CA  . THR K  251 ? 0.8088 0.7082 0.9714 0.1063  0.1227  0.0715  251 THR K CA  
20986 C C   . THR K  251 ? 0.8204 0.7168 0.9949 0.1038  0.1218  0.0694  251 THR K C   
20987 O O   . THR K  251 ? 0.8996 0.7915 1.0811 0.1045  0.1261  0.0701  251 THR K O   
20988 C CB  . THR K  251 ? 0.8705 0.7680 1.0315 0.1096  0.1268  0.0741  251 THR K CB  
20989 O OG1 . THR K  251 ? 0.9351 0.8338 1.0978 0.1093  0.1238  0.0731  251 THR K OG1 
20990 C CG2 . THR K  251 ? 0.7629 0.6632 0.9129 0.1124  0.1286  0.0769  251 THR K CG2 
20991 N N   . GLY K  252 ? 0.8382 0.7373 1.0149 0.1008  0.1162  0.0669  252 GLY K N   
20992 C CA  . GLY K  252 ? 0.8583 0.7557 1.0460 0.0980  0.1144  0.0651  252 GLY K CA  
20993 C C   . GLY K  252 ? 0.7960 0.6967 0.9849 0.0955  0.1081  0.0629  252 GLY K C   
20994 O O   . GLY K  252 ? 0.8299 0.7337 1.0114 0.0961  0.1055  0.0628  252 GLY K O   
20995 N N   . ASN K  253 ? 0.7253 0.6254 0.9237 0.0926  0.1056  0.0613  253 ASN K N   
20996 C CA  . ASN K  253 ? 0.6717 0.5745 0.8723 0.0898  0.0998  0.0592  253 ASN K CA  
20997 C C   . ASN K  253 ? 0.7586 0.6663 0.9528 0.0883  0.0943  0.0582  253 ASN K C   
20998 O O   . ASN K  253 ? 0.6796 0.5900 0.8735 0.0862  0.0894  0.0566  253 ASN K O   
20999 C CB  . ASN K  253 ? 0.6482 0.5504 0.8472 0.0907  0.1003  0.0591  253 ASN K CB  
21000 C CG  . ASN K  253 ? 0.7015 0.5987 0.9070 0.0920  0.1058  0.0601  253 ASN K CG  
21001 O OD1 . ASN K  253 ? 0.6921 0.5878 0.9050 0.0900  0.1051  0.0588  253 ASN K OD1 
21002 N ND2 . ASN K  253 ? 0.7449 0.6395 0.9476 0.0952  0.1114  0.0624  253 ASN K ND2 
21003 N N   . LEU K  254 ? 0.7460 0.6548 0.9348 0.0892  0.0953  0.0589  254 LEU K N   
21004 C CA  . LEU K  254 ? 0.6221 0.5354 0.8043 0.0880  0.0906  0.0579  254 LEU K CA  
21005 C C   . LEU K  254 ? 0.6209 0.5350 0.8086 0.0854  0.0880  0.0569  254 LEU K C   
21006 O O   . LEU K  254 ? 0.7301 0.6425 0.9193 0.0858  0.0912  0.0576  254 LEU K O   
21007 C CB  . LEU K  254 ? 0.6523 0.5671 0.8235 0.0905  0.0928  0.0591  254 LEU K CB  
21008 C CG  . LEU K  254 ? 0.6098 0.5291 0.7738 0.0893  0.0886  0.0581  254 LEU K CG  
21009 C CD1 . LEU K  254 ? 0.6270 0.5498 0.7890 0.0878  0.0830  0.0567  254 LEU K CD1 
21010 C CD2 . LEU K  254 ? 0.6195 0.5402 0.7729 0.0916  0.0912  0.0594  254 LEU K CD2 
21011 N N   . VAL K  255 ? 0.6477 0.5645 0.8387 0.0826  0.0824  0.0554  255 VAL K N   
21012 C CA  . VAL K  255 ? 0.5577 0.4761 0.7529 0.0801  0.0793  0.0547  255 VAL K CA  
21013 C C   . VAL K  255 ? 0.6036 0.5253 0.7891 0.0803  0.0774  0.0542  255 VAL K C   
21014 O O   . VAL K  255 ? 0.6170 0.5423 0.7975 0.0792  0.0728  0.0532  255 VAL K O   
21015 C CB  . VAL K  255 ? 0.5310 0.4515 0.7329 0.0769  0.0737  0.0534  255 VAL K CB  
21016 C CG1 . VAL K  255 ? 0.6154 0.5378 0.8221 0.0746  0.0706  0.0532  255 VAL K CG1 
21017 C CG2 . VAL K  255 ? 0.4771 0.3947 0.6883 0.0764  0.0755  0.0536  255 VAL K CG2 
21018 N N   . VAL K  256 ? 0.5803 0.5007 0.7630 0.0815  0.0812  0.0550  256 VAL K N   
21019 C CA  . VAL K  256 ? 0.6251 0.5483 0.7976 0.0819  0.0804  0.0546  256 VAL K CA  
21020 C C   . VAL K  256 ? 0.6338 0.5599 0.8076 0.0792  0.0757  0.0533  256 VAL K C   
21021 O O   . VAL K  256 ? 0.7459 0.6711 0.9292 0.0773  0.0745  0.0531  256 VAL K O   
21022 C CB  . VAL K  256 ? 0.7195 0.6403 0.8884 0.0836  0.0861  0.0556  256 VAL K CB  
21023 C CG1 . VAL K  256 ? 0.7303 0.6484 0.8976 0.0864  0.0909  0.0572  256 VAL K CG1 
21024 C CG2 . VAL K  256 ? 0.8474 0.7654 1.0253 0.0823  0.0883  0.0555  256 VAL K CG2 
21025 N N   . PRO K  257 ? 0.6901 0.6198 0.8544 0.0790  0.0730  0.0525  257 PRO K N   
21026 C CA  . PRO K  257 ? 0.5976 0.5300 0.7618 0.0766  0.0690  0.0513  257 PRO K CA  
21027 C C   . PRO K  257 ? 0.6851 0.6154 0.8520 0.0762  0.0724  0.0514  257 PRO K C   
21028 O O   . PRO K  257 ? 0.7397 0.6679 0.9028 0.0778  0.0774  0.0520  257 PRO K O   
21029 C CB  . PRO K  257 ? 0.5730 0.5092 0.7252 0.0771  0.0668  0.0506  257 PRO K CB  
21030 C CG  . PRO K  257 ? 0.6503 0.5865 0.7983 0.0793  0.0681  0.0514  257 PRO K CG  
21031 C CD  . PRO K  257 ? 0.6737 0.6054 0.8273 0.0809  0.0735  0.0528  257 PRO K CD  
21032 N N   . ARG K  258 ? 0.8212 0.7520 0.9947 0.0739  0.0698  0.0509  258 ARG K N   
21033 C CA  . ARG K  258 ? 0.7440 0.6730 0.9200 0.0733  0.0728  0.0509  258 ARG K CA  
21034 C C   . ARG K  258 ? 0.6390 0.5713 0.8098 0.0716  0.0693  0.0496  258 ARG K C   
21035 O O   . ARG K  258 ? 0.6410 0.5731 0.8056 0.0716  0.0718  0.0489  258 ARG K O   
21036 C CB  . ARG K  258 ? 0.7418 0.6682 0.9315 0.0723  0.0735  0.0518  258 ARG K CB  
21037 C CG  . ARG K  258 ? 0.7454 0.6697 0.9391 0.0715  0.0768  0.0518  258 ARG K CG  
21038 C CD  . ARG K  258 ? 0.8993 0.8215 1.1074 0.0706  0.0774  0.0530  258 ARG K CD  
21039 N NE  . ARG K  258 ? 0.9844 0.9061 1.1972 0.0693  0.0781  0.0530  258 ARG K NE  
21040 C CZ  . ARG K  258 ? 1.0653 0.9831 1.2811 0.0697  0.0840  0.0533  258 ARG K CZ  
21041 N NH1 . ARG K  258 ? 1.1367 1.0510 1.3512 0.0715  0.0894  0.0536  258 ARG K NH1 
21042 N NH2 . ARG K  258 ? 1.0356 0.9529 1.2560 0.0684  0.0846  0.0532  258 ARG K NH2 
21043 N N   . TYR K  259 ? 0.6896 0.6249 0.8628 0.0699  0.0635  0.0492  259 TYR K N   
21044 C CA  . TYR K  259 ? 0.6377 0.5764 0.8058 0.0682  0.0596  0.0481  259 TYR K CA  
21045 C C   . TYR K  259 ? 0.5750 0.5175 0.7347 0.0683  0.0553  0.0473  259 TYR K C   
21046 O O   . TYR K  259 ? 0.6485 0.5915 0.8104 0.0685  0.0531  0.0476  259 TYR K O   
21047 C CB  . TYR K  259 ? 0.7331 0.6724 0.9110 0.0660  0.0563  0.0485  259 TYR K CB  
21048 C CG  . TYR K  259 ? 0.7986 0.7347 0.9843 0.0657  0.0603  0.0492  259 TYR K CG  
21049 C CD1 . TYR K  259 ? 0.8423 0.7752 1.0385 0.0662  0.0631  0.0506  259 TYR K CD1 
21050 C CD2 . TYR K  259 ? 0.8865 0.8227 1.0695 0.0648  0.0615  0.0484  259 TYR K CD2 
21051 C CE1 . TYR K  259 ? 1.0146 0.9445 1.2184 0.0660  0.0671  0.0513  259 TYR K CE1 
21052 C CE2 . TYR K  259 ? 0.8793 0.8122 1.0697 0.0645  0.0656  0.0490  259 TYR K CE2 
21053 C CZ  . TYR K  259 ? 0.9457 0.8755 1.1466 0.0651  0.0684  0.0505  259 TYR K CZ  
21054 O OH  . TYR K  259 ? 1.1112 1.0377 1.3200 0.0649  0.0727  0.0512  259 TYR K OH  
21055 N N   . ALA K  260 ? 0.6279 0.5729 0.7779 0.0681  0.0544  0.0461  260 ALA K N   
21056 C CA  . ALA K  260 ? 0.6862 0.6352 0.8283 0.0680  0.0502  0.0453  260 ALA K CA  
21057 C C   . ALA K  260 ? 0.6135 0.5653 0.7550 0.0656  0.0457  0.0443  260 ALA K C   
21058 O O   . ALA K  260 ? 0.6865 0.6371 0.8343 0.0642  0.0459  0.0444  260 ALA K O   
21059 C CB  . ALA K  260 ? 0.6722 0.6225 0.8032 0.0698  0.0526  0.0450  260 ALA K CB  
21060 N N   . PHE K  261 ? 0.7137 0.6691 0.8477 0.0652  0.0418  0.0433  261 PHE K N   
21061 C CA  . PHE K  261 ? 0.5563 0.5145 0.6893 0.0629  0.0374  0.0424  261 PHE K CA  
21062 C C   . PHE K  261 ? 0.6049 0.5666 0.7265 0.0630  0.0362  0.0410  261 PHE K C   
21063 O O   . PHE K  261 ? 0.6723 0.6363 0.7882 0.0636  0.0339  0.0407  261 PHE K O   
21064 C CB  . PHE K  261 ? 0.4290 0.3886 0.5674 0.0614  0.0323  0.0426  261 PHE K CB  
21065 C CG  . PHE K  261 ? 0.5481 0.5049 0.6982 0.0609  0.0328  0.0439  261 PHE K CG  
21066 C CD1 . PHE K  261 ? 0.6654 0.6203 0.8189 0.0621  0.0344  0.0446  261 PHE K CD1 
21067 C CD2 . PHE K  261 ? 0.5722 0.5285 0.7304 0.0592  0.0319  0.0446  261 PHE K CD2 
21068 C CE1 . PHE K  261 ? 0.6575 0.6102 0.8220 0.0615  0.0349  0.0458  261 PHE K CE1 
21069 C CE2 . PHE K  261 ? 0.5102 0.4646 0.6797 0.0587  0.0323  0.0461  261 PHE K CE2 
21070 C CZ  . PHE K  261 ? 0.5848 0.5375 0.7574 0.0598  0.0337  0.0466  261 PHE K CZ  
21071 N N   . ALA K  262 ? 0.6635 0.6254 0.7817 0.0623  0.0379  0.0402  262 ALA K N   
21072 C CA  . ALA K  262 ? 0.6524 0.6180 0.7607 0.0616  0.0360  0.0387  262 ALA K CA  
21073 C C   . ALA K  262 ? 0.7370 0.7051 0.8466 0.0597  0.0303  0.0382  262 ALA K C   
21074 O O   . ALA K  262 ? 0.7546 0.7218 0.8713 0.0580  0.0288  0.0385  262 ALA K O   
21075 C CB  . ALA K  262 ? 0.8111 0.7760 0.9166 0.0608  0.0392  0.0378  262 ALA K CB  
21076 N N   . MET K  263 ? 0.6599 0.6312 0.7630 0.0599  0.0271  0.0376  263 MET K N   
21077 C CA  . MET K  263 ? 0.7038 0.6773 0.8079 0.0580  0.0217  0.0371  263 MET K CA  
21078 C C   . MET K  263 ? 0.7637 0.7413 0.8582 0.0579  0.0189  0.0359  263 MET K C   
21079 O O   . MET K  263 ? 0.9027 0.8815 0.9914 0.0597  0.0201  0.0359  263 MET K O   
21080 C CB  . MET K  263 ? 0.7055 0.6777 0.8171 0.0578  0.0197  0.0381  263 MET K CB  
21081 C CG  . MET K  263 ? 0.7202 0.6944 0.8272 0.0584  0.0173  0.0377  263 MET K CG  
21082 S SD  . MET K  263 ? 0.7224 0.6944 0.8382 0.0579  0.0159  0.0386  263 MET K SD  
21083 C CE  . MET K  263 ? 0.8451 0.8187 0.9534 0.0592  0.0151  0.0379  263 MET K CE  
21084 N N   . GLU K  264 ? 0.7638 0.7435 0.8569 0.0558  0.0154  0.0349  264 GLU K N   
21085 C CA  . GLU K  264 ? 0.7902 0.7737 0.8752 0.0553  0.0122  0.0337  264 GLU K CA  
21086 C C   . GLU K  264 ? 0.7484 0.7327 0.8367 0.0535  0.0074  0.0336  264 GLU K C   
21087 O O   . GLU K  264 ? 0.8526 0.8365 0.9461 0.0515  0.0050  0.0338  264 GLU K O   
21088 C CB  . GLU K  264 ? 0.8698 0.8552 0.9498 0.0539  0.0121  0.0324  264 GLU K CB  
21089 C CG  . GLU K  264 ? 1.0818 1.0695 1.1525 0.0553  0.0146  0.0316  264 GLU K CG  
21090 C CD  . GLU K  264 ? 1.3307 1.3186 1.3984 0.0540  0.0165  0.0305  264 GLU K CD  
21091 O OE1 . GLU K  264 ? 1.3560 1.3474 1.4167 0.0530  0.0149  0.0291  264 GLU K OE1 
21092 O OE2 . GLU K  264 ? 1.3828 1.3675 1.4556 0.0538  0.0198  0.0308  264 GLU K OE2 
21093 N N   . ARG K  265 ? 0.8680 0.8534 0.9535 0.0543  0.0059  0.0335  265 ARG K N   
21094 C CA  . ARG K  265 ? 0.8625 0.8485 0.9506 0.0525  0.0016  0.0333  265 ARG K CA  
21095 C C   . ARG K  265 ? 0.9673 0.9568 1.0476 0.0516  -0.0017 0.0319  265 ARG K C   
21096 O O   . ARG K  265 ? 0.9692 0.9607 1.0422 0.0531  -0.0003 0.0313  265 ARG K O   
21097 C CB  . ARG K  265 ? 0.6689 0.6529 0.7607 0.0536  0.0025  0.0340  265 ARG K CB  
21098 C CG  . ARG K  265 ? 0.7584 0.7421 0.8455 0.0566  0.0064  0.0343  265 ARG K CG  
21099 C CD  . ARG K  265 ? 0.8813 0.8628 0.9724 0.0576  0.0075  0.0349  265 ARG K CD  
21100 N NE  . ARG K  265 ? 0.9770 0.9601 1.0626 0.0581  0.0063  0.0342  265 ARG K NE  
21101 C CZ  . ARG K  265 ? 0.9219 0.9059 1.0020 0.0607  0.0090  0.0346  265 ARG K CZ  
21102 N NH1 . ARG K  265 ? 0.9487 0.9322 1.0274 0.0629  0.0129  0.0357  265 ARG K NH1 
21103 N NH2 . ARG K  265 ? 0.9184 0.9038 0.9943 0.0611  0.0079  0.0340  265 ARG K NH2 
21104 N N   . ASN K  266 ? 1.0222 1.0126 1.1044 0.0491  -0.0060 0.0314  266 ASN K N   
21105 C CA  . ASN K  266 ? 1.0917 1.0850 1.1674 0.0479  -0.0094 0.0301  266 ASN K CA  
21106 C C   . ASN K  266 ? 1.0884 1.0814 1.1639 0.0478  -0.0108 0.0298  266 ASN K C   
21107 O O   . ASN K  266 ? 1.0902 1.0811 1.1688 0.0494  -0.0083 0.0305  266 ASN K O   
21108 C CB  . ASN K  266 ? 1.1289 1.1234 1.2060 0.0450  -0.0132 0.0298  266 ASN K CB  
21109 C CG  . ASN K  266 ? 1.2045 1.1967 1.2904 0.0441  -0.0128 0.0313  266 ASN K CG  
21110 O OD1 . ASN K  266 ? 1.0700 1.0626 1.1568 0.0433  -0.0129 0.0314  266 ASN K OD1 
21111 N ND2 . ASN K  266 ? 1.1509 1.1409 1.2439 0.0443  -0.0123 0.0324  266 ASN K ND2 
21112 N N   . ALA K  267 ? 1.0337 1.0287 1.1054 0.0460  -0.0144 0.0286  267 ALA K N   
21113 C CA  . ALA K  267 ? 1.0593 1.0536 1.1318 0.0450  -0.0161 0.0281  267 ALA K CA  
21114 C C   . ALA K  267 ? 1.0796 1.0729 1.1594 0.0422  -0.0192 0.0288  267 ALA K C   
21115 O O   . ALA K  267 ? 1.0641 1.0550 1.1507 0.0422  -0.0182 0.0298  267 ALA K O   
21116 C CB  . ALA K  267 ? 1.0617 1.0585 1.1270 0.0441  -0.0185 0.0266  267 ALA K CB  
21117 N N   . GLY K  268 ? 1.0414 1.0366 1.1198 0.0397  -0.0230 0.0284  268 GLY K N   
21118 C CA  . GLY K  268 ? 1.1778 1.1726 1.2631 0.0371  -0.0261 0.0294  268 GLY K CA  
21119 C C   . GLY K  268 ? 1.2332 1.2264 1.3240 0.0357  -0.0272 0.0298  268 GLY K C   
21120 O O   . GLY K  268 ? 1.1084 1.1011 1.1962 0.0358  -0.0269 0.0286  268 GLY K O   
21121 N N   . SER K  269 ? 1.0389 1.0313 1.1381 0.0345  -0.0282 0.0315  269 SER K N   
21122 C CA  . SER K  269 ? 0.8776 0.8699 0.9826 0.0316  -0.0314 0.0320  269 SER K CA  
21123 C C   . SER K  269 ? 0.8969 0.8871 1.0054 0.0320  -0.0296 0.0318  269 SER K C   
21124 O O   . SER K  269 ? 1.0203 1.0088 1.1261 0.0346  -0.0257 0.0311  269 SER K O   
21125 C CB  . SER K  269 ? 0.8643 0.8570 0.9778 0.0305  -0.0329 0.0344  269 SER K CB  
21126 O OG  . SER K  269 ? 0.8166 0.8076 0.9333 0.0333  -0.0287 0.0354  269 SER K OG  
21127 N N   . GLY K  270 ? 0.5039 0.4943 0.6187 0.0291  -0.0325 0.0325  270 GLY K N   
21128 C CA  . GLY K  270 ? 0.5908 0.5791 0.7108 0.0288  -0.0312 0.0325  270 GLY K CA  
21129 C C   . GLY K  270 ? 0.5084 0.4967 0.6390 0.0279  -0.0320 0.0349  270 GLY K C   
21130 O O   . GLY K  270 ? 0.5476 0.5362 0.6813 0.0289  -0.0315 0.0366  270 GLY K O   
21131 N N   . ILE K  271 ? 0.4891 0.4768 0.6254 0.0259  -0.0330 0.0351  271 ILE K N   
21132 C CA  . ILE K  271 ? 0.3780 0.3660 0.5250 0.0249  -0.0338 0.0375  271 ILE K CA  
21133 C C   . ILE K  271 ? 0.6176 0.6082 0.7679 0.0204  -0.0392 0.0379  271 ILE K C   
21134 O O   . ILE K  271 ? 0.7143 0.7047 0.8607 0.0183  -0.0405 0.0359  271 ILE K O   
21135 C CB  . ILE K  271 ? 0.4308 0.4155 0.5834 0.0273  -0.0290 0.0379  271 ILE K CB  
21136 C CG1 . ILE K  271 ? 0.4794 0.4637 0.6365 0.0246  -0.0302 0.0373  271 ILE K CG1 
21137 C CG2 . ILE K  271 ? 0.5628 0.5450 0.7084 0.0310  -0.0240 0.0364  271 ILE K CG2 
21138 C CD1 . ILE K  271 ? 0.6200 0.6053 0.7885 0.0230  -0.0318 0.0397  271 ILE K CD1 
21139 N N   . ILE K  272 ? 0.6262 0.6192 0.7831 0.0188  -0.0424 0.0405  272 ILE K N   
21140 C CA  . ILE K  272 ? 0.6173 0.6133 0.7778 0.0143  -0.0479 0.0414  272 ILE K CA  
21141 C C   . ILE K  272 ? 0.5675 0.5636 0.7395 0.0134  -0.0479 0.0434  272 ILE K C   
21142 O O   . ILE K  272 ? 0.6121 0.6077 0.7916 0.0155  -0.0458 0.0458  272 ILE K O   
21143 C CB  . ILE K  272 ? 0.5763 0.5758 0.7364 0.0127  -0.0523 0.0433  272 ILE K CB  
21144 C CG1 . ILE K  272 ? 0.6067 0.6064 0.7553 0.0130  -0.0529 0.0411  272 ILE K CG1 
21145 C CG2 . ILE K  272 ? 0.6274 0.6305 0.7923 0.0081  -0.0581 0.0448  272 ILE K CG2 
21146 C CD1 . ILE K  272 ? 0.6634 0.6662 0.8109 0.0113  -0.0571 0.0427  272 ILE K CD1 
21147 N N   . ILE K  273 ? 0.5550 0.5517 0.7284 0.0103  -0.0498 0.0424  273 ILE K N   
21148 C CA  . ILE K  273 ? 0.6967 0.6942 0.8811 0.0088  -0.0505 0.0443  273 ILE K CA  
21149 C C   . ILE K  273 ? 0.8150 0.8173 1.0037 0.0045  -0.0570 0.0466  273 ILE K C   
21150 O O   . ILE K  273 ? 0.8968 0.9011 1.0816 0.0005  -0.0608 0.0452  273 ILE K O   
21151 C CB  . ILE K  273 ? 0.6851 0.6803 0.8695 0.0077  -0.0485 0.0419  273 ILE K CB  
21152 C CG1 . ILE K  273 ? 0.6246 0.6151 0.8050 0.0121  -0.0419 0.0400  273 ILE K CG1 
21153 C CG2 . ILE K  273 ? 0.8072 0.8036 1.0032 0.0057  -0.0495 0.0439  273 ILE K CG2 
21154 C CD1 . ILE K  273 ? 1.0090 0.9981 1.1773 0.0129  -0.0409 0.0371  273 ILE K CD1 
21155 N N   . SER K  274 ? 0.8906 0.8949 1.0873 0.0052  -0.0580 0.0502  274 SER K N   
21156 C CA  . SER K  274 ? 0.7333 0.7426 0.9344 0.0016  -0.0642 0.0531  274 SER K CA  
21157 C C   . SER K  274 ? 0.8146 0.8256 1.0289 0.0025  -0.0643 0.0574  274 SER K C   
21158 O O   . SER K  274 ? 0.8766 0.8846 1.0951 0.0063  -0.0595 0.0582  274 SER K O   
21159 C CB  . SER K  274 ? 0.7093 0.7201 0.9023 0.0015  -0.0666 0.0530  274 SER K CB  
21160 O OG  . SER K  274 ? 0.9013 0.9165 1.1003 -0.0007 -0.0715 0.0568  274 SER K OG  
21161 N N   . ASP K  275 ? 1.1178 1.1335 1.3386 -0.0013 -0.0697 0.0602  275 ASP K N   
21162 C CA  . ASP K  275 ? 1.1217 1.1399 1.3557 -0.0009 -0.0705 0.0648  275 ASP K CA  
21163 C C   . ASP K  275 ? 0.9209 0.9409 1.1551 0.0001  -0.0723 0.0677  275 ASP K C   
21164 O O   . ASP K  275 ? 1.1549 1.1753 1.3988 0.0020  -0.0710 0.0712  275 ASP K O   
21165 C CB  . ASP K  275 ? 1.2909 1.3139 1.5324 -0.0055 -0.0758 0.0669  275 ASP K CB  
21166 C CG  . ASP K  275 ? 1.4942 1.5154 1.7361 -0.0069 -0.0741 0.0640  275 ASP K CG  
21167 O OD1 . ASP K  275 ? 1.6101 1.6320 1.8443 -0.0103 -0.0766 0.0611  275 ASP K OD1 
21168 O OD2 . ASP K  275 ? 1.4204 1.4393 1.6702 -0.0046 -0.0699 0.0646  275 ASP K OD2 
21169 N N   . THR K  276 ? 0.7789 0.7998 1.0026 -0.0012 -0.0750 0.0661  276 THR K N   
21170 C CA  . THR K  276 ? 0.7693 0.7921 0.9921 -0.0008 -0.0770 0.0685  276 THR K CA  
21171 C C   . THR K  276 ? 0.8718 0.8917 1.0997 0.0037  -0.0720 0.0701  276 THR K C   
21172 O O   . THR K  276 ? 0.9380 0.9533 1.1631 0.0070  -0.0663 0.0676  276 THR K O   
21173 C CB  . THR K  276 ? 0.6996 0.7219 0.9084 -0.0016 -0.0784 0.0653  276 THR K CB  
21174 O OG1 . THR K  276 ? 0.6661 0.6907 0.8698 -0.0059 -0.0827 0.0635  276 THR K OG1 
21175 C CG2 . THR K  276 ? 0.7708 0.7954 0.9790 -0.0016 -0.0809 0.0680  276 THR K CG2 
21176 N N   . PRO K  277 ? 0.8890 0.9115 1.1243 0.0037  -0.0739 0.0744  277 PRO K N   
21177 C CA  . PRO K  277 ? 0.8392 0.8594 1.0803 0.0074  -0.0695 0.0765  277 PRO K CA  
21178 C C   . PRO K  277 ? 0.8316 0.8478 1.0621 0.0101  -0.0655 0.0733  277 PRO K C   
21179 O O   . PRO K  277 ? 0.8643 0.8816 1.0852 0.0088  -0.0682 0.0718  277 PRO K O   
21180 C CB  . PRO K  277 ? 0.9972 1.0220 1.2457 0.0057  -0.0740 0.0814  277 PRO K CB  
21181 C CG  . PRO K  277 ? 1.1173 1.1471 1.3691 0.0014  -0.0801 0.0830  277 PRO K CG  
21182 C CD  . PRO K  277 ? 0.8490 0.8774 1.0888 -0.0003 -0.0807 0.0780  277 PRO K CD  
21183 N N   . VAL K  278 ? 0.7637 0.7756 0.9960 0.0138  -0.0592 0.0724  278 VAL K N   
21184 C CA  . VAL K  278 ? 0.8517 0.8603 1.0756 0.0164  -0.0553 0.0700  278 VAL K CA  
21185 C C   . VAL K  278 ? 0.8900 0.8999 1.1181 0.0166  -0.0561 0.0732  278 VAL K C   
21186 O O   . VAL K  278 ? 0.9849 0.9964 1.2250 0.0165  -0.0567 0.0773  278 VAL K O   
21187 C CB  . VAL K  278 ? 0.7687 0.7724 0.9931 0.0200  -0.0483 0.0681  278 VAL K CB  
21188 C CG1 . VAL K  278 ? 0.9968 0.9999 1.2353 0.0213  -0.0458 0.0716  278 VAL K CG1 
21189 C CG2 . VAL K  278 ? 0.6376 0.6385 0.8533 0.0224  -0.0445 0.0658  278 VAL K CG2 
21190 N N   . HIS K  279 ? 0.8894 0.8988 1.1081 0.0170  -0.0560 0.0714  279 HIS K N   
21191 C CA  . HIS K  279 ? 0.8993 0.9100 1.1210 0.0168  -0.0571 0.0742  279 HIS K CA  
21192 C C   . HIS K  279 ? 0.8753 0.8827 1.0898 0.0192  -0.0526 0.0719  279 HIS K C   
21193 O O   . HIS K  279 ? 1.1497 1.1547 1.3540 0.0202  -0.0502 0.0678  279 HIS K O   
21194 C CB  . HIS K  279 ? 1.1071 1.1223 1.3252 0.0134  -0.0640 0.0755  279 HIS K CB  
21195 C CG  . HIS K  279 ? 1.2520 1.2714 1.4819 0.0114  -0.0683 0.0807  279 HIS K CG  
21196 N ND1 . HIS K  279 ? 1.0969 1.1181 1.3329 0.0114  -0.0694 0.0847  279 HIS K ND1 
21197 C CD2 . HIS K  279 ? 1.2679 1.2904 1.5047 0.0092  -0.0718 0.0828  279 HIS K CD2 
21198 C CE1 . HIS K  279 ? 1.3206 1.3459 1.5670 0.0094  -0.0735 0.0893  279 HIS K CE1 
21199 N NE2 . HIS K  279 ? 1.3293 1.3557 1.5763 0.0080  -0.0752 0.0881  279 HIS K NE2 
21200 N N   . ASP K  280 ? 0.9862 0.9934 1.2063 0.0198  -0.0515 0.0746  280 ASP K N   
21201 C CA  . ASP K  280 ? 1.1152 1.1198 1.3287 0.0213  -0.0479 0.0726  280 ASP K CA  
21202 C C   . ASP K  280 ? 1.1357 1.1431 1.3414 0.0192  -0.0524 0.0723  280 ASP K C   
21203 O O   . ASP K  280 ? 1.3070 1.3157 1.5170 0.0186  -0.0538 0.0753  280 ASP K O   
21204 C CB  . ASP K  280 ? 1.2064 1.2089 1.4298 0.0231  -0.0437 0.0754  280 ASP K CB  
21205 C CG  . ASP K  280 ? 1.4124 1.4126 1.6294 0.0241  -0.0403 0.0735  280 ASP K CG  
21206 O OD1 . ASP K  280 ? 1.4288 1.4285 1.6334 0.0239  -0.0403 0.0696  280 ASP K OD1 
21207 O OD2 . ASP K  280 ? 1.5954 1.5942 1.8198 0.0249  -0.0375 0.0759  280 ASP K OD2 
21208 N N   . CYS K  281 ? 1.0494 1.0574 1.2437 0.0182  -0.0546 0.0688  281 CYS K N   
21209 C CA  . CYS K  281 ? 1.0333 1.0437 1.2190 0.0161  -0.0587 0.0680  281 CYS K CA  
21210 C C   . CYS K  281 ? 0.9493 0.9583 1.1216 0.0166  -0.0573 0.0630  281 CYS K C   
21211 O O   . CYS K  281 ? 1.0023 1.0092 1.1723 0.0181  -0.0545 0.0605  281 CYS K O   
21212 C CB  . CYS K  281 ? 0.9546 0.9694 1.1429 0.0129  -0.0654 0.0705  281 CYS K CB  
21213 S SG  . CYS K  281 ? 1.3246 1.3399 1.5118 0.0117  -0.0671 0.0686  281 CYS K SG  
21214 N N   . ASN K  282 ? 0.9216 0.9316 1.0852 0.0156  -0.0592 0.0616  282 ASN K N   
21215 C CA  . ASN K  282 ? 0.7614 0.7706 0.9125 0.0159  -0.0584 0.0571  282 ASN K CA  
21216 C C   . ASN K  282 ? 0.7577 0.7696 0.9030 0.0132  -0.0636 0.0561  282 ASN K C   
21217 O O   . ASN K  282 ? 0.8741 0.8888 1.0233 0.0106  -0.0683 0.0589  282 ASN K O   
21218 C CB  . ASN K  282 ? 0.9380 0.9465 1.0824 0.0165  -0.0566 0.0555  282 ASN K CB  
21219 C CG  . ASN K  282 ? 1.2219 1.2271 1.3627 0.0193  -0.0505 0.0527  282 ASN K CG  
21220 O OD1 . ASN K  282 ? 1.2328 1.2368 1.3707 0.0206  -0.0484 0.0505  282 ASN K OD1 
21221 N ND2 . ASN K  282 ? 1.4720 1.4759 1.6131 0.0201  -0.0475 0.0528  282 ASN K ND2 
21222 N N   . THR K  283 ? 0.8559 0.8669 0.9922 0.0136  -0.0625 0.0523  283 THR K N   
21223 C CA  . THR K  283 ? 0.7743 0.7871 0.9039 0.0111  -0.0666 0.0507  283 THR K CA  
21224 C C   . THR K  283 ? 0.6018 0.6132 0.7207 0.0125  -0.0640 0.0464  283 THR K C   
21225 O O   . THR K  283 ? 0.6121 0.6211 0.7301 0.0154  -0.0592 0.0450  283 THR K O   
21226 C CB  . THR K  283 ? 0.7074 0.7210 0.8427 0.0097  -0.0686 0.0517  283 THR K CB  
21227 O OG1 . THR K  283 ? 0.4825 0.4981 0.6115 0.0066  -0.0729 0.0503  283 THR K OG1 
21228 C CG2 . THR K  283 ? 0.6465 0.6573 0.7825 0.0123  -0.0640 0.0498  283 THR K CG2 
21229 N N   . THR K  284 ? 0.5174 0.5303 0.6281 0.0105  -0.0670 0.0445  284 THR K N   
21230 C CA  . THR K  284 ? 0.7394 0.7512 0.8402 0.0117  -0.0648 0.0407  284 THR K CA  
21231 C C   . THR K  284 ? 0.7046 0.7161 0.8036 0.0106  -0.0657 0.0391  284 THR K C   
21232 O O   . THR K  284 ? 0.6085 0.6189 0.7008 0.0119  -0.0635 0.0362  284 THR K O   
21233 C CB  . THR K  284 ? 0.5986 0.6119 0.6907 0.0103  -0.0669 0.0393  284 THR K CB  
21234 O OG1 . THR K  284 ? 0.7001 0.7125 0.7833 0.0119  -0.0642 0.0358  284 THR K OG1 
21235 C CG2 . THR K  284 ? 0.6046 0.6201 0.6950 0.0065  -0.0723 0.0399  284 THR K CG2 
21236 N N   . CYS K  285 ? 0.5203 0.5330 0.6257 0.0082  -0.0689 0.0412  285 CYS K N   
21237 C CA  . CYS K  285 ? 0.4509 0.4633 0.5555 0.0067  -0.0700 0.0398  285 CYS K CA  
21238 C C   . CYS K  285 ? 0.5150 0.5278 0.6303 0.0058  -0.0710 0.0425  285 CYS K C   
21239 O O   . CYS K  285 ? 0.5639 0.5790 0.6852 0.0038  -0.0745 0.0456  285 CYS K O   
21240 C CB  . CYS K  285 ? 0.4476 0.4620 0.5453 0.0030  -0.0744 0.0386  285 CYS K CB  
21241 S SG  . CYS K  285 ? 0.6290 0.6430 0.7254 0.0003  -0.0757 0.0366  285 CYS K SG  
21242 N N   . GLN K  286 ? 0.5020 0.5126 0.6198 0.0073  -0.0680 0.0415  286 GLN K N   
21243 C CA  . GLN K  286 ? 0.3777 0.3884 0.5059 0.0068  -0.0682 0.0438  286 GLN K CA  
21244 C C   . GLN K  286 ? 0.5371 0.5477 0.6650 0.0045  -0.0694 0.0423  286 GLN K C   
21245 O O   . GLN K  286 ? 0.6975 0.7059 0.8196 0.0055  -0.0667 0.0392  286 GLN K O   
21246 C CB  . GLN K  286 ? 0.3822 0.3903 0.5159 0.0107  -0.0629 0.0445  286 GLN K CB  
21247 C CG  . GLN K  286 ? 0.5008 0.5090 0.6462 0.0105  -0.0629 0.0472  286 GLN K CG  
21248 C CD  . GLN K  286 ? 0.5943 0.6055 0.7471 0.0086  -0.0668 0.0511  286 GLN K CD  
21249 O OE1 . GLN K  286 ? 0.6769 0.6882 0.8308 0.0099  -0.0661 0.0526  286 GLN K OE1 
21250 N NE2 . GLN K  286 ? 0.4593 0.4730 0.6174 0.0053  -0.0710 0.0528  286 GLN K NE2 
21251 N N   . THR K  287 ? 0.5477 0.5607 0.6822 0.0013  -0.0734 0.0445  287 THR K N   
21252 C CA  . THR K  287 ? 0.5464 0.5595 0.6820 -0.0014 -0.0746 0.0432  287 THR K CA  
21253 C C   . THR K  287 ? 0.5465 0.5598 0.6939 -0.0011 -0.0741 0.0459  287 THR K C   
21254 O O   . THR K  287 ? 0.5509 0.5652 0.7059 0.0002  -0.0741 0.0491  287 THR K O   
21255 C CB  . THR K  287 ? 0.6104 0.6267 0.7422 -0.0064 -0.0804 0.0431  287 THR K CB  
21256 O OG1 . THR K  287 ? 0.4501 0.4699 0.5911 -0.0089 -0.0845 0.0469  287 THR K OG1 
21257 C CG2 . THR K  287 ? 0.5072 0.5245 0.6303 -0.0067 -0.0821 0.0423  287 THR K CG2 
21258 N N   . PRO K  288 ? 0.5959 0.6082 0.7452 -0.0025 -0.0734 0.0444  288 PRO K N   
21259 C CA  . PRO K  288 ? 0.6684 0.6811 0.8292 -0.0026 -0.0730 0.0467  288 PRO K CA  
21260 C C   . PRO K  288 ? 0.6031 0.6204 0.7717 -0.0057 -0.0784 0.0507  288 PRO K C   
21261 O O   . PRO K  288 ? 0.6864 0.7044 0.8657 -0.0049 -0.0779 0.0537  288 PRO K O   
21262 C CB  . PRO K  288 ? 0.6679 0.6791 0.8268 -0.0046 -0.0722 0.0438  288 PRO K CB  
21263 C CG  . PRO K  288 ? 0.5442 0.5526 0.6917 -0.0031 -0.0694 0.0400  288 PRO K CG  
21264 C CD  . PRO K  288 ? 0.5691 0.5793 0.7101 -0.0035 -0.0721 0.0403  288 PRO K CD  
21265 N N   . LYS K  289 ? 0.5180 0.5384 0.6814 -0.0093 -0.0835 0.0508  289 LYS K N   
21266 C CA  . LYS K  289 ? 0.6315 0.6570 0.8018 -0.0127 -0.0891 0.0548  289 LYS K CA  
21267 C C   . LYS K  289 ? 0.5782 0.6050 0.7515 -0.0107 -0.0898 0.0583  289 LYS K C   
21268 O O   . LYS K  289 ? 0.7109 0.7410 0.8935 -0.0117 -0.0926 0.0626  289 LYS K O   
21269 C CB  . LYS K  289 ? 0.6771 0.7054 0.8402 -0.0179 -0.0944 0.0535  289 LYS K CB  
21270 C CG  . LYS K  289 ? 0.7543 0.7813 0.9145 -0.0205 -0.0938 0.0499  289 LYS K CG  
21271 C CD  . LYS K  289 ? 0.8520 0.8808 1.0028 -0.0254 -0.0980 0.0476  289 LYS K CD  
21272 C CE  . LYS K  289 ? 0.9205 0.9552 1.0761 -0.0302 -0.1047 0.0512  289 LYS K CE  
21273 N NZ  . LYS K  289 ? 0.9668 1.0031 1.1132 -0.0356 -0.1086 0.0486  289 LYS K NZ  
21274 N N   . GLY K  290 ? 0.5260 0.5503 0.6916 -0.0079 -0.0870 0.0564  290 GLY K N   
21275 C CA  . GLY K  290 ? 0.5017 0.5267 0.6690 -0.0060 -0.0869 0.0590  290 GLY K CA  
21276 C C   . GLY K  290 ? 0.6286 0.6514 0.7845 -0.0044 -0.0850 0.0560  290 GLY K C   
21277 O O   . GLY K  290 ? 0.6666 0.6880 0.8133 -0.0051 -0.0844 0.0522  290 GLY K O   
21278 N N   . ALA K  291 ? 0.6017 0.6244 0.7585 -0.0023 -0.0840 0.0578  291 ALA K N   
21279 C CA  . ALA K  291 ? 0.6032 0.6242 0.7499 -0.0007 -0.0820 0.0551  291 ALA K CA  
21280 C C   . ALA K  291 ? 0.6609 0.6846 0.8004 -0.0041 -0.0869 0.0550  291 ALA K C   
21281 O O   . ALA K  291 ? 0.6502 0.6775 0.7937 -0.0073 -0.0918 0.0579  291 ALA K O   
21282 C CB  . ALA K  291 ? 0.5290 0.5484 0.6794 0.0028  -0.0784 0.0567  291 ALA K CB  
21283 N N   . ILE K  292 ? 0.6305 0.6527 0.7593 -0.0033 -0.0856 0.0517  292 ILE K N   
21284 C CA  . ILE K  292 ? 0.5737 0.5982 0.6948 -0.0063 -0.0896 0.0512  292 ILE K CA  
21285 C C   . ILE K  292 ? 0.7916 0.8154 0.9086 -0.0043 -0.0881 0.0512  292 ILE K C   
21286 O O   . ILE K  292 ? 0.8605 0.8818 0.9716 -0.0016 -0.0841 0.0483  292 ILE K O   
21287 C CB  . ILE K  292 ? 0.4973 0.5209 0.6085 -0.0082 -0.0901 0.0470  292 ILE K CB  
21288 C CG1 . ILE K  292 ? 0.3900 0.4144 0.5049 -0.0108 -0.0919 0.0469  292 ILE K CG1 
21289 C CG2 . ILE K  292 ? 0.6986 0.7242 0.8015 -0.0111 -0.0939 0.0464  292 ILE K CG2 
21290 C CD1 . ILE K  292 ? 0.7035 0.7268 0.8093 -0.0129 -0.0920 0.0427  292 ILE K CD1 
21291 N N   . ASN K  293 ? 1.0616 1.0879 1.1819 -0.0058 -0.0914 0.0547  293 ASN K N   
21292 C CA  . ASN K  293 ? 1.1804 1.2065 1.2970 -0.0046 -0.0906 0.0549  293 ASN K CA  
21293 C C   . ASN K  293 ? 1.2305 1.2585 1.3379 -0.0078 -0.0945 0.0537  293 ASN K C   
21294 O O   . ASN K  293 ? 1.3403 1.3713 1.4498 -0.0106 -0.0990 0.0568  293 ASN K O   
21295 C CB  . ASN K  293 ? 1.2931 1.3205 1.4201 -0.0041 -0.0913 0.0598  293 ASN K CB  
21296 C CG  . ASN K  293 ? 1.4761 1.5031 1.6003 -0.0029 -0.0901 0.0603  293 ASN K CG  
21297 O OD1 . ASN K  293 ? 1.3713 1.3966 1.4863 -0.0020 -0.0880 0.0568  293 ASN K OD1 
21298 N ND2 . ASN K  293 ? 1.4782 1.5067 1.6106 -0.0031 -0.0914 0.0648  293 ASN K ND2 
21299 N N   . THR K  294 ? 1.0607 1.0870 1.1578 -0.0075 -0.0928 0.0494  294 THR K N   
21300 C CA  . THR K  294 ? 1.2155 1.2433 1.3035 -0.0107 -0.0964 0.0477  294 THR K CA  
21301 C C   . THR K  294 ? 1.0495 1.0758 1.1272 -0.0094 -0.0939 0.0441  294 THR K C   
21302 O O   . THR K  294 ? 0.9106 0.9345 0.9866 -0.0061 -0.0893 0.0418  294 THR K O   
21303 C CB  . THR K  294 ? 1.0586 1.0868 1.1443 -0.0136 -0.0983 0.0459  294 THR K CB  
21304 O OG1 . THR K  294 ? 0.8117 0.8418 0.8901 -0.0175 -0.1025 0.0452  294 THR K OG1 
21305 C CG2 . THR K  294 ? 1.0110 1.0361 1.0917 -0.0112 -0.0939 0.0417  294 THR K CG2 
21306 N N   . SER K  295 ? 0.8529 0.8807 0.9238 -0.0122 -0.0971 0.0436  295 SER K N   
21307 C CA  . SER K  295 ? 0.9861 1.0129 1.0468 -0.0117 -0.0955 0.0401  295 SER K CA  
21308 C C   . SER K  295 ? 0.7751 0.8020 0.8283 -0.0146 -0.0973 0.0371  295 SER K C   
21309 O O   . SER K  295 ? 0.7356 0.7611 0.7804 -0.0140 -0.0953 0.0336  295 SER K O   
21310 C CB  . SER K  295 ? 0.9444 0.9725 1.0028 -0.0125 -0.0973 0.0416  295 SER K CB  
21311 O OG  . SER K  295 ? 1.2443 1.2709 1.3019 -0.0092 -0.0932 0.0407  295 SER K OG  
21312 N N   . LEU K  296 ? 0.6657 0.6940 0.7218 -0.0179 -0.1009 0.0386  296 LEU K N   
21313 C CA  . LEU K  296 ? 0.6031 0.6316 0.6525 -0.0214 -0.1029 0.0359  296 LEU K CA  
21314 C C   . LEU K  296 ? 0.6484 0.6740 0.6943 -0.0195 -0.0987 0.0319  296 LEU K C   
21315 O O   . LEU K  296 ? 0.6326 0.6566 0.6838 -0.0163 -0.0954 0.0321  296 LEU K O   
21316 C CB  . LEU K  296 ? 0.5920 0.6229 0.6464 -0.0253 -0.1075 0.0385  296 LEU K CB  
21317 C CG  . LEU K  296 ? 0.7088 0.7430 0.7671 -0.0274 -0.1120 0.0430  296 LEU K CG  
21318 C CD1 . LEU K  296 ? 0.6953 0.7325 0.7579 -0.0317 -0.1168 0.0454  296 LEU K CD1 
21319 C CD2 . LEU K  296 ? 0.5805 0.6153 0.6301 -0.0289 -0.1136 0.0422  296 LEU K CD2 
21320 N N   . PRO K  297 ? 0.6325 0.6573 0.6695 -0.0214 -0.0988 0.0285  297 PRO K N   
21321 C CA  . PRO K  297 ? 0.5501 0.5722 0.5829 -0.0197 -0.0946 0.0247  297 PRO K CA  
21322 C C   . PRO K  297 ? 0.5698 0.5907 0.6068 -0.0207 -0.0941 0.0241  297 PRO K C   
21323 O O   . PRO K  297 ? 0.5866 0.6051 0.6232 -0.0181 -0.0900 0.0219  297 PRO K O   
21324 C CB  . PRO K  297 ? 0.5659 0.5878 0.5885 -0.0224 -0.0956 0.0217  297 PRO K CB  
21325 C CG  . PRO K  297 ? 0.7511 0.7754 0.7720 -0.0245 -0.0995 0.0239  297 PRO K CG  
21326 C CD  . PRO K  297 ? 0.6174 0.6438 0.6475 -0.0254 -0.1025 0.0282  297 PRO K CD  
21327 N N   . PHE K  298 ? 0.5807 0.6036 0.6216 -0.0245 -0.0983 0.0262  298 PHE K N   
21328 C CA  . PHE K  298 ? 0.5407 0.5628 0.5850 -0.0263 -0.0982 0.0254  298 PHE K CA  
21329 C C   . PHE K  298 ? 0.5206 0.5450 0.5751 -0.0273 -0.1011 0.0293  298 PHE K C   
21330 O O   . PHE K  298 ? 0.6395 0.6669 0.6968 -0.0288 -0.1049 0.0327  298 PHE K O   
21331 C CB  . PHE K  298 ? 0.4810 0.5031 0.5180 -0.0312 -0.1004 0.0226  298 PHE K CB  
21332 C CG  . PHE K  298 ? 0.6243 0.6448 0.6511 -0.0310 -0.0986 0.0193  298 PHE K CG  
21333 C CD1 . PHE K  298 ? 0.4552 0.4725 0.4788 -0.0280 -0.0935 0.0160  298 PHE K CD1 
21334 C CD2 . PHE K  298 ? 0.6078 0.6302 0.6288 -0.0336 -0.1018 0.0196  298 PHE K CD2 
21335 C CE1 . PHE K  298 ? 0.6325 0.6486 0.6473 -0.0277 -0.0917 0.0131  298 PHE K CE1 
21336 C CE2 . PHE K  298 ? 0.5784 0.5993 0.5903 -0.0334 -0.1000 0.0165  298 PHE K CE2 
21337 C CZ  . PHE K  298 ? 0.5210 0.5388 0.5300 -0.0304 -0.0950 0.0133  298 PHE K CZ  
21338 N N   . GLN K  299 ? 0.5370 0.5600 0.5972 -0.0263 -0.0990 0.0291  299 GLN K N   
21339 C CA  . GLN K  299 ? 0.5216 0.5468 0.5919 -0.0275 -0.1014 0.0325  299 GLN K CA  
21340 C C   . GLN K  299 ? 0.5629 0.5875 0.6338 -0.0307 -0.1017 0.0305  299 GLN K C   
21341 O O   . GLN K  299 ? 0.9017 0.9232 0.9671 -0.0303 -0.0984 0.0266  299 GLN K O   
21342 C CB  . GLN K  299 ? 0.4011 0.4252 0.4797 -0.0225 -0.0979 0.0346  299 GLN K CB  
21343 C CG  . GLN K  299 ? 0.6157 0.6358 0.6927 -0.0185 -0.0920 0.0317  299 GLN K CG  
21344 C CD  . GLN K  299 ? 0.6337 0.6526 0.7169 -0.0188 -0.0905 0.0313  299 GLN K CD  
21345 O OE1 . GLN K  299 ? 0.4878 0.5090 0.5775 -0.0215 -0.0938 0.0336  299 GLN K OE1 
21346 N NE2 . GLN K  299 ? 0.5598 0.5753 0.6410 -0.0159 -0.0855 0.0286  299 GLN K NE2 
21347 N N   . ASN K  300 ? 0.5846 0.6122 0.6623 -0.0339 -0.1057 0.0332  300 ASN K N   
21348 C CA  . ASN K  300 ? 0.5978 0.6251 0.6770 -0.0373 -0.1061 0.0315  300 ASN K CA  
21349 C C   . ASN K  300 ? 0.4949 0.5234 0.5861 -0.0363 -0.1062 0.0346  300 ASN K C   
21350 O O   . ASN K  300 ? 0.6052 0.6351 0.6999 -0.0399 -0.1082 0.0346  300 ASN K O   
21351 C CB  . ASN K  300 ? 0.4897 0.5199 0.5639 -0.0438 -0.1114 0.0311  300 ASN K CB  
21352 C CG  . ASN K  300 ? 0.6045 0.6399 0.6846 -0.0462 -0.1172 0.0362  300 ASN K CG  
21353 O OD1 . ASN K  300 ? 0.6795 0.7161 0.7667 -0.0428 -0.1172 0.0399  300 ASN K OD1 
21354 N ND2 . ASN K  300 ? 0.5665 0.6052 0.6438 -0.0522 -0.1222 0.0363  300 ASN K ND2 
21355 N N   . ILE K  301 ? 0.4757 0.5037 0.5731 -0.0315 -0.1038 0.0371  301 ILE K N   
21356 C CA  . ILE K  301 ? 0.5597 0.5887 0.6690 -0.0300 -0.1035 0.0404  301 ILE K CA  
21357 C C   . ILE K  301 ? 0.5672 0.5926 0.6792 -0.0283 -0.0989 0.0379  301 ILE K C   
21358 O O   . ILE K  301 ? 0.5952 0.6217 0.7132 -0.0307 -0.1001 0.0385  301 ILE K O   
21359 C CB  . ILE K  301 ? 0.6491 0.6781 0.7639 -0.0255 -0.1019 0.0437  301 ILE K CB  
21360 C CG1 . ILE K  301 ? 0.4769 0.5097 0.5909 -0.0273 -0.1067 0.0468  301 ILE K CG1 
21361 C CG2 . ILE K  301 ? 0.4734 0.5027 0.6005 -0.0235 -0.1006 0.0466  301 ILE K CG2 
21362 C CD1 . ILE K  301 ? 0.7097 0.7422 0.8282 -0.0231 -0.1048 0.0497  301 ILE K CD1 
21363 N N   . HIS K  302 ? 0.6136 0.6349 0.7211 -0.0241 -0.0935 0.0352  302 HIS K N   
21364 C CA  . HIS K  302 ? 0.5816 0.5993 0.6917 -0.0217 -0.0886 0.0332  302 HIS K CA  
21365 C C   . HIS K  302 ? 0.5725 0.5862 0.6740 -0.0187 -0.0838 0.0294  302 HIS K C   
21366 O O   . HIS K  302 ? 0.4895 0.5029 0.5863 -0.0161 -0.0827 0.0294  302 HIS K O   
21367 C CB  . HIS K  302 ? 0.4738 0.4912 0.5944 -0.0179 -0.0863 0.0363  302 HIS K CB  
21368 C CG  . HIS K  302 ? 0.6549 0.6698 0.7810 -0.0169 -0.0828 0.0353  302 HIS K CG  
21369 N ND1 . HIS K  302 ? 0.7174 0.7279 0.8404 -0.0133 -0.0771 0.0326  302 HIS K ND1 
21370 C CD2 . HIS K  302 ? 0.6855 0.7018 0.8202 -0.0191 -0.0843 0.0368  302 HIS K CD2 
21371 C CE1 . HIS K  302 ? 0.6216 0.6307 0.7510 -0.0133 -0.0750 0.0324  302 HIS K CE1 
21372 N NE2 . HIS K  302 ? 0.5067 0.5192 0.6433 -0.0168 -0.0792 0.0348  302 HIS K NE2 
21373 N N   . PRO K  303 ? 0.5765 0.5873 0.6760 -0.0192 -0.0807 0.0263  303 PRO K N   
21374 C CA  . PRO K  303 ? 0.5156 0.5226 0.6077 -0.0164 -0.0759 0.0229  303 PRO K CA  
21375 C C   . PRO K  303 ? 0.5837 0.5885 0.6786 -0.0103 -0.0710 0.0238  303 PRO K C   
21376 O O   . PRO K  303 ? 0.5073 0.5109 0.5960 -0.0074 -0.0685 0.0226  303 PRO K O   
21377 C CB  . PRO K  303 ? 0.4638 0.4684 0.5559 -0.0187 -0.0741 0.0201  303 PRO K CB  
21378 C CG  . PRO K  303 ? 0.7110 0.7188 0.8074 -0.0242 -0.0792 0.0213  303 PRO K CG  
21379 C CD  . PRO K  303 ? 0.6540 0.6651 0.7582 -0.0229 -0.0821 0.0258  303 PRO K CD  
21380 N N   . ILE K  304 ? 0.3291 0.3334 0.4331 -0.0087 -0.0695 0.0258  304 ILE K N   
21381 C CA  . ILE K  304 ? 0.4919 0.4942 0.5989 -0.0033 -0.0648 0.0268  304 ILE K CA  
21382 C C   . ILE K  304 ? 0.4832 0.4876 0.5918 -0.0016 -0.0664 0.0296  304 ILE K C   
21383 O O   . ILE K  304 ? 0.6260 0.6332 0.7409 -0.0034 -0.0700 0.0325  304 ILE K O   
21384 C CB  . ILE K  304 ? 0.4828 0.4835 0.5991 -0.0021 -0.0623 0.0280  304 ILE K CB  
21385 C CG1 . ILE K  304 ? 0.3965 0.3938 0.5104 -0.0022 -0.0587 0.0249  304 ILE K CG1 
21386 C CG2 . ILE K  304 ? 0.6539 0.6533 0.7743 0.0029  -0.0585 0.0299  304 ILE K CG2 
21387 C CD1 . ILE K  304 ? 0.5244 0.5225 0.6347 -0.0075 -0.0618 0.0226  304 ILE K CD1 
21388 N N   . THR K  305 ? 0.5031 0.5065 0.6064 0.0020  -0.0635 0.0288  305 THR K N   
21389 C CA  . THR K  305 ? 0.4335 0.4387 0.5366 0.0033  -0.0648 0.0308  305 THR K CA  
21390 C C   . THR K  305 ? 0.5546 0.5578 0.6563 0.0082  -0.0598 0.0306  305 THR K C   
21391 O O   . THR K  305 ? 0.5773 0.5782 0.6748 0.0104  -0.0560 0.0285  305 THR K O   
21392 C CB  . THR K  305 ? 0.4801 0.4873 0.5750 0.0007  -0.0683 0.0297  305 THR K CB  
21393 O OG1 . THR K  305 ? 0.8201 0.8302 0.9186 -0.0009 -0.0724 0.0326  305 THR K OG1 
21394 C CG2 . THR K  305 ? 0.5156 0.5217 0.6023 0.0038  -0.0653 0.0278  305 THR K CG2 
21395 N N   . ILE K  306 ? 0.4346 0.4387 0.5397 0.0098  -0.0597 0.0329  306 ILE K N   
21396 C CA  . ILE K  306 ? 0.5206 0.5231 0.6238 0.0140  -0.0553 0.0326  306 ILE K CA  
21397 C C   . ILE K  306 ? 0.5742 0.5786 0.6740 0.0142  -0.0568 0.0333  306 ILE K C   
21398 O O   . ILE K  306 ? 0.5706 0.5769 0.6744 0.0123  -0.0601 0.0355  306 ILE K O   
21399 C CB  . ILE K  306 ? 0.3716 0.3725 0.4837 0.0165  -0.0521 0.0346  306 ILE K CB  
21400 C CG1 . ILE K  306 ? 0.3777 0.3768 0.4940 0.0162  -0.0507 0.0341  306 ILE K CG1 
21401 C CG2 . ILE K  306 ? 0.4434 0.4426 0.5524 0.0206  -0.0473 0.0340  306 ILE K CG2 
21402 C CD1 . ILE K  306 ? 0.4584 0.4555 0.5827 0.0189  -0.0469 0.0358  306 ILE K CD1 
21403 N N   . GLY K  307 ? 0.4803 0.4841 0.5726 0.0165  -0.0541 0.0314  307 GLY K N   
21404 C CA  . GLY K  307 ? 0.5181 0.5235 0.6064 0.0167  -0.0550 0.0316  307 GLY K CA  
21405 C C   . GLY K  307 ? 0.5560 0.5627 0.6350 0.0151  -0.0572 0.0294  307 GLY K C   
21406 O O   . GLY K  307 ? 0.6773 0.6833 0.7518 0.0148  -0.0565 0.0273  307 GLY K O   
21407 N N   . LYS K  308 ? 0.5635 0.5720 0.6398 0.0139  -0.0595 0.0299  308 LYS K N   
21408 C CA  . LYS K  308 ? 0.6146 0.6246 0.6826 0.0119  -0.0620 0.0280  308 LYS K CA  
21409 C C   . LYS K  308 ? 0.5316 0.5433 0.6016 0.0078  -0.0671 0.0293  308 LYS K C   
21410 O O   . LYS K  308 ? 0.6653 0.6785 0.7378 0.0064  -0.0697 0.0314  308 LYS K O   
21411 C CB  . LYS K  308 ? 0.6405 0.6516 0.7038 0.0130  -0.0613 0.0277  308 LYS K CB  
21412 C CG  . LYS K  308 ? 0.8969 0.9095 0.9516 0.0112  -0.0635 0.0257  308 LYS K CG  
21413 C CD  . LYS K  308 ? 1.0271 1.0408 1.0775 0.0121  -0.0628 0.0253  308 LYS K CD  
21414 C CE  . LYS K  308 ? 1.0242 1.0373 1.0718 0.0157  -0.0581 0.0239  308 LYS K CE  
21415 N NZ  . LYS K  308 ? 1.0787 1.0934 1.1187 0.0160  -0.0578 0.0223  308 LYS K NZ  
21416 N N   . CYS K  309 ? 0.5198 0.5311 0.5886 0.0056  -0.0684 0.0280  309 CYS K N   
21417 C CA  . CYS K  309 ? 0.5698 0.5827 0.6414 0.0015  -0.0732 0.0294  309 CYS K CA  
21418 C C   . CYS K  309 ? 0.5313 0.5451 0.5948 -0.0018 -0.0760 0.0272  309 CYS K C   
21419 O O   . CYS K  309 ? 0.5159 0.5285 0.5722 -0.0009 -0.0738 0.0243  309 CYS K O   
21420 C CB  . CYS K  309 ? 0.3990 0.4108 0.4775 0.0009  -0.0728 0.0300  309 CYS K CB  
21421 S SG  . CYS K  309 ? 0.8222 0.8326 0.9107 0.0047  -0.0692 0.0325  309 CYS K SG  
21422 N N   . PRO K  310 ? 0.5869 0.6029 0.6515 -0.0058 -0.0809 0.0288  310 PRO K N   
21423 C CA  . PRO K  310 ? 0.5585 0.5752 0.6157 -0.0096 -0.0838 0.0268  310 PRO K CA  
21424 C C   . PRO K  310 ? 0.6030 0.6178 0.6590 -0.0107 -0.0823 0.0242  310 PRO K C   
21425 O O   . PRO K  310 ? 0.6057 0.6192 0.6680 -0.0093 -0.0803 0.0248  310 PRO K O   
21426 C CB  . PRO K  310 ? 0.5406 0.5602 0.6019 -0.0135 -0.0892 0.0298  310 PRO K CB  
21427 C CG  . PRO K  310 ? 0.5581 0.5786 0.6271 -0.0111 -0.0889 0.0333  310 PRO K CG  
21428 C CD  . PRO K  310 ? 0.4188 0.4367 0.4916 -0.0068 -0.0839 0.0327  310 PRO K CD  
21429 N N   . LYS K  311 ? 0.5474 0.5617 0.5954 -0.0132 -0.0830 0.0214  311 LYS K N   
21430 C CA  . LYS K  311 ? 0.5407 0.5528 0.5870 -0.0143 -0.0811 0.0187  311 LYS K CA  
21431 C C   . LYS K  311 ? 0.5617 0.5748 0.6124 -0.0187 -0.0846 0.0195  311 LYS K C   
21432 O O   . LYS K  311 ? 0.5962 0.6121 0.6467 -0.0224 -0.0894 0.0211  311 LYS K O   
21433 C CB  . LYS K  311 ? 0.4353 0.4463 0.4716 -0.0155 -0.0802 0.0152  311 LYS K CB  
21434 C CG  . LYS K  311 ? 0.4465 0.4545 0.4805 -0.0123 -0.0748 0.0126  311 LYS K CG  
21435 C CD  . LYS K  311 ? 0.4808 0.4883 0.5184 -0.0068 -0.0711 0.0140  311 LYS K CD  
21436 C CE  . LYS K  311 ? 0.5587 0.5669 0.5903 -0.0044 -0.0698 0.0133  311 LYS K CE  
21437 N NZ  . LYS K  311 ? 0.5111 0.5185 0.5449 0.0007  -0.0654 0.0138  311 LYS K NZ  
21438 N N   . TYR K  312 ? 0.4934 0.5046 0.5483 -0.0183 -0.0821 0.0187  312 TYR K N   
21439 C CA  . TYR K  312 ? 0.5464 0.5586 0.6058 -0.0225 -0.0851 0.0192  312 TYR K CA  
21440 C C   . TYR K  312 ? 0.5448 0.5567 0.5967 -0.0275 -0.0870 0.0163  312 TYR K C   
21441 O O   . TYR K  312 ? 0.5979 0.6069 0.6439 -0.0271 -0.0836 0.0128  312 TYR K O   
21442 C CB  . TYR K  312 ? 0.4273 0.4371 0.4934 -0.0206 -0.0815 0.0190  312 TYR K CB  
21443 C CG  . TYR K  312 ? 0.5427 0.5537 0.6137 -0.0251 -0.0844 0.0194  312 TYR K CG  
21444 C CD1 . TYR K  312 ? 0.5568 0.5713 0.6351 -0.0270 -0.0887 0.0231  312 TYR K CD1 
21445 C CD2 . TYR K  312 ? 0.6232 0.6318 0.6917 -0.0276 -0.0826 0.0161  312 TYR K CD2 
21446 C CE1 . TYR K  312 ? 0.5363 0.5525 0.6192 -0.0313 -0.0916 0.0236  312 TYR K CE1 
21447 C CE2 . TYR K  312 ? 0.5602 0.5700 0.6330 -0.0321 -0.0853 0.0163  312 TYR K CE2 
21448 C CZ  . TYR K  312 ? 0.6377 0.6516 0.7177 -0.0339 -0.0899 0.0201  312 TYR K CZ  
21449 O OH  . TYR K  312 ? 0.7023 0.7179 0.7867 -0.0385 -0.0928 0.0204  312 TYR K OH  
21450 N N   . VAL K  313 ? 0.6904 0.7055 0.7428 -0.0323 -0.0924 0.0177  313 VAL K N   
21451 C CA  . VAL K  313 ? 0.5681 0.5834 0.6133 -0.0378 -0.0947 0.0151  313 VAL K CA  
21452 C C   . VAL K  313 ? 0.5668 0.5842 0.6168 -0.0427 -0.0985 0.0161  313 VAL K C   
21453 O O   . VAL K  313 ? 0.6312 0.6516 0.6895 -0.0427 -0.1014 0.0200  313 VAL K O   
21454 C CB  . VAL K  313 ? 0.5800 0.5974 0.6182 -0.0396 -0.0981 0.0155  313 VAL K CB  
21455 C CG1 . VAL K  313 ? 0.7054 0.7230 0.7361 -0.0457 -0.1007 0.0128  313 VAL K CG1 
21456 C CG2 . VAL K  313 ? 0.6894 0.7048 0.7224 -0.0350 -0.0943 0.0141  313 VAL K CG2 
21457 N N   . LYS K  314 ? 0.5202 0.5362 0.5654 -0.0471 -0.0984 0.0127  314 LYS K N   
21458 C CA  . LYS K  314 ? 0.6491 0.6672 0.6981 -0.0523 -0.1018 0.0131  314 LYS K CA  
21459 C C   . LYS K  314 ? 0.6545 0.6771 0.7003 -0.0578 -0.1083 0.0148  314 LYS K C   
21460 O O   . LYS K  314 ? 0.7720 0.7971 0.8197 -0.0630 -0.1120 0.0152  314 LYS K O   
21461 C CB  . LYS K  314 ? 0.6582 0.6725 0.7032 -0.0549 -0.0983 0.0083  314 LYS K CB  
21462 C CG  . LYS K  314 ? 0.9232 0.9386 0.9744 -0.0587 -0.0998 0.0084  314 LYS K CG  
21463 C CD  . LYS K  314 ? 1.2587 1.2695 1.3057 -0.0607 -0.0954 0.0033  314 LYS K CD  
21464 C CE  . LYS K  314 ? 1.2063 1.2122 1.2526 -0.0544 -0.0885 0.0016  314 LYS K CE  
21465 N NZ  . LYS K  314 ? 0.9540 0.9554 0.9930 -0.0561 -0.0842 -0.0035 314 LYS K NZ  
21466 N N   . SER K  315 ? 0.7528 0.7765 0.7936 -0.0566 -0.1097 0.0158  315 SER K N   
21467 C CA  . SER K  315 ? 0.7643 0.7920 0.8012 -0.0614 -0.1157 0.0176  315 SER K CA  
21468 C C   . SER K  315 ? 0.7337 0.7665 0.7799 -0.0626 -0.1208 0.0229  315 SER K C   
21469 O O   . SER K  315 ? 0.6828 0.7160 0.7381 -0.0584 -0.1195 0.0258  315 SER K O   
21470 C CB  . SER K  315 ? 0.6876 0.7150 0.7178 -0.0592 -0.1155 0.0177  315 SER K CB  
21471 O OG  . SER K  315 ? 0.8863 0.9096 0.9075 -0.0588 -0.1114 0.0129  315 SER K OG  
21472 N N   . THR K  316 ? 0.7157 0.7525 0.7596 -0.0685 -0.1264 0.0243  316 THR K N   
21473 C CA  . THR K  316 ? 0.7841 0.8265 0.8363 -0.0701 -0.1319 0.0298  316 THR K CA  
21474 C C   . THR K  316 ? 0.7975 0.8424 0.8481 -0.0689 -0.1348 0.0333  316 THR K C   
21475 O O   . THR K  316 ? 0.7886 0.8368 0.8478 -0.0669 -0.1370 0.0384  316 THR K O   
21476 C CB  . THR K  316 ? 0.7851 0.8311 0.8362 -0.0776 -0.1369 0.0298  316 THR K CB  
21477 O OG1 . THR K  316 ? 1.1566 1.2088 1.2140 -0.0794 -0.1430 0.0356  316 THR K OG1 
21478 C CG2 . THR K  316 ? 0.8655 0.9103 0.9038 -0.0824 -0.1376 0.0256  316 THR K CG2 
21479 N N   . LYS K  317 ? 0.9067 0.9501 0.9466 -0.0702 -0.1345 0.0307  317 LYS K N   
21480 C CA  . LYS K  317 ? 0.8120 0.8572 0.8492 -0.0691 -0.1367 0.0334  317 LYS K CA  
21481 C C   . LYS K  317 ? 0.6769 0.7181 0.7034 -0.0675 -0.1331 0.0292  317 LYS K C   
21482 O O   . LYS K  317 ? 0.7905 0.8289 0.8094 -0.0701 -0.1312 0.0245  317 LYS K O   
21483 C CB  . LYS K  317 ? 0.8896 0.9401 0.9253 -0.0750 -0.1437 0.0366  317 LYS K CB  
21484 C CG  . LYS K  317 ? 0.9356 0.9861 0.9622 -0.0816 -0.1455 0.0328  317 LYS K CG  
21485 C CD  . LYS K  317 ? 1.1841 1.2402 1.2085 -0.0874 -0.1525 0.0362  317 LYS K CD  
21486 C CE  . LYS K  317 ? 1.1589 1.2154 1.1775 -0.0864 -0.1537 0.0378  317 LYS K CE  
21487 N NZ  . LYS K  317 ? 0.9246 0.9867 0.9406 -0.0921 -0.1604 0.0414  317 LYS K NZ  
21488 N N   . LEU K  318 ? 0.6916 0.7325 0.7180 -0.0634 -0.1321 0.0310  318 LEU K N   
21489 C CA  . LEU K  318 ? 0.7573 0.7951 0.7743 -0.0619 -0.1290 0.0276  318 LEU K CA  
21490 C C   . LEU K  318 ? 0.6938 0.7340 0.7083 -0.0620 -0.1322 0.0307  318 LEU K C   
21491 O O   . LEU K  318 ? 0.6937 0.7326 0.7081 -0.0576 -0.1296 0.0310  318 LEU K O   
21492 C CB  . LEU K  318 ? 0.5887 0.6225 0.6076 -0.0555 -0.1228 0.0256  318 LEU K CB  
21493 C CG  . LEU K  318 ? 0.5295 0.5597 0.5486 -0.0548 -0.1185 0.0217  318 LEU K CG  
21494 C CD1 . LEU K  318 ? 0.7364 0.7637 0.7590 -0.0482 -0.1130 0.0211  318 LEU K CD1 
21495 C CD2 . LEU K  318 ? 0.5235 0.5513 0.5321 -0.0583 -0.1173 0.0168  318 LEU K CD2 
21496 N N   . ARG K  319 ? 0.7359 0.7799 0.7486 -0.0673 -0.1378 0.0330  319 ARG K N   
21497 C CA  . ARG K  319 ? 0.7783 0.8252 0.7896 -0.0678 -0.1412 0.0366  319 ARG K CA  
21498 C C   . ARG K  319 ? 0.6565 0.7009 0.6564 -0.0681 -0.1395 0.0332  319 ARG K C   
21499 O O   . ARG K  319 ? 0.5649 0.6082 0.5560 -0.0723 -0.1399 0.0296  319 ARG K O   
21500 C CB  . ARG K  319 ? 0.8655 0.9176 0.8785 -0.0734 -0.1479 0.0405  319 ARG K CB  
21501 C CG  . ARG K  319 ? 0.8312 0.8865 0.8443 -0.0737 -0.1516 0.0452  319 ARG K CG  
21502 C CD  . ARG K  319 ? 0.9165 0.9775 0.9382 -0.0763 -0.1572 0.0513  319 ARG K CD  
21503 N NE  . ARG K  319 ? 0.9184 0.9799 0.9528 -0.0717 -0.1557 0.0545  319 ARG K NE  
21504 C CZ  . ARG K  319 ? 0.9430 1.0049 0.9838 -0.0673 -0.1547 0.0583  319 ARG K CZ  
21505 N NH1 . ARG K  319 ? 0.9980 1.0599 1.0339 -0.0668 -0.1553 0.0593  319 ARG K NH1 
21506 N NH2 . ARG K  319 ? 0.9994 1.0615 1.0516 -0.0635 -0.1530 0.0609  319 ARG K NH2 
21507 N N   . LEU K  320 ? 0.6385 0.6820 0.6390 -0.0638 -0.1374 0.0343  320 LEU K N   
21508 C CA  . LEU K  320 ? 0.5405 0.5816 0.5312 -0.0633 -0.1353 0.0312  320 LEU K CA  
21509 C C   . LEU K  320 ? 0.6210 0.6651 0.6087 -0.0657 -0.1395 0.0344  320 LEU K C   
21510 O O   . LEU K  320 ? 0.7449 0.7911 0.7390 -0.0635 -0.1409 0.0389  320 LEU K O   
21511 C CB  . LEU K  320 ? 0.6585 0.6968 0.6513 -0.0569 -0.1299 0.0299  320 LEU K CB  
21512 C CG  . LEU K  320 ? 0.6402 0.6758 0.6238 -0.0556 -0.1267 0.0261  320 LEU K CG  
21513 C CD1 . LEU K  320 ? 0.5256 0.5581 0.5023 -0.0573 -0.1239 0.0208  320 LEU K CD1 
21514 C CD2 . LEU K  320 ? 0.5021 0.5361 0.4893 -0.0495 -0.1225 0.0262  320 LEU K CD2 
21515 N N   . ALA K  321 ? 0.6390 0.6830 0.6167 -0.0704 -0.1413 0.0322  321 ALA K N   
21516 C CA  . ALA K  321 ? 0.6508 0.6974 0.6244 -0.0732 -0.1454 0.0351  321 ALA K CA  
21517 C C   . ALA K  321 ? 0.6467 0.6920 0.6192 -0.0690 -0.1428 0.0355  321 ALA K C   
21518 O O   . ALA K  321 ? 0.7169 0.7586 0.6842 -0.0665 -0.1383 0.0313  321 ALA K O   
21519 C CB  . ALA K  321 ? 0.6073 0.6536 0.5699 -0.0791 -0.1472 0.0319  321 ALA K CB  
21520 N N   . THR K  322 ? 0.7302 0.7783 0.7077 -0.0682 -0.1456 0.0406  322 THR K N   
21521 C CA  . THR K  322 ? 0.7427 0.7897 0.7192 -0.0648 -0.1435 0.0414  322 THR K CA  
21522 C C   . THR K  322 ? 0.7906 0.8397 0.7610 -0.0685 -0.1473 0.0434  322 THR K C   
21523 O O   . THR K  322 ? 0.6794 0.7267 0.6432 -0.0677 -0.1454 0.0416  322 THR K O   
21524 C CB  . THR K  322 ? 0.6623 0.7104 0.6503 -0.0602 -0.1427 0.0457  322 THR K CB  
21525 O OG1 . THR K  322 ? 0.7700 0.8222 0.7647 -0.0626 -0.1478 0.0514  322 THR K OG1 
21526 C CG2 . THR K  322 ? 0.8398 0.8857 0.8336 -0.0564 -0.1386 0.0436  322 THR K CG2 
21527 N N   . GLY K  323 ? 0.8112 0.8641 0.7837 -0.0726 -0.1527 0.0475  323 GLY K N   
21528 C CA  . GLY K  323 ? 0.7495 0.8047 0.7159 -0.0768 -0.1568 0.0498  323 GLY K CA  
21529 C C   . GLY K  323 ? 0.8156 0.8697 0.7703 -0.0819 -0.1576 0.0453  323 GLY K C   
21530 O O   . GLY K  323 ? 0.8078 0.8584 0.7577 -0.0813 -0.1537 0.0398  323 GLY K O   
21531 N N   . LEU K  324 ? 0.7587 0.8160 0.7089 -0.0870 -0.1626 0.0480  324 LEU K N   
21532 C CA  . LEU K  324 ? 0.8419 0.8983 0.7802 -0.0925 -0.1637 0.0443  324 LEU K CA  
21533 C C   . LEU K  324 ? 0.9000 0.9598 0.8388 -0.0981 -0.1684 0.0456  324 LEU K C   
21534 O O   . LEU K  324 ? 1.0257 1.0881 0.9743 -0.0970 -0.1701 0.0488  324 LEU K O   
21535 C CB  . LEU K  324 ? 0.9036 0.9607 0.8348 -0.0945 -0.1655 0.0459  324 LEU K CB  
21536 C CG  . LEU K  324 ? 0.8638 0.9236 0.8013 -0.0922 -0.1678 0.0524  324 LEU K CG  
21537 C CD1 . LEU K  324 ? 0.8627 0.9219 0.7910 -0.0941 -0.1682 0.0522  324 LEU K CD1 
21538 C CD2 . LEU K  324 ? 0.7864 0.8446 0.7333 -0.0853 -0.1638 0.0534  324 LEU K CD2 
21539 N N   . ARG K  325 ? 0.9031 0.9629 0.8314 -0.1041 -0.1703 0.0429  325 ARG K N   
21540 C CA  . ARG K  325 ? 0.9487 1.0125 0.8767 -0.1101 -0.1754 0.0446  325 ARG K CA  
21541 C C   . ARG K  325 ? 0.9623 1.0319 0.8975 -0.1107 -0.1811 0.0526  325 ARG K C   
21542 O O   . ARG K  325 ? 0.9093 0.9792 0.8491 -0.1065 -0.1805 0.0561  325 ARG K O   
21543 C CB  . ARG K  325 ? 0.9051 0.9680 0.8197 -0.1168 -0.1766 0.0408  325 ARG K CB  
21544 C CG  . ARG K  325 ? 0.9729 1.0309 0.8812 -0.1179 -0.1719 0.0333  325 ARG K CG  
21545 C CD  . ARG K  325 ? 1.1006 1.1601 1.0023 -0.1258 -0.1751 0.0313  325 ARG K CD  
21546 N NE  . ARG K  325 ? 1.2209 1.2751 1.1124 -0.1281 -0.1706 0.0240  325 ARG K NE  
21547 C CZ  . ARG K  325 ? 1.2449 1.2976 1.1342 -0.1316 -0.1694 0.0198  325 ARG K CZ  
21548 N NH1 . ARG K  325 ? 1.0752 1.1314 0.9718 -0.1333 -0.1726 0.0221  325 ARG K NH1 
21549 N NH2 . ARG K  325 ? 1.1674 1.2150 1.0476 -0.1335 -0.1649 0.0132  325 ARG K NH2 
21550 N N   . ASN K  326 ? 1.1525 1.2270 1.0890 -0.1159 -0.1865 0.0555  326 ASN K N   
21551 C CA  . ASN K  326 ? 1.1544 1.2351 1.0978 -0.1169 -0.1923 0.0635  326 ASN K CA  
21552 C C   . ASN K  326 ? 1.1664 1.2518 1.1029 -0.1249 -0.1985 0.0654  326 ASN K C   
21553 O O   . ASN K  326 ? 1.2153 1.3013 1.1481 -0.1297 -0.1998 0.0623  326 ASN K O   
21554 C CB  . ASN K  326 ? 1.1729 1.2563 1.1308 -0.1135 -0.1930 0.0675  326 ASN K CB  
21555 C CG  . ASN K  326 ? 1.2846 1.3734 1.2514 -0.1124 -0.1975 0.0760  326 ASN K CG  
21556 O OD1 . ASN K  326 ? 1.3529 1.4416 1.3178 -0.1109 -0.1976 0.0786  326 ASN K OD1 
21557 N ND2 . ASN K  326 ? 1.3302 1.4239 1.3073 -0.1131 -0.2010 0.0805  326 ASN K ND2 
21558 N N   . ILE K  327 ? 1.2484 1.3373 1.1834 -0.1263 -0.2024 0.0707  327 ILE K N   
21559 C CA  . ILE K  327 ? 1.2750 1.3686 1.2027 -0.1339 -0.2085 0.0729  327 ILE K CA  
21560 C C   . ILE K  327 ? 1.1322 1.2328 1.0680 -0.1342 -0.2145 0.0822  327 ILE K C   
21561 O O   . ILE K  327 ? 1.0404 1.1413 0.9864 -0.1284 -0.2133 0.0866  327 ILE K O   
21562 C CB  . ILE K  327 ? 1.1077 1.1980 1.0208 -0.1370 -0.2072 0.0689  327 ILE K CB  
21563 C CG1 . ILE K  327 ? 1.0000 1.0830 0.9060 -0.1357 -0.2006 0.0600  327 ILE K CG1 
21564 C CG2 . ILE K  327 ? 1.2346 1.3293 1.1389 -0.1455 -0.2131 0.0703  327 ILE K CG2 
21565 C CD1 . ILE K  327 ? 0.9553 1.0379 0.8574 -0.1407 -0.2007 0.0552  327 ILE K CD1 
21566 N N   . LEU L  2   ? 0.9640 0.9909 0.8153 -0.1175 -0.1409 -0.0025 2   LEU L N   
21567 C CA  . LEU L  2   ? 0.9954 1.0173 0.8406 -0.1162 -0.1348 -0.0082 2   LEU L CA  
21568 C C   . LEU L  2   ? 0.9008 0.9222 0.7387 -0.1168 -0.1345 -0.0083 2   LEU L C   
21569 O O   . LEU L  2   ? 0.8930 0.9106 0.7232 -0.1181 -0.1305 -0.0130 2   LEU L O   
21570 C CB  . LEU L  2   ? 0.8742 0.8942 0.7272 -0.1089 -0.1298 -0.0094 2   LEU L CB  
21571 C CG  . LEU L  2   ? 0.9338 0.9488 0.7828 -0.1076 -0.1232 -0.0154 2   LEU L CG  
21572 C CD1 . LEU L  2   ? 0.9612 0.9740 0.8071 -0.1125 -0.1224 -0.0189 2   LEU L CD1 
21573 C CD2 . LEU L  2   ? 0.5362 0.5502 0.3933 -0.1000 -0.1189 -0.0155 2   LEU L CD2 
21574 N N   . PHE L  3   ? 0.8630 0.8880 0.7036 -0.1158 -0.1386 -0.0031 3   PHE L N   
21575 C CA  . PHE L  3   ? 0.9524 0.9771 0.7865 -0.1163 -0.1387 -0.0027 3   PHE L CA  
21576 C C   . PHE L  3   ? 1.0310 1.0582 0.8582 -0.1231 -0.1441 -0.0002 3   PHE L C   
21577 O O   . PHE L  3   ? 1.0021 1.0296 0.8239 -0.1241 -0.1449 0.0008  3   PHE L O   
21578 C CB  . PHE L  3   ? 0.9388 0.9652 0.7803 -0.1100 -0.1385 0.0011  3   PHE L CB  
21579 C CG  . PHE L  3   ? 0.9724 0.9962 0.8186 -0.1035 -0.1327 -0.0018 3   PHE L CG  
21580 C CD1 . PHE L  3   ? 0.9165 0.9408 0.7719 -0.0996 -0.1317 -0.0011 3   PHE L CD1 
21581 C CD2 . PHE L  3   ? 1.0263 1.0474 0.8676 -0.1015 -0.1284 -0.0050 3   PHE L CD2 
21582 C CE1 . PHE L  3   ? 0.8116 0.8337 0.6709 -0.0939 -0.1265 -0.0035 3   PHE L CE1 
21583 C CE2 . PHE L  3   ? 0.8851 0.9044 0.7307 -0.0957 -0.1234 -0.0074 3   PHE L CE2 
21584 C CZ  . PHE L  3   ? 0.9030 0.9229 0.7575 -0.0919 -0.1225 -0.0066 3   PHE L CZ  
21585 N N   . GLY L  4   ? 1.1184 1.1478 0.9459 -0.1277 -0.1478 0.0008  4   GLY L N   
21586 C CA  . GLY L  4   ? 1.1117 1.1437 0.9320 -0.1349 -0.1530 0.0028  4   GLY L CA  
21587 C C   . GLY L  4   ? 1.1459 1.1830 0.9700 -0.1348 -0.1587 0.0099  4   GLY L C   
21588 O O   . GLY L  4   ? 1.2352 1.2750 1.0535 -0.1406 -0.1635 0.0123  4   GLY L O   
21589 N N   . ALA L  5   ? 1.0190 1.0573 0.8526 -0.1283 -0.1582 0.0134  5   ALA L N   
21590 C CA  . ALA L  5   ? 0.9239 0.9666 0.7621 -0.1274 -0.1630 0.0203  5   ALA L CA  
21591 C C   . ALA L  5   ? 0.9174 0.9650 0.7637 -0.1288 -0.1683 0.0254  5   ALA L C   
21592 O O   . ALA L  5   ? 0.8911 0.9424 0.7341 -0.1343 -0.1736 0.0287  5   ALA L O   
21593 C CB  . ALA L  5   ? 0.8536 0.8954 0.6986 -0.1201 -0.1599 0.0218  5   ALA L CB  
21594 N N   . ILE L  6   ? 1.0020 1.0499 0.8590 -0.1239 -0.1667 0.0261  6   ILE L N   
21595 C CA  . ILE L  6   ? 0.8567 0.9092 0.7226 -0.1245 -0.1713 0.0309  6   ILE L CA  
21596 C C   . ILE L  6   ? 0.9251 0.9783 0.7867 -0.1308 -0.1734 0.0284  6   ILE L C   
21597 O O   . ILE L  6   ? 0.8888 0.9381 0.7473 -0.1312 -0.1692 0.0225  6   ILE L O   
21598 C CB  . ILE L  6   ? 0.7959 0.8479 0.6740 -0.1176 -0.1685 0.0318  6   ILE L CB  
21599 C CG1 . ILE L  6   ? 0.6478 0.6991 0.5302 -0.1117 -0.1665 0.0344  6   ILE L CG1 
21600 C CG2 . ILE L  6   ? 0.6651 0.7219 0.5527 -0.1184 -0.1731 0.0368  6   ILE L CG2 
21601 C CD1 . ILE L  6   ? 0.7434 0.7948 0.6380 -0.1052 -0.1643 0.0361  6   ILE L CD1 
21602 N N   . ALA L  7   ? 0.9481 1.0065 0.8097 -0.1358 -0.1797 0.0331  7   ALA L N   
21603 C CA  . ALA L  7   ? 0.9261 0.9860 0.7825 -0.1429 -0.1824 0.0311  7   ALA L CA  
21604 C C   . ALA L  7   ? 0.9894 1.0452 0.8316 -0.1478 -0.1800 0.0250  7   ALA L C   
21605 O O   . ALA L  7   ? 1.0333 1.0877 0.8701 -0.1527 -0.1792 0.0205  7   ALA L O   
21606 C CB  . ALA L  7   ? 0.9095 0.9684 0.7730 -0.1412 -0.1803 0.0286  7   ALA L CB  
21607 N N   . GLY L  8   ? 1.0826 1.1365 0.9190 -0.1466 -0.1784 0.0249  8   GLY L N   
21608 C CA  . GLY L  8   ? 1.0824 1.1324 0.9054 -0.1510 -0.1759 0.0195  8   GLY L CA  
21609 C C   . GLY L  8   ? 1.1819 1.2347 0.9974 -0.1556 -0.1804 0.0232  8   GLY L C   
21610 O O   . GLY L  8   ? 1.1993 1.2571 1.0138 -0.1609 -0.1864 0.0270  8   GLY L O   
21611 N N   . PHE L  9   ? 0.9191 0.9692 0.7295 -0.1536 -0.1777 0.0221  9   PHE L N   
21612 C CA  . PHE L  9   ? 0.9791 1.0315 0.7824 -0.1574 -0.1816 0.0258  9   PHE L CA  
21613 C C   . PHE L  9   ? 1.1593 1.2172 0.9721 -0.1544 -0.1864 0.0343  9   PHE L C   
21614 O O   . PHE L  9   ? 1.3895 1.4511 1.1987 -0.1581 -0.1912 0.0390  9   PHE L O   
21615 C CB  . PHE L  9   ? 1.0980 1.1455 0.8926 -0.1565 -0.1769 0.0219  9   PHE L CB  
21616 C CG  . PHE L  9   ? 1.1372 1.1819 0.9387 -0.1483 -0.1721 0.0213  9   PHE L CG  
21617 C CD1 . PHE L  9   ? 1.1773 1.2248 0.9861 -0.1439 -0.1739 0.0272  9   PHE L CD1 
21618 C CD2 . PHE L  9   ? 1.2069 1.2464 1.0075 -0.1451 -0.1655 0.0148  9   PHE L CD2 
21619 C CE1 . PHE L  9   ? 1.0644 1.1093 0.8790 -0.1368 -0.1694 0.0264  9   PHE L CE1 
21620 C CE2 . PHE L  9   ? 1.2271 1.2645 1.0338 -0.1379 -0.1612 0.0143  9   PHE L CE2 
21621 C CZ  . PHE L  9   ? 1.2437 1.2838 1.0571 -0.1339 -0.1632 0.0200  9   PHE L CZ  
21622 N N   . ILE L  10  ? 0.9201 0.9784 0.7452 -0.1478 -0.1849 0.0362  10  ILE L N   
21623 C CA  . ILE L  10  ? 0.9208 0.9843 0.7568 -0.1450 -0.1893 0.0441  10  ILE L CA  
21624 C C   . ILE L  10  ? 1.0554 1.1225 0.8988 -0.1464 -0.1923 0.0457  10  ILE L C   
21625 O O   . ILE L  10  ? 1.0638 1.1293 0.9155 -0.1418 -0.1893 0.0441  10  ILE L O   
21626 C CB  . ILE L  10  ? 0.7784 0.8400 0.6235 -0.1367 -0.1854 0.0454  10  ILE L CB  
21627 C CG1 . ILE L  10  ? 0.8726 0.9299 0.7101 -0.1352 -0.1813 0.0423  10  ILE L CG1 
21628 C CG2 . ILE L  10  ? 0.7007 0.7675 0.5564 -0.1343 -0.1898 0.0539  10  ILE L CG2 
21629 C CD1 . ILE L  10  ? 0.8349 0.8904 0.6804 -0.1275 -0.1774 0.0433  10  ILE L CD1 
21630 N N   . GLU L  11  ? 1.2779 1.3500 1.1183 -0.1529 -0.1983 0.0490  11  GLU L N   
21631 C CA  . GLU L  11  ? 1.3186 1.3940 1.1634 -0.1560 -0.2014 0.0494  11  GLU L CA  
21632 C C   . GLU L  11  ? 1.0650 1.1440 0.9253 -0.1509 -0.2030 0.0547  11  GLU L C   
21633 O O   . GLU L  11  ? 1.0877 1.1666 0.9535 -0.1503 -0.2021 0.0528  11  GLU L O   
21634 C CB  . GLU L  11  ? 1.4738 1.5543 1.3112 -0.1646 -0.2079 0.0521  11  GLU L CB  
21635 C CG  . GLU L  11  ? 1.6454 1.7224 1.4669 -0.1704 -0.2064 0.0467  11  GLU L CG  
21636 C CD  . GLU L  11  ? 2.1104 2.1928 1.9244 -0.1789 -0.2131 0.0500  11  GLU L CD  
21637 O OE1 . GLU L  11  ? 2.1954 2.2754 1.9960 -0.1844 -0.2124 0.0460  11  GLU L OE1 
21638 O OE2 . GLU L  11  ? 2.0832 2.1724 1.9046 -0.1802 -0.2191 0.0565  11  GLU L OE2 
21639 N N   . GLY L  12  ? 1.0193 1.1012 0.8866 -0.1472 -0.2051 0.0614  12  GLY L N   
21640 C CA  . GLY L  12  ? 0.9858 1.0715 0.8677 -0.1430 -0.2071 0.0672  12  GLY L CA  
21641 C C   . GLY L  12  ? 0.9684 1.0522 0.8593 -0.1350 -0.2036 0.0697  12  GLY L C   
21642 O O   . GLY L  12  ? 1.0221 1.1021 0.9078 -0.1328 -0.2003 0.0679  12  GLY L O   
21643 N N   . GLY L  13  ? 0.9342 1.0204 0.8385 -0.1309 -0.2043 0.0737  13  GLY L N   
21644 C CA  . GLY L  13  ? 0.9196 1.0043 0.8335 -0.1236 -0.2012 0.0765  13  GLY L CA  
21645 C C   . GLY L  13  ? 0.8907 0.9809 0.8121 -0.1231 -0.2059 0.0856  13  GLY L C   
21646 O O   . GLY L  13  ? 0.9862 1.0819 0.9063 -0.1283 -0.2119 0.0900  13  GLY L O   
21647 N N   . TRP L  14  ? 0.8455 0.9342 0.7750 -0.1169 -0.2030 0.0883  14  TRP L N   
21648 C CA  . TRP L  14  ? 0.9533 1.0464 0.8904 -0.1158 -0.2066 0.0969  14  TRP L CA  
21649 C C   . TRP L  14  ? 1.0230 1.1179 0.9760 -0.1106 -0.2059 0.1014  14  TRP L C   
21650 O O   . TRP L  14  ? 0.9818 1.0727 0.9403 -0.1046 -0.2007 0.0999  14  TRP L O   
21651 C CB  . TRP L  14  ? 0.9660 1.0561 0.8988 -0.1135 -0.2038 0.0972  14  TRP L CB  
21652 C CG  . TRP L  14  ? 0.9638 1.0525 0.8815 -0.1186 -0.2048 0.0940  14  TRP L CG  
21653 C CD1 . TRP L  14  ? 0.9879 1.0795 0.8968 -0.1256 -0.2092 0.0933  14  TRP L CD1 
21654 C CD2 . TRP L  14  ? 0.9169 1.0011 0.8267 -0.1173 -0.2010 0.0910  14  TRP L CD2 
21655 N NE1 . TRP L  14  ? 0.9348 1.0237 0.8307 -0.1287 -0.2083 0.0900  14  TRP L NE1 
21656 C CE2 . TRP L  14  ? 1.0044 1.0889 0.9007 -0.1237 -0.2034 0.0886  14  TRP L CE2 
21657 C CE3 . TRP L  14  ? 0.8849 0.9651 0.7976 -0.1117 -0.1959 0.0899  14  TRP L CE3 
21658 C CZ2 . TRP L  14  ? 1.0615 1.1421 0.9475 -0.1243 -0.2006 0.0854  14  TRP L CZ2 
21659 C CZ3 . TRP L  14  ? 1.0580 1.1346 0.9606 -0.1123 -0.1933 0.0867  14  TRP L CZ3 
21660 C CH2 . TRP L  14  ? 1.1334 1.2103 1.0230 -0.1185 -0.1957 0.0845  14  TRP L CH2 
21661 N N   . THR L  15  ? 1.1161 1.2170 1.0764 -0.1129 -0.2112 0.1069  15  THR L N   
21662 C CA  . THR L  15  ? 1.0875 1.1908 1.0635 -0.1084 -0.2112 0.1121  15  THR L CA  
21663 C C   . THR L  15  ? 1.1996 1.3026 1.1822 -0.1040 -0.2097 0.1176  15  THR L C   
21664 O O   . THR L  15  ? 1.1921 1.2942 1.1865 -0.0985 -0.2069 0.1199  15  THR L O   
21665 C CB  . THR L  15  ? 1.1231 1.2340 1.1055 -0.1124 -0.2179 0.1182  15  THR L CB  
21666 O OG1 . THR L  15  ? 1.5728 1.6886 1.5518 -0.1163 -0.2233 0.1243  15  THR L OG1 
21667 C CG2 . THR L  15  ? 1.1202 1.2316 1.0961 -0.1173 -0.2194 0.1128  15  THR L CG2 
21668 N N   . GLY L  16  ? 1.1532 1.2567 1.1278 -0.1064 -0.2115 0.1195  16  GLY L N   
21669 C CA  . GLY L  16  ? 1.2475 1.3510 1.2275 -0.1030 -0.2106 0.1251  16  GLY L CA  
21670 C C   . GLY L  16  ? 1.1533 1.2500 1.1341 -0.0971 -0.2034 0.1208  16  GLY L C   
21671 O O   . GLY L  16  ? 1.2044 1.3007 1.1951 -0.0925 -0.2012 0.1251  16  GLY L O   
21672 N N   . MET L  17  ? 1.2068 1.2984 1.1774 -0.0974 -0.1995 0.1124  17  MET L N   
21673 C CA  . MET L  17  ? 1.2290 1.3145 1.1998 -0.0921 -0.1926 0.1078  17  MET L CA  
21674 C C   . MET L  17  ? 1.2495 1.3333 1.2301 -0.0876 -0.1891 0.1058  17  MET L C   
21675 O O   . MET L  17  ? 1.2740 1.3568 1.2518 -0.0886 -0.1883 0.1008  17  MET L O   
21676 C CB  . MET L  17  ? 1.0254 1.1064 0.9819 -0.0940 -0.1898 0.0999  17  MET L CB  
21677 C CG  . MET L  17  ? 1.1560 1.2313 1.1120 -0.0888 -0.1829 0.0953  17  MET L CG  
21678 S SD  . MET L  17  ? 1.1677 1.2382 1.1074 -0.0911 -0.1798 0.0866  17  MET L SD  
21679 C CE  . MET L  17  ? 1.1212 1.1923 1.0566 -0.0947 -0.1813 0.0817  17  MET L CE  
21680 N N   . VAL L  18  ? 1.3887 1.4721 1.3807 -0.0826 -0.1866 0.1098  18  VAL L N   
21681 C CA  . VAL L  18  ? 1.4026 1.4846 1.4050 -0.0783 -0.1834 0.1088  18  VAL L CA  
21682 C C   . VAL L  18  ? 1.3876 1.4642 1.3921 -0.0728 -0.1765 0.1055  18  VAL L C   
21683 O O   . VAL L  18  ? 1.3998 1.4751 1.4141 -0.0685 -0.1733 0.1059  18  VAL L O   
21684 C CB  . VAL L  18  ? 1.4756 1.5625 1.4921 -0.0773 -0.1866 0.1170  18  VAL L CB  
21685 C CG1 . VAL L  18  ? 1.3049 1.3978 1.3198 -0.0829 -0.1937 0.1204  18  VAL L CG1 
21686 C CG2 . VAL L  18  ? 1.4781 1.5655 1.5005 -0.0750 -0.1861 0.1232  18  VAL L CG2 
21687 N N   . ASP L  19  ? 1.4887 1.5622 1.4838 -0.0730 -0.1743 0.1023  19  ASP L N   
21688 C CA  . ASP L  19  ? 1.5445 1.6132 1.5406 -0.0683 -0.1680 0.0991  19  ASP L CA  
21689 C C   . ASP L  19  ? 1.4259 1.4905 1.4152 -0.0671 -0.1637 0.0907  19  ASP L C   
21690 O O   . ASP L  19  ? 1.3451 1.4064 1.3382 -0.0627 -0.1586 0.0879  19  ASP L O   
21691 C CB  . ASP L  19  ? 1.6816 1.7492 1.6719 -0.0690 -0.1675 0.1003  19  ASP L CB  
21692 C CG  . ASP L  19  ? 1.8096 1.8815 1.8052 -0.0707 -0.1721 0.1088  19  ASP L CG  
21693 O OD1 . ASP L  19  ? 1.8060 1.8810 1.8131 -0.0695 -0.1741 0.1143  19  ASP L OD1 
21694 O OD2 . ASP L  19  ? 1.7770 1.8493 1.7655 -0.0732 -0.1738 0.1102  19  ASP L OD2 
21695 N N   . GLY L  20  ? 1.2974 1.3623 1.2766 -0.0711 -0.1658 0.0867  20  GLY L N   
21696 C CA  . GLY L  20  ? 1.0121 1.0732 0.9845 -0.0703 -0.1620 0.0790  20  GLY L CA  
21697 C C   . GLY L  20  ? 0.9506 1.0129 0.9155 -0.0749 -0.1650 0.0760  20  GLY L C   
21698 O O   . GLY L  20  ? 1.0017 1.0680 0.9677 -0.0787 -0.1702 0.0800  20  GLY L O   
21699 N N   . TRP L  21  ? 0.8775 0.9364 0.8350 -0.0747 -0.1616 0.0690  21  TRP L N   
21700 C CA  . TRP L  21  ? 0.9126 0.9718 0.8627 -0.0789 -0.1634 0.0653  21  TRP L CA  
21701 C C   . TRP L  21  ? 0.8274 0.8867 0.7653 -0.0838 -0.1656 0.0639  21  TRP L C   
21702 O O   . TRP L  21  ? 0.8164 0.8778 0.7496 -0.0888 -0.1695 0.0641  21  TRP L O   
21703 C CB  . TRP L  21  ? 0.9460 1.0014 0.8943 -0.0763 -0.1585 0.0587  21  TRP L CB  
21704 C CG  . TRP L  21  ? 0.8747 0.9308 0.8332 -0.0735 -0.1577 0.0596  21  TRP L CG  
21705 C CD1 . TRP L  21  ? 0.8531 0.9128 0.8197 -0.0747 -0.1617 0.0646  21  TRP L CD1 
21706 C CD2 . TRP L  21  ? 0.8960 0.9489 0.8575 -0.0691 -0.1526 0.0556  21  TRP L CD2 
21707 N NE1 . TRP L  21  ? 0.7880 0.8469 0.7628 -0.0713 -0.1592 0.0637  21  TRP L NE1 
21708 C CE2 . TRP L  21  ? 0.8128 0.8675 0.7844 -0.0679 -0.1537 0.0583  21  TRP L CE2 
21709 C CE3 . TRP L  21  ? 0.8184 0.8674 0.7752 -0.0662 -0.1474 0.0501  21  TRP L CE3 
21710 C CZ2 . TRP L  21  ? 0.8676 0.9200 0.8443 -0.0638 -0.1495 0.0556  21  TRP L CZ2 
21711 C CZ3 . TRP L  21  ? 0.6822 0.7294 0.6442 -0.0622 -0.1435 0.0477  21  TRP L CZ3 
21712 C CH2 . TRP L  21  ? 0.7567 0.8054 0.7283 -0.0610 -0.1445 0.0504  21  TRP L CH2 
21713 N N   . TYR L  22  ? 0.8850 0.9418 0.8177 -0.0825 -0.1629 0.0623  22  TYR L N   
21714 C CA  . TYR L  22  ? 0.8871 0.9437 0.8085 -0.0868 -0.1646 0.0611  22  TYR L CA  
21715 C C   . TYR L  22  ? 0.9949 1.0524 0.9175 -0.0861 -0.1654 0.0658  22  TYR L C   
21716 O O   . TYR L  22  ? 1.1487 1.2051 1.0782 -0.0814 -0.1624 0.0672  22  TYR L O   
21717 C CB  . TYR L  22  ? 0.9949 1.0471 0.9068 -0.0865 -0.1600 0.0536  22  TYR L CB  
21718 C CG  . TYR L  22  ? 1.0202 1.0703 0.9352 -0.0835 -0.1562 0.0491  22  TYR L CG  
21719 C CD1 . TYR L  22  ? 0.9030 0.9507 0.8229 -0.0779 -0.1513 0.0473  22  TYR L CD1 
21720 C CD2 . TYR L  22  ? 0.9361 0.9864 0.8489 -0.0863 -0.1574 0.0466  22  TYR L CD2 
21721 C CE1 . TYR L  22  ? 0.9109 0.9567 0.8335 -0.0751 -0.1479 0.0434  22  TYR L CE1 
21722 C CE2 . TYR L  22  ? 0.9387 0.9868 0.8544 -0.0834 -0.1538 0.0426  22  TYR L CE2 
21723 C CZ  . TYR L  22  ? 0.9315 0.9775 0.8522 -0.0777 -0.1491 0.0412  22  TYR L CZ  
21724 O OH  . TYR L  22  ? 0.7093 0.7532 0.6327 -0.0748 -0.1455 0.0375  22  TYR L OH  
21725 N N   . GLY L  23  ? 1.2523 1.3118 1.1681 -0.0908 -0.1693 0.0682  23  GLY L N   
21726 C CA  . GLY L  23  ? 1.3185 1.3789 1.2350 -0.0905 -0.1704 0.0730  23  GLY L CA  
21727 C C   . GLY L  23  ? 1.4320 1.4942 1.3388 -0.0962 -0.1745 0.0747  23  GLY L C   
21728 O O   . GLY L  23  ? 1.2549 1.3167 1.1524 -0.1005 -0.1757 0.0708  23  GLY L O   
21729 N N   . TYR L  24  ? 1.3446 1.4086 1.2533 -0.0964 -0.1765 0.0805  24  TYR L N   
21730 C CA  . TYR L  24  ? 1.1470 1.2127 1.0465 -0.1016 -0.1802 0.0826  24  TYR L CA  
21731 C C   . TYR L  24  ? 1.3068 1.3781 1.2122 -0.1038 -0.1862 0.0912  24  TYR L C   
21732 O O   . TYR L  24  ? 1.1044 1.1780 1.0218 -0.1008 -0.1871 0.0959  24  TYR L O   
21733 C CB  . TYR L  24  ? 1.0565 1.1189 0.9508 -0.1002 -0.1768 0.0813  24  TYR L CB  
21734 C CG  . TYR L  24  ? 1.0706 1.1280 0.9624 -0.0966 -0.1704 0.0741  24  TYR L CG  
21735 C CD1 . TYR L  24  ? 1.0412 1.0970 0.9424 -0.0908 -0.1663 0.0739  24  TYR L CD1 
21736 C CD2 . TYR L  24  ? 1.0257 1.0801 0.9057 -0.0991 -0.1683 0.0676  24  TYR L CD2 
21737 C CE1 . TYR L  24  ? 1.2110 1.2627 1.1098 -0.0876 -0.1607 0.0675  24  TYR L CE1 
21738 C CE2 . TYR L  24  ? 1.0193 1.0697 0.8975 -0.0957 -0.1626 0.0614  24  TYR L CE2 
21739 C CZ  . TYR L  24  ? 1.2126 1.2618 1.1001 -0.0900 -0.1590 0.0614  24  TYR L CZ  
21740 O OH  . TYR L  24  ? 1.0211 1.0668 0.9067 -0.0868 -0.1535 0.0554  24  TYR L OH  
21741 N N   . HIS L  25  ? 1.3657 1.4391 1.2625 -0.1091 -0.1902 0.0934  25  HIS L N   
21742 C CA  . HIS L  25  ? 1.2968 1.3757 1.1980 -0.1114 -0.1960 0.1022  25  HIS L CA  
21743 C C   . HIS L  25  ? 1.4356 1.5144 1.3272 -0.1147 -0.1974 0.1040  25  HIS L C   
21744 O O   . HIS L  25  ? 1.4435 1.5231 1.3239 -0.1203 -0.2001 0.1021  25  HIS L O   
21745 C CB  . HIS L  25  ? 1.4096 1.4934 1.3110 -0.1160 -0.2016 0.1040  25  HIS L CB  
21746 C CG  . HIS L  25  ? 1.4341 1.5241 1.3370 -0.1197 -0.2082 0.1126  25  HIS L CG  
21747 N ND1 . HIS L  25  ? 1.3783 1.4704 1.2696 -0.1261 -0.2122 0.1130  25  HIS L ND1 
21748 C CD2 . HIS L  25  ? 1.2890 1.3837 1.2039 -0.1178 -0.2113 0.1211  25  HIS L CD2 
21749 C CE1 . HIS L  25  ? 1.4506 1.5487 1.3464 -0.1282 -0.2178 0.1216  25  HIS L CE1 
21750 N NE2 . HIS L  25  ? 1.5059 1.6056 1.4163 -0.1231 -0.2174 0.1268  25  HIS L NE2 
21751 N N   . HIS L  26  ? 1.6371 1.7147 1.5333 -0.1111 -0.1952 0.1074  26  HIS L N   
21752 C CA  . HIS L  26  ? 1.6160 1.6930 1.5042 -0.1134 -0.1958 0.1094  26  HIS L CA  
21753 C C   . HIS L  26  ? 1.7496 1.8327 1.6386 -0.1175 -0.2027 0.1177  26  HIS L C   
21754 O O   . HIS L  26  ? 1.7734 1.8612 1.6716 -0.1175 -0.2064 0.1228  26  HIS L O   
21755 C CB  . HIS L  26  ? 1.6032 1.6770 1.4975 -0.1081 -0.1911 0.1107  26  HIS L CB  
21756 C CG  . HIS L  26  ? 1.5959 1.6731 1.5036 -0.1051 -0.1929 0.1194  26  HIS L CG  
21757 N ND1 . HIS L  26  ? 1.5516 1.6299 1.4720 -0.1011 -0.1921 0.1210  26  HIS L ND1 
21758 C CD2 . HIS L  26  ? 1.8849 1.9646 1.7956 -0.1055 -0.1953 0.1271  26  HIS L CD2 
21759 C CE1 . HIS L  26  ? 1.7599 1.8411 1.6907 -0.0992 -0.1938 0.1292  26  HIS L CE1 
21760 N NE2 . HIS L  26  ? 2.0002 2.0824 1.9255 -0.1017 -0.1958 0.1332  26  HIS L NE2 
21761 N N   . GLN L  27  ? 2.0064 2.0898 1.8862 -0.1211 -0.2043 0.1195  27  GLN L N   
21762 C CA  . GLN L  27  ? 1.9957 2.0852 1.8749 -0.1256 -0.2111 0.1274  27  GLN L CA  
21763 C C   . GLN L  27  ? 1.8861 1.9737 1.7564 -0.1273 -0.2103 0.1286  27  GLN L C   
21764 O O   . GLN L  27  ? 1.7893 1.8767 1.6464 -0.1327 -0.2121 0.1260  27  GLN L O   
21765 C CB  . GLN L  27  ? 1.9468 2.0397 1.8188 -0.1317 -0.2159 0.1255  27  GLN L CB  
21766 C CG  . GLN L  27  ? 2.0611 2.1601 1.9277 -0.1380 -0.2230 0.1321  27  GLN L CG  
21767 C CD  . GLN L  27  ? 2.1489 2.2549 2.0284 -0.1371 -0.2282 0.1421  27  GLN L CD  
21768 O OE1 . GLN L  27  ? 2.0683 2.1793 1.9504 -0.1401 -0.2328 0.1438  27  GLN L OE1 
21769 N NE2 . GLN L  27  ? 2.1583 2.2648 2.0461 -0.1332 -0.2274 0.1487  27  GLN L NE2 
21770 N N   . ASN L  28  ? 1.9130 1.9990 1.7908 -0.1226 -0.2074 0.1324  28  ASN L N   
21771 C CA  . ASN L  28  ? 2.0061 2.0902 1.8776 -0.1234 -0.2063 0.1343  28  ASN L CA  
21772 C C   . ASN L  28  ? 2.0990 2.1880 1.9790 -0.1230 -0.2103 0.1452  28  ASN L C   
21773 O O   . ASN L  28  ? 2.0945 2.1891 1.9824 -0.1236 -0.2150 0.1510  28  ASN L O   
21774 C CB  . ASN L  28  ? 1.8206 1.8981 1.6923 -0.1186 -0.1988 0.1291  28  ASN L CB  
21775 C CG  . ASN L  28  ? 1.7859 1.8626 1.6729 -0.1120 -0.1956 0.1322  28  ASN L CG  
21776 O OD1 . ASN L  28  ? 1.6800 1.7519 1.5687 -0.1080 -0.1897 0.1288  28  ASN L OD1 
21777 N ND2 . ASN L  28  ? 1.8598 1.9412 1.7579 -0.1110 -0.1992 0.1386  28  ASN L ND2 
21778 N N   . GLU L  29  ? 2.0041 2.0911 1.8831 -0.1217 -0.2082 0.1482  29  GLU L N   
21779 C CA  . GLU L  29  ? 1.9818 2.0732 1.8671 -0.1218 -0.2119 0.1587  29  GLU L CA  
21780 C C   . GLU L  29  ? 1.9493 2.0417 1.8521 -0.1158 -0.2102 0.1646  29  GLU L C   
21781 O O   . GLU L  29  ? 1.9749 2.0717 1.8853 -0.1154 -0.2135 0.1740  29  GLU L O   
21782 C CB  . GLU L  29  ? 2.1624 2.2510 2.0394 -0.1230 -0.2101 0.1595  29  GLU L CB  
21783 C CG  . GLU L  29  ? 2.2155 2.3025 2.0749 -0.1289 -0.2111 0.1535  29  GLU L CG  
21784 C CD  . GLU L  29  ? 2.3384 2.4199 2.1901 -0.1284 -0.2063 0.1504  29  GLU L CD  
21785 O OE1 . GLU L  29  ? 2.2545 2.3320 2.1134 -0.1230 -0.2008 0.1494  29  GLU L OE1 
21786 O OE2 . GLU L  29  ? 2.3463 2.4275 2.1846 -0.1335 -0.2079 0.1487  29  GLU L OE2 
21787 N N   . GLN L  30  ? 1.9400 2.0283 1.8492 -0.1110 -0.2050 0.1590  30  GLN L N   
21788 C CA  . GLN L  30  ? 1.9063 1.9948 1.8318 -0.1052 -0.2026 0.1637  30  GLN L CA  
21789 C C   . GLN L  30  ? 1.9200 2.0125 1.8547 -0.1044 -0.2054 0.1649  30  GLN L C   
21790 O O   . GLN L  30  ? 1.8688 1.9611 1.8171 -0.0997 -0.2031 0.1678  30  GLN L O   
21791 C CB  . GLN L  30  ? 1.7819 1.8634 1.7098 -0.1001 -0.1946 0.1576  30  GLN L CB  
21792 C CG  . GLN L  30  ? 1.6638 1.7416 1.5866 -0.0998 -0.1913 0.1580  30  GLN L CG  
21793 C CD  . GLN L  30  ? 1.7097 1.7816 1.6214 -0.0999 -0.1863 0.1478  30  GLN L CD  
21794 O OE1 . GLN L  30  ? 1.6449 1.7122 1.5607 -0.0956 -0.1802 0.1433  30  GLN L OE1 
21795 N NE2 . GLN L  30  ? 1.7906 1.8628 1.6883 -0.1050 -0.1887 0.1442  30  GLN L NE2 
21796 N N   . GLY L  31  ? 2.2949 2.3905 2.2220 -0.1093 -0.2100 0.1627  31  GLY L N   
21797 C CA  . GLY L  31  ? 2.2974 2.3971 2.2325 -0.1092 -0.2131 0.1639  31  GLY L CA  
21798 C C   . GLY L  31  ? 2.1776 2.2752 2.1050 -0.1111 -0.2123 0.1546  31  GLY L C   
21799 O O   . GLY L  31  ? 2.0348 2.1283 1.9498 -0.1131 -0.2098 0.1473  31  GLY L O   
21800 N N   . SER L  32  ? 2.0764 2.1770 2.0117 -0.1105 -0.2141 0.1551  32  SER L N   
21801 C CA  . SER L  32  ? 1.9407 2.0396 1.8702 -0.1121 -0.2134 0.1468  32  SER L CA  
21802 C C   . SER L  32  ? 1.8538 1.9503 1.7948 -0.1064 -0.2091 0.1443  32  SER L C   
21803 O O   . SER L  32  ? 1.8352 1.9298 1.7862 -0.1012 -0.2054 0.1470  32  SER L O   
21804 C CB  . SER L  32  ? 1.8773 1.9825 1.8032 -0.1181 -0.2204 0.1491  32  SER L CB  
21805 O OG  . SER L  32  ? 1.9551 2.0629 1.8708 -0.1235 -0.2247 0.1523  32  SER L OG  
21806 N N   . GLY L  33  ? 1.7584 1.8550 1.6979 -0.1076 -0.2095 0.1391  33  GLY L N   
21807 C CA  . GLY L  33  ? 1.7569 1.8517 1.7069 -0.1028 -0.2059 0.1367  33  GLY L CA  
21808 C C   . GLY L  33  ? 1.5418 1.6313 1.4847 -0.1020 -0.2013 0.1266  33  GLY L C   
21809 O O   . GLY L  33  ? 1.4156 1.5021 1.3457 -0.1047 -0.2000 0.1210  33  GLY L O   
21810 N N   . TYR L  34  ? 1.4556 1.5440 1.4070 -0.0984 -0.1988 0.1244  34  TYR L N   
21811 C CA  . TYR L  34  ? 1.2173 1.3010 1.1637 -0.0971 -0.1942 0.1153  34  TYR L CA  
21812 C C   . TYR L  34  ? 1.1985 1.2771 1.1505 -0.0909 -0.1875 0.1126  34  TYR L C   
21813 O O   . TYR L  34  ? 1.1811 1.2603 1.1446 -0.0870 -0.1863 0.1176  34  TYR L O   
21814 C CB  . TYR L  34  ? 1.1026 1.1885 1.0535 -0.0979 -0.1962 0.1141  34  TYR L CB  
21815 C CG  . TYR L  34  ? 1.1424 1.2339 1.0893 -0.1042 -0.2030 0.1170  34  TYR L CG  
21816 C CD1 . TYR L  34  ? 1.0709 1.1686 1.0269 -0.1052 -0.2083 0.1257  34  TYR L CD1 
21817 C CD2 . TYR L  34  ? 1.1186 1.2092 1.0527 -0.1092 -0.2041 0.1112  34  TYR L CD2 
21818 C CE1 . TYR L  34  ? 1.1109 1.2142 1.0631 -0.1112 -0.2148 0.1285  34  TYR L CE1 
21819 C CE2 . TYR L  34  ? 0.9592 1.0549 0.8892 -0.1153 -0.2103 0.1137  34  TYR L CE2 
21820 C CZ  . TYR L  34  ? 0.9564 1.0587 0.8954 -0.1164 -0.2158 0.1223  34  TYR L CZ  
21821 O OH  . TYR L  34  ? 0.9185 1.0263 0.8531 -0.1228 -0.2221 0.1248  34  TYR L OH  
21822 N N   . ALA L  35  ? 1.2011 1.2747 1.1448 -0.0900 -0.1829 0.1046  35  ALA L N   
21823 C CA  . ALA L  35  ? 1.1564 1.2254 1.1042 -0.0845 -0.1764 0.1012  35  ALA L CA  
21824 C C   . ALA L  35  ? 1.2328 1.2983 1.1754 -0.0836 -0.1727 0.0926  35  ALA L C   
21825 O O   . ALA L  35  ? 1.3771 1.4405 1.3080 -0.0862 -0.1719 0.0874  35  ALA L O   
21826 C CB  . ALA L  35  ? 1.2257 1.2922 1.1690 -0.0838 -0.1740 0.1014  35  ALA L CB  
21827 N N   . ALA L  36  ? 1.1783 1.2429 1.1294 -0.0798 -0.1701 0.0915  36  ALA L N   
21828 C CA  . ALA L  36  ? 1.2255 1.2871 1.1730 -0.0785 -0.1666 0.0840  36  ALA L CA  
21829 C C   . ALA L  36  ? 1.1439 1.2008 1.0863 -0.0757 -0.1608 0.0786  36  ALA L C   
21830 O O   . ALA L  36  ? 1.2108 1.2664 1.1580 -0.0725 -0.1581 0.0805  36  ALA L O   
21831 C CB  . ALA L  36  ? 1.2698 1.3320 1.2283 -0.0752 -0.1655 0.0847  36  ALA L CB  
21832 N N   . ASP L  37  ? 1.1161 1.1707 1.0491 -0.0771 -0.1590 0.0718  37  ASP L N   
21833 C CA  . ASP L  37  ? 1.0777 1.1283 1.0057 -0.0746 -0.1536 0.0664  37  ASP L CA  
21834 C C   . ASP L  37  ? 1.1532 1.2020 1.0896 -0.0691 -0.1490 0.0648  37  ASP L C   
21835 O O   . ASP L  37  ? 1.1319 1.1807 1.0719 -0.0678 -0.1483 0.0629  37  ASP L O   
21836 C CB  . ASP L  37  ? 0.9716 1.0204 0.8883 -0.0772 -0.1527 0.0598  37  ASP L CB  
21837 C CG  . ASP L  37  ? 1.1616 1.2068 1.0727 -0.0751 -0.1475 0.0545  37  ASP L CG  
21838 O OD1 . ASP L  37  ? 1.3463 1.3897 1.2491 -0.0765 -0.1459 0.0490  37  ASP L OD1 
21839 O OD2 . ASP L  37  ? 1.3123 1.3566 1.2274 -0.0720 -0.1450 0.0559  37  ASP L OD2 
21840 N N   . LEU L  38  ? 1.3107 1.3579 1.2501 -0.0662 -0.1458 0.0656  38  LEU L N   
21841 C CA  . LEU L  38  ? 1.4540 1.4995 1.4015 -0.0612 -0.1413 0.0646  38  LEU L CA  
21842 C C   . LEU L  38  ? 1.3226 1.3657 1.2663 -0.0592 -0.1373 0.0576  38  LEU L C   
21843 O O   . LEU L  38  ? 1.2366 1.2797 1.1859 -0.0571 -0.1362 0.0567  38  LEU L O   
21844 C CB  . LEU L  38  ? 1.7491 1.7932 1.6990 -0.0592 -0.1386 0.0664  38  LEU L CB  
21845 C CG  . LEU L  38  ? 1.8601 1.9026 1.8193 -0.0544 -0.1341 0.0665  38  LEU L CG  
21846 C CD1 . LEU L  38  ? 1.8213 1.8647 1.7890 -0.0524 -0.1342 0.0674  38  LEU L CD1 
21847 C CD2 . LEU L  38  ? 1.8176 1.8601 1.7825 -0.0537 -0.1339 0.0719  38  LEU L CD2 
21848 N N   . LYS L  39  ? 1.6138 1.6550 1.5483 -0.0600 -0.1351 0.0530  39  LYS L N   
21849 C CA  . LYS L  39  ? 1.6427 1.6819 1.5737 -0.0579 -0.1310 0.0467  39  LYS L CA  
21850 C C   . LYS L  39  ? 1.5686 1.6081 1.4971 -0.0593 -0.1323 0.0440  39  LYS L C   
21851 O O   . LYS L  39  ? 1.6390 1.6776 1.5701 -0.0565 -0.1294 0.0409  39  LYS L O   
21852 C CB  . LYS L  39  ? 1.7385 1.7760 1.6604 -0.0586 -0.1285 0.0426  39  LYS L CB  
21853 C CG  . LYS L  39  ? 1.9914 2.0271 1.9102 -0.0561 -0.1240 0.0365  39  LYS L CG  
21854 C CD  . LYS L  39  ? 2.2505 2.2848 2.1615 -0.0566 -0.1215 0.0330  39  LYS L CD  
21855 C CE  . LYS L  39  ? 2.2539 2.2871 2.1631 -0.0538 -0.1170 0.0275  39  LYS L CE  
21856 N NZ  . LYS L  39  ? 2.0676 2.0998 1.9700 -0.0541 -0.1144 0.0243  39  LYS L NZ  
21857 N N   . SER L  40  ? 1.2111 1.2519 1.1346 -0.0637 -0.1364 0.0452  40  SER L N   
21858 C CA  . SER L  40  ? 1.0545 1.0955 0.9747 -0.0657 -0.1376 0.0423  40  SER L CA  
21859 C C   . SER L  40  ? 1.0457 1.0880 0.9752 -0.0641 -0.1386 0.0446  40  SER L C   
21860 O O   . SER L  40  ? 1.0941 1.1352 1.0247 -0.0623 -0.1363 0.0411  40  SER L O   
21861 C CB  . SER L  40  ? 1.0898 1.1319 1.0020 -0.0713 -0.1418 0.0431  40  SER L CB  
21862 O OG  . SER L  40  ? 1.2917 1.3332 1.1993 -0.0735 -0.1421 0.0393  40  SER L OG  
21863 N N   . THR L  41  ? 1.0898 1.1346 1.0263 -0.0647 -0.1421 0.0506  41  THR L N   
21864 C CA  . THR L  41  ? 1.0248 1.0712 0.9709 -0.0634 -0.1435 0.0534  41  THR L CA  
21865 C C   . THR L  41  ? 1.0229 1.0675 0.9761 -0.0581 -0.1387 0.0517  41  THR L C   
21866 O O   . THR L  41  ? 0.8490 0.8935 0.8066 -0.0567 -0.1380 0.0506  41  THR L O   
21867 C CB  . THR L  41  ? 0.7881 0.8378 0.7415 -0.0645 -0.1477 0.0607  41  THR L CB  
21868 O OG1 . THR L  41  ? 1.0039 1.0559 0.9509 -0.0698 -0.1526 0.0625  41  THR L OG1 
21869 C CG2 . THR L  41  ? 0.8822 0.9335 0.8464 -0.0627 -0.1486 0.0635  41  THR L CG2 
21870 N N   . GLN L  42  ? 1.1780 1.2211 1.1319 -0.0553 -0.1354 0.0513  42  GLN L N   
21871 C CA  . GLN L  42  ? 1.1994 1.2408 1.1594 -0.0506 -0.1308 0.0497  42  GLN L CA  
21872 C C   . GLN L  42  ? 1.0496 1.0891 1.0051 -0.0492 -0.1275 0.0437  42  GLN L C   
21873 O O   . GLN L  42  ? 1.0496 1.0887 1.0108 -0.0465 -0.1257 0.0430  42  GLN L O   
21874 C CB  . GLN L  42  ? 1.2914 1.3315 1.2518 -0.0485 -0.1278 0.0501  42  GLN L CB  
21875 C CG  . GLN L  42  ? 1.3796 1.4181 1.3467 -0.0439 -0.1232 0.0490  42  GLN L CG  
21876 C CD  . GLN L  42  ? 1.4877 1.5273 1.4660 -0.0423 -0.1240 0.0532  42  GLN L CD  
21877 O OE1 . GLN L  42  ? 1.5313 1.5729 1.5141 -0.0441 -0.1279 0.0583  42  GLN L OE1 
21878 N NE2 . GLN L  42  ? 1.4017 1.4400 1.3848 -0.0388 -0.1204 0.0512  42  GLN L NE2 
21879 N N   . ASN L  43  ? 0.9480 0.9864 0.8936 -0.0509 -0.1268 0.0396  43  ASN L N   
21880 C CA  . ASN L  43  ? 1.0004 1.0372 0.9414 -0.0498 -0.1237 0.0341  43  ASN L CA  
21881 C C   . ASN L  43  ? 0.9437 0.9810 0.8863 -0.0509 -0.1253 0.0336  43  ASN L C   
21882 O O   . ASN L  43  ? 0.8537 0.8899 0.7989 -0.0482 -0.1224 0.0311  43  ASN L O   
21883 C CB  . ASN L  43  ? 1.0255 1.0613 0.9558 -0.0519 -0.1229 0.0303  43  ASN L CB  
21884 C CG  . ASN L  43  ? 1.2216 1.2562 1.1501 -0.0491 -0.1187 0.0277  43  ASN L CG  
21885 O OD1 . ASN L  43  ? 1.4458 1.4807 1.3770 -0.0482 -0.1183 0.0301  43  ASN L OD1 
21886 N ND2 . ASN L  43  ? 1.2809 1.3144 1.2050 -0.0477 -0.1154 0.0228  43  ASN L ND2 
21887 N N   . ALA L  44  ? 0.9235 0.9623 0.8643 -0.0551 -0.1298 0.0358  44  ALA L N   
21888 C CA  . ALA L  44  ? 0.7987 0.8381 0.7407 -0.0568 -0.1316 0.0354  44  ALA L CA  
21889 C C   . ALA L  44  ? 0.7962 0.8361 0.7489 -0.0535 -0.1308 0.0377  44  ALA L C   
21890 O O   . ALA L  44  ? 0.8000 0.8389 0.7543 -0.0521 -0.1289 0.0351  44  ALA L O   
21891 C CB  . ALA L  44  ? 0.7515 0.7931 0.6908 -0.0620 -0.1370 0.0384  44  ALA L CB  
21892 N N   . ILE L  45  ? 0.6903 0.7318 0.6507 -0.0523 -0.1321 0.0426  45  ILE L N   
21893 C CA  . ILE L  45  ? 0.7993 0.8411 0.7704 -0.0491 -0.1312 0.0451  45  ILE L CA  
21894 C C   . ILE L  45  ? 0.9244 0.9638 0.8969 -0.0447 -0.1258 0.0412  45  ILE L C   
21895 O O   . ILE L  45  ? 0.9038 0.9427 0.8806 -0.0430 -0.1245 0.0403  45  ILE L O   
21896 C CB  . ILE L  45  ? 0.8892 0.9326 0.8682 -0.0481 -0.1325 0.0508  45  ILE L CB  
21897 C CG1 . ILE L  45  ? 0.8009 0.8475 0.7815 -0.0521 -0.1383 0.0557  45  ILE L CG1 
21898 C CG2 . ILE L  45  ? 0.8999 0.9427 0.8895 -0.0439 -0.1299 0.0523  45  ILE L CG2 
21899 C CD1 . ILE L  45  ? 1.0126 1.0610 1.0019 -0.0511 -0.1398 0.0619  45  ILE L CD1 
21900 N N   . ASP L  46  ? 0.9738 1.0118 0.9423 -0.0429 -0.1227 0.0390  46  ASP L N   
21901 C CA  . ASP L  46  ? 0.8231 0.8593 0.7921 -0.0389 -0.1176 0.0354  46  ASP L CA  
21902 C C   . ASP L  46  ? 0.7189 0.7540 0.6834 -0.0389 -0.1162 0.0310  46  ASP L C   
21903 O O   . ASP L  46  ? 0.8381 0.8723 0.8068 -0.0361 -0.1136 0.0299  46  ASP L O   
21904 C CB  . ASP L  46  ? 0.8720 0.9073 0.8360 -0.0378 -0.1150 0.0334  46  ASP L CB  
21905 C CG  . ASP L  46  ? 1.2075 1.2430 1.1774 -0.0366 -0.1147 0.0372  46  ASP L CG  
21906 O OD1 . ASP L  46  ? 1.2513 1.2875 1.2301 -0.0355 -0.1155 0.0409  46  ASP L OD1 
21907 O OD2 . ASP L  46  ? 1.4136 1.4487 1.3794 -0.0366 -0.1135 0.0363  46  ASP L OD2 
21908 N N   . GLU L  47  ? 0.7328 0.7676 0.6888 -0.0422 -0.1177 0.0287  47  GLU L N   
21909 C CA  . GLU L  47  ? 0.6748 0.7083 0.6259 -0.0424 -0.1159 0.0244  47  GLU L CA  
21910 C C   . GLU L  47  ? 0.6932 0.7270 0.6485 -0.0436 -0.1176 0.0252  47  GLU L C   
21911 O O   . GLU L  47  ? 0.6131 0.6456 0.5692 -0.0417 -0.1149 0.0226  47  GLU L O   
21912 C CB  . GLU L  47  ? 0.5430 0.5760 0.4839 -0.0457 -0.1165 0.0215  47  GLU L CB  
21913 C CG  . GLU L  47  ? 0.7843 0.8168 0.7207 -0.0443 -0.1140 0.0197  47  GLU L CG  
21914 C CD  . GLU L  47  ? 0.9541 0.9856 0.8804 -0.0472 -0.1138 0.0163  47  GLU L CD  
21915 O OE1 . GLU L  47  ? 0.8381 0.8695 0.7606 -0.0510 -0.1165 0.0161  47  GLU L OE1 
21916 O OE2 . GLU L  47  ? 1.1136 1.1445 1.0358 -0.0457 -0.1110 0.0138  47  GLU L OE2 
21917 N N   . ILE L  48  ? 0.6747 0.7104 0.6328 -0.0467 -0.1221 0.0290  48  ILE L N   
21918 C CA  . ILE L  48  ? 0.5642 0.6006 0.5271 -0.0480 -0.1241 0.0302  48  ILE L CA  
21919 C C   . ILE L  48  ? 0.6029 0.6391 0.5756 -0.0437 -0.1218 0.0318  48  ILE L C   
21920 O O   . ILE L  48  ? 0.5933 0.6288 0.5691 -0.0429 -0.1207 0.0306  48  ILE L O   
21921 C CB  . ILE L  48  ? 0.6422 0.6814 0.6065 -0.0523 -0.1297 0.0345  48  ILE L CB  
21922 C CG1 . ILE L  48  ? 0.7185 0.7577 0.6725 -0.0572 -0.1319 0.0324  48  ILE L CG1 
21923 C CG2 . ILE L  48  ? 0.5296 0.5701 0.5012 -0.0530 -0.1316 0.0365  48  ILE L CG2 
21924 C CD1 . ILE L  48  ? 0.7320 0.7692 0.6805 -0.0586 -0.1301 0.0275  48  ILE L CD1 
21925 N N   . THR L  49  ? 0.6291 0.6658 0.6068 -0.0411 -0.1209 0.0345  49  THR L N   
21926 C CA  . THR L  49  ? 0.5680 0.6042 0.5546 -0.0369 -0.1182 0.0357  49  THR L CA  
21927 C C   . THR L  49  ? 0.7338 0.7678 0.7180 -0.0338 -0.1134 0.0312  49  THR L C   
21928 O O   . THR L  49  ? 0.7728 0.8061 0.7619 -0.0320 -0.1119 0.0309  49  THR L O   
21929 C CB  . THR L  49  ? 0.6191 0.6556 0.6099 -0.0348 -0.1172 0.0385  49  THR L CB  
21930 O OG1 . THR L  49  ? 0.8972 0.9359 0.8924 -0.0371 -0.1214 0.0436  49  THR L OG1 
21931 C CG2 . THR L  49  ? 0.5666 0.6019 0.5652 -0.0304 -0.1134 0.0388  49  THR L CG2 
21932 N N   . ASN L  50  ? 0.5529 0.5858 0.5297 -0.0331 -0.1111 0.0280  50  ASN L N   
21933 C CA  . ASN L  50  ? 0.6363 0.6676 0.6104 -0.0302 -0.1067 0.0239  50  ASN L CA  
21934 C C   . ASN L  50  ? 0.6691 0.6995 0.6415 -0.0313 -0.1066 0.0216  50  ASN L C   
21935 O O   . ASN L  50  ? 0.6431 0.6724 0.6179 -0.0285 -0.1035 0.0200  50  ASN L O   
21936 C CB  . ASN L  50  ? 0.6728 0.7037 0.6386 -0.0302 -0.1050 0.0209  50  ASN L CB  
21937 C CG  . ASN L  50  ? 0.7287 0.7586 0.6926 -0.0267 -0.1003 0.0174  50  ASN L CG  
21938 O OD1 . ASN L  50  ? 0.8899 0.9199 0.8567 -0.0236 -0.0977 0.0175  50  ASN L OD1 
21939 N ND2 . ASN L  50  ? 0.7478 0.7768 0.7070 -0.0273 -0.0992 0.0143  50  ASN L ND2 
21940 N N   . LYS L  51  ? 0.6666 0.6975 0.6349 -0.0356 -0.1100 0.0216  51  LYS L N   
21941 C CA  . LYS L  51  ? 0.5345 0.5644 0.5009 -0.0374 -0.1101 0.0194  51  LYS L CA  
21942 C C   . LYS L  51  ? 0.5644 0.5944 0.5396 -0.0361 -0.1101 0.0214  51  LYS L C   
21943 O O   . LYS L  51  ? 0.6963 0.7248 0.6725 -0.0342 -0.1072 0.0191  51  LYS L O   
21944 C CB  . LYS L  51  ? 0.6554 0.6861 0.6163 -0.0429 -0.1142 0.0196  51  LYS L CB  
21945 C CG  . LYS L  51  ? 0.5837 0.6132 0.5420 -0.0455 -0.1143 0.0171  51  LYS L CG  
21946 C CD  . LYS L  51  ? 0.6344 0.6643 0.5849 -0.0509 -0.1175 0.0162  51  LYS L CD  
21947 C CE  . LYS L  51  ? 0.7019 0.7301 0.6490 -0.0538 -0.1170 0.0130  51  LYS L CE  
21948 N NZ  . LYS L  51  ? 0.8312 0.8588 0.7686 -0.0585 -0.1184 0.0107  51  LYS L NZ  
21949 N N   . VAL L  52  ? 0.5949 0.6268 0.5767 -0.0369 -0.1133 0.0257  52  VAL L N   
21950 C CA  . VAL L  52  ? 0.5597 0.5920 0.5505 -0.0358 -0.1137 0.0280  52  VAL L CA  
21951 C C   . VAL L  52  ? 0.6757 0.7065 0.6714 -0.0307 -0.1090 0.0273  52  VAL L C   
21952 O O   . VAL L  52  ? 0.7940 0.8239 0.7939 -0.0292 -0.1073 0.0267  52  VAL L O   
21953 C CB  . VAL L  52  ? 0.5454 0.5804 0.5430 -0.0374 -0.1179 0.0333  52  VAL L CB  
21954 C CG1 . VAL L  52  ? 0.5824 0.6180 0.5896 -0.0365 -0.1182 0.0356  52  VAL L CG1 
21955 C CG2 . VAL L  52  ? 0.5613 0.5982 0.5536 -0.0427 -0.1227 0.0343  52  VAL L CG2 
21956 N N   . ASN L  53  ? 0.6329 0.6636 0.6279 -0.0281 -0.1070 0.0274  53  ASN L N   
21957 C CA  . ASN L  53  ? 0.7274 0.7569 0.7262 -0.0235 -0.1025 0.0267  53  ASN L CA  
21958 C C   . ASN L  53  ? 0.7751 0.8028 0.7696 -0.0216 -0.0989 0.0226  53  ASN L C   
21959 O O   . ASN L  53  ? 0.6812 0.7079 0.6801 -0.0185 -0.0959 0.0222  53  ASN L O   
21960 C CB  . ASN L  53  ? 0.7819 0.8116 0.7797 -0.0217 -0.1010 0.0271  53  ASN L CB  
21961 C CG  . ASN L  53  ? 0.8282 0.8590 0.8337 -0.0216 -0.1028 0.0316  53  ASN L CG  
21962 O OD1 . ASN L  53  ? 0.6972 0.7288 0.7096 -0.0224 -0.1049 0.0345  53  ASN L OD1 
21963 N ND2 . ASN L  53  ? 0.7643 0.7952 0.7689 -0.0206 -0.1017 0.0322  53  ASN L ND2 
21964 N N   . SER L  54  ? 0.6284 0.6557 0.6145 -0.0235 -0.0990 0.0196  54  SER L N   
21965 C CA  . SER L  54  ? 0.5628 0.5885 0.5447 -0.0219 -0.0954 0.0158  54  SER L CA  
21966 C C   . SER L  54  ? 0.6796 0.7042 0.6652 -0.0221 -0.0950 0.0155  54  SER L C   
21967 O O   . SER L  54  ? 0.6910 0.7144 0.6792 -0.0188 -0.0915 0.0145  54  SER L O   
21968 C CB  . SER L  54  ? 0.5207 0.5461 0.4933 -0.0242 -0.0957 0.0129  54  SER L CB  
21969 O OG  . SER L  54  ? 0.6964 0.7228 0.6655 -0.0236 -0.0954 0.0129  54  SER L OG  
21970 N N   . VAL L  55  ? 0.6068 0.6318 0.5923 -0.0262 -0.0986 0.0163  55  VAL L N   
21971 C CA  . VAL L  55  ? 0.6518 0.6758 0.6407 -0.0271 -0.0986 0.0159  55  VAL L CA  
21972 C C   . VAL L  55  ? 0.6643 0.6881 0.6624 -0.0238 -0.0970 0.0182  55  VAL L C   
21973 O O   . VAL L  55  ? 0.5902 0.6125 0.5910 -0.0226 -0.0948 0.0171  55  VAL L O   
21974 C CB  . VAL L  55  ? 0.6536 0.6788 0.6420 -0.0324 -0.1034 0.0172  55  VAL L CB  
21975 C CG1 . VAL L  55  ? 0.6679 0.6923 0.6608 -0.0334 -0.1034 0.0171  55  VAL L CG1 
21976 C CG2 . VAL L  55  ? 0.4341 0.4590 0.4128 -0.0360 -0.1046 0.0146  55  VAL L CG2 
21977 N N   . ILE L  56  ? 0.6075 0.6327 0.6104 -0.0224 -0.0979 0.0212  56  ILE L N   
21978 C CA  . ILE L  56  ? 0.5678 0.5929 0.5797 -0.0194 -0.0964 0.0236  56  ILE L CA  
21979 C C   . ILE L  56  ? 0.6470 0.6708 0.6590 -0.0147 -0.0916 0.0222  56  ILE L C   
21980 O O   . ILE L  56  ? 0.5748 0.5973 0.5906 -0.0121 -0.0887 0.0218  56  ILE L O   
21981 C CB  . ILE L  56  ? 0.5858 0.6129 0.6039 -0.0202 -0.0995 0.0279  56  ILE L CB  
21982 C CG1 . ILE L  56  ? 0.6918 0.7207 0.7116 -0.0247 -0.1045 0.0300  56  ILE L CG1 
21983 C CG2 . ILE L  56  ? 0.5522 0.5787 0.5792 -0.0166 -0.0971 0.0301  56  ILE L CG2 
21984 C CD1 . ILE L  56  ? 0.5969 0.6281 0.6229 -0.0256 -0.1078 0.0347  56  ILE L CD1 
21985 N N   . GLU L  57  ? 0.6349 0.6593 0.6425 -0.0137 -0.0907 0.0215  57  GLU L N   
21986 C CA  . GLU L  57  ? 0.7001 0.7239 0.7077 -0.0096 -0.0865 0.0205  57  GLU L CA  
21987 C C   . GLU L  57  ? 0.6811 0.7036 0.6851 -0.0074 -0.0829 0.0174  57  GLU L C   
21988 O O   . GLU L  57  ? 0.7622 0.7842 0.7685 -0.0039 -0.0793 0.0171  57  GLU L O   
21989 C CB  . GLU L  57  ? 0.8853 0.9102 0.8883 -0.0097 -0.0867 0.0202  57  GLU L CB  
21990 C CG  . GLU L  57  ? 1.3030 1.3279 1.3076 -0.0061 -0.0830 0.0200  57  GLU L CG  
21991 C CD  . GLU L  57  ? 1.3120 1.3369 1.3098 -0.0042 -0.0799 0.0167  57  GLU L CD  
21992 O OE1 . GLU L  57  ? 1.1367 1.1619 1.1278 -0.0059 -0.0808 0.0147  57  GLU L OE1 
21993 O OE2 . GLU L  57  ? 1.1210 1.1458 1.1202 -0.0010 -0.0764 0.0162  57  GLU L OE2 
21994 N N   . LYS L  58  ? 0.5495 0.5714 0.5482 -0.0096 -0.0836 0.0152  58  LYS L N   
21995 C CA  . LYS L  58  ? 0.5013 0.5219 0.4967 -0.0076 -0.0800 0.0124  58  LYS L CA  
21996 C C   . LYS L  58  ? 0.6665 0.6855 0.6675 -0.0062 -0.0783 0.0128  58  LYS L C   
21997 O O   . LYS L  58  ? 0.7310 0.7488 0.7302 -0.0045 -0.0752 0.0108  58  LYS L O   
21998 C CB  . LYS L  58  ? 0.6041 0.6243 0.5919 -0.0104 -0.0809 0.0098  58  LYS L CB  
21999 C CG  . LYS L  58  ? 0.6272 0.6488 0.6086 -0.0112 -0.0816 0.0088  58  LYS L CG  
22000 C CD  . LYS L  58  ? 0.6562 0.6786 0.6364 -0.0072 -0.0781 0.0080  58  LYS L CD  
22001 C CE  . LYS L  58  ? 0.6799 0.7037 0.6539 -0.0082 -0.0788 0.0069  58  LYS L CE  
22002 N NZ  . LYS L  58  ? 0.6420 0.6671 0.6148 -0.0046 -0.0755 0.0061  58  LYS L NZ  
22003 N N   . MET L  59  ? 0.6047 0.6239 0.6129 -0.0069 -0.0801 0.0155  59  MET L N   
22004 C CA  . MET L  59  ? 0.5313 0.5491 0.5455 -0.0058 -0.0787 0.0161  59  MET L CA  
22005 C C   . MET L  59  ? 0.6809 0.6983 0.7006 -0.0017 -0.0756 0.0175  59  MET L C   
22006 O O   . MET L  59  ? 0.9375 0.9553 0.9642 -0.0016 -0.0767 0.0202  59  MET L O   
22007 C CB  . MET L  59  ? 0.7916 0.8098 0.8105 -0.0093 -0.0826 0.0180  59  MET L CB  
22008 C CG  . MET L  59  ? 0.7090 0.7256 0.7336 -0.0088 -0.0812 0.0182  59  MET L CG  
22009 S SD  . MET L  59  ? 0.7943 0.8084 0.8138 -0.0076 -0.0771 0.0144  59  MET L SD  
22010 C CE  . MET L  59  ? 0.4823 0.4959 0.5011 -0.0129 -0.0803 0.0134  59  MET L CE  
22011 N N   . ASN L  60  ? 0.7775 0.7944 0.7942 0.0016  -0.0716 0.0158  60  ASN L N   
22012 C CA  . ASN L  60  ? 0.8537 0.8702 0.8748 0.0054  -0.0683 0.0169  60  ASN L CA  
22013 C C   . ASN L  60  ? 0.8049 0.8196 0.8290 0.0074  -0.0653 0.0164  60  ASN L C   
22014 O O   . ASN L  60  ? 0.9293 0.9433 0.9492 0.0092  -0.0625 0.0145  60  ASN L O   
22015 C CB  . ASN L  60  ? 1.0234 1.0411 1.0397 0.0077  -0.0660 0.0158  60  ASN L CB  
22016 C CG  . ASN L  60  ? 1.2778 1.2955 1.2884 0.0095  -0.0632 0.0134  60  ASN L CG  
22017 O OD1 . ASN L  60  ? 1.3230 1.3401 1.3348 0.0127  -0.0597 0.0132  60  ASN L OD1 
22018 N ND2 . ASN L  60  ? 1.1864 1.2046 1.1908 0.0075  -0.0646 0.0115  60  ASN L ND2 
22019 N N   . THR L  61  ? 0.7736 0.7873 0.8050 0.0070  -0.0659 0.0183  61  THR L N   
22020 C CA  . THR L  61  ? 0.7890 0.8006 0.8238 0.0083  -0.0634 0.0179  61  THR L CA  
22021 C C   . THR L  61  ? 0.7011 0.7120 0.7386 0.0126  -0.0591 0.0185  61  THR L C   
22022 O O   . THR L  61  ? 0.6245 0.6362 0.6634 0.0141  -0.0584 0.0197  61  THR L O   
22023 C CB  . THR L  61  ? 0.8397 0.8508 0.8814 0.0058  -0.0659 0.0196  61  THR L CB  
22024 O OG1 . THR L  61  ? 0.8334 0.8454 0.8814 0.0062  -0.0671 0.0224  61  THR L OG1 
22025 C CG2 . THR L  61  ? 0.7438 0.7557 0.7821 0.0013  -0.0700 0.0188  61  THR L CG2 
22026 N N   . GLN L  62  ? 0.7614 0.7705 0.7994 0.0145  -0.0559 0.0176  62  GLN L N   
22027 C CA  . GLN L  62  ? 0.8631 0.8714 0.9036 0.0184  -0.0517 0.0183  62  GLN L CA  
22028 C C   . GLN L  62  ? 0.8194 0.8264 0.8686 0.0186  -0.0516 0.0205  62  GLN L C   
22029 O O   . GLN L  62  ? 0.7665 0.7731 0.8200 0.0159  -0.0543 0.0212  62  GLN L O   
22030 C CB  . GLN L  62  ? 0.8069 0.8136 0.8449 0.0204  -0.0483 0.0168  62  GLN L CB  
22031 C CG  . GLN L  62  ? 0.6185 0.6265 0.6484 0.0209  -0.0476 0.0148  62  GLN L CG  
22032 C CD  . GLN L  62  ? 0.8035 0.8137 0.8302 0.0234  -0.0461 0.0151  62  GLN L CD  
22033 O OE1 . GLN L  62  ? 0.9256 0.9375 0.9510 0.0221  -0.0484 0.0154  62  GLN L OE1 
22034 N NE2 . GLN L  62  ? 0.7350 0.7453 0.7604 0.0269  -0.0423 0.0150  62  GLN L NE2 
22035 N N   . PHE L  63  ? 0.8063 0.8129 0.8583 0.0217  -0.0485 0.0216  63  PHE L N   
22036 C CA  . PHE L  63  ? 0.6553 0.6604 0.7158 0.0223  -0.0475 0.0236  63  PHE L CA  
22037 C C   . PHE L  63  ? 0.5884 0.5913 0.6511 0.0235  -0.0450 0.0231  63  PHE L C   
22038 O O   . PHE L  63  ? 0.7665 0.7685 0.8271 0.0266  -0.0411 0.0226  63  PHE L O   
22039 C CB  . PHE L  63  ? 0.6484 0.6535 0.7109 0.0250  -0.0447 0.0247  63  PHE L CB  
22040 C CG  . PHE L  63  ? 0.7343 0.7378 0.8059 0.0256  -0.0437 0.0268  63  PHE L CG  
22041 C CD1 . PHE L  63  ? 0.6658 0.6698 0.7426 0.0242  -0.0456 0.0287  63  PHE L CD1 
22042 C CD2 . PHE L  63  ? 0.6732 0.6745 0.7483 0.0275  -0.0405 0.0271  63  PHE L CD2 
22043 C CE1 . PHE L  63  ? 0.7076 0.7102 0.7933 0.0248  -0.0445 0.0308  63  PHE L CE1 
22044 C CE2 . PHE L  63  ? 0.7313 0.7310 0.8149 0.0280  -0.0394 0.0290  63  PHE L CE2 
22045 C CZ  . PHE L  63  ? 0.7830 0.7834 0.8720 0.0266  -0.0414 0.0309  63  PHE L CZ  
22046 N N   . THR L  64  ? 0.4926 0.4946 0.5593 0.0209  -0.0471 0.0233  64  THR L N   
22047 C CA  . THR L  64  ? 0.7751 0.7748 0.8443 0.0216  -0.0448 0.0228  64  THR L CA  
22048 C C   . THR L  64  ? 0.5625 0.5614 0.6406 0.0200  -0.0461 0.0245  64  THR L C   
22049 O O   . THR L  64  ? 0.5245 0.5249 0.6057 0.0171  -0.0500 0.0256  64  THR L O   
22050 C CB  . THR L  64  ? 0.7778 0.7772 0.8415 0.0196  -0.0456 0.0204  64  THR L CB  
22051 O OG1 . THR L  64  ? 0.7295 0.7306 0.7913 0.0156  -0.0504 0.0201  64  THR L OG1 
22052 C CG2 . THR L  64  ? 0.7758 0.7755 0.8319 0.0222  -0.0430 0.0189  64  THR L CG2 
22053 N N   . ALA L  65  ? 0.5529 0.5494 0.6353 0.0220  -0.0426 0.0248  65  ALA L N   
22054 C CA  . ALA L  65  ? 0.4174 0.4130 0.5084 0.0204  -0.0434 0.0261  65  ALA L CA  
22055 C C   . ALA L  65  ? 0.4541 0.4480 0.5446 0.0187  -0.0431 0.0243  65  ALA L C   
22056 O O   . ALA L  65  ? 0.6670 0.6584 0.7591 0.0208  -0.0392 0.0239  65  ALA L O   
22057 C CB  . ALA L  65  ? 0.4629 0.4568 0.5600 0.0237  -0.0397 0.0278  65  ALA L CB  
22058 N N   . VAL L  66  ? 0.4406 0.4358 0.5285 0.0146  -0.0471 0.0233  66  VAL L N   
22059 C CA  . VAL L  66  ? 0.4681 0.4618 0.5560 0.0121  -0.0472 0.0215  66  VAL L CA  
22060 C C   . VAL L  66  ? 0.6044 0.5970 0.7016 0.0117  -0.0465 0.0229  66  VAL L C   
22061 O O   . VAL L  66  ? 0.7319 0.7256 0.8356 0.0122  -0.0476 0.0254  66  VAL L O   
22062 C CB  . VAL L  66  ? 0.4713 0.4670 0.5551 0.0073  -0.0520 0.0202  66  VAL L CB  
22063 C CG1 . VAL L  66  ? 0.5131 0.5120 0.5982 0.0057  -0.0565 0.0223  66  VAL L CG1 
22064 C CG2 . VAL L  66  ? 0.4720 0.4667 0.5590 0.0035  -0.0532 0.0192  66  VAL L CG2 
22065 N N   . GLY L  67  ? 0.5421 0.5323 0.6403 0.0109  -0.0444 0.0213  67  GLY L N   
22066 C CA  . GLY L  67  ? 0.7025 0.6911 0.8093 0.0109  -0.0429 0.0224  67  GLY L CA  
22067 C C   . GLY L  67  ? 0.7097 0.6954 0.8180 0.0158  -0.0371 0.0227  67  GLY L C   
22068 O O   . GLY L  67  ? 0.4669 0.4530 0.5748 0.0192  -0.0354 0.0242  67  GLY L O   
22069 N N   . LYS L  68  ? 0.7309 0.7137 0.8407 0.0160  -0.0338 0.0214  68  LYS L N   
22070 C CA  . LYS L  68  ? 0.4271 0.4069 0.5386 0.0204  -0.0281 0.0218  68  LYS L CA  
22071 C C   . LYS L  68  ? 0.6592 0.6369 0.7790 0.0196  -0.0264 0.0222  68  LYS L C   
22072 O O   . LYS L  68  ? 0.6810 0.6594 0.8041 0.0154  -0.0295 0.0216  68  LYS L O   
22073 C CB  . LYS L  68  ? 0.7256 0.7036 0.8297 0.0223  -0.0247 0.0198  68  LYS L CB  
22074 C CG  . LYS L  68  ? 0.6549 0.6351 0.7508 0.0230  -0.0262 0.0192  68  LYS L CG  
22075 C CD  . LYS L  68  ? 0.6835 0.6646 0.7790 0.0272  -0.0243 0.0212  68  LYS L CD  
22076 C CE  . LYS L  68  ? 0.7682 0.7519 0.8562 0.0277  -0.0261 0.0208  68  LYS L CE  
22077 N NZ  . LYS L  68  ? 0.7461 0.7322 0.8367 0.0271  -0.0292 0.0226  68  LYS L NZ  
22078 N N   . GLU L  69  ? 0.6846 0.6598 0.8078 0.0235  -0.0215 0.0233  69  GLU L N   
22079 C CA  . GLU L  69  ? 0.4828 0.4556 0.6139 0.0230  -0.0194 0.0237  69  GLU L CA  
22080 C C   . GLU L  69  ? 0.5079 0.4768 0.6373 0.0254  -0.0138 0.0223  69  GLU L C   
22081 O O   . GLU L  69  ? 0.5961 0.5639 0.7218 0.0296  -0.0101 0.0229  69  GLU L O   
22082 C CB  . GLU L  69  ? 0.6091 0.5822 0.7476 0.0253  -0.0184 0.0265  69  GLU L CB  
22083 C CG  . GLU L  69  ? 0.7925 0.7692 0.9344 0.0230  -0.0235 0.0282  69  GLU L CG  
22084 C CD  . GLU L  69  ? 0.8443 0.8209 0.9929 0.0256  -0.0218 0.0309  69  GLU L CD  
22085 O OE1 . GLU L  69  ? 0.9284 0.9025 1.0761 0.0297  -0.0170 0.0314  69  GLU L OE1 
22086 O OE2 . GLU L  69  ? 0.7051 0.6839 0.8598 0.0236  -0.0253 0.0327  69  GLU L OE2 
22087 N N   . PHE L  70  ? 0.5273 0.4943 0.6597 0.0226  -0.0133 0.0207  70  PHE L N   
22088 C CA  . PHE L  70  ? 0.5106 0.4736 0.6421 0.0245  -0.0079 0.0194  70  PHE L CA  
22089 C C   . PHE L  70  ? 0.5142 0.4748 0.6543 0.0232  -0.0059 0.0194  70  PHE L C   
22090 O O   . PHE L  70  ? 0.6527 0.6148 0.7975 0.0190  -0.0097 0.0191  70  PHE L O   
22091 C CB  . PHE L  70  ? 0.5455 0.5078 0.6701 0.0221  -0.0082 0.0164  70  PHE L CB  
22092 C CG  . PHE L  70  ? 0.6035 0.5683 0.7197 0.0228  -0.0104 0.0161  70  PHE L CG  
22093 C CD1 . PHE L  70  ? 0.4600 0.4241 0.5712 0.0275  -0.0068 0.0168  70  PHE L CD1 
22094 C CD2 . PHE L  70  ? 0.5398 0.5078 0.6533 0.0187  -0.0160 0.0153  70  PHE L CD2 
22095 C CE1 . PHE L  70  ? 0.4795 0.4462 0.5834 0.0280  -0.0088 0.0165  70  PHE L CE1 
22096 C CE2 . PHE L  70  ? 0.4620 0.4322 0.5679 0.0193  -0.0179 0.0149  70  PHE L CE2 
22097 C CZ  . PHE L  70  ? 0.4352 0.4048 0.5365 0.0239  -0.0143 0.0155  70  PHE L CZ  
22098 N N   . ASN L  71  ? 0.5565 0.5135 0.6986 0.0269  -0.0001 0.0200  71  ASN L N   
22099 C CA  . ASN L  71  ? 0.5676 0.5219 0.7178 0.0259  0.0023  0.0199  71  ASN L CA  
22100 C C   . ASN L  71  ? 0.5962 0.5481 0.7454 0.0224  0.0033  0.0168  71  ASN L C   
22101 O O   . ASN L  71  ? 0.6453 0.5973 0.7875 0.0211  0.0026  0.0148  71  ASN L O   
22102 C CB  . ASN L  71  ? 0.6072 0.5584 0.7602 0.0312  0.0083  0.0219  71  ASN L CB  
22103 C CG  . ASN L  71  ? 0.6506 0.5992 0.7972 0.0347  0.0131  0.0213  71  ASN L CG  
22104 O OD1 . ASN L  71  ? 0.7276 0.6740 0.8719 0.0332  0.0148  0.0190  71  ASN L OD1 
22105 N ND2 . ASN L  71  ? 0.7111 0.6599 0.8547 0.0395  0.0155  0.0234  71  ASN L ND2 
22106 N N   . HIS L  72  ? 0.5785 0.5282 0.7350 0.0208  0.0052  0.0164  72  HIS L N   
22107 C CA  . HIS L  72  ? 0.6886 0.6359 0.8452 0.0168  0.0061  0.0133  72  HIS L CA  
22108 C C   . HIS L  72  ? 0.6315 0.5751 0.7819 0.0190  0.0112  0.0115  72  HIS L C   
22109 O O   . HIS L  72  ? 0.7479 0.6899 0.8957 0.0154  0.0115  0.0084  72  HIS L O   
22110 C CB  . HIS L  72  ? 0.6986 0.6440 0.8646 0.0153  0.0080  0.0134  72  HIS L CB  
22111 C CG  . HIS L  72  ? 0.9986 0.9405 1.1684 0.0206  0.0142  0.0153  72  HIS L CG  
22112 N ND1 . HIS L  72  ? 1.0213 0.9644 1.1949 0.0241  0.0144  0.0185  72  HIS L ND1 
22113 C CD2 . HIS L  72  ? 1.1082 1.0452 1.2785 0.0229  0.0206  0.0145  72  HIS L CD2 
22114 C CE1 . HIS L  72  ? 1.0777 1.0169 1.2536 0.0283  0.0205  0.0196  72  HIS L CE1 
22115 N NE2 . HIS L  72  ? 1.0975 1.0331 1.2716 0.0277  0.0243  0.0174  72  HIS L NE2 
22116 N N   . LEU L  73  ? 0.5597 0.5019 0.7078 0.0247  0.0153  0.0134  73  LEU L N   
22117 C CA  . LEU L  73  ? 0.6686 0.6076 0.8114 0.0275  0.0203  0.0124  73  LEU L CA  
22118 C C   . LEU L  73  ? 0.5796 0.5211 0.7137 0.0288  0.0183  0.0124  73  LEU L C   
22119 O O   . LEU L  73  ? 0.5159 0.4559 0.6457 0.0327  0.0224  0.0129  73  LEU L O   
22120 C CB  . LEU L  73  ? 0.5647 0.5004 0.7105 0.0330  0.0266  0.0148  73  LEU L CB  
22121 C CG  . LEU L  73  ? 0.6063 0.5383 0.7602 0.0322  0.0302  0.0145  73  LEU L CG  
22122 C CD1 . LEU L  73  ? 0.7151 0.6445 0.8716 0.0379  0.0359  0.0173  73  LEU L CD1 
22123 C CD2 . LEU L  73  ? 0.5423 0.4708 0.6956 0.0290  0.0327  0.0111  73  LEU L CD2 
22124 N N   . GLU L  74  ? 0.5533 0.4989 0.6850 0.0256  0.0122  0.0120  74  GLU L N   
22125 C CA  . GLU L  74  ? 0.5453 0.4936 0.6688 0.0263  0.0098  0.0118  74  GLU L CA  
22126 C C   . GLU L  74  ? 0.6401 0.5905 0.7605 0.0205  0.0045  0.0092  74  GLU L C   
22127 O O   . GLU L  74  ? 0.5449 0.4989 0.6606 0.0197  0.0002  0.0094  74  GLU L O   
22128 C CB  . GLU L  74  ? 0.4363 0.3879 0.5591 0.0295  0.0077  0.0147  74  GLU L CB  
22129 C CG  . GLU L  74  ? 0.5600 0.5099 0.6841 0.0354  0.0129  0.0173  74  GLU L CG  
22130 C CD  . GLU L  74  ? 0.7416 0.6949 0.8652 0.0380  0.0109  0.0199  74  GLU L CD  
22131 O OE1 . GLU L  74  ? 0.5959 0.5512 0.7237 0.0358  0.0070  0.0206  74  GLU L OE1 
22132 O OE2 . GLU L  74  ? 0.5237 0.4774 0.6428 0.0422  0.0133  0.0213  74  GLU L OE2 
22133 N N   . LYS L  75  ? 0.5334 0.4816 0.6562 0.0162  0.0049  0.0066  75  LYS L N   
22134 C CA  . LYS L  75  ? 0.5164 0.4663 0.6362 0.0101  0.0001  0.0040  75  LYS L CA  
22135 C C   . LYS L  75  ? 0.5211 0.4713 0.6318 0.0099  -0.0001 0.0021  75  LYS L C   
22136 O O   . LYS L  75  ? 0.5592 0.5123 0.6658 0.0059  -0.0050 0.0009  75  LYS L O   
22137 C CB  . LYS L  75  ? 0.6005 0.5476 0.7243 0.0055  0.0015  0.0013  75  LYS L CB  
22138 C CG  . LYS L  75  ? 0.7980 0.7467 0.9182 -0.0012 -0.0031 -0.0018 75  LYS L CG  
22139 C CD  . LYS L  75  ? 0.6592 0.6135 0.7806 -0.0041 -0.0105 -0.0001 75  LYS L CD  
22140 C CE  . LYS L  75  ? 0.9905 0.9460 1.1213 -0.0061 -0.0123 0.0012  75  LYS L CE  
22141 N NZ  . LYS L  75  ? 1.2008 1.1618 1.3333 -0.0089 -0.0194 0.0032  75  LYS L NZ  
22142 N N   . ARG L  76  ? 0.5259 0.4732 0.6337 0.0141  0.0055  0.0021  76  ARG L N   
22143 C CA  . ARG L  76  ? 0.5113 0.4585 0.6110 0.0143  0.0060  0.0005  76  ARG L CA  
22144 C C   . ARG L  76  ? 0.5589 0.5106 0.6538 0.0159  0.0018  0.0022  76  ARG L C   
22145 O O   . ARG L  76  ? 0.5133 0.4670 0.6027 0.0127  -0.0018 0.0005  76  ARG L O   
22146 C CB  . ARG L  76  ? 0.4709 0.4142 0.5697 0.0188  0.0132  0.0007  76  ARG L CB  
22147 C CG  . ARG L  76  ? 0.4951 0.4333 0.5963 0.0163  0.0176  -0.0021 76  ARG L CG  
22148 C CD  . ARG L  76  ? 0.5824 0.5167 0.6835 0.0214  0.0249  -0.0013 76  ARG L CD  
22149 N NE  . ARG L  76  ? 0.5072 0.4419 0.6126 0.0269  0.0272  0.0024  76  ARG L NE  
22150 C CZ  . ARG L  76  ? 0.5404 0.4749 0.6440 0.0326  0.0310  0.0049  76  ARG L CZ  
22151 N NH1 . ARG L  76  ? 0.6029 0.5369 0.7010 0.0338  0.0331  0.0041  76  ARG L NH1 
22152 N NH2 . ARG L  76  ? 0.5875 0.5223 0.6948 0.0371  0.0329  0.0082  76  ARG L NH2 
22153 N N   . ILE L  77  ? 0.5460 0.4994 0.6428 0.0207  0.0025  0.0055  77  ILE L N   
22154 C CA  . ILE L  77  ? 0.4913 0.4489 0.5840 0.0221  -0.0013 0.0071  77  ILE L CA  
22155 C C   . ILE L  77  ? 0.4424 0.4034 0.5366 0.0177  -0.0078 0.0071  77  ILE L C   
22156 O O   . ILE L  77  ? 0.5084 0.4727 0.5979 0.0168  -0.0118 0.0073  77  ILE L O   
22157 C CB  . ILE L  77  ? 0.4053 0.3638 0.4996 0.0279  0.0011  0.0104  77  ILE L CB  
22158 C CG1 . ILE L  77  ? 0.6895 0.6460 0.7918 0.0291  0.0034  0.0120  77  ILE L CG1 
22159 C CG2 . ILE L  77  ? 0.4690 0.4261 0.5589 0.0323  0.0060  0.0108  77  ILE L CG2 
22160 C CD1 . ILE L  77  ? 0.7490 0.7059 0.8527 0.0346  0.0062  0.0151  77  ILE L CD1 
22161 N N   . GLU L  78  ? 0.4846 0.4450 0.5857 0.0151  -0.0089 0.0072  78  GLU L N   
22162 C CA  . GLU L  78  ? 0.4695 0.4332 0.5729 0.0106  -0.0151 0.0075  78  GLU L CA  
22163 C C   . GLU L  78  ? 0.4796 0.4442 0.5770 0.0055  -0.0185 0.0046  78  GLU L C   
22164 O O   . GLU L  78  ? 0.5368 0.5051 0.6319 0.0030  -0.0238 0.0050  78  GLU L O   
22165 C CB  . GLU L  78  ? 0.5189 0.4817 0.6311 0.0086  -0.0151 0.0080  78  GLU L CB  
22166 C CG  . GLU L  78  ? 0.5251 0.4917 0.6406 0.0040  -0.0215 0.0087  78  GLU L CG  
22167 C CD  . GLU L  78  ? 0.8664 0.8323 0.9907 0.0016  -0.0216 0.0090  78  GLU L CD  
22168 O OE1 . GLU L  78  ? 1.1369 1.0999 1.2662 0.0049  -0.0168 0.0098  78  GLU L OE1 
22169 O OE2 . GLU L  78  ? 0.9338 0.9024 1.0604 -0.0035 -0.0265 0.0086  78  GLU L OE2 
22170 N N   . ASN L  79  ? 0.3852 0.3463 0.4802 0.0039  -0.0151 0.0017  79  ASN L N   
22171 C CA  . ASN L  79  ? 0.5130 0.4743 0.6019 -0.0011 -0.0175 -0.0015 79  ASN L CA  
22172 C C   . ASN L  79  ? 0.6297 0.5922 0.7104 0.0008  -0.0176 -0.0018 79  ASN L C   
22173 O O   . ASN L  79  ? 0.5439 0.5084 0.6194 -0.0030 -0.0216 -0.0033 79  ASN L O   
22174 C CB  . ASN L  79  ? 0.5471 0.5040 0.6364 -0.0037 -0.0134 -0.0047 79  ASN L CB  
22175 C CG  . ASN L  79  ? 0.7727 0.7296 0.8687 -0.0081 -0.0152 -0.0052 79  ASN L CG  
22176 O OD1 . ASN L  79  ? 0.7348 0.6956 0.8332 -0.0111 -0.0209 -0.0040 79  ASN L OD1 
22177 N ND2 . ASN L  79  ? 0.6858 0.6383 0.7851 -0.0084 -0.0103 -0.0069 79  ASN L ND2 
22178 N N   . LEU L  80  ? 0.4923 0.4535 0.5718 0.0066  -0.0132 -0.0005 80  LEU L N   
22179 C CA  . LEU L  80  ? 0.4240 0.3869 0.4966 0.0089  -0.0133 -0.0003 80  LEU L CA  
22180 C C   . LEU L  80  ? 0.5441 0.5117 0.6156 0.0081  -0.0193 0.0015  80  LEU L C   
22181 O O   . LEU L  80  ? 0.5613 0.5310 0.6269 0.0058  -0.0225 0.0003  80  LEU L O   
22182 C CB  . LEU L  80  ? 0.4377 0.3994 0.5106 0.0155  -0.0081 0.0017  80  LEU L CB  
22183 C CG  . LEU L  80  ? 0.5080 0.4700 0.5741 0.0182  -0.0059 0.0012  80  LEU L CG  
22184 C CD1 . LEU L  80  ? 0.3637 0.3269 0.4304 0.0244  -0.0031 0.0043  80  LEU L CD1 
22185 C CD2 . LEU L  80  ? 0.5812 0.5464 0.6410 0.0152  -0.0108 0.0001  80  LEU L CD2 
22186 N N   . ASN L  81  ? 0.4676 0.4367 0.5449 0.0099  -0.0204 0.0042  81  ASN L N   
22187 C CA  . ASN L  81  ? 0.3789 0.3522 0.4566 0.0093  -0.0256 0.0062  81  ASN L CA  
22188 C C   . ASN L  81  ? 0.5660 0.5414 0.6428 0.0031  -0.0312 0.0050  81  ASN L C   
22189 O O   . ASN L  81  ? 0.5454 0.5239 0.6183 0.0018  -0.0353 0.0053  81  ASN L O   
22190 C CB  . ASN L  81  ? 0.3914 0.3652 0.4768 0.0119  -0.0252 0.0092  81  ASN L CB  
22191 C CG  . ASN L  81  ? 0.5355 0.5133 0.6222 0.0111  -0.0302 0.0113  81  ASN L CG  
22192 O OD1 . ASN L  81  ? 0.4945 0.4743 0.5766 0.0130  -0.0312 0.0121  81  ASN L OD1 
22193 N ND2 . ASN L  81  ? 0.5821 0.5610 0.6753 0.0083  -0.0332 0.0124  81  ASN L ND2 
22194 N N   . LYS L  82  ? 0.4610 0.4348 0.5415 -0.0007 -0.0315 0.0036  82  LYS L N   
22195 C CA  . LYS L  82  ? 0.5164 0.4923 0.5959 -0.0069 -0.0368 0.0024  82  LYS L CA  
22196 C C   . LYS L  82  ? 0.5305 0.5062 0.6010 -0.0095 -0.0376 -0.0004 82  LYS L C   
22197 O O   . LYS L  82  ? 0.5461 0.5248 0.6134 -0.0133 -0.0427 -0.0006 82  LYS L O   
22198 C CB  . LYS L  82  ? 0.5637 0.5377 0.6486 -0.0106 -0.0363 0.0010  82  LYS L CB  
22199 C CG  . LYS L  82  ? 0.6725 0.6485 0.7551 -0.0176 -0.0413 -0.0008 82  LYS L CG  
22200 C CD  . LYS L  82  ? 0.8455 0.8200 0.9337 -0.0215 -0.0408 -0.0022 82  LYS L CD  
22201 C CE  . LYS L  82  ? 1.0476 1.0238 1.1319 -0.0288 -0.0452 -0.0046 82  LYS L CE  
22202 N NZ  . LYS L  82  ? 0.8939 0.8754 0.9776 -0.0312 -0.0521 -0.0022 82  LYS L NZ  
22203 N N   . LYS L  83  ? 0.5814 0.5537 0.6480 -0.0073 -0.0325 -0.0025 83  LYS L N   
22204 C CA  . LYS L  83  ? 0.5621 0.5337 0.6203 -0.0094 -0.0324 -0.0052 83  LYS L CA  
22205 C C   . LYS L  83  ? 0.5238 0.4988 0.5770 -0.0077 -0.0352 -0.0039 83  LYS L C   
22206 O O   . LYS L  83  ? 0.4992 0.4757 0.5466 -0.0113 -0.0386 -0.0053 83  LYS L O   
22207 C CB  . LYS L  83  ? 0.3889 0.3561 0.4450 -0.0069 -0.0258 -0.0073 83  LYS L CB  
22208 C CG  . LYS L  83  ? 0.5172 0.4836 0.5649 -0.0088 -0.0252 -0.0101 83  LYS L CG  
22209 C CD  . LYS L  83  ? 0.5083 0.4698 0.5548 -0.0075 -0.0186 -0.0125 83  LYS L CD  
22210 C CE  . LYS L  83  ? 0.5258 0.4864 0.5734 -0.0005 -0.0137 -0.0103 83  LYS L CE  
22211 N NZ  . LYS L  83  ? 0.5978 0.5542 0.6432 0.0007  -0.0075 -0.0125 83  LYS L NZ  
22212 N N   . VAL L  84  ? 0.5083 0.4844 0.5633 -0.0022 -0.0337 -0.0012 84  VAL L N   
22213 C CA  . VAL L  84  ? 0.5061 0.4853 0.5565 -0.0003 -0.0359 0.0000  84  VAL L CA  
22214 C C   . VAL L  84  ? 0.4228 0.4058 0.4744 -0.0035 -0.0422 0.0016  84  VAL L C   
22215 O O   . VAL L  84  ? 0.5375 0.5230 0.5841 -0.0043 -0.0452 0.0016  84  VAL L O   
22216 C CB  . VAL L  84  ? 0.4002 0.3797 0.4522 0.0061  -0.0326 0.0024  84  VAL L CB  
22217 C CG1 . VAL L  84  ? 0.6152 0.5957 0.6749 0.0076  -0.0335 0.0053  84  VAL L CG1 
22218 C CG2 . VAL L  84  ? 0.6052 0.5876 0.6513 0.0077  -0.0342 0.0030  84  VAL L CG2 
22219 N N   . ASP L  85  ? 0.5203 0.5037 0.5788 -0.0052 -0.0441 0.0029  85  ASP L N   
22220 C CA  . ASP L  85  ? 0.4670 0.4542 0.5278 -0.0085 -0.0501 0.0048  85  ASP L CA  
22221 C C   . ASP L  85  ? 0.4476 0.4356 0.5040 -0.0147 -0.0540 0.0025  85  ASP L C   
22222 O O   . ASP L  85  ? 0.5412 0.5323 0.5944 -0.0170 -0.0585 0.0033  85  ASP L O   
22223 C CB  . ASP L  85  ? 0.4011 0.3887 0.4714 -0.0083 -0.0508 0.0071  85  ASP L CB  
22224 C CG  . ASP L  85  ? 0.6394 0.6274 0.7140 -0.0029 -0.0488 0.0100  85  ASP L CG  
22225 O OD1 . ASP L  85  ? 0.5947 0.5836 0.6648 0.0001  -0.0480 0.0104  85  ASP L OD1 
22226 O OD2 . ASP L  85  ? 0.7908 0.7784 0.8732 -0.0018 -0.0479 0.0117  85  ASP L OD2 
22227 N N   . ASP L  86  ? 0.4218 0.4069 0.4777 -0.0176 -0.0520 -0.0002 86  ASP L N   
22228 C CA  . ASP L  86  ? 0.4399 0.4255 0.4912 -0.0239 -0.0551 -0.0027 86  ASP L CA  
22229 C C   . ASP L  86  ? 0.5790 0.5641 0.6209 -0.0244 -0.0546 -0.0049 86  ASP L C   
22230 O O   . ASP L  86  ? 0.5039 0.4905 0.5407 -0.0293 -0.0584 -0.0063 86  ASP L O   
22231 C CB  . ASP L  86  ? 0.6457 0.6280 0.6991 -0.0269 -0.0524 -0.0053 86  ASP L CB  
22232 C CG  . ASP L  86  ? 0.9144 0.8981 0.9767 -0.0286 -0.0545 -0.0034 86  ASP L CG  
22233 O OD1 . ASP L  86  ? 0.9423 0.9299 1.0085 -0.0285 -0.0590 -0.0002 86  ASP L OD1 
22234 O OD2 . ASP L  86  ? 1.0321 1.0130 1.0976 -0.0299 -0.0516 -0.0052 86  ASP L OD2 
22235 N N   . GLY L  87  ? 0.5890 0.5721 0.6284 -0.0194 -0.0500 -0.0053 87  GLY L N   
22236 C CA  . GLY L  87  ? 0.4379 0.4208 0.4691 -0.0192 -0.0491 -0.0071 87  GLY L CA  
22237 C C   . GLY L  87  ? 0.4149 0.4017 0.4432 -0.0192 -0.0538 -0.0052 87  GLY L C   
22238 O O   . GLY L  87  ? 0.4392 0.4272 0.4614 -0.0230 -0.0567 -0.0066 87  GLY L O   
22239 N N   . PHE L  88  ? 0.3971 0.3860 0.4297 -0.0150 -0.0542 -0.0020 88  PHE L N   
22240 C CA  . PHE L  88  ? 0.3739 0.3665 0.4048 -0.0147 -0.0582 0.0001  88  PHE L CA  
22241 C C   . PHE L  88  ? 0.4608 0.4560 0.4923 -0.0202 -0.0642 0.0008  88  PHE L C   
22242 O O   . PHE L  88  ? 0.6184 0.6160 0.6453 -0.0221 -0.0678 0.0012  88  PHE L O   
22243 C CB  . PHE L  88  ? 0.3395 0.3333 0.3759 -0.0097 -0.0573 0.0033  88  PHE L CB  
22244 C CG  . PHE L  88  ? 0.4447 0.4370 0.4796 -0.0042 -0.0521 0.0031  88  PHE L CG  
22245 C CD1 . PHE L  88  ? 0.4093 0.4015 0.4497 0.0003  -0.0497 0.0054  88  PHE L CD1 
22246 C CD2 . PHE L  88  ? 0.4339 0.4249 0.4619 -0.0037 -0.0496 0.0007  88  PHE L CD2 
22247 C CE1 . PHE L  88  ? 0.4221 0.4133 0.4608 0.0051  -0.0451 0.0054  88  PHE L CE1 
22248 C CE2 . PHE L  88  ? 0.4684 0.4586 0.4953 0.0013  -0.0450 0.0009  88  PHE L CE2 
22249 C CZ  . PHE L  88  ? 0.5070 0.4974 0.5391 0.0057  -0.0429 0.0032  88  PHE L CZ  
22250 N N   . LEU L  89  ? 0.5210 0.5158 0.5582 -0.0227 -0.0653 0.0012  89  LEU L N   
22251 C CA  . LEU L  89  ? 0.4503 0.4481 0.4889 -0.0282 -0.0711 0.0022  89  LEU L CA  
22252 C C   . LEU L  89  ? 0.4617 0.4593 0.4919 -0.0334 -0.0730 -0.0008 89  LEU L C   
22253 O O   . LEU L  89  ? 0.4556 0.4563 0.4832 -0.0368 -0.0780 0.0003  89  LEU L O   
22254 C CB  . LEU L  89  ? 0.4653 0.4627 0.5116 -0.0300 -0.0713 0.0029  89  LEU L CB  
22255 C CG  . LEU L  89  ? 0.4825 0.4832 0.5307 -0.0361 -0.0773 0.0038  89  LEU L CG  
22256 C CD1 . LEU L  89  ? 0.5354 0.5405 0.5845 -0.0361 -0.0823 0.0074  89  LEU L CD1 
22257 C CD2 . LEU L  89  ? 0.4445 0.4452 0.5015 -0.0371 -0.0772 0.0048  89  LEU L CD2 
22258 N N   . ASP L  90  ? 0.4374 0.4313 0.4636 -0.0341 -0.0689 -0.0044 90  ASP L N   
22259 C CA  . ASP L  90  ? 0.4354 0.4284 0.4535 -0.0393 -0.0699 -0.0077 90  ASP L CA  
22260 C C   . ASP L  90  ? 0.4222 0.4160 0.4327 -0.0382 -0.0703 -0.0082 90  ASP L C   
22261 O O   . ASP L  90  ? 0.5231 0.5183 0.5277 -0.0427 -0.0738 -0.0092 90  ASP L O   
22262 C CB  . ASP L  90  ? 0.5032 0.4914 0.5196 -0.0402 -0.0647 -0.0116 90  ASP L CB  
22263 C CG  . ASP L  90  ? 0.7013 0.6890 0.7230 -0.0439 -0.0654 -0.0121 90  ASP L CG  
22264 O OD1 . ASP L  90  ? 0.8964 0.8878 0.9214 -0.0472 -0.0708 -0.0100 90  ASP L OD1 
22265 O OD2 . ASP L  90  ? 0.8551 0.8388 0.8779 -0.0436 -0.0605 -0.0146 90  ASP L OD2 
22266 N N   . ILE L  91  ? 0.4816 0.4746 0.4922 -0.0323 -0.0667 -0.0075 91  ILE L N   
22267 C CA  . ILE L  91  ? 0.5597 0.5536 0.5637 -0.0308 -0.0668 -0.0078 91  ILE L CA  
22268 C C   . ILE L  91  ? 0.5022 0.5004 0.5061 -0.0321 -0.0725 -0.0050 91  ILE L C   
22269 O O   . ILE L  91  ? 0.4569 0.4562 0.4544 -0.0353 -0.0753 -0.0059 91  ILE L O   
22270 C CB  . ILE L  91  ? 0.4937 0.4867 0.4987 -0.0241 -0.0621 -0.0072 91  ILE L CB  
22271 C CG1 . ILE L  91  ? 0.3992 0.3879 0.4035 -0.0226 -0.0561 -0.0099 91  ILE L CG1 
22272 C CG2 . ILE L  91  ? 0.4777 0.4724 0.4766 -0.0227 -0.0628 -0.0071 91  ILE L CG2 
22273 C CD1 . ILE L  91  ? 0.6270 0.6150 0.6325 -0.0161 -0.0515 -0.0089 91  ILE L CD1 
22274 N N   . TRP L  92  ? 0.3798 0.3800 0.3909 -0.0296 -0.0740 -0.0015 92  TRP L N   
22275 C CA  . TRP L  92  ? 0.3071 0.3112 0.3194 -0.0301 -0.0788 0.0016  92  TRP L CA  
22276 C C   . TRP L  92  ? 0.5213 0.5277 0.5326 -0.0363 -0.0844 0.0021  92  TRP L C   
22277 O O   . TRP L  92  ? 0.5396 0.5485 0.5472 -0.0382 -0.0881 0.0032  92  TRP L O   
22278 C CB  . TRP L  92  ? 0.3850 0.3903 0.4059 -0.0260 -0.0785 0.0051  92  TRP L CB  
22279 C CG  . TRP L  92  ? 0.4178 0.4222 0.4381 -0.0202 -0.0745 0.0053  92  TRP L CG  
22280 C CD1 . TRP L  92  ? 0.3704 0.3728 0.3946 -0.0158 -0.0699 0.0053  92  TRP L CD1 
22281 C CD2 . TRP L  92  ? 0.4584 0.4642 0.4737 -0.0183 -0.0746 0.0054  92  TRP L CD2 
22282 N NE1 . TRP L  92  ? 0.5819 0.5846 0.6037 -0.0114 -0.0673 0.0056  92  TRP L NE1 
22283 C CE2 . TRP L  92  ? 0.4384 0.4432 0.4548 -0.0129 -0.0702 0.0056  92  TRP L CE2 
22284 C CE3 . TRP L  92  ? 0.4565 0.4644 0.4663 -0.0209 -0.0781 0.0055  92  TRP L CE3 
22285 C CZ2 . TRP L  92  ? 0.4496 0.4556 0.4621 -0.0101 -0.0692 0.0057  92  TRP L CZ2 
22286 C CZ3 . TRP L  92  ? 0.5499 0.5587 0.5560 -0.0179 -0.0770 0.0056  92  TRP L CZ3 
22287 C CH2 . TRP L  92  ? 0.5094 0.5173 0.5168 -0.0127 -0.0726 0.0056  92  TRP L CH2 
22288 N N   . THR L  93  ? 0.5881 0.5939 0.6027 -0.0396 -0.0851 0.0015  93  THR L N   
22289 C CA  . THR L  93  ? 0.4583 0.4666 0.4718 -0.0460 -0.0904 0.0019  93  THR L CA  
22290 C C   . THR L  93  ? 0.4615 0.4690 0.4647 -0.0500 -0.0913 -0.0012 93  THR L C   
22291 O O   . THR L  93  ? 0.4751 0.4856 0.4750 -0.0531 -0.0959 0.0002  93  THR L O   
22292 C CB  . THR L  93  ? 0.4771 0.4845 0.4953 -0.0491 -0.0904 0.0010  93  THR L CB  
22293 O OG1 . THR L  93  ? 0.5422 0.5506 0.5703 -0.0458 -0.0901 0.0042  93  THR L OG1 
22294 C CG2 . THR L  93  ? 0.4753 0.4856 0.4912 -0.0562 -0.0960 0.0011  93  THR L CG2 
22295 N N   . TYR L  94  ? 0.4760 0.4796 0.4744 -0.0498 -0.0866 -0.0052 94  TYR L N   
22296 C CA  . TYR L  94  ? 0.4522 0.4545 0.4408 -0.0535 -0.0865 -0.0086 94  TYR L CA  
22297 C C   . TYR L  94  ? 0.5465 0.5502 0.5300 -0.0517 -0.0876 -0.0076 94  TYR L C   
22298 O O   . TYR L  94  ? 0.5781 0.5835 0.5557 -0.0559 -0.0912 -0.0079 94  TYR L O   
22299 C CB  . TYR L  94  ? 0.4163 0.4137 0.4019 -0.0527 -0.0803 -0.0128 94  TYR L CB  
22300 C CG  . TYR L  94  ? 0.5663 0.5616 0.5422 -0.0573 -0.0797 -0.0167 94  TYR L CG  
22301 C CD1 . TYR L  94  ? 0.6009 0.5962 0.5738 -0.0642 -0.0823 -0.0186 94  TYR L CD1 
22302 C CD2 . TYR L  94  ? 0.5941 0.5877 0.5640 -0.0548 -0.0766 -0.0184 94  TYR L CD2 
22303 C CE1 . TYR L  94  ? 0.6475 0.6408 0.6113 -0.0687 -0.0815 -0.0224 94  TYR L CE1 
22304 C CE2 . TYR L  94  ? 0.6448 0.6365 0.6062 -0.0590 -0.0757 -0.0220 94  TYR L CE2 
22305 C CZ  . TYR L  94  ? 0.7419 0.7332 0.7000 -0.0659 -0.0781 -0.0241 94  TYR L CZ  
22306 O OH  . TYR L  94  ? 0.6936 0.6826 0.6428 -0.0703 -0.0770 -0.0278 94  TYR L OH  
22307 N N   . ASN L  95  ? 0.5554 0.5588 0.5412 -0.0455 -0.0845 -0.0065 95  ASN L N   
22308 C CA  . ASN L  95  ? 0.5177 0.5225 0.4990 -0.0434 -0.0851 -0.0057 95  ASN L CA  
22309 C C   . ASN L  95  ? 0.6109 0.6199 0.5938 -0.0451 -0.0909 -0.0021 95  ASN L C   
22310 O O   . ASN L  95  ? 0.5931 0.6033 0.5699 -0.0472 -0.0933 -0.0023 95  ASN L O   
22311 C CB  . ASN L  95  ? 0.5157 0.5197 0.4997 -0.0366 -0.0807 -0.0051 95  ASN L CB  
22312 C CG  . ASN L  95  ? 0.6840 0.6842 0.6648 -0.0347 -0.0749 -0.0085 95  ASN L CG  
22313 O OD1 . ASN L  95  ? 0.6401 0.6377 0.6182 -0.0381 -0.0736 -0.0114 95  ASN L OD1 
22314 N ND2 . ASN L  95  ? 0.6780 0.6779 0.6591 -0.0292 -0.0713 -0.0082 95  ASN L ND2 
22315 N N   . ALA L  96  ? 0.5189 0.5298 0.5100 -0.0442 -0.0930 0.0012  96  ALA L N   
22316 C CA  . ALA L  96  ? 0.5124 0.5273 0.5065 -0.0454 -0.0983 0.0052  96  ALA L CA  
22317 C C   . ALA L  96  ? 0.5283 0.5451 0.5179 -0.0522 -0.1032 0.0050  96  ALA L C   
22318 O O   . ALA L  96  ? 0.5827 0.6019 0.5691 -0.0538 -0.1068 0.0067  96  ALA L O   
22319 C CB  . ALA L  96  ? 0.5568 0.5732 0.5613 -0.0432 -0.0991 0.0086  96  ALA L CB  
22320 N N   . GLU L  97  ? 0.4278 0.4434 0.4170 -0.0561 -0.1033 0.0030  97  GLU L N   
22321 C CA  . GLU L  97  ? 0.5578 0.5753 0.5423 -0.0630 -0.1079 0.0025  97  GLU L CA  
22322 C C   . GLU L  97  ? 0.6024 0.6188 0.5763 -0.0653 -0.1076 -0.0003 97  GLU L C   
22323 O O   . GLU L  97  ? 0.6424 0.6615 0.6123 -0.0689 -0.1122 0.0012  97  GLU L O   
22324 C CB  . GLU L  97  ? 0.6492 0.6651 0.6348 -0.0668 -0.1071 0.0000  97  GLU L CB  
22325 C CG  . GLU L  97  ? 0.5626 0.5803 0.5588 -0.0660 -0.1083 0.0029  97  GLU L CG  
22326 C CD  . GLU L  97  ? 0.7317 0.7546 0.7314 -0.0699 -0.1151 0.0070  97  GLU L CD  
22327 O OE1 . GLU L  97  ? 0.7721 0.7968 0.7795 -0.0710 -0.1168 0.0089  97  GLU L OE1 
22328 O OE2 . GLU L  97  ? 0.9908 1.0161 0.9857 -0.0721 -0.1188 0.0084  97  GLU L OE2 
22329 N N   . LEU L  98  ? 0.5285 0.5408 0.4978 -0.0631 -0.1022 -0.0042 98  LEU L N   
22330 C CA  . LEU L  98  ? 0.4967 0.5075 0.4562 -0.0648 -0.1012 -0.0071 98  LEU L CA  
22331 C C   . LEU L  98  ? 0.5671 0.5800 0.5250 -0.0620 -0.1026 -0.0047 98  LEU L C   
22332 O O   . LEU L  98  ? 0.5269 0.5406 0.4777 -0.0651 -0.1048 -0.0052 98  LEU L O   
22333 C CB  . LEU L  98  ? 0.4989 0.5050 0.4553 -0.0625 -0.0946 -0.0114 98  LEU L CB  
22334 C CG  . LEU L  98  ? 0.6216 0.6245 0.5734 -0.0674 -0.0927 -0.0156 98  LEU L CG  
22335 C CD1 . LEU L  98  ? 0.8339 0.8363 0.7755 -0.0724 -0.0940 -0.0181 98  LEU L CD1 
22336 C CD2 . LEU L  98  ? 0.6908 0.6951 0.6476 -0.0713 -0.0957 -0.0147 98  LEU L CD2 
22337 N N   . LEU L  99  ? 0.6231 0.6367 0.5873 -0.0562 -0.1011 -0.0023 99  LEU L N   
22338 C CA  . LEU L  99  ? 0.6651 0.6805 0.6284 -0.0532 -0.1020 -0.0001 99  LEU L CA  
22339 C C   . LEU L  99  ? 0.5567 0.5758 0.5196 -0.0570 -0.1080 0.0031  99  LEU L C   
22340 O O   . LEU L  99  ? 0.5323 0.5522 0.4894 -0.0580 -0.1094 0.0032  99  LEU L O   
22341 C CB  . LEU L  99  ? 0.6180 0.6338 0.5891 -0.0470 -0.0996 0.0022  99  LEU L CB  
22342 C CG  . LEU L  99  ? 0.6270 0.6445 0.5976 -0.0438 -0.1001 0.0042  99  LEU L CG  
22343 C CD1 . LEU L  99  ? 0.6145 0.6304 0.5771 -0.0429 -0.0971 0.0011  99  LEU L CD1 
22344 C CD2 . LEU L  99  ? 0.7086 0.7266 0.6873 -0.0384 -0.0980 0.0066  99  LEU L CD2 
22345 N N   . VAL L  100 ? 0.4824 0.5038 0.4518 -0.0589 -0.1116 0.0061  100 VAL L N   
22346 C CA  . VAL L  100 ? 0.6430 0.6684 0.6130 -0.0625 -0.1175 0.0098  100 VAL L CA  
22347 C C   . VAL L  100 ? 0.5202 0.5458 0.4809 -0.0687 -0.1202 0.0077  100 VAL L C   
22348 O O   . VAL L  100 ? 0.6138 0.6413 0.5702 -0.0703 -0.1230 0.0092  100 VAL L O   
22349 C CB  . VAL L  100 ? 0.5630 0.5910 0.5422 -0.0636 -0.1207 0.0133  100 VAL L CB  
22350 C CG1 . VAL L  100 ? 0.4886 0.5210 0.4676 -0.0683 -0.1272 0.0169  100 VAL L CG1 
22351 C CG2 . VAL L  100 ? 0.6049 0.6332 0.5936 -0.0576 -0.1187 0.0160  100 VAL L CG2 
22352 N N   . LEU L  101 ? 0.4957 0.5192 0.4530 -0.0723 -0.1190 0.0042  101 LEU L N   
22353 C CA  . LEU L  101 ? 0.5703 0.5935 0.5181 -0.0786 -0.1209 0.0017  101 LEU L CA  
22354 C C   . LEU L  101 ? 0.6149 0.6364 0.5543 -0.0777 -0.1189 -0.0005 101 LEU L C   
22355 O O   . LEU L  101 ? 0.6920 0.7154 0.6260 -0.0810 -0.1224 0.0006  101 LEU L O   
22356 C CB  . LEU L  101 ? 0.5231 0.5433 0.4684 -0.0818 -0.1183 -0.0027 101 LEU L CB  
22357 C CG  . LEU L  101 ? 0.5581 0.5799 0.5105 -0.0840 -0.1204 -0.0014 101 LEU L CG  
22358 C CD1 . LEU L  101 ? 0.6014 0.6199 0.5494 -0.0882 -0.1177 -0.0063 101 LEU L CD1 
22359 C CD2 . LEU L  101 ? 0.5121 0.5392 0.4668 -0.0881 -0.1274 0.0031  101 LEU L CD2 
22360 N N   . LEU L  102 ? 0.5845 0.6025 0.5231 -0.0732 -0.1132 -0.0033 102 LEU L N   
22361 C CA  . LEU L  102 ? 0.5364 0.5527 0.4676 -0.0719 -0.1107 -0.0056 102 LEU L CA  
22362 C C   . LEU L  102 ? 0.5966 0.6159 0.5282 -0.0702 -0.1136 -0.0020 102 LEU L C   
22363 O O   . LEU L  102 ? 0.5187 0.5382 0.4430 -0.0727 -0.1149 -0.0026 102 LEU L O   
22364 C CB  . LEU L  102 ? 0.6406 0.6536 0.5731 -0.0665 -0.1043 -0.0083 102 LEU L CB  
22365 C CG  . LEU L  102 ? 0.8356 0.8444 0.7622 -0.0682 -0.0998 -0.0134 102 LEU L CG  
22366 C CD1 . LEU L  102 ? 0.7453 0.7534 0.6702 -0.0744 -0.1017 -0.0150 102 LEU L CD1 
22367 C CD2 . LEU L  102 ? 1.1297 1.1360 1.0605 -0.0625 -0.0940 -0.0148 102 LEU L CD2 
22368 N N   . GLU L  103 ? 0.5504 0.5716 0.4905 -0.0659 -0.1142 0.0017  103 GLU L N   
22369 C CA  . GLU L  103 ? 0.5445 0.5682 0.4859 -0.0638 -0.1163 0.0051  103 GLU L CA  
22370 C C   . GLU L  103 ? 0.6007 0.6278 0.5408 -0.0686 -0.1224 0.0084  103 GLU L C   
22371 O O   . GLU L  103 ? 0.6661 0.6943 0.6023 -0.0691 -0.1239 0.0096  103 GLU L O   
22372 C CB  . GLU L  103 ? 0.5113 0.5359 0.4623 -0.0582 -0.1150 0.0080  103 GLU L CB  
22373 C CG  . GLU L  103 ? 0.7477 0.7697 0.6990 -0.0528 -0.1093 0.0054  103 GLU L CG  
22374 C CD  . GLU L  103 ? 1.0008 1.0217 0.9439 -0.0524 -0.1072 0.0029  103 GLU L CD  
22375 O OE1 . GLU L  103 ? 0.9437 0.9662 0.8865 -0.0509 -0.1082 0.0048  103 GLU L OE1 
22376 O OE2 . GLU L  103 ? 1.0476 1.0660 0.9850 -0.0535 -0.1043 -0.0011 103 GLU L OE2 
22377 N N   . ASN L  104 ? 0.5771 0.6059 0.5205 -0.0722 -0.1258 0.0100  104 ASN L N   
22378 C CA  . ASN L  104 ? 0.5913 0.6238 0.5335 -0.0771 -0.1318 0.0134  104 ASN L CA  
22379 C C   . ASN L  104 ? 0.6629 0.6946 0.5937 -0.0820 -0.1327 0.0107  104 ASN L C   
22380 O O   . ASN L  104 ? 0.5989 0.6330 0.5268 -0.0841 -0.1363 0.0133  104 ASN L O   
22381 C CB  . ASN L  104 ? 0.4355 0.4702 0.3830 -0.0805 -0.1350 0.0150  104 ASN L CB  
22382 C CG  . ASN L  104 ? 0.5076 0.5444 0.4670 -0.0765 -0.1357 0.0193  104 ASN L CG  
22383 O OD1 . ASN L  104 ? 0.5653 0.6023 0.5289 -0.0717 -0.1343 0.0215  104 ASN L OD1 
22384 N ND2 . ASN L  104 ? 0.6069 0.6453 0.5719 -0.0786 -0.1377 0.0204  104 ASN L ND2 
22385 N N   . GLU L  105 ? 0.4857 0.5139 0.4103 -0.0837 -0.1293 0.0055  105 GLU L N   
22386 C CA  . GLU L  105 ? 0.6730 0.6996 0.5865 -0.0881 -0.1292 0.0024  105 GLU L CA  
22387 C C   . GLU L  105 ? 0.7372 0.7633 0.6470 -0.0851 -0.1277 0.0025  105 GLU L C   
22388 O O   . GLU L  105 ? 0.8273 0.8543 0.7303 -0.0885 -0.1302 0.0029  105 GLU L O   
22389 C CB  . GLU L  105 ? 0.7753 0.7976 0.6839 -0.0896 -0.1246 -0.0034 105 GLU L CB  
22390 C CG  . GLU L  105 ? 0.8612 0.8815 0.7583 -0.0943 -0.1240 -0.0071 105 GLU L CG  
22391 C CD  . GLU L  105 ? 1.3226 1.3460 1.2151 -0.1011 -0.1300 -0.0050 105 GLU L CD  
22392 O OE1 . GLU L  105 ? 1.2789 1.3051 1.1759 -0.1038 -0.1338 -0.0027 105 GLU L OE1 
22393 O OE2 . GLU L  105 ? 1.3181 1.3414 1.2025 -0.1037 -0.1311 -0.0056 105 GLU L OE2 
22394 N N   . ARG L  106 ? 0.7095 0.7341 0.6236 -0.0788 -0.1236 0.0021  106 ARG L N   
22395 C CA  . ARG L  106 ? 0.6768 0.7011 0.5882 -0.0756 -0.1218 0.0020  106 ARG L CA  
22396 C C   . ARG L  106 ? 0.7215 0.7493 0.6361 -0.0752 -0.1260 0.0071  106 ARG L C   
22397 O O   . ARG L  106 ? 0.7399 0.7680 0.6494 -0.0757 -0.1265 0.0074  106 ARG L O   
22398 C CB  . ARG L  106 ? 0.6934 0.7157 0.6088 -0.0692 -0.1164 0.0004  106 ARG L CB  
22399 C CG  . ARG L  106 ? 0.7109 0.7294 0.6225 -0.0690 -0.1115 -0.0046 106 ARG L CG  
22400 C CD  . ARG L  106 ? 0.9468 0.9640 0.8607 -0.0628 -0.1065 -0.0060 106 ARG L CD  
22401 N NE  . ARG L  106 ? 1.0345 1.0526 0.9451 -0.0611 -0.1063 -0.0054 106 ARG L NE  
22402 C CZ  . ARG L  106 ? 1.1149 1.1316 1.0172 -0.0631 -0.1051 -0.0081 106 ARG L CZ  
22403 N NH1 . ARG L  106 ? 1.0321 1.0463 0.9284 -0.0669 -0.1038 -0.0116 106 ARG L NH1 
22404 N NH2 . ARG L  106 ? 1.1231 1.1409 1.0231 -0.0615 -0.1050 -0.0074 106 ARG L NH2 
22405 N N   . THR L  107 ? 0.6331 0.6635 0.5566 -0.0742 -0.1287 0.0112  107 THR L N   
22406 C CA  . THR L  107 ? 0.6702 0.7039 0.5982 -0.0735 -0.1324 0.0165  107 THR L CA  
22407 C C   . THR L  107 ? 0.7582 0.7942 0.6803 -0.0793 -0.1374 0.0184  107 THR L C   
22408 O O   . THR L  107 ? 0.6833 0.7205 0.6037 -0.0791 -0.1389 0.0208  107 THR L O   
22409 C CB  . THR L  107 ? 0.6865 0.7224 0.6257 -0.0714 -0.1341 0.0205  107 THR L CB  
22410 O OG1 . THR L  107 ? 0.7140 0.7479 0.6586 -0.0659 -0.1294 0.0190  107 THR L OG1 
22411 C CG2 . THR L  107 ? 0.5971 0.6363 0.5413 -0.0708 -0.1377 0.0261  107 THR L CG2 
22412 N N   . LEU L  108 ? 0.7861 0.8225 0.7048 -0.0845 -0.1398 0.0173  108 LEU L N   
22413 C CA  . LEU L  108 ? 0.6389 0.6777 0.5513 -0.0906 -0.1446 0.0189  108 LEU L CA  
22414 C C   . LEU L  108 ? 0.6051 0.6414 0.5066 -0.0923 -0.1427 0.0155  108 LEU L C   
22415 O O   . LEU L  108 ? 0.7202 0.7584 0.6178 -0.0945 -0.1457 0.0180  108 LEU L O   
22416 C CB  . LEU L  108 ? 0.6045 0.6442 0.5153 -0.0962 -0.1472 0.0179  108 LEU L CB  
22417 C CG  . LEU L  108 ? 0.5687 0.6115 0.4902 -0.0955 -0.1498 0.0216  108 LEU L CG  
22418 C CD1 . LEU L  108 ? 0.5129 0.5570 0.4318 -0.1018 -0.1529 0.0206  108 LEU L CD1 
22419 C CD2 . LEU L  108 ? 0.6359 0.6829 0.5644 -0.0940 -0.1540 0.0283  108 LEU L CD2 
22420 N N   . ASP L  109 ? 0.6190 0.6513 0.5160 -0.0910 -0.1376 0.0101  109 ASP L N   
22421 C CA  . ASP L  109 ? 0.7172 0.7469 0.6046 -0.0921 -0.1351 0.0065  109 ASP L CA  
22422 C C   . ASP L  109 ? 0.7331 0.7632 0.6219 -0.0877 -0.1340 0.0085  109 ASP L C   
22423 O O   . ASP L  109 ? 0.6485 0.6782 0.5303 -0.0894 -0.1342 0.0078  109 ASP L O   
22424 C CB  . ASP L  109 ? 0.8061 0.8314 0.6899 -0.0910 -0.1294 0.0006  109 ASP L CB  
22425 C CG  . ASP L  109 ? 1.0808 1.1049 0.9601 -0.0966 -0.1300 -0.0023 109 ASP L CG  
22426 O OD1 . ASP L  109 ? 1.1023 1.1290 0.9794 -0.1020 -0.1350 -0.0002 109 ASP L OD1 
22427 O OD2 . ASP L  109 ? 1.0733 1.0939 0.9515 -0.0957 -0.1254 -0.0067 109 ASP L OD2 
22428 N N   . TYR L  110 ? 0.7489 0.7799 0.6469 -0.0822 -0.1328 0.0107  110 TYR L N   
22429 C CA  . TYR L  110 ? 0.5899 0.6215 0.4903 -0.0780 -0.1317 0.0127  110 TYR L CA  
22430 C C   . TYR L  110 ? 0.7893 0.8239 0.6896 -0.0805 -0.1365 0.0175  110 TYR L C   
22431 O O   . TYR L  110 ? 0.6262 0.6606 0.5220 -0.0804 -0.1362 0.0177  110 TYR L O   
22432 C CB  . TYR L  110 ? 0.4903 0.5220 0.4007 -0.0721 -0.1294 0.0141  110 TYR L CB  
22433 C CG  . TYR L  110 ? 0.5921 0.6248 0.5061 -0.0682 -0.1287 0.0167  110 TYR L CG  
22434 C CD1 . TYR L  110 ? 0.5136 0.5444 0.4244 -0.0650 -0.1244 0.0138  110 TYR L CD1 
22435 C CD2 . TYR L  110 ? 0.6166 0.6521 0.5374 -0.0678 -0.1321 0.0221  110 TYR L CD2 
22436 C CE1 . TYR L  110 ? 0.5318 0.5635 0.4458 -0.0617 -0.1236 0.0158  110 TYR L CE1 
22437 C CE2 . TYR L  110 ? 0.6728 0.7088 0.5969 -0.0643 -0.1310 0.0242  110 TYR L CE2 
22438 C CZ  . TYR L  110 ? 0.6662 0.7003 0.5867 -0.0614 -0.1268 0.0210  110 TYR L CZ  
22439 O OH  . TYR L  110 ? 0.7308 0.7653 0.6544 -0.0584 -0.1256 0.0229  110 TYR L OH  
22440 N N   . HIS L  111 ? 0.7289 0.7665 0.6346 -0.0826 -0.1410 0.0217  111 HIS L N   
22441 C CA  . HIS L  111 ? 0.5857 0.6267 0.4920 -0.0851 -0.1459 0.0269  111 HIS L CA  
22442 C C   . HIS L  111 ? 0.7260 0.7669 0.6213 -0.0909 -0.1481 0.0256  111 HIS L C   
22443 O O   . HIS L  111 ? 0.6571 0.6987 0.5490 -0.0916 -0.1496 0.0277  111 HIS L O   
22444 C CB  . HIS L  111 ? 0.5813 0.6259 0.4960 -0.0863 -0.1503 0.0316  111 HIS L CB  
22445 C CG  . HIS L  111 ? 0.5273 0.5724 0.4535 -0.0808 -0.1487 0.0342  111 HIS L CG  
22446 N ND1 . HIS L  111 ? 0.6697 0.7155 0.6010 -0.0770 -0.1481 0.0376  111 HIS L ND1 
22447 C CD2 . HIS L  111 ? 0.6675 0.7124 0.6011 -0.0785 -0.1474 0.0339  111 HIS L CD2 
22448 C CE1 . HIS L  111 ? 0.7052 0.7511 0.6464 -0.0727 -0.1465 0.0391  111 HIS L CE1 
22449 N NE2 . HIS L  111 ? 0.7443 0.7898 0.6870 -0.0734 -0.1460 0.0370  111 HIS L NE2 
22450 N N   . ASP L  112 ? 0.6507 0.6904 0.5402 -0.0950 -0.1482 0.0220  112 ASP L N   
22451 C CA  . ASP L  112 ? 0.6335 0.6726 0.5117 -0.1009 -0.1497 0.0199  112 ASP L CA  
22452 C C   . ASP L  112 ? 0.6175 0.6538 0.4891 -0.0992 -0.1463 0.0173  112 ASP L C   
22453 O O   . ASP L  112 ? 0.7688 0.8058 0.6337 -0.1025 -0.1483 0.0183  112 ASP L O   
22454 C CB  . ASP L  112 ? 0.7601 0.7970 0.6334 -0.1046 -0.1484 0.0150  112 ASP L CB  
22455 C CG  . ASP L  112 ? 0.8591 0.8957 0.7209 -0.1116 -0.1505 0.0132  112 ASP L CG  
22456 O OD1 . ASP L  112 ? 0.9852 1.0189 0.8410 -0.1145 -0.1481 0.0082  112 ASP L OD1 
22457 O OD2 . ASP L  112 ? 1.0683 1.1076 0.9273 -0.1142 -0.1545 0.0169  112 ASP L OD2 
22458 N N   . SER L  113 ? 0.8238 0.8573 0.6975 -0.0942 -0.1409 0.0140  113 SER L N   
22459 C CA  . SER L  113 ? 0.7079 0.7390 0.5763 -0.0922 -0.1372 0.0111  113 SER L CA  
22460 C C   . SER L  113 ? 0.8015 0.8345 0.6717 -0.0905 -0.1388 0.0153  113 SER L C   
22461 O O   . SER L  113 ? 0.7187 0.7509 0.5817 -0.0924 -0.1388 0.0146  113 SER L O   
22462 C CB  . SER L  113 ? 0.6535 0.6820 0.5254 -0.0867 -0.1315 0.0075  113 SER L CB  
22463 O OG  . SER L  113 ? 0.8792 0.9062 0.7476 -0.0841 -0.1281 0.0056  113 SER L OG  
22464 N N   . ASN L  114 ? 0.7968 0.8320 0.6768 -0.0869 -0.1401 0.0196  114 ASN L N   
22465 C CA  . ASN L  114 ? 0.7564 0.7932 0.6395 -0.0849 -0.1412 0.0236  114 ASN L CA  
22466 C C   . ASN L  114 ? 0.8045 0.8434 0.6828 -0.0898 -0.1460 0.0272  114 ASN L C   
22467 O O   . ASN L  114 ? 0.7914 0.8303 0.6668 -0.0896 -0.1459 0.0285  114 ASN L O   
22468 C CB  . ASN L  114 ? 0.7617 0.8003 0.6567 -0.0805 -0.1416 0.0277  114 ASN L CB  
22469 C CG  . ASN L  114 ? 0.8159 0.8525 0.7155 -0.0752 -0.1366 0.0244  114 ASN L CG  
22470 O OD1 . ASN L  114 ? 0.8918 0.9258 0.7861 -0.0739 -0.1326 0.0198  114 ASN L OD1 
22471 N ND2 . ASN L  114 ? 0.8040 0.8417 0.7134 -0.0721 -0.1367 0.0270  114 ASN L ND2 
22472 N N   . VAL L  115 ? 0.7493 0.7903 0.6268 -0.0943 -0.1502 0.0289  115 VAL L N   
22473 C CA  . VAL L  115 ? 0.6865 0.7299 0.5587 -0.0996 -0.1551 0.0323  115 VAL L CA  
22474 C C   . VAL L  115 ? 0.7624 0.8032 0.6223 -0.1029 -0.1534 0.0281  115 VAL L C   
22475 O O   . VAL L  115 ? 0.8372 0.8783 0.6932 -0.1038 -0.1543 0.0300  115 VAL L O   
22476 C CB  . VAL L  115 ? 0.7429 0.7892 0.6158 -0.1043 -0.1598 0.0343  115 VAL L CB  
22477 C CG1 . VAL L  115 ? 0.8804 0.9291 0.7459 -0.1104 -0.1647 0.0371  115 VAL L CG1 
22478 C CG2 . VAL L  115 ? 0.5808 0.6303 0.4664 -0.1013 -0.1619 0.0392  115 VAL L CG2 
22479 N N   . LYS L  116 ? 0.6751 0.7130 0.5291 -0.1047 -0.1507 0.0224  116 LYS L N   
22480 C CA  . LYS L  116 ? 0.7770 0.8119 0.6197 -0.1077 -0.1483 0.0178  116 LYS L CA  
22481 C C   . LYS L  116 ? 0.8032 0.8364 0.6447 -0.1040 -0.1450 0.0171  116 LYS L C   
22482 O O   . LYS L  116 ? 0.9044 0.9370 0.7381 -0.1068 -0.1453 0.0167  116 LYS L O   
22483 C CB  . LYS L  116 ? 0.7381 0.7697 0.5775 -0.1081 -0.1443 0.0116  116 LYS L CB  
22484 C CG  . LYS L  116 ? 0.7584 0.7861 0.5876 -0.1097 -0.1403 0.0062  116 LYS L CG  
22485 C CD  . LYS L  116 ? 0.9721 0.9992 0.7911 -0.1170 -0.1424 0.0044  116 LYS L CD  
22486 C CE  . LYS L  116 ? 1.1489 1.1715 0.9586 -0.1183 -0.1374 -0.0017 116 LYS L CE  
22487 N NZ  . LYS L  116 ? 1.4575 1.4789 1.2573 -0.1256 -0.1387 -0.0044 116 LYS L NZ  
22488 N N   . ASN L  117 ? 0.7403 0.7731 0.5896 -0.0979 -0.1418 0.0169  117 ASN L N   
22489 C CA  . ASN L  117 ? 0.7969 0.8283 0.6460 -0.0941 -0.1384 0.0161  117 ASN L CA  
22490 C C   . ASN L  117 ? 0.8668 0.9005 0.7174 -0.0945 -0.1415 0.0214  117 ASN L C   
22491 O O   . ASN L  117 ? 0.9527 0.9852 0.7982 -0.0946 -0.1401 0.0207  117 ASN L O   
22492 C CB  . ASN L  117 ? 0.8001 0.8309 0.6574 -0.0878 -0.1345 0.0149  117 ASN L CB  
22493 C CG  . ASN L  117 ? 0.8207 0.8487 0.6753 -0.0867 -0.1301 0.0091  117 ASN L CG  
22494 O OD1 . ASN L  117 ? 0.9100 0.9360 0.7562 -0.0904 -0.1292 0.0055  117 ASN L OD1 
22495 N ND2 . ASN L  117 ? 0.8993 0.9271 0.7611 -0.0817 -0.1271 0.0082  117 ASN L ND2 
22496 N N   . LEU L  118 ? 0.8251 0.8619 0.6828 -0.0946 -0.1456 0.0269  118 LEU L N   
22497 C CA  . LEU L  118 ? 0.8751 0.9142 0.7352 -0.0949 -0.1487 0.0326  118 LEU L CA  
22498 C C   . LEU L  118 ? 0.9065 0.9460 0.7565 -0.1007 -0.1516 0.0332  118 LEU L C   
22499 O O   . LEU L  118 ? 1.0437 1.0831 0.8909 -0.1009 -0.1516 0.0350  118 LEU L O   
22500 C CB  . LEU L  118 ? 0.8390 0.8817 0.7093 -0.0940 -0.1525 0.0384  118 LEU L CB  
22501 C CG  . LEU L  118 ? 0.8904 0.9346 0.7683 -0.0909 -0.1532 0.0439  118 LEU L CG  
22502 C CD1 . LEU L  118 ? 0.9876 1.0292 0.8681 -0.0856 -0.1478 0.0410  118 LEU L CD1 
22503 C CD2 . LEU L  118 ? 1.0088 1.0562 0.8975 -0.0897 -0.1564 0.0493  118 LEU L CD2 
22504 N N   . TYR L  119 ? 0.7993 0.8392 0.6438 -0.1055 -0.1539 0.0317  119 TYR L N   
22505 C CA  . TYR L  119 ? 0.8887 0.9287 0.7225 -0.1117 -0.1565 0.0316  119 TYR L CA  
22506 C C   . TYR L  119 ? 0.9209 0.9571 0.7459 -0.1118 -0.1522 0.0268  119 TYR L C   
22507 O O   . TYR L  119 ? 1.0914 1.1277 0.9109 -0.1138 -0.1532 0.0284  119 TYR L O   
22508 C CB  . TYR L  119 ? 0.9462 0.9868 0.7756 -0.1168 -0.1589 0.0297  119 TYR L CB  
22509 C CG  . TYR L  119 ? 1.0942 1.1347 0.9117 -0.1236 -0.1613 0.0289  119 TYR L CG  
22510 C CD1 . TYR L  119 ? 1.1546 1.1990 0.9709 -0.1279 -0.1672 0.0346  119 TYR L CD1 
22511 C CD2 . TYR L  119 ? 1.1290 1.1654 0.9364 -0.1258 -0.1575 0.0227  119 TYR L CD2 
22512 C CE1 . TYR L  119 ? 1.2336 1.2781 1.0386 -0.1344 -0.1695 0.0339  119 TYR L CE1 
22513 C CE2 . TYR L  119 ? 1.3216 1.3576 1.1177 -0.1322 -0.1594 0.0218  119 TYR L CE2 
22514 C CZ  . TYR L  119 ? 1.3166 1.3567 1.1113 -0.1366 -0.1654 0.0274  119 TYR L CZ  
22515 O OH  . TYR L  119 ? 1.3795 1.4194 1.1626 -0.1432 -0.1674 0.0265  119 TYR L OH  
22516 N N   . GLU L  120 ? 1.0495 1.0826 0.8734 -0.1095 -0.1473 0.0209  120 GLU L N   
22517 C CA  . GLU L  120 ? 1.0747 1.1043 0.8909 -0.1094 -0.1428 0.0159  120 GLU L CA  
22518 C C   . GLU L  120 ? 1.0296 1.0591 0.8481 -0.1056 -0.1410 0.0176  120 GLU L C   
22519 O O   . GLU L  120 ? 1.2451 1.2731 1.0563 -0.1075 -0.1399 0.0163  120 GLU L O   
22520 C CB  . GLU L  120 ? 1.1645 1.1912 0.9810 -0.1068 -0.1378 0.0100  120 GLU L CB  
22521 C CG  . GLU L  120 ? 1.3762 1.4012 1.1855 -0.1117 -0.1377 0.0060  120 GLU L CG  
22522 C CD  . GLU L  120 ? 1.6698 1.6924 1.4672 -0.1164 -0.1367 0.0031  120 GLU L CD  
22523 O OE1 . GLU L  120 ? 1.5850 1.6066 1.3801 -0.1146 -0.1345 0.0026  120 GLU L OE1 
22524 O OE2 . GLU L  120 ? 1.7725 1.7943 1.5629 -0.1219 -0.1380 0.0012  120 GLU L OE2 
22525 N N   . LYS L  121 ? 0.9883 1.0192 0.8171 -0.1006 -0.1406 0.0204  121 LYS L N   
22526 C CA  . LYS L  121 ? 1.1102 1.1409 0.9420 -0.0969 -0.1385 0.0218  121 LYS L CA  
22527 C C   . LYS L  121 ? 1.2239 1.2560 1.0525 -0.0999 -0.1419 0.0264  121 LYS L C   
22528 O O   . LYS L  121 ? 1.3994 1.4303 1.2252 -0.0991 -0.1398 0.0260  121 LYS L O   
22529 C CB  . LYS L  121 ? 1.1253 1.1574 0.9689 -0.0915 -0.1377 0.0242  121 LYS L CB  
22530 C CG  . LYS L  121 ? 1.3351 1.3667 1.1820 -0.0876 -0.1349 0.0249  121 LYS L CG  
22531 C CD  . LYS L  121 ? 1.4609 1.4936 1.3190 -0.0825 -0.1337 0.0270  121 LYS L CD  
22532 C CE  . LYS L  121 ? 1.5663 1.5983 1.4272 -0.0790 -0.1306 0.0272  121 LYS L CE  
22533 N NZ  . LYS L  121 ? 1.7102 1.7430 1.5818 -0.0743 -0.1293 0.0291  121 LYS L NZ  
22534 N N   . VAL L  122 ? 1.2531 1.2879 1.0823 -0.1034 -0.1471 0.0309  122 VAL L N   
22535 C CA  . VAL L  122 ? 1.1784 1.2148 1.0043 -0.1067 -0.1508 0.0358  122 VAL L CA  
22536 C C   . VAL L  122 ? 1.2112 1.2457 1.0242 -0.1119 -0.1507 0.0326  122 VAL L C   
22537 O O   . VAL L  122 ? 1.4696 1.5035 1.2779 -0.1130 -0.1505 0.0338  122 VAL L O   
22538 C CB  . VAL L  122 ? 1.0782 1.1187 0.9088 -0.1090 -0.1567 0.0419  122 VAL L CB  
22539 C CG1 . VAL L  122 ? 1.2061 1.2484 1.0304 -0.1139 -0.1609 0.0462  122 VAL L CG1 
22540 C CG2 . VAL L  122 ? 1.0591 1.1016 0.9028 -0.1040 -0.1570 0.0464  122 VAL L CG2 
22541 N N   . ARG L  123 ? 1.1538 1.1873 0.9612 -0.1150 -0.1506 0.0285  123 ARG L N   
22542 C CA  . ARG L  123 ? 1.2254 1.2570 1.0204 -0.1206 -0.1505 0.0252  123 ARG L CA  
22543 C C   . ARG L  123 ? 1.2587 1.2865 1.0480 -0.1191 -0.1451 0.0203  123 ARG L C   
22544 O O   . ARG L  123 ? 1.4921 1.5188 1.2729 -0.1225 -0.1452 0.0200  123 ARG L O   
22545 C CB  . ARG L  123 ? 1.1860 1.2169 0.9770 -0.1241 -0.1509 0.0215  123 ARG L CB  
22546 C CG  . ARG L  123 ? 1.2295 1.2589 1.0077 -0.1309 -0.1517 0.0190  123 ARG L CG  
22547 C CD  . ARG L  123 ? 1.3431 1.3692 1.1163 -0.1325 -0.1482 0.0122  123 ARG L CD  
22548 N NE  . ARG L  123 ? 1.6365 1.6592 1.4108 -0.1278 -0.1419 0.0072  123 ARG L NE  
22549 C CZ  . ARG L  123 ? 1.8351 1.8540 1.6032 -0.1291 -0.1376 0.0010  123 ARG L CZ  
22550 N NH1 . ARG L  123 ? 1.8212 1.8390 1.5815 -0.1350 -0.1385 -0.0015 123 ARG L NH1 
22551 N NH2 . ARG L  123 ? 1.8353 1.8518 1.6054 -0.1245 -0.1321 -0.0028 123 ARG L NH2 
22552 N N   . SER L  124 ? 1.2801 1.3061 1.0741 -0.1141 -0.1404 0.0165  124 SER L N   
22553 C CA  . SER L  124 ? 1.5538 1.5768 1.3433 -0.1125 -0.1353 0.0119  124 SER L CA  
22554 C C   . SER L  124 ? 1.5836 1.6074 1.3769 -0.1094 -0.1347 0.0151  124 SER L C   
22555 O O   . SER L  124 ? 1.6306 1.6526 1.4238 -0.1064 -0.1303 0.0120  124 SER L O   
22556 C CB  . SER L  124 ? 1.6980 1.7192 1.4911 -0.1085 -0.1306 0.0068  124 SER L CB  
22557 O OG  . SER L  124 ? 1.6881 1.7111 1.4921 -0.1031 -0.1303 0.0091  124 SER L OG  
22558 N N   . GLN L  125 ? 1.4883 1.5147 1.2852 -0.1102 -0.1390 0.0213  125 GLN L N   
22559 C CA  . GLN L  125 ? 1.4603 1.4873 1.2615 -0.1074 -0.1386 0.0248  125 GLN L CA  
22560 C C   . GLN L  125 ? 1.6190 1.6470 1.4144 -0.1118 -0.1423 0.0292  125 GLN L C   
22561 O O   . GLN L  125 ? 1.6158 1.6425 1.4077 -0.1119 -0.1406 0.0293  125 GLN L O   
22562 C CB  . GLN L  125 ? 1.2540 1.2834 1.0675 -0.1029 -0.1396 0.0288  125 GLN L CB  
22563 C CG  . GLN L  125 ? 1.4093 1.4388 1.2281 -0.0995 -0.1382 0.0318  125 GLN L CG  
22564 C CD  . GLN L  125 ? 1.5752 1.6067 1.4062 -0.0952 -0.1388 0.0354  125 GLN L CD  
22565 O OE1 . GLN L  125 ? 1.4029 1.4364 1.2383 -0.0958 -0.1421 0.0382  125 GLN L OE1 
22566 N NE2 . GLN L  125 ? 1.7259 1.7566 1.5623 -0.0909 -0.1353 0.0352  125 GLN L NE2 
22567 N N   . LEU L  126 ? 1.6453 1.6757 1.4396 -0.1157 -0.1474 0.0329  126 LEU L N   
22568 C CA  . LEU L  126 ? 1.4470 1.4780 1.2324 -0.1213 -0.1508 0.0355  126 LEU L CA  
22569 C C   . LEU L  126 ? 1.6293 1.6578 1.4039 -0.1256 -0.1493 0.0295  126 LEU L C   
22570 O O   . LEU L  126 ? 1.8937 1.9224 1.6685 -0.1267 -0.1498 0.0270  126 LEU L O   
22571 C CB  . LEU L  126 ? 1.4320 1.4673 1.2209 -0.1239 -0.1571 0.0421  126 LEU L CB  
22572 C CG  . LEU L  126 ? 1.3054 1.3438 1.1075 -0.1198 -0.1591 0.0469  126 LEU L CG  
22573 C CD1 . LEU L  126 ? 1.3907 1.4332 1.1936 -0.1239 -0.1653 0.0517  126 LEU L CD1 
22574 C CD2 . LEU L  126 ? 1.2512 1.2901 1.0612 -0.1156 -0.1582 0.0515  126 LEU L CD2 
22575 N N   . LYS L  127 ? 1.5203 1.5463 1.2856 -0.1282 -0.1472 0.0270  127 LYS L N   
22576 C CA  . LYS L  127 ? 1.6540 1.6772 1.4087 -0.1325 -0.1454 0.0213  127 LYS L CA  
22577 C C   . LYS L  127 ? 1.8493 1.8731 1.5937 -0.1393 -0.1492 0.0236  127 LYS L C   
22578 O O   . LYS L  127 ? 1.6060 1.6314 1.3471 -0.1438 -0.1529 0.0244  127 LYS L O   
22579 C CB  . LYS L  127 ? 1.6808 1.7001 1.4325 -0.1301 -0.1390 0.0153  127 LYS L CB  
22580 C CG  . LYS L  127 ? 1.6351 1.6543 1.3966 -0.1234 -0.1354 0.0133  127 LYS L CG  
22581 C CD  . LYS L  127 ? 1.5193 1.5372 1.2824 -0.1198 -0.1317 0.0126  127 LYS L CD  
22582 C CE  . LYS L  127 ? 1.7555 1.7738 1.5285 -0.1134 -0.1285 0.0110  127 LYS L CE  
22583 N NZ  . LYS L  127 ? 1.7170 1.7343 1.4919 -0.1098 -0.1246 0.0098  127 LYS L NZ  
22584 N N   . ASN L  128 ? 2.2050 2.2277 1.9444 -0.1403 -0.1483 0.0247  128 ASN L N   
22585 C CA  . ASN L  128 ? 2.1567 2.1802 1.8865 -0.1465 -0.1519 0.0275  128 ASN L CA  
22586 C C   . ASN L  128 ? 2.1541 2.1820 1.8895 -0.1465 -0.1575 0.0361  128 ASN L C   
22587 O O   . ASN L  128 ? 2.0774 2.1076 1.8071 -0.1518 -0.1623 0.0397  128 ASN L O   
22588 C CB  . ASN L  128 ? 2.0162 2.0361 1.7373 -0.1478 -0.1482 0.0247  128 ASN L CB  
22589 C CG  . ASN L  128 ? 2.1973 2.2128 1.9119 -0.1494 -0.1427 0.0168  128 ASN L CG  
22590 O OD1 . ASN L  128 ? 2.2281 2.2428 1.9380 -0.1534 -0.1432 0.0141  128 ASN L OD1 
22591 N ND2 . ASN L  128 ? 2.3303 2.3427 2.0449 -0.1462 -0.1371 0.0130  128 ASN L ND2 
22592 N N   . ASN L  129 ? 2.3228 2.3520 2.0695 -0.1406 -0.1568 0.0393  129 ASN L N   
22593 C CA  . ASN L  129 ? 2.3416 2.3745 2.0947 -0.1398 -0.1612 0.0476  129 ASN L CA  
22594 C C   . ASN L  129 ? 2.2122 2.2497 1.9693 -0.1421 -0.1672 0.0524  129 ASN L C   
22595 O O   . ASN L  129 ? 2.2057 2.2468 1.9689 -0.1415 -0.1711 0.0597  129 ASN L O   
22596 C CB  . ASN L  129 ? 2.2126 2.2453 1.9771 -0.1329 -0.1583 0.0493  129 ASN L CB  
22597 C CG  . ASN L  129 ? 2.1152 2.1441 1.8763 -0.1309 -0.1529 0.0455  129 ASN L CG  
22598 O OD1 . ASN L  129 ? 2.0483 2.0767 1.8170 -0.1261 -0.1503 0.0466  129 ASN L OD1 
22599 N ND2 . ASN L  129 ? 2.2032 2.2293 1.9526 -0.1349 -0.1511 0.0409  129 ASN L ND2 
22600 N N   . ALA L  130 ? 1.9796 2.0169 1.7334 -0.1447 -0.1677 0.0483  130 ALA L N   
22601 C CA  . ALA L  130 ? 1.9011 1.9427 1.6581 -0.1473 -0.1732 0.0520  130 ALA L CA  
22602 C C   . ALA L  130 ? 1.7685 1.8088 1.5180 -0.1517 -0.1728 0.0461  130 ALA L C   
22603 O O   . ALA L  130 ? 1.8019 1.8377 1.5456 -0.1515 -0.1678 0.0390  130 ALA L O   
22604 C CB  . ALA L  130 ? 1.8415 1.8855 1.6131 -0.1415 -0.1737 0.0552  130 ALA L CB  
22605 N N   . LYS L  131 ? 1.8712 1.9153 1.6208 -0.1556 -0.1780 0.0489  131 LYS L N   
22606 C CA  . LYS L  131 ? 2.0665 2.1094 1.8089 -0.1603 -0.1779 0.0435  131 LYS L CA  
22607 C C   . LYS L  131 ? 2.1419 2.1878 1.8933 -0.1590 -0.1802 0.0444  131 LYS L C   
22608 O O   . LYS L  131 ? 2.0248 2.0751 1.7856 -0.1571 -0.1843 0.0510  131 LYS L O   
22609 C CB  . LYS L  131 ? 1.9282 1.9726 1.6583 -0.1685 -0.1819 0.0447  131 LYS L CB  
22610 C CG  . LYS L  131 ? 1.9845 2.0355 1.7181 -0.1715 -0.1894 0.0527  131 LYS L CG  
22611 C CD  . LYS L  131 ? 2.0661 2.1186 1.7870 -0.1803 -0.1933 0.0524  131 LYS L CD  
22612 C CE  . LYS L  131 ? 2.0605 2.1203 1.7854 -0.1834 -0.2010 0.0603  131 LYS L CE  
22613 N NZ  . LYS L  131 ? 1.9291 1.9908 1.6416 -0.1925 -0.2049 0.0595  131 LYS L NZ  
22614 N N   . GLU L  132 ? 2.1942 2.2374 1.9429 -0.1601 -0.1774 0.0379  132 GLU L N   
22615 C CA  . GLU L  132 ? 2.0363 2.0818 1.7923 -0.1595 -0.1792 0.0380  132 GLU L CA  
22616 C C   . GLU L  132 ? 2.0228 2.0728 1.7743 -0.1666 -0.1856 0.0413  132 GLU L C   
22617 O O   . GLU L  132 ? 2.1335 2.1826 1.8729 -0.1731 -0.1866 0.0394  132 GLU L O   
22618 C CB  . GLU L  132 ? 2.1603 2.2011 1.9143 -0.1586 -0.1738 0.0298  132 GLU L CB  
22619 C CG  . GLU L  132 ? 2.1595 2.1962 1.9176 -0.1519 -0.1674 0.0262  132 GLU L CG  
22620 C CD  . GLU L  132 ? 2.2231 2.2554 1.9786 -0.1514 -0.1621 0.0184  132 GLU L CD  
22621 O OE1 . GLU L  132 ? 2.1688 2.1976 1.9253 -0.1470 -0.1566 0.0146  132 GLU L OE1 
22622 O OE2 . GLU L  132 ? 2.2231 2.2557 1.9759 -0.1555 -0.1633 0.0161  132 GLU L OE2 
22623 N N   . ILE L  133 ? 1.8018 1.8565 1.5630 -0.1655 -0.1899 0.0462  133 ILE L N   
22624 C CA  . ILE L  133 ? 2.0150 2.0746 1.7733 -0.1721 -0.1961 0.0493  133 ILE L CA  
22625 C C   . ILE L  133 ? 2.0075 2.0655 1.7642 -0.1745 -0.1946 0.0433  133 ILE L C   
22626 O O   . ILE L  133 ? 2.0674 2.1268 1.8157 -0.1817 -0.1974 0.0419  133 ILE L O   
22627 C CB  . ILE L  133 ? 1.9307 1.9969 1.7008 -0.1700 -0.2018 0.0582  133 ILE L CB  
22628 C CG1 . ILE L  133 ? 1.8319 1.8996 1.6038 -0.1678 -0.2032 0.0646  133 ILE L CG1 
22629 C CG2 . ILE L  133 ? 1.8308 1.9026 1.5982 -0.1770 -0.2084 0.0613  133 ILE L CG2 
22630 C CD1 . ILE L  133 ? 1.9940 2.0633 1.7538 -0.1746 -0.2068 0.0668  133 ILE L CD1 
22631 N N   . GLY L  134 ? 1.9614 2.0164 1.7259 -0.1687 -0.1900 0.0397  134 GLY L N   
22632 C CA  . GLY L  134 ? 1.9078 1.9609 1.6722 -0.1700 -0.1878 0.0340  134 GLY L CA  
22633 C C   . GLY L  134 ? 1.7167 1.7736 1.4941 -0.1667 -0.1904 0.0376  134 GLY L C   
22634 O O   . GLY L  134 ? 1.5199 1.5751 1.3004 -0.1659 -0.1880 0.0335  134 GLY L O   
22635 N N   . ASN L  135 ? 1.5470 1.6090 1.3324 -0.1648 -0.1950 0.0455  135 ASN L N   
22636 C CA  . ASN L  135 ? 1.3600 1.4264 1.1583 -0.1620 -0.1981 0.0501  135 ASN L CA  
22637 C C   . ASN L  135 ? 1.3839 1.4481 1.1934 -0.1533 -0.1938 0.0503  135 ASN L C   
22638 O O   . ASN L  135 ? 1.1215 1.1887 0.9428 -0.1497 -0.1955 0.0544  135 ASN L O   
22639 C CB  . ASN L  135 ? 1.4329 1.5061 1.2346 -0.1644 -0.2052 0.0590  135 ASN L CB  
22640 C CG  . ASN L  135 ? 1.5779 1.6514 1.3830 -0.1601 -0.2049 0.0639  135 ASN L CG  
22641 O OD1 . ASN L  135 ? 1.5518 1.6214 1.3616 -0.1537 -0.1999 0.0620  135 ASN L OD1 
22642 N ND2 . ASN L  135 ? 1.8130 1.8909 1.6152 -0.1637 -0.2102 0.0703  135 ASN L ND2 
22643 N N   . GLY L  136 ? 1.3565 1.4155 1.1621 -0.1501 -0.1882 0.0460  136 GLY L N   
22644 C CA  . GLY L  136 ? 1.2490 1.3060 1.0639 -0.1421 -0.1842 0.0464  136 GLY L CA  
22645 C C   . GLY L  136 ? 1.3581 1.4173 1.1770 -0.1397 -0.1861 0.0528  136 GLY L C   
22646 O O   . GLY L  136 ? 1.3565 1.4155 1.1853 -0.1334 -0.1840 0.0550  136 GLY L O   
22647 N N   . CYS L  137 ? 1.6992 1.7604 1.5103 -0.1447 -0.1898 0.0559  137 CYS L N   
22648 C CA  . CYS L  137 ? 1.6535 1.7169 1.4675 -0.1430 -0.1918 0.0624  137 CYS L CA  
22649 C C   . CYS L  137 ? 1.6891 1.7500 1.4906 -0.1464 -0.1907 0.0606  137 CYS L C   
22650 O O   . CYS L  137 ? 1.7725 1.8325 1.5628 -0.1524 -0.1915 0.0570  137 CYS L O   
22651 C CB  . CYS L  137 ? 1.5612 1.6313 1.3807 -0.1456 -0.1988 0.0707  137 CYS L CB  
22652 S SG  . CYS L  137 ? 1.9122 1.9859 1.7456 -0.1428 -0.2009 0.0733  137 CYS L SG  
22653 N N   . PHE L  138 ? 1.5850 1.6448 1.3888 -0.1427 -0.1889 0.0631  138 PHE L N   
22654 C CA  . PHE L  138 ? 1.8231 1.8801 1.6163 -0.1449 -0.1871 0.0613  138 PHE L CA  
22655 C C   . PHE L  138 ? 1.9015 1.9624 1.6935 -0.1476 -0.1920 0.0690  138 PHE L C   
22656 O O   . PHE L  138 ? 1.7383 1.8035 1.5400 -0.1458 -0.1957 0.0761  138 PHE L O   
22657 C CB  . PHE L  138 ? 1.8190 1.8714 1.6151 -0.1388 -0.1807 0.0579  138 PHE L CB  
22658 C CG  . PHE L  138 ? 1.6036 1.6522 1.4007 -0.1358 -0.1756 0.0505  138 PHE L CG  
22659 C CD1 . PHE L  138 ? 1.4908 1.5403 1.2991 -0.1313 -0.1748 0.0508  138 PHE L CD1 
22660 C CD2 . PHE L  138 ? 1.5985 1.6425 1.3856 -0.1375 -0.1713 0.0435  138 PHE L CD2 
22661 C CE1 . PHE L  138 ? 1.4843 1.5303 1.2934 -0.1285 -0.1700 0.0443  138 PHE L CE1 
22662 C CE2 . PHE L  138 ? 1.5041 1.5448 1.2924 -0.1347 -0.1665 0.0371  138 PHE L CE2 
22663 C CZ  . PHE L  138 ? 1.4863 1.5280 1.2855 -0.1302 -0.1659 0.0375  138 PHE L CZ  
22664 N N   . GLU L  139 ? 2.1022 2.1614 1.8823 -0.1518 -0.1919 0.0677  139 GLU L N   
22665 C CA  . GLU L  139 ? 1.9950 2.0573 1.7732 -0.1541 -0.1959 0.0748  139 GLU L CA  
22666 C C   . GLU L  139 ? 1.9322 1.9904 1.7062 -0.1518 -0.1915 0.0734  139 GLU L C   
22667 O O   . GLU L  139 ? 1.9815 2.0353 1.7452 -0.1539 -0.1879 0.0670  139 GLU L O   
22668 C CB  . GLU L  139 ? 2.1553 2.2206 1.9226 -0.1623 -0.2011 0.0762  139 GLU L CB  
22669 C CG  . GLU L  139 ? 2.3557 2.4247 2.1207 -0.1648 -0.2054 0.0839  139 GLU L CG  
22670 C CD  . GLU L  139 ? 2.4195 2.4930 2.1759 -0.1729 -0.2117 0.0867  139 GLU L CD  
22671 O OE1 . GLU L  139 ? 2.2710 2.3448 2.0234 -0.1767 -0.2126 0.0824  139 GLU L OE1 
22672 O OE2 . GLU L  139 ? 2.4299 2.5068 2.1835 -0.1756 -0.2157 0.0932  139 GLU L OE2 
22673 N N   . PHE L  140 ? 2.1748 2.2343 1.9572 -0.1476 -0.1917 0.0793  140 PHE L N   
22674 C CA  . PHE L  140 ? 2.3107 2.3665 2.0908 -0.1451 -0.1876 0.0785  140 PHE L CA  
22675 C C   . PHE L  140 ? 2.3369 2.3930 2.1054 -0.1506 -0.1898 0.0807  140 PHE L C   
22676 O O   . PHE L  140 ? 2.3102 2.3710 2.0778 -0.1544 -0.1956 0.0872  140 PHE L O   
22677 C CB  . PHE L  140 ? 2.2468 2.3038 2.0400 -0.1390 -0.1869 0.0843  140 PHE L CB  
22678 C CG  . PHE L  140 ? 2.1485 2.2041 1.9524 -0.1329 -0.1833 0.0815  140 PHE L CG  
22679 C CD1 . PHE L  140 ? 2.1416 2.2010 1.9561 -0.1313 -0.1863 0.0853  140 PHE L CD1 
22680 C CD2 . PHE L  140 ? 2.1789 2.2296 1.9825 -0.1290 -0.1769 0.0751  140 PHE L CD2 
22681 C CE1 . PHE L  140 ? 2.1315 2.1894 1.9555 -0.1258 -0.1829 0.0826  140 PHE L CE1 
22682 C CE2 . PHE L  140 ? 2.1541 2.2037 1.9672 -0.1236 -0.1737 0.0726  140 PHE L CE2 
22683 C CZ  . PHE L  140 ? 2.1198 2.1728 1.9429 -0.1220 -0.1766 0.0763  140 PHE L CZ  
22684 N N   . TYR L  141 ? 2.0132 2.0645 1.7731 -0.1510 -0.1852 0.0754  141 TYR L N   
22685 C CA  . TYR L  141 ? 1.9754 2.0262 1.7251 -0.1552 -0.1863 0.0775  141 TYR L CA  
22686 C C   . TYR L  141 ? 1.9341 1.9846 1.6905 -0.1508 -0.1848 0.0825  141 TYR L C   
22687 O O   . TYR L  141 ? 2.0477 2.0990 1.7992 -0.1533 -0.1867 0.0870  141 TYR L O   
22688 C CB  . TYR L  141 ? 2.0401 2.0857 1.7772 -0.1580 -0.1818 0.0693  141 TYR L CB  
22689 C CG  . TYR L  141 ? 1.9675 2.0127 1.6966 -0.1630 -0.1827 0.0638  141 TYR L CG  
22690 C CD1 . TYR L  141 ? 1.9121 1.9526 1.6381 -0.1619 -0.1772 0.0552  141 TYR L CD1 
22691 C CD2 . TYR L  141 ? 1.9058 1.9553 1.6306 -0.1689 -0.1887 0.0674  141 TYR L CD2 
22692 C CE1 . TYR L  141 ? 1.8990 1.9387 1.6179 -0.1664 -0.1775 0.0502  141 TYR L CE1 
22693 C CE2 . TYR L  141 ? 1.9001 1.9490 1.6175 -0.1738 -0.1892 0.0622  141 TYR L CE2 
22694 C CZ  . TYR L  141 ? 1.8979 1.9416 1.6124 -0.1724 -0.1834 0.0535  141 TYR L CZ  
22695 O OH  . TYR L  141 ? 1.7618 1.8045 1.4692 -0.1772 -0.1835 0.0482  141 TYR L OH  
22696 N N   . HIS L  142 ? 1.9549 2.0041 1.7226 -0.1442 -0.1812 0.0817  142 HIS L N   
22697 C CA  . HIS L  142 ? 1.9395 1.9878 1.7144 -0.1396 -0.1789 0.0857  142 HIS L CA  
22698 C C   . HIS L  142 ? 1.9195 1.9716 1.7088 -0.1355 -0.1814 0.0926  142 HIS L C   
22699 O O   . HIS L  142 ? 2.0970 2.1494 1.8944 -0.1322 -0.1804 0.0906  142 HIS L O   
22700 C CB  . HIS L  142 ? 1.8905 1.9335 1.6654 -0.1354 -0.1718 0.0786  142 HIS L CB  
22701 C CG  . HIS L  142 ? 1.9456 1.9883 1.7338 -0.1287 -0.1689 0.0787  142 HIS L CG  
22702 N ND1 . HIS L  142 ? 1.9361 1.9780 1.7318 -0.1245 -0.1665 0.0822  142 HIS L ND1 
22703 C CD2 . HIS L  142 ? 1.8771 1.9199 1.6720 -0.1257 -0.1677 0.0756  142 HIS L CD2 
22704 C CE1 . HIS L  142 ? 1.9101 1.9517 1.7164 -0.1193 -0.1640 0.0811  142 HIS L CE1 
22705 N NE2 . HIS L  142 ? 1.8966 1.9388 1.7027 -0.1198 -0.1648 0.0772  142 HIS L NE2 
22706 N N   . LYS L  143 ? 1.8710 1.9259 1.6637 -0.1359 -0.1846 0.1008  143 LYS L N   
22707 C CA  . LYS L  143 ? 1.8911 1.9499 1.6977 -0.1324 -0.1871 0.1083  143 LYS L CA  
22708 C C   . LYS L  143 ? 1.8797 1.9362 1.6975 -0.1258 -0.1823 0.1053  143 LYS L C   
22709 O O   . LYS L  143 ? 1.8106 1.8633 1.6304 -0.1221 -0.1772 0.1030  143 LYS L O   
22710 C CB  . LYS L  143 ? 1.9613 2.0216 1.7706 -0.1321 -0.1886 0.1166  143 LYS L CB  
22711 C CG  . LYS L  143 ? 2.0076 2.0720 1.8086 -0.1384 -0.1947 0.1221  143 LYS L CG  
22712 C CD  . LYS L  143 ? 2.0388 2.1099 1.8476 -0.1395 -0.2012 0.1295  143 LYS L CD  
22713 C CE  . LYS L  143 ? 2.0779 2.1506 1.8836 -0.1424 -0.2035 0.1248  143 LYS L CE  
22714 N NZ  . LYS L  143 ? 1.9392 2.0189 1.7524 -0.1438 -0.2100 0.1321  143 LYS L NZ  
22715 N N   . CYS L  144 ? 1.9811 2.0399 1.8061 -0.1245 -0.1841 0.1052  144 CYS L N   
22716 C CA  . CYS L  144 ? 2.1070 2.1638 1.9422 -0.1186 -0.1798 0.1021  144 CYS L CA  
22717 C C   . CYS L  144 ? 1.9492 2.0096 1.7988 -0.1153 -0.1821 0.1095  144 CYS L C   
22718 O O   . CYS L  144 ? 1.9194 1.9835 1.7731 -0.1163 -0.1860 0.1116  144 CYS L O   
22719 C CB  . CYS L  144 ? 2.1352 2.1906 1.9668 -0.1192 -0.1785 0.0945  144 CYS L CB  
22720 S SG  . CYS L  144 ? 2.2165 2.2689 2.0584 -0.1122 -0.1726 0.0895  144 CYS L SG  
22721 N N   . ASP L  145 ? 2.0362 2.0955 1.8936 -0.1113 -0.1794 0.1134  145 ASP L N   
22722 C CA  . ASP L  145 ? 2.0774 2.1394 1.9493 -0.1076 -0.1805 0.1203  145 ASP L CA  
22723 C C   . ASP L  145 ? 2.0492 2.1095 1.9300 -0.1028 -0.1769 0.1161  145 ASP L C   
22724 O O   . ASP L  145 ? 2.1305 2.1886 2.0061 -0.1030 -0.1747 0.1085  145 ASP L O   
22725 C CB  . ASP L  145 ? 2.2233 2.2843 2.1004 -0.1052 -0.1786 0.1260  145 ASP L CB  
22726 C CG  . ASP L  145 ? 2.3178 2.3732 2.1898 -0.1034 -0.1724 0.1201  145 ASP L CG  
22727 O OD1 . ASP L  145 ? 2.2079 2.2616 2.0860 -0.1004 -0.1694 0.1235  145 ASP L OD1 
22728 O OD2 . ASP L  145 ? 2.3337 2.3864 2.1959 -0.1050 -0.1703 0.1123  145 ASP L OD2 
22729 N N   . ASN L  146 ? 1.9298 1.9911 1.8240 -0.0986 -0.1761 0.1213  146 ASN L N   
22730 C CA  . ASN L  146 ? 1.8136 1.8739 1.7173 -0.0942 -0.1731 0.1184  146 ASN L CA  
22731 C C   . ASN L  146 ? 1.9170 1.9720 1.8182 -0.0911 -0.1664 0.1101  146 ASN L C   
22732 O O   . ASN L  146 ? 2.1388 2.1927 2.0405 -0.0897 -0.1646 0.1046  146 ASN L O   
22733 C CB  . ASN L  146 ? 1.5916 1.6538 1.5104 -0.0904 -0.1731 0.1259  146 ASN L CB  
22734 C CG  . ASN L  146 ? 1.5790 1.6472 1.5028 -0.0927 -0.1797 0.1336  146 ASN L CG  
22735 O OD1 . ASN L  146 ? 1.6107 1.6812 1.5464 -0.0903 -0.1806 0.1408  146 ASN L OD1 
22736 N ND2 . ASN L  146 ? 1.5771 1.6481 1.4922 -0.0975 -0.1844 0.1321  146 ASN L ND2 
22737 N N   . THR L  147 ? 2.0132 2.0650 1.9120 -0.0900 -0.1626 0.1095  147 THR L N   
22738 C CA  . THR L  147 ? 2.1354 2.1826 2.0322 -0.0871 -0.1563 0.1021  147 THR L CA  
22739 C C   . THR L  147 ? 2.1966 2.2419 2.0798 -0.0903 -0.1557 0.0947  147 THR L C   
22740 O O   . THR L  147 ? 2.2401 2.2822 2.1205 -0.0884 -0.1510 0.0879  147 THR L O   
22741 C CB  . THR L  147 ? 2.1032 2.1476 2.0031 -0.0848 -0.1522 0.1040  147 THR L CB  
22742 O OG1 . THR L  147 ? 2.2530 2.2973 2.1440 -0.0884 -0.1539 0.1059  147 THR L OG1 
22743 C CG2 . THR L  147 ? 1.2166 1.2625 1.1304 -0.0817 -0.1524 0.1115  147 THR L CG2 
22744 N N   . CYS L  148 ? 2.1311 2.1788 2.0061 -0.0952 -0.1605 0.0964  148 CYS L N   
22745 C CA  . CYS L  148 ? 2.1342 2.1805 1.9965 -0.0988 -0.1605 0.0898  148 CYS L CA  
22746 C C   . CYS L  148 ? 2.2046 2.2519 2.0684 -0.0986 -0.1615 0.0862  148 CYS L C   
22747 O O   . CYS L  148 ? 2.1692 2.2140 2.0288 -0.0978 -0.1582 0.0789  148 CYS L O   
22748 C CB  . CYS L  148 ? 2.1694 2.2178 2.0225 -0.1044 -0.1653 0.0933  148 CYS L CB  
22749 S SG  . CYS L  148 ? 2.2070 2.2539 2.0444 -0.1097 -0.1659 0.0859  148 CYS L SG  
22750 N N   . MET L  149 ? 2.2068 2.2581 2.0774 -0.0992 -0.1660 0.0916  149 MET L N   
22751 C CA  . MET L  149 ? 2.0493 2.1020 1.9230 -0.0989 -0.1673 0.0892  149 MET L CA  
22752 C C   . MET L  149 ? 1.9819 2.0318 1.8620 -0.0936 -0.1619 0.0843  149 MET L C   
22753 O O   . MET L  149 ? 1.9160 1.9655 1.7954 -0.0933 -0.1613 0.0797  149 MET L O   
22754 C CB  . MET L  149 ? 1.9081 1.9657 1.7907 -0.0994 -0.1725 0.0969  149 MET L CB  
22755 C CG  . MET L  149 ? 1.8908 1.9521 1.7668 -0.1052 -0.1787 0.1014  149 MET L CG  
22756 S SD  . MET L  149 ? 1.7427 1.8041 1.6060 -0.1107 -0.1808 0.0949  149 MET L SD  
22757 C CE  . MET L  149 ? 1.8208 1.8878 1.6797 -0.1171 -0.1886 0.1023  149 MET L CE  
22758 N N   . GLU L  150 ? 2.5045 2.5524 2.3907 -0.0897 -0.1580 0.0853  150 GLU L N   
22759 C CA  . GLU L  150 ? 2.4846 2.5300 2.3771 -0.0848 -0.1530 0.0812  150 GLU L CA  
22760 C C   . GLU L  150 ? 2.4367 2.4787 2.3206 -0.0845 -0.1486 0.0729  150 GLU L C   
22761 O O   . GLU L  150 ? 2.4231 2.4640 2.3085 -0.0823 -0.1461 0.0680  150 GLU L O   
22762 C CB  . GLU L  150 ? 2.5845 2.6289 2.4864 -0.0809 -0.1501 0.0851  150 GLU L CB  
22763 C CG  . GLU L  150 ? 2.6459 2.6917 2.5607 -0.0773 -0.1498 0.0880  150 GLU L CG  
22764 C CD  . GLU L  150 ? 2.6360 2.6860 2.5566 -0.0790 -0.1555 0.0956  150 GLU L CD  
22765 O OE1 . GLU L  150 ? 2.6641 2.7153 2.5965 -0.0760 -0.1553 0.1000  150 GLU L OE1 
22766 O OE2 . GLU L  150 ? 2.4999 2.5523 2.4133 -0.0835 -0.1602 0.0973  150 GLU L OE2 
22767 N N   . SER L  151 ? 2.1740 2.2143 2.0493 -0.0867 -0.1477 0.0715  151 SER L N   
22768 C CA  . SER L  151 ? 2.1732 2.2105 2.0404 -0.0866 -0.1436 0.0640  151 SER L CA  
22769 C C   . SER L  151 ? 2.1037 2.1411 1.9655 -0.0884 -0.1444 0.0591  151 SER L C   
22770 O O   . SER L  151 ? 2.1790 2.2143 2.0377 -0.0869 -0.1406 0.0527  151 SER L O   
22771 C CB  . SER L  151 ? 2.2116 2.2476 2.0695 -0.0897 -0.1434 0.0639  151 SER L CB  
22772 O OG  . SER L  151 ? 2.1698 2.2076 2.0203 -0.0948 -0.1482 0.0661  151 SER L OG  
22773 N N   . VAL L  152 ? 1.7139 1.7540 1.5750 -0.0915 -0.1493 0.0621  152 VAL L N   
22774 C CA  . VAL L  152 ? 1.6364 1.6766 1.4928 -0.0936 -0.1503 0.0578  152 VAL L CA  
22775 C C   . VAL L  152 ? 1.6753 1.7159 1.5407 -0.0897 -0.1489 0.0565  152 VAL L C   
22776 O O   . VAL L  152 ? 1.5799 1.6188 1.4429 -0.0886 -0.1461 0.0507  152 VAL L O   
22777 C CB  . VAL L  152 ? 1.4263 1.4694 1.2785 -0.0988 -0.1562 0.0615  152 VAL L CB  
22778 C CG1 . VAL L  152 ? 1.3212 1.3637 1.1663 -0.1017 -0.1565 0.0560  152 VAL L CG1 
22779 C CG2 . VAL L  152 ? 1.4988 1.5421 1.3437 -0.1025 -0.1582 0.0644  152 VAL L CG2 
22780 N N   . LYS L  153 ? 1.6881 1.7309 1.5641 -0.0875 -0.1507 0.0621  153 LYS L N   
22781 C CA  . LYS L  153 ? 1.6189 1.6621 1.5041 -0.0838 -0.1494 0.0615  153 LYS L CA  
22782 C C   . LYS L  153 ? 1.8332 1.8735 1.7206 -0.0793 -0.1435 0.0567  153 LYS L C   
22783 O O   . LYS L  153 ? 1.8445 1.8837 1.7315 -0.0777 -0.1411 0.0518  153 LYS L O   
22784 C CB  . LYS L  153 ? 1.5328 1.5787 1.4293 -0.0822 -0.1521 0.0688  153 LYS L CB  
22785 C CG  . LYS L  153 ? 1.2299 1.2797 1.1262 -0.0863 -0.1583 0.0739  153 LYS L CG  
22786 C CD  . LYS L  153 ? 1.2702 1.3228 1.1793 -0.0841 -0.1604 0.0806  153 LYS L CD  
22787 C CE  . LYS L  153 ? 1.2172 1.2743 1.1263 -0.0883 -0.1670 0.0862  153 LYS L CE  
22788 N NZ  . LYS L  153 ? 1.4374 1.4956 1.3394 -0.0921 -0.1698 0.0896  153 LYS L NZ  
22789 N N   . ASN L  154 ? 2.4574 2.4966 2.3474 -0.0772 -0.1410 0.0583  154 ASN L N   
22790 C CA  . ASN L  154 ? 2.4566 2.4933 2.3485 -0.0733 -0.1354 0.0540  154 ASN L CA  
22791 C C   . ASN L  154 ? 2.5150 2.5496 2.3965 -0.0745 -0.1327 0.0473  154 ASN L C   
22792 O O   . ASN L  154 ? 2.5866 2.6194 2.4679 -0.0719 -0.1282 0.0437  154 ASN L O   
22793 C CB  . ASN L  154 ? 2.5652 2.6012 2.4627 -0.0712 -0.1335 0.0576  154 ASN L CB  
22794 C CG  . ASN L  154 ? 2.5591 2.5969 2.4681 -0.0694 -0.1355 0.0641  154 ASN L CG  
22795 O OD1 . ASN L  154 ? 2.4828 2.5229 2.3946 -0.0705 -0.1392 0.0667  154 ASN L OD1 
22796 N ND2 . ASN L  154 ? 2.6049 2.6417 2.5207 -0.0667 -0.1327 0.0667  154 ASN L ND2 
22797 N N   . GLY L  155 ? 2.2185 2.2535 2.0917 -0.0785 -0.1353 0.0457  155 GLY L N   
22798 C CA  . GLY L  155 ? 2.1733 2.2063 2.0369 -0.0798 -0.1327 0.0395  155 GLY L CA  
22799 C C   . GLY L  155 ? 2.2204 2.2516 2.0785 -0.0801 -0.1299 0.0377  155 GLY L C   
22800 O O   . GLY L  155 ? 2.1522 2.1818 2.0028 -0.0810 -0.1275 0.0325  155 GLY L O   
22801 N N   . THR L  156 ? 2.4408 2.4722 2.3029 -0.0793 -0.1301 0.0420  156 THR L N   
22802 C CA  . THR L  156 ? 2.5135 2.5432 2.3712 -0.0796 -0.1274 0.0408  156 THR L CA  
22803 C C   . THR L  156 ? 2.3205 2.3506 2.1717 -0.0840 -0.1309 0.0444  156 THR L C   
22804 O O   . THR L  156 ? 2.2071 2.2379 2.0622 -0.0841 -0.1324 0.0499  156 THR L O   
22805 C CB  . THR L  156 ? 2.6032 2.6325 2.4694 -0.0759 -0.1247 0.0431  156 THR L CB  
22806 O OG1 . THR L  156 ? 2.5034 2.5344 2.3774 -0.0756 -0.1279 0.0498  156 THR L OG1 
22807 C CG2 . THR L  156 ? 2.6296 2.6585 2.5009 -0.0717 -0.1207 0.0389  156 THR L CG2 
22808 N N   . TYR L  157 ? 1.9708 2.0004 1.8122 -0.0877 -0.1321 0.0414  157 TYR L N   
22809 C CA  . TYR L  157 ? 1.9447 1.9748 1.7789 -0.0925 -0.1357 0.0446  157 TYR L CA  
22810 C C   . TYR L  157 ? 2.0170 2.0447 1.8432 -0.0939 -0.1329 0.0418  157 TYR L C   
22811 O O   . TYR L  157 ? 1.9029 1.9288 1.7269 -0.0922 -0.1286 0.0362  157 TYR L O   
22812 C CB  . TYR L  157 ? 1.9184 1.9494 1.7470 -0.0964 -0.1392 0.0434  157 TYR L CB  
22813 C CG  . TYR L  157 ? 1.7294 1.7615 1.5506 -0.1017 -0.1435 0.0471  157 TYR L CG  
22814 C CD1 . TYR L  157 ? 1.6951 1.7303 1.5208 -0.1031 -0.1485 0.0539  157 TYR L CD1 
22815 C CD2 . TYR L  157 ? 1.6379 1.6680 1.4479 -0.1053 -0.1425 0.0437  157 TYR L CD2 
22816 C CE1 . TYR L  157 ? 1.6057 1.6423 1.4247 -0.1081 -0.1526 0.0575  157 TYR L CE1 
22817 C CE2 . TYR L  157 ? 1.7044 1.7355 1.5072 -0.1104 -0.1464 0.0471  157 TYR L CE2 
22818 C CZ  . TYR L  157 ? 1.5847 1.6191 1.3919 -0.1118 -0.1516 0.0540  157 TYR L CZ  
22819 O OH  . TYR L  157 ? 1.5178 1.5537 1.3178 -0.1170 -0.1558 0.0577  157 TYR L OH  
22820 N N   . ASP L  158 ? 1.8930 1.9210 1.7150 -0.0971 -0.1354 0.0459  158 ASP L N   
22821 C CA  . ASP L  158 ? 1.8876 1.9135 1.7033 -0.0982 -0.1328 0.0444  158 ASP L CA  
22822 C C   . ASP L  158 ? 1.5521 1.5772 1.3557 -0.1036 -0.1346 0.0428  158 ASP L C   
22823 O O   . ASP L  158 ? 1.4993 1.5247 1.2987 -0.1057 -0.1360 0.0401  158 ASP L O   
22824 C CB  . ASP L  158 ? 1.6115 1.6377 1.4323 -0.0972 -0.1333 0.0505  158 ASP L CB  
22825 C CG  . ASP L  158 ? 1.9292 1.9581 1.7603 -0.0955 -0.1366 0.0567  158 ASP L CG  
22826 O OD1 . ASP L  158 ? 1.7142 1.7453 1.5450 -0.0976 -0.1409 0.0588  158 ASP L OD1 
22827 O OD2 . ASP L  158 ? 1.9288 1.9575 1.7687 -0.0920 -0.1347 0.0595  158 ASP L OD2 
22828 N N   . TYR L  159 ? 1.1710 1.1328 0.9622 -0.1166 -0.0892 0.0230  159 TYR L N   
22829 C CA  . TYR L  159 ? 1.2384 1.1950 1.0181 -0.1212 -0.0909 0.0238  159 TYR L CA  
22830 C C   . TYR L  159 ? 1.4604 1.4130 1.2334 -0.1240 -0.0908 0.0260  159 TYR L C   
22831 O O   . TYR L  159 ? 1.3192 1.2685 1.0845 -0.1260 -0.0872 0.0228  159 TYR L O   
22832 C CB  . TYR L  159 ? 0.4517 0.4080 0.2278 -0.1212 -0.0862 0.0178  159 TYR L CB  
22833 C CG  . TYR L  159 ? 0.4585 0.4116 0.2262 -0.1246 -0.0878 0.0163  159 TYR L CG  
22834 C CD1 . TYR L  159 ? 0.4643 0.4137 0.2229 -0.1272 -0.0841 0.0122  159 TYR L CD1 
22835 C CD2 . TYR L  159 ? 0.4594 0.4131 0.2283 -0.1253 -0.0927 0.0189  159 TYR L CD2 
22836 C CE1 . TYR L  159 ? 0.4710 0.4171 0.2217 -0.1304 -0.0850 0.0106  159 TYR L CE1 
22837 C CE2 . TYR L  159 ? 0.4660 0.4167 0.2270 -0.1286 -0.0939 0.0174  159 TYR L CE2 
22838 C CZ  . TYR L  159 ? 0.4719 0.4186 0.2236 -0.1312 -0.0899 0.0131  159 TYR L CZ  
22839 O OH  . TYR L  159 ? 0.4792 0.4223 0.2225 -0.1348 -0.0907 0.0113  159 TYR L OH  
22840 N N   . PRO L  160 ? 1.2777 1.3029 1.0660 -0.1132 -0.1407 0.0549  160 PRO L N   
22841 C CA  . PRO L  160 ? 1.3180 1.3439 1.1004 -0.1174 -0.1440 0.0601  160 PRO L CA  
22842 C C   . PRO L  160 ? 1.2605 1.2885 1.0361 -0.1224 -0.1490 0.0610  160 PRO L C   
22843 O O   . PRO L  160 ? 0.9868 1.0181 0.7678 -0.1226 -0.1534 0.0657  160 PRO L O   
22844 C CB  . PRO L  160 ? 1.1071 1.1352 0.9001 -0.1147 -0.1459 0.0678  160 PRO L CB  
22845 C CG  . PRO L  160 ? 1.0815 1.1083 0.8839 -0.1090 -0.1413 0.0652  160 PRO L CG  
22846 C CD  . PRO L  160 ? 0.8738 0.8999 0.6747 -0.1082 -0.1396 0.0583  160 PRO L CD  
22847 N N   . LYS L  161 ? 1.3826 1.4085 1.1463 -0.1265 -0.1481 0.0563  161 LYS L N   
22848 C CA  . LYS L  161 ? 1.3256 1.3530 1.0815 -0.1318 -0.1522 0.0561  161 LYS L CA  
22849 C C   . LYS L  161 ? 1.6078 1.6353 1.3538 -0.1372 -0.1549 0.0595  161 LYS L C   
22850 O O   . LYS L  161 ? 1.7079 1.7344 1.4536 -0.1365 -0.1535 0.0621  161 LYS L O   
22851 C CB  . LYS L  161 ? 1.4740 1.4987 1.2235 -0.1329 -0.1490 0.0478  161 LYS L CB  
22852 C CG  . LYS L  161 ? 1.3650 1.3864 1.1020 -0.1368 -0.1464 0.0434  161 LYS L CG  
22853 C CD  . LYS L  161 ? 1.4575 1.4781 1.1853 -0.1416 -0.1474 0.0389  161 LYS L CD  
22854 C CE  . LYS L  161 ? 1.2228 1.2405 0.9373 -0.1467 -0.1460 0.0362  161 LYS L CE  
22855 N NZ  . LYS L  161 ? 1.1787 1.1933 0.8860 -0.1486 -0.1424 0.0282  161 LYS L NZ  
22856 N N   . TYR L  162 ? 1.4857 1.5146 1.2235 -0.1427 -0.1587 0.0594  162 TYR L N   
22857 C CA  . TYR L  162 ? 1.6079 1.6372 1.3349 -0.1486 -0.1615 0.0622  162 TYR L CA  
22858 C C   . TYR L  162 ? 1.4931 1.5203 1.2176 -0.1480 -0.1591 0.0642  162 TYR L C   
22859 O O   . TYR L  162 ? 1.3860 1.4153 1.1090 -0.1502 -0.1626 0.0709  162 TYR L O   
22860 C CB  . TYR L  162 ? 1.3867 1.4137 1.1013 -0.1538 -0.1606 0.0556  162 TYR L CB  
22861 C CG  . TYR L  162 ? 1.2177 1.2475 0.9237 -0.1606 -0.1663 0.0592  162 TYR L CG  
22862 C CD1 . TYR L  162 ? 1.1017 1.1344 0.8080 -0.1632 -0.1702 0.0593  162 TYR L CD1 
22863 C CD2 . TYR L  162 ? 1.4425 1.4722 1.1401 -0.1646 -0.1679 0.0627  162 TYR L CD2 
22864 C CE1 . TYR L  162 ? 1.4981 1.5337 1.1964 -0.1698 -0.1756 0.0626  162 TYR L CE1 
22865 C CE2 . TYR L  162 ? 1.3809 1.4135 1.0703 -0.1711 -0.1732 0.0662  162 TYR L CE2 
22866 C CZ  . TYR L  162 ? 1.4853 1.5210 1.1750 -0.1738 -0.1772 0.0661  162 TYR L CZ  
22867 O OH  . TYR L  162 ? 1.2650 1.3040 0.9464 -0.1806 -0.1827 0.0695  162 TYR L OH  
22868 C C1  . NAG M  .   ? 0.8711 0.8996 0.7861 -0.0491 -0.1023 0.0312  601 NAG A C1  
22869 C C2  . NAG M  .   ? 1.0079 1.0374 0.9236 -0.0480 -0.1033 0.0294  601 NAG A C2  
22870 C C3  . NAG M  .   ? 1.2054 1.2349 1.1239 -0.0447 -0.0991 0.0256  601 NAG A C3  
22871 C C4  . NAG M  .   ? 1.2062 1.2348 1.1314 -0.0426 -0.0958 0.0266  601 NAG A C4  
22872 C C5  . NAG M  .   ? 1.3403 1.3679 1.2656 -0.0442 -0.0959 0.0296  601 NAG A C5  
22873 C C6  . NAG M  .   ? 0.9870 1.0143 0.9197 -0.0444 -0.0984 0.0360  601 NAG A C6  
22874 C C7  . NAG M  .   ? 1.0631 1.0937 0.9684 -0.0525 -0.1090 0.0285  601 NAG A C7  
22875 C C8  . NAG M  .   ? 0.7504 0.7809 0.6463 -0.0550 -0.1099 0.0250  601 NAG A C8  
22876 N N2  . NAG M  .   ? 1.1766 1.2065 1.0836 -0.0503 -0.1050 0.0266  601 NAG A N2  
22877 O O3  . NAG M  .   ? 0.9549 0.9852 0.8767 -0.0434 -0.1003 0.0256  601 NAG A O3  
22878 O O4  . NAG M  .   ? 0.7476 0.7764 0.6705 -0.0410 -0.0918 0.0217  601 NAG A O4  
22879 O O5  . NAG M  .   ? 1.1459 1.1737 1.0626 -0.0470 -0.0977 0.0284  601 NAG A O5  
22880 O O6  . NAG M  .   ? 0.6946 0.7208 0.6272 -0.0457 -0.0982 0.0387  601 NAG A O6  
22881 O O7  . NAG M  .   ? 1.0566 1.0878 0.9677 -0.0527 -0.1118 0.0330  601 NAG A O7  
22882 C C1  . NAG N  .   ? 1.3856 1.3647 1.5870 0.0283  -0.0063 0.0637  602 NAG A C1  
22883 C C2  . NAG N  .   ? 1.0939 1.0700 1.2975 0.0300  -0.0016 0.0623  602 NAG A C2  
22884 C C3  . NAG N  .   ? 1.1214 1.0999 1.3293 0.0304  -0.0057 0.0643  602 NAG A C3  
22885 C C4  . NAG N  .   ? 1.3778 1.3605 1.5760 0.0292  -0.0122 0.0629  602 NAG A C4  
22886 C C5  . NAG N  .   ? 1.4022 1.3874 1.5964 0.0275  -0.0162 0.0635  602 NAG A C5  
22887 C C6  . NAG N  .   ? 1.5562 1.5445 1.7381 0.0264  -0.0209 0.0607  602 NAG A C6  
22888 C C7  . NAG N  .   ? 1.0687 1.0368 1.2805 0.0319  0.0111  0.0610  602 NAG A C7  
22889 C C8  . NAG N  .   ? 1.2289 1.1936 1.4533 0.0333  0.0158  0.0635  602 NAG A C8  
22890 N N2  . NAG N  .   ? 0.9787 0.9508 1.1926 0.0309  0.0045  0.0640  602 NAG A N2  
22891 O O3  . NAG N  .   ? 1.5831 1.5587 1.7912 0.0320  -0.0009 0.0623  602 NAG A O3  
22892 O O4  . NAG N  .   ? 1.4597 1.4449 1.6636 0.0291  -0.0165 0.0655  602 NAG A O4  
22893 O O5  . NAG N  .   ? 1.4301 1.4127 1.6212 0.0274  -0.0118 0.0617  602 NAG A O5  
22894 O O6  . NAG N  .   ? 1.5944 1.5819 1.7718 0.0276  -0.0194 0.0580  602 NAG A O6  
22895 O O7  . NAG N  .   ? 1.0475 1.0145 1.2476 0.0315  0.0133  0.0565  602 NAG A O7  
22896 C C1  . NAG O  .   ? 1.7772 1.7601 1.9821 0.0307  -0.0128 0.0640  603 NAG A C1  
22897 C C2  . NAG O  .   ? 1.7653 1.7507 1.9668 0.0305  -0.0170 0.0633  603 NAG A C2  
22898 C C3  . NAG O  .   ? 1.6073 1.5897 1.8054 0.0323  -0.0121 0.0604  603 NAG A C3  
22899 C C4  . NAG O  .   ? 1.8216 1.8007 2.0315 0.0336  -0.0071 0.0626  603 NAG A C4  
22900 C C5  . NAG O  .   ? 1.7509 1.7281 1.9664 0.0335  -0.0039 0.0642  603 NAG A C5  
22901 C C6  . NAG O  .   ? 1.6938 1.6682 1.9230 0.0347  0.0006  0.0671  603 NAG A C6  
22902 C C7  . NAG O  .   ? 1.9035 1.8956 2.0970 0.0274  -0.0281 0.0637  603 NAG A C7  
22903 C C8  . NAG O  .   ? 1.8311 1.8265 2.0182 0.0253  -0.0334 0.0638  603 NAG A C8  
22904 N N2  . NAG O  .   ? 1.8281 1.8167 2.0193 0.0289  -0.0221 0.0616  603 NAG A N2  
22905 O O3  . NAG O  .   ? 1.4643 1.4484 1.6591 0.0322  -0.0152 0.0596  603 NAG A O3  
22906 O O4  . NAG O  .   ? 1.9002 1.8761 2.1062 0.0353  -0.0018 0.0598  603 NAG A O4  
22907 O O5  . NAG O  .   ? 1.8205 1.8010 2.0379 0.0319  -0.0091 0.0668  603 NAG A O5  
22908 O O6  . NAG O  .   ? 2.1355 2.1099 2.3687 0.0356  0.0003  0.0676  603 NAG A O6  
22909 O O7  . NAG O  .   ? 1.9038 1.8965 2.1044 0.0276  -0.0292 0.0656  603 NAG A O7  
22910 C C1  . NAG P  .   ? 1.2838 1.2364 1.5269 0.0088  0.0227  0.1081  604 NAG A C1  
22911 C C2  . NAG P  .   ? 1.3102 1.2641 1.5704 0.0113  0.0216  0.1178  604 NAG A C2  
22912 C C3  . NAG P  .   ? 1.2467 1.1952 1.5193 0.0131  0.0301  0.1182  604 NAG A C3  
22913 C C4  . NAG P  .   ? 1.3930 1.3346 1.6603 0.0116  0.0392  0.1114  604 NAG A C4  
22914 C C5  . NAG P  .   ? 1.3910 1.3331 1.6426 0.0096  0.0386  0.1020  604 NAG A C5  
22915 C C6  . NAG P  .   ? 1.3896 1.3262 1.6335 0.0074  0.0461  0.0949  604 NAG A C6  
22916 C C7  . NAG P  .   ? 1.1415 1.1074 1.4008 0.0113  0.0049  0.1273  604 NAG A C7  
22917 C C8  . NAG P  .   ? 0.7886 0.7614 1.0485 0.0117  -0.0044 0.1315  604 NAG A C8  
22918 N N2  . NAG P  .   ? 1.3012 1.2622 1.5611 0.0118  0.0120  0.1218  604 NAG A N2  
22919 O O3  . NAG P  .   ? 1.3516 1.3006 1.6406 0.0153  0.0303  0.1275  604 NAG A O3  
22920 O O4  . NAG P  .   ? 1.5282 1.4628 1.8059 0.0124  0.0495  0.1111  604 NAG A O4  
22921 O O5  . NAG P  .   ? 1.4199 1.3685 1.6607 0.0087  0.0290  0.1015  604 NAG A O5  
22922 O O6  . NAG P  .   ? 1.2318 1.1692 1.4718 0.0062  0.0441  0.0964  604 NAG A O6  
22923 O O7  . NAG P  .   ? 1.1585 1.1232 1.4166 0.0105  0.0059  0.1288  604 NAG A O7  
22924 C C1  . NAG Q  .   ? 1.6252 1.5582 1.9209 0.0151  0.0526  0.1185  605 NAG A C1  
22925 C C2  . NAG Q  .   ? 1.5697 1.5019 1.8694 0.0164  0.0547  0.1166  605 NAG A C2  
22926 C C3  . NAG Q  .   ? 1.6210 1.5485 1.9391 0.0187  0.0622  0.1222  605 NAG A C3  
22927 C C4  . NAG Q  .   ? 1.7758 1.7080 2.1062 0.0206  0.0565  0.1329  605 NAG A C4  
22928 C C5  . NAG Q  .   ? 1.7571 1.6912 2.0810 0.0192  0.0528  0.1344  605 NAG A C5  
22929 C C6  . NAG Q  .   ? 1.4979 1.4372 1.8333 0.0210  0.0468  0.1453  605 NAG A C6  
22930 C C7  . NAG Q  .   ? 1.6160 1.5454 1.9006 0.0148  0.0588  0.1032  605 NAG A C7  
22931 C C8  . NAG Q  .   ? 1.5237 1.4513 1.7929 0.0124  0.0613  0.0932  605 NAG A C8  
22932 N N2  . NAG Q  .   ? 1.7104 1.6389 1.9981 0.0144  0.0595  0.1067  605 NAG A N2  
22933 O O3  . NAG Q  .   ? 1.4896 1.4153 1.8129 0.0199  0.0655  0.1207  605 NAG A O3  
22934 O O4  . NAG Q  .   ? 1.7861 1.7141 2.1342 0.0229  0.0636  0.1386  605 NAG A O4  
22935 O O5  . NAG Q  .   ? 1.7885 1.7262 2.0944 0.0168  0.0467  0.1282  605 NAG A O5  
22936 O O6  . NAG Q  .   ? 1.6506 1.5952 1.9924 0.0226  0.0409  0.1498  605 NAG A O6  
22937 O O7  . NAG Q  .   ? 1.5168 1.4486 1.8106 0.0169  0.0561  0.1079  605 NAG A O7  
22938 C C1  . NAG R  .   ? 1.6039 1.5900 1.7665 -0.0055 -0.0319 0.1099  606 NAG A C1  
22939 C C2  . NAG R  .   ? 1.6533 1.6435 1.8169 -0.0063 -0.0386 0.1170  606 NAG A C2  
22940 C C3  . NAG R  .   ? 1.7292 1.7205 1.9082 -0.0044 -0.0394 0.1265  606 NAG A C3  
22941 C C4  . NAG R  .   ? 1.7630 1.7487 1.9540 -0.0024 -0.0306 0.1275  606 NAG A C4  
22942 C C5  . NAG R  .   ? 1.6977 1.6801 1.8861 -0.0018 -0.0255 0.1199  606 NAG A C5  
22943 C C6  . NAG R  .   ? 1.6362 1.6128 1.8367 0.0001  -0.0165 0.1209  606 NAG A C6  
22944 C C7  . NAG R  .   ? 1.4433 1.4401 1.5841 -0.0100 -0.0494 0.1116  606 NAG A C7  
22945 C C8  . NAG R  .   ? 1.5598 1.5582 1.6895 -0.0108 -0.0514 0.1043  606 NAG A C8  
22946 N N2  . NAG R  .   ? 1.5078 1.5033 1.6619 -0.0078 -0.0465 0.1158  606 NAG A N2  
22947 O O3  . NAG R  .   ? 1.3074 1.3012 1.4871 -0.0054 -0.0436 0.1327  606 NAG A O3  
22948 O O4  . NAG R  .   ? 1.4690 1.4563 1.6749 -0.0004 -0.0317 0.1361  606 NAG A O4  
22949 O O5  . NAG R  .   ? 1.6011 1.5823 1.7753 -0.0038 -0.0243 0.1117  606 NAG A O5  
22950 O O6  . NAG R  .   ? 1.4116 1.3842 1.6115 -0.0007 -0.0114 0.1203  606 NAG A O6  
22951 O O7  . NAG R  .   ? 1.2702 1.2670 1.4081 -0.0112 -0.0503 0.1136  606 NAG A O7  
22952 C C1  . NAG S  .   ? 2.1684 2.2821 2.0250 -0.0441 -0.0346 -0.0601 601 NAG C C1  
22953 C C2  . NAG S  .   ? 2.2829 2.3964 2.1418 -0.0412 -0.0362 -0.0579 601 NAG C C2  
22954 C C3  . NAG S  .   ? 2.2344 2.3503 2.0934 -0.0386 -0.0358 -0.0577 601 NAG C C3  
22955 C C4  . NAG S  .   ? 2.2883 2.4122 2.1484 -0.0382 -0.0344 -0.0594 601 NAG C C4  
22956 C C5  . NAG S  .   ? 2.3156 2.4420 2.1752 -0.0411 -0.0332 -0.0614 601 NAG C C5  
22957 C C6  . NAG S  .   ? 2.3951 2.5314 2.2580 -0.0402 -0.0330 -0.0622 601 NAG C C6  
22958 C C7  . NAG S  .   ? 2.3144 2.4200 2.1743 -0.0397 -0.0391 -0.0545 601 NAG C C7  
22959 C C8  . NAG S  .   ? 2.0040 2.1031 1.8625 -0.0390 -0.0406 -0.0526 601 NAG C C8  
22960 N N2  . NAG S  .   ? 2.4525 2.5584 2.3100 -0.0417 -0.0376 -0.0562 601 NAG C N2  
22961 O O3  . NAG S  .   ? 2.5152 2.6322 2.3767 -0.0358 -0.0371 -0.0559 601 NAG C O3  
22962 O O4  . NAG S  .   ? 2.3858 2.5088 2.2440 -0.0373 -0.0332 -0.0598 601 NAG C O4  
22963 O O5  . NAG S  .   ? 2.2435 2.3657 2.1025 -0.0435 -0.0336 -0.0614 601 NAG C O5  
22964 O O6  . NAG S  .   ? 2.3499 2.4883 2.2157 -0.0385 -0.0344 -0.0606 601 NAG C O6  
22965 O O7  . NAG S  .   ? 2.2842 2.3949 2.1472 -0.0387 -0.0391 -0.0545 601 NAG C O7  
22966 C C1  . NAG T  .   ? 1.0251 1.1481 0.8929 -0.0647 -0.0236 -0.0766 602 NAG C C1  
22967 C C2  . NAG T  .   ? 0.9398 1.0582 0.8097 -0.0617 -0.0248 -0.0735 602 NAG C C2  
22968 C C3  . NAG T  .   ? 1.0912 1.2148 0.9616 -0.0606 -0.0252 -0.0736 602 NAG C C3  
22969 C C4  . NAG T  .   ? 0.9077 1.0373 0.7767 -0.0640 -0.0228 -0.0776 602 NAG C C4  
22970 C C5  . NAG T  .   ? 0.9818 1.1169 0.8490 -0.0659 -0.0229 -0.0797 602 NAG C C5  
22971 C C6  . NAG T  .   ? 0.9686 1.1116 0.8343 -0.0694 -0.0211 -0.0835 602 NAG C C6  
22972 C C7  . NAG T  .   ? 1.0774 1.1854 0.9490 -0.0573 -0.0283 -0.0674 602 NAG C C7  
22973 C C8  . NAG T  .   ? 0.8167 0.9217 0.6877 -0.0550 -0.0311 -0.0645 602 NAG C C8  
22974 N N2  . NAG T  .   ? 0.9522 1.0679 0.8222 -0.0586 -0.0278 -0.0701 602 NAG C N2  
22975 O O3  . NAG T  .   ? 0.8469 0.9645 0.7194 -0.0590 -0.0250 -0.0716 602 NAG C O3  
22976 O O4  . NAG T  .   ? 1.0232 1.1587 0.8922 -0.0627 -0.0238 -0.0773 602 NAG C O4  
22977 O O5  . NAG T  .   ? 1.2069 1.3357 1.0740 -0.0675 -0.0215 -0.0800 602 NAG C O5  
22978 O O6  . NAG T  .   ? 0.7731 0.9128 0.6383 -0.0733 -0.0179 -0.0865 602 NAG C O6  
22979 O O7  . NAG T  .   ? 1.3063 1.4096 1.1797 -0.0582 -0.0265 -0.0673 602 NAG C O7  
22980 C C1  . NAG U  .   ? 1.0949 1.2312 0.9636 -0.0654 -0.0209 -0.0799 603 NAG C C1  
22981 C C2  . NAG U  .   ? 1.0164 1.1601 0.8845 -0.0641 -0.0223 -0.0796 603 NAG C C2  
22982 C C3  . NAG U  .   ? 1.0648 1.2101 0.9319 -0.0671 -0.0194 -0.0824 603 NAG C C3  
22983 C C4  . NAG U  .   ? 1.2682 1.4037 1.1371 -0.0681 -0.0165 -0.0826 603 NAG C C4  
22984 C C5  . NAG U  .   ? 1.2057 1.3345 1.0756 -0.0689 -0.0156 -0.0825 603 NAG C C5  
22985 C C6  . NAG U  .   ? 0.9739 1.0932 0.8463 -0.0697 -0.0126 -0.0823 603 NAG C C6  
22986 C C7  . NAG U  .   ? 0.9710 1.1283 0.8405 -0.0602 -0.0264 -0.0765 603 NAG C C7  
22987 C C8  . NAG U  .   ? 0.9343 1.1018 0.8046 -0.0603 -0.0272 -0.0766 603 NAG C C8  
22988 N N2  . NAG U  .   ? 0.6945 0.8474 0.5620 -0.0639 -0.0239 -0.0798 603 NAG C N2  
22989 O O3  . NAG U  .   ? 1.4125 1.5632 1.2793 -0.0651 -0.0210 -0.0811 603 NAG C O3  
22990 O O4  . NAG U  .   ? 1.3249 1.4618 1.1924 -0.0722 -0.0130 -0.0864 603 NAG C O4  
22991 O O5  . NAG U  .   ? 1.1839 1.3117 1.0545 -0.0656 -0.0189 -0.0793 603 NAG C O5  
22992 O O6  . NAG U  .   ? 1.5308 1.6456 1.4056 -0.0660 -0.0141 -0.0786 603 NAG C O6  
22993 O O7  . NAG U  .   ? 0.9758 1.1290 0.8464 -0.0569 -0.0278 -0.0736 603 NAG C O7  
22994 C C1  . BMA V  .   ? 1.4619 1.5990 1.3294 -0.0720 -0.0119 -0.0865 604 BMA C C1  
22995 C C2  . BMA V  .   ? 1.3238 1.4633 1.1921 -0.0676 -0.0151 -0.0828 604 BMA C C2  
22996 C C3  . BMA V  .   ? 1.3135 1.4506 1.1821 -0.0679 -0.0130 -0.0832 604 BMA C C3  
22997 C C4  . BMA V  .   ? 1.5797 1.7172 1.4464 -0.0731 -0.0087 -0.0879 604 BMA C C4  
22998 C C5  . BMA V  .   ? 1.3945 1.5240 1.2631 -0.0752 -0.0058 -0.0892 604 BMA C C5  
22999 C C6  . BMA V  .   ? 1.4289 1.5611 1.2949 -0.0807 -0.0022 -0.0943 604 BMA C C6  
23000 O O2  . BMA V  .   ? 1.4918 1.6417 1.3577 -0.0674 -0.0175 -0.0831 604 BMA C O2  
23001 O O3  . BMA V  .   ? 1.5615 1.7057 1.4288 -0.0660 -0.0152 -0.0818 604 BMA C O3  
23002 O O4  . BMA V  .   ? 1.9120 2.0594 1.7752 -0.0759 -0.0094 -0.0906 604 BMA C O4  
23003 O O5  . BMA V  .   ? 1.4956 1.6237 1.3654 -0.0729 -0.0085 -0.0868 604 BMA C O5  
23004 O O6  . BMA V  .   ? 1.1390 1.2752 1.0037 -0.0819 -0.0036 -0.0953 604 BMA C O6  
23005 C C1  . NAG W  .   ? 1.1350 1.3147 1.0352 0.0410  -0.0236 0.0242  605 NAG C C1  
23006 C C2  . NAG W  .   ? 1.2163 1.3981 1.1128 0.0405  -0.0218 0.0256  605 NAG C C2  
23007 C C3  . NAG W  .   ? 1.0648 1.2587 0.9561 0.0392  -0.0230 0.0274  605 NAG C C3  
23008 C C4  . NAG W  .   ? 0.9816 1.1807 0.8696 0.0351  -0.0251 0.0239  605 NAG C C4  
23009 C C5  . NAG W  .   ? 1.1650 1.3606 1.0578 0.0365  -0.0265 0.0229  605 NAG C C5  
23010 C C6  . NAG W  .   ? 0.9939 1.1947 0.8841 0.0329  -0.0286 0.0197  605 NAG C C6  
23011 C C7  . NAG W  .   ? 1.0485 1.2171 0.9515 0.0456  -0.0181 0.0287  605 NAG C C7  
23012 C C8  . NAG W  .   ? 1.0538 1.2196 0.9612 0.0504  -0.0165 0.0331  605 NAG C C8  
23013 N N2  . NAG W  .   ? 1.1324 1.3105 1.0328 0.0450  -0.0202 0.0296  605 NAG C N2  
23014 O O3  . NAG W  .   ? 0.8699 1.0651 0.7567 0.0376  -0.0213 0.0278  605 NAG C O3  
23015 O O4  . NAG W  .   ? 1.1661 1.3772 1.0506 0.0347  -0.0267 0.0265  605 NAG C O4  
23016 O O5  . NAG W  .   ? 1.0232 1.2074 0.9196 0.0369  -0.0252 0.0207  605 NAG C O5  
23017 O O6  . NAG W  .   ? 1.2284 1.4239 1.1158 0.0284  -0.0278 0.0146  605 NAG C O6  
23018 O O7  . NAG W  .   ? 1.0731 1.2355 0.9755 0.0425  -0.0173 0.0247  605 NAG C O7  
23019 C C1  . NAG X  .   ? 1.1217 1.3380 0.9992 0.0299  -0.0265 0.0240  606 NAG C C1  
23020 C C2  . NAG X  .   ? 1.3200 1.5473 1.1952 0.0279  -0.0293 0.0240  606 NAG C C2  
23021 C C3  . NAG X  .   ? 1.4335 1.6699 1.3013 0.0235  -0.0297 0.0231  606 NAG C C3  
23022 C C4  . NAG X  .   ? 1.5641 1.8037 1.4301 0.0257  -0.0286 0.0276  606 NAG C C4  
23023 C C5  . NAG X  .   ? 1.4266 1.6545 1.2942 0.0269  -0.0255 0.0267  606 NAG C C5  
23024 C C6  . NAG X  .   ? 1.6984 1.9297 1.5646 0.0295  -0.0243 0.0316  606 NAG C C6  
23025 C C7  . NAG X  .   ? 1.4015 1.6331 1.2797 0.0267  -0.0328 0.0213  606 NAG C C7  
23026 C C8  . NAG X  .   ? 1.1235 1.3558 1.0001 0.0226  -0.0340 0.0165  606 NAG C C8  
23027 N N2  . NAG X  .   ? 1.4753 1.6996 1.3520 0.0260  -0.0304 0.0200  606 NAG C N2  
23028 O O3  . NAG X  .   ? 1.1400 1.3872 1.0067 0.0225  -0.0325 0.0239  606 NAG C O3  
23029 O O4  . NAG X  .   ? 1.2113 1.4598 1.0701 0.0215  -0.0290 0.0269  606 NAG C O4  
23030 O O5  . NAG X  .   ? 1.2939 1.5126 1.1686 0.0306  -0.0250 0.0269  606 NAG C O5  
23031 O O6  . NAG X  .   ? 1.7892 2.0296 1.6578 0.0331  -0.0264 0.0371  606 NAG C O6  
23032 O O7  . NAG X  .   ? 1.1599 1.3973 1.0409 0.0306  -0.0337 0.0262  606 NAG C O7  
23033 C C1  . NAG Y  .   ? 1.2213 1.2838 1.1371 0.0079  -0.0520 -0.0157 607 NAG C C1  
23034 C C2  . NAG Y  .   ? 1.3606 1.4201 1.2795 0.0096  -0.0508 -0.0147 607 NAG C C2  
23035 C C3  . NAG Y  .   ? 1.4011 1.4561 1.3181 0.0075  -0.0509 -0.0159 607 NAG C C3  
23036 C C4  . NAG Y  .   ? 1.6624 1.7195 1.5764 0.0074  -0.0492 -0.0173 607 NAG C C4  
23037 C C5  . NAG Y  .   ? 1.5843 1.6445 1.4952 0.0058  -0.0505 -0.0183 607 NAG C C5  
23038 C C6  . NAG Y  .   ? 1.8118 1.8752 1.7212 0.0070  -0.0480 -0.0193 607 NAG C C6  
23039 C C7  . NAG Y  .   ? 1.5737 1.6318 1.4996 0.0130  -0.0504 -0.0117 607 NAG C C7  
23040 C C8  . NAG Y  .   ? 1.4817 1.5391 1.4108 0.0136  -0.0513 -0.0102 607 NAG C C8  
23041 N N2  . NAG Y  .   ? 1.2407 1.2982 1.1630 0.0099  -0.0520 -0.0132 607 NAG C N2  
23042 O O3  . NAG Y  .   ? 1.2678 1.3203 1.1878 0.0091  -0.0494 -0.0151 607 NAG C O3  
23043 O O4  . NAG Y  .   ? 1.6486 1.7013 1.5606 0.0052  -0.0490 -0.0187 607 NAG C O4  
23044 O O5  . NAG Y  .   ? 1.3501 1.4139 1.2626 0.0071  -0.0511 -0.0173 607 NAG C O5  
23045 O O6  . NAG Y  .   ? 1.8620 1.9250 1.7742 0.0098  -0.0453 -0.0184 607 NAG C O6  
23046 O O7  . NAG Y  .   ? 1.5566 1.6156 1.4833 0.0153  -0.0479 -0.0114 607 NAG C O7  
23047 C C1  . NAG Z  .   ? 1.8782 1.8022 1.8530 -0.1223 0.1416  -0.0930 601 NAG E C1  
23048 C C2  . NAG Z  .   ? 2.1490 2.0811 2.1140 -0.1269 0.1401  -0.1014 601 NAG E C2  
23049 C C3  . NAG Z  .   ? 2.2172 2.1477 2.1813 -0.1322 0.1479  -0.1094 601 NAG E C3  
23050 C C4  . NAG Z  .   ? 2.2999 2.2263 2.2695 -0.1302 0.1506  -0.1077 601 NAG E C4  
23051 C C5  . NAG Z  .   ? 2.0148 1.9327 1.9946 -0.1254 0.1523  -0.0991 601 NAG E C5  
23052 C C6  . NAG Z  .   ? 2.0158 1.9302 2.0013 -0.1234 0.1548  -0.0974 601 NAG E C6  
23053 C C7  . NAG Z  .   ? 2.1017 2.0426 2.0555 -0.1312 0.1358  -0.1068 601 NAG E C7  
23054 C C8  . NAG Z  .   ? 1.5245 1.4648 1.4765 -0.1335 0.1373  -0.1079 601 NAG E C8  
23055 N N2  . NAG Z  .   ? 2.2802 2.2128 2.2424 -0.1289 0.1403  -0.1024 601 NAG E N2  
23056 O O3  . NAG Z  .   ? 1.9650 1.9048 1.9199 -0.1356 0.1445  -0.1161 601 NAG E O3  
23057 O O4  . NAG Z  .   ? 2.5024 2.4256 2.4721 -0.1354 0.1594  -0.1149 601 NAG E O4  
23058 O O5  . NAG Z  .   ? 1.6991 1.6200 1.6789 -0.1206 0.1439  -0.0918 601 NAG E O5  
23059 O O6  . NAG Z  .   ? 2.3817 2.3032 2.3603 -0.1250 0.1516  -0.1025 601 NAG E O6  
23060 O O7  . NAG Z  .   ? 1.9590 1.9078 1.9071 -0.1315 0.1308  -0.1097 601 NAG E O7  
23061 C C1  . NAG AA .   ? 1.5756 1.5141 1.4661 -0.1260 0.1933  -0.1434 602 NAG E C1  
23062 C C2  . NAG AA .   ? 1.5198 1.4516 1.4076 -0.1297 0.2025  -0.1471 602 NAG E C2  
23063 C C3  . NAG AA .   ? 1.7481 1.6664 1.6471 -0.1301 0.2129  -0.1483 602 NAG E C3  
23064 C C4  . NAG AA .   ? 1.7627 1.6769 1.6764 -0.1239 0.2103  -0.1424 602 NAG E C4  
23065 C C5  . NAG AA .   ? 1.6963 1.6176 1.6075 -0.1240 0.2034  -0.1422 602 NAG E C5  
23066 C C6  . NAG AA .   ? 1.7172 1.6401 1.6392 -0.1157 0.1952  -0.1340 602 NAG E C6  
23067 C C7  . NAG AA .   ? 1.7087 1.6435 1.5754 -0.1408 0.2103  -0.1570 602 NAG E C7  
23068 C C8  . NAG AA .   ? 1.4493 1.3901 1.3002 -0.1493 0.2124  -0.1641 602 NAG E C8  
23069 N N2  . NAG AA .   ? 1.6173 1.5535 1.4905 -0.1378 0.2056  -0.1544 602 NAG E N2  
23070 O O3  . NAG AA .   ? 1.6602 1.5731 1.5614 -0.1290 0.2177  -0.1474 602 NAG E O3  
23071 O O4  . NAG AA .   ? 1.7574 1.6596 1.6814 -0.1249 0.2204  -0.1438 602 NAG E O4  
23072 O O5  . NAG AA .   ? 1.7042 1.6366 1.6011 -0.1277 0.1979  -0.1454 602 NAG E O5  
23073 O O6  . NAG AA .   ? 1.6837 1.6081 1.6076 -0.1108 0.1914  -0.1293 602 NAG E O6  
23074 O O7  . NAG AA .   ? 1.7821 1.7111 1.6550 -0.1371 0.2128  -0.1538 602 NAG E O7  
23075 C C1  . NAG BA .   ? 1.6996 1.5945 1.6306 -0.1222 0.2254  -0.1414 603 NAG E C1  
23076 C C2  . NAG BA .   ? 1.8198 1.7037 1.7674 -0.1187 0.2314  -0.1382 603 NAG E C2  
23077 C C3  . NAG BA .   ? 1.6747 1.5515 1.6302 -0.1155 0.2361  -0.1353 603 NAG E C3  
23078 C C4  . NAG BA .   ? 1.8650 1.7400 1.8099 -0.1214 0.2432  -0.1415 603 NAG E C4  
23079 C C5  . NAG BA .   ? 1.9553 1.8420 1.8834 -0.1249 0.2364  -0.1446 603 NAG E C5  
23080 C C6  . NAG BA .   ? 2.1777 2.0631 2.0943 -0.1314 0.2433  -0.1510 603 NAG E C6  
23081 C C7  . NAG BA .   ? 2.0497 1.9316 2.0140 -0.1129 0.2265  -0.1316 603 NAG E C7  
23082 C C8  . NAG BA .   ? 1.5544 1.4382 1.5293 -0.1060 0.2186  -0.1240 603 NAG E C8  
23083 N N2  . NAG BA .   ? 2.0623 1.9490 2.0186 -0.1128 0.2234  -0.1318 603 NAG E N2  
23084 O O3  . NAG BA .   ? 1.6712 1.5373 1.6414 -0.1135 0.2434  -0.1333 603 NAG E O3  
23085 O O4  . NAG BA .   ? 1.7655 1.6360 1.7168 -0.1177 0.2455  -0.1381 603 NAG E O4  
23086 O O5  . NAG BA .   ? 1.7295 1.6212 1.6521 -0.1282 0.2335  -0.1475 603 NAG E O5  
23087 O O6  . NAG BA .   ? 2.5217 2.3953 2.4437 -0.1351 0.2557  -0.1550 603 NAG E O6  
23088 O O7  . NAG BA .   ? 2.0914 1.9673 2.0546 -0.1184 0.2353  -0.1372 603 NAG E O7  
23089 C C1  . NAG CA .   ? 0.3129 0.4980 0.2804 -0.1022 0.0116  -0.1193 604 NAG E C1  
23090 C C2  . NAG CA .   ? 0.3087 0.4940 0.2745 -0.0967 0.0078  -0.1139 604 NAG E C2  
23091 C C3  . NAG CA .   ? 0.3076 0.5027 0.2723 -0.0953 0.0005  -0.1126 604 NAG E C3  
23092 C C4  . NAG CA .   ? 0.3158 0.5163 0.2750 -0.1006 -0.0018 -0.1170 604 NAG E C4  
23093 C C5  . NAG CA .   ? 0.3191 0.5187 0.2808 -0.1059 0.0025  -0.1223 604 NAG E C5  
23094 C C6  . NAG CA .   ? 0.3282 0.5326 0.2838 -0.1117 0.0004  -0.1269 604 NAG E C6  
23095 C C7  . NAG CA .   ? 0.2989 0.4730 0.2711 -0.0893 0.0119  -0.1068 604 NAG E C7  
23096 C C8  . NAG CA .   ? 0.2911 0.4625 0.2701 -0.0852 0.0126  -0.1029 604 NAG E C8  
23097 N N2  . NAG CA .   ? 0.3007 0.4823 0.2731 -0.0922 0.0092  -0.1099 604 NAG E N2  
23098 O O3  . NAG CA .   ? 0.3062 0.5003 0.2673 -0.0912 -0.0024 -0.1083 604 NAG E O3  
23099 O O4  . NAG CA .   ? 0.3136 0.5240 0.2746 -0.0993 -0.0085 -0.1156 604 NAG E O4  
23100 O O5  . NAG CA .   ? 0.3208 0.5104 0.2820 -0.1068 0.0095  -0.1232 604 NAG E O5  
23101 O O6  . NAG CA .   ? 0.3361 0.5347 0.2825 -0.1139 0.0025  -0.1281 604 NAG E O6  
23102 O O7  . NAG CA .   ? 0.3037 0.4730 0.2705 -0.0900 0.0138  -0.1070 604 NAG E O7  
23103 C C1  . NAG DA .   ? 2.0658 2.1076 1.9535 -0.1235 0.0821  -0.1319 605 NAG E C1  
23104 C C2  . NAG DA .   ? 2.2498 2.2813 2.1439 -0.1242 0.0880  -0.1316 605 NAG E C2  
23105 C C3  . NAG DA .   ? 2.4279 2.4600 2.3184 -0.1309 0.0934  -0.1383 605 NAG E C3  
23106 C C4  . NAG DA .   ? 2.4725 2.5151 2.3567 -0.1326 0.0881  -0.1403 605 NAG E C4  
23107 C C5  . NAG DA .   ? 2.4259 2.4786 2.3052 -0.1302 0.0807  -0.1386 605 NAG E C5  
23108 C C6  . NAG DA .   ? 2.4065 2.4679 2.2820 -0.1303 0.0751  -0.1387 605 NAG E C6  
23109 C C7  . NAG DA .   ? 2.0318 2.0457 1.9397 -0.1193 0.0945  -0.1254 605 NAG E C7  
23110 C C8  . NAG DA .   ? 1.7353 1.7394 1.6492 -0.1198 0.1021  -0.1255 605 NAG E C8  
23111 N N2  . NAG DA .   ? 2.1793 2.2017 2.0791 -0.1230 0.0933  -0.1302 605 NAG E N2  
23112 O O3  . NAG DA .   ? 2.5565 2.5794 2.4532 -0.1311 0.0983  -0.1374 605 NAG E O3  
23113 O O4  . NAG DA .   ? 2.3699 2.4149 2.2493 -0.1396 0.0931  -0.1474 605 NAG E O4  
23114 O O5  . NAG DA .   ? 2.1885 2.2387 2.0717 -0.1239 0.0768  -0.1325 605 NAG E O5  
23115 O O6  . NAG DA .   ? 2.1899 2.2575 2.0644 -0.1252 0.0673  -0.1340 605 NAG E O6  
23116 O O7  . NAG DA .   ? 2.0224 2.0366 1.9328 -0.1157 0.0898  -0.1209 605 NAG E O7  
23117 C C1  . NAG EA .   ? 2.4184 2.4697 2.2706 -0.1271 0.0427  -0.1084 601 NAG F C1  
23118 C C2  . NAG EA .   ? 2.3678 2.4265 2.2207 -0.1309 0.0454  -0.1149 601 NAG F C2  
23119 C C3  . NAG EA .   ? 2.1979 2.2660 2.0486 -0.1304 0.0418  -0.1169 601 NAG F C3  
23120 C C4  . NAG EA .   ? 2.2090 2.2755 2.0565 -0.1286 0.0394  -0.1139 601 NAG F C4  
23121 C C5  . NAG EA .   ? 2.3306 2.3894 2.1771 -0.1251 0.0368  -0.1078 601 NAG F C5  
23122 C C6  . NAG EA .   ? 2.3430 2.3994 2.1858 -0.1242 0.0353  -0.1053 601 NAG F C6  
23123 C C7  . NAG EA .   ? 2.2201 2.2741 2.0785 -0.1329 0.0509  -0.1170 601 NAG F C7  
23124 C C8  . NAG EA .   ? 2.0200 2.0744 1.8808 -0.1318 0.0503  -0.1168 601 NAG F C8  
23125 N N2  . NAG EA .   ? 2.3149 2.3755 2.1705 -0.1316 0.0467  -0.1171 601 NAG F N2  
23126 O O3  . NAG EA .   ? 1.9839 2.0583 1.8353 -0.1344 0.0448  -0.1226 601 NAG F O3  
23127 O O4  . NAG EA .   ? 2.0526 2.1277 1.8988 -0.1274 0.0357  -0.1152 601 NAG F O4  
23128 O O5  . NAG EA .   ? 2.5013 2.5519 2.3499 -0.1258 0.0402  -0.1060 601 NAG F O5  
23129 O O6  . NAG EA .   ? 2.3166 2.3708 2.1591 -0.1276 0.0397  -0.1077 601 NAG F O6  
23130 O O7  . NAG EA .   ? 2.2227 2.2707 2.0820 -0.1350 0.0552  -0.1171 601 NAG F O7  
23131 C C1  . NAG FA .   ? 2.1211 2.0105 1.8742 -0.1998 0.0020  -0.1407 601 NAG G C1  
23132 C C2  . NAG FA .   ? 2.2477 2.1302 1.9936 -0.2093 0.0077  -0.1480 601 NAG G C2  
23133 C C3  . NAG FA .   ? 2.2293 2.1153 1.9752 -0.2156 0.0018  -0.1481 601 NAG G C3  
23134 C C4  . NAG FA .   ? 2.2388 2.1342 1.9818 -0.2176 -0.0101 -0.1428 601 NAG G C4  
23135 C C5  . NAG FA .   ? 2.3042 2.2051 2.0550 -0.2073 -0.0141 -0.1358 601 NAG G C5  
23136 C C6  . NAG FA .   ? 2.3558 2.2654 2.1034 -0.2096 -0.0256 -0.1307 601 NAG G C6  
23137 C C7  . NAG FA .   ? 2.2613 2.1287 2.0075 -0.2070 0.0271  -0.1563 601 NAG G C7  
23138 C C8  . NAG FA .   ? 2.0138 1.8730 1.7662 -0.2041 0.0384  -0.1601 601 NAG G C8  
23139 N N2  . NAG FA .   ? 2.4228 2.2973 2.1743 -0.2056 0.0187  -0.1516 601 NAG G N2  
23140 O O3  . NAG FA .   ? 2.0157 1.8961 1.7525 -0.2259 0.0059  -0.1551 601 NAG G O3  
23141 O O4  . NAG FA .   ? 1.9096 1.8092 1.6556 -0.2214 -0.0158 -0.1415 601 NAG G O4  
23142 O O5  . NAG FA .   ? 2.1303 2.0273 1.8789 -0.2032 -0.0085 -0.1368 601 NAG G O5  
23143 O O6  . NAG FA .   ? 2.1012 2.0124 1.8448 -0.2067 -0.0271 -0.1285 601 NAG G O6  
23144 O O7  . NAG FA .   ? 2.0947 1.9622 1.8318 -0.2104 0.0260  -0.1575 601 NAG G O7  
23145 C C1  . NAG GA .   ? 2.2373 2.1753 2.1246 -0.0516 0.0151  -0.0708 602 NAG G C1  
23146 C C2  . NAG GA .   ? 2.4262 2.3586 2.3185 -0.0501 0.0231  -0.0724 602 NAG G C2  
23147 C C3  . NAG GA .   ? 2.4819 2.4133 2.3779 -0.0446 0.0303  -0.0718 602 NAG G C3  
23148 C C4  . NAG GA .   ? 2.5360 2.4745 2.4360 -0.0379 0.0275  -0.0670 602 NAG G C4  
23149 C C5  . NAG GA .   ? 2.5737 2.5163 2.4672 -0.0412 0.0200  -0.0669 602 NAG G C5  
23150 C C6  . NAG GA .   ? 2.4500 2.3994 2.3459 -0.0356 0.0171  -0.0628 602 NAG G C6  
23151 C C7  . NAG GA .   ? 2.3828 2.3045 2.2742 -0.0576 0.0297  -0.0786 602 NAG G C7  
23152 C C8  . NAG GA .   ? 2.2362 2.1503 2.1231 -0.0638 0.0355  -0.0842 602 NAG G C8  
23153 N N2  . NAG GA .   ? 2.3360 2.2619 2.2233 -0.0573 0.0257  -0.0774 602 NAG G N2  
23154 O O3  . NAG GA .   ? 2.6243 2.5516 2.5268 -0.0418 0.0369  -0.0720 602 NAG G O3  
23155 O O4  . NAG GA .   ? 2.2785 2.2166 2.1811 -0.0338 0.0335  -0.0667 602 NAG G O4  
23156 O O5  . NAG GA .   ? 2.4970 2.4404 2.3897 -0.0443 0.0143  -0.0664 602 NAG G O5  
23157 O O6  . NAG GA .   ? 2.3011 2.2551 2.2007 -0.0330 0.0116  -0.0592 602 NAG G O6  
23158 O O7  . NAG GA .   ? 2.4674 2.3912 2.3659 -0.0533 0.0288  -0.0754 602 NAG G O7  
23159 C C1  . NAG HA .   ? 1.9289 1.8896 1.9402 -0.1537 -0.0519 -0.0737 603 NAG G C1  
23160 C C2  . NAG HA .   ? 2.1213 2.0898 2.1270 -0.1609 -0.0614 -0.0723 603 NAG G C2  
23161 C C3  . NAG HA .   ? 2.2756 2.2503 2.2880 -0.1667 -0.0670 -0.0709 603 NAG G C3  
23162 C C4  . NAG HA .   ? 2.1318 2.1091 2.1568 -0.1588 -0.0679 -0.0652 603 NAG G C4  
23163 C C5  . NAG HA .   ? 2.0690 2.0381 2.0990 -0.1527 -0.0583 -0.0673 603 NAG G C5  
23164 C C6  . NAG HA .   ? 1.9941 1.9658 2.0362 -0.1448 -0.0593 -0.0614 603 NAG G C6  
23165 C C7  . NAG HA .   ? 2.3634 2.3344 2.3493 -0.1733 -0.0670 -0.0770 603 NAG G C7  
23166 C C8  . NAG HA .   ? 2.0442 2.0106 2.0177 -0.1759 -0.0638 -0.0813 603 NAG G C8  
23167 N N2  . NAG HA .   ? 2.2280 2.1937 2.2216 -0.1681 -0.0600 -0.0778 603 NAG G N2  
23168 O O3  . NAG HA .   ? 2.2982 2.2809 2.3061 -0.1731 -0.0760 -0.0690 603 NAG G O3  
23169 O O4  . NAG HA .   ? 1.9563 1.9404 1.9881 -0.1636 -0.0739 -0.0630 603 NAG G O4  
23170 O O5  . NAG HA .   ? 2.0471 2.0095 2.0704 -0.1482 -0.0520 -0.0695 603 NAG G O5  
23171 O O6  . NAG HA .   ? 1.7534 1.7320 1.7961 -0.1422 -0.0668 -0.0557 603 NAG G O6  
23172 O O7  . NAG HA .   ? 2.5310 2.5103 2.5196 -0.1760 -0.0755 -0.0728 603 NAG G O7  
23173 C C1  . NAG IA .   ? 1.0381 1.0742 0.9897 -0.0060 -0.0739 0.0024  601 NAG I C1  
23174 C C2  . NAG IA .   ? 1.0625 1.0975 1.0165 -0.0050 -0.0738 0.0027  601 NAG I C2  
23175 C C3  . NAG IA .   ? 1.0975 1.1322 1.0573 -0.0021 -0.0717 0.0038  601 NAG I C3  
23176 C C4  . NAG IA .   ? 1.0863 1.1206 1.0509 -0.0019 -0.0715 0.0057  601 NAG I C4  
23177 C C5  . NAG IA .   ? 0.9867 1.0222 0.9481 -0.0030 -0.0714 0.0049  601 NAG I C5  
23178 C C6  . NAG IA .   ? 0.9130 0.9475 0.8797 -0.0032 -0.0713 0.0071  601 NAG I C6  
23179 C C7  . NAG IA .   ? 1.1874 1.2215 1.1356 -0.0058 -0.0739 0.0002  601 NAG I C7  
23180 C C8  . NAG IA .   ? 0.9717 1.0061 0.9169 -0.0045 -0.0718 -0.0019 601 NAG I C8  
23181 N N2  . NAG IA .   ? 0.9918 1.0276 0.9409 -0.0044 -0.0726 0.0004  601 NAG I N2  
23182 O O3  . NAG IA .   ? 0.9524 0.9853 0.9153 -0.0022 -0.0727 0.0049  601 NAG I O3  
23183 O O4  . NAG IA .   ? 1.2124 1.2470 1.1802 0.0011  -0.0685 0.0057  601 NAG I O4  
23184 O O5  . NAG IA .   ? 1.0442 1.0797 1.0013 -0.0058 -0.0740 0.0045  601 NAG I O5  
23185 O O6  . NAG IA .   ? 1.2384 1.2710 1.2108 -0.0039 -0.0734 0.0098  601 NAG I O6  
23186 O O7  . NAG IA .   ? 1.1776 1.2102 1.1278 -0.0081 -0.0768 0.0018  601 NAG I O7  
23187 C C1  . NAG JA .   ? 1.1696 1.2025 1.1445 0.0015  -0.0685 0.0082  602 NAG I C1  
23188 C C2  . NAG JA .   ? 1.2180 1.2514 1.1951 0.0045  -0.0649 0.0077  602 NAG I C2  
23189 C C3  . NAG JA .   ? 1.4891 1.5204 1.4738 0.0054  -0.0644 0.0101  602 NAG I C3  
23190 C C4  . NAG JA .   ? 1.6761 1.7060 1.6636 0.0047  -0.0667 0.0114  602 NAG I C4  
23191 C C5  . NAG JA .   ? 1.3636 1.3933 1.3495 0.0015  -0.0705 0.0122  602 NAG I C5  
23192 C C6  . NAG JA .   ? 1.5532 1.5817 1.5413 0.0004  -0.0729 0.0133  602 NAG I C6  
23193 C C7  . NAG JA .   ? 1.5412 1.5785 1.5123 0.0072  -0.0601 0.0044  602 NAG I C7  
23194 C C8  . NAG JA .   ? 1.4852 1.5245 1.4538 0.0074  -0.0578 0.0030  602 NAG I C8  
23195 N N2  . NAG JA .   ? 1.4694 1.5047 1.4432 0.0050  -0.0627 0.0061  602 NAG I N2  
23196 O O3  . NAG JA .   ? 1.6795 1.7112 1.6656 0.0080  -0.0609 0.0095  602 NAG I O3  
23197 O O4  . NAG JA .   ? 1.7403 1.7685 1.7350 0.0059  -0.0659 0.0135  602 NAG I O4  
23198 O O5  . NAG JA .   ? 1.1659 1.1971 1.1444 0.0005  -0.0709 0.0099  602 NAG I O5  
23199 O O6  . NAG JA .   ? 1.8376 1.8660 1.8240 0.0022  -0.0710 0.0116  602 NAG I O6  
23200 O O7  . NAG JA .   ? 1.6290 1.6665 1.5996 0.0087  -0.0594 0.0041  602 NAG I O7  
23201 C C1  . BMA KA .   ? 1.7333 1.7604 1.7338 0.0048  -0.0670 0.0160  603 BMA I C1  
23202 C C2  . BMA KA .   ? 1.8049 1.8305 1.8124 0.0069  -0.0647 0.0174  603 BMA I C2  
23203 C C3  . BMA KA .   ? 1.7532 1.7777 1.7649 0.0065  -0.0667 0.0190  603 BMA I C3  
23204 C C4  . BMA KA .   ? 1.7006 1.7249 1.7158 0.0038  -0.0706 0.0216  603 BMA I C4  
23205 C C5  . BMA KA .   ? 1.7460 1.7716 1.7553 0.0015  -0.0727 0.0208  603 BMA I C5  
23206 C C6  . BMA KA .   ? 1.6025 1.6278 1.6152 0.0006  -0.0731 0.0229  603 BMA I C6  
23207 O O2  . BMA KA .   ? 1.7256 1.7501 1.7383 0.0068  -0.0638 0.0193  603 BMA I O2  
23208 O O3  . BMA KA .   ? 1.5057 1.5287 1.5236 0.0086  -0.0643 0.0202  603 BMA I O3  
23209 O O4  . BMA KA .   ? 1.4522 1.4754 1.4750 0.0044  -0.0696 0.0241  603 BMA I O4  
23210 O O5  . BMA KA .   ? 1.7954 1.8222 1.7969 0.0022  -0.0710 0.0176  603 BMA I O5  
23211 O O6  . BMA KA .   ? 1.3628 1.3886 1.3759 -0.0023 -0.0774 0.0249  603 BMA I O6  
23212 C C1  . NAG LA .   ? 1.4230 1.5005 1.4115 0.1120  0.0353  0.0851  604 NAG I C1  
23213 C C2  . NAG LA .   ? 1.3478 1.4239 1.3347 0.1128  0.0382  0.0873  604 NAG I C2  
23214 C C3  . NAG LA .   ? 1.5335 1.6156 1.5127 0.1101  0.0363  0.0867  604 NAG I C3  
23215 C C4  . NAG LA .   ? 1.7481 1.8282 1.7256 0.1055  0.0330  0.0807  604 NAG I C4  
23216 C C5  . NAG LA .   ? 1.5533 1.6362 1.5321 0.1054  0.0302  0.0796  604 NAG I C5  
23217 C C6  . NAG LA .   ? 1.4250 1.5074 1.4014 0.1009  0.0266  0.0741  604 NAG I C6  
23218 C C7  . NAG LA .   ? 1.3112 1.3809 1.3064 0.1193  0.0452  0.0937  604 NAG I C7  
23219 C C8  . NAG LA .   ? 1.1739 1.2444 1.1728 0.1242  0.0488  0.0994  604 NAG I C8  
23220 N N2  . NAG LA .   ? 1.2192 1.2964 1.2086 0.1173  0.0417  0.0930  604 NAG I N2  
23221 O O3  . NAG LA .   ? 1.5214 1.6007 1.4996 0.1106  0.0393  0.0882  604 NAG I O3  
23222 O O4  . NAG LA .   ? 1.8828 1.9664 1.8539 0.1019  0.0312  0.0784  604 NAG I O4  
23223 O O5  . NAG LA .   ? 1.6499 1.7270 1.6356 0.1077  0.0319  0.0799  604 NAG I O5  
23224 O O6  . NAG LA .   ? 1.3065 1.3804 1.2864 0.0991  0.0274  0.0707  604 NAG I O6  
23225 O O7  . NAG LA .   ? 1.5307 1.5929 1.5285 0.1172  0.0457  0.0900  604 NAG I O7  
23226 C C1  . NAG MA .   ? 1.7798 1.8691 1.7449 0.1021  0.0323  0.0813  605 NAG I C1  
23227 C C2  . NAG MA .   ? 1.7162 1.8158 1.6754 0.1013  0.0293  0.0826  605 NAG I C2  
23228 C C3  . NAG MA .   ? 1.6046 1.7095 1.5564 0.0999  0.0300  0.0841  605 NAG I C3  
23229 C C4  . NAG MA .   ? 1.6976 1.7998 1.6505 0.1027  0.0340  0.0881  605 NAG I C4  
23230 C C5  . NAG MA .   ? 1.6620 1.7537 1.6224 0.1043  0.0370  0.0871  605 NAG I C5  
23231 C C6  . NAG MA .   ? 1.7048 1.7953 1.6669 0.1081  0.0409  0.0923  605 NAG I C6  
23232 C C7  . NAG MA .   ? 1.6723 1.7801 1.6274 0.0973  0.0228  0.0781  605 NAG I C7  
23233 C C8  . NAG MA .   ? 1.6184 1.7265 1.5712 0.0931  0.0195  0.0729  605 NAG I C8  
23234 N N2  . NAG MA .   ? 1.8424 1.9426 1.8004 0.0979  0.0258  0.0778  605 NAG I N2  
23235 O O3  . NAG MA .   ? 1.6223 1.7376 1.5695 0.1002  0.0277  0.0869  605 NAG I O3  
23236 O O4  . NAG MA .   ? 1.6909 1.7947 1.6374 0.0999  0.0348  0.0873  605 NAG I O4  
23237 O O5  . NAG MA .   ? 1.6977 1.7864 1.6641 0.1056  0.0358  0.0861  605 NAG I O5  
23238 O O6  . NAG MA .   ? 1.6635 1.7608 1.6258 0.1117  0.0407  0.0975  605 NAG I O6  
23239 O O7  . NAG MA .   ? 1.7176 1.8322 1.6721 0.1001  0.0228  0.0826  605 NAG I O7  
23240 C C1  . NAG NA .   ? 1.2481 1.3603 1.3232 -0.0844 -0.2040 0.1270  601 NAG K C1  
23241 C C2  . NAG NA .   ? 1.4977 1.6137 1.5841 -0.0847 -0.2058 0.1293  601 NAG K C2  
23242 C C3  . NAG NA .   ? 1.5239 1.6389 1.6256 -0.0786 -0.2022 0.1332  601 NAG K C3  
23243 C C4  . NAG NA .   ? 1.7082 1.8261 1.8163 -0.0770 -0.2039 0.1410  601 NAG K C4  
23244 C C5  . NAG NA .   ? 1.7399 1.8534 1.8372 -0.0762 -0.2014 0.1383  601 NAG K C5  
23245 C C6  . NAG NA .   ? 1.5504 1.6681 1.6521 -0.0765 -0.2048 0.1465  601 NAG K C6  
23246 C C7  . NAG NA .   ? 1.4447 1.5611 1.5300 -0.0888 -0.2064 0.1223  601 NAG K C7  
23247 C C8  . NAG NA .   ? 1.1900 1.3016 1.2758 -0.0866 -0.2015 0.1157  601 NAG K C8  
23248 N N2  . NAG NA .   ? 1.3721 1.4849 1.4524 -0.0861 -0.2036 0.1218  601 NAG K N2  
23249 O O3  . NAG NA .   ? 1.3241 1.4431 1.4363 -0.0792 -0.2042 0.1356  601 NAG K O3  
23250 O O4  . NAG NA .   ? 1.3504 1.4674 1.4731 -0.0716 -0.2004 0.1448  601 NAG K O4  
23251 O O5  . NAG NA .   ? 1.5223 1.6342 1.6037 -0.0805 -0.2025 0.1323  601 NAG K O5  
23252 O O6  . NAG NA .   ? 1.2149 1.3400 1.3280 -0.0782 -0.2100 0.1540  601 NAG K O6  
23253 O O7  . NAG NA .   ? 1.0524 1.1760 1.1420 -0.0928 -0.2126 0.1279  601 NAG K O7  
23254 C C1  . NAG OA .   ? 1.3633 1.4283 1.3445 -0.1250 -0.1697 0.0263  602 NAG K C1  
23255 C C2  . NAG OA .   ? 1.4423 1.5114 1.4283 -0.1305 -0.1732 0.0269  602 NAG K C2  
23256 C C3  . NAG OA .   ? 1.5439 1.6080 1.5244 -0.1338 -0.1688 0.0197  602 NAG K C3  
23257 C C4  . NAG OA .   ? 1.5713 1.6285 1.5541 -0.1265 -0.1611 0.0163  602 NAG K C4  
23258 C C5  . NAG OA .   ? 1.5397 1.5935 1.5153 -0.1228 -0.1585 0.0153  602 NAG K C5  
23259 C C6  . NAG OA .   ? 1.2001 1.2470 1.1760 -0.1163 -0.1506 0.0113  602 NAG K C6  
23260 C C7  . NAG OA .   ? 1.6328 1.7153 1.6246 -0.1393 -0.1861 0.0358  602 NAG K C7  
23261 C C8  . NAG OA .   ? 1.2614 1.3512 1.2515 -0.1437 -0.1937 0.0415  602 NAG K C8  
23262 N N2  . NAG OA .   ? 1.6633 1.7390 1.6461 -0.1371 -0.1806 0.0305  602 NAG K N2  
23263 O O3  . NAG OA .   ? 1.7514 1.8189 1.7377 -0.1380 -0.1714 0.0203  602 NAG K O3  
23264 O O4  . NAG OA .   ? 1.4096 1.4621 1.3888 -0.1290 -0.1566 0.0101  602 NAG K O4  
23265 O O5  . NAG OA .   ? 1.4210 1.4791 1.4017 -0.1197 -0.1623 0.0216  602 NAG K O5  
23266 O O6  . NAG OA .   ? 0.8543 0.9016 0.8421 -0.1104 -0.1492 0.0144  602 NAG K O6  
23267 O O7  . NAG OA .   ? 1.7291 1.8122 1.7306 -0.1377 -0.1851 0.0363  602 NAG K O7  
23268 C C1  . NAG PA .   ? 1.4296 1.4313 1.5633 0.0221  -0.0428 0.0492  603 NAG K C1  
23269 C C2  . NAG PA .   ? 1.3287 1.3308 1.4503 0.0222  -0.0419 0.0455  603 NAG K C2  
23270 C C3  . NAG PA .   ? 1.7582 1.7588 1.8794 0.0227  -0.0383 0.0450  603 NAG K C3  
23271 C C4  . NAG PA .   ? 1.9002 1.8977 2.0294 0.0244  -0.0331 0.0461  603 NAG K C4  
23272 C C5  . NAG PA .   ? 1.7615 1.7587 1.9024 0.0245  -0.0343 0.0497  603 NAG K C5  
23273 C C6  . NAG PA .   ? 1.7728 1.7665 1.9196 0.0266  -0.0284 0.0498  603 NAG K C6  
23274 C C7  . NAG PA .   ? 1.0289 1.0349 1.1354 0.0198  -0.0480 0.0422  603 NAG K C7  
23275 C C8  . NAG PA .   ? 1.1683 1.1770 1.2696 0.0173  -0.0532 0.0421  603 NAG K C8  
23276 N N2  . NAG PA .   ? 1.2034 1.2083 1.3194 0.0200  -0.0470 0.0452  603 NAG K N2  
23277 O O3  . NAG PA .   ? 1.7432 1.7440 1.8536 0.0232  -0.0365 0.0413  603 NAG K O3  
23278 O O4  . NAG PA .   ? 1.6693 1.6655 1.7998 0.0242  -0.0306 0.0463  603 NAG K O4  
23279 O O5  . NAG PA .   ? 1.5568 1.5555 1.6962 0.0241  -0.0375 0.0495  603 NAG K O5  
23280 O O6  . NAG PA .   ? 1.8233 1.8161 1.9632 0.0280  -0.0258 0.0467  603 NAG K O6  
23281 O O7  . NAG PA .   ? 1.1293 1.1342 1.2312 0.0216  -0.0449 0.0398  603 NAG K O7  
23282 C C1  . NAG QA .   ? 1.6121 1.6387 1.7434 -0.0009 -0.0881 0.0646  604 NAG K C1  
23283 C C2  . NAG QA .   ? 1.7014 1.7292 1.8344 -0.0015 -0.0894 0.0676  604 NAG K C2  
23284 C C3  . NAG QA .   ? 1.8012 1.8276 1.9451 0.0009  -0.0860 0.0710  604 NAG K C3  
23285 C C4  . NAG QA .   ? 1.6968 1.7193 1.8418 0.0042  -0.0798 0.0682  604 NAG K C4  
23286 C C5  . NAG QA .   ? 1.6904 1.7127 1.8345 0.0043  -0.0798 0.0661  604 NAG K C5  
23287 C C6  . NAG QA .   ? 1.8939 1.9125 2.0391 0.0076  -0.0736 0.0636  604 NAG K C6  
23288 C C7  . NAG QA .   ? 1.4952 1.5284 1.6211 -0.0072 -0.0986 0.0701  604 NAG K C7  
23289 C C8  . NAG QA .   ? 1.6065 1.6439 1.7355 -0.0106 -0.1046 0.0746  604 NAG K C8  
23290 N N2  . NAG QA .   ? 1.4739 1.5057 1.6082 -0.0050 -0.0956 0.0709  604 NAG K N2  
23291 O O3  . NAG QA .   ? 1.6757 1.7019 1.8184 0.0009  -0.0856 0.0723  604 NAG K O3  
23292 O O4  . NAG QA .   ? 1.7407 1.7621 1.8971 0.0060  -0.0769 0.0717  604 NAG K O4  
23293 O O5  . NAG QA .   ? 1.5771 1.6002 1.7100 0.0025  -0.0822 0.0626  604 NAG K O5  
23294 O O6  . NAG QA .   ? 1.6389 1.6556 1.7739 0.0088  -0.0706 0.0596  604 NAG K O6  
23295 O O7  . NAG QA .   ? 1.3282 1.3596 1.4443 -0.0067 -0.0967 0.0661  604 NAG K O7  
23296 C C1  . NAG RA .   ? 2.0805 2.1192 2.0073 -0.0653 -0.1348 0.0730  601 NAG L C1  
23297 C C2  . NAG RA .   ? 2.0544 2.0933 1.9925 -0.0615 -0.1331 0.0741  601 NAG L C2  
23298 C C3  . NAG RA .   ? 1.9782 2.0174 1.9273 -0.0595 -0.1326 0.0806  601 NAG L C3  
23299 C C4  . NAG RA .   ? 2.1833 2.2251 2.1321 -0.0626 -0.1378 0.0873  601 NAG L C4  
23300 C C5  . NAG RA .   ? 2.1898 2.2307 2.1273 -0.0656 -0.1382 0.0855  601 NAG L C5  
23301 C C6  . NAG RA .   ? 2.2725 2.3161 2.2113 -0.0683 -0.1430 0.0932  601 NAG L C6  
23302 C C7  . NAG RA .   ? 1.9762 2.0121 1.9070 -0.0590 -0.1271 0.0620  601 NAG L C7  
23303 C C8  . NAG RA .   ? 1.6946 1.7282 1.6181 -0.0587 -0.1230 0.0562  601 NAG L C8  
23304 N N2  . NAG RA .   ? 1.9744 2.0107 1.9119 -0.0586 -0.1278 0.0679  601 NAG L N2  
23305 O O3  . NAG RA .   ? 1.8321 1.8720 1.7911 -0.0568 -0.1322 0.0821  601 NAG L O3  
23306 O O4  . NAG RA .   ? 2.1233 2.1655 2.0824 -0.0607 -0.1372 0.0938  601 NAG L O4  
23307 O O5  . NAG RA .   ? 2.2160 2.2569 2.1436 -0.0679 -0.1392 0.0797  601 NAG L O5  
23308 O O6  . NAG RA .   ? 2.3790 2.4259 2.3258 -0.0681 -0.1467 0.0978  601 NAG L O6  
23309 O O7  . NAG RA .   ? 1.6873 1.7246 1.6180 -0.0598 -0.1295 0.0614  601 NAG L O7  
23310 O O   . HOH SA .   ? 0.4429 0.4320 0.4721 0.0028  0.0296  -0.0072 334 HOH A O   
23311 O O   . HOH SA .   ? 0.9523 0.8669 1.2593 0.0222  0.0845  0.0865  335 HOH A O   
23312 O O   . HOH SA .   ? 0.6661 0.6480 0.6986 0.0264  0.0480  0.0049  336 HOH A O   
23313 O O   . HOH SA .   ? 0.6159 0.5343 0.9179 0.0206  0.0782  0.0900  337 HOH A O   
23314 O O   . HOH SA .   ? 0.6371 0.6531 0.5621 -0.0586 -0.0963 0.0653  338 HOH A O   
23315 O O   . HOH SA .   ? 0.7843 0.7662 0.9263 0.0199  -0.0063 0.0459  339 HOH A O   
23316 O O   . HOH SA .   ? 0.9975 0.8412 1.1785 -0.0167 0.2020  -0.0203 340 HOH A O   
23317 O O   . HOH SA .   ? 1.1043 1.0517 1.3537 0.0393  0.0421  0.0623  341 HOH A O   
23318 O O   . HOH SA .   ? 1.2630 1.1743 1.2969 -0.0214 0.1495  -0.0418 342 HOH A O   
23319 O O   . HOH SA .   ? 0.9926 0.8898 1.2054 0.0333  0.1211  0.0296  343 HOH A O   
23320 O O   . HOH SA .   ? 0.5007 0.4909 0.5235 0.0072  0.0348  -0.0076 344 HOH A O   
23321 O O   . HOH SA .   ? 0.5841 0.4802 0.6737 -0.0348 0.1482  -0.0393 345 HOH A O   
23322 O O   . HOH SA .   ? 0.9777 0.9075 1.0179 -0.0249 0.1197  -0.0397 346 HOH A O   
23323 O O   . HOH SA .   ? 0.6754 0.6952 0.5547 -0.0591 -0.0783 0.0143  347 HOH A O   
23324 O O   . HOH SA .   ? 0.6080 0.6646 0.6025 -0.0659 -0.1548 0.1550  348 HOH A O   
23325 O O   . HOH SA .   ? 0.8038 0.8073 0.8039 -0.0371 -0.0644 0.0651  349 HOH A O   
23326 O O   . HOH SA .   ? 0.7591 0.7871 0.6608 -0.0453 -0.0782 0.0078  350 HOH A O   
23327 O O   . HOH SA .   ? 0.8686 0.8716 1.0336 -0.0093 -0.0581 0.1371  351 HOH A O   
23328 O O   . HOH SA .   ? 0.5816 0.5627 0.7160 0.0357  -0.0020 0.0399  353 HOH A O   
23329 O O   . HOH SA .   ? 0.7664 0.7097 0.8136 -0.0163 0.0956  -0.0282 354 HOH A O   
23330 O O   . HOH SA .   ? 0.4919 0.4475 0.7361 0.0073  0.0168  0.1191  355 HOH A O   
23331 O O   . HOH SA .   ? 0.5315 0.5288 0.6482 -0.0156 -0.0530 0.1088  356 HOH A O   
23332 O O   . HOH SA .   ? 0.4932 0.4493 0.5340 -0.0088 0.0793  -0.0219 357 HOH A O   
23333 O O   . HOH SA .   ? 1.3102 1.1752 1.4763 0.0206  0.1757  0.0035  358 HOH A O   
23334 O O   . HOH SA .   ? 1.3513 1.1952 1.6374 0.0191  0.1902  0.0263  359 HOH A O   
23335 O O   . HOH SA .   ? 0.8157 0.8350 0.9113 -0.0133 -0.0812 0.0880  360 HOH A O   
23336 O O   . HOH SA .   ? 0.6588 0.6411 0.7144 -0.0219 -0.0138 0.0401  361 HOH A O   
23337 O O   . HOH SA .   ? 1.2585 1.2020 1.5443 0.0282  0.0458  0.0848  362 HOH A O   
23338 O O   . HOH SA .   ? 0.7018 0.6303 0.9769 0.0184  0.0636  0.0837  363 HOH A O   
23339 O O   . HOH SA .   ? 0.7391 0.7208 0.9097 0.0183  -0.0106 0.0604  364 HOH A O   
23340 O O   . HOH SA .   ? 0.6376 0.6679 0.5618 -0.0367 -0.0866 0.0151  365 HOH A O   
23341 O O   . HOH SA .   ? 0.8925 0.8144 0.9475 0.0065  0.1264  -0.0150 366 HOH A O   
23342 O O   . HOH SA .   ? 1.7141 1.5728 1.9879 0.0267  0.1707  0.0302  367 HOH A O   
23343 O O   . HOH SA .   ? 0.5571 0.5546 0.6400 0.0048  -0.0277 0.0364  368 HOH A O   
23344 O O   . HOH SA .   ? 0.5519 0.5821 0.4896 -0.0341 -0.0908 0.0213  369 HOH A O   
23345 O O   . HOH SA .   ? 0.7833 0.7307 0.8828 -0.0085 0.0602  0.0045  370 HOH A O   
23346 O O   . HOH TA .   ? 0.9831 0.9874 0.8241 -0.0895 -0.1000 0.0741  182 HOH B O   
23347 O O   . HOH TA .   ? 0.8511 0.8083 0.9194 -0.0247 0.0437  0.0034  183 HOH B O   
23348 O O   . HOH TA .   ? 0.3786 0.3825 0.3425 -0.0429 -0.0548 0.0377  184 HOH B O   
23349 O O   . HOH TA .   ? 1.1513 1.1363 0.9827 -0.0928 -0.0701 0.0650  185 HOH B O   
23350 O O   . HOH TA .   ? 0.8755 0.8812 0.7698 -0.0767 -0.0986 0.0982  186 HOH B O   
23351 O O   . HOH TA .   ? 0.9003 0.8852 0.8013 -0.0717 -0.0258 0.0190  187 HOH B O   
23352 O O   . HOH TA .   ? 0.6424 0.6770 0.5834 -0.0304 -0.0323 -0.0197 188 HOH B O   
23353 O O   . HOH TA .   ? 0.8685 0.8435 0.6730 -0.1112 -0.0833 0.1376  189 HOH B O   
23354 O O   . HOH TA .   ? 0.8821 0.9012 0.7984 -0.0473 -0.0607 0.0091  190 HOH B O   
23355 O O   . HOH TA .   ? 1.1960 1.1593 1.0633 -0.0890 -0.0144 0.0346  191 HOH B O   
23356 O O   . HOH TA .   ? 0.9832 0.9889 0.8508 -0.0707 -0.0669 0.0236  192 HOH B O   
23357 O O   . HOH TA .   ? 0.8429 0.8509 0.7658 -0.0527 -0.0596 0.0261  193 HOH B O   
23358 O O   . HOH TA .   ? 1.0814 1.0003 0.9338 -0.1029 -0.0007 0.1289  211 HOH B O   
23359 O O   . HOH TA .   ? 0.9596 0.9257 0.8451 -0.0833 -0.0133 0.0323  212 HOH B O   
23360 O O   . HOH TA .   ? 0.9812 0.9287 0.7639 -0.1178 -0.0476 0.1201  238 HOH B O   
23361 O O   . HOH TA .   ? 0.7069 0.7243 0.7236 0.0064  -0.0317 0.0103  299 HOH B O   
23362 O O   . HOH TA .   ? 1.0729 1.0192 0.8398 -0.1212 -0.0414 0.0948  307 HOH B O   
23363 O O   . HOH UA .   ? 0.6605 0.7230 0.5991 0.0145  -0.0515 -0.0067 334 HOH C O   
23364 O O   . HOH UA .   ? 0.7208 0.7903 0.6607 0.0099  -0.0197 -0.0137 335 HOH C O   
23365 O O   . HOH UA .   ? 0.4995 0.5655 0.4302 0.0064  0.0051  -0.0176 336 HOH C O   
23366 O O   . HOH UA .   ? 0.5414 0.5629 0.5432 0.0266  -0.0011 0.0056  337 HOH C O   
23367 O O   . HOH UA .   ? 0.4395 0.4905 0.4145 0.0488  -0.0052 0.0183  338 HOH C O   
23368 O O   . HOH UA .   ? 0.6778 0.7474 0.5854 -0.0103 -0.0581 -0.0213 339 HOH C O   
23369 O O   . HOH UA .   ? 0.8283 0.8639 0.8175 0.0360  -0.0348 0.0115  340 HOH C O   
23370 O O   . HOH UA .   ? 0.8605 0.9158 0.8467 0.0733  0.0021  0.0375  341 HOH C O   
23371 O O   . HOH UA .   ? 0.9718 1.0187 0.7895 -0.0787 -0.0334 -0.0540 342 HOH C O   
23372 O O   . HOH UA .   ? 0.6406 0.6864 0.6258 0.0833  0.0286  0.0527  343 HOH C O   
23373 O O   . HOH UA .   ? 0.6975 0.7648 0.5318 -0.0709 -0.0328 -0.0602 344 HOH C O   
23374 O O   . HOH UA .   ? 0.8679 0.9457 0.7468 -0.0513 -0.0338 -0.0529 345 HOH C O   
23375 O O   . HOH UA .   ? 1.1725 1.2445 1.1072 0.0499  0.0223  0.0266  346 HOH C O   
23376 O O   . HOH UA .   ? 0.6993 0.7127 0.7096 0.0921  0.0513  0.0611  347 HOH C O   
23377 O O   . HOH UA .   ? 0.5379 0.6930 0.4372 0.0057  -0.0451 -0.0225 348 HOH C O   
23378 O O   . HOH UA .   ? 0.4174 0.4453 0.4214 0.0251  -0.0361 0.0115  349 HOH C O   
23379 O O   . HOH UA .   ? 0.6912 0.7981 0.5667 0.0571  0.0500  0.0599  350 HOH C O   
23380 O O   . HOH UA .   ? 0.8732 0.9702 0.7701 -0.0080 -0.0522 -0.0289 351 HOH C O   
23381 O O   . HOH UA .   ? 0.7387 0.8619 0.6658 0.0774  0.0143  0.0623  352 HOH C O   
23382 O O   . HOH UA .   ? 0.5915 0.5762 0.6532 0.0299  0.0237  0.0152  353 HOH C O   
23383 O O   . HOH UA .   ? 0.7644 0.7855 0.7486 0.0470  0.0326  0.0193  354 HOH C O   
23384 O O   . HOH UA .   ? 0.5746 0.7051 0.4421 0.0310  0.0236  0.0266  355 HOH C O   
23385 O O   . HOH UA .   ? 0.8435 0.9781 0.7081 -0.0815 -0.0102 -0.0933 356 HOH C O   
23386 O O   . HOH UA .   ? 0.8542 0.9094 0.6770 -0.0738 -0.0356 -0.0557 357 HOH C O   
23387 O O   . HOH UA .   ? 0.8223 0.8554 0.7919 0.0032  0.0028  -0.0155 358 HOH C O   
23388 O O   . HOH UA .   ? 1.1912 1.2162 1.1958 0.0379  -0.0073 0.0137  359 HOH C O   
23389 O O   . HOH UA .   ? 0.6810 0.7628 0.6354 0.0503  -0.0177 0.0179  360 HOH C O   
23390 O O   . HOH UA .   ? 0.6040 0.6278 0.6172 0.0270  -0.0381 0.0147  361 HOH C O   
23391 O O   . HOH UA .   ? 0.7866 0.9996 0.6692 0.0172  -0.0356 0.0035  362 HOH C O   
23392 O O   . HOH UA .   ? 0.5777 0.6924 0.4537 -0.0555 -0.0251 -0.0686 363 HOH C O   
23393 O O   . HOH UA .   ? 1.0459 1.1162 0.9691 0.0176  -0.0458 -0.0121 364 HOH C O   
23394 O O   . HOH UA .   ? 0.5505 0.6583 0.4485 -0.0018 -0.0506 -0.0272 365 HOH C O   
23395 O O   . HOH UA .   ? 1.1206 1.2161 0.9664 -0.0658 -0.0292 -0.0677 366 HOH C O   
23396 O O   . HOH UA .   ? 1.1526 1.2757 1.0762 0.0932  0.0331  0.0888  367 HOH C O   
23397 O O   . HOH UA .   ? 0.6006 0.5968 0.6159 0.0211  0.0344  0.0001  368 HOH C O   
23398 O O   . HOH UA .   ? 0.5832 0.5889 0.5483 0.0532  0.0729  0.0303  369 HOH C O   
23399 O O   . HOH UA .   ? 0.7847 0.8323 0.7538 0.0187  -0.0359 0.0000  370 HOH C O   
23400 O O   . HOH UA .   ? 1.3885 1.5665 1.3125 0.0690  -0.0161 0.0522  371 HOH C O   
23401 O O   . HOH VA .   ? 0.5041 0.5808 0.3282 -0.0752 -0.0254 -0.0692 182 HOH D O   
23402 O O   . HOH VA .   ? 0.3494 0.4002 0.2276 -0.0497 -0.0469 -0.0337 183 HOH D O   
23403 O O   . HOH VA .   ? 0.7432 0.7641 0.5953 -0.0666 -0.0862 0.0100  184 HOH D O   
23404 O O   . HOH VA .   ? 0.8608 0.9325 0.7719 -0.0096 0.0162  -0.0315 185 HOH D O   
23405 O O   . HOH VA .   ? 1.0675 1.0744 0.8528 -0.0966 -0.0929 0.0177  186 HOH D O   
23406 O O   . HOH VA .   ? 1.7970 1.7644 1.4905 -0.1339 -0.0436 -0.0014 187 HOH D O   
23407 O O   . HOH VA .   ? 0.4823 0.5782 0.3667 -0.0318 0.0141  -0.0510 188 HOH D O   
23408 O O   . HOH VA .   ? 0.5865 0.5963 0.3205 -0.1054 -0.0178 -0.0700 189 HOH D O   
23409 O O   . HOH VA .   ? 1.1293 1.1324 0.8934 -0.0995 -0.0557 -0.0202 244 HOH D O   
23410 O O   . HOH VA .   ? 1.3971 1.3792 1.1722 -0.1075 -0.0333 -0.0033 265 HOH D O   
23411 O O   . HOH WA .   ? 0.7005 0.6662 0.7135 -0.0465 0.0161  0.0172  334 HOH E O   
23412 O O   . HOH WA .   ? 0.6450 0.7546 0.5285 -0.0021 0.0099  -0.0204 335 HOH E O   
23413 O O   . HOH WA .   ? 0.5314 0.5015 0.5141 -0.0629 0.0415  -0.0263 336 HOH E O   
23414 O O   . HOH WA .   ? 1.2361 1.3742 0.9182 -0.1385 0.1068  -0.1068 337 HOH E O   
23415 O O   . HOH WA .   ? 0.6066 0.7114 0.4750 -0.0504 0.0205  -0.0673 338 HOH E O   
23416 O O   . HOH WA .   ? 0.7825 0.7287 0.7442 -0.0877 0.0676  -0.0294 339 HOH E O   
23417 O O   . HOH WA .   ? 0.7457 0.7179 0.6687 -0.0543 0.1257  -0.0742 340 HOH E O   
23418 O O   . HOH WA .   ? 1.1819 1.3435 0.9104 -0.1528 0.0789  -0.1373 341 HOH E O   
23419 O O   . HOH WA .   ? 1.1137 1.0582 1.0681 -0.0276 0.1417  -0.0493 342 HOH E O   
23420 O O   . HOH WA .   ? 1.5725 1.6535 1.3501 -0.1536 0.1172  -0.1553 343 HOH E O   
23421 O O   . HOH WA .   ? 0.7616 0.7629 0.7022 -0.0403 0.0770  -0.0597 344 HOH E O   
23422 O O   . HOH WA .   ? 0.5116 0.5542 0.4451 -0.0235 0.0251  -0.0429 345 HOH E O   
23423 O O   . HOH WA .   ? 0.5773 0.6953 0.4278 -0.0325 0.0259  -0.0445 346 HOH E O   
23424 O O   . HOH WA .   ? 0.9419 1.0599 0.8175 0.0011  0.0120  -0.0145 347 HOH E O   
23425 O O   . HOH WA .   ? 0.9980 1.2076 0.7676 -0.1060 0.0233  -0.0956 348 HOH E O   
23426 O O   . HOH WA .   ? 0.7393 0.7119 0.6847 -0.0747 0.0285  -0.0197 349 HOH E O   
23427 O O   . HOH WA .   ? 1.1485 1.0258 1.1454 -0.0615 0.2113  -0.0835 350 HOH E O   
23428 O O   . HOH WA .   ? 1.2696 1.2040 1.2300 -0.0838 0.1571  -0.1009 351 HOH E O   
23429 O O   . HOH WA .   ? 1.0841 1.2208 0.8717 -0.1099 0.0592  -0.1103 352 HOH E O   
23430 O O   . HOH WA .   ? 1.1449 1.0960 1.0778 -0.0973 0.0640  -0.0348 353 HOH E O   
23431 O O   . HOH WA .   ? 0.9019 0.7484 0.9058 -0.1050 0.2547  -0.1242 354 HOH E O   
23432 O O   . HOH WA .   ? 0.8984 0.8408 0.8963 -0.0660 0.0469  0.0103  355 HOH E O   
23433 O O   . HOH WA .   ? 0.7822 0.7550 0.7575 -0.0728 0.0655  -0.0564 356 HOH E O   
23434 O O   . HOH WA .   ? 0.5273 0.5697 0.4177 -0.0425 0.0653  -0.0609 357 HOH E O   
23435 O O   . HOH WA .   ? 1.0862 1.3269 0.8809 -0.0715 -0.0078 -0.0627 358 HOH E O   
23436 O O   . HOH WA .   ? 0.9142 1.0660 0.6469 -0.0796 0.0703  -0.0552 359 HOH E O   
23437 O O   . HOH WA .   ? 0.6456 0.7175 0.5266 -0.0343 0.0418  -0.0522 360 HOH E O   
23438 O O   . HOH WA .   ? 0.6221 0.5944 0.5725 -0.0987 0.0832  -0.0794 361 HOH E O   
23439 O O   . HOH WA .   ? 1.1630 1.0296 1.1821 -0.0603 0.2172  -0.0817 362 HOH E O   
23440 O O   . HOH WA .   ? 0.9041 0.8241 0.9507 -0.0631 0.0886  -0.0066 363 HOH E O   
23441 O O   . HOH WA .   ? 0.7834 0.9337 0.6324 -0.0551 0.0031  -0.0687 364 HOH E O   
23442 O O   . HOH XA .   ? 0.4873 0.4886 0.4239 -0.0679 0.0171  -0.0400 182 HOH F O   
23443 O O   . HOH XA .   ? 1.2853 1.2756 1.1582 -0.1304 0.0721  -0.0895 183 HOH F O   
23444 O O   . HOH XA .   ? 1.5839 1.5446 1.4192 -0.1099 0.0235  -0.0160 184 HOH F O   
23445 O O   . HOH XA .   ? 0.6532 0.6579 0.6183 -0.0428 0.0441  -0.0514 185 HOH F O   
23446 O O   . HOH XA .   ? 1.2866 1.2917 1.1353 -0.1044 0.0185  -0.0569 186 HOH F O   
23447 O O   . HOH XA .   ? 0.7555 0.7568 0.5987 -0.0944 -0.0033 -0.0358 187 HOH F O   
23448 O O   . HOH XA .   ? 1.1585 1.1600 0.9755 -0.1057 0.0043  -0.0471 188 HOH F O   
23449 O O   . HOH XA .   ? 0.8341 0.7655 0.6512 -0.1281 0.0570  -0.0159 189 HOH F O   
23450 O O   . HOH XA .   ? 0.6890 0.7008 0.5675 -0.0925 0.0155  -0.0560 190 HOH F O   
23451 O O   . HOH XA .   ? 0.6581 0.6793 0.5701 -0.0623 -0.0107 -0.0354 191 HOH F O   
23452 O O   . HOH XA .   ? 0.6540 0.5906 0.4563 -0.1318 0.0549  -0.0238 192 HOH F O   
23453 O O   . HOH XA .   ? 1.0015 0.9179 0.9485 -0.1163 0.1133  -0.0465 193 HOH F O   
23454 O O   . HOH XA .   ? 1.3282 1.2659 1.1501 -0.1234 0.0483  -0.0141 284 HOH F O   
23455 O O   . HOH YA .   ? 1.1078 1.0565 0.8341 -0.1741 -0.0645 -0.0899 334 HOH G O   
23456 O O   . HOH YA .   ? 1.3409 1.1996 1.4428 0.0223  0.1205  -0.0290 335 HOH G O   
23457 O O   . HOH YA .   ? 0.6956 0.5111 0.9287 0.0204  0.1609  -0.0191 336 HOH G O   
23458 O O   . HOH YA .   ? 0.9978 0.9104 0.7376 -0.1574 -0.0090 -0.1149 337 HOH G O   
23459 O O   . HOH YA .   ? 1.1780 1.1218 0.9525 -0.1382 -0.0431 -0.0882 338 HOH G O   
23460 O O   . HOH YA .   ? 0.9082 0.8553 1.0225 -0.0335 -0.0114 -0.0182 339 HOH G O   
23461 O O   . HOH YA .   ? 0.9734 0.8885 0.7369 -0.1394 -0.0033 -0.1096 340 HOH G O   
23462 O O   . HOH YA .   ? 0.8143 0.6662 1.0078 0.1407  0.1915  0.0851  341 HOH G O   
23463 O O   . HOH YA .   ? 0.7864 0.7596 0.6571 -0.1062 -0.0706 -0.0548 342 HOH G O   
23464 O O   . HOH YA .   ? 0.9667 0.8759 0.7039 -0.1526 -0.0006 -0.1168 343 HOH G O   
23465 O O   . HOH YA .   ? 0.6378 0.6036 0.6562 -0.0530 -0.0427 -0.0295 344 HOH G O   
23466 O O   . HOH YA .   ? 1.2792 1.1219 1.3161 -0.0735 0.0995  -0.0945 345 HOH G O   
23467 O O   . HOH YA .   ? 0.7508 0.5977 0.9721 0.0262  0.1259  -0.0072 346 HOH G O   
23468 O O   . HOH YA .   ? 1.1775 1.0862 1.3646 0.0068  0.0478  -0.0034 347 HOH G O   
23469 O O   . HOH YA .   ? 0.8990 0.8469 0.8289 -0.0437 -0.0065 -0.0538 348 HOH G O   
23470 O O   . HOH YA .   ? 0.9196 0.8427 1.0837 -0.0927 0.0133  -0.0537 349 HOH G O   
23471 O O   . HOH YA .   ? 1.2547 1.1574 1.3279 -0.0590 0.0318  -0.0570 350 HOH G O   
23472 O O   . HOH YA .   ? 1.1881 1.0402 1.2204 -0.1056 0.0790  -0.1061 351 HOH G O   
23473 O O   . HOH YA .   ? 0.8961 0.7850 0.6387 -0.2329 -0.0052 -0.1527 352 HOH G O   
23474 O O   . HOH YA .   ? 0.6079 0.5331 0.7418 0.0638  0.0581  0.0272  353 HOH G O   
23475 O O   . HOH YA .   ? 0.7423 0.6334 0.9124 0.0970  0.1145  0.0511  354 HOH G O   
23476 O O   . HOH YA .   ? 0.8098 0.6703 0.8636 -0.0537 0.0841  -0.0754 355 HOH G O   
23477 O O   . HOH YA .   ? 0.6040 0.4842 0.8090 0.0559  0.0992  0.0216  356 HOH G O   
23478 O O   . HOH YA .   ? 0.9587 0.8727 0.9279 -0.0319 0.0391  -0.0593 357 HOH G O   
23479 O O   . HOH YA .   ? 0.5500 0.4768 0.7647 0.0463  0.0436  0.0332  358 HOH G O   
23480 O O   . HOH YA .   ? 0.8522 0.7004 0.8993 -0.0892 0.0880  -0.0983 359 HOH G O   
23481 O O   . HOH YA .   ? 1.1149 1.0520 1.3458 0.0084  0.0198  0.0170  360 HOH G O   
23482 O O   . HOH YA .   ? 0.8535 0.7673 1.1722 0.0258  0.0599  0.0321  361 HOH G O   
23483 O O   . HOH YA .   ? 0.6726 0.5997 0.8565 0.0213  0.0315  0.0120  362 HOH G O   
23484 O O   . HOH YA .   ? 0.4738 0.4033 0.6114 0.0561  0.0475  0.0244  363 HOH G O   
23485 O O   . HOH YA .   ? 0.8611 0.7706 0.8304 -0.0430 0.0363  -0.0645 364 HOH G O   
23486 O O   . HOH YA .   ? 1.1422 1.0851 1.1798 -0.1176 -0.0271 -0.0663 365 HOH G O   
23487 O O   . HOH YA .   ? 0.9313 0.7460 1.1950 0.0896  0.1881  0.0419  366 HOH G O   
23488 O O   . HOH YA .   ? 0.4360 0.2607 0.6483 0.1054  0.1931  0.0465  367 HOH G O   
23489 O O   . HOH YA .   ? 1.4074 1.2171 1.5880 -0.0317 0.1520  -0.0634 368 HOH G O   
23490 O O   . HOH YA .   ? 1.0867 0.8918 1.3167 0.0535  0.1858  0.0015  369 HOH G O   
23491 O O   . HOH YA .   ? 1.3358 1.2457 1.0719 -0.1792 -0.0168 -0.1211 370 HOH G O   
23492 O O   . HOH YA .   ? 1.1116 1.0565 1.1313 -0.1206 -0.0316 -0.0677 371 HOH G O   
23493 O O   . HOH YA .   ? 0.9638 0.7699 1.1796 0.0810  0.2008  0.0203  372 HOH G O   
23494 O O   . HOH YA .   ? 0.8160 0.7285 1.0244 -0.0256 0.0376  -0.0170 373 HOH G O   
23495 O O   . HOH YA .   ? 1.8619 1.7237 1.9910 -0.0920 0.0771  -0.0846 374 HOH G O   
23496 O O   . HOH YA .   ? 0.7638 0.7083 0.8730 -0.0739 -0.0162 -0.0388 375 HOH G O   
23497 O O   . HOH YA .   ? 1.3543 1.2718 1.0790 -0.1629 -0.0175 -0.1126 376 HOH G O   
23498 O O   . HOH YA .   ? 0.9974 0.8799 0.9913 -0.1504 0.0337  -0.1161 377 HOH G O   
23499 O O   . HOH YA .   ? 0.8815 0.6942 1.0542 0.0289  0.1709  -0.0253 378 HOH G O   
23500 O O   . HOH ZA .   ? 1.4258 1.4929 1.1068 -0.2578 -0.2128 0.0061  182 HOH H O   
23501 O O   . HOH ZA .   ? 0.9945 0.9765 0.6119 -0.2623 -0.1288 -0.0747 183 HOH H O   
23502 O O   . HOH ZA .   ? 1.1400 1.0734 0.8824 -0.1502 -0.0332 -0.0986 184 HOH H O   
23503 O O   . HOH ZA .   ? 1.9136 1.9316 1.4653 -0.3056 -0.1767 -0.0418 185 HOH H O   
23504 O O   . HOH ZA .   ? 1.5623 1.5826 1.1741 -0.2537 -0.1725 -0.0205 186 HOH H O   
23505 O O   . HOH ZA .   ? 0.4909 0.4697 0.4578 -0.0044 -0.0213 -0.0234 187 HOH H O   
23506 O O   . HOH ZA .   ? 1.4304 1.4511 1.1855 -0.1480 -0.1467 -0.0022 188 HOH H O   
23507 O O   . HOH ZA .   ? 0.8191 0.8271 0.6427 -0.1263 -0.1214 -0.0266 189 HOH H O   
23508 O O   . HOH ZA .   ? 0.8666 0.9028 0.7131 -0.1510 -0.1574 -0.0055 190 HOH H O   
23509 O O   . HOH ZA .   ? 0.9580 0.9068 1.0167 -0.0080 -0.0045 -0.0164 191 HOH H O   
23510 O O   . HOH ZA .   ? 0.7291 0.6634 0.8067 0.0543  0.0535  0.0096  192 HOH H O   
23511 O O   . HOH ZA .   ? 1.6557 1.6675 1.2076 -0.2869 -0.1700 -0.0309 193 HOH H O   
23512 O O   . HOH ZA .   ? 0.6533 0.6094 0.6820 -0.0459 -0.0285 -0.0313 194 HOH H O   
23513 O O   . HOH ZA .   ? 1.0295 0.9992 0.5885 -0.2343 -0.1149 -0.0404 195 HOH H O   
23514 O O   . HOH ZA .   ? 0.9117 0.8811 0.9333 0.0346  0.0113  -0.0023 196 HOH H O   
23515 O O   . HOH ZA .   ? 1.4106 1.4156 0.9350 -0.3323 -0.1649 -0.0672 197 HOH H O   
23516 O O   . HOH ZA .   ? 0.8381 0.8505 0.6421 -0.1223 -0.1259 -0.0181 198 HOH H O   
23517 O O   . HOH ZA .   ? 1.0207 0.9948 0.6069 -0.2182 -0.1147 -0.0371 208 HOH H O   
23518 O O   . HOH ZA .   ? 1.0011 1.0196 0.6058 -0.2301 -0.1700 0.0101  231 HOH H O   
23519 O O   . HOH ZA .   ? 1.5129 1.5483 1.1404 -0.2284 -0.1868 0.0236  233 HOH H O   
23520 O O   . HOH ZA .   ? 0.6422 0.6028 0.6838 -0.0228 -0.0248 -0.0189 246 HOH H O   
23521 O O   . HOH ZA .   ? 1.0401 1.0080 0.5917 -0.2444 -0.1152 -0.0484 256 HOH H O   
23522 O O   . HOH ZA .   ? 1.2712 1.3550 0.9718 -0.2544 -0.2272 0.0235  277 HOH H O   
23523 O O   . HOH AB .   ? 0.6762 0.7002 0.5552 -0.0490 -0.0947 -0.0107 334 HOH I O   
23524 O O   . HOH AB .   ? 0.6078 0.5437 0.7231 0.0955  0.0757  0.0507  335 HOH I O   
23525 O O   . HOH AB .   ? 0.4784 0.3844 0.6038 0.1633  0.1710  0.1308  336 HOH I O   
23526 O O   . HOH AB .   ? 0.7181 0.6550 0.8337 0.1004  0.0792  0.0563  337 HOH I O   
23527 O O   . HOH AB .   ? 1.5171 1.5317 1.5379 0.0838  0.0377  0.0301  338 HOH I O   
23528 O O   . HOH AB .   ? 1.2290 1.2276 1.3466 0.2016  0.1540  0.1771  339 HOH I O   
23529 O O   . HOH AB .   ? 1.2415 1.2492 1.3421 0.1980  0.1452  0.1784  340 HOH I O   
23530 O O   . HOH AB .   ? 0.7709 0.7226 0.8496 0.0659  0.0421  0.0232  341 HOH I O   
23531 O O   . HOH AB .   ? 0.8673 0.8995 0.7327 -0.0390 -0.0775 -0.0226 342 HOH I O   
23532 O O   . HOH AB .   ? 0.6744 0.6492 0.7583 0.1574  0.1191  0.1230  343 HOH I O   
23533 O O   . HOH AB .   ? 0.8411 0.8693 0.8108 0.0079  -0.0621 0.0025  344 HOH I O   
23534 O O   . HOH AB .   ? 1.4456 1.5147 1.4361 0.1031  0.0278  0.0716  345 HOH I O   
23535 O O   . HOH AB .   ? 0.9705 1.0032 0.9303 0.0003  -0.0698 0.0023  346 HOH I O   
23536 O O   . HOH AB .   ? 0.9861 1.0616 0.8680 -0.0115 -0.0529 -0.0313 347 HOH I O   
23537 O O   . HOH AB .   ? 0.9807 0.9193 1.0612 0.0750  0.0682  0.0237  348 HOH I O   
23538 O O   . HOH AB .   ? 1.2722 1.2990 1.2270 -0.0267 -0.0958 0.0093  349 HOH I O   
23539 O O   . HOH AB .   ? 0.8223 0.8698 0.7856 0.0447  -0.0202 0.0045  350 HOH I O   
23540 O O   . HOH AB .   ? 0.6688 0.6128 0.7498 0.0966  0.0941  0.0369  351 HOH I O   
23541 O O   . HOH AB .   ? 0.5535 0.5710 0.5248 0.0386  -0.0079 -0.0026 352 HOH I O   
23542 O O   . HOH AB .   ? 1.2938 1.3105 1.3373 0.1134  0.0511  0.0674  353 HOH I O   
23543 O O   . HOH AB .   ? 1.1162 1.1152 0.8617 -0.0991 -0.0552 -0.0500 354 HOH I O   
23544 O O   . HOH AB .   ? 0.8053 0.9283 0.7401 0.1026  0.0350  0.0978  356 HOH I O   
23545 O O   . HOH AB .   ? 0.8279 0.7717 0.9889 0.2233  0.2084  0.2005  357 HOH I O   
23546 O O   . HOH AB .   ? 0.7601 0.7916 0.6580 -0.0096 -0.0487 -0.0266 358 HOH I O   
23547 O O   . HOH AB .   ? 1.4448 1.5157 1.4793 0.1375  0.0547  0.1017  359 HOH I O   
23548 O O   . HOH AB .   ? 0.8395 0.8699 0.8118 0.0011  -0.0707 0.0067  360 HOH I O   
23549 O O   . HOH AB .   ? 0.9280 0.9462 1.0047 0.1600  0.0997  0.1226  361 HOH I O   
23550 O O   . HOH AB .   ? 0.8478 0.7972 1.0025 0.2282  0.2099  0.2118  362 HOH I O   
23551 O O   . HOH AB .   ? 1.1420 1.0232 1.2953 0.1060  0.1408  0.0486  363 HOH I O   
23552 O O   . HOH AB .   ? 0.7746 0.7814 0.5322 -0.0962 -0.0679 -0.0327 364 HOH I O   
23553 O O   . HOH AB .   ? 0.9175 0.8502 1.0421 0.1026  0.0847  0.0621  365 HOH I O   
23554 O O   . HOH AB .   ? 0.4147 0.4761 0.3569 0.0326  -0.0326 -0.0039 366 HOH I O   
23555 O O   . HOH AB .   ? 0.9232 0.8461 1.0092 0.1420  0.1507  0.1150  367 HOH I O   
23556 O O   . HOH AB .   ? 0.9068 0.9535 0.8118 -0.0022 -0.0529 -0.0211 368 HOH I O   
23557 O O   . HOH AB .   ? 1.1544 1.0671 1.2702 0.1028  0.1168  0.0440  369 HOH I O   
23558 O O   . HOH AB .   ? 1.0516 1.0223 1.1481 0.1804  0.1468  0.1540  370 HOH I O   
23559 O O   . HOH AB .   ? 0.6205 0.6488 0.5580 -0.0085 -0.0709 -0.0065 371 HOH I O   
23560 O O   . HOH BB .   ? 0.4911 0.5152 0.4428 -0.0077 -0.0720 -0.0027 182 HOH J O   
23561 O O   . HOH BB .   ? 1.3697 1.3388 1.0517 -0.1522 -0.0764 -0.0615 183 HOH J O   
23562 O O   . HOH BB .   ? 0.6929 0.6958 0.6433 0.0112  -0.0220 -0.0180 184 HOH J O   
23563 O O   . HOH BB .   ? 0.4348 0.4361 0.4558 -0.0012 -0.0587 0.0057  185 HOH J O   
23564 O O   . HOH BB .   ? 0.4436 0.4396 0.4845 0.0580  -0.0012 0.0243  186 HOH J O   
23565 O O   . HOH BB .   ? 0.8836 0.8778 0.8762 0.0348  -0.0038 -0.0025 187 HOH J O   
23566 O O   . HOH BB .   ? 0.7670 0.7543 0.4375 -0.1468 -0.0986 -0.0076 188 HOH J O   
23567 O O   . HOH BB .   ? 0.3156 0.3095 0.3593 0.0499  -0.0089 0.0208  189 HOH J O   
23568 O O   . HOH BB .   ? 0.7700 0.7574 0.8554 0.0131  -0.0397 0.0172  190 HOH J O   
23569 O O   . HOH BB .   ? 0.8761 0.8469 0.6568 -0.0798 -0.0048 -0.0818 199 HOH J O   
23570 O O   . HOH BB .   ? 0.8106 0.7784 0.8150 0.0327  0.0210  -0.0096 205 HOH J O   
23571 O O   . HOH BB .   ? 1.6915 1.6768 1.4639 -0.0830 -0.0300 -0.0708 210 HOH J O   
23572 O O   . HOH BB .   ? 1.4692 1.5026 1.2696 -0.0656 -0.0446 -0.0529 234 HOH J O   
23573 O O   . HOH BB .   ? 1.3676 1.3350 1.0622 -0.1432 -0.0679 -0.0664 248 HOH J O   
23574 O O   . HOH BB .   ? 0.8069 0.8093 0.6192 -0.0961 -0.0981 -0.0313 252 HOH J O   
23575 O O   . HOH BB .   ? 0.8495 0.8458 0.7941 -0.0026 -0.0312 -0.0224 257 HOH J O   
23576 O O   . HOH BB .   ? 1.3857 1.3754 1.1075 -0.1149 -0.0641 -0.0455 260 HOH J O   
23577 O O   . HOH BB .   ? 1.1746 1.1525 1.2678 0.0348  -0.0153 0.0221  295 HOH J O   
23578 O O   . HOH BB .   ? 1.0816 1.0501 0.7467 -0.1453 -0.0576 -0.0557 313 HOH J O   
23579 O O   . HOH BB .   ? 0.4449 0.4496 0.4639 0.0634  0.0066  0.0213  318 HOH J O   
23580 O O   . HOH BB .   ? 0.7864 0.7822 0.7812 0.0321  -0.0113 -0.0014 319 HOH J O   
23581 O O   . HOH CB .   ? 0.5709 0.5010 0.8028 0.0426  0.0392  0.0355  334 HOH K O   
23582 O O   . HOH CB .   ? 0.3728 0.2703 0.6571 0.0673  0.0901  0.0516  335 HOH K O   
23583 O O   . HOH CB .   ? 0.7670 0.8286 0.6404 -0.1583 -0.1823 0.0168  336 HOH K O   
23584 O O   . HOH CB .   ? 0.3309 0.3337 0.3780 -0.0158 -0.0713 0.0107  337 HOH K O   
23585 O O   . HOH CB .   ? 0.5072 0.4614 0.7078 0.0546  0.0265  0.0502  338 HOH K O   
23586 O O   . HOH CB .   ? 0.5363 0.5742 0.6628 -0.0153 -0.1076 0.0660  339 HOH K O   
23587 O O   . HOH CB .   ? 0.6053 0.5567 0.9058 0.0444  0.0250  0.0611  340 HOH K O   
23588 O O   . HOH CB .   ? 0.9573 0.9144 1.2360 0.0294  0.0095  0.0484  341 HOH K O   
23589 O O   . HOH CB .   ? 0.9469 1.0045 0.9601 -0.1050 -0.1565 0.0277  342 HOH K O   
23590 O O   . HOH CB .   ? 0.8785 0.8242 1.0211 0.0751  0.0502  0.0475  343 HOH K O   
23591 O O   . HOH CB .   ? 0.8356 0.8937 0.8207 -0.1075 -0.1613 0.0288  344 HOH K O   
23592 O O   . HOH CB .   ? 0.9074 0.8073 1.1562 0.0790  0.1020  0.0596  345 HOH K O   
23593 O O   . HOH CB .   ? 0.5440 0.5199 0.6119 0.1025  0.0607  0.0635  346 HOH K O   
23594 O O   . HOH CB .   ? 0.5097 0.5159 0.5714 -0.0099 -0.0725 0.0181  347 HOH K O   
23595 O O   . HOH CB .   ? 0.9628 0.8857 1.2206 0.0663  0.0679  0.0576  348 HOH K O   
23596 O O   . HOH CB .   ? 0.6917 0.6514 0.9732 0.0361  0.0099  0.0554  350 HOH K O   
23597 O O   . HOH CB .   ? 0.7720 0.6416 1.0041 0.1006  0.1374  0.0650  351 HOH K O   
23598 O O   . HOH CB .   ? 0.9245 1.0193 0.9788 -0.0887 -0.1896 0.0898  352 HOH K O   
23599 O O   . HOH CB .   ? 0.7416 0.8030 0.6482 -0.0991 -0.1739 0.0634  353 HOH K O   
23600 O O   . HOH CB .   ? 0.7389 0.6888 1.0514 0.0195  0.0188  0.0434  354 HOH K O   
23601 O O   . HOH CB .   ? 0.5064 0.4578 0.7523 0.0460  0.0206  0.0509  355 HOH K O   
23602 O O   . HOH CB .   ? 0.5056 0.4913 0.7228 0.0328  -0.0219 0.0602  356 HOH K O   
23603 O O   . HOH CB .   ? 0.5429 0.4449 0.6843 0.1292  0.1377  0.0900  357 HOH K O   
23604 O O   . HOH CB .   ? 1.0897 1.0818 1.1804 0.0313  -0.0312 0.0275  358 HOH K O   
23605 O O   . HOH CB .   ? 0.5799 0.5065 0.6819 0.1269  0.1252  0.0924  359 HOH K O   
23606 O O   . HOH CB .   ? 0.9063 0.9408 1.0576 -0.0100 -0.1000 0.0676  360 HOH K O   
23607 O O   . HOH CB .   ? 0.6592 0.5618 0.8066 0.1205  0.1285  0.0814  361 HOH K O   
23608 O O   . HOH CB .   ? 0.6380 0.6579 0.7177 -0.0274 -0.0949 0.0283  362 HOH K O   
23609 O O   . HOH CB .   ? 0.7120 0.6046 0.8729 0.1176  0.1360  0.0803  363 HOH K O   
23610 O O   . HOH CB .   ? 0.6067 0.5885 0.6675 0.0827  0.0436  0.0485  364 HOH K O   
23611 O O   . HOH CB .   ? 0.7763 0.6929 0.8877 0.1237  0.1307  0.0895  365 HOH K O   
23612 O O   . HOH CB .   ? 0.8823 0.7946 1.0537 0.0897  0.0875  0.0537  366 HOH K O   
23613 O O   . HOH CB .   ? 0.7677 0.8665 0.7690 -0.1203 -0.2023 0.0730  367 HOH K O   
23614 O O   . HOH CB .   ? 0.5282 0.4832 0.6500 0.0543  0.0202  0.0294  368 HOH K O   
23615 O O   . HOH CB .   ? 1.1102 1.2080 0.8934 -0.1714 -0.2332 0.1321  369 HOH K O   
23616 O O   . HOH DB .   ? 0.6424 0.6772 0.6020 -0.0639 -0.1296 0.0214  182 HOH L O   
23617 O O   . HOH DB .   ? 1.4253 1.4479 1.1809 -0.1445 -0.1482 0.0041  183 HOH L O   
23618 O O   . HOH DB .   ? 0.6413 0.6637 0.4690 -0.0966 -0.1270 0.0002  184 HOH L O   
23619 O O   . HOH DB .   ? 0.8782 0.9893 0.8354 -0.1186 -0.2219 0.1237  203 HOH L O   
23620 O O   . HOH DB .   ? 0.5792 0.5628 0.6951 0.0073  -0.0391 0.0197  219 HOH L O   
23621 O O   . HOH DB .   ? 0.6373 0.6708 0.3881 -0.1395 -0.1634 0.0775  227 HOH L O   
23622 O O   . HOH DB .   ? 0.9945 1.0425 0.6989 -0.1753 -0.1900 0.0784  235 HOH L O   
23623 O O   . HOH DB .   ? 1.6784 1.7121 1.4423 -0.1371 -0.1604 0.0384  247 HOH L O   
23624 O O   . HOH DB .   ? 1.4511 1.4912 1.2736 -0.1101 -0.1581 0.0704  262 HOH L O   
23625 O O   . HOH DB .   ? 1.2025 1.2948 0.9951 -0.1618 -0.2264 0.1375  276 HOH L O   
23626 O O   . HOH DB .   ? 0.4692 0.4455 0.4993 -0.0400 -0.0505 -0.0171 279 HOH L O   
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   ?   ?   ?   A . n 
A 1 2   ASP 2   2   ?   ?   ?   A . n 
A 1 3   LEU 3   3   ?   ?   ?   A . n 
A 1 4   GLY 4   4   ?   ?   ?   A . n 
A 1 5   SER 5   5   ?   ?   ?   A . n 
A 1 6   ARG 6   6   ?   ?   ?   A . n 
A 1 7   ASP 7   7   7   ASP ASP A . n 
A 1 8   THR 8   8   8   THR THR A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  CYS 10  10  10  CYS CYS A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  TYR 13  13  13  TYR TYR A . n 
A 1 14  HIS 14  14  14  HIS HIS A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  ASN 17  17  17  ASN ASN A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  ASP 20  20  20  ASP ASP A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  VAL 22  22  22  VAL VAL A . n 
A 1 23  ASP 23  23  23  ASP ASP A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  ASN 29  29  29  ASN ASN A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  THR 31  31  31  THR THR A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  HIS 34  34  34  HIS HIS A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  CYS 48  48  48  CYS CYS A . n 
A 1 49  LYS 49  49  49  LYS LYS A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ARG 51  51  51  ARG ARG A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  PRO 55  55  55  PRO PRO A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  HIS 57  57  57  HIS HIS A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  CYS 61  61  61  CYS CYS A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  TRP 66  66  66  TRP TRP A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  ASN 70  70  70  ASN ASN A . n 
A 1 71  PRO 71  71  71  PRO PRO A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  CYS 73  73  73  CYS CYS A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  THR 78  78  78  THR THR A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  TRP 82  82  82  TRP TRP A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  TYR 84  84  84  TYR TYR A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  SER 90  90  90  SER SER A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  ASN 93  93  93  ASN ASN A . n 
A 1 94  GLY 94  94  94  GLY GLY A . n 
A 1 95  THR 95  95  95  THR THR A . n 
A 1 96  CYS 96  96  96  CYS CYS A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 ASP 100 100 100 ASP ASP A . n 
A 1 101 PHE 101 101 101 PHE PHE A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 TYR 104 104 104 TYR TYR A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 PHE 117 117 117 PHE PHE A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 PHE 120 120 120 PHE PHE A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 PHE 123 123 123 PHE PHE A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 LYS 125 125 125 LYS LYS A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 TRP 129 129 129 TRP TRP A . n 
A 1 130 PRO 130 130 130 PRO PRO A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 HIS 132 132 132 HIS HIS A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 ASN 135 135 135 ASN ASN A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 THR 139 139 139 THR THR A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 CYS 142 142 142 CYS CYS A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 HIS 144 144 144 HIS HIS A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 TYR 151 151 151 TYR TYR A . n 
A 1 152 LYS 152 152 152 LYS LYS A . n 
A 1 153 ASN 153 153 153 ASN ASN A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 TRP 156 156 156 TRP TRP A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 LYS 159 159 159 LYS LYS A . n 
A 1 160 LYS 160 160 160 LYS LYS A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 TYR 164 164 164 TYR TYR A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 SER 170 170 170 SER SER A . n 
A 1 171 TYR 171 171 171 TYR TYR A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 ASN 173 173 173 ASN ASN A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 LYS 175 175 175 LYS LYS A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 LYS 177 177 177 LYS LYS A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 TRP 183 183 183 TRP TRP A . n 
A 1 184 GLY 184 184 184 GLY GLY A . n 
A 1 185 ILE 185 185 185 ILE ILE A . n 
A 1 186 HIS 186 186 186 HIS HIS A . n 
A 1 187 HIS 187 187 187 HIS HIS A . n 
A 1 188 PRO 188 188 188 PRO PRO A . n 
A 1 189 SER 189 189 189 SER SER A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 SER 191 191 191 SER SER A . n 
A 1 192 ALA 192 192 192 ALA ALA A . n 
A 1 193 ASP 193 193 193 ASP ASP A . n 
A 1 194 GLN 194 194 194 GLN GLN A . n 
A 1 195 GLN 195 195 195 GLN GLN A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 TYR 198 198 198 TYR TYR A . n 
A 1 199 GLN 199 199 199 GLN GLN A . n 
A 1 200 ASN 200 200 200 ASN ASN A . n 
A 1 201 ALA 201 201 201 ALA ALA A . n 
A 1 202 ASP 202 202 202 ASP ASP A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 TYR 204 204 204 TYR TYR A . n 
A 1 205 VAL 205 205 205 VAL VAL A . n 
A 1 206 PHE 206 206 206 PHE PHE A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 GLY 208 208 208 GLY GLY A . n 
A 1 209 SER 209 209 209 SER SER A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 ARG 211 211 211 ARG ARG A . n 
A 1 212 TYR 212 212 212 TYR TYR A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 LYS 214 214 214 LYS LYS A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 PHE 216 216 216 PHE PHE A . n 
A 1 217 LYS 217 217 217 LYS LYS A . n 
A 1 218 PRO 218 218 218 PRO PRO A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 ARG 223 223 223 ARG ARG A . n 
A 1 224 PRO 224 224 224 PRO PRO A . n 
A 1 225 LYS 225 225 225 LYS LYS A . n 
A 1 226 VAL 226 226 226 VAL VAL A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 ASP 228 228 228 ASP ASP A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 GLU 230 230 230 GLU GLU A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 ARG 232 232 232 ARG ARG A . n 
A 1 233 MET 233 233 233 MET MET A . n 
A 1 234 ASN 234 234 234 ASN ASN A . n 
A 1 235 TYR 235 235 235 TYR TYR A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 TRP 237 237 237 TRP TRP A . n 
A 1 238 THR 238 238 238 THR THR A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 VAL 240 240 240 VAL VAL A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 PRO 242 242 242 PRO PRO A . n 
A 1 243 GLY 243 243 243 GLY GLY A . n 
A 1 244 ASP 244 244 244 ASP ASP A . n 
A 1 245 LYS 245 245 245 LYS LYS A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 THR 247 247 247 THR THR A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 GLU 249 249 249 GLU GLU A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 THR 251 251 251 THR THR A . n 
A 1 252 GLY 252 252 252 GLY GLY A . n 
A 1 253 ASN 253 253 253 ASN ASN A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 VAL 256 256 256 VAL VAL A . n 
A 1 257 PRO 257 257 257 PRO PRO A . n 
A 1 258 ARG 258 258 258 ARG ARG A . n 
A 1 259 TYR 259 259 259 TYR TYR A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 ALA 262 262 262 ALA ALA A . n 
A 1 263 MET 263 263 263 MET MET A . n 
A 1 264 GLU 264 264 264 GLU GLU A . n 
A 1 265 ARG 265 265 265 ARG ARG A . n 
A 1 266 ASN 266 266 266 ASN ASN A . n 
A 1 267 ALA 267 267 267 ALA ALA A . n 
A 1 268 GLY 268 268 268 GLY GLY A . n 
A 1 269 SER 269 269 269 SER SER A . n 
A 1 270 GLY 270 270 270 GLY GLY A . n 
A 1 271 ILE 271 271 271 ILE ILE A . n 
A 1 272 ILE 272 272 272 ILE ILE A . n 
A 1 273 ILE 273 273 273 ILE ILE A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 ASP 275 275 275 ASP ASP A . n 
A 1 276 THR 276 276 276 THR THR A . n 
A 1 277 PRO 277 277 277 PRO PRO A . n 
A 1 278 VAL 278 278 278 VAL VAL A . n 
A 1 279 HIS 279 279 279 HIS HIS A . n 
A 1 280 ASP 280 280 280 ASP ASP A . n 
A 1 281 CYS 281 281 281 CYS CYS A . n 
A 1 282 ASN 282 282 282 ASN ASN A . n 
A 1 283 THR 283 283 283 THR THR A . n 
A 1 284 THR 284 284 284 THR THR A . n 
A 1 285 CYS 285 285 285 CYS CYS A . n 
A 1 286 GLN 286 286 286 GLN GLN A . n 
A 1 287 THR 287 287 287 THR THR A . n 
A 1 288 PRO 288 288 288 PRO PRO A . n 
A 1 289 LYS 289 289 289 LYS LYS A . n 
A 1 290 GLY 290 290 290 GLY GLY A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 ILE 292 292 292 ILE ILE A . n 
A 1 293 ASN 293 293 293 ASN ASN A . n 
A 1 294 THR 294 294 294 THR THR A . n 
A 1 295 SER 295 295 295 SER SER A . n 
A 1 296 LEU 296 296 296 LEU LEU A . n 
A 1 297 PRO 297 297 297 PRO PRO A . n 
A 1 298 PHE 298 298 298 PHE PHE A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 ASN 300 300 300 ASN ASN A . n 
A 1 301 ILE 301 301 301 ILE ILE A . n 
A 1 302 HIS 302 302 302 HIS HIS A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 ILE 304 304 304 ILE ILE A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 ILE 306 306 306 ILE ILE A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 CYS 309 309 309 CYS CYS A . n 
A 1 310 PRO 310 310 310 PRO PRO A . n 
A 1 311 LYS 311 311 311 LYS LYS A . n 
A 1 312 TYR 312 312 312 TYR TYR A . n 
A 1 313 VAL 313 313 313 VAL VAL A . n 
A 1 314 LYS 314 314 314 LYS LYS A . n 
A 1 315 SER 315 315 315 SER SER A . n 
A 1 316 THR 316 316 316 THR THR A . n 
A 1 317 LYS 317 317 317 LYS LYS A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 ARG 319 319 319 ARG ARG A . n 
A 1 320 LEU 320 320 320 LEU LEU A . n 
A 1 321 ALA 321 321 321 ALA ALA A . n 
A 1 322 THR 322 322 322 THR THR A . n 
A 1 323 GLY 323 323 323 GLY GLY A . n 
A 1 324 LEU 324 324 324 LEU LEU A . n 
A 1 325 ARG 325 325 325 ARG ARG A . n 
A 1 326 ASN 326 326 326 ASN ASN A . n 
A 1 327 ILE 327 327 327 ILE ILE A . n 
A 1 328 PRO 328 328 ?   ?   ?   A . n 
A 1 329 SER 329 329 ?   ?   ?   A . n 
A 1 330 ILE 330 330 ?   ?   ?   A . n 
A 1 331 GLN 331 331 ?   ?   ?   A . n 
A 1 332 SER 332 332 ?   ?   ?   A . n 
A 1 333 ARG 333 333 ?   ?   ?   A . n 
B 2 1   GLY 1   1   1   GLY GLY B . n 
B 2 2   LEU 2   2   2   LEU LEU B . n 
B 2 3   PHE 3   3   3   PHE PHE B . n 
B 2 4   GLY 4   4   4   GLY GLY B . n 
B 2 5   ALA 5   5   5   ALA ALA B . n 
B 2 6   ILE 6   6   6   ILE ILE B . n 
B 2 7   ALA 7   7   7   ALA ALA B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   PHE 9   9   9   PHE PHE B . n 
B 2 10  ILE 10  10  10  ILE ILE B . n 
B 2 11  GLU 11  11  11  GLU GLU B . n 
B 2 12  GLY 12  12  12  GLY GLY B . n 
B 2 13  GLY 13  13  13  GLY GLY B . n 
B 2 14  TRP 14  14  14  TRP TRP B . n 
B 2 15  THR 15  15  15  THR THR B . n 
B 2 16  GLY 16  16  16  GLY GLY B . n 
B 2 17  MET 17  17  17  MET MET B . n 
B 2 18  VAL 18  18  18  VAL VAL B . n 
B 2 19  ASP 19  19  19  ASP ASP B . n 
B 2 20  GLY 20  20  20  GLY GLY B . n 
B 2 21  TRP 21  21  21  TRP TRP B . n 
B 2 22  TYR 22  22  22  TYR TYR B . n 
B 2 23  GLY 23  23  23  GLY GLY B . n 
B 2 24  TYR 24  24  24  TYR TYR B . n 
B 2 25  HIS 25  25  25  HIS HIS B . n 
B 2 26  HIS 26  26  26  HIS HIS B . n 
B 2 27  GLN 27  27  27  GLN GLN B . n 
B 2 28  ASN 28  28  28  ASN ASN B . n 
B 2 29  GLU 29  29  29  GLU GLU B . n 
B 2 30  GLN 30  30  30  GLN GLN B . n 
B 2 31  GLY 31  31  31  GLY GLY B . n 
B 2 32  SER 32  32  32  SER SER B . n 
B 2 33  GLY 33  33  33  GLY GLY B . n 
B 2 34  TYR 34  34  34  TYR TYR B . n 
B 2 35  ALA 35  35  35  ALA ALA B . n 
B 2 36  ALA 36  36  36  ALA ALA B . n 
B 2 37  ASP 37  37  37  ASP ASP B . n 
B 2 38  LEU 38  38  38  LEU LEU B . n 
B 2 39  LYS 39  39  39  LYS LYS B . n 
B 2 40  SER 40  40  40  SER SER B . n 
B 2 41  THR 41  41  41  THR THR B . n 
B 2 42  GLN 42  42  42  GLN GLN B . n 
B 2 43  ASN 43  43  43  ASN ASN B . n 
B 2 44  ALA 44  44  44  ALA ALA B . n 
B 2 45  ILE 45  45  45  ILE ILE B . n 
B 2 46  ASP 46  46  46  ASP ASP B . n 
B 2 47  GLU 47  47  47  GLU GLU B . n 
B 2 48  ILE 48  48  48  ILE ILE B . n 
B 2 49  THR 49  49  49  THR THR B . n 
B 2 50  ASN 50  50  50  ASN ASN B . n 
B 2 51  LYS 51  51  51  LYS LYS B . n 
B 2 52  VAL 52  52  52  VAL VAL B . n 
B 2 53  ASN 53  53  53  ASN ASN B . n 
B 2 54  SER 54  54  54  SER SER B . n 
B 2 55  VAL 55  55  55  VAL VAL B . n 
B 2 56  ILE 56  56  56  ILE ILE B . n 
B 2 57  GLU 57  57  57  GLU GLU B . n 
B 2 58  LYS 58  58  58  LYS LYS B . n 
B 2 59  MET 59  59  59  MET MET B . n 
B 2 60  ASN 60  60  60  ASN ASN B . n 
B 2 61  THR 61  61  61  THR THR B . n 
B 2 62  GLN 62  62  62  GLN GLN B . n 
B 2 63  PHE 63  63  63  PHE PHE B . n 
B 2 64  THR 64  64  64  THR THR B . n 
B 2 65  ALA 65  65  65  ALA ALA B . n 
B 2 66  VAL 66  66  66  VAL VAL B . n 
B 2 67  GLY 67  67  67  GLY GLY B . n 
B 2 68  LYS 68  68  68  LYS LYS B . n 
B 2 69  GLU 69  69  69  GLU GLU B . n 
B 2 70  PHE 70  70  70  PHE PHE B . n 
B 2 71  ASN 71  71  71  ASN ASN B . n 
B 2 72  HIS 72  72  72  HIS HIS B . n 
B 2 73  LEU 73  73  73  LEU LEU B . n 
B 2 74  GLU 74  74  74  GLU GLU B . n 
B 2 75  LYS 75  75  75  LYS LYS B . n 
B 2 76  ARG 76  76  76  ARG ARG B . n 
B 2 77  ILE 77  77  77  ILE ILE B . n 
B 2 78  GLU 78  78  78  GLU GLU B . n 
B 2 79  ASN 79  79  79  ASN ASN B . n 
B 2 80  LEU 80  80  80  LEU LEU B . n 
B 2 81  ASN 81  81  81  ASN ASN B . n 
B 2 82  LYS 82  82  82  LYS LYS B . n 
B 2 83  LYS 83  83  83  LYS LYS B . n 
B 2 84  VAL 84  84  84  VAL VAL B . n 
B 2 85  ASP 85  85  85  ASP ASP B . n 
B 2 86  ASP 86  86  86  ASP ASP B . n 
B 2 87  GLY 87  87  87  GLY GLY B . n 
B 2 88  PHE 88  88  88  PHE PHE B . n 
B 2 89  LEU 89  89  89  LEU LEU B . n 
B 2 90  ASP 90  90  90  ASP ASP B . n 
B 2 91  ILE 91  91  91  ILE ILE B . n 
B 2 92  TRP 92  92  92  TRP TRP B . n 
B 2 93  THR 93  93  93  THR THR B . n 
B 2 94  TYR 94  94  94  TYR TYR B . n 
B 2 95  ASN 95  95  95  ASN ASN B . n 
B 2 96  ALA 96  96  96  ALA ALA B . n 
B 2 97  GLU 97  97  97  GLU GLU B . n 
B 2 98  LEU 98  98  98  LEU LEU B . n 
B 2 99  LEU 99  99  99  LEU LEU B . n 
B 2 100 VAL 100 100 100 VAL VAL B . n 
B 2 101 LEU 101 101 101 LEU LEU B . n 
B 2 102 LEU 102 102 102 LEU LEU B . n 
B 2 103 GLU 103 103 103 GLU GLU B . n 
B 2 104 ASN 104 104 104 ASN ASN B . n 
B 2 105 GLU 105 105 105 GLU GLU B . n 
B 2 106 ARG 106 106 106 ARG ARG B . n 
B 2 107 THR 107 107 107 THR THR B . n 
B 2 108 LEU 108 108 108 LEU LEU B . n 
B 2 109 ASP 109 109 109 ASP ASP B . n 
B 2 110 TYR 110 110 110 TYR TYR B . n 
B 2 111 HIS 111 111 111 HIS HIS B . n 
B 2 112 ASP 112 112 112 ASP ASP B . n 
B 2 113 SER 113 113 113 SER SER B . n 
B 2 114 ASN 114 114 114 ASN ASN B . n 
B 2 115 VAL 115 115 115 VAL VAL B . n 
B 2 116 LYS 116 116 116 LYS LYS B . n 
B 2 117 ASN 117 117 117 ASN ASN B . n 
B 2 118 LEU 118 118 118 LEU LEU B . n 
B 2 119 TYR 119 119 119 TYR TYR B . n 
B 2 120 GLU 120 120 120 GLU GLU B . n 
B 2 121 LYS 121 121 121 LYS LYS B . n 
B 2 122 VAL 122 122 122 VAL VAL B . n 
B 2 123 ARG 123 123 123 ARG ARG B . n 
B 2 124 SER 124 124 124 SER SER B . n 
B 2 125 GLN 125 125 125 GLN GLN B . n 
B 2 126 LEU 126 126 126 LEU LEU B . n 
B 2 127 LYS 127 127 127 LYS LYS B . n 
B 2 128 ASN 128 128 128 ASN ASN B . n 
B 2 129 ASN 129 129 129 ASN ASN B . n 
B 2 130 ALA 130 130 130 ALA ALA B . n 
B 2 131 LYS 131 131 131 LYS LYS B . n 
B 2 132 GLU 132 132 132 GLU GLU B . n 
B 2 133 ILE 133 133 133 ILE ILE B . n 
B 2 134 GLY 134 134 134 GLY GLY B . n 
B 2 135 ASN 135 135 135 ASN ASN B . n 
B 2 136 GLY 136 136 136 GLY GLY B . n 
B 2 137 CYS 137 137 137 CYS CYS B . n 
B 2 138 PHE 138 138 138 PHE PHE B . n 
B 2 139 GLU 139 139 139 GLU GLU B . n 
B 2 140 PHE 140 140 140 PHE PHE B . n 
B 2 141 TYR 141 141 141 TYR TYR B . n 
B 2 142 HIS 142 142 142 HIS HIS B . n 
B 2 143 LYS 143 143 143 LYS LYS B . n 
B 2 144 CYS 144 144 144 CYS CYS B . n 
B 2 145 ASP 145 145 145 ASP ASP B . n 
B 2 146 ASN 146 146 146 ASN ASN B . n 
B 2 147 THR 147 147 147 THR THR B . n 
B 2 148 CYS 148 148 148 CYS CYS B . n 
B 2 149 MET 149 149 149 MET MET B . n 
B 2 150 GLU 150 150 150 GLU GLU B . n 
B 2 151 SER 151 151 151 SER SER B . n 
B 2 152 VAL 152 152 152 VAL VAL B . n 
B 2 153 LYS 153 153 153 LYS LYS B . n 
B 2 154 ASN 154 154 154 ASN ASN B . n 
B 2 155 GLY 155 155 155 GLY GLY B . n 
B 2 156 THR 156 156 156 THR THR B . n 
B 2 157 TYR 157 157 157 TYR TYR B . n 
B 2 158 ASP 158 158 158 ASP ASP B . n 
B 2 159 TYR 159 159 159 TYR TYR B . n 
B 2 160 PRO 160 160 160 PRO PRO B . n 
B 2 161 LYS 161 161 161 LYS LYS B . n 
B 2 162 TYR 162 162 162 TYR TYR B . n 
B 2 163 SER 163 163 ?   ?   ?   B . n 
B 2 164 GLU 164 164 ?   ?   ?   B . n 
B 2 165 GLU 165 165 ?   ?   ?   B . n 
B 2 166 ALA 166 166 ?   ?   ?   B . n 
B 2 167 LYS 167 167 ?   ?   ?   B . n 
B 2 168 LEU 168 168 ?   ?   ?   B . n 
B 2 169 ASN 169 169 ?   ?   ?   B . n 
B 2 170 ARG 170 170 ?   ?   ?   B . n 
B 2 171 GLU 171 171 ?   ?   ?   B . n 
B 2 172 GLU 172 172 ?   ?   ?   B . n 
B 2 173 ILE 173 173 ?   ?   ?   B . n 
B 2 174 ASP 174 174 ?   ?   ?   B . n 
B 2 175 GLY 175 175 ?   ?   ?   B . n 
B 2 176 VAL 176 176 ?   ?   ?   B . n 
B 2 177 ARG 177 177 ?   ?   ?   B . n 
B 2 178 LEU 178 178 ?   ?   ?   B . n 
B 2 179 VAL 179 179 ?   ?   ?   B . n 
B 2 180 PRO 180 180 ?   ?   ?   B . n 
B 2 181 ARG 181 181 ?   ?   ?   B . n 
C 1 1   ALA 1   1   ?   ?   ?   C . n 
C 1 2   ASP 2   2   ?   ?   ?   C . n 
C 1 3   LEU 3   3   ?   ?   ?   C . n 
C 1 4   GLY 4   4   ?   ?   ?   C . n 
C 1 5   SER 5   5   ?   ?   ?   C . n 
C 1 6   ARG 6   6   ?   ?   ?   C . n 
C 1 7   ASP 7   7   7   ASP ASP C . n 
C 1 8   THR 8   8   8   THR THR C . n 
C 1 9   LEU 9   9   9   LEU LEU C . n 
C 1 10  CYS 10  10  10  CYS CYS C . n 
C 1 11  ILE 11  11  11  ILE ILE C . n 
C 1 12  GLY 12  12  12  GLY GLY C . n 
C 1 13  TYR 13  13  13  TYR TYR C . n 
C 1 14  HIS 14  14  14  HIS HIS C . n 
C 1 15  ALA 15  15  15  ALA ALA C . n 
C 1 16  ASN 16  16  16  ASN ASN C . n 
C 1 17  ASN 17  17  17  ASN ASN C . n 
C 1 18  SER 18  18  18  SER SER C . n 
C 1 19  THR 19  19  19  THR THR C . n 
C 1 20  ASP 20  20  20  ASP ASP C . n 
C 1 21  THR 21  21  21  THR THR C . n 
C 1 22  VAL 22  22  22  VAL VAL C . n 
C 1 23  ASP 23  23  23  ASP ASP C . n 
C 1 24  THR 24  24  24  THR THR C . n 
C 1 25  VAL 25  25  25  VAL VAL C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLU 27  27  27  GLU GLU C . n 
C 1 28  LYS 28  28  28  LYS LYS C . n 
C 1 29  ASN 29  29  29  ASN ASN C . n 
C 1 30  VAL 30  30  30  VAL VAL C . n 
C 1 31  THR 31  31  31  THR THR C . n 
C 1 32  VAL 32  32  32  VAL VAL C . n 
C 1 33  THR 33  33  33  THR THR C . n 
C 1 34  HIS 34  34  34  HIS HIS C . n 
C 1 35  SER 35  35  35  SER SER C . n 
C 1 36  VAL 36  36  36  VAL VAL C . n 
C 1 37  ASN 37  37  37  ASN ASN C . n 
C 1 38  LEU 38  38  38  LEU LEU C . n 
C 1 39  LEU 39  39  39  LEU LEU C . n 
C 1 40  GLU 40  40  40  GLU GLU C . n 
C 1 41  ASP 41  41  41  ASP ASP C . n 
C 1 42  LYS 42  42  42  LYS LYS C . n 
C 1 43  HIS 43  43  43  HIS HIS C . n 
C 1 44  ASN 44  44  44  ASN ASN C . n 
C 1 45  GLY 45  45  45  GLY GLY C . n 
C 1 46  LYS 46  46  46  LYS LYS C . n 
C 1 47  LEU 47  47  47  LEU LEU C . n 
C 1 48  CYS 48  48  48  CYS CYS C . n 
C 1 49  LYS 49  49  49  LYS LYS C . n 
C 1 50  LEU 50  50  50  LEU LEU C . n 
C 1 51  ARG 51  51  51  ARG ARG C . n 
C 1 52  GLY 52  52  52  GLY GLY C . n 
C 1 53  VAL 53  53  53  VAL VAL C . n 
C 1 54  ALA 54  54  54  ALA ALA C . n 
C 1 55  PRO 55  55  55  PRO PRO C . n 
C 1 56  LEU 56  56  56  LEU LEU C . n 
C 1 57  HIS 57  57  57  HIS HIS C . n 
C 1 58  LEU 58  58  58  LEU LEU C . n 
C 1 59  GLY 59  59  59  GLY GLY C . n 
C 1 60  LYS 60  60  60  LYS LYS C . n 
C 1 61  CYS 61  61  61  CYS CYS C . n 
C 1 62  ASN 62  62  62  ASN ASN C . n 
C 1 63  ILE 63  63  63  ILE ILE C . n 
C 1 64  ALA 64  64  64  ALA ALA C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  TRP 66  66  66  TRP TRP C . n 
C 1 67  ILE 67  67  67  ILE ILE C . n 
C 1 68  LEU 68  68  68  LEU LEU C . n 
C 1 69  GLY 69  69  69  GLY GLY C . n 
C 1 70  ASN 70  70  70  ASN ASN C . n 
C 1 71  PRO 71  71  71  PRO PRO C . n 
C 1 72  GLU 72  72  72  GLU GLU C . n 
C 1 73  CYS 73  73  73  CYS CYS C . n 
C 1 74  GLU 74  74  74  GLU GLU C . n 
C 1 75  SER 75  75  75  SER SER C . n 
C 1 76  LEU 76  76  76  LEU LEU C . n 
C 1 77  SER 77  77  77  SER SER C . n 
C 1 78  THR 78  78  78  THR THR C . n 
C 1 79  ALA 79  79  79  ALA ALA C . n 
C 1 80  SER 80  80  80  SER SER C . n 
C 1 81  SER 81  81  81  SER SER C . n 
C 1 82  TRP 82  82  82  TRP TRP C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  TYR 84  84  84  TYR TYR C . n 
C 1 85  ILE 85  85  85  ILE ILE C . n 
C 1 86  VAL 86  86  86  VAL VAL C . n 
C 1 87  GLU 87  87  87  GLU GLU C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  PRO 89  89  89  PRO PRO C . n 
C 1 90  SER 90  90  90  SER SER C . n 
C 1 91  SER 91  91  91  SER SER C . n 
C 1 92  ASP 92  92  92  ASP ASP C . n 
C 1 93  ASN 93  93  93  ASN ASN C . n 
C 1 94  GLY 94  94  94  GLY GLY C . n 
C 1 95  THR 95  95  95  THR THR C . n 
C 1 96  CYS 96  96  96  CYS CYS C . n 
C 1 97  TYR 97  97  97  TYR TYR C . n 
C 1 98  PRO 98  98  98  PRO PRO C . n 
C 1 99  GLY 99  99  99  GLY GLY C . n 
C 1 100 ASP 100 100 100 ASP ASP C . n 
C 1 101 PHE 101 101 101 PHE PHE C . n 
C 1 102 ILE 102 102 102 ILE ILE C . n 
C 1 103 ASP 103 103 103 ASP ASP C . n 
C 1 104 TYR 104 104 104 TYR TYR C . n 
C 1 105 GLU 105 105 105 GLU GLU C . n 
C 1 106 GLU 106 106 106 GLU GLU C . n 
C 1 107 LEU 107 107 107 LEU LEU C . n 
C 1 108 ARG 108 108 108 ARG ARG C . n 
C 1 109 GLU 109 109 109 GLU GLU C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 LEU 111 111 111 LEU LEU C . n 
C 1 112 SER 112 112 112 SER SER C . n 
C 1 113 SER 113 113 113 SER SER C . n 
C 1 114 VAL 114 114 114 VAL VAL C . n 
C 1 115 SER 115 115 115 SER SER C . n 
C 1 116 SER 116 116 116 SER SER C . n 
C 1 117 PHE 117 117 117 PHE PHE C . n 
C 1 118 GLU 118 118 118 GLU GLU C . n 
C 1 119 ARG 119 119 119 ARG ARG C . n 
C 1 120 PHE 120 120 120 PHE PHE C . n 
C 1 121 GLU 121 121 121 GLU GLU C . n 
C 1 122 ILE 122 122 122 ILE ILE C . n 
C 1 123 PHE 123 123 123 PHE PHE C . n 
C 1 124 PRO 124 124 124 PRO PRO C . n 
C 1 125 LYS 125 125 125 LYS LYS C . n 
C 1 126 THR 126 126 126 THR THR C . n 
C 1 127 SER 127 127 127 SER SER C . n 
C 1 128 SER 128 128 128 SER SER C . n 
C 1 129 TRP 129 129 129 TRP TRP C . n 
C 1 130 PRO 130 130 130 PRO PRO C . n 
C 1 131 ASN 131 131 131 ASN ASN C . n 
C 1 132 HIS 132 132 132 HIS HIS C . n 
C 1 133 ASP 133 133 133 ASP ASP C . n 
C 1 134 SER 134 134 134 SER SER C . n 
C 1 135 ASN 135 135 135 ASN ASN C . n 
C 1 136 LYS 136 136 136 LYS LYS C . n 
C 1 137 GLY 137 137 137 GLY GLY C . n 
C 1 138 VAL 138 138 138 VAL VAL C . n 
C 1 139 THR 139 139 139 THR THR C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 ALA 141 141 141 ALA ALA C . n 
C 1 142 CYS 142 142 142 CYS CYS C . n 
C 1 143 PRO 143 143 143 PRO PRO C . n 
C 1 144 HIS 144 144 144 HIS HIS C . n 
C 1 145 ALA 145 145 145 ALA ALA C . n 
C 1 146 GLY 146 146 146 GLY GLY C . n 
C 1 147 ALA 147 147 147 ALA ALA C . n 
C 1 148 LYS 148 148 148 LYS LYS C . n 
C 1 149 SER 149 149 149 SER SER C . n 
C 1 150 PHE 150 150 150 PHE PHE C . n 
C 1 151 TYR 151 151 151 TYR TYR C . n 
C 1 152 LYS 152 152 152 LYS LYS C . n 
C 1 153 ASN 153 153 153 ASN ASN C . n 
C 1 154 LEU 154 154 154 LEU LEU C . n 
C 1 155 ILE 155 155 155 ILE ILE C . n 
C 1 156 TRP 156 156 156 TRP TRP C . n 
C 1 157 LEU 157 157 157 LEU LEU C . n 
C 1 158 VAL 158 158 158 VAL VAL C . n 
C 1 159 LYS 159 159 159 LYS LYS C . n 
C 1 160 LYS 160 160 160 LYS LYS C . n 
C 1 161 GLY 161 161 161 GLY GLY C . n 
C 1 162 ASN 162 162 162 ASN ASN C . n 
C 1 163 SER 163 163 163 SER SER C . n 
C 1 164 TYR 164 164 164 TYR TYR C . n 
C 1 165 PRO 165 165 165 PRO PRO C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 LEU 167 167 167 LEU LEU C . n 
C 1 168 SER 168 168 168 SER SER C . n 
C 1 169 LYS 169 169 169 LYS LYS C . n 
C 1 170 SER 170 170 170 SER SER C . n 
C 1 171 TYR 171 171 171 TYR TYR C . n 
C 1 172 ILE 172 172 172 ILE ILE C . n 
C 1 173 ASN 173 173 173 ASN ASN C . n 
C 1 174 ASP 174 174 174 ASP ASP C . n 
C 1 175 LYS 175 175 175 LYS LYS C . n 
C 1 176 GLY 176 176 176 GLY GLY C . n 
C 1 177 LYS 177 177 177 LYS LYS C . n 
C 1 178 GLU 178 178 178 GLU GLU C . n 
C 1 179 VAL 179 179 179 VAL VAL C . n 
C 1 180 LEU 180 180 180 LEU LEU C . n 
C 1 181 VAL 181 181 181 VAL VAL C . n 
C 1 182 LEU 182 182 182 LEU LEU C . n 
C 1 183 TRP 183 183 183 TRP TRP C . n 
C 1 184 GLY 184 184 184 GLY GLY C . n 
C 1 185 ILE 185 185 185 ILE ILE C . n 
C 1 186 HIS 186 186 186 HIS HIS C . n 
C 1 187 HIS 187 187 187 HIS HIS C . n 
C 1 188 PRO 188 188 188 PRO PRO C . n 
C 1 189 SER 189 189 189 SER SER C . n 
C 1 190 THR 190 190 190 THR THR C . n 
C 1 191 SER 191 191 191 SER SER C . n 
C 1 192 ALA 192 192 192 ALA ALA C . n 
C 1 193 ASP 193 193 193 ASP ASP C . n 
C 1 194 GLN 194 194 194 GLN GLN C . n 
C 1 195 GLN 195 195 195 GLN GLN C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 LEU 197 197 197 LEU LEU C . n 
C 1 198 TYR 198 198 198 TYR TYR C . n 
C 1 199 GLN 199 199 199 GLN GLN C . n 
C 1 200 ASN 200 200 200 ASN ASN C . n 
C 1 201 ALA 201 201 201 ALA ALA C . n 
C 1 202 ASP 202 202 202 ASP ASP C . n 
C 1 203 THR 203 203 203 THR THR C . n 
C 1 204 TYR 204 204 204 TYR TYR C . n 
C 1 205 VAL 205 205 205 VAL VAL C . n 
C 1 206 PHE 206 206 206 PHE PHE C . n 
C 1 207 VAL 207 207 207 VAL VAL C . n 
C 1 208 GLY 208 208 208 GLY GLY C . n 
C 1 209 SER 209 209 209 SER SER C . n 
C 1 210 SER 210 210 210 SER SER C . n 
C 1 211 ARG 211 211 211 ARG ARG C . n 
C 1 212 TYR 212 212 212 TYR TYR C . n 
C 1 213 SER 213 213 213 SER SER C . n 
C 1 214 LYS 214 214 214 LYS LYS C . n 
C 1 215 LYS 215 215 215 LYS LYS C . n 
C 1 216 PHE 216 216 216 PHE PHE C . n 
C 1 217 LYS 217 217 217 LYS LYS C . n 
C 1 218 PRO 218 218 218 PRO PRO C . n 
C 1 219 GLU 219 219 219 GLU GLU C . n 
C 1 220 ILE 220 220 220 ILE ILE C . n 
C 1 221 ALA 221 221 221 ALA ALA C . n 
C 1 222 ILE 222 222 222 ILE ILE C . n 
C 1 223 ARG 223 223 223 ARG ARG C . n 
C 1 224 PRO 224 224 224 PRO PRO C . n 
C 1 225 LYS 225 225 225 LYS LYS C . n 
C 1 226 VAL 226 226 226 VAL VAL C . n 
C 1 227 ARG 227 227 227 ARG ARG C . n 
C 1 228 ASP 228 228 228 ASP ASP C . n 
C 1 229 GLN 229 229 229 GLN GLN C . n 
C 1 230 GLU 230 230 230 GLU GLU C . n 
C 1 231 GLY 231 231 231 GLY GLY C . n 
C 1 232 ARG 232 232 232 ARG ARG C . n 
C 1 233 MET 233 233 233 MET MET C . n 
C 1 234 ASN 234 234 234 ASN ASN C . n 
C 1 235 TYR 235 235 235 TYR TYR C . n 
C 1 236 TYR 236 236 236 TYR TYR C . n 
C 1 237 TRP 237 237 237 TRP TRP C . n 
C 1 238 THR 238 238 238 THR THR C . n 
C 1 239 LEU 239 239 239 LEU LEU C . n 
C 1 240 VAL 240 240 240 VAL VAL C . n 
C 1 241 GLU 241 241 241 GLU GLU C . n 
C 1 242 PRO 242 242 242 PRO PRO C . n 
C 1 243 GLY 243 243 243 GLY GLY C . n 
C 1 244 ASP 244 244 244 ASP ASP C . n 
C 1 245 LYS 245 245 245 LYS LYS C . n 
C 1 246 ILE 246 246 246 ILE ILE C . n 
C 1 247 THR 247 247 247 THR THR C . n 
C 1 248 PHE 248 248 248 PHE PHE C . n 
C 1 249 GLU 249 249 249 GLU GLU C . n 
C 1 250 ALA 250 250 250 ALA ALA C . n 
C 1 251 THR 251 251 251 THR THR C . n 
C 1 252 GLY 252 252 252 GLY GLY C . n 
C 1 253 ASN 253 253 253 ASN ASN C . n 
C 1 254 LEU 254 254 254 LEU LEU C . n 
C 1 255 VAL 255 255 255 VAL VAL C . n 
C 1 256 VAL 256 256 256 VAL VAL C . n 
C 1 257 PRO 257 257 257 PRO PRO C . n 
C 1 258 ARG 258 258 258 ARG ARG C . n 
C 1 259 TYR 259 259 259 TYR TYR C . n 
C 1 260 ALA 260 260 260 ALA ALA C . n 
C 1 261 PHE 261 261 261 PHE PHE C . n 
C 1 262 ALA 262 262 262 ALA ALA C . n 
C 1 263 MET 263 263 263 MET MET C . n 
C 1 264 GLU 264 264 264 GLU GLU C . n 
C 1 265 ARG 265 265 265 ARG ARG C . n 
C 1 266 ASN 266 266 266 ASN ASN C . n 
C 1 267 ALA 267 267 267 ALA ALA C . n 
C 1 268 GLY 268 268 268 GLY GLY C . n 
C 1 269 SER 269 269 269 SER SER C . n 
C 1 270 GLY 270 270 270 GLY GLY C . n 
C 1 271 ILE 271 271 271 ILE ILE C . n 
C 1 272 ILE 272 272 272 ILE ILE C . n 
C 1 273 ILE 273 273 273 ILE ILE C . n 
C 1 274 SER 274 274 274 SER SER C . n 
C 1 275 ASP 275 275 275 ASP ASP C . n 
C 1 276 THR 276 276 276 THR THR C . n 
C 1 277 PRO 277 277 277 PRO PRO C . n 
C 1 278 VAL 278 278 278 VAL VAL C . n 
C 1 279 HIS 279 279 279 HIS HIS C . n 
C 1 280 ASP 280 280 280 ASP ASP C . n 
C 1 281 CYS 281 281 281 CYS CYS C . n 
C 1 282 ASN 282 282 282 ASN ASN C . n 
C 1 283 THR 283 283 283 THR THR C . n 
C 1 284 THR 284 284 284 THR THR C . n 
C 1 285 CYS 285 285 285 CYS CYS C . n 
C 1 286 GLN 286 286 286 GLN GLN C . n 
C 1 287 THR 287 287 287 THR THR C . n 
C 1 288 PRO 288 288 288 PRO PRO C . n 
C 1 289 LYS 289 289 289 LYS LYS C . n 
C 1 290 GLY 290 290 290 GLY GLY C . n 
C 1 291 ALA 291 291 291 ALA ALA C . n 
C 1 292 ILE 292 292 292 ILE ILE C . n 
C 1 293 ASN 293 293 293 ASN ASN C . n 
C 1 294 THR 294 294 294 THR THR C . n 
C 1 295 SER 295 295 295 SER SER C . n 
C 1 296 LEU 296 296 296 LEU LEU C . n 
C 1 297 PRO 297 297 297 PRO PRO C . n 
C 1 298 PHE 298 298 298 PHE PHE C . n 
C 1 299 GLN 299 299 299 GLN GLN C . n 
C 1 300 ASN 300 300 300 ASN ASN C . n 
C 1 301 ILE 301 301 301 ILE ILE C . n 
C 1 302 HIS 302 302 302 HIS HIS C . n 
C 1 303 PRO 303 303 303 PRO PRO C . n 
C 1 304 ILE 304 304 304 ILE ILE C . n 
C 1 305 THR 305 305 305 THR THR C . n 
C 1 306 ILE 306 306 306 ILE ILE C . n 
C 1 307 GLY 307 307 307 GLY GLY C . n 
C 1 308 LYS 308 308 308 LYS LYS C . n 
C 1 309 CYS 309 309 309 CYS CYS C . n 
C 1 310 PRO 310 310 310 PRO PRO C . n 
C 1 311 LYS 311 311 311 LYS LYS C . n 
C 1 312 TYR 312 312 312 TYR TYR C . n 
C 1 313 VAL 313 313 313 VAL VAL C . n 
C 1 314 LYS 314 314 314 LYS LYS C . n 
C 1 315 SER 315 315 315 SER SER C . n 
C 1 316 THR 316 316 316 THR THR C . n 
C 1 317 LYS 317 317 317 LYS LYS C . n 
C 1 318 LEU 318 318 318 LEU LEU C . n 
C 1 319 ARG 319 319 319 ARG ARG C . n 
C 1 320 LEU 320 320 320 LEU LEU C . n 
C 1 321 ALA 321 321 321 ALA ALA C . n 
C 1 322 THR 322 322 322 THR THR C . n 
C 1 323 GLY 323 323 323 GLY GLY C . n 
C 1 324 LEU 324 324 324 LEU LEU C . n 
C 1 325 ARG 325 325 325 ARG ARG C . n 
C 1 326 ASN 326 326 326 ASN ASN C . n 
C 1 327 ILE 327 327 327 ILE ILE C . n 
C 1 328 PRO 328 328 ?   ?   ?   C . n 
C 1 329 SER 329 329 ?   ?   ?   C . n 
C 1 330 ILE 330 330 ?   ?   ?   C . n 
C 1 331 GLN 331 331 ?   ?   ?   C . n 
C 1 332 SER 332 332 ?   ?   ?   C . n 
C 1 333 ARG 333 333 ?   ?   ?   C . n 
D 2 1   GLY 1   1   1   GLY GLY D . n 
D 2 2   LEU 2   2   2   LEU LEU D . n 
D 2 3   PHE 3   3   3   PHE PHE D . n 
D 2 4   GLY 4   4   4   GLY GLY D . n 
D 2 5   ALA 5   5   5   ALA ALA D . n 
D 2 6   ILE 6   6   6   ILE ILE D . n 
D 2 7   ALA 7   7   7   ALA ALA D . n 
D 2 8   GLY 8   8   8   GLY GLY D . n 
D 2 9   PHE 9   9   9   PHE PHE D . n 
D 2 10  ILE 10  10  10  ILE ILE D . n 
D 2 11  GLU 11  11  11  GLU GLU D . n 
D 2 12  GLY 12  12  12  GLY GLY D . n 
D 2 13  GLY 13  13  13  GLY GLY D . n 
D 2 14  TRP 14  14  14  TRP TRP D . n 
D 2 15  THR 15  15  15  THR THR D . n 
D 2 16  GLY 16  16  16  GLY GLY D . n 
D 2 17  MET 17  17  17  MET MET D . n 
D 2 18  VAL 18  18  18  VAL VAL D . n 
D 2 19  ASP 19  19  19  ASP ASP D . n 
D 2 20  GLY 20  20  20  GLY GLY D . n 
D 2 21  TRP 21  21  21  TRP TRP D . n 
D 2 22  TYR 22  22  22  TYR TYR D . n 
D 2 23  GLY 23  23  23  GLY GLY D . n 
D 2 24  TYR 24  24  24  TYR TYR D . n 
D 2 25  HIS 25  25  25  HIS HIS D . n 
D 2 26  HIS 26  26  26  HIS HIS D . n 
D 2 27  GLN 27  27  27  GLN GLN D . n 
D 2 28  ASN 28  28  28  ASN ASN D . n 
D 2 29  GLU 29  29  29  GLU GLU D . n 
D 2 30  GLN 30  30  30  GLN GLN D . n 
D 2 31  GLY 31  31  31  GLY GLY D . n 
D 2 32  SER 32  32  32  SER SER D . n 
D 2 33  GLY 33  33  33  GLY GLY D . n 
D 2 34  TYR 34  34  34  TYR TYR D . n 
D 2 35  ALA 35  35  35  ALA ALA D . n 
D 2 36  ALA 36  36  36  ALA ALA D . n 
D 2 37  ASP 37  37  37  ASP ASP D . n 
D 2 38  LEU 38  38  38  LEU LEU D . n 
D 2 39  LYS 39  39  39  LYS LYS D . n 
D 2 40  SER 40  40  40  SER SER D . n 
D 2 41  THR 41  41  41  THR THR D . n 
D 2 42  GLN 42  42  42  GLN GLN D . n 
D 2 43  ASN 43  43  43  ASN ASN D . n 
D 2 44  ALA 44  44  44  ALA ALA D . n 
D 2 45  ILE 45  45  45  ILE ILE D . n 
D 2 46  ASP 46  46  46  ASP ASP D . n 
D 2 47  GLU 47  47  47  GLU GLU D . n 
D 2 48  ILE 48  48  48  ILE ILE D . n 
D 2 49  THR 49  49  49  THR THR D . n 
D 2 50  ASN 50  50  50  ASN ASN D . n 
D 2 51  LYS 51  51  51  LYS LYS D . n 
D 2 52  VAL 52  52  52  VAL VAL D . n 
D 2 53  ASN 53  53  53  ASN ASN D . n 
D 2 54  SER 54  54  54  SER SER D . n 
D 2 55  VAL 55  55  55  VAL VAL D . n 
D 2 56  ILE 56  56  56  ILE ILE D . n 
D 2 57  GLU 57  57  57  GLU GLU D . n 
D 2 58  LYS 58  58  58  LYS LYS D . n 
D 2 59  MET 59  59  59  MET MET D . n 
D 2 60  ASN 60  60  60  ASN ASN D . n 
D 2 61  THR 61  61  61  THR THR D . n 
D 2 62  GLN 62  62  62  GLN GLN D . n 
D 2 63  PHE 63  63  63  PHE PHE D . n 
D 2 64  THR 64  64  64  THR THR D . n 
D 2 65  ALA 65  65  65  ALA ALA D . n 
D 2 66  VAL 66  66  66  VAL VAL D . n 
D 2 67  GLY 67  67  67  GLY GLY D . n 
D 2 68  LYS 68  68  68  LYS LYS D . n 
D 2 69  GLU 69  69  69  GLU GLU D . n 
D 2 70  PHE 70  70  70  PHE PHE D . n 
D 2 71  ASN 71  71  71  ASN ASN D . n 
D 2 72  HIS 72  72  72  HIS HIS D . n 
D 2 73  LEU 73  73  73  LEU LEU D . n 
D 2 74  GLU 74  74  74  GLU GLU D . n 
D 2 75  LYS 75  75  75  LYS LYS D . n 
D 2 76  ARG 76  76  76  ARG ARG D . n 
D 2 77  ILE 77  77  77  ILE ILE D . n 
D 2 78  GLU 78  78  78  GLU GLU D . n 
D 2 79  ASN 79  79  79  ASN ASN D . n 
D 2 80  LEU 80  80  80  LEU LEU D . n 
D 2 81  ASN 81  81  81  ASN ASN D . n 
D 2 82  LYS 82  82  82  LYS LYS D . n 
D 2 83  LYS 83  83  83  LYS LYS D . n 
D 2 84  VAL 84  84  84  VAL VAL D . n 
D 2 85  ASP 85  85  85  ASP ASP D . n 
D 2 86  ASP 86  86  86  ASP ASP D . n 
D 2 87  GLY 87  87  87  GLY GLY D . n 
D 2 88  PHE 88  88  88  PHE PHE D . n 
D 2 89  LEU 89  89  89  LEU LEU D . n 
D 2 90  ASP 90  90  90  ASP ASP D . n 
D 2 91  ILE 91  91  91  ILE ILE D . n 
D 2 92  TRP 92  92  92  TRP TRP D . n 
D 2 93  THR 93  93  93  THR THR D . n 
D 2 94  TYR 94  94  94  TYR TYR D . n 
D 2 95  ASN 95  95  95  ASN ASN D . n 
D 2 96  ALA 96  96  96  ALA ALA D . n 
D 2 97  GLU 97  97  97  GLU GLU D . n 
D 2 98  LEU 98  98  98  LEU LEU D . n 
D 2 99  LEU 99  99  99  LEU LEU D . n 
D 2 100 VAL 100 100 100 VAL VAL D . n 
D 2 101 LEU 101 101 101 LEU LEU D . n 
D 2 102 LEU 102 102 102 LEU LEU D . n 
D 2 103 GLU 103 103 103 GLU GLU D . n 
D 2 104 ASN 104 104 104 ASN ASN D . n 
D 2 105 GLU 105 105 105 GLU GLU D . n 
D 2 106 ARG 106 106 106 ARG ARG D . n 
D 2 107 THR 107 107 107 THR THR D . n 
D 2 108 LEU 108 108 108 LEU LEU D . n 
D 2 109 ASP 109 109 109 ASP ASP D . n 
D 2 110 TYR 110 110 110 TYR TYR D . n 
D 2 111 HIS 111 111 111 HIS HIS D . n 
D 2 112 ASP 112 112 112 ASP ASP D . n 
D 2 113 SER 113 113 113 SER SER D . n 
D 2 114 ASN 114 114 114 ASN ASN D . n 
D 2 115 VAL 115 115 115 VAL VAL D . n 
D 2 116 LYS 116 116 116 LYS LYS D . n 
D 2 117 ASN 117 117 117 ASN ASN D . n 
D 2 118 LEU 118 118 118 LEU LEU D . n 
D 2 119 TYR 119 119 119 TYR TYR D . n 
D 2 120 GLU 120 120 120 GLU GLU D . n 
D 2 121 LYS 121 121 121 LYS LYS D . n 
D 2 122 VAL 122 122 122 VAL VAL D . n 
D 2 123 ARG 123 123 123 ARG ARG D . n 
D 2 124 SER 124 124 124 SER SER D . n 
D 2 125 GLN 125 125 125 GLN GLN D . n 
D 2 126 LEU 126 126 126 LEU LEU D . n 
D 2 127 LYS 127 127 127 LYS LYS D . n 
D 2 128 ASN 128 128 128 ASN ASN D . n 
D 2 129 ASN 129 129 129 ASN ASN D . n 
D 2 130 ALA 130 130 130 ALA ALA D . n 
D 2 131 LYS 131 131 131 LYS LYS D . n 
D 2 132 GLU 132 132 132 GLU GLU D . n 
D 2 133 ILE 133 133 133 ILE ILE D . n 
D 2 134 GLY 134 134 134 GLY GLY D . n 
D 2 135 ASN 135 135 135 ASN ASN D . n 
D 2 136 GLY 136 136 136 GLY GLY D . n 
D 2 137 CYS 137 137 137 CYS CYS D . n 
D 2 138 PHE 138 138 138 PHE PHE D . n 
D 2 139 GLU 139 139 139 GLU GLU D . n 
D 2 140 PHE 140 140 140 PHE PHE D . n 
D 2 141 TYR 141 141 141 TYR TYR D . n 
D 2 142 HIS 142 142 142 HIS HIS D . n 
D 2 143 LYS 143 143 143 LYS LYS D . n 
D 2 144 CYS 144 144 144 CYS CYS D . n 
D 2 145 ASP 145 145 145 ASP ASP D . n 
D 2 146 ASN 146 146 146 ASN ASN D . n 
D 2 147 THR 147 147 147 THR THR D . n 
D 2 148 CYS 148 148 148 CYS CYS D . n 
D 2 149 MET 149 149 149 MET MET D . n 
D 2 150 GLU 150 150 150 GLU GLU D . n 
D 2 151 SER 151 151 151 SER SER D . n 
D 2 152 VAL 152 152 152 VAL VAL D . n 
D 2 153 LYS 153 153 153 LYS LYS D . n 
D 2 154 ASN 154 154 154 ASN ASN D . n 
D 2 155 GLY 155 155 155 GLY GLY D . n 
D 2 156 THR 156 156 156 THR THR D . n 
D 2 157 TYR 157 157 157 TYR TYR D . n 
D 2 158 ASP 158 158 158 ASP ASP D . n 
D 2 159 TYR 159 159 159 TYR TYR D . n 
D 2 160 PRO 160 160 160 PRO PRO D . n 
D 2 161 LYS 161 161 161 LYS LYS D . n 
D 2 162 TYR 162 162 162 TYR TYR D . n 
D 2 163 SER 163 163 ?   ?   ?   D . n 
D 2 164 GLU 164 164 ?   ?   ?   D . n 
D 2 165 GLU 165 165 ?   ?   ?   D . n 
D 2 166 ALA 166 166 ?   ?   ?   D . n 
D 2 167 LYS 167 167 ?   ?   ?   D . n 
D 2 168 LEU 168 168 ?   ?   ?   D . n 
D 2 169 ASN 169 169 ?   ?   ?   D . n 
D 2 170 ARG 170 170 ?   ?   ?   D . n 
D 2 171 GLU 171 171 ?   ?   ?   D . n 
D 2 172 GLU 172 172 ?   ?   ?   D . n 
D 2 173 ILE 173 173 ?   ?   ?   D . n 
D 2 174 ASP 174 174 ?   ?   ?   D . n 
D 2 175 GLY 175 175 ?   ?   ?   D . n 
D 2 176 VAL 176 176 ?   ?   ?   D . n 
D 2 177 ARG 177 177 ?   ?   ?   D . n 
D 2 178 LEU 178 178 ?   ?   ?   D . n 
D 2 179 VAL 179 179 ?   ?   ?   D . n 
D 2 180 PRO 180 180 ?   ?   ?   D . n 
D 2 181 ARG 181 181 ?   ?   ?   D . n 
E 1 1   ALA 1   1   ?   ?   ?   E . n 
E 1 2   ASP 2   2   ?   ?   ?   E . n 
E 1 3   LEU 3   3   ?   ?   ?   E . n 
E 1 4   GLY 4   4   ?   ?   ?   E . n 
E 1 5   SER 5   5   ?   ?   ?   E . n 
E 1 6   ARG 6   6   ?   ?   ?   E . n 
E 1 7   ASP 7   7   7   ASP ASP E . n 
E 1 8   THR 8   8   8   THR THR E . n 
E 1 9   LEU 9   9   9   LEU LEU E . n 
E 1 10  CYS 10  10  10  CYS CYS E . n 
E 1 11  ILE 11  11  11  ILE ILE E . n 
E 1 12  GLY 12  12  12  GLY GLY E . n 
E 1 13  TYR 13  13  13  TYR TYR E . n 
E 1 14  HIS 14  14  14  HIS HIS E . n 
E 1 15  ALA 15  15  15  ALA ALA E . n 
E 1 16  ASN 16  16  16  ASN ASN E . n 
E 1 17  ASN 17  17  17  ASN ASN E . n 
E 1 18  SER 18  18  18  SER SER E . n 
E 1 19  THR 19  19  19  THR THR E . n 
E 1 20  ASP 20  20  20  ASP ASP E . n 
E 1 21  THR 21  21  21  THR THR E . n 
E 1 22  VAL 22  22  22  VAL VAL E . n 
E 1 23  ASP 23  23  23  ASP ASP E . n 
E 1 24  THR 24  24  24  THR THR E . n 
E 1 25  VAL 25  25  25  VAL VAL E . n 
E 1 26  LEU 26  26  26  LEU LEU E . n 
E 1 27  GLU 27  27  27  GLU GLU E . n 
E 1 28  LYS 28  28  28  LYS LYS E . n 
E 1 29  ASN 29  29  29  ASN ASN E . n 
E 1 30  VAL 30  30  30  VAL VAL E . n 
E 1 31  THR 31  31  31  THR THR E . n 
E 1 32  VAL 32  32  32  VAL VAL E . n 
E 1 33  THR 33  33  33  THR THR E . n 
E 1 34  HIS 34  34  34  HIS HIS E . n 
E 1 35  SER 35  35  35  SER SER E . n 
E 1 36  VAL 36  36  36  VAL VAL E . n 
E 1 37  ASN 37  37  37  ASN ASN E . n 
E 1 38  LEU 38  38  38  LEU LEU E . n 
E 1 39  LEU 39  39  39  LEU LEU E . n 
E 1 40  GLU 40  40  40  GLU GLU E . n 
E 1 41  ASP 41  41  41  ASP ASP E . n 
E 1 42  LYS 42  42  42  LYS LYS E . n 
E 1 43  HIS 43  43  43  HIS HIS E . n 
E 1 44  ASN 44  44  44  ASN ASN E . n 
E 1 45  GLY 45  45  45  GLY GLY E . n 
E 1 46  LYS 46  46  46  LYS LYS E . n 
E 1 47  LEU 47  47  47  LEU LEU E . n 
E 1 48  CYS 48  48  48  CYS CYS E . n 
E 1 49  LYS 49  49  49  LYS LYS E . n 
E 1 50  LEU 50  50  50  LEU LEU E . n 
E 1 51  ARG 51  51  51  ARG ARG E . n 
E 1 52  GLY 52  52  52  GLY GLY E . n 
E 1 53  VAL 53  53  53  VAL VAL E . n 
E 1 54  ALA 54  54  54  ALA ALA E . n 
E 1 55  PRO 55  55  55  PRO PRO E . n 
E 1 56  LEU 56  56  56  LEU LEU E . n 
E 1 57  HIS 57  57  57  HIS HIS E . n 
E 1 58  LEU 58  58  58  LEU LEU E . n 
E 1 59  GLY 59  59  59  GLY GLY E . n 
E 1 60  LYS 60  60  60  LYS LYS E . n 
E 1 61  CYS 61  61  61  CYS CYS E . n 
E 1 62  ASN 62  62  62  ASN ASN E . n 
E 1 63  ILE 63  63  63  ILE ILE E . n 
E 1 64  ALA 64  64  64  ALA ALA E . n 
E 1 65  GLY 65  65  65  GLY GLY E . n 
E 1 66  TRP 66  66  66  TRP TRP E . n 
E 1 67  ILE 67  67  67  ILE ILE E . n 
E 1 68  LEU 68  68  68  LEU LEU E . n 
E 1 69  GLY 69  69  69  GLY GLY E . n 
E 1 70  ASN 70  70  70  ASN ASN E . n 
E 1 71  PRO 71  71  71  PRO PRO E . n 
E 1 72  GLU 72  72  72  GLU GLU E . n 
E 1 73  CYS 73  73  73  CYS CYS E . n 
E 1 74  GLU 74  74  74  GLU GLU E . n 
E 1 75  SER 75  75  75  SER SER E . n 
E 1 76  LEU 76  76  76  LEU LEU E . n 
E 1 77  SER 77  77  77  SER SER E . n 
E 1 78  THR 78  78  78  THR THR E . n 
E 1 79  ALA 79  79  79  ALA ALA E . n 
E 1 80  SER 80  80  80  SER SER E . n 
E 1 81  SER 81  81  81  SER SER E . n 
E 1 82  TRP 82  82  82  TRP TRP E . n 
E 1 83  SER 83  83  83  SER SER E . n 
E 1 84  TYR 84  84  84  TYR TYR E . n 
E 1 85  ILE 85  85  85  ILE ILE E . n 
E 1 86  VAL 86  86  86  VAL VAL E . n 
E 1 87  GLU 87  87  87  GLU GLU E . n 
E 1 88  THR 88  88  88  THR THR E . n 
E 1 89  PRO 89  89  89  PRO PRO E . n 
E 1 90  SER 90  90  90  SER SER E . n 
E 1 91  SER 91  91  91  SER SER E . n 
E 1 92  ASP 92  92  92  ASP ASP E . n 
E 1 93  ASN 93  93  93  ASN ASN E . n 
E 1 94  GLY 94  94  94  GLY GLY E . n 
E 1 95  THR 95  95  95  THR THR E . n 
E 1 96  CYS 96  96  96  CYS CYS E . n 
E 1 97  TYR 97  97  97  TYR TYR E . n 
E 1 98  PRO 98  98  98  PRO PRO E . n 
E 1 99  GLY 99  99  99  GLY GLY E . n 
E 1 100 ASP 100 100 100 ASP ASP E . n 
E 1 101 PHE 101 101 101 PHE PHE E . n 
E 1 102 ILE 102 102 102 ILE ILE E . n 
E 1 103 ASP 103 103 103 ASP ASP E . n 
E 1 104 TYR 104 104 104 TYR TYR E . n 
E 1 105 GLU 105 105 105 GLU GLU E . n 
E 1 106 GLU 106 106 106 GLU GLU E . n 
E 1 107 LEU 107 107 107 LEU LEU E . n 
E 1 108 ARG 108 108 108 ARG ARG E . n 
E 1 109 GLU 109 109 109 GLU GLU E . n 
E 1 110 GLN 110 110 110 GLN GLN E . n 
E 1 111 LEU 111 111 111 LEU LEU E . n 
E 1 112 SER 112 112 112 SER SER E . n 
E 1 113 SER 113 113 113 SER SER E . n 
E 1 114 VAL 114 114 114 VAL VAL E . n 
E 1 115 SER 115 115 115 SER SER E . n 
E 1 116 SER 116 116 116 SER SER E . n 
E 1 117 PHE 117 117 117 PHE PHE E . n 
E 1 118 GLU 118 118 118 GLU GLU E . n 
E 1 119 ARG 119 119 119 ARG ARG E . n 
E 1 120 PHE 120 120 120 PHE PHE E . n 
E 1 121 GLU 121 121 121 GLU GLU E . n 
E 1 122 ILE 122 122 122 ILE ILE E . n 
E 1 123 PHE 123 123 123 PHE PHE E . n 
E 1 124 PRO 124 124 124 PRO PRO E . n 
E 1 125 LYS 125 125 125 LYS LYS E . n 
E 1 126 THR 126 126 126 THR THR E . n 
E 1 127 SER 127 127 127 SER SER E . n 
E 1 128 SER 128 128 128 SER SER E . n 
E 1 129 TRP 129 129 129 TRP TRP E . n 
E 1 130 PRO 130 130 130 PRO PRO E . n 
E 1 131 ASN 131 131 131 ASN ASN E . n 
E 1 132 HIS 132 132 132 HIS HIS E . n 
E 1 133 ASP 133 133 133 ASP ASP E . n 
E 1 134 SER 134 134 134 SER SER E . n 
E 1 135 ASN 135 135 135 ASN ASN E . n 
E 1 136 LYS 136 136 136 LYS LYS E . n 
E 1 137 GLY 137 137 137 GLY GLY E . n 
E 1 138 VAL 138 138 138 VAL VAL E . n 
E 1 139 THR 139 139 139 THR THR E . n 
E 1 140 ALA 140 140 140 ALA ALA E . n 
E 1 141 ALA 141 141 141 ALA ALA E . n 
E 1 142 CYS 142 142 142 CYS CYS E . n 
E 1 143 PRO 143 143 143 PRO PRO E . n 
E 1 144 HIS 144 144 144 HIS HIS E . n 
E 1 145 ALA 145 145 145 ALA ALA E . n 
E 1 146 GLY 146 146 146 GLY GLY E . n 
E 1 147 ALA 147 147 147 ALA ALA E . n 
E 1 148 LYS 148 148 148 LYS LYS E . n 
E 1 149 SER 149 149 149 SER SER E . n 
E 1 150 PHE 150 150 150 PHE PHE E . n 
E 1 151 TYR 151 151 151 TYR TYR E . n 
E 1 152 LYS 152 152 152 LYS LYS E . n 
E 1 153 ASN 153 153 153 ASN ASN E . n 
E 1 154 LEU 154 154 154 LEU LEU E . n 
E 1 155 ILE 155 155 155 ILE ILE E . n 
E 1 156 TRP 156 156 156 TRP TRP E . n 
E 1 157 LEU 157 157 157 LEU LEU E . n 
E 1 158 VAL 158 158 158 VAL VAL E . n 
E 1 159 LYS 159 159 159 LYS LYS E . n 
E 1 160 LYS 160 160 160 LYS LYS E . n 
E 1 161 GLY 161 161 161 GLY GLY E . n 
E 1 162 ASN 162 162 162 ASN ASN E . n 
E 1 163 SER 163 163 163 SER SER E . n 
E 1 164 TYR 164 164 164 TYR TYR E . n 
E 1 165 PRO 165 165 165 PRO PRO E . n 
E 1 166 LYS 166 166 166 LYS LYS E . n 
E 1 167 LEU 167 167 167 LEU LEU E . n 
E 1 168 SER 168 168 168 SER SER E . n 
E 1 169 LYS 169 169 169 LYS LYS E . n 
E 1 170 SER 170 170 170 SER SER E . n 
E 1 171 TYR 171 171 171 TYR TYR E . n 
E 1 172 ILE 172 172 172 ILE ILE E . n 
E 1 173 ASN 173 173 173 ASN ASN E . n 
E 1 174 ASP 174 174 174 ASP ASP E . n 
E 1 175 LYS 175 175 175 LYS LYS E . n 
E 1 176 GLY 176 176 176 GLY GLY E . n 
E 1 177 LYS 177 177 177 LYS LYS E . n 
E 1 178 GLU 178 178 178 GLU GLU E . n 
E 1 179 VAL 179 179 179 VAL VAL E . n 
E 1 180 LEU 180 180 180 LEU LEU E . n 
E 1 181 VAL 181 181 181 VAL VAL E . n 
E 1 182 LEU 182 182 182 LEU LEU E . n 
E 1 183 TRP 183 183 183 TRP TRP E . n 
E 1 184 GLY 184 184 184 GLY GLY E . n 
E 1 185 ILE 185 185 185 ILE ILE E . n 
E 1 186 HIS 186 186 186 HIS HIS E . n 
E 1 187 HIS 187 187 187 HIS HIS E . n 
E 1 188 PRO 188 188 188 PRO PRO E . n 
E 1 189 SER 189 189 189 SER SER E . n 
E 1 190 THR 190 190 190 THR THR E . n 
E 1 191 SER 191 191 191 SER SER E . n 
E 1 192 ALA 192 192 192 ALA ALA E . n 
E 1 193 ASP 193 193 193 ASP ASP E . n 
E 1 194 GLN 194 194 194 GLN GLN E . n 
E 1 195 GLN 195 195 195 GLN GLN E . n 
E 1 196 SER 196 196 196 SER SER E . n 
E 1 197 LEU 197 197 197 LEU LEU E . n 
E 1 198 TYR 198 198 198 TYR TYR E . n 
E 1 199 GLN 199 199 199 GLN GLN E . n 
E 1 200 ASN 200 200 200 ASN ASN E . n 
E 1 201 ALA 201 201 201 ALA ALA E . n 
E 1 202 ASP 202 202 202 ASP ASP E . n 
E 1 203 THR 203 203 203 THR THR E . n 
E 1 204 TYR 204 204 204 TYR TYR E . n 
E 1 205 VAL 205 205 205 VAL VAL E . n 
E 1 206 PHE 206 206 206 PHE PHE E . n 
E 1 207 VAL 207 207 207 VAL VAL E . n 
E 1 208 GLY 208 208 208 GLY GLY E . n 
E 1 209 SER 209 209 209 SER SER E . n 
E 1 210 SER 210 210 210 SER SER E . n 
E 1 211 ARG 211 211 211 ARG ARG E . n 
E 1 212 TYR 212 212 212 TYR TYR E . n 
E 1 213 SER 213 213 213 SER SER E . n 
E 1 214 LYS 214 214 214 LYS LYS E . n 
E 1 215 LYS 215 215 215 LYS LYS E . n 
E 1 216 PHE 216 216 216 PHE PHE E . n 
E 1 217 LYS 217 217 217 LYS LYS E . n 
E 1 218 PRO 218 218 218 PRO PRO E . n 
E 1 219 GLU 219 219 219 GLU GLU E . n 
E 1 220 ILE 220 220 220 ILE ILE E . n 
E 1 221 ALA 221 221 221 ALA ALA E . n 
E 1 222 ILE 222 222 222 ILE ILE E . n 
E 1 223 ARG 223 223 223 ARG ARG E . n 
E 1 224 PRO 224 224 224 PRO PRO E . n 
E 1 225 LYS 225 225 225 LYS LYS E . n 
E 1 226 VAL 226 226 226 VAL VAL E . n 
E 1 227 ARG 227 227 227 ARG ARG E . n 
E 1 228 ASP 228 228 228 ASP ASP E . n 
E 1 229 GLN 229 229 229 GLN GLN E . n 
E 1 230 GLU 230 230 230 GLU GLU E . n 
E 1 231 GLY 231 231 231 GLY GLY E . n 
E 1 232 ARG 232 232 232 ARG ARG E . n 
E 1 233 MET 233 233 233 MET MET E . n 
E 1 234 ASN 234 234 234 ASN ASN E . n 
E 1 235 TYR 235 235 235 TYR TYR E . n 
E 1 236 TYR 236 236 236 TYR TYR E . n 
E 1 237 TRP 237 237 237 TRP TRP E . n 
E 1 238 THR 238 238 238 THR THR E . n 
E 1 239 LEU 239 239 239 LEU LEU E . n 
E 1 240 VAL 240 240 240 VAL VAL E . n 
E 1 241 GLU 241 241 241 GLU GLU E . n 
E 1 242 PRO 242 242 242 PRO PRO E . n 
E 1 243 GLY 243 243 243 GLY GLY E . n 
E 1 244 ASP 244 244 244 ASP ASP E . n 
E 1 245 LYS 245 245 245 LYS LYS E . n 
E 1 246 ILE 246 246 246 ILE ILE E . n 
E 1 247 THR 247 247 247 THR THR E . n 
E 1 248 PHE 248 248 248 PHE PHE E . n 
E 1 249 GLU 249 249 249 GLU GLU E . n 
E 1 250 ALA 250 250 250 ALA ALA E . n 
E 1 251 THR 251 251 251 THR THR E . n 
E 1 252 GLY 252 252 252 GLY GLY E . n 
E 1 253 ASN 253 253 253 ASN ASN E . n 
E 1 254 LEU 254 254 254 LEU LEU E . n 
E 1 255 VAL 255 255 255 VAL VAL E . n 
E 1 256 VAL 256 256 256 VAL VAL E . n 
E 1 257 PRO 257 257 257 PRO PRO E . n 
E 1 258 ARG 258 258 258 ARG ARG E . n 
E 1 259 TYR 259 259 259 TYR TYR E . n 
E 1 260 ALA 260 260 260 ALA ALA E . n 
E 1 261 PHE 261 261 261 PHE PHE E . n 
E 1 262 ALA 262 262 262 ALA ALA E . n 
E 1 263 MET 263 263 263 MET MET E . n 
E 1 264 GLU 264 264 264 GLU GLU E . n 
E 1 265 ARG 265 265 265 ARG ARG E . n 
E 1 266 ASN 266 266 266 ASN ASN E . n 
E 1 267 ALA 267 267 267 ALA ALA E . n 
E 1 268 GLY 268 268 268 GLY GLY E . n 
E 1 269 SER 269 269 269 SER SER E . n 
E 1 270 GLY 270 270 270 GLY GLY E . n 
E 1 271 ILE 271 271 271 ILE ILE E . n 
E 1 272 ILE 272 272 272 ILE ILE E . n 
E 1 273 ILE 273 273 273 ILE ILE E . n 
E 1 274 SER 274 274 274 SER SER E . n 
E 1 275 ASP 275 275 275 ASP ASP E . n 
E 1 276 THR 276 276 276 THR THR E . n 
E 1 277 PRO 277 277 277 PRO PRO E . n 
E 1 278 VAL 278 278 278 VAL VAL E . n 
E 1 279 HIS 279 279 279 HIS HIS E . n 
E 1 280 ASP 280 280 280 ASP ASP E . n 
E 1 281 CYS 281 281 281 CYS CYS E . n 
E 1 282 ASN 282 282 282 ASN ASN E . n 
E 1 283 THR 283 283 283 THR THR E . n 
E 1 284 THR 284 284 284 THR THR E . n 
E 1 285 CYS 285 285 285 CYS CYS E . n 
E 1 286 GLN 286 286 286 GLN GLN E . n 
E 1 287 THR 287 287 287 THR THR E . n 
E 1 288 PRO 288 288 288 PRO PRO E . n 
E 1 289 LYS 289 289 289 LYS LYS E . n 
E 1 290 GLY 290 290 290 GLY GLY E . n 
E 1 291 ALA 291 291 291 ALA ALA E . n 
E 1 292 ILE 292 292 292 ILE ILE E . n 
E 1 293 ASN 293 293 293 ASN ASN E . n 
E 1 294 THR 294 294 294 THR THR E . n 
E 1 295 SER 295 295 295 SER SER E . n 
E 1 296 LEU 296 296 296 LEU LEU E . n 
E 1 297 PRO 297 297 297 PRO PRO E . n 
E 1 298 PHE 298 298 298 PHE PHE E . n 
E 1 299 GLN 299 299 299 GLN GLN E . n 
E 1 300 ASN 300 300 300 ASN ASN E . n 
E 1 301 ILE 301 301 301 ILE ILE E . n 
E 1 302 HIS 302 302 302 HIS HIS E . n 
E 1 303 PRO 303 303 303 PRO PRO E . n 
E 1 304 ILE 304 304 304 ILE ILE E . n 
E 1 305 THR 305 305 305 THR THR E . n 
E 1 306 ILE 306 306 306 ILE ILE E . n 
E 1 307 GLY 307 307 307 GLY GLY E . n 
E 1 308 LYS 308 308 308 LYS LYS E . n 
E 1 309 CYS 309 309 309 CYS CYS E . n 
E 1 310 PRO 310 310 310 PRO PRO E . n 
E 1 311 LYS 311 311 311 LYS LYS E . n 
E 1 312 TYR 312 312 312 TYR TYR E . n 
E 1 313 VAL 313 313 313 VAL VAL E . n 
E 1 314 LYS 314 314 314 LYS LYS E . n 
E 1 315 SER 315 315 315 SER SER E . n 
E 1 316 THR 316 316 316 THR THR E . n 
E 1 317 LYS 317 317 317 LYS LYS E . n 
E 1 318 LEU 318 318 318 LEU LEU E . n 
E 1 319 ARG 319 319 319 ARG ARG E . n 
E 1 320 LEU 320 320 320 LEU LEU E . n 
E 1 321 ALA 321 321 321 ALA ALA E . n 
E 1 322 THR 322 322 322 THR THR E . n 
E 1 323 GLY 323 323 323 GLY GLY E . n 
E 1 324 LEU 324 324 324 LEU LEU E . n 
E 1 325 ARG 325 325 325 ARG ARG E . n 
E 1 326 ASN 326 326 326 ASN ASN E . n 
E 1 327 ILE 327 327 327 ILE ILE E . n 
E 1 328 PRO 328 328 ?   ?   ?   E . n 
E 1 329 SER 329 329 ?   ?   ?   E . n 
E 1 330 ILE 330 330 ?   ?   ?   E . n 
E 1 331 GLN 331 331 ?   ?   ?   E . n 
E 1 332 SER 332 332 ?   ?   ?   E . n 
E 1 333 ARG 333 333 ?   ?   ?   E . n 
F 2 1   GLY 1   1   ?   ?   ?   F . n 
F 2 2   LEU 2   2   2   LEU LEU F . n 
F 2 3   PHE 3   3   3   PHE PHE F . n 
F 2 4   GLY 4   4   4   GLY GLY F . n 
F 2 5   ALA 5   5   5   ALA ALA F . n 
F 2 6   ILE 6   6   6   ILE ILE F . n 
F 2 7   ALA 7   7   7   ALA ALA F . n 
F 2 8   GLY 8   8   8   GLY GLY F . n 
F 2 9   PHE 9   9   9   PHE PHE F . n 
F 2 10  ILE 10  10  10  ILE ILE F . n 
F 2 11  GLU 11  11  11  GLU GLU F . n 
F 2 12  GLY 12  12  12  GLY GLY F . n 
F 2 13  GLY 13  13  13  GLY GLY F . n 
F 2 14  TRP 14  14  14  TRP TRP F . n 
F 2 15  THR 15  15  15  THR THR F . n 
F 2 16  GLY 16  16  16  GLY GLY F . n 
F 2 17  MET 17  17  17  MET MET F . n 
F 2 18  VAL 18  18  18  VAL VAL F . n 
F 2 19  ASP 19  19  19  ASP ASP F . n 
F 2 20  GLY 20  20  20  GLY GLY F . n 
F 2 21  TRP 21  21  21  TRP TRP F . n 
F 2 22  TYR 22  22  22  TYR TYR F . n 
F 2 23  GLY 23  23  23  GLY GLY F . n 
F 2 24  TYR 24  24  24  TYR TYR F . n 
F 2 25  HIS 25  25  25  HIS HIS F . n 
F 2 26  HIS 26  26  26  HIS HIS F . n 
F 2 27  GLN 27  27  27  GLN GLN F . n 
F 2 28  ASN 28  28  28  ASN ASN F . n 
F 2 29  GLU 29  29  29  GLU GLU F . n 
F 2 30  GLN 30  30  30  GLN GLN F . n 
F 2 31  GLY 31  31  31  GLY GLY F . n 
F 2 32  SER 32  32  32  SER SER F . n 
F 2 33  GLY 33  33  33  GLY GLY F . n 
F 2 34  TYR 34  34  34  TYR TYR F . n 
F 2 35  ALA 35  35  35  ALA ALA F . n 
F 2 36  ALA 36  36  36  ALA ALA F . n 
F 2 37  ASP 37  37  37  ASP ASP F . n 
F 2 38  LEU 38  38  38  LEU LEU F . n 
F 2 39  LYS 39  39  39  LYS LYS F . n 
F 2 40  SER 40  40  40  SER SER F . n 
F 2 41  THR 41  41  41  THR THR F . n 
F 2 42  GLN 42  42  42  GLN GLN F . n 
F 2 43  ASN 43  43  43  ASN ASN F . n 
F 2 44  ALA 44  44  44  ALA ALA F . n 
F 2 45  ILE 45  45  45  ILE ILE F . n 
F 2 46  ASP 46  46  46  ASP ASP F . n 
F 2 47  GLU 47  47  47  GLU GLU F . n 
F 2 48  ILE 48  48  48  ILE ILE F . n 
F 2 49  THR 49  49  49  THR THR F . n 
F 2 50  ASN 50  50  50  ASN ASN F . n 
F 2 51  LYS 51  51  51  LYS LYS F . n 
F 2 52  VAL 52  52  52  VAL VAL F . n 
F 2 53  ASN 53  53  53  ASN ASN F . n 
F 2 54  SER 54  54  54  SER SER F . n 
F 2 55  VAL 55  55  55  VAL VAL F . n 
F 2 56  ILE 56  56  56  ILE ILE F . n 
F 2 57  GLU 57  57  57  GLU GLU F . n 
F 2 58  LYS 58  58  58  LYS LYS F . n 
F 2 59  MET 59  59  59  MET MET F . n 
F 2 60  ASN 60  60  60  ASN ASN F . n 
F 2 61  THR 61  61  61  THR THR F . n 
F 2 62  GLN 62  62  62  GLN GLN F . n 
F 2 63  PHE 63  63  63  PHE PHE F . n 
F 2 64  THR 64  64  64  THR THR F . n 
F 2 65  ALA 65  65  65  ALA ALA F . n 
F 2 66  VAL 66  66  66  VAL VAL F . n 
F 2 67  GLY 67  67  67  GLY GLY F . n 
F 2 68  LYS 68  68  68  LYS LYS F . n 
F 2 69  GLU 69  69  69  GLU GLU F . n 
F 2 70  PHE 70  70  70  PHE PHE F . n 
F 2 71  ASN 71  71  71  ASN ASN F . n 
F 2 72  HIS 72  72  72  HIS HIS F . n 
F 2 73  LEU 73  73  73  LEU LEU F . n 
F 2 74  GLU 74  74  74  GLU GLU F . n 
F 2 75  LYS 75  75  75  LYS LYS F . n 
F 2 76  ARG 76  76  76  ARG ARG F . n 
F 2 77  ILE 77  77  77  ILE ILE F . n 
F 2 78  GLU 78  78  78  GLU GLU F . n 
F 2 79  ASN 79  79  79  ASN ASN F . n 
F 2 80  LEU 80  80  80  LEU LEU F . n 
F 2 81  ASN 81  81  81  ASN ASN F . n 
F 2 82  LYS 82  82  82  LYS LYS F . n 
F 2 83  LYS 83  83  83  LYS LYS F . n 
F 2 84  VAL 84  84  84  VAL VAL F . n 
F 2 85  ASP 85  85  85  ASP ASP F . n 
F 2 86  ASP 86  86  86  ASP ASP F . n 
F 2 87  GLY 87  87  87  GLY GLY F . n 
F 2 88  PHE 88  88  88  PHE PHE F . n 
F 2 89  LEU 89  89  89  LEU LEU F . n 
F 2 90  ASP 90  90  90  ASP ASP F . n 
F 2 91  ILE 91  91  91  ILE ILE F . n 
F 2 92  TRP 92  92  92  TRP TRP F . n 
F 2 93  THR 93  93  93  THR THR F . n 
F 2 94  TYR 94  94  94  TYR TYR F . n 
F 2 95  ASN 95  95  95  ASN ASN F . n 
F 2 96  ALA 96  96  96  ALA ALA F . n 
F 2 97  GLU 97  97  97  GLU GLU F . n 
F 2 98  LEU 98  98  98  LEU LEU F . n 
F 2 99  LEU 99  99  99  LEU LEU F . n 
F 2 100 VAL 100 100 100 VAL VAL F . n 
F 2 101 LEU 101 101 101 LEU LEU F . n 
F 2 102 LEU 102 102 102 LEU LEU F . n 
F 2 103 GLU 103 103 103 GLU GLU F . n 
F 2 104 ASN 104 104 104 ASN ASN F . n 
F 2 105 GLU 105 105 105 GLU GLU F . n 
F 2 106 ARG 106 106 106 ARG ARG F . n 
F 2 107 THR 107 107 107 THR THR F . n 
F 2 108 LEU 108 108 108 LEU LEU F . n 
F 2 109 ASP 109 109 109 ASP ASP F . n 
F 2 110 TYR 110 110 110 TYR TYR F . n 
F 2 111 HIS 111 111 111 HIS HIS F . n 
F 2 112 ASP 112 112 112 ASP ASP F . n 
F 2 113 SER 113 113 113 SER SER F . n 
F 2 114 ASN 114 114 114 ASN ASN F . n 
F 2 115 VAL 115 115 115 VAL VAL F . n 
F 2 116 LYS 116 116 116 LYS LYS F . n 
F 2 117 ASN 117 117 117 ASN ASN F . n 
F 2 118 LEU 118 118 118 LEU LEU F . n 
F 2 119 TYR 119 119 119 TYR TYR F . n 
F 2 120 GLU 120 120 120 GLU GLU F . n 
F 2 121 LYS 121 121 121 LYS LYS F . n 
F 2 122 VAL 122 122 122 VAL VAL F . n 
F 2 123 ARG 123 123 123 ARG ARG F . n 
F 2 124 SER 124 124 124 SER SER F . n 
F 2 125 GLN 125 125 125 GLN GLN F . n 
F 2 126 LEU 126 126 126 LEU LEU F . n 
F 2 127 LYS 127 127 127 LYS LYS F . n 
F 2 128 ASN 128 128 128 ASN ASN F . n 
F 2 129 ASN 129 129 129 ASN ASN F . n 
F 2 130 ALA 130 130 130 ALA ALA F . n 
F 2 131 LYS 131 131 131 LYS LYS F . n 
F 2 132 GLU 132 132 132 GLU GLU F . n 
F 2 133 ILE 133 133 133 ILE ILE F . n 
F 2 134 GLY 134 134 134 GLY GLY F . n 
F 2 135 ASN 135 135 135 ASN ASN F . n 
F 2 136 GLY 136 136 136 GLY GLY F . n 
F 2 137 CYS 137 137 137 CYS CYS F . n 
F 2 138 PHE 138 138 138 PHE PHE F . n 
F 2 139 GLU 139 139 139 GLU GLU F . n 
F 2 140 PHE 140 140 140 PHE PHE F . n 
F 2 141 TYR 141 141 141 TYR TYR F . n 
F 2 142 HIS 142 142 142 HIS HIS F . n 
F 2 143 LYS 143 143 143 LYS LYS F . n 
F 2 144 CYS 144 144 144 CYS CYS F . n 
F 2 145 ASP 145 145 145 ASP ASP F . n 
F 2 146 ASN 146 146 146 ASN ASN F . n 
F 2 147 THR 147 147 147 THR THR F . n 
F 2 148 CYS 148 148 148 CYS CYS F . n 
F 2 149 MET 149 149 149 MET MET F . n 
F 2 150 GLU 150 150 150 GLU GLU F . n 
F 2 151 SER 151 151 151 SER SER F . n 
F 2 152 VAL 152 152 152 VAL VAL F . n 
F 2 153 LYS 153 153 153 LYS LYS F . n 
F 2 154 ASN 154 154 154 ASN ASN F . n 
F 2 155 GLY 155 155 155 GLY GLY F . n 
F 2 156 THR 156 156 156 THR THR F . n 
F 2 157 TYR 157 157 157 TYR TYR F . n 
F 2 158 ASP 158 158 158 ASP ASP F . n 
F 2 159 TYR 159 159 159 TYR TYR F . n 
F 2 160 PRO 160 160 160 PRO PRO F . n 
F 2 161 LYS 161 161 161 LYS LYS F . n 
F 2 162 TYR 162 162 162 TYR TYR F . n 
F 2 163 SER 163 163 ?   ?   ?   F . n 
F 2 164 GLU 164 164 ?   ?   ?   F . n 
F 2 165 GLU 165 165 ?   ?   ?   F . n 
F 2 166 ALA 166 166 ?   ?   ?   F . n 
F 2 167 LYS 167 167 ?   ?   ?   F . n 
F 2 168 LEU 168 168 ?   ?   ?   F . n 
F 2 169 ASN 169 169 ?   ?   ?   F . n 
F 2 170 ARG 170 170 ?   ?   ?   F . n 
F 2 171 GLU 171 171 ?   ?   ?   F . n 
F 2 172 GLU 172 172 ?   ?   ?   F . n 
F 2 173 ILE 173 173 ?   ?   ?   F . n 
F 2 174 ASP 174 174 ?   ?   ?   F . n 
F 2 175 GLY 175 175 ?   ?   ?   F . n 
F 2 176 VAL 176 176 ?   ?   ?   F . n 
F 2 177 ARG 177 177 ?   ?   ?   F . n 
F 2 178 LEU 178 178 ?   ?   ?   F . n 
F 2 179 VAL 179 179 ?   ?   ?   F . n 
F 2 180 PRO 180 180 ?   ?   ?   F . n 
F 2 181 ARG 181 181 ?   ?   ?   F . n 
G 1 1   ALA 1   1   ?   ?   ?   G . n 
G 1 2   ASP 2   2   ?   ?   ?   G . n 
G 1 3   LEU 3   3   ?   ?   ?   G . n 
G 1 4   GLY 4   4   ?   ?   ?   G . n 
G 1 5   SER 5   5   ?   ?   ?   G . n 
G 1 6   ARG 6   6   ?   ?   ?   G . n 
G 1 7   ASP 7   7   7   ASP ASP G . n 
G 1 8   THR 8   8   8   THR THR G . n 
G 1 9   LEU 9   9   9   LEU LEU G . n 
G 1 10  CYS 10  10  10  CYS CYS G . n 
G 1 11  ILE 11  11  11  ILE ILE G . n 
G 1 12  GLY 12  12  12  GLY GLY G . n 
G 1 13  TYR 13  13  13  TYR TYR G . n 
G 1 14  HIS 14  14  14  HIS HIS G . n 
G 1 15  ALA 15  15  15  ALA ALA G . n 
G 1 16  ASN 16  16  16  ASN ASN G . n 
G 1 17  ASN 17  17  17  ASN ASN G . n 
G 1 18  SER 18  18  18  SER SER G . n 
G 1 19  THR 19  19  19  THR THR G . n 
G 1 20  ASP 20  20  20  ASP ASP G . n 
G 1 21  THR 21  21  21  THR THR G . n 
G 1 22  VAL 22  22  22  VAL VAL G . n 
G 1 23  ASP 23  23  23  ASP ASP G . n 
G 1 24  THR 24  24  24  THR THR G . n 
G 1 25  VAL 25  25  25  VAL VAL G . n 
G 1 26  LEU 26  26  26  LEU LEU G . n 
G 1 27  GLU 27  27  27  GLU GLU G . n 
G 1 28  LYS 28  28  28  LYS LYS G . n 
G 1 29  ASN 29  29  29  ASN ASN G . n 
G 1 30  VAL 30  30  30  VAL VAL G . n 
G 1 31  THR 31  31  31  THR THR G . n 
G 1 32  VAL 32  32  32  VAL VAL G . n 
G 1 33  THR 33  33  33  THR THR G . n 
G 1 34  HIS 34  34  34  HIS HIS G . n 
G 1 35  SER 35  35  35  SER SER G . n 
G 1 36  VAL 36  36  36  VAL VAL G . n 
G 1 37  ASN 37  37  37  ASN ASN G . n 
G 1 38  LEU 38  38  38  LEU LEU G . n 
G 1 39  LEU 39  39  39  LEU LEU G . n 
G 1 40  GLU 40  40  40  GLU GLU G . n 
G 1 41  ASP 41  41  41  ASP ASP G . n 
G 1 42  LYS 42  42  42  LYS LYS G . n 
G 1 43  HIS 43  43  43  HIS HIS G . n 
G 1 44  ASN 44  44  44  ASN ASN G . n 
G 1 45  GLY 45  45  45  GLY GLY G . n 
G 1 46  LYS 46  46  46  LYS LYS G . n 
G 1 47  LEU 47  47  47  LEU LEU G . n 
G 1 48  CYS 48  48  48  CYS CYS G . n 
G 1 49  LYS 49  49  49  LYS LYS G . n 
G 1 50  LEU 50  50  50  LEU LEU G . n 
G 1 51  ARG 51  51  51  ARG ARG G . n 
G 1 52  GLY 52  52  52  GLY GLY G . n 
G 1 53  VAL 53  53  53  VAL VAL G . n 
G 1 54  ALA 54  54  54  ALA ALA G . n 
G 1 55  PRO 55  55  55  PRO PRO G . n 
G 1 56  LEU 56  56  56  LEU LEU G . n 
G 1 57  HIS 57  57  57  HIS HIS G . n 
G 1 58  LEU 58  58  58  LEU LEU G . n 
G 1 59  GLY 59  59  59  GLY GLY G . n 
G 1 60  LYS 60  60  60  LYS LYS G . n 
G 1 61  CYS 61  61  61  CYS CYS G . n 
G 1 62  ASN 62  62  62  ASN ASN G . n 
G 1 63  ILE 63  63  63  ILE ILE G . n 
G 1 64  ALA 64  64  64  ALA ALA G . n 
G 1 65  GLY 65  65  65  GLY GLY G . n 
G 1 66  TRP 66  66  66  TRP TRP G . n 
G 1 67  ILE 67  67  67  ILE ILE G . n 
G 1 68  LEU 68  68  68  LEU LEU G . n 
G 1 69  GLY 69  69  69  GLY GLY G . n 
G 1 70  ASN 70  70  70  ASN ASN G . n 
G 1 71  PRO 71  71  71  PRO PRO G . n 
G 1 72  GLU 72  72  72  GLU GLU G . n 
G 1 73  CYS 73  73  73  CYS CYS G . n 
G 1 74  GLU 74  74  74  GLU GLU G . n 
G 1 75  SER 75  75  75  SER SER G . n 
G 1 76  LEU 76  76  76  LEU LEU G . n 
G 1 77  SER 77  77  77  SER SER G . n 
G 1 78  THR 78  78  78  THR THR G . n 
G 1 79  ALA 79  79  79  ALA ALA G . n 
G 1 80  SER 80  80  80  SER SER G . n 
G 1 81  SER 81  81  81  SER SER G . n 
G 1 82  TRP 82  82  82  TRP TRP G . n 
G 1 83  SER 83  83  83  SER SER G . n 
G 1 84  TYR 84  84  84  TYR TYR G . n 
G 1 85  ILE 85  85  85  ILE ILE G . n 
G 1 86  VAL 86  86  86  VAL VAL G . n 
G 1 87  GLU 87  87  87  GLU GLU G . n 
G 1 88  THR 88  88  88  THR THR G . n 
G 1 89  PRO 89  89  89  PRO PRO G . n 
G 1 90  SER 90  90  90  SER SER G . n 
G 1 91  SER 91  91  91  SER SER G . n 
G 1 92  ASP 92  92  92  ASP ASP G . n 
G 1 93  ASN 93  93  93  ASN ASN G . n 
G 1 94  GLY 94  94  94  GLY GLY G . n 
G 1 95  THR 95  95  95  THR THR G . n 
G 1 96  CYS 96  96  96  CYS CYS G . n 
G 1 97  TYR 97  97  97  TYR TYR G . n 
G 1 98  PRO 98  98  98  PRO PRO G . n 
G 1 99  GLY 99  99  99  GLY GLY G . n 
G 1 100 ASP 100 100 100 ASP ASP G . n 
G 1 101 PHE 101 101 101 PHE PHE G . n 
G 1 102 ILE 102 102 102 ILE ILE G . n 
G 1 103 ASP 103 103 103 ASP ASP G . n 
G 1 104 TYR 104 104 104 TYR TYR G . n 
G 1 105 GLU 105 105 105 GLU GLU G . n 
G 1 106 GLU 106 106 106 GLU GLU G . n 
G 1 107 LEU 107 107 107 LEU LEU G . n 
G 1 108 ARG 108 108 108 ARG ARG G . n 
G 1 109 GLU 109 109 109 GLU GLU G . n 
G 1 110 GLN 110 110 110 GLN GLN G . n 
G 1 111 LEU 111 111 111 LEU LEU G . n 
G 1 112 SER 112 112 112 SER SER G . n 
G 1 113 SER 113 113 113 SER SER G . n 
G 1 114 VAL 114 114 114 VAL VAL G . n 
G 1 115 SER 115 115 115 SER SER G . n 
G 1 116 SER 116 116 116 SER SER G . n 
G 1 117 PHE 117 117 117 PHE PHE G . n 
G 1 118 GLU 118 118 118 GLU GLU G . n 
G 1 119 ARG 119 119 119 ARG ARG G . n 
G 1 120 PHE 120 120 120 PHE PHE G . n 
G 1 121 GLU 121 121 121 GLU GLU G . n 
G 1 122 ILE 122 122 122 ILE ILE G . n 
G 1 123 PHE 123 123 123 PHE PHE G . n 
G 1 124 PRO 124 124 124 PRO PRO G . n 
G 1 125 LYS 125 125 125 LYS LYS G . n 
G 1 126 THR 126 126 126 THR THR G . n 
G 1 127 SER 127 127 127 SER SER G . n 
G 1 128 SER 128 128 128 SER SER G . n 
G 1 129 TRP 129 129 129 TRP TRP G . n 
G 1 130 PRO 130 130 130 PRO PRO G . n 
G 1 131 ASN 131 131 131 ASN ASN G . n 
G 1 132 HIS 132 132 132 HIS HIS G . n 
G 1 133 ASP 133 133 133 ASP ASP G . n 
G 1 134 SER 134 134 134 SER SER G . n 
G 1 135 ASN 135 135 135 ASN ASN G . n 
G 1 136 LYS 136 136 136 LYS LYS G . n 
G 1 137 GLY 137 137 137 GLY GLY G . n 
G 1 138 VAL 138 138 138 VAL VAL G . n 
G 1 139 THR 139 139 139 THR THR G . n 
G 1 140 ALA 140 140 140 ALA ALA G . n 
G 1 141 ALA 141 141 141 ALA ALA G . n 
G 1 142 CYS 142 142 142 CYS CYS G . n 
G 1 143 PRO 143 143 143 PRO PRO G . n 
G 1 144 HIS 144 144 144 HIS HIS G . n 
G 1 145 ALA 145 145 145 ALA ALA G . n 
G 1 146 GLY 146 146 146 GLY GLY G . n 
G 1 147 ALA 147 147 147 ALA ALA G . n 
G 1 148 LYS 148 148 148 LYS LYS G . n 
G 1 149 SER 149 149 149 SER SER G . n 
G 1 150 PHE 150 150 150 PHE PHE G . n 
G 1 151 TYR 151 151 151 TYR TYR G . n 
G 1 152 LYS 152 152 152 LYS LYS G . n 
G 1 153 ASN 153 153 153 ASN ASN G . n 
G 1 154 LEU 154 154 154 LEU LEU G . n 
G 1 155 ILE 155 155 155 ILE ILE G . n 
G 1 156 TRP 156 156 156 TRP TRP G . n 
G 1 157 LEU 157 157 157 LEU LEU G . n 
G 1 158 VAL 158 158 158 VAL VAL G . n 
G 1 159 LYS 159 159 159 LYS LYS G . n 
G 1 160 LYS 160 160 160 LYS LYS G . n 
G 1 161 GLY 161 161 161 GLY GLY G . n 
G 1 162 ASN 162 162 162 ASN ASN G . n 
G 1 163 SER 163 163 163 SER SER G . n 
G 1 164 TYR 164 164 164 TYR TYR G . n 
G 1 165 PRO 165 165 165 PRO PRO G . n 
G 1 166 LYS 166 166 166 LYS LYS G . n 
G 1 167 LEU 167 167 167 LEU LEU G . n 
G 1 168 SER 168 168 168 SER SER G . n 
G 1 169 LYS 169 169 169 LYS LYS G . n 
G 1 170 SER 170 170 170 SER SER G . n 
G 1 171 TYR 171 171 171 TYR TYR G . n 
G 1 172 ILE 172 172 172 ILE ILE G . n 
G 1 173 ASN 173 173 173 ASN ASN G . n 
G 1 174 ASP 174 174 174 ASP ASP G . n 
G 1 175 LYS 175 175 175 LYS LYS G . n 
G 1 176 GLY 176 176 176 GLY GLY G . n 
G 1 177 LYS 177 177 177 LYS LYS G . n 
G 1 178 GLU 178 178 178 GLU GLU G . n 
G 1 179 VAL 179 179 179 VAL VAL G . n 
G 1 180 LEU 180 180 180 LEU LEU G . n 
G 1 181 VAL 181 181 181 VAL VAL G . n 
G 1 182 LEU 182 182 182 LEU LEU G . n 
G 1 183 TRP 183 183 183 TRP TRP G . n 
G 1 184 GLY 184 184 184 GLY GLY G . n 
G 1 185 ILE 185 185 185 ILE ILE G . n 
G 1 186 HIS 186 186 186 HIS HIS G . n 
G 1 187 HIS 187 187 187 HIS HIS G . n 
G 1 188 PRO 188 188 188 PRO PRO G . n 
G 1 189 SER 189 189 189 SER SER G . n 
G 1 190 THR 190 190 190 THR THR G . n 
G 1 191 SER 191 191 191 SER SER G . n 
G 1 192 ALA 192 192 192 ALA ALA G . n 
G 1 193 ASP 193 193 193 ASP ASP G . n 
G 1 194 GLN 194 194 194 GLN GLN G . n 
G 1 195 GLN 195 195 195 GLN GLN G . n 
G 1 196 SER 196 196 196 SER SER G . n 
G 1 197 LEU 197 197 197 LEU LEU G . n 
G 1 198 TYR 198 198 198 TYR TYR G . n 
G 1 199 GLN 199 199 199 GLN GLN G . n 
G 1 200 ASN 200 200 200 ASN ASN G . n 
G 1 201 ALA 201 201 201 ALA ALA G . n 
G 1 202 ASP 202 202 202 ASP ASP G . n 
G 1 203 THR 203 203 203 THR THR G . n 
G 1 204 TYR 204 204 204 TYR TYR G . n 
G 1 205 VAL 205 205 205 VAL VAL G . n 
G 1 206 PHE 206 206 206 PHE PHE G . n 
G 1 207 VAL 207 207 207 VAL VAL G . n 
G 1 208 GLY 208 208 208 GLY GLY G . n 
G 1 209 SER 209 209 209 SER SER G . n 
G 1 210 SER 210 210 210 SER SER G . n 
G 1 211 ARG 211 211 211 ARG ARG G . n 
G 1 212 TYR 212 212 212 TYR TYR G . n 
G 1 213 SER 213 213 213 SER SER G . n 
G 1 214 LYS 214 214 214 LYS LYS G . n 
G 1 215 LYS 215 215 215 LYS LYS G . n 
G 1 216 PHE 216 216 216 PHE PHE G . n 
G 1 217 LYS 217 217 217 LYS LYS G . n 
G 1 218 PRO 218 218 218 PRO PRO G . n 
G 1 219 GLU 219 219 219 GLU GLU G . n 
G 1 220 ILE 220 220 220 ILE ILE G . n 
G 1 221 ALA 221 221 221 ALA ALA G . n 
G 1 222 ILE 222 222 222 ILE ILE G . n 
G 1 223 ARG 223 223 223 ARG ARG G . n 
G 1 224 PRO 224 224 224 PRO PRO G . n 
G 1 225 LYS 225 225 225 LYS LYS G . n 
G 1 226 VAL 226 226 226 VAL VAL G . n 
G 1 227 ARG 227 227 227 ARG ARG G . n 
G 1 228 ASP 228 228 228 ASP ASP G . n 
G 1 229 GLN 229 229 229 GLN GLN G . n 
G 1 230 GLU 230 230 230 GLU GLU G . n 
G 1 231 GLY 231 231 231 GLY GLY G . n 
G 1 232 ARG 232 232 232 ARG ARG G . n 
G 1 233 MET 233 233 233 MET MET G . n 
G 1 234 ASN 234 234 234 ASN ASN G . n 
G 1 235 TYR 235 235 235 TYR TYR G . n 
G 1 236 TYR 236 236 236 TYR TYR G . n 
G 1 237 TRP 237 237 237 TRP TRP G . n 
G 1 238 THR 238 238 238 THR THR G . n 
G 1 239 LEU 239 239 239 LEU LEU G . n 
G 1 240 VAL 240 240 240 VAL VAL G . n 
G 1 241 GLU 241 241 241 GLU GLU G . n 
G 1 242 PRO 242 242 242 PRO PRO G . n 
G 1 243 GLY 243 243 243 GLY GLY G . n 
G 1 244 ASP 244 244 244 ASP ASP G . n 
G 1 245 LYS 245 245 245 LYS LYS G . n 
G 1 246 ILE 246 246 246 ILE ILE G . n 
G 1 247 THR 247 247 247 THR THR G . n 
G 1 248 PHE 248 248 248 PHE PHE G . n 
G 1 249 GLU 249 249 249 GLU GLU G . n 
G 1 250 ALA 250 250 250 ALA ALA G . n 
G 1 251 THR 251 251 251 THR THR G . n 
G 1 252 GLY 252 252 252 GLY GLY G . n 
G 1 253 ASN 253 253 253 ASN ASN G . n 
G 1 254 LEU 254 254 254 LEU LEU G . n 
G 1 255 VAL 255 255 255 VAL VAL G . n 
G 1 256 VAL 256 256 256 VAL VAL G . n 
G 1 257 PRO 257 257 257 PRO PRO G . n 
G 1 258 ARG 258 258 258 ARG ARG G . n 
G 1 259 TYR 259 259 259 TYR TYR G . n 
G 1 260 ALA 260 260 260 ALA ALA G . n 
G 1 261 PHE 261 261 261 PHE PHE G . n 
G 1 262 ALA 262 262 262 ALA ALA G . n 
G 1 263 MET 263 263 263 MET MET G . n 
G 1 264 GLU 264 264 264 GLU GLU G . n 
G 1 265 ARG 265 265 265 ARG ARG G . n 
G 1 266 ASN 266 266 266 ASN ASN G . n 
G 1 267 ALA 267 267 267 ALA ALA G . n 
G 1 268 GLY 268 268 268 GLY GLY G . n 
G 1 269 SER 269 269 269 SER SER G . n 
G 1 270 GLY 270 270 270 GLY GLY G . n 
G 1 271 ILE 271 271 271 ILE ILE G . n 
G 1 272 ILE 272 272 272 ILE ILE G . n 
G 1 273 ILE 273 273 273 ILE ILE G . n 
G 1 274 SER 274 274 274 SER SER G . n 
G 1 275 ASP 275 275 275 ASP ASP G . n 
G 1 276 THR 276 276 276 THR THR G . n 
G 1 277 PRO 277 277 277 PRO PRO G . n 
G 1 278 VAL 278 278 278 VAL VAL G . n 
G 1 279 HIS 279 279 279 HIS HIS G . n 
G 1 280 ASP 280 280 280 ASP ASP G . n 
G 1 281 CYS 281 281 281 CYS CYS G . n 
G 1 282 ASN 282 282 282 ASN ASN G . n 
G 1 283 THR 283 283 283 THR THR G . n 
G 1 284 THR 284 284 284 THR THR G . n 
G 1 285 CYS 285 285 285 CYS CYS G . n 
G 1 286 GLN 286 286 286 GLN GLN G . n 
G 1 287 THR 287 287 287 THR THR G . n 
G 1 288 PRO 288 288 288 PRO PRO G . n 
G 1 289 LYS 289 289 289 LYS LYS G . n 
G 1 290 GLY 290 290 290 GLY GLY G . n 
G 1 291 ALA 291 291 291 ALA ALA G . n 
G 1 292 ILE 292 292 292 ILE ILE G . n 
G 1 293 ASN 293 293 293 ASN ASN G . n 
G 1 294 THR 294 294 294 THR THR G . n 
G 1 295 SER 295 295 295 SER SER G . n 
G 1 296 LEU 296 296 296 LEU LEU G . n 
G 1 297 PRO 297 297 297 PRO PRO G . n 
G 1 298 PHE 298 298 298 PHE PHE G . n 
G 1 299 GLN 299 299 299 GLN GLN G . n 
G 1 300 ASN 300 300 300 ASN ASN G . n 
G 1 301 ILE 301 301 301 ILE ILE G . n 
G 1 302 HIS 302 302 302 HIS HIS G . n 
G 1 303 PRO 303 303 303 PRO PRO G . n 
G 1 304 ILE 304 304 304 ILE ILE G . n 
G 1 305 THR 305 305 305 THR THR G . n 
G 1 306 ILE 306 306 306 ILE ILE G . n 
G 1 307 GLY 307 307 307 GLY GLY G . n 
G 1 308 LYS 308 308 308 LYS LYS G . n 
G 1 309 CYS 309 309 309 CYS CYS G . n 
G 1 310 PRO 310 310 310 PRO PRO G . n 
G 1 311 LYS 311 311 311 LYS LYS G . n 
G 1 312 TYR 312 312 312 TYR TYR G . n 
G 1 313 VAL 313 313 313 VAL VAL G . n 
G 1 314 LYS 314 314 314 LYS LYS G . n 
G 1 315 SER 315 315 315 SER SER G . n 
G 1 316 THR 316 316 316 THR THR G . n 
G 1 317 LYS 317 317 317 LYS LYS G . n 
G 1 318 LEU 318 318 318 LEU LEU G . n 
G 1 319 ARG 319 319 319 ARG ARG G . n 
G 1 320 LEU 320 320 320 LEU LEU G . n 
G 1 321 ALA 321 321 321 ALA ALA G . n 
G 1 322 THR 322 322 322 THR THR G . n 
G 1 323 GLY 323 323 323 GLY GLY G . n 
G 1 324 LEU 324 324 324 LEU LEU G . n 
G 1 325 ARG 325 325 325 ARG ARG G . n 
G 1 326 ASN 326 326 326 ASN ASN G . n 
G 1 327 ILE 327 327 327 ILE ILE G . n 
G 1 328 PRO 328 328 ?   ?   ?   G . n 
G 1 329 SER 329 329 ?   ?   ?   G . n 
G 1 330 ILE 330 330 ?   ?   ?   G . n 
G 1 331 GLN 331 331 ?   ?   ?   G . n 
G 1 332 SER 332 332 ?   ?   ?   G . n 
G 1 333 ARG 333 333 ?   ?   ?   G . n 
H 2 1   GLY 1   1   1   GLY GLY H . n 
H 2 2   LEU 2   2   2   LEU LEU H . n 
H 2 3   PHE 3   3   3   PHE PHE H . n 
H 2 4   GLY 4   4   4   GLY GLY H . n 
H 2 5   ALA 5   5   5   ALA ALA H . n 
H 2 6   ILE 6   6   6   ILE ILE H . n 
H 2 7   ALA 7   7   7   ALA ALA H . n 
H 2 8   GLY 8   8   8   GLY GLY H . n 
H 2 9   PHE 9   9   9   PHE PHE H . n 
H 2 10  ILE 10  10  10  ILE ILE H . n 
H 2 11  GLU 11  11  11  GLU GLU H . n 
H 2 12  GLY 12  12  12  GLY GLY H . n 
H 2 13  GLY 13  13  13  GLY GLY H . n 
H 2 14  TRP 14  14  14  TRP TRP H . n 
H 2 15  THR 15  15  15  THR THR H . n 
H 2 16  GLY 16  16  16  GLY GLY H . n 
H 2 17  MET 17  17  17  MET MET H . n 
H 2 18  VAL 18  18  18  VAL VAL H . n 
H 2 19  ASP 19  19  19  ASP ASP H . n 
H 2 20  GLY 20  20  20  GLY GLY H . n 
H 2 21  TRP 21  21  21  TRP TRP H . n 
H 2 22  TYR 22  22  22  TYR TYR H . n 
H 2 23  GLY 23  23  23  GLY GLY H . n 
H 2 24  TYR 24  24  24  TYR TYR H . n 
H 2 25  HIS 25  25  25  HIS HIS H . n 
H 2 26  HIS 26  26  26  HIS HIS H . n 
H 2 27  GLN 27  27  27  GLN GLN H . n 
H 2 28  ASN 28  28  28  ASN ASN H . n 
H 2 29  GLU 29  29  29  GLU GLU H . n 
H 2 30  GLN 30  30  30  GLN GLN H . n 
H 2 31  GLY 31  31  31  GLY GLY H . n 
H 2 32  SER 32  32  32  SER SER H . n 
H 2 33  GLY 33  33  33  GLY GLY H . n 
H 2 34  TYR 34  34  34  TYR TYR H . n 
H 2 35  ALA 35  35  35  ALA ALA H . n 
H 2 36  ALA 36  36  36  ALA ALA H . n 
H 2 37  ASP 37  37  37  ASP ASP H . n 
H 2 38  LEU 38  38  38  LEU LEU H . n 
H 2 39  LYS 39  39  39  LYS LYS H . n 
H 2 40  SER 40  40  40  SER SER H . n 
H 2 41  THR 41  41  41  THR THR H . n 
H 2 42  GLN 42  42  42  GLN GLN H . n 
H 2 43  ASN 43  43  43  ASN ASN H . n 
H 2 44  ALA 44  44  44  ALA ALA H . n 
H 2 45  ILE 45  45  45  ILE ILE H . n 
H 2 46  ASP 46  46  46  ASP ASP H . n 
H 2 47  GLU 47  47  47  GLU GLU H . n 
H 2 48  ILE 48  48  48  ILE ILE H . n 
H 2 49  THR 49  49  49  THR THR H . n 
H 2 50  ASN 50  50  50  ASN ASN H . n 
H 2 51  LYS 51  51  51  LYS LYS H . n 
H 2 52  VAL 52  52  52  VAL VAL H . n 
H 2 53  ASN 53  53  53  ASN ASN H . n 
H 2 54  SER 54  54  54  SER SER H . n 
H 2 55  VAL 55  55  55  VAL VAL H . n 
H 2 56  ILE 56  56  56  ILE ILE H . n 
H 2 57  GLU 57  57  57  GLU GLU H . n 
H 2 58  LYS 58  58  58  LYS LYS H . n 
H 2 59  MET 59  59  59  MET MET H . n 
H 2 60  ASN 60  60  60  ASN ASN H . n 
H 2 61  THR 61  61  61  THR THR H . n 
H 2 62  GLN 62  62  62  GLN GLN H . n 
H 2 63  PHE 63  63  63  PHE PHE H . n 
H 2 64  THR 64  64  64  THR THR H . n 
H 2 65  ALA 65  65  65  ALA ALA H . n 
H 2 66  VAL 66  66  66  VAL VAL H . n 
H 2 67  GLY 67  67  67  GLY GLY H . n 
H 2 68  LYS 68  68  68  LYS LYS H . n 
H 2 69  GLU 69  69  69  GLU GLU H . n 
H 2 70  PHE 70  70  70  PHE PHE H . n 
H 2 71  ASN 71  71  71  ASN ASN H . n 
H 2 72  HIS 72  72  72  HIS HIS H . n 
H 2 73  LEU 73  73  73  LEU LEU H . n 
H 2 74  GLU 74  74  74  GLU GLU H . n 
H 2 75  LYS 75  75  75  LYS LYS H . n 
H 2 76  ARG 76  76  76  ARG ARG H . n 
H 2 77  ILE 77  77  77  ILE ILE H . n 
H 2 78  GLU 78  78  78  GLU GLU H . n 
H 2 79  ASN 79  79  79  ASN ASN H . n 
H 2 80  LEU 80  80  80  LEU LEU H . n 
H 2 81  ASN 81  81  81  ASN ASN H . n 
H 2 82  LYS 82  82  82  LYS LYS H . n 
H 2 83  LYS 83  83  83  LYS LYS H . n 
H 2 84  VAL 84  84  84  VAL VAL H . n 
H 2 85  ASP 85  85  85  ASP ASP H . n 
H 2 86  ASP 86  86  86  ASP ASP H . n 
H 2 87  GLY 87  87  87  GLY GLY H . n 
H 2 88  PHE 88  88  88  PHE PHE H . n 
H 2 89  LEU 89  89  89  LEU LEU H . n 
H 2 90  ASP 90  90  90  ASP ASP H . n 
H 2 91  ILE 91  91  91  ILE ILE H . n 
H 2 92  TRP 92  92  92  TRP TRP H . n 
H 2 93  THR 93  93  93  THR THR H . n 
H 2 94  TYR 94  94  94  TYR TYR H . n 
H 2 95  ASN 95  95  95  ASN ASN H . n 
H 2 96  ALA 96  96  96  ALA ALA H . n 
H 2 97  GLU 97  97  97  GLU GLU H . n 
H 2 98  LEU 98  98  98  LEU LEU H . n 
H 2 99  LEU 99  99  99  LEU LEU H . n 
H 2 100 VAL 100 100 100 VAL VAL H . n 
H 2 101 LEU 101 101 101 LEU LEU H . n 
H 2 102 LEU 102 102 102 LEU LEU H . n 
H 2 103 GLU 103 103 103 GLU GLU H . n 
H 2 104 ASN 104 104 104 ASN ASN H . n 
H 2 105 GLU 105 105 105 GLU GLU H . n 
H 2 106 ARG 106 106 106 ARG ARG H . n 
H 2 107 THR 107 107 107 THR THR H . n 
H 2 108 LEU 108 108 108 LEU LEU H . n 
H 2 109 ASP 109 109 109 ASP ASP H . n 
H 2 110 TYR 110 110 110 TYR TYR H . n 
H 2 111 HIS 111 111 111 HIS HIS H . n 
H 2 112 ASP 112 112 112 ASP ASP H . n 
H 2 113 SER 113 113 113 SER SER H . n 
H 2 114 ASN 114 114 114 ASN ASN H . n 
H 2 115 VAL 115 115 115 VAL VAL H . n 
H 2 116 LYS 116 116 116 LYS LYS H . n 
H 2 117 ASN 117 117 117 ASN ASN H . n 
H 2 118 LEU 118 118 118 LEU LEU H . n 
H 2 119 TYR 119 119 119 TYR TYR H . n 
H 2 120 GLU 120 120 120 GLU GLU H . n 
H 2 121 LYS 121 121 121 LYS LYS H . n 
H 2 122 VAL 122 122 122 VAL VAL H . n 
H 2 123 ARG 123 123 123 ARG ARG H . n 
H 2 124 SER 124 124 124 SER SER H . n 
H 2 125 GLN 125 125 125 GLN GLN H . n 
H 2 126 LEU 126 126 126 LEU LEU H . n 
H 2 127 LYS 127 127 127 LYS LYS H . n 
H 2 128 ASN 128 128 128 ASN ASN H . n 
H 2 129 ASN 129 129 129 ASN ASN H . n 
H 2 130 ALA 130 130 130 ALA ALA H . n 
H 2 131 LYS 131 131 131 LYS LYS H . n 
H 2 132 GLU 132 132 132 GLU GLU H . n 
H 2 133 ILE 133 133 133 ILE ILE H . n 
H 2 134 GLY 134 134 134 GLY GLY H . n 
H 2 135 ASN 135 135 135 ASN ASN H . n 
H 2 136 GLY 136 136 136 GLY GLY H . n 
H 2 137 CYS 137 137 137 CYS CYS H . n 
H 2 138 PHE 138 138 138 PHE PHE H . n 
H 2 139 GLU 139 139 139 GLU GLU H . n 
H 2 140 PHE 140 140 140 PHE PHE H . n 
H 2 141 TYR 141 141 141 TYR TYR H . n 
H 2 142 HIS 142 142 142 HIS HIS H . n 
H 2 143 LYS 143 143 143 LYS LYS H . n 
H 2 144 CYS 144 144 144 CYS CYS H . n 
H 2 145 ASP 145 145 145 ASP ASP H . n 
H 2 146 ASN 146 146 146 ASN ASN H . n 
H 2 147 THR 147 147 147 THR THR H . n 
H 2 148 CYS 148 148 148 CYS CYS H . n 
H 2 149 MET 149 149 149 MET MET H . n 
H 2 150 GLU 150 150 150 GLU GLU H . n 
H 2 151 SER 151 151 151 SER SER H . n 
H 2 152 VAL 152 152 152 VAL VAL H . n 
H 2 153 LYS 153 153 153 LYS LYS H . n 
H 2 154 ASN 154 154 154 ASN ASN H . n 
H 2 155 GLY 155 155 155 GLY GLY H . n 
H 2 156 THR 156 156 156 THR THR H . n 
H 2 157 TYR 157 157 157 TYR TYR H . n 
H 2 158 ASP 158 158 158 ASP ASP H . n 
H 2 159 TYR 159 159 159 TYR TYR H . n 
H 2 160 PRO 160 160 160 PRO PRO H . n 
H 2 161 LYS 161 161 161 LYS LYS H . n 
H 2 162 TYR 162 162 162 TYR TYR H . n 
H 2 163 SER 163 163 ?   ?   ?   H . n 
H 2 164 GLU 164 164 ?   ?   ?   H . n 
H 2 165 GLU 165 165 ?   ?   ?   H . n 
H 2 166 ALA 166 166 ?   ?   ?   H . n 
H 2 167 LYS 167 167 ?   ?   ?   H . n 
H 2 168 LEU 168 168 ?   ?   ?   H . n 
H 2 169 ASN 169 169 ?   ?   ?   H . n 
H 2 170 ARG 170 170 ?   ?   ?   H . n 
H 2 171 GLU 171 171 ?   ?   ?   H . n 
H 2 172 GLU 172 172 ?   ?   ?   H . n 
H 2 173 ILE 173 173 ?   ?   ?   H . n 
H 2 174 ASP 174 174 ?   ?   ?   H . n 
H 2 175 GLY 175 175 ?   ?   ?   H . n 
H 2 176 VAL 176 176 ?   ?   ?   H . n 
H 2 177 ARG 177 177 ?   ?   ?   H . n 
H 2 178 LEU 178 178 ?   ?   ?   H . n 
H 2 179 VAL 179 179 ?   ?   ?   H . n 
H 2 180 PRO 180 180 ?   ?   ?   H . n 
H 2 181 ARG 181 181 ?   ?   ?   H . n 
I 1 1   ALA 1   1   ?   ?   ?   I . n 
I 1 2   ASP 2   2   ?   ?   ?   I . n 
I 1 3   LEU 3   3   ?   ?   ?   I . n 
I 1 4   GLY 4   4   ?   ?   ?   I . n 
I 1 5   SER 5   5   ?   ?   ?   I . n 
I 1 6   ARG 6   6   ?   ?   ?   I . n 
I 1 7   ASP 7   7   7   ASP ASP I . n 
I 1 8   THR 8   8   8   THR THR I . n 
I 1 9   LEU 9   9   9   LEU LEU I . n 
I 1 10  CYS 10  10  10  CYS CYS I . n 
I 1 11  ILE 11  11  11  ILE ILE I . n 
I 1 12  GLY 12  12  12  GLY GLY I . n 
I 1 13  TYR 13  13  13  TYR TYR I . n 
I 1 14  HIS 14  14  14  HIS HIS I . n 
I 1 15  ALA 15  15  15  ALA ALA I . n 
I 1 16  ASN 16  16  16  ASN ASN I . n 
I 1 17  ASN 17  17  17  ASN ASN I . n 
I 1 18  SER 18  18  18  SER SER I . n 
I 1 19  THR 19  19  19  THR THR I . n 
I 1 20  ASP 20  20  20  ASP ASP I . n 
I 1 21  THR 21  21  21  THR THR I . n 
I 1 22  VAL 22  22  22  VAL VAL I . n 
I 1 23  ASP 23  23  23  ASP ASP I . n 
I 1 24  THR 24  24  24  THR THR I . n 
I 1 25  VAL 25  25  25  VAL VAL I . n 
I 1 26  LEU 26  26  26  LEU LEU I . n 
I 1 27  GLU 27  27  27  GLU GLU I . n 
I 1 28  LYS 28  28  28  LYS LYS I . n 
I 1 29  ASN 29  29  29  ASN ASN I . n 
I 1 30  VAL 30  30  30  VAL VAL I . n 
I 1 31  THR 31  31  31  THR THR I . n 
I 1 32  VAL 32  32  32  VAL VAL I . n 
I 1 33  THR 33  33  33  THR THR I . n 
I 1 34  HIS 34  34  34  HIS HIS I . n 
I 1 35  SER 35  35  35  SER SER I . n 
I 1 36  VAL 36  36  36  VAL VAL I . n 
I 1 37  ASN 37  37  37  ASN ASN I . n 
I 1 38  LEU 38  38  38  LEU LEU I . n 
I 1 39  LEU 39  39  39  LEU LEU I . n 
I 1 40  GLU 40  40  40  GLU GLU I . n 
I 1 41  ASP 41  41  41  ASP ASP I . n 
I 1 42  LYS 42  42  42  LYS LYS I . n 
I 1 43  HIS 43  43  43  HIS HIS I . n 
I 1 44  ASN 44  44  44  ASN ASN I . n 
I 1 45  GLY 45  45  45  GLY GLY I . n 
I 1 46  LYS 46  46  46  LYS LYS I . n 
I 1 47  LEU 47  47  47  LEU LEU I . n 
I 1 48  CYS 48  48  48  CYS CYS I . n 
I 1 49  LYS 49  49  49  LYS LYS I . n 
I 1 50  LEU 50  50  50  LEU LEU I . n 
I 1 51  ARG 51  51  51  ARG ARG I . n 
I 1 52  GLY 52  52  52  GLY GLY I . n 
I 1 53  VAL 53  53  53  VAL VAL I . n 
I 1 54  ALA 54  54  54  ALA ALA I . n 
I 1 55  PRO 55  55  55  PRO PRO I . n 
I 1 56  LEU 56  56  56  LEU LEU I . n 
I 1 57  HIS 57  57  57  HIS HIS I . n 
I 1 58  LEU 58  58  58  LEU LEU I . n 
I 1 59  GLY 59  59  59  GLY GLY I . n 
I 1 60  LYS 60  60  60  LYS LYS I . n 
I 1 61  CYS 61  61  61  CYS CYS I . n 
I 1 62  ASN 62  62  62  ASN ASN I . n 
I 1 63  ILE 63  63  63  ILE ILE I . n 
I 1 64  ALA 64  64  64  ALA ALA I . n 
I 1 65  GLY 65  65  65  GLY GLY I . n 
I 1 66  TRP 66  66  66  TRP TRP I . n 
I 1 67  ILE 67  67  67  ILE ILE I . n 
I 1 68  LEU 68  68  68  LEU LEU I . n 
I 1 69  GLY 69  69  69  GLY GLY I . n 
I 1 70  ASN 70  70  70  ASN ASN I . n 
I 1 71  PRO 71  71  71  PRO PRO I . n 
I 1 72  GLU 72  72  72  GLU GLU I . n 
I 1 73  CYS 73  73  73  CYS CYS I . n 
I 1 74  GLU 74  74  74  GLU GLU I . n 
I 1 75  SER 75  75  75  SER SER I . n 
I 1 76  LEU 76  76  76  LEU LEU I . n 
I 1 77  SER 77  77  77  SER SER I . n 
I 1 78  THR 78  78  78  THR THR I . n 
I 1 79  ALA 79  79  79  ALA ALA I . n 
I 1 80  SER 80  80  80  SER SER I . n 
I 1 81  SER 81  81  81  SER SER I . n 
I 1 82  TRP 82  82  82  TRP TRP I . n 
I 1 83  SER 83  83  83  SER SER I . n 
I 1 84  TYR 84  84  84  TYR TYR I . n 
I 1 85  ILE 85  85  85  ILE ILE I . n 
I 1 86  VAL 86  86  86  VAL VAL I . n 
I 1 87  GLU 87  87  87  GLU GLU I . n 
I 1 88  THR 88  88  88  THR THR I . n 
I 1 89  PRO 89  89  89  PRO PRO I . n 
I 1 90  SER 90  90  90  SER SER I . n 
I 1 91  SER 91  91  91  SER SER I . n 
I 1 92  ASP 92  92  92  ASP ASP I . n 
I 1 93  ASN 93  93  93  ASN ASN I . n 
I 1 94  GLY 94  94  94  GLY GLY I . n 
I 1 95  THR 95  95  95  THR THR I . n 
I 1 96  CYS 96  96  96  CYS CYS I . n 
I 1 97  TYR 97  97  97  TYR TYR I . n 
I 1 98  PRO 98  98  98  PRO PRO I . n 
I 1 99  GLY 99  99  99  GLY GLY I . n 
I 1 100 ASP 100 100 100 ASP ASP I . n 
I 1 101 PHE 101 101 101 PHE PHE I . n 
I 1 102 ILE 102 102 102 ILE ILE I . n 
I 1 103 ASP 103 103 103 ASP ASP I . n 
I 1 104 TYR 104 104 104 TYR TYR I . n 
I 1 105 GLU 105 105 105 GLU GLU I . n 
I 1 106 GLU 106 106 106 GLU GLU I . n 
I 1 107 LEU 107 107 107 LEU LEU I . n 
I 1 108 ARG 108 108 108 ARG ARG I . n 
I 1 109 GLU 109 109 109 GLU GLU I . n 
I 1 110 GLN 110 110 110 GLN GLN I . n 
I 1 111 LEU 111 111 111 LEU LEU I . n 
I 1 112 SER 112 112 112 SER SER I . n 
I 1 113 SER 113 113 113 SER SER I . n 
I 1 114 VAL 114 114 114 VAL VAL I . n 
I 1 115 SER 115 115 115 SER SER I . n 
I 1 116 SER 116 116 116 SER SER I . n 
I 1 117 PHE 117 117 117 PHE PHE I . n 
I 1 118 GLU 118 118 118 GLU GLU I . n 
I 1 119 ARG 119 119 119 ARG ARG I . n 
I 1 120 PHE 120 120 120 PHE PHE I . n 
I 1 121 GLU 121 121 121 GLU GLU I . n 
I 1 122 ILE 122 122 122 ILE ILE I . n 
I 1 123 PHE 123 123 123 PHE PHE I . n 
I 1 124 PRO 124 124 124 PRO PRO I . n 
I 1 125 LYS 125 125 125 LYS LYS I . n 
I 1 126 THR 126 126 126 THR THR I . n 
I 1 127 SER 127 127 127 SER SER I . n 
I 1 128 SER 128 128 128 SER SER I . n 
I 1 129 TRP 129 129 129 TRP TRP I . n 
I 1 130 PRO 130 130 130 PRO PRO I . n 
I 1 131 ASN 131 131 131 ASN ASN I . n 
I 1 132 HIS 132 132 132 HIS HIS I . n 
I 1 133 ASP 133 133 133 ASP ASP I . n 
I 1 134 SER 134 134 134 SER SER I . n 
I 1 135 ASN 135 135 135 ASN ASN I . n 
I 1 136 LYS 136 136 136 LYS LYS I . n 
I 1 137 GLY 137 137 137 GLY GLY I . n 
I 1 138 VAL 138 138 138 VAL VAL I . n 
I 1 139 THR 139 139 139 THR THR I . n 
I 1 140 ALA 140 140 140 ALA ALA I . n 
I 1 141 ALA 141 141 141 ALA ALA I . n 
I 1 142 CYS 142 142 142 CYS CYS I . n 
I 1 143 PRO 143 143 143 PRO PRO I . n 
I 1 144 HIS 144 144 144 HIS HIS I . n 
I 1 145 ALA 145 145 145 ALA ALA I . n 
I 1 146 GLY 146 146 146 GLY GLY I . n 
I 1 147 ALA 147 147 147 ALA ALA I . n 
I 1 148 LYS 148 148 148 LYS LYS I . n 
I 1 149 SER 149 149 149 SER SER I . n 
I 1 150 PHE 150 150 150 PHE PHE I . n 
I 1 151 TYR 151 151 151 TYR TYR I . n 
I 1 152 LYS 152 152 152 LYS LYS I . n 
I 1 153 ASN 153 153 153 ASN ASN I . n 
I 1 154 LEU 154 154 154 LEU LEU I . n 
I 1 155 ILE 155 155 155 ILE ILE I . n 
I 1 156 TRP 156 156 156 TRP TRP I . n 
I 1 157 LEU 157 157 157 LEU LEU I . n 
I 1 158 VAL 158 158 158 VAL VAL I . n 
I 1 159 LYS 159 159 159 LYS LYS I . n 
I 1 160 LYS 160 160 160 LYS LYS I . n 
I 1 161 GLY 161 161 161 GLY GLY I . n 
I 1 162 ASN 162 162 162 ASN ASN I . n 
I 1 163 SER 163 163 163 SER SER I . n 
I 1 164 TYR 164 164 164 TYR TYR I . n 
I 1 165 PRO 165 165 165 PRO PRO I . n 
I 1 166 LYS 166 166 166 LYS LYS I . n 
I 1 167 LEU 167 167 167 LEU LEU I . n 
I 1 168 SER 168 168 168 SER SER I . n 
I 1 169 LYS 169 169 169 LYS LYS I . n 
I 1 170 SER 170 170 170 SER SER I . n 
I 1 171 TYR 171 171 171 TYR TYR I . n 
I 1 172 ILE 172 172 172 ILE ILE I . n 
I 1 173 ASN 173 173 173 ASN ASN I . n 
I 1 174 ASP 174 174 174 ASP ASP I . n 
I 1 175 LYS 175 175 175 LYS LYS I . n 
I 1 176 GLY 176 176 176 GLY GLY I . n 
I 1 177 LYS 177 177 177 LYS LYS I . n 
I 1 178 GLU 178 178 178 GLU GLU I . n 
I 1 179 VAL 179 179 179 VAL VAL I . n 
I 1 180 LEU 180 180 180 LEU LEU I . n 
I 1 181 VAL 181 181 181 VAL VAL I . n 
I 1 182 LEU 182 182 182 LEU LEU I . n 
I 1 183 TRP 183 183 183 TRP TRP I . n 
I 1 184 GLY 184 184 184 GLY GLY I . n 
I 1 185 ILE 185 185 185 ILE ILE I . n 
I 1 186 HIS 186 186 186 HIS HIS I . n 
I 1 187 HIS 187 187 187 HIS HIS I . n 
I 1 188 PRO 188 188 188 PRO PRO I . n 
I 1 189 SER 189 189 189 SER SER I . n 
I 1 190 THR 190 190 190 THR THR I . n 
I 1 191 SER 191 191 191 SER SER I . n 
I 1 192 ALA 192 192 192 ALA ALA I . n 
I 1 193 ASP 193 193 193 ASP ASP I . n 
I 1 194 GLN 194 194 194 GLN GLN I . n 
I 1 195 GLN 195 195 195 GLN GLN I . n 
I 1 196 SER 196 196 196 SER SER I . n 
I 1 197 LEU 197 197 197 LEU LEU I . n 
I 1 198 TYR 198 198 198 TYR TYR I . n 
I 1 199 GLN 199 199 199 GLN GLN I . n 
I 1 200 ASN 200 200 200 ASN ASN I . n 
I 1 201 ALA 201 201 201 ALA ALA I . n 
I 1 202 ASP 202 202 202 ASP ASP I . n 
I 1 203 THR 203 203 203 THR THR I . n 
I 1 204 TYR 204 204 204 TYR TYR I . n 
I 1 205 VAL 205 205 205 VAL VAL I . n 
I 1 206 PHE 206 206 206 PHE PHE I . n 
I 1 207 VAL 207 207 207 VAL VAL I . n 
I 1 208 GLY 208 208 208 GLY GLY I . n 
I 1 209 SER 209 209 209 SER SER I . n 
I 1 210 SER 210 210 210 SER SER I . n 
I 1 211 ARG 211 211 211 ARG ARG I . n 
I 1 212 TYR 212 212 212 TYR TYR I . n 
I 1 213 SER 213 213 213 SER SER I . n 
I 1 214 LYS 214 214 214 LYS LYS I . n 
I 1 215 LYS 215 215 215 LYS LYS I . n 
I 1 216 PHE 216 216 216 PHE PHE I . n 
I 1 217 LYS 217 217 217 LYS LYS I . n 
I 1 218 PRO 218 218 218 PRO PRO I . n 
I 1 219 GLU 219 219 219 GLU GLU I . n 
I 1 220 ILE 220 220 220 ILE ILE I . n 
I 1 221 ALA 221 221 221 ALA ALA I . n 
I 1 222 ILE 222 222 222 ILE ILE I . n 
I 1 223 ARG 223 223 223 ARG ARG I . n 
I 1 224 PRO 224 224 224 PRO PRO I . n 
I 1 225 LYS 225 225 225 LYS LYS I . n 
I 1 226 VAL 226 226 226 VAL VAL I . n 
I 1 227 ARG 227 227 227 ARG ARG I . n 
I 1 228 ASP 228 228 228 ASP ASP I . n 
I 1 229 GLN 229 229 229 GLN GLN I . n 
I 1 230 GLU 230 230 230 GLU GLU I . n 
I 1 231 GLY 231 231 231 GLY GLY I . n 
I 1 232 ARG 232 232 232 ARG ARG I . n 
I 1 233 MET 233 233 233 MET MET I . n 
I 1 234 ASN 234 234 234 ASN ASN I . n 
I 1 235 TYR 235 235 235 TYR TYR I . n 
I 1 236 TYR 236 236 236 TYR TYR I . n 
I 1 237 TRP 237 237 237 TRP TRP I . n 
I 1 238 THR 238 238 238 THR THR I . n 
I 1 239 LEU 239 239 239 LEU LEU I . n 
I 1 240 VAL 240 240 240 VAL VAL I . n 
I 1 241 GLU 241 241 241 GLU GLU I . n 
I 1 242 PRO 242 242 242 PRO PRO I . n 
I 1 243 GLY 243 243 243 GLY GLY I . n 
I 1 244 ASP 244 244 244 ASP ASP I . n 
I 1 245 LYS 245 245 245 LYS LYS I . n 
I 1 246 ILE 246 246 246 ILE ILE I . n 
I 1 247 THR 247 247 247 THR THR I . n 
I 1 248 PHE 248 248 248 PHE PHE I . n 
I 1 249 GLU 249 249 249 GLU GLU I . n 
I 1 250 ALA 250 250 250 ALA ALA I . n 
I 1 251 THR 251 251 251 THR THR I . n 
I 1 252 GLY 252 252 252 GLY GLY I . n 
I 1 253 ASN 253 253 253 ASN ASN I . n 
I 1 254 LEU 254 254 254 LEU LEU I . n 
I 1 255 VAL 255 255 255 VAL VAL I . n 
I 1 256 VAL 256 256 256 VAL VAL I . n 
I 1 257 PRO 257 257 257 PRO PRO I . n 
I 1 258 ARG 258 258 258 ARG ARG I . n 
I 1 259 TYR 259 259 259 TYR TYR I . n 
I 1 260 ALA 260 260 260 ALA ALA I . n 
I 1 261 PHE 261 261 261 PHE PHE I . n 
I 1 262 ALA 262 262 262 ALA ALA I . n 
I 1 263 MET 263 263 263 MET MET I . n 
I 1 264 GLU 264 264 264 GLU GLU I . n 
I 1 265 ARG 265 265 265 ARG ARG I . n 
I 1 266 ASN 266 266 266 ASN ASN I . n 
I 1 267 ALA 267 267 267 ALA ALA I . n 
I 1 268 GLY 268 268 268 GLY GLY I . n 
I 1 269 SER 269 269 269 SER SER I . n 
I 1 270 GLY 270 270 270 GLY GLY I . n 
I 1 271 ILE 271 271 271 ILE ILE I . n 
I 1 272 ILE 272 272 272 ILE ILE I . n 
I 1 273 ILE 273 273 273 ILE ILE I . n 
I 1 274 SER 274 274 274 SER SER I . n 
I 1 275 ASP 275 275 275 ASP ASP I . n 
I 1 276 THR 276 276 276 THR THR I . n 
I 1 277 PRO 277 277 277 PRO PRO I . n 
I 1 278 VAL 278 278 278 VAL VAL I . n 
I 1 279 HIS 279 279 279 HIS HIS I . n 
I 1 280 ASP 280 280 280 ASP ASP I . n 
I 1 281 CYS 281 281 281 CYS CYS I . n 
I 1 282 ASN 282 282 282 ASN ASN I . n 
I 1 283 THR 283 283 283 THR THR I . n 
I 1 284 THR 284 284 284 THR THR I . n 
I 1 285 CYS 285 285 285 CYS CYS I . n 
I 1 286 GLN 286 286 286 GLN GLN I . n 
I 1 287 THR 287 287 287 THR THR I . n 
I 1 288 PRO 288 288 288 PRO PRO I . n 
I 1 289 LYS 289 289 289 LYS LYS I . n 
I 1 290 GLY 290 290 290 GLY GLY I . n 
I 1 291 ALA 291 291 291 ALA ALA I . n 
I 1 292 ILE 292 292 292 ILE ILE I . n 
I 1 293 ASN 293 293 293 ASN ASN I . n 
I 1 294 THR 294 294 294 THR THR I . n 
I 1 295 SER 295 295 295 SER SER I . n 
I 1 296 LEU 296 296 296 LEU LEU I . n 
I 1 297 PRO 297 297 297 PRO PRO I . n 
I 1 298 PHE 298 298 298 PHE PHE I . n 
I 1 299 GLN 299 299 299 GLN GLN I . n 
I 1 300 ASN 300 300 300 ASN ASN I . n 
I 1 301 ILE 301 301 301 ILE ILE I . n 
I 1 302 HIS 302 302 302 HIS HIS I . n 
I 1 303 PRO 303 303 303 PRO PRO I . n 
I 1 304 ILE 304 304 304 ILE ILE I . n 
I 1 305 THR 305 305 305 THR THR I . n 
I 1 306 ILE 306 306 306 ILE ILE I . n 
I 1 307 GLY 307 307 307 GLY GLY I . n 
I 1 308 LYS 308 308 308 LYS LYS I . n 
I 1 309 CYS 309 309 309 CYS CYS I . n 
I 1 310 PRO 310 310 310 PRO PRO I . n 
I 1 311 LYS 311 311 311 LYS LYS I . n 
I 1 312 TYR 312 312 312 TYR TYR I . n 
I 1 313 VAL 313 313 313 VAL VAL I . n 
I 1 314 LYS 314 314 314 LYS LYS I . n 
I 1 315 SER 315 315 315 SER SER I . n 
I 1 316 THR 316 316 316 THR THR I . n 
I 1 317 LYS 317 317 317 LYS LYS I . n 
I 1 318 LEU 318 318 318 LEU LEU I . n 
I 1 319 ARG 319 319 319 ARG ARG I . n 
I 1 320 LEU 320 320 320 LEU LEU I . n 
I 1 321 ALA 321 321 321 ALA ALA I . n 
I 1 322 THR 322 322 322 THR THR I . n 
I 1 323 GLY 323 323 323 GLY GLY I . n 
I 1 324 LEU 324 324 324 LEU LEU I . n 
I 1 325 ARG 325 325 325 ARG ARG I . n 
I 1 326 ASN 326 326 326 ASN ASN I . n 
I 1 327 ILE 327 327 327 ILE ILE I . n 
I 1 328 PRO 328 328 ?   ?   ?   I . n 
I 1 329 SER 329 329 ?   ?   ?   I . n 
I 1 330 ILE 330 330 ?   ?   ?   I . n 
I 1 331 GLN 331 331 ?   ?   ?   I . n 
I 1 332 SER 332 332 ?   ?   ?   I . n 
I 1 333 ARG 333 333 ?   ?   ?   I . n 
J 2 1   GLY 1   1   1   GLY GLY J . n 
J 2 2   LEU 2   2   2   LEU LEU J . n 
J 2 3   PHE 3   3   3   PHE PHE J . n 
J 2 4   GLY 4   4   4   GLY GLY J . n 
J 2 5   ALA 5   5   5   ALA ALA J . n 
J 2 6   ILE 6   6   6   ILE ILE J . n 
J 2 7   ALA 7   7   7   ALA ALA J . n 
J 2 8   GLY 8   8   8   GLY GLY J . n 
J 2 9   PHE 9   9   9   PHE PHE J . n 
J 2 10  ILE 10  10  10  ILE ILE J . n 
J 2 11  GLU 11  11  11  GLU GLU J . n 
J 2 12  GLY 12  12  12  GLY GLY J . n 
J 2 13  GLY 13  13  13  GLY GLY J . n 
J 2 14  TRP 14  14  14  TRP TRP J . n 
J 2 15  THR 15  15  15  THR THR J . n 
J 2 16  GLY 16  16  16  GLY GLY J . n 
J 2 17  MET 17  17  17  MET MET J . n 
J 2 18  VAL 18  18  18  VAL VAL J . n 
J 2 19  ASP 19  19  19  ASP ASP J . n 
J 2 20  GLY 20  20  20  GLY GLY J . n 
J 2 21  TRP 21  21  21  TRP TRP J . n 
J 2 22  TYR 22  22  22  TYR TYR J . n 
J 2 23  GLY 23  23  23  GLY GLY J . n 
J 2 24  TYR 24  24  24  TYR TYR J . n 
J 2 25  HIS 25  25  25  HIS HIS J . n 
J 2 26  HIS 26  26  26  HIS HIS J . n 
J 2 27  GLN 27  27  27  GLN GLN J . n 
J 2 28  ASN 28  28  28  ASN ASN J . n 
J 2 29  GLU 29  29  29  GLU GLU J . n 
J 2 30  GLN 30  30  30  GLN GLN J . n 
J 2 31  GLY 31  31  31  GLY GLY J . n 
J 2 32  SER 32  32  32  SER SER J . n 
J 2 33  GLY 33  33  33  GLY GLY J . n 
J 2 34  TYR 34  34  34  TYR TYR J . n 
J 2 35  ALA 35  35  35  ALA ALA J . n 
J 2 36  ALA 36  36  36  ALA ALA J . n 
J 2 37  ASP 37  37  37  ASP ASP J . n 
J 2 38  LEU 38  38  38  LEU LEU J . n 
J 2 39  LYS 39  39  39  LYS LYS J . n 
J 2 40  SER 40  40  40  SER SER J . n 
J 2 41  THR 41  41  41  THR THR J . n 
J 2 42  GLN 42  42  42  GLN GLN J . n 
J 2 43  ASN 43  43  43  ASN ASN J . n 
J 2 44  ALA 44  44  44  ALA ALA J . n 
J 2 45  ILE 45  45  45  ILE ILE J . n 
J 2 46  ASP 46  46  46  ASP ASP J . n 
J 2 47  GLU 47  47  47  GLU GLU J . n 
J 2 48  ILE 48  48  48  ILE ILE J . n 
J 2 49  THR 49  49  49  THR THR J . n 
J 2 50  ASN 50  50  50  ASN ASN J . n 
J 2 51  LYS 51  51  51  LYS LYS J . n 
J 2 52  VAL 52  52  52  VAL VAL J . n 
J 2 53  ASN 53  53  53  ASN ASN J . n 
J 2 54  SER 54  54  54  SER SER J . n 
J 2 55  VAL 55  55  55  VAL VAL J . n 
J 2 56  ILE 56  56  56  ILE ILE J . n 
J 2 57  GLU 57  57  57  GLU GLU J . n 
J 2 58  LYS 58  58  58  LYS LYS J . n 
J 2 59  MET 59  59  59  MET MET J . n 
J 2 60  ASN 60  60  60  ASN ASN J . n 
J 2 61  THR 61  61  61  THR THR J . n 
J 2 62  GLN 62  62  62  GLN GLN J . n 
J 2 63  PHE 63  63  63  PHE PHE J . n 
J 2 64  THR 64  64  64  THR THR J . n 
J 2 65  ALA 65  65  65  ALA ALA J . n 
J 2 66  VAL 66  66  66  VAL VAL J . n 
J 2 67  GLY 67  67  67  GLY GLY J . n 
J 2 68  LYS 68  68  68  LYS LYS J . n 
J 2 69  GLU 69  69  69  GLU GLU J . n 
J 2 70  PHE 70  70  70  PHE PHE J . n 
J 2 71  ASN 71  71  71  ASN ASN J . n 
J 2 72  HIS 72  72  72  HIS HIS J . n 
J 2 73  LEU 73  73  73  LEU LEU J . n 
J 2 74  GLU 74  74  74  GLU GLU J . n 
J 2 75  LYS 75  75  75  LYS LYS J . n 
J 2 76  ARG 76  76  76  ARG ARG J . n 
J 2 77  ILE 77  77  77  ILE ILE J . n 
J 2 78  GLU 78  78  78  GLU GLU J . n 
J 2 79  ASN 79  79  79  ASN ASN J . n 
J 2 80  LEU 80  80  80  LEU LEU J . n 
J 2 81  ASN 81  81  81  ASN ASN J . n 
J 2 82  LYS 82  82  82  LYS LYS J . n 
J 2 83  LYS 83  83  83  LYS LYS J . n 
J 2 84  VAL 84  84  84  VAL VAL J . n 
J 2 85  ASP 85  85  85  ASP ASP J . n 
J 2 86  ASP 86  86  86  ASP ASP J . n 
J 2 87  GLY 87  87  87  GLY GLY J . n 
J 2 88  PHE 88  88  88  PHE PHE J . n 
J 2 89  LEU 89  89  89  LEU LEU J . n 
J 2 90  ASP 90  90  90  ASP ASP J . n 
J 2 91  ILE 91  91  91  ILE ILE J . n 
J 2 92  TRP 92  92  92  TRP TRP J . n 
J 2 93  THR 93  93  93  THR THR J . n 
J 2 94  TYR 94  94  94  TYR TYR J . n 
J 2 95  ASN 95  95  95  ASN ASN J . n 
J 2 96  ALA 96  96  96  ALA ALA J . n 
J 2 97  GLU 97  97  97  GLU GLU J . n 
J 2 98  LEU 98  98  98  LEU LEU J . n 
J 2 99  LEU 99  99  99  LEU LEU J . n 
J 2 100 VAL 100 100 100 VAL VAL J . n 
J 2 101 LEU 101 101 101 LEU LEU J . n 
J 2 102 LEU 102 102 102 LEU LEU J . n 
J 2 103 GLU 103 103 103 GLU GLU J . n 
J 2 104 ASN 104 104 104 ASN ASN J . n 
J 2 105 GLU 105 105 105 GLU GLU J . n 
J 2 106 ARG 106 106 106 ARG ARG J . n 
J 2 107 THR 107 107 107 THR THR J . n 
J 2 108 LEU 108 108 108 LEU LEU J . n 
J 2 109 ASP 109 109 109 ASP ASP J . n 
J 2 110 TYR 110 110 110 TYR TYR J . n 
J 2 111 HIS 111 111 111 HIS HIS J . n 
J 2 112 ASP 112 112 112 ASP ASP J . n 
J 2 113 SER 113 113 113 SER SER J . n 
J 2 114 ASN 114 114 114 ASN ASN J . n 
J 2 115 VAL 115 115 115 VAL VAL J . n 
J 2 116 LYS 116 116 116 LYS LYS J . n 
J 2 117 ASN 117 117 117 ASN ASN J . n 
J 2 118 LEU 118 118 118 LEU LEU J . n 
J 2 119 TYR 119 119 119 TYR TYR J . n 
J 2 120 GLU 120 120 120 GLU GLU J . n 
J 2 121 LYS 121 121 121 LYS LYS J . n 
J 2 122 VAL 122 122 122 VAL VAL J . n 
J 2 123 ARG 123 123 123 ARG ARG J . n 
J 2 124 SER 124 124 124 SER SER J . n 
J 2 125 GLN 125 125 125 GLN GLN J . n 
J 2 126 LEU 126 126 126 LEU LEU J . n 
J 2 127 LYS 127 127 127 LYS LYS J . n 
J 2 128 ASN 128 128 128 ASN ASN J . n 
J 2 129 ASN 129 129 129 ASN ASN J . n 
J 2 130 ALA 130 130 130 ALA ALA J . n 
J 2 131 LYS 131 131 131 LYS LYS J . n 
J 2 132 GLU 132 132 132 GLU GLU J . n 
J 2 133 ILE 133 133 133 ILE ILE J . n 
J 2 134 GLY 134 134 134 GLY GLY J . n 
J 2 135 ASN 135 135 135 ASN ASN J . n 
J 2 136 GLY 136 136 136 GLY GLY J . n 
J 2 137 CYS 137 137 137 CYS CYS J . n 
J 2 138 PHE 138 138 138 PHE PHE J . n 
J 2 139 GLU 139 139 139 GLU GLU J . n 
J 2 140 PHE 140 140 140 PHE PHE J . n 
J 2 141 TYR 141 141 141 TYR TYR J . n 
J 2 142 HIS 142 142 142 HIS HIS J . n 
J 2 143 LYS 143 143 143 LYS LYS J . n 
J 2 144 CYS 144 144 144 CYS CYS J . n 
J 2 145 ASP 145 145 145 ASP ASP J . n 
J 2 146 ASN 146 146 146 ASN ASN J . n 
J 2 147 THR 147 147 147 THR THR J . n 
J 2 148 CYS 148 148 148 CYS CYS J . n 
J 2 149 MET 149 149 149 MET MET J . n 
J 2 150 GLU 150 150 150 GLU GLU J . n 
J 2 151 SER 151 151 151 SER SER J . n 
J 2 152 VAL 152 152 152 VAL VAL J . n 
J 2 153 LYS 153 153 153 LYS LYS J . n 
J 2 154 ASN 154 154 154 ASN ASN J . n 
J 2 155 GLY 155 155 155 GLY GLY J . n 
J 2 156 THR 156 156 156 THR THR J . n 
J 2 157 TYR 157 157 157 TYR TYR J . n 
J 2 158 ASP 158 158 158 ASP ASP J . n 
J 2 159 TYR 159 159 159 TYR TYR J . n 
J 2 160 PRO 160 160 160 PRO PRO J . n 
J 2 161 LYS 161 161 161 LYS LYS J . n 
J 2 162 TYR 162 162 162 TYR TYR J . n 
J 2 163 SER 163 163 ?   ?   ?   J . n 
J 2 164 GLU 164 164 ?   ?   ?   J . n 
J 2 165 GLU 165 165 ?   ?   ?   J . n 
J 2 166 ALA 166 166 ?   ?   ?   J . n 
J 2 167 LYS 167 167 ?   ?   ?   J . n 
J 2 168 LEU 168 168 ?   ?   ?   J . n 
J 2 169 ASN 169 169 ?   ?   ?   J . n 
J 2 170 ARG 170 170 ?   ?   ?   J . n 
J 2 171 GLU 171 171 ?   ?   ?   J . n 
J 2 172 GLU 172 172 ?   ?   ?   J . n 
J 2 173 ILE 173 173 ?   ?   ?   J . n 
J 2 174 ASP 174 174 ?   ?   ?   J . n 
J 2 175 GLY 175 175 ?   ?   ?   J . n 
J 2 176 VAL 176 176 ?   ?   ?   J . n 
J 2 177 ARG 177 177 ?   ?   ?   J . n 
J 2 178 LEU 178 178 ?   ?   ?   J . n 
J 2 179 VAL 179 179 ?   ?   ?   J . n 
J 2 180 PRO 180 180 ?   ?   ?   J . n 
J 2 181 ARG 181 181 ?   ?   ?   J . n 
K 1 1   ALA 1   1   ?   ?   ?   K . n 
K 1 2   ASP 2   2   ?   ?   ?   K . n 
K 1 3   LEU 3   3   ?   ?   ?   K . n 
K 1 4   GLY 4   4   ?   ?   ?   K . n 
K 1 5   SER 5   5   ?   ?   ?   K . n 
K 1 6   ARG 6   6   ?   ?   ?   K . n 
K 1 7   ASP 7   7   7   ASP ASP K . n 
K 1 8   THR 8   8   8   THR THR K . n 
K 1 9   LEU 9   9   9   LEU LEU K . n 
K 1 10  CYS 10  10  10  CYS CYS K . n 
K 1 11  ILE 11  11  11  ILE ILE K . n 
K 1 12  GLY 12  12  12  GLY GLY K . n 
K 1 13  TYR 13  13  13  TYR TYR K . n 
K 1 14  HIS 14  14  14  HIS HIS K . n 
K 1 15  ALA 15  15  15  ALA ALA K . n 
K 1 16  ASN 16  16  16  ASN ASN K . n 
K 1 17  ASN 17  17  17  ASN ASN K . n 
K 1 18  SER 18  18  18  SER SER K . n 
K 1 19  THR 19  19  19  THR THR K . n 
K 1 20  ASP 20  20  20  ASP ASP K . n 
K 1 21  THR 21  21  21  THR THR K . n 
K 1 22  VAL 22  22  22  VAL VAL K . n 
K 1 23  ASP 23  23  23  ASP ASP K . n 
K 1 24  THR 24  24  24  THR THR K . n 
K 1 25  VAL 25  25  25  VAL VAL K . n 
K 1 26  LEU 26  26  26  LEU LEU K . n 
K 1 27  GLU 27  27  27  GLU GLU K . n 
K 1 28  LYS 28  28  28  LYS LYS K . n 
K 1 29  ASN 29  29  29  ASN ASN K . n 
K 1 30  VAL 30  30  30  VAL VAL K . n 
K 1 31  THR 31  31  31  THR THR K . n 
K 1 32  VAL 32  32  32  VAL VAL K . n 
K 1 33  THR 33  33  33  THR THR K . n 
K 1 34  HIS 34  34  34  HIS HIS K . n 
K 1 35  SER 35  35  35  SER SER K . n 
K 1 36  VAL 36  36  36  VAL VAL K . n 
K 1 37  ASN 37  37  37  ASN ASN K . n 
K 1 38  LEU 38  38  38  LEU LEU K . n 
K 1 39  LEU 39  39  39  LEU LEU K . n 
K 1 40  GLU 40  40  40  GLU GLU K . n 
K 1 41  ASP 41  41  41  ASP ASP K . n 
K 1 42  LYS 42  42  42  LYS LYS K . n 
K 1 43  HIS 43  43  43  HIS HIS K . n 
K 1 44  ASN 44  44  44  ASN ASN K . n 
K 1 45  GLY 45  45  45  GLY GLY K . n 
K 1 46  LYS 46  46  46  LYS LYS K . n 
K 1 47  LEU 47  47  47  LEU LEU K . n 
K 1 48  CYS 48  48  48  CYS CYS K . n 
K 1 49  LYS 49  49  49  LYS LYS K . n 
K 1 50  LEU 50  50  50  LEU LEU K . n 
K 1 51  ARG 51  51  51  ARG ARG K . n 
K 1 52  GLY 52  52  52  GLY GLY K . n 
K 1 53  VAL 53  53  53  VAL VAL K . n 
K 1 54  ALA 54  54  54  ALA ALA K . n 
K 1 55  PRO 55  55  55  PRO PRO K . n 
K 1 56  LEU 56  56  56  LEU LEU K . n 
K 1 57  HIS 57  57  57  HIS HIS K . n 
K 1 58  LEU 58  58  58  LEU LEU K . n 
K 1 59  GLY 59  59  59  GLY GLY K . n 
K 1 60  LYS 60  60  60  LYS LYS K . n 
K 1 61  CYS 61  61  61  CYS CYS K . n 
K 1 62  ASN 62  62  62  ASN ASN K . n 
K 1 63  ILE 63  63  63  ILE ILE K . n 
K 1 64  ALA 64  64  64  ALA ALA K . n 
K 1 65  GLY 65  65  65  GLY GLY K . n 
K 1 66  TRP 66  66  66  TRP TRP K . n 
K 1 67  ILE 67  67  67  ILE ILE K . n 
K 1 68  LEU 68  68  68  LEU LEU K . n 
K 1 69  GLY 69  69  69  GLY GLY K . n 
K 1 70  ASN 70  70  70  ASN ASN K . n 
K 1 71  PRO 71  71  71  PRO PRO K . n 
K 1 72  GLU 72  72  72  GLU GLU K . n 
K 1 73  CYS 73  73  73  CYS CYS K . n 
K 1 74  GLU 74  74  74  GLU GLU K . n 
K 1 75  SER 75  75  75  SER SER K . n 
K 1 76  LEU 76  76  76  LEU LEU K . n 
K 1 77  SER 77  77  77  SER SER K . n 
K 1 78  THR 78  78  78  THR THR K . n 
K 1 79  ALA 79  79  79  ALA ALA K . n 
K 1 80  SER 80  80  80  SER SER K . n 
K 1 81  SER 81  81  81  SER SER K . n 
K 1 82  TRP 82  82  82  TRP TRP K . n 
K 1 83  SER 83  83  83  SER SER K . n 
K 1 84  TYR 84  84  84  TYR TYR K . n 
K 1 85  ILE 85  85  85  ILE ILE K . n 
K 1 86  VAL 86  86  86  VAL VAL K . n 
K 1 87  GLU 87  87  87  GLU GLU K . n 
K 1 88  THR 88  88  88  THR THR K . n 
K 1 89  PRO 89  89  89  PRO PRO K . n 
K 1 90  SER 90  90  90  SER SER K . n 
K 1 91  SER 91  91  91  SER SER K . n 
K 1 92  ASP 92  92  92  ASP ASP K . n 
K 1 93  ASN 93  93  93  ASN ASN K . n 
K 1 94  GLY 94  94  94  GLY GLY K . n 
K 1 95  THR 95  95  95  THR THR K . n 
K 1 96  CYS 96  96  96  CYS CYS K . n 
K 1 97  TYR 97  97  97  TYR TYR K . n 
K 1 98  PRO 98  98  98  PRO PRO K . n 
K 1 99  GLY 99  99  99  GLY GLY K . n 
K 1 100 ASP 100 100 100 ASP ASP K . n 
K 1 101 PHE 101 101 101 PHE PHE K . n 
K 1 102 ILE 102 102 102 ILE ILE K . n 
K 1 103 ASP 103 103 103 ASP ASP K . n 
K 1 104 TYR 104 104 104 TYR TYR K . n 
K 1 105 GLU 105 105 105 GLU GLU K . n 
K 1 106 GLU 106 106 106 GLU GLU K . n 
K 1 107 LEU 107 107 107 LEU LEU K . n 
K 1 108 ARG 108 108 108 ARG ARG K . n 
K 1 109 GLU 109 109 109 GLU GLU K . n 
K 1 110 GLN 110 110 110 GLN GLN K . n 
K 1 111 LEU 111 111 111 LEU LEU K . n 
K 1 112 SER 112 112 112 SER SER K . n 
K 1 113 SER 113 113 113 SER SER K . n 
K 1 114 VAL 114 114 114 VAL VAL K . n 
K 1 115 SER 115 115 115 SER SER K . n 
K 1 116 SER 116 116 116 SER SER K . n 
K 1 117 PHE 117 117 117 PHE PHE K . n 
K 1 118 GLU 118 118 118 GLU GLU K . n 
K 1 119 ARG 119 119 119 ARG ARG K . n 
K 1 120 PHE 120 120 120 PHE PHE K . n 
K 1 121 GLU 121 121 121 GLU GLU K . n 
K 1 122 ILE 122 122 122 ILE ILE K . n 
K 1 123 PHE 123 123 123 PHE PHE K . n 
K 1 124 PRO 124 124 124 PRO PRO K . n 
K 1 125 LYS 125 125 125 LYS LYS K . n 
K 1 126 THR 126 126 126 THR THR K . n 
K 1 127 SER 127 127 127 SER SER K . n 
K 1 128 SER 128 128 128 SER SER K . n 
K 1 129 TRP 129 129 129 TRP TRP K . n 
K 1 130 PRO 130 130 130 PRO PRO K . n 
K 1 131 ASN 131 131 131 ASN ASN K . n 
K 1 132 HIS 132 132 132 HIS HIS K . n 
K 1 133 ASP 133 133 133 ASP ASP K . n 
K 1 134 SER 134 134 134 SER SER K . n 
K 1 135 ASN 135 135 135 ASN ASN K . n 
K 1 136 LYS 136 136 136 LYS LYS K . n 
K 1 137 GLY 137 137 137 GLY GLY K . n 
K 1 138 VAL 138 138 138 VAL VAL K . n 
K 1 139 THR 139 139 139 THR THR K . n 
K 1 140 ALA 140 140 140 ALA ALA K . n 
K 1 141 ALA 141 141 141 ALA ALA K . n 
K 1 142 CYS 142 142 142 CYS CYS K . n 
K 1 143 PRO 143 143 143 PRO PRO K . n 
K 1 144 HIS 144 144 144 HIS HIS K . n 
K 1 145 ALA 145 145 145 ALA ALA K . n 
K 1 146 GLY 146 146 146 GLY GLY K . n 
K 1 147 ALA 147 147 147 ALA ALA K . n 
K 1 148 LYS 148 148 148 LYS LYS K . n 
K 1 149 SER 149 149 149 SER SER K . n 
K 1 150 PHE 150 150 150 PHE PHE K . n 
K 1 151 TYR 151 151 151 TYR TYR K . n 
K 1 152 LYS 152 152 152 LYS LYS K . n 
K 1 153 ASN 153 153 153 ASN ASN K . n 
K 1 154 LEU 154 154 154 LEU LEU K . n 
K 1 155 ILE 155 155 155 ILE ILE K . n 
K 1 156 TRP 156 156 156 TRP TRP K . n 
K 1 157 LEU 157 157 157 LEU LEU K . n 
K 1 158 VAL 158 158 158 VAL VAL K . n 
K 1 159 LYS 159 159 159 LYS LYS K . n 
K 1 160 LYS 160 160 160 LYS LYS K . n 
K 1 161 GLY 161 161 161 GLY GLY K . n 
K 1 162 ASN 162 162 162 ASN ASN K . n 
K 1 163 SER 163 163 163 SER SER K . n 
K 1 164 TYR 164 164 164 TYR TYR K . n 
K 1 165 PRO 165 165 165 PRO PRO K . n 
K 1 166 LYS 166 166 166 LYS LYS K . n 
K 1 167 LEU 167 167 167 LEU LEU K . n 
K 1 168 SER 168 168 168 SER SER K . n 
K 1 169 LYS 169 169 169 LYS LYS K . n 
K 1 170 SER 170 170 170 SER SER K . n 
K 1 171 TYR 171 171 171 TYR TYR K . n 
K 1 172 ILE 172 172 172 ILE ILE K . n 
K 1 173 ASN 173 173 173 ASN ASN K . n 
K 1 174 ASP 174 174 174 ASP ASP K . n 
K 1 175 LYS 175 175 175 LYS LYS K . n 
K 1 176 GLY 176 176 176 GLY GLY K . n 
K 1 177 LYS 177 177 177 LYS LYS K . n 
K 1 178 GLU 178 178 178 GLU GLU K . n 
K 1 179 VAL 179 179 179 VAL VAL K . n 
K 1 180 LEU 180 180 180 LEU LEU K . n 
K 1 181 VAL 181 181 181 VAL VAL K . n 
K 1 182 LEU 182 182 182 LEU LEU K . n 
K 1 183 TRP 183 183 183 TRP TRP K . n 
K 1 184 GLY 184 184 184 GLY GLY K . n 
K 1 185 ILE 185 185 185 ILE ILE K . n 
K 1 186 HIS 186 186 186 HIS HIS K . n 
K 1 187 HIS 187 187 187 HIS HIS K . n 
K 1 188 PRO 188 188 188 PRO PRO K . n 
K 1 189 SER 189 189 189 SER SER K . n 
K 1 190 THR 190 190 190 THR THR K . n 
K 1 191 SER 191 191 191 SER SER K . n 
K 1 192 ALA 192 192 192 ALA ALA K . n 
K 1 193 ASP 193 193 193 ASP ASP K . n 
K 1 194 GLN 194 194 194 GLN GLN K . n 
K 1 195 GLN 195 195 195 GLN GLN K . n 
K 1 196 SER 196 196 196 SER SER K . n 
K 1 197 LEU 197 197 197 LEU LEU K . n 
K 1 198 TYR 198 198 198 TYR TYR K . n 
K 1 199 GLN 199 199 199 GLN GLN K . n 
K 1 200 ASN 200 200 200 ASN ASN K . n 
K 1 201 ALA 201 201 201 ALA ALA K . n 
K 1 202 ASP 202 202 202 ASP ASP K . n 
K 1 203 THR 203 203 203 THR THR K . n 
K 1 204 TYR 204 204 204 TYR TYR K . n 
K 1 205 VAL 205 205 205 VAL VAL K . n 
K 1 206 PHE 206 206 206 PHE PHE K . n 
K 1 207 VAL 207 207 207 VAL VAL K . n 
K 1 208 GLY 208 208 208 GLY GLY K . n 
K 1 209 SER 209 209 209 SER SER K . n 
K 1 210 SER 210 210 210 SER SER K . n 
K 1 211 ARG 211 211 211 ARG ARG K . n 
K 1 212 TYR 212 212 212 TYR TYR K . n 
K 1 213 SER 213 213 213 SER SER K . n 
K 1 214 LYS 214 214 214 LYS LYS K . n 
K 1 215 LYS 215 215 215 LYS LYS K . n 
K 1 216 PHE 216 216 216 PHE PHE K . n 
K 1 217 LYS 217 217 217 LYS LYS K . n 
K 1 218 PRO 218 218 218 PRO PRO K . n 
K 1 219 GLU 219 219 219 GLU GLU K . n 
K 1 220 ILE 220 220 220 ILE ILE K . n 
K 1 221 ALA 221 221 221 ALA ALA K . n 
K 1 222 ILE 222 222 222 ILE ILE K . n 
K 1 223 ARG 223 223 223 ARG ARG K . n 
K 1 224 PRO 224 224 224 PRO PRO K . n 
K 1 225 LYS 225 225 225 LYS LYS K . n 
K 1 226 VAL 226 226 226 VAL VAL K . n 
K 1 227 ARG 227 227 227 ARG ARG K . n 
K 1 228 ASP 228 228 228 ASP ASP K . n 
K 1 229 GLN 229 229 229 GLN GLN K . n 
K 1 230 GLU 230 230 230 GLU GLU K . n 
K 1 231 GLY 231 231 231 GLY GLY K . n 
K 1 232 ARG 232 232 232 ARG ARG K . n 
K 1 233 MET 233 233 233 MET MET K . n 
K 1 234 ASN 234 234 234 ASN ASN K . n 
K 1 235 TYR 235 235 235 TYR TYR K . n 
K 1 236 TYR 236 236 236 TYR TYR K . n 
K 1 237 TRP 237 237 237 TRP TRP K . n 
K 1 238 THR 238 238 238 THR THR K . n 
K 1 239 LEU 239 239 239 LEU LEU K . n 
K 1 240 VAL 240 240 240 VAL VAL K . n 
K 1 241 GLU 241 241 241 GLU GLU K . n 
K 1 242 PRO 242 242 242 PRO PRO K . n 
K 1 243 GLY 243 243 243 GLY GLY K . n 
K 1 244 ASP 244 244 244 ASP ASP K . n 
K 1 245 LYS 245 245 245 LYS LYS K . n 
K 1 246 ILE 246 246 246 ILE ILE K . n 
K 1 247 THR 247 247 247 THR THR K . n 
K 1 248 PHE 248 248 248 PHE PHE K . n 
K 1 249 GLU 249 249 249 GLU GLU K . n 
K 1 250 ALA 250 250 250 ALA ALA K . n 
K 1 251 THR 251 251 251 THR THR K . n 
K 1 252 GLY 252 252 252 GLY GLY K . n 
K 1 253 ASN 253 253 253 ASN ASN K . n 
K 1 254 LEU 254 254 254 LEU LEU K . n 
K 1 255 VAL 255 255 255 VAL VAL K . n 
K 1 256 VAL 256 256 256 VAL VAL K . n 
K 1 257 PRO 257 257 257 PRO PRO K . n 
K 1 258 ARG 258 258 258 ARG ARG K . n 
K 1 259 TYR 259 259 259 TYR TYR K . n 
K 1 260 ALA 260 260 260 ALA ALA K . n 
K 1 261 PHE 261 261 261 PHE PHE K . n 
K 1 262 ALA 262 262 262 ALA ALA K . n 
K 1 263 MET 263 263 263 MET MET K . n 
K 1 264 GLU 264 264 264 GLU GLU K . n 
K 1 265 ARG 265 265 265 ARG ARG K . n 
K 1 266 ASN 266 266 266 ASN ASN K . n 
K 1 267 ALA 267 267 267 ALA ALA K . n 
K 1 268 GLY 268 268 268 GLY GLY K . n 
K 1 269 SER 269 269 269 SER SER K . n 
K 1 270 GLY 270 270 270 GLY GLY K . n 
K 1 271 ILE 271 271 271 ILE ILE K . n 
K 1 272 ILE 272 272 272 ILE ILE K . n 
K 1 273 ILE 273 273 273 ILE ILE K . n 
K 1 274 SER 274 274 274 SER SER K . n 
K 1 275 ASP 275 275 275 ASP ASP K . n 
K 1 276 THR 276 276 276 THR THR K . n 
K 1 277 PRO 277 277 277 PRO PRO K . n 
K 1 278 VAL 278 278 278 VAL VAL K . n 
K 1 279 HIS 279 279 279 HIS HIS K . n 
K 1 280 ASP 280 280 280 ASP ASP K . n 
K 1 281 CYS 281 281 281 CYS CYS K . n 
K 1 282 ASN 282 282 282 ASN ASN K . n 
K 1 283 THR 283 283 283 THR THR K . n 
K 1 284 THR 284 284 284 THR THR K . n 
K 1 285 CYS 285 285 285 CYS CYS K . n 
K 1 286 GLN 286 286 286 GLN GLN K . n 
K 1 287 THR 287 287 287 THR THR K . n 
K 1 288 PRO 288 288 288 PRO PRO K . n 
K 1 289 LYS 289 289 289 LYS LYS K . n 
K 1 290 GLY 290 290 290 GLY GLY K . n 
K 1 291 ALA 291 291 291 ALA ALA K . n 
K 1 292 ILE 292 292 292 ILE ILE K . n 
K 1 293 ASN 293 293 293 ASN ASN K . n 
K 1 294 THR 294 294 294 THR THR K . n 
K 1 295 SER 295 295 295 SER SER K . n 
K 1 296 LEU 296 296 296 LEU LEU K . n 
K 1 297 PRO 297 297 297 PRO PRO K . n 
K 1 298 PHE 298 298 298 PHE PHE K . n 
K 1 299 GLN 299 299 299 GLN GLN K . n 
K 1 300 ASN 300 300 300 ASN ASN K . n 
K 1 301 ILE 301 301 301 ILE ILE K . n 
K 1 302 HIS 302 302 302 HIS HIS K . n 
K 1 303 PRO 303 303 303 PRO PRO K . n 
K 1 304 ILE 304 304 304 ILE ILE K . n 
K 1 305 THR 305 305 305 THR THR K . n 
K 1 306 ILE 306 306 306 ILE ILE K . n 
K 1 307 GLY 307 307 307 GLY GLY K . n 
K 1 308 LYS 308 308 308 LYS LYS K . n 
K 1 309 CYS 309 309 309 CYS CYS K . n 
K 1 310 PRO 310 310 310 PRO PRO K . n 
K 1 311 LYS 311 311 311 LYS LYS K . n 
K 1 312 TYR 312 312 312 TYR TYR K . n 
K 1 313 VAL 313 313 313 VAL VAL K . n 
K 1 314 LYS 314 314 314 LYS LYS K . n 
K 1 315 SER 315 315 315 SER SER K . n 
K 1 316 THR 316 316 316 THR THR K . n 
K 1 317 LYS 317 317 317 LYS LYS K . n 
K 1 318 LEU 318 318 318 LEU LEU K . n 
K 1 319 ARG 319 319 319 ARG ARG K . n 
K 1 320 LEU 320 320 320 LEU LEU K . n 
K 1 321 ALA 321 321 321 ALA ALA K . n 
K 1 322 THR 322 322 322 THR THR K . n 
K 1 323 GLY 323 323 323 GLY GLY K . n 
K 1 324 LEU 324 324 324 LEU LEU K . n 
K 1 325 ARG 325 325 325 ARG ARG K . n 
K 1 326 ASN 326 326 326 ASN ASN K . n 
K 1 327 ILE 327 327 327 ILE ILE K . n 
K 1 328 PRO 328 328 ?   ?   ?   K . n 
K 1 329 SER 329 329 ?   ?   ?   K . n 
K 1 330 ILE 330 330 ?   ?   ?   K . n 
K 1 331 GLN 331 331 ?   ?   ?   K . n 
K 1 332 SER 332 332 ?   ?   ?   K . n 
K 1 333 ARG 333 333 ?   ?   ?   K . n 
L 2 1   GLY 1   1   ?   ?   ?   L . n 
L 2 2   LEU 2   2   2   LEU LEU L . n 
L 2 3   PHE 3   3   3   PHE PHE L . n 
L 2 4   GLY 4   4   4   GLY GLY L . n 
L 2 5   ALA 5   5   5   ALA ALA L . n 
L 2 6   ILE 6   6   6   ILE ILE L . n 
L 2 7   ALA 7   7   7   ALA ALA L . n 
L 2 8   GLY 8   8   8   GLY GLY L . n 
L 2 9   PHE 9   9   9   PHE PHE L . n 
L 2 10  ILE 10  10  10  ILE ILE L . n 
L 2 11  GLU 11  11  11  GLU GLU L . n 
L 2 12  GLY 12  12  12  GLY GLY L . n 
L 2 13  GLY 13  13  13  GLY GLY L . n 
L 2 14  TRP 14  14  14  TRP TRP L . n 
L 2 15  THR 15  15  15  THR THR L . n 
L 2 16  GLY 16  16  16  GLY GLY L . n 
L 2 17  MET 17  17  17  MET MET L . n 
L 2 18  VAL 18  18  18  VAL VAL L . n 
L 2 19  ASP 19  19  19  ASP ASP L . n 
L 2 20  GLY 20  20  20  GLY GLY L . n 
L 2 21  TRP 21  21  21  TRP TRP L . n 
L 2 22  TYR 22  22  22  TYR TYR L . n 
L 2 23  GLY 23  23  23  GLY GLY L . n 
L 2 24  TYR 24  24  24  TYR TYR L . n 
L 2 25  HIS 25  25  25  HIS HIS L . n 
L 2 26  HIS 26  26  26  HIS HIS L . n 
L 2 27  GLN 27  27  27  GLN GLN L . n 
L 2 28  ASN 28  28  28  ASN ASN L . n 
L 2 29  GLU 29  29  29  GLU GLU L . n 
L 2 30  GLN 30  30  30  GLN GLN L . n 
L 2 31  GLY 31  31  31  GLY GLY L . n 
L 2 32  SER 32  32  32  SER SER L . n 
L 2 33  GLY 33  33  33  GLY GLY L . n 
L 2 34  TYR 34  34  34  TYR TYR L . n 
L 2 35  ALA 35  35  35  ALA ALA L . n 
L 2 36  ALA 36  36  36  ALA ALA L . n 
L 2 37  ASP 37  37  37  ASP ASP L . n 
L 2 38  LEU 38  38  38  LEU LEU L . n 
L 2 39  LYS 39  39  39  LYS LYS L . n 
L 2 40  SER 40  40  40  SER SER L . n 
L 2 41  THR 41  41  41  THR THR L . n 
L 2 42  GLN 42  42  42  GLN GLN L . n 
L 2 43  ASN 43  43  43  ASN ASN L . n 
L 2 44  ALA 44  44  44  ALA ALA L . n 
L 2 45  ILE 45  45  45  ILE ILE L . n 
L 2 46  ASP 46  46  46  ASP ASP L . n 
L 2 47  GLU 47  47  47  GLU GLU L . n 
L 2 48  ILE 48  48  48  ILE ILE L . n 
L 2 49  THR 49  49  49  THR THR L . n 
L 2 50  ASN 50  50  50  ASN ASN L . n 
L 2 51  LYS 51  51  51  LYS LYS L . n 
L 2 52  VAL 52  52  52  VAL VAL L . n 
L 2 53  ASN 53  53  53  ASN ASN L . n 
L 2 54  SER 54  54  54  SER SER L . n 
L 2 55  VAL 55  55  55  VAL VAL L . n 
L 2 56  ILE 56  56  56  ILE ILE L . n 
L 2 57  GLU 57  57  57  GLU GLU L . n 
L 2 58  LYS 58  58  58  LYS LYS L . n 
L 2 59  MET 59  59  59  MET MET L . n 
L 2 60  ASN 60  60  60  ASN ASN L . n 
L 2 61  THR 61  61  61  THR THR L . n 
L 2 62  GLN 62  62  62  GLN GLN L . n 
L 2 63  PHE 63  63  63  PHE PHE L . n 
L 2 64  THR 64  64  64  THR THR L . n 
L 2 65  ALA 65  65  65  ALA ALA L . n 
L 2 66  VAL 66  66  66  VAL VAL L . n 
L 2 67  GLY 67  67  67  GLY GLY L . n 
L 2 68  LYS 68  68  68  LYS LYS L . n 
L 2 69  GLU 69  69  69  GLU GLU L . n 
L 2 70  PHE 70  70  70  PHE PHE L . n 
L 2 71  ASN 71  71  71  ASN ASN L . n 
L 2 72  HIS 72  72  72  HIS HIS L . n 
L 2 73  LEU 73  73  73  LEU LEU L . n 
L 2 74  GLU 74  74  74  GLU GLU L . n 
L 2 75  LYS 75  75  75  LYS LYS L . n 
L 2 76  ARG 76  76  76  ARG ARG L . n 
L 2 77  ILE 77  77  77  ILE ILE L . n 
L 2 78  GLU 78  78  78  GLU GLU L . n 
L 2 79  ASN 79  79  79  ASN ASN L . n 
L 2 80  LEU 80  80  80  LEU LEU L . n 
L 2 81  ASN 81  81  81  ASN ASN L . n 
L 2 82  LYS 82  82  82  LYS LYS L . n 
L 2 83  LYS 83  83  83  LYS LYS L . n 
L 2 84  VAL 84  84  84  VAL VAL L . n 
L 2 85  ASP 85  85  85  ASP ASP L . n 
L 2 86  ASP 86  86  86  ASP ASP L . n 
L 2 87  GLY 87  87  87  GLY GLY L . n 
L 2 88  PHE 88  88  88  PHE PHE L . n 
L 2 89  LEU 89  89  89  LEU LEU L . n 
L 2 90  ASP 90  90  90  ASP ASP L . n 
L 2 91  ILE 91  91  91  ILE ILE L . n 
L 2 92  TRP 92  92  92  TRP TRP L . n 
L 2 93  THR 93  93  93  THR THR L . n 
L 2 94  TYR 94  94  94  TYR TYR L . n 
L 2 95  ASN 95  95  95  ASN ASN L . n 
L 2 96  ALA 96  96  96  ALA ALA L . n 
L 2 97  GLU 97  97  97  GLU GLU L . n 
L 2 98  LEU 98  98  98  LEU LEU L . n 
L 2 99  LEU 99  99  99  LEU LEU L . n 
L 2 100 VAL 100 100 100 VAL VAL L . n 
L 2 101 LEU 101 101 101 LEU LEU L . n 
L 2 102 LEU 102 102 102 LEU LEU L . n 
L 2 103 GLU 103 103 103 GLU GLU L . n 
L 2 104 ASN 104 104 104 ASN ASN L . n 
L 2 105 GLU 105 105 105 GLU GLU L . n 
L 2 106 ARG 106 106 106 ARG ARG L . n 
L 2 107 THR 107 107 107 THR THR L . n 
L 2 108 LEU 108 108 108 LEU LEU L . n 
L 2 109 ASP 109 109 109 ASP ASP L . n 
L 2 110 TYR 110 110 110 TYR TYR L . n 
L 2 111 HIS 111 111 111 HIS HIS L . n 
L 2 112 ASP 112 112 112 ASP ASP L . n 
L 2 113 SER 113 113 113 SER SER L . n 
L 2 114 ASN 114 114 114 ASN ASN L . n 
L 2 115 VAL 115 115 115 VAL VAL L . n 
L 2 116 LYS 116 116 116 LYS LYS L . n 
L 2 117 ASN 117 117 117 ASN ASN L . n 
L 2 118 LEU 118 118 118 LEU LEU L . n 
L 2 119 TYR 119 119 119 TYR TYR L . n 
L 2 120 GLU 120 120 120 GLU GLU L . n 
L 2 121 LYS 121 121 121 LYS LYS L . n 
L 2 122 VAL 122 122 122 VAL VAL L . n 
L 2 123 ARG 123 123 123 ARG ARG L . n 
L 2 124 SER 124 124 124 SER SER L . n 
L 2 125 GLN 125 125 125 GLN GLN L . n 
L 2 126 LEU 126 126 126 LEU LEU L . n 
L 2 127 LYS 127 127 127 LYS LYS L . n 
L 2 128 ASN 128 128 128 ASN ASN L . n 
L 2 129 ASN 129 129 129 ASN ASN L . n 
L 2 130 ALA 130 130 130 ALA ALA L . n 
L 2 131 LYS 131 131 131 LYS LYS L . n 
L 2 132 GLU 132 132 132 GLU GLU L . n 
L 2 133 ILE 133 133 133 ILE ILE L . n 
L 2 134 GLY 134 134 134 GLY GLY L . n 
L 2 135 ASN 135 135 135 ASN ASN L . n 
L 2 136 GLY 136 136 136 GLY GLY L . n 
L 2 137 CYS 137 137 137 CYS CYS L . n 
L 2 138 PHE 138 138 138 PHE PHE L . n 
L 2 139 GLU 139 139 139 GLU GLU L . n 
L 2 140 PHE 140 140 140 PHE PHE L . n 
L 2 141 TYR 141 141 141 TYR TYR L . n 
L 2 142 HIS 142 142 142 HIS HIS L . n 
L 2 143 LYS 143 143 143 LYS LYS L . n 
L 2 144 CYS 144 144 144 CYS CYS L . n 
L 2 145 ASP 145 145 145 ASP ASP L . n 
L 2 146 ASN 146 146 146 ASN ASN L . n 
L 2 147 THR 147 147 147 THR THR L . n 
L 2 148 CYS 148 148 148 CYS CYS L . n 
L 2 149 MET 149 149 149 MET MET L . n 
L 2 150 GLU 150 150 150 GLU GLU L . n 
L 2 151 SER 151 151 151 SER SER L . n 
L 2 152 VAL 152 152 152 VAL VAL L . n 
L 2 153 LYS 153 153 153 LYS LYS L . n 
L 2 154 ASN 154 154 154 ASN ASN L . n 
L 2 155 GLY 155 155 155 GLY GLY L . n 
L 2 156 THR 156 156 156 THR THR L . n 
L 2 157 TYR 157 157 157 TYR TYR L . n 
L 2 158 ASP 158 158 158 ASP ASP L . n 
L 2 159 TYR 159 159 159 TYR TYR L . n 
L 2 160 PRO 160 160 160 PRO PRO L . n 
L 2 161 LYS 161 161 161 LYS LYS L . n 
L 2 162 TYR 162 162 162 TYR TYR L . n 
L 2 163 SER 163 163 ?   ?   ?   L . n 
L 2 164 GLU 164 164 ?   ?   ?   L . n 
L 2 165 GLU 165 165 ?   ?   ?   L . n 
L 2 166 ALA 166 166 ?   ?   ?   L . n 
L 2 167 LYS 167 167 ?   ?   ?   L . n 
L 2 168 LEU 168 168 ?   ?   ?   L . n 
L 2 169 ASN 169 169 ?   ?   ?   L . n 
L 2 170 ARG 170 170 ?   ?   ?   L . n 
L 2 171 GLU 171 171 ?   ?   ?   L . n 
L 2 172 GLU 172 172 ?   ?   ?   L . n 
L 2 173 ILE 173 173 ?   ?   ?   L . n 
L 2 174 ASP 174 174 ?   ?   ?   L . n 
L 2 175 GLY 175 175 ?   ?   ?   L . n 
L 2 176 VAL 176 176 ?   ?   ?   L . n 
L 2 177 ARG 177 177 ?   ?   ?   L . n 
L 2 178 LEU 178 178 ?   ?   ?   L . n 
L 2 179 VAL 179 179 ?   ?   ?   L . n 
L 2 180 PRO 180 180 ?   ?   ?   L . n 
L 2 181 ARG 181 181 ?   ?   ?   L . n 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1  G ASN 282 G ASN 282 ? ASN 'GLYCOSYLATION SITE' 
2  C ASN 17  C ASN 17  ? ASN 'GLYCOSYLATION SITE' 
3  E ASN 282 E ASN 282 ? ASN 'GLYCOSYLATION SITE' 
4  A ASN 29  A ASN 29  ? ASN 'GLYCOSYLATION SITE' 
5  K ASN 29  K ASN 29  ? ASN 'GLYCOSYLATION SITE' 
6  G ASN 17  G ASN 17  ? ASN 'GLYCOSYLATION SITE' 
7  F ASN 154 F ASN 154 ? ASN 'GLYCOSYLATION SITE' 
8  A ASN 282 A ASN 282 ? ASN 'GLYCOSYLATION SITE' 
9  A ASN 293 A ASN 293 ? ASN 'GLYCOSYLATION SITE' 
10 E ASN 93  E ASN 93  ? ASN 'GLYCOSYLATION SITE' 
11 G ASN 29  G ASN 29  ? ASN 'GLYCOSYLATION SITE' 
12 I ASN 93  I ASN 93  ? ASN 'GLYCOSYLATION SITE' 
13 K ASN 282 K ASN 282 ? ASN 'GLYCOSYLATION SITE' 
14 L ASN 154 L ASN 154 ? ASN 'GLYCOSYLATION SITE' 
15 K ASN 17  K ASN 17  ? ASN 'GLYCOSYLATION SITE' 
16 A ASN 93  A ASN 93  ? ASN 'GLYCOSYLATION SITE' 
17 C ASN 93  C ASN 93  ? ASN 'GLYCOSYLATION SITE' 
18 K ASN 293 K ASN 293 ? ASN 'GLYCOSYLATION SITE' 
19 C ASN 282 C ASN 282 ? ASN 'GLYCOSYLATION SITE' 
20 C ASN 29  C ASN 29  ? ASN 'GLYCOSYLATION SITE' 
21 I ASN 29  I ASN 29  ? ASN 'GLYCOSYLATION SITE' 
22 E ASN 293 E ASN 293 ? ASN 'GLYCOSYLATION SITE' 
23 E ASN 17  E ASN 17  ? ASN 'GLYCOSYLATION SITE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
3 author_and_software_defined_assembly PISA dimeric 2 
4 author_and_software_defined_assembly PISA dimeric 2 
5 author_and_software_defined_assembly PISA dimeric 2 
6 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,M,N,O,P,Q,R,SA,TA      
2 1 C,D,S,T,U,V,W,X,Y,UA,VA    
3 1 E,F,Z,AA,BA,CA,DA,EA,WA,XA 
4 1 G,H,FA,GA,HA,YA,ZA         
5 1 I,J,IA,JA,KA,LA,MA,AB,BB   
6 1 K,L,NA,OA,PA,QA,RA,CB,DB   
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5330  ? 
1 MORE         -41   ? 
1 'SSA (A^2)'  23620 ? 
2 'ABSA (A^2)' 5350  ? 
2 MORE         -41   ? 
2 'SSA (A^2)'  23650 ? 
3 'ABSA (A^2)' 5260  ? 
3 MORE         -42   ? 
3 'SSA (A^2)'  23700 ? 
4 'ABSA (A^2)' 5220  ? 
4 MORE         -39   ? 
4 'SSA (A^2)'  23530 ? 
5 'ABSA (A^2)' 5340  ? 
5 MORE         -41   ? 
5 'SSA (A^2)'  23430 ? 
6 'ABSA (A^2)' 5190  ? 
6 MORE         -42   ? 
6 'SSA (A^2)'  23650 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2010-08-04 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2012-06-27 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Database references'       
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -20.2272 
_pdbx_refine_tls.origin_y         -28.1217 
_pdbx_refine_tls.origin_z         -32.6646 
_pdbx_refine_tls.T[1][1]          0.1288 
_pdbx_refine_tls.T[2][2]          0.1607 
_pdbx_refine_tls.T[3][3]          0.1165 
_pdbx_refine_tls.T[1][2]          0.0127 
_pdbx_refine_tls.T[1][3]          -0.0565 
_pdbx_refine_tls.T[2][3]          0.0090 
_pdbx_refine_tls.L[1][1]          0.2871 
_pdbx_refine_tls.L[2][2]          0.2431 
_pdbx_refine_tls.L[3][3]          0.1527 
_pdbx_refine_tls.L[1][2]          0.1286 
_pdbx_refine_tls.L[1][3]          -0.1928 
_pdbx_refine_tls.L[2][3]          -0.0709 
_pdbx_refine_tls.S[1][1]          0.0345 
_pdbx_refine_tls.S[2][2]          -0.0623 
_pdbx_refine_tls.S[3][3]          -0.0000 
_pdbx_refine_tls.S[1][2]          -0.0095 
_pdbx_refine_tls.S[1][3]          -0.0120 
_pdbx_refine_tls.S[2][3]          -0.1407 
_pdbx_refine_tls.S[2][1]          0.0208 
_pdbx_refine_tls.S[3][1]          -0.0011 
_pdbx_refine_tls.S[3][2]          -0.0542 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1  1 A 7 A 370 ALL ? ? ? ? ? 
'X-RAY DIFFRACTION' 2  1 B 1 B 307 ALL ? ? ? ? ? 
'X-RAY DIFFRACTION' 3  1 C 7 C 371 ALL ? ? ? ? ? 
'X-RAY DIFFRACTION' 4  1 D 1 D 265 ALL ? ? ? ? ? 
'X-RAY DIFFRACTION' 5  1 E 7 E 364 ALL ? ? ? ? ? 
'X-RAY DIFFRACTION' 6  1 F 2 F 284 ALL ? ? ? ? ? 
'X-RAY DIFFRACTION' 7  1 G 7 G 378 ALL ? ? ? ? ? 
'X-RAY DIFFRACTION' 8  1 H 1 H 277 ALL ? ? ? ? ? 
'X-RAY DIFFRACTION' 9  1 I 7 I 371 ALL ? ? ? ? ? 
'X-RAY DIFFRACTION' 10 1 J 1 J 319 ALL ? ? ? ? ? 
'X-RAY DIFFRACTION' 11 1 K 7 K 369 ALL ? ? ? ? ? 
'X-RAY DIFFRACTION' 12 1 L 2 L 279 ALL ? ? ? ? ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
MAR345dtb 'data collection' .                        ? 1 
PHASER    phasing           .                        ? 2 
PHENIX    refinement        '(PHENIX.REFINE: 1.5_2)' ? 3 
HKL-2000  'data reduction'  .                        ? 4 
SCALEPACK 'data scaling'    .                        ? 5 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 ND2 H ASN 154 ? ? O   H HOH 182 ? ? 1.37 
2  1 OD1 K ASP 280 ? ? O7  A NAG 603 ? ? 1.65 
3  1 OD1 C ASN 282 ? ? O7  C NAG 607 ? ? 1.67 
4  1 O   E ALA 141 ? ? NH1 E ARG 227 ? ? 2.00 
5  1 CG  A ASN 282 ? ? C1  A NAG 604 ? ? 2.06 
6  1 O   E THR 88  ? ? OG  E SER 91  ? ? 2.06 
7  1 CG  C ASN 282 ? ? O7  C NAG 607 ? ? 2.09 
8  1 O   K SER 83  ? ? OG  K SER 269 ? ? 2.09 
9  1 SG  K CYS 10  ? ? CB  L CYS 137 ? ? 2.10 
10 1 O   A THR 31  ? ? O   A HOH 338 ? ? 2.10 
11 1 O   E LEU 50  ? ? O   E THR 283 ? ? 2.11 
12 1 ND2 K ASN 293 ? ? O5  K NAG 604 ? ? 2.11 
13 1 ND2 C ASN 282 ? ? O5  C NAG 607 ? ? 2.14 
14 1 OE2 I GLU 106 ? ? O   I HOH 341 ? ? 2.14 
15 1 CG  H ASN 154 ? ? O   H HOH 182 ? ? 2.15 
16 1 ND2 E ASN 93  ? ? O5  E NAG 602 ? ? 2.15 
17 1 O   B ASN 104 ? ? O   B HOH 193 ? ? 2.16 
18 1 ND2 K ASN 293 ? ? O7  K NAG 604 ? ? 2.16 
19 1 O   B LEU 101 ? ? O   B HOH 190 ? ? 2.17 
20 1 OE1 E GLU 178 ? ? NH1 E ARG 265 ? ? 2.17 
21 1 O4  A NAG 602 ? ? O5  A NAG 603 ? ? 2.17 
22 1 ND2 A ASN 93  ? ? O5  A NAG 602 ? ? 2.17 
23 1 N   A SER 149 ? ? O   A HOH 341 ? ? 2.18 
24 1 ND2 G ASN 282 ? ? O5  G NAG 603 ? ? 2.18 
25 1 ND2 K ASN 29  ? ? C2  K NAG 602 ? ? 2.18 
26 1 CE3 I TRP 66  ? ? O   I HOH 353 ? ? 2.18 
27 1 O   A GLY 252 ? ? O   A HOH 366 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 OE1 C GLU 74 ? ? 1_555 NE2 K HIS 144 ? ? 1_455 1.89 
2 1 OE1 C GLU 74 ? ? 1_555 CD2 K HIS 144 ? ? 1_455 2.04 
3 1 OE2 C GLU 74 ? ? 1_555 ND1 K HIS 144 ? ? 1_455 2.13 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 N  A ARG 51  ? ? CA A ARG 51  ? ? CB A ARG 51  ? ? 97.53  110.60 -13.07 1.80 N 
2  1 N  A ARG 51  ? ? CA A ARG 51  ? ? C  A ARG 51  ? ? 91.11  111.00 -19.89 2.70 N 
3  1 N  A TYR 198 ? ? CA A TYR 198 ? ? C  A TYR 198 ? ? 87.71  111.00 -23.29 2.70 N 
4  1 N  A GLN 199 ? ? CA A GLN 199 ? ? CB A GLN 199 ? ? 89.81  110.60 -20.79 1.80 N 
5  1 N  C ALA 79  ? ? CA C ALA 79  ? ? CB C ALA 79  ? ? 99.72  110.10 -10.38 1.40 N 
6  1 N  E SER 75  ? ? CA E SER 75  ? ? C  E SER 75  ? ? 129.28 111.00 18.28  2.70 N 
7  1 N  E LEU 76  ? ? CA E LEU 76  ? ? CB E LEU 76  ? ? 89.75  110.40 -20.65 2.00 N 
8  1 N  E LEU 76  ? ? CA E LEU 76  ? ? C  E LEU 76  ? ? 130.60 111.00 19.60  2.70 N 
9  1 CA E VAL 226 ? ? C  E VAL 226 ? ? N  E ARG 227 ? ? 137.55 117.20 20.35  2.20 Y 
10 1 O  E VAL 226 ? ? C  E VAL 226 ? ? N  E ARG 227 ? ? 99.76  122.70 -22.94 1.60 Y 
11 1 C  E VAL 226 ? ? N  E ARG 227 ? ? CA E ARG 227 ? ? 143.00 121.70 21.30  2.50 Y 
12 1 CB G SER 269 ? ? CA G SER 269 ? ? C  G SER 269 ? ? 95.12  110.10 -14.98 1.90 N 
13 1 N  I ASN 200 ? ? CA I ASN 200 ? ? CB I ASN 200 ? ? 123.98 110.60 13.38  1.80 N 
14 1 N  I ASN 200 ? ? CA I ASN 200 ? ? C  I ASN 200 ? ? 91.68  111.00 -19.32 2.70 N 
15 1 N  K ASP 92  ? ? CA K ASP 92  ? ? C  K ASP 92  ? ? 130.77 111.00 19.77  2.70 N 
16 1 N  K ASN 93  ? ? CA K ASN 93  ? ? CB K ASN 93  ? ? 123.41 110.60 12.81  1.80 N 
17 1 N  K ASN 200 ? ? CA K ASN 200 ? ? CB K ASN 200 ? ? 122.29 110.60 11.69  1.80 N 
18 1 N  K ASN 200 ? ? CA K ASN 200 ? ? C  K ASN 200 ? ? 93.10  111.00 -17.90 2.70 N 
19 1 CB L ASP 158 ? ? CA L ASP 158 ? ? C  L ASP 158 ? ? 92.16  110.40 -18.24 2.00 N 
20 1 N  L TYR 159 ? ? CA L TYR 159 ? ? CB L TYR 159 ? ? 90.19  110.60 -20.41 1.80 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1   1 CYS A 10  ? ? -110.15 -168.81 
2   1 TYR A 13  ? ? -125.11 -150.42 
3   1 ASN A 16  ? ? -165.44 -168.72 
4   1 ASN A 29  ? ? 37.56   64.38   
5   1 SER A 35  ? ? -170.17 -178.65 
6   1 ASP A 41  ? ? -140.35 34.06   
7   1 LEU A 50  ? ? -89.70  -70.42  
8   1 ARG A 51  ? ? -92.52  -78.42  
9   1 SER A 75  ? ? -113.54 62.34   
10  1 LEU A 76  ? ? -148.35 -14.58  
11  1 SER A 77  ? ? -108.03 71.69   
12  1 TRP A 129 ? ? -114.56 78.50   
13  1 CYS A 142 ? ? -113.52 70.36   
14  1 SER A 149 ? ? -128.40 -158.52 
15  1 SER A 168 ? ? -154.07 81.88   
16  1 ASN A 173 ? ? -66.44  95.51   
17  1 GLN A 199 ? ? -38.68  -29.20  
18  1 ASP A 228 ? ? 76.83   -8.23   
19  1 SER A 269 ? ? -126.04 -159.27 
20  1 LEU A 324 ? ? -105.59 -159.76 
21  1 ARG A 325 ? ? -62.72  -179.40 
22  1 ALA B 5   ? ? -82.36  -74.40  
23  1 GLN B 27  ? ? -149.71 57.13   
24  1 ASN B 28  ? ? -100.50 -166.96 
25  1 SER B 32  ? ? -125.89 -162.05 
26  1 LYS B 127 ? ? -106.97 -84.81  
27  1 ASN B 129 ? ? -65.64  0.29    
28  1 ASN B 135 ? ? -98.31  30.06   
29  1 ASP B 145 ? ? -78.53  -162.86 
30  1 MET B 149 ? ? -55.29  -70.65  
31  1 ASP B 158 ? ? -64.81  -176.96 
32  1 TYR B 159 ? ? -149.69 58.68   
33  1 TYR C 13  ? ? -123.57 -162.52 
34  1 ASN C 29  ? ? 37.42   64.12   
35  1 ARG C 51  ? ? -100.31 -84.85  
36  1 CYS C 73  ? ? -107.38 63.99   
37  1 LEU C 76  ? ? 49.36   22.35   
38  1 THR C 78  ? ? 76.80   -158.65 
39  1 ALA C 79  ? ? -111.60 -166.77 
40  1 SER C 127 ? ? -143.62 -27.86  
41  1 CYS C 142 ? ? -113.31 74.50   
42  1 ALA C 145 ? ? 50.93   70.27   
43  1 SER C 149 ? ? -121.20 -156.94 
44  1 SER C 168 ? ? -157.21 82.06   
45  1 ASN C 173 ? ? -69.67  95.53   
46  1 GLN C 199 ? ? 80.78   -7.23   
47  1 ALA C 201 ? ? -106.63 -61.85  
48  1 ASP C 228 ? ? 76.67   -6.30   
49  1 SER C 269 ? ? -109.69 -156.70 
50  1 ARG C 325 ? ? -48.33  156.74  
51  1 ALA D 5   ? ? -81.51  -72.91  
52  1 GLN D 27  ? ? -154.43 55.23   
53  1 ASN D 28  ? ? -100.53 -166.81 
54  1 SER D 32  ? ? -126.05 -161.42 
55  1 MET D 59  ? ? -100.50 79.14   
56  1 LYS D 127 ? ? -111.22 -80.66  
57  1 ASN D 129 ? ? -65.85  0.16    
58  1 ASP D 145 ? ? -77.51  -164.90 
59  1 PRO D 160 ? ? -66.26  72.03   
60  1 LYS D 161 ? ? -153.67 13.89   
61  1 TYR E 13  ? ? -124.74 -167.25 
62  1 ASN E 29  ? ? 37.41   64.67   
63  1 ARG E 51  ? ? -101.23 -84.76  
64  1 CYS E 73  ? ? -99.82  39.15   
65  1 SER E 75  ? ? -58.70  4.14    
66  1 LEU E 76  ? ? -97.83  -79.80  
67  1 THR E 78  ? ? -148.77 -1.13   
68  1 ASP E 92  ? ? -169.33 -12.94  
69  1 ASN E 93  ? ? -66.51  80.42   
70  1 SER E 127 ? ? -143.93 -13.48  
71  1 CYS E 142 ? ? -113.47 75.09   
72  1 SER E 149 ? ? -120.83 -157.34 
73  1 SER E 168 ? ? -152.63 81.49   
74  1 ASN E 173 ? ? -68.02  95.08   
75  1 GLN E 199 ? ? -31.69  -35.28  
76  1 SER E 213 ? ? -168.70 117.54  
77  1 ARG E 227 ? ? 82.27   41.76   
78  1 ASP E 228 ? ? 75.36   -7.21   
79  1 SER E 269 ? ? -115.06 -157.93 
80  1 ALA F 5   ? ? -82.04  -72.40  
81  1 GLN F 27  ? ? -160.97 82.56   
82  1 ASN F 28  ? ? -119.82 -142.84 
83  1 SER F 32  ? ? -126.50 -161.56 
84  1 LYS F 127 ? ? -100.47 -77.07  
85  1 ASN F 129 ? ? -67.04  5.73    
86  1 ASP F 145 ? ? -77.59  -164.93 
87  1 TYR F 159 ? ? -117.02 71.00   
88  1 ASN G 16  ? ? -162.03 -169.33 
89  1 ARG G 51  ? ? -100.06 -83.93  
90  1 SER G 75  ? ? 86.01   -6.66   
91  1 SER G 77  ? ? -145.01 -16.17  
92  1 THR G 78  ? ? -67.41  65.94   
93  1 SER G 127 ? ? -143.65 -12.93  
94  1 CYS G 142 ? ? -107.96 73.22   
95  1 SER G 149 ? ? -107.53 -155.56 
96  1 SER G 168 ? ? -153.22 81.83   
97  1 ASN G 173 ? ? -68.94  96.44   
98  1 ARG G 227 ? ? 70.26   30.48   
99  1 ASP G 228 ? ? 82.48   -6.82   
100 1 SER G 269 ? ? -57.25  174.33  
101 1 ALA H 5   ? ? -82.44  -72.69  
102 1 GLN H 27  ? ? -153.14 55.98   
103 1 ASN H 28  ? ? -101.18 -168.80 
104 1 SER H 32  ? ? -126.03 -160.67 
105 1 LYS H 127 ? ? -113.44 -82.18  
106 1 ASN H 129 ? ? -65.09  0.26    
107 1 ASP H 145 ? ? -78.55  -165.49 
108 1 TYR H 159 ? ? -108.34 66.21   
109 1 ASN I 29  ? ? 37.40   63.35   
110 1 ARG I 51  ? ? -104.27 -83.27  
111 1 CYS I 73  ? ? -100.49 47.41   
112 1 THR I 78  ? ? 65.54   73.24   
113 1 SER I 90  ? ? 74.18   31.95   
114 1 SER I 127 ? ? -140.25 -13.58  
115 1 CYS I 142 ? ? -109.30 71.12   
116 1 SER I 149 ? ? -120.50 -157.13 
117 1 ASN I 162 ? ? -152.12 5.20    
118 1 TYR I 164 ? ? -154.98 85.93   
119 1 SER I 168 ? ? -153.44 81.77   
120 1 ASN I 173 ? ? -69.59  97.00   
121 1 GLN I 199 ? ? 35.18   52.18   
122 1 SER I 209 ? ? -132.91 -159.97 
123 1 ASP I 228 ? ? 74.25   -7.98   
124 1 SER I 269 ? ? -133.34 -157.74 
125 1 ALA J 5   ? ? -83.04  -71.39  
126 1 GLN J 27  ? ? -152.12 84.98   
127 1 ASN J 28  ? ? -120.97 -143.62 
128 1 SER J 124 ? ? -76.17  23.63   
129 1 GLN J 125 ? ? -142.88 -16.99  
130 1 LYS J 127 ? ? -93.70  -80.08  
131 1 ASN J 129 ? ? -65.96  0.20    
132 1 ASP J 145 ? ? -78.43  -164.53 
133 1 TYR K 13  ? ? -73.64  -164.87 
134 1 ASN K 29  ? ? 26.96   64.25   
135 1 ASP K 41  ? ? -143.42 34.57   
136 1 ARG K 51  ? ? -105.38 -85.39  
137 1 CYS K 73  ? ? -100.05 42.57   
138 1 THR K 78  ? ? -65.44  78.06   
139 1 SER K 90  ? ? -99.00  39.51   
140 1 SER K 91  ? ? -72.18  -165.78 
141 1 ASN K 93  ? ? 59.31   -139.19 
142 1 THR K 95  ? ? -48.61  152.49  
143 1 ALA K 141 ? ? -75.60  -74.73  
144 1 SER K 149 ? ? -127.69 -162.51 
145 1 SER K 168 ? ? -152.51 81.50   
146 1 ASN K 173 ? ? -69.57  95.00   
147 1 GLN K 199 ? ? 34.44   47.50   
148 1 ASP K 228 ? ? 75.07   -7.30   
149 1 ALA K 267 ? ? -88.40  -76.99  
150 1 SER K 269 ? ? -75.35  -169.57 
151 1 ARG K 325 ? ? -58.79  177.89  
152 1 ALA L 5   ? ? -82.73  -71.94  
153 1 GLN L 27  ? ? -165.40 76.16   
154 1 ASN L 28  ? ? -115.30 -161.02 
155 1 SER L 32  ? ? -125.64 -161.65 
156 1 LYS L 127 ? ? -113.44 -74.70  
157 1 ASN L 129 ? ? -66.12  0.78    
158 1 ASP L 145 ? ? -77.03  -165.01 
159 1 ASN L 154 ? ? -69.59  12.07   
160 1 THR L 156 ? ? -101.09 79.78   
161 1 TYR L 159 ? ? -108.52 72.81   
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 CYS C 73  ? ? GLU C 74  ? ? -148.14 
2 1 SER C 77  ? ? THR C 78  ? ? 140.14  
3 1 GLN F 125 ? ? LEU F 126 ? ? 149.75  
4 1 TYR L 159 ? ? PRO L 160 ? ? 147.07  
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             VAL 
_pdbx_validate_main_chain_plane.auth_asym_id             E 
_pdbx_validate_main_chain_plane.auth_seq_id              226 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   12.95 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A THR 78  ? CG2 ? A THR 78  CG2 
2  1 Y 1 A GLU 230 ? CG  ? A GLU 230 CG  
3  1 Y 1 A GLU 230 ? CD  ? A GLU 230 CD  
4  1 Y 1 A GLU 230 ? OE1 ? A GLU 230 OE1 
5  1 Y 1 A GLU 230 ? OE2 ? A GLU 230 OE2 
6  1 Y 1 A THR 247 ? CG2 ? A THR 247 CG2 
7  1 Y 1 A THR 294 ? CG2 ? A THR 294 CG2 
8  1 Y 1 B THR 147 ? CG2 ? B THR 147 CG2 
9  1 Y 1 C THR 95  ? CG2 ? C THR 95  CG2 
10 1 Y 1 C THR 126 ? CG2 ? C THR 126 CG2 
11 1 Y 1 C THR 190 ? CG2 ? C THR 190 CG2 
12 1 Y 1 D THR 147 ? CG2 ? D THR 147 CG2 
13 1 Y 1 D LYS 153 ? CB  ? D LYS 153 CB  
14 1 Y 1 D LYS 153 ? CG  ? D LYS 153 CG  
15 1 Y 1 D LYS 153 ? CD  ? D LYS 153 CD  
16 1 Y 1 D LYS 153 ? CE  ? D LYS 153 CE  
17 1 Y 1 D LYS 153 ? NZ  ? D LYS 153 NZ  
18 1 Y 1 E THR 95  ? CG2 ? E THR 95  CG2 
19 1 Y 1 E THR 126 ? CG2 ? E THR 126 CG2 
20 1 Y 1 E THR 251 ? CG2 ? E THR 251 CG2 
21 1 Y 1 G THR 126 ? CG2 ? G THR 126 CG2 
22 1 Y 1 G GLU 230 ? CG  ? G GLU 230 CG  
23 1 Y 1 G GLU 230 ? CD  ? G GLU 230 CD  
24 1 Y 1 G GLU 230 ? OE1 ? G GLU 230 OE1 
25 1 Y 1 G GLU 230 ? OE2 ? G GLU 230 OE2 
26 1 Y 1 G THR 284 ? CG2 ? G THR 284 CG2 
27 1 Y 1 G THR 294 ? CG2 ? G THR 294 CG2 
28 1 Y 1 H THR 147 ? CG2 ? H THR 147 CG2 
29 1 Y 1 I THR 95  ? CG2 ? I THR 95  CG2 
30 1 Y 1 I THR 126 ? CG2 ? I THR 126 CG2 
31 1 Y 1 I THR 190 ? CG2 ? I THR 190 CG2 
32 1 Y 1 J THR 147 ? CG2 ? J THR 147 CG2 
33 1 Y 1 K THR 126 ? CG2 ? K THR 126 CG2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A ALA 1   ? A ALA 1   
2   1 Y 1 A ASP 2   ? A ASP 2   
3   1 Y 1 A LEU 3   ? A LEU 3   
4   1 Y 1 A GLY 4   ? A GLY 4   
5   1 Y 1 A SER 5   ? A SER 5   
6   1 Y 1 A ARG 6   ? A ARG 6   
7   1 Y 1 A PRO 328 ? A PRO 328 
8   1 Y 1 A SER 329 ? A SER 329 
9   1 Y 1 A ILE 330 ? A ILE 330 
10  1 Y 1 A GLN 331 ? A GLN 331 
11  1 Y 1 A SER 332 ? A SER 332 
12  1 Y 1 A ARG 333 ? A ARG 333 
13  1 Y 1 B SER 163 ? B SER 163 
14  1 Y 1 B GLU 164 ? B GLU 164 
15  1 Y 1 B GLU 165 ? B GLU 165 
16  1 Y 1 B ALA 166 ? B ALA 166 
17  1 Y 1 B LYS 167 ? B LYS 167 
18  1 Y 1 B LEU 168 ? B LEU 168 
19  1 Y 1 B ASN 169 ? B ASN 169 
20  1 Y 1 B ARG 170 ? B ARG 170 
21  1 Y 1 B GLU 171 ? B GLU 171 
22  1 Y 1 B GLU 172 ? B GLU 172 
23  1 Y 1 B ILE 173 ? B ILE 173 
24  1 Y 1 B ASP 174 ? B ASP 174 
25  1 Y 1 B GLY 175 ? B GLY 175 
26  1 Y 1 B VAL 176 ? B VAL 176 
27  1 Y 1 B ARG 177 ? B ARG 177 
28  1 Y 1 B LEU 178 ? B LEU 178 
29  1 Y 1 B VAL 179 ? B VAL 179 
30  1 Y 1 B PRO 180 ? B PRO 180 
31  1 Y 1 B ARG 181 ? B ARG 181 
32  1 Y 1 C ALA 1   ? C ALA 1   
33  1 Y 1 C ASP 2   ? C ASP 2   
34  1 Y 1 C LEU 3   ? C LEU 3   
35  1 Y 1 C GLY 4   ? C GLY 4   
36  1 Y 1 C SER 5   ? C SER 5   
37  1 Y 1 C ARG 6   ? C ARG 6   
38  1 Y 1 C PRO 328 ? C PRO 328 
39  1 Y 1 C SER 329 ? C SER 329 
40  1 Y 1 C ILE 330 ? C ILE 330 
41  1 Y 1 C GLN 331 ? C GLN 331 
42  1 Y 1 C SER 332 ? C SER 332 
43  1 Y 1 C ARG 333 ? C ARG 333 
44  1 Y 1 D SER 163 ? D SER 163 
45  1 Y 1 D GLU 164 ? D GLU 164 
46  1 Y 1 D GLU 165 ? D GLU 165 
47  1 Y 1 D ALA 166 ? D ALA 166 
48  1 Y 1 D LYS 167 ? D LYS 167 
49  1 Y 1 D LEU 168 ? D LEU 168 
50  1 Y 1 D ASN 169 ? D ASN 169 
51  1 Y 1 D ARG 170 ? D ARG 170 
52  1 Y 1 D GLU 171 ? D GLU 171 
53  1 Y 1 D GLU 172 ? D GLU 172 
54  1 Y 1 D ILE 173 ? D ILE 173 
55  1 Y 1 D ASP 174 ? D ASP 174 
56  1 Y 1 D GLY 175 ? D GLY 175 
57  1 Y 1 D VAL 176 ? D VAL 176 
58  1 Y 1 D ARG 177 ? D ARG 177 
59  1 Y 1 D LEU 178 ? D LEU 178 
60  1 Y 1 D VAL 179 ? D VAL 179 
61  1 Y 1 D PRO 180 ? D PRO 180 
62  1 Y 1 D ARG 181 ? D ARG 181 
63  1 Y 1 E ALA 1   ? E ALA 1   
64  1 Y 1 E ASP 2   ? E ASP 2   
65  1 Y 1 E LEU 3   ? E LEU 3   
66  1 Y 1 E GLY 4   ? E GLY 4   
67  1 Y 1 E SER 5   ? E SER 5   
68  1 Y 1 E ARG 6   ? E ARG 6   
69  1 Y 1 E PRO 328 ? E PRO 328 
70  1 Y 1 E SER 329 ? E SER 329 
71  1 Y 1 E ILE 330 ? E ILE 330 
72  1 Y 1 E GLN 331 ? E GLN 331 
73  1 Y 1 E SER 332 ? E SER 332 
74  1 Y 1 E ARG 333 ? E ARG 333 
75  1 Y 1 F GLY 1   ? F GLY 1   
76  1 Y 1 F SER 163 ? F SER 163 
77  1 Y 1 F GLU 164 ? F GLU 164 
78  1 Y 1 F GLU 165 ? F GLU 165 
79  1 Y 1 F ALA 166 ? F ALA 166 
80  1 Y 1 F LYS 167 ? F LYS 167 
81  1 Y 1 F LEU 168 ? F LEU 168 
82  1 Y 1 F ASN 169 ? F ASN 169 
83  1 Y 1 F ARG 170 ? F ARG 170 
84  1 Y 1 F GLU 171 ? F GLU 171 
85  1 Y 1 F GLU 172 ? F GLU 172 
86  1 Y 1 F ILE 173 ? F ILE 173 
87  1 Y 1 F ASP 174 ? F ASP 174 
88  1 Y 1 F GLY 175 ? F GLY 175 
89  1 Y 1 F VAL 176 ? F VAL 176 
90  1 Y 1 F ARG 177 ? F ARG 177 
91  1 Y 1 F LEU 178 ? F LEU 178 
92  1 Y 1 F VAL 179 ? F VAL 179 
93  1 Y 1 F PRO 180 ? F PRO 180 
94  1 Y 1 F ARG 181 ? F ARG 181 
95  1 Y 1 G ALA 1   ? G ALA 1   
96  1 Y 1 G ASP 2   ? G ASP 2   
97  1 Y 1 G LEU 3   ? G LEU 3   
98  1 Y 1 G GLY 4   ? G GLY 4   
99  1 Y 1 G SER 5   ? G SER 5   
100 1 Y 1 G ARG 6   ? G ARG 6   
101 1 Y 1 G PRO 328 ? G PRO 328 
102 1 Y 1 G SER 329 ? G SER 329 
103 1 Y 1 G ILE 330 ? G ILE 330 
104 1 Y 1 G GLN 331 ? G GLN 331 
105 1 Y 1 G SER 332 ? G SER 332 
106 1 Y 1 G ARG 333 ? G ARG 333 
107 1 Y 1 H SER 163 ? H SER 163 
108 1 Y 1 H GLU 164 ? H GLU 164 
109 1 Y 1 H GLU 165 ? H GLU 165 
110 1 Y 1 H ALA 166 ? H ALA 166 
111 1 Y 1 H LYS 167 ? H LYS 167 
112 1 Y 1 H LEU 168 ? H LEU 168 
113 1 Y 1 H ASN 169 ? H ASN 169 
114 1 Y 1 H ARG 170 ? H ARG 170 
115 1 Y 1 H GLU 171 ? H GLU 171 
116 1 Y 1 H GLU 172 ? H GLU 172 
117 1 Y 1 H ILE 173 ? H ILE 173 
118 1 Y 1 H ASP 174 ? H ASP 174 
119 1 Y 1 H GLY 175 ? H GLY 175 
120 1 Y 1 H VAL 176 ? H VAL 176 
121 1 Y 1 H ARG 177 ? H ARG 177 
122 1 Y 1 H LEU 178 ? H LEU 178 
123 1 Y 1 H VAL 179 ? H VAL 179 
124 1 Y 1 H PRO 180 ? H PRO 180 
125 1 Y 1 H ARG 181 ? H ARG 181 
126 1 Y 1 I ALA 1   ? I ALA 1   
127 1 Y 1 I ASP 2   ? I ASP 2   
128 1 Y 1 I LEU 3   ? I LEU 3   
129 1 Y 1 I GLY 4   ? I GLY 4   
130 1 Y 1 I SER 5   ? I SER 5   
131 1 Y 1 I ARG 6   ? I ARG 6   
132 1 Y 1 I PRO 328 ? I PRO 328 
133 1 Y 1 I SER 329 ? I SER 329 
134 1 Y 1 I ILE 330 ? I ILE 330 
135 1 Y 1 I GLN 331 ? I GLN 331 
136 1 Y 1 I SER 332 ? I SER 332 
137 1 Y 1 I ARG 333 ? I ARG 333 
138 1 Y 1 J SER 163 ? J SER 163 
139 1 Y 1 J GLU 164 ? J GLU 164 
140 1 Y 1 J GLU 165 ? J GLU 165 
141 1 Y 1 J ALA 166 ? J ALA 166 
142 1 Y 1 J LYS 167 ? J LYS 167 
143 1 Y 1 J LEU 168 ? J LEU 168 
144 1 Y 1 J ASN 169 ? J ASN 169 
145 1 Y 1 J ARG 170 ? J ARG 170 
146 1 Y 1 J GLU 171 ? J GLU 171 
147 1 Y 1 J GLU 172 ? J GLU 172 
148 1 Y 1 J ILE 173 ? J ILE 173 
149 1 Y 1 J ASP 174 ? J ASP 174 
150 1 Y 1 J GLY 175 ? J GLY 175 
151 1 Y 1 J VAL 176 ? J VAL 176 
152 1 Y 1 J ARG 177 ? J ARG 177 
153 1 Y 1 J LEU 178 ? J LEU 178 
154 1 Y 1 J VAL 179 ? J VAL 179 
155 1 Y 1 J PRO 180 ? J PRO 180 
156 1 Y 1 J ARG 181 ? J ARG 181 
157 1 Y 1 K ALA 1   ? K ALA 1   
158 1 Y 1 K ASP 2   ? K ASP 2   
159 1 Y 1 K LEU 3   ? K LEU 3   
160 1 Y 1 K GLY 4   ? K GLY 4   
161 1 Y 1 K SER 5   ? K SER 5   
162 1 Y 1 K ARG 6   ? K ARG 6   
163 1 Y 1 K PRO 328 ? K PRO 328 
164 1 Y 1 K SER 329 ? K SER 329 
165 1 Y 1 K ILE 330 ? K ILE 330 
166 1 Y 1 K GLN 331 ? K GLN 331 
167 1 Y 1 K SER 332 ? K SER 332 
168 1 Y 1 K ARG 333 ? K ARG 333 
169 1 Y 1 L GLY 1   ? L GLY 1   
170 1 Y 1 L SER 163 ? L SER 163 
171 1 Y 1 L GLU 164 ? L GLU 164 
172 1 Y 1 L GLU 165 ? L GLU 165 
173 1 Y 1 L ALA 166 ? L ALA 166 
174 1 Y 1 L LYS 167 ? L LYS 167 
175 1 Y 1 L LEU 168 ? L LEU 168 
176 1 Y 1 L ASN 169 ? L ASN 169 
177 1 Y 1 L ARG 170 ? L ARG 170 
178 1 Y 1 L GLU 171 ? L GLU 171 
179 1 Y 1 L GLU 172 ? L GLU 172 
180 1 Y 1 L ILE 173 ? L ILE 173 
181 1 Y 1 L ASP 174 ? L ASP 174 
182 1 Y 1 L GLY 175 ? L GLY 175 
183 1 Y 1 L VAL 176 ? L VAL 176 
184 1 Y 1 L ARG 177 ? L ARG 177 
185 1 Y 1 L LEU 178 ? L LEU 178 
186 1 Y 1 L VAL 179 ? L VAL 179 
187 1 Y 1 L PRO 180 ? L PRO 180 
188 1 Y 1 L ARG 181 ? L ARG 181 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 N-ACETYL-D-GLUCOSAMINE NAG 
4 BETA-D-MANNOSE         BMA 
5 water                  HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
M  3 NAG 1  601 601 NAG NAG A . 
N  3 NAG 1  602 602 NAG NAG A . 
O  3 NAG 2  603 603 NAG NAG A . 
P  3 NAG 1  604 604 NAG NAG A . 
Q  3 NAG 2  605 605 NAG NAG A . 
R  3 NAG 1  606 606 NAG NAG A . 
S  3 NAG 1  601 601 NAG NAG C . 
T  3 NAG 1  602 602 NAG NAG C . 
U  3 NAG 2  603 603 NAG NAG C . 
V  4 BMA 3  604 604 BMA BMA C . 
W  3 NAG 1  605 605 NAG NAG C . 
X  3 NAG 2  606 606 NAG NAG C . 
Y  3 NAG 1  607 607 NAG NAG C . 
Z  3 NAG 1  601 601 NAG NAG E . 
AA 3 NAG 1  602 602 NAG NAG E . 
BA 3 NAG 2  603 603 NAG NAG E . 
CA 3 NAG 1  604 604 NAG NAG E . 
DA 3 NAG 1  605 605 NAG NAG E . 
EA 3 NAG 1  601 601 NAG NAG F . 
FA 3 NAG 1  601 601 NAG NAG G . 
GA 3 NAG 1  602 602 NAG NAG G . 
HA 3 NAG 1  603 603 NAG NAG G . 
IA 3 NAG 1  601 601 NAG NAG I . 
JA 3 NAG 2  602 602 NAG NAG I . 
KA 4 BMA 3  603 603 BMA BMA I . 
LA 3 NAG 1  604 604 NAG NAG I . 
MA 3 NAG 2  605 605 NAG NAG I . 
NA 3 NAG 1  601 601 NAG NAG K . 
OA 3 NAG 1  602 602 NAG NAG K . 
PA 3 NAG 1  603 603 NAG NAG K . 
QA 3 NAG 1  604 604 NAG NAG K . 
RA 3 NAG 1  601 601 NAG NAG L . 
SA 5 HOH 1  334 334 HOH HOH A . 
SA 5 HOH 2  335 335 HOH HOH A . 
SA 5 HOH 3  336 336 HOH HOH A . 
SA 5 HOH 4  337 337 HOH HOH A . 
SA 5 HOH 5  338 338 HOH HOH A . 
SA 5 HOH 6  339 339 HOH HOH A . 
SA 5 HOH 7  340 340 HOH HOH A . 
SA 5 HOH 8  341 341 HOH HOH A . 
SA 5 HOH 9  342 342 HOH HOH A . 
SA 5 HOH 10 343 343 HOH HOH A . 
SA 5 HOH 11 344 344 HOH HOH A . 
SA 5 HOH 12 345 345 HOH HOH A . 
SA 5 HOH 13 346 346 HOH HOH A . 
SA 5 HOH 14 347 347 HOH HOH A . 
SA 5 HOH 15 348 348 HOH HOH A . 
SA 5 HOH 16 349 349 HOH HOH A . 
SA 5 HOH 17 350 350 HOH HOH A . 
SA 5 HOH 18 351 351 HOH HOH A . 
SA 5 HOH 19 353 353 HOH HOH A . 
SA 5 HOH 20 354 354 HOH HOH A . 
SA 5 HOH 21 355 355 HOH HOH A . 
SA 5 HOH 22 356 356 HOH HOH A . 
SA 5 HOH 23 357 357 HOH HOH A . 
SA 5 HOH 24 358 358 HOH HOH A . 
SA 5 HOH 25 359 359 HOH HOH A . 
SA 5 HOH 26 360 360 HOH HOH A . 
SA 5 HOH 27 361 361 HOH HOH A . 
SA 5 HOH 28 362 362 HOH HOH A . 
SA 5 HOH 29 363 363 HOH HOH A . 
SA 5 HOH 30 364 364 HOH HOH A . 
SA 5 HOH 31 365 365 HOH HOH A . 
SA 5 HOH 32 366 366 HOH HOH A . 
SA 5 HOH 33 367 367 HOH HOH A . 
SA 5 HOH 34 368 368 HOH HOH A . 
SA 5 HOH 35 369 369 HOH HOH A . 
SA 5 HOH 36 370 370 HOH HOH A . 
TA 5 HOH 1  182 182 HOH HOH B . 
TA 5 HOH 2  183 183 HOH HOH B . 
TA 5 HOH 3  184 184 HOH HOH B . 
TA 5 HOH 4  185 185 HOH HOH B . 
TA 5 HOH 5  186 186 HOH HOH B . 
TA 5 HOH 6  187 187 HOH HOH B . 
TA 5 HOH 7  188 188 HOH HOH B . 
TA 5 HOH 8  189 189 HOH HOH B . 
TA 5 HOH 9  190 190 HOH HOH B . 
TA 5 HOH 10 191 191 HOH HOH B . 
TA 5 HOH 11 192 192 HOH HOH B . 
TA 5 HOH 12 193 193 HOH HOH B . 
TA 5 HOH 13 211 211 HOH HOH B . 
TA 5 HOH 14 212 212 HOH HOH B . 
TA 5 HOH 15 238 238 HOH HOH B . 
TA 5 HOH 16 299 299 HOH HOH B . 
TA 5 HOH 17 307 307 HOH HOH B . 
UA 5 HOH 1  334 334 HOH HOH C . 
UA 5 HOH 2  335 335 HOH HOH C . 
UA 5 HOH 3  336 336 HOH HOH C . 
UA 5 HOH 4  337 337 HOH HOH C . 
UA 5 HOH 5  338 338 HOH HOH C . 
UA 5 HOH 6  339 339 HOH HOH C . 
UA 5 HOH 7  340 340 HOH HOH C . 
UA 5 HOH 8  341 341 HOH HOH C . 
UA 5 HOH 9  342 342 HOH HOH C . 
UA 5 HOH 10 343 343 HOH HOH C . 
UA 5 HOH 11 344 344 HOH HOH C . 
UA 5 HOH 12 345 345 HOH HOH C . 
UA 5 HOH 13 346 346 HOH HOH C . 
UA 5 HOH 14 347 347 HOH HOH C . 
UA 5 HOH 15 348 348 HOH HOH C . 
UA 5 HOH 16 349 349 HOH HOH C . 
UA 5 HOH 17 350 350 HOH HOH C . 
UA 5 HOH 18 351 351 HOH HOH C . 
UA 5 HOH 19 352 352 HOH HOH C . 
UA 5 HOH 20 353 353 HOH HOH C . 
UA 5 HOH 21 354 354 HOH HOH C . 
UA 5 HOH 22 355 355 HOH HOH C . 
UA 5 HOH 23 356 356 HOH HOH C . 
UA 5 HOH 24 357 357 HOH HOH C . 
UA 5 HOH 25 358 358 HOH HOH C . 
UA 5 HOH 26 359 359 HOH HOH C . 
UA 5 HOH 27 360 360 HOH HOH C . 
UA 5 HOH 28 361 361 HOH HOH C . 
UA 5 HOH 29 362 362 HOH HOH C . 
UA 5 HOH 30 363 363 HOH HOH C . 
UA 5 HOH 31 364 364 HOH HOH C . 
UA 5 HOH 32 365 365 HOH HOH C . 
UA 5 HOH 33 366 366 HOH HOH C . 
UA 5 HOH 34 367 367 HOH HOH C . 
UA 5 HOH 35 368 368 HOH HOH C . 
UA 5 HOH 36 369 369 HOH HOH C . 
UA 5 HOH 37 370 370 HOH HOH C . 
UA 5 HOH 38 371 371 HOH HOH C . 
VA 5 HOH 1  182 182 HOH HOH D . 
VA 5 HOH 2  183 183 HOH HOH D . 
VA 5 HOH 3  184 184 HOH HOH D . 
VA 5 HOH 4  185 185 HOH HOH D . 
VA 5 HOH 5  186 186 HOH HOH D . 
VA 5 HOH 6  187 187 HOH HOH D . 
VA 5 HOH 7  188 188 HOH HOH D . 
VA 5 HOH 8  189 189 HOH HOH D . 
VA 5 HOH 9  244 244 HOH HOH D . 
VA 5 HOH 10 265 265 HOH HOH D . 
WA 5 HOH 1  334 334 HOH HOH E . 
WA 5 HOH 2  335 335 HOH HOH E . 
WA 5 HOH 3  336 336 HOH HOH E . 
WA 5 HOH 4  337 337 HOH HOH E . 
WA 5 HOH 5  338 338 HOH HOH E . 
WA 5 HOH 6  339 339 HOH HOH E . 
WA 5 HOH 7  340 340 HOH HOH E . 
WA 5 HOH 8  341 341 HOH HOH E . 
WA 5 HOH 9  342 342 HOH HOH E . 
WA 5 HOH 10 343 343 HOH HOH E . 
WA 5 HOH 11 344 344 HOH HOH E . 
WA 5 HOH 12 345 345 HOH HOH E . 
WA 5 HOH 13 346 346 HOH HOH E . 
WA 5 HOH 14 347 347 HOH HOH E . 
WA 5 HOH 15 348 348 HOH HOH E . 
WA 5 HOH 16 349 349 HOH HOH E . 
WA 5 HOH 17 350 350 HOH HOH E . 
WA 5 HOH 18 351 351 HOH HOH E . 
WA 5 HOH 19 352 352 HOH HOH E . 
WA 5 HOH 20 353 353 HOH HOH E . 
WA 5 HOH 21 354 354 HOH HOH E . 
WA 5 HOH 22 355 355 HOH HOH E . 
WA 5 HOH 23 356 356 HOH HOH E . 
WA 5 HOH 24 357 357 HOH HOH E . 
WA 5 HOH 25 358 358 HOH HOH E . 
WA 5 HOH 26 359 359 HOH HOH E . 
WA 5 HOH 27 360 360 HOH HOH E . 
WA 5 HOH 28 361 361 HOH HOH E . 
WA 5 HOH 29 362 362 HOH HOH E . 
WA 5 HOH 30 363 363 HOH HOH E . 
WA 5 HOH 31 364 364 HOH HOH E . 
XA 5 HOH 1  182 182 HOH HOH F . 
XA 5 HOH 2  183 183 HOH HOH F . 
XA 5 HOH 3  184 184 HOH HOH F . 
XA 5 HOH 4  185 185 HOH HOH F . 
XA 5 HOH 5  186 186 HOH HOH F . 
XA 5 HOH 6  187 187 HOH HOH F . 
XA 5 HOH 7  188 188 HOH HOH F . 
XA 5 HOH 8  189 189 HOH HOH F . 
XA 5 HOH 9  190 190 HOH HOH F . 
XA 5 HOH 10 191 191 HOH HOH F . 
XA 5 HOH 11 192 192 HOH HOH F . 
XA 5 HOH 12 193 193 HOH HOH F . 
XA 5 HOH 13 284 284 HOH HOH F . 
YA 5 HOH 1  334 334 HOH HOH G . 
YA 5 HOH 2  335 335 HOH HOH G . 
YA 5 HOH 3  336 336 HOH HOH G . 
YA 5 HOH 4  337 337 HOH HOH G . 
YA 5 HOH 5  338 338 HOH HOH G . 
YA 5 HOH 6  339 339 HOH HOH G . 
YA 5 HOH 7  340 340 HOH HOH G . 
YA 5 HOH 8  341 341 HOH HOH G . 
YA 5 HOH 9  342 342 HOH HOH G . 
YA 5 HOH 10 343 343 HOH HOH G . 
YA 5 HOH 11 344 344 HOH HOH G . 
YA 5 HOH 12 345 345 HOH HOH G . 
YA 5 HOH 13 346 346 HOH HOH G . 
YA 5 HOH 14 347 347 HOH HOH G . 
YA 5 HOH 15 348 348 HOH HOH G . 
YA 5 HOH 16 349 349 HOH HOH G . 
YA 5 HOH 17 350 350 HOH HOH G . 
YA 5 HOH 18 351 351 HOH HOH G . 
YA 5 HOH 19 352 352 HOH HOH G . 
YA 5 HOH 20 353 353 HOH HOH G . 
YA 5 HOH 21 354 354 HOH HOH G . 
YA 5 HOH 22 355 355 HOH HOH G . 
YA 5 HOH 23 356 356 HOH HOH G . 
YA 5 HOH 24 357 357 HOH HOH G . 
YA 5 HOH 25 358 358 HOH HOH G . 
YA 5 HOH 26 359 359 HOH HOH G . 
YA 5 HOH 27 360 360 HOH HOH G . 
YA 5 HOH 28 361 361 HOH HOH G . 
YA 5 HOH 29 362 362 HOH HOH G . 
YA 5 HOH 30 363 363 HOH HOH G . 
YA 5 HOH 31 364 364 HOH HOH G . 
YA 5 HOH 32 365 365 HOH HOH G . 
YA 5 HOH 33 366 366 HOH HOH G . 
YA 5 HOH 34 367 367 HOH HOH G . 
YA 5 HOH 35 368 368 HOH HOH G . 
YA 5 HOH 36 369 369 HOH HOH G . 
YA 5 HOH 37 370 370 HOH HOH G . 
YA 5 HOH 38 371 371 HOH HOH G . 
YA 5 HOH 39 372 372 HOH HOH G . 
YA 5 HOH 40 373 373 HOH HOH G . 
YA 5 HOH 41 374 374 HOH HOH G . 
YA 5 HOH 42 375 375 HOH HOH G . 
YA 5 HOH 43 376 376 HOH HOH G . 
YA 5 HOH 44 377 377 HOH HOH G . 
YA 5 HOH 45 378 378 HOH HOH G . 
ZA 5 HOH 1  182 182 HOH HOH H . 
ZA 5 HOH 2  183 183 HOH HOH H . 
ZA 5 HOH 3  184 184 HOH HOH H . 
ZA 5 HOH 4  185 185 HOH HOH H . 
ZA 5 HOH 5  186 186 HOH HOH H . 
ZA 5 HOH 6  187 187 HOH HOH H . 
ZA 5 HOH 7  188 188 HOH HOH H . 
ZA 5 HOH 8  189 189 HOH HOH H . 
ZA 5 HOH 9  190 190 HOH HOH H . 
ZA 5 HOH 10 191 191 HOH HOH H . 
ZA 5 HOH 11 192 192 HOH HOH H . 
ZA 5 HOH 12 193 193 HOH HOH H . 
ZA 5 HOH 13 194 194 HOH HOH H . 
ZA 5 HOH 14 195 195 HOH HOH H . 
ZA 5 HOH 15 196 196 HOH HOH H . 
ZA 5 HOH 16 197 197 HOH HOH H . 
ZA 5 HOH 17 198 198 HOH HOH H . 
ZA 5 HOH 18 208 208 HOH HOH H . 
ZA 5 HOH 19 231 231 HOH HOH H . 
ZA 5 HOH 20 233 233 HOH HOH H . 
ZA 5 HOH 21 246 246 HOH HOH H . 
ZA 5 HOH 22 256 256 HOH HOH H . 
ZA 5 HOH 23 277 277 HOH HOH H . 
AB 5 HOH 1  334 334 HOH HOH I . 
AB 5 HOH 2  335 335 HOH HOH I . 
AB 5 HOH 3  336 336 HOH HOH I . 
AB 5 HOH 4  337 337 HOH HOH I . 
AB 5 HOH 5  338 338 HOH HOH I . 
AB 5 HOH 6  339 339 HOH HOH I . 
AB 5 HOH 7  340 340 HOH HOH I . 
AB 5 HOH 8  341 341 HOH HOH I . 
AB 5 HOH 9  342 342 HOH HOH I . 
AB 5 HOH 10 343 343 HOH HOH I . 
AB 5 HOH 11 344 344 HOH HOH I . 
AB 5 HOH 12 345 345 HOH HOH I . 
AB 5 HOH 13 346 346 HOH HOH I . 
AB 5 HOH 14 347 347 HOH HOH I . 
AB 5 HOH 15 348 348 HOH HOH I . 
AB 5 HOH 16 349 349 HOH HOH I . 
AB 5 HOH 17 350 350 HOH HOH I . 
AB 5 HOH 18 351 351 HOH HOH I . 
AB 5 HOH 19 352 352 HOH HOH I . 
AB 5 HOH 20 353 353 HOH HOH I . 
AB 5 HOH 21 354 354 HOH HOH I . 
AB 5 HOH 22 356 356 HOH HOH I . 
AB 5 HOH 23 357 357 HOH HOH I . 
AB 5 HOH 24 358 358 HOH HOH I . 
AB 5 HOH 25 359 359 HOH HOH I . 
AB 5 HOH 26 360 360 HOH HOH I . 
AB 5 HOH 27 361 361 HOH HOH I . 
AB 5 HOH 28 362 362 HOH HOH I . 
AB 5 HOH 29 363 363 HOH HOH I . 
AB 5 HOH 30 364 364 HOH HOH I . 
AB 5 HOH 31 365 365 HOH HOH I . 
AB 5 HOH 32 366 366 HOH HOH I . 
AB 5 HOH 33 367 367 HOH HOH I . 
AB 5 HOH 34 368 368 HOH HOH I . 
AB 5 HOH 35 369 369 HOH HOH I . 
AB 5 HOH 36 370 370 HOH HOH I . 
AB 5 HOH 37 371 371 HOH HOH I . 
BB 5 HOH 1  182 182 HOH HOH J . 
BB 5 HOH 2  183 183 HOH HOH J . 
BB 5 HOH 3  184 184 HOH HOH J . 
BB 5 HOH 4  185 185 HOH HOH J . 
BB 5 HOH 5  186 186 HOH HOH J . 
BB 5 HOH 6  187 187 HOH HOH J . 
BB 5 HOH 7  188 188 HOH HOH J . 
BB 5 HOH 8  189 189 HOH HOH J . 
BB 5 HOH 9  190 190 HOH HOH J . 
BB 5 HOH 10 199 199 HOH HOH J . 
BB 5 HOH 11 205 205 HOH HOH J . 
BB 5 HOH 12 210 210 HOH HOH J . 
BB 5 HOH 13 234 234 HOH HOH J . 
BB 5 HOH 14 248 248 HOH HOH J . 
BB 5 HOH 15 252 252 HOH HOH J . 
BB 5 HOH 16 257 257 HOH HOH J . 
BB 5 HOH 17 260 260 HOH HOH J . 
BB 5 HOH 18 295 295 HOH HOH J . 
BB 5 HOH 19 313 313 HOH HOH J . 
BB 5 HOH 20 318 318 HOH HOH J . 
BB 5 HOH 21 319 319 HOH HOH J . 
CB 5 HOH 1  334 334 HOH HOH K . 
CB 5 HOH 2  335 335 HOH HOH K . 
CB 5 HOH 3  336 336 HOH HOH K . 
CB 5 HOH 4  337 337 HOH HOH K . 
CB 5 HOH 5  338 338 HOH HOH K . 
CB 5 HOH 6  339 339 HOH HOH K . 
CB 5 HOH 7  340 340 HOH HOH K . 
CB 5 HOH 8  341 341 HOH HOH K . 
CB 5 HOH 9  342 342 HOH HOH K . 
CB 5 HOH 10 343 343 HOH HOH K . 
CB 5 HOH 11 344 344 HOH HOH K . 
CB 5 HOH 12 345 345 HOH HOH K . 
CB 5 HOH 13 346 346 HOH HOH K . 
CB 5 HOH 14 347 347 HOH HOH K . 
CB 5 HOH 15 348 348 HOH HOH K . 
CB 5 HOH 16 350 350 HOH HOH K . 
CB 5 HOH 17 351 351 HOH HOH K . 
CB 5 HOH 18 352 352 HOH HOH K . 
CB 5 HOH 19 353 353 HOH HOH K . 
CB 5 HOH 20 354 354 HOH HOH K . 
CB 5 HOH 21 355 355 HOH HOH K . 
CB 5 HOH 22 356 356 HOH HOH K . 
CB 5 HOH 23 357 357 HOH HOH K . 
CB 5 HOH 24 358 358 HOH HOH K . 
CB 5 HOH 25 359 359 HOH HOH K . 
CB 5 HOH 26 360 360 HOH HOH K . 
CB 5 HOH 27 361 361 HOH HOH K . 
CB 5 HOH 28 362 362 HOH HOH K . 
CB 5 HOH 29 363 363 HOH HOH K . 
CB 5 HOH 30 364 364 HOH HOH K . 
CB 5 HOH 31 365 365 HOH HOH K . 
CB 5 HOH 32 366 366 HOH HOH K . 
CB 5 HOH 33 367 367 HOH HOH K . 
CB 5 HOH 34 368 368 HOH HOH K . 
CB 5 HOH 35 369 369 HOH HOH K . 
DB 5 HOH 1  182 182 HOH HOH L . 
DB 5 HOH 2  183 183 HOH HOH L . 
DB 5 HOH 3  184 184 HOH HOH L . 
DB 5 HOH 4  203 203 HOH HOH L . 
DB 5 HOH 5  219 219 HOH HOH L . 
DB 5 HOH 6  227 227 HOH HOH L . 
DB 5 HOH 7  235 235 HOH HOH L . 
DB 5 HOH 8  247 247 HOH HOH L . 
DB 5 HOH 9  262 262 HOH HOH L . 
DB 5 HOH 10 276 276 HOH HOH L . 
DB 5 HOH 11 279 279 HOH HOH L . 
# 
