data_4EDA
# 
_entry.id   4EDA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4EDA         
RCSB  RCSB071472   
WWPDB D_1000071472 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          4EDB 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.entry_id                        4EDA 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2012-03-27 
_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.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Kim, K.H.'  1 
'Cho, K.J.'  2 
'Lee, J.H.'  3 
'Park, Y.H.' 4 
'Khan, T.G.' 5 
'Lee, J.Y.'  6 
'Kang, S.H.' 7 
'Alam, I.'   8 
# 
_citation.id                        primary 
_citation.title                     'Insight into structural diversity of influenza virus haemagglutinin' 
_citation.journal_abbrev            J.Gen.Virol. 
_citation.journal_volume            94 
_citation.page_first                1712 
_citation.page_last                 1722 
_citation.year                      2013 
_citation.journal_id_ASTM           JGVIAY 
_citation.country                   US 
_citation.journal_id_ISSN           0022-1317 
_citation.journal_id_CSD            2058 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   23636824 
_citation.pdbx_database_id_DOI      10.1099/vir.0.051136-0 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Cho, K.J.'   1  
primary 'Lee, J.H.'   2  
primary 'Hong, K.W.'  3  
primary 'Kim, S.H.'   4  
primary 'Park, Y.'    5  
primary 'Lee, J.Y.'   6  
primary 'Kang, S.'    7  
primary 'Kim, S.'     8  
primary 'Yang, J.H.'  9  
primary 'Kim, E.K.'   10 
primary 'Seok, J.H.'  11 
primary 'Unzai, S.'   12 
primary 'Park, S.Y.'  13 
primary 'Saelens, X.' 14 
primary 'Kim, C.J.'   15 
primary 'Lee, J.Y.'   16 
primary 'Kang, C.'    17 
primary 'Oh, H.B.'    18 
primary 'Chung, M.S.' 19 
primary 'Kim, K.H.'   20 
# 
_cell.entry_id           4EDA 
_cell.length_a           208.126 
_cell.length_b           208.126 
_cell.length_c           65.765 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              12 
_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                         4EDA 
_symmetry.space_group_name_H-M             'P 6' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                168 
_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          37341.082 2  ? ? 'HA1 SUBUNIT, UNP residues 18-344'  ? 
2 polymer     man Hemagglutinin          20844.113 2  ? ? 'HA2 SUBUNIT, UNP residues 345-520' ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   8  ? ? ?                                   ? 
4 water       nat water                  18.015    63 ? ? ?                                   ? 
# 
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 
;ADPGYLLEFDTLCIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDKHNGKLCKLRGVAPLHLGKCNIAGWILGNPECESLS
TASSWSYIVETSSSDNGTCYPGDFIDYEELREQLSSVSSFERFEIFPKTSSWPNHDSNKGVTAACPHAGAKSFYKNLIWL
VKKGNSYPKLSKSYINDKGKEVLVLWGIHHPSTSADQQSLYQNADAYVFVGSSRYSKKFKPEIAIRPKVRDQEGRMNYYW
TLVEPGDKITFEATGNLVVPRYAFAMERNAGSGIIISDTPVHDCNTTCQTPKGAINTSLPFQNIHPITIGKCPKYVKSTK
LRLATGLRNVPSIQSR
;
;ADPGYLLEFDTLCIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDKHNGKLCKLRGVAPLHLGKCNIAGWILGNPECESLS
TASSWSYIVETSSSDNGTCYPGDFIDYEELREQLSSVSSFERFEIFPKTSSWPNHDSNKGVTAACPHAGAKSFYKNLIWL
VKKGNSYPKLSKSYINDKGKEVLVLWGIHHPSTSADQQSLYQNADAYVFVGSSRYSKKFKPEIAIRPKVRDQEGRMNYYW
TLVEPGDKITFEATGNLVVPRYAFAMERNAGSGIIISDTPVHDCNTTCQTPKGAINTSLPFQNIHPITIGKCPKYVKSTK
LRLATGLRNVPSIQSR
;
A,C ? 
2 'polypeptide(L)' no no 
;GLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADLKSTQNAIDEITNKVNSVIEKMNTQFTAVGKEFNHLEKRIENL
NKKVDDGFLDIWTYNAELLVLLENERTLDYHDSNVKNLYEKVRSQLKNNAKEIGNGCFEFYHKCDNTCMESVKNGTYDYP
KYSEEAKLNREEIDGVRSLVPR
;
;GLFGAIAGFIEGGWTGMVDGWYGYHHQNEQGSGYAADLKSTQNAIDEITNKVNSVIEKMNTQFTAVGKEFNHLEKRIENL
NKKVDDGFLDIWTYNAELLVLLENERTLDYHDSNVKNLYEKVRSQLKNNAKEIGNGCFEFYHKCDNTCMESVKNGTYDYP
KYSEEAKLNREEIDGVRSLVPR
;
B,D ? 
# 
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   PRO n 
1 4   GLY n 
1 5   TYR n 
1 6   LEU n 
1 7   LEU n 
1 8   GLU n 
1 9   PHE n 
1 10  ASP n 
1 11  THR n 
1 12  LEU n 
1 13  CYS n 
1 14  ILE n 
1 15  GLY n 
1 16  TYR n 
1 17  HIS n 
1 18  ALA n 
1 19  ASN n 
1 20  ASN n 
1 21  SER n 
1 22  THR n 
1 23  ASP n 
1 24  THR n 
1 25  VAL n 
1 26  ASP n 
1 27  THR n 
1 28  VAL n 
1 29  LEU n 
1 30  GLU n 
1 31  LYS n 
1 32  ASN n 
1 33  VAL n 
1 34  THR n 
1 35  VAL n 
1 36  THR n 
1 37  HIS n 
1 38  SER n 
1 39  VAL n 
1 40  ASN n 
1 41  LEU n 
1 42  LEU n 
1 43  GLU n 
1 44  ASP n 
1 45  LYS n 
1 46  HIS n 
1 47  ASN n 
1 48  GLY n 
1 49  LYS n 
1 50  LEU n 
1 51  CYS n 
1 52  LYS n 
1 53  LEU n 
1 54  ARG n 
1 55  GLY n 
1 56  VAL n 
1 57  ALA n 
1 58  PRO n 
1 59  LEU n 
1 60  HIS n 
1 61  LEU n 
1 62  GLY n 
1 63  LYS n 
1 64  CYS n 
1 65  ASN n 
1 66  ILE n 
1 67  ALA n 
1 68  GLY n 
1 69  TRP n 
1 70  ILE n 
1 71  LEU n 
1 72  GLY n 
1 73  ASN n 
1 74  PRO n 
1 75  GLU n 
1 76  CYS n 
1 77  GLU n 
1 78  SER n 
1 79  LEU n 
1 80  SER n 
1 81  THR n 
1 82  ALA n 
1 83  SER n 
1 84  SER n 
1 85  TRP n 
1 86  SER n 
1 87  TYR n 
1 88  ILE n 
1 89  VAL n 
1 90  GLU n 
1 91  THR n 
1 92  SER n 
1 93  SER n 
1 94  SER n 
1 95  ASP n 
1 96  ASN n 
1 97  GLY n 
1 98  THR n 
1 99  CYS n 
1 100 TYR n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 PHE n 
1 105 ILE n 
1 106 ASP n 
1 107 TYR n 
1 108 GLU n 
1 109 GLU n 
1 110 LEU n 
1 111 ARG n 
1 112 GLU n 
1 113 GLN n 
1 114 LEU n 
1 115 SER n 
1 116 SER n 
1 117 VAL n 
1 118 SER n 
1 119 SER n 
1 120 PHE n 
1 121 GLU n 
1 122 ARG n 
1 123 PHE n 
1 124 GLU n 
1 125 ILE n 
1 126 PHE n 
1 127 PRO n 
1 128 LYS n 
1 129 THR n 
1 130 SER n 
1 131 SER n 
1 132 TRP n 
1 133 PRO n 
1 134 ASN n 
1 135 HIS n 
1 136 ASP n 
1 137 SER n 
1 138 ASN n 
1 139 LYS n 
1 140 GLY n 
1 141 VAL n 
1 142 THR n 
1 143 ALA n 
1 144 ALA n 
1 145 CYS n 
1 146 PRO n 
1 147 HIS n 
1 148 ALA n 
1 149 GLY n 
1 150 ALA n 
1 151 LYS n 
1 152 SER n 
1 153 PHE n 
1 154 TYR n 
1 155 LYS n 
1 156 ASN n 
1 157 LEU n 
1 158 ILE n 
1 159 TRP n 
1 160 LEU n 
1 161 VAL n 
1 162 LYS n 
1 163 LYS n 
1 164 GLY n 
1 165 ASN n 
1 166 SER n 
1 167 TYR n 
1 168 PRO n 
1 169 LYS n 
1 170 LEU n 
1 171 SER n 
1 172 LYS n 
1 173 SER n 
1 174 TYR n 
1 175 ILE n 
1 176 ASN n 
1 177 ASP n 
1 178 LYS n 
1 179 GLY n 
1 180 LYS n 
1 181 GLU n 
1 182 VAL n 
1 183 LEU n 
1 184 VAL n 
1 185 LEU n 
1 186 TRP n 
1 187 GLY n 
1 188 ILE n 
1 189 HIS n 
1 190 HIS n 
1 191 PRO n 
1 192 SER n 
1 193 THR n 
1 194 SER n 
1 195 ALA n 
1 196 ASP n 
1 197 GLN n 
1 198 GLN n 
1 199 SER n 
1 200 LEU n 
1 201 TYR n 
1 202 GLN n 
1 203 ASN n 
1 204 ALA n 
1 205 ASP n 
1 206 ALA n 
1 207 TYR n 
1 208 VAL n 
1 209 PHE n 
1 210 VAL n 
1 211 GLY n 
1 212 SER n 
1 213 SER n 
1 214 ARG n 
1 215 TYR n 
1 216 SER n 
1 217 LYS n 
1 218 LYS n 
1 219 PHE n 
1 220 LYS n 
1 221 PRO n 
1 222 GLU n 
1 223 ILE n 
1 224 ALA n 
1 225 ILE n 
1 226 ARG n 
1 227 PRO n 
1 228 LYS n 
1 229 VAL n 
1 230 ARG n 
1 231 ASP n 
1 232 GLN n 
1 233 GLU n 
1 234 GLY n 
1 235 ARG n 
1 236 MET n 
1 237 ASN n 
1 238 TYR n 
1 239 TYR n 
1 240 TRP n 
1 241 THR n 
1 242 LEU n 
1 243 VAL n 
1 244 GLU n 
1 245 PRO n 
1 246 GLY n 
1 247 ASP n 
1 248 LYS n 
1 249 ILE n 
1 250 THR n 
1 251 PHE n 
1 252 GLU n 
1 253 ALA n 
1 254 THR n 
1 255 GLY n 
1 256 ASN n 
1 257 LEU n 
1 258 VAL n 
1 259 VAL n 
1 260 PRO n 
1 261 ARG n 
1 262 TYR n 
1 263 ALA n 
1 264 PHE n 
1 265 ALA n 
1 266 MET n 
1 267 GLU n 
1 268 ARG n 
1 269 ASN n 
1 270 ALA n 
1 271 GLY n 
1 272 SER n 
1 273 GLY n 
1 274 ILE n 
1 275 ILE n 
1 276 ILE n 
1 277 SER n 
1 278 ASP n 
1 279 THR n 
1 280 PRO n 
1 281 VAL n 
1 282 HIS n 
1 283 ASP n 
1 284 CYS n 
1 285 ASN n 
1 286 THR n 
1 287 THR n 
1 288 CYS n 
1 289 GLN n 
1 290 THR n 
1 291 PRO n 
1 292 LYS n 
1 293 GLY n 
1 294 ALA n 
1 295 ILE n 
1 296 ASN n 
1 297 THR n 
1 298 SER n 
1 299 LEU n 
1 300 PRO n 
1 301 PHE n 
1 302 GLN n 
1 303 ASN n 
1 304 ILE n 
1 305 HIS n 
1 306 PRO n 
1 307 ILE n 
1 308 THR n 
1 309 ILE n 
1 310 GLY n 
1 311 LYS n 
1 312 CYS n 
1 313 PRO n 
1 314 LYS n 
1 315 TYR n 
1 316 VAL n 
1 317 LYS n 
1 318 SER n 
1 319 THR n 
1 320 LYS n 
1 321 LEU n 
1 322 ARG n 
1 323 LEU n 
1 324 ALA n 
1 325 THR n 
1 326 GLY n 
1 327 LEU n 
1 328 ARG n 
1 329 ASN n 
1 330 VAL n 
1 331 PRO n 
1 332 SER n 
1 333 ILE n 
1 334 GLN n 
1 335 SER n 
1 336 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 SER n 
2 179 LEU n 
2 180 VAL n 
2 181 PRO n 
2 182 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 ? ? ? ? ? HA ? 'A/Korea/01/2009 H1N1' ? ? ? ? 'Influenza A virus' 644289 ? ? ? ? ? ? ? ? 'Trichoplusia ni' 7111 ? ? ? ? 
? ? ? ? Hi5 ? ? ? ? ? Baculovirus ? ? ? pAcGP67A ? ? 
2 1 sample ? ? ? ? ? HA ? 'A/Korea/01/2009 H1N1' ? ? ? ? 'Influenza A virus' 644289 ? ? ? ? ? ? ? ? 'Trichoplusia ni' 7111 ? ? ? ? 
? ? ? ? Hi5 ? ? ? ? ? Baculovirus ? ? ? pAcGP67A ? ? 
# 
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 C5MQE6_9INFA C5MQE6 1 
;DTLCIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDKHNGKLCKLRGVAPLHLGKCNIAGWILGNPECESLSTASSWSYIV
ETSSSDNGTCYPGDFIDYEELREQLSSVSSFERFEIFPKTSSWPNHDSNKGVTAACPHAGAKSFYKNLIWLVKKGNSYPK
LSKSYINDKGKEVLVLWGIHHPSTSADQQSLYQNADAYVFVGSSRYSKKFKPEIAIRPKVRDQEGRMNYYWTLVEPGDKI
TFEATGNLVVPRYAFAMERNAGSGIIISDTPVHDCNTTCQTPKGAINTSLPFQNIHPITIGKCPKYVKSTKLRLATGLRN
VPSIQSR
;
18  ? 
2 UNP C5MQE6_9INFA C5MQE6 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 4EDA A 10 ? 336 ? C5MQE6 18  ? 344 ? 1 327 
2 2 4EDA B 1  ? 176 ? C5MQE6 345 ? 520 ? 1 176 
3 1 4EDA C 10 ? 336 ? C5MQE6 18  ? 344 ? 1 327 
4 2 4EDA D 1  ? 176 ? C5MQE6 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 4EDA ALA A 1   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -8  1  
1 4EDA ASP A 2   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -7  2  
1 4EDA PRO A 3   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -6  3  
1 4EDA GLY A 4   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -5  4  
1 4EDA TYR A 5   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -4  5  
1 4EDA LEU A 6   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -3  6  
1 4EDA LEU A 7   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -2  7  
1 4EDA GLU A 8   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -1  8  
1 4EDA PHE A 9   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' 0   9  
2 4EDA ARG B 177 ? UNP C5MQE6 ? ? 'EXPRESSION TAG' 177 10 
2 4EDA SER B 178 ? UNP C5MQE6 ? ? 'EXPRESSION TAG' 178 11 
2 4EDA LEU B 179 ? UNP C5MQE6 ? ? 'EXPRESSION TAG' 179 12 
2 4EDA VAL B 180 ? UNP C5MQE6 ? ? 'EXPRESSION TAG' 180 13 
2 4EDA PRO B 181 ? UNP C5MQE6 ? ? 'EXPRESSION TAG' 181 14 
2 4EDA ARG B 182 ? UNP C5MQE6 ? ? 'EXPRESSION TAG' 182 15 
3 4EDA ALA C 1   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -8  16 
3 4EDA ASP C 2   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -7  17 
3 4EDA PRO C 3   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -6  18 
3 4EDA GLY C 4   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -5  19 
3 4EDA TYR C 5   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -4  20 
3 4EDA LEU C 6   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -3  21 
3 4EDA LEU C 7   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -2  22 
3 4EDA GLU C 8   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' -1  23 
3 4EDA PHE C 9   ? UNP C5MQE6 ? ? 'EXPRESSION TAG' 0   24 
4 4EDA ARG D 177 ? UNP C5MQE6 ? ? 'EXPRESSION TAG' 177 25 
4 4EDA SER D 178 ? UNP C5MQE6 ? ? 'EXPRESSION TAG' 178 26 
4 4EDA LEU D 179 ? UNP C5MQE6 ? ? 'EXPRESSION TAG' 179 27 
4 4EDA VAL D 180 ? UNP C5MQE6 ? ? 'EXPRESSION TAG' 180 28 
4 4EDA PRO D 181 ? UNP C5MQE6 ? ? 'EXPRESSION TAG' 181 29 
4 4EDA ARG D 182 ? UNP C5MQE6 ? ? 'EXPRESSION TAG' 182 30 
# 
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 
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.crystals_number   1 
_exptl.entry_id          4EDA 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.pdbx_mosaicity        ? 
_exptl_crystal.pdbx_mosaicity_esd    ? 
_exptl_crystal.density_Matthews      3.53 
_exptl_crystal.density_diffrn        ? 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_meas_temp     ? 
_exptl_crystal.density_percent_sol   65.19 
_exptl_crystal.size_max              ? 
_exptl_crystal.size_mid              ? 
_exptl_crystal.size_min              ? 
_exptl_crystal.size_rad              ? 
_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.pH              7.5 
_exptl_crystal_grow.temp            277 
_exptl_crystal_grow.pdbx_details    
'100mM HEPES (pH7.5), 20% PEG 3350, 200mM sodium chloride, VAPOR DIFFUSION, HANGING DROP, temperature 277K' 
_exptl_crystal_grow.temp_details    ? 
_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                   'ADSC QUANTUM 315' 
_diffrn_detector.pdbx_collection_date   2011-06-18 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.98 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'PHOTON FACTORY BEAMLINE BL-17A' 
_diffrn_source.pdbx_wavelength_list        0.98 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
_diffrn_source.pdbx_synchrotron_beamline   BL-17A 
# 
_reflns.entry_id                     4EDA 
_reflns.observed_criterion_sigma_F   ? 
_reflns.observed_criterion_sigma_I   ? 
_reflns.d_resolution_high            2.7 
_reflns.d_resolution_low             50.0 
_reflns.number_all                   44988 
_reflns.number_obs                   44808 
_reflns.percent_possible_obs         99.6 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_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                  2.7 
_reflns_shell.d_res_low                   2.8 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.percent_possible_all        95.7 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.meanI_over_sigI_obs         ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_redundancy             ? 
_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_rejects                ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.number_possible             ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
# 
_refine.entry_id                                 4EDA 
_refine.ls_d_res_high                            2.7010 
_refine.ls_d_res_low                             49.9900 
_refine.pdbx_ls_sigma_F                          1.380 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.5100 
_refine.ls_number_reflns_obs                     44808 
_refine.ls_number_reflns_all                     45029 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2397 
_refine.ls_R_factor_R_work                       0.2373 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.2892 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 5.0500 
_refine.ls_number_reflns_R_free                  2265 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               86.5383 
_refine.solvent_model_param_bsol                 78.2470 
_refine.solvent_model_param_ksol                 0.3350 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            13.3152 
_refine.aniso_B[2][2]                            13.3152 
_refine.aniso_B[3][3]                            -26.6304 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            -0.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.2000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9500 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       TWIN_LSQ_F 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   0.7263 
_refine.B_iso_max                                163.250 
_refine.B_iso_min                                34.210 
_refine.pdbx_overall_phase_error                 34.0000 
_refine.occupancy_max                            1.000 
_refine.occupancy_min                            1.000 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_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        7050 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         112 
_refine_hist.number_atoms_solvent             63 
_refine_hist.number_atoms_total               7225 
_refine_hist.d_res_high                       2.7010 
_refine_hist.d_res_low                        49.9900 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
f_bond_d           7324 0.007  ? ? ? 'X-RAY DIFFRACTION' 
f_angle_d          9905 1.210  ? ? ? 'X-RAY DIFFRACTION' 
f_chiral_restr     1102 0.076  ? ? ? 'X-RAY DIFFRACTION' 
f_plane_restr      1263 0.005  ? ? ? 'X-RAY DIFFRACTION' 
f_dihedral_angle_d 2700 18.146 ? ? ? 'X-RAY DIFFRACTION' 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.redundancy_reflns_obs 
2.7023 2.7610  16 90.0000 2506 . 0.3205 0.3876 . 128 . 2634 . 'X-RAY DIFFRACTION' . 
2.7610 2.8252  16 93.0000 2574 . 0.3092 0.3288 . 146 . 2720 . 'X-RAY DIFFRACTION' . 
2.8252 2.8958  16 95.0000 2646 . 0.2988 0.3286 . 148 . 2794 . 'X-RAY DIFFRACTION' . 
2.8958 2.9741  16 95.0000 2642 . 0.2906 0.3259 . 150 . 2792 . 'X-RAY DIFFRACTION' . 
2.9741 3.0616  16 95.0000 2638 . 0.2732 0.2873 . 139 . 2777 . 'X-RAY DIFFRACTION' . 
3.0616 3.1604  16 96.0000 2692 . 0.2670 0.2999 . 126 . 2818 . 'X-RAY DIFFRACTION' . 
3.1604 3.2733  16 95.0000 2656 . 0.2575 0.3063 . 129 . 2785 . 'X-RAY DIFFRACTION' . 
3.2733 3.4043  16 95.0000 2631 . 0.2511 0.2980 . 150 . 2781 . 'X-RAY DIFFRACTION' . 
3.4043 3.5592  16 96.0000 2662 . 0.2388 0.3001 . 125 . 2787 . 'X-RAY DIFFRACTION' . 
3.5592 3.7467  16 95.0000 2682 . 0.2325 0.2621 . 140 . 2822 . 'X-RAY DIFFRACTION' . 
3.7467 3.9813  16 94.0000 2648 . 0.2249 0.2554 . 163 . 2811 . 'X-RAY DIFFRACTION' . 
3.9813 4.2884  16 94.0000 2648 . 0.2187 0.3134 . 160 . 2808 . 'X-RAY DIFFRACTION' . 
4.2884 4.7194  16 96.0000 2706 . 0.2113 0.2972 . 125 . 2831 . 'X-RAY DIFFRACTION' . 
4.7194 5.4010  16 95.0000 2691 . 0.2078 0.2663 . 139 . 2830 . 'X-RAY DIFFRACTION' . 
5.4010 6.7998  16 95.0000 2706 . 0.2418 0.2988 . 143 . 2849 . 'X-RAY DIFFRACTION' . 
6.7998 41.3553 16 95.0000 2791 . 0.2203 0.2700 . 149 . 2940 . 'X-RAY DIFFRACTION' . 
# 
_struct.entry_id                  4EDA 
_struct.title                     
;Structures of monomeric hemagglutinin and its complex with an Fab fragment of a neutralizing antibody that binds to H1 subtype influenza viruses: molecular basis of infectivity of 2009 pandemic H1N1 influenza A viruses
;
_struct.pdbx_descriptor           Hemagglutinin 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4EDA 
_struct_keywords.text            'influenza virus, haemagglutinin, conformation, antibody, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
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 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
P N N 4 ? 
# 
_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 65  ? GLY A 72  ? ASN A 56  GLY A 63  1 ? 8  
HELX_P HELX_P2  2  ASN A 73  ? GLU A 77  ? ASN A 64  GLU A 68  5 ? 5  
HELX_P HELX_P3  3  ASP A 106 ? LEU A 114 ? ASP A 97  LEU A 105 1 ? 9  
HELX_P HELX_P4  4  THR A 193 ? GLN A 202 ? THR A 184 GLN A 193 1 ? 10 
HELX_P HELX_P5  5  LEU B 38  ? ASN B 60  ? LEU B 38  ASN B 60  1 ? 23 
HELX_P HELX_P6  6  ASP B 85  ? LYS B 127 ? ASP B 85  LYS B 127 1 ? 43 
HELX_P HELX_P7  7  CYS B 148 ? GLY B 155 ? CYS B 148 GLY B 155 1 ? 8  
HELX_P HELX_P8  8  ASP B 158 ? ASP B 174 ? ASP B 158 ASP B 174 1 ? 17 
HELX_P HELX_P9  9  ASN C 65  ? GLY C 72  ? ASN C 56  GLY C 63  1 ? 8  
HELX_P HELX_P10 10 ASN C 73  ? GLU C 77  ? ASN C 64  GLU C 68  5 ? 5  
HELX_P HELX_P11 11 ASP C 106 ? LEU C 114 ? ASP C 97  LEU C 105 1 ? 9  
HELX_P HELX_P12 12 PRO C 127 ? TRP C 132 ? PRO C 118 TRP C 123 1 ? 6  
HELX_P HELX_P13 13 THR C 193 ? GLN C 202 ? THR C 184 GLN C 193 1 ? 10 
HELX_P HELX_P14 14 LEU D 38  ? LYS D 58  ? LEU D 38  LYS D 58  1 ? 21 
HELX_P HELX_P15 15 ASP D 85  ? VAL D 115 ? ASP D 85  VAL D 115 1 ? 31 
HELX_P HELX_P16 16 LEU D 118 ? ARG D 123 ? LEU D 118 ARG D 123 1 ? 6  
HELX_P HELX_P17 17 ASN D 146 ? GLU D 150 ? ASN D 146 GLU D 150 5 ? 5  
HELX_P HELX_P18 18 LYS D 161 ? ALA D 166 ? LYS D 161 ALA D 166 1 ? 6  
HELX_P HELX_P19 19 LYS D 167 ? ARG D 170 ? LYS D 167 ARG D 170 5 ? 4  
# 
_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 13  SG  ? ? ? 1_555 B CYS 137 SG ? ? A CYS 4   B CYS 137 1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf2  disulf ? ? A CYS 51  SG  ? ? ? 1_555 A CYS 284 SG ? ? A CYS 42  A CYS 275 1_555 ? ? ? ? ? ? ? 2.052 ? 
disulf3  disulf ? ? A CYS 64  SG  ? ? ? 1_555 A CYS 76  SG ? ? A CYS 55  A CYS 67  1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf4  disulf ? ? A CYS 99  SG  ? ? ? 1_555 A CYS 145 SG ? ? A CYS 90  A CYS 136 1_555 ? ? ? ? ? ? ? 2.073 ? 
disulf5  disulf ? ? A CYS 288 SG  ? ? ? 1_555 A CYS 312 SG ? ? A CYS 279 A CYS 303 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf6  disulf ? ? B CYS 144 SG  ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf7  disulf ? ? C CYS 51  SG  ? ? ? 1_555 C CYS 284 SG ? ? C CYS 42  C CYS 275 1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf8  disulf ? ? C CYS 64  SG  ? ? ? 1_555 C CYS 76  SG ? ? C CYS 55  C CYS 67  1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf9  disulf ? ? C CYS 99  SG  ? ? ? 1_555 C CYS 145 SG ? ? C CYS 90  C CYS 136 1_555 ? ? ? ? ? ? ? 2.057 ? 
disulf10 disulf ? ? C CYS 288 SG  ? ? ? 1_555 C CYS 312 SG ? ? C CYS 279 C CYS 303 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf11 disulf ? ? D CYS 144 SG  ? ? ? 1_555 D CYS 148 SG ? ? D CYS 144 D CYS 148 1_555 ? ? ? ? ? ? ? 2.032 ? 
covale1  covale ? ? A ASN 96  ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 87  A NAG 401 1_555 ? ? ? ? ? ? ? 1.404 ? 
covale2  covale ? ? A ASN 296 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 287 A NAG 404 1_555 ? ? ? ? ? ? ? 1.404 ? 
covale3  covale ? ? C ASN 296 ND2 ? ? ? 1_555 L NAG .   C1 ? ? C ASN 287 C NAG 404 1_555 ? ? ? ? ? ? ? 1.411 ? 
covale4  covale ? ? C ASN 96  ND2 ? ? ? 1_555 I NAG .   C1 ? ? C ASN 87  C NAG 401 1_555 ? ? ? ? ? ? ? 1.419 ? 
covale5  covale ? ? A ASN 285 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 276 A NAG 403 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale6  covale ? ? C ASN 285 ND2 ? ? ? 1_555 K NAG .   C1 ? ? C ASN 276 C NAG 403 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale7  covale ? ? E NAG .   O4  ? ? ? 1_555 F NAG .   C1 ? ? A NAG 401 A NAG 402 1_555 ? ? ? ? ? ? ? 1.481 ? 
covale8  covale ? ? I NAG .   O4  ? ? ? 1_555 J NAG .   C1 ? ? C NAG 401 C NAG 402 1_555 ? ? ? ? ? ? ? 1.624 ? 
# 
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 ? 3 ? 
B ? 2 ? 
C ? 2 ? 
D ? 2 ? 
E ? 3 ? 
F ? 5 ? 
G ? 4 ? 
H ? 2 ? 
I ? 2 ? 
J ? 4 ? 
K ? 3 ? 
L ? 2 ? 
M ? 3 ? 
N ? 2 ? 
O ? 3 ? 
P ? 5 ? 
Q ? 4 ? 
R ? 2 ? 
S ? 2 ? 
T ? 4 ? 
U ? 3 ? 
# 
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 ? anti-parallel 
A 2 3 ? anti-parallel 
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
D 1 2 ? parallel      
E 1 2 ? parallel      
E 2 3 ? parallel      
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
F 4 5 ? anti-parallel 
G 1 2 ? anti-parallel 
G 2 3 ? anti-parallel 
G 3 4 ? anti-parallel 
H 1 2 ? anti-parallel 
I 1 2 ? anti-parallel 
J 1 2 ? anti-parallel 
J 2 3 ? anti-parallel 
J 3 4 ? anti-parallel 
K 1 2 ? anti-parallel 
K 2 3 ? anti-parallel 
L 1 2 ? parallel      
M 1 2 ? parallel      
M 2 3 ? parallel      
N 1 2 ? parallel      
O 1 2 ? parallel      
O 2 3 ? parallel      
P 1 2 ? anti-parallel 
P 2 3 ? anti-parallel 
P 3 4 ? anti-parallel 
P 4 5 ? anti-parallel 
Q 1 2 ? anti-parallel 
Q 2 3 ? anti-parallel 
Q 3 4 ? anti-parallel 
R 1 2 ? anti-parallel 
S 1 2 ? anti-parallel 
T 1 2 ? anti-parallel 
T 2 3 ? anti-parallel 
T 3 4 ? anti-parallel 
U 1 2 ? anti-parallel 
U 2 3 ? 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 THR A 11  ? LEU A 12  ? THR A 2   LEU A 3   
A 2 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 
A 3 ALA B 130 ? GLY B 134 ? ALA B 130 GLY B 134 
B 1 GLY A 15  ? TYR A 16  ? GLY A 6   TYR A 7   
B 2 TYR B 22  ? GLY B 23  ? TYR B 22  GLY B 23  
C 1 VAL A 39  ? ASN A 40  ? VAL A 30  ASN A 31  
C 2 ARG A 322 ? LEU A 323 ? ARG A 313 LEU A 314 
D 1 LEU A 50  ? LEU A 53  ? LEU A 41  LEU A 44  
D 2 VAL A 281 ? THR A 286 ? VAL A 272 THR A 277 
E 1 LEU A 59  ? LEU A 61  ? LEU A 50  LEU A 52  
E 2 ILE A 88  ? GLU A 90  ? ILE A 79  GLU A 81  
E 3 ILE A 274 ? ILE A 276 ? ILE A 265 ILE A 267 
F 1 VAL A 117 ? GLU A 124 ? VAL A 108 GLU A 115 
F 2 TYR A 262 ? ARG A 268 ? TYR A 253 ARG A 259 
F 3 GLU A 181 ? HIS A 190 ? GLU A 172 HIS A 181 
F 4 LEU A 257 ? PRO A 260 ? LEU A 248 PRO A 251 
F 5 LEU A 157 ? TRP A 159 ? LEU A 148 TRP A 150 
G 1 VAL A 117 ? GLU A 124 ? VAL A 108 GLU A 115 
G 2 TYR A 262 ? ARG A 268 ? TYR A 253 ARG A 259 
G 3 GLU A 181 ? HIS A 190 ? GLU A 172 HIS A 181 
G 4 ARG A 235 ? VAL A 243 ? ARG A 226 VAL A 234 
H 1 HIS A 135 ? ASP A 136 ? HIS A 126 ASP A 127 
H 2 VAL A 161 ? LYS A 162 ? VAL A 152 LYS A 153 
I 1 THR A 142 ? HIS A 147 ? THR A 133 HIS A 138 
I 2 ALA A 150 ? SER A 152 ? ALA A 141 SER A 143 
J 1 LEU A 170 ? ILE A 175 ? LEU A 161 ILE A 166 
J 2 LYS A 248 ? ALA A 253 ? LYS A 239 ALA A 244 
J 3 VAL A 208 ? GLY A 211 ? VAL A 199 GLY A 202 
J 4 SER A 216 ? PHE A 219 ? SER A 207 PHE A 210 
K 1 ALA A 294 ? ILE A 295 ? ALA A 285 ILE A 286 
K 2 CYS A 288 ? GLN A 289 ? CYS A 279 GLN A 280 
K 3 ILE A 309 ? GLY A 310 ? ILE A 300 GLY A 301 
L 1 PHE A 301 ? GLN A 302 ? PHE A 292 GLN A 293 
L 2 LYS A 314 ? TYR A 315 ? LYS A 305 TYR A 306 
M 1 LEU C 42  ? GLU C 43  ? LEU C 33  GLU C 34  
M 2 PHE C 301 ? GLN C 302 ? PHE C 292 GLN C 293 
M 3 LYS C 314 ? TYR C 315 ? LYS C 305 TYR C 306 
N 1 LEU C 50  ? LEU C 53  ? LEU C 41  LEU C 44  
N 2 VAL C 281 ? THR C 286 ? VAL C 272 THR C 277 
O 1 LEU C 59  ? HIS C 60  ? LEU C 50  HIS C 51  
O 2 ILE C 88  ? GLU C 90  ? ILE C 79  GLU C 81  
O 3 ILE C 274 ? ILE C 276 ? ILE C 265 ILE C 267 
P 1 VAL C 117 ? GLU C 124 ? VAL C 108 GLU C 115 
P 2 TYR C 262 ? ARG C 268 ? TYR C 253 ARG C 259 
P 3 GLU C 181 ? HIS C 190 ? GLU C 172 HIS C 181 
P 4 LEU C 257 ? PRO C 260 ? LEU C 248 PRO C 251 
P 5 LEU C 157 ? TRP C 159 ? LEU C 148 TRP C 150 
Q 1 VAL C 117 ? GLU C 124 ? VAL C 108 GLU C 115 
Q 2 TYR C 262 ? ARG C 268 ? TYR C 253 ARG C 259 
Q 3 GLU C 181 ? HIS C 190 ? GLU C 172 HIS C 181 
Q 4 ARG C 235 ? VAL C 243 ? ARG C 226 VAL C 234 
R 1 HIS C 135 ? ASP C 136 ? HIS C 126 ASP C 127 
R 2 VAL C 161 ? LYS C 162 ? VAL C 152 LYS C 153 
S 1 THR C 142 ? PRO C 146 ? THR C 133 PRO C 137 
S 2 LYS C 151 ? SER C 152 ? LYS C 142 SER C 143 
T 1 LEU C 170 ? ILE C 175 ? LEU C 161 ILE C 166 
T 2 LYS C 248 ? ALA C 253 ? LYS C 239 ALA C 244 
T 3 VAL C 208 ? GLY C 211 ? VAL C 199 GLY C 202 
T 4 SER C 216 ? PHE C 219 ? SER C 207 PHE C 210 
U 1 ALA C 294 ? ILE C 295 ? ALA C 285 ILE C 286 
U 2 CYS C 288 ? GLN C 289 ? CYS C 279 GLN C 280 
U 3 ILE C 309 ? GLY C 310 ? ILE C 300 GLY C 301 
# 
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 N LEU A 12  ? N LEU A 3   O PHE B 138 ? O PHE B 138 
A 2 3 O CYS B 137 ? O CYS B 137 N GLY B 134 ? N GLY B 134 
B 1 2 N GLY A 15  ? N GLY A 6   O GLY B 23  ? O GLY B 23  
C 1 2 N VAL A 39  ? N VAL A 30  O LEU A 323 ? O LEU A 314 
D 1 2 N LYS A 52  ? N LYS A 43  O CYS A 284 ? O CYS A 275 
E 1 2 N LEU A 59  ? N LEU A 50  O VAL A 89  ? O VAL A 80  
E 2 3 N ILE A 88  ? N ILE A 79  O ILE A 275 ? O ILE A 266 
F 1 2 N GLU A 121 ? N GLU A 112 O ALA A 265 ? O ALA A 256 
F 2 3 O PHE A 264 ? O PHE A 255 N LEU A 183 ? N LEU A 174 
F 3 4 N GLY A 187 ? N GLY A 178 O VAL A 258 ? O VAL A 249 
F 4 5 O VAL A 259 ? O VAL A 250 N ILE A 158 ? N ILE A 149 
G 1 2 N GLU A 121 ? N GLU A 112 O ALA A 265 ? O ALA A 256 
G 2 3 O PHE A 264 ? O PHE A 255 N LEU A 183 ? N LEU A 174 
G 3 4 N TRP A 186 ? N TRP A 177 O TYR A 239 ? O TYR A 230 
H 1 2 N ASP A 136 ? N ASP A 127 O VAL A 161 ? O VAL A 152 
I 1 2 N HIS A 147 ? N HIS A 138 O ALA A 150 ? O ALA A 141 
J 1 2 N TYR A 174 ? N TYR A 165 O ILE A 249 ? O ILE A 240 
J 2 3 O GLU A 252 ? O GLU A 243 N PHE A 209 ? N PHE A 200 
J 3 4 N VAL A 208 ? N VAL A 199 O PHE A 219 ? O PHE A 210 
K 1 2 O ILE A 295 ? O ILE A 286 N CYS A 288 ? N CYS A 279 
K 2 3 N GLN A 289 ? N GLN A 280 O ILE A 309 ? O ILE A 300 
L 1 2 N GLN A 302 ? N GLN A 293 O LYS A 314 ? O LYS A 305 
M 1 2 N GLU C 43  ? N GLU C 34  O PHE C 301 ? O PHE C 292 
M 2 3 N GLN C 302 ? N GLN C 293 O LYS C 314 ? O LYS C 305 
N 1 2 N LEU C 50  ? N LEU C 41  O HIS C 282 ? O HIS C 273 
O 1 2 N LEU C 59  ? N LEU C 50  O VAL C 89  ? O VAL C 80  
O 2 3 N GLU C 90  ? N GLU C 81  O ILE C 275 ? O ILE C 266 
P 1 2 N GLU C 121 ? N GLU C 112 O ALA C 265 ? O ALA C 256 
P 2 3 O PHE C 264 ? O PHE C 255 N LEU C 183 ? N LEU C 174 
P 3 4 N GLY C 187 ? N GLY C 178 O VAL C 258 ? O VAL C 249 
P 4 5 O VAL C 259 ? O VAL C 250 N ILE C 158 ? N ILE C 149 
Q 1 2 N GLU C 121 ? N GLU C 112 O ALA C 265 ? O ALA C 256 
Q 2 3 O PHE C 264 ? O PHE C 255 N LEU C 183 ? N LEU C 174 
Q 3 4 N HIS C 190 ? N HIS C 181 O ARG C 235 ? O ARG C 226 
R 1 2 N ASP C 136 ? N ASP C 127 O VAL C 161 ? O VAL C 152 
S 1 2 N THR C 142 ? N THR C 133 O SER C 152 ? O SER C 143 
T 1 2 N TYR C 174 ? N TYR C 165 O ILE C 249 ? O ILE C 240 
T 2 3 O GLU C 252 ? O GLU C 243 N PHE C 209 ? N PHE C 200 
T 3 4 N VAL C 208 ? N VAL C 199 O PHE C 219 ? O PHE C 210 
U 1 2 O ILE C 295 ? O ILE C 286 N CYS C 288 ? N CYS C 279 
U 2 3 N GLN C 289 ? N GLN C 280 O ILE C 309 ? O ILE C 300 
# 
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 ? ? ? ? 6 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 87 RESIDUES 401 TO 402' 
AC2 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A 403 BOUND TO ASN A 276'           
AC3 Software ? ? ? ? 1 'BINDING SITE FOR MONO-SACCHARIDE NAG A 404 BOUND TO ASN A 287'           
AC4 Software ? ? ? ? 6 'BINDING SITE FOR CHAIN C OF SUGAR BOUND TO ASN C 87 RESIDUES 401 TO 402' 
AC5 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG C 403 BOUND TO ASN C 276'           
AC6 Software ? ? ? ? 1 'BINDING SITE FOR MONO-SACCHARIDE NAG C 404 BOUND TO ASN C 287'           
# 
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 6 ASN A 73  ? ASN A 64  . ? 1_555 ? 
2  AC1 6 GLU A 75  ? GLU A 66  . ? 1_555 ? 
3  AC1 6 ASP A 95  ? ASP A 86  . ? 1_555 ? 
4  AC1 6 ASN A 96  ? ASN A 87  . ? 1_555 ? 
5  AC1 6 CYS A 99  ? CYS A 90  . ? 1_555 ? 
6  AC1 6 ARG A 230 ? ARG A 221 . ? 1_555 ? 
7  AC2 2 ARG A 54  ? ARG A 45  . ? 1_555 ? 
8  AC2 2 ASN A 285 ? ASN A 276 . ? 1_555 ? 
9  AC3 1 ASN A 296 ? ASN A 287 . ? 1_555 ? 
10 AC4 6 ASN C 73  ? ASN C 64  . ? 1_555 ? 
11 AC4 6 ASP C 95  ? ASP C 86  . ? 1_555 ? 
12 AC4 6 ASN C 96  ? ASN C 87  . ? 1_555 ? 
13 AC4 6 CYS C 99  ? CYS C 90  . ? 1_555 ? 
14 AC4 6 ARG C 230 ? ARG C 221 . ? 1_555 ? 
15 AC4 6 HOH O .   ? HOH C 514 . ? 1_555 ? 
16 AC5 3 ARG C 54  ? ARG C 45  . ? 1_555 ? 
17 AC5 3 GLY C 55  ? GLY C 46  . ? 1_555 ? 
18 AC5 3 ASN C 285 ? ASN C 276 . ? 1_555 ? 
19 AC6 1 ASN C 296 ? ASN C 287 . ? 1_555 ? 
# 
_atom_sites.entry_id                    4EDA 
_atom_sites.fract_transf_matrix[1][1]   0.004805 
_atom_sites.fract_transf_matrix[1][2]   0.002774 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005548 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_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]   0.015206 
_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 10  ? -31.024 -124.935 -3.769  1.00 110.64 ? 1   ASP A N   1 
ATOM   2    C CA  . ASP A 1 10  ? -31.705 -123.987 -4.645  1.00 113.16 ? 1   ASP A CA  1 
ATOM   3    C C   . ASP A 1 10  ? -31.917 -122.638 -3.958  1.00 115.46 ? 1   ASP A C   1 
ATOM   4    O O   . ASP A 1 10  ? -33.046 -122.169 -3.827  1.00 113.58 ? 1   ASP A O   1 
ATOM   5    C CB  . ASP A 1 10  ? -33.049 -124.553 -5.089  1.00 112.43 ? 1   ASP A CB  1 
ATOM   6    C CG  . ASP A 1 10  ? -33.292 -124.363 -6.565  1.00 117.38 ? 1   ASP A CG  1 
ATOM   7    O OD1 . ASP A 1 10  ? -32.405 -124.738 -7.361  1.00 119.57 ? 1   ASP A OD1 1 
ATOM   8    O OD2 . ASP A 1 10  ? -34.359 -123.827 -6.930  1.00 116.14 ? 1   ASP A OD2 1 
ATOM   9    N N   . THR A 1 11  ? -30.818 -122.027 -3.524  1.00 117.71 ? 2   THR A N   1 
ATOM   10   C CA  . THR A 1 11  ? -30.839 -120.818 -2.694  1.00 114.53 ? 2   THR A CA  1 
ATOM   11   C C   . THR A 1 11  ? -31.070 -119.471 -3.387  1.00 113.08 ? 2   THR A C   1 
ATOM   12   O O   . THR A 1 11  ? -30.857 -119.316 -4.590  1.00 112.76 ? 2   THR A O   1 
ATOM   13   C CB  . THR A 1 11  ? -29.537 -120.672 -1.887  1.00 112.79 ? 2   THR A CB  1 
ATOM   14   O OG1 . THR A 1 11  ? -28.528 -120.078 -2.714  1.00 113.64 ? 2   THR A OG1 1 
ATOM   15   C CG2 . THR A 1 11  ? -29.064 -122.026 -1.379  1.00 114.24 ? 2   THR A CG2 1 
ATOM   16   N N   . LEU A 1 12  ? -31.510 -118.504 -2.586  1.00 113.41 ? 3   LEU A N   1 
ATOM   17   C CA  . LEU A 1 12  ? -31.430 -117.085 -2.922  1.00 111.76 ? 3   LEU A CA  1 
ATOM   18   C C   . LEU A 1 12  ? -30.943 -116.318 -1.690  1.00 109.30 ? 3   LEU A C   1 
ATOM   19   O O   . LEU A 1 12  ? -31.522 -116.432 -0.608  1.00 108.98 ? 3   LEU A O   1 
ATOM   20   C CB  . LEU A 1 12  ? -32.784 -116.551 -3.384  1.00 110.26 ? 3   LEU A CB  1 
ATOM   21   C CG  . LEU A 1 12  ? -32.829 -115.075 -3.773  1.00 109.81 ? 3   LEU A CG  1 
ATOM   22   C CD1 . LEU A 1 12  ? -31.693 -114.755 -4.725  1.00 112.58 ? 3   LEU A CD1 1 
ATOM   23   C CD2 . LEU A 1 12  ? -34.173 -114.723 -4.392  1.00 107.95 ? 3   LEU A CD2 1 
ATOM   24   N N   . CYS A 1 13  ? -29.876 -115.543 -1.852  1.00 110.35 ? 4   CYS A N   1 
ATOM   25   C CA  . CYS A 1 13  ? -29.264 -114.847 -0.722  1.00 111.13 ? 4   CYS A CA  1 
ATOM   26   C C   . CYS A 1 13  ? -29.284 -113.327 -0.853  1.00 110.38 ? 4   CYS A C   1 
ATOM   27   O O   . CYS A 1 13  ? -29.794 -112.783 -1.830  1.00 110.11 ? 4   CYS A O   1 
ATOM   28   C CB  . CYS A 1 13  ? -27.831 -115.336 -0.508  1.00 110.84 ? 4   CYS A CB  1 
ATOM   29   S SG  . CYS A 1 13  ? -27.722 -116.853 0.459   1.00 113.13 ? 4   CYS A SG  1 
ATOM   30   N N   . ILE A 1 14  ? -28.727 -112.646 0.144   1.00 111.33 ? 5   ILE A N   1 
ATOM   31   C CA  . ILE A 1 14  ? -28.639 -111.187 0.123   1.00 113.04 ? 5   ILE A CA  1 
ATOM   32   C C   . ILE A 1 14  ? -27.312 -110.677 0.698   1.00 113.44 ? 5   ILE A C   1 
ATOM   33   O O   . ILE A 1 14  ? -26.846 -111.139 1.741   1.00 111.16 ? 5   ILE A O   1 
ATOM   34   C CB  . ILE A 1 14  ? -29.827 -110.539 0.861   1.00 111.43 ? 5   ILE A CB  1 
ATOM   35   C CG1 . ILE A 1 14  ? -31.140 -110.854 0.138   1.00 108.31 ? 5   ILE A CG1 1 
ATOM   36   C CG2 . ILE A 1 14  ? -29.621 -109.040 0.990   1.00 110.32 ? 5   ILE A CG2 1 
ATOM   37   C CD1 . ILE A 1 14  ? -32.367 -110.281 0.814   1.00 106.49 ? 5   ILE A CD1 1 
ATOM   38   N N   . GLY A 1 15  ? -26.709 -109.720 0.000   1.00 115.31 ? 6   GLY A N   1 
ATOM   39   C CA  . GLY A 1 15  ? -25.407 -109.197 0.370   1.00 119.38 ? 6   GLY A CA  1 
ATOM   40   C C   . GLY A 1 15  ? -25.159 -107.851 -0.286  1.00 122.71 ? 6   GLY A C   1 
ATOM   41   O O   . GLY A 1 15  ? -26.061 -107.288 -0.914  1.00 120.38 ? 6   GLY A O   1 
ATOM   42   N N   . TYR A 1 16  ? -23.938 -107.334 -0.153  1.00 124.76 ? 7   TYR A N   1 
ATOM   43   C CA  . TYR A 1 16  ? -23.625 -105.984 -0.631  1.00 126.55 ? 7   TYR A CA  1 
ATOM   44   C C   . TYR A 1 16  ? -22.219 -105.846 -1.218  1.00 127.62 ? 7   TYR A C   1 
ATOM   45   O O   . TYR A 1 16  ? -21.478 -106.823 -1.332  1.00 126.17 ? 7   TYR A O   1 
ATOM   46   C CB  . TYR A 1 16  ? -23.806 -104.971 0.498   1.00 123.88 ? 7   TYR A CB  1 
ATOM   47   C CG  . TYR A 1 16  ? -23.184 -105.436 1.784   1.00 124.77 ? 7   TYR A CG  1 
ATOM   48   C CD1 . TYR A 1 16  ? -21.851 -105.180 2.065   1.00 127.34 ? 7   TYR A CD1 1 
ATOM   49   C CD2 . TYR A 1 16  ? -23.922 -106.157 2.712   1.00 124.70 ? 7   TYR A CD2 1 
ATOM   50   C CE1 . TYR A 1 16  ? -21.271 -105.615 3.247   1.00 126.49 ? 7   TYR A CE1 1 
ATOM   51   C CE2 . TYR A 1 16  ? -23.353 -106.598 3.894   1.00 125.73 ? 7   TYR A CE2 1 
ATOM   52   C CZ  . TYR A 1 16  ? -22.029 -106.326 4.157   1.00 124.45 ? 7   TYR A CZ  1 
ATOM   53   O OH  . TYR A 1 16  ? -21.468 -106.768 5.334   1.00 123.67 ? 7   TYR A OH  1 
ATOM   54   N N   . HIS A 1 17  ? -21.864 -104.611 -1.568  1.00 129.55 ? 8   HIS A N   1 
ATOM   55   C CA  . HIS A 1 17  ? -20.613 -104.309 -2.259  1.00 128.00 ? 8   HIS A CA  1 
ATOM   56   C C   . HIS A 1 17  ? -19.443 -104.074 -1.300  1.00 128.45 ? 8   HIS A C   1 
ATOM   57   O O   . HIS A 1 17  ? -19.572 -103.344 -0.315  1.00 128.18 ? 8   HIS A O   1 
ATOM   58   C CB  . HIS A 1 17  ? -20.797 -103.071 -3.143  1.00 125.75 ? 8   HIS A CB  1 
ATOM   59   C CG  . HIS A 1 17  ? -19.727 -102.896 -4.176  1.00 125.96 ? 8   HIS A CG  1 
ATOM   60   N ND1 . HIS A 1 17  ? -18.390 -102.784 -3.858  1.00 125.69 ? 8   HIS A ND1 1 
ATOM   61   C CD2 . HIS A 1 17  ? -19.800 -102.809 -5.525  1.00 125.92 ? 8   HIS A CD2 1 
ATOM   62   C CE1 . HIS A 1 17  ? -17.687 -102.641 -4.967  1.00 125.58 ? 8   HIS A CE1 1 
ATOM   63   N NE2 . HIS A 1 17  ? -18.519 -102.652 -5.992  1.00 125.07 ? 8   HIS A NE2 1 
ATOM   64   N N   . ALA A 1 18  ? -18.308 -104.710 -1.584  1.00 128.70 ? 9   ALA A N   1 
ATOM   65   C CA  . ALA A 1 18  ? -17.048 -104.372 -0.925  1.00 128.78 ? 9   ALA A CA  1 
ATOM   66   C C   . ALA A 1 18  ? -16.078 -103.840 -1.974  1.00 127.84 ? 9   ALA A C   1 
ATOM   67   O O   . ALA A 1 18  ? -15.589 -104.588 -2.819  1.00 127.48 ? 9   ALA A O   1 
ATOM   68   C CB  . ALA A 1 18  ? -16.466 -105.579 -0.219  1.00 127.82 ? 9   ALA A CB  1 
ATOM   69   N N   . ASN A 1 19  ? -15.801 -102.544 -1.919  1.00 127.01 ? 10  ASN A N   1 
ATOM   70   C CA  . ASN A 1 19  ? -15.113 -101.890 -3.023  1.00 124.60 ? 10  ASN A CA  1 
ATOM   71   C C   . ASN A 1 19  ? -13.599 -102.043 -3.056  1.00 124.13 ? 10  ASN A C   1 
ATOM   72   O O   . ASN A 1 19  ? -12.956 -102.265 -2.031  1.00 123.64 ? 10  ASN A O   1 
ATOM   73   C CB  . ASN A 1 19  ? -15.496 -100.414 -3.100  1.00 123.91 ? 10  ASN A CB  1 
ATOM   74   C CG  . ASN A 1 19  ? -15.724 -99.955  -4.522  1.00 123.34 ? 10  ASN A CG  1 
ATOM   75   O OD1 . ASN A 1 19  ? -15.251 -100.579 -5.471  1.00 122.26 ? 10  ASN A OD1 1 
ATOM   76   N ND2 . ASN A 1 19  ? -16.451 -98.862  -4.678  1.00 122.95 ? 10  ASN A ND2 1 
ATOM   77   N N   . ASN A 1 20  ? -13.039 -101.921 -4.254  1.00 124.45 ? 11  ASN A N   1 
ATOM   78   C CA  . ASN A 1 20  ? -11.597 -101.813 -4.407  1.00 124.77 ? 11  ASN A CA  1 
ATOM   79   C C   . ASN A 1 20  ? -11.088 -100.534 -3.734  1.00 126.97 ? 11  ASN A C   1 
ATOM   80   O O   . ASN A 1 20  ? -9.907  -100.430 -3.395  1.00 128.19 ? 11  ASN A O   1 
ATOM   81   C CB  . ASN A 1 20  ? -11.208 -101.831 -5.891  1.00 123.16 ? 11  ASN A CB  1 
ATOM   82   C CG  . ASN A 1 20  ? -11.693 -100.598 -6.644  1.00 121.60 ? 11  ASN A CG  1 
ATOM   83   O OD1 . ASN A 1 20  ? -12.731 -100.018 -6.315  1.00 119.80 ? 11  ASN A OD1 1 
ATOM   84   N ND2 . ASN A 1 20  ? -10.938 -100.194 -7.661  1.00 120.70 ? 11  ASN A ND2 1 
ATOM   85   N N   . SER A 1 21  ? -11.998 -99.579  -3.530  1.00 126.69 ? 12  SER A N   1 
ATOM   86   C CA  . SER A 1 21  ? -11.660 -98.249  -3.007  1.00 125.61 ? 12  SER A CA  1 
ATOM   87   C C   . SER A 1 21  ? -11.441 -98.239  -1.493  1.00 122.91 ? 12  SER A C   1 
ATOM   88   O O   . SER A 1 21  ? -12.277 -98.722  -0.726  1.00 120.93 ? 12  SER A O   1 
ATOM   89   C CB  . SER A 1 21  ? -12.725 -97.219  -3.408  1.00 124.80 ? 12  SER A CB  1 
ATOM   90   O OG  . SER A 1 21  ? -13.219 -96.518  -2.277  1.00 124.69 ? 12  SER A OG  1 
ATOM   91   N N   . THR A 1 22  ? -10.294 -97.703  -1.082  1.00 121.91 ? 13  THR A N   1 
ATOM   92   C CA  . THR A 1 22  ? -9.846  -97.781  0.305   1.00 120.43 ? 13  THR A CA  1 
ATOM   93   C C   . THR A 1 22  ? -10.054 -96.562  1.212   1.00 120.27 ? 13  THR A C   1 
ATOM   94   O O   . THR A 1 22  ? -9.750  -96.635  2.404   1.00 118.76 ? 13  THR A O   1 
ATOM   95   C CB  . THR A 1 22  ? -8.353  -98.108  0.359   1.00 119.77 ? 13  THR A CB  1 
ATOM   96   O OG1 . THR A 1 22  ? -7.881  -97.919  1.698   1.00 120.47 ? 13  THR A OG1 1 
ATOM   97   C CG2 . THR A 1 22  ? -7.582  -97.186  -0.580  1.00 117.82 ? 13  THR A CG2 1 
ATOM   98   N N   . ASP A 1 23  ? -10.553 -95.452  0.678   1.00 119.09 ? 14  ASP A N   1 
ATOM   99   C CA  . ASP A 1 23  ? -10.575 -94.215  1.462   1.00 117.05 ? 14  ASP A CA  1 
ATOM   100  C C   . ASP A 1 23  ? -11.508 -94.286  2.674   1.00 116.36 ? 14  ASP A C   1 
ATOM   101  O O   . ASP A 1 23  ? -12.688 -94.610  2.544   1.00 116.09 ? 14  ASP A O   1 
ATOM   102  C CB  . ASP A 1 23  ? -10.930 -93.020  0.585   1.00 115.15 ? 14  ASP A CB  1 
ATOM   103  C CG  . ASP A 1 23  ? -12.281 -93.159  -0.060  1.00 116.21 ? 14  ASP A CG  1 
ATOM   104  O OD1 . ASP A 1 23  ? -13.299 -92.968  0.639   1.00 115.77 ? 14  ASP A OD1 1 
ATOM   105  O OD2 . ASP A 1 23  ? -12.321 -93.458  -1.270  1.00 117.64 ? 14  ASP A OD2 1 
ATOM   106  N N   . THR A 1 24  ? -10.977 -93.951  3.848   1.00 116.01 ? 15  THR A N   1 
ATOM   107  C CA  . THR A 1 24  ? -11.728 -94.070  5.097   1.00 116.33 ? 15  THR A CA  1 
ATOM   108  C C   . THR A 1 24  ? -12.310 -92.731  5.541   1.00 115.86 ? 15  THR A C   1 
ATOM   109  O O   . THR A 1 24  ? -11.731 -91.672  5.293   1.00 115.13 ? 15  THR A O   1 
ATOM   110  C CB  . THR A 1 24  ? -10.861 -94.631  6.253   1.00 115.09 ? 15  THR A CB  1 
ATOM   111  O OG1 . THR A 1 24  ? -10.043 -93.589  6.801   1.00 114.10 ? 15  THR A OG1 1 
ATOM   112  C CG2 . THR A 1 24  ? -9.980  -95.774  5.772   1.00 114.50 ? 15  THR A CG2 1 
ATOM   113  N N   . VAL A 1 25  ? -13.469 -92.787  6.189   1.00 115.45 ? 16  VAL A N   1 
ATOM   114  C CA  . VAL A 1 25  ? -14.116 -91.589  6.707   1.00 113.89 ? 16  VAL A CA  1 
ATOM   115  C C   . VAL A 1 25  ? -14.401 -91.746  8.194   1.00 113.67 ? 16  VAL A C   1 
ATOM   116  O O   . VAL A 1 25  ? -13.957 -92.714  8.814   1.00 114.22 ? 16  VAL A O   1 
ATOM   117  C CB  . VAL A 1 25  ? -15.412 -91.292  5.956   1.00 113.73 ? 16  VAL A CB  1 
ATOM   118  C CG1 . VAL A 1 25  ? -15.150 -91.336  4.463   1.00 114.46 ? 16  VAL A CG1 1 
ATOM   119  C CG2 . VAL A 1 25  ? -16.484 -92.298  6.337   1.00 114.33 ? 16  VAL A CG2 1 
ATOM   120  N N   . ASP A 1 26  ? -15.122 -90.786  8.767   1.00 114.29 ? 17  ASP A N   1 
ATOM   121  C CA  . ASP A 1 26  ? -15.395 -90.801  10.202  1.00 116.10 ? 17  ASP A CA  1 
ATOM   122  C C   . ASP A 1 26  ? -16.882 -90.779  10.573  1.00 114.83 ? 17  ASP A C   1 
ATOM   123  O O   . ASP A 1 26  ? -17.707 -90.176  9.883   1.00 111.78 ? 17  ASP A O   1 
ATOM   124  C CB  . ASP A 1 26  ? -14.659 -89.653  10.903  1.00 117.95 ? 17  ASP A CB  1 
ATOM   125  C CG  . ASP A 1 26  ? -13.149 -89.819  10.870  1.00 119.27 ? 17  ASP A CG  1 
ATOM   126  O OD1 . ASP A 1 26  ? -12.633 -90.708  11.582  1.00 119.54 ? 17  ASP A OD1 1 
ATOM   127  O OD2 . ASP A 1 26  ? -12.477 -89.049  10.147  1.00 118.65 ? 17  ASP A OD2 1 
ATOM   128  N N   . THR A 1 27  ? -17.196 -91.449  11.681  1.00 116.50 ? 18  THR A N   1 
ATOM   129  C CA  . THR A 1 27  ? -18.540 -91.486  12.254  1.00 116.19 ? 18  THR A CA  1 
ATOM   130  C C   . THR A 1 27  ? -18.497 -91.193  13.746  1.00 116.82 ? 18  THR A C   1 
ATOM   131  O O   . THR A 1 27  ? -17.427 -91.184  14.360  1.00 118.18 ? 18  THR A O   1 
ATOM   132  C CB  . THR A 1 27  ? -19.195 -92.864  12.093  1.00 117.18 ? 18  THR A CB  1 
ATOM   133  O OG1 . THR A 1 27  ? -18.230 -93.887  12.378  1.00 116.72 ? 18  THR A OG1 1 
ATOM   134  C CG2 . THR A 1 27  ? -19.739 -93.038  10.686  1.00 118.14 ? 18  THR A CG2 1 
ATOM   135  N N   . VAL A 1 28  ? -19.672 -90.956  14.320  1.00 117.19 ? 19  VAL A N   1 
ATOM   136  C CA  . VAL A 1 28  ? -19.805 -90.751  15.753  1.00 114.93 ? 19  VAL A CA  1 
ATOM   137  C C   . VAL A 1 28  ? -19.125 -91.886  16.499  1.00 115.89 ? 19  VAL A C   1 
ATOM   138  O O   . VAL A 1 28  ? -18.059 -91.709  17.088  1.00 115.80 ? 19  VAL A O   1 
ATOM   139  C CB  . VAL A 1 28  ? -21.284 -90.736  16.168  1.00 112.57 ? 19  VAL A CB  1 
ATOM   140  C CG1 . VAL A 1 28  ? -21.420 -90.375  17.632  1.00 114.99 ? 19  VAL A CG1 1 
ATOM   141  C CG2 . VAL A 1 28  ? -22.066 -89.767  15.301  1.00 114.05 ? 19  VAL A CG2 1 
ATOM   142  N N   . LEU A 1 29  ? -19.735 -93.064  16.427  1.00 116.00 ? 20  LEU A N   1 
ATOM   143  C CA  . LEU A 1 29  ? -19.338 -94.212  17.236  1.00 115.56 ? 20  LEU A CA  1 
ATOM   144  C C   . LEU A 1 29  ? -17.993 -94.826  16.837  1.00 116.53 ? 20  LEU A C   1 
ATOM   145  O O   . LEU A 1 29  ? -17.332 -95.469  17.654  1.00 117.11 ? 20  LEU A O   1 
ATOM   146  C CB  . LEU A 1 29  ? -20.438 -95.268  17.189  1.00 114.62 ? 20  LEU A CB  1 
ATOM   147  C CG  . LEU A 1 29  ? -21.841 -94.673  17.311  1.00 113.79 ? 20  LEU A CG  1 
ATOM   148  C CD1 . LEU A 1 29  ? -22.717 -95.105  16.145  1.00 114.19 ? 20  LEU A CD1 1 
ATOM   149  C CD2 . LEU A 1 29  ? -22.480 -95.041  18.641  1.00 116.27 ? 20  LEU A CD2 1 
ATOM   150  N N   . GLU A 1 30  ? -17.593 -94.638  15.584  1.00 117.26 ? 21  GLU A N   1 
ATOM   151  C CA  . GLU A 1 30  ? -16.306 -95.151  15.117  1.00 118.72 ? 21  GLU A CA  1 
ATOM   152  C C   . GLU A 1 30  ? -15.616 -94.156  14.180  1.00 118.83 ? 21  GLU A C   1 
ATOM   153  O O   . GLU A 1 30  ? -16.225 -93.653  13.237  1.00 117.59 ? 21  GLU A O   1 
ATOM   154  C CB  . GLU A 1 30  ? -16.484 -96.515  14.438  1.00 118.88 ? 21  GLU A CB  1 
ATOM   155  C CG  . GLU A 1 30  ? -15.439 -97.556  14.842  1.00 121.16 ? 21  GLU A CG  1 
ATOM   156  C CD  . GLU A 1 30  ? -15.994 -98.974  14.879  1.00 121.20 ? 21  GLU A CD  1 
ATOM   157  O OE1 . GLU A 1 30  ? -15.224 -99.914  15.174  1.00 118.67 ? 21  GLU A OE1 1 
ATOM   158  O OE2 . GLU A 1 30  ? -17.204 -99.147  14.622  1.00 122.00 ? 21  GLU A OE2 1 
ATOM   159  N N   . LYS A 1 31  ? -14.342 -93.883  14.443  1.00 118.18 ? 22  LYS A N   1 
ATOM   160  C CA  . LYS A 1 31  ? -13.602 -92.874  13.689  1.00 117.49 ? 22  LYS A CA  1 
ATOM   161  C C   . LYS A 1 31  ? -12.894 -93.450  12.467  1.00 117.90 ? 22  LYS A C   1 
ATOM   162  O O   . LYS A 1 31  ? -13.221 -93.104  11.330  1.00 116.38 ? 22  LYS A O   1 
ATOM   163  C CB  . LYS A 1 31  ? -12.615 -92.144  14.606  1.00 116.16 ? 22  LYS A CB  1 
ATOM   164  C CG  . LYS A 1 31  ? -12.118 -92.992  15.775  1.00 118.32 ? 22  LYS A CG  1 
ATOM   165  C CD  . LYS A 1 31  ? -11.772 -92.142  16.995  1.00 115.74 ? 22  LYS A CD  1 
ATOM   166  C CE  . LYS A 1 31  ? -13.010 -91.491  17.592  1.00 110.65 ? 22  LYS A CE  1 
ATOM   167  N NZ  . LYS A 1 31  ? -13.639 -90.489  16.685  1.00 109.71 ? 22  LYS A NZ  1 
ATOM   168  N N   . ASN A 1 32  ? -11.952 -94.353  12.711  1.00 118.02 ? 23  ASN A N   1 
ATOM   169  C CA  . ASN A 1 32  ? -11.066 -94.867  11.668  1.00 121.27 ? 23  ASN A CA  1 
ATOM   170  C C   . ASN A 1 32  ? -11.779 -95.451  10.453  1.00 119.46 ? 23  ASN A C   1 
ATOM   171  O O   . ASN A 1 32  ? -11.186 -95.587  9.379   1.00 116.37 ? 23  ASN A O   1 
ATOM   172  C CB  . ASN A 1 32  ? -10.146 -95.941  12.258  1.00 122.22 ? 23  ASN A CB  1 
ATOM   173  C CG  . ASN A 1 32  ? -8.734  -95.444  12.479  1.00 122.73 ? 23  ASN A CG  1 
ATOM   174  O OD1 . ASN A 1 32  ? -8.255  -94.566  11.759  1.00 123.74 ? 23  ASN A OD1 1 
ATOM   175  N ND2 . ASN A 1 32  ? -8.056  -96.004  13.474  1.00 119.78 ? 23  ASN A ND2 1 
ATOM   176  N N   . VAL A 1 33  ? -13.062 -95.750  10.615  1.00 120.06 ? 24  VAL A N   1 
ATOM   177  C CA  . VAL A 1 33  ? -13.745 -96.702  9.744   1.00 118.84 ? 24  VAL A CA  1 
ATOM   178  C C   . VAL A 1 33  ? -13.545 -96.505  8.239   1.00 117.82 ? 24  VAL A C   1 
ATOM   179  O O   . VAL A 1 33  ? -13.587 -95.388  7.711   1.00 115.31 ? 24  VAL A O   1 
ATOM   180  C CB  . VAL A 1 33  ? -15.251 -96.779  10.063  1.00 117.87 ? 24  VAL A CB  1 
ATOM   181  C CG1 . VAL A 1 33  ? -16.061 -97.014  8.788   1.00 116.14 ? 24  VAL A CG1 1 
ATOM   182  C CG2 . VAL A 1 33  ? -15.519 -97.864  11.102  1.00 119.58 ? 24  VAL A CG2 1 
ATOM   183  N N   . THR A 1 34  ? -13.301 -97.635  7.578   1.00 119.28 ? 25  THR A N   1 
ATOM   184  C CA  . THR A 1 34  ? -13.074 -97.717  6.144   1.00 117.56 ? 25  THR A CA  1 
ATOM   185  C C   . THR A 1 34  ? -14.395 -97.884  5.422   1.00 117.89 ? 25  THR A C   1 
ATOM   186  O O   . THR A 1 34  ? -15.284 -98.583  5.904   1.00 117.71 ? 25  THR A O   1 
ATOM   187  C CB  . THR A 1 34  ? -12.219 -98.945  5.803   1.00 117.24 ? 25  THR A CB  1 
ATOM   188  O OG1 . THR A 1 34  ? -11.011 -98.929  6.579   1.00 118.80 ? 25  THR A OG1 1 
ATOM   189  C CG2 . THR A 1 34  ? -11.887 -98.967  4.319   1.00 118.27 ? 25  THR A CG2 1 
ATOM   190  N N   . VAL A 1 35  ? -14.528 -97.250  4.264   1.00 118.39 ? 26  VAL A N   1 
ATOM   191  C CA  . VAL A 1 35  ? -15.760 -97.376  3.503   1.00 118.85 ? 26  VAL A CA  1 
ATOM   192  C C   . VAL A 1 35  ? -15.493 -97.744  2.055   1.00 120.28 ? 26  VAL A C   1 
ATOM   193  O O   . VAL A 1 35  ? -14.343 -97.822  1.621   1.00 119.97 ? 26  VAL A O   1 
ATOM   194  C CB  . VAL A 1 35  ? -16.546 -96.068  3.521   1.00 117.90 ? 26  VAL A CB  1 
ATOM   195  C CG1 . VAL A 1 35  ? -16.746 -95.597  4.956   1.00 117.97 ? 26  VAL A CG1 1 
ATOM   196  C CG2 . VAL A 1 35  ? -15.815 -95.023  2.710   1.00 117.52 ? 26  VAL A CG2 1 
ATOM   197  N N   . THR A 1 36  ? -16.572 -97.976  1.316   1.00 121.72 ? 27  THR A N   1 
ATOM   198  C CA  . THR A 1 36  ? -16.491 -98.239  -0.114  1.00 123.49 ? 27  THR A CA  1 
ATOM   199  C C   . THR A 1 36  ? -16.413 -96.930  -0.879  1.00 122.17 ? 27  THR A C   1 
ATOM   200  O O   . THR A 1 36  ? -15.657 -96.795  -1.841  1.00 123.18 ? 27  THR A O   1 
ATOM   201  C CB  . THR A 1 36  ? -17.709 -99.040  -0.619  1.00 124.39 ? 27  THR A CB  1 
ATOM   202  O OG1 . THR A 1 36  ? -18.905 -98.271  -0.436  1.00 123.52 ? 27  THR A OG1 1 
ATOM   203  C CG2 . THR A 1 36  ? -17.831 -100.369 0.122   1.00 122.74 ? 27  THR A CG2 1 
ATOM   204  N N   . HIS A 1 37  ? -17.210 -95.965  -0.443  1.00 121.39 ? 28  HIS A N   1 
ATOM   205  C CA  . HIS A 1 37  ? -17.297 -94.697  -1.142  1.00 122.23 ? 28  HIS A CA  1 
ATOM   206  C C   . HIS A 1 37  ? -17.330 -93.531  -0.183  1.00 121.97 ? 28  HIS A C   1 
ATOM   207  O O   . HIS A 1 37  ? -17.834 -93.647  0.931   1.00 120.90 ? 28  HIS A O   1 
ATOM   208  C CB  . HIS A 1 37  ? -18.541 -94.668  -2.016  1.00 121.80 ? 28  HIS A CB  1 
ATOM   209  C CG  . HIS A 1 37  ? -18.564 -95.748  -3.043  1.00 123.24 ? 28  HIS A CG  1 
ATOM   210  N ND1 . HIS A 1 37  ? -19.289 -96.909  -2.886  1.00 126.28 ? 28  HIS A ND1 1 
ATOM   211  C CD2 . HIS A 1 37  ? -17.928 -95.856  -4.232  1.00 123.35 ? 28  HIS A CD2 1 
ATOM   212  C CE1 . HIS A 1 37  ? -19.112 -97.679  -3.945  1.00 126.88 ? 28  HIS A CE1 1 
ATOM   213  N NE2 . HIS A 1 37  ? -18.291 -97.063  -4.776  1.00 124.96 ? 28  HIS A NE2 1 
ATOM   214  N N   . SER A 1 38  ? -16.794 -92.403  -0.634  1.00 122.23 ? 29  SER A N   1 
ATOM   215  C CA  . SER A 1 38  ? -16.773 -91.187  0.156   1.00 118.20 ? 29  SER A CA  1 
ATOM   216  C C   . SER A 1 38  ? -16.697 -89.995  -0.775  1.00 116.12 ? 29  SER A C   1 
ATOM   217  O O   . SER A 1 38  ? -16.702 -90.142  -1.997  1.00 115.32 ? 29  SER A O   1 
ATOM   218  C CB  . SER A 1 38  ? -15.557 -91.177  1.086   1.00 117.67 ? 29  SER A CB  1 
ATOM   219  O OG  . SER A 1 38  ? -14.347 -91.105  0.349   1.00 115.78 ? 29  SER A OG  1 
ATOM   220  N N   . VAL A 1 39  ? -16.654 -88.810  -0.181  1.00 117.58 ? 30  VAL A N   1 
ATOM   221  C CA  . VAL A 1 39  ? -16.265 -87.604  -0.894  1.00 116.52 ? 30  VAL A CA  1 
ATOM   222  C C   . VAL A 1 39  ? -15.421 -86.760  0.048   1.00 116.15 ? 30  VAL A C   1 
ATOM   223  O O   . VAL A 1 39  ? -15.657 -86.742  1.260   1.00 116.07 ? 30  VAL A O   1 
ATOM   224  C CB  . VAL A 1 39  ? -17.474 -86.781  -1.389  1.00 113.04 ? 30  VAL A CB  1 
ATOM   225  C CG1 . VAL A 1 39  ? -18.726 -87.633  -1.408  1.00 114.29 ? 30  VAL A CG1 1 
ATOM   226  C CG2 . VAL A 1 39  ? -17.677 -85.547  -0.520  1.00 112.70 ? 30  VAL A CG2 1 
ATOM   227  N N   . ASN A 1 40  ? -14.419 -86.087  -0.506  1.00 114.75 ? 31  ASN A N   1 
ATOM   228  C CA  . ASN A 1 40  ? -13.597 -85.182  0.280   1.00 112.15 ? 31  ASN A CA  1 
ATOM   229  C C   . ASN A 1 40  ? -13.837 -83.740  -0.138  1.00 109.96 ? 31  ASN A C   1 
ATOM   230  O O   . ASN A 1 40  ? -13.718 -83.399  -1.314  1.00 110.19 ? 31  ASN A O   1 
ATOM   231  C CB  . ASN A 1 40  ? -12.117 -85.535  0.155   1.00 110.52 ? 31  ASN A CB  1 
ATOM   232  C CG  . ASN A 1 40  ? -11.349 -85.249  1.427   1.00 112.43 ? 31  ASN A CG  1 
ATOM   233  O OD1 . ASN A 1 40  ? -11.008 -84.100  1.720   1.00 108.17 ? 31  ASN A OD1 1 
ATOM   234  N ND2 . ASN A 1 40  ? -11.081 -86.296  2.200   1.00 114.25 ? 31  ASN A ND2 1 
ATOM   235  N N   . LEU A 1 41  ? -14.175 -82.897  0.830   1.00 109.97 ? 32  LEU A N   1 
ATOM   236  C CA  . LEU A 1 41  ? -14.537 -81.514  0.543   1.00 109.04 ? 32  LEU A CA  1 
ATOM   237  C C   . LEU A 1 41  ? -13.356 -80.568  0.688   1.00 105.22 ? 32  LEU A C   1 
ATOM   238  O O   . LEU A 1 41  ? -13.464 -79.365  0.441   1.00 103.05 ? 32  LEU A O   1 
ATOM   239  C CB  . LEU A 1 41  ? -15.679 -81.083  1.452   1.00 109.80 ? 32  LEU A CB  1 
ATOM   240  C CG  . LEU A 1 41  ? -16.716 -82.195  1.572   1.00 108.64 ? 32  LEU A CG  1 
ATOM   241  C CD1 . LEU A 1 41  ? -16.401 -83.086  2.768   1.00 109.67 ? 32  LEU A CD1 1 
ATOM   242  C CD2 . LEU A 1 41  ? -18.106 -81.608  1.680   1.00 106.88 ? 32  LEU A CD2 1 
ATOM   243  N N   . LEU A 1 42  ? -12.222 -81.123  1.088   1.00 104.57 ? 33  LEU A N   1 
ATOM   244  C CA  . LEU A 1 42  ? -11.008 -80.348  1.170   1.00 100.51 ? 33  LEU A CA  1 
ATOM   245  C C   . LEU A 1 42  ? -10.194 -80.579  -0.079  1.00 98.80  ? 33  LEU A C   1 
ATOM   246  O O   . LEU A 1 42  ? -10.542 -81.394  -0.929  1.00 98.21  ? 33  LEU A O   1 
ATOM   247  C CB  . LEU A 1 42  ? -10.189 -80.794  2.377   1.00 99.61  ? 33  LEU A CB  1 
ATOM   248  C CG  . LEU A 1 42  ? -10.131 -79.815  3.545   1.00 99.89  ? 33  LEU A CG  1 
ATOM   249  C CD1 . LEU A 1 42  ? -11.498 -79.179  3.770   1.00 100.08 ? 33  LEU A CD1 1 
ATOM   250  C CD2 . LEU A 1 42  ? -9.615  -80.507  4.801   1.00 99.03  ? 33  LEU A CD2 1 
ATOM   251  N N   . GLU A 1 43  ? -9.097  -79.852  -0.181  1.00 98.56  ? 34  GLU A N   1 
ATOM   252  C CA  . GLU A 1 43  ? -8.097  -80.141  -1.178  1.00 95.01  ? 34  GLU A CA  1 
ATOM   253  C C   . GLU A 1 43  ? -6.762  -80.067  -0.461  1.00 93.10  ? 34  GLU A C   1 
ATOM   254  O O   . GLU A 1 43  ? -6.371  -79.011  0.031   1.00 93.12  ? 34  GLU A O   1 
ATOM   255  C CB  . GLU A 1 43  ? -8.175  -79.123  -2.312  1.00 93.59  ? 34  GLU A CB  1 
ATOM   256  C CG  . GLU A 1 43  ? -7.066  -79.239  -3.339  1.00 95.14  ? 34  GLU A CG  1 
ATOM   257  C CD  . GLU A 1 43  ? -7.052  -80.575  -4.054  1.00 95.36  ? 34  GLU A CD  1 
ATOM   258  O OE1 . GLU A 1 43  ? -6.507  -81.543  -3.482  1.00 93.40  ? 34  GLU A OE1 1 
ATOM   259  O OE2 . GLU A 1 43  ? -7.576  -80.655  -5.187  1.00 96.15  ? 34  GLU A OE2 1 
ATOM   260  N N   . ASP A 1 44  ? -6.087  -81.204  -0.359  1.00 92.36  ? 35  ASP A N   1 
ATOM   261  C CA  . ASP A 1 44  ? -4.756  -81.248  0.226   1.00 93.63  ? 35  ASP A CA  1 
ATOM   262  C C   . ASP A 1 44  ? -3.739  -80.867  -0.830  1.00 93.06  ? 35  ASP A C   1 
ATOM   263  O O   . ASP A 1 44  ? -2.666  -80.339  -0.534  1.00 92.05  ? 35  ASP A O   1 
ATOM   264  C CB  . ASP A 1 44  ? -4.438  -82.654  0.719   1.00 96.46  ? 35  ASP A CB  1 
ATOM   265  C CG  . ASP A 1 44  ? -5.664  -83.397  1.181   1.00 101.69 ? 35  ASP A CG  1 
ATOM   266  O OD1 . ASP A 1 44  ? -6.347  -82.904  2.105   1.00 102.27 ? 35  ASP A OD1 1 
ATOM   267  O OD2 . ASP A 1 44  ? -5.948  -84.473  0.609   1.00 101.65 ? 35  ASP A OD2 1 
ATOM   268  N N   . LYS A 1 45  ? -4.089  -81.148  -2.076  1.00 90.35  ? 36  LYS A N   1 
ATOM   269  C CA  . LYS A 1 45  ? -3.087  -81.223  -3.116  1.00 86.71  ? 36  LYS A CA  1 
ATOM   270  C C   . LYS A 1 45  ? -3.013  -79.976  -3.968  1.00 85.73  ? 36  LYS A C   1 
ATOM   271  O O   . LYS A 1 45  ? -4.017  -79.321  -4.244  1.00 87.54  ? 36  LYS A O   1 
ATOM   272  C CB  . LYS A 1 45  ? -3.308  -82.468  -3.971  1.00 89.26  ? 36  LYS A CB  1 
ATOM   273  C CG  . LYS A 1 45  ? -3.416  -83.747  -3.148  1.00 94.25  ? 36  LYS A CG  1 
ATOM   274  C CD  . LYS A 1 45  ? -2.203  -83.939  -2.240  1.00 95.63  ? 36  LYS A CD  1 
ATOM   275  C CE  . LYS A 1 45  ? -2.391  -85.133  -1.307  1.00 95.26  ? 36  LYS A CE  1 
ATOM   276  N NZ  . LYS A 1 45  ? -1.151  -85.438  -0.538  1.00 99.73  ? 36  LYS A NZ  1 
ATOM   277  N N   . HIS A 1 46  ? -1.789  -79.666  -4.370  1.00 85.11  ? 37  HIS A N   1 
ATOM   278  C CA  . HIS A 1 46  ? -1.472  -78.480  -5.143  1.00 83.82  ? 37  HIS A CA  1 
ATOM   279  C C   . HIS A 1 46  ? -0.288  -78.832  -6.032  1.00 82.38  ? 37  HIS A C   1 
ATOM   280  O O   . HIS A 1 46  ? 0.385   -79.842  -5.814  1.00 82.23  ? 37  HIS A O   1 
ATOM   281  C CB  . HIS A 1 46  ? -1.084  -77.340  -4.210  1.00 81.72  ? 37  HIS A CB  1 
ATOM   282  C CG  . HIS A 1 46  ? 0.054   -77.680  -3.301  1.00 81.46  ? 37  HIS A CG  1 
ATOM   283  N ND1 . HIS A 1 46  ? 1.360   -77.740  -3.735  1.00 77.43  ? 37  HIS A ND1 1 
ATOM   284  C CD2 . HIS A 1 46  ? 0.079   -78.003  -1.986  1.00 82.48  ? 37  HIS A CD2 1 
ATOM   285  C CE1 . HIS A 1 46  ? 2.143   -78.075  -2.725  1.00 79.07  ? 37  HIS A CE1 1 
ATOM   286  N NE2 . HIS A 1 46  ? 1.391   -78.241  -1.652  1.00 79.49  ? 37  HIS A NE2 1 
ATOM   287  N N   . ASN A 1 47  ? -0.015  -77.985  -7.014  1.00 80.60  ? 38  ASN A N   1 
ATOM   288  C CA  . ASN A 1 47  ? 1.017   -78.280  -7.995  1.00 81.01  ? 38  ASN A CA  1 
ATOM   289  C C   . ASN A 1 47  ? 2.412   -77.997  -7.447  1.00 79.34  ? 38  ASN A C   1 
ATOM   290  O O   . ASN A 1 47  ? 3.407   -78.143  -8.153  1.00 80.31  ? 38  ASN A O   1 
ATOM   291  C CB  . ASN A 1 47  ? 0.778   -77.489  -9.279  1.00 80.67  ? 38  ASN A CB  1 
ATOM   292  C CG  . ASN A 1 47  ? 0.901   -75.993  -9.071  1.00 83.14  ? 38  ASN A CG  1 
ATOM   293  O OD1 . ASN A 1 47  ? 0.690   -75.487  -7.965  1.00 84.46  ? 38  ASN A OD1 1 
ATOM   294  N ND2 . ASN A 1 47  ? 1.252   -75.274  -10.136 1.00 82.53  ? 38  ASN A ND2 1 
ATOM   295  N N   . GLY A 1 48  ? 2.473   -77.564  -6.194  1.00 79.10  ? 39  GLY A N   1 
ATOM   296  C CA  . GLY A 1 48  ? 3.741   -77.321  -5.532  1.00 79.14  ? 39  GLY A CA  1 
ATOM   297  C C   . GLY A 1 48  ? 4.557   -76.285  -6.269  1.00 80.33  ? 39  GLY A C   1 
ATOM   298  O O   . GLY A 1 48  ? 5.785   -76.305  -6.223  1.00 79.80  ? 39  GLY A O   1 
ATOM   299  N N   . LYS A 1 49  ? 3.867   -75.376  -6.950  1.00 79.91  ? 40  LYS A N   1 
ATOM   300  C CA  . LYS A 1 49  ? 4.527   -74.335  -7.726  1.00 80.85  ? 40  LYS A CA  1 
ATOM   301  C C   . LYS A 1 49  ? 3.831   -72.984  -7.558  1.00 82.12  ? 40  LYS A C   1 
ATOM   302  O O   . LYS A 1 49  ? 2.700   -72.918  -7.073  1.00 81.72  ? 40  LYS A O   1 
ATOM   303  C CB  . LYS A 1 49  ? 4.565   -74.721  -9.210  1.00 84.15  ? 40  LYS A CB  1 
ATOM   304  C CG  . LYS A 1 49  ? 5.778   -75.556  -9.616  1.00 84.76  ? 40  LYS A CG  1 
ATOM   305  C CD  . LYS A 1 49  ? 6.002   -75.527  -11.127 1.00 87.94  ? 40  LYS A CD  1 
ATOM   306  C CE  . LYS A 1 49  ? 7.487   -75.623  -11.492 1.00 89.50  ? 40  LYS A CE  1 
ATOM   307  N NZ  . LYS A 1 49  ? 8.178   -74.294  -11.478 1.00 83.60  ? 40  LYS A NZ  1 
ATOM   308  N N   . LEU A 1 50  ? 4.513   -71.912  -7.961  1.00 80.15  ? 41  LEU A N   1 
ATOM   309  C CA  . LEU A 1 50  ? 3.907   -70.585  -8.028  1.00 77.10  ? 41  LEU A CA  1 
ATOM   310  C C   . LEU A 1 50  ? 3.839   -70.165  -9.476  1.00 77.02  ? 41  LEU A C   1 
ATOM   311  O O   . LEU A 1 50  ? 4.864   -70.076  -10.144 1.00 80.78  ? 41  LEU A O   1 
ATOM   312  C CB  . LEU A 1 50  ? 4.731   -69.577  -7.242  1.00 77.22  ? 41  LEU A CB  1 
ATOM   313  C CG  . LEU A 1 50  ? 4.781   -69.860  -5.743  1.00 76.34  ? 41  LEU A CG  1 
ATOM   314  C CD1 . LEU A 1 50  ? 5.520   -68.747  -5.051  1.00 73.22  ? 41  LEU A CD1 1 
ATOM   315  C CD2 . LEU A 1 50  ? 3.383   -70.010  -5.165  1.00 76.59  ? 41  LEU A CD2 1 
ATOM   316  N N   . CYS A 1 51  ? 2.637   -69.892  -9.963  1.00 77.17  ? 42  CYS A N   1 
ATOM   317  C CA  . CYS A 1 51  ? 2.429   -69.814  -11.397 1.00 78.12  ? 42  CYS A CA  1 
ATOM   318  C C   . CYS A 1 51  ? 2.073   -68.426  -11.853 1.00 77.45  ? 42  CYS A C   1 
ATOM   319  O O   . CYS A 1 51  ? 1.886   -67.522  -11.043 1.00 75.56  ? 42  CYS A O   1 
ATOM   320  C CB  . CYS A 1 51  ? 1.296   -70.757  -11.774 1.00 81.18  ? 42  CYS A CB  1 
ATOM   321  S SG  . CYS A 1 51  ? 1.438   -72.368  -10.966 1.00 88.49  ? 42  CYS A SG  1 
ATOM   322  N N   . LYS A 1 52  ? 1.978   -68.266  -13.166 1.00 79.23  ? 43  LYS A N   1 
ATOM   323  C CA  . LYS A 1 52  ? 1.369   -67.085  -13.724 1.00 78.16  ? 43  LYS A CA  1 
ATOM   324  C C   . LYS A 1 52  ? -0.098  -67.241  -13.378 1.00 81.36  ? 43  LYS A C   1 
ATOM   325  O O   . LYS A 1 52  ? -0.683  -68.306  -13.573 1.00 82.11  ? 43  LYS A O   1 
ATOM   326  C CB  . LYS A 1 52  ? 1.549   -67.047  -15.237 1.00 78.24  ? 43  LYS A CB  1 
ATOM   327  C CG  . LYS A 1 52  ? 2.988   -67.152  -15.697 1.00 79.09  ? 43  LYS A CG  1 
ATOM   328  C CD  . LYS A 1 52  ? 3.062   -67.588  -17.150 1.00 83.43  ? 43  LYS A CD  1 
ATOM   329  C CE  . LYS A 1 52  ? 2.405   -66.567  -18.066 1.00 83.50  ? 43  LYS A CE  1 
ATOM   330  N NZ  . LYS A 1 52  ? 3.217   -65.324  -18.209 1.00 83.75  ? 43  LYS A NZ  1 
ATOM   331  N N   . LEU A 1 53  ? -0.692  -66.192  -12.833 1.00 81.06  ? 44  LEU A N   1 
ATOM   332  C CA  . LEU A 1 53  ? -2.109  -66.233  -12.556 1.00 81.09  ? 44  LEU A CA  1 
ATOM   333  C C   . LEU A 1 53  ? -2.787  -65.736  -13.810 1.00 82.83  ? 44  LEU A C   1 
ATOM   334  O O   . LEU A 1 53  ? -2.605  -64.583  -14.210 1.00 79.55  ? 44  LEU A O   1 
ATOM   335  C CB  . LEU A 1 53  ? -2.462  -65.329  -11.381 1.00 81.08  ? 44  LEU A CB  1 
ATOM   336  C CG  . LEU A 1 53  ? -3.846  -65.624  -10.809 1.00 85.97  ? 44  LEU A CG  1 
ATOM   337  C CD1 . LEU A 1 53  ? -3.843  -66.999  -10.165 1.00 86.09  ? 44  LEU A CD1 1 
ATOM   338  C CD2 . LEU A 1 53  ? -4.266  -64.569  -9.810  1.00 86.48  ? 44  LEU A CD2 1 
ATOM   339  N N   . ARG A 1 54  ? -3.551  -66.618  -14.443 1.00 85.00  ? 45  ARG A N   1 
ATOM   340  C CA  . ARG A 1 54  ? -4.204  -66.272  -15.688 1.00 84.95  ? 45  ARG A CA  1 
ATOM   341  C C   . ARG A 1 54  ? -3.232  -65.496  -16.554 1.00 82.39  ? 45  ARG A C   1 
ATOM   342  O O   . ARG A 1 54  ? -3.424  -64.306  -16.801 1.00 81.12  ? 45  ARG A O   1 
ATOM   343  C CB  . ARG A 1 54  ? -5.426  -65.406  -15.415 1.00 88.28  ? 45  ARG A CB  1 
ATOM   344  C CG  . ARG A 1 54  ? -6.161  -65.773  -14.136 1.00 88.87  ? 45  ARG A CG  1 
ATOM   345  C CD  . ARG A 1 54  ? -7.479  -65.022  -14.039 1.00 94.21  ? 45  ARG A CD  1 
ATOM   346  N NE  . ARG A 1 54  ? -8.116  -65.168  -12.732 1.00 99.99  ? 45  ARG A NE  1 
ATOM   347  C CZ  . ARG A 1 54  ? -8.158  -64.211  -11.808 1.00 97.78  ? 45  ARG A CZ  1 
ATOM   348  N NH1 . ARG A 1 54  ? -7.595  -63.031  -12.043 1.00 95.15  ? 45  ARG A NH1 1 
ATOM   349  N NH2 . ARG A 1 54  ? -8.763  -64.432  -10.647 1.00 95.29  ? 45  ARG A NH2 1 
ATOM   350  N N   . GLY A 1 55  ? -2.161  -66.159  -16.969 1.00 81.11  ? 46  GLY A N   1 
ATOM   351  C CA  . GLY A 1 55  ? -1.287  -65.619  -17.993 1.00 83.18  ? 46  GLY A CA  1 
ATOM   352  C C   . GLY A 1 55  ? -0.384  -64.473  -17.582 1.00 80.49  ? 46  GLY A C   1 
ATOM   353  O O   . GLY A 1 55  ? 0.505   -64.075  -18.337 1.00 80.34  ? 46  GLY A O   1 
ATOM   354  N N   . VAL A 1 56  ? -0.606  -63.926  -16.392 1.00 82.46  ? 47  VAL A N   1 
ATOM   355  C CA  . VAL A 1 56  ? 0.291   -62.895  -15.885 1.00 77.61  ? 47  VAL A CA  1 
ATOM   356  C C   . VAL A 1 56  ? 1.168   -63.433  -14.763 1.00 74.45  ? 47  VAL A C   1 
ATOM   357  O O   . VAL A 1 56  ? 0.691   -64.072  -13.822 1.00 72.64  ? 47  VAL A O   1 
ATOM   358  C CB  . VAL A 1 56  ? -0.450  -61.639  -15.408 1.00 73.28  ? 47  VAL A CB  1 
ATOM   359  C CG1 . VAL A 1 56  ? 0.526   -60.470  -15.313 1.00 68.10  ? 47  VAL A CG1 1 
ATOM   360  C CG2 . VAL A 1 56  ? -1.589  -61.308  -16.356 1.00 73.57  ? 47  VAL A CG2 1 
ATOM   361  N N   . ALA A 1 57  ? 2.461   -63.173  -14.884 1.00 73.23  ? 48  ALA A N   1 
ATOM   362  C CA  . ALA A 1 57  ? 3.422   -63.621  -13.894 1.00 72.60  ? 48  ALA A CA  1 
ATOM   363  C C   . ALA A 1 57  ? 3.439   -62.697  -12.674 1.00 70.27  ? 48  ALA A C   1 
ATOM   364  O O   . ALA A 1 57  ? 3.247   -61.481  -12.795 1.00 68.78  ? 48  ALA A O   1 
ATOM   365  C CB  . ALA A 1 57  ? 4.803   -63.713  -14.514 1.00 72.36  ? 48  ALA A CB  1 
ATOM   366  N N   . PRO A 1 58  ? 3.658   -63.274  -11.484 1.00 66.81  ? 49  PRO A N   1 
ATOM   367  C CA  . PRO A 1 58  ? 3.794   -62.419  -10.311 1.00 65.47  ? 49  PRO A CA  1 
ATOM   368  C C   . PRO A 1 58  ? 5.120   -61.707  -10.405 1.00 63.93  ? 49  PRO A C   1 
ATOM   369  O O   . PRO A 1 58  ? 5.873   -61.935  -11.350 1.00 64.68  ? 49  PRO A O   1 
ATOM   370  C CB  . PRO A 1 58  ? 3.841   -63.419  -9.159  1.00 63.11  ? 49  PRO A CB  1 
ATOM   371  C CG  . PRO A 1 58  ? 4.414   -64.635  -9.751  1.00 64.97  ? 49  PRO A CG  1 
ATOM   372  C CD  . PRO A 1 58  ? 3.880   -64.691  -11.156 1.00 68.42  ? 49  PRO A CD  1 
ATOM   373  N N   . LEU A 1 59  ? 5.403   -60.852  -9.436  1.00 61.19  ? 50  LEU A N   1 
ATOM   374  C CA  . LEU A 1 59  ? 6.711   -60.238  -9.344  1.00 60.96  ? 50  LEU A CA  1 
ATOM   375  C C   . LEU A 1 59  ? 7.466   -60.896  -8.204  1.00 61.39  ? 50  LEU A C   1 
ATOM   376  O O   . LEU A 1 59  ? 6.899   -61.166  -7.144  1.00 62.05  ? 50  LEU A O   1 
ATOM   377  C CB  . LEU A 1 59  ? 6.600   -58.732  -9.115  1.00 60.90  ? 50  LEU A CB  1 
ATOM   378  C CG  . LEU A 1 59  ? 7.931   -58.007  -8.875  1.00 61.55  ? 50  LEU A CG  1 
ATOM   379  C CD1 . LEU A 1 59  ? 8.983   -58.418  -9.897  1.00 62.64  ? 50  LEU A CD1 1 
ATOM   380  C CD2 . LEU A 1 59  ? 7.735   -56.497  -8.901  1.00 61.67  ? 50  LEU A CD2 1 
ATOM   381  N N   . HIS A 1 60  ? 8.749   -61.154  -8.425  1.00 61.47  ? 51  HIS A N   1 
ATOM   382  C CA  . HIS A 1 60  ? 9.551   -61.898  -7.462  1.00 61.50  ? 51  HIS A CA  1 
ATOM   383  C C   . HIS A 1 60  ? 10.796  -61.113  -7.066  1.00 62.68  ? 51  HIS A C   1 
ATOM   384  O O   . HIS A 1 60  ? 11.644  -60.805  -7.908  1.00 66.93  ? 51  HIS A O   1 
ATOM   385  C CB  . HIS A 1 60  ? 9.942   -63.263  -8.041  1.00 61.57  ? 51  HIS A CB  1 
ATOM   386  C CG  . HIS A 1 60  ? 10.563  -64.191  -7.044  1.00 60.60  ? 51  HIS A CG  1 
ATOM   387  N ND1 . HIS A 1 60  ? 9.821   -65.067  -6.280  1.00 61.13  ? 51  HIS A ND1 1 
ATOM   388  C CD2 . HIS A 1 60  ? 11.855  -64.386  -6.689  1.00 62.52  ? 51  HIS A CD2 1 
ATOM   389  C CE1 . HIS A 1 60  ? 10.627  -65.760  -5.495  1.00 60.00  ? 51  HIS A CE1 1 
ATOM   390  N NE2 . HIS A 1 60  ? 11.868  -65.363  -5.721  1.00 64.14  ? 51  HIS A NE2 1 
ATOM   391  N N   . LEU A 1 61  ? 10.896  -60.787  -5.782  1.00 61.73  ? 52  LEU A N   1 
ATOM   392  C CA  . LEU A 1 61  ? 12.029  -60.034  -5.268  1.00 62.60  ? 52  LEU A CA  1 
ATOM   393  C C   . LEU A 1 61  ? 12.785  -60.995  -4.379  1.00 65.96  ? 52  LEU A C   1 
ATOM   394  O O   . LEU A 1 61  ? 12.307  -61.351  -3.302  1.00 70.25  ? 52  LEU A O   1 
ATOM   395  C CB  . LEU A 1 61  ? 11.529  -58.853  -4.442  1.00 60.37  ? 52  LEU A CB  1 
ATOM   396  C CG  . LEU A 1 61  ? 10.184  -58.263  -4.884  1.00 60.83  ? 52  LEU A CG  1 
ATOM   397  C CD1 . LEU A 1 61  ? 9.362   -57.817  -3.687  1.00 55.65  ? 52  LEU A CD1 1 
ATOM   398  C CD2 . LEU A 1 61  ? 10.367  -57.118  -5.876  1.00 57.70  ? 52  LEU A CD2 1 
ATOM   399  N N   . GLY A 1 62  ? 13.947  -61.453  -4.827  1.00 64.83  ? 53  GLY A N   1 
ATOM   400  C CA  . GLY A 1 62  ? 14.573  -62.549  -4.120  1.00 62.22  ? 53  GLY A CA  1 
ATOM   401  C C   . GLY A 1 62  ? 15.134  -62.232  -2.750  1.00 66.13  ? 53  GLY A C   1 
ATOM   402  O O   . GLY A 1 62  ? 14.615  -62.721  -1.736  1.00 67.17  ? 53  GLY A O   1 
ATOM   403  N N   . LYS A 1 63  ? 16.148  -61.367  -2.711  1.00 66.96  ? 54  LYS A N   1 
ATOM   404  C CA  . LYS A 1 63  ? 16.841  -61.069  -1.463  1.00 64.52  ? 54  LYS A CA  1 
ATOM   405  C C   . LYS A 1 63  ? 16.301  -59.793  -0.886  1.00 62.37  ? 54  LYS A C   1 
ATOM   406  O O   . LYS A 1 63  ? 16.713  -59.352  0.185   1.00 65.05  ? 54  LYS A O   1 
ATOM   407  C CB  . LYS A 1 63  ? 18.360  -60.979  -1.649  1.00 64.93  ? 54  LYS A CB  1 
ATOM   408  C CG  . LYS A 1 63  ? 18.878  -59.877  -2.576  1.00 67.19  ? 54  LYS A CG  1 
ATOM   409  C CD  . LYS A 1 63  ? 20.422  -59.876  -2.574  1.00 67.55  ? 54  LYS A CD  1 
ATOM   410  C CE  . LYS A 1 63  ? 20.996  -59.363  -3.894  1.00 69.37  ? 54  LYS A CE  1 
ATOM   411  N NZ  . LYS A 1 63  ? 22.484  -59.417  -3.939  1.00 71.20  ? 54  LYS A NZ  1 
ATOM   412  N N   . CYS A 1 64  ? 15.369  -59.200  -1.613  1.00 57.65  ? 55  CYS A N   1 
ATOM   413  C CA  . CYS A 1 64  ? 14.777  -57.965  -1.167  1.00 58.46  ? 55  CYS A CA  1 
ATOM   414  C C   . CYS A 1 64  ? 13.348  -58.168  -0.717  1.00 56.70  ? 55  CYS A C   1 
ATOM   415  O O   . CYS A 1 64  ? 12.654  -59.072  -1.178  1.00 54.72  ? 55  CYS A O   1 
ATOM   416  C CB  . CYS A 1 64  ? 14.865  -56.915  -2.260  1.00 56.42  ? 55  CYS A CB  1 
ATOM   417  S SG  . CYS A 1 64  ? 16.543  -56.389  -2.546  1.00 61.76  ? 55  CYS A SG  1 
ATOM   418  N N   . ASN A 1 65  ? 12.940  -57.356  0.245   1.00 54.76  ? 56  ASN A N   1 
ATOM   419  C CA  . ASN A 1 65  ? 11.541  -57.271  0.580   1.00 53.67  ? 56  ASN A CA  1 
ATOM   420  C C   . ASN A 1 65  ? 11.005  -56.035  -0.123  1.00 50.26  ? 56  ASN A C   1 
ATOM   421  O O   . ASN A 1 65  ? 11.783  -55.276  -0.703  1.00 51.27  ? 56  ASN A O   1 
ATOM   422  C CB  . ASN A 1 65  ? 11.372  -57.157  2.099   1.00 53.54  ? 56  ASN A CB  1 
ATOM   423  C CG  . ASN A 1 65  ? 11.622  -55.752  2.618   1.00 50.79  ? 56  ASN A CG  1 
ATOM   424  O OD1 . ASN A 1 65  ? 12.224  -54.912  1.932   1.00 48.28  ? 56  ASN A OD1 1 
ATOM   425  N ND2 . ASN A 1 65  ? 11.149  -55.485  3.841   1.00 49.56  ? 56  ASN A ND2 1 
ATOM   426  N N   . ILE A 1 66  ? 9.696   -55.810  -0.055  1.00 47.82  ? 57  ILE A N   1 
ATOM   427  C CA  . ILE A 1 66  ? 9.074   -54.761  -0.861  1.00 47.65  ? 57  ILE A CA  1 
ATOM   428  C C   . ILE A 1 66  ? 9.694   -53.363  -0.653  1.00 45.92  ? 57  ILE A C   1 
ATOM   429  O O   . ILE A 1 66  ? 9.901   -52.605  -1.612  1.00 45.18  ? 57  ILE A O   1 
ATOM   430  C CB  . ILE A 1 66  ? 7.555   -54.736  -0.652  1.00 42.93  ? 57  ILE A CB  1 
ATOM   431  C CG1 . ILE A 1 66  ? 6.897   -55.811  -1.517  1.00 42.79  ? 57  ILE A CG1 1 
ATOM   432  C CG2 . ILE A 1 66  ? 6.998   -53.400  -1.041  1.00 43.29  ? 57  ILE A CG2 1 
ATOM   433  C CD1 . ILE A 1 66  ? 5.438   -56.065  -1.194  1.00 44.88  ? 57  ILE A CD1 1 
ATOM   434  N N   . ALA A 1 67  ? 10.014  -53.045  0.594   1.00 43.48  ? 58  ALA A N   1 
ATOM   435  C CA  . ALA A 1 67  ? 10.622  -51.767  0.942   1.00 43.48  ? 58  ALA A CA  1 
ATOM   436  C C   . ALA A 1 67  ? 11.949  -51.473  0.224   1.00 44.45  ? 58  ALA A C   1 
ATOM   437  O O   . ALA A 1 67  ? 12.144  -50.386  -0.313  1.00 44.26  ? 58  ALA A O   1 
ATOM   438  C CB  . ALA A 1 67  ? 10.808  -51.683  2.445   1.00 44.10  ? 58  ALA A CB  1 
ATOM   439  N N   . GLY A 1 68  ? 12.872  -52.430  0.236   1.00 47.68  ? 59  GLY A N   1 
ATOM   440  C CA  . GLY A 1 68  ? 14.188  -52.211  -0.337  1.00 47.11  ? 59  GLY A CA  1 
ATOM   441  C C   . GLY A 1 68  ? 14.024  -52.106  -1.829  1.00 47.79  ? 59  GLY A C   1 
ATOM   442  O O   . GLY A 1 68  ? 14.616  -51.264  -2.505  1.00 48.19  ? 59  GLY A O   1 
ATOM   443  N N   . TRP A 1 69  ? 13.192  -52.984  -2.347  1.00 47.58  ? 60  TRP A N   1 
ATOM   444  C CA  . TRP A 1 69  ? 12.857  -52.930  -3.747  1.00 49.81  ? 60  TRP A CA  1 
ATOM   445  C C   . TRP A 1 69  ? 12.353  -51.544  -4.150  1.00 47.41  ? 60  TRP A C   1 
ATOM   446  O O   . TRP A 1 69  ? 12.977  -50.857  -4.964  1.00 47.62  ? 60  TRP A O   1 
ATOM   447  C CB  . TRP A 1 69  ? 11.809  -53.980  -4.053  1.00 50.62  ? 60  TRP A CB  1 
ATOM   448  C CG  . TRP A 1 69  ? 11.278  -53.855  -5.408  1.00 50.27  ? 60  TRP A CG  1 
ATOM   449  C CD1 . TRP A 1 69  ? 11.966  -54.014  -6.568  1.00 52.42  ? 60  TRP A CD1 1 
ATOM   450  C CD2 . TRP A 1 69  ? 9.934   -53.547  -5.771  1.00 52.14  ? 60  TRP A CD2 1 
ATOM   451  N NE1 . TRP A 1 69  ? 11.132  -53.822  -7.640  1.00 53.25  ? 60  TRP A NE1 1 
ATOM   452  C CE2 . TRP A 1 69  ? 9.876   -53.535  -7.175  1.00 51.62  ? 60  TRP A CE2 1 
ATOM   453  C CE3 . TRP A 1 69  ? 8.772   -53.276  -5.048  1.00 49.74  ? 60  TRP A CE3 1 
ATOM   454  C CZ2 . TRP A 1 69  ? 8.702   -53.262  -7.866  1.00 52.76  ? 60  TRP A CZ2 1 
ATOM   455  C CZ3 . TRP A 1 69  ? 7.609   -53.007  -5.735  1.00 49.50  ? 60  TRP A CZ3 1 
ATOM   456  C CH2 . TRP A 1 69  ? 7.580   -53.005  -7.127  1.00 54.10  ? 60  TRP A CH2 1 
ATOM   457  N N   . ILE A 1 70  ? 11.219  -51.141  -3.584  1.00 46.17  ? 61  ILE A N   1 
ATOM   458  C CA  . ILE A 1 70  ? 10.608  -49.870  -3.957  1.00 46.01  ? 61  ILE A CA  1 
ATOM   459  C C   . ILE A 1 70  ? 11.529  -48.690  -3.660  1.00 43.48  ? 61  ILE A C   1 
ATOM   460  O O   . ILE A 1 70  ? 11.619  -47.760  -4.448  1.00 42.61  ? 61  ILE A O   1 
ATOM   461  C CB  . ILE A 1 70  ? 9.241   -49.654  -3.273  1.00 44.00  ? 61  ILE A CB  1 
ATOM   462  C CG1 . ILE A 1 70  ? 8.479   -48.512  -3.948  1.00 45.73  ? 61  ILE A CG1 1 
ATOM   463  C CG2 . ILE A 1 70  ? 9.425   -49.362  -1.814  1.00 41.48  ? 61  ILE A CG2 1 
ATOM   464  C CD1 . ILE A 1 70  ? 8.276   -48.708  -5.423  1.00 45.52  ? 61  ILE A CD1 1 
ATOM   465  N N   . LEU A 1 71  ? 12.215  -48.726  -2.526  1.00 44.01  ? 62  LEU A N   1 
ATOM   466  C CA  . LEU A 1 71  ? 13.174  -47.671  -2.203  1.00 44.24  ? 62  LEU A CA  1 
ATOM   467  C C   . LEU A 1 71  ? 14.349  -47.663  -3.164  1.00 43.88  ? 62  LEU A C   1 
ATOM   468  O O   . LEU A 1 71  ? 15.012  -46.643  -3.355  1.00 43.67  ? 62  LEU A O   1 
ATOM   469  C CB  . LEU A 1 71  ? 13.708  -47.838  -0.785  1.00 43.49  ? 62  LEU A CB  1 
ATOM   470  C CG  . LEU A 1 71  ? 12.728  -47.543  0.341   1.00 42.43  ? 62  LEU A CG  1 
ATOM   471  C CD1 . LEU A 1 71  ? 13.444  -47.693  1.663   1.00 44.81  ? 62  LEU A CD1 1 
ATOM   472  C CD2 . LEU A 1 71  ? 12.136  -46.155  0.187   1.00 37.66  ? 62  LEU A CD2 1 
ATOM   473  N N   . GLY A 1 72  ? 14.603  -48.806  -3.778  1.00 44.80  ? 63  GLY A N   1 
ATOM   474  C CA  . GLY A 1 72  ? 15.768  -48.935  -4.619  1.00 46.15  ? 63  GLY A CA  1 
ATOM   475  C C   . GLY A 1 72  ? 17.013  -49.162  -3.793  1.00 46.96  ? 63  GLY A C   1 
ATOM   476  O O   . GLY A 1 72  ? 18.046  -48.537  -4.016  1.00 46.72  ? 63  GLY A O   1 
ATOM   477  N N   . ASN A 1 73  ? 16.893  -50.036  -2.803  1.00 47.99  ? 64  ASN A N   1 
ATOM   478  C CA  . ASN A 1 73  ? 18.054  -50.560  -2.119  1.00 51.28  ? 64  ASN A CA  1 
ATOM   479  C C   . ASN A 1 73  ? 18.995  -51.108  -3.180  1.00 54.59  ? 64  ASN A C   1 
ATOM   480  O O   . ASN A 1 73  ? 18.559  -51.786  -4.104  1.00 56.55  ? 64  ASN A O   1 
ATOM   481  C CB  . ASN A 1 73  ? 17.625  -51.664  -1.153  1.00 53.71  ? 64  ASN A CB  1 
ATOM   482  C CG  . ASN A 1 73  ? 18.794  -52.333  -0.459  1.00 56.60  ? 64  ASN A CG  1 
ATOM   483  O OD1 . ASN A 1 73  ? 19.867  -52.498  -1.035  1.00 57.17  ? 64  ASN A OD1 1 
ATOM   484  N ND2 . ASN A 1 73  ? 18.583  -52.736  0.788   1.00 55.90  ? 64  ASN A ND2 1 
ATOM   485  N N   . PRO A 1 74  ? 20.291  -50.797  -3.061  1.00 56.49  ? 65  PRO A N   1 
ATOM   486  C CA  . PRO A 1 74  ? 21.296  -51.224  -4.041  1.00 56.88  ? 65  PRO A CA  1 
ATOM   487  C C   . PRO A 1 74  ? 21.485  -52.741  -4.132  1.00 59.18  ? 65  PRO A C   1 
ATOM   488  O O   . PRO A 1 74  ? 21.984  -53.216  -5.149  1.00 61.67  ? 65  PRO A O   1 
ATOM   489  C CB  . PRO A 1 74  ? 22.581  -50.542  -3.553  1.00 58.31  ? 65  PRO A CB  1 
ATOM   490  C CG  . PRO A 1 74  ? 22.323  -50.204  -2.114  1.00 56.80  ? 65  PRO A CG  1 
ATOM   491  C CD  . PRO A 1 74  ? 20.862  -49.912  -2.032  1.00 55.39  ? 65  PRO A CD  1 
ATOM   492  N N   . GLU A 1 75  ? 21.101  -53.488  -3.101  1.00 59.19  ? 66  GLU A N   1 
ATOM   493  C CA  . GLU A 1 75  ? 21.138  -54.944  -3.179  1.00 60.18  ? 66  GLU A CA  1 
ATOM   494  C C   . GLU A 1 75  ? 20.030  -55.419  -4.096  1.00 60.85  ? 66  GLU A C   1 
ATOM   495  O O   . GLU A 1 75  ? 20.013  -56.566  -4.526  1.00 61.98  ? 66  GLU A O   1 
ATOM   496  C CB  . GLU A 1 75  ? 20.976  -55.580  -1.799  1.00 61.79  ? 66  GLU A CB  1 
ATOM   497  C CG  . GLU A 1 75  ? 22.226  -55.537  -0.959  1.00 63.61  ? 66  GLU A CG  1 
ATOM   498  C CD  . GLU A 1 75  ? 23.449  -56.012  -1.730  1.00 70.04  ? 66  GLU A CD  1 
ATOM   499  O OE1 . GLU A 1 75  ? 24.538  -55.413  -1.561  1.00 71.53  ? 66  GLU A OE1 1 
ATOM   500  O OE2 . GLU A 1 75  ? 23.317  -56.987  -2.504  1.00 69.80  ? 66  GLU A OE2 1 
ATOM   501  N N   . CYS A 1 76  ? 19.091  -54.525  -4.379  1.00 61.25  ? 67  CYS A N   1 
ATOM   502  C CA  . CYS A 1 76  ? 17.999  -54.810  -5.302  1.00 62.33  ? 67  CYS A CA  1 
ATOM   503  C C   . CYS A 1 76  ? 18.304  -54.330  -6.708  1.00 67.36  ? 67  CYS A C   1 
ATOM   504  O O   . CYS A 1 76  ? 17.421  -54.347  -7.564  1.00 70.41  ? 67  CYS A O   1 
ATOM   505  C CB  . CYS A 1 76  ? 16.712  -54.154  -4.823  1.00 59.57  ? 67  CYS A CB  1 
ATOM   506  S SG  . CYS A 1 76  ? 16.394  -54.430  -3.081  1.00 65.06  ? 67  CYS A SG  1 
ATOM   507  N N   . GLU A 1 77  ? 19.534  -53.867  -6.939  1.00 70.74  ? 68  GLU A N   1 
ATOM   508  C CA  . GLU A 1 77  ? 19.864  -53.222  -8.212  1.00 69.66  ? 68  GLU A CA  1 
ATOM   509  C C   . GLU A 1 77  ? 19.446  -54.081  -9.401  1.00 74.22  ? 68  GLU A C   1 
ATOM   510  O O   . GLU A 1 77  ? 18.668  -53.630  -10.244 1.00 76.52  ? 68  GLU A O   1 
ATOM   511  C CB  . GLU A 1 77  ? 21.345  -52.763  -8.303  1.00 69.60  ? 68  GLU A CB  1 
ATOM   512  C CG  . GLU A 1 77  ? 22.408  -53.840  -8.624  1.00 72.19  ? 68  GLU A CG  1 
ATOM   513  C CD  . GLU A 1 77  ? 23.831  -53.256  -8.796  1.00 71.23  ? 68  GLU A CD  1 
ATOM   514  O OE1 . GLU A 1 77  ? 23.970  -52.011  -8.890  1.00 70.26  ? 68  GLU A OE1 1 
ATOM   515  O OE2 . GLU A 1 77  ? 24.814  -54.037  -8.833  1.00 66.51  ? 68  GLU A OE2 1 
ATOM   516  N N   . SER A 1 78  ? 19.910  -55.326  -9.452  1.00 76.08  ? 69  SER A N   1 
ATOM   517  C CA  . SER A 1 78  ? 19.630  -56.163  -10.614 1.00 76.93  ? 69  SER A CA  1 
ATOM   518  C C   . SER A 1 78  ? 18.176  -56.653  -10.617 1.00 78.75  ? 69  SER A C   1 
ATOM   519  O O   . SER A 1 78  ? 17.357  -56.157  -11.389 1.00 81.77  ? 69  SER A O   1 
ATOM   520  C CB  . SER A 1 78  ? 20.608  -57.336  -10.667 1.00 77.51  ? 69  SER A CB  1 
ATOM   521  O OG  . SER A 1 78  ? 20.753  -57.920  -9.383  1.00 78.42  ? 69  SER A OG  1 
ATOM   522  N N   . LEU A 1 79  ? 17.843  -57.593  -9.740  1.00 79.61  ? 70  LEU A N   1 
ATOM   523  C CA  . LEU A 1 79  ? 16.450  -58.029  -9.578  1.00 83.51  ? 70  LEU A CA  1 
ATOM   524  C C   . LEU A 1 79  ? 15.720  -58.244  -10.916 1.00 86.48  ? 70  LEU A C   1 
ATOM   525  O O   . LEU A 1 79  ? 16.186  -58.991  -11.782 1.00 86.51  ? 70  LEU A O   1 
ATOM   526  C CB  . LEU A 1 79  ? 15.673  -57.066  -8.663  1.00 78.51  ? 70  LEU A CB  1 
ATOM   527  C CG  . LEU A 1 79  ? 14.842  -57.664  -7.514  1.00 73.99  ? 70  LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 79  ? 15.529  -58.873  -6.880  1.00 73.72  ? 70  LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 79  ? 14.529  -56.609  -6.453  1.00 65.62  ? 70  LEU A CD2 1 
ATOM   530  N N   . SER A 1 80  ? 14.570  -57.594  -11.067 1.00 89.12  ? 71  SER A N   1 
ATOM   531  C CA  . SER A 1 80  ? 13.769  -57.694  -12.287 1.00 90.92  ? 71  SER A CA  1 
ATOM   532  C C   . SER A 1 80  ? 13.071  -56.366  -12.552 1.00 95.86  ? 71  SER A C   1 
ATOM   533  O O   . SER A 1 80  ? 13.394  -55.344  -11.933 1.00 98.33  ? 71  SER A O   1 
ATOM   534  C CB  . SER A 1 80  ? 12.717  -58.805  -12.175 1.00 86.91  ? 71  SER A CB  1 
ATOM   535  O OG  . SER A 1 80  ? 12.758  -59.435  -10.904 1.00 86.00  ? 71  SER A OG  1 
ATOM   536  N N   . THR A 1 81  ? 12.135  -56.388  -13.495 1.00 94.33  ? 72  THR A N   1 
ATOM   537  C CA  . THR A 1 81  ? 11.243  -55.260  -13.739 1.00 94.92  ? 72  THR A CA  1 
ATOM   538  C C   . THR A 1 81  ? 10.000  -55.753  -14.467 1.00 91.19  ? 72  THR A C   1 
ATOM   539  O O   . THR A 1 81  ? 9.866   -56.945  -14.753 1.00 90.52  ? 72  THR A O   1 
ATOM   540  C CB  . THR A 1 81  ? 11.924  -54.111  -14.548 1.00 93.67  ? 72  THR A CB  1 
ATOM   541  O OG1 . THR A 1 81  ? 10.936  -53.145  -14.940 1.00 92.39  ? 72  THR A OG1 1 
ATOM   542  C CG2 . THR A 1 81  ? 12.637  -54.655  -15.791 1.00 90.20  ? 72  THR A CG2 1 
ATOM   543  N N   . ALA A 1 82  ? 9.090   -54.831  -14.747 1.00 87.05  ? 73  ALA A N   1 
ATOM   544  C CA  . ALA A 1 82  ? 7.901   -55.141  -15.513 1.00 81.56  ? 73  ALA A CA  1 
ATOM   545  C C   . ALA A 1 82  ? 7.052   -53.897  -15.541 1.00 79.10  ? 73  ALA A C   1 
ATOM   546  O O   . ALA A 1 82  ? 7.317   -52.949  -14.799 1.00 78.24  ? 73  ALA A O   1 
ATOM   547  C CB  . ALA A 1 82  ? 7.133   -56.283  -14.871 1.00 78.40  ? 73  ALA A CB  1 
ATOM   548  N N   . SER A 1 83  ? 6.062   -53.890  -16.427 1.00 79.07  ? 74  SER A N   1 
ATOM   549  C CA  . SER A 1 83  ? 4.982   -52.915  -16.376 1.00 75.22  ? 74  SER A CA  1 
ATOM   550  C C   . SER A 1 83  ? 3.805   -53.508  -15.606 1.00 70.76  ? 74  SER A C   1 
ATOM   551  O O   . SER A 1 83  ? 2.878   -52.793  -15.221 1.00 70.88  ? 74  SER A O   1 
ATOM   552  C CB  . SER A 1 83  ? 4.538   -52.516  -17.795 1.00 78.35  ? 74  SER A CB  1 
ATOM   553  O OG  . SER A 1 83  ? 3.906   -53.594  -18.486 1.00 80.77  ? 74  SER A OG  1 
ATOM   554  N N   . SER A 1 84  ? 3.867   -54.815  -15.360 1.00 68.75  ? 75  SER A N   1 
ATOM   555  C CA  . SER A 1 84  ? 2.714   -55.549  -14.849 1.00 69.06  ? 75  SER A CA  1 
ATOM   556  C C   . SER A 1 84  ? 3.113   -56.778  -14.038 1.00 65.54  ? 75  SER A C   1 
ATOM   557  O O   . SER A 1 84  ? 4.138   -57.398  -14.311 1.00 67.38  ? 75  SER A O   1 
ATOM   558  C CB  . SER A 1 84  ? 1.821   -55.961  -16.026 1.00 71.41  ? 75  SER A CB  1 
ATOM   559  O OG  . SER A 1 84  ? 1.193   -57.214  -15.800 1.00 72.35  ? 75  SER A OG  1 
ATOM   560  N N   . TRP A 1 85  ? 2.318   -57.108  -13.025 1.00 61.84  ? 76  TRP A N   1 
ATOM   561  C CA  . TRP A 1 85  ? 2.454   -58.389  -12.333 1.00 63.90  ? 76  TRP A CA  1 
ATOM   562  C C   . TRP A 1 85  ? 1.154   -58.819  -11.679 1.00 63.26  ? 76  TRP A C   1 
ATOM   563  O O   . TRP A 1 85  ? 0.371   -57.996  -11.203 1.00 61.54  ? 76  TRP A O   1 
ATOM   564  C CB  . TRP A 1 85  ? 3.577   -58.361  -11.296 1.00 64.00  ? 76  TRP A CB  1 
ATOM   565  C CG  . TRP A 1 85  ? 3.462   -57.211  -10.355 1.00 63.99  ? 76  TRP A CG  1 
ATOM   566  C CD1 . TRP A 1 85  ? 2.789   -57.179  -9.169  1.00 63.05  ? 76  TRP A CD1 1 
ATOM   567  C CD2 . TRP A 1 85  ? 4.027   -55.909  -10.534 1.00 63.53  ? 76  TRP A CD2 1 
ATOM   568  N NE1 . TRP A 1 85  ? 2.904   -55.935  -8.597  1.00 60.60  ? 76  TRP A NE1 1 
ATOM   569  C CE2 . TRP A 1 85  ? 3.659   -55.137  -9.415  1.00 60.27  ? 76  TRP A CE2 1 
ATOM   570  C CE3 . TRP A 1 85  ? 4.811   -55.320  -11.534 1.00 63.80  ? 76  TRP A CE3 1 
ATOM   571  C CZ2 . TRP A 1 85  ? 4.045   -53.805  -9.268  1.00 60.92  ? 76  TRP A CZ2 1 
ATOM   572  C CZ3 . TRP A 1 85  ? 5.196   -53.997  -11.387 1.00 64.98  ? 76  TRP A CZ3 1 
ATOM   573  C CH2 . TRP A 1 85  ? 4.812   -53.254  -10.263 1.00 63.02  ? 76  TRP A CH2 1 
ATOM   574  N N   . SER A 1 86  ? 0.940   -60.123  -11.643 1.00 62.86  ? 77  SER A N   1 
ATOM   575  C CA  . SER A 1 86  ? -0.299  -60.659  -11.123 1.00 65.59  ? 77  SER A CA  1 
ATOM   576  C C   . SER A 1 86  ? -0.338  -60.427  -9.623  1.00 64.98  ? 77  SER A C   1 
ATOM   577  O O   . SER A 1 86  ? -1.278  -59.836  -9.085  1.00 62.82  ? 77  SER A O   1 
ATOM   578  C CB  . SER A 1 86  ? -0.354  -62.148  -11.430 1.00 69.79  ? 77  SER A CB  1 
ATOM   579  O OG  . SER A 1 86  ? 0.963   -62.649  -11.565 1.00 68.95  ? 77  SER A OG  1 
ATOM   580  N N   . TYR A 1 87  ? 0.712   -60.884  -8.956  1.00 64.60  ? 78  TYR A N   1 
ATOM   581  C CA  . TYR A 1 87  ? 0.855   -60.677  -7.531  1.00 63.28  ? 78  TYR A CA  1 
ATOM   582  C C   . TYR A 1 87  ? 2.306   -60.454  -7.204  1.00 61.17  ? 78  TYR A C   1 
ATOM   583  O O   . TYR A 1 87  ? 3.128   -60.234  -8.093  1.00 59.93  ? 78  TYR A O   1 
ATOM   584  C CB  . TYR A 1 87  ? 0.299   -61.851  -6.727  1.00 62.39  ? 78  TYR A CB  1 
ATOM   585  C CG  . TYR A 1 87  ? 0.836   -63.211  -7.097  1.00 63.13  ? 78  TYR A CG  1 
ATOM   586  C CD1 . TYR A 1 87  ? 0.549   -63.786  -8.334  1.00 67.81  ? 78  TYR A CD1 1 
ATOM   587  C CD2 . TYR A 1 87  ? 1.592   -63.945  -6.197  1.00 63.06  ? 78  TYR A CD2 1 
ATOM   588  C CE1 . TYR A 1 87  ? 1.025   -65.053  -8.670  1.00 66.01  ? 78  TYR A CE1 1 
ATOM   589  C CE2 . TYR A 1 87  ? 2.068   -65.207  -6.522  1.00 65.55  ? 78  TYR A CE2 1 
ATOM   590  C CZ  . TYR A 1 87  ? 1.780   -65.753  -7.756  1.00 68.29  ? 78  TYR A CZ  1 
ATOM   591  O OH  . TYR A 1 87  ? 2.256   -67.000  -8.069  1.00 73.53  ? 78  TYR A OH  1 
ATOM   592  N N   . ILE A 1 88  ? 2.611   -60.469  -5.917  1.00 60.47  ? 79  ILE A N   1 
ATOM   593  C CA  . ILE A 1 88  ? 3.983   -60.300  -5.483  1.00 59.54  ? 79  ILE A CA  1 
ATOM   594  C C   . ILE A 1 88  ? 4.415   -61.414  -4.552  1.00 60.29  ? 79  ILE A C   1 
ATOM   595  O O   . ILE A 1 88  ? 3.667   -61.836  -3.666  1.00 61.04  ? 79  ILE A O   1 
ATOM   596  C CB  . ILE A 1 88  ? 4.193   -58.977  -4.760  1.00 59.20  ? 79  ILE A CB  1 
ATOM   597  C CG1 . ILE A 1 88  ? 3.842   -57.807  -5.677  1.00 61.70  ? 79  ILE A CG1 1 
ATOM   598  C CG2 . ILE A 1 88  ? 5.633   -58.875  -4.289  1.00 55.40  ? 79  ILE A CG2 1 
ATOM   599  C CD1 . ILE A 1 88  ? 4.203   -56.461  -5.091  1.00 56.82  ? 79  ILE A CD1 1 
ATOM   600  N N   . VAL A 1 89  ? 5.633   -61.888  -4.761  1.00 58.91  ? 80  VAL A N   1 
ATOM   601  C CA  . VAL A 1 89  ? 6.192   -62.917  -3.914  1.00 60.89  ? 80  VAL A CA  1 
ATOM   602  C C   . VAL A 1 89  ? 7.510   -62.429  -3.351  1.00 59.95  ? 80  VAL A C   1 
ATOM   603  O O   . VAL A 1 89  ? 8.346   -61.914  -4.089  1.00 57.31  ? 80  VAL A O   1 
ATOM   604  C CB  . VAL A 1 89  ? 6.420   -64.225  -4.701  1.00 61.16  ? 80  VAL A CB  1 
ATOM   605  C CG1 . VAL A 1 89  ? 7.416   -65.104  -3.989  1.00 63.10  ? 80  VAL A CG1 1 
ATOM   606  C CG2 . VAL A 1 89  ? 5.102   -64.962  -4.898  1.00 63.01  ? 80  VAL A CG2 1 
ATOM   607  N N   . GLU A 1 90  ? 7.679   -62.556  -2.037  1.00 61.69  ? 81  GLU A N   1 
ATOM   608  C CA  . GLU A 1 90  ? 8.986   -62.344  -1.411  1.00 63.65  ? 81  GLU A CA  1 
ATOM   609  C C   . GLU A 1 90  ? 9.357   -63.545  -0.549  1.00 64.48  ? 81  GLU A C   1 
ATOM   610  O O   . GLU A 1 90  ? 8.491   -64.176  0.064   1.00 64.10  ? 81  GLU A O   1 
ATOM   611  C CB  . GLU A 1 90  ? 9.077   -61.012  -0.640  1.00 57.43  ? 81  GLU A CB  1 
ATOM   612  C CG  . GLU A 1 90  ? 7.987   -60.754  0.388   1.00 58.59  ? 81  GLU A CG  1 
ATOM   613  C CD  . GLU A 1 90  ? 7.852   -59.272  0.740   1.00 54.26  ? 81  GLU A CD  1 
ATOM   614  O OE1 . GLU A 1 90  ? 7.411   -58.952  1.867   1.00 49.80  ? 81  GLU A OE1 1 
ATOM   615  O OE2 . GLU A 1 90  ? 8.173   -58.421  -0.116  1.00 51.19  ? 81  GLU A OE2 1 
ATOM   616  N N   . THR A 1 91  ? 10.645  -63.869  -0.528  1.00 65.47  ? 82  THR A N   1 
ATOM   617  C CA  . THR A 1 91  ? 11.081  -65.103  0.090   1.00 67.72  ? 82  THR A CA  1 
ATOM   618  C C   . THR A 1 91  ? 11.225  -64.933  1.579   1.00 67.41  ? 82  THR A C   1 
ATOM   619  O O   . THR A 1 91  ? 11.163  -63.824  2.096   1.00 69.04  ? 82  THR A O   1 
ATOM   620  C CB  . THR A 1 91  ? 12.442  -65.522  -0.461  1.00 68.99  ? 82  THR A CB  1 
ATOM   621  O OG1 . THR A 1 91  ? 13.472  -64.741  0.158   1.00 69.40  ? 82  THR A OG1 1 
ATOM   622  C CG2 . THR A 1 91  ? 12.486  -65.274  -1.945  1.00 66.49  ? 82  THR A CG2 1 
ATOM   623  N N   . SER A 1 92  ? 11.479  -66.042  2.256   1.00 70.82  ? 83  SER A N   1 
ATOM   624  C CA  . SER A 1 92  ? 11.673  -66.028  3.692   1.00 71.46  ? 83  SER A CA  1 
ATOM   625  C C   . SER A 1 92  ? 13.034  -65.432  3.908   1.00 71.59  ? 83  SER A C   1 
ATOM   626  O O   . SER A 1 92  ? 13.378  -64.974  4.989   1.00 74.05  ? 83  SER A O   1 
ATOM   627  C CB  . SER A 1 92  ? 11.681  -67.455  4.224   1.00 72.87  ? 83  SER A CB  1 
ATOM   628  O OG  . SER A 1 92  ? 12.757  -68.183  3.648   1.00 71.66  ? 83  SER A OG  1 
ATOM   629  N N   . SER A 1 93  ? 13.814  -65.474  2.842   1.00 71.08  ? 84  SER A N   1 
ATOM   630  C CA  . SER A 1 93  ? 15.199  -65.078  2.878   1.00 72.22  ? 84  SER A CA  1 
ATOM   631  C C   . SER A 1 93  ? 15.384  -63.645  2.392   1.00 71.36  ? 84  SER A C   1 
ATOM   632  O O   . SER A 1 93  ? 16.517  -63.183  2.258   1.00 74.58  ? 84  SER A O   1 
ATOM   633  C CB  . SER A 1 93  ? 16.026  -66.052  2.034   1.00 76.56  ? 84  SER A CB  1 
ATOM   634  O OG  . SER A 1 93  ? 15.252  -67.198  1.696   1.00 77.12  ? 84  SER A OG  1 
ATOM   635  N N   . SER A 1 94  ? 14.301  -62.929  2.104   1.00 67.25  ? 85  SER A N   1 
ATOM   636  C CA  . SER A 1 94  ? 14.518  -61.624  1.509   1.00 67.00  ? 85  SER A CA  1 
ATOM   637  C C   . SER A 1 94  ? 14.595  -60.608  2.622   1.00 62.70  ? 85  SER A C   1 
ATOM   638  O O   . SER A 1 94  ? 13.591  -60.162  3.163   1.00 61.28  ? 85  SER A O   1 
ATOM   639  C CB  . SER A 1 94  ? 13.390  -61.279  0.522   1.00 68.17  ? 85  SER A CB  1 
ATOM   640  O OG  . SER A 1 94  ? 12.100  -61.437  1.093   1.00 65.14  ? 85  SER A OG  1 
ATOM   641  N N   . ASP A 1 95  ? 15.832  -60.244  2.928   1.00 66.02  ? 86  ASP A N   1 
ATOM   642  C CA  . ASP A 1 95  ? 16.160  -59.349  4.023   1.00 64.98  ? 86  ASP A CA  1 
ATOM   643  C C   . ASP A 1 95  ? 16.517  -57.952  3.609   1.00 62.07  ? 86  ASP A C   1 
ATOM   644  O O   . ASP A 1 95  ? 16.810  -57.122  4.465   1.00 63.85  ? 86  ASP A O   1 
ATOM   645  C CB  . ASP A 1 95  ? 17.310  -59.919  4.834   1.00 70.67  ? 86  ASP A CB  1 
ATOM   646  C CG  . ASP A 1 95  ? 16.960  -61.229  5.466   1.00 76.25  ? 86  ASP A CG  1 
ATOM   647  O OD1 . ASP A 1 95  ? 15.803  -61.354  5.933   1.00 77.66  ? 86  ASP A OD1 1 
ATOM   648  O OD2 . ASP A 1 95  ? 17.830  -62.129  5.483   1.00 79.56  ? 86  ASP A OD2 1 
ATOM   649  N N   . ASN A 1 96  ? 16.533  -57.670  2.314   1.00 58.90  ? 87  ASN A N   1 
ATOM   650  C CA  . ASN A 1 96  ? 17.061  -56.382  1.943   1.00 56.39  ? 87  ASN A CA  1 
ATOM   651  C C   . ASN A 1 96  ? 15.963  -55.333  1.903   1.00 53.81  ? 87  ASN A C   1 
ATOM   652  O O   . ASN A 1 96  ? 15.167  -55.219  0.977   1.00 53.19  ? 87  ASN A O   1 
ATOM   653  C CB  . ASN A 1 96  ? 17.847  -56.496  0.649   1.00 58.92  ? 87  ASN A CB  1 
ATOM   654  C CG  . ASN A 1 96  ? 19.259  -56.953  0.898   1.00 62.59  ? 87  ASN A CG  1 
ATOM   655  O OD1 . ASN A 1 96  ? 19.655  -58.063  0.552   1.00 63.37  ? 87  ASN A OD1 1 
ATOM   656  N ND2 . ASN A 1 96  ? 20.030  -56.091  1.531   1.00 62.13  ? 87  ASN A ND2 1 
ATOM   657  N N   . GLY A 1 97  ? 15.971  -54.586  2.993   1.00 52.49  ? 88  GLY A N   1 
ATOM   658  C CA  . GLY A 1 97  ? 14.980  -53.605  3.391   1.00 52.72  ? 88  GLY A CA  1 
ATOM   659  C C   . GLY A 1 97  ? 15.497  -52.183  3.376   1.00 49.61  ? 88  GLY A C   1 
ATOM   660  O O   . GLY A 1 97  ? 16.177  -51.724  2.452   1.00 47.58  ? 88  GLY A O   1 
ATOM   661  N N   . THR A 1 98  ? 15.141  -51.474  4.445   1.00 48.34  ? 89  THR A N   1 
ATOM   662  C CA  . THR A 1 98  ? 15.667  -50.143  4.652   1.00 45.70  ? 89  THR A CA  1 
ATOM   663  C C   . THR A 1 98  ? 17.048  -50.318  5.258   1.00 45.06  ? 89  THR A C   1 
ATOM   664  O O   . THR A 1 98  ? 17.173  -50.676  6.422   1.00 49.25  ? 89  THR A O   1 
ATOM   665  C CB  . THR A 1 98  ? 14.789  -49.396  5.677   1.00 44.13  ? 89  THR A CB  1 
ATOM   666  O OG1 . THR A 1 98  ? 14.583  -50.237  6.816   1.00 45.98  ? 89  THR A OG1 1 
ATOM   667  C CG2 . THR A 1 98  ? 13.431  -49.098  5.088   1.00 45.20  ? 89  THR A CG2 1 
ATOM   668  N N   . CYS A 1 99  ? 18.087  -49.989  4.497   1.00 46.97  ? 90  CYS A N   1 
ATOM   669  C CA  . CYS A 1 99  ? 19.453  -50.216  4.953   1.00 46.58  ? 90  CYS A CA  1 
ATOM   670  C C   . CYS A 1 99  ? 19.884  -49.138  5.926   1.00 45.57  ? 90  CYS A C   1 
ATOM   671  O O   . CYS A 1 99  ? 20.693  -49.388  6.814   1.00 47.12  ? 90  CYS A O   1 
ATOM   672  C CB  . CYS A 1 99  ? 20.436  -50.352  3.780   1.00 52.38  ? 90  CYS A CB  1 
ATOM   673  S SG  . CYS A 1 99  ? 20.226  -49.180  2.426   1.00 54.30  ? 90  CYS A SG  1 
ATOM   674  N N   . TYR A 1 100 ? 19.322  -47.945  5.770   1.00 43.81  ? 91  TYR A N   1 
ATOM   675  C CA  . TYR A 1 100 ? 19.407  -46.956  6.821   1.00 41.58  ? 91  TYR A CA  1 
ATOM   676  C C   . TYR A 1 100 ? 18.207  -47.210  7.704   1.00 43.03  ? 91  TYR A C   1 
ATOM   677  O O   . TYR A 1 100 ? 17.081  -47.295  7.208   1.00 42.48  ? 91  TYR A O   1 
ATOM   678  C CB  . TYR A 1 100 ? 19.356  -45.534  6.274   1.00 40.73  ? 91  TYR A CB  1 
ATOM   679  C CG  . TYR A 1 100 ? 19.784  -44.539  7.305   1.00 40.73  ? 91  TYR A CG  1 
ATOM   680  C CD1 . TYR A 1 100 ? 18.872  -44.017  8.213   1.00 43.94  ? 91  TYR A CD1 1 
ATOM   681  C CD2 . TYR A 1 100 ? 21.108  -44.155  7.409   1.00 42.16  ? 91  TYR A CD2 1 
ATOM   682  C CE1 . TYR A 1 100 ? 19.266  -43.111  9.193   1.00 44.16  ? 91  TYR A CE1 1 
ATOM   683  C CE2 . TYR A 1 100 ? 21.518  -43.255  8.376   1.00 44.09  ? 91  TYR A CE2 1 
ATOM   684  C CZ  . TYR A 1 100 ? 20.599  -42.731  9.268   1.00 45.07  ? 91  TYR A CZ  1 
ATOM   685  O OH  . TYR A 1 100 ? 21.031  -41.834  10.229  1.00 45.87  ? 91  TYR A OH  1 
ATOM   686  N N   . PRO A 1 101 ? 18.440  -47.337  9.015   1.00 41.34  ? 92  PRO A N   1 
ATOM   687  C CA  . PRO A 1 101 ? 17.390  -47.790  9.926   1.00 39.07  ? 92  PRO A CA  1 
ATOM   688  C C   . PRO A 1 101 ? 16.305  -46.731  10.075  1.00 41.19  ? 92  PRO A C   1 
ATOM   689  O O   . PRO A 1 101 ? 16.577  -45.531  9.981   1.00 41.41  ? 92  PRO A O   1 
ATOM   690  C CB  . PRO A 1 101 ? 18.142  -47.982  11.231  1.00 39.70  ? 92  PRO A CB  1 
ATOM   691  C CG  . PRO A 1 101 ? 19.229  -46.975  11.171  1.00 40.77  ? 92  PRO A CG  1 
ATOM   692  C CD  . PRO A 1 101 ? 19.655  -46.922  9.731   1.00 39.36  ? 92  PRO A CD  1 
ATOM   693  N N   . GLY A 1 102 ? 15.078  -47.177  10.304  1.00 40.23  ? 93  GLY A N   1 
ATOM   694  C CA  . GLY A 1 102 ? 13.956  -46.264  10.377  1.00 39.92  ? 93  GLY A CA  1 
ATOM   695  C C   . GLY A 1 102 ? 12.645  -46.963  10.093  1.00 40.65  ? 93  GLY A C   1 
ATOM   696  O O   . GLY A 1 102 ? 12.620  -48.135  9.701   1.00 40.28  ? 93  GLY A O   1 
ATOM   697  N N   . ASP A 1 103 ? 11.549  -46.239  10.290  1.00 40.49  ? 94  ASP A N   1 
ATOM   698  C CA  . ASP A 1 103 ? 10.219  -46.784  10.055  1.00 40.94  ? 94  ASP A CA  1 
ATOM   699  C C   . ASP A 1 103 ? 9.707   -46.462  8.658   1.00 41.85  ? 94  ASP A C   1 
ATOM   700  O O   . ASP A 1 103 ? 9.708   -45.299  8.220   1.00 41.46  ? 94  ASP A O   1 
ATOM   701  C CB  . ASP A 1 103 ? 9.201   -46.214  11.041  1.00 41.24  ? 94  ASP A CB  1 
ATOM   702  C CG  . ASP A 1 103 ? 9.551   -46.495  12.481  1.00 43.23  ? 94  ASP A CG  1 
ATOM   703  O OD1 . ASP A 1 103 ? 10.178  -47.549  12.746  1.00 40.92  ? 94  ASP A OD1 1 
ATOM   704  O OD2 . ASP A 1 103 ? 9.186   -45.646  13.339  1.00 41.11  ? 94  ASP A OD2 1 
ATOM   705  N N   . PHE A 1 104 ? 9.240   -47.497  7.974   1.00 38.74  ? 95  PHE A N   1 
ATOM   706  C CA  . PHE A 1 104 ? 8.439   -47.284  6.790   1.00 39.96  ? 95  PHE A CA  1 
ATOM   707  C C   . PHE A 1 104 ? 7.005   -47.001  7.225   1.00 39.91  ? 95  PHE A C   1 
ATOM   708  O O   . PHE A 1 104 ? 6.421   -47.747  8.010   1.00 39.54  ? 95  PHE A O   1 
ATOM   709  C CB  . PHE A 1 104 ? 8.479   -48.501  5.892   1.00 41.15  ? 95  PHE A CB  1 
ATOM   710  C CG  . PHE A 1 104 ? 8.278   -48.177  4.457   1.00 42.40  ? 95  PHE A CG  1 
ATOM   711  C CD1 . PHE A 1 104 ? 7.039   -47.780  3.994   1.00 41.72  ? 95  PHE A CD1 1 
ATOM   712  C CD2 . PHE A 1 104 ? 9.336   -48.254  3.565   1.00 42.99  ? 95  PHE A CD2 1 
ATOM   713  C CE1 . PHE A 1 104 ? 6.854   -47.472  2.658   1.00 39.90  ? 95  PHE A CE1 1 
ATOM   714  C CE2 . PHE A 1 104 ? 9.161   -47.949  2.225   1.00 38.93  ? 95  PHE A CE2 1 
ATOM   715  C CZ  . PHE A 1 104 ? 7.920   -47.551  1.773   1.00 36.10  ? 95  PHE A CZ  1 
ATOM   716  N N   . ILE A 1 105 ? 6.442   -45.920  6.704   1.00 40.45  ? 96  ILE A N   1 
ATOM   717  C CA  . ILE A 1 105 ? 5.141   -45.441  7.158   1.00 42.16  ? 96  ILE A CA  1 
ATOM   718  C C   . ILE A 1 105 ? 3.999   -45.908  6.228   1.00 42.86  ? 96  ILE A C   1 
ATOM   719  O O   . ILE A 1 105 ? 4.138   -45.910  4.992   1.00 43.50  ? 96  ILE A O   1 
ATOM   720  C CB  . ILE A 1 105 ? 5.194   -43.901  7.354   1.00 42.18  ? 96  ILE A CB  1 
ATOM   721  C CG1 . ILE A 1 105 ? 6.292   -43.552  8.364   1.00 40.44  ? 96  ILE A CG1 1 
ATOM   722  C CG2 . ILE A 1 105 ? 3.852   -43.344  7.795   1.00 41.95  ? 96  ILE A CG2 1 
ATOM   723  C CD1 . ILE A 1 105 ? 6.107   -44.202  9.702   1.00 37.91  ? 96  ILE A CD1 1 
ATOM   724  N N   . ASP A 1 106 ? 2.884   -46.344  6.812   1.00 40.22  ? 97  ASP A N   1 
ATOM   725  C CA  . ASP A 1 106 ? 1.782   -46.872  5.997   1.00 42.58  ? 97  ASP A CA  1 
ATOM   726  C C   . ASP A 1 106 ? 2.234   -48.045  5.114   1.00 43.16  ? 97  ASP A C   1 
ATOM   727  O O   . ASP A 1 106 ? 1.647   -48.320  4.064   1.00 43.08  ? 97  ASP A O   1 
ATOM   728  C CB  . ASP A 1 106 ? 1.200   -45.776  5.110   1.00 46.57  ? 97  ASP A CB  1 
ATOM   729  C CG  . ASP A 1 106 ? 0.393   -44.780  5.884   1.00 47.05  ? 97  ASP A CG  1 
ATOM   730  O OD1 . ASP A 1 106 ? -0.649  -45.193  6.440   1.00 46.29  ? 97  ASP A OD1 1 
ATOM   731  O OD2 . ASP A 1 106 ? 0.788   -43.591  5.922   1.00 47.10  ? 97  ASP A OD2 1 
ATOM   732  N N   . TYR A 1 107 ? 3.265   -48.747  5.566   1.00 42.31  ? 98  TYR A N   1 
ATOM   733  C CA  . TYR A 1 107 ? 3.868   -49.837  4.814   1.00 41.95  ? 98  TYR A CA  1 
ATOM   734  C C   . TYR A 1 107 ? 2.853   -50.858  4.329   1.00 40.73  ? 98  TYR A C   1 
ATOM   735  O O   . TYR A 1 107 ? 2.823   -51.222  3.161   1.00 41.06  ? 98  TYR A O   1 
ATOM   736  C CB  . TYR A 1 107 ? 4.896   -50.534  5.693   1.00 40.75  ? 98  TYR A CB  1 
ATOM   737  C CG  . TYR A 1 107 ? 5.738   -51.574  4.988   1.00 40.38  ? 98  TYR A CG  1 
ATOM   738  C CD1 . TYR A 1 107 ? 6.014   -51.488  3.628   1.00 40.59  ? 98  TYR A CD1 1 
ATOM   739  C CD2 . TYR A 1 107 ? 6.254   -52.651  5.689   1.00 40.73  ? 98  TYR A CD2 1 
ATOM   740  C CE1 . TYR A 1 107 ? 6.797   -52.445  2.995   1.00 39.68  ? 98  TYR A CE1 1 
ATOM   741  C CE2 . TYR A 1 107 ? 7.033   -53.612  5.065   1.00 42.60  ? 98  TYR A CE2 1 
ATOM   742  C CZ  . TYR A 1 107 ? 7.301   -53.503  3.717   1.00 41.11  ? 98  TYR A CZ  1 
ATOM   743  O OH  . TYR A 1 107 ? 8.073   -54.459  3.107   1.00 42.69  ? 98  TYR A OH  1 
ATOM   744  N N   . GLU A 1 108 ? 2.035   -51.339  5.244   1.00 43.82  ? 99  GLU A N   1 
ATOM   745  C CA  . GLU A 1 108 ? 1.081   -52.375  4.906   1.00 46.20  ? 99  GLU A CA  1 
ATOM   746  C C   . GLU A 1 108 ? 0.186   -51.892  3.781   1.00 44.00  ? 99  GLU A C   1 
ATOM   747  O O   . GLU A 1 108 ? -0.067  -52.618  2.827   1.00 45.94  ? 99  GLU A O   1 
ATOM   748  C CB  . GLU A 1 108 ? 0.247   -52.741  6.137   1.00 49.79  ? 99  GLU A CB  1 
ATOM   749  C CG  . GLU A 1 108 ? -0.286  -54.167  6.115   1.00 54.85  ? 99  GLU A CG  1 
ATOM   750  C CD  . GLU A 1 108 ? 0.819   -55.195  6.319   1.00 58.05  ? 99  GLU A CD  1 
ATOM   751  O OE1 . GLU A 1 108 ? 1.996   -54.778  6.479   1.00 53.38  ? 99  GLU A OE1 1 
ATOM   752  O OE2 . GLU A 1 108 ? 0.505   -56.412  6.332   1.00 60.32  ? 99  GLU A OE2 1 
ATOM   753  N N   . GLU A 1 109 ? -0.288  -50.656  3.899   1.00 42.88  ? 100 GLU A N   1 
ATOM   754  C CA  . GLU A 1 109 ? -1.182  -50.079  2.903   1.00 44.29  ? 100 GLU A CA  1 
ATOM   755  C C   . GLU A 1 109 ? -0.499  -49.991  1.551   1.00 47.41  ? 100 GLU A C   1 
ATOM   756  O O   . GLU A 1 109 ? -1.103  -50.262  0.519   1.00 50.63  ? 100 GLU A O   1 
ATOM   757  C CB  . GLU A 1 109 ? -1.641  -48.684  3.327   1.00 44.87  ? 100 GLU A CB  1 
ATOM   758  C CG  . GLU A 1 109 ? -2.354  -47.887  2.228   1.00 44.74  ? 100 GLU A CG  1 
ATOM   759  C CD  . GLU A 1 109 ? -2.564  -46.433  2.621   1.00 50.51  ? 100 GLU A CD  1 
ATOM   760  O OE1 . GLU A 1 109 ? -2.286  -46.094  3.795   1.00 53.29  ? 100 GLU A OE1 1 
ATOM   761  O OE2 . GLU A 1 109 ? -2.985  -45.622  1.764   1.00 51.96  ? 100 GLU A OE2 1 
ATOM   762  N N   . LEU A 1 110 ? 0.762   -49.589  1.553   1.00 44.83  ? 101 LEU A N   1 
ATOM   763  C CA  . LEU A 1 110 ? 1.501   -49.535  0.316   1.00 44.26  ? 101 LEU A CA  1 
ATOM   764  C C   . LEU A 1 110 ? 1.607   -50.932  -0.258  1.00 47.37  ? 101 LEU A C   1 
ATOM   765  O O   . LEU A 1 110 ? 1.319   -51.151  -1.430  1.00 50.33  ? 101 LEU A O   1 
ATOM   766  C CB  . LEU A 1 110 ? 2.884   -48.958  0.537   1.00 43.22  ? 101 LEU A CB  1 
ATOM   767  C CG  . LEU A 1 110 ? 3.683   -48.919  -0.761  1.00 43.31  ? 101 LEU A CG  1 
ATOM   768  C CD1 . LEU A 1 110 ? 2.904   -48.150  -1.816  1.00 45.12  ? 101 LEU A CD1 1 
ATOM   769  C CD2 . LEU A 1 110 ? 5.037   -48.284  -0.524  1.00 42.67  ? 101 LEU A CD2 1 
ATOM   770  N N   . ARG A 1 111 ? 2.004   -51.887  0.570   1.00 46.72  ? 102 ARG A N   1 
ATOM   771  C CA  . ARG A 1 111 ? 2.122   -53.264  0.110   1.00 47.57  ? 102 ARG A CA  1 
ATOM   772  C C   . ARG A 1 111 ? 0.871   -53.723  -0.612  1.00 51.08  ? 102 ARG A C   1 
ATOM   773  O O   . ARG A 1 111 ? 0.954   -54.480  -1.565  1.00 52.26  ? 102 ARG A O   1 
ATOM   774  C CB  . ARG A 1 111 ? 2.379   -54.206  1.282   1.00 46.26  ? 102 ARG A CB  1 
ATOM   775  C CG  . ARG A 1 111 ? 3.781   -54.130  1.809   1.00 44.47  ? 102 ARG A CG  1 
ATOM   776  C CD  . ARG A 1 111 ? 3.863   -54.693  3.183   1.00 42.57  ? 102 ARG A CD  1 
ATOM   777  N NE  . ARG A 1 111 ? 3.607   -56.126  3.200   1.00 48.32  ? 102 ARG A NE  1 
ATOM   778  C CZ  . ARG A 1 111 ? 4.528   -57.049  2.944   1.00 45.80  ? 102 ARG A CZ  1 
ATOM   779  N NH1 . ARG A 1 111 ? 5.757   -56.676  2.626   1.00 37.00  ? 102 ARG A NH1 1 
ATOM   780  N NH2 . ARG A 1 111 ? 4.215   -58.342  3.004   1.00 47.65  ? 102 ARG A NH2 1 
ATOM   781  N N   . GLU A 1 112 ? -0.291  -53.294  -0.133  1.00 52.50  ? 103 GLU A N   1 
ATOM   782  C CA  . GLU A 1 112 ? -1.550  -53.705  -0.738  1.00 55.11  ? 103 GLU A CA  1 
ATOM   783  C C   . GLU A 1 112 ? -1.811  -53.013  -2.075  1.00 56.24  ? 103 GLU A C   1 
ATOM   784  O O   . GLU A 1 112 ? -2.290  -53.631  -3.019  1.00 57.29  ? 103 GLU A O   1 
ATOM   785  C CB  . GLU A 1 112 ? -2.713  -53.438  0.213   1.00 59.07  ? 103 GLU A CB  1 
ATOM   786  C CG  . GLU A 1 112 ? -4.063  -53.835  -0.366  1.00 66.53  ? 103 GLU A CG  1 
ATOM   787  C CD  . GLU A 1 112 ? -5.093  -54.107  0.708   1.00 76.80  ? 103 GLU A CD  1 
ATOM   788  O OE1 . GLU A 1 112 ? -6.259  -54.384  0.350   1.00 81.54  ? 103 GLU A OE1 1 
ATOM   789  O OE2 . GLU A 1 112 ? -4.732  -54.054  1.909   1.00 76.45  ? 103 GLU A OE2 1 
ATOM   790  N N   . GLN A 1 113 ? -1.517  -51.722  -2.149  1.00 54.73  ? 104 GLN A N   1 
ATOM   791  C CA  . GLN A 1 113 ? -1.659  -50.997  -3.404  1.00 58.72  ? 104 GLN A CA  1 
ATOM   792  C C   . GLN A 1 113 ? -0.907  -51.675  -4.534  1.00 58.67  ? 104 GLN A C   1 
ATOM   793  O O   . GLN A 1 113 ? -1.334  -51.638  -5.683  1.00 63.35  ? 104 GLN A O   1 
ATOM   794  C CB  . GLN A 1 113 ? -1.146  -49.567  -3.254  1.00 58.92  ? 104 GLN A CB  1 
ATOM   795  C CG  . GLN A 1 113 ? -2.070  -48.667  -2.450  1.00 62.66  ? 104 GLN A CG  1 
ATOM   796  C CD  . GLN A 1 113 ? -3.419  -48.487  -3.118  1.00 71.38  ? 104 GLN A CD  1 
ATOM   797  O OE1 . GLN A 1 113 ? -3.513  -47.885  -4.199  1.00 75.91  ? 104 GLN A OE1 1 
ATOM   798  N NE2 . GLN A 1 113 ? -4.473  -49.025  -2.492  1.00 67.49  ? 104 GLN A NE2 1 
ATOM   799  N N   . LEU A 1 114 ? 0.223   -52.280  -4.196  1.00 56.72  ? 105 LEU A N   1 
ATOM   800  C CA  . LEU A 1 114 ? 1.145   -52.803  -5.191  1.00 55.52  ? 105 LEU A CA  1 
ATOM   801  C C   . LEU A 1 114 ? 1.046   -54.303  -5.470  1.00 56.88  ? 105 LEU A C   1 
ATOM   802  O O   . LEU A 1 114 ? 1.779   -54.821  -6.303  1.00 60.81  ? 105 LEU A O   1 
ATOM   803  C CB  . LEU A 1 114 ? 2.569   -52.413  -4.809  1.00 52.26  ? 105 LEU A CB  1 
ATOM   804  C CG  . LEU A 1 114 ? 2.663   -50.902  -4.635  1.00 51.66  ? 105 LEU A CG  1 
ATOM   805  C CD1 . LEU A 1 114 ? 4.021   -50.514  -4.124  1.00 51.97  ? 105 LEU A CD1 1 
ATOM   806  C CD2 . LEU A 1 114 ? 2.359   -50.214  -5.947  1.00 55.91  ? 105 LEU A CD2 1 
ATOM   807  N N   . SER A 1 115 ? 0.158   -55.008  -4.786  1.00 54.82  ? 106 SER A N   1 
ATOM   808  C CA  . SER A 1 115 ? 0.019   -56.440  -5.026  1.00 60.25  ? 106 SER A CA  1 
ATOM   809  C C   . SER A 1 115 ? -0.196  -56.749  -6.514  1.00 64.42  ? 106 SER A C   1 
ATOM   810  O O   . SER A 1 115 ? 0.517   -57.569  -7.102  1.00 62.69  ? 106 SER A O   1 
ATOM   811  C CB  . SER A 1 115 ? -1.126  -57.005  -4.189  1.00 63.06  ? 106 SER A CB  1 
ATOM   812  O OG  . SER A 1 115 ? -2.230  -56.114  -4.166  1.00 65.50  ? 106 SER A OG  1 
ATOM   813  N N   . SER A 1 116 ? -1.172  -56.075  -7.117  1.00 64.28  ? 107 SER A N   1 
ATOM   814  C CA  . SER A 1 116 ? -1.448  -56.252  -8.531  1.00 65.40  ? 107 SER A CA  1 
ATOM   815  C C   . SER A 1 116 ? -1.377  -54.932  -9.292  1.00 64.93  ? 107 SER A C   1 
ATOM   816  O O   . SER A 1 116 ? -1.916  -53.916  -8.862  1.00 66.50  ? 107 SER A O   1 
ATOM   817  C CB  . SER A 1 116 ? -2.808  -56.915  -8.733  1.00 67.79  ? 107 SER A CB  1 
ATOM   818  O OG  . SER A 1 116 ? -2.926  -57.412  -10.059 1.00 70.91  ? 107 SER A OG  1 
ATOM   819  N N   . VAL A 1 117 ? -0.697  -54.966  -10.428 1.00 64.07  ? 108 VAL A N   1 
ATOM   820  C CA  . VAL A 1 117 ? -0.469  -53.775  -11.226 1.00 67.50  ? 108 VAL A CA  1 
ATOM   821  C C   . VAL A 1 117 ? -0.629  -54.097  -12.722 1.00 72.57  ? 108 VAL A C   1 
ATOM   822  O O   . VAL A 1 117 ? -0.201  -55.161  -13.189 1.00 71.96  ? 108 VAL A O   1 
ATOM   823  C CB  . VAL A 1 117 ? 0.940   -53.185  -10.926 1.00 65.28  ? 108 VAL A CB  1 
ATOM   824  C CG1 . VAL A 1 117 ? 1.695   -52.887  -12.208 1.00 66.92  ? 108 VAL A CG1 1 
ATOM   825  C CG2 . VAL A 1 117 ? 0.839   -51.941  -10.046 1.00 63.93  ? 108 VAL A CG2 1 
ATOM   826  N N   . SER A 1 118 ? -1.259  -53.186  -13.465 1.00 71.27  ? 109 SER A N   1 
ATOM   827  C CA  . SER A 1 118 ? -1.441  -53.356  -14.905 1.00 69.22  ? 109 SER A CA  1 
ATOM   828  C C   . SER A 1 118 ? -0.348  -52.603  -15.672 1.00 73.76  ? 109 SER A C   1 
ATOM   829  O O   . SER A 1 118 ? 0.395   -53.203  -16.448 1.00 79.86  ? 109 SER A O   1 
ATOM   830  C CB  . SER A 1 118 ? -2.845  -52.923  -15.354 1.00 70.01  ? 109 SER A CB  1 
ATOM   831  O OG  . SER A 1 118 ? -2.915  -51.524  -15.577 1.00 70.10  ? 109 SER A OG  1 
ATOM   832  N N   . SER A 1 119 ? -0.282  -51.285  -15.494 1.00 72.87  ? 110 SER A N   1 
ATOM   833  C CA  . SER A 1 119 ? 0.858   -50.511  -15.987 1.00 68.18  ? 110 SER A CA  1 
ATOM   834  C C   . SER A 1 119 ? 1.698   -49.964  -14.826 1.00 66.87  ? 110 SER A C   1 
ATOM   835  O O   . SER A 1 119 ? 1.174   -49.329  -13.913 1.00 66.09  ? 110 SER A O   1 
ATOM   836  C CB  . SER A 1 119 ? 0.417   -49.379  -16.934 1.00 66.84  ? 110 SER A CB  1 
ATOM   837  O OG  . SER A 1 119 ? -0.634  -48.590  -16.397 1.00 67.30  ? 110 SER A OG  1 
ATOM   838  N N   . PHE A 1 120 ? 2.999   -50.239  -14.850 1.00 66.06  ? 111 PHE A N   1 
ATOM   839  C CA  . PHE A 1 120 ? 3.907   -49.683  -13.852 1.00 64.76  ? 111 PHE A CA  1 
ATOM   840  C C   . PHE A 1 120 ? 5.119   -49.007  -14.503 1.00 64.91  ? 111 PHE A C   1 
ATOM   841  O O   . PHE A 1 120 ? 5.981   -49.677  -15.070 1.00 67.00  ? 111 PHE A O   1 
ATOM   842  C CB  . PHE A 1 120 ? 4.360   -50.782  -12.889 1.00 66.71  ? 111 PHE A CB  1 
ATOM   843  C CG  . PHE A 1 120 ? 5.087   -50.262  -11.676 1.00 66.92  ? 111 PHE A CG  1 
ATOM   844  C CD1 . PHE A 1 120 ? 4.413   -49.533  -10.709 1.00 66.39  ? 111 PHE A CD1 1 
ATOM   845  C CD2 . PHE A 1 120 ? 6.441   -50.505  -11.499 1.00 66.64  ? 111 PHE A CD2 1 
ATOM   846  C CE1 . PHE A 1 120 ? 5.080   -49.045  -9.601  1.00 64.58  ? 111 PHE A CE1 1 
ATOM   847  C CE2 . PHE A 1 120 ? 7.111   -50.021  -10.388 1.00 59.91  ? 111 PHE A CE2 1 
ATOM   848  C CZ  . PHE A 1 120 ? 6.432   -49.293  -9.443  1.00 60.10  ? 111 PHE A CZ  1 
ATOM   849  N N   . GLU A 1 121 ? 5.196   -47.681  -14.410 1.00 62.79  ? 112 GLU A N   1 
ATOM   850  C CA  . GLU A 1 121 ? 6.220   -46.935  -15.153 1.00 64.38  ? 112 GLU A CA  1 
ATOM   851  C C   . GLU A 1 121 ? 7.121   -46.085  -14.250 1.00 62.40  ? 112 GLU A C   1 
ATOM   852  O O   . GLU A 1 121 ? 6.696   -45.058  -13.727 1.00 60.90  ? 112 GLU A O   1 
ATOM   853  C CB  . GLU A 1 121 ? 5.568   -46.032  -16.218 1.00 63.07  ? 112 GLU A CB  1 
ATOM   854  C CG  . GLU A 1 121 ? 5.453   -46.619  -17.631 1.00 63.94  ? 112 GLU A CG  1 
ATOM   855  C CD  . GLU A 1 121 ? 6.750   -46.522  -18.415 1.00 64.38  ? 112 GLU A CD  1 
ATOM   856  O OE1 . GLU A 1 121 ? 7.267   -45.390  -18.587 1.00 65.24  ? 112 GLU A OE1 1 
ATOM   857  O OE2 . GLU A 1 121 ? 7.261   -47.582  -18.843 1.00 64.00  ? 112 GLU A OE2 1 
ATOM   858  N N   . ARG A 1 122 ? 8.379   -46.487  -14.117 1.00 62.03  ? 113 ARG A N   1 
ATOM   859  C CA  . ARG A 1 122 ? 9.334   -45.756  -13.295 1.00 57.95  ? 113 ARG A CA  1 
ATOM   860  C C   . ARG A 1 122 ? 9.898   -44.559  -14.040 1.00 58.03  ? 113 ARG A C   1 
ATOM   861  O O   . ARG A 1 122 ? 10.524  -44.713  -15.084 1.00 63.80  ? 113 ARG A O   1 
ATOM   862  C CB  . ARG A 1 122 ? 10.475  -46.686  -12.882 1.00 57.94  ? 113 ARG A CB  1 
ATOM   863  C CG  . ARG A 1 122 ? 11.686  -45.986  -12.268 1.00 60.23  ? 113 ARG A CG  1 
ATOM   864  C CD  . ARG A 1 122 ? 12.596  -47.007  -11.579 1.00 65.76  ? 113 ARG A CD  1 
ATOM   865  N NE  . ARG A 1 122 ? 13.972  -46.533  -11.436 1.00 64.51  ? 113 ARG A NE  1 
ATOM   866  C CZ  . ARG A 1 122 ? 14.899  -46.651  -12.386 1.00 66.10  ? 113 ARG A CZ  1 
ATOM   867  N NH1 . ARG A 1 122 ? 14.595  -47.224  -13.548 1.00 65.50  ? 113 ARG A NH1 1 
ATOM   868  N NH2 . ARG A 1 122 ? 16.130  -46.192  -12.180 1.00 66.82  ? 113 ARG A NH2 1 
ATOM   869  N N   . PHE A 1 123 ? 9.696   -43.365  -13.502 1.00 56.98  ? 114 PHE A N   1 
ATOM   870  C CA  . PHE A 1 123 ? 10.268  -42.172  -14.114 1.00 56.00  ? 114 PHE A CA  1 
ATOM   871  C C   . PHE A 1 123 ? 10.978  -41.330  -13.075 1.00 56.54  ? 114 PHE A C   1 
ATOM   872  O O   . PHE A 1 123 ? 10.661  -41.416  -11.889 1.00 57.50  ? 114 PHE A O   1 
ATOM   873  C CB  . PHE A 1 123 ? 9.191   -41.348  -14.806 1.00 55.61  ? 114 PHE A CB  1 
ATOM   874  C CG  . PHE A 1 123 ? 8.309   -40.577  -13.871 1.00 58.00  ? 114 PHE A CG  1 
ATOM   875  C CD1 . PHE A 1 123 ? 7.214   -41.185  -13.271 1.00 56.77  ? 114 PHE A CD1 1 
ATOM   876  C CD2 . PHE A 1 123 ? 8.553   -39.232  -13.617 1.00 56.33  ? 114 PHE A CD2 1 
ATOM   877  C CE1 . PHE A 1 123 ? 6.382   -40.473  -12.435 1.00 54.05  ? 114 PHE A CE1 1 
ATOM   878  C CE2 . PHE A 1 123 ? 7.723   -38.512  -12.775 1.00 56.62  ? 114 PHE A CE2 1 
ATOM   879  C CZ  . PHE A 1 123 ? 6.634   -39.132  -12.187 1.00 54.90  ? 114 PHE A CZ  1 
ATOM   880  N N   . GLU A 1 124 ? 11.912  -40.488  -13.504 1.00 57.97  ? 115 GLU A N   1 
ATOM   881  C CA  . GLU A 1 124 ? 12.722  -39.774  -12.524 1.00 58.25  ? 115 GLU A CA  1 
ATOM   882  C C   . GLU A 1 124 ? 12.140  -38.384  -12.337 1.00 56.25  ? 115 GLU A C   1 
ATOM   883  O O   . GLU A 1 124 ? 12.412  -37.459  -13.098 1.00 56.09  ? 115 GLU A O   1 
ATOM   884  C CB  . GLU A 1 124 ? 14.182  -39.705  -12.995 1.00 54.86  ? 115 GLU A CB  1 
ATOM   885  C CG  . GLU A 1 124 ? 14.982  -38.548  -12.434 1.00 59.43  ? 115 GLU A CG  1 
ATOM   886  C CD  . GLU A 1 124 ? 16.416  -38.528  -12.939 1.00 63.04  ? 115 GLU A CD  1 
ATOM   887  O OE1 . GLU A 1 124 ? 16.701  -37.801  -13.918 1.00 64.91  ? 115 GLU A OE1 1 
ATOM   888  O OE2 . GLU A 1 124 ? 17.264  -39.234  -12.348 1.00 64.61  ? 115 GLU A OE2 1 
ATOM   889  N N   . ILE A 1 125 ? 11.417  -38.240  -11.233 1.00 57.35  ? 116 ILE A N   1 
ATOM   890  C CA  . ILE A 1 125 ? 10.472  -37.151  -11.048 1.00 56.00  ? 116 ILE A CA  1 
ATOM   891  C C   . ILE A 1 125 ? 11.169  -35.843  -10.708 1.00 58.06  ? 116 ILE A C   1 
ATOM   892  O O   . ILE A 1 125 ? 10.618  -34.763  -10.926 1.00 59.51  ? 116 ILE A O   1 
ATOM   893  C CB  . ILE A 1 125 ? 9.408   -37.522  -9.987  1.00 55.79  ? 116 ILE A CB  1 
ATOM   894  C CG1 . ILE A 1 125 ? 8.510   -36.331  -9.674  1.00 57.03  ? 116 ILE A CG1 1 
ATOM   895  C CG2 . ILE A 1 125 ? 10.048  -38.044  -8.713  1.00 50.46  ? 116 ILE A CG2 1 
ATOM   896  C CD1 . ILE A 1 125 ? 7.384   -36.683  -8.751  1.00 53.91  ? 116 ILE A CD1 1 
ATOM   897  N N   . PHE A 1 126 ? 12.380  -35.946  -10.167 1.00 57.91  ? 117 PHE A N   1 
ATOM   898  C CA  . PHE A 1 126 ? 13.240  -34.783  -9.954  1.00 58.32  ? 117 PHE A CA  1 
ATOM   899  C C   . PHE A 1 126 ? 14.661  -35.102  -10.422 1.00 59.39  ? 117 PHE A C   1 
ATOM   900  O O   . PHE A 1 126 ? 15.475  -35.595  -9.641  1.00 59.77  ? 117 PHE A O   1 
ATOM   901  C CB  . PHE A 1 126 ? 13.253  -34.363  -8.478  1.00 58.01  ? 117 PHE A CB  1 
ATOM   902  C CG  . PHE A 1 126 ? 11.971  -33.705  -8.000  1.00 57.98  ? 117 PHE A CG  1 
ATOM   903  C CD1 . PHE A 1 126 ? 11.579  -32.462  -8.486  1.00 58.48  ? 117 PHE A CD1 1 
ATOM   904  C CD2 . PHE A 1 126 ? 11.184  -34.314  -7.030  1.00 56.37  ? 117 PHE A CD2 1 
ATOM   905  C CE1 . PHE A 1 126 ? 10.412  -31.860  -8.034  1.00 55.68  ? 117 PHE A CE1 1 
ATOM   906  C CE2 . PHE A 1 126 ? 10.019  -33.719  -6.580  1.00 54.55  ? 117 PHE A CE2 1 
ATOM   907  C CZ  . PHE A 1 126 ? 9.634   -32.488  -7.081  1.00 54.58  ? 117 PHE A CZ  1 
ATOM   908  N N   . PRO A 1 127 ? 14.963  -34.830  -11.700 1.00 59.75  ? 118 PRO A N   1 
ATOM   909  C CA  . PRO A 1 127 ? 16.255  -35.205  -12.282 1.00 58.50  ? 118 PRO A CA  1 
ATOM   910  C C   . PRO A 1 127 ? 17.395  -34.776  -11.388 1.00 57.59  ? 118 PRO A C   1 
ATOM   911  O O   . PRO A 1 127 ? 17.457  -33.628  -10.952 1.00 56.33  ? 118 PRO A O   1 
ATOM   912  C CB  . PRO A 1 127 ? 16.298  -34.396  -13.577 1.00 60.68  ? 118 PRO A CB  1 
ATOM   913  C CG  . PRO A 1 127 ? 14.866  -34.264  -13.957 1.00 63.32  ? 118 PRO A CG  1 
ATOM   914  C CD  . PRO A 1 127 ? 14.094  -34.151  -12.672 1.00 60.31  ? 118 PRO A CD  1 
ATOM   915  N N   . LYS A 1 128 ? 18.315  -35.695  -11.143 1.00 57.70  ? 119 LYS A N   1 
ATOM   916  C CA  . LYS A 1 128 ? 19.386  -35.439  -10.196 1.00 56.80  ? 119 LYS A CA  1 
ATOM   917  C C   . LYS A 1 128 ? 20.280  -34.282  -10.639 1.00 55.82  ? 119 LYS A C   1 
ATOM   918  O O   . LYS A 1 128 ? 20.885  -33.604  -9.823  1.00 55.02  ? 119 LYS A O   1 
ATOM   919  C CB  . LYS A 1 128 ? 20.224  -36.698  -9.992  1.00 54.02  ? 119 LYS A CB  1 
ATOM   920  C CG  . LYS A 1 128 ? 21.449  -36.461  -9.138  1.00 52.11  ? 119 LYS A CG  1 
ATOM   921  C CD  . LYS A 1 128 ? 22.225  -37.741  -8.890  1.00 54.12  ? 119 LYS A CD  1 
ATOM   922  C CE  . LYS A 1 128 ? 23.360  -37.489  -7.914  1.00 53.28  ? 119 LYS A CE  1 
ATOM   923  N NZ  . LYS A 1 128 ? 24.133  -38.722  -7.631  1.00 54.51  ? 119 LYS A NZ  1 
ATOM   924  N N   . THR A 1 129 ? 20.383  -34.083  -11.943 1.00 54.86  ? 120 THR A N   1 
ATOM   925  C CA  . THR A 1 129 ? 21.273  -33.079  -12.501 1.00 54.06  ? 120 THR A CA  1 
ATOM   926  C C   . THR A 1 129 ? 20.624  -31.701  -12.454 1.00 55.70  ? 120 THR A C   1 
ATOM   927  O O   . THR A 1 129 ? 21.243  -30.700  -12.110 1.00 51.93  ? 120 THR A O   1 
ATOM   928  C CB  . THR A 1 129 ? 21.556  -33.434  -13.953 1.00 59.72  ? 120 THR A CB  1 
ATOM   929  O OG1 . THR A 1 129 ? 20.659  -32.706  -14.807 1.00 56.62  ? 120 THR A OG1 1 
ATOM   930  C CG2 . THR A 1 129 ? 21.337  -34.932  -14.145 1.00 58.02  ? 120 THR A CG2 1 
ATOM   931  N N   . SER A 1 130 ? 19.349  -31.672  -12.803 1.00 59.13  ? 121 SER A N   1 
ATOM   932  C CA  . SER A 1 130 ? 18.624  -30.424  -12.958 1.00 59.35  ? 121 SER A CA  1 
ATOM   933  C C   . SER A 1 130 ? 18.082  -29.801  -11.668 1.00 56.11  ? 121 SER A C   1 
ATOM   934  O O   . SER A 1 130 ? 18.150  -28.586  -11.490 1.00 54.98  ? 121 SER A O   1 
ATOM   935  C CB  . SER A 1 130 ? 17.493  -30.624  -13.974 1.00 59.93  ? 121 SER A CB  1 
ATOM   936  O OG  . SER A 1 130 ? 16.532  -29.579  -13.902 1.00 66.59  ? 121 SER A OG  1 
ATOM   937  N N   . SER A 1 131 ? 17.575  -30.641  -10.767 1.00 57.20  ? 122 SER A N   1 
ATOM   938  C CA  . SER A 1 131 ? 16.607  -30.210  -9.740  1.00 55.45  ? 122 SER A CA  1 
ATOM   939  C C   . SER A 1 131 ? 17.081  -29.396  -8.516  1.00 56.02  ? 122 SER A C   1 
ATOM   940  O O   . SER A 1 131 ? 16.308  -28.577  -8.003  1.00 56.23  ? 122 SER A O   1 
ATOM   941  C CB  . SER A 1 131 ? 15.775  -31.406  -9.254  1.00 54.42  ? 122 SER A CB  1 
ATOM   942  O OG  . SER A 1 131 ? 15.467  -32.295  -10.319 1.00 56.69  ? 122 SER A OG  1 
ATOM   943  N N   . TRP A 1 132 ? 18.315  -29.602  -8.045  1.00 55.44  ? 123 TRP A N   1 
ATOM   944  C CA  . TRP A 1 132 ? 18.708  -29.097  -6.717  1.00 52.56  ? 123 TRP A CA  1 
ATOM   945  C C   . TRP A 1 132 ? 19.942  -28.210  -6.737  1.00 53.95  ? 123 TRP A C   1 
ATOM   946  O O   . TRP A 1 132 ? 20.943  -28.524  -6.099  1.00 56.81  ? 123 TRP A O   1 
ATOM   947  C CB  . TRP A 1 132 ? 18.962  -30.271  -5.763  1.00 50.44  ? 123 TRP A CB  1 
ATOM   948  C CG  . TRP A 1 132 ? 17.913  -31.345  -5.839  1.00 48.06  ? 123 TRP A CG  1 
ATOM   949  C CD1 . TRP A 1 132 ? 18.066  -32.624  -6.317  1.00 49.72  ? 123 TRP A CD1 1 
ATOM   950  C CD2 . TRP A 1 132 ? 16.545  -31.228  -5.444  1.00 48.50  ? 123 TRP A CD2 1 
ATOM   951  N NE1 . TRP A 1 132 ? 16.873  -33.314  -6.236  1.00 44.72  ? 123 TRP A NE1 1 
ATOM   952  C CE2 . TRP A 1 132 ? 15.923  -32.478  -5.707  1.00 48.56  ? 123 TRP A CE2 1 
ATOM   953  C CE3 . TRP A 1 132 ? 15.780  -30.191  -4.892  1.00 47.45  ? 123 TRP A CE3 1 
ATOM   954  C CZ2 . TRP A 1 132 ? 14.572  -32.710  -5.437  1.00 50.08  ? 123 TRP A CZ2 1 
ATOM   955  C CZ3 . TRP A 1 132 ? 14.440  -30.422  -4.622  1.00 47.47  ? 123 TRP A CZ3 1 
ATOM   956  C CH2 . TRP A 1 132 ? 13.849  -31.674  -4.895  1.00 50.22  ? 123 TRP A CH2 1 
ATOM   957  N N   . PRO A 1 133 ? 19.864  -27.076  -7.436  1.00 57.40  ? 124 PRO A N   1 
ATOM   958  C CA  . PRO A 1 133 ? 21.068  -26.282  -7.680  1.00 55.29  ? 124 PRO A CA  1 
ATOM   959  C C   . PRO A 1 133 ? 21.708  -25.733  -6.417  1.00 58.18  ? 124 PRO A C   1 
ATOM   960  O O   . PRO A 1 133 ? 22.934  -25.569  -6.414  1.00 58.44  ? 124 PRO A O   1 
ATOM   961  C CB  . PRO A 1 133 ? 20.557  -25.132  -8.548  1.00 56.97  ? 124 PRO A CB  1 
ATOM   962  C CG  . PRO A 1 133 ? 19.115  -25.020  -8.222  1.00 58.20  ? 124 PRO A CG  1 
ATOM   963  C CD  . PRO A 1 133 ? 18.659  -26.433  -7.985  1.00 59.82  ? 124 PRO A CD  1 
ATOM   964  N N   . ASN A 1 134 ? 20.915  -25.432  -5.386  1.00 57.60  ? 125 ASN A N   1 
ATOM   965  C CA  . ASN A 1 134 ? 21.469  -24.797  -4.179  1.00 59.20  ? 125 ASN A CA  1 
ATOM   966  C C   . ASN A 1 134 ? 21.776  -25.720  -3.004  1.00 58.92  ? 125 ASN A C   1 
ATOM   967  O O   . ASN A 1 134 ? 22.232  -25.271  -1.946  1.00 60.32  ? 125 ASN A O   1 
ATOM   968  C CB  . ASN A 1 134 ? 20.614  -23.621  -3.729  1.00 56.34  ? 125 ASN A CB  1 
ATOM   969  C CG  . ASN A 1 134 ? 20.324  -22.684  -4.850  1.00 58.84  ? 125 ASN A CG  1 
ATOM   970  O OD1 . ASN A 1 134 ? 19.234  -22.721  -5.431  1.00 61.43  ? 125 ASN A OD1 1 
ATOM   971  N ND2 . ASN A 1 134 ? 21.307  -21.857  -5.200  1.00 55.07  ? 125 ASN A ND2 1 
ATOM   972  N N   . HIS A 1 135 ? 21.533  -27.007  -3.191  1.00 58.07  ? 126 HIS A N   1 
ATOM   973  C CA  . HIS A 1 135 ? 21.870  -27.982  -2.170  1.00 56.78  ? 126 HIS A CA  1 
ATOM   974  C C   . HIS A 1 135 ? 22.743  -29.058  -2.788  1.00 55.97  ? 126 HIS A C   1 
ATOM   975  O O   . HIS A 1 135 ? 22.827  -29.161  -4.006  1.00 56.13  ? 126 HIS A O   1 
ATOM   976  C CB  . HIS A 1 135 ? 20.601  -28.580  -1.586  1.00 54.04  ? 126 HIS A CB  1 
ATOM   977  C CG  . HIS A 1 135 ? 19.621  -27.552  -1.123  1.00 53.83  ? 126 HIS A CG  1 
ATOM   978  N ND1 . HIS A 1 135 ? 18.653  -27.020  -1.949  1.00 51.24  ? 126 HIS A ND1 1 
ATOM   979  C CD2 . HIS A 1 135 ? 19.471  -26.939  0.077   1.00 54.46  ? 126 HIS A CD2 1 
ATOM   980  C CE1 . HIS A 1 135 ? 17.938  -26.140  -1.272  1.00 54.58  ? 126 HIS A CE1 1 
ATOM   981  N NE2 . HIS A 1 135 ? 18.415  -26.067  -0.040  1.00 54.14  ? 126 HIS A NE2 1 
ATOM   982  N N   . ASP A 1 136 ? 23.397  -29.853  -1.949  1.00 54.88  ? 127 ASP A N   1 
ATOM   983  C CA  . ASP A 1 136 ? 24.378  -30.819  -2.431  1.00 51.65  ? 127 ASP A CA  1 
ATOM   984  C C   . ASP A 1 136 ? 23.842  -32.236  -2.612  1.00 48.90  ? 127 ASP A C   1 
ATOM   985  O O   . ASP A 1 136 ? 23.478  -32.917  -1.654  1.00 50.82  ? 127 ASP A O   1 
ATOM   986  C CB  . ASP A 1 136 ? 25.578  -30.838  -1.499  1.00 55.00  ? 127 ASP A CB  1 
ATOM   987  C CG  . ASP A 1 136 ? 26.598  -31.890  -1.889  1.00 58.75  ? 127 ASP A CG  1 
ATOM   988  O OD1 . ASP A 1 136 ? 26.211  -32.901  -2.529  1.00 58.24  ? 127 ASP A OD1 1 
ATOM   989  O OD2 . ASP A 1 136 ? 27.792  -31.701  -1.556  1.00 58.32  ? 127 ASP A OD2 1 
ATOM   990  N N   . SER A 1 137 ? 23.850  -32.696  -3.849  1.00 48.21  ? 128 SER A N   1 
ATOM   991  C CA  . SER A 1 137 ? 23.242  -33.973  -4.185  1.00 51.26  ? 128 SER A CA  1 
ATOM   992  C C   . SER A 1 137 ? 24.223  -35.141  -4.231  1.00 51.95  ? 128 SER A C   1 
ATOM   993  O O   . SER A 1 137 ? 23.812  -36.272  -4.489  1.00 53.86  ? 128 SER A O   1 
ATOM   994  C CB  . SER A 1 137 ? 22.547  -33.858  -5.535  1.00 51.11  ? 128 SER A CB  1 
ATOM   995  O OG  . SER A 1 137 ? 23.445  -33.278  -6.469  1.00 52.17  ? 128 SER A OG  1 
ATOM   996  N N   . ASN A 1 138 ? 25.511  -34.877  -4.023  1.00 50.63  ? 129 ASN A N   1 
ATOM   997  C CA  . ASN A 1 138 ? 26.524  -35.945  -4.064  1.00 51.16  ? 129 ASN A CA  1 
ATOM   998  C C   . ASN A 1 138 ? 27.062  -36.531  -2.762  1.00 55.00  ? 129 ASN A C   1 
ATOM   999  O O   . ASN A 1 138 ? 27.931  -37.392  -2.810  1.00 61.76  ? 129 ASN A O   1 
ATOM   1000 C CB  . ASN A 1 138 ? 27.708  -35.531  -4.919  1.00 52.49  ? 129 ASN A CB  1 
ATOM   1001 C CG  . ASN A 1 138 ? 27.295  -35.111  -6.297  1.00 57.69  ? 129 ASN A CG  1 
ATOM   1002 O OD1 . ASN A 1 138 ? 26.486  -35.777  -6.952  1.00 57.70  ? 129 ASN A OD1 1 
ATOM   1003 N ND2 . ASN A 1 138 ? 27.830  -33.982  -6.747  1.00 59.78  ? 129 ASN A ND2 1 
ATOM   1004 N N   . LYS A 1 139 ? 26.609  -36.057  -1.610  1.00 50.70  ? 130 LYS A N   1 
ATOM   1005 C CA  . LYS A 1 139 ? 27.197  -36.516  -0.354  1.00 50.77  ? 130 LYS A CA  1 
ATOM   1006 C C   . LYS A 1 139 ? 26.408  -37.625  0.326   1.00 50.28  ? 130 LYS A C   1 
ATOM   1007 O O   . LYS A 1 139 ? 26.774  -38.111  1.393   1.00 49.16  ? 130 LYS A O   1 
ATOM   1008 C CB  . LYS A 1 139 ? 27.358  -35.345  0.601   1.00 55.93  ? 130 LYS A CB  1 
ATOM   1009 C CG  . LYS A 1 139 ? 28.110  -34.183  0.001   1.00 58.55  ? 130 LYS A CG  1 
ATOM   1010 C CD  . LYS A 1 139 ? 29.606  -34.325  0.186   1.00 59.44  ? 130 LYS A CD  1 
ATOM   1011 C CE  . LYS A 1 139 ? 30.314  -32.975  0.065   1.00 64.62  ? 130 LYS A CE  1 
ATOM   1012 N NZ  . LYS A 1 139 ? 29.897  -32.015  1.140   1.00 68.60  ? 130 LYS A NZ  1 
ATOM   1013 N N   . GLY A 1 140 ? 25.366  -38.074  -0.341  1.00 53.97  ? 131 GLY A N   1 
ATOM   1014 C CA  . GLY A 1 140 ? 24.250  -38.745  0.294   1.00 52.22  ? 131 GLY A CA  1 
ATOM   1015 C C   . GLY A 1 140 ? 24.440  -40.221  0.582   1.00 49.82  ? 131 GLY A C   1 
ATOM   1016 O O   . GLY A 1 140 ? 23.512  -41.000  0.385   1.00 53.39  ? 131 GLY A O   1 
ATOM   1017 N N   . VAL A 1 141 ? 25.655  -40.634  0.920   1.00 48.58  ? 132 VAL A N   1 
ATOM   1018 C CA  . VAL A 1 141 ? 25.933  -42.063  1.131   1.00 52.88  ? 132 VAL A CA  1 
ATOM   1019 C C   . VAL A 1 141 ? 26.261  -42.442  2.563   1.00 52.40  ? 132 VAL A C   1 
ATOM   1020 O O   . VAL A 1 141 ? 26.708  -41.612  3.348   1.00 55.96  ? 132 VAL A O   1 
ATOM   1021 C CB  . VAL A 1 141 ? 27.129  -42.533  0.301   1.00 54.41  ? 132 VAL A CB  1 
ATOM   1022 C CG1 . VAL A 1 141 ? 26.701  -42.796  -1.120  1.00 52.27  ? 132 VAL A CG1 1 
ATOM   1023 C CG2 . VAL A 1 141 ? 28.248  -41.500  0.378   1.00 53.22  ? 132 VAL A CG2 1 
ATOM   1024 N N   . THR A 1 142 ? 26.051  -43.713  2.884   1.00 49.93  ? 133 THR A N   1 
ATOM   1025 C CA  . THR A 1 142 ? 26.282  -44.221  4.218   1.00 49.73  ? 133 THR A CA  1 
ATOM   1026 C C   . THR A 1 142 ? 26.990  -45.554  4.084   1.00 49.49  ? 133 THR A C   1 
ATOM   1027 O O   . THR A 1 142 ? 26.968  -46.167  3.021   1.00 51.48  ? 133 THR A O   1 
ATOM   1028 C CB  . THR A 1 142 ? 24.934  -44.464  4.921   1.00 51.87  ? 133 THR A CB  1 
ATOM   1029 O OG1 . THR A 1 142 ? 25.154  -44.948  6.257   1.00 49.96  ? 133 THR A OG1 1 
ATOM   1030 C CG2 . THR A 1 142 ? 24.097  -45.485  4.122   1.00 47.90  ? 133 THR A CG2 1 
ATOM   1031 N N   . ALA A 1 143 ? 27.617  -46.013  5.157   1.00 46.63  ? 134 ALA A N   1 
ATOM   1032 C CA  . ALA A 1 143 ? 28.100  -47.383  5.183   1.00 46.58  ? 134 ALA A CA  1 
ATOM   1033 C C   . ALA A 1 143 ? 26.967  -48.320  5.561   1.00 47.23  ? 134 ALA A C   1 
ATOM   1034 O O   . ALA A 1 143 ? 27.082  -49.541  5.421   1.00 47.44  ? 134 ALA A O   1 
ATOM   1035 C CB  . ALA A 1 143 ? 29.236  -47.525  6.152   1.00 48.86  ? 134 ALA A CB  1 
ATOM   1036 N N   . ALA A 1 144 ? 25.882  -47.736  6.063   1.00 44.91  ? 135 ALA A N   1 
ATOM   1037 C CA  . ALA A 1 144 ? 24.679  -48.494  6.363   1.00 46.26  ? 135 ALA A CA  1 
ATOM   1038 C C   . ALA A 1 144 ? 24.142  -49.127  5.086   1.00 49.35  ? 135 ALA A C   1 
ATOM   1039 O O   . ALA A 1 144 ? 23.445  -50.140  5.138   1.00 49.20  ? 135 ALA A O   1 
ATOM   1040 C CB  . ALA A 1 144 ? 23.625  -47.597  6.984   1.00 44.16  ? 135 ALA A CB  1 
ATOM   1041 N N   . CYS A 1 145 ? 24.469  -48.525  3.943   1.00 46.66  ? 136 CYS A N   1 
ATOM   1042 C CA  . CYS A 1 145 ? 23.977  -49.000  2.649   1.00 50.85  ? 136 CYS A CA  1 
ATOM   1043 C C   . CYS A 1 145 ? 25.121  -49.258  1.677   1.00 51.24  ? 136 CYS A C   1 
ATOM   1044 O O   . CYS A 1 145 ? 25.260  -48.553  0.685   1.00 48.69  ? 136 CYS A O   1 
ATOM   1045 C CB  . CYS A 1 145 ? 23.022  -47.983  2.019   1.00 50.39  ? 136 CYS A CB  1 
ATOM   1046 S SG  . CYS A 1 145 ? 21.534  -47.668  2.975   1.00 52.79  ? 136 CYS A SG  1 
ATOM   1047 N N   . PRO A 1 146 ? 25.953  -50.264  1.961   1.00 50.51  ? 137 PRO A N   1 
ATOM   1048 C CA  . PRO A 1 146 ? 27.106  -50.492  1.096   1.00 51.42  ? 137 PRO A CA  1 
ATOM   1049 C C   . PRO A 1 146 ? 26.690  -51.131  -0.209  1.00 54.87  ? 137 PRO A C   1 
ATOM   1050 O O   . PRO A 1 146 ? 25.828  -52.001  -0.222  1.00 58.00  ? 137 PRO A O   1 
ATOM   1051 C CB  . PRO A 1 146 ? 27.928  -51.490  1.892   1.00 52.13  ? 137 PRO A CB  1 
ATOM   1052 C CG  . PRO A 1 146 ? 26.898  -52.288  2.626   1.00 51.96  ? 137 PRO A CG  1 
ATOM   1053 C CD  . PRO A 1 146 ? 25.810  -51.315  2.982   1.00 50.26  ? 137 PRO A CD  1 
ATOM   1054 N N   . HIS A 1 147 ? 27.299  -50.699  -1.299  1.00 55.28  ? 138 HIS A N   1 
ATOM   1055 C CA  . HIS A 1 147 ? 27.214  -51.445  -2.533  1.00 59.04  ? 138 HIS A CA  1 
ATOM   1056 C C   . HIS A 1 147 ? 28.583  -51.466  -3.173  1.00 60.57  ? 138 HIS A C   1 
ATOM   1057 O O   . HIS A 1 147 ? 29.253  -50.436  -3.236  1.00 61.26  ? 138 HIS A O   1 
ATOM   1058 C CB  . HIS A 1 147 ? 26.219  -50.833  -3.500  1.00 58.72  ? 138 HIS A CB  1 
ATOM   1059 C CG  . HIS A 1 147 ? 26.141  -51.568  -4.799  1.00 60.54  ? 138 HIS A CG  1 
ATOM   1060 N ND1 . HIS A 1 147 ? 25.841  -52.913  -4.867  1.00 60.15  ? 138 HIS A ND1 1 
ATOM   1061 C CD2 . HIS A 1 147 ? 26.351  -51.162  -6.072  1.00 62.91  ? 138 HIS A CD2 1 
ATOM   1062 C CE1 . HIS A 1 147 ? 25.855  -53.299  -6.132  1.00 64.83  ? 138 HIS A CE1 1 
ATOM   1063 N NE2 . HIS A 1 147 ? 26.161  -52.255  -6.884  1.00 66.40  ? 138 HIS A NE2 1 
ATOM   1064 N N   . ALA A 1 148 ? 28.996  -52.639  -3.642  1.00 61.05  ? 139 ALA A N   1 
ATOM   1065 C CA  . ALA A 1 148 ? 30.297  -52.789  -4.276  1.00 63.53  ? 139 ALA A CA  1 
ATOM   1066 C C   . ALA A 1 148 ? 31.410  -52.344  -3.334  1.00 62.06  ? 139 ALA A C   1 
ATOM   1067 O O   . ALA A 1 148 ? 32.388  -51.733  -3.759  1.00 61.79  ? 139 ALA A O   1 
ATOM   1068 C CB  . ALA A 1 148 ? 30.346  -51.993  -5.571  1.00 62.33  ? 139 ALA A CB  1 
ATOM   1069 N N   . GLY A 1 149 ? 31.244  -52.635  -2.050  1.00 61.61  ? 140 GLY A N   1 
ATOM   1070 C CA  . GLY A 1 149 ? 32.288  -52.380  -1.080  1.00 61.68  ? 140 GLY A CA  1 
ATOM   1071 C C   . GLY A 1 149 ? 32.482  -50.921  -0.721  1.00 61.67  ? 140 GLY A C   1 
ATOM   1072 O O   . GLY A 1 149 ? 33.412  -50.576  0.011   1.00 61.35  ? 140 GLY A O   1 
ATOM   1073 N N   . ALA A 1 150 ? 31.604  -50.058  -1.219  1.00 62.01  ? 141 ALA A N   1 
ATOM   1074 C CA  . ALA A 1 150 ? 31.676  -48.640  -0.872  1.00 61.12  ? 141 ALA A CA  1 
ATOM   1075 C C   . ALA A 1 150 ? 30.347  -48.088  -0.334  1.00 59.33  ? 141 ALA A C   1 
ATOM   1076 O O   . ALA A 1 150 ? 29.291  -48.703  -0.505  1.00 59.96  ? 141 ALA A O   1 
ATOM   1077 C CB  . ALA A 1 150 ? 32.158  -47.826  -2.058  1.00 58.65  ? 141 ALA A CB  1 
ATOM   1078 N N   . LYS A 1 151 ? 30.412  -46.931  0.323   1.00 57.87  ? 142 LYS A N   1 
ATOM   1079 C CA  . LYS A 1 151 ? 29.226  -46.297  0.894   1.00 54.25  ? 142 LYS A CA  1 
ATOM   1080 C C   . LYS A 1 151 ? 28.184  -46.007  -0.154  1.00 52.44  ? 142 LYS A C   1 
ATOM   1081 O O   . LYS A 1 151 ? 28.504  -45.539  -1.239  1.00 54.60  ? 142 LYS A O   1 
ATOM   1082 C CB  . LYS A 1 151 ? 29.589  -44.997  1.595   1.00 49.63  ? 142 LYS A CB  1 
ATOM   1083 C CG  . LYS A 1 151 ? 30.274  -45.199  2.914   1.00 50.73  ? 142 LYS A CG  1 
ATOM   1084 C CD  . LYS A 1 151 ? 30.554  -43.860  3.554   1.00 55.49  ? 142 LYS A CD  1 
ATOM   1085 C CE  . LYS A 1 151 ? 31.743  -43.946  4.494   1.00 61.24  ? 142 LYS A CE  1 
ATOM   1086 N NZ  . LYS A 1 151 ? 32.302  -42.599  4.786   1.00 62.72  ? 142 LYS A NZ  1 
ATOM   1087 N N   . SER A 1 152 ? 26.926  -46.270  0.161   1.00 51.29  ? 143 SER A N   1 
ATOM   1088 C CA  . SER A 1 152 ? 25.895  -46.031  -0.839  1.00 52.92  ? 143 SER A CA  1 
ATOM   1089 C C   . SER A 1 152 ? 24.528  -45.703  -0.249  1.00 51.26  ? 143 SER A C   1 
ATOM   1090 O O   . SER A 1 152 ? 24.379  -45.571  0.972   1.00 51.87  ? 143 SER A O   1 
ATOM   1091 C CB  . SER A 1 152 ? 25.801  -47.214  -1.803  1.00 52.94  ? 143 SER A CB  1 
ATOM   1092 O OG  . SER A 1 152 ? 24.721  -47.046  -2.690  1.00 52.93  ? 143 SER A OG  1 
ATOM   1093 N N   . PHE A 1 153 ? 23.536  -45.564  -1.125  1.00 46.97  ? 144 PHE A N   1 
ATOM   1094 C CA  . PHE A 1 153 ? 22.199  -45.184  -0.695  1.00 47.27  ? 144 PHE A CA  1 
ATOM   1095 C C   . PHE A 1 153 ? 21.137  -45.776  -1.608  1.00 48.58  ? 144 PHE A C   1 
ATOM   1096 O O   . PHE A 1 153 ? 21.458  -46.443  -2.593  1.00 48.73  ? 144 PHE A O   1 
ATOM   1097 C CB  . PHE A 1 153 ? 22.069  -43.666  -0.684  1.00 42.76  ? 144 PHE A CB  1 
ATOM   1098 C CG  . PHE A 1 153 ? 21.039  -43.170  0.253   1.00 44.72  ? 144 PHE A CG  1 
ATOM   1099 C CD1 . PHE A 1 153 ? 21.057  -43.563  1.577   1.00 44.14  ? 144 PHE A CD1 1 
ATOM   1100 C CD2 . PHE A 1 153 ? 20.058  -42.294  -0.174  1.00 47.01  ? 144 PHE A CD2 1 
ATOM   1101 C CE1 . PHE A 1 153 ? 20.105  -43.099  2.456   1.00 42.91  ? 144 PHE A CE1 1 
ATOM   1102 C CE2 . PHE A 1 153 ? 19.098  -41.819  0.706   1.00 45.35  ? 144 PHE A CE2 1 
ATOM   1103 C CZ  . PHE A 1 153 ? 19.121  -42.223  2.019   1.00 42.08  ? 144 PHE A CZ  1 
ATOM   1104 N N   . TYR A 1 154 ? 19.869  -45.527  -1.293  1.00 46.20  ? 145 TYR A N   1 
ATOM   1105 C CA  . TYR A 1 154 ? 18.793  -46.032  -2.134  1.00 45.71  ? 145 TYR A CA  1 
ATOM   1106 C C   . TYR A 1 154 ? 18.913  -45.356  -3.486  1.00 45.49  ? 145 TYR A C   1 
ATOM   1107 O O   . TYR A 1 154 ? 19.424  -44.241  -3.576  1.00 45.14  ? 145 TYR A O   1 
ATOM   1108 C CB  . TYR A 1 154 ? 17.427  -45.750  -1.504  1.00 45.92  ? 145 TYR A CB  1 
ATOM   1109 C CG  . TYR A 1 154 ? 17.338  -46.153  -0.050  1.00 45.11  ? 145 TYR A CG  1 
ATOM   1110 C CD1 . TYR A 1 154 ? 17.046  -47.458  0.316   1.00 45.08  ? 145 TYR A CD1 1 
ATOM   1111 C CD2 . TYR A 1 154 ? 17.564  -45.229  0.956   1.00 43.78  ? 145 TYR A CD2 1 
ATOM   1112 C CE1 . TYR A 1 154 ? 16.974  -47.829  1.649   1.00 43.91  ? 145 TYR A CE1 1 
ATOM   1113 C CE2 . TYR A 1 154 ? 17.495  -45.591  2.285   1.00 43.22  ? 145 TYR A CE2 1 
ATOM   1114 C CZ  . TYR A 1 154 ? 17.200  -46.891  2.629   1.00 42.07  ? 145 TYR A CZ  1 
ATOM   1115 O OH  . TYR A 1 154 ? 17.125  -47.254  3.957   1.00 43.62  ? 145 TYR A OH  1 
ATOM   1116 N N   . LYS A 1 155 ? 18.471  -46.024  -4.544  1.00 45.63  ? 146 LYS A N   1 
ATOM   1117 C CA  . LYS A 1 155 ? 18.637  -45.455  -5.874  1.00 45.00  ? 146 LYS A CA  1 
ATOM   1118 C C   . LYS A 1 155 ? 17.570  -44.408  -6.113  1.00 47.59  ? 146 LYS A C   1 
ATOM   1119 O O   . LYS A 1 155 ? 17.802  -43.421  -6.813  1.00 46.89  ? 146 LYS A O   1 
ATOM   1120 C CB  . LYS A 1 155 ? 18.591  -46.528  -6.964  1.00 46.77  ? 146 LYS A CB  1 
ATOM   1121 C CG  . LYS A 1 155 ? 19.747  -46.458  -7.970  1.00 52.71  ? 146 LYS A CG  1 
ATOM   1122 C CD  . LYS A 1 155 ? 19.501  -45.435  -9.085  1.00 55.17  ? 146 LYS A CD  1 
ATOM   1123 C CE  . LYS A 1 155 ? 20.455  -45.643  -10.273 1.00 59.08  ? 146 LYS A CE  1 
ATOM   1124 N NZ  . LYS A 1 155 ? 21.899  -45.430  -9.920  1.00 55.85  ? 146 LYS A NZ  1 
ATOM   1125 N N   . ASN A 1 156 ? 16.406  -44.622  -5.507  1.00 49.43  ? 147 ASN A N   1 
ATOM   1126 C CA  . ASN A 1 156 ? 15.226  -43.798  -5.779  1.00 48.72  ? 147 ASN A CA  1 
ATOM   1127 C C   . ASN A 1 156 ? 15.110  -42.511  -4.964  1.00 48.53  ? 147 ASN A C   1 
ATOM   1128 O O   . ASN A 1 156 ? 14.246  -41.682  -5.237  1.00 48.80  ? 147 ASN A O   1 
ATOM   1129 C CB  . ASN A 1 156 ? 13.962  -44.639  -5.619  1.00 46.65  ? 147 ASN A CB  1 
ATOM   1130 C CG  . ASN A 1 156 ? 13.982  -45.851  -6.500  1.00 46.99  ? 147 ASN A CG  1 
ATOM   1131 O OD1 . ASN A 1 156 ? 14.513  -45.800  -7.604  1.00 51.90  ? 147 ASN A OD1 1 
ATOM   1132 N ND2 . ASN A 1 156 ? 13.433  -46.955  -6.019  1.00 47.96  ? 147 ASN A ND2 1 
ATOM   1133 N N   . LEU A 1 157 ? 15.980  -42.341  -3.972  1.00 48.14  ? 148 LEU A N   1 
ATOM   1134 C CA  . LEU A 1 157 ? 16.004  -41.109  -3.184  1.00 47.64  ? 148 LEU A CA  1 
ATOM   1135 C C   . LEU A 1 157 ? 17.399  -40.464  -3.154  1.00 47.56  ? 148 LEU A C   1 
ATOM   1136 O O   . LEU A 1 157 ? 18.419  -41.133  -3.345  1.00 45.76  ? 148 LEU A O   1 
ATOM   1137 C CB  . LEU A 1 157 ? 15.565  -41.389  -1.751  1.00 48.45  ? 148 LEU A CB  1 
ATOM   1138 C CG  . LEU A 1 157 ? 14.309  -42.208  -1.456  1.00 47.29  ? 148 LEU A CG  1 
ATOM   1139 C CD1 . LEU A 1 157 ? 14.269  -42.540  0.040   1.00 42.28  ? 148 LEU A CD1 1 
ATOM   1140 C CD2 . LEU A 1 157 ? 13.062  -41.445  -1.867  1.00 46.45  ? 148 LEU A CD2 1 
ATOM   1141 N N   . ILE A 1 158 ? 17.433  -39.162  -2.897  1.00 46.82  ? 149 ILE A N   1 
ATOM   1142 C CA  . ILE A 1 158 ? 18.696  -38.457  -2.726  1.00 46.57  ? 149 ILE A CA  1 
ATOM   1143 C C   . ILE A 1 158 ? 18.761  -37.828  -1.339  1.00 44.61  ? 149 ILE A C   1 
ATOM   1144 O O   . ILE A 1 158 ? 17.842  -37.118  -0.913  1.00 44.66  ? 149 ILE A O   1 
ATOM   1145 C CB  . ILE A 1 158 ? 18.894  -37.349  -3.779  1.00 43.60  ? 149 ILE A CB  1 
ATOM   1146 C CG1 . ILE A 1 158 ? 18.838  -37.925  -5.181  1.00 43.68  ? 149 ILE A CG1 1 
ATOM   1147 C CG2 . ILE A 1 158 ? 20.231  -36.660  -3.591  1.00 47.94  ? 149 ILE A CG2 1 
ATOM   1148 C CD1 . ILE A 1 158 ? 18.982  -36.883  -6.254  1.00 48.85  ? 149 ILE A CD1 1 
ATOM   1149 N N   . TRP A 1 159 ? 19.863  -38.063  -0.645  1.00 44.53  ? 150 TRP A N   1 
ATOM   1150 C CA  . TRP A 1 159 ? 20.025  -37.477  0.661   1.00 44.42  ? 150 TRP A CA  1 
ATOM   1151 C C   . TRP A 1 159 ? 20.703  -36.147  0.451   1.00 44.51  ? 150 TRP A C   1 
ATOM   1152 O O   . TRP A 1 159 ? 21.892  -36.080  0.139   1.00 49.16  ? 150 TRP A O   1 
ATOM   1153 C CB  . TRP A 1 159 ? 20.900  -38.380  1.512   1.00 46.91  ? 150 TRP A CB  1 
ATOM   1154 C CG  . TRP A 1 159 ? 20.934  -37.987  2.937   1.00 47.43  ? 150 TRP A CG  1 
ATOM   1155 C CD1 . TRP A 1 159 ? 20.392  -36.867  3.491   1.00 48.46  ? 150 TRP A CD1 1 
ATOM   1156 C CD2 . TRP A 1 159 ? 21.546  -38.709  4.000   1.00 45.00  ? 150 TRP A CD2 1 
ATOM   1157 N NE1 . TRP A 1 159 ? 20.635  -36.845  4.841   1.00 45.30  ? 150 TRP A NE1 1 
ATOM   1158 C CE2 . TRP A 1 159 ? 21.343  -37.971  5.175   1.00 45.65  ? 150 TRP A CE2 1 
ATOM   1159 C CE3 . TRP A 1 159 ? 22.245  -39.912  4.076   1.00 46.07  ? 150 TRP A CE3 1 
ATOM   1160 C CZ2 . TRP A 1 159 ? 21.812  -38.402  6.404   1.00 46.67  ? 150 TRP A CZ2 1 
ATOM   1161 C CZ3 . TRP A 1 159 ? 22.715  -40.326  5.291   1.00 42.13  ? 150 TRP A CZ3 1 
ATOM   1162 C CH2 . TRP A 1 159 ? 22.501  -39.581  6.432   1.00 43.16  ? 150 TRP A CH2 1 
ATOM   1163 N N   . LEU A 1 160 ? 19.943  -35.083  0.662   1.00 45.62  ? 151 LEU A N   1 
ATOM   1164 C CA  . LEU A 1 160 ? 20.390  -33.741  0.324   1.00 46.93  ? 151 LEU A CA  1 
ATOM   1165 C C   . LEU A 1 160 ? 21.062  -33.097  1.519   1.00 46.34  ? 151 LEU A C   1 
ATOM   1166 O O   . LEU A 1 160 ? 20.681  -33.322  2.663   1.00 43.91  ? 151 LEU A O   1 
ATOM   1167 C CB  . LEU A 1 160 ? 19.225  -32.877  -0.161  1.00 46.06  ? 151 LEU A CB  1 
ATOM   1168 C CG  . LEU A 1 160 ? 19.133  -32.612  -1.664  1.00 47.89  ? 151 LEU A CG  1 
ATOM   1169 C CD1 . LEU A 1 160 ? 17.912  -31.767  -1.957  1.00 46.37  ? 151 LEU A CD1 1 
ATOM   1170 C CD2 . LEU A 1 160 ? 20.385  -31.916  -2.172  1.00 49.71  ? 151 LEU A CD2 1 
ATOM   1171 N N   . VAL A 1 161 ? 22.079  -32.298  1.241   1.00 50.32  ? 152 VAL A N   1 
ATOM   1172 C CA  . VAL A 1 161 ? 22.978  -31.850  2.279   1.00 48.37  ? 152 VAL A CA  1 
ATOM   1173 C C   . VAL A 1 161 ? 23.401  -30.429  1.981   1.00 50.96  ? 152 VAL A C   1 
ATOM   1174 O O   . VAL A 1 161 ? 23.415  -30.018  0.818   1.00 54.50  ? 152 VAL A O   1 
ATOM   1175 C CB  . VAL A 1 161 ? 24.195  -32.758  2.298   1.00 45.39  ? 152 VAL A CB  1 
ATOM   1176 C CG1 . VAL A 1 161 ? 25.390  -32.035  2.844   1.00 50.43  ? 152 VAL A CG1 1 
ATOM   1177 C CG2 . VAL A 1 161 ? 23.876  -34.036  3.071   1.00 42.27  ? 152 VAL A CG2 1 
ATOM   1178 N N   . LYS A 1 162 ? 23.743  -29.674  3.018   1.00 49.61  ? 153 LYS A N   1 
ATOM   1179 C CA  . LYS A 1 162 ? 24.134  -28.293  2.816   1.00 51.31  ? 153 LYS A CA  1 
ATOM   1180 C C   . LYS A 1 162 ? 25.270  -28.182  1.798   1.00 56.03  ? 153 LYS A C   1 
ATOM   1181 O O   . LYS A 1 162 ? 26.318  -28.822  1.932   1.00 56.92  ? 153 LYS A O   1 
ATOM   1182 C CB  . LYS A 1 162 ? 24.556  -27.651  4.142   1.00 52.74  ? 153 LYS A CB  1 
ATOM   1183 C CG  . LYS A 1 162 ? 25.875  -28.163  4.729   1.00 50.78  ? 153 LYS A CG  1 
ATOM   1184 C CD  . LYS A 1 162 ? 26.236  -27.422  6.025   1.00 51.75  ? 153 LYS A CD  1 
ATOM   1185 C CE  . LYS A 1 162 ? 27.642  -27.788  6.523   1.00 51.01  ? 153 LYS A CE  1 
ATOM   1186 N NZ  . LYS A 1 162 ? 28.000  -27.151  7.830   1.00 44.46  ? 153 LYS A NZ  1 
ATOM   1187 N N   . LYS A 1 163 ? 25.030  -27.378  0.769   1.00 57.96  ? 154 LYS A N   1 
ATOM   1188 C CA  . LYS A 1 163 ? 26.070  -26.854  -0.110  1.00 57.66  ? 154 LYS A CA  1 
ATOM   1189 C C   . LYS A 1 163 ? 26.364  -25.538  0.563   1.00 61.17  ? 154 LYS A C   1 
ATOM   1190 O O   . LYS A 1 163 ? 25.449  -24.959  1.135   1.00 64.81  ? 154 LYS A O   1 
ATOM   1191 C CB  . LYS A 1 163 ? 25.507  -26.598  -1.493  1.00 57.00  ? 154 LYS A CB  1 
ATOM   1192 C CG  . LYS A 1 163 ? 26.426  -25.817  -2.393  1.00 59.62  ? 154 LYS A CG  1 
ATOM   1193 C CD  . LYS A 1 163 ? 25.845  -25.694  -3.802  1.00 61.85  ? 154 LYS A CD  1 
ATOM   1194 C CE  . LYS A 1 163 ? 25.862  -27.018  -4.562  1.00 58.72  ? 154 LYS A CE  1 
ATOM   1195 N NZ  . LYS A 1 163 ? 25.461  -26.850  -5.990  1.00 56.65  ? 154 LYS A NZ  1 
ATOM   1196 N N   . GLY A 1 164 ? 27.571  -24.996  0.511   1.00 59.84  ? 155 GLY A N   1 
ATOM   1197 C CA  . GLY A 1 164 ? 27.844  -24.028  1.552   1.00 61.81  ? 155 GLY A CA  1 
ATOM   1198 C C   . GLY A 1 164 ? 28.366  -24.596  2.865   1.00 61.14  ? 155 GLY A C   1 
ATOM   1199 O O   . GLY A 1 164 ? 29.518  -25.024  2.917   1.00 65.10  ? 155 GLY A O   1 
ATOM   1200 N N   . ASN A 1 165 ? 27.553  -24.686  3.910   1.00 60.14  ? 156 ASN A N   1 
ATOM   1201 C CA  . ASN A 1 165 ? 27.724  -23.965  5.154   1.00 59.48  ? 156 ASN A CA  1 
ATOM   1202 C C   . ASN A 1 165 ? 26.518  -23.037  5.145   1.00 61.68  ? 156 ASN A C   1 
ATOM   1203 O O   . ASN A 1 165 ? 26.159  -22.426  6.160   1.00 61.63  ? 156 ASN A O   1 
ATOM   1204 C CB  . ASN A 1 165 ? 29.043  -23.181  5.108   1.00 59.68  ? 156 ASN A CB  1 
ATOM   1205 C CG  . ASN A 1 165 ? 28.908  -21.736  5.597   1.00 60.94  ? 156 ASN A CG  1 
ATOM   1206 O OD1 . ASN A 1 165 ? 28.555  -20.826  4.835   1.00 60.23  ? 156 ASN A OD1 1 
ATOM   1207 N ND2 . ASN A 1 165 ? 29.221  -21.520  6.868   1.00 59.48  ? 156 ASN A ND2 1 
ATOM   1208 N N   . SER A 1 166 ? 25.811  -23.061  4.020   1.00 58.18  ? 157 SER A N   1 
ATOM   1209 C CA  . SER A 1 166 ? 24.415  -22.642  3.992   1.00 61.10  ? 157 SER A CA  1 
ATOM   1210 C C   . SER A 1 166 ? 23.510  -23.746  3.424   1.00 58.86  ? 157 SER A C   1 
ATOM   1211 O O   . SER A 1 166 ? 23.822  -24.357  2.412   1.00 57.51  ? 157 SER A O   1 
ATOM   1212 C CB  . SER A 1 166 ? 24.236  -21.374  3.159   1.00 64.64  ? 157 SER A CB  1 
ATOM   1213 O OG  . SER A 1 166 ? 22.849  -21.084  3.002   1.00 66.00  ? 157 SER A OG  1 
ATOM   1214 N N   . TYR A 1 167 ? 22.381  -23.994  4.068   1.00 57.02  ? 158 TYR A N   1 
ATOM   1215 C CA  . TYR A 1 167 ? 21.395  -24.909  3.508   1.00 54.39  ? 158 TYR A CA  1 
ATOM   1216 C C   . TYR A 1 167 ? 20.133  -24.097  3.338   1.00 54.38  ? 158 TYR A C   1 
ATOM   1217 O O   . TYR A 1 167 ? 19.318  -24.004  4.253   1.00 53.95  ? 158 TYR A O   1 
ATOM   1218 C CB  . TYR A 1 167 ? 21.148  -26.110  4.426   1.00 52.66  ? 158 TYR A CB  1 
ATOM   1219 C CG  . TYR A 1 167 ? 20.135  -27.119  3.918   1.00 49.99  ? 158 TYR A CG  1 
ATOM   1220 C CD1 . TYR A 1 167 ? 18.782  -26.795  3.806   1.00 50.46  ? 158 TYR A CD1 1 
ATOM   1221 C CD2 . TYR A 1 167 ? 20.526  -28.409  3.574   1.00 48.86  ? 158 TYR A CD2 1 
ATOM   1222 C CE1 . TYR A 1 167 ? 17.851  -27.729  3.353   1.00 46.47  ? 158 TYR A CE1 1 
ATOM   1223 C CE2 . TYR A 1 167 ? 19.611  -29.348  3.125   1.00 43.68  ? 158 TYR A CE2 1 
ATOM   1224 C CZ  . TYR A 1 167 ? 18.278  -29.008  3.016   1.00 47.17  ? 158 TYR A CZ  1 
ATOM   1225 O OH  . TYR A 1 167 ? 17.382  -29.961  2.568   1.00 46.69  ? 158 TYR A OH  1 
ATOM   1226 N N   . PRO A 1 168 ? 19.980  -23.487  2.157   1.00 57.27  ? 159 PRO A N   1 
ATOM   1227 C CA  . PRO A 1 168 ? 18.885  -22.563  1.857   1.00 56.29  ? 159 PRO A CA  1 
ATOM   1228 C C   . PRO A 1 168 ? 17.558  -23.279  1.955   1.00 52.88  ? 159 PRO A C   1 
ATOM   1229 O O   . PRO A 1 168 ? 17.528  -24.502  2.069   1.00 53.44  ? 159 PRO A O   1 
ATOM   1230 C CB  . PRO A 1 168 ? 19.130  -22.202  0.384   1.00 53.30  ? 159 PRO A CB  1 
ATOM   1231 C CG  . PRO A 1 168 ? 20.574  -22.452  0.152   1.00 57.32  ? 159 PRO A CG  1 
ATOM   1232 C CD  . PRO A 1 168 ? 20.913  -23.629  1.027   1.00 61.33  ? 159 PRO A CD  1 
ATOM   1233 N N   . LYS A 1 169 ? 16.473  -22.522  1.846   1.00 53.30  ? 160 LYS A N   1 
ATOM   1234 C CA  . LYS A 1 169 ? 15.140  -23.098  1.897   1.00 52.84  ? 160 LYS A CA  1 
ATOM   1235 C C   . LYS A 1 169 ? 14.915  -23.827  0.601   1.00 50.73  ? 160 LYS A C   1 
ATOM   1236 O O   . LYS A 1 169 ? 15.464  -23.461  -0.426  1.00 54.90  ? 160 LYS A O   1 
ATOM   1237 C CB  . LYS A 1 169 ? 14.075  -22.021  2.089   1.00 52.90  ? 160 LYS A CB  1 
ATOM   1238 C CG  . LYS A 1 169 ? 12.633  -22.542  2.009   1.00 55.26  ? 160 LYS A CG  1 
ATOM   1239 C CD  . LYS A 1 169 ? 11.630  -21.423  2.300   1.00 61.86  ? 160 LYS A CD  1 
ATOM   1240 C CE  . LYS A 1 169 ? 10.200  -21.790  1.891   1.00 60.87  ? 160 LYS A CE  1 
ATOM   1241 N NZ  . LYS A 1 169 ? 9.223   -20.708  2.254   1.00 61.62  ? 160 LYS A NZ  1 
ATOM   1242 N N   . LEU A 1 170 ? 14.112  -24.872  0.643   1.00 51.81  ? 161 LEU A N   1 
ATOM   1243 C CA  . LEU A 1 170 ? 13.987  -25.727  -0.517  1.00 49.64  ? 161 LEU A CA  1 
ATOM   1244 C C   . LEU A 1 170 ? 12.539  -25.983  -0.893  1.00 49.66  ? 161 LEU A C   1 
ATOM   1245 O O   . LEU A 1 170 ? 11.761  -26.533  -0.113  1.00 52.06  ? 161 LEU A O   1 
ATOM   1246 C CB  . LEU A 1 170 ? 14.719  -27.043  -0.273  1.00 46.69  ? 161 LEU A CB  1 
ATOM   1247 C CG  . LEU A 1 170 ? 14.469  -28.143  -1.293  1.00 48.65  ? 161 LEU A CG  1 
ATOM   1248 C CD1 . LEU A 1 170 ? 15.695  -29.066  -1.356  1.00 52.70  ? 161 LEU A CD1 1 
ATOM   1249 C CD2 . LEU A 1 170 ? 13.176  -28.941  -1.002  1.00 43.91  ? 161 LEU A CD2 1 
ATOM   1250 N N   . SER A 1 171 ? 12.182  -25.583  -2.102  1.00 50.80  ? 162 SER A N   1 
ATOM   1251 C CA  . SER A 1 171 ? 10.866  -25.884  -2.621  1.00 50.16  ? 162 SER A CA  1 
ATOM   1252 C C   . SER A 1 171 ? 10.967  -26.351  -4.064  1.00 51.78  ? 162 SER A C   1 
ATOM   1253 O O   . SER A 1 171 ? 11.530  -25.663  -4.913  1.00 51.80  ? 162 SER A O   1 
ATOM   1254 C CB  . SER A 1 171 ? 9.962   -24.662  -2.526  1.00 51.92  ? 162 SER A CB  1 
ATOM   1255 O OG  . SER A 1 171 ? 8.660   -25.005  -2.961  1.00 58.79  ? 162 SER A OG  1 
ATOM   1256 N N   . LYS A 1 172 ? 10.450  -27.542  -4.326  1.00 49.96  ? 163 LYS A N   1 
ATOM   1257 C CA  . LYS A 1 172 ? 10.333  -28.028  -5.682  1.00 49.80  ? 163 LYS A CA  1 
ATOM   1258 C C   . LYS A 1 172 ? 8.935   -28.603  -5.806  1.00 50.45  ? 163 LYS A C   1 
ATOM   1259 O O   . LYS A 1 172 ? 8.393   -29.121  -4.834  1.00 49.32  ? 163 LYS A O   1 
ATOM   1260 C CB  . LYS A 1 172 ? 11.406  -29.075  -5.999  1.00 52.00  ? 163 LYS A CB  1 
ATOM   1261 C CG  . LYS A 1 172 ? 11.808  -29.133  -7.493  1.00 54.24  ? 163 LYS A CG  1 
ATOM   1262 C CD  . LYS A 1 172 ? 12.667  -27.917  -7.887  1.00 56.79  ? 163 LYS A CD  1 
ATOM   1263 C CE  . LYS A 1 172 ? 12.946  -27.848  -9.401  1.00 62.05  ? 163 LYS A CE  1 
ATOM   1264 N NZ  . LYS A 1 172 ? 13.920  -26.754  -9.750  1.00 62.24  ? 163 LYS A NZ  1 
ATOM   1265 N N   . SER A 1 173 ? 8.339   -28.478  -6.988  1.00 52.09  ? 164 SER A N   1 
ATOM   1266 C CA  . SER A 1 173 ? 6.981   -28.946  -7.200  1.00 50.47  ? 164 SER A CA  1 
ATOM   1267 C C   . SER A 1 173 ? 6.938   -29.807  -8.438  1.00 51.03  ? 164 SER A C   1 
ATOM   1268 O O   . SER A 1 173 ? 7.729   -29.618  -9.360  1.00 52.43  ? 164 SER A O   1 
ATOM   1269 C CB  . SER A 1 173 ? 6.036   -27.761  -7.339  1.00 50.28  ? 164 SER A CB  1 
ATOM   1270 O OG  . SER A 1 173 ? 6.164   -26.904  -6.214  1.00 55.85  ? 164 SER A OG  1 
ATOM   1271 N N   . TYR A 1 174 ? 6.030   -30.770  -8.443  1.00 47.67  ? 165 TYR A N   1 
ATOM   1272 C CA  . TYR A 1 174 ? 5.802   -31.574  -9.616  1.00 48.92  ? 165 TYR A CA  1 
ATOM   1273 C C   . TYR A 1 174 ? 4.309   -31.623  -9.859  1.00 52.03  ? 165 TYR A C   1 
ATOM   1274 O O   . TYR A 1 174 ? 3.536   -31.818  -8.921  1.00 53.08  ? 165 TYR A O   1 
ATOM   1275 C CB  . TYR A 1 174 ? 6.359   -32.982  -9.412  1.00 49.05  ? 165 TYR A CB  1 
ATOM   1276 C CG  . TYR A 1 174 ? 5.792   -34.026  -10.357 1.00 50.50  ? 165 TYR A CG  1 
ATOM   1277 C CD1 . TYR A 1 174 ? 4.608   -34.679  -10.063 1.00 48.14  ? 165 TYR A CD1 1 
ATOM   1278 C CD2 . TYR A 1 174 ? 6.445   -34.360  -11.542 1.00 53.02  ? 165 TYR A CD2 1 
ATOM   1279 C CE1 . TYR A 1 174 ? 4.086   -35.632  -10.908 1.00 52.48  ? 165 TYR A CE1 1 
ATOM   1280 C CE2 . TYR A 1 174 ? 5.926   -35.319  -12.400 1.00 52.41  ? 165 TYR A CE2 1 
ATOM   1281 C CZ  . TYR A 1 174 ? 4.743   -35.947  -12.075 1.00 52.49  ? 165 TYR A CZ  1 
ATOM   1282 O OH  . TYR A 1 174 ? 4.208   -36.893  -12.908 1.00 53.97  ? 165 TYR A OH  1 
ATOM   1283 N N   . ILE A 1 175 ? 3.906   -31.405  -11.109 1.00 49.32  ? 166 ILE A N   1 
ATOM   1284 C CA  . ILE A 1 175 ? 2.527   -31.638  -11.513 1.00 51.11  ? 166 ILE A CA  1 
ATOM   1285 C C   . ILE A 1 175 ? 2.487   -33.007  -12.161 1.00 52.28  ? 166 ILE A C   1 
ATOM   1286 O O   . ILE A 1 175 ? 3.411   -33.375  -12.884 1.00 54.29  ? 166 ILE A O   1 
ATOM   1287 C CB  . ILE A 1 175 ? 2.011   -30.594  -12.550 1.00 51.00  ? 166 ILE A CB  1 
ATOM   1288 C CG1 . ILE A 1 175 ? 2.081   -29.156  -12.013 1.00 54.12  ? 166 ILE A CG1 1 
ATOM   1289 C CG2 . ILE A 1 175 ? 0.570   -30.915  -12.971 1.00 48.72  ? 166 ILE A CG2 1 
ATOM   1290 C CD1 . ILE A 1 175 ? 3.479   -28.557  -11.921 1.00 55.58  ? 166 ILE A CD1 1 
ATOM   1291 N N   . ASN A 1 176 ? 1.409   -33.750  -11.958 1.00 49.98  ? 167 ASN A N   1 
ATOM   1292 C CA  . ASN A 1 176 ? 1.364   -35.065  -12.546 1.00 52.47  ? 167 ASN A CA  1 
ATOM   1293 C C   . ASN A 1 176 ? 0.772   -34.913  -13.937 1.00 57.34  ? 167 ASN A C   1 
ATOM   1294 O O   . ASN A 1 176 ? -0.425  -34.709  -14.098 1.00 61.99  ? 167 ASN A O   1 
ATOM   1295 C CB  . ASN A 1 176 ? 0.511   -36.004  -11.678 1.00 51.50  ? 167 ASN A CB  1 
ATOM   1296 C CG  . ASN A 1 176 ? 0.304   -37.373  -12.319 1.00 54.42  ? 167 ASN A CG  1 
ATOM   1297 O OD1 . ASN A 1 176 ? 0.861   -37.658  -13.381 1.00 57.78  ? 167 ASN A OD1 1 
ATOM   1298 N ND2 . ASN A 1 176 ? -0.490  -38.227  -11.674 1.00 52.62  ? 167 ASN A ND2 1 
ATOM   1299 N N   . ASP A 1 177 ? 1.628   -35.024  -14.949 1.00 59.32  ? 168 ASP A N   1 
ATOM   1300 C CA  . ASP A 1 177 ? 1.199   -34.951  -16.348 1.00 57.61  ? 168 ASP A CA  1 
ATOM   1301 C C   . ASP A 1 177 ? 1.062   -36.342  -16.928 1.00 58.28  ? 168 ASP A C   1 
ATOM   1302 O O   . ASP A 1 177 ? 0.694   -36.505  -18.087 1.00 59.84  ? 168 ASP A O   1 
ATOM   1303 C CB  . ASP A 1 177 ? 2.179   -34.125  -17.176 1.00 55.87  ? 168 ASP A CB  1 
ATOM   1304 C CG  . ASP A 1 177 ? 3.615   -34.412  -16.817 1.00 61.27  ? 168 ASP A CG  1 
ATOM   1305 O OD1 . ASP A 1 177 ? 4.016   -35.601  -16.857 1.00 61.56  ? 168 ASP A OD1 1 
ATOM   1306 O OD2 . ASP A 1 177 ? 4.335   -33.447  -16.478 1.00 60.32  ? 168 ASP A OD2 1 
ATOM   1307 N N   . LYS A 1 178 ? 1.366   -37.350  -16.121 1.00 56.62  ? 169 LYS A N   1 
ATOM   1308 C CA  . LYS A 1 178 ? 1.244   -38.711  -16.588 1.00 55.31  ? 169 LYS A CA  1 
ATOM   1309 C C   . LYS A 1 178 ? -0.230  -39.033  -16.666 1.00 56.02  ? 169 LYS A C   1 
ATOM   1310 O O   . LYS A 1 178 ? -1.083  -38.233  -16.251 1.00 54.99  ? 169 LYS A O   1 
ATOM   1311 C CB  . LYS A 1 178 ? 1.947   -39.673  -15.630 1.00 58.90  ? 169 LYS A CB  1 
ATOM   1312 C CG  . LYS A 1 178 ? 3.408   -39.947  -15.967 1.00 57.79  ? 169 LYS A CG  1 
ATOM   1313 C CD  . LYS A 1 178 ? 4.238   -38.667  -16.020 1.00 54.41  ? 169 LYS A CD  1 
ATOM   1314 C CE  . LYS A 1 178 ? 5.568   -38.923  -16.731 1.00 57.64  ? 169 LYS A CE  1 
ATOM   1315 N NZ  . LYS A 1 178 ? 6.424   -37.708  -16.808 1.00 58.07  ? 169 LYS A NZ  1 
ATOM   1316 N N   . GLY A 1 179 ? -0.534  -40.220  -17.163 1.00 56.45  ? 170 GLY A N   1 
ATOM   1317 C CA  . GLY A 1 179 ? -1.915  -40.587  -17.369 1.00 58.16  ? 170 GLY A CA  1 
ATOM   1318 C C   . GLY A 1 179 ? -2.533  -41.188  -16.132 1.00 57.52  ? 170 GLY A C   1 
ATOM   1319 O O   . GLY A 1 179 ? -3.750  -41.336  -16.058 1.00 58.26  ? 170 GLY A O   1 
ATOM   1320 N N   . LYS A 1 180 ? -1.701  -41.516  -15.149 1.00 59.05  ? 171 LYS A N   1 
ATOM   1321 C CA  . LYS A 1 180 ? -2.140  -42.359  -14.042 1.00 59.34  ? 171 LYS A CA  1 
ATOM   1322 C C   . LYS A 1 180 ? -1.804  -41.821  -12.653 1.00 56.35  ? 171 LYS A C   1 
ATOM   1323 O O   . LYS A 1 180 ? -1.305  -40.699  -12.498 1.00 53.69  ? 171 LYS A O   1 
ATOM   1324 C CB  . LYS A 1 180 ? -1.509  -43.748  -14.180 1.00 61.20  ? 171 LYS A CB  1 
ATOM   1325 C CG  . LYS A 1 180 ? -1.354  -44.244  -15.620 1.00 60.89  ? 171 LYS A CG  1 
ATOM   1326 C CD  . LYS A 1 180 ? 0.104   -44.158  -16.093 1.00 61.65  ? 171 LYS A CD  1 
ATOM   1327 C CE  . LYS A 1 180 ? 0.358   -45.064  -17.306 1.00 63.76  ? 171 LYS A CE  1 
ATOM   1328 N NZ  . LYS A 1 180 ? 1.777   -45.514  -17.371 1.00 56.95  ? 171 LYS A NZ  1 
ATOM   1329 N N   . GLU A 1 181 ? -2.095  -42.643  -11.645 1.00 57.53  ? 172 GLU A N   1 
ATOM   1330 C CA  . GLU A 1 181 ? -1.610  -42.400  -10.292 1.00 57.66  ? 172 GLU A CA  1 
ATOM   1331 C C   . GLU A 1 181 ? -0.099  -42.333  -10.333 1.00 54.80  ? 172 GLU A C   1 
ATOM   1332 O O   . GLU A 1 181 ? 0.551   -43.048  -11.089 1.00 56.99  ? 172 GLU A O   1 
ATOM   1333 C CB  . GLU A 1 181 ? -2.025  -43.527  -9.348  1.00 56.74  ? 172 GLU A CB  1 
ATOM   1334 C CG  . GLU A 1 181 ? -3.505  -43.719  -9.210  1.00 58.46  ? 172 GLU A CG  1 
ATOM   1335 C CD  . GLU A 1 181 ? -4.139  -42.656  -8.342  1.00 64.27  ? 172 GLU A CD  1 
ATOM   1336 O OE1 . GLU A 1 181 ? -3.873  -41.452  -8.592  1.00 65.07  ? 172 GLU A OE1 1 
ATOM   1337 O OE2 . GLU A 1 181 ? -4.897  -43.024  -7.408  1.00 64.73  ? 172 GLU A OE2 1 
ATOM   1338 N N   . VAL A 1 182 ? 0.471   -41.443  -9.550  1.00 52.70  ? 173 VAL A N   1 
ATOM   1339 C CA  . VAL A 1 182 ? 1.914   -41.439  -9.438  1.00 54.28  ? 173 VAL A CA  1 
ATOM   1340 C C   . VAL A 1 182 ? 2.353   -41.606  -7.987  1.00 52.33  ? 173 VAL A C   1 
ATOM   1341 O O   . VAL A 1 182 ? 2.177   -40.719  -7.148  1.00 50.30  ? 173 VAL A O   1 
ATOM   1342 C CB  . VAL A 1 182 ? 2.545   -40.179  -10.054 1.00 53.82  ? 173 VAL A CB  1 
ATOM   1343 C CG1 . VAL A 1 182 ? 3.978   -40.021  -9.566  1.00 51.94  ? 173 VAL A CG1 1 
ATOM   1344 C CG2 . VAL A 1 182 ? 2.496   -40.264  -11.559 1.00 52.75  ? 173 VAL A CG2 1 
ATOM   1345 N N   . LEU A 1 183 ? 2.942   -42.760  -7.712  1.00 52.79  ? 174 LEU A N   1 
ATOM   1346 C CA  . LEU A 1 183 ? 3.458   -43.069  -6.399  1.00 49.37  ? 174 LEU A CA  1 
ATOM   1347 C C   . LEU A 1 183 ? 4.748   -42.308  -6.150  1.00 45.94  ? 174 LEU A C   1 
ATOM   1348 O O   . LEU A 1 183 ? 5.715   -42.474  -6.877  1.00 47.72  ? 174 LEU A O   1 
ATOM   1349 C CB  . LEU A 1 183 ? 3.742   -44.564  -6.305  1.00 50.27  ? 174 LEU A CB  1 
ATOM   1350 C CG  . LEU A 1 183 ? 4.649   -44.897  -5.115  1.00 48.38  ? 174 LEU A CG  1 
ATOM   1351 C CD1 . LEU A 1 183 ? 3.988   -44.403  -3.838  1.00 47.38  ? 174 LEU A CD1 1 
ATOM   1352 C CD2 . LEU A 1 183 ? 4.950   -46.385  -5.048  1.00 48.97  ? 174 LEU A CD2 1 
ATOM   1353 N N   . VAL A 1 184 ? 4.764   -41.501  -5.099  1.00 44.29  ? 175 VAL A N   1 
ATOM   1354 C CA  . VAL A 1 184 ? 5.921   -40.684  -4.773  1.00 45.39  ? 175 VAL A CA  1 
ATOM   1355 C C   . VAL A 1 184 ? 6.377   -40.980  -3.343  1.00 44.09  ? 175 VAL A C   1 
ATOM   1356 O O   . VAL A 1 184 ? 5.557   -40.992  -2.420  1.00 44.66  ? 175 VAL A O   1 
ATOM   1357 C CB  . VAL A 1 184 ? 5.575   -39.188  -4.891  1.00 46.91  ? 175 VAL A CB  1 
ATOM   1358 C CG1 . VAL A 1 184 ? 6.728   -38.327  -4.390  1.00 44.38  ? 175 VAL A CG1 1 
ATOM   1359 C CG2 . VAL A 1 184 ? 5.216   -38.850  -6.320  1.00 45.38  ? 175 VAL A CG2 1 
ATOM   1360 N N   . LEU A 1 185 ? 7.677   -41.218  -3.165  1.00 41.97  ? 176 LEU A N   1 
ATOM   1361 C CA  . LEU A 1 185 ? 8.233   -41.587  -1.859  1.00 40.45  ? 176 LEU A CA  1 
ATOM   1362 C C   . LEU A 1 185 ? 9.343   -40.643  -1.438  1.00 40.31  ? 176 LEU A C   1 
ATOM   1363 O O   . LEU A 1 185 ? 10.206  -40.289  -2.236  1.00 40.18  ? 176 LEU A O   1 
ATOM   1364 C CB  . LEU A 1 185 ? 8.806   -43.007  -1.884  1.00 37.98  ? 176 LEU A CB  1 
ATOM   1365 C CG  . LEU A 1 185 ? 7.935   -44.127  -2.440  1.00 41.26  ? 176 LEU A CG  1 
ATOM   1366 C CD1 . LEU A 1 185 ? 8.229   -44.335  -3.924  1.00 42.35  ? 176 LEU A CD1 1 
ATOM   1367 C CD2 . LEU A 1 185 ? 8.154   -45.418  -1.651  1.00 39.84  ? 176 LEU A CD2 1 
ATOM   1368 N N   . TRP A 1 186 ? 9.337   -40.244  -0.175  1.00 40.75  ? 177 TRP A N   1 
ATOM   1369 C CA  . TRP A 1 186 ? 10.413  -39.414  0.328   1.00 40.09  ? 177 TRP A CA  1 
ATOM   1370 C C   . TRP A 1 186 ? 10.647  -39.886  1.729   1.00 40.86  ? 177 TRP A C   1 
ATOM   1371 O O   . TRP A 1 186 ? 9.899   -40.723  2.217   1.00 41.29  ? 177 TRP A O   1 
ATOM   1372 C CB  . TRP A 1 186 ? 9.991   -37.950  0.340   1.00 39.27  ? 177 TRP A CB  1 
ATOM   1373 C CG  . TRP A 1 186 ? 8.899   -37.687  1.335   1.00 41.27  ? 177 TRP A CG  1 
ATOM   1374 C CD1 . TRP A 1 186 ? 9.049   -37.179  2.584   1.00 41.50  ? 177 TRP A CD1 1 
ATOM   1375 C CD2 . TRP A 1 186 ? 7.493   -37.959  1.177   1.00 41.55  ? 177 TRP A CD2 1 
ATOM   1376 N NE1 . TRP A 1 186 ? 7.834   -37.099  3.207   1.00 44.97  ? 177 TRP A NE1 1 
ATOM   1377 C CE2 . TRP A 1 186 ? 6.861   -37.570  2.363   1.00 42.87  ? 177 TRP A CE2 1 
ATOM   1378 C CE3 . TRP A 1 186 ? 6.713   -38.478  0.142   1.00 41.17  ? 177 TRP A CE3 1 
ATOM   1379 C CZ2 . TRP A 1 186 ? 5.482   -37.685  2.547   1.00 45.08  ? 177 TRP A CZ2 1 
ATOM   1380 C CZ3 . TRP A 1 186 ? 5.350   -38.596  0.326   1.00 41.49  ? 177 TRP A CZ3 1 
ATOM   1381 C CH2 . TRP A 1 186 ? 4.750   -38.204  1.514   1.00 46.13  ? 177 TRP A CH2 1 
ATOM   1382 N N   . GLY A 1 187 ? 11.646  -39.310  2.391   1.00 43.83  ? 178 GLY A N   1 
ATOM   1383 C CA  . GLY A 1 187 ? 11.937  -39.638  3.770   1.00 39.73  ? 178 GLY A CA  1 
ATOM   1384 C C   . GLY A 1 187 ? 12.457  -38.465  4.587   1.00 44.19  ? 178 GLY A C   1 
ATOM   1385 O O   . GLY A 1 187 ? 12.859  -37.424  4.046   1.00 44.03  ? 178 GLY A O   1 
ATOM   1386 N N   . ILE A 1 188 ? 12.450  -38.650  5.906   1.00 43.11  ? 179 ILE A N   1 
ATOM   1387 C CA  . ILE A 1 188 ? 12.818  -37.625  6.858   1.00 42.48  ? 179 ILE A CA  1 
ATOM   1388 C C   . ILE A 1 188 ? 14.001  -38.115  7.669   1.00 44.42  ? 179 ILE A C   1 
ATOM   1389 O O   . ILE A 1 188 ? 13.929  -39.183  8.279   1.00 43.76  ? 179 ILE A O   1 
ATOM   1390 C CB  . ILE A 1 188 ? 11.676  -37.410  7.855   1.00 48.98  ? 179 ILE A CB  1 
ATOM   1391 C CG1 . ILE A 1 188 ? 10.335  -37.216  7.127   1.00 45.93  ? 179 ILE A CG1 1 
ATOM   1392 C CG2 . ILE A 1 188 ? 12.013  -36.263  8.818   1.00 47.77  ? 179 ILE A CG2 1 
ATOM   1393 C CD1 . ILE A 1 188 ? 10.217  -35.925  6.316   1.00 43.06  ? 179 ILE A CD1 1 
ATOM   1394 N N   . HIS A 1 189 ? 15.083  -37.342  7.699   1.00 42.97  ? 180 HIS A N   1 
ATOM   1395 C CA  . HIS A 1 189 ? 16.232  -37.753  8.487   1.00 43.60  ? 180 HIS A CA  1 
ATOM   1396 C C   . HIS A 1 189 ? 16.267  -37.138  9.880   1.00 46.05  ? 180 HIS A C   1 
ATOM   1397 O O   . HIS A 1 189 ? 16.400  -35.923  10.028  1.00 47.37  ? 180 HIS A O   1 
ATOM   1398 C CB  . HIS A 1 189 ? 17.561  -37.482  7.786   1.00 43.54  ? 180 HIS A CB  1 
ATOM   1399 C CG  . HIS A 1 189 ? 18.748  -37.921  8.592   1.00 45.81  ? 180 HIS A CG  1 
ATOM   1400 N ND1 . HIS A 1 189 ? 19.723  -37.047  9.031   1.00 44.20  ? 180 HIS A ND1 1 
ATOM   1401 C CD2 . HIS A 1 189 ? 19.091  -39.141  9.078   1.00 43.28  ? 180 HIS A CD2 1 
ATOM   1402 C CE1 . HIS A 1 189 ? 20.626  -37.714  9.729   1.00 45.84  ? 180 HIS A CE1 1 
ATOM   1403 N NE2 . HIS A 1 189 ? 20.270  -38.987  9.768   1.00 44.82  ? 180 HIS A NE2 1 
ATOM   1404 N N   . HIS A 1 190 ? 16.168  -37.990  10.897  1.00 43.91  ? 181 HIS A N   1 
ATOM   1405 C CA  . HIS A 1 190 ? 16.320  -37.563  12.269  1.00 40.46  ? 181 HIS A CA  1 
ATOM   1406 C C   . HIS A 1 190 ? 17.726  -37.873  12.721  1.00 41.22  ? 181 HIS A C   1 
ATOM   1407 O O   . HIS A 1 190 ? 18.031  -39.027  13.022  1.00 38.93  ? 181 HIS A O   1 
ATOM   1408 C CB  . HIS A 1 190 ? 15.388  -38.379  13.130  1.00 44.20  ? 181 HIS A CB  1 
ATOM   1409 C CG  . HIS A 1 190 ? 13.962  -38.304  12.706  1.00 44.68  ? 181 HIS A CG  1 
ATOM   1410 N ND1 . HIS A 1 190 ? 13.129  -37.271  13.074  1.00 43.34  ? 181 HIS A ND1 1 
ATOM   1411 C CD2 . HIS A 1 190 ? 13.216  -39.142  11.952  1.00 44.34  ? 181 HIS A CD2 1 
ATOM   1412 C CE1 . HIS A 1 190 ? 11.928  -37.475  12.568  1.00 46.04  ? 181 HIS A CE1 1 
ATOM   1413 N NE2 . HIS A 1 190 ? 11.956  -38.605  11.880  1.00 47.82  ? 181 HIS A NE2 1 
ATOM   1414 N N   . PRO A 1 191 ? 18.575  -36.844  12.838  1.00 41.56  ? 182 PRO A N   1 
ATOM   1415 C CA  . PRO A 1 191 ? 19.947  -37.230  13.174  1.00 41.72  ? 182 PRO A CA  1 
ATOM   1416 C C   . PRO A 1 191 ? 20.137  -37.421  14.683  1.00 43.87  ? 182 PRO A C   1 
ATOM   1417 O O   . PRO A 1 191 ? 19.257  -37.079  15.493  1.00 41.72  ? 182 PRO A O   1 
ATOM   1418 C CB  . PRO A 1 191 ? 20.777  -36.040  12.666  1.00 43.87  ? 182 PRO A CB  1 
ATOM   1419 C CG  . PRO A 1 191 ? 19.827  -34.880  12.679  1.00 44.25  ? 182 PRO A CG  1 
ATOM   1420 C CD  . PRO A 1 191 ? 18.447  -35.427  12.445  1.00 42.12  ? 182 PRO A CD  1 
ATOM   1421 N N   . SER A 1 192 ? 21.311  -37.928  15.050  1.00 43.43  ? 183 SER A N   1 
ATOM   1422 C CA  . SER A 1 192 ? 21.546  -38.450  16.388  1.00 39.81  ? 183 SER A CA  1 
ATOM   1423 C C   . SER A 1 192 ? 21.844  -37.349  17.391  1.00 40.87  ? 183 SER A C   1 
ATOM   1424 O O   . SER A 1 192 ? 21.459  -37.434  18.559  1.00 43.49  ? 183 SER A O   1 
ATOM   1425 C CB  . SER A 1 192 ? 22.701  -39.444  16.364  1.00 39.65  ? 183 SER A CB  1 
ATOM   1426 O OG  . SER A 1 192 ? 23.925  -38.768  16.143  1.00 44.77  ? 183 SER A OG  1 
ATOM   1427 N N   . THR A 1 193 ? 22.555  -36.328  16.933  1.00 43.45  ? 184 THR A N   1 
ATOM   1428 C CA  . THR A 1 193 ? 23.004  -35.253  17.805  1.00 43.98  ? 184 THR A CA  1 
ATOM   1429 C C   . THR A 1 193 ? 22.831  -33.918  17.108  1.00 43.98  ? 184 THR A C   1 
ATOM   1430 O O   . THR A 1 193 ? 22.767  -33.855  15.883  1.00 44.94  ? 184 THR A O   1 
ATOM   1431 C CB  . THR A 1 193 ? 24.500  -35.389  18.132  1.00 41.84  ? 184 THR A CB  1 
ATOM   1432 O OG1 . THR A 1 193 ? 25.264  -34.907  17.020  1.00 47.22  ? 184 THR A OG1 1 
ATOM   1433 C CG2 . THR A 1 193 ? 24.866  -36.840  18.397  1.00 37.62  ? 184 THR A CG2 1 
ATOM   1434 N N   . SER A 1 194 ? 22.795  -32.845  17.890  1.00 45.31  ? 185 SER A N   1 
ATOM   1435 C CA  . SER A 1 194 ? 22.667  -31.502  17.341  1.00 43.95  ? 185 SER A CA  1 
ATOM   1436 C C   . SER A 1 194 ? 23.820  -31.209  16.405  1.00 44.67  ? 185 SER A C   1 
ATOM   1437 O O   . SER A 1 194 ? 23.653  -30.543  15.388  1.00 47.94  ? 185 SER A O   1 
ATOM   1438 C CB  . SER A 1 194 ? 22.632  -30.475  18.463  1.00 44.24  ? 185 SER A CB  1 
ATOM   1439 O OG  . SER A 1 194 ? 21.549  -30.746  19.340  1.00 51.98  ? 185 SER A OG  1 
ATOM   1440 N N   . ALA A 1 195 ? 24.995  -31.716  16.747  1.00 42.18  ? 186 ALA A N   1 
ATOM   1441 C CA  . ALA A 1 195 ? 26.165  -31.522  15.905  1.00 44.19  ? 186 ALA A CA  1 
ATOM   1442 C C   . ALA A 1 195 ? 25.900  -32.156  14.542  1.00 47.23  ? 186 ALA A C   1 
ATOM   1443 O O   . ALA A 1 195 ? 26.177  -31.568  13.494  1.00 48.34  ? 186 ALA A O   1 
ATOM   1444 C CB  . ALA A 1 195 ? 27.382  -32.148  16.553  1.00 42.45  ? 186 ALA A CB  1 
ATOM   1445 N N   . ASP A 1 196 ? 25.341  -33.359  14.573  1.00 47.30  ? 187 ASP A N   1 
ATOM   1446 C CA  . ASP A 1 196 ? 25.022  -34.088  13.364  1.00 43.31  ? 187 ASP A CA  1 
ATOM   1447 C C   . ASP A 1 196 ? 24.053  -33.277  12.547  1.00 44.45  ? 187 ASP A C   1 
ATOM   1448 O O   . ASP A 1 196 ? 24.293  -33.000  11.382  1.00 46.43  ? 187 ASP A O   1 
ATOM   1449 C CB  . ASP A 1 196 ? 24.381  -35.412  13.731  1.00 48.99  ? 187 ASP A CB  1 
ATOM   1450 C CG  . ASP A 1 196 ? 24.748  -36.501  12.782  1.00 54.38  ? 187 ASP A CG  1 
ATOM   1451 O OD1 . ASP A 1 196 ? 25.950  -36.866  12.741  1.00 59.51  ? 187 ASP A OD1 1 
ATOM   1452 O OD2 . ASP A 1 196 ? 23.832  -37.006  12.094  1.00 53.65  ? 187 ASP A OD2 1 
ATOM   1453 N N   . GLN A 1 197 ? 22.957  -32.873  13.174  1.00 46.38  ? 188 GLN A N   1 
ATOM   1454 C CA  . GLN A 1 197 ? 21.978  -32.032  12.510  1.00 44.46  ? 188 GLN A CA  1 
ATOM   1455 C C   . GLN A 1 197 ? 22.664  -30.896  11.782  1.00 44.75  ? 188 GLN A C   1 
ATOM   1456 O O   . GLN A 1 197 ? 22.385  -30.646  10.609  1.00 46.11  ? 188 GLN A O   1 
ATOM   1457 C CB  . GLN A 1 197 ? 21.024  -31.424  13.527  1.00 42.68  ? 188 GLN A CB  1 
ATOM   1458 C CG  . GLN A 1 197 ? 20.173  -30.321  12.945  1.00 41.71  ? 188 GLN A CG  1 
ATOM   1459 C CD  . GLN A 1 197 ? 19.296  -30.840  11.865  1.00 40.72  ? 188 GLN A CD  1 
ATOM   1460 O OE1 . GLN A 1 197 ? 18.990  -32.021  11.846  1.00 41.07  ? 188 GLN A OE1 1 
ATOM   1461 N NE2 . GLN A 1 197 ? 18.897  -29.978  10.941  1.00 44.07  ? 188 GLN A NE2 1 
ATOM   1462 N N   . GLN A 1 198 ? 23.571  -30.213  12.472  1.00 43.67  ? 189 GLN A N   1 
ATOM   1463 C CA  . GLN A 1 198 ? 24.162  -28.987  11.933  1.00 49.28  ? 189 GLN A CA  1 
ATOM   1464 C C   . GLN A 1 198 ? 25.074  -29.227  10.736  1.00 47.71  ? 189 GLN A C   1 
ATOM   1465 O O   . GLN A 1 198 ? 25.024  -28.484  9.757   1.00 47.95  ? 189 GLN A O   1 
ATOM   1466 C CB  . GLN A 1 198 ? 24.914  -28.209  13.006  1.00 51.41  ? 189 GLN A CB  1 
ATOM   1467 C CG  . GLN A 1 198 ? 25.251  -26.790  12.573  1.00 54.28  ? 189 GLN A CG  1 
ATOM   1468 C CD  . GLN A 1 198 ? 26.307  -26.161  13.455  1.00 58.76  ? 189 GLN A CD  1 
ATOM   1469 O OE1 . GLN A 1 198 ? 27.308  -26.799  13.790  1.00 59.41  ? 189 GLN A OE1 1 
ATOM   1470 N NE2 . GLN A 1 198 ? 26.088  -24.909  13.848  1.00 60.16  ? 189 GLN A NE2 1 
ATOM   1471 N N   . SER A 1 199 ? 25.891  -30.270  10.809  1.00 45.77  ? 190 SER A N   1 
ATOM   1472 C CA  . SER A 1 199 ? 26.740  -30.631  9.678   1.00 47.64  ? 190 SER A CA  1 
ATOM   1473 C C   . SER A 1 199 ? 25.929  -30.838  8.415   1.00 48.88  ? 190 SER A C   1 
ATOM   1474 O O   . SER A 1 199 ? 26.197  -30.206  7.405   1.00 53.66  ? 190 SER A O   1 
ATOM   1475 C CB  . SER A 1 199 ? 27.533  -31.896  9.968   1.00 45.95  ? 190 SER A CB  1 
ATOM   1476 O OG  . SER A 1 199 ? 27.153  -32.411  11.226  1.00 52.36  ? 190 SER A OG  1 
ATOM   1477 N N   . LEU A 1 200 ? 24.949  -31.731  8.457   1.00 45.73  ? 191 LEU A N   1 
ATOM   1478 C CA  . LEU A 1 200 ? 24.129  -31.978  7.279   1.00 44.55  ? 191 LEU A CA  1 
ATOM   1479 C C   . LEU A 1 200 ? 23.435  -30.725  6.776   1.00 47.16  ? 191 LEU A C   1 
ATOM   1480 O O   . LEU A 1 200 ? 23.722  -30.253  5.683   1.00 52.14  ? 191 LEU A O   1 
ATOM   1481 C CB  . LEU A 1 200 ? 23.085  -33.046  7.568   1.00 47.86  ? 191 LEU A CB  1 
ATOM   1482 C CG  . LEU A 1 200 ? 23.644  -34.203  8.389   1.00 48.37  ? 191 LEU A CG  1 
ATOM   1483 C CD1 . LEU A 1 200 ? 22.584  -35.286  8.594   1.00 45.74  ? 191 LEU A CD1 1 
ATOM   1484 C CD2 . LEU A 1 200 ? 24.874  -34.747  7.692   1.00 44.62  ? 191 LEU A CD2 1 
ATOM   1485 N N   . TYR A 1 201 ? 22.498  -30.206  7.559   1.00 48.75  ? 192 TYR A N   1 
ATOM   1486 C CA  . TYR A 1 201 ? 21.619  -29.129  7.086   1.00 50.50  ? 192 TYR A CA  1 
ATOM   1487 C C   . TYR A 1 201 ? 21.933  -27.685  7.534   1.00 50.32  ? 192 TYR A C   1 
ATOM   1488 O O   . TYR A 1 201 ? 21.242  -26.746  7.139   1.00 49.92  ? 192 TYR A O   1 
ATOM   1489 C CB  . TYR A 1 201 ? 20.175  -29.522  7.392   1.00 47.54  ? 192 TYR A CB  1 
ATOM   1490 C CG  . TYR A 1 201 ? 20.021  -31.021  7.341   1.00 45.14  ? 192 TYR A CG  1 
ATOM   1491 C CD1 . TYR A 1 201 ? 19.973  -31.682  6.131   1.00 46.32  ? 192 TYR A CD1 1 
ATOM   1492 C CD2 . TYR A 1 201 ? 19.974  -31.786  8.501   1.00 46.12  ? 192 TYR A CD2 1 
ATOM   1493 C CE1 . TYR A 1 201 ? 19.849  -33.065  6.065   1.00 46.77  ? 192 TYR A CE1 1 
ATOM   1494 C CE2 . TYR A 1 201 ? 19.850  -33.180  8.445   1.00 45.15  ? 192 TYR A CE2 1 
ATOM   1495 C CZ  . TYR A 1 201 ? 19.790  -33.809  7.220   1.00 46.86  ? 192 TYR A CZ  1 
ATOM   1496 O OH  . TYR A 1 201 ? 19.664  -35.183  7.128   1.00 47.39  ? 192 TYR A OH  1 
ATOM   1497 N N   . GLN A 1 202 ? 22.946  -27.525  8.377   1.00 50.46  ? 193 GLN A N   1 
ATOM   1498 C CA  . GLN A 1 202 ? 23.385  -26.209  8.855   1.00 52.74  ? 193 GLN A CA  1 
ATOM   1499 C C   . GLN A 1 202 ? 22.345  -25.536  9.725   1.00 53.19  ? 193 GLN A C   1 
ATOM   1500 O O   . GLN A 1 202 ? 22.654  -24.616  10.474  1.00 55.75  ? 193 GLN A O   1 
ATOM   1501 C CB  . GLN A 1 202 ? 23.711  -25.267  7.691   1.00 54.33  ? 193 GLN A CB  1 
ATOM   1502 C CG  . GLN A 1 202 ? 23.734  -23.781  8.086   1.00 57.52  ? 193 GLN A CG  1 
ATOM   1503 C CD  . GLN A 1 202 ? 24.805  -23.462  9.119   1.00 60.58  ? 193 GLN A CD  1 
ATOM   1504 O OE1 . GLN A 1 202 ? 25.882  -24.066  9.116   1.00 58.47  ? 193 GLN A OE1 1 
ATOM   1505 N NE2 . GLN A 1 202 ? 24.514  -22.510  10.011  1.00 59.26  ? 193 GLN A NE2 1 
ATOM   1506 N N   . ASN A 1 203 ? 21.115  -26.021  9.656   1.00 51.70  ? 194 ASN A N   1 
ATOM   1507 C CA  . ASN A 1 203 ? 20.016  -25.317  10.288  1.00 52.27  ? 194 ASN A CA  1 
ATOM   1508 C C   . ASN A 1 203 ? 19.378  -26.144  11.403  1.00 54.02  ? 194 ASN A C   1 
ATOM   1509 O O   . ASN A 1 203 ? 18.733  -27.160  11.139  1.00 54.15  ? 194 ASN A O   1 
ATOM   1510 C CB  . ASN A 1 203 ? 18.974  -24.931  9.237   1.00 50.49  ? 194 ASN A CB  1 
ATOM   1511 C CG  . ASN A 1 203 ? 19.567  -24.136  8.090   1.00 55.48  ? 194 ASN A CG  1 
ATOM   1512 O OD1 . ASN A 1 203 ? 20.507  -23.353  8.276   1.00 58.17  ? 194 ASN A OD1 1 
ATOM   1513 N ND2 . ASN A 1 203 ? 19.018  -24.329  6.889   1.00 52.53  ? 194 ASN A ND2 1 
ATOM   1514 N N   . ALA A 1 204 ? 19.545  -25.705  12.646  1.00 53.22  ? 195 ALA A N   1 
ATOM   1515 C CA  . ALA A 1 204 ? 18.951  -26.415  13.769  1.00 53.55  ? 195 ALA A CA  1 
ATOM   1516 C C   . ALA A 1 204 ? 17.441  -26.285  13.737  1.00 53.37  ? 195 ALA A C   1 
ATOM   1517 O O   . ALA A 1 204 ? 16.724  -27.145  14.222  1.00 54.07  ? 195 ALA A O   1 
ATOM   1518 C CB  . ALA A 1 204 ? 19.488  -25.888  15.071  1.00 51.65  ? 195 ALA A CB  1 
ATOM   1519 N N   . ASP A 1 205 ? 16.954  -25.221  13.122  1.00 56.55  ? 196 ASP A N   1 
ATOM   1520 C CA  . ASP A 1 205 ? 15.522  -24.949  13.116  1.00 59.35  ? 196 ASP A CA  1 
ATOM   1521 C C   . ASP A 1 205 ? 14.762  -25.793  12.096  1.00 60.56  ? 196 ASP A C   1 
ATOM   1522 O O   . ASP A 1 205 ? 13.537  -25.705  12.014  1.00 62.39  ? 196 ASP A O   1 
ATOM   1523 C CB  . ASP A 1 205 ? 15.289  -23.480  12.768  1.00 63.70  ? 196 ASP A CB  1 
ATOM   1524 C CG  . ASP A 1 205 ? 15.739  -23.140  11.350  1.00 71.89  ? 196 ASP A CG  1 
ATOM   1525 O OD1 . ASP A 1 205 ? 16.936  -22.808  11.166  1.00 72.24  ? 196 ASP A OD1 1 
ATOM   1526 O OD2 . ASP A 1 205 ? 14.897  -23.204  10.419  1.00 70.85  ? 196 ASP A OD2 1 
ATOM   1527 N N   . ALA A 1 206 ? 15.490  -26.609  11.336  1.00 57.87  ? 197 ALA A N   1 
ATOM   1528 C CA  . ALA A 1 206 ? 14.983  -27.235  10.112  1.00 51.02  ? 197 ALA A CA  1 
ATOM   1529 C C   . ALA A 1 206 ? 13.643  -27.980  10.224  1.00 51.39  ? 197 ALA A C   1 
ATOM   1530 O O   . ALA A 1 206 ? 13.419  -28.749  11.159  1.00 55.49  ? 197 ALA A O   1 
ATOM   1531 C CB  . ALA A 1 206 ? 16.040  -28.156  9.556   1.00 51.90  ? 197 ALA A CB  1 
ATOM   1532 N N   . TYR A 1 207 ? 12.759  -27.735  9.261   1.00 48.45  ? 198 TYR A N   1 
ATOM   1533 C CA  . TYR A 1 207 ? 11.505  -28.470  9.125   1.00 46.71  ? 198 TYR A CA  1 
ATOM   1534 C C   . TYR A 1 207 ? 11.350  -28.959  7.693   1.00 48.16  ? 198 TYR A C   1 
ATOM   1535 O O   . TYR A 1 207 ? 12.160  -28.671  6.811   1.00 47.15  ? 198 TYR A O   1 
ATOM   1536 C CB  . TYR A 1 207 ? 10.293  -27.581  9.431   1.00 47.67  ? 198 TYR A CB  1 
ATOM   1537 C CG  . TYR A 1 207 ? 9.972   -26.617  8.302   1.00 50.51  ? 198 TYR A CG  1 
ATOM   1538 C CD1 . TYR A 1 207 ? 9.156   -26.992  7.238   1.00 50.72  ? 198 TYR A CD1 1 
ATOM   1539 C CD2 . TYR A 1 207 ? 10.518  -25.337  8.281   1.00 54.19  ? 198 TYR A CD2 1 
ATOM   1540 C CE1 . TYR A 1 207 ? 8.886   -26.108  6.200   1.00 51.15  ? 198 TYR A CE1 1 
ATOM   1541 C CE2 . TYR A 1 207 ? 10.253  -24.456  7.247   1.00 50.45  ? 198 TYR A CE2 1 
ATOM   1542 C CZ  . TYR A 1 207 ? 9.444   -24.840  6.217   1.00 48.62  ? 198 TYR A CZ  1 
ATOM   1543 O OH  . TYR A 1 207 ? 9.200   -23.937  5.212   1.00 54.34  ? 198 TYR A OH  1 
ATOM   1544 N N   . VAL A 1 208 ? 10.268  -29.682  7.465   1.00 48.99  ? 199 VAL A N   1 
ATOM   1545 C CA  . VAL A 1 208 ? 9.963   -30.203  6.157   1.00 46.65  ? 199 VAL A CA  1 
ATOM   1546 C C   . VAL A 1 208 ? 8.458   -30.156  5.984   1.00 47.38  ? 199 VAL A C   1 
ATOM   1547 O O   . VAL A 1 208 ? 7.707   -30.419  6.923   1.00 48.71  ? 199 VAL A O   1 
ATOM   1548 C CB  . VAL A 1 208 ? 10.456  -31.653  6.029   1.00 45.28  ? 199 VAL A CB  1 
ATOM   1549 C CG1 . VAL A 1 208 ? 9.939   -32.279  4.741   1.00 46.70  ? 199 VAL A CG1 1 
ATOM   1550 C CG2 . VAL A 1 208 ? 11.987  -31.712  6.109   1.00 44.12  ? 199 VAL A CG2 1 
ATOM   1551 N N   . PHE A 1 209 ? 8.006   -29.813  4.791   1.00 48.75  ? 200 PHE A N   1 
ATOM   1552 C CA  . PHE A 1 209 ? 6.581   -29.833  4.539   1.00 48.56  ? 200 PHE A CA  1 
ATOM   1553 C C   . PHE A 1 209 ? 6.295   -30.480  3.201   1.00 48.18  ? 200 PHE A C   1 
ATOM   1554 O O   . PHE A 1 209 ? 7.101   -30.398  2.275   1.00 48.41  ? 200 PHE A O   1 
ATOM   1555 C CB  . PHE A 1 209 ? 5.986   -28.429  4.598   1.00 48.61  ? 200 PHE A CB  1 
ATOM   1556 C CG  . PHE A 1 209 ? 4.546   -28.386  4.203   1.00 50.53  ? 200 PHE A CG  1 
ATOM   1557 C CD1 . PHE A 1 209 ? 3.554   -28.759  5.098   1.00 52.70  ? 200 PHE A CD1 1 
ATOM   1558 C CD2 . PHE A 1 209 ? 4.181   -28.025  2.918   1.00 51.13  ? 200 PHE A CD2 1 
ATOM   1559 C CE1 . PHE A 1 209 ? 2.212   -28.742  4.725   1.00 51.26  ? 200 PHE A CE1 1 
ATOM   1560 C CE2 . PHE A 1 209 ? 2.850   -28.009  2.533   1.00 51.27  ? 200 PHE A CE2 1 
ATOM   1561 C CZ  . PHE A 1 209 ? 1.862   -28.367  3.440   1.00 50.67  ? 200 PHE A CZ  1 
ATOM   1562 N N   . VAL A 1 210 ? 5.149   -31.141  3.116   1.00 46.39  ? 201 VAL A N   1 
ATOM   1563 C CA  . VAL A 1 210 ? 4.786   -31.864  1.916   1.00 48.81  ? 201 VAL A CA  1 
ATOM   1564 C C   . VAL A 1 210 ? 3.287   -31.769  1.713   1.00 51.32  ? 201 VAL A C   1 
ATOM   1565 O O   . VAL A 1 210 ? 2.536   -31.960  2.670   1.00 52.55  ? 201 VAL A O   1 
ATOM   1566 C CB  . VAL A 1 210 ? 5.167   -33.335  2.063   1.00 45.64  ? 201 VAL A CB  1 
ATOM   1567 C CG1 . VAL A 1 210 ? 4.756   -34.116  0.836   1.00 46.86  ? 201 VAL A CG1 1 
ATOM   1568 C CG2 . VAL A 1 210 ? 6.657   -33.459  2.327   1.00 41.71  ? 201 VAL A CG2 1 
ATOM   1569 N N   . GLY A 1 211 ? 2.841   -31.489  0.486   1.00 52.57  ? 202 GLY A N   1 
ATOM   1570 C CA  . GLY A 1 211 ? 1.418   -31.267  0.248   1.00 56.44  ? 202 GLY A CA  1 
ATOM   1571 C C   . GLY A 1 211 ? 0.844   -31.612  -1.121  1.00 54.56  ? 202 GLY A C   1 
ATOM   1572 O O   . GLY A 1 211 ? 1.565   -31.731  -2.108  1.00 52.08  ? 202 GLY A O   1 
ATOM   1573 N N   . SER A 1 212 ? -0.474  -31.780  -1.161  1.00 54.80  ? 203 SER A N   1 
ATOM   1574 C CA  . SER A 1 212 ? -1.187  -32.163  -2.370  1.00 55.49  ? 203 SER A CA  1 
ATOM   1575 C C   . SER A 1 212 ? -2.694  -32.044  -2.131  1.00 56.88  ? 203 SER A C   1 
ATOM   1576 O O   . SER A 1 212 ? -3.128  -31.542  -1.097  1.00 59.30  ? 203 SER A O   1 
ATOM   1577 C CB  . SER A 1 212 ? -0.810  -33.585  -2.800  1.00 54.40  ? 203 SER A CB  1 
ATOM   1578 O OG  . SER A 1 212 ? -1.600  -34.560  -2.144  1.00 54.51  ? 203 SER A OG  1 
ATOM   1579 N N   . SER A 1 213 ? -3.490  -32.472  -3.104  1.00 58.73  ? 204 SER A N   1 
ATOM   1580 C CA  . SER A 1 213 ? -4.938  -32.498  -2.938  1.00 60.46  ? 204 SER A CA  1 
ATOM   1581 C C   . SER A 1 213 ? -5.296  -33.572  -1.930  1.00 57.16  ? 204 SER A C   1 
ATOM   1582 O O   . SER A 1 213 ? -6.222  -33.418  -1.133  1.00 61.44  ? 204 SER A O   1 
ATOM   1583 C CB  . SER A 1 213 ? -5.636  -32.772  -4.281  1.00 61.68  ? 204 SER A CB  1 
ATOM   1584 O OG  . SER A 1 213 ? -6.876  -33.446  -4.104  1.00 58.52  ? 204 SER A OG  1 
ATOM   1585 N N   . ARG A 1 214 ? -4.561  -34.673  -1.987  1.00 55.60  ? 205 ARG A N   1 
ATOM   1586 C CA  . ARG A 1 214 ? -4.836  -35.829  -1.147  1.00 57.20  ? 205 ARG A CA  1 
ATOM   1587 C C   . ARG A 1 214 ? -4.009  -35.836  0.138   1.00 58.18  ? 205 ARG A C   1 
ATOM   1588 O O   . ARG A 1 214 ? -4.176  -36.718  0.993   1.00 55.78  ? 205 ARG A O   1 
ATOM   1589 C CB  . ARG A 1 214 ? -4.559  -37.105  -1.946  1.00 56.59  ? 205 ARG A CB  1 
ATOM   1590 C CG  . ARG A 1 214 ? -5.304  -38.336  -1.458  1.00 58.49  ? 205 ARG A CG  1 
ATOM   1591 C CD  . ARG A 1 214 ? -5.935  -39.102  -2.630  1.00 56.74  ? 205 ARG A CD  1 
ATOM   1592 N NE  . ARG A 1 214 ? -4.931  -39.663  -3.530  1.00 57.60  ? 205 ARG A NE  1 
ATOM   1593 C CZ  . ARG A 1 214 ? -5.207  -40.369  -4.627  1.00 61.53  ? 205 ARG A CZ  1 
ATOM   1594 N NH1 . ARG A 1 214 ? -6.467  -40.605  -4.980  1.00 62.98  ? 205 ARG A NH1 1 
ATOM   1595 N NH2 . ARG A 1 214 ? -4.218  -40.848  -5.373  1.00 58.85  ? 205 ARG A NH2 1 
ATOM   1596 N N   . TYR A 1 215 ? -3.063  -34.906  0.242   1.00 55.28  ? 206 TYR A N   1 
ATOM   1597 C CA  . TYR A 1 215 ? -2.051  -35.020  1.283   1.00 53.13  ? 206 TYR A CA  1 
ATOM   1598 C C   . TYR A 1 215 ? -1.532  -33.705  1.846   1.00 55.71  ? 206 TYR A C   1 
ATOM   1599 O O   . TYR A 1 215 ? -1.104  -32.824  1.100   1.00 55.75  ? 206 TYR A O   1 
ATOM   1600 C CB  . TYR A 1 215 ? -0.875  -35.817  0.724   1.00 52.97  ? 206 TYR A CB  1 
ATOM   1601 C CG  . TYR A 1 215 ? 0.059   -36.314  1.782   1.00 54.17  ? 206 TYR A CG  1 
ATOM   1602 C CD1 . TYR A 1 215 ? 1.145   -35.554  2.185   1.00 54.82  ? 206 TYR A CD1 1 
ATOM   1603 C CD2 . TYR A 1 215 ? -0.129  -37.557  2.367   1.00 52.91  ? 206 TYR A CD2 1 
ATOM   1604 C CE1 . TYR A 1 215 ? 2.016   -36.012  3.171   1.00 55.22  ? 206 TYR A CE1 1 
ATOM   1605 C CE2 . TYR A 1 215 ? 0.728   -38.025  3.348   1.00 55.31  ? 206 TYR A CE2 1 
ATOM   1606 C CZ  . TYR A 1 215 ? 1.801   -37.249  3.753   1.00 54.52  ? 206 TYR A CZ  1 
ATOM   1607 O OH  . TYR A 1 215 ? 2.659   -37.720  4.734   1.00 51.00  ? 206 TYR A OH  1 
ATOM   1608 N N   . SER A 1 216 ? -1.528  -33.578  3.165   1.00 56.11  ? 207 SER A N   1 
ATOM   1609 C CA  . SER A 1 216 ? -0.798  -32.483  3.769   1.00 54.42  ? 207 SER A CA  1 
ATOM   1610 C C   . SER A 1 216 ? -0.174  -32.904  5.094   1.00 52.62  ? 207 SER A C   1 
ATOM   1611 O O   . SER A 1 216 ? -0.881  -33.367  5.981   1.00 57.04  ? 207 SER A O   1 
ATOM   1612 C CB  . SER A 1 216 ? -1.732  -31.289  3.967   1.00 59.83  ? 207 SER A CB  1 
ATOM   1613 O OG  . SER A 1 216 ? -1.025  -30.063  3.873   1.00 58.69  ? 207 SER A OG  1 
ATOM   1614 N N   . LYS A 1 217 ? 1.135   -32.723  5.230   1.00 48.65  ? 208 LYS A N   1 
ATOM   1615 C CA  . LYS A 1 217 ? 1.834   -32.999  6.481   1.00 50.34  ? 208 LYS A CA  1 
ATOM   1616 C C   . LYS A 1 217 ? 3.087   -32.138  6.645   1.00 50.95  ? 208 LYS A C   1 
ATOM   1617 O O   . LYS A 1 217 ? 3.796   -31.857  5.668   1.00 48.54  ? 208 LYS A O   1 
ATOM   1618 C CB  . LYS A 1 217 ? 2.195   -34.486  6.613   1.00 51.59  ? 208 LYS A CB  1 
ATOM   1619 C CG  . LYS A 1 217 ? 1.194   -35.314  7.443   1.00 56.99  ? 208 LYS A CG  1 
ATOM   1620 C CD  . LYS A 1 217 ? 1.140   -34.884  8.911   1.00 55.84  ? 208 LYS A CD  1 
ATOM   1621 C CE  . LYS A 1 217 ? 0.366   -35.901  9.787   1.00 62.06  ? 208 LYS A CE  1 
ATOM   1622 N NZ  . LYS A 1 217 ? -1.131  -35.834  9.667   1.00 63.32  ? 208 LYS A NZ  1 
ATOM   1623 N N   . LYS A 1 218 ? 3.354   -31.731  7.885   1.00 49.46  ? 209 LYS A N   1 
ATOM   1624 C CA  . LYS A 1 218 ? 4.596   -31.050  8.214   1.00 48.07  ? 209 LYS A CA  1 
ATOM   1625 C C   . LYS A 1 218 ? 5.441   -31.959  9.089   1.00 46.32  ? 209 LYS A C   1 
ATOM   1626 O O   . LYS A 1 218 ? 4.912   -32.743  9.864   1.00 49.91  ? 209 LYS A O   1 
ATOM   1627 C CB  . LYS A 1 218 ? 4.328   -29.735  8.937   1.00 45.88  ? 209 LYS A CB  1 
ATOM   1628 C CG  . LYS A 1 218 ? 5.595   -28.963  9.300   1.00 47.54  ? 209 LYS A CG  1 
ATOM   1629 C CD  . LYS A 1 218 ? 5.280   -27.483  9.554   1.00 55.53  ? 209 LYS A CD  1 
ATOM   1630 C CE  . LYS A 1 218 ? 6.354   -26.784  10.403  1.00 55.66  ? 209 LYS A CE  1 
ATOM   1631 N NZ  . LYS A 1 218 ? 6.076   -25.331  10.548  1.00 49.43  ? 209 LYS A NZ  1 
ATOM   1632 N N   . PHE A 1 219 ? 6.755   -31.855  8.980   1.00 45.27  ? 210 PHE A N   1 
ATOM   1633 C CA  . PHE A 1 219 ? 7.611   -32.738  9.753   1.00 44.20  ? 210 PHE A CA  1 
ATOM   1634 C C   . PHE A 1 219 ? 8.673   -31.973  10.507  1.00 44.59  ? 210 PHE A C   1 
ATOM   1635 O O   . PHE A 1 219 ? 9.313   -31.069  9.976   1.00 45.36  ? 210 PHE A O   1 
ATOM   1636 C CB  . PHE A 1 219 ? 8.283   -33.788  8.863   1.00 46.82  ? 210 PHE A CB  1 
ATOM   1637 C CG  . PHE A 1 219 ? 7.330   -34.541  7.975   1.00 47.38  ? 210 PHE A CG  1 
ATOM   1638 C CD1 . PHE A 1 219 ? 7.028   -34.070  6.703   1.00 46.44  ? 210 PHE A CD1 1 
ATOM   1639 C CD2 . PHE A 1 219 ? 6.744   -35.725  8.401   1.00 44.55  ? 210 PHE A CD2 1 
ATOM   1640 C CE1 . PHE A 1 219 ? 6.147   -34.764  5.878   1.00 45.17  ? 210 PHE A CE1 1 
ATOM   1641 C CE2 . PHE A 1 219 ? 5.867   -36.424  7.571   1.00 47.20  ? 210 PHE A CE2 1 
ATOM   1642 C CZ  . PHE A 1 219 ? 5.568   -35.938  6.312   1.00 45.11  ? 210 PHE A CZ  1 
ATOM   1643 N N   . LYS A 1 220 ? 8.807   -32.325  11.775  1.00 48.48  ? 211 LYS A N   1 
ATOM   1644 C CA  . LYS A 1 220 ? 9.926   -31.922  12.603  1.00 48.09  ? 211 LYS A CA  1 
ATOM   1645 C C   . LYS A 1 220 ? 10.755  -33.167  12.873  1.00 48.19  ? 211 LYS A C   1 
ATOM   1646 O O   . LYS A 1 220 ? 10.222  -34.198  13.270  1.00 51.98  ? 211 LYS A O   1 
ATOM   1647 C CB  . LYS A 1 220 ? 9.428   -31.303  13.905  1.00 46.88  ? 211 LYS A CB  1 
ATOM   1648 C CG  . LYS A 1 220 ? 10.481  -31.140  14.998  1.00 56.19  ? 211 LYS A CG  1 
ATOM   1649 C CD  . LYS A 1 220 ? 9.865   -30.492  16.256  1.00 58.25  ? 211 LYS A CD  1 
ATOM   1650 C CE  . LYS A 1 220 ? 10.822  -30.490  17.452  1.00 59.01  ? 211 LYS A CE  1 
ATOM   1651 N NZ  . LYS A 1 220 ? 10.205  -29.808  18.626  1.00 59.29  ? 211 LYS A NZ  1 
ATOM   1652 N N   . PRO A 1 221 ? 12.057  -33.095  12.615  1.00 47.36  ? 212 PRO A N   1 
ATOM   1653 C CA  . PRO A 1 221 ? 12.952  -34.206  12.941  1.00 46.00  ? 212 PRO A CA  1 
ATOM   1654 C C   . PRO A 1 221 ? 13.206  -34.273  14.447  1.00 47.23  ? 212 PRO A C   1 
ATOM   1655 O O   . PRO A 1 221 ? 13.102  -33.250  15.121  1.00 48.77  ? 212 PRO A O   1 
ATOM   1656 C CB  . PRO A 1 221 ? 14.234  -33.814  12.218  1.00 50.35  ? 212 PRO A CB  1 
ATOM   1657 C CG  . PRO A 1 221 ? 14.224  -32.311  12.304  1.00 52.56  ? 212 PRO A CG  1 
ATOM   1658 C CD  . PRO A 1 221 ? 12.786  -31.929  12.091  1.00 48.93  ? 212 PRO A CD  1 
ATOM   1659 N N   . GLU A 1 222 ? 13.522  -35.461  14.965  1.00 48.68  ? 213 GLU A N   1 
ATOM   1660 C CA  . GLU A 1 222 ? 13.880  -35.632  16.377  1.00 44.87  ? 213 GLU A CA  1 
ATOM   1661 C C   . GLU A 1 222 ? 15.362  -35.993  16.500  1.00 41.97  ? 213 GLU A C   1 
ATOM   1662 O O   . GLU A 1 222 ? 15.777  -37.083  16.101  1.00 37.41  ? 213 GLU A O   1 
ATOM   1663 C CB  . GLU A 1 222 ? 13.008  -36.709  17.037  1.00 42.07  ? 213 GLU A CB  1 
ATOM   1664 C CG  . GLU A 1 222 ? 13.013  -36.696  18.578  1.00 48.83  ? 213 GLU A CG  1 
ATOM   1665 C CD  . GLU A 1 222 ? 12.121  -37.793  19.183  1.00 54.48  ? 213 GLU A CD  1 
ATOM   1666 O OE1 . GLU A 1 222 ? 11.360  -37.524  20.145  1.00 52.66  ? 213 GLU A OE1 1 
ATOM   1667 O OE2 . GLU A 1 222 ? 12.177  -38.942  18.692  1.00 56.57  ? 213 GLU A OE2 1 
ATOM   1668 N N   . ILE A 1 223 ? 16.152  -35.058  17.031  1.00 42.38  ? 214 ILE A N   1 
ATOM   1669 C CA  . ILE A 1 223 ? 17.562  -35.305  17.317  1.00 42.93  ? 214 ILE A CA  1 
ATOM   1670 C C   . ILE A 1 223 ? 17.619  -36.120  18.591  1.00 40.89  ? 214 ILE A C   1 
ATOM   1671 O O   . ILE A 1 223 ? 17.019  -35.766  19.595  1.00 43.20  ? 214 ILE A O   1 
ATOM   1672 C CB  . ILE A 1 223 ? 18.385  -33.996  17.547  1.00 42.99  ? 214 ILE A CB  1 
ATOM   1673 C CG1 . ILE A 1 223 ? 18.629  -33.244  16.246  1.00 40.87  ? 214 ILE A CG1 1 
ATOM   1674 C CG2 . ILE A 1 223 ? 19.748  -34.313  18.162  1.00 41.18  ? 214 ILE A CG2 1 
ATOM   1675 C CD1 . ILE A 1 223 ? 17.389  -32.729  15.618  1.00 47.45  ? 214 ILE A CD1 1 
ATOM   1676 N N   . ALA A 1 224 ? 18.348  -37.215  18.558  1.00 40.11  ? 215 ALA A N   1 
ATOM   1677 C CA  . ALA A 1 224 ? 18.430  -38.061  19.722  1.00 36.77  ? 215 ALA A CA  1 
ATOM   1678 C C   . ALA A 1 224 ? 19.299  -39.211  19.327  1.00 37.47  ? 215 ALA A C   1 
ATOM   1679 O O   . ALA A 1 224 ? 19.458  -39.496  18.136  1.00 38.99  ? 215 ALA A O   1 
ATOM   1680 C CB  . ALA A 1 224 ? 17.069  -38.568  20.088  1.00 39.95  ? 215 ALA A CB  1 
ATOM   1681 N N   . ILE A 1 225 ? 19.820  -39.905  20.320  1.00 35.17  ? 216 ILE A N   1 
ATOM   1682 C CA  . ILE A 1 225 ? 20.706  -41.003  20.047  1.00 36.99  ? 216 ILE A CA  1 
ATOM   1683 C C   . ILE A 1 225 ? 19.971  -42.312  20.236  1.00 37.35  ? 216 ILE A C   1 
ATOM   1684 O O   . ILE A 1 225 ? 19.755  -42.776  21.359  1.00 39.69  ? 216 ILE A O   1 
ATOM   1685 C CB  . ILE A 1 225 ? 21.909  -40.928  20.981  1.00 38.55  ? 216 ILE A CB  1 
ATOM   1686 C CG1 . ILE A 1 225 ? 22.727  -39.686  20.621  1.00 39.09  ? 216 ILE A CG1 1 
ATOM   1687 C CG2 . ILE A 1 225 ? 22.727  -42.220  20.909  1.00 38.07  ? 216 ILE A CG2 1 
ATOM   1688 C CD1 . ILE A 1 225 ? 23.955  -39.505  21.456  1.00 42.37  ? 216 ILE A CD1 1 
ATOM   1689 N N   . ARG A 1 226 ? 19.613  -42.926  19.119  1.00 36.49  ? 217 ARG A N   1 
ATOM   1690 C CA  . ARG A 1 226 ? 18.998  -44.238  19.157  1.00 38.42  ? 217 ARG A CA  1 
ATOM   1691 C C   . ARG A 1 226 ? 20.123  -45.260  19.213  1.00 39.62  ? 217 ARG A C   1 
ATOM   1692 O O   . ARG A 1 226 ? 21.288  -44.936  18.942  1.00 40.87  ? 217 ARG A O   1 
ATOM   1693 C CB  . ARG A 1 226 ? 18.112  -44.482  17.930  1.00 37.24  ? 217 ARG A CB  1 
ATOM   1694 C CG  . ARG A 1 226 ? 16.843  -43.643  17.861  1.00 36.92  ? 217 ARG A CG  1 
ATOM   1695 C CD  . ARG A 1 226 ? 17.137  -42.219  17.423  1.00 35.74  ? 217 ARG A CD  1 
ATOM   1696 N NE  . ARG A 1 226 ? 15.904  -41.531  17.058  1.00 37.75  ? 217 ARG A NE  1 
ATOM   1697 C CZ  . ARG A 1 226 ? 15.834  -40.243  16.745  1.00 40.41  ? 217 ARG A CZ  1 
ATOM   1698 N NH1 . ARG A 1 226 ? 16.936  -39.497  16.760  1.00 39.11  ? 217 ARG A NH1 1 
ATOM   1699 N NH2 . ARG A 1 226 ? 14.662  -39.708  16.416  1.00 40.40  ? 217 ARG A NH2 1 
ATOM   1700 N N   . PRO A 1 227 ? 19.788  -46.496  19.577  1.00 37.87  ? 218 PRO A N   1 
ATOM   1701 C CA  . PRO A 1 227 ? 20.790  -47.562  19.588  1.00 40.89  ? 218 PRO A CA  1 
ATOM   1702 C C   . PRO A 1 227 ? 21.417  -47.755  18.202  1.00 43.78  ? 218 PRO A C   1 
ATOM   1703 O O   . PRO A 1 227 ? 20.730  -47.563  17.190  1.00 46.05  ? 218 PRO A O   1 
ATOM   1704 C CB  . PRO A 1 227 ? 19.966  -48.780  19.989  1.00 39.90  ? 218 PRO A CB  1 
ATOM   1705 C CG  . PRO A 1 227 ? 18.858  -48.196  20.832  1.00 38.13  ? 218 PRO A CG  1 
ATOM   1706 C CD  . PRO A 1 227 ? 18.491  -46.952  20.101  1.00 39.13  ? 218 PRO A CD  1 
ATOM   1707 N N   . LYS A 1 228 ? 22.701  -48.104  18.150  1.00 43.23  ? 219 LYS A N   1 
ATOM   1708 C CA  . LYS A 1 228 ? 23.353  -48.312  16.869  1.00 41.36  ? 219 LYS A CA  1 
ATOM   1709 C C   . LYS A 1 228 ? 22.733  -49.473  16.128  1.00 45.59  ? 219 LYS A C   1 
ATOM   1710 O O   . LYS A 1 228 ? 22.645  -50.578  16.657  1.00 45.86  ? 219 LYS A O   1 
ATOM   1711 C CB  . LYS A 1 228 ? 24.838  -48.583  17.037  1.00 42.31  ? 219 LYS A CB  1 
ATOM   1712 C CG  . LYS A 1 228 ? 25.657  -47.326  17.182  1.00 46.91  ? 219 LYS A CG  1 
ATOM   1713 C CD  . LYS A 1 228 ? 27.130  -47.602  16.983  1.00 49.87  ? 219 LYS A CD  1 
ATOM   1714 C CE  . LYS A 1 228 ? 27.932  -46.363  17.291  1.00 53.68  ? 219 LYS A CE  1 
ATOM   1715 N NZ  . LYS A 1 228 ? 29.352  -46.710  17.497  1.00 55.88  ? 219 LYS A NZ  1 
ATOM   1716 N N   . VAL A 1 229 ? 22.316  -49.203  14.892  1.00 46.56  ? 220 VAL A N   1 
ATOM   1717 C CA  . VAL A 1 229 ? 21.847  -50.227  13.962  1.00 45.96  ? 220 VAL A CA  1 
ATOM   1718 C C   . VAL A 1 229 ? 22.547  -50.047  12.633  1.00 44.38  ? 220 VAL A C   1 
ATOM   1719 O O   . VAL A 1 229 ? 22.495  -48.955  12.065  1.00 45.21  ? 220 VAL A O   1 
ATOM   1720 C CB  . VAL A 1 229 ? 20.348  -50.075  13.686  1.00 45.13  ? 220 VAL A CB  1 
ATOM   1721 C CG1 . VAL A 1 229 ? 19.982  -50.767  12.393  1.00 39.35  ? 220 VAL A CG1 1 
ATOM   1722 C CG2 . VAL A 1 229 ? 19.530  -50.602  14.864  1.00 43.40  ? 220 VAL A CG2 1 
ATOM   1723 N N   . ARG A 1 230 ? 23.187  -51.095  12.118  1.00 45.19  ? 221 ARG A N   1 
ATOM   1724 C CA  . ARG A 1 230 ? 23.976  -50.939  10.897  1.00 47.06  ? 221 ARG A CA  1 
ATOM   1725 C C   . ARG A 1 230 ? 24.801  -49.680  11.103  1.00 45.27  ? 221 ARG A C   1 
ATOM   1726 O O   . ARG A 1 230 ? 25.033  -48.897  10.181  1.00 39.21  ? 221 ARG A O   1 
ATOM   1727 C CB  . ARG A 1 230 ? 23.082  -50.833  9.670   1.00 44.09  ? 221 ARG A CB  1 
ATOM   1728 C CG  . ARG A 1 230 ? 22.205  -52.040  9.522   1.00 45.27  ? 221 ARG A CG  1 
ATOM   1729 C CD  . ARG A 1 230 ? 21.502  -52.068  8.196   1.00 49.69  ? 221 ARG A CD  1 
ATOM   1730 N NE  . ARG A 1 230 ? 22.431  -52.121  7.070   1.00 54.20  ? 221 ARG A NE  1 
ATOM   1731 C CZ  . ARG A 1 230 ? 22.729  -53.223  6.386   1.00 55.36  ? 221 ARG A CZ  1 
ATOM   1732 N NH1 . ARG A 1 230 ? 22.181  -54.388  6.705   1.00 57.91  ? 221 ARG A NH1 1 
ATOM   1733 N NH2 . ARG A 1 230 ? 23.577  -53.151  5.373   1.00 58.48  ? 221 ARG A NH2 1 
ATOM   1734 N N   . ASP A 1 231 ? 25.191  -49.487  12.361  1.00 45.80  ? 222 ASP A N   1 
ATOM   1735 C CA  . ASP A 1 231 ? 26.065  -48.396  12.744  1.00 47.58  ? 222 ASP A CA  1 
ATOM   1736 C C   . ASP A 1 231 ? 25.407  -47.015  12.809  1.00 45.28  ? 222 ASP A C   1 
ATOM   1737 O O   . ASP A 1 231 ? 26.073  -46.007  13.056  1.00 44.47  ? 222 ASP A O   1 
ATOM   1738 C CB  . ASP A 1 231 ? 27.350  -48.401  11.921  1.00 46.80  ? 222 ASP A CB  1 
ATOM   1739 C CG  . ASP A 1 231 ? 28.575  -48.374  12.800  1.00 54.57  ? 222 ASP A CG  1 
ATOM   1740 O OD1 . ASP A 1 231 ? 28.807  -49.362  13.553  1.00 56.06  ? 222 ASP A OD1 1 
ATOM   1741 O OD2 . ASP A 1 231 ? 29.287  -47.350  12.754  1.00 57.69  ? 222 ASP A OD2 1 
ATOM   1742 N N   . GLN A 1 232 ? 24.110  -46.965  12.542  1.00 43.66  ? 223 GLN A N   1 
ATOM   1743 C CA  . GLN A 1 232 ? 23.386  -45.714  12.652  1.00 40.03  ? 223 GLN A CA  1 
ATOM   1744 C C   . GLN A 1 232 ? 22.780  -45.516  14.039  1.00 41.13  ? 223 GLN A C   1 
ATOM   1745 O O   . GLN A 1 232 ? 22.101  -46.403  14.567  1.00 42.91  ? 223 GLN A O   1 
ATOM   1746 C CB  . GLN A 1 232 ? 22.314  -45.627  11.563  1.00 41.72  ? 223 GLN A CB  1 
ATOM   1747 C CG  . GLN A 1 232 ? 22.867  -45.833  10.159  1.00 42.28  ? 223 GLN A CG  1 
ATOM   1748 C CD  . GLN A 1 232 ? 24.237  -45.207  10.000  1.00 44.55  ? 223 GLN A CD  1 
ATOM   1749 O OE1 . GLN A 1 232 ? 24.386  -43.980  10.074  1.00 44.50  ? 223 GLN A OE1 1 
ATOM   1750 N NE2 . GLN A 1 232 ? 25.256  -46.048  9.820   1.00 41.89  ? 223 GLN A NE2 1 
ATOM   1751 N N   . GLU A 1 233 ? 23.070  -44.366  14.645  1.00 40.71  ? 224 GLU A N   1 
ATOM   1752 C CA  . GLU A 1 233 ? 22.316  -43.903  15.814  1.00 41.10  ? 224 GLU A CA  1 
ATOM   1753 C C   . GLU A 1 233 ? 21.235  -42.895  15.453  1.00 38.76  ? 224 GLU A C   1 
ATOM   1754 O O   . GLU A 1 233 ? 20.436  -42.520  16.298  1.00 37.67  ? 224 GLU A O   1 
ATOM   1755 C CB  . GLU A 1 233 ? 23.242  -43.271  16.843  1.00 42.71  ? 224 GLU A CB  1 
ATOM   1756 C CG  . GLU A 1 233 ? 24.301  -44.203  17.364  1.00 43.14  ? 224 GLU A CG  1 
ATOM   1757 C CD  . GLU A 1 233 ? 25.233  -43.483  18.270  1.00 47.20  ? 224 GLU A CD  1 
ATOM   1758 O OE1 . GLU A 1 233 ? 25.700  -42.396  17.874  1.00 49.31  ? 224 GLU A OE1 1 
ATOM   1759 O OE2 . GLU A 1 233 ? 25.464  -43.975  19.391  1.00 53.48  ? 224 GLU A OE2 1 
ATOM   1760 N N   . GLY A 1 234 ? 21.204  -42.471  14.194  1.00 41.78  ? 225 GLY A N   1 
ATOM   1761 C CA  . GLY A 1 234 ? 20.136  -41.617  13.701  1.00 41.06  ? 225 GLY A CA  1 
ATOM   1762 C C   . GLY A 1 234 ? 19.042  -42.487  13.102  1.00 41.44  ? 225 GLY A C   1 
ATOM   1763 O O   . GLY A 1 234 ? 19.232  -43.704  12.952  1.00 39.57  ? 225 GLY A O   1 
ATOM   1764 N N   . ARG A 1 235 ? 17.899  -41.891  12.766  1.00 39.79  ? 226 ARG A N   1 
ATOM   1765 C CA  . ARG A 1 235 ? 16.850  -42.650  12.084  1.00 41.97  ? 226 ARG A CA  1 
ATOM   1766 C C   . ARG A 1 235 ? 16.328  -41.966  10.822  1.00 43.55  ? 226 ARG A C   1 
ATOM   1767 O O   . ARG A 1 235 ? 16.554  -40.769  10.592  1.00 45.49  ? 226 ARG A O   1 
ATOM   1768 C CB  . ARG A 1 235 ? 15.676  -42.982  13.022  1.00 40.42  ? 226 ARG A CB  1 
ATOM   1769 C CG  . ARG A 1 235 ? 15.971  -44.005  14.116  1.00 34.92  ? 226 ARG A CG  1 
ATOM   1770 C CD  . ARG A 1 235 ? 16.543  -45.288  13.564  1.00 37.14  ? 226 ARG A CD  1 
ATOM   1771 N NE  . ARG A 1 235 ? 16.664  -46.311  14.592  1.00 34.21  ? 226 ARG A NE  1 
ATOM   1772 C CZ  . ARG A 1 235 ? 17.809  -46.673  15.149  1.00 37.59  ? 226 ARG A CZ  1 
ATOM   1773 N NH1 . ARG A 1 235 ? 18.951  -46.103  14.780  1.00 41.18  ? 226 ARG A NH1 1 
ATOM   1774 N NH2 . ARG A 1 235 ? 17.818  -47.616  16.075  1.00 39.16  ? 226 ARG A NH2 1 
ATOM   1775 N N   . MET A 1 236 ? 15.634  -42.749  10.005  1.00 42.71  ? 227 MET A N   1 
ATOM   1776 C CA  . MET A 1 236 ? 15.051  -42.251  8.776   1.00 41.65  ? 227 MET A CA  1 
ATOM   1777 C C   . MET A 1 236 ? 13.651  -42.818  8.638   1.00 41.34  ? 227 MET A C   1 
ATOM   1778 O O   . MET A 1 236 ? 13.480  -44.030  8.563   1.00 41.32  ? 227 MET A O   1 
ATOM   1779 C CB  . MET A 1 236 ? 15.918  -42.700  7.607   1.00 43.47  ? 227 MET A CB  1 
ATOM   1780 C CG  . MET A 1 236 ? 15.832  -41.837  6.382   1.00 44.95  ? 227 MET A CG  1 
ATOM   1781 S SD  . MET A 1 236 ? 17.276  -42.061  5.310   1.00 40.93  ? 227 MET A SD  1 
ATOM   1782 C CE  . MET A 1 236 ? 18.540  -41.233  6.254   1.00 40.08  ? 227 MET A CE  1 
ATOM   1783 N N   . ASN A 1 237 ? 12.642  -41.956  8.621   1.00 41.47  ? 228 ASN A N   1 
ATOM   1784 C CA  . ASN A 1 237 ? 11.299  -42.435  8.341   1.00 41.41  ? 228 ASN A CA  1 
ATOM   1785 C C   . ASN A 1 237 ? 10.955  -42.321  6.865   1.00 43.08  ? 228 ASN A C   1 
ATOM   1786 O O   . ASN A 1 237 ? 11.283  -41.341  6.206   1.00 42.62  ? 228 ASN A O   1 
ATOM   1787 C CB  . ASN A 1 237 ? 10.255  -41.760  9.217   1.00 44.02  ? 228 ASN A CB  1 
ATOM   1788 C CG  . ASN A 1 237 ? 10.191  -42.386  10.595  1.00 48.26  ? 228 ASN A CG  1 
ATOM   1789 O OD1 . ASN A 1 237 ? 10.717  -43.487  10.791  1.00 47.91  ? 228 ASN A OD1 1 
ATOM   1790 N ND2 . ASN A 1 237 ? 9.555   -41.702  11.557  1.00 46.12  ? 228 ASN A ND2 1 
ATOM   1791 N N   . TYR A 1 238 ? 10.299  -43.342  6.338   1.00 42.86  ? 229 TYR A N   1 
ATOM   1792 C CA  . TYR A 1 238 ? 9.994   -43.357  4.924   1.00 40.99  ? 229 TYR A CA  1 
ATOM   1793 C C   . TYR A 1 238 ? 8.497   -43.168  4.711   1.00 39.74  ? 229 TYR A C   1 
ATOM   1794 O O   . TYR A 1 238 ? 7.692   -43.921  5.247   1.00 42.05  ? 229 TYR A O   1 
ATOM   1795 C CB  . TYR A 1 238 ? 10.497  -44.664  4.321   1.00 38.57  ? 229 TYR A CB  1 
ATOM   1796 C CG  . TYR A 1 238 ? 11.951  -44.978  4.679   1.00 40.73  ? 229 TYR A CG  1 
ATOM   1797 C CD1 . TYR A 1 238 ? 12.998  -44.351  4.022   1.00 42.25  ? 229 TYR A CD1 1 
ATOM   1798 C CD2 . TYR A 1 238 ? 12.274  -45.898  5.668   1.00 40.28  ? 229 TYR A CD2 1 
ATOM   1799 C CE1 . TYR A 1 238 ? 14.328  -44.623  4.341   1.00 42.33  ? 229 TYR A CE1 1 
ATOM   1800 C CE2 . TYR A 1 238 ? 13.601  -46.182  5.986   1.00 39.60  ? 229 TYR A CE2 1 
ATOM   1801 C CZ  . TYR A 1 238 ? 14.623  -45.543  5.317   1.00 40.77  ? 229 TYR A CZ  1 
ATOM   1802 O OH  . TYR A 1 238 ? 15.946  -45.804  5.605   1.00 40.08  ? 229 TYR A OH  1 
ATOM   1803 N N   . TYR A 1 239 ? 8.128   -42.146  3.946   1.00 39.79  ? 230 TYR A N   1 
ATOM   1804 C CA  . TYR A 1 239 ? 6.720   -41.829  3.696   1.00 42.44  ? 230 TYR A CA  1 
ATOM   1805 C C   . TYR A 1 239 ? 6.389   -41.855  2.188   1.00 43.60  ? 230 TYR A C   1 
ATOM   1806 O O   . TYR A 1 239 ? 7.289   -41.800  1.339   1.00 41.78  ? 230 TYR A O   1 
ATOM   1807 C CB  . TYR A 1 239 ? 6.382   -40.442  4.229   1.00 43.50  ? 230 TYR A CB  1 
ATOM   1808 C CG  . TYR A 1 239 ? 6.429   -40.242  5.733   1.00 44.40  ? 230 TYR A CG  1 
ATOM   1809 C CD1 . TYR A 1 239 ? 7.628   -39.999  6.385   1.00 45.33  ? 230 TYR A CD1 1 
ATOM   1810 C CD2 . TYR A 1 239 ? 5.260   -40.222  6.487   1.00 44.02  ? 230 TYR A CD2 1 
ATOM   1811 C CE1 . TYR A 1 239 ? 7.670   -39.778  7.766   1.00 46.80  ? 230 TYR A CE1 1 
ATOM   1812 C CE2 . TYR A 1 239 ? 5.283   -39.997  7.851   1.00 47.22  ? 230 TYR A CE2 1 
ATOM   1813 C CZ  . TYR A 1 239 ? 6.493   -39.769  8.495   1.00 48.32  ? 230 TYR A CZ  1 
ATOM   1814 O OH  . TYR A 1 239 ? 6.518   -39.546  9.864   1.00 50.73  ? 230 TYR A OH  1 
ATOM   1815 N N   . TRP A 1 240 ? 5.099   -41.932  1.856   1.00 41.44  ? 231 TRP A N   1 
ATOM   1816 C CA  . TRP A 1 240 ? 4.660   -41.999  0.464   1.00 38.83  ? 231 TRP A CA  1 
ATOM   1817 C C   . TRP A 1 240 ? 3.218   -41.536  0.244   1.00 43.18  ? 231 TRP A C   1 
ATOM   1818 O O   . TRP A 1 240 ? 2.419   -41.446  1.178   1.00 43.06  ? 231 TRP A O   1 
ATOM   1819 C CB  . TRP A 1 240 ? 4.797   -43.429  -0.053  1.00 41.46  ? 231 TRP A CB  1 
ATOM   1820 C CG  . TRP A 1 240 ? 3.831   -44.388  0.595   1.00 42.38  ? 231 TRP A CG  1 
ATOM   1821 C CD1 . TRP A 1 240 ? 4.050   -45.124  1.719   1.00 43.22  ? 231 TRP A CD1 1 
ATOM   1822 C CD2 . TRP A 1 240 ? 2.495   -44.700  0.167   1.00 41.03  ? 231 TRP A CD2 1 
ATOM   1823 N NE1 . TRP A 1 240 ? 2.944   -45.878  2.016   1.00 46.71  ? 231 TRP A NE1 1 
ATOM   1824 C CE2 . TRP A 1 240 ? 1.974   -45.637  1.081   1.00 44.35  ? 231 TRP A CE2 1 
ATOM   1825 C CE3 . TRP A 1 240 ? 1.694   -44.284  -0.896  1.00 44.32  ? 231 TRP A CE3 1 
ATOM   1826 C CZ2 . TRP A 1 240 ? 0.684   -46.161  0.971   1.00 45.07  ? 231 TRP A CZ2 1 
ATOM   1827 C CZ3 . TRP A 1 240 ? 0.408   -44.814  -1.009  1.00 47.59  ? 231 TRP A CZ3 1 
ATOM   1828 C CH2 . TRP A 1 240 ? -0.080  -45.740  -0.077  1.00 45.94  ? 231 TRP A CH2 1 
ATOM   1829 N N   . THR A 1 241 ? 2.876   -41.268  -1.009  1.00 44.15  ? 232 THR A N   1 
ATOM   1830 C CA  . THR A 1 241 ? 1.496   -40.964  -1.342  1.00 45.00  ? 232 THR A CA  1 
ATOM   1831 C C   . THR A 1 241 ? 1.238   -41.234  -2.814  1.00 47.32  ? 232 THR A C   1 
ATOM   1832 O O   . THR A 1 241 ? 2.176   -41.383  -3.594  1.00 46.48  ? 232 THR A O   1 
ATOM   1833 C CB  . THR A 1 241 ? 1.133   -39.498  -0.968  1.00 46.76  ? 232 THR A CB  1 
ATOM   1834 O OG1 . THR A 1 241 ? -0.264  -39.271  -1.186  1.00 51.81  ? 232 THR A OG1 1 
ATOM   1835 C CG2 . THR A 1 241 ? 1.956   -38.502  -1.771  1.00 44.16  ? 232 THR A CG2 1 
ATOM   1836 N N   . LEU A 1 242 ? -0.037  -41.324  -3.181  1.00 49.10  ? 233 LEU A N   1 
ATOM   1837 C CA  . LEU A 1 242 ? -0.431  -41.392  -4.579  1.00 46.11  ? 233 LEU A CA  1 
ATOM   1838 C C   . LEU A 1 242 ? -0.913  -40.044  -5.049  1.00 50.55  ? 233 LEU A C   1 
ATOM   1839 O O   . LEU A 1 242 ? -1.916  -39.524  -4.560  1.00 56.23  ? 233 LEU A O   1 
ATOM   1840 C CB  . LEU A 1 242 ? -1.553  -42.389  -4.763  1.00 46.29  ? 233 LEU A CB  1 
ATOM   1841 C CG  . LEU A 1 242 ? -1.035  -43.811  -4.669  1.00 47.39  ? 233 LEU A CG  1 
ATOM   1842 C CD1 . LEU A 1 242 ? -2.165  -44.779  -4.902  1.00 51.20  ? 233 LEU A CD1 1 
ATOM   1843 C CD2 . LEU A 1 242 ? 0.080   -44.019  -5.680  1.00 49.48  ? 233 LEU A CD2 1 
ATOM   1844 N N   . VAL A 1 243 ? -0.196  -39.462  -5.996  1.00 52.63  ? 234 VAL A N   1 
ATOM   1845 C CA  . VAL A 1 243 ? -0.648  -38.214  -6.577  1.00 53.72  ? 234 VAL A CA  1 
ATOM   1846 C C   . VAL A 1 243 ? -1.582  -38.481  -7.754  1.00 56.37  ? 234 VAL A C   1 
ATOM   1847 O O   . VAL A 1 243 ? -1.229  -39.200  -8.695  1.00 54.32  ? 234 VAL A O   1 
ATOM   1848 C CB  . VAL A 1 243 ? 0.499   -37.358  -7.073  1.00 53.00  ? 234 VAL A CB  1 
ATOM   1849 C CG1 . VAL A 1 243 ? -0.066  -36.092  -7.676  1.00 57.36  ? 234 VAL A CG1 1 
ATOM   1850 C CG2 . VAL A 1 243 ? 1.452   -37.031  -5.945  1.00 50.98  ? 234 VAL A CG2 1 
ATOM   1851 N N   . GLU A 1 244 ? -2.778  -37.903  -7.684  1.00 58.70  ? 235 GLU A N   1 
ATOM   1852 C CA  . GLU A 1 244 ? -3.798  -38.069  -8.717  1.00 58.94  ? 235 GLU A CA  1 
ATOM   1853 C C   . GLU A 1 244 ? -3.313  -37.593  -10.080 1.00 57.07  ? 235 GLU A C   1 
ATOM   1854 O O   . GLU A 1 244 ? -2.401  -36.763  -10.170 1.00 57.09  ? 235 GLU A O   1 
ATOM   1855 C CB  . GLU A 1 244 ? -5.047  -37.274  -8.342  1.00 58.89  ? 235 GLU A CB  1 
ATOM   1856 C CG  . GLU A 1 244 ? -5.806  -37.826  -7.164  1.00 63.71  ? 235 GLU A CG  1 
ATOM   1857 C CD  . GLU A 1 244 ? -6.709  -36.785  -6.548  1.00 70.73  ? 235 GLU A CD  1 
ATOM   1858 O OE1 . GLU A 1 244 ? -7.345  -37.090  -5.510  1.00 67.96  ? 235 GLU A OE1 1 
ATOM   1859 O OE2 . GLU A 1 244 ? -6.769  -35.658  -7.106  1.00 71.31  ? 235 GLU A OE2 1 
ATOM   1860 N N   . PRO A 1 245 ? -3.934  -38.106  -11.150 1.00 55.89  ? 236 PRO A N   1 
ATOM   1861 C CA  . PRO A 1 245 ? -3.497  -37.672  -12.475 1.00 54.40  ? 236 PRO A CA  1 
ATOM   1862 C C   . PRO A 1 245 ? -3.426  -36.150  -12.600 1.00 55.91  ? 236 PRO A C   1 
ATOM   1863 O O   . PRO A 1 245 ? -2.391  -35.639  -13.005 1.00 57.89  ? 236 PRO A O   1 
ATOM   1864 C CB  . PRO A 1 245 ? -4.570  -38.256  -13.389 1.00 53.42  ? 236 PRO A CB  1 
ATOM   1865 C CG  . PRO A 1 245 ? -4.944  -39.540  -12.711 1.00 55.68  ? 236 PRO A CG  1 
ATOM   1866 C CD  . PRO A 1 245 ? -4.827  -39.278  -11.216 1.00 56.29  ? 236 PRO A CD  1 
ATOM   1867 N N   . GLY A 1 246 ? -4.452  -35.417  -12.203 1.00 54.84  ? 237 GLY A N   1 
ATOM   1868 C CA  . GLY A 1 246 ? -4.403  -33.987  -12.445 1.00 56.40  ? 237 GLY A CA  1 
ATOM   1869 C C   . GLY A 1 246 ? -3.479  -33.262  -11.491 1.00 56.96  ? 237 GLY A C   1 
ATOM   1870 O O   . GLY A 1 246 ? -2.940  -32.194  -11.807 1.00 55.84  ? 237 GLY A O   1 
ATOM   1871 N N   . ASP A 1 247 ? -3.273  -33.893  -10.337 1.00 55.88  ? 238 ASP A N   1 
ATOM   1872 C CA  . ASP A 1 247 ? -2.835  -33.237  -9.095  1.00 58.42  ? 238 ASP A CA  1 
ATOM   1873 C C   . ASP A 1 247 ? -1.383  -32.719  -9.072  1.00 58.78  ? 238 ASP A C   1 
ATOM   1874 O O   . ASP A 1 247 ? -0.534  -33.151  -9.860  1.00 58.98  ? 238 ASP A O   1 
ATOM   1875 C CB  . ASP A 1 247 ? -3.092  -34.195  -7.921  1.00 58.33  ? 238 ASP A CB  1 
ATOM   1876 C CG  . ASP A 1 247 ? -3.193  -33.489  -6.587  1.00 59.39  ? 238 ASP A CG  1 
ATOM   1877 O OD1 . ASP A 1 247 ? -3.428  -32.260  -6.567  1.00 59.47  ? 238 ASP A OD1 1 
ATOM   1878 O OD2 . ASP A 1 247 ? -3.048  -34.186  -5.553  1.00 56.94  ? 238 ASP A OD2 1 
ATOM   1879 N N   . LYS A 1 248 ? -1.114  -31.787  -8.159  1.00 56.11  ? 239 LYS A N   1 
ATOM   1880 C CA  . LYS A 1 248 ? 0.222   -31.221  -7.973  1.00 53.28  ? 239 LYS A CA  1 
ATOM   1881 C C   . LYS A 1 248 ? 0.737   -31.490  -6.559  1.00 59.85  ? 239 LYS A C   1 
ATOM   1882 O O   . LYS A 1 248 ? -0.042  -31.461  -5.596  1.00 59.22  ? 239 LYS A O   1 
ATOM   1883 C CB  . LYS A 1 248 ? 0.187   -29.713  -8.203  1.00 51.39  ? 239 LYS A CB  1 
ATOM   1884 C CG  . LYS A 1 248 ? 1.482   -28.990  -7.860  1.00 51.66  ? 239 LYS A CG  1 
ATOM   1885 C CD  . LYS A 1 248 ? 1.276   -27.482  -7.828  1.00 52.71  ? 239 LYS A CD  1 
ATOM   1886 C CE  . LYS A 1 248 ? 2.593   -26.706  -7.922  1.00 54.89  ? 239 LYS A CE  1 
ATOM   1887 N NZ  . LYS A 1 248 ? 2.390   -25.215  -7.981  1.00 52.79  ? 239 LYS A NZ  1 
ATOM   1888 N N   . ILE A 1 249 ? 2.046   -31.730  -6.430  1.00 58.99  ? 240 ILE A N   1 
ATOM   1889 C CA  . ILE A 1 249 ? 2.660   -31.984  -5.122  1.00 52.77  ? 240 ILE A CA  1 
ATOM   1890 C C   . ILE A 1 249 ? 3.914   -31.167  -4.872  1.00 51.32  ? 240 ILE A C   1 
ATOM   1891 O O   . ILE A 1 249 ? 4.778   -31.053  -5.736  1.00 55.35  ? 240 ILE A O   1 
ATOM   1892 C CB  . ILE A 1 249 ? 3.028   -33.453  -4.931  1.00 52.53  ? 240 ILE A CB  1 
ATOM   1893 C CG1 . ILE A 1 249 ? 3.650   -33.652  -3.543  1.00 51.92  ? 240 ILE A CG1 1 
ATOM   1894 C CG2 . ILE A 1 249 ? 3.988   -33.903  -6.006  1.00 49.66  ? 240 ILE A CG2 1 
ATOM   1895 C CD1 . ILE A 1 249 ? 3.644   -35.093  -3.070  1.00 49.92  ? 240 ILE A CD1 1 
ATOM   1896 N N   . THR A 1 250 ? 4.027   -30.625  -3.669  1.00 50.92  ? 241 THR A N   1 
ATOM   1897 C CA  . THR A 1 250 ? 5.102   -29.701  -3.376  1.00 51.50  ? 241 THR A CA  1 
ATOM   1898 C C   . THR A 1 250 ? 5.937   -30.211  -2.212  1.00 50.59  ? 241 THR A C   1 
ATOM   1899 O O   . THR A 1 250 ? 5.481   -31.056  -1.441  1.00 51.15  ? 241 THR A O   1 
ATOM   1900 C CB  . THR A 1 250 ? 4.545   -28.298  -3.058  1.00 55.50  ? 241 THR A CB  1 
ATOM   1901 O OG1 . THR A 1 250 ? 3.704   -27.858  -4.136  1.00 56.31  ? 241 THR A OG1 1 
ATOM   1902 C CG2 . THR A 1 250 ? 5.684   -27.292  -2.868  1.00 55.52  ? 241 THR A CG2 1 
ATOM   1903 N N   . PHE A 1 251 ? 7.167   -29.707  -2.107  1.00 49.25  ? 242 PHE A N   1 
ATOM   1904 C CA  . PHE A 1 251 ? 8.093   -30.120  -1.057  1.00 48.77  ? 242 PHE A CA  1 
ATOM   1905 C C   . PHE A 1 251 ? 8.894   -28.959  -0.485  1.00 48.89  ? 242 PHE A C   1 
ATOM   1906 O O   . PHE A 1 251 ? 9.640   -28.310  -1.212  1.00 49.67  ? 242 PHE A O   1 
ATOM   1907 C CB  . PHE A 1 251 ? 9.084   -31.149  -1.602  1.00 44.93  ? 242 PHE A CB  1 
ATOM   1908 C CG  . PHE A 1 251 ? 8.514   -32.534  -1.750  1.00 48.38  ? 242 PHE A CG  1 
ATOM   1909 C CD1 . PHE A 1 251 ? 7.721   -32.857  -2.848  1.00 46.92  ? 242 PHE A CD1 1 
ATOM   1910 C CD2 . PHE A 1 251 ? 8.791   -33.525  -0.807  1.00 44.86  ? 242 PHE A CD2 1 
ATOM   1911 C CE1 . PHE A 1 251 ? 7.197   -34.130  -2.999  1.00 44.65  ? 242 PHE A CE1 1 
ATOM   1912 C CE2 . PHE A 1 251 ? 8.268   -34.804  -0.950  1.00 43.02  ? 242 PHE A CE2 1 
ATOM   1913 C CZ  . PHE A 1 251 ? 7.471   -35.105  -2.056  1.00 45.15  ? 242 PHE A CZ  1 
ATOM   1914 N N   . GLU A 1 252 ? 8.797   -28.733  0.819   1.00 45.55  ? 243 GLU A N   1 
ATOM   1915 C CA  . GLU A 1 252 ? 9.607   -27.705  1.450   1.00 48.22  ? 243 GLU A CA  1 
ATOM   1916 C C   . GLU A 1 252 ? 10.514  -28.274  2.535   1.00 47.75  ? 243 GLU A C   1 
ATOM   1917 O O   . GLU A 1 252 ? 10.087  -29.144  3.290   1.00 49.98  ? 243 GLU A O   1 
ATOM   1918 C CB  . GLU A 1 252 ? 8.709   -26.655  2.068   1.00 53.56  ? 243 GLU A CB  1 
ATOM   1919 C CG  . GLU A 1 252 ? 8.553   -25.422  1.237   1.00 56.44  ? 243 GLU A CG  1 
ATOM   1920 C CD  . GLU A 1 252 ? 7.381   -24.606  1.701   1.00 62.50  ? 243 GLU A CD  1 
ATOM   1921 O OE1 . GLU A 1 252 ? 7.502   -23.952  2.767   1.00 61.18  ? 243 GLU A OE1 1 
ATOM   1922 O OE2 . GLU A 1 252 ? 6.339   -24.643  1.004   1.00 61.75  ? 243 GLU A OE2 1 
ATOM   1923 N N   . ALA A 1 253 ? 11.765  -27.817  2.593   1.00 42.45  ? 244 ALA A N   1 
ATOM   1924 C CA  . ALA A 1 253 ? 12.636  -28.155  3.715   1.00 45.04  ? 244 ALA A CA  1 
ATOM   1925 C C   . ALA A 1 253 ? 13.764  -27.152  3.993   1.00 44.97  ? 244 ALA A C   1 
ATOM   1926 O O   . ALA A 1 253 ? 14.404  -26.654  3.070   1.00 44.97  ? 244 ALA A O   1 
ATOM   1927 C CB  . ALA A 1 253 ? 13.208  -29.551  3.534   1.00 47.70  ? 244 ALA A CB  1 
ATOM   1928 N N   . THR A 1 254 ? 14.012  -26.895  5.276   1.00 43.52  ? 245 THR A N   1 
ATOM   1929 C CA  . THR A 1 254 ? 15.197  -26.186  5.738   1.00 43.77  ? 245 THR A CA  1 
ATOM   1930 C C   . THR A 1 254 ? 16.224  -27.187  6.221   1.00 46.11  ? 245 THR A C   1 
ATOM   1931 O O   . THR A 1 254 ? 17.260  -26.823  6.783   1.00 47.93  ? 245 THR A O   1 
ATOM   1932 C CB  . THR A 1 254 ? 14.873  -25.180  6.831   1.00 49.73  ? 245 THR A CB  1 
ATOM   1933 O OG1 . THR A 1 254 ? 13.885  -25.737  7.698   1.00 53.09  ? 245 THR A OG1 1 
ATOM   1934 C CG2 . THR A 1 254 ? 14.304  -23.910  6.226   1.00 50.17  ? 245 THR A CG2 1 
ATOM   1935 N N   . GLY A 1 255 ? 15.905  -28.461  6.025   1.00 47.14  ? 246 GLY A N   1 
ATOM   1936 C CA  . GLY A 1 255 ? 16.845  -29.537  6.267   1.00 44.57  ? 246 GLY A CA  1 
ATOM   1937 C C   . GLY A 1 255 ? 16.151  -30.882  6.307   1.00 46.17  ? 246 GLY A C   1 
ATOM   1938 O O   . GLY A 1 255 ? 14.940  -30.977  6.054   1.00 45.06  ? 246 GLY A O   1 
ATOM   1939 N N   . ASN A 1 256 ? 16.939  -31.927  6.571   1.00 46.75  ? 247 ASN A N   1 
ATOM   1940 C CA  . ASN A 1 256 ? 16.438  -33.244  6.988   1.00 44.98  ? 247 ASN A CA  1 
ATOM   1941 C C   . ASN A 1 256 ? 15.590  -33.997  5.974   1.00 43.02  ? 247 ASN A C   1 
ATOM   1942 O O   . ASN A 1 256 ? 15.142  -35.112  6.235   1.00 45.95  ? 247 ASN A O   1 
ATOM   1943 C CB  . ASN A 1 256 ? 15.696  -33.156  8.319   1.00 46.66  ? 247 ASN A CB  1 
ATOM   1944 C CG  . ASN A 1 256 ? 16.431  -32.305  9.339   1.00 49.41  ? 247 ASN A CG  1 
ATOM   1945 O OD1 . ASN A 1 256 ? 16.390  -31.066  9.273   1.00 48.19  ? 247 ASN A OD1 1 
ATOM   1946 N ND2 . ASN A 1 256 ? 17.094  -32.962  10.302  1.00 48.75  ? 247 ASN A ND2 1 
ATOM   1947 N N   . LEU A 1 257 ? 15.333  -33.381  4.833   1.00 45.82  ? 248 LEU A N   1 
ATOM   1948 C CA  . LEU A 1 257 ? 14.525  -34.040  3.808   1.00 47.64  ? 248 LEU A CA  1 
ATOM   1949 C C   . LEU A 1 257 ? 15.359  -34.888  2.849   1.00 42.90  ? 248 LEU A C   1 
ATOM   1950 O O   . LEU A 1 257 ? 16.379  -34.441  2.321   1.00 41.25  ? 248 LEU A O   1 
ATOM   1951 C CB  . LEU A 1 257 ? 13.693  -33.039  3.007   1.00 45.12  ? 248 LEU A CB  1 
ATOM   1952 C CG  . LEU A 1 257 ? 12.931  -33.810  1.940   1.00 45.15  ? 248 LEU A CG  1 
ATOM   1953 C CD1 . LEU A 1 257 ? 11.945  -34.747  2.621   1.00 43.87  ? 248 LEU A CD1 1 
ATOM   1954 C CD2 . LEU A 1 257 ? 12.241  -32.867  0.965   1.00 43.06  ? 248 LEU A CD2 1 
ATOM   1955 N N   . VAL A 1 258 ? 14.894  -36.112  2.630   1.00 42.52  ? 249 VAL A N   1 
ATOM   1956 C CA  . VAL A 1 258 ? 15.513  -37.023  1.690   1.00 41.94  ? 249 VAL A CA  1 
ATOM   1957 C C   . VAL A 1 258 ? 14.601  -37.042  0.487   1.00 44.94  ? 249 VAL A C   1 
ATOM   1958 O O   . VAL A 1 258 ? 13.497  -37.594  0.534   1.00 45.76  ? 249 VAL A O   1 
ATOM   1959 C CB  . VAL A 1 258 ? 15.569  -38.428  2.268   1.00 41.39  ? 249 VAL A CB  1 
ATOM   1960 C CG1 . VAL A 1 258 ? 16.470  -39.330  1.418   1.00 43.88  ? 249 VAL A CG1 1 
ATOM   1961 C CG2 . VAL A 1 258 ? 16.056  -38.370  3.700   1.00 42.79  ? 249 VAL A CG2 1 
ATOM   1962 N N   . VAL A 1 259 ? 15.071  -36.442  -0.592  1.00 41.82  ? 250 VAL A N   1 
ATOM   1963 C CA  . VAL A 1 259 ? 14.196  -36.046  -1.674  1.00 43.48  ? 250 VAL A CA  1 
ATOM   1964 C C   . VAL A 1 259 ? 13.922  -37.205  -2.618  1.00 46.19  ? 250 VAL A C   1 
ATOM   1965 O O   . VAL A 1 259 ? 14.755  -38.108  -2.769  1.00 47.61  ? 250 VAL A O   1 
ATOM   1966 C CB  . VAL A 1 259 ? 14.841  -34.907  -2.470  1.00 44.25  ? 250 VAL A CB  1 
ATOM   1967 C CG1 . VAL A 1 259 ? 15.045  -33.686  -1.588  1.00 43.52  ? 250 VAL A CG1 1 
ATOM   1968 C CG2 . VAL A 1 259 ? 16.177  -35.369  -3.015  1.00 45.28  ? 250 VAL A CG2 1 
ATOM   1969 N N   . PRO A 1 260 ? 12.742  -37.193  -3.248  1.00 43.04  ? 251 PRO A N   1 
ATOM   1970 C CA  . PRO A 1 260 ? 12.488  -38.129  -4.338  1.00 44.52  ? 251 PRO A CA  1 
ATOM   1971 C C   . PRO A 1 260 ? 13.406  -37.841  -5.507  1.00 48.65  ? 251 PRO A C   1 
ATOM   1972 O O   . PRO A 1 260 ? 13.780  -36.691  -5.765  1.00 49.35  ? 251 PRO A O   1 
ATOM   1973 C CB  . PRO A 1 260 ? 11.034  -37.836  -4.722  1.00 44.32  ? 251 PRO A CB  1 
ATOM   1974 C CG  . PRO A 1 260 ? 10.426  -37.315  -3.475  1.00 44.20  ? 251 PRO A CG  1 
ATOM   1975 C CD  . PRO A 1 260 ? 11.516  -36.496  -2.832  1.00 45.18  ? 251 PRO A CD  1 
ATOM   1976 N N   . ARG A 1 261 ? 13.796  -38.912  -6.186  1.00 51.99  ? 252 ARG A N   1 
ATOM   1977 C CA  . ARG A 1 261 ? 14.462  -38.827  -7.473  1.00 53.09  ? 252 ARG A CA  1 
ATOM   1978 C C   . ARG A 1 261 ? 13.586  -39.580  -8.467  1.00 54.13  ? 252 ARG A C   1 
ATOM   1979 O O   . ARG A 1 261 ? 13.072  -38.989  -9.417  1.00 58.89  ? 252 ARG A O   1 
ATOM   1980 C CB  . ARG A 1 261 ? 15.869  -39.424  -7.433  1.00 49.31  ? 252 ARG A CB  1 
ATOM   1981 C CG  . ARG A 1 261 ? 16.503  -39.501  -8.803  1.00 56.25  ? 252 ARG A CG  1 
ATOM   1982 C CD  . ARG A 1 261 ? 17.975  -39.890  -8.760  1.00 56.47  ? 252 ARG A CD  1 
ATOM   1983 N NE  . ARG A 1 261 ? 18.608  -39.632  -10.052 1.00 57.10  ? 252 ARG A NE  1 
ATOM   1984 C CZ  . ARG A 1 261 ? 19.889  -39.862  -10.322 1.00 59.14  ? 252 ARG A CZ  1 
ATOM   1985 N NH1 . ARG A 1 261 ? 20.692  -40.366  -9.397  1.00 55.85  ? 252 ARG A NH1 1 
ATOM   1986 N NH2 . ARG A 1 261 ? 20.374  -39.580  -11.525 1.00 62.94  ? 252 ARG A NH2 1 
ATOM   1987 N N   . TYR A 1 262 ? 13.420  -40.884  -8.250  1.00 50.77  ? 253 TYR A N   1 
ATOM   1988 C CA  . TYR A 1 262 ? 12.566  -41.701  -9.110  1.00 53.91  ? 253 TYR A CA  1 
ATOM   1989 C C   . TYR A 1 262 ? 11.190  -41.905  -8.474  1.00 55.42  ? 253 TYR A C   1 
ATOM   1990 O O   . TYR A 1 262 ? 11.094  -42.154  -7.274  1.00 56.15  ? 253 TYR A O   1 
ATOM   1991 C CB  . TYR A 1 262 ? 13.219  -43.063  -9.417  1.00 52.41  ? 253 TYR A CB  1 
ATOM   1992 C CG  . TYR A 1 262 ? 14.439  -42.969  -10.299 1.00 55.36  ? 253 TYR A CG  1 
ATOM   1993 C CD1 . TYR A 1 262 ? 15.701  -42.805  -9.747  1.00 57.10  ? 253 TYR A CD1 1 
ATOM   1994 C CD2 . TYR A 1 262 ? 14.333  -43.022  -11.687 1.00 58.83  ? 253 TYR A CD2 1 
ATOM   1995 C CE1 . TYR A 1 262 ? 16.835  -42.704  -10.546 1.00 58.67  ? 253 TYR A CE1 1 
ATOM   1996 C CE2 . TYR A 1 262 ? 15.460  -42.923  -12.495 1.00 59.99  ? 253 TYR A CE2 1 
ATOM   1997 C CZ  . TYR A 1 262 ? 16.711  -42.763  -11.914 1.00 62.32  ? 253 TYR A CZ  1 
ATOM   1998 O OH  . TYR A 1 262 ? 17.847  -42.658  -12.692 1.00 61.17  ? 253 TYR A OH  1 
ATOM   1999 N N   . ALA A 1 263 ? 10.132  -41.794  -9.278  1.00 56.06  ? 254 ALA A N   1 
ATOM   2000 C CA  . ALA A 1 263 ? 8.765   -42.075  -8.828  1.00 52.62  ? 254 ALA A CA  1 
ATOM   2001 C C   . ALA A 1 263 ? 8.122   -43.081  -9.780  1.00 54.74  ? 254 ALA A C   1 
ATOM   2002 O O   . ALA A 1 263 ? 8.760   -43.516  -10.737 1.00 56.75  ? 254 ALA A O   1 
ATOM   2003 C CB  . ALA A 1 263 ? 7.947   -40.788  -8.759  1.00 50.03  ? 254 ALA A CB  1 
ATOM   2004 N N   . PHE A 1 264 ? 6.872   -43.458  -9.535  1.00 50.89  ? 255 PHE A N   1 
ATOM   2005 C CA  . PHE A 1 264 ? 6.240   -44.453  -10.396 1.00 52.16  ? 255 PHE A CA  1 
ATOM   2006 C C   . PHE A 1 264 ? 4.822   -44.088  -10.838 1.00 55.54  ? 255 PHE A C   1 
ATOM   2007 O O   . PHE A 1 264 ? 3.919   -43.971  -10.010 1.00 57.71  ? 255 PHE A O   1 
ATOM   2008 C CB  . PHE A 1 264 ? 6.245   -45.827  -9.712  1.00 56.22  ? 255 PHE A CB  1 
ATOM   2009 C CG  . PHE A 1 264 ? 7.604   -46.257  -9.216  1.00 56.81  ? 255 PHE A CG  1 
ATOM   2010 C CD1 . PHE A 1 264 ? 8.481   -46.945  -10.040 1.00 58.14  ? 255 PHE A CD1 1 
ATOM   2011 C CD2 . PHE A 1 264 ? 8.003   -45.975  -7.922  1.00 55.59  ? 255 PHE A CD2 1 
ATOM   2012 C CE1 . PHE A 1 264 ? 9.733   -47.343  -9.583  1.00 56.58  ? 255 PHE A CE1 1 
ATOM   2013 C CE2 . PHE A 1 264 ? 9.248   -46.364  -7.462  1.00 55.08  ? 255 PHE A CE2 1 
ATOM   2014 C CZ  . PHE A 1 264 ? 10.114  -47.054  -8.292  1.00 55.99  ? 255 PHE A CZ  1 
ATOM   2015 N N   . ALA A 1 265 ? 4.640   -43.909  -12.150 1.00 58.19  ? 256 ALA A N   1 
ATOM   2016 C CA  . ALA A 1 265 ? 3.310   -43.838  -12.760 1.00 57.75  ? 256 ALA A CA  1 
ATOM   2017 C C   . ALA A 1 265 ? 2.730   -45.243  -12.771 1.00 56.40  ? 256 ALA A C   1 
ATOM   2018 O O   . ALA A 1 265 ? 3.421   -46.201  -13.099 1.00 59.03  ? 256 ALA A O   1 
ATOM   2019 C CB  . ALA A 1 265 ? 3.389   -43.271  -14.181 1.00 60.32  ? 256 ALA A CB  1 
ATOM   2020 N N   . MET A 1 266 ? 1.478   -45.384  -12.369 1.00 56.05  ? 257 MET A N   1 
ATOM   2021 C CA  . MET A 1 266 ? 0.911   -46.714  -12.291 1.00 59.56  ? 257 MET A CA  1 
ATOM   2022 C C   . MET A 1 266 ? -0.605  -46.723  -12.275 1.00 63.41  ? 257 MET A C   1 
ATOM   2023 O O   . MET A 1 266 ? -1.256  -45.745  -11.895 1.00 64.36  ? 257 MET A O   1 
ATOM   2024 C CB  . MET A 1 266 ? 1.428   -47.423  -11.042 1.00 62.75  ? 257 MET A CB  1 
ATOM   2025 C CG  . MET A 1 266 ? 1.236   -46.605  -9.776  1.00 62.08  ? 257 MET A CG  1 
ATOM   2026 S SD  . MET A 1 266 ? 1.301   -47.562  -8.252  1.00 65.57  ? 257 MET A SD  1 
ATOM   2027 C CE  . MET A 1 266 ? -0.116  -48.637  -8.491  1.00 68.98  ? 257 MET A CE  1 
ATOM   2028 N N   . GLU A 1 267 ? -1.157  -47.865  -12.656 1.00 63.72  ? 258 GLU A N   1 
ATOM   2029 C CA  . GLU A 1 267 ? -2.578  -48.099  -12.551 1.00 68.60  ? 258 GLU A CA  1 
ATOM   2030 C C   . GLU A 1 267 ? -2.744  -49.467  -11.907 1.00 70.52  ? 258 GLU A C   1 
ATOM   2031 O O   . GLU A 1 267 ? -2.135  -50.446  -12.354 1.00 67.62  ? 258 GLU A O   1 
ATOM   2032 C CB  . GLU A 1 267 ? -3.235  -48.058  -13.932 1.00 72.66  ? 258 GLU A CB  1 
ATOM   2033 C CG  . GLU A 1 267 ? -4.737  -47.775  -13.890 1.00 77.74  ? 258 GLU A CG  1 
ATOM   2034 C CD  . GLU A 1 267 ? -5.430  -48.021  -15.220 1.00 82.72  ? 258 GLU A CD  1 
ATOM   2035 O OE1 . GLU A 1 267 ? -4.742  -48.407  -16.195 1.00 86.64  ? 258 GLU A OE1 1 
ATOM   2036 O OE2 . GLU A 1 267 ? -6.668  -47.836  -15.283 1.00 84.37  ? 258 GLU A OE2 1 
ATOM   2037 N N   . ARG A 1 268 ? -3.560  -49.527  -10.854 1.00 71.29  ? 259 ARG A N   1 
ATOM   2038 C CA  . ARG A 1 268 ? -3.711  -50.740  -10.046 1.00 69.79  ? 259 ARG A CA  1 
ATOM   2039 C C   . ARG A 1 268 ? -4.529  -51.836  -10.699 1.00 70.35  ? 259 ARG A C   1 
ATOM   2040 O O   . ARG A 1 268 ? -4.976  -51.719  -11.835 1.00 73.09  ? 259 ARG A O   1 
ATOM   2041 C CB  . ARG A 1 268 ? -4.401  -50.423  -8.723  1.00 69.44  ? 259 ARG A CB  1 
ATOM   2042 C CG  . ARG A 1 268 ? -3.578  -49.690  -7.703  1.00 71.11  ? 259 ARG A CG  1 
ATOM   2043 C CD  . ARG A 1 268 ? -4.333  -49.681  -6.380  1.00 73.31  ? 259 ARG A CD  1 
ATOM   2044 N NE  . ARG A 1 268 ? -4.428  -51.019  -5.785  1.00 74.40  ? 259 ARG A NE  1 
ATOM   2045 C CZ  . ARG A 1 268 ? -5.536  -51.541  -5.257  1.00 78.29  ? 259 ARG A CZ  1 
ATOM   2046 N NH1 . ARG A 1 268 ? -6.671  -50.843  -5.254  1.00 81.99  ? 259 ARG A NH1 1 
ATOM   2047 N NH2 . ARG A 1 268 ? -5.513  -52.767  -4.735  1.00 74.12  ? 259 ARG A NH2 1 
ATOM   2048 N N   . ASN A 1 269 ? -4.699  -52.911  -9.940  1.00 69.88  ? 260 ASN A N   1 
ATOM   2049 C CA  . ASN A 1 269 ? -5.713  -53.917  -10.182 1.00 70.88  ? 260 ASN A CA  1 
ATOM   2050 C C   . ASN A 1 269 ? -6.320  -54.211  -8.818  1.00 75.87  ? 260 ASN A C   1 
ATOM   2051 O O   . ASN A 1 269 ? -5.661  -53.999  -7.797  1.00 76.88  ? 260 ASN A O   1 
ATOM   2052 C CB  . ASN A 1 269 ? -5.091  -55.188  -10.756 1.00 70.72  ? 260 ASN A CB  1 
ATOM   2053 C CG  . ASN A 1 269 ? -4.478  -54.974  -12.121 1.00 72.40  ? 260 ASN A CG  1 
ATOM   2054 O OD1 . ASN A 1 269 ? -5.052  -54.298  -12.977 1.00 75.32  ? 260 ASN A OD1 1 
ATOM   2055 N ND2 . ASN A 1 269 ? -3.298  -55.546  -12.334 1.00 72.41  ? 260 ASN A ND2 1 
ATOM   2056 N N   . ALA A 1 270 ? -7.562  -54.690  -8.778  1.00 77.64  ? 261 ALA A N   1 
ATOM   2057 C CA  . ALA A 1 270 ? -8.168  -55.054  -7.499  1.00 75.66  ? 261 ALA A CA  1 
ATOM   2058 C C   . ALA A 1 270 ? -7.237  -56.043  -6.816  1.00 76.74  ? 261 ALA A C   1 
ATOM   2059 O O   . ALA A 1 270 ? -6.921  -57.105  -7.361  1.00 79.62  ? 261 ALA A O   1 
ATOM   2060 C CB  . ALA A 1 270 ? -9.544  -55.667  -7.700  1.00 79.54  ? 261 ALA A CB  1 
ATOM   2061 N N   . GLY A 1 271 ? -6.832  -55.709  -5.601  1.00 77.00  ? 262 GLY A N   1 
ATOM   2062 C CA  . GLY A 1 271 ? -5.702  -56.367  -4.986  1.00 74.74  ? 262 GLY A CA  1 
ATOM   2063 C C   . GLY A 1 271 ? -5.702  -57.880  -5.019  1.00 75.42  ? 262 GLY A C   1 
ATOM   2064 O O   . GLY A 1 271 ? -6.670  -58.540  -4.635  1.00 78.37  ? 262 GLY A O   1 
ATOM   2065 N N   . SER A 1 272 ? -4.589  -58.415  -5.506  1.00 74.40  ? 263 SER A N   1 
ATOM   2066 C CA  . SER A 1 272 ? -4.148  -59.759  -5.168  1.00 72.87  ? 263 SER A CA  1 
ATOM   2067 C C   . SER A 1 272 ? -3.461  -59.619  -3.810  1.00 69.02  ? 263 SER A C   1 
ATOM   2068 O O   . SER A 1 272 ? -3.677  -58.634  -3.111  1.00 69.41  ? 263 SER A O   1 
ATOM   2069 C CB  . SER A 1 272 ? -3.182  -60.305  -6.225  1.00 69.97  ? 263 SER A CB  1 
ATOM   2070 O OG  . SER A 1 272 ? -2.183  -59.354  -6.565  1.00 67.65  ? 263 SER A OG  1 
ATOM   2071 N N   . GLY A 1 273 ? -2.698  -60.617  -3.389  1.00 68.53  ? 264 GLY A N   1 
ATOM   2072 C CA  . GLY A 1 273 ? -1.936  -60.470  -2.162  1.00 68.30  ? 264 GLY A CA  1 
ATOM   2073 C C   . GLY A 1 273 ? -0.432  -60.336  -2.345  1.00 65.45  ? 264 GLY A C   1 
ATOM   2074 O O   . GLY A 1 273 ? 0.063   -60.115  -3.454  1.00 62.72  ? 264 GLY A O   1 
ATOM   2075 N N   . ILE A 1 274 ? 0.290   -60.462  -1.232  1.00 62.14  ? 265 ILE A N   1 
ATOM   2076 C CA  . ILE A 1 274 ? 1.723   -60.693  -1.253  1.00 59.15  ? 265 ILE A CA  1 
ATOM   2077 C C   . ILE A 1 274 ? 1.917   -62.073  -0.677  1.00 59.63  ? 265 ILE A C   1 
ATOM   2078 O O   . ILE A 1 274 ? 1.586   -62.316  0.477   1.00 63.34  ? 265 ILE A O   1 
ATOM   2079 C CB  . ILE A 1 274 ? 2.486   -59.702  -0.362  1.00 60.56  ? 265 ILE A CB  1 
ATOM   2080 C CG1 . ILE A 1 274 ? 2.634   -58.351  -1.061  1.00 58.43  ? 265 ILE A CG1 1 
ATOM   2081 C CG2 . ILE A 1 274 ? 3.845   -60.259  0.018   1.00 58.53  ? 265 ILE A CG2 1 
ATOM   2082 C CD1 . ILE A 1 274 ? 1.544   -57.375  -0.689  1.00 56.46  ? 265 ILE A CD1 1 
ATOM   2083 N N   . ILE A 1 275 ? 2.435   -62.987  -1.479  1.00 61.63  ? 266 ILE A N   1 
ATOM   2084 C CA  . ILE A 1 275 ? 2.717   -64.320  -0.976  1.00 65.46  ? 266 ILE A CA  1 
ATOM   2085 C C   . ILE A 1 275 ? 4.160   -64.397  -0.506  1.00 64.23  ? 266 ILE A C   1 
ATOM   2086 O O   . ILE A 1 275 ? 5.073   -63.943  -1.197  1.00 64.45  ? 266 ILE A O   1 
ATOM   2087 C CB  . ILE A 1 275 ? 2.447   -65.408  -2.033  1.00 68.89  ? 266 ILE A CB  1 
ATOM   2088 C CG1 . ILE A 1 275 ? 0.954   -65.737  -2.075  1.00 71.27  ? 266 ILE A CG1 1 
ATOM   2089 C CG2 . ILE A 1 275 ? 3.231   -66.665  -1.715  1.00 70.96  ? 266 ILE A CG2 1 
ATOM   2090 C CD1 . ILE A 1 275 ? 0.613   -66.948  -2.907  1.00 73.32  ? 266 ILE A CD1 1 
ATOM   2091 N N   . ILE A 1 276 ? 4.361   -64.945  0.684   1.00 65.05  ? 267 ILE A N   1 
ATOM   2092 C CA  . ILE A 1 276 ? 5.708   -65.126  1.200   1.00 65.07  ? 267 ILE A CA  1 
ATOM   2093 C C   . ILE A 1 276 ? 6.052   -66.611  1.204   1.00 69.08  ? 267 ILE A C   1 
ATOM   2094 O O   . ILE A 1 276 ? 5.587   -67.376  2.056   1.00 68.29  ? 267 ILE A O   1 
ATOM   2095 C CB  . ILE A 1 276 ? 5.816   -64.573  2.625   1.00 65.77  ? 267 ILE A CB  1 
ATOM   2096 C CG1 . ILE A 1 276 ? 5.147   -63.200  2.705   1.00 63.88  ? 267 ILE A CG1 1 
ATOM   2097 C CG2 . ILE A 1 276 ? 7.266   -64.510  3.058   1.00 66.44  ? 267 ILE A CG2 1 
ATOM   2098 C CD1 . ILE A 1 276 ? 5.172   -62.600  4.079   1.00 58.69  ? 267 ILE A CD1 1 
ATOM   2099 N N   . SER A 1 277 ? 6.895   -67.013  0.263   1.00 71.01  ? 268 SER A N   1 
ATOM   2100 C CA  . SER A 1 277 ? 7.191   -68.425  0.081   1.00 73.88  ? 268 SER A CA  1 
ATOM   2101 C C   . SER A 1 277 ? 8.559   -68.606  -0.560  1.00 73.65  ? 268 SER A C   1 
ATOM   2102 O O   . SER A 1 277 ? 9.043   -67.721  -1.276  1.00 71.87  ? 268 SER A O   1 
ATOM   2103 C CB  . SER A 1 277 ? 6.110   -69.088  -0.782  1.00 72.31  ? 268 SER A CB  1 
ATOM   2104 O OG  . SER A 1 277 ? 6.427   -70.443  -1.058  1.00 74.77  ? 268 SER A OG  1 
ATOM   2105 N N   . ASP A 1 278 ? 9.183   -69.751  -0.307  1.00 72.42  ? 269 ASP A N   1 
ATOM   2106 C CA  . ASP A 1 278 ? 10.459  -70.038  -0.937  1.00 74.22  ? 269 ASP A CA  1 
ATOM   2107 C C   . ASP A 1 278 ? 10.219  -70.898  -2.170  1.00 75.30  ? 269 ASP A C   1 
ATOM   2108 O O   . ASP A 1 278 ? 11.153  -71.309  -2.852  1.00 77.44  ? 269 ASP A O   1 
ATOM   2109 C CB  . ASP A 1 278 ? 11.448  -70.651  0.061   1.00 74.20  ? 269 ASP A CB  1 
ATOM   2110 C CG  . ASP A 1 278 ? 11.941  -69.628  1.096   1.00 74.04  ? 269 ASP A CG  1 
ATOM   2111 O OD1 . ASP A 1 278 ? 11.324  -68.552  1.201   1.00 74.18  ? 269 ASP A OD1 1 
ATOM   2112 O OD2 . ASP A 1 278 ? 12.940  -69.887  1.805   1.00 73.54  ? 269 ASP A OD2 1 
ATOM   2113 N N   . THR A 1 279 ? 8.940   -71.149  -2.441  1.00 73.34  ? 270 THR A N   1 
ATOM   2114 C CA  . THR A 1 279 ? 8.499   -71.830  -3.651  1.00 73.32  ? 270 THR A CA  1 
ATOM   2115 C C   . THR A 1 279 ? 8.908   -71.061  -4.898  1.00 73.64  ? 270 THR A C   1 
ATOM   2116 O O   . THR A 1 279 ? 8.816   -69.837  -4.935  1.00 74.83  ? 270 THR A O   1 
ATOM   2117 C CB  . THR A 1 279 ? 6.970   -71.972  -3.676  1.00 74.50  ? 270 THR A CB  1 
ATOM   2118 O OG1 . THR A 1 279 ? 6.533   -72.645  -2.493  1.00 75.21  ? 270 THR A OG1 1 
ATOM   2119 C CG2 . THR A 1 279 ? 6.521   -72.753  -4.900  1.00 75.81  ? 270 THR A CG2 1 
ATOM   2120 N N   . PRO A 1 280 ? 9.390   -71.786  -5.916  1.00 73.13  ? 271 PRO A N   1 
ATOM   2121 C CA  . PRO A 1 280 ? 9.797   -71.285  -7.237  1.00 77.89  ? 271 PRO A CA  1 
ATOM   2122 C C   . PRO A 1 280 ? 8.657   -70.988  -8.217  1.00 78.65  ? 271 PRO A C   1 
ATOM   2123 O O   . PRO A 1 280 ? 7.618   -71.651  -8.228  1.00 80.62  ? 271 PRO A O   1 
ATOM   2124 C CB  . PRO A 1 280 ? 10.656  -72.423  -7.781  1.00 78.24  ? 271 PRO A CB  1 
ATOM   2125 C CG  . PRO A 1 280 ? 10.104  -73.635  -7.128  1.00 78.15  ? 271 PRO A CG  1 
ATOM   2126 C CD  . PRO A 1 280 ? 9.744   -73.204  -5.740  1.00 74.05  ? 271 PRO A CD  1 
ATOM   2127 N N   . VAL A 1 281 ? 8.879   -69.982  -9.049  1.00 76.05  ? 272 VAL A N   1 
ATOM   2128 C CA  . VAL A 1 281 ? 7.945   -69.623  -10.097 1.00 80.50  ? 272 VAL A CA  1 
ATOM   2129 C C   . VAL A 1 281 ? 8.028   -70.602  -11.258 1.00 83.92  ? 272 VAL A C   1 
ATOM   2130 O O   . VAL A 1 281 ? 9.020   -71.313  -11.401 1.00 86.59  ? 272 VAL A O   1 
ATOM   2131 C CB  . VAL A 1 281 ? 8.257   -68.221  -10.621 1.00 84.04  ? 272 VAL A CB  1 
ATOM   2132 C CG1 . VAL A 1 281 ? 7.035   -67.321  -10.487 1.00 83.29  ? 272 VAL A CG1 1 
ATOM   2133 C CG2 . VAL A 1 281 ? 9.456   -67.639  -9.868  1.00 76.26  ? 272 VAL A CG2 1 
ATOM   2134 N N   . HIS A 1 282 ? 6.985   -70.642  -12.082 1.00 85.85  ? 273 HIS A N   1 
ATOM   2135 C CA  . HIS A 1 282 ? 7.029   -71.417  -13.318 1.00 89.17  ? 273 HIS A CA  1 
ATOM   2136 C C   . HIS A 1 282 ? 6.301   -70.682  -14.440 1.00 92.64  ? 273 HIS A C   1 
ATOM   2137 O O   . HIS A 1 282 ? 5.675   -69.643  -14.209 1.00 91.13  ? 273 HIS A O   1 
ATOM   2138 C CB  . HIS A 1 282 ? 6.387   -72.789  -13.108 1.00 89.82  ? 273 HIS A CB  1 
ATOM   2139 C CG  . HIS A 1 282 ? 6.575   -73.730  -14.259 1.00 94.09  ? 273 HIS A CG  1 
ATOM   2140 N ND1 . HIS A 1 282 ? 5.554   -74.068  -15.122 1.00 97.06  ? 273 HIS A ND1 1 
ATOM   2141 C CD2 . HIS A 1 282 ? 7.668   -74.403  -14.690 1.00 96.25  ? 273 HIS A CD2 1 
ATOM   2142 C CE1 . HIS A 1 282 ? 6.009   -74.909  -16.034 1.00 97.24  ? 273 HIS A CE1 1 
ATOM   2143 N NE2 . HIS A 1 282 ? 7.289   -75.129  -15.795 1.00 98.13  ? 273 HIS A NE2 1 
ATOM   2144 N N   . ASP A 1 283 ? 6.362   -71.247  -15.647 1.00 93.12  ? 274 ASP A N   1 
ATOM   2145 C CA  . ASP A 1 283 ? 5.658   -70.708  -16.806 1.00 89.34  ? 274 ASP A CA  1 
ATOM   2146 C C   . ASP A 1 283 ? 4.234   -71.230  -16.768 1.00 90.44  ? 274 ASP A C   1 
ATOM   2147 O O   . ASP A 1 283 ? 3.421   -70.934  -17.648 1.00 91.37  ? 274 ASP A O   1 
ATOM   2148 C CB  . ASP A 1 283 ? 6.332   -71.141  -18.108 1.00 89.50  ? 274 ASP A CB  1 
ATOM   2149 C CG  . ASP A 1 283 ? 5.820   -70.367  -19.320 1.00 94.40  ? 274 ASP A CG  1 
ATOM   2150 O OD1 . ASP A 1 283 ? 4.753   -69.716  -19.218 1.00 91.43  ? 274 ASP A OD1 1 
ATOM   2151 O OD2 . ASP A 1 283 ? 6.488   -70.410  -20.378 1.00 96.51  ? 274 ASP A OD2 1 
ATOM   2152 N N   . CYS A 1 284 ? 3.929   -71.981  -15.713 1.00 89.48  ? 275 CYS A N   1 
ATOM   2153 C CA  . CYS A 1 284 ? 2.635   -72.622  -15.583 1.00 87.44  ? 275 CYS A CA  1 
ATOM   2154 C C   . CYS A 1 284 ? 1.614   -71.528  -15.398 1.00 86.42  ? 275 CYS A C   1 
ATOM   2155 O O   . CYS A 1 284 ? 1.940   -70.341  -15.392 1.00 86.09  ? 275 CYS A O   1 
ATOM   2156 C CB  . CYS A 1 284 ? 2.596   -73.522  -14.351 1.00 86.22  ? 275 CYS A CB  1 
ATOM   2157 S SG  . CYS A 1 284 ? 2.335   -72.618  -12.794 1.00 99.44  ? 275 CYS A SG  1 
ATOM   2158 N N   . ASN A 1 285 ? 0.367   -71.933  -15.244 1.00 84.44  ? 276 ASN A N   1 
ATOM   2159 C CA  . ASN A 1 285 ? -0.753  -70.977  -15.001 1.00 87.48  ? 276 ASN A CA  1 
ATOM   2160 C C   . ASN A 1 285 ? -1.756  -71.509  -14.204 1.00 84.53  ? 276 ASN A C   1 
ATOM   2161 O O   . ASN A 1 285 ? -1.952  -72.715  -14.119 1.00 86.74  ? 276 ASN A O   1 
ATOM   2162 C CB  . ASN A 1 285 ? -1.107  -70.945  -16.474 1.00 89.74  ? 276 ASN A CB  1 
ATOM   2163 C CG  . ASN A 1 285 ? -2.325  -70.122  -16.789 1.00 105.16 ? 276 ASN A CG  1 
ATOM   2164 O OD1 . ASN A 1 285 ? -3.092  -69.689  -15.915 1.00 100.85 ? 276 ASN A OD1 1 
ATOM   2165 N ND2 . ASN A 1 285 ? -2.508  -69.919  -18.097 1.00 114.34 ? 276 ASN A ND2 1 
ATOM   2166 N N   . THR A 1 286 ? -2.421  -70.627  -13.466 1.00 84.80  ? 277 THR A N   1 
ATOM   2167 C CA  . THR A 1 286 ? -3.583  -71.081  -12.721 1.00 84.30  ? 277 THR A CA  1 
ATOM   2168 C C   . THR A 1 286 ? -4.575  -69.987  -12.377 1.00 87.13  ? 277 THR A C   1 
ATOM   2169 O O   . THR A 1 286 ? -4.315  -68.797  -12.575 1.00 86.52  ? 277 THR A O   1 
ATOM   2170 C CB  . THR A 1 286 ? -3.177  -71.743  -11.403 1.00 84.23  ? 277 THR A CB  1 
ATOM   2171 O OG1 . THR A 1 286 ? -4.339  -72.302  -10.777 1.00 88.40  ? 277 THR A OG1 1 
ATOM   2172 C CG2 . THR A 1 286 ? -2.563  -70.717  -10.476 1.00 85.32  ? 277 THR A CG2 1 
ATOM   2173 N N   . THR A 1 287 ? -5.713  -70.432  -11.851 1.00 87.55  ? 278 THR A N   1 
ATOM   2174 C CA  . THR A 1 287 ? -6.746  -69.571  -11.302 1.00 89.15  ? 278 THR A CA  1 
ATOM   2175 C C   . THR A 1 287 ? -6.432  -69.229  -9.857  1.00 90.73  ? 278 THR A C   1 
ATOM   2176 O O   . THR A 1 287 ? -6.607  -68.090  -9.414  1.00 92.81  ? 278 THR A O   1 
ATOM   2177 C CB  . THR A 1 287 ? -8.110  -70.280  -11.306 1.00 90.43  ? 278 THR A CB  1 
ATOM   2178 O OG1 . THR A 1 287 ? -8.478  -70.610  -12.647 1.00 90.29  ? 278 THR A OG1 1 
ATOM   2179 C CG2 . THR A 1 287 ? -9.178  -69.384  -10.696 1.00 93.75  ? 278 THR A CG2 1 
ATOM   2180 N N   . CYS A 1 288 ? -5.986  -70.246  -9.123  1.00 90.34  ? 279 CYS A N   1 
ATOM   2181 C CA  . CYS A 1 288 ? -5.881  -70.175  -7.670  1.00 87.27  ? 279 CYS A CA  1 
ATOM   2182 C C   . CYS A 1 288 ? -4.468  -70.433  -7.148  1.00 86.52  ? 279 CYS A C   1 
ATOM   2183 O O   . CYS A 1 288 ? -3.973  -71.559  -7.213  1.00 86.05  ? 279 CYS A O   1 
ATOM   2184 C CB  . CYS A 1 288 ? -6.845  -71.188  -7.060  1.00 85.96  ? 279 CYS A CB  1 
ATOM   2185 S SG  . CYS A 1 288 ? -6.682  -71.402  -5.292  1.00 89.89  ? 279 CYS A SG  1 
ATOM   2186 N N   . GLN A 1 289 ? -3.835  -69.398  -6.599  1.00 83.23  ? 280 GLN A N   1 
ATOM   2187 C CA  . GLN A 1 289 ? -2.460  -69.513  -6.119  1.00 79.79  ? 280 GLN A CA  1 
ATOM   2188 C C   . GLN A 1 289 ? -2.355  -69.514  -4.601  1.00 80.88  ? 280 GLN A C   1 
ATOM   2189 O O   . GLN A 1 289 ? -3.121  -68.855  -3.898  1.00 81.30  ? 280 GLN A O   1 
ATOM   2190 C CB  . GLN A 1 289 ? -1.594  -68.394  -6.691  1.00 77.06  ? 280 GLN A CB  1 
ATOM   2191 C CG  . GLN A 1 289 ? -0.103  -68.604  -6.510  1.00 73.66  ? 280 GLN A CG  1 
ATOM   2192 C CD  . GLN A 1 289 ? 0.382   -69.880  -7.158  1.00 77.64  ? 280 GLN A CD  1 
ATOM   2193 O OE1 . GLN A 1 289 ? 0.769   -69.895  -8.328  1.00 76.35  ? 280 GLN A OE1 1 
ATOM   2194 N NE2 . GLN A 1 289 ? 0.359   -70.965  -6.402  1.00 78.31  ? 280 GLN A NE2 1 
ATOM   2195 N N   . THR A 1 290 ? -1.381  -70.259  -4.104  1.00 79.35  ? 281 THR A N   1 
ATOM   2196 C CA  . THR A 1 290 ? -1.202  -70.433  -2.679  1.00 78.22  ? 281 THR A CA  1 
ATOM   2197 C C   . THR A 1 290 ? 0.278   -70.288  -2.355  1.00 80.15  ? 281 THR A C   1 
ATOM   2198 O O   . THR A 1 290 ? 1.126   -70.447  -3.240  1.00 78.33  ? 281 THR A O   1 
ATOM   2199 C CB  . THR A 1 290 ? -1.736  -71.815  -2.241  1.00 77.58  ? 281 THR A CB  1 
ATOM   2200 O OG1 . THR A 1 290 ? -3.128  -71.702  -1.924  1.00 79.62  ? 281 THR A OG1 1 
ATOM   2201 C CG2 . THR A 1 290 ? -0.988  -72.352  -1.031  1.00 75.05  ? 281 THR A CG2 1 
ATOM   2202 N N   . PRO A 1 291 ? 0.598   -69.942  -1.095  1.00 78.97  ? 282 PRO A N   1 
ATOM   2203 C CA  . PRO A 1 291 ? 2.001   -69.900  -0.676  1.00 76.05  ? 282 PRO A CA  1 
ATOM   2204 C C   . PRO A 1 291 ? 2.726   -71.204  -1.004  1.00 78.60  ? 282 PRO A C   1 
ATOM   2205 O O   . PRO A 1 291 ? 3.879   -71.164  -1.428  1.00 78.85  ? 282 PRO A O   1 
ATOM   2206 C CB  . PRO A 1 291 ? 1.899   -69.726  0.839   1.00 77.06  ? 282 PRO A CB  1 
ATOM   2207 C CG  . PRO A 1 291 ? 0.621   -68.979  1.034   1.00 77.81  ? 282 PRO A CG  1 
ATOM   2208 C CD  . PRO A 1 291 ? -0.310  -69.444  -0.043  1.00 77.48  ? 282 PRO A CD  1 
ATOM   2209 N N   . LYS A 1 292 ? 2.056   -72.340  -0.813  1.00 80.26  ? 283 LYS A N   1 
ATOM   2210 C CA  . LYS A 1 292 ? 2.656   -73.655  -1.056  1.00 77.80  ? 283 LYS A CA  1 
ATOM   2211 C C   . LYS A 1 292 ? 2.676   -74.037  -2.536  1.00 79.84  ? 283 LYS A C   1 
ATOM   2212 O O   . LYS A 1 292 ? 3.616   -74.678  -3.005  1.00 81.36  ? 283 LYS A O   1 
ATOM   2213 C CB  . LYS A 1 292 ? 1.922   -74.751  -0.277  1.00 80.21  ? 283 LYS A CB  1 
ATOM   2214 C CG  . LYS A 1 292 ? 2.027   -74.692  1.252   1.00 82.24  ? 283 LYS A CG  1 
ATOM   2215 C CD  . LYS A 1 292 ? 1.655   -76.055  1.860   1.00 84.09  ? 283 LYS A CD  1 
ATOM   2216 C CE  . LYS A 1 292 ? 0.815   -75.935  3.123   1.00 84.54  ? 283 LYS A CE  1 
ATOM   2217 N NZ  . LYS A 1 292 ? 1.639   -75.679  4.327   1.00 87.62  ? 283 LYS A NZ  1 
ATOM   2218 N N   . GLY A 1 293 ? 1.622   -73.667  -3.257  1.00 78.76  ? 284 GLY A N   1 
ATOM   2219 C CA  . GLY A 1 293 ? 1.473   -74.047  -4.650  1.00 78.21  ? 284 GLY A CA  1 
ATOM   2220 C C   . GLY A 1 293 ? 0.211   -73.430  -5.210  1.00 81.84  ? 284 GLY A C   1 
ATOM   2221 O O   . GLY A 1 293 ? -0.284  -72.443  -4.671  1.00 81.96  ? 284 GLY A O   1 
ATOM   2222 N N   . ALA A 1 294 ? -0.302  -73.983  -6.305  1.00 83.77  ? 285 ALA A N   1 
ATOM   2223 C CA  . ALA A 1 294 ? -1.611  -73.570  -6.803  1.00 82.78  ? 285 ALA A CA  1 
ATOM   2224 C C   . ALA A 1 294 ? -2.610  -74.719  -6.682  1.00 83.18  ? 285 ALA A C   1 
ATOM   2225 O O   . ALA A 1 294 ? -2.246  -75.826  -6.294  1.00 81.41  ? 285 ALA A O   1 
ATOM   2226 C CB  . ALA A 1 294 ? -1.511  -73.106  -8.242  1.00 83.03  ? 285 ALA A CB  1 
ATOM   2227 N N   . ILE A 1 295 ? -3.868  -74.457  -7.024  1.00 88.15  ? 286 ILE A N   1 
ATOM   2228 C CA  . ILE A 1 295 ? -4.889  -75.503  -6.989  1.00 91.83  ? 286 ILE A CA  1 
ATOM   2229 C C   . ILE A 1 295 ? -5.871  -75.444  -8.147  1.00 94.40  ? 286 ILE A C   1 
ATOM   2230 O O   . ILE A 1 295 ? -6.492  -74.410  -8.398  1.00 94.35  ? 286 ILE A O   1 
ATOM   2231 C CB  . ILE A 1 295 ? -5.713  -75.459  -5.693  1.00 92.04  ? 286 ILE A CB  1 
ATOM   2232 C CG1 . ILE A 1 295 ? -5.176  -74.384  -4.749  1.00 90.68  ? 286 ILE A CG1 1 
ATOM   2233 C CG2 . ILE A 1 295 ? -5.711  -76.817  -5.027  1.00 92.74  ? 286 ILE A CG2 1 
ATOM   2234 C CD1 . ILE A 1 295 ? -5.743  -74.459  -3.341  1.00 87.23  ? 286 ILE A CD1 1 
ATOM   2235 N N   . ASN A 1 296 ? -6.019  -76.564  -8.845  1.00 98.11  ? 287 ASN A N   1 
ATOM   2236 C CA  . ASN A 1 296 ? -7.144  -76.702  -9.748  1.00 101.38 ? 287 ASN A CA  1 
ATOM   2237 C C   . ASN A 1 296 ? -8.177  -77.570  -9.080  1.00 100.05 ? 287 ASN A C   1 
ATOM   2238 O O   . ASN A 1 296 ? -7.989  -78.773  -8.893  1.00 101.34 ? 287 ASN A O   1 
ATOM   2239 C CB  . ASN A 1 296 ? -6.758  -77.291  -11.101 1.00 106.49 ? 287 ASN A CB  1 
ATOM   2240 C CG  . ASN A 1 296 ? -7.900  -77.217  -12.106 1.00 109.38 ? 287 ASN A CG  1 
ATOM   2241 O OD1 . ASN A 1 296 ? -9.004  -76.776  -11.780 1.00 112.18 ? 287 ASN A OD1 1 
ATOM   2242 N ND2 . ASN A 1 296 ? -7.632  -77.635  -13.341 1.00 109.71 ? 287 ASN A ND2 1 
ATOM   2243 N N   . THR A 1 297 ? -9.266  -76.928  -8.696  1.00 100.06 ? 288 THR A N   1 
ATOM   2244 C CA  . THR A 1 297 ? -10.337 -77.601  -8.012  1.00 100.84 ? 288 THR A CA  1 
ATOM   2245 C C   . THR A 1 297 ? -11.634 -76.901  -8.320  1.00 103.28 ? 288 THR A C   1 
ATOM   2246 O O   . THR A 1 297 ? -11.690 -75.673  -8.423  1.00 101.53 ? 288 THR A O   1 
ATOM   2247 C CB  . THR A 1 297 ? -10.140 -77.540  -6.499  1.00 100.12 ? 288 THR A CB  1 
ATOM   2248 O OG1 . THR A 1 297 ? -9.684  -76.230  -6.139  1.00 99.10  ? 288 THR A OG1 1 
ATOM   2249 C CG2 . THR A 1 297 ? -9.115  -78.549  -6.063  1.00 100.00 ? 288 THR A CG2 1 
ATOM   2250 N N   . SER A 1 298 ? -12.679 -77.698  -8.464  1.00 105.63 ? 289 SER A N   1 
ATOM   2251 C CA  . SER A 1 298 ? -14.027 -77.188  -8.385  1.00 108.08 ? 289 SER A CA  1 
ATOM   2252 C C   . SER A 1 298 ? -14.410 -77.383  -6.923  1.00 109.78 ? 289 SER A C   1 
ATOM   2253 O O   . SER A 1 298 ? -15.541 -77.112  -6.511  1.00 112.40 ? 289 SER A O   1 
ATOM   2254 C CB  . SER A 1 298 ? -14.943 -77.964  -9.328  1.00 109.75 ? 289 SER A CB  1 
ATOM   2255 O OG  . SER A 1 298 ? -14.471 -77.872  -10.666 1.00 111.00 ? 289 SER A OG  1 
ATOM   2256 N N   . LEU A 1 299 ? -13.427 -77.855  -6.152  1.00 106.78 ? 290 LEU A N   1 
ATOM   2257 C CA  . LEU A 1 299 ? -13.564 -78.142  -4.720  1.00 103.52 ? 290 LEU A CA  1 
ATOM   2258 C C   . LEU A 1 299 ? -13.865 -76.903  -3.865  1.00 105.69 ? 290 LEU A C   1 
ATOM   2259 O O   . LEU A 1 299 ? -13.376 -75.805  -4.153  1.00 104.55 ? 290 LEU A O   1 
ATOM   2260 C CB  . LEU A 1 299 ? -12.304 -78.843  -4.209  1.00 101.84 ? 290 LEU A CB  1 
ATOM   2261 C CG  . LEU A 1 299 ? -12.220 -80.339  -4.489  1.00 101.09 ? 290 LEU A CG  1 
ATOM   2262 C CD1 . LEU A 1 299 ? -10.775 -80.814  -4.486  1.00 99.75  ? 290 LEU A CD1 1 
ATOM   2263 C CD2 . LEU A 1 299 ? -13.050 -81.094  -3.465  1.00 100.06 ? 290 LEU A CD2 1 
ATOM   2264 N N   . PRO A 1 300 ? -14.682 -77.089  -2.811  1.00 105.86 ? 291 PRO A N   1 
ATOM   2265 C CA  . PRO A 1 300 ? -15.226 -76.047  -1.927  1.00 102.85 ? 291 PRO A CA  1 
ATOM   2266 C C   . PRO A 1 300 ? -14.222 -75.422  -0.952  1.00 102.31 ? 291 PRO A C   1 
ATOM   2267 O O   . PRO A 1 300 ? -14.392 -74.264  -0.565  1.00 102.62 ? 291 PRO A O   1 
ATOM   2268 C CB  . PRO A 1 300 ? -16.289 -76.805  -1.134  1.00 101.67 ? 291 PRO A CB  1 
ATOM   2269 C CG  . PRO A 1 300 ? -15.720 -78.176  -1.008  1.00 102.10 ? 291 PRO A CG  1 
ATOM   2270 C CD  . PRO A 1 300 ? -15.015 -78.441  -2.321  1.00 104.86 ? 291 PRO A CD  1 
ATOM   2271 N N   . PHE A 1 301 ? -13.206 -76.179  -0.548  1.00 99.88  ? 292 PHE A N   1 
ATOM   2272 C CA  . PHE A 1 301 ? -12.342 -75.756  0.545   1.00 97.79  ? 292 PHE A CA  1 
ATOM   2273 C C   . PHE A 1 301 ? -10.922 -76.219  0.356   1.00 97.35  ? 292 PHE A C   1 
ATOM   2274 O O   . PHE A 1 301 ? -10.556 -76.744  -0.691  1.00 98.18  ? 292 PHE A O   1 
ATOM   2275 C CB  . PHE A 1 301 ? -12.843 -76.334  1.866   1.00 96.44  ? 292 PHE A CB  1 
ATOM   2276 C CG  . PHE A 1 301 ? -14.211 -75.871  2.248   1.00 100.33 ? 292 PHE A CG  1 
ATOM   2277 C CD1 . PHE A 1 301 ? -14.538 -74.528  2.213   1.00 100.64 ? 292 PHE A CD1 1 
ATOM   2278 C CD2 . PHE A 1 301 ? -15.176 -76.780  2.640   1.00 103.09 ? 292 PHE A CD2 1 
ATOM   2279 C CE1 . PHE A 1 301 ? -15.803 -74.102  2.565   1.00 102.35 ? 292 PHE A CE1 1 
ATOM   2280 C CE2 . PHE A 1 301 ? -16.442 -76.357  2.994   1.00 101.81 ? 292 PHE A CE2 1 
ATOM   2281 C CZ  . PHE A 1 301 ? -16.755 -75.015  2.956   1.00 102.98 ? 292 PHE A CZ  1 
ATOM   2282 N N   . GLN A 1 302 ? -10.137 -76.054  1.411   1.00 95.14  ? 293 GLN A N   1 
ATOM   2283 C CA  . GLN A 1 302 ? -8.800  -76.596  1.450   1.00 92.14  ? 293 GLN A CA  1 
ATOM   2284 C C   . GLN A 1 302 ? -8.217  -76.328  2.812   1.00 92.28  ? 293 GLN A C   1 
ATOM   2285 O O   . GLN A 1 302 ? -8.586  -75.370  3.489   1.00 93.03  ? 293 GLN A O   1 
ATOM   2286 C CB  . GLN A 1 302 ? -7.942  -75.881  0.415   1.00 91.69  ? 293 GLN A CB  1 
ATOM   2287 C CG  . GLN A 1 302 ? -8.093  -74.355  0.441   1.00 91.67  ? 293 GLN A CG  1 
ATOM   2288 C CD  . GLN A 1 302 ? -7.077  -73.650  1.335   1.00 89.92  ? 293 GLN A CD  1 
ATOM   2289 O OE1 . GLN A 1 302 ? -6.322  -74.286  2.072   1.00 87.90  ? 293 GLN A OE1 1 
ATOM   2290 N NE2 . GLN A 1 302 ? -7.056  -72.324  1.266   1.00 88.95  ? 293 GLN A NE2 1 
ATOM   2291 N N   . ASN A 1 303 ? -7.283  -77.182  3.197   1.00 89.93  ? 294 ASN A N   1 
ATOM   2292 C CA  . ASN A 1 303 ? -6.554  -77.028  4.435   1.00 89.97  ? 294 ASN A CA  1 
ATOM   2293 C C   . ASN A 1 303 ? -5.186  -76.452  4.144   1.00 88.42  ? 294 ASN A C   1 
ATOM   2294 O O   . ASN A 1 303 ? -4.346  -76.317  5.030   1.00 89.64  ? 294 ASN A O   1 
ATOM   2295 C CB  . ASN A 1 303 ? -6.450  -78.364  5.150   1.00 92.95  ? 294 ASN A CB  1 
ATOM   2296 C CG  . ASN A 1 303 ? -5.924  -79.447  4.255   1.00 95.07  ? 294 ASN A CG  1 
ATOM   2297 O OD1 . ASN A 1 303 ? -5.952  -79.320  3.026   1.00 93.65  ? 294 ASN A OD1 1 
ATOM   2298 N ND2 . ASN A 1 303 ? -5.435  -80.525  4.857   1.00 98.69  ? 294 ASN A ND2 1 
ATOM   2299 N N   . ILE A 1 304 ? -4.958  -76.115  2.886   1.00 88.13  ? 295 ILE A N   1 
ATOM   2300 C CA  . ILE A 1 304 ? -3.599  -75.903  2.423   1.00 88.77  ? 295 ILE A CA  1 
ATOM   2301 C C   . ILE A 1 304 ? -3.000  -74.645  3.029   1.00 87.43  ? 295 ILE A C   1 
ATOM   2302 O O   . ILE A 1 304 ? -2.067  -74.739  3.826   1.00 87.38  ? 295 ILE A O   1 
ATOM   2303 C CB  . ILE A 1 304 ? -3.538  -75.844  0.895   1.00 87.19  ? 295 ILE A CB  1 
ATOM   2304 C CG1 . ILE A 1 304 ? -3.995  -77.182  0.318   1.00 89.38  ? 295 ILE A CG1 1 
ATOM   2305 C CG2 . ILE A 1 304 ? -2.134  -75.516  0.436   1.00 83.52  ? 295 ILE A CG2 1 
ATOM   2306 C CD1 . ILE A 1 304 ? -4.156  -77.172  -1.169  1.00 90.54  ? 295 ILE A CD1 1 
ATOM   2307 N N   . HIS A 1 305 ? -3.524  -73.477  2.673   1.00 85.73  ? 296 HIS A N   1 
ATOM   2308 C CA  . HIS A 1 305 ? -3.040  -72.251  3.292   1.00 83.98  ? 296 HIS A CA  1 
ATOM   2309 C C   . HIS A 1 305 ? -4.126  -71.217  3.533   1.00 84.08  ? 296 HIS A C   1 
ATOM   2310 O O   . HIS A 1 305 ? -5.043  -71.063  2.726   1.00 83.02  ? 296 HIS A O   1 
ATOM   2311 C CB  . HIS A 1 305 ? -1.915  -71.627  2.469   1.00 80.84  ? 296 HIS A CB  1 
ATOM   2312 C CG  . HIS A 1 305 ? -1.057  -70.685  3.252   1.00 81.62  ? 296 HIS A CG  1 
ATOM   2313 N ND1 . HIS A 1 305 ? -1.479  -69.427  3.623   1.00 81.94  ? 296 HIS A ND1 1 
ATOM   2314 C CD2 . HIS A 1 305 ? 0.196   -70.822  3.745   1.00 82.54  ? 296 HIS A CD2 1 
ATOM   2315 C CE1 . HIS A 1 305 ? -0.521  -68.828  4.307   1.00 82.50  ? 296 HIS A CE1 1 
ATOM   2316 N NE2 . HIS A 1 305 ? 0.507   -69.652  4.394   1.00 84.01  ? 296 HIS A NE2 1 
ATOM   2317 N N   . PRO A 1 306 ? -4.010  -70.494  4.653   1.00 83.61  ? 297 PRO A N   1 
ATOM   2318 C CA  . PRO A 1 306 ? -4.905  -69.379  4.967   1.00 83.34  ? 297 PRO A CA  1 
ATOM   2319 C C   . PRO A 1 306 ? -4.884  -68.331  3.856   1.00 81.83  ? 297 PRO A C   1 
ATOM   2320 O O   . PRO A 1 306 ? -5.856  -67.599  3.663   1.00 82.69  ? 297 PRO A O   1 
ATOM   2321 C CB  . PRO A 1 306 ? -4.294  -68.805  6.245   1.00 82.22  ? 297 PRO A CB  1 
ATOM   2322 C CG  . PRO A 1 306 ? -3.605  -69.969  6.886   1.00 82.65  ? 297 PRO A CG  1 
ATOM   2323 C CD  . PRO A 1 306 ? -3.063  -70.775  5.747   1.00 81.54  ? 297 PRO A CD  1 
ATOM   2324 N N   . ILE A 1 307 ? -3.779  -68.268  3.126   1.00 79.22  ? 298 ILE A N   1 
ATOM   2325 C CA  . ILE A 1 307 ? -3.603  -67.228  2.129   1.00 79.58  ? 298 ILE A CA  1 
ATOM   2326 C C   . ILE A 1 307 ? -3.768  -67.774  0.730   1.00 79.30  ? 298 ILE A C   1 
ATOM   2327 O O   . ILE A 1 307 ? -2.999  -68.624  0.289   1.00 78.61  ? 298 ILE A O   1 
ATOM   2328 C CB  . ILE A 1 307 ? -2.217  -66.572  2.226   1.00 81.50  ? 298 ILE A CB  1 
ATOM   2329 C CG1 . ILE A 1 307 ? -1.973  -66.033  3.633   1.00 80.94  ? 298 ILE A CG1 1 
ATOM   2330 C CG2 . ILE A 1 307 ? -2.085  -65.458  1.200   1.00 75.93  ? 298 ILE A CG2 1 
ATOM   2331 C CD1 . ILE A 1 307 ? -0.544  -65.597  3.853   1.00 82.59  ? 298 ILE A CD1 1 
ATOM   2332 N N   . THR A 1 308 ? -4.776  -67.267  0.034   1.00 79.29  ? 299 THR A N   1 
ATOM   2333 C CA  . THR A 1 308 ? -5.043  -67.681  -1.330  1.00 81.15  ? 299 THR A CA  1 
ATOM   2334 C C   . THR A 1 308 ? -5.219  -66.457  -2.206  1.00 81.98  ? 299 THR A C   1 
ATOM   2335 O O   . THR A 1 308 ? -5.493  -65.365  -1.716  1.00 82.18  ? 299 THR A O   1 
ATOM   2336 C CB  . THR A 1 308 ? -6.317  -68.538  -1.426  1.00 84.29  ? 299 THR A CB  1 
ATOM   2337 O OG1 . THR A 1 308 ? -7.476  -67.710  -1.250  1.00 85.58  ? 299 THR A OG1 1 
ATOM   2338 C CG2 . THR A 1 308 ? -6.305  -69.643  -0.379  1.00 83.30  ? 299 THR A CG2 1 
ATOM   2339 N N   . ILE A 1 309 ? -5.066  -66.647  -3.509  1.00 81.83  ? 300 ILE A N   1 
ATOM   2340 C CA  . ILE A 1 309 ? -5.122  -65.539  -4.447  1.00 82.12  ? 300 ILE A CA  1 
ATOM   2341 C C   . ILE A 1 309 ? -6.071  -65.818  -5.608  1.00 87.90  ? 300 ILE A C   1 
ATOM   2342 O O   . ILE A 1 309 ? -6.235  -66.964  -6.028  1.00 88.52  ? 300 ILE A O   1 
ATOM   2343 C CB  . ILE A 1 309 ? -3.726  -65.220  -4.999  1.00 81.07  ? 300 ILE A CB  1 
ATOM   2344 C CG1 . ILE A 1 309 ? -2.915  -64.439  -3.969  1.00 76.25  ? 300 ILE A CG1 1 
ATOM   2345 C CG2 . ILE A 1 309 ? -3.828  -64.422  -6.276  1.00 84.27  ? 300 ILE A CG2 1 
ATOM   2346 C CD1 . ILE A 1 309 ? -2.472  -65.259  -2.800  1.00 77.19  ? 300 ILE A CD1 1 
ATOM   2347 N N   . GLY A 1 310 ? -6.687  -64.758  -6.127  1.00 91.41  ? 301 GLY A N   1 
ATOM   2348 C CA  . GLY A 1 310 ? -7.654  -64.885  -7.202  1.00 92.82  ? 301 GLY A CA  1 
ATOM   2349 C C   . GLY A 1 310 ? -8.858  -65.673  -6.726  1.00 95.64  ? 301 GLY A C   1 
ATOM   2350 O O   . GLY A 1 310 ? -9.215  -65.618  -5.545  1.00 95.86  ? 301 GLY A O   1 
ATOM   2351 N N   . LYS A 1 311 ? -9.480  -66.427  -7.627  1.00 95.14  ? 302 LYS A N   1 
ATOM   2352 C CA  . LYS A 1 311 ? -10.634 -67.229  -7.235  1.00 96.00  ? 302 LYS A CA  1 
ATOM   2353 C C   . LYS A 1 311 ? -10.181 -68.560  -6.644  1.00 95.49  ? 302 LYS A C   1 
ATOM   2354 O O   . LYS A 1 311 ? -9.605  -69.401  -7.341  1.00 95.08  ? 302 LYS A O   1 
ATOM   2355 C CB  . LYS A 1 311 ? -11.571 -67.450  -8.424  1.00 95.22  ? 302 LYS A CB  1 
ATOM   2356 C CG  . LYS A 1 311 ? -12.627 -66.352  -8.592  1.00 101.81 ? 302 LYS A CG  1 
ATOM   2357 C CD  . LYS A 1 311 ? -12.004 -64.975  -8.821  1.00 104.21 ? 302 LYS A CD  1 
ATOM   2358 C CE  . LYS A 1 311 ? -13.015 -63.843  -8.601  1.00 106.20 ? 302 LYS A CE  1 
ATOM   2359 N NZ  . LYS A 1 311 ? -14.187 -63.922  -9.522  1.00 105.97 ? 302 LYS A NZ  1 
ATOM   2360 N N   . CYS A 1 312 ? -10.478 -68.753  -5.361  1.00 93.68  ? 303 CYS A N   1 
ATOM   2361 C CA  . CYS A 1 312 ? -9.919  -69.866  -4.603  1.00 93.84  ? 303 CYS A CA  1 
ATOM   2362 C C   . CYS A 1 312 ? -10.906 -70.460  -3.614  1.00 92.54  ? 303 CYS A C   1 
ATOM   2363 O O   . CYS A 1 312 ? -11.798 -69.767  -3.131  1.00 92.97  ? 303 CYS A O   1 
ATOM   2364 C CB  . CYS A 1 312 ? -8.672  -69.409  -3.844  1.00 92.31  ? 303 CYS A CB  1 
ATOM   2365 S SG  . CYS A 1 312 ? -7.145  -69.486  -4.800  1.00 97.60  ? 303 CYS A SG  1 
ATOM   2366 N N   . PRO A 1 313 ? -10.736 -71.757  -3.309  1.00 91.89  ? 304 PRO A N   1 
ATOM   2367 C CA  . PRO A 1 313 ? -11.523 -72.486  -2.309  1.00 93.00  ? 304 PRO A CA  1 
ATOM   2368 C C   . PRO A 1 313 ? -11.304 -71.968  -0.890  1.00 93.78  ? 304 PRO A C   1 
ATOM   2369 O O   . PRO A 1 313 ? -10.169 -71.715  -0.481  1.00 94.60  ? 304 PRO A O   1 
ATOM   2370 C CB  . PRO A 1 313 ? -11.008 -73.928  -2.437  1.00 94.69  ? 304 PRO A CB  1 
ATOM   2371 C CG  . PRO A 1 313 ? -9.694  -73.823  -3.124  1.00 93.08  ? 304 PRO A CG  1 
ATOM   2372 C CD  . PRO A 1 313 ? -9.815  -72.647  -4.037  1.00 92.61  ? 304 PRO A CD  1 
ATOM   2373 N N   . LYS A 1 314 ? -12.397 -71.825  -0.149  1.00 93.26  ? 305 LYS A N   1 
ATOM   2374 C CA  . LYS A 1 314 ? -12.363 -71.296  1.209   1.00 95.70  ? 305 LYS A CA  1 
ATOM   2375 C C   . LYS A 1 314 ? -11.369 -72.065  2.088   1.00 93.98  ? 305 LYS A C   1 
ATOM   2376 O O   . LYS A 1 314 ? -11.353 -73.298  2.092   1.00 93.89  ? 305 LYS A O   1 
ATOM   2377 C CB  . LYS A 1 314 ? -13.769 -71.349  1.822   1.00 99.47  ? 305 LYS A CB  1 
ATOM   2378 C CG  . LYS A 1 314 ? -14.881 -70.706  0.977   1.00 104.29 ? 305 LYS A CG  1 
ATOM   2379 C CD  . LYS A 1 314 ? -16.271 -71.146  1.475   1.00 108.29 ? 305 LYS A CD  1 
ATOM   2380 C CE  . LYS A 1 314 ? -17.416 -70.619  0.607   1.00 109.27 ? 305 LYS A CE  1 
ATOM   2381 N NZ  . LYS A 1 314 ? -18.730 -71.259  0.947   1.00 110.02 ? 305 LYS A NZ  1 
ATOM   2382 N N   . TYR A 1 315 ? -10.535 -71.339  2.828   1.00 91.50  ? 306 TYR A N   1 
ATOM   2383 C CA  . TYR A 1 315 ? -9.554  -71.999  3.681   1.00 91.46  ? 306 TYR A CA  1 
ATOM   2384 C C   . TYR A 1 315 ? -10.199 -72.581  4.932   1.00 90.33  ? 306 TYR A C   1 
ATOM   2385 O O   . TYR A 1 315 ? -11.171 -72.039  5.453   1.00 90.78  ? 306 TYR A O   1 
ATOM   2386 C CB  . TYR A 1 315 ? -8.391  -71.077  4.067   1.00 88.02  ? 306 TYR A CB  1 
ATOM   2387 C CG  . TYR A 1 315 ? -7.528  -71.697  5.144   1.00 85.06  ? 306 TYR A CG  1 
ATOM   2388 C CD1 . TYR A 1 315 ? -6.540  -72.620  4.827   1.00 86.16  ? 306 TYR A CD1 1 
ATOM   2389 C CD2 . TYR A 1 315 ? -7.738  -71.401  6.477   1.00 83.87  ? 306 TYR A CD2 1 
ATOM   2390 C CE1 . TYR A 1 315 ? -5.771  -73.206  5.808   1.00 83.98  ? 306 TYR A CE1 1 
ATOM   2391 C CE2 . TYR A 1 315 ? -6.978  -71.982  7.461   1.00 86.90  ? 306 TYR A CE2 1 
ATOM   2392 C CZ  . TYR A 1 315 ? -5.999  -72.883  7.122   1.00 84.80  ? 306 TYR A CZ  1 
ATOM   2393 O OH  . TYR A 1 315 ? -5.249  -73.456  8.116   1.00 86.34  ? 306 TYR A OH  1 
ATOM   2394 N N   . VAL A 1 316 ? -9.641  -73.690  5.405   1.00 88.77  ? 307 VAL A N   1 
ATOM   2395 C CA  . VAL A 1 316 ? -10.168 -74.390  6.560   1.00 89.91  ? 307 VAL A CA  1 
ATOM   2396 C C   . VAL A 1 316 ? -9.049  -75.073  7.335   1.00 92.05  ? 307 VAL A C   1 
ATOM   2397 O O   . VAL A 1 316 ? -8.112  -75.609  6.745   1.00 91.43  ? 307 VAL A O   1 
ATOM   2398 C CB  . VAL A 1 316 ? -11.204 -75.428  6.126   1.00 91.00  ? 307 VAL A CB  1 
ATOM   2399 C CG1 . VAL A 1 316 ? -11.147 -76.645  7.025   1.00 95.79  ? 307 VAL A CG1 1 
ATOM   2400 C CG2 . VAL A 1 316 ? -12.590 -74.807  6.110   1.00 89.20  ? 307 VAL A CG2 1 
ATOM   2401 N N   . LYS A 1 317 ? -9.158  -75.059  8.659   1.00 94.55  ? 308 LYS A N   1 
ATOM   2402 C CA  . LYS A 1 317 ? -8.103  -75.577  9.519   1.00 96.65  ? 308 LYS A CA  1 
ATOM   2403 C C   . LYS A 1 317 ? -8.289  -77.045  9.900   1.00 103.28 ? 308 LYS A C   1 
ATOM   2404 O O   . LYS A 1 317 ? -7.467  -77.613  10.618  1.00 106.71 ? 308 LYS A O   1 
ATOM   2405 C CB  . LYS A 1 317 ? -7.978  -74.712  10.775  1.00 100.11 ? 308 LYS A CB  1 
ATOM   2406 C CG  . LYS A 1 317 ? -9.296  -74.443  11.503  1.00 107.48 ? 308 LYS A CG  1 
ATOM   2407 C CD  . LYS A 1 317 ? -9.680  -75.575  12.462  1.00 113.26 ? 308 LYS A CD  1 
ATOM   2408 C CE  . LYS A 1 317 ? -10.489 -75.046  13.652  1.00 117.11 ? 308 LYS A CE  1 
ATOM   2409 N NZ  . LYS A 1 317 ? -10.915 -76.108  14.616  1.00 114.59 ? 308 LYS A NZ  1 
ATOM   2410 N N   . SER A 1 318 ? -9.368  -77.658  9.424   1.00 104.72 ? 309 SER A N   1 
ATOM   2411 C CA  . SER A 1 318 ? -9.636  -79.066  9.716   1.00 107.36 ? 309 SER A CA  1 
ATOM   2412 C C   . SER A 1 318 ? -8.666  -79.971  8.967   1.00 106.72 ? 309 SER A C   1 
ATOM   2413 O O   . SER A 1 318 ? -8.176  -79.622  7.890   1.00 105.95 ? 309 SER A O   1 
ATOM   2414 C CB  . SER A 1 318 ? -11.061 -79.438  9.320   1.00 107.47 ? 309 SER A CB  1 
ATOM   2415 O OG  . SER A 1 318 ? -11.125 -79.707  7.931   1.00 106.24 ? 309 SER A OG  1 
ATOM   2416 N N   . THR A 1 319 ? -8.388  -81.134  9.546   1.00 109.35 ? 310 THR A N   1 
ATOM   2417 C CA  . THR A 1 319 ? -7.497  -82.106  8.926   1.00 109.71 ? 310 THR A CA  1 
ATOM   2418 C C   . THR A 1 319 ? -8.122  -82.719  7.684   1.00 107.96 ? 310 THR A C   1 
ATOM   2419 O O   . THR A 1 319 ? -7.584  -82.614  6.583   1.00 108.68 ? 310 THR A O   1 
ATOM   2420 C CB  . THR A 1 319 ? -7.199  -83.256  9.892   1.00 111.24 ? 310 THR A CB  1 
ATOM   2421 O OG1 . THR A 1 319 ? -8.391  -84.029  10.075  1.00 112.97 ? 310 THR A OG1 1 
ATOM   2422 C CG2 . THR A 1 319 ? -6.737  -82.716  11.243  1.00 113.59 ? 310 THR A CG2 1 
ATOM   2423 N N   . LYS A 1 320 ? -9.276  -83.350  7.872   1.00 108.55 ? 311 LYS A N   1 
ATOM   2424 C CA  . LYS A 1 320 ? -9.937  -84.062  6.788   1.00 111.16 ? 311 LYS A CA  1 
ATOM   2425 C C   . LYS A 1 320 ? -11.445 -83.917  6.876   1.00 112.55 ? 311 LYS A C   1 
ATOM   2426 O O   . LYS A 1 320 ? -12.036 -84.032  7.954   1.00 112.75 ? 311 LYS A O   1 
ATOM   2427 C CB  . LYS A 1 320 ? -9.561  -85.554  6.788   1.00 111.53 ? 311 LYS A CB  1 
ATOM   2428 C CG  . LYS A 1 320 ? -10.125 -86.360  7.960   1.00 113.78 ? 311 LYS A CG  1 
ATOM   2429 C CD  . LYS A 1 320 ? -9.792  -87.855  7.854   1.00 115.52 ? 311 LYS A CD  1 
ATOM   2430 C CE  . LYS A 1 320 ? -10.795 -88.614  6.992   1.00 113.20 ? 311 LYS A CE  1 
ATOM   2431 N NZ  . LYS A 1 320 ? -10.470 -90.069  6.915   1.00 112.46 ? 311 LYS A NZ  1 
ATOM   2432 N N   . LEU A 1 321 ? -12.059 -83.640  5.734   1.00 112.12 ? 312 LEU A N   1 
ATOM   2433 C CA  . LEU A 1 321 ? -13.503 -83.698  5.621   1.00 112.41 ? 312 LEU A CA  1 
ATOM   2434 C C   . LEU A 1 321 ? -13.880 -84.778  4.630   1.00 114.23 ? 312 LEU A C   1 
ATOM   2435 O O   . LEU A 1 321 ? -13.713 -84.606  3.422   1.00 113.41 ? 312 LEU A O   1 
ATOM   2436 C CB  . LEU A 1 321 ? -14.048 -82.355  5.157   1.00 111.64 ? 312 LEU A CB  1 
ATOM   2437 C CG  . LEU A 1 321 ? -14.634 -81.506  6.277   1.00 111.88 ? 312 LEU A CG  1 
ATOM   2438 C CD1 . LEU A 1 321 ? -16.111 -81.311  6.027   1.00 110.38 ? 312 LEU A CD1 1 
ATOM   2439 C CD2 . LEU A 1 321 ? -14.390 -82.164  7.632   1.00 113.34 ? 312 LEU A CD2 1 
ATOM   2440 N N   . ARG A 1 322 ? -14.406 -85.885  5.142   1.00 116.71 ? 313 ARG A N   1 
ATOM   2441 C CA  . ARG A 1 322 ? -14.805 -86.996  4.290   1.00 117.53 ? 313 ARG A CA  1 
ATOM   2442 C C   . ARG A 1 322 ? -16.230 -87.444  4.602   1.00 117.74 ? 313 ARG A C   1 
ATOM   2443 O O   . ARG A 1 322 ? -16.516 -87.955  5.690   1.00 117.19 ? 313 ARG A O   1 
ATOM   2444 C CB  . ARG A 1 322 ? -13.817 -88.165  4.420   1.00 117.20 ? 313 ARG A CB  1 
ATOM   2445 C CG  . ARG A 1 322 ? -13.229 -88.635  3.089   1.00 115.14 ? 313 ARG A CG  1 
ATOM   2446 C CD  . ARG A 1 322 ? -11.998 -89.503  3.287   1.00 115.66 ? 313 ARG A CD  1 
ATOM   2447 N NE  . ARG A 1 322 ? -11.312 -89.768  2.026   1.00 116.26 ? 313 ARG A NE  1 
ATOM   2448 C CZ  . ARG A 1 322 ? -10.118 -90.348  1.933   1.00 116.53 ? 313 ARG A CZ  1 
ATOM   2449 N NH1 . ARG A 1 322 ? -9.472  -90.726  3.028   1.00 114.50 ? 313 ARG A NH1 1 
ATOM   2450 N NH2 . ARG A 1 322 ? -9.565  -90.549  0.744   1.00 112.90 ? 313 ARG A NH2 1 
ATOM   2451 N N   . LEU A 1 323 ? -17.119 -87.239  3.635   1.00 115.69 ? 314 LEU A N   1 
ATOM   2452 C CA  . LEU A 1 323 ? -18.487 -87.722  3.728   1.00 115.44 ? 314 LEU A CA  1 
ATOM   2453 C C   . LEU A 1 323 ? -18.555 -89.179  3.308   1.00 118.24 ? 314 LEU A C   1 
ATOM   2454 O O   . LEU A 1 323 ? -17.530 -89.842  3.159   1.00 118.01 ? 314 LEU A O   1 
ATOM   2455 C CB  . LEU A 1 323 ? -19.422 -86.899  2.846   1.00 115.95 ? 314 LEU A CB  1 
ATOM   2456 C CG  . LEU A 1 323 ? -20.133 -85.715  3.494   1.00 116.36 ? 314 LEU A CG  1 
ATOM   2457 C CD1 . LEU A 1 323 ? -21.251 -85.241  2.582   1.00 117.76 ? 314 LEU A CD1 1 
ATOM   2458 C CD2 . LEU A 1 323 ? -20.681 -86.097  4.856   1.00 115.83 ? 314 LEU A CD2 1 
ATOM   2459 N N   . ALA A 1 324 ? -19.774 -89.675  3.130   1.00 120.83 ? 315 ALA A N   1 
ATOM   2460 C CA  . ALA A 1 324 ? -19.982 -91.054  2.713   1.00 120.11 ? 315 ALA A CA  1 
ATOM   2461 C C   . ALA A 1 324 ? -21.012 -91.150  1.589   1.00 122.65 ? 315 ALA A C   1 
ATOM   2462 O O   . ALA A 1 324 ? -22.170 -90.780  1.766   1.00 125.03 ? 315 ALA A O   1 
ATOM   2463 C CB  . ALA A 1 324 ? -20.402 -91.905  3.905   1.00 117.88 ? 315 ALA A CB  1 
ATOM   2464 N N   . THR A 1 325 ? -20.583 -91.633  0.428   1.00 121.56 ? 316 THR A N   1 
ATOM   2465 C CA  . THR A 1 325 ? -21.515 -91.924  -0.654  1.00 123.83 ? 316 THR A CA  1 
ATOM   2466 C C   . THR A 1 325 ? -22.192 -93.280  -0.442  1.00 124.66 ? 316 THR A C   1 
ATOM   2467 O O   . THR A 1 325 ? -23.340 -93.476  -0.844  1.00 125.62 ? 316 THR A O   1 
ATOM   2468 C CB  . THR A 1 325 ? -20.821 -91.904  -2.034  1.00 123.83 ? 316 THR A CB  1 
ATOM   2469 O OG1 . THR A 1 325 ? -19.440 -91.557  -1.874  1.00 122.31 ? 316 THR A OG1 1 
ATOM   2470 C CG2 . THR A 1 325 ? -21.491 -90.893  -2.961  1.00 121.69 ? 316 THR A CG2 1 
ATOM   2471 N N   . GLY A 1 326 ? -21.490 -94.194  0.225   1.00 123.41 ? 317 GLY A N   1 
ATOM   2472 C CA  . GLY A 1 326 ? -21.911 -95.582  0.293   1.00 123.49 ? 317 GLY A CA  1 
ATOM   2473 C C   . GLY A 1 326 ? -21.450 -96.308  1.542   1.00 124.20 ? 317 GLY A C   1 
ATOM   2474 O O   . GLY A 1 326 ? -20.899 -95.701  2.456   1.00 124.44 ? 317 GLY A O   1 
ATOM   2475 N N   . LEU A 1 327 ? -21.690 -97.614  1.576   1.00 124.38 ? 318 LEU A N   1 
ATOM   2476 C CA  . LEU A 1 327 ? -21.536 -98.424  2.783   1.00 123.25 ? 318 LEU A CA  1 
ATOM   2477 C C   . LEU A 1 327 ? -20.098 -98.815  3.132   1.00 122.78 ? 318 LEU A C   1 
ATOM   2478 O O   . LEU A 1 327 ? -19.154 -98.474  2.418   1.00 123.21 ? 318 LEU A O   1 
ATOM   2479 C CB  . LEU A 1 327 ? -22.390 -99.686  2.656   1.00 124.98 ? 318 LEU A CB  1 
ATOM   2480 C CG  . LEU A 1 327 ? -22.641 -100.201 1.234   1.00 126.37 ? 318 LEU A CG  1 
ATOM   2481 C CD1 . LEU A 1 327 ? -22.945 -101.695 1.230   1.00 125.72 ? 318 LEU A CD1 1 
ATOM   2482 C CD2 . LEU A 1 327 ? -23.765 -99.422  0.556   1.00 126.55 ? 318 LEU A CD2 1 
ATOM   2483 N N   . ARG A 1 328 ? -19.953 -99.553  4.234   1.00 120.64 ? 319 ARG A N   1 
ATOM   2484 C CA  . ARG A 1 328 ? -18.657 -100.060 4.674   1.00 120.76 ? 319 ARG A CA  1 
ATOM   2485 C C   . ARG A 1 328 ? -18.257 -101.178 3.729   1.00 122.65 ? 319 ARG A C   1 
ATOM   2486 O O   . ARG A 1 328 ? -18.929 -101.415 2.724   1.00 122.90 ? 319 ARG A O   1 
ATOM   2487 C CB  . ARG A 1 328 ? -18.745 -100.625 6.098   1.00 117.22 ? 319 ARG A CB  1 
ATOM   2488 C CG  . ARG A 1 328 ? -19.494 -99.759  7.099   1.00 115.80 ? 319 ARG A CG  1 
ATOM   2489 C CD  . ARG A 1 328 ? -19.544 -100.421 8.476   1.00 113.85 ? 319 ARG A CD  1 
ATOM   2490 N NE  . ARG A 1 328 ? -20.193 -99.574  9.477   1.00 113.69 ? 319 ARG A NE  1 
ATOM   2491 C CZ  . ARG A 1 328 ? -21.114 -99.997  10.337  1.00 112.65 ? 319 ARG A CZ  1 
ATOM   2492 N NH1 . ARG A 1 328 ? -21.504 -101.266 10.326  1.00 115.90 ? 319 ARG A NH1 1 
ATOM   2493 N NH2 . ARG A 1 328 ? -21.648 -99.153  11.210  1.00 108.71 ? 319 ARG A NH2 1 
ATOM   2494 N N   . ASN A 1 329 ? -17.157 -101.857 4.034   1.00 124.66 ? 320 ASN A N   1 
ATOM   2495 C CA  . ASN A 1 329 ? -16.833 -103.079 3.307   1.00 127.25 ? 320 ASN A CA  1 
ATOM   2496 C C   . ASN A 1 329 ? -15.979 -104.087 4.070   1.00 127.46 ? 320 ASN A C   1 
ATOM   2497 O O   . ASN A 1 329 ? -15.227 -103.732 4.982   1.00 126.21 ? 320 ASN A O   1 
ATOM   2498 C CB  . ASN A 1 329 ? -16.228 -102.771 1.934   1.00 125.11 ? 320 ASN A CB  1 
ATOM   2499 C CG  . ASN A 1 329 ? -15.119 -101.756 1.997   1.00 120.21 ? 320 ASN A CG  1 
ATOM   2500 O OD1 . ASN A 1 329 ? -15.123 -100.866 2.845   1.00 119.44 ? 320 ASN A OD1 1 
ATOM   2501 N ND2 . ASN A 1 329 ? -14.159 -101.879 1.092   1.00 121.19 ? 320 ASN A ND2 1 
ATOM   2502 N N   . VAL A 1 330 ? -16.120 -105.350 3.678   1.00 129.59 ? 321 VAL A N   1 
ATOM   2503 C CA  . VAL A 1 330 ? -15.337 -106.445 4.241   1.00 133.38 ? 321 VAL A CA  1 
ATOM   2504 C C   . VAL A 1 330 ? -14.827 -107.382 3.146   1.00 134.23 ? 321 VAL A C   1 
ATOM   2505 O O   . VAL A 1 330 ? -15.184 -107.243 1.975   1.00 132.63 ? 321 VAL A O   1 
ATOM   2506 C CB  . VAL A 1 330 ? -16.162 -107.271 5.241   1.00 132.70 ? 321 VAL A CB  1 
ATOM   2507 C CG1 . VAL A 1 330 ? -15.408 -108.541 5.637   1.00 134.88 ? 321 VAL A CG1 1 
ATOM   2508 C CG2 . VAL A 1 330 ? -16.513 -106.430 6.462   1.00 131.93 ? 321 VAL A CG2 1 
ATOM   2509 N N   . ILE B 2 10  ? -26.368 -109.859 8.212   1.00 116.45 ? 10  ILE B N   1 
ATOM   2510 C CA  . ILE B 2 10  ? -25.490 -110.673 7.378   1.00 113.98 ? 10  ILE B CA  1 
ATOM   2511 C C   . ILE B 2 10  ? -24.025 -110.379 7.688   1.00 117.19 ? 10  ILE B C   1 
ATOM   2512 O O   . ILE B 2 10  ? -23.644 -109.233 7.928   1.00 117.85 ? 10  ILE B O   1 
ATOM   2513 C CB  . ILE B 2 10  ? -25.772 -110.457 5.886   1.00 111.15 ? 10  ILE B CB  1 
ATOM   2514 C CG1 . ILE B 2 10  ? -24.615 -109.723 5.218   1.00 113.10 ? 10  ILE B CG1 1 
ATOM   2515 C CG2 . ILE B 2 10  ? -27.086 -109.703 5.691   1.00 107.78 ? 10  ILE B CG2 1 
ATOM   2516 C CD1 . ILE B 2 10  ? -24.826 -109.546 3.742   1.00 116.83 ? 10  ILE B CD1 1 
ATOM   2517 N N   . GLU B 2 11  ? -23.206 -111.423 7.672   1.00 118.08 ? 11  GLU B N   1 
ATOM   2518 C CA  . GLU B 2 11  ? -21.868 -111.352 8.249   1.00 121.58 ? 11  GLU B CA  1 
ATOM   2519 C C   . GLU B 2 11  ? -20.776 -110.901 7.275   1.00 122.23 ? 11  GLU B C   1 
ATOM   2520 O O   . GLU B 2 11  ? -19.593 -110.914 7.618   1.00 122.82 ? 11  GLU B O   1 
ATOM   2521 C CB  . GLU B 2 11  ? -21.490 -112.693 8.898   1.00 122.19 ? 11  GLU B CB  1 
ATOM   2522 C CG  . GLU B 2 11  ? -20.835 -112.571 10.276  1.00 120.76 ? 11  GLU B CG  1 
ATOM   2523 C CD  . GLU B 2 11  ? -21.840 -112.348 11.396  1.00 124.64 ? 11  GLU B CD  1 
ATOM   2524 O OE1 . GLU B 2 11  ? -22.324 -113.350 11.965  1.00 128.13 ? 11  GLU B OE1 1 
ATOM   2525 O OE2 . GLU B 2 11  ? -22.139 -111.176 11.716  1.00 122.66 ? 11  GLU B OE2 1 
ATOM   2526 N N   . GLY B 2 12  ? -21.155 -110.515 6.063   1.00 121.54 ? 12  GLY B N   1 
ATOM   2527 C CA  . GLY B 2 12  ? -20.161 -110.057 5.108   1.00 123.39 ? 12  GLY B CA  1 
ATOM   2528 C C   . GLY B 2 12  ? -20.709 -109.375 3.870   1.00 125.16 ? 12  GLY B C   1 
ATOM   2529 O O   . GLY B 2 12  ? -21.918 -109.366 3.632   1.00 126.05 ? 12  GLY B O   1 
ATOM   2530 N N   . GLY B 2 13  ? -19.802 -108.797 3.085   1.00 123.76 ? 13  GLY B N   1 
ATOM   2531 C CA  . GLY B 2 13  ? -20.148 -108.162 1.828   1.00 124.57 ? 13  GLY B CA  1 
ATOM   2532 C C   . GLY B 2 13  ? -19.777 -109.039 0.652   1.00 126.25 ? 13  GLY B C   1 
ATOM   2533 O O   . GLY B 2 13  ? -19.278 -110.153 0.831   1.00 126.25 ? 13  GLY B O   1 
ATOM   2534 N N   . TRP B 2 14  ? -20.004 -108.538 -0.557  1.00 127.41 ? 14  TRP B N   1 
ATOM   2535 C CA  . TRP B 2 14  ? -19.740 -109.325 -1.760  1.00 128.37 ? 14  TRP B CA  1 
ATOM   2536 C C   . TRP B 2 14  ? -18.758 -108.669 -2.728  1.00 130.16 ? 14  TRP B C   1 
ATOM   2537 O O   . TRP B 2 14  ? -19.082 -107.665 -3.371  1.00 129.00 ? 14  TRP B O   1 
ATOM   2538 C CB  . TRP B 2 14  ? -21.049 -109.613 -2.492  1.00 126.32 ? 14  TRP B CB  1 
ATOM   2539 C CG  . TRP B 2 14  ? -21.924 -110.602 -1.811  1.00 122.42 ? 14  TRP B CG  1 
ATOM   2540 C CD1 . TRP B 2 14  ? -21.586 -111.444 -0.788  1.00 123.28 ? 14  TRP B CD1 1 
ATOM   2541 C CD2 . TRP B 2 14  ? -23.293 -110.851 -2.103  1.00 118.56 ? 14  TRP B CD2 1 
ATOM   2542 N NE1 . TRP B 2 14  ? -22.671 -112.205 -0.429  1.00 120.60 ? 14  TRP B NE1 1 
ATOM   2543 C CE2 . TRP B 2 14  ? -23.733 -111.858 -1.224  1.00 119.02 ? 14  TRP B CE2 1 
ATOM   2544 C CE3 . TRP B 2 14  ? -24.193 -110.317 -3.027  1.00 118.93 ? 14  TRP B CE3 1 
ATOM   2545 C CZ2 . TRP B 2 14  ? -25.034 -112.341 -1.242  1.00 118.24 ? 14  TRP B CZ2 1 
ATOM   2546 C CZ3 . TRP B 2 14  ? -25.479 -110.792 -3.046  1.00 117.86 ? 14  TRP B CZ3 1 
ATOM   2547 C CH2 . TRP B 2 14  ? -25.892 -111.796 -2.160  1.00 119.05 ? 14  TRP B CH2 1 
ATOM   2548 N N   . THR B 2 15  ? -17.575 -109.268 -2.857  1.00 132.36 ? 15  THR B N   1 
ATOM   2549 C CA  . THR B 2 15  ? -16.562 -108.774 -3.786  1.00 131.67 ? 15  THR B CA  1 
ATOM   2550 C C   . THR B 2 15  ? -17.112 -108.829 -5.211  1.00 130.51 ? 15  THR B C   1 
ATOM   2551 O O   . THR B 2 15  ? -16.797 -107.982 -6.050  1.00 129.20 ? 15  THR B O   1 
ATOM   2552 C CB  . THR B 2 15  ? -15.210 -109.562 -3.671  1.00 128.70 ? 15  THR B CB  1 
ATOM   2553 O OG1 . THR B 2 15  ? -15.159 -110.628 -4.630  1.00 124.97 ? 15  THR B OG1 1 
ATOM   2554 C CG2 . THR B 2 15  ? -15.023 -110.139 -2.267  1.00 126.20 ? 15  THR B CG2 1 
ATOM   2555 N N   . GLY B 2 16  ? -17.971 -109.814 -5.459  1.00 128.34 ? 16  GLY B N   1 
ATOM   2556 C CA  . GLY B 2 16  ? -18.472 -110.082 -6.794  1.00 128.20 ? 16  GLY B CA  1 
ATOM   2557 C C   . GLY B 2 16  ? -19.661 -109.249 -7.232  1.00 127.59 ? 16  GLY B C   1 
ATOM   2558 O O   . GLY B 2 16  ? -20.065 -109.310 -8.395  1.00 125.71 ? 16  GLY B O   1 
ATOM   2559 N N   . MET B 2 17  ? -20.232 -108.477 -6.312  1.00 128.26 ? 17  MET B N   1 
ATOM   2560 C CA  . MET B 2 17  ? -21.334 -107.595 -6.673  1.00 128.06 ? 17  MET B CA  1 
ATOM   2561 C C   . MET B 2 17  ? -20.846 -106.610 -7.731  1.00 126.88 ? 17  MET B C   1 
ATOM   2562 O O   . MET B 2 17  ? -19.692 -106.186 -7.708  1.00 127.18 ? 17  MET B O   1 
ATOM   2563 C CB  . MET B 2 17  ? -21.878 -106.856 -5.449  1.00 127.99 ? 17  MET B CB  1 
ATOM   2564 C CG  . MET B 2 17  ? -23.131 -106.032 -5.735  1.00 131.33 ? 17  MET B CG  1 
ATOM   2565 S SD  . MET B 2 17  ? -24.558 -107.014 -6.260  1.00 133.77 ? 17  MET B SD  1 
ATOM   2566 C CE  . MET B 2 17  ? -25.109 -107.690 -4.696  1.00 126.60 ? 17  MET B CE  1 
ATOM   2567 N N   . VAL B 2 18  ? -21.723 -106.252 -8.661  1.00 126.26 ? 18  VAL B N   1 
ATOM   2568 C CA  . VAL B 2 18  ? -21.315 -105.452 -9.811  1.00 128.86 ? 18  VAL B CA  1 
ATOM   2569 C C   . VAL B 2 18  ? -22.189 -104.217 -10.067 1.00 126.32 ? 18  VAL B C   1 
ATOM   2570 O O   . VAL B 2 18  ? -21.748 -103.081 -9.886  1.00 121.51 ? 18  VAL B O   1 
ATOM   2571 C CB  . VAL B 2 18  ? -21.273 -106.327 -11.093 1.00 129.54 ? 18  VAL B CB  1 
ATOM   2572 C CG1 . VAL B 2 18  ? -19.844 -106.756 -11.415 1.00 126.60 ? 18  VAL B CG1 1 
ATOM   2573 C CG2 . VAL B 2 18  ? -22.187 -107.544 -10.939 1.00 125.54 ? 18  VAL B CG2 1 
ATOM   2574 N N   . ASP B 2 19  ? -23.430 -104.455 -10.479 1.00 128.31 ? 19  ASP B N   1 
ATOM   2575 C CA  . ASP B 2 19  ? -24.311 -103.403 -10.983 1.00 129.49 ? 19  ASP B CA  1 
ATOM   2576 C C   . ASP B 2 19  ? -24.706 -102.347 -9.952  1.00 129.90 ? 19  ASP B C   1 
ATOM   2577 O O   . ASP B 2 19  ? -25.242 -101.297 -10.317 1.00 128.70 ? 19  ASP B O   1 
ATOM   2578 C CB  . ASP B 2 19  ? -25.587 -104.016 -11.581 1.00 133.26 ? 19  ASP B CB  1 
ATOM   2579 C CG  . ASP B 2 19  ? -25.305 -104.935 -12.755 1.00 135.99 ? 19  ASP B CG  1 
ATOM   2580 O OD1 . ASP B 2 19  ? -24.158 -105.413 -12.874 1.00 136.65 ? 19  ASP B OD1 1 
ATOM   2581 O OD2 . ASP B 2 19  ? -26.234 -105.181 -13.556 1.00 136.19 ? 19  ASP B OD2 1 
ATOM   2582 N N   . GLY B 2 20  ? -24.461 -102.619 -8.671  1.00 131.86 ? 20  GLY B N   1 
ATOM   2583 C CA  . GLY B 2 20  ? -24.931 -101.723 -7.626  1.00 132.18 ? 20  GLY B CA  1 
ATOM   2584 C C   . GLY B 2 20  ? -24.472 -101.994 -6.203  1.00 129.47 ? 20  GLY B C   1 
ATOM   2585 O O   . GLY B 2 20  ? -23.585 -102.815 -5.960  1.00 126.25 ? 20  GLY B O   1 
ATOM   2586 N N   . TRP B 2 21  ? -25.087 -101.287 -5.257  1.00 129.28 ? 21  TRP B N   1 
ATOM   2587 C CA  . TRP B 2 21  ? -24.699 -101.375 -3.853  1.00 129.86 ? 21  TRP B CA  1 
ATOM   2588 C C   . TRP B 2 21  ? -25.171 -102.685 -3.214  1.00 128.28 ? 21  TRP B C   1 
ATOM   2589 O O   . TRP B 2 21  ? -24.425 -103.321 -2.464  1.00 124.79 ? 21  TRP B O   1 
ATOM   2590 C CB  . TRP B 2 21  ? -25.232 -100.170 -3.062  1.00 132.18 ? 21  TRP B CB  1 
ATOM   2591 C CG  . TRP B 2 21  ? -24.337 -98.929  -3.043  1.00 134.30 ? 21  TRP B CG  1 
ATOM   2592 C CD1 . TRP B 2 21  ? -22.994 -98.879  -2.772  1.00 133.10 ? 21  TRP B CD1 1 
ATOM   2593 C CD2 . TRP B 2 21  ? -24.748 -97.566  -3.254  1.00 133.93 ? 21  TRP B CD2 1 
ATOM   2594 N NE1 . TRP B 2 21  ? -22.546 -97.578  -2.824  1.00 131.17 ? 21  TRP B NE1 1 
ATOM   2595 C CE2 . TRP B 2 21  ? -23.602 -96.754  -3.116  1.00 131.95 ? 21  TRP B CE2 1 
ATOM   2596 C CE3 . TRP B 2 21  ? -25.971 -96.958  -3.555  1.00 132.91 ? 21  TRP B CE3 1 
ATOM   2597 C CZ2 . TRP B 2 21  ? -23.646 -95.369  -3.271  1.00 130.04 ? 21  TRP B CZ2 1 
ATOM   2598 C CZ3 . TRP B 2 21  ? -26.011 -95.584  -3.704  1.00 130.58 ? 21  TRP B CZ3 1 
ATOM   2599 C CH2 . TRP B 2 21  ? -24.858 -94.805  -3.565  1.00 130.30 ? 21  TRP B CH2 1 
ATOM   2600 N N   . TYR B 2 22  ? -26.408 -103.084 -3.513  1.00 130.09 ? 22  TYR B N   1 
ATOM   2601 C CA  . TYR B 2 22  ? -26.969 -104.314 -2.948  1.00 128.46 ? 22  TYR B CA  1 
ATOM   2602 C C   . TYR B 2 22  ? -27.976 -105.047 -3.842  1.00 125.64 ? 22  TYR B C   1 
ATOM   2603 O O   . TYR B 2 22  ? -28.557 -104.466 -4.761  1.00 124.71 ? 22  TYR B O   1 
ATOM   2604 C CB  . TYR B 2 22  ? -27.583 -104.054 -1.569  1.00 129.53 ? 22  TYR B CB  1 
ATOM   2605 C CG  . TYR B 2 22  ? -28.186 -102.675 -1.384  1.00 130.13 ? 22  TYR B CG  1 
ATOM   2606 C CD1 . TYR B 2 22  ? -29.266 -102.250 -2.155  1.00 128.74 ? 22  TYR B CD1 1 
ATOM   2607 C CD2 . TYR B 2 22  ? -27.676 -101.799 -0.428  1.00 126.82 ? 22  TYR B CD2 1 
ATOM   2608 C CE1 . TYR B 2 22  ? -29.818 -100.989 -1.976  1.00 130.18 ? 22  TYR B CE1 1 
ATOM   2609 C CE2 . TYR B 2 22  ? -28.221 -100.540 -0.242  1.00 123.87 ? 22  TYR B CE2 1 
ATOM   2610 C CZ  . TYR B 2 22  ? -29.289 -100.138 -1.015  1.00 128.79 ? 22  TYR B CZ  1 
ATOM   2611 O OH  . TYR B 2 22  ? -29.824 -98.882  -0.819  1.00 126.95 ? 22  TYR B OH  1 
ATOM   2612 N N   . GLY B 2 23  ? -28.186 -106.325 -3.532  1.00 123.98 ? 23  GLY B N   1 
ATOM   2613 C CA  . GLY B 2 23  ? -28.991 -107.215 -4.350  1.00 121.75 ? 23  GLY B CA  1 
ATOM   2614 C C   . GLY B 2 23  ? -28.889 -108.654 -3.872  1.00 117.89 ? 23  GLY B C   1 
ATOM   2615 O O   . GLY B 2 23  ? -28.596 -108.906 -2.701  1.00 116.00 ? 23  GLY B O   1 
ATOM   2616 N N   . TYR B 2 24  ? -29.131 -109.601 -4.775  1.00 117.33 ? 24  TYR B N   1 
ATOM   2617 C CA  . TYR B 2 24  ? -29.141 -111.020 -4.418  1.00 115.69 ? 24  TYR B CA  1 
ATOM   2618 C C   . TYR B 2 24  ? -28.198 -111.893 -5.267  1.00 116.97 ? 24  TYR B C   1 
ATOM   2619 O O   . TYR B 2 24  ? -27.861 -111.542 -6.399  1.00 118.78 ? 24  TYR B O   1 
ATOM   2620 C CB  . TYR B 2 24  ? -30.565 -111.567 -4.501  1.00 113.09 ? 24  TYR B CB  1 
ATOM   2621 C CG  . TYR B 2 24  ? -31.639 -110.515 -4.692  1.00 112.40 ? 24  TYR B CG  1 
ATOM   2622 C CD1 . TYR B 2 24  ? -31.816 -109.888 -5.918  1.00 112.04 ? 24  TYR B CD1 1 
ATOM   2623 C CD2 . TYR B 2 24  ? -32.495 -110.172 -3.654  1.00 112.47 ? 24  TYR B CD2 1 
ATOM   2624 C CE1 . TYR B 2 24  ? -32.802 -108.937 -6.100  1.00 111.56 ? 24  TYR B CE1 1 
ATOM   2625 C CE2 . TYR B 2 24  ? -33.486 -109.223 -3.828  1.00 111.19 ? 24  TYR B CE2 1 
ATOM   2626 C CZ  . TYR B 2 24  ? -33.634 -108.609 -5.053  1.00 111.15 ? 24  TYR B CZ  1 
ATOM   2627 O OH  . TYR B 2 24  ? -34.619 -107.665 -5.228  1.00 110.80 ? 24  TYR B OH  1 
ATOM   2628 N N   . HIS B 2 25  ? -27.782 -113.028 -4.704  1.00 117.08 ? 25  HIS B N   1 
ATOM   2629 C CA  . HIS B 2 25  ? -26.923 -114.008 -5.384  1.00 118.49 ? 25  HIS B CA  1 
ATOM   2630 C C   . HIS B 2 25  ? -27.550 -115.390 -5.233  1.00 119.89 ? 25  HIS B C   1 
ATOM   2631 O O   . HIS B 2 25  ? -27.671 -115.905 -4.120  1.00 118.48 ? 25  HIS B O   1 
ATOM   2632 C CB  . HIS B 2 25  ? -25.505 -113.990 -4.787  1.00 118.79 ? 25  HIS B CB  1 
ATOM   2633 C CG  . HIS B 2 25  ? -24.689 -115.223 -5.066  1.00 120.42 ? 25  HIS B CG  1 
ATOM   2634 N ND1 . HIS B 2 25  ? -24.653 -115.840 -6.300  1.00 120.17 ? 25  HIS B ND1 1 
ATOM   2635 C CD2 . HIS B 2 25  ? -23.853 -115.934 -4.270  1.00 118.94 ? 25  HIS B CD2 1 
ATOM   2636 C CE1 . HIS B 2 25  ? -23.842 -116.884 -6.247  1.00 119.35 ? 25  HIS B CE1 1 
ATOM   2637 N NE2 . HIS B 2 25  ? -23.344 -116.963 -5.025  1.00 116.82 ? 25  HIS B NE2 1 
ATOM   2638 N N   . HIS B 2 26  ? -27.945 -115.995 -6.350  1.00 120.77 ? 26  HIS B N   1 
ATOM   2639 C CA  . HIS B 2 26  ? -28.720 -117.229 -6.295  1.00 120.08 ? 26  HIS B CA  1 
ATOM   2640 C C   . HIS B 2 26  ? -28.144 -118.353 -7.144  1.00 120.14 ? 26  HIS B C   1 
ATOM   2641 O O   . HIS B 2 26  ? -27.840 -118.162 -8.322  1.00 119.27 ? 26  HIS B O   1 
ATOM   2642 C CB  . HIS B 2 26  ? -30.169 -116.966 -6.723  1.00 119.62 ? 26  HIS B CB  1 
ATOM   2643 C CG  . HIS B 2 26  ? -30.305 -116.419 -8.112  1.00 121.40 ? 26  HIS B CG  1 
ATOM   2644 N ND1 . HIS B 2 26  ? -29.515 -116.840 -9.162  1.00 123.49 ? 26  HIS B ND1 1 
ATOM   2645 C CD2 . HIS B 2 26  ? -31.149 -115.493 -8.626  1.00 119.02 ? 26  HIS B CD2 1 
ATOM   2646 C CE1 . HIS B 2 26  ? -29.863 -116.191 -10.259 1.00 122.08 ? 26  HIS B CE1 1 
ATOM   2647 N NE2 . HIS B 2 26  ? -30.851 -115.366 -9.961  1.00 119.43 ? 26  HIS B NE2 1 
ATOM   2648 N N   . GLN B 2 27  ? -28.003 -119.527 -6.540  1.00 121.26 ? 27  GLN B N   1 
ATOM   2649 C CA  . GLN B 2 27  ? -27.719 -120.736 -7.305  1.00 125.09 ? 27  GLN B CA  1 
ATOM   2650 C C   . GLN B 2 27  ? -28.947 -121.641 -7.382  1.00 123.71 ? 27  GLN B C   1 
ATOM   2651 O O   . GLN B 2 27  ? -29.372 -122.230 -6.384  1.00 121.09 ? 27  GLN B O   1 
ATOM   2652 C CB  . GLN B 2 27  ? -26.506 -121.504 -6.758  1.00 124.41 ? 27  GLN B CB  1 
ATOM   2653 C CG  . GLN B 2 27  ? -26.346 -121.478 -5.247  1.00 123.53 ? 27  GLN B CG  1 
ATOM   2654 C CD  . GLN B 2 27  ? -25.439 -120.352 -4.776  1.00 124.78 ? 27  GLN B CD  1 
ATOM   2655 O OE1 . GLN B 2 27  ? -25.567 -119.209 -5.219  1.00 124.63 ? 27  GLN B OE1 1 
ATOM   2656 N NE2 . GLN B 2 27  ? -24.510 -120.675 -3.881  1.00 124.10 ? 27  GLN B NE2 1 
ATOM   2657 N N   . ASN B 2 28  ? -29.510 -121.746 -8.582  1.00 124.84 ? 28  ASN B N   1 
ATOM   2658 C CA  . ASN B 2 28  ? -30.648 -122.620 -8.816  1.00 123.09 ? 28  ASN B CA  1 
ATOM   2659 C C   . ASN B 2 28  ? -30.236 -123.785 -9.705  1.00 123.28 ? 28  ASN B C   1 
ATOM   2660 O O   . ASN B 2 28  ? -29.088 -123.856 -10.148 1.00 122.64 ? 28  ASN B O   1 
ATOM   2661 C CB  . ASN B 2 28  ? -31.826 -121.841 -9.425  1.00 122.71 ? 28  ASN B CB  1 
ATOM   2662 C CG  . ASN B 2 28  ? -31.437 -121.037 -10.663 1.00 122.41 ? 28  ASN B CG  1 
ATOM   2663 O OD1 . ASN B 2 28  ? -30.273 -120.683 -10.853 1.00 122.12 ? 28  ASN B OD1 1 
ATOM   2664 N ND2 . ASN B 2 28  ? -32.423 -120.737 -11.505 1.00 120.36 ? 28  ASN B ND2 1 
ATOM   2665 N N   . GLU B 2 29  ? -31.167 -124.697 -9.966  1.00 123.98 ? 29  GLU B N   1 
ATOM   2666 C CA  . GLU B 2 29  ? -30.863 -125.859 -10.787 1.00 125.44 ? 29  GLU B CA  1 
ATOM   2667 C C   . GLU B 2 29  ? -30.329 -125.402 -12.143 1.00 126.52 ? 29  GLU B C   1 
ATOM   2668 O O   . GLU B 2 29  ? -29.640 -126.151 -12.837 1.00 127.53 ? 29  GLU B O   1 
ATOM   2669 C CB  . GLU B 2 29  ? -32.098 -126.747 -10.948 1.00 126.23 ? 29  GLU B CB  1 
ATOM   2670 C CG  . GLU B 2 29  ? -31.846 -128.021 -11.732 1.00 129.54 ? 29  GLU B CG  1 
ATOM   2671 C CD  . GLU B 2 29  ? -31.992 -127.817 -13.227 1.00 136.87 ? 29  GLU B CD  1 
ATOM   2672 O OE1 . GLU B 2 29  ? -32.844 -126.994 -13.630 1.00 135.45 ? 29  GLU B OE1 1 
ATOM   2673 O OE2 . GLU B 2 29  ? -31.256 -128.475 -13.997 1.00 139.75 ? 29  GLU B OE2 1 
ATOM   2674 N N   . GLN B 2 30  ? -30.637 -124.156 -12.496 1.00 125.84 ? 30  GLN B N   1 
ATOM   2675 C CA  . GLN B 2 30  ? -30.108 -123.531 -13.702 1.00 124.98 ? 30  GLN B CA  1 
ATOM   2676 C C   . GLN B 2 30  ? -28.630 -123.183 -13.514 1.00 126.29 ? 30  GLN B C   1 
ATOM   2677 O O   . GLN B 2 30  ? -27.759 -123.766 -14.164 1.00 126.13 ? 30  GLN B O   1 
ATOM   2678 C CB  . GLN B 2 30  ? -30.886 -122.252 -14.035 1.00 122.13 ? 30  GLN B CB  1 
ATOM   2679 C CG  . GLN B 2 30  ? -31.972 -122.397 -15.092 1.00 121.13 ? 30  GLN B CG  1 
ATOM   2680 C CD  . GLN B 2 30  ? -32.419 -121.051 -15.651 1.00 121.87 ? 30  GLN B CD  1 
ATOM   2681 O OE1 . GLN B 2 30  ? -31.704 -120.052 -15.542 1.00 120.11 ? 30  GLN B OE1 1 
ATOM   2682 N NE2 . GLN B 2 30  ? -33.607 -121.019 -16.247 1.00 121.63 ? 30  GLN B NE2 1 
ATOM   2683 N N   . GLY B 2 31  ? -28.357 -122.249 -12.603 1.00 125.99 ? 31  GLY B N   1 
ATOM   2684 C CA  . GLY B 2 31  ? -27.031 -121.665 -12.462 1.00 125.57 ? 31  GLY B CA  1 
ATOM   2685 C C   . GLY B 2 31  ? -26.839 -120.835 -11.201 1.00 126.15 ? 31  GLY B C   1 
ATOM   2686 O O   . GLY B 2 31  ? -27.601 -120.965 -10.244 1.00 125.88 ? 31  GLY B O   1 
ATOM   2687 N N   . SER B 2 32  ? -25.812 -119.985 -11.205 1.00 126.49 ? 32  SER B N   1 
ATOM   2688 C CA  . SER B 2 32  ? -25.387 -119.228 -10.022 1.00 124.50 ? 32  SER B CA  1 
ATOM   2689 C C   . SER B 2 32  ? -25.053 -117.780 -10.385 1.00 124.19 ? 32  SER B C   1 
ATOM   2690 O O   . SER B 2 32  ? -25.376 -117.324 -11.482 1.00 125.41 ? 32  SER B O   1 
ATOM   2691 C CB  . SER B 2 32  ? -24.171 -119.893 -9.365  1.00 123.72 ? 32  SER B CB  1 
ATOM   2692 O OG  . SER B 2 32  ? -23.667 -120.953 -10.162 1.00 124.16 ? 32  SER B OG  1 
ATOM   2693 N N   . GLY B 2 33  ? -24.443 -117.049 -9.454  1.00 123.27 ? 33  GLY B N   1 
ATOM   2694 C CA  . GLY B 2 33  ? -23.951 -115.712 -9.749  1.00 123.86 ? 33  GLY B CA  1 
ATOM   2695 C C   . GLY B 2 33  ? -24.715 -114.538 -9.152  1.00 122.52 ? 33  GLY B C   1 
ATOM   2696 O O   . GLY B 2 33  ? -25.666 -114.725 -8.387  1.00 120.86 ? 33  GLY B O   1 
ATOM   2697 N N   . TYR B 2 34  ? -24.284 -113.323 -9.502  1.00 122.18 ? 34  TYR B N   1 
ATOM   2698 C CA  . TYR B 2 34  ? -24.775 -112.097 -8.863  1.00 118.72 ? 34  TYR B CA  1 
ATOM   2699 C C   . TYR B 2 34  ? -25.731 -111.239 -9.688  1.00 118.85 ? 34  TYR B C   1 
ATOM   2700 O O   . TYR B 2 34  ? -26.004 -111.516 -10.854 1.00 118.01 ? 34  TYR B O   1 
ATOM   2701 C CB  . TYR B 2 34  ? -23.595 -111.238 -8.407  1.00 116.58 ? 34  TYR B CB  1 
ATOM   2702 C CG  . TYR B 2 34  ? -22.683 -111.976 -7.469  1.00 117.73 ? 34  TYR B CG  1 
ATOM   2703 C CD1 . TYR B 2 34  ? -21.800 -112.936 -7.945  1.00 117.71 ? 34  TYR B CD1 1 
ATOM   2704 C CD2 . TYR B 2 34  ? -22.717 -111.732 -6.104  1.00 118.99 ? 34  TYR B CD2 1 
ATOM   2705 C CE1 . TYR B 2 34  ? -20.971 -113.627 -7.090  1.00 118.56 ? 34  TYR B CE1 1 
ATOM   2706 C CE2 . TYR B 2 34  ? -21.889 -112.418 -5.239  1.00 118.48 ? 34  TYR B CE2 1 
ATOM   2707 C CZ  . TYR B 2 34  ? -21.018 -113.362 -5.738  1.00 118.33 ? 34  TYR B CZ  1 
ATOM   2708 O OH  . TYR B 2 34  ? -20.196 -114.045 -4.875  1.00 116.15 ? 34  TYR B OH  1 
ATOM   2709 N N   . ALA B 2 35  ? -26.207 -110.175 -9.052  1.00 119.78 ? 35  ALA B N   1 
ATOM   2710 C CA  . ALA B 2 35  ? -27.165 -109.243 -9.626  1.00 119.16 ? 35  ALA B CA  1 
ATOM   2711 C C   . ALA B 2 35  ? -27.498 -108.256 -8.523  1.00 120.63 ? 35  ALA B C   1 
ATOM   2712 O O   . ALA B 2 35  ? -27.132 -108.468 -7.369  1.00 120.73 ? 35  ALA B O   1 
ATOM   2713 C CB  . ALA B 2 35  ? -28.419 -109.966 -10.078 1.00 117.46 ? 35  ALA B CB  1 
ATOM   2714 N N   . ALA B 2 36  ? -28.188 -107.177 -8.862  1.00 122.23 ? 36  ALA B N   1 
ATOM   2715 C CA  . ALA B 2 36  ? -28.612 -106.232 -7.840  1.00 123.51 ? 36  ALA B CA  1 
ATOM   2716 C C   . ALA B 2 36  ? -29.904 -105.542 -8.240  1.00 125.52 ? 36  ALA B C   1 
ATOM   2717 O O   . ALA B 2 36  ? -30.412 -105.744 -9.343  1.00 125.20 ? 36  ALA B O   1 
ATOM   2718 C CB  . ALA B 2 36  ? -27.521 -105.219 -7.568  1.00 124.05 ? 36  ALA B CB  1 
ATOM   2719 N N   . ASP B 2 37  ? -30.422 -104.705 -7.351  1.00 125.94 ? 37  ASP B N   1 
ATOM   2720 C CA  . ASP B 2 37  ? -31.730 -104.109 -7.570  1.00 129.66 ? 37  ASP B CA  1 
ATOM   2721 C C   . ASP B 2 37  ? -31.643 -102.802 -8.363  1.00 132.52 ? 37  ASP B C   1 
ATOM   2722 O O   . ASP B 2 37  ? -30.556 -102.363 -8.741  1.00 131.71 ? 37  ASP B O   1 
ATOM   2723 C CB  . ASP B 2 37  ? -32.445 -103.901 -6.233  1.00 128.38 ? 37  ASP B CB  1 
ATOM   2724 C CG  . ASP B 2 37  ? -33.940 -104.155 -6.325  1.00 128.44 ? 37  ASP B CG  1 
ATOM   2725 O OD1 . ASP B 2 37  ? -34.365 -104.929 -7.208  1.00 128.98 ? 37  ASP B OD1 1 
ATOM   2726 O OD2 . ASP B 2 37  ? -34.693 -103.586 -5.510  1.00 126.93 ? 37  ASP B OD2 1 
ATOM   2727 N N   . LEU B 2 38  ? -32.799 -102.193 -8.613  1.00 135.03 ? 38  LEU B N   1 
ATOM   2728 C CA  . LEU B 2 38  ? -32.871 -100.957 -9.380  1.00 135.49 ? 38  LEU B CA  1 
ATOM   2729 C C   . LEU B 2 38  ? -33.371 -99.803  -8.522  1.00 135.68 ? 38  LEU B C   1 
ATOM   2730 O O   . LEU B 2 38  ? -32.598 -98.914  -8.165  1.00 137.49 ? 38  LEU B O   1 
ATOM   2731 C CB  . LEU B 2 38  ? -33.767 -101.129 -10.616 1.00 137.72 ? 38  LEU B CB  1 
ATOM   2732 C CG  . LEU B 2 38  ? -33.387 -102.204 -11.645 1.00 138.03 ? 38  LEU B CG  1 
ATOM   2733 C CD1 . LEU B 2 38  ? -34.379 -102.242 -12.810 1.00 134.57 ? 38  LEU B CD1 1 
ATOM   2734 C CD2 . LEU B 2 38  ? -31.967 -101.990 -12.155 1.00 135.73 ? 38  LEU B CD2 1 
ATOM   2735 N N   . LYS B 2 39  ? -34.662 -99.821  -8.197  1.00 135.10 ? 39  LYS B N   1 
ATOM   2736 C CA  . LYS B 2 39  ? -35.283 -98.717  -7.472  1.00 136.82 ? 39  LYS B CA  1 
ATOM   2737 C C   . LYS B 2 39  ? -34.616 -98.516  -6.110  1.00 137.75 ? 39  LYS B C   1 
ATOM   2738 O O   . LYS B 2 39  ? -34.423 -97.380  -5.664  1.00 138.16 ? 39  LYS B O   1 
ATOM   2739 C CB  . LYS B 2 39  ? -36.794 -98.939  -7.328  1.00 134.00 ? 39  LYS B CB  1 
ATOM   2740 C CG  . LYS B 2 39  ? -37.643 -97.707  -7.647  1.00 133.81 ? 39  LYS B CG  1 
ATOM   2741 C CD  . LYS B 2 39  ? -39.090 -98.076  -7.920  1.00 129.98 ? 39  LYS B CD  1 
ATOM   2742 C CE  . LYS B 2 39  ? -39.836 -96.925  -8.583  1.00 126.97 ? 39  LYS B CE  1 
ATOM   2743 N NZ  . LYS B 2 39  ? -39.922 -95.726  -7.696  1.00 123.20 ? 39  LYS B NZ  1 
ATOM   2744 N N   . SER B 2 40  ? -34.285 -99.621  -5.445  1.00 137.94 ? 40  SER B N   1 
ATOM   2745 C CA  . SER B 2 40  ? -33.639 -99.559  -4.134  1.00 138.20 ? 40  SER B CA  1 
ATOM   2746 C C   . SER B 2 40  ? -32.287 -98.850  -4.199  1.00 136.77 ? 40  SER B C   1 
ATOM   2747 O O   . SER B 2 40  ? -31.920 -98.114  -3.283  1.00 136.99 ? 40  SER B O   1 
ATOM   2748 C CB  . SER B 2 40  ? -33.481 -100.957 -3.527  1.00 135.74 ? 40  SER B CB  1 
ATOM   2749 O OG  . SER B 2 40  ? -32.630 -101.769 -4.317  1.00 133.86 ? 40  SER B OG  1 
ATOM   2750 N N   . THR B 2 41  ? -31.544 -99.084  -5.274  1.00 136.10 ? 41  THR B N   1 
ATOM   2751 C CA  . THR B 2 41  ? -30.285 -98.383  -5.484  1.00 135.23 ? 41  THR B CA  1 
ATOM   2752 C C   . THR B 2 41  ? -30.542 -96.977  -6.046  1.00 136.10 ? 41  THR B C   1 
ATOM   2753 O O   . THR B 2 41  ? -29.824 -96.028  -5.720  1.00 134.96 ? 41  THR B O   1 
ATOM   2754 C CB  . THR B 2 41  ? -29.335 -99.192  -6.394  1.00 132.72 ? 41  THR B CB  1 
ATOM   2755 O OG1 . THR B 2 41  ? -29.969 -100.420 -6.773  1.00 134.20 ? 41  THR B OG1 1 
ATOM   2756 C CG2 . THR B 2 41  ? -28.043 -99.517  -5.661  1.00 126.98 ? 41  THR B CG2 1 
ATOM   2757 N N   . GLN B 2 42  ? -31.566 -96.852  -6.891  1.00 136.67 ? 42  GLN B N   1 
ATOM   2758 C CA  . GLN B 2 42  ? -31.959 -95.552  -7.437  1.00 136.82 ? 42  GLN B CA  1 
ATOM   2759 C C   . GLN B 2 42  ? -32.322 -94.549  -6.353  1.00 136.84 ? 42  GLN B C   1 
ATOM   2760 O O   . GLN B 2 42  ? -31.555 -93.630  -6.059  1.00 136.86 ? 42  GLN B O   1 
ATOM   2761 C CB  . GLN B 2 42  ? -33.157 -95.691  -8.385  1.00 137.10 ? 42  GLN B CB  1 
ATOM   2762 C CG  . GLN B 2 42  ? -33.710 -94.341  -8.867  1.00 137.70 ? 42  GLN B CG  1 
ATOM   2763 C CD  . GLN B 2 42  ? -35.086 -94.438  -9.516  1.00 137.99 ? 42  GLN B CD  1 
ATOM   2764 O OE1 . GLN B 2 42  ? -35.785 -95.443  -9.383  1.00 136.51 ? 42  GLN B OE1 1 
ATOM   2765 N NE2 . GLN B 2 42  ? -35.479 -93.381  -10.221 1.00 137.38 ? 42  GLN B NE2 1 
ATOM   2766 N N   . ASN B 2 43  ? -33.487 -94.749  -5.742  1.00 136.55 ? 43  ASN B N   1 
ATOM   2767 C CA  . ASN B 2 43  ? -34.018 -93.788  -4.782  1.00 137.01 ? 43  ASN B CA  1 
ATOM   2768 C C   . ASN B 2 43  ? -33.103 -93.656  -3.568  1.00 137.50 ? 43  ASN B C   1 
ATOM   2769 O O   . ASN B 2 43  ? -33.282 -92.762  -2.739  1.00 136.27 ? 43  ASN B O   1 
ATOM   2770 C CB  . ASN B 2 43  ? -35.457 -94.136  -4.376  1.00 135.83 ? 43  ASN B CB  1 
ATOM   2771 C CG  . ASN B 2 43  ? -36.497 -93.352  -5.170  1.00 137.78 ? 43  ASN B CG  1 
ATOM   2772 O OD1 . ASN B 2 43  ? -36.244 -92.227  -5.601  1.00 139.77 ? 43  ASN B OD1 1 
ATOM   2773 N ND2 . ASN B 2 43  ? -37.674 -93.943  -5.360  1.00 135.67 ? 43  ASN B ND2 1 
ATOM   2774 N N   . ALA B 2 44  ? -32.138 -94.571  -3.466  1.00 137.62 ? 44  ALA B N   1 
ATOM   2775 C CA  . ALA B 2 44  ? -31.042 -94.459  -2.504  1.00 135.58 ? 44  ALA B CA  1 
ATOM   2776 C C   . ALA B 2 44  ? -30.239 -93.187  -2.740  1.00 135.13 ? 44  ALA B C   1 
ATOM   2777 O O   . ALA B 2 44  ? -30.193 -92.305  -1.887  1.00 136.53 ? 44  ALA B O   1 
ATOM   2778 C CB  . ALA B 2 44  ? -30.133 -95.676  -2.570  1.00 134.02 ? 44  ALA B CB  1 
ATOM   2779 N N   . ILE B 2 45  ? -29.596 -93.105  -3.898  1.00 134.05 ? 45  ILE B N   1 
ATOM   2780 C CA  . ILE B 2 45  ? -28.762 -91.956  -4.222  1.00 133.89 ? 45  ILE B CA  1 
ATOM   2781 C C   . ILE B 2 45  ? -29.593 -90.696  -4.464  1.00 132.57 ? 45  ILE B C   1 
ATOM   2782 O O   . ILE B 2 45  ? -29.123 -89.583  -4.230  1.00 131.42 ? 45  ILE B O   1 
ATOM   2783 C CB  . ILE B 2 45  ? -27.889 -92.247  -5.443  1.00 132.04 ? 45  ILE B CB  1 
ATOM   2784 C CG1 . ILE B 2 45  ? -27.674 -93.753  -5.562  1.00 130.74 ? 45  ILE B CG1 1 
ATOM   2785 C CG2 . ILE B 2 45  ? -26.565 -91.495  -5.347  1.00 131.53 ? 45  ILE B CG2 1 
ATOM   2786 C CD1 . ILE B 2 45  ? -26.743 -94.148  -6.667  1.00 130.56 ? 45  ILE B CD1 1 
ATOM   2787 N N   . ASP B 2 46  ? -30.826 -90.877  -4.932  1.00 133.52 ? 46  ASP B N   1 
ATOM   2788 C CA  . ASP B 2 46  ? -31.764 -89.766  -5.103  1.00 136.51 ? 46  ASP B CA  1 
ATOM   2789 C C   . ASP B 2 46  ? -31.934 -89.053  -3.767  1.00 135.46 ? 46  ASP B C   1 
ATOM   2790 O O   . ASP B 2 46  ? -32.028 -87.825  -3.701  1.00 135.14 ? 46  ASP B O   1 
ATOM   2791 C CB  . ASP B 2 46  ? -33.121 -90.281  -5.606  1.00 138.15 ? 46  ASP B CB  1 
ATOM   2792 C CG  . ASP B 2 46  ? -34.091 -89.154  -5.964  1.00 140.57 ? 46  ASP B CG  1 
ATOM   2793 O OD1 . ASP B 2 46  ? -33.626 -88.031  -6.259  1.00 140.90 ? 46  ASP B OD1 1 
ATOM   2794 O OD2 . ASP B 2 46  ? -35.320 -89.395  -5.960  1.00 139.22 ? 46  ASP B OD2 1 
ATOM   2795 N N   . GLU B 2 47  ? -31.995 -89.848  -2.705  1.00 135.17 ? 47  GLU B N   1 
ATOM   2796 C CA  . GLU B 2 47  ? -32.057 -89.325  -1.347  1.00 135.81 ? 47  GLU B CA  1 
ATOM   2797 C C   . GLU B 2 47  ? -30.682 -88.947  -0.780  1.00 135.12 ? 47  GLU B C   1 
ATOM   2798 O O   . GLU B 2 47  ? -30.579 -88.006  0.004   1.00 135.92 ? 47  GLU B O   1 
ATOM   2799 C CB  . GLU B 2 47  ? -32.789 -90.305  -0.418  1.00 133.68 ? 47  GLU B CB  1 
ATOM   2800 C CG  . GLU B 2 47  ? -34.014 -89.708  0.260   1.00 131.19 ? 47  GLU B CG  1 
ATOM   2801 C CD  . GLU B 2 47  ? -35.016 -90.760  0.697   1.00 127.33 ? 47  GLU B CD  1 
ATOM   2802 O OE1 . GLU B 2 47  ? -34.598 -91.911  0.950   1.00 125.79 ? 47  GLU B OE1 1 
ATOM   2803 O OE2 . GLU B 2 47  ? -36.222 -90.437  0.777   1.00 124.75 ? 47  GLU B OE2 1 
ATOM   2804 N N   . ILE B 2 48  ? -29.632 -89.667  -1.176  1.00 134.87 ? 48  ILE B N   1 
ATOM   2805 C CA  . ILE B 2 48  ? -28.298 -89.455  -0.598  1.00 133.90 ? 48  ILE B CA  1 
ATOM   2806 C C   . ILE B 2 48  ? -27.644 -88.171  -1.101  1.00 134.86 ? 48  ILE B C   1 
ATOM   2807 O O   . ILE B 2 48  ? -27.377 -87.255  -0.322  1.00 134.38 ? 48  ILE B O   1 
ATOM   2808 C CB  . ILE B 2 48  ? -27.341 -90.651  -0.841  1.00 132.82 ? 48  ILE B CB  1 
ATOM   2809 C CG1 . ILE B 2 48  ? -27.921 -91.931  -0.241  1.00 131.25 ? 48  ILE B CG1 1 
ATOM   2810 C CG2 . ILE B 2 48  ? -25.967 -90.371  -0.246  1.00 128.73 ? 48  ILE B CG2 1 
ATOM   2811 C CD1 . ILE B 2 48  ? -28.402 -91.771  1.183   1.00 128.14 ? 48  ILE B CD1 1 
ATOM   2812 N N   . THR B 2 49  ? -27.370 -88.111  -2.400  1.00 135.50 ? 49  THR B N   1 
ATOM   2813 C CA  . THR B 2 49  ? -26.818 -86.899  -2.989  1.00 134.00 ? 49  THR B CA  1 
ATOM   2814 C C   . THR B 2 49  ? -27.695 -85.685  -2.670  1.00 133.71 ? 49  THR B C   1 
ATOM   2815 O O   . THR B 2 49  ? -27.196 -84.566  -2.563  1.00 135.01 ? 49  THR B O   1 
ATOM   2816 C CB  . THR B 2 49  ? -26.626 -87.050  -4.502  1.00 132.00 ? 49  THR B CB  1 
ATOM   2817 O OG1 . THR B 2 49  ? -27.594 -87.976  -5.008  1.00 131.98 ? 49  THR B OG1 1 
ATOM   2818 C CG2 . THR B 2 49  ? -25.232 -87.580  -4.805  1.00 126.98 ? 49  THR B CG2 1 
ATOM   2819 N N   . ASN B 2 50  ? -28.997 -85.913  -2.511  1.00 132.64 ? 50  ASN B N   1 
ATOM   2820 C CA  . ASN B 2 50  ? -29.915 -84.874  -2.047  1.00 134.50 ? 50  ASN B CA  1 
ATOM   2821 C C   . ASN B 2 50  ? -29.504 -84.387  -0.661  1.00 133.33 ? 50  ASN B C   1 
ATOM   2822 O O   . ASN B 2 50  ? -29.458 -83.184  -0.389  1.00 133.19 ? 50  ASN B O   1 
ATOM   2823 C CB  . ASN B 2 50  ? -31.355 -85.407  -2.010  1.00 135.72 ? 50  ASN B CB  1 
ATOM   2824 C CG  . ASN B 2 50  ? -32.375 -84.345  -1.602  1.00 136.94 ? 50  ASN B CG  1 
ATOM   2825 O OD1 . ASN B 2 50  ? -32.080 -83.446  -0.810  1.00 138.46 ? 50  ASN B OD1 1 
ATOM   2826 N ND2 . ASN B 2 50  ? -33.585 -84.449  -2.147  1.00 135.71 ? 50  ASN B ND2 1 
ATOM   2827 N N   . LYS B 2 51  ? -29.213 -85.338  0.218   1.00 132.83 ? 51  LYS B N   1 
ATOM   2828 C CA  . LYS B 2 51  ? -28.790 -85.024  1.574   1.00 132.59 ? 51  LYS B CA  1 
ATOM   2829 C C   . LYS B 2 51  ? -27.404 -84.397  1.558   1.00 131.90 ? 51  LYS B C   1 
ATOM   2830 O O   . LYS B 2 51  ? -27.168 -83.380  2.210   1.00 132.34 ? 51  LYS B O   1 
ATOM   2831 C CB  . LYS B 2 51  ? -28.808 -86.281  2.452   1.00 130.37 ? 51  LYS B CB  1 
ATOM   2832 C CG  . LYS B 2 51  ? -29.939 -86.308  3.476   1.00 127.81 ? 51  LYS B CG  1 
ATOM   2833 C CD  . LYS B 2 51  ? -30.669 -87.648  3.490   1.00 127.66 ? 51  LYS B CD  1 
ATOM   2834 C CE  . LYS B 2 51  ? -30.225 -88.536  4.649   1.00 123.08 ? 51  LYS B CE  1 
ATOM   2835 N NZ  . LYS B 2 51  ? -31.007 -89.806  4.701   1.00 112.12 ? 51  LYS B NZ  1 
ATOM   2836 N N   . VAL B 2 52  ? -26.498 -85.009  0.800   1.00 130.93 ? 52  VAL B N   1 
ATOM   2837 C CA  . VAL B 2 52  ? -25.127 -84.526  0.690   1.00 131.57 ? 52  VAL B CA  1 
ATOM   2838 C C   . VAL B 2 52  ? -25.099 -83.032  0.371   1.00 133.05 ? 52  VAL B C   1 
ATOM   2839 O O   . VAL B 2 52  ? -24.295 -82.281  0.921   1.00 132.41 ? 52  VAL B O   1 
ATOM   2840 C CB  . VAL B 2 52  ? -24.345 -85.300  -0.389  1.00 128.91 ? 52  VAL B CB  1 
ATOM   2841 C CG1 . VAL B 2 52  ? -22.946 -84.735  -0.537  1.00 123.23 ? 52  VAL B CG1 1 
ATOM   2842 C CG2 . VAL B 2 52  ? -24.292 -86.784  -0.047  1.00 129.08 ? 52  VAL B CG2 1 
ATOM   2843 N N   . ASN B 2 53  ? -25.961 -82.614  -0.547  1.00 134.26 ? 53  ASN B N   1 
ATOM   2844 C CA  . ASN B 2 53  ? -26.156 -81.196  -0.832  1.00 133.83 ? 53  ASN B CA  1 
ATOM   2845 C C   . ASN B 2 53  ? -26.654 -80.393  0.365   1.00 130.70 ? 53  ASN B C   1 
ATOM   2846 O O   . ASN B 2 53  ? -25.952 -79.538  0.898   1.00 129.94 ? 53  ASN B O   1 
ATOM   2847 C CB  . ASN B 2 53  ? -27.118 -81.014  -2.004  1.00 136.61 ? 53  ASN B CB  1 
ATOM   2848 C CG  . ASN B 2 53  ? -26.555 -81.543  -3.306  1.00 137.26 ? 53  ASN B CG  1 
ATOM   2849 O OD1 . ASN B 2 53  ? -25.574 -82.291  -3.316  1.00 137.66 ? 53  ASN B OD1 1 
ATOM   2850 N ND2 . ASN B 2 53  ? -27.174 -81.157  -4.416  1.00 136.74 ? 53  ASN B ND2 1 
ATOM   2851 N N   . SER B 2 54  ? -27.881 -80.687  0.778   1.00 130.89 ? 54  SER B N   1 
ATOM   2852 C CA  . SER B 2 54  ? -28.579 -79.870  1.760   1.00 131.47 ? 54  SER B CA  1 
ATOM   2853 C C   . SER B 2 54  ? -27.732 -79.559  2.990   1.00 130.18 ? 54  SER B C   1 
ATOM   2854 O O   . SER B 2 54  ? -27.864 -78.485  3.571   1.00 131.67 ? 54  SER B O   1 
ATOM   2855 C CB  . SER B 2 54  ? -29.894 -80.525  2.174   1.00 131.65 ? 54  SER B CB  1 
ATOM   2856 O OG  . SER B 2 54  ? -30.651 -79.653  2.997   1.00 131.78 ? 54  SER B OG  1 
ATOM   2857 N N   . VAL B 2 55  ? -26.887 -80.501  3.402   1.00 129.86 ? 55  VAL B N   1 
ATOM   2858 C CA  . VAL B 2 55  ? -25.963 -80.260  4.517   1.00 131.65 ? 55  VAL B CA  1 
ATOM   2859 C C   . VAL B 2 55  ? -25.007 -79.094  4.261   1.00 132.59 ? 55  VAL B C   1 
ATOM   2860 O O   . VAL B 2 55  ? -25.058 -78.067  4.942   1.00 133.50 ? 55  VAL B O   1 
ATOM   2861 C CB  . VAL B 2 55  ? -25.146 -81.520  4.915   1.00 128.41 ? 55  VAL B CB  1 
ATOM   2862 C CG1 . VAL B 2 55  ? -24.685 -82.281  3.697   1.00 129.13 ? 55  VAL B CG1 1 
ATOM   2863 C CG2 . VAL B 2 55  ? -23.952 -81.128  5.776   1.00 123.93 ? 55  VAL B CG2 1 
ATOM   2864 N N   . ILE B 2 56  ? -24.122 -79.266  3.288   1.00 131.17 ? 56  ILE B N   1 
ATOM   2865 C CA  . ILE B 2 56  ? -23.140 -78.239  2.978   1.00 130.47 ? 56  ILE B CA  1 
ATOM   2866 C C   . ILE B 2 56  ? -23.815 -76.924  2.586   1.00 131.53 ? 56  ILE B C   1 
ATOM   2867 O O   . ILE B 2 56  ? -23.361 -75.846  2.968   1.00 130.93 ? 56  ILE B O   1 
ATOM   2868 C CB  . ILE B 2 56  ? -22.199 -78.699  1.859   1.00 130.16 ? 56  ILE B CB  1 
ATOM   2869 C CG1 . ILE B 2 56  ? -21.393 -77.516  1.326   1.00 129.70 ? 56  ILE B CG1 1 
ATOM   2870 C CG2 . ILE B 2 56  ? -22.987 -79.369  0.743   1.00 128.66 ? 56  ILE B CG2 1 
ATOM   2871 C CD1 . ILE B 2 56  ? -20.571 -77.857  0.113   1.00 123.91 ? 56  ILE B CD1 1 
ATOM   2872 N N   . GLU B 2 57  ? -24.909 -77.020  1.836   1.00 132.28 ? 57  GLU B N   1 
ATOM   2873 C CA  . GLU B 2 57  ? -25.655 -75.838  1.417   1.00 132.05 ? 57  GLU B CA  1 
ATOM   2874 C C   . GLU B 2 57  ? -26.092 -75.018  2.624   1.00 133.68 ? 57  GLU B C   1 
ATOM   2875 O O   . GLU B 2 57  ? -26.085 -73.785  2.590   1.00 134.51 ? 57  GLU B O   1 
ATOM   2876 C CB  . GLU B 2 57  ? -26.884 -76.237  0.594   1.00 132.04 ? 57  GLU B CB  1 
ATOM   2877 C CG  . GLU B 2 57  ? -27.662 -75.059  0.013   1.00 134.20 ? 57  GLU B CG  1 
ATOM   2878 C CD  . GLU B 2 57  ? -28.803 -74.600  0.901   1.00 134.89 ? 57  GLU B CD  1 
ATOM   2879 O OE1 . GLU B 2 57  ? -29.107 -75.302  1.887   1.00 133.39 ? 57  GLU B OE1 1 
ATOM   2880 O OE2 . GLU B 2 57  ? -29.399 -73.539  0.608   1.00 133.54 ? 57  GLU B OE2 1 
ATOM   2881 N N   . LYS B 2 58  ? -26.457 -75.712  3.697   1.00 134.62 ? 58  LYS B N   1 
ATOM   2882 C CA  . LYS B 2 58  ? -27.029 -75.058  4.866   1.00 134.64 ? 58  LYS B CA  1 
ATOM   2883 C C   . LYS B 2 58  ? -26.003 -74.254  5.657   1.00 135.65 ? 58  LYS B C   1 
ATOM   2884 O O   . LYS B 2 58  ? -26.371 -73.335  6.392   1.00 136.09 ? 58  LYS B O   1 
ATOM   2885 C CB  . LYS B 2 58  ? -27.733 -76.070  5.782   1.00 131.47 ? 58  LYS B CB  1 
ATOM   2886 C CG  . LYS B 2 58  ? -26.900 -76.560  6.962   1.00 130.55 ? 58  LYS B CG  1 
ATOM   2887 C CD  . LYS B 2 58  ? -27.763 -76.701  8.208   1.00 128.96 ? 58  LYS B CD  1 
ATOM   2888 C CE  . LYS B 2 58  ? -28.234 -75.334  8.683   1.00 128.52 ? 58  LYS B CE  1 
ATOM   2889 N NZ  . LYS B 2 58  ? -29.419 -75.423  9.569   1.00 123.57 ? 58  LYS B NZ  1 
ATOM   2890 N N   . MET B 2 59  ? -24.720 -74.552  5.474   1.00 134.80 ? 59  MET B N   1 
ATOM   2891 C CA  . MET B 2 59  ? -23.717 -74.001  6.378   1.00 135.33 ? 59  MET B CA  1 
ATOM   2892 C C   . MET B 2 59  ? -23.561 -72.492  6.172   1.00 137.20 ? 59  MET B C   1 
ATOM   2893 O O   . MET B 2 59  ? -23.940 -71.703  7.042   1.00 137.03 ? 59  MET B O   1 
ATOM   2894 C CB  . MET B 2 59  ? -22.377 -74.746  6.246   1.00 129.89 ? 59  MET B CB  1 
ATOM   2895 C CG  . MET B 2 59  ? -21.765 -74.771  4.843   1.00 131.50 ? 59  MET B CG  1 
ATOM   2896 S SD  . MET B 2 59  ? -20.941 -73.245  4.321   1.00 133.29 ? 59  MET B SD  1 
ATOM   2897 C CE  . MET B 2 59  ? -21.168 -73.290  2.543   1.00 125.72 ? 59  MET B CE  1 
ATOM   2898 N N   . ASN B 2 60  ? -23.021 -72.087  5.029   1.00 137.11 ? 60  ASN B N   1 
ATOM   2899 C CA  . ASN B 2 60  ? -22.993 -70.673  4.684   1.00 138.79 ? 60  ASN B CA  1 
ATOM   2900 C C   . ASN B 2 60  ? -22.581 -69.771  5.836   1.00 142.12 ? 60  ASN B C   1 
ATOM   2901 O O   . ASN B 2 60  ? -21.594 -70.013  6.536   1.00 141.47 ? 60  ASN B O   1 
ATOM   2902 C CB  . ASN B 2 60  ? -24.364 -70.225  4.178   1.00 137.44 ? 60  ASN B CB  1 
ATOM   2903 C CG  . ASN B 2 60  ? -24.585 -70.574  2.733   1.00 136.86 ? 60  ASN B CG  1 
ATOM   2904 O OD1 . ASN B 2 60  ? -23.637 -70.867  2.006   1.00 137.02 ? 60  ASN B OD1 1 
ATOM   2905 N ND2 . ASN B 2 60  ? -25.839 -70.538  2.299   1.00 136.79 ? 60  ASN B ND2 1 
ATOM   2906 N N   . THR B 2 61  ? -23.377 -68.729  6.023   1.00 144.16 ? 61  THR B N   1 
ATOM   2907 C CA  . THR B 2 61  ? -23.145 -67.757  7.068   1.00 147.48 ? 61  THR B CA  1 
ATOM   2908 C C   . THR B 2 61  ? -24.485 -67.153  7.458   1.00 150.91 ? 61  THR B C   1 
ATOM   2909 O O   . THR B 2 61  ? -25.539 -67.580  6.980   1.00 151.28 ? 61  THR B O   1 
ATOM   2910 C CB  . THR B 2 61  ? -22.177 -66.656  6.589   1.00 144.81 ? 61  THR B CB  1 
ATOM   2911 O OG1 . THR B 2 61  ? -22.311 -65.492  7.414   1.00 147.34 ? 61  THR B OG1 1 
ATOM   2912 C CG2 . THR B 2 61  ? -22.474 -66.285  5.144   1.00 142.06 ? 61  THR B CG2 1 
ATOM   2913 N N   . GLN B 2 62  ? -24.436 -66.166  8.338   1.00 150.74 ? 62  GLN B N   1 
ATOM   2914 C CA  . GLN B 2 62  ? -25.620 -65.411  8.731   1.00 151.08 ? 62  GLN B CA  1 
ATOM   2915 C C   . GLN B 2 62  ? -25.992 -64.299  7.749   1.00 152.93 ? 62  GLN B C   1 
ATOM   2916 O O   . GLN B 2 62  ? -25.667 -64.387  6.562   1.00 151.21 ? 62  GLN B O   1 
ATOM   2917 C CB  . GLN B 2 62  ? -25.636 -65.002  10.204  1.00 147.59 ? 62  GLN B CB  1 
ATOM   2918 C CG  . GLN B 2 62  ? -26.688 -65.787  11.002  1.00 149.03 ? 62  GLN B CG  1 
ATOM   2919 C CD  . GLN B 2 62  ? -27.272 -66.969  10.220  1.00 153.01 ? 62  GLN B CD  1 
ATOM   2920 O OE1 . GLN B 2 62  ? -28.275 -66.832  9.514   1.00 153.88 ? 62  GLN B OE1 1 
ATOM   2921 N NE2 . GLN B 2 62  ? -26.644 -68.134  10.348  1.00 152.66 ? 62  GLN B NE2 1 
ATOM   2922 N N   . PHE B 2 63  ? -26.654 -63.259  8.247   1.00 155.59 ? 63  PHE B N   1 
ATOM   2923 C CA  . PHE B 2 63  ? -27.787 -62.612  7.598   1.00 158.84 ? 63  PHE B CA  1 
ATOM   2924 C C   . PHE B 2 63  ? -28.991 -63.536  7.733   1.00 159.48 ? 63  PHE B C   1 
ATOM   2925 O O   . PHE B 2 63  ? -29.549 -64.041  6.755   1.00 159.46 ? 63  PHE B O   1 
ATOM   2926 C CB  . PHE B 2 63  ? -27.513 -62.355  6.112   1.00 159.35 ? 63  PHE B CB  1 
ATOM   2927 C CG  . PHE B 2 63  ? -26.808 -61.055  5.825   1.00 159.50 ? 63  PHE B CG  1 
ATOM   2928 C CD1 . PHE B 2 63  ? -26.915 -59.974  6.690   1.00 158.73 ? 63  PHE B CD1 1 
ATOM   2929 C CD2 . PHE B 2 63  ? -26.049 -60.912  4.674   1.00 158.37 ? 63  PHE B CD2 1 
ATOM   2930 C CE1 . PHE B 2 63  ? -26.269 -58.779  6.412   1.00 158.23 ? 63  PHE B CE1 1 
ATOM   2931 C CE2 . PHE B 2 63  ? -25.403 -59.724  4.392   1.00 159.13 ? 63  PHE B CE2 1 
ATOM   2932 C CZ  . PHE B 2 63  ? -25.513 -58.655  5.262   1.00 158.98 ? 63  PHE B CZ  1 
ATOM   2933 N N   . THR B 2 64  ? -29.364 -63.732  8.997   1.00 159.29 ? 64  THR B N   1 
ATOM   2934 C CA  . THR B 2 64  ? -30.684 -64.184  9.400   1.00 159.02 ? 64  THR B CA  1 
ATOM   2935 C C   . THR B 2 64  ? -31.322 -62.942  10.004  1.00 160.05 ? 64  THR B C   1 
ATOM   2936 O O   . THR B 2 64  ? -30.931 -62.495  11.087  1.00 160.19 ? 64  THR B O   1 
ATOM   2937 C CB  . THR B 2 64  ? -30.612 -65.298  10.475  1.00 157.47 ? 64  THR B CB  1 
ATOM   2938 O OG1 . THR B 2 64  ? -30.534 -66.584  9.841   1.00 154.75 ? 64  THR B OG1 1 
ATOM   2939 C CG2 . THR B 2 64  ? -31.837 -65.260  11.390  1.00 157.82 ? 64  THR B CG2 1 
ATOM   2940 N N   . ALA B 2 65  ? -32.289 -62.374  9.291   1.00 160.36 ? 65  ALA B N   1 
ATOM   2941 C CA  . ALA B 2 65  ? -32.906 -61.120  9.702   1.00 158.04 ? 65  ALA B CA  1 
ATOM   2942 C C   . ALA B 2 65  ? -34.320 -61.336  10.231  1.00 154.06 ? 65  ALA B C   1 
ATOM   2943 O O   . ALA B 2 65  ? -35.052 -60.376  10.469  1.00 150.68 ? 65  ALA B O   1 
ATOM   2944 C CB  . ALA B 2 65  ? -32.913 -60.127  8.545   1.00 155.17 ? 65  ALA B CB  1 
ATOM   2945 N N   . LYS B 2 83  ? -11.027 -62.975  18.316  1.00 135.74 ? 83  LYS B N   1 
ATOM   2946 C CA  . LYS B 2 83  ? -12.163 -63.553  17.607  1.00 135.02 ? 83  LYS B CA  1 
ATOM   2947 C C   . LYS B 2 83  ? -12.208 -63.078  16.166  1.00 135.86 ? 83  LYS B C   1 
ATOM   2948 O O   . LYS B 2 83  ? -13.248 -63.200  15.517  1.00 136.06 ? 83  LYS B O   1 
ATOM   2949 C CB  . LYS B 2 83  ? -13.488 -63.150  18.273  1.00 136.26 ? 83  LYS B CB  1 
ATOM   2950 C CG  . LYS B 2 83  ? -13.787 -63.803  19.614  1.00 136.54 ? 83  LYS B CG  1 
ATOM   2951 C CD  . LYS B 2 83  ? -15.097 -63.277  20.201  1.00 133.69 ? 83  LYS B CD  1 
ATOM   2952 C CE  . LYS B 2 83  ? -15.031 -61.775  20.442  1.00 131.28 ? 83  LYS B CE  1 
ATOM   2953 N NZ  . LYS B 2 83  ? -16.288 -61.247  21.037  1.00 128.46 ? 83  LYS B NZ  1 
ATOM   2954 N N   . VAL B 2 84  ? -11.094 -62.550  15.661  1.00 137.46 ? 84  VAL B N   1 
ATOM   2955 C CA  . VAL B 2 84  ? -11.150 -61.740  14.448  1.00 138.93 ? 84  VAL B CA  1 
ATOM   2956 C C   . VAL B 2 84  ? -11.983 -62.472  13.405  1.00 139.72 ? 84  VAL B C   1 
ATOM   2957 O O   . VAL B 2 84  ? -13.166 -62.164  13.227  1.00 138.71 ? 84  VAL B O   1 
ATOM   2958 C CB  . VAL B 2 84  ? -9.736  -61.531  13.878  1.00 136.95 ? 84  VAL B CB  1 
ATOM   2959 C CG1 . VAL B 2 84  ? -9.632  -60.181  13.183  1.00 132.83 ? 84  VAL B CG1 1 
ATOM   2960 C CG2 . VAL B 2 84  ? -8.696  -61.659  14.988  1.00 135.82 ? 84  VAL B CG2 1 
ATOM   2961 N N   . ASP B 2 85  ? -11.376 -63.428  12.706  1.00 137.89 ? 85  ASP B N   1 
ATOM   2962 C CA  . ASP B 2 85  ? -12.072 -64.637  12.281  1.00 137.94 ? 85  ASP B CA  1 
ATOM   2963 C C   . ASP B 2 85  ? -11.569 -65.841  13.087  1.00 135.79 ? 85  ASP B C   1 
ATOM   2964 O O   . ASP B 2 85  ? -12.083 -66.954  12.961  1.00 133.33 ? 85  ASP B O   1 
ATOM   2965 C CB  . ASP B 2 85  ? -11.976 -64.855  10.765  1.00 139.79 ? 85  ASP B CB  1 
ATOM   2966 C CG  . ASP B 2 85  ? -13.005 -64.031  9.989   1.00 139.74 ? 85  ASP B CG  1 
ATOM   2967 O OD1 . ASP B 2 85  ? -13.111 -62.808  10.240  1.00 141.00 ? 85  ASP B OD1 1 
ATOM   2968 O OD2 . ASP B 2 85  ? -13.708 -64.604  9.127   1.00 137.87 ? 85  ASP B OD2 1 
ATOM   2969 N N   . ASP B 2 86  ? -10.562 -65.593  13.922  1.00 135.63 ? 86  ASP B N   1 
ATOM   2970 C CA  . ASP B 2 86  ? -9.856  -66.652  14.638  1.00 133.14 ? 86  ASP B CA  1 
ATOM   2971 C C   . ASP B 2 86  ? -10.788 -67.416  15.565  1.00 132.34 ? 86  ASP B C   1 
ATOM   2972 O O   . ASP B 2 86  ? -10.701 -68.641  15.680  1.00 131.61 ? 86  ASP B O   1 
ATOM   2973 C CB  . ASP B 2 86  ? -8.678  -66.073  15.428  1.00 134.67 ? 86  ASP B CB  1 
ATOM   2974 C CG  . ASP B 2 86  ? -7.341  -66.613  14.958  1.00 134.19 ? 86  ASP B CG  1 
ATOM   2975 O OD1 . ASP B 2 86  ? -7.324  -67.739  14.421  1.00 133.85 ? 86  ASP B OD1 1 
ATOM   2976 O OD2 . ASP B 2 86  ? -6.314  -65.917  15.120  1.00 131.47 ? 86  ASP B OD2 1 
ATOM   2977 N N   . GLY B 2 87  ? -11.673 -66.686  16.235  1.00 133.71 ? 87  GLY B N   1 
ATOM   2978 C CA  . GLY B 2 87  ? -12.665 -67.299  17.097  1.00 133.12 ? 87  GLY B CA  1 
ATOM   2979 C C   . GLY B 2 87  ? -13.837 -67.856  16.310  1.00 131.02 ? 87  GLY B C   1 
ATOM   2980 O O   . GLY B 2 87  ? -14.387 -68.903  16.655  1.00 128.37 ? 87  GLY B O   1 
ATOM   2981 N N   . PHE B 2 88  ? -14.219 -67.146  15.251  1.00 131.05 ? 88  PHE B N   1 
ATOM   2982 C CA  . PHE B 2 88  ? -15.327 -67.561  14.397  1.00 128.78 ? 88  PHE B CA  1 
ATOM   2983 C C   . PHE B 2 88  ? -14.969 -68.834  13.643  1.00 127.07 ? 88  PHE B C   1 
ATOM   2984 O O   . PHE B 2 88  ? -15.709 -69.816  13.681  1.00 125.25 ? 88  PHE B O   1 
ATOM   2985 C CB  . PHE B 2 88  ? -15.675 -66.454  13.398  1.00 129.15 ? 88  PHE B CB  1 
ATOM   2986 C CG  . PHE B 2 88  ? -16.977 -66.673  12.664  1.00 129.81 ? 88  PHE B CG  1 
ATOM   2987 C CD1 . PHE B 2 88  ? -17.039 -67.498  11.550  1.00 128.02 ? 88  PHE B CD1 1 
ATOM   2988 C CD2 . PHE B 2 88  ? -18.137 -66.036  13.078  1.00 129.06 ? 88  PHE B CD2 1 
ATOM   2989 C CE1 . PHE B 2 88  ? -18.237 -67.689  10.874  1.00 125.98 ? 88  PHE B CE1 1 
ATOM   2990 C CE2 . PHE B 2 88  ? -19.336 -66.224  12.405  1.00 127.42 ? 88  PHE B CE2 1 
ATOM   2991 C CZ  . PHE B 2 88  ? -19.386 -67.050  11.303  1.00 126.11 ? 88  PHE B CZ  1 
ATOM   2992 N N   . LEU B 2 89  ? -13.824 -68.803  12.965  1.00 127.12 ? 89  LEU B N   1 
ATOM   2993 C CA  . LEU B 2 89  ? -13.349 -69.922  12.156  1.00 125.61 ? 89  LEU B CA  1 
ATOM   2994 C C   . LEU B 2 89  ? -13.305 -71.241  12.921  1.00 124.14 ? 89  LEU B C   1 
ATOM   2995 O O   . LEU B 2 89  ? -13.899 -72.231  12.494  1.00 123.98 ? 89  LEU B O   1 
ATOM   2996 C CB  . LEU B 2 89  ? -11.959 -69.613  11.590  1.00 127.58 ? 89  LEU B CB  1 
ATOM   2997 C CG  . LEU B 2 89  ? -11.169 -70.777  10.980  1.00 123.97 ? 89  LEU B CG  1 
ATOM   2998 C CD1 . LEU B 2 89  ? -11.961 -71.448  9.868   1.00 116.60 ? 89  LEU B CD1 1 
ATOM   2999 C CD2 . LEU B 2 89  ? -9.810  -70.310  10.467  1.00 119.16 ? 89  LEU B CD2 1 
ATOM   3000 N N   . ASP B 2 90  ? -12.601 -71.251  14.048  1.00 123.99 ? 90  ASP B N   1 
ATOM   3001 C CA  . ASP B 2 90  ? -12.426 -72.473  14.827  1.00 123.20 ? 90  ASP B CA  1 
ATOM   3002 C C   . ASP B 2 90  ? -13.759 -73.148  15.154  1.00 122.83 ? 90  ASP B C   1 
ATOM   3003 O O   . ASP B 2 90  ? -13.840 -74.374  15.193  1.00 121.98 ? 90  ASP B O   1 
ATOM   3004 C CB  . ASP B 2 90  ? -11.633 -72.194  16.108  1.00 123.75 ? 90  ASP B CB  1 
ATOM   3005 C CG  . ASP B 2 90  ? -10.227 -71.691  15.825  1.00 124.47 ? 90  ASP B CG  1 
ATOM   3006 O OD1 . ASP B 2 90  ? -9.966  -71.296  14.669  1.00 124.50 ? 90  ASP B OD1 1 
ATOM   3007 O OD2 . ASP B 2 90  ? -9.388  -71.681  16.753  1.00 125.10 ? 90  ASP B OD2 1 
ATOM   3008 N N   . ILE B 2 91  ? -14.793 -72.344  15.397  1.00 123.36 ? 91  ILE B N   1 
ATOM   3009 C CA  . ILE B 2 91  ? -16.142 -72.862  15.641  1.00 123.08 ? 91  ILE B CA  1 
ATOM   3010 C C   . ILE B 2 91  ? -16.891 -73.226  14.358  1.00 120.34 ? 91  ILE B C   1 
ATOM   3011 O O   . ILE B 2 91  ? -17.611 -74.221  14.315  1.00 119.87 ? 91  ILE B O   1 
ATOM   3012 C CB  . ILE B 2 91  ? -16.994 -71.886  16.480  1.00 124.13 ? 91  ILE B CB  1 
ATOM   3013 C CG1 . ILE B 2 91  ? -16.841 -72.203  17.971  1.00 125.80 ? 91  ILE B CG1 1 
ATOM   3014 C CG2 . ILE B 2 91  ? -18.461 -71.963  16.062  1.00 120.59 ? 91  ILE B CG2 1 
ATOM   3015 C CD1 . ILE B 2 91  ? -17.103 -71.024  18.892  1.00 128.95 ? 91  ILE B CD1 1 
ATOM   3016 N N   . TRP B 2 92  ? -16.731 -72.412  13.320  1.00 120.78 ? 92  TRP B N   1 
ATOM   3017 C CA  . TRP B 2 92  ? -17.311 -72.722  12.021  1.00 120.10 ? 92  TRP B CA  1 
ATOM   3018 C C   . TRP B 2 92  ? -16.927 -74.129  11.622  1.00 118.76 ? 92  TRP B C   1 
ATOM   3019 O O   . TRP B 2 92  ? -17.775 -74.942  11.261  1.00 118.06 ? 92  TRP B O   1 
ATOM   3020 C CB  . TRP B 2 92  ? -16.788 -71.770  10.954  1.00 122.92 ? 92  TRP B CB  1 
ATOM   3021 C CG  . TRP B 2 92  ? -17.315 -72.115  9.610   1.00 120.52 ? 92  TRP B CG  1 
ATOM   3022 C CD1 . TRP B 2 92  ? -16.599 -72.375  8.477   1.00 118.28 ? 92  TRP B CD1 1 
ATOM   3023 C CD2 . TRP B 2 92  ? -18.686 -72.265  9.263   1.00 120.97 ? 92  TRP B CD2 1 
ATOM   3024 N NE1 . TRP B 2 92  ? -17.450 -72.660  7.438   1.00 116.56 ? 92  TRP B NE1 1 
ATOM   3025 C CE2 . TRP B 2 92  ? -18.738 -72.600  7.898   1.00 120.93 ? 92  TRP B CE2 1 
ATOM   3026 C CE3 . TRP B 2 92  ? -19.881 -72.139  9.975   1.00 122.52 ? 92  TRP B CE3 1 
ATOM   3027 C CZ2 . TRP B 2 92  ? -19.934 -72.812  7.234   1.00 125.62 ? 92  TRP B CZ2 1 
ATOM   3028 C CZ3 . TRP B 2 92  ? -21.065 -72.348  9.316   1.00 125.76 ? 92  TRP B CZ3 1 
ATOM   3029 C CH2 . TRP B 2 92  ? -21.085 -72.680  7.959   1.00 127.28 ? 92  TRP B CH2 1 
ATOM   3030 N N   . THR B 2 93  ? -15.627 -74.396  11.676  1.00 119.31 ? 93  THR B N   1 
ATOM   3031 C CA  . THR B 2 93  ? -15.104 -75.735  11.464  1.00 119.43 ? 93  THR B CA  1 
ATOM   3032 C C   . THR B 2 93  ? -15.813 -76.713  12.392  1.00 119.28 ? 93  THR B C   1 
ATOM   3033 O O   . THR B 2 93  ? -16.518 -77.617  11.940  1.00 118.09 ? 93  THR B O   1 
ATOM   3034 C CB  . THR B 2 93  ? -13.585 -75.810  11.748  1.00 118.50 ? 93  THR B CB  1 
ATOM   3035 O OG1 . THR B 2 93  ? -13.336 -75.530  13.133  1.00 119.06 ? 93  THR B OG1 1 
ATOM   3036 C CG2 . THR B 2 93  ? -12.816 -74.821  10.876  1.00 115.30 ? 93  THR B CG2 1 
ATOM   3037 N N   . TYR B 2 94  ? -15.618 -76.521  13.695  1.00 120.15 ? 94  TYR B N   1 
ATOM   3038 C CA  . TYR B 2 94  ? -16.173 -77.415  14.704  1.00 119.07 ? 94  TYR B CA  1 
ATOM   3039 C C   . TYR B 2 94  ? -17.647 -77.615  14.442  1.00 118.08 ? 94  TYR B C   1 
ATOM   3040 O O   . TYR B 2 94  ? -18.187 -78.685  14.690  1.00 119.61 ? 94  TYR B O   1 
ATOM   3041 C CB  . TYR B 2 94  ? -15.977 -76.843  16.110  1.00 119.91 ? 94  TYR B CB  1 
ATOM   3042 C CG  . TYR B 2 94  ? -16.010 -77.882  17.217  1.00 120.28 ? 94  TYR B CG  1 
ATOM   3043 C CD1 . TYR B 2 94  ? -15.075 -78.911  17.256  1.00 119.09 ? 94  TYR B CD1 1 
ATOM   3044 C CD2 . TYR B 2 94  ? -16.958 -77.821  18.235  1.00 121.32 ? 94  TYR B CD2 1 
ATOM   3045 C CE1 . TYR B 2 94  ? -15.091 -79.861  18.271  1.00 120.90 ? 94  TYR B CE1 1 
ATOM   3046 C CE2 . TYR B 2 94  ? -16.980 -78.769  19.256  1.00 120.59 ? 94  TYR B CE2 1 
ATOM   3047 C CZ  . TYR B 2 94  ? -16.044 -79.784  19.267  1.00 120.64 ? 94  TYR B CZ  1 
ATOM   3048 O OH  . TYR B 2 94  ? -16.066 -80.722  20.276  1.00 119.98 ? 94  TYR B OH  1 
ATOM   3049 N N   . ASN B 2 95  ? -18.295 -76.575  13.936  1.00 117.39 ? 95  ASN B N   1 
ATOM   3050 C CA  . ASN B 2 95  ? -19.696 -76.673  13.571  1.00 116.25 ? 95  ASN B CA  1 
ATOM   3051 C C   . ASN B 2 95  ? -19.871 -77.524  12.327  1.00 116.78 ? 95  ASN B C   1 
ATOM   3052 O O   . ASN B 2 95  ? -20.793 -78.330  12.243  1.00 116.67 ? 95  ASN B O   1 
ATOM   3053 C CB  . ASN B 2 95  ? -20.286 -75.289  13.334  1.00 117.82 ? 95  ASN B CB  1 
ATOM   3054 C CG  . ASN B 2 95  ? -21.783 -75.324  13.175  1.00 117.14 ? 95  ASN B CG  1 
ATOM   3055 O OD1 . ASN B 2 95  ? -22.517 -75.448  14.156  1.00 118.02 ? 95  ASN B OD1 1 
ATOM   3056 N ND2 . ASN B 2 95  ? -22.249 -75.219  11.935  1.00 115.96 ? 95  ASN B ND2 1 
ATOM   3057 N N   . ALA B 2 96  ? -18.977 -77.331  11.362  1.00 117.09 ? 96  ALA B N   1 
ATOM   3058 C CA  . ALA B 2 96  ? -19.032 -78.055  10.100  1.00 115.91 ? 96  ALA B CA  1 
ATOM   3059 C C   . ALA B 2 96  ? -18.594 -79.511  10.248  1.00 117.68 ? 96  ALA B C   1 
ATOM   3060 O O   . ALA B 2 96  ? -19.292 -80.419  9.799   1.00 117.56 ? 96  ALA B O   1 
ATOM   3061 C CB  . ALA B 2 96  ? -18.187 -77.351  9.053   1.00 114.86 ? 96  ALA B CB  1 
ATOM   3062 N N   . GLU B 2 97  ? -17.447 -79.729  10.890  1.00 119.67 ? 97  GLU B N   1 
ATOM   3063 C CA  . GLU B 2 97  ? -16.874 -81.072  11.022  1.00 119.78 ? 97  GLU B CA  1 
ATOM   3064 C C   . GLU B 2 97  ? -17.913 -82.094  11.479  1.00 120.06 ? 97  GLU B C   1 
ATOM   3065 O O   . GLU B 2 97  ? -17.914 -83.241  11.023  1.00 119.00 ? 97  GLU B O   1 
ATOM   3066 C CB  . GLU B 2 97  ? -15.682 -81.068  11.988  1.00 118.37 ? 97  GLU B CB  1 
ATOM   3067 C CG  . GLU B 2 97  ? -14.470 -80.309  11.474  1.00 115.83 ? 97  GLU B CG  1 
ATOM   3068 C CD  . GLU B 2 97  ? -13.281 -80.392  12.409  1.00 116.36 ? 97  GLU B CD  1 
ATOM   3069 O OE1 . GLU B 2 97  ? -13.441 -80.913  13.532  1.00 115.90 ? 97  GLU B OE1 1 
ATOM   3070 O OE2 . GLU B 2 97  ? -12.185 -79.934  12.019  1.00 116.61 ? 97  GLU B OE2 1 
ATOM   3071 N N   . LEU B 2 98  ? -18.788 -81.666  12.385  1.00 120.69 ? 98  LEU B N   1 
ATOM   3072 C CA  . LEU B 2 98  ? -19.805 -82.533  12.973  1.00 119.90 ? 98  LEU B CA  1 
ATOM   3073 C C   . LEU B 2 98  ? -20.951 -82.808  12.006  1.00 117.85 ? 98  LEU B C   1 
ATOM   3074 O O   . LEU B 2 98  ? -21.524 -83.898  12.004  1.00 117.42 ? 98  LEU B O   1 
ATOM   3075 C CB  . LEU B 2 98  ? -20.337 -81.912  14.266  1.00 121.19 ? 98  LEU B CB  1 
ATOM   3076 C CG  . LEU B 2 98  ? -19.262 -81.273  15.155  1.00 121.73 ? 98  LEU B CG  1 
ATOM   3077 C CD1 . LEU B 2 98  ? -19.844 -80.779  16.476  1.00 121.38 ? 98  LEU B CD1 1 
ATOM   3078 C CD2 . LEU B 2 98  ? -18.107 -82.234  15.407  1.00 122.49 ? 98  LEU B CD2 1 
ATOM   3079 N N   . LEU B 2 99  ? -21.278 -81.818  11.181  1.00 117.77 ? 99  LEU B N   1 
ATOM   3080 C CA  . LEU B 2 99  ? -22.297 -81.998  10.155  1.00 117.50 ? 99  LEU B CA  1 
ATOM   3081 C C   . LEU B 2 99  ? -22.018 -83.266  9.353   1.00 117.53 ? 99  LEU B C   1 
ATOM   3082 O O   . LEU B 2 99  ? -22.943 -83.977  8.954   1.00 116.88 ? 99  LEU B O   1 
ATOM   3083 C CB  . LEU B 2 99  ? -22.349 -80.784  9.228   1.00 116.19 ? 99  LEU B CB  1 
ATOM   3084 C CG  . LEU B 2 99  ? -23.644 -79.975  9.296   1.00 118.46 ? 99  LEU B CG  1 
ATOM   3085 C CD1 . LEU B 2 99  ? -24.078 -79.797  10.748  1.00 120.15 ? 99  LEU B CD1 1 
ATOM   3086 C CD2 . LEU B 2 99  ? -23.494 -78.629  8.591   1.00 120.64 ? 99  LEU B CD2 1 
ATOM   3087 N N   . VAL B 2 100 ? -20.736 -83.545  9.129   1.00 117.66 ? 100 VAL B N   1 
ATOM   3088 C CA  . VAL B 2 100 ? -20.316 -84.764  8.446   1.00 117.16 ? 100 VAL B CA  1 
ATOM   3089 C C   . VAL B 2 100 ? -20.430 -85.965  9.363   1.00 116.54 ? 100 VAL B C   1 
ATOM   3090 O O   . VAL B 2 100 ? -20.977 -86.997  8.983   1.00 117.20 ? 100 VAL B O   1 
ATOM   3091 C CB  . VAL B 2 100 ? -18.854 -84.687  7.983   1.00 116.87 ? 100 VAL B CB  1 
ATOM   3092 C CG1 . VAL B 2 100 ? -18.366 -86.067  7.559   1.00 117.83 ? 100 VAL B CG1 1 
ATOM   3093 C CG2 . VAL B 2 100 ? -18.708 -83.689  6.852   1.00 115.99 ? 100 VAL B CG2 1 
ATOM   3094 N N   . LEU B 2 101 ? -19.921 -85.823  10.580  1.00 115.45 ? 101 LEU B N   1 
ATOM   3095 C CA  . LEU B 2 101 ? -19.930 -86.927  11.527  1.00 115.77 ? 101 LEU B CA  1 
ATOM   3096 C C   . LEU B 2 101 ? -21.363 -87.370  11.777  1.00 116.92 ? 101 LEU B C   1 
ATOM   3097 O O   . LEU B 2 101 ? -21.609 -88.415  12.380  1.00 117.63 ? 101 LEU B O   1 
ATOM   3098 C CB  . LEU B 2 101 ? -19.234 -86.535  12.831  1.00 115.07 ? 101 LEU B CB  1 
ATOM   3099 C CG  . LEU B 2 101 ? -17.707 -86.607  12.775  1.00 116.98 ? 101 LEU B CG  1 
ATOM   3100 C CD1 . LEU B 2 101 ? -17.175 -87.611  13.792  1.00 117.13 ? 101 LEU B CD1 1 
ATOM   3101 C CD2 . LEU B 2 101 ? -17.234 -86.955  11.366  1.00 117.96 ? 101 LEU B CD2 1 
ATOM   3102 N N   . LEU B 2 102 ? -22.308 -86.562  11.308  1.00 115.83 ? 102 LEU B N   1 
ATOM   3103 C CA  . LEU B 2 102 ? -23.716 -86.926  11.366  1.00 115.74 ? 102 LEU B CA  1 
ATOM   3104 C C   . LEU B 2 102 ? -24.179 -87.639  10.115  1.00 117.06 ? 102 LEU B C   1 
ATOM   3105 O O   . LEU B 2 102 ? -24.441 -88.841  10.138  1.00 119.31 ? 102 LEU B O   1 
ATOM   3106 C CB  . LEU B 2 102 ? -24.581 -85.694  11.558  1.00 115.71 ? 102 LEU B CB  1 
ATOM   3107 C CG  . LEU B 2 102 ? -24.995 -85.500  13.006  1.00 116.71 ? 102 LEU B CG  1 
ATOM   3108 C CD1 . LEU B 2 102 ? -23.789 -85.062  13.812  1.00 115.12 ? 102 LEU B CD1 1 
ATOM   3109 C CD2 . LEU B 2 102 ? -26.108 -84.480  13.074  1.00 119.42 ? 102 LEU B CD2 1 
ATOM   3110 N N   . GLU B 2 103 ? -24.287 -86.888  9.023   1.00 115.80 ? 103 GLU B N   1 
ATOM   3111 C CA  . GLU B 2 103 ? -24.813 -87.434  7.782   1.00 115.54 ? 103 GLU B CA  1 
ATOM   3112 C C   . GLU B 2 103 ? -24.044 -88.685  7.376   1.00 117.21 ? 103 GLU B C   1 
ATOM   3113 O O   . GLU B 2 103 ? -24.602 -89.578  6.739   1.00 117.82 ? 103 GLU B O   1 
ATOM   3114 C CB  . GLU B 2 103 ? -24.810 -86.381  6.675   1.00 113.94 ? 103 GLU B CB  1 
ATOM   3115 C CG  . GLU B 2 103 ? -25.817 -85.254  6.899   1.00 117.95 ? 103 GLU B CG  1 
ATOM   3116 C CD  . GLU B 2 103 ? -27.263 -85.718  6.800   1.00 118.82 ? 103 GLU B CD  1 
ATOM   3117 O OE1 . GLU B 2 103 ? -28.175 -84.892  7.025   1.00 117.47 ? 103 GLU B OE1 1 
ATOM   3118 O OE2 . GLU B 2 103 ? -27.488 -86.907  6.490   1.00 120.31 ? 103 GLU B OE2 1 
ATOM   3119 N N   . ASN B 2 104 ? -22.768 -88.745  7.751   1.00 117.32 ? 104 ASN B N   1 
ATOM   3120 C CA  . ASN B 2 104 ? -22.014 -89.994  7.681   1.00 117.26 ? 104 ASN B CA  1 
ATOM   3121 C C   . ASN B 2 104 ? -22.741 -91.076  8.477   1.00 118.70 ? 104 ASN B C   1 
ATOM   3122 O O   . ASN B 2 104 ? -23.223 -92.058  7.911   1.00 120.25 ? 104 ASN B O   1 
ATOM   3123 C CB  . ASN B 2 104 ? -20.594 -89.821  8.233   1.00 117.41 ? 104 ASN B CB  1 
ATOM   3124 C CG  . ASN B 2 104 ? -19.610 -89.341  7.185   1.00 116.11 ? 104 ASN B CG  1 
ATOM   3125 O OD1 . ASN B 2 104 ? -19.998 -88.760  6.174   1.00 114.14 ? 104 ASN B OD1 1 
ATOM   3126 N ND2 . ASN B 2 104 ? -18.324 -89.588  7.422   1.00 115.48 ? 104 ASN B ND2 1 
ATOM   3127 N N   . GLU B 2 105 ? -22.822 -90.875  9.792   1.00 118.00 ? 105 GLU B N   1 
ATOM   3128 C CA  . GLU B 2 105 ? -23.473 -91.816  10.707  1.00 118.20 ? 105 GLU B CA  1 
ATOM   3129 C C   . GLU B 2 105 ? -24.897 -92.139  10.279  1.00 117.72 ? 105 GLU B C   1 
ATOM   3130 O O   . GLU B 2 105 ? -25.350 -93.280  10.392  1.00 117.78 ? 105 GLU B O   1 
ATOM   3131 C CB  . GLU B 2 105 ? -23.499 -91.251  12.131  1.00 118.34 ? 105 GLU B CB  1 
ATOM   3132 C CG  . GLU B 2 105 ? -24.099 -92.197  13.145  1.00 117.39 ? 105 GLU B CG  1 
ATOM   3133 C CD  . GLU B 2 105 ? -23.310 -93.476  13.243  1.00 118.68 ? 105 GLU B CD  1 
ATOM   3134 O OE1 . GLU B 2 105 ? -22.101 -93.391  13.546  1.00 119.19 ? 105 GLU B OE1 1 
ATOM   3135 O OE2 . GLU B 2 105 ? -23.885 -94.560  13.001  1.00 120.55 ? 105 GLU B OE2 1 
ATOM   3136 N N   . ARG B 2 106 ? -25.600 -91.121  9.797   1.00 117.81 ? 106 ARG B N   1 
ATOM   3137 C CA  . ARG B 2 106 ? -26.989 -91.270  9.378   1.00 119.74 ? 106 ARG B CA  1 
ATOM   3138 C C   . ARG B 2 106 ? -27.110 -92.076  8.082   1.00 118.87 ? 106 ARG B C   1 
ATOM   3139 O O   . ARG B 2 106 ? -28.211 -92.440  7.659   1.00 118.96 ? 106 ARG B O   1 
ATOM   3140 C CB  . ARG B 2 106 ? -27.643 -89.893  9.224   1.00 118.19 ? 106 ARG B CB  1 
ATOM   3141 C CG  . ARG B 2 106 ? -27.568 -89.044  10.487  1.00 117.59 ? 106 ARG B CG  1 
ATOM   3142 C CD  . ARG B 2 106 ? -28.444 -87.815  10.389  1.00 118.08 ? 106 ARG B CD  1 
ATOM   3143 N NE  . ARG B 2 106 ? -29.289 -87.673  11.569  1.00 118.33 ? 106 ARG B NE  1 
ATOM   3144 C CZ  . ARG B 2 106 ? -30.147 -86.677  11.758  1.00 119.83 ? 106 ARG B CZ  1 
ATOM   3145 N NH1 . ARG B 2 106 ? -30.271 -85.724  10.842  1.00 118.08 ? 106 ARG B NH1 1 
ATOM   3146 N NH2 . ARG B 2 106 ? -30.881 -86.633  12.864  1.00 121.17 ? 106 ARG B NH2 1 
ATOM   3147 N N   . THR B 2 107 ? -25.967 -92.358  7.467   1.00 117.85 ? 107 THR B N   1 
ATOM   3148 C CA  . THR B 2 107 ? -25.917 -93.100  6.212   1.00 116.60 ? 107 THR B CA  1 
ATOM   3149 C C   . THR B 2 107 ? -25.639 -94.587  6.426   1.00 115.72 ? 107 THR B C   1 
ATOM   3150 O O   . THR B 2 107 ? -26.449 -95.433  6.048   1.00 116.54 ? 107 THR B O   1 
ATOM   3151 C CB  . THR B 2 107 ? -24.887 -92.508  5.252   1.00 116.75 ? 107 THR B CB  1 
ATOM   3152 O OG1 . THR B 2 107 ? -25.176 -91.118  5.054   1.00 115.79 ? 107 THR B OG1 1 
ATOM   3153 C CG2 . THR B 2 107 ? -24.941 -93.228  3.920   1.00 118.08 ? 107 THR B CG2 1 
ATOM   3154 N N   . LEU B 2 108 ? -24.492 -94.903  7.022   1.00 115.02 ? 108 LEU B N   1 
ATOM   3155 C CA  . LEU B 2 108 ? -24.135 -96.293  7.287   1.00 115.04 ? 108 LEU B CA  1 
ATOM   3156 C C   . LEU B 2 108 ? -25.272 -96.996  8.007   1.00 115.07 ? 108 LEU B C   1 
ATOM   3157 O O   . LEU B 2 108 ? -25.392 -98.222  7.949   1.00 114.81 ? 108 LEU B O   1 
ATOM   3158 C CB  . LEU B 2 108 ? -22.863 -96.380  8.127   1.00 114.43 ? 108 LEU B CB  1 
ATOM   3159 C CG  . LEU B 2 108 ? -21.614 -95.821  7.451   1.00 115.25 ? 108 LEU B CG  1 
ATOM   3160 C CD1 . LEU B 2 108 ? -20.371 -96.512  7.984   1.00 115.55 ? 108 LEU B CD1 1 
ATOM   3161 C CD2 . LEU B 2 108 ? -21.719 -96.006  5.950   1.00 118.07 ? 108 LEU B CD2 1 
ATOM   3162 N N   . ASP B 2 109 ? -26.097 -96.213  8.696   1.00 115.17 ? 109 ASP B N   1 
ATOM   3163 C CA  . ASP B 2 109 ? -27.357 -96.723  9.218   1.00 113.39 ? 109 ASP B CA  1 
ATOM   3164 C C   . ASP B 2 109 ? -28.436 -96.748  8.135   1.00 112.74 ? 109 ASP B C   1 
ATOM   3165 O O   . ASP B 2 109 ? -29.273 -97.649  8.109   1.00 112.51 ? 109 ASP B O   1 
ATOM   3166 C CB  . ASP B 2 109 ? -27.832 -95.902  10.417  1.00 112.60 ? 109 ASP B CB  1 
ATOM   3167 C CG  . ASP B 2 109 ? -29.084 -96.475  11.048  1.00 111.84 ? 109 ASP B CG  1 
ATOM   3168 O OD1 . ASP B 2 109 ? -28.971 -97.441  11.835  1.00 112.11 ? 109 ASP B OD1 1 
ATOM   3169 O OD2 . ASP B 2 109 ? -30.182 -95.963  10.749  1.00 111.81 ? 109 ASP B OD2 1 
ATOM   3170 N N   . TYR B 2 110 ? -28.409 -95.767  7.234   1.00 112.71 ? 110 TYR B N   1 
ATOM   3171 C CA  . TYR B 2 110 ? -29.406 -95.692  6.169   1.00 112.08 ? 110 TYR B CA  1 
ATOM   3172 C C   . TYR B 2 110 ? -29.438 -96.946  5.303   1.00 113.24 ? 110 TYR B C   1 
ATOM   3173 O O   . TYR B 2 110 ? -30.476 -97.592  5.184   1.00 114.61 ? 110 TYR B O   1 
ATOM   3174 C CB  . TYR B 2 110 ? -29.178 -94.468  5.285   1.00 112.84 ? 110 TYR B CB  1 
ATOM   3175 C CG  . TYR B 2 110 ? -30.111 -94.426  4.099   1.00 116.40 ? 110 TYR B CG  1 
ATOM   3176 C CD1 . TYR B 2 110 ? -31.482 -94.319  4.281   1.00 118.07 ? 110 TYR B CD1 1 
ATOM   3177 C CD2 . TYR B 2 110 ? -29.627 -94.499  2.797   1.00 118.89 ? 110 TYR B CD2 1 
ATOM   3178 C CE1 . TYR B 2 110 ? -32.351 -94.284  3.207   1.00 120.93 ? 110 TYR B CE1 1 
ATOM   3179 C CE2 . TYR B 2 110 ? -30.491 -94.462  1.708   1.00 121.39 ? 110 TYR B CE2 1 
ATOM   3180 C CZ  . TYR B 2 110 ? -31.854 -94.354  1.925   1.00 123.14 ? 110 TYR B CZ  1 
ATOM   3181 O OH  . TYR B 2 110 ? -32.730 -94.315  0.866   1.00 124.04 ? 110 TYR B OH  1 
ATOM   3182 N N   . HIS B 2 111 ? -28.303 -97.287  4.699   1.00 113.27 ? 111 HIS B N   1 
ATOM   3183 C CA  . HIS B 2 111 ? -28.224 -98.461  3.832   1.00 114.44 ? 111 HIS B CA  1 
ATOM   3184 C C   . HIS B 2 111 ? -28.484 -99.737  4.619   1.00 110.70 ? 111 HIS B C   1 
ATOM   3185 O O   . HIS B 2 111 ? -29.226 -100.609 4.173   1.00 109.85 ? 111 HIS B O   1 
ATOM   3186 C CB  . HIS B 2 111 ? -26.861 -98.535  3.132   1.00 118.42 ? 111 HIS B CB  1 
ATOM   3187 C CG  . HIS B 2 111 ? -26.579 -97.366  2.239   1.00 120.54 ? 111 HIS B CG  1 
ATOM   3188 N ND1 . HIS B 2 111 ? -27.573 -96.692  1.562   1.00 121.49 ? 111 HIS B ND1 1 
ATOM   3189 C CD2 . HIS B 2 111 ? -25.418 -96.744  1.920   1.00 120.30 ? 111 HIS B CD2 1 
ATOM   3190 C CE1 . HIS B 2 111 ? -27.038 -95.713  0.856   1.00 122.06 ? 111 HIS B CE1 1 
ATOM   3191 N NE2 . HIS B 2 111 ? -25.731 -95.723  1.053   1.00 122.72 ? 111 HIS B NE2 1 
ATOM   3192 N N   . ASP B 2 112 ? -27.868 -99.837  5.792   1.00 108.53 ? 112 ASP B N   1 
ATOM   3193 C CA  . ASP B 2 112 ? -28.088 -100.966 6.681   1.00 107.85 ? 112 ASP B CA  1 
ATOM   3194 C C   . ASP B 2 112 ? -29.583 -101.208 6.796   1.00 108.79 ? 112 ASP B C   1 
ATOM   3195 O O   . ASP B 2 112 ? -30.051 -102.342 6.704   1.00 108.91 ? 112 ASP B O   1 
ATOM   3196 C CB  . ASP B 2 112 ? -27.498 -100.665 8.060   1.00 109.65 ? 112 ASP B CB  1 
ATOM   3197 C CG  . ASP B 2 112 ? -27.911 -101.677 9.109   1.00 110.18 ? 112 ASP B CG  1 
ATOM   3198 O OD1 . ASP B 2 112 ? -28.969 -101.476 9.745   1.00 110.29 ? 112 ASP B OD1 1 
ATOM   3199 O OD2 . ASP B 2 112 ? -27.176 -102.669 9.301   1.00 112.95 ? 112 ASP B OD2 1 
ATOM   3200 N N   . SER B 2 113 ? -30.332 -100.127 6.979   1.00 109.06 ? 113 SER B N   1 
ATOM   3201 C CA  . SER B 2 113 ? -31.780 -100.203 7.037   1.00 106.11 ? 113 SER B CA  1 
ATOM   3202 C C   . SER B 2 113 ? -32.323 -100.789 5.747   1.00 107.55 ? 113 SER B C   1 
ATOM   3203 O O   . SER B 2 113 ? -33.273 -101.566 5.761   1.00 108.61 ? 113 SER B O   1 
ATOM   3204 C CB  . SER B 2 113 ? -32.374 -98.815  7.235   1.00 107.62 ? 113 SER B CB  1 
ATOM   3205 O OG  . SER B 2 113 ? -31.675 -98.110  8.238   1.00 110.95 ? 113 SER B OG  1 
ATOM   3206 N N   . ASN B 2 114 ? -31.721 -100.405 4.627   1.00 109.00 ? 114 ASN B N   1 
ATOM   3207 C CA  . ASN B 2 114 ? -32.186 -100.865 3.325   1.00 109.65 ? 114 ASN B CA  1 
ATOM   3208 C C   . ASN B 2 114 ? -31.814 -102.316 3.048   1.00 109.20 ? 114 ASN B C   1 
ATOM   3209 O O   . ASN B 2 114 ? -32.433 -102.977 2.216   1.00 107.74 ? 114 ASN B O   1 
ATOM   3210 C CB  . ASN B 2 114 ? -31.669 -99.957  2.209   1.00 111.80 ? 114 ASN B CB  1 
ATOM   3211 C CG  . ASN B 2 114 ? -32.310 -98.583  2.236   1.00 114.78 ? 114 ASN B CG  1 
ATOM   3212 O OD1 . ASN B 2 114 ? -31.709 -97.610  2.687   1.00 115.98 ? 114 ASN B OD1 1 
ATOM   3213 N ND2 . ASN B 2 114 ? -33.543 -98.500  1.754   1.00 114.84 ? 114 ASN B ND2 1 
ATOM   3214 N N   . VAL B 2 115 ? -30.793 -102.810 3.737   1.00 108.64 ? 115 VAL B N   1 
ATOM   3215 C CA  . VAL B 2 115 ? -30.436 -104.215 3.623   1.00 106.24 ? 115 VAL B CA  1 
ATOM   3216 C C   . VAL B 2 115 ? -31.459 -105.033 4.393   1.00 106.82 ? 115 VAL B C   1 
ATOM   3217 O O   . VAL B 2 115 ? -32.034 -105.980 3.862   1.00 107.31 ? 115 VAL B O   1 
ATOM   3218 C CB  . VAL B 2 115 ? -29.037 -104.491 4.185   1.00 107.43 ? 115 VAL B CB  1 
ATOM   3219 C CG1 . VAL B 2 115 ? -28.622 -105.922 3.892   1.00 106.68 ? 115 VAL B CG1 1 
ATOM   3220 C CG2 . VAL B 2 115 ? -28.036 -103.524 3.593   1.00 108.62 ? 115 VAL B CG2 1 
ATOM   3221 N N   . LYS B 2 116 ? -31.699 -104.642 5.641   1.00 105.01 ? 116 LYS B N   1 
ATOM   3222 C CA  . LYS B 2 116 ? -32.765 -105.243 6.424   1.00 103.77 ? 116 LYS B CA  1 
ATOM   3223 C C   . LYS B 2 116 ? -34.019 -105.277 5.563   1.00 104.38 ? 116 LYS B C   1 
ATOM   3224 O O   . LYS B 2 116 ? -34.554 -106.343 5.280   1.00 107.77 ? 116 LYS B O   1 
ATOM   3225 C CB  . LYS B 2 116 ? -33.019 -104.468 7.715   1.00 104.91 ? 116 LYS B CB  1 
ATOM   3226 C CG  . LYS B 2 116 ? -31.804 -104.337 8.629   1.00 105.16 ? 116 LYS B CG  1 
ATOM   3227 C CD  . LYS B 2 116 ? -32.232 -104.100 10.080  1.00 106.47 ? 116 LYS B CD  1 
ATOM   3228 C CE  . LYS B 2 116 ? -31.167 -103.370 10.885  1.00 104.87 ? 116 LYS B CE  1 
ATOM   3229 N NZ  . LYS B 2 116 ? -31.179 -101.900 10.618  1.00 107.28 ? 116 LYS B NZ  1 
ATOM   3230 N N   . ASN B 2 117 ? -34.487 -104.107 5.149   1.00 104.35 ? 117 ASN B N   1 
ATOM   3231 C CA  . ASN B 2 117 ? -35.704 -104.014 4.352   1.00 105.44 ? 117 ASN B CA  1 
ATOM   3232 C C   . ASN B 2 117 ? -35.736 -104.914 3.133   1.00 107.59 ? 117 ASN B C   1 
ATOM   3233 O O   . ASN B 2 117 ? -36.797 -105.396 2.746   1.00 109.57 ? 117 ASN B O   1 
ATOM   3234 C CB  . ASN B 2 117 ? -35.953 -102.580 3.924   1.00 105.92 ? 117 ASN B CB  1 
ATOM   3235 C CG  . ASN B 2 117 ? -36.427 -101.720 5.064   1.00 109.33 ? 117 ASN B CG  1 
ATOM   3236 O OD1 . ASN B 2 117 ? -36.402 -102.132 6.228   1.00 108.44 ? 117 ASN B OD1 1 
ATOM   3237 N ND2 . ASN B 2 117 ? -36.863 -100.512 4.740   1.00 107.62 ? 117 ASN B ND2 1 
ATOM   3238 N N   . LEU B 2 118 ? -34.583 -105.127 2.513   1.00 108.44 ? 118 LEU B N   1 
ATOM   3239 C CA  . LEU B 2 118 ? -34.517 -106.046 1.383   1.00 107.94 ? 118 LEU B CA  1 
ATOM   3240 C C   . LEU B 2 118 ? -34.780 -107.464 1.873   1.00 107.25 ? 118 LEU B C   1 
ATOM   3241 O O   . LEU B 2 118 ? -35.617 -108.185 1.328   1.00 106.81 ? 118 LEU B O   1 
ATOM   3242 C CB  . LEU B 2 118 ? -33.151 -105.981 0.708   1.00 108.68 ? 118 LEU B CB  1 
ATOM   3243 C CG  . LEU B 2 118 ? -33.071 -106.581 -0.703  1.00 112.01 ? 118 LEU B CG  1 
ATOM   3244 C CD1 . LEU B 2 118 ? -33.168 -105.500 -1.777  1.00 115.34 ? 118 LEU B CD1 1 
ATOM   3245 C CD2 . LEU B 2 118 ? -31.791 -107.376 -0.881  1.00 112.84 ? 118 LEU B CD2 1 
ATOM   3246 N N   . TYR B 2 119 ? -34.061 -107.848 2.920   1.00 105.92 ? 119 TYR B N   1 
ATOM   3247 C CA  . TYR B 2 119 ? -34.179 -109.174 3.493   1.00 102.81 ? 119 TYR B CA  1 
ATOM   3248 C C   . TYR B 2 119 ? -35.619 -109.499 3.876   1.00 104.53 ? 119 TYR B C   1 
ATOM   3249 O O   . TYR B 2 119 ? -36.152 -110.531 3.478   1.00 105.39 ? 119 TYR B O   1 
ATOM   3250 C CB  . TYR B 2 119 ? -33.280 -109.284 4.719   1.00 102.99 ? 119 TYR B CB  1 
ATOM   3251 C CG  . TYR B 2 119 ? -33.165 -110.684 5.247   1.00 102.85 ? 119 TYR B CG  1 
ATOM   3252 C CD1 . TYR B 2 119 ? -34.140 -111.216 6.075   1.00 102.41 ? 119 TYR B CD1 1 
ATOM   3253 C CD2 . TYR B 2 119 ? -32.084 -111.480 4.911   1.00 104.12 ? 119 TYR B CD2 1 
ATOM   3254 C CE1 . TYR B 2 119 ? -34.037 -112.507 6.555   1.00 102.78 ? 119 TYR B CE1 1 
ATOM   3255 C CE2 . TYR B 2 119 ? -31.972 -112.767 5.389   1.00 103.98 ? 119 TYR B CE2 1 
ATOM   3256 C CZ  . TYR B 2 119 ? -32.948 -113.276 6.207   1.00 102.77 ? 119 TYR B CZ  1 
ATOM   3257 O OH  . TYR B 2 119 ? -32.823 -114.562 6.673   1.00 103.70 ? 119 TYR B OH  1 
ATOM   3258 N N   . GLU B 2 120 ? -36.249 -108.614 4.641   1.00 105.44 ? 120 GLU B N   1 
ATOM   3259 C CA  . GLU B 2 120 ? -37.567 -108.900 5.210   1.00 106.01 ? 120 GLU B CA  1 
ATOM   3260 C C   . GLU B 2 120 ? -38.669 -108.942 4.165   1.00 107.12 ? 120 GLU B C   1 
ATOM   3261 O O   . GLU B 2 120 ? -39.621 -109.712 4.292   1.00 109.06 ? 120 GLU B O   1 
ATOM   3262 C CB  . GLU B 2 120 ? -37.930 -107.888 6.296   1.00 103.94 ? 120 GLU B CB  1 
ATOM   3263 C CG  . GLU B 2 120 ? -38.252 -108.517 7.638   1.00 104.06 ? 120 GLU B CG  1 
ATOM   3264 C CD  . GLU B 2 120 ? -37.037 -109.144 8.287   1.00 104.97 ? 120 GLU B CD  1 
ATOM   3265 O OE1 . GLU B 2 120 ? -35.902 -108.714 7.983   1.00 103.06 ? 120 GLU B OE1 1 
ATOM   3266 O OE2 . GLU B 2 120 ? -37.221 -110.073 9.100   1.00 106.28 ? 120 GLU B OE2 1 
ATOM   3267 N N   . LYS B 2 121 ? -38.551 -108.109 3.139   1.00 106.63 ? 121 LYS B N   1 
ATOM   3268 C CA  . LYS B 2 121 ? -39.558 -108.084 2.087   1.00 111.03 ? 121 LYS B CA  1 
ATOM   3269 C C   . LYS B 2 121 ? -39.651 -109.437 1.380   1.00 109.80 ? 121 LYS B C   1 
ATOM   3270 O O   . LYS B 2 121 ? -40.713 -109.815 0.881   1.00 108.90 ? 121 LYS B O   1 
ATOM   3271 C CB  . LYS B 2 121 ? -39.280 -106.953 1.090   1.00 113.26 ? 121 LYS B CB  1 
ATOM   3272 C CG  . LYS B 2 121 ? -39.822 -105.578 1.520   1.00 118.12 ? 121 LYS B CG  1 
ATOM   3273 C CD  . LYS B 2 121 ? -41.201 -105.288 0.901   1.00 121.32 ? 121 LYS B CD  1 
ATOM   3274 C CE  . LYS B 2 121 ? -41.866 -104.035 1.486   1.00 117.49 ? 121 LYS B CE  1 
ATOM   3275 N NZ  . LYS B 2 121 ? -41.217 -102.757 1.070   1.00 112.03 ? 121 LYS B NZ  1 
ATOM   3276 N N   . VAL B 2 122 ? -38.532 -110.155 1.333   1.00 108.93 ? 122 VAL B N   1 
ATOM   3277 C CA  . VAL B 2 122 ? -38.516 -111.528 0.839   1.00 107.99 ? 122 VAL B CA  1 
ATOM   3278 C C   . VAL B 2 122 ? -38.966 -112.505 1.920   1.00 107.39 ? 122 VAL B C   1 
ATOM   3279 O O   . VAL B 2 122 ? -39.716 -113.443 1.653   1.00 107.91 ? 122 VAL B O   1 
ATOM   3280 C CB  . VAL B 2 122 ? -37.113 -111.933 0.340   1.00 107.35 ? 122 VAL B CB  1 
ATOM   3281 C CG1 . VAL B 2 122 ? -37.020 -113.443 0.146   1.00 105.88 ? 122 VAL B CG1 1 
ATOM   3282 C CG2 . VAL B 2 122 ? -36.786 -111.202 -0.944  1.00 107.46 ? 122 VAL B CG2 1 
ATOM   3283 N N   . ARG B 2 123 ? -38.501 -112.275 3.144   1.00 107.12 ? 123 ARG B N   1 
ATOM   3284 C CA  . ARG B 2 123 ? -38.757 -113.192 4.248   1.00 105.89 ? 123 ARG B CA  1 
ATOM   3285 C C   . ARG B 2 123 ? -40.242 -113.329 4.566   1.00 105.71 ? 123 ARG B C   1 
ATOM   3286 O O   . ARG B 2 123 ? -40.699 -114.390 4.987   1.00 105.36 ? 123 ARG B O   1 
ATOM   3287 C CB  . ARG B 2 123 ? -37.987 -112.757 5.495   1.00 102.91 ? 123 ARG B CB  1 
ATOM   3288 C CG  . ARG B 2 123 ? -38.158 -113.683 6.673   1.00 103.34 ? 123 ARG B CG  1 
ATOM   3289 C CD  . ARG B 2 123 ? -38.744 -112.945 7.849   1.00 104.57 ? 123 ARG B CD  1 
ATOM   3290 N NE  . ARG B 2 123 ? -39.985 -112.272 7.488   1.00 105.87 ? 123 ARG B NE  1 
ATOM   3291 C CZ  . ARG B 2 123 ? -40.705 -111.546 8.334   1.00 107.12 ? 123 ARG B CZ  1 
ATOM   3292 N NH1 . ARG B 2 123 ? -40.301 -111.399 9.590   1.00 106.92 ? 123 ARG B NH1 1 
ATOM   3293 N NH2 . ARG B 2 123 ? -41.825 -110.966 7.926   1.00 106.46 ? 123 ARG B NH2 1 
ATOM   3294 N N   . SER B 2 124 ? -40.989 -112.248 4.376   1.00 107.50 ? 124 SER B N   1 
ATOM   3295 C CA  . SER B 2 124 ? -42.432 -112.289 4.558   1.00 106.54 ? 124 SER B CA  1 
ATOM   3296 C C   . SER B 2 124 ? -43.088 -112.917 3.343   1.00 106.00 ? 124 SER B C   1 
ATOM   3297 O O   . SER B 2 124 ? -44.085 -113.627 3.454   1.00 108.49 ? 124 SER B O   1 
ATOM   3298 C CB  . SER B 2 124 ? -42.996 -110.887 4.802   1.00 105.21 ? 124 SER B CB  1 
ATOM   3299 O OG  . SER B 2 124 ? -42.817 -110.498 6.154   1.00 102.92 ? 124 SER B OG  1 
ATOM   3300 N N   . GLN B 2 125 ? -42.514 -112.653 2.179   1.00 106.89 ? 125 GLN B N   1 
ATOM   3301 C CA  . GLN B 2 125 ? -43.050 -113.180 0.938   1.00 108.30 ? 125 GLN B CA  1 
ATOM   3302 C C   . GLN B 2 125 ? -42.955 -114.702 0.921   1.00 109.12 ? 125 GLN B C   1 
ATOM   3303 O O   . GLN B 2 125 ? -43.940 -115.394 0.669   1.00 108.52 ? 125 GLN B O   1 
ATOM   3304 C CB  . GLN B 2 125 ? -42.290 -112.592 -0.242  1.00 107.11 ? 125 GLN B CB  1 
ATOM   3305 C CG  . GLN B 2 125 ? -43.173 -112.228 -1.412  1.00 112.18 ? 125 GLN B CG  1 
ATOM   3306 C CD  . GLN B 2 125 ? -42.380 -111.683 -2.584  1.00 116.11 ? 125 GLN B CD  1 
ATOM   3307 O OE1 . GLN B 2 125 ? -41.160 -111.538 -2.505  1.00 116.08 ? 125 GLN B OE1 1 
ATOM   3308 N NE2 . GLN B 2 125 ? -43.068 -111.379 -3.681  1.00 114.69 ? 125 GLN B NE2 1 
ATOM   3309 N N   . LEU B 2 126 ? -41.762 -115.221 1.193   1.00 108.11 ? 126 LEU B N   1 
ATOM   3310 C CA  . LEU B 2 126 ? -41.541 -116.661 1.173   1.00 107.30 ? 126 LEU B CA  1 
ATOM   3311 C C   . LEU B 2 126 ? -42.126 -117.352 2.403   1.00 106.70 ? 126 LEU B C   1 
ATOM   3312 O O   . LEU B 2 126 ? -42.777 -118.384 2.282   1.00 108.36 ? 126 LEU B O   1 
ATOM   3313 C CB  . LEU B 2 126 ? -40.048 -116.981 1.067   1.00 106.76 ? 126 LEU B CB  1 
ATOM   3314 C CG  . LEU B 2 126 ? -39.241 -116.284 -0.028  1.00 103.91 ? 126 LEU B CG  1 
ATOM   3315 C CD1 . LEU B 2 126 ? -37.846 -116.875 -0.104  1.00 99.49  ? 126 LEU B CD1 1 
ATOM   3316 C CD2 . LEU B 2 126 ? -39.948 -116.412 -1.355  1.00 108.51 ? 126 LEU B CD2 1 
ATOM   3317 N N   . LYS B 2 127 ? -41.891 -116.777 3.580   1.00 106.63 ? 127 LYS B N   1 
ATOM   3318 C CA  . LYS B 2 127 ? -42.283 -117.401 4.845   1.00 106.68 ? 127 LYS B CA  1 
ATOM   3319 C C   . LYS B 2 127 ? -41.881 -118.870 4.897   1.00 106.89 ? 127 LYS B C   1 
ATOM   3320 O O   . LYS B 2 127 ? -40.714 -119.219 4.722   1.00 107.17 ? 127 LYS B O   1 
ATOM   3321 C CB  . LYS B 2 127 ? -43.791 -117.299 5.082   1.00 103.89 ? 127 LYS B CB  1 
ATOM   3322 C CG  . LYS B 2 127 ? -44.497 -116.302 4.216   1.00 103.00 ? 127 LYS B CG  1 
ATOM   3323 C CD  . LYS B 2 127 ? -45.987 -116.453 4.367   1.00 105.17 ? 127 LYS B CD  1 
ATOM   3324 C CE  . LYS B 2 127 ? -46.730 -115.590 3.370   1.00 109.12 ? 127 LYS B CE  1 
ATOM   3325 N NZ  . LYS B 2 127 ? -48.198 -115.815 3.456   1.00 109.83 ? 127 LYS B NZ  1 
ATOM   3326 N N   . ASN B 2 128 ? -42.875 -119.721 5.133   1.00 107.82 ? 128 ASN B N   1 
ATOM   3327 C CA  . ASN B 2 128 ? -42.673 -121.160 5.271   1.00 106.24 ? 128 ASN B CA  1 
ATOM   3328 C C   . ASN B 2 128 ? -41.963 -121.771 4.068   1.00 104.91 ? 128 ASN B C   1 
ATOM   3329 O O   . ASN B 2 128 ? -41.335 -122.818 4.170   1.00 105.71 ? 128 ASN B O   1 
ATOM   3330 C CB  . ASN B 2 128 ? -44.021 -121.864 5.482   1.00 104.94 ? 128 ASN B CB  1 
ATOM   3331 C CG  . ASN B 2 128 ? -44.880 -121.188 6.544   1.00 106.91 ? 128 ASN B CG  1 
ATOM   3332 O OD1 . ASN B 2 128 ? -45.927 -120.605 6.247   1.00 103.25 ? 128 ASN B OD1 1 
ATOM   3333 N ND2 . ASN B 2 128 ? -44.438 -121.268 7.794   1.00 110.33 ? 128 ASN B ND2 1 
ATOM   3334 N N   . ASN B 2 129 ? -42.059 -121.108 2.924   1.00 105.55 ? 129 ASN B N   1 
ATOM   3335 C CA  . ASN B 2 129 ? -41.534 -121.667 1.688   1.00 105.25 ? 129 ASN B CA  1 
ATOM   3336 C C   . ASN B 2 129 ? -40.028 -121.881 1.642   1.00 104.51 ? 129 ASN B C   1 
ATOM   3337 O O   . ASN B 2 129 ? -39.561 -122.812 0.996   1.00 106.99 ? 129 ASN B O   1 
ATOM   3338 C CB  . ASN B 2 129 ? -41.997 -120.847 0.489   1.00 107.90 ? 129 ASN B CB  1 
ATOM   3339 C CG  . ASN B 2 129 ? -43.430 -121.145 0.116   1.00 110.74 ? 129 ASN B CG  1 
ATOM   3340 O OD1 . ASN B 2 129 ? -44.013 -122.113 0.602   1.00 109.73 ? 129 ASN B OD1 1 
ATOM   3341 N ND2 . ASN B 2 129 ? -44.005 -120.324 -0.754  1.00 113.78 ? 129 ASN B ND2 1 
ATOM   3342 N N   . ALA B 2 130 ? -39.267 -121.031 2.319   1.00 104.52 ? 130 ALA B N   1 
ATOM   3343 C CA  . ALA B 2 130 ? -37.814 -121.169 2.303   1.00 103.21 ? 130 ALA B CA  1 
ATOM   3344 C C   . ALA B 2 130 ? -37.234 -121.143 3.708   1.00 103.19 ? 130 ALA B C   1 
ATOM   3345 O O   . ALA B 2 130 ? -37.815 -120.547 4.612   1.00 105.55 ? 130 ALA B O   1 
ATOM   3346 C CB  . ALA B 2 130 ? -37.188 -120.081 1.450   1.00 107.06 ? 130 ALA B CB  1 
ATOM   3347 N N   . LYS B 2 131 ? -36.088 -121.792 3.885   1.00 102.34 ? 131 LYS B N   1 
ATOM   3348 C CA  . LYS B 2 131 ? -35.401 -121.798 5.172   1.00 103.53 ? 131 LYS B CA  1 
ATOM   3349 C C   . LYS B 2 131 ? -34.590 -120.531 5.361   1.00 103.68 ? 131 LYS B C   1 
ATOM   3350 O O   . LYS B 2 131 ? -33.843 -120.128 4.470   1.00 105.86 ? 131 LYS B O   1 
ATOM   3351 C CB  . LYS B 2 131 ? -34.480 -123.016 5.286   1.00 103.15 ? 131 LYS B CB  1 
ATOM   3352 C CG  . LYS B 2 131 ? -33.719 -123.104 6.607   1.00 101.83 ? 131 LYS B CG  1 
ATOM   3353 C CD  . LYS B 2 131 ? -32.657 -124.205 6.580   1.00 102.29 ? 131 LYS B CD  1 
ATOM   3354 C CE  . LYS B 2 131 ? -32.063 -124.422 7.968   1.00 103.78 ? 131 LYS B CE  1 
ATOM   3355 N NZ  . LYS B 2 131 ? -31.007 -125.471 7.995   1.00 101.80 ? 131 LYS B NZ  1 
ATOM   3356 N N   . GLU B 2 132 ? -34.731 -119.899 6.518   1.00 100.42 ? 132 GLU B N   1 
ATOM   3357 C CA  . GLU B 2 132 ? -33.870 -118.777 6.813   1.00 102.19 ? 132 GLU B CA  1 
ATOM   3358 C C   . GLU B 2 132 ? -32.676 -119.377 7.510   1.00 103.51 ? 132 GLU B C   1 
ATOM   3359 O O   . GLU B 2 132 ? -32.756 -119.790 8.666   1.00 107.10 ? 132 GLU B O   1 
ATOM   3360 C CB  . GLU B 2 132 ? -34.550 -117.796 7.765   1.00 104.16 ? 132 GLU B CB  1 
ATOM   3361 C CG  . GLU B 2 132 ? -35.239 -116.615 7.106   1.00 102.59 ? 132 GLU B CG  1 
ATOM   3362 C CD  . GLU B 2 132 ? -35.344 -115.432 8.047   1.00 105.54 ? 132 GLU B CD  1 
ATOM   3363 O OE1 . GLU B 2 132 ? -34.287 -114.875 8.412   1.00 105.76 ? 132 GLU B OE1 1 
ATOM   3364 O OE2 . GLU B 2 132 ? -36.475 -115.077 8.443   1.00 107.55 ? 132 GLU B OE2 1 
ATOM   3365 N N   . ILE B 2 133 ? -31.554 -119.408 6.809   1.00 102.41 ? 133 ILE B N   1 
ATOM   3366 C CA  . ILE B 2 133 ? -30.329 -119.887 7.403   1.00 103.64 ? 133 ILE B CA  1 
ATOM   3367 C C   . ILE B 2 133 ? -29.612 -118.650 7.906   1.00 105.75 ? 133 ILE B C   1 
ATOM   3368 O O   . ILE B 2 133 ? -28.551 -118.729 8.519   1.00 104.23 ? 133 ILE B O   1 
ATOM   3369 C CB  . ILE B 2 133 ? -29.472 -120.642 6.379   1.00 104.06 ? 133 ILE B CB  1 
ATOM   3370 C CG1 . ILE B 2 133 ? -28.264 -121.271 7.071   1.00 108.11 ? 133 ILE B CG1 1 
ATOM   3371 C CG2 . ILE B 2 133 ? -29.058 -119.717 5.255   1.00 104.26 ? 133 ILE B CG2 1 
ATOM   3372 C CD1 . ILE B 2 133 ? -28.628 -122.165 8.243   1.00 107.52 ? 133 ILE B CD1 1 
ATOM   3373 N N   . GLY B 2 134 ? -30.236 -117.501 7.653   1.00 108.24 ? 134 GLY B N   1 
ATOM   3374 C CA  . GLY B 2 134 ? -29.665 -116.213 7.994   1.00 108.48 ? 134 GLY B CA  1 
ATOM   3375 C C   . GLY B 2 134 ? -28.671 -115.755 6.944   1.00 108.74 ? 134 GLY B C   1 
ATOM   3376 O O   . GLY B 2 134 ? -28.712 -116.209 5.798   1.00 108.30 ? 134 GLY B O   1 
ATOM   3377 N N   . ASN B 2 135 ? -27.780 -114.848 7.333   1.00 110.20 ? 135 ASN B N   1 
ATOM   3378 C CA  . ASN B 2 135 ? -26.721 -114.380 6.444   1.00 108.62 ? 135 ASN B CA  1 
ATOM   3379 C C   . ASN B 2 135 ? -27.276 -113.864 5.129   1.00 108.01 ? 135 ASN B C   1 
ATOM   3380 O O   . ASN B 2 135 ? -26.608 -113.930 4.098   1.00 106.61 ? 135 ASN B O   1 
ATOM   3381 C CB  . ASN B 2 135 ? -25.729 -115.503 6.160   1.00 107.92 ? 135 ASN B CB  1 
ATOM   3382 C CG  . ASN B 2 135 ? -25.824 -116.632 7.165   1.00 110.46 ? 135 ASN B CG  1 
ATOM   3383 O OD1 . ASN B 2 135 ? -26.165 -116.422 8.331   1.00 107.96 ? 135 ASN B OD1 1 
ATOM   3384 N ND2 . ASN B 2 135 ? -25.525 -117.845 6.713   1.00 111.34 ? 135 ASN B ND2 1 
ATOM   3385 N N   . GLY B 2 136 ? -28.502 -113.351 5.175   1.00 108.74 ? 136 GLY B N   1 
ATOM   3386 C CA  . GLY B 2 136 ? -29.190 -112.898 3.979   1.00 109.09 ? 136 GLY B CA  1 
ATOM   3387 C C   . GLY B 2 136 ? -29.610 -114.067 3.111   1.00 106.98 ? 136 GLY B C   1 
ATOM   3388 O O   . GLY B 2 136 ? -30.256 -113.894 2.079   1.00 104.89 ? 136 GLY B O   1 
ATOM   3389 N N   . CYS B 2 137 ? -29.258 -115.268 3.558   1.00 108.58 ? 137 CYS B N   1 
ATOM   3390 C CA  . CYS B 2 137 ? -29.439 -116.474 2.762   1.00 108.88 ? 137 CYS B CA  1 
ATOM   3391 C C   . CYS B 2 137 ? -30.745 -117.210 3.011   1.00 108.18 ? 137 CYS B C   1 
ATOM   3392 O O   . CYS B 2 137 ? -31.170 -117.404 4.152   1.00 106.71 ? 137 CYS B O   1 
ATOM   3393 C CB  . CYS B 2 137 ? -28.268 -117.432 2.981   1.00 108.40 ? 137 CYS B CB  1 
ATOM   3394 S SG  . CYS B 2 137 ? -26.734 -116.862 2.249   1.00 118.60 ? 137 CYS B SG  1 
ATOM   3395 N N   . PHE B 2 138 ? -31.370 -117.628 1.921   1.00 106.82 ? 138 PHE B N   1 
ATOM   3396 C CA  . PHE B 2 138 ? -32.544 -118.468 1.996   1.00 106.78 ? 138 PHE B CA  1 
ATOM   3397 C C   . PHE B 2 138 ? -32.248 -119.746 1.240   1.00 108.81 ? 138 PHE B C   1 
ATOM   3398 O O   . PHE B 2 138 ? -31.590 -119.725 0.201   1.00 108.57 ? 138 PHE B O   1 
ATOM   3399 C CB  . PHE B 2 138 ? -33.739 -117.768 1.358   1.00 107.30 ? 138 PHE B CB  1 
ATOM   3400 C CG  . PHE B 2 138 ? -34.040 -116.423 1.944   1.00 106.05 ? 138 PHE B CG  1 
ATOM   3401 C CD1 . PHE B 2 138 ? -33.258 -115.326 1.633   1.00 106.77 ? 138 PHE B CD1 1 
ATOM   3402 C CD2 . PHE B 2 138 ? -35.120 -116.250 2.792   1.00 104.26 ? 138 PHE B CD2 1 
ATOM   3403 C CE1 . PHE B 2 138 ? -33.541 -114.084 2.168   1.00 106.75 ? 138 PHE B CE1 1 
ATOM   3404 C CE2 . PHE B 2 138 ? -35.407 -115.014 3.329   1.00 105.51 ? 138 PHE B CE2 1 
ATOM   3405 C CZ  . PHE B 2 138 ? -34.618 -113.928 3.017   1.00 105.56 ? 138 PHE B CZ  1 
ATOM   3406 N N   . GLU B 2 139 ? -32.719 -120.866 1.769   1.00 109.23 ? 139 GLU B N   1 
ATOM   3407 C CA  . GLU B 2 139 ? -32.644 -122.113 1.029   1.00 110.91 ? 139 GLU B CA  1 
ATOM   3408 C C   . GLU B 2 139 ? -34.048 -122.547 0.664   1.00 108.76 ? 139 GLU B C   1 
ATOM   3409 O O   . GLU B 2 139 ? -34.825 -122.957 1.525   1.00 107.39 ? 139 GLU B O   1 
ATOM   3410 C CB  . GLU B 2 139 ? -31.952 -123.195 1.849   1.00 110.47 ? 139 GLU B CB  1 
ATOM   3411 C CG  . GLU B 2 139 ? -30.856 -123.919 1.089   1.00 111.97 ? 139 GLU B CG  1 
ATOM   3412 C CD  . GLU B 2 139 ? -29.716 -124.318 1.994   1.00 115.42 ? 139 GLU B CD  1 
ATOM   3413 O OE1 . GLU B 2 139 ? -29.968 -124.513 3.203   1.00 111.11 ? 139 GLU B OE1 1 
ATOM   3414 O OE2 . GLU B 2 139 ? -28.571 -124.423 1.500   1.00 116.92 ? 139 GLU B OE2 1 
ATOM   3415 N N   . PHE B 2 140 ? -34.369 -122.461 -0.618  1.00 109.24 ? 140 PHE B N   1 
ATOM   3416 C CA  . PHE B 2 140 ? -35.712 -122.781 -1.071  1.00 110.62 ? 140 PHE B CA  1 
ATOM   3417 C C   . PHE B 2 140 ? -36.072 -124.241 -0.807  1.00 111.64 ? 140 PHE B C   1 
ATOM   3418 O O   . PHE B 2 140 ? -35.303 -125.149 -1.132  1.00 112.43 ? 140 PHE B O   1 
ATOM   3419 C CB  . PHE B 2 140 ? -35.862 -122.466 -2.557  1.00 112.15 ? 140 PHE B CB  1 
ATOM   3420 C CG  . PHE B 2 140 ? -36.026 -121.006 -2.853  1.00 113.31 ? 140 PHE B CG  1 
ATOM   3421 C CD1 . PHE B 2 140 ? -34.922 -120.196 -3.060  1.00 113.02 ? 140 PHE B CD1 1 
ATOM   3422 C CD2 . PHE B 2 140 ? -37.290 -120.444 -2.935  1.00 113.23 ? 140 PHE B CD2 1 
ATOM   3423 C CE1 . PHE B 2 140 ? -35.077 -118.855 -3.338  1.00 112.53 ? 140 PHE B CE1 1 
ATOM   3424 C CE2 . PHE B 2 140 ? -37.452 -119.102 -3.212  1.00 112.87 ? 140 PHE B CE2 1 
ATOM   3425 C CZ  . PHE B 2 140 ? -36.345 -118.306 -3.414  1.00 113.10 ? 140 PHE B CZ  1 
ATOM   3426 N N   . TYR B 2 141 ? -37.245 -124.459 -0.215  1.00 110.58 ? 141 TYR B N   1 
ATOM   3427 C CA  . TYR B 2 141 ? -37.764 -125.809 -0.024  1.00 108.63 ? 141 TYR B CA  1 
ATOM   3428 C C   . TYR B 2 141 ? -38.250 -126.353 -1.360  1.00 110.67 ? 141 TYR B C   1 
ATOM   3429 O O   . TYR B 2 141 ? -38.014 -127.514 -1.692  1.00 110.45 ? 141 TYR B O   1 
ATOM   3430 C CB  . TYR B 2 141 ? -38.908 -125.824 0.992   1.00 106.23 ? 141 TYR B CB  1 
ATOM   3431 C CG  . TYR B 2 141 ? -38.472 -125.737 2.438   1.00 105.89 ? 141 TYR B CG  1 
ATOM   3432 C CD1 . TYR B 2 141 ? -37.621 -126.690 2.989   1.00 107.48 ? 141 TYR B CD1 1 
ATOM   3433 C CD2 . TYR B 2 141 ? -38.933 -124.718 3.262   1.00 104.88 ? 141 TYR B CD2 1 
ATOM   3434 C CE1 . TYR B 2 141 ? -37.226 -126.618 4.319   1.00 107.46 ? 141 TYR B CE1 1 
ATOM   3435 C CE2 . TYR B 2 141 ? -38.547 -124.639 4.592   1.00 105.57 ? 141 TYR B CE2 1 
ATOM   3436 C CZ  . TYR B 2 141 ? -37.692 -125.590 5.116   1.00 105.51 ? 141 TYR B CZ  1 
ATOM   3437 O OH  . TYR B 2 141 ? -37.307 -125.512 6.438   1.00 101.10 ? 141 TYR B OH  1 
ATOM   3438 N N   . HIS B 2 142 ? -38.926 -125.499 -2.125  1.00 112.42 ? 142 HIS B N   1 
ATOM   3439 C CA  . HIS B 2 142 ? -39.395 -125.857 -3.461  1.00 114.94 ? 142 HIS B CA  1 
ATOM   3440 C C   . HIS B 2 142 ? -38.364 -125.509 -4.533  1.00 116.44 ? 142 HIS B C   1 
ATOM   3441 O O   . HIS B 2 142 ? -37.271 -125.036 -4.224  1.00 117.58 ? 142 HIS B O   1 
ATOM   3442 C CB  . HIS B 2 142 ? -40.721 -125.156 -3.769  1.00 116.89 ? 142 HIS B CB  1 
ATOM   3443 C CG  . HIS B 2 142 ? -40.591 -123.686 -4.037  1.00 117.73 ? 142 HIS B CG  1 
ATOM   3444 N ND1 . HIS B 2 142 ? -40.072 -123.183 -5.211  1.00 118.47 ? 142 HIS B ND1 1 
ATOM   3445 C CD2 . HIS B 2 142 ? -40.936 -122.610 -3.289  1.00 115.56 ? 142 HIS B CD2 1 
ATOM   3446 C CE1 . HIS B 2 142 ? -40.094 -121.862 -5.171  1.00 117.64 ? 142 HIS B CE1 1 
ATOM   3447 N NE2 . HIS B 2 142 ? -40.616 -121.489 -4.017  1.00 117.12 ? 142 HIS B NE2 1 
ATOM   3448 N N   . LYS B 2 143 ? -38.711 -125.742 -5.793  1.00 117.17 ? 143 LYS B N   1 
ATOM   3449 C CA  . LYS B 2 143 ? -37.811 -125.399 -6.888  1.00 117.98 ? 143 LYS B CA  1 
ATOM   3450 C C   . LYS B 2 143 ? -38.140 -124.020 -7.444  1.00 118.71 ? 143 LYS B C   1 
ATOM   3451 O O   . LYS B 2 143 ? -39.203 -123.825 -8.038  1.00 117.98 ? 143 LYS B O   1 
ATOM   3452 C CB  . LYS B 2 143 ? -37.887 -126.446 -8.004  1.00 117.51 ? 143 LYS B CB  1 
ATOM   3453 C CG  . LYS B 2 143 ? -37.140 -127.741 -7.709  1.00 116.47 ? 143 LYS B CG  1 
ATOM   3454 C CD  . LYS B 2 143 ? -35.647 -127.496 -7.521  1.00 116.85 ? 143 LYS B CD  1 
ATOM   3455 C CE  . LYS B 2 143 ? -34.906 -128.781 -7.190  1.00 117.01 ? 143 LYS B CE  1 
ATOM   3456 N NZ  . LYS B 2 143 ? -33.478 -128.525 -6.845  1.00 119.08 ? 143 LYS B NZ  1 
ATOM   3457 N N   . CYS B 2 144 ? -37.231 -123.065 -7.257  1.00 118.84 ? 144 CYS B N   1 
ATOM   3458 C CA  . CYS B 2 144 ? -37.427 -121.731 -7.820  1.00 118.39 ? 144 CYS B CA  1 
ATOM   3459 C C   . CYS B 2 144 ? -36.493 -121.472 -8.999  1.00 120.20 ? 144 CYS B C   1 
ATOM   3460 O O   . CYS B 2 144 ? -35.269 -121.527 -8.867  1.00 120.32 ? 144 CYS B O   1 
ATOM   3461 C CB  . CYS B 2 144 ? -37.267 -120.638 -6.755  1.00 115.58 ? 144 CYS B CB  1 
ATOM   3462 S SG  . CYS B 2 144 ? -38.066 -119.048 -7.168  1.00 115.61 ? 144 CYS B SG  1 
ATOM   3463 N N   . ASP B 2 145 ? -37.090 -121.204 -10.156 1.00 120.38 ? 145 ASP B N   1 
ATOM   3464 C CA  . ASP B 2 145 ? -36.343 -120.799 -11.331 1.00 118.85 ? 145 ASP B CA  1 
ATOM   3465 C C   . ASP B 2 145 ? -36.962 -119.527 -11.881 1.00 118.72 ? 145 ASP B C   1 
ATOM   3466 O O   . ASP B 2 145 ? -38.075 -119.150 -11.514 1.00 116.40 ? 145 ASP B O   1 
ATOM   3467 C CB  . ASP B 2 145 ? -36.326 -121.898 -12.389 1.00 118.02 ? 145 ASP B CB  1 
ATOM   3468 C CG  . ASP B 2 145 ? -35.028 -121.923 -13.177 1.00 121.92 ? 145 ASP B CG  1 
ATOM   3469 O OD1 . ASP B 2 145 ? -34.025 -122.441 -12.640 1.00 123.34 ? 145 ASP B OD1 1 
ATOM   3470 O OD2 . ASP B 2 145 ? -35.010 -121.432 -14.328 1.00 122.06 ? 145 ASP B OD2 1 
ATOM   3471 N N   . ASN B 2 146 ? -36.233 -118.891 -12.785 1.00 120.33 ? 146 ASN B N   1 
ATOM   3472 C CA  . ASN B 2 146 ? -36.479 -117.510 -13.166 1.00 119.11 ? 146 ASN B CA  1 
ATOM   3473 C C   . ASN B 2 146 ? -37.918 -117.226 -13.607 1.00 119.16 ? 146 ASN B C   1 
ATOM   3474 O O   . ASN B 2 146 ? -38.603 -118.099 -14.139 1.00 119.45 ? 146 ASN B O   1 
ATOM   3475 C CB  . ASN B 2 146 ? -35.466 -117.098 -14.234 1.00 121.10 ? 146 ASN B CB  1 
ATOM   3476 C CG  . ASN B 2 146 ? -34.136 -117.834 -14.083 1.00 121.93 ? 146 ASN B CG  1 
ATOM   3477 O OD1 . ASN B 2 146 ? -33.790 -118.299 -12.991 1.00 119.37 ? 146 ASN B OD1 1 
ATOM   3478 N ND2 . ASN B 2 146 ? -33.393 -117.953 -15.183 1.00 123.63 ? 146 ASN B ND2 1 
ATOM   3479 N N   . THR B 2 147 ? -38.351 -115.994 -13.350 1.00 118.87 ? 147 THR B N   1 
ATOM   3480 C CA  . THR B 2 147 ? -39.742 -115.542 -13.459 1.00 120.35 ? 147 THR B CA  1 
ATOM   3481 C C   . THR B 2 147 ? -40.560 -115.982 -12.243 1.00 119.02 ? 147 THR B C   1 
ATOM   3482 O O   . THR B 2 147 ? -41.615 -115.413 -11.967 1.00 118.89 ? 147 THR B O   1 
ATOM   3483 C CB  . THR B 2 147 ? -40.432 -116.010 -14.772 1.00 120.69 ? 147 THR B CB  1 
ATOM   3484 O OG1 . THR B 2 147 ? -40.922 -114.875 -15.500 1.00 121.19 ? 147 THR B OG1 1 
ATOM   3485 C CG2 . THR B 2 147 ? -41.594 -116.936 -14.467 1.00 119.21 ? 147 THR B CG2 1 
ATOM   3486 N N   . CYS B 2 148 ? -40.068 -116.985 -11.515 1.00 117.74 ? 148 CYS B N   1 
ATOM   3487 C CA  . CYS B 2 148 ? -40.448 -117.177 -10.117 1.00 115.93 ? 148 CYS B CA  1 
ATOM   3488 C C   . CYS B 2 148 ? -39.547 -116.305 -9.273  1.00 115.67 ? 148 CYS B C   1 
ATOM   3489 O O   . CYS B 2 148 ? -39.981 -115.656 -8.324  1.00 115.93 ? 148 CYS B O   1 
ATOM   3490 C CB  . CYS B 2 148 ? -40.268 -118.621 -9.674  1.00 118.17 ? 148 CYS B CB  1 
ATOM   3491 S SG  . CYS B 2 148 ? -39.943 -118.757 -7.891  1.00 119.38 ? 148 CYS B SG  1 
ATOM   3492 N N   . MET B 2 149 ? -38.268 -116.334 -9.625  1.00 116.80 ? 149 MET B N   1 
ATOM   3493 C CA  . MET B 2 149 ? -37.258 -115.514 -8.984  1.00 115.38 ? 149 MET B CA  1 
ATOM   3494 C C   . MET B 2 149 ? -37.624 -114.053 -9.136  1.00 115.03 ? 149 MET B C   1 
ATOM   3495 O O   . MET B 2 149 ? -37.938 -113.371 -8.163  1.00 113.27 ? 149 MET B O   1 
ATOM   3496 C CB  . MET B 2 149 ? -35.901 -115.757 -9.636  1.00 115.25 ? 149 MET B CB  1 
ATOM   3497 C CG  . MET B 2 149 ? -34.814 -116.131 -8.660  1.00 115.80 ? 149 MET B CG  1 
ATOM   3498 S SD  . MET B 2 149 ? -34.358 -117.863 -8.821  1.00 126.08 ? 149 MET B SD  1 
ATOM   3499 C CE  . MET B 2 149 ? -33.313 -118.087 -7.384  1.00 116.07 ? 149 MET B CE  1 
ATOM   3500 N N   . GLU B 2 150 ? -37.571 -113.578 -10.375 1.00 115.72 ? 150 GLU B N   1 
ATOM   3501 C CA  . GLU B 2 150 ? -37.920 -112.203 -10.682 1.00 115.60 ? 150 GLU B CA  1 
ATOM   3502 C C   . GLU B 2 150 ? -39.315 -111.891 -10.159 1.00 116.77 ? 150 GLU B C   1 
ATOM   3503 O O   . GLU B 2 150 ? -39.605 -110.755 -9.787  1.00 116.72 ? 150 GLU B O   1 
ATOM   3504 C CB  . GLU B 2 150 ? -37.826 -111.944 -12.190 1.00 115.98 ? 150 GLU B CB  1 
ATOM   3505 C CG  . GLU B 2 150 ? -36.409 -111.640 -12.695 1.00 118.19 ? 150 GLU B CG  1 
ATOM   3506 C CD  . GLU B 2 150 ? -35.430 -112.786 -12.475 1.00 115.94 ? 150 GLU B CD  1 
ATOM   3507 O OE1 . GLU B 2 150 ? -35.878 -113.904 -12.145 1.00 118.59 ? 150 GLU B OE1 1 
ATOM   3508 O OE2 . GLU B 2 150 ? -34.209 -112.565 -12.629 1.00 111.41 ? 150 GLU B OE2 1 
ATOM   3509 N N   . SER B 2 151 ? -40.171 -112.909 -10.120 1.00 117.49 ? 151 SER B N   1 
ATOM   3510 C CA  . SER B 2 151 ? -41.498 -112.758 -9.536  1.00 116.41 ? 151 SER B CA  1 
ATOM   3511 C C   . SER B 2 151 ? -41.350 -112.256 -8.109  1.00 114.61 ? 151 SER B C   1 
ATOM   3512 O O   . SER B 2 151 ? -41.955 -111.256 -7.727  1.00 114.09 ? 151 SER B O   1 
ATOM   3513 C CB  . SER B 2 151 ? -42.263 -114.085 -9.547  1.00 118.15 ? 151 SER B CB  1 
ATOM   3514 O OG  . SER B 2 151 ? -41.834 -114.947 -8.504  1.00 116.62 ? 151 SER B OG  1 
ATOM   3515 N N   . VAL B 2 152 ? -40.546 -112.963 -7.322  1.00 114.62 ? 152 VAL B N   1 
ATOM   3516 C CA  . VAL B 2 152 ? -40.235 -112.522 -5.971  1.00 114.95 ? 152 VAL B CA  1 
ATOM   3517 C C   . VAL B 2 152 ? -39.747 -111.081 -6.015  1.00 115.30 ? 152 VAL B C   1 
ATOM   3518 O O   . VAL B 2 152 ? -40.274 -110.218 -5.316  1.00 113.45 ? 152 VAL B O   1 
ATOM   3519 C CB  . VAL B 2 152 ? -39.141 -113.387 -5.326  1.00 113.53 ? 152 VAL B CB  1 
ATOM   3520 C CG1 . VAL B 2 152 ? -38.731 -112.800 -3.992  1.00 109.53 ? 152 VAL B CG1 1 
ATOM   3521 C CG2 . VAL B 2 152 ? -39.615 -114.820 -5.164  1.00 114.07 ? 152 VAL B CG2 1 
ATOM   3522 N N   . LYS B 2 153 ? -38.743 -110.829 -6.852  1.00 116.13 ? 153 LYS B N   1 
ATOM   3523 C CA  . LYS B 2 153 ? -38.180 -109.491 -7.011  1.00 114.67 ? 153 LYS B CA  1 
ATOM   3524 C C   . LYS B 2 153 ? -39.225 -108.444 -7.391  1.00 117.31 ? 153 LYS B C   1 
ATOM   3525 O O   . LYS B 2 153 ? -39.250 -107.363 -6.807  1.00 118.44 ? 153 LYS B O   1 
ATOM   3526 C CB  . LYS B 2 153 ? -37.044 -109.506 -8.032  1.00 112.25 ? 153 LYS B CB  1 
ATOM   3527 C CG  . LYS B 2 153 ? -35.799 -110.192 -7.525  1.00 112.22 ? 153 LYS B CG  1 
ATOM   3528 C CD  . LYS B 2 153 ? -34.946 -110.698 -8.674  1.00 114.20 ? 153 LYS B CD  1 
ATOM   3529 C CE  . LYS B 2 153 ? -33.826 -111.596 -8.173  1.00 113.03 ? 153 LYS B CE  1 
ATOM   3530 N NZ  . LYS B 2 153 ? -33.121 -112.284 -9.293  1.00 116.13 ? 153 LYS B NZ  1 
ATOM   3531 N N   . ASN B 2 154 ? -40.094 -108.767 -8.349  1.00 116.80 ? 154 ASN B N   1 
ATOM   3532 C CA  . ASN B 2 154 ? -41.147 -107.837 -8.769  1.00 117.37 ? 154 ASN B CA  1 
ATOM   3533 C C   . ASN B 2 154 ? -42.093 -107.466 -7.619  1.00 117.36 ? 154 ASN B C   1 
ATOM   3534 O O   . ASN B 2 154 ? -42.893 -106.530 -7.730  1.00 115.68 ? 154 ASN B O   1 
ATOM   3535 C CB  . ASN B 2 154 ? -41.943 -108.392 -9.967  1.00 114.89 ? 154 ASN B CB  1 
ATOM   3536 C CG  . ASN B 2 154 ? -42.778 -107.320 -10.668 1.00 112.63 ? 154 ASN B CG  1 
ATOM   3537 O OD1 . ASN B 2 154 ? -43.871 -106.965 -10.220 1.00 111.06 ? 154 ASN B OD1 1 
ATOM   3538 N ND2 . ASN B 2 154 ? -42.264 -106.808 -11.780 1.00 109.87 ? 154 ASN B ND2 1 
ATOM   3539 N N   . GLY B 2 155 ? -41.987 -108.204 -6.516  1.00 116.01 ? 155 GLY B N   1 
ATOM   3540 C CA  . GLY B 2 155 ? -42.864 -108.021 -5.377  1.00 113.23 ? 155 GLY B CA  1 
ATOM   3541 C C   . GLY B 2 155 ? -44.052 -108.950 -5.496  1.00 113.92 ? 155 GLY B C   1 
ATOM   3542 O O   . GLY B 2 155 ? -44.948 -108.954 -4.652  1.00 111.32 ? 155 GLY B O   1 
ATOM   3543 N N   . THR B 2 156 ? -44.068 -109.733 -6.569  1.00 115.95 ? 156 THR B N   1 
ATOM   3544 C CA  . THR B 2 156 ? -45.154 -110.670 -6.805  1.00 118.06 ? 156 THR B CA  1 
ATOM   3545 C C   . THR B 2 156 ? -44.645 -112.107 -6.800  1.00 118.17 ? 156 THR B C   1 
ATOM   3546 O O   . THR B 2 156 ? -43.984 -112.551 -7.738  1.00 116.27 ? 156 THR B O   1 
ATOM   3547 C CB  . THR B 2 156 ? -45.856 -110.379 -8.143  1.00 116.37 ? 156 THR B CB  1 
ATOM   3548 O OG1 . THR B 2 156 ? -44.877 -110.299 -9.186  1.00 114.63 ? 156 THR B OG1 1 
ATOM   3549 C CG2 . THR B 2 156 ? -46.616 -109.060 -8.075  1.00 114.78 ? 156 THR B CG2 1 
ATOM   3550 N N   . TYR B 2 157 ? -44.988 -112.836 -5.746  1.00 117.97 ? 157 TYR B N   1 
ATOM   3551 C CA  . TYR B 2 157 ? -44.549 -114.213 -5.580  1.00 117.69 ? 157 TYR B CA  1 
ATOM   3552 C C   . TYR B 2 157 ? -45.709 -115.000 -5.004  1.00 120.74 ? 157 TYR B C   1 
ATOM   3553 O O   . TYR B 2 157 ? -46.429 -114.506 -4.131  1.00 119.04 ? 157 TYR B O   1 
ATOM   3554 C CB  . TYR B 2 157 ? -43.337 -114.291 -4.645  1.00 116.05 ? 157 TYR B CB  1 
ATOM   3555 C CG  . TYR B 2 157 ? -43.075 -115.677 -4.094  1.00 113.66 ? 157 TYR B CG  1 
ATOM   3556 C CD1 . TYR B 2 157 ? -42.299 -116.588 -4.796  1.00 113.46 ? 157 TYR B CD1 1 
ATOM   3557 C CD2 . TYR B 2 157 ? -43.608 -116.073 -2.872  1.00 112.83 ? 157 TYR B CD2 1 
ATOM   3558 C CE1 . TYR B 2 157 ? -42.061 -117.852 -4.300  1.00 113.52 ? 157 TYR B CE1 1 
ATOM   3559 C CE2 . TYR B 2 157 ? -43.376 -117.335 -2.369  1.00 112.56 ? 157 TYR B CE2 1 
ATOM   3560 C CZ  . TYR B 2 157 ? -42.602 -118.221 -3.089  1.00 112.99 ? 157 TYR B CZ  1 
ATOM   3561 O OH  . TYR B 2 157 ? -42.361 -119.482 -2.598  1.00 112.75 ? 157 TYR B OH  1 
ATOM   3562 N N   . ASP B 2 158 ? -45.891 -116.224 -5.489  1.00 121.69 ? 158 ASP B N   1 
ATOM   3563 C CA  . ASP B 2 158 ? -47.036 -117.025 -5.084  1.00 120.43 ? 158 ASP B CA  1 
ATOM   3564 C C   . ASP B 2 158 ? -46.640 -118.035 -4.014  1.00 118.75 ? 158 ASP B C   1 
ATOM   3565 O O   . ASP B 2 158 ? -45.948 -119.018 -4.285  1.00 118.42 ? 158 ASP B O   1 
ATOM   3566 C CB  . ASP B 2 158 ? -47.625 -117.754 -6.296  1.00 120.33 ? 158 ASP B CB  1 
ATOM   3567 C CG  . ASP B 2 158 ? -49.111 -117.486 -6.482  1.00 119.41 ? 158 ASP B CG  1 
ATOM   3568 O OD1 . ASP B 2 158 ? -49.916 -118.019 -5.689  1.00 118.81 ? 158 ASP B OD1 1 
ATOM   3569 O OD2 . ASP B 2 158 ? -49.475 -116.744 -7.424  1.00 117.92 ? 158 ASP B OD2 1 
ATOM   3570 N N   . TYR B 2 159 ? -47.090 -117.781 -2.792  1.00 118.43 ? 159 TYR B N   1 
ATOM   3571 C CA  . TYR B 2 159 ? -46.937 -118.738 -1.710  1.00 118.23 ? 159 TYR B CA  1 
ATOM   3572 C C   . TYR B 2 159 ? -47.784 -119.970 -2.022  1.00 119.01 ? 159 TYR B C   1 
ATOM   3573 O O   . TYR B 2 159 ? -47.325 -121.099 -1.847  1.00 117.97 ? 159 TYR B O   1 
ATOM   3574 C CB  . TYR B 2 159 ? -47.360 -118.105 -0.383  1.00 115.15 ? 159 TYR B CB  1 
ATOM   3575 C CG  . TYR B 2 159 ? -47.168 -118.978 0.834   1.00 113.90 ? 159 TYR B CG  1 
ATOM   3576 C CD1 . TYR B 2 159 ? -46.403 -120.134 0.780   1.00 113.23 ? 159 TYR B CD1 1 
ATOM   3577 C CD2 . TYR B 2 159 ? -47.764 -118.644 2.039   1.00 114.09 ? 159 TYR B CD2 1 
ATOM   3578 C CE1 . TYR B 2 159 ? -46.230 -120.930 1.896   1.00 112.57 ? 159 TYR B CE1 1 
ATOM   3579 C CE2 . TYR B 2 159 ? -47.598 -119.432 3.160   1.00 113.48 ? 159 TYR B CE2 1 
ATOM   3580 C CZ  . TYR B 2 159 ? -46.831 -120.574 3.084   1.00 111.03 ? 159 TYR B CZ  1 
ATOM   3581 O OH  . TYR B 2 159 ? -46.664 -121.361 4.199   1.00 109.79 ? 159 TYR B OH  1 
ATOM   3582 N N   . PRO B 2 160 ? -49.034 -119.757 -2.479  1.00 120.43 ? 160 PRO B N   1 
ATOM   3583 C CA  . PRO B 2 160 ? -49.878 -120.883 -2.895  1.00 119.78 ? 160 PRO B CA  1 
ATOM   3584 C C   . PRO B 2 160 ? -49.246 -121.721 -4.005  1.00 119.55 ? 160 PRO B C   1 
ATOM   3585 O O   . PRO B 2 160 ? -49.219 -122.949 -3.881  1.00 119.99 ? 160 PRO B O   1 
ATOM   3586 C CB  . PRO B 2 160 ? -51.137 -120.193 -3.426  1.00 119.96 ? 160 PRO B CB  1 
ATOM   3587 C CG  . PRO B 2 160 ? -51.192 -118.906 -2.689  1.00 119.80 ? 160 PRO B CG  1 
ATOM   3588 C CD  . PRO B 2 160 ? -49.767 -118.478 -2.530  1.00 120.55 ? 160 PRO B CD  1 
ATOM   3589 N N   . LYS B 2 161 ? -48.733 -121.071 -5.051  1.00 119.11 ? 161 LYS B N   1 
ATOM   3590 C CA  . LYS B 2 161 ? -48.151 -121.785 -6.185  1.00 119.37 ? 161 LYS B CA  1 
ATOM   3591 C C   . LYS B 2 161 ? -47.213 -122.861 -5.675  1.00 120.11 ? 161 LYS B C   1 
ATOM   3592 O O   . LYS B 2 161 ? -47.285 -124.017 -6.089  1.00 118.39 ? 161 LYS B O   1 
ATOM   3593 C CB  . LYS B 2 161 ? -47.347 -120.833 -7.074  1.00 118.61 ? 161 LYS B CB  1 
ATOM   3594 C CG  . LYS B 2 161 ? -48.028 -120.398 -8.352  1.00 118.63 ? 161 LYS B CG  1 
ATOM   3595 C CD  . LYS B 2 161 ? -47.073 -119.565 -9.192  1.00 120.24 ? 161 LYS B CD  1 
ATOM   3596 C CE  . LYS B 2 161 ? -47.730 -119.119 -10.478 1.00 120.72 ? 161 LYS B CE  1 
ATOM   3597 N NZ  . LYS B 2 161 ? -48.295 -120.278 -11.221 1.00 119.64 ? 161 LYS B NZ  1 
ATOM   3598 N N   . TYR B 2 162 ? -46.321 -122.458 -4.779  1.00 120.59 ? 162 TYR B N   1 
ATOM   3599 C CA  . TYR B 2 162 ? -45.254 -123.326 -4.300  1.00 120.05 ? 162 TYR B CA  1 
ATOM   3600 C C   . TYR B 2 162 ? -45.499 -124.000 -2.933  1.00 117.58 ? 162 TYR B C   1 
ATOM   3601 O O   . TYR B 2 162 ? -44.636 -124.728 -2.437  1.00 115.83 ? 162 TYR B O   1 
ATOM   3602 C CB  . TYR B 2 162 ? -43.926 -122.560 -4.337  1.00 118.49 ? 162 TYR B CB  1 
ATOM   3603 C CG  . TYR B 2 162 ? -43.637 -121.939 -5.695  1.00 118.26 ? 162 TYR B CG  1 
ATOM   3604 C CD1 . TYR B 2 162 ? -44.216 -120.731 -6.067  1.00 118.74 ? 162 TYR B CD1 1 
ATOM   3605 C CD2 . TYR B 2 162 ? -42.799 -122.569 -6.606  1.00 119.05 ? 162 TYR B CD2 1 
ATOM   3606 C CE1 . TYR B 2 162 ? -43.962 -120.166 -7.300  1.00 119.41 ? 162 TYR B CE1 1 
ATOM   3607 C CE2 . TYR B 2 162 ? -42.537 -122.012 -7.840  1.00 119.04 ? 162 TYR B CE2 1 
ATOM   3608 C CZ  . TYR B 2 162 ? -43.121 -120.811 -8.183  1.00 121.12 ? 162 TYR B CZ  1 
ATOM   3609 O OH  . TYR B 2 162 ? -42.862 -120.257 -9.415  1.00 124.56 ? 162 TYR B OH  1 
ATOM   3610 N N   . SER B 2 163 ? -46.672 -123.766 -2.342  1.00 117.75 ? 163 SER B N   1 
ATOM   3611 C CA  . SER B 2 163 ? -46.998 -124.245 -0.986  1.00 118.12 ? 163 SER B CA  1 
ATOM   3612 C C   . SER B 2 163 ? -46.705 -125.729 -0.701  1.00 116.56 ? 163 SER B C   1 
ATOM   3613 O O   . SER B 2 163 ? -45.914 -126.062 0.188   1.00 114.82 ? 163 SER B O   1 
ATOM   3614 C CB  . SER B 2 163 ? -48.453 -123.917 -0.626  1.00 115.26 ? 163 SER B CB  1 
ATOM   3615 O OG  . SER B 2 163 ? -48.586 -122.560 -0.241  1.00 114.48 ? 163 SER B OG  1 
ATOM   3616 N N   . GLU B 2 164 ? -47.384 -126.610 -1.425  1.00 116.36 ? 164 GLU B N   1 
ATOM   3617 C CA  . GLU B 2 164 ? -47.174 -128.049 -1.299  1.00 116.14 ? 164 GLU B CA  1 
ATOM   3618 C C   . GLU B 2 164 ? -45.736 -128.443 -1.646  1.00 115.32 ? 164 GLU B C   1 
ATOM   3619 O O   . GLU B 2 164 ? -45.081 -129.177 -0.901  1.00 112.93 ? 164 GLU B O   1 
ATOM   3620 C CB  . GLU B 2 164 ? -48.153 -128.799 -2.206  1.00 119.26 ? 164 GLU B CB  1 
ATOM   3621 C CG  . GLU B 2 164 ? -47.913 -128.584 -3.701  1.00 121.37 ? 164 GLU B CG  1 
ATOM   3622 C CD  . GLU B 2 164 ? -47.663 -127.122 -4.063  1.00 121.52 ? 164 GLU B CD  1 
ATOM   3623 O OE1 . GLU B 2 164 ? -48.287 -126.230 -3.439  1.00 121.20 ? 164 GLU B OE1 1 
ATOM   3624 O OE2 . GLU B 2 164 ? -46.831 -126.866 -4.965  1.00 120.69 ? 164 GLU B OE2 1 
ATOM   3625 N N   . GLU B 2 165 ? -45.249 -127.939 -2.777  1.00 116.28 ? 165 GLU B N   1 
ATOM   3626 C CA  . GLU B 2 165 ? -43.901 -128.224 -3.252  1.00 116.13 ? 165 GLU B CA  1 
ATOM   3627 C C   . GLU B 2 165 ? -42.922 -127.955 -2.115  1.00 114.18 ? 165 GLU B C   1 
ATOM   3628 O O   . GLU B 2 165 ? -41.846 -128.549 -2.046  1.00 113.29 ? 165 GLU B O   1 
ATOM   3629 C CB  . GLU B 2 165 ? -43.593 -127.333 -4.459  1.00 118.46 ? 165 GLU B CB  1 
ATOM   3630 C CG  . GLU B 2 165 ? -42.360 -127.704 -5.277  1.00 118.66 ? 165 GLU B CG  1 
ATOM   3631 C CD  . GLU B 2 165 ? -42.262 -126.895 -6.576  1.00 120.98 ? 165 GLU B CD  1 
ATOM   3632 O OE1 . GLU B 2 165 ? -43.312 -126.441 -7.087  1.00 121.02 ? 165 GLU B OE1 1 
ATOM   3633 O OE2 . GLU B 2 165 ? -41.135 -126.708 -7.087  1.00 118.75 ? 165 GLU B OE2 1 
ATOM   3634 N N   . ALA B 2 166 ? -43.314 -127.048 -1.226  1.00 114.05 ? 166 ALA B N   1 
ATOM   3635 C CA  . ALA B 2 166 ? -42.538 -126.726 -0.038  1.00 111.59 ? 166 ALA B CA  1 
ATOM   3636 C C   . ALA B 2 166 ? -42.862 -127.676 1.107   1.00 109.06 ? 166 ALA B C   1 
ATOM   3637 O O   . ALA B 2 166 ? -41.999 -128.427 1.562   1.00 108.20 ? 166 ALA B O   1 
ATOM   3638 C CB  . ALA B 2 166 ? -42.797 -125.285 0.385   1.00 110.82 ? 166 ALA B CB  1 
ATOM   3639 N N   . LYS B 2 167 ? -44.113 -127.641 1.560   1.00 108.27 ? 167 LYS B N   1 
ATOM   3640 C CA  . LYS B 2 167 ? -44.529 -128.387 2.744   1.00 106.21 ? 167 LYS B CA  1 
ATOM   3641 C C   . LYS B 2 167 ? -44.047 -129.840 2.746   1.00 104.40 ? 167 LYS B C   1 
ATOM   3642 O O   . LYS B 2 167 ? -43.592 -130.347 3.773   1.00 102.60 ? 167 LYS B O   1 
ATOM   3643 C CB  . LYS B 2 167 ? -46.051 -128.329 2.903   1.00 104.39 ? 167 LYS B CB  1 
ATOM   3644 C CG  . LYS B 2 167 ? -46.625 -129.415 3.809   1.00 104.94 ? 167 LYS B CG  1 
ATOM   3645 C CD  . LYS B 2 167 ? -48.036 -129.066 4.280   1.00 104.83 ? 167 LYS B CD  1 
ATOM   3646 C CE  . LYS B 2 167 ? -48.982 -130.265 4.206   1.00 101.07 ? 167 LYS B CE  1 
ATOM   3647 N NZ  . LYS B 2 167 ? -48.479 -131.459 4.944   1.00 99.31  ? 167 LYS B NZ  1 
ATOM   3648 N N   . LEU B 2 168 ? -44.144 -130.504 1.599   1.00 105.37 ? 168 LEU B N   1 
ATOM   3649 C CA  . LEU B 2 168 ? -43.647 -131.870 1.464   1.00 102.68 ? 168 LEU B CA  1 
ATOM   3650 C C   . LEU B 2 168 ? -42.172 -131.935 1.839   1.00 102.86 ? 168 LEU B C   1 
ATOM   3651 O O   . LEU B 2 168 ? -41.784 -132.589 2.812   1.00 100.89 ? 168 LEU B O   1 
ATOM   3652 C CB  . LEU B 2 168 ? -43.845 -132.371 0.032   1.00 99.04  ? 168 LEU B CB  1 
ATOM   3653 C CG  . LEU B 2 168 ? -43.417 -133.804 -0.292  1.00 93.07  ? 168 LEU B CG  1 
ATOM   3654 C CD1 . LEU B 2 168 ? -44.148 -134.810 0.572   1.00 90.24  ? 168 LEU B CD1 1 
ATOM   3655 C CD2 . LEU B 2 168 ? -43.676 -134.102 -1.754  1.00 85.85  ? 168 LEU B CD2 1 
ATOM   3656 N N   . ASN B 2 169 ? -41.355 -131.242 1.055   1.00 105.21 ? 169 ASN B N   1 
ATOM   3657 C CA  . ASN B 2 169 ? -39.915 -131.243 1.259   1.00 106.65 ? 169 ASN B CA  1 
ATOM   3658 C C   . ASN B 2 169 ? -39.485 -130.777 2.643   1.00 104.84 ? 169 ASN B C   1 
ATOM   3659 O O   . ASN B 2 169 ? -38.490 -131.255 3.186   1.00 105.61 ? 169 ASN B O   1 
ATOM   3660 C CB  . ASN B 2 169 ? -39.237 -130.399 0.183   1.00 109.18 ? 169 ASN B CB  1 
ATOM   3661 C CG  . ASN B 2 169 ? -39.169 -131.112 -1.146  1.00 109.98 ? 169 ASN B CG  1 
ATOM   3662 O OD1 . ASN B 2 169 ? -39.055 -132.341 -1.195  1.00 108.82 ? 169 ASN B OD1 1 
ATOM   3663 N ND2 . ASN B 2 169 ? -39.241 -130.349 -2.236  1.00 110.97 ? 169 ASN B ND2 1 
ATOM   3664 N N   . ARG B 2 170 ? -40.240 -129.846 3.213   1.00 104.86 ? 170 ARG B N   1 
ATOM   3665 C CA  . ARG B 2 170 ? -39.911 -129.309 4.524   1.00 104.83 ? 170 ARG B CA  1 
ATOM   3666 C C   . ARG B 2 170 ? -40.138 -130.335 5.628   1.00 106.53 ? 170 ARG B C   1 
ATOM   3667 O O   . ARG B 2 170 ? -39.362 -130.415 6.584   1.00 108.62 ? 170 ARG B O   1 
ATOM   3668 C CB  . ARG B 2 170 ? -40.744 -128.064 4.816   1.00 103.62 ? 170 ARG B CB  1 
ATOM   3669 C CG  . ARG B 2 170 ? -40.435 -127.424 6.154   1.00 102.95 ? 170 ARG B CG  1 
ATOM   3670 C CD  . ARG B 2 170 ? -41.548 -126.486 6.575   1.00 103.16 ? 170 ARG B CD  1 
ATOM   3671 N NE  . ARG B 2 170 ? -42.224 -125.883 5.429   1.00 103.86 ? 170 ARG B NE  1 
ATOM   3672 C CZ  . ARG B 2 170 ? -43.517 -126.035 5.157   1.00 102.43 ? 170 ARG B CZ  1 
ATOM   3673 N NH1 . ARG B 2 170 ? -44.281 -126.769 5.953   1.00 98.76  ? 170 ARG B NH1 1 
ATOM   3674 N NH2 . ARG B 2 170 ? -44.046 -125.449 4.090   1.00 104.79 ? 170 ARG B NH2 1 
ATOM   3675 N N   . GLU B 2 171 ? -41.207 -131.113 5.494   1.00 104.56 ? 171 GLU B N   1 
ATOM   3676 C CA  . GLU B 2 171 ? -41.617 -132.033 6.549   1.00 104.57 ? 171 GLU B CA  1 
ATOM   3677 C C   . GLU B 2 171 ? -40.798 -133.319 6.586   1.00 105.19 ? 171 GLU B C   1 
ATOM   3678 O O   . GLU B 2 171 ? -40.640 -133.933 7.646   1.00 107.07 ? 171 GLU B O   1 
ATOM   3679 C CB  . GLU B 2 171 ? -43.116 -132.319 6.456   1.00 102.16 ? 171 GLU B CB  1 
ATOM   3680 C CG  . GLU B 2 171 ? -43.960 -131.221 7.087   1.00 101.26 ? 171 GLU B CG  1 
ATOM   3681 C CD  . GLU B 2 171 ? -45.406 -131.266 6.653   1.00 98.88  ? 171 GLU B CD  1 
ATOM   3682 O OE1 . GLU B 2 171 ? -45.776 -132.203 5.911   1.00 98.59  ? 171 GLU B OE1 1 
ATOM   3683 O OE2 . GLU B 2 171 ? -46.167 -130.355 7.048   1.00 97.04  ? 171 GLU B OE2 1 
ATOM   3684 N N   . GLU B 2 172 ? -40.278 -133.723 5.432   1.00 101.62 ? 172 GLU B N   1 
ATOM   3685 C CA  . GLU B 2 172 ? -39.363 -134.848 5.385   1.00 101.21 ? 172 GLU B CA  1 
ATOM   3686 C C   . GLU B 2 172 ? -38.175 -134.561 6.294   1.00 106.33 ? 172 GLU B C   1 
ATOM   3687 O O   . GLU B 2 172 ? -37.608 -135.463 6.917   1.00 106.49 ? 172 GLU B O   1 
ATOM   3688 C CB  . GLU B 2 172 ? -38.890 -135.091 3.958   1.00 98.33  ? 172 GLU B CB  1 
ATOM   3689 C CG  . GLU B 2 172 ? -39.280 -136.449 3.432   1.00 97.24  ? 172 GLU B CG  1 
ATOM   3690 C CD  . GLU B 2 172 ? -38.818 -137.572 4.337   1.00 97.59  ? 172 GLU B CD  1 
ATOM   3691 O OE1 . GLU B 2 172 ? -37.873 -137.359 5.127   1.00 98.63  ? 172 GLU B OE1 1 
ATOM   3692 O OE2 . GLU B 2 172 ? -39.401 -138.673 4.259   1.00 95.76  ? 172 GLU B OE2 1 
ATOM   3693 N N   . ILE B 2 173 ? -37.814 -133.285 6.367   1.00 106.98 ? 173 ILE B N   1 
ATOM   3694 C CA  . ILE B 2 173 ? -36.728 -132.825 7.221   1.00 108.65 ? 173 ILE B CA  1 
ATOM   3695 C C   . ILE B 2 173 ? -37.034 -133.076 8.695   1.00 110.61 ? 173 ILE B C   1 
ATOM   3696 O O   . ILE B 2 173 ? -36.194 -133.579 9.444   1.00 112.99 ? 173 ILE B O   1 
ATOM   3697 C CB  . ILE B 2 173 ? -36.451 -131.321 6.988   1.00 108.05 ? 173 ILE B CB  1 
ATOM   3698 C CG1 . ILE B 2 173 ? -35.484 -131.139 5.816   1.00 107.89 ? 173 ILE B CG1 1 
ATOM   3699 C CG2 . ILE B 2 173 ? -35.894 -130.663 8.242   1.00 110.03 ? 173 ILE B CG2 1 
ATOM   3700 C CD1 . ILE B 2 173 ? -35.896 -131.878 4.551   1.00 104.10 ? 173 ILE B CD1 1 
ATOM   3701 N N   . ASP B 2 174 ? -38.250 -132.736 9.103   1.00 109.71 ? 174 ASP B N   1 
ATOM   3702 C CA  . ASP B 2 174 ? -38.641 -132.820 10.503  1.00 111.64 ? 174 ASP B CA  1 
ATOM   3703 C C   . ASP B 2 174 ? -39.118 -134.223 10.878  1.00 110.40 ? 174 ASP B C   1 
ATOM   3704 O O   . ASP B 2 174 ? -39.867 -134.857 10.131  1.00 108.26 ? 174 ASP B O   1 
ATOM   3705 C CB  . ASP B 2 174 ? -39.733 -131.788 10.798  1.00 114.97 ? 174 ASP B CB  1 
ATOM   3706 C CG  . ASP B 2 174 ? -39.482 -130.453 10.097  1.00 114.74 ? 174 ASP B CG  1 
ATOM   3707 O OD1 . ASP B 2 174 ? -38.299 -130.098 9.883   1.00 116.91 ? 174 ASP B OD1 1 
ATOM   3708 O OD2 . ASP B 2 174 ? -40.469 -129.765 9.751   1.00 112.88 ? 174 ASP B OD2 1 
ATOM   3709 N N   . ASN C 1 20  ? 62.908  -83.720  33.529  1.00 130.70 ? 11  ASN C N   1 
ATOM   3710 C CA  . ASN C 1 20  ? 61.647  -84.051  34.188  1.00 133.74 ? 11  ASN C CA  1 
ATOM   3711 C C   . ASN C 1 20  ? 60.576  -83.009  33.877  1.00 130.98 ? 11  ASN C C   1 
ATOM   3712 O O   . ASN C 1 20  ? 59.384  -83.235  34.091  1.00 129.71 ? 11  ASN C O   1 
ATOM   3713 C CB  . ASN C 1 20  ? 61.853  -84.165  35.705  1.00 137.33 ? 11  ASN C CB  1 
ATOM   3714 C CG  . ASN C 1 20  ? 60.805  -85.041  36.381  1.00 136.71 ? 11  ASN C CG  1 
ATOM   3715 O OD1 . ASN C 1 20  ? 60.018  -85.717  35.717  1.00 135.90 ? 11  ASN C OD1 1 
ATOM   3716 N ND2 . ASN C 1 20  ? 60.801  -85.038  37.711  1.00 134.44 ? 11  ASN C ND2 1 
ATOM   3717 N N   . SER C 1 21  ? 61.019  -81.870  33.359  1.00 129.73 ? 12  SER C N   1 
ATOM   3718 C CA  . SER C 1 21  ? 60.145  -80.729  33.137  1.00 125.47 ? 12  SER C CA  1 
ATOM   3719 C C   . SER C 1 21  ? 59.153  -80.927  32.004  1.00 124.47 ? 12  SER C C   1 
ATOM   3720 O O   . SER C 1 21  ? 59.520  -81.335  30.902  1.00 122.90 ? 12  SER C O   1 
ATOM   3721 C CB  . SER C 1 21  ? 60.975  -79.485  32.850  1.00 124.40 ? 12  SER C CB  1 
ATOM   3722 O OG  . SER C 1 21  ? 60.324  -78.674  31.892  1.00 123.65 ? 12  SER C OG  1 
ATOM   3723 N N   . THR C 1 22  ? 57.894  -80.615  32.288  1.00 124.21 ? 13  THR C N   1 
ATOM   3724 C CA  . THR C 1 22  ? 56.843  -80.622  31.282  1.00 126.10 ? 13  THR C CA  1 
ATOM   3725 C C   . THR C 1 22  ? 57.135  -79.600  30.198  1.00 124.90 ? 13  THR C C   1 
ATOM   3726 O O   . THR C 1 22  ? 56.876  -79.830  29.015  1.00 123.62 ? 13  THR C O   1 
ATOM   3727 C CB  . THR C 1 22  ? 55.479  -80.247  31.909  1.00 127.75 ? 13  THR C CB  1 
ATOM   3728 O OG1 . THR C 1 22  ? 54.664  -81.419  32.029  1.00 129.38 ? 13  THR C OG1 1 
ATOM   3729 C CG2 . THR C 1 22  ? 54.751  -79.215  31.049  1.00 124.75 ? 13  THR C CG2 1 
ATOM   3730 N N   . ASP C 1 23  ? 57.695  -78.473  30.618  1.00 125.08 ? 14  ASP C N   1 
ATOM   3731 C CA  . ASP C 1 23  ? 57.715  -77.278  29.792  1.00 124.57 ? 14  ASP C CA  1 
ATOM   3732 C C   . ASP C 1 23  ? 58.345  -77.505  28.433  1.00 124.52 ? 14  ASP C C   1 
ATOM   3733 O O   . ASP C 1 23  ? 59.488  -77.951  28.311  1.00 124.20 ? 14  ASP C O   1 
ATOM   3734 C CB  . ASP C 1 23  ? 58.420  -76.148  30.531  1.00 123.60 ? 14  ASP C CB  1 
ATOM   3735 C CG  . ASP C 1 23  ? 58.139  -76.182  32.011  1.00 125.15 ? 14  ASP C CG  1 
ATOM   3736 O OD1 . ASP C 1 23  ? 58.272  -77.275  32.602  1.00 125.74 ? 14  ASP C OD1 1 
ATOM   3737 O OD2 . ASP C 1 23  ? 57.773  -75.132  32.579  1.00 124.21 ? 14  ASP C OD2 1 
ATOM   3738 N N   . THR C 1 24  ? 57.568  -77.181  27.411  1.00 124.23 ? 15  THR C N   1 
ATOM   3739 C CA  . THR C 1 24  ? 58.011  -77.264  26.039  1.00 123.71 ? 15  THR C CA  1 
ATOM   3740 C C   . THR C 1 24  ? 57.587  -75.974  25.360  1.00 124.82 ? 15  THR C C   1 
ATOM   3741 O O   . THR C 1 24  ? 56.401  -75.654  25.313  1.00 126.49 ? 15  THR C O   1 
ATOM   3742 C CB  . THR C 1 24  ? 57.392  -78.471  25.323  1.00 122.42 ? 15  THR C CB  1 
ATOM   3743 O OG1 . THR C 1 24  ? 56.972  -78.084  24.008  1.00 121.99 ? 15  THR C OG1 1 
ATOM   3744 C CG2 . THR C 1 24  ? 56.193  -79.001  26.106  1.00 121.93 ? 15  THR C CG2 1 
ATOM   3745 N N   . VAL C 1 25  ? 58.560  -75.230  24.845  1.00 123.99 ? 16  VAL C N   1 
ATOM   3746 C CA  . VAL C 1 25  ? 58.294  -73.893  24.328  1.00 123.24 ? 16  VAL C CA  1 
ATOM   3747 C C   . VAL C 1 25  ? 58.736  -73.726  22.875  1.00 122.50 ? 16  VAL C C   1 
ATOM   3748 O O   . VAL C 1 25  ? 59.125  -74.694  22.220  1.00 122.80 ? 16  VAL C O   1 
ATOM   3749 C CB  . VAL C 1 25  ? 58.936  -72.809  25.215  1.00 122.53 ? 16  VAL C CB  1 
ATOM   3750 C CG1 . VAL C 1 25  ? 58.561  -73.044  26.666  1.00 122.58 ? 16  VAL C CG1 1 
ATOM   3751 C CG2 . VAL C 1 25  ? 60.447  -72.804  25.048  1.00 122.80 ? 16  VAL C CG2 1 
ATOM   3752 N N   . ASP C 1 26  ? 58.649  -72.497  22.375  1.00 120.90 ? 17  ASP C N   1 
ATOM   3753 C CA  . ASP C 1 26  ? 58.902  -72.214  20.964  1.00 120.81 ? 17  ASP C CA  1 
ATOM   3754 C C   . ASP C 1 26  ? 60.077  -71.271  20.725  1.00 121.26 ? 17  ASP C C   1 
ATOM   3755 O O   . ASP C 1 26  ? 60.229  -70.253  21.405  1.00 120.70 ? 17  ASP C O   1 
ATOM   3756 C CB  . ASP C 1 26  ? 57.651  -71.631  20.301  1.00 122.32 ? 17  ASP C CB  1 
ATOM   3757 C CG  . ASP C 1 26  ? 56.833  -72.676  19.568  1.00 124.63 ? 17  ASP C CG  1 
ATOM   3758 O OD1 . ASP C 1 26  ? 56.093  -73.432  20.233  1.00 125.94 ? 17  ASP C OD1 1 
ATOM   3759 O OD2 . ASP C 1 26  ? 56.920  -72.734  18.323  1.00 124.28 ? 17  ASP C OD2 1 
ATOM   3760 N N   . THR C 1 27  ? 60.897  -71.621  19.739  1.00 122.35 ? 18  THR C N   1 
ATOM   3761 C CA  . THR C 1 27  ? 61.989  -70.769  19.290  1.00 120.34 ? 18  THR C CA  1 
ATOM   3762 C C   . THR C 1 27  ? 61.821  -70.427  17.817  1.00 119.26 ? 18  THR C C   1 
ATOM   3763 O O   . THR C 1 27  ? 60.892  -70.895  17.157  1.00 119.39 ? 18  THR C O   1 
ATOM   3764 C CB  . THR C 1 27  ? 63.345  -71.462  19.455  1.00 119.97 ? 18  THR C CB  1 
ATOM   3765 O OG1 . THR C 1 27  ? 63.272  -72.782  18.898  1.00 120.42 ? 18  THR C OG1 1 
ATOM   3766 C CG2 . THR C 1 27  ? 63.731  -71.541  20.929  1.00 121.04 ? 18  THR C CG2 1 
ATOM   3767 N N   . VAL C 1 28  ? 62.744  -69.625  17.302  1.00 118.04 ? 19  VAL C N   1 
ATOM   3768 C CA  . VAL C 1 28  ? 62.711  -69.220  15.909  1.00 118.50 ? 19  VAL C CA  1 
ATOM   3769 C C   . VAL C 1 28  ? 62.694  -70.434  14.971  1.00 121.14 ? 19  VAL C C   1 
ATOM   3770 O O   . VAL C 1 28  ? 62.133  -70.373  13.876  1.00 120.49 ? 19  VAL C O   1 
ATOM   3771 C CB  . VAL C 1 28  ? 63.895  -68.293  15.579  1.00 116.37 ? 19  VAL C CB  1 
ATOM   3772 C CG1 . VAL C 1 28  ? 63.797  -67.792  14.146  1.00 117.77 ? 19  VAL C CG1 1 
ATOM   3773 C CG2 . VAL C 1 28  ? 63.925  -67.127  16.550  1.00 114.52 ? 19  VAL C CG2 1 
ATOM   3774 N N   . LEU C 1 29  ? 63.292  -71.538  15.410  1.00 120.20 ? 20  LEU C N   1 
ATOM   3775 C CA  . LEU C 1 29  ? 63.326  -72.753  14.599  1.00 121.70 ? 20  LEU C CA  1 
ATOM   3776 C C   . LEU C 1 29  ? 62.183  -73.726  14.888  1.00 123.27 ? 20  LEU C C   1 
ATOM   3777 O O   . LEU C 1 29  ? 61.327  -73.963  14.034  1.00 123.86 ? 20  LEU C O   1 
ATOM   3778 C CB  . LEU C 1 29  ? 64.666  -73.481  14.756  1.00 123.96 ? 20  LEU C CB  1 
ATOM   3779 C CG  . LEU C 1 29  ? 64.697  -74.960  14.333  1.00 127.17 ? 20  LEU C CG  1 
ATOM   3780 C CD1 . LEU C 1 29  ? 64.163  -75.182  12.908  1.00 122.58 ? 20  LEU C CD1 1 
ATOM   3781 C CD2 . LEU C 1 29  ? 66.103  -75.550  14.493  1.00 125.71 ? 20  LEU C CD2 1 
ATOM   3782 N N   . GLU C 1 30  ? 62.181  -74.293  16.090  1.00 122.74 ? 21  GLU C N   1 
ATOM   3783 C CA  . GLU C 1 30  ? 61.339  -75.448  16.383  1.00 122.59 ? 21  GLU C CA  1 
ATOM   3784 C C   . GLU C 1 30  ? 60.184  -75.136  17.333  1.00 121.61 ? 21  GLU C C   1 
ATOM   3785 O O   . GLU C 1 30  ? 60.330  -74.350  18.267  1.00 120.43 ? 21  GLU C O   1 
ATOM   3786 C CB  . GLU C 1 30  ? 62.200  -76.579  16.946  1.00 124.66 ? 21  GLU C CB  1 
ATOM   3787 C CG  . GLU C 1 30  ? 61.685  -77.972  16.647  1.00 127.46 ? 21  GLU C CG  1 
ATOM   3788 C CD  . GLU C 1 30  ? 62.711  -79.043  16.971  1.00 134.27 ? 21  GLU C CD  1 
ATOM   3789 O OE1 . GLU C 1 30  ? 63.909  -78.703  17.091  1.00 135.00 ? 21  GLU C OE1 1 
ATOM   3790 O OE2 . GLU C 1 30  ? 62.320  -80.222  17.111  1.00 135.92 ? 21  GLU C OE2 1 
ATOM   3791 N N   . LYS C 1 31  ? 59.043  -75.776  17.091  1.00 121.52 ? 22  LYS C N   1 
ATOM   3792 C CA  . LYS C 1 31  ? 57.832  -75.524  17.866  1.00 122.69 ? 22  LYS C CA  1 
ATOM   3793 C C   . LYS C 1 31  ? 57.819  -76.195  19.242  1.00 122.04 ? 22  LYS C C   1 
ATOM   3794 O O   . LYS C 1 31  ? 57.518  -75.561  20.250  1.00 122.90 ? 22  LYS C O   1 
ATOM   3795 C CB  . LYS C 1 31  ? 56.585  -75.936  17.064  1.00 122.30 ? 22  LYS C CB  1 
ATOM   3796 C CG  . LYS C 1 31  ? 56.339  -77.446  16.975  1.00 121.09 ? 22  LYS C CG  1 
ATOM   3797 C CD  . LYS C 1 31  ? 54.949  -77.810  17.504  1.00 117.56 ? 22  LYS C CD  1 
ATOM   3798 C CE  . LYS C 1 31  ? 54.696  -79.308  17.466  1.00 112.93 ? 22  LYS C CE  1 
ATOM   3799 N NZ  . LYS C 1 31  ? 53.444  -79.668  18.190  1.00 107.72 ? 22  LYS C NZ  1 
ATOM   3800 N N   . ASN C 1 32  ? 58.170  -77.473  19.281  1.00 122.26 ? 23  ASN C N   1 
ATOM   3801 C CA  . ASN C 1 32  ? 57.911  -78.298  20.459  1.00 122.27 ? 23  ASN C CA  1 
ATOM   3802 C C   . ASN C 1 32  ? 59.003  -78.337  21.521  1.00 123.22 ? 23  ASN C C   1 
ATOM   3803 O O   . ASN C 1 32  ? 58.929  -79.148  22.447  1.00 124.46 ? 23  ASN C O   1 
ATOM   3804 C CB  . ASN C 1 32  ? 57.498  -79.718  20.067  1.00 122.46 ? 23  ASN C CB  1 
ATOM   3805 C CG  . ASN C 1 32  ? 56.159  -80.112  20.659  1.00 120.27 ? 23  ASN C CG  1 
ATOM   3806 O OD1 . ASN C 1 32  ? 55.176  -79.373  20.554  1.00 116.55 ? 23  ASN C OD1 1 
ATOM   3807 N ND2 . ASN C 1 32  ? 56.116  -81.273  21.303  1.00 119.94 ? 23  ASN C ND2 1 
ATOM   3808 N N   . VAL C 1 33  ? 60.009  -77.476  21.395  1.00 122.46 ? 24  VAL C N   1 
ATOM   3809 C CA  . VAL C 1 33  ? 61.205  -77.602  22.219  1.00 123.42 ? 24  VAL C CA  1 
ATOM   3810 C C   . VAL C 1 33  ? 60.835  -77.736  23.692  1.00 123.59 ? 24  VAL C C   1 
ATOM   3811 O O   . VAL C 1 33  ? 60.192  -76.858  24.267  1.00 123.77 ? 24  VAL C O   1 
ATOM   3812 C CB  . VAL C 1 33  ? 62.099  -76.356  22.081  1.00 122.58 ? 24  VAL C CB  1 
ATOM   3813 C CG1 . VAL C 1 33  ? 63.336  -76.488  22.956  1.00 123.64 ? 24  VAL C CG1 1 
ATOM   3814 C CG2 . VAL C 1 33  ? 62.473  -76.120  20.624  1.00 123.35 ? 24  VAL C CG2 1 
ATOM   3815 N N   . THR C 1 34  ? 61.283  -78.829  24.304  1.00 122.48 ? 25  THR C N   1 
ATOM   3816 C CA  . THR C 1 34  ? 60.906  -79.148  25.672  1.00 120.93 ? 25  THR C CA  1 
ATOM   3817 C C   . THR C 1 34  ? 62.029  -78.711  26.588  1.00 121.66 ? 25  THR C C   1 
ATOM   3818 O O   . THR C 1 34  ? 63.128  -79.264  26.554  1.00 123.05 ? 25  THR C O   1 
ATOM   3819 C CB  . THR C 1 34  ? 60.612  -80.650  25.860  1.00 119.28 ? 25  THR C CB  1 
ATOM   3820 O OG1 . THR C 1 34  ? 59.641  -81.077  24.896  1.00 118.63 ? 25  THR C OG1 1 
ATOM   3821 C CG2 . THR C 1 34  ? 60.073  -80.908  27.256  1.00 119.25 ? 25  THR C CG2 1 
ATOM   3822 N N   . VAL C 1 35  ? 61.742  -77.706  27.403  1.00 121.93 ? 26  VAL C N   1 
ATOM   3823 C CA  . VAL C 1 35  ? 62.771  -77.046  28.188  1.00 122.79 ? 26  VAL C CA  1 
ATOM   3824 C C   . VAL C 1 35  ? 62.559  -77.222  29.682  1.00 124.21 ? 26  VAL C C   1 
ATOM   3825 O O   . VAL C 1 35  ? 61.433  -77.159  30.173  1.00 125.16 ? 26  VAL C O   1 
ATOM   3826 C CB  . VAL C 1 35  ? 62.803  -75.561  27.868  1.00 122.65 ? 26  VAL C CB  1 
ATOM   3827 C CG1 . VAL C 1 35  ? 61.397  -75.072  27.587  1.00 122.97 ? 26  VAL C CG1 1 
ATOM   3828 C CG2 . VAL C 1 35  ? 63.440  -74.789  29.008  1.00 123.69 ? 26  VAL C CG2 1 
ATOM   3829 N N   . THR C 1 36  ? 63.658  -77.425  30.401  1.00 124.45 ? 27  THR C N   1 
ATOM   3830 C CA  . THR C 1 36  ? 63.609  -77.770  31.818  1.00 126.52 ? 27  THR C CA  1 
ATOM   3831 C C   . THR C 1 36  ? 63.189  -76.627  32.745  1.00 125.69 ? 27  THR C C   1 
ATOM   3832 O O   . THR C 1 36  ? 62.825  -76.862  33.897  1.00 124.76 ? 27  THR C O   1 
ATOM   3833 C CB  . THR C 1 36  ? 64.954  -78.346  32.298  1.00 127.42 ? 27  THR C CB  1 
ATOM   3834 O OG1 . THR C 1 36  ? 65.982  -77.358  32.154  1.00 126.51 ? 27  THR C OG1 1 
ATOM   3835 C CG2 . THR C 1 36  ? 65.319  -79.569  31.484  1.00 125.93 ? 27  THR C CG2 1 
ATOM   3836 N N   . HIS C 1 37  ? 63.239  -75.398  32.245  1.00 124.63 ? 28  HIS C N   1 
ATOM   3837 C CA  . HIS C 1 37  ? 62.830  -74.240  33.032  1.00 126.81 ? 28  HIS C CA  1 
ATOM   3838 C C   . HIS C 1 37  ? 61.875  -73.386  32.213  1.00 126.83 ? 28  HIS C C   1 
ATOM   3839 O O   . HIS C 1 37  ? 61.756  -73.593  31.009  1.00 126.20 ? 28  HIS C O   1 
ATOM   3840 C CB  . HIS C 1 37  ? 64.047  -73.411  33.437  1.00 128.61 ? 28  HIS C CB  1 
ATOM   3841 C CG  . HIS C 1 37  ? 64.630  -73.799  34.759  1.00 128.27 ? 28  HIS C CG  1 
ATOM   3842 N ND1 . HIS C 1 37  ? 64.341  -74.994  35.378  1.00 127.79 ? 28  HIS C ND1 1 
ATOM   3843 C CD2 . HIS C 1 37  ? 65.483  -73.141  35.582  1.00 125.84 ? 28  HIS C CD2 1 
ATOM   3844 C CE1 . HIS C 1 37  ? 64.995  -75.061  36.526  1.00 128.91 ? 28  HIS C CE1 1 
ATOM   3845 N NE2 . HIS C 1 37  ? 65.695  -73.951  36.671  1.00 128.63 ? 28  HIS C NE2 1 
ATOM   3846 N N   . SER C 1 38  ? 61.196  -72.433  32.855  1.00 128.11 ? 29  SER C N   1 
ATOM   3847 C CA  . SER C 1 38  ? 60.246  -71.569  32.146  1.00 126.87 ? 29  SER C CA  1 
ATOM   3848 C C   . SER C 1 38  ? 59.542  -70.518  33.014  1.00 124.92 ? 29  SER C C   1 
ATOM   3849 O O   . SER C 1 38  ? 59.504  -70.626  34.241  1.00 123.91 ? 29  SER C O   1 
ATOM   3850 C CB  . SER C 1 38  ? 59.185  -72.427  31.453  1.00 126.00 ? 29  SER C CB  1 
ATOM   3851 O OG  . SER C 1 38  ? 58.574  -73.309  32.380  1.00 126.35 ? 29  SER C OG  1 
ATOM   3852 N N   . VAL C 1 39  ? 58.981  -69.504  32.356  1.00 124.39 ? 30  VAL C N   1 
ATOM   3853 C CA  . VAL C 1 39  ? 58.101  -68.533  33.009  1.00 124.61 ? 30  VAL C CA  1 
ATOM   3854 C C   . VAL C 1 39  ? 56.898  -68.188  32.129  1.00 124.26 ? 30  VAL C C   1 
ATOM   3855 O O   . VAL C 1 39  ? 57.065  -67.709  31.008  1.00 123.85 ? 30  VAL C O   1 
ATOM   3856 C CB  . VAL C 1 39  ? 58.837  -67.228  33.360  1.00 122.25 ? 30  VAL C CB  1 
ATOM   3857 C CG1 . VAL C 1 39  ? 59.705  -66.776  32.203  1.00 121.40 ? 30  VAL C CG1 1 
ATOM   3858 C CG2 . VAL C 1 39  ? 57.834  -66.142  33.738  1.00 121.41 ? 30  VAL C CG2 1 
ATOM   3859 N N   . ASN C 1 40  ? 55.688  -68.404  32.640  1.00 124.20 ? 31  ASN C N   1 
ATOM   3860 C CA  . ASN C 1 40  ? 54.494  -68.202  31.823  1.00 120.59 ? 31  ASN C CA  1 
ATOM   3861 C C   . ASN C 1 40  ? 54.066  -66.745  31.752  1.00 116.37 ? 31  ASN C C   1 
ATOM   3862 O O   . ASN C 1 40  ? 54.652  -65.878  32.399  1.00 115.63 ? 31  ASN C O   1 
ATOM   3863 C CB  . ASN C 1 40  ? 53.329  -69.052  32.335  1.00 120.93 ? 31  ASN C CB  1 
ATOM   3864 C CG  . ASN C 1 40  ? 52.160  -69.081  31.368  1.00 118.76 ? 31  ASN C CG  1 
ATOM   3865 O OD1 . ASN C 1 40  ? 51.412  -68.108  31.247  1.00 116.16 ? 31  ASN C OD1 1 
ATOM   3866 N ND2 . ASN C 1 40  ? 51.996  -70.200  30.672  1.00 120.11 ? 31  ASN C ND2 1 
ATOM   3867 N N   . LEU C 1 41  ? 53.048  -66.485  30.940  1.00 114.50 ? 32  LEU C N   1 
ATOM   3868 C CA  . LEU C 1 41  ? 52.553  -65.132  30.740  1.00 113.46 ? 32  LEU C CA  1 
ATOM   3869 C C   . LEU C 1 41  ? 51.030  -65.025  30.775  1.00 111.48 ? 32  LEU C C   1 
ATOM   3870 O O   . LEU C 1 41  ? 50.459  -64.412  31.677  1.00 110.94 ? 32  LEU C O   1 
ATOM   3871 C CB  . LEU C 1 41  ? 53.110  -64.588  29.434  1.00 114.58 ? 32  LEU C CB  1 
ATOM   3872 C CG  . LEU C 1 41  ? 54.620  -64.824  29.405  1.00 115.66 ? 32  LEU C CG  1 
ATOM   3873 C CD1 . LEU C 1 41  ? 55.093  -65.277  28.032  1.00 116.25 ? 32  LEU C CD1 1 
ATOM   3874 C CD2 . LEU C 1 41  ? 55.372  -63.589  29.893  1.00 112.28 ? 32  LEU C CD2 1 
ATOM   3875 N N   . LEU C 1 42  ? 50.377  -65.620  29.781  1.00 111.28 ? 33  LEU C N   1 
ATOM   3876 C CA  . LEU C 1 42  ? 48.927  -65.520  29.658  1.00 108.72 ? 33  LEU C CA  1 
ATOM   3877 C C   . LEU C 1 42  ? 48.222  -66.530  30.548  1.00 107.95 ? 33  LEU C C   1 
ATOM   3878 O O   . LEU C 1 42  ? 48.580  -67.712  30.580  1.00 106.89 ? 33  LEU C O   1 
ATOM   3879 C CB  . LEU C 1 42  ? 48.484  -65.680  28.200  1.00 107.45 ? 33  LEU C CB  1 
ATOM   3880 C CG  . LEU C 1 42  ? 48.306  -67.076  27.597  1.00 108.30 ? 33  LEU C CG  1 
ATOM   3881 C CD1 . LEU C 1 42  ? 47.964  -66.936  26.124  1.00 107.06 ? 33  LEU C CD1 1 
ATOM   3882 C CD2 . LEU C 1 42  ? 49.542  -67.947  27.784  1.00 110.39 ? 33  LEU C CD2 1 
ATOM   3883 N N   . GLU C 1 43  ? 47.221  -66.052  31.279  1.00 106.04 ? 34  GLU C N   1 
ATOM   3884 C CA  . GLU C 1 43  ? 46.486  -66.914  32.182  1.00 103.21 ? 34  GLU C CA  1 
ATOM   3885 C C   . GLU C 1 43  ? 45.446  -67.651  31.367  1.00 100.11 ? 34  GLU C C   1 
ATOM   3886 O O   . GLU C 1 43  ? 44.567  -67.047  30.759  1.00 99.90  ? 34  GLU C O   1 
ATOM   3887 C CB  . GLU C 1 43  ? 45.817  -66.101  33.286  1.00 102.19 ? 34  GLU C CB  1 
ATOM   3888 C CG  . GLU C 1 43  ? 45.975  -66.707  34.664  1.00 104.68 ? 34  GLU C CG  1 
ATOM   3889 C CD  . GLU C 1 43  ? 45.843  -68.218  34.655  1.00 103.75 ? 34  GLU C CD  1 
ATOM   3890 O OE1 . GLU C 1 43  ? 45.004  -68.744  33.890  1.00 101.25 ? 34  GLU C OE1 1 
ATOM   3891 O OE2 . GLU C 1 43  ? 46.582  -68.878  35.420  1.00 103.27 ? 34  GLU C OE2 1 
ATOM   3892 N N   . ASP C 1 44  ? 45.563  -68.966  31.341  1.00 98.94  ? 35  ASP C N   1 
ATOM   3893 C CA  . ASP C 1 44  ? 44.701  -69.756  30.493  1.00 99.80  ? 35  ASP C CA  1 
ATOM   3894 C C   . ASP C 1 44  ? 43.346  -70.028  31.118  1.00 99.20  ? 35  ASP C C   1 
ATOM   3895 O O   . ASP C 1 44  ? 42.350  -70.186  30.417  1.00 99.36  ? 35  ASP C O   1 
ATOM   3896 C CB  . ASP C 1 44  ? 45.374  -71.074  30.139  1.00 100.80 ? 35  ASP C CB  1 
ATOM   3897 C CG  . ASP C 1 44  ? 44.633  -71.815  29.058  1.00 102.16 ? 35  ASP C CG  1 
ATOM   3898 O OD1 . ASP C 1 44  ? 44.021  -71.139  28.204  1.00 98.78  ? 35  ASP C OD1 1 
ATOM   3899 O OD2 . ASP C 1 44  ? 44.649  -73.063  29.061  1.00 103.16 ? 35  ASP C OD2 1 
ATOM   3900 N N   . LYS C 1 45  ? 43.312  -70.081  32.441  1.00 101.17 ? 36  LYS C N   1 
ATOM   3901 C CA  . LYS C 1 45  ? 42.181  -70.684  33.133  1.00 100.34 ? 36  LYS C CA  1 
ATOM   3902 C C   . LYS C 1 45  ? 41.466  -69.767  34.126  1.00 97.04  ? 36  LYS C C   1 
ATOM   3903 O O   . LYS C 1 45  ? 42.013  -68.757  34.573  1.00 96.39  ? 36  LYS C O   1 
ATOM   3904 C CB  . LYS C 1 45  ? 42.629  -71.976  33.828  1.00 102.00 ? 36  LYS C CB  1 
ATOM   3905 C CG  . LYS C 1 45  ? 43.866  -71.829  34.721  1.00 102.03 ? 36  LYS C CG  1 
ATOM   3906 C CD  . LYS C 1 45  ? 45.170  -71.835  33.917  1.00 102.61 ? 36  LYS C CD  1 
ATOM   3907 C CE  . LYS C 1 45  ? 46.396  -71.837  34.834  1.00 101.74 ? 36  LYS C CE  1 
ATOM   3908 N NZ  . LYS C 1 45  ? 47.676  -71.810  34.067  1.00 101.58 ? 36  LYS C NZ  1 
ATOM   3909 N N   . HIS C 1 46  ? 40.236  -70.148  34.465  1.00 96.50  ? 37  HIS C N   1 
ATOM   3910 C CA  . HIS C 1 46  ? 39.388  -69.379  35.371  1.00 97.65  ? 37  HIS C CA  1 
ATOM   3911 C C   . HIS C 1 46  ? 38.445  -70.303  36.127  1.00 95.97  ? 37  HIS C C   1 
ATOM   3912 O O   . HIS C 1 46  ? 38.210  -71.447  35.716  1.00 95.42  ? 37  HIS C O   1 
ATOM   3913 C CB  . HIS C 1 46  ? 38.544  -68.386  34.582  1.00 93.83  ? 37  HIS C CB  1 
ATOM   3914 C CG  . HIS C 1 46  ? 37.655  -69.037  33.575  1.00 90.60  ? 37  HIS C CG  1 
ATOM   3915 N ND1 . HIS C 1 46  ? 36.594  -69.839  33.930  1.00 89.60  ? 37  HIS C ND1 1 
ATOM   3916 C CD2 . HIS C 1 46  ? 37.689  -69.032  32.222  1.00 91.50  ? 37  HIS C CD2 1 
ATOM   3917 C CE1 . HIS C 1 46  ? 36.000  -70.288  32.839  1.00 92.23  ? 37  HIS C CE1 1 
ATOM   3918 N NE2 . HIS C 1 46  ? 36.646  -69.814  31.788  1.00 92.18  ? 37  HIS C NE2 1 
ATOM   3919 N N   . ASN C 1 47  ? 37.882  -69.789  37.215  1.00 92.95  ? 38  ASN C N   1 
ATOM   3920 C CA  . ASN C 1 47  ? 36.970  -70.571  38.034  1.00 91.34  ? 38  ASN C CA  1 
ATOM   3921 C C   . ASN C 1 47  ? 35.699  -70.923  37.285  1.00 90.97  ? 38  ASN C C   1 
ATOM   3922 O O   . ASN C 1 47  ? 35.143  -71.996  37.488  1.00 91.96  ? 38  ASN C O   1 
ATOM   3923 C CB  . ASN C 1 47  ? 36.637  -69.836  39.329  1.00 90.17  ? 38  ASN C CB  1 
ATOM   3924 C CG  . ASN C 1 47  ? 36.253  -68.400  39.090  1.00 91.50  ? 38  ASN C CG  1 
ATOM   3925 O OD1 . ASN C 1 47  ? 35.528  -68.091  38.145  1.00 92.56  ? 38  ASN C OD1 1 
ATOM   3926 N ND2 . ASN C 1 47  ? 36.762  -67.505  39.927  1.00 89.01  ? 38  ASN C ND2 1 
ATOM   3927 N N   . GLY C 1 48  ? 35.248  -70.028  36.412  1.00 91.86  ? 39  GLY C N   1 
ATOM   3928 C CA  . GLY C 1 48  ? 34.028  -70.265  35.660  1.00 92.28  ? 39  GLY C CA  1 
ATOM   3929 C C   . GLY C 1 48  ? 32.780  -69.899  36.442  1.00 90.57  ? 39  GLY C C   1 
ATOM   3930 O O   . GLY C 1 48  ? 31.718  -70.497  36.268  1.00 89.06  ? 39  GLY C O   1 
ATOM   3931 N N   . LYS C 1 49  ? 32.914  -68.914  37.319  1.00 89.67  ? 40  LYS C N   1 
ATOM   3932 C CA  . LYS C 1 49  ? 31.792  -68.456  38.118  1.00 90.14  ? 40  LYS C CA  1 
ATOM   3933 C C   . LYS C 1 49  ? 31.662  -66.956  37.969  1.00 87.81  ? 40  LYS C C   1 
ATOM   3934 O O   . LYS C 1 49  ? 32.589  -66.294  37.512  1.00 87.79  ? 40  LYS C O   1 
ATOM   3935 C CB  . LYS C 1 49  ? 32.016  -68.791  39.591  1.00 93.40  ? 40  LYS C CB  1 
ATOM   3936 C CG  . LYS C 1 49  ? 32.326  -70.251  39.860  1.00 96.45  ? 40  LYS C CG  1 
ATOM   3937 C CD  . LYS C 1 49  ? 31.265  -71.162  39.239  1.00 99.00  ? 40  LYS C CD  1 
ATOM   3938 C CE  . LYS C 1 49  ? 31.423  -72.610  39.705  1.00 101.19 ? 40  LYS C CE  1 
ATOM   3939 N NZ  . LYS C 1 49  ? 30.383  -73.524  39.135  1.00 103.50 ? 40  LYS C NZ  1 
ATOM   3940 N N   . LEU C 1 50  ? 30.511  -66.419  38.353  1.00 85.77  ? 41  LEU C N   1 
ATOM   3941 C CA  . LEU C 1 50  ? 30.363  -64.976  38.467  1.00 85.07  ? 41  LEU C CA  1 
ATOM   3942 C C   . LEU C 1 50  ? 30.395  -64.630  39.945  1.00 84.02  ? 41  LEU C C   1 
ATOM   3943 O O   . LEU C 1 50  ? 29.546  -65.082  40.702  1.00 86.05  ? 41  LEU C O   1 
ATOM   3944 C CB  . LEU C 1 50  ? 29.053  -64.510  37.837  1.00 86.19  ? 41  LEU C CB  1 
ATOM   3945 C CG  . LEU C 1 50  ? 28.862  -64.747  36.338  1.00 80.04  ? 41  LEU C CG  1 
ATOM   3946 C CD1 . LEU C 1 50  ? 27.649  -63.993  35.874  1.00 77.87  ? 41  LEU C CD1 1 
ATOM   3947 C CD2 . LEU C 1 50  ? 30.072  -64.297  35.569  1.00 79.36  ? 41  LEU C CD2 1 
ATOM   3948 N N   . CYS C 1 51  ? 31.371  -63.828  40.356  1.00 83.18  ? 42  CYS C N   1 
ATOM   3949 C CA  . CYS C 1 51  ? 31.679  -63.686  41.776  1.00 85.80  ? 42  CYS C CA  1 
ATOM   3950 C C   . CYS C 1 51  ? 31.345  -62.308  42.309  1.00 84.30  ? 42  CYS C C   1 
ATOM   3951 O O   . CYS C 1 51  ? 30.821  -61.479  41.577  1.00 85.27  ? 42  CYS C O   1 
ATOM   3952 C CB  . CYS C 1 51  ? 33.163  -63.974  42.015  1.00 90.06  ? 42  CYS C CB  1 
ATOM   3953 S SG  . CYS C 1 51  ? 33.703  -65.640  41.522  1.00 98.76  ? 42  CYS C SG  1 
ATOM   3954 N N   . LYS C 1 52  ? 31.629  -62.075  43.589  1.00 83.22  ? 43  LYS C N   1 
ATOM   3955 C CA  . LYS C 1 52  ? 31.602  -60.719  44.125  1.00 84.28  ? 43  LYS C CA  1 
ATOM   3956 C C   . LYS C 1 52  ? 32.916  -60.042  43.754  1.00 84.25  ? 43  LYS C C   1 
ATOM   3957 O O   . LYS C 1 52  ? 33.975  -60.659  43.829  1.00 85.03  ? 43  LYS C O   1 
ATOM   3958 C CB  . LYS C 1 52  ? 31.446  -60.713  45.647  1.00 89.33  ? 43  LYS C CB  1 
ATOM   3959 C CG  . LYS C 1 52  ? 30.175  -61.349  46.187  1.00 90.04  ? 43  LYS C CG  1 
ATOM   3960 C CD  . LYS C 1 52  ? 29.992  -60.996  47.658  1.00 88.42  ? 43  LYS C CD  1 
ATOM   3961 C CE  . LYS C 1 52  ? 29.201  -62.057  48.403  1.00 93.89  ? 43  LYS C CE  1 
ATOM   3962 N NZ  . LYS C 1 52  ? 29.940  -63.348  48.452  1.00 94.88  ? 43  LYS C NZ  1 
ATOM   3963 N N   . LEU C 1 53  ? 32.851  -58.775  43.360  1.00 86.89  ? 44  LEU C N   1 
ATOM   3964 C CA  . LEU C 1 53  ? 34.056  -58.044  42.987  1.00 86.75  ? 44  LEU C CA  1 
ATOM   3965 C C   . LEU C 1 53  ? 34.486  -57.151  44.133  1.00 86.66  ? 44  LEU C C   1 
ATOM   3966 O O   . LEU C 1 53  ? 33.851  -56.131  44.403  1.00 84.85  ? 44  LEU C O   1 
ATOM   3967 C CB  . LEU C 1 53  ? 33.814  -57.187  41.747  1.00 81.38  ? 44  LEU C CB  1 
ATOM   3968 C CG  . LEU C 1 53  ? 35.099  -56.810  41.014  1.00 83.92  ? 44  LEU C CG  1 
ATOM   3969 C CD1 . LEU C 1 53  ? 35.510  -57.938  40.081  1.00 85.33  ? 44  LEU C CD1 1 
ATOM   3970 C CD2 . LEU C 1 53  ? 34.928  -55.520  40.238  1.00 87.19  ? 44  LEU C CD2 1 
ATOM   3971 N N   . ARG C 1 54  ? 35.582  -57.529  44.783  1.00 89.77  ? 45  ARG C N   1 
ATOM   3972 C CA  . ARG C 1 54  ? 36.059  -56.825  45.966  1.00 94.56  ? 45  ARG C CA  1 
ATOM   3973 C C   . ARG C 1 54  ? 35.051  -56.936  47.112  1.00 91.72  ? 45  ARG C C   1 
ATOM   3974 O O   . ARG C 1 54  ? 34.915  -56.020  47.928  1.00 89.65  ? 45  ARG C O   1 
ATOM   3975 C CB  . ARG C 1 54  ? 36.312  -55.352  45.649  1.00 97.56  ? 45  ARG C CB  1 
ATOM   3976 C CG  . ARG C 1 54  ? 37.219  -55.095  44.465  1.00 96.73  ? 45  ARG C CG  1 
ATOM   3977 C CD  . ARG C 1 54  ? 37.677  -53.647  44.479  1.00 103.85 ? 45  ARG C CD  1 
ATOM   3978 N NE  . ARG C 1 54  ? 38.344  -53.306  45.737  1.00 110.66 ? 45  ARG C NE  1 
ATOM   3979 C CZ  . ARG C 1 54  ? 37.735  -52.806  46.813  1.00 109.80 ? 45  ARG C CZ  1 
ATOM   3980 N NH1 . ARG C 1 54  ? 36.424  -52.581  46.805  1.00 107.14 ? 45  ARG C NH1 1 
ATOM   3981 N NH2 . ARG C 1 54  ? 38.445  -52.532  47.903  1.00 111.28 ? 45  ARG C NH2 1 
ATOM   3982 N N   . GLY C 1 55  ? 34.340  -58.056  47.165  1.00 90.38  ? 46  GLY C N   1 
ATOM   3983 C CA  . GLY C 1 55  ? 33.364  -58.276  48.216  1.00 92.21  ? 46  GLY C CA  1 
ATOM   3984 C C   . GLY C 1 55  ? 31.946  -57.843  47.879  1.00 91.01  ? 46  GLY C C   1 
ATOM   3985 O O   . GLY C 1 55  ? 30.989  -58.336  48.482  1.00 91.61  ? 46  GLY C O   1 
ATOM   3986 N N   . VAL C 1 56  ? 31.799  -56.935  46.915  1.00 89.54  ? 47  VAL C N   1 
ATOM   3987 C CA  . VAL C 1 56  ? 30.473  -56.434  46.541  1.00 84.68  ? 47  VAL C CA  1 
ATOM   3988 C C   . VAL C 1 56  ? 29.863  -57.218  45.384  1.00 81.82  ? 47  VAL C C   1 
ATOM   3989 O O   . VAL C 1 56  ? 30.469  -57.359  44.323  1.00 80.93  ? 47  VAL C O   1 
ATOM   3990 C CB  . VAL C 1 56  ? 30.485  -54.934  46.187  1.00 80.78  ? 47  VAL C CB  1 
ATOM   3991 C CG1 . VAL C 1 56  ? 29.079  -54.469  45.826  1.00 73.35  ? 47  VAL C CG1 1 
ATOM   3992 C CG2 . VAL C 1 56  ? 31.049  -54.117  47.343  1.00 82.10  ? 47  VAL C CG2 1 
ATOM   3993 N N   . ALA C 1 57  ? 28.651  -57.717  45.602  1.00 81.24  ? 48  ALA C N   1 
ATOM   3994 C CA  . ALA C 1 57  ? 27.969  -58.546  44.621  1.00 79.63  ? 48  ALA C CA  1 
ATOM   3995 C C   . ALA C 1 57  ? 27.509  -57.730  43.410  1.00 77.99  ? 48  ALA C C   1 
ATOM   3996 O O   . ALA C 1 57  ? 27.211  -56.538  43.528  1.00 76.47  ? 48  ALA C O   1 
ATOM   3997 C CB  . ALA C 1 57  ? 26.787  -59.262  45.269  1.00 77.61  ? 48  ALA C CB  1 
ATOM   3998 N N   . PRO C 1 58  ? 27.471  -58.377  42.235  1.00 76.15  ? 49  PRO C N   1 
ATOM   3999 C CA  . PRO C 1 58  ? 26.983  -57.802  40.976  1.00 74.73  ? 49  PRO C CA  1 
ATOM   4000 C C   . PRO C 1 58  ? 25.470  -57.775  40.942  1.00 74.04  ? 49  PRO C C   1 
ATOM   4001 O O   . PRO C 1 58  ? 24.849  -58.712  41.440  1.00 76.38  ? 49  PRO C O   1 
ATOM   4002 C CB  . PRO C 1 58  ? 27.441  -58.822  39.943  1.00 74.59  ? 49  PRO C CB  1 
ATOM   4003 C CG  . PRO C 1 58  ? 27.382  -60.120  40.680  1.00 77.71  ? 49  PRO C CG  1 
ATOM   4004 C CD  . PRO C 1 58  ? 27.851  -59.793  42.077  1.00 78.31  ? 49  PRO C CD  1 
ATOM   4005 N N   . LEU C 1 59  ? 24.882  -56.757  40.329  1.00 69.68  ? 50  LEU C N   1 
ATOM   4006 C CA  . LEU C 1 59  ? 23.450  -56.772  40.100  1.00 67.37  ? 50  LEU C CA  1 
ATOM   4007 C C   . LEU C 1 59  ? 23.142  -57.655  38.901  1.00 69.36  ? 50  LEU C C   1 
ATOM   4008 O O   . LEU C 1 59  ? 23.687  -57.455  37.814  1.00 70.27  ? 50  LEU C O   1 
ATOM   4009 C CB  . LEU C 1 59  ? 22.925  -55.365  39.859  1.00 67.46  ? 50  LEU C CB  1 
ATOM   4010 C CG  . LEU C 1 59  ? 21.506  -55.362  39.300  1.00 65.21  ? 50  LEU C CG  1 
ATOM   4011 C CD1 . LEU C 1 59  ? 20.571  -56.112  40.226  1.00 68.65  ? 50  LEU C CD1 1 
ATOM   4012 C CD2 . LEU C 1 59  ? 21.042  -53.937  39.086  1.00 64.88  ? 50  LEU C CD2 1 
ATOM   4013 N N   . HIS C 1 60  ? 22.264  -58.630  39.088  1.00 68.43  ? 51  HIS C N   1 
ATOM   4014 C CA  . HIS C 1 60  ? 22.018  -59.596  38.028  1.00 67.98  ? 51  HIS C CA  1 
ATOM   4015 C C   . HIS C 1 60  ? 20.563  -59.584  37.582  1.00 68.95  ? 51  HIS C C   1 
ATOM   4016 O O   . HIS C 1 60  ? 19.664  -59.920  38.355  1.00 71.92  ? 51  HIS C O   1 
ATOM   4017 C CB  . HIS C 1 60  ? 22.438  -60.991  38.478  1.00 67.11  ? 51  HIS C CB  1 
ATOM   4018 C CG  . HIS C 1 60  ? 22.094  -62.070  37.504  1.00 66.74  ? 51  HIS C CG  1 
ATOM   4019 N ND1 . HIS C 1 60  ? 20.794  -62.370  37.155  1.00 67.31  ? 51  HIS C ND1 1 
ATOM   4020 C CD2 . HIS C 1 60  ? 22.877  -62.933  36.815  1.00 68.10  ? 51  HIS C CD2 1 
ATOM   4021 C CE1 . HIS C 1 60  ? 20.793  -63.369  36.289  1.00 68.14  ? 51  HIS C CE1 1 
ATOM   4022 N NE2 . HIS C 1 60  ? 22.043  -63.729  36.068  1.00 67.65  ? 51  HIS C NE2 1 
ATOM   4023 N N   . LEU C 1 61  ? 20.341  -59.180  36.334  1.00 69.17  ? 52  LEU C N   1 
ATOM   4024 C CA  . LEU C 1 61  ? 18.995  -59.057  35.778  1.00 65.71  ? 52  LEU C CA  1 
ATOM   4025 C C   . LEU C 1 61  ? 18.386  -60.359  35.281  1.00 67.30  ? 52  LEU C C   1 
ATOM   4026 O O   . LEU C 1 61  ? 19.074  -61.274  34.827  1.00 64.43  ? 52  LEU C O   1 
ATOM   4027 C CB  . LEU C 1 61  ? 18.976  -58.020  34.670  1.00 62.73  ? 52  LEU C CB  1 
ATOM   4028 C CG  . LEU C 1 61  ? 19.654  -56.771  35.208  1.00 64.64  ? 52  LEU C CG  1 
ATOM   4029 C CD1 . LEU C 1 61  ? 20.051  -55.825  34.086  1.00 59.37  ? 52  LEU C CD1 1 
ATOM   4030 C CD2 . LEU C 1 61  ? 18.738  -56.108  36.228  1.00 62.90  ? 52  LEU C CD2 1 
ATOM   4031 N N   . GLY C 1 62  ? 17.065  -60.395  35.307  1.00 70.97  ? 53  GLY C N   1 
ATOM   4032 C CA  . GLY C 1 62  ? 16.327  -61.617  35.076  1.00 72.72  ? 53  GLY C CA  1 
ATOM   4033 C C   . GLY C 1 62  ? 16.185  -61.834  33.590  1.00 72.19  ? 53  GLY C C   1 
ATOM   4034 O O   . GLY C 1 62  ? 17.125  -61.596  32.825  1.00 71.10  ? 53  GLY C O   1 
ATOM   4035 N N   . LYS C 1 63  ? 15.031  -62.359  33.192  1.00 73.00  ? 54  LYS C N   1 
ATOM   4036 C CA  . LYS C 1 63  ? 14.654  -62.398  31.785  1.00 72.15  ? 54  LYS C CA  1 
ATOM   4037 C C   . LYS C 1 63  ? 14.591  -60.966  31.264  1.00 68.98  ? 54  LYS C C   1 
ATOM   4038 O O   . LYS C 1 63  ? 14.404  -60.737  30.072  1.00 70.03  ? 54  LYS C O   1 
ATOM   4039 C CB  . LYS C 1 63  ? 13.296  -63.082  31.605  1.00 69.86  ? 54  LYS C CB  1 
ATOM   4040 C CG  . LYS C 1 63  ? 12.174  -62.437  32.398  1.00 71.72  ? 54  LYS C CG  1 
ATOM   4041 C CD  . LYS C 1 63  ? 11.637  -63.381  33.461  1.00 70.10  ? 54  LYS C CD  1 
ATOM   4042 C CE  . LYS C 1 63  ? 10.603  -62.691  34.327  1.00 64.86  ? 54  LYS C CE  1 
ATOM   4043 N NZ  . LYS C 1 63  ? 9.635   -63.680  34.853  1.00 64.44  ? 54  LYS C NZ  1 
ATOM   4044 N N   . CYS C 1 64  ? 14.727  -59.999  32.166  1.00 66.31  ? 55  CYS C N   1 
ATOM   4045 C CA  . CYS C 1 64  ? 14.687  -58.611  31.757  1.00 65.31  ? 55  CYS C CA  1 
ATOM   4046 C C   . CYS C 1 64  ? 16.053  -58.085  31.363  1.00 64.19  ? 55  CYS C C   1 
ATOM   4047 O O   . CYS C 1 64  ? 17.073  -58.748  31.531  1.00 66.60  ? 55  CYS C O   1 
ATOM   4048 C CB  . CYS C 1 64  ? 14.133  -57.768  32.896  1.00 64.35  ? 55  CYS C CB  1 
ATOM   4049 S SG  . CYS C 1 64  ? 12.492  -58.314  33.405  1.00 72.25  ? 55  CYS C SG  1 
ATOM   4050 N N   . ASN C 1 65  ? 16.065  -56.861  30.859  1.00 62.26  ? 56  ASN C N   1 
ATOM   4051 C CA  . ASN C 1 65  ? 17.304  -56.185  30.524  1.00 57.86  ? 56  ASN C CA  1 
ATOM   4052 C C   . ASN C 1 65  ? 17.222  -54.796  31.108  1.00 52.39  ? 56  ASN C C   1 
ATOM   4053 O O   . ASN C 1 65  ? 16.154  -54.374  31.546  1.00 53.24  ? 56  ASN C O   1 
ATOM   4054 C CB  . ASN C 1 65  ? 17.558  -56.168  29.005  1.00 59.59  ? 56  ASN C CB  1 
ATOM   4055 C CG  . ASN C 1 65  ? 16.513  -55.352  28.221  1.00 57.67  ? 56  ASN C CG  1 
ATOM   4056 O OD1 . ASN C 1 65  ? 16.154  -54.235  28.604  1.00 55.12  ? 56  ASN C OD1 1 
ATOM   4057 N ND2 . ASN C 1 65  ? 16.040  -55.912  27.107  1.00 55.65  ? 56  ASN C ND2 1 
ATOM   4058 N N   . ILE C 1 66  ? 18.341  -54.088  31.124  1.00 49.05  ? 57  ILE C N   1 
ATOM   4059 C CA  . ILE C 1 66  ? 18.418  -52.819  31.832  1.00 50.27  ? 57  ILE C CA  1 
ATOM   4060 C C   . ILE C 1 66  ? 17.196  -51.937  31.541  1.00 49.37  ? 57  ILE C C   1 
ATOM   4061 O O   . ILE C 1 66  ? 16.583  -51.369  32.449  1.00 48.89  ? 57  ILE C O   1 
ATOM   4062 C CB  . ILE C 1 66  ? 19.734  -52.087  31.495  1.00 47.36  ? 57  ILE C CB  1 
ATOM   4063 C CG1 . ILE C 1 66  ? 20.923  -52.876  32.043  1.00 51.70  ? 57  ILE C CG1 1 
ATOM   4064 C CG2 . ILE C 1 66  ? 19.746  -50.677  32.059  1.00 42.81  ? 57  ILE C CG2 1 
ATOM   4065 C CD1 . ILE C 1 66  ? 22.265  -52.342  31.617  1.00 53.88  ? 57  ILE C CD1 1 
ATOM   4066 N N   . ALA C 1 67  ? 16.828  -51.849  30.274  1.00 48.41  ? 58  ALA C N   1 
ATOM   4067 C CA  . ALA C 1 67  ? 15.657  -51.084  29.887  1.00 47.68  ? 58  ALA C CA  1 
ATOM   4068 C C   . ALA C 1 67  ? 14.425  -51.547  30.656  1.00 49.72  ? 58  ALA C C   1 
ATOM   4069 O O   . ALA C 1 67  ? 13.765  -50.751  31.323  1.00 47.87  ? 58  ALA C O   1 
ATOM   4070 C CB  . ALA C 1 67  ? 15.419  -51.232  28.409  1.00 48.20  ? 58  ALA C CB  1 
ATOM   4071 N N   . GLY C 1 68  ? 14.109  -52.835  30.549  1.00 50.54  ? 59  GLY C N   1 
ATOM   4072 C CA  . GLY C 1 68  ? 12.910  -53.362  31.168  1.00 51.74  ? 59  GLY C CA  1 
ATOM   4073 C C   . GLY C 1 68  ? 12.964  -53.128  32.651  1.00 50.79  ? 59  GLY C C   1 
ATOM   4074 O O   . GLY C 1 68  ? 11.999  -52.694  33.290  1.00 51.63  ? 59  GLY C O   1 
ATOM   4075 N N   . TRP C 1 69  ? 14.131  -53.421  33.194  1.00 52.02  ? 60  TRP C N   1 
ATOM   4076 C CA  . TRP C 1 69  ? 14.331  -53.347  34.619  1.00 51.35  ? 60  TRP C CA  1 
ATOM   4077 C C   . TRP C 1 69  ? 14.151  -51.920  35.150  1.00 47.68  ? 60  TRP C C   1 
ATOM   4078 O O   . TRP C 1 69  ? 13.336  -51.677  36.035  1.00 49.57  ? 60  TRP C O   1 
ATOM   4079 C CB  . TRP C 1 69  ? 15.692  -53.923  34.959  1.00 52.13  ? 60  TRP C CB  1 
ATOM   4080 C CG  . TRP C 1 69  ? 16.170  -53.579  36.289  1.00 53.19  ? 60  TRP C CG  1 
ATOM   4081 C CD1 . TRP C 1 69  ? 15.719  -54.065  37.471  1.00 56.22  ? 60  TRP C CD1 1 
ATOM   4082 C CD2 . TRP C 1 69  ? 17.195  -52.639  36.599  1.00 51.65  ? 60  TRP C CD2 1 
ATOM   4083 N NE1 . TRP C 1 69  ? 16.410  -53.484  38.509  1.00 56.43  ? 60  TRP C NE1 1 
ATOM   4084 C CE2 . TRP C 1 69  ? 17.324  -52.606  37.993  1.00 49.80  ? 60  TRP C CE2 1 
ATOM   4085 C CE3 . TRP C 1 69  ? 18.022  -51.826  35.828  1.00 52.24  ? 60  TRP C CE3 1 
ATOM   4086 C CZ2 . TRP C 1 69  ? 18.243  -51.793  38.633  1.00 51.89  ? 60  TRP C CZ2 1 
ATOM   4087 C CZ3 . TRP C 1 69  ? 18.939  -51.022  36.471  1.00 53.00  ? 60  TRP C CZ3 1 
ATOM   4088 C CH2 . TRP C 1 69  ? 19.041  -51.012  37.853  1.00 51.11  ? 60  TRP C CH2 1 
ATOM   4089 N N   . ILE C 1 70  ? 14.903  -50.974  34.614  1.00 48.03  ? 61  ILE C N   1 
ATOM   4090 C CA  . ILE C 1 70  ? 14.809  -49.600  35.095  1.00 49.63  ? 61  ILE C CA  1 
ATOM   4091 C C   . ILE C 1 70  ? 13.459  -48.951  34.777  1.00 46.41  ? 61  ILE C C   1 
ATOM   4092 O O   . ILE C 1 70  ? 13.053  -47.996  35.427  1.00 46.10  ? 61  ILE C O   1 
ATOM   4093 C CB  . ILE C 1 70  ? 15.916  -48.733  34.499  1.00 49.19  ? 61  ILE C CB  1 
ATOM   4094 C CG1 . ILE C 1 70  ? 16.085  -47.444  35.309  1.00 48.77  ? 61  ILE C CG1 1 
ATOM   4095 C CG2 . ILE C 1 70  ? 15.634  -48.460  33.032  1.00 45.15  ? 61  ILE C CG2 1 
ATOM   4096 C CD1 . ILE C 1 70  ? 16.775  -47.642  36.638  1.00 48.09  ? 61  ILE C CD1 1 
ATOM   4097 N N   . LEU C 1 71  ? 12.789  -49.435  33.742  1.00 48.12  ? 62  LEU C N   1 
ATOM   4098 C CA  . LEU C 1 71  ? 11.446  -48.958  33.422  1.00 46.96  ? 62  LEU C CA  1 
ATOM   4099 C C   . LEU C 1 71  ? 10.374  -49.641  34.268  1.00 49.29  ? 62  LEU C C   1 
ATOM   4100 O O   . LEU C 1 71  ? 9.301   -49.085  34.524  1.00 47.08  ? 62  LEU C O   1 
ATOM   4101 C CB  . LEU C 1 71  ? 11.146  -49.180  31.943  1.00 45.42  ? 62  LEU C CB  1 
ATOM   4102 C CG  . LEU C 1 71  ? 11.968  -48.350  30.959  1.00 43.07  ? 62  LEU C CG  1 
ATOM   4103 C CD1 . LEU C 1 71  ? 11.786  -48.906  29.585  1.00 43.58  ? 62  LEU C CD1 1 
ATOM   4104 C CD2 . LEU C 1 71  ? 11.587  -46.879  30.990  1.00 38.64  ? 62  LEU C CD2 1 
ATOM   4105 N N   . GLY C 1 72  ? 10.670  -50.854  34.712  1.00 48.92  ? 63  GLY C N   1 
ATOM   4106 C CA  . GLY C 1 72  ? 9.667   -51.643  35.390  1.00 49.56  ? 63  GLY C CA  1 
ATOM   4107 C C   . GLY C 1 72  ? 8.718   -52.340  34.443  1.00 48.54  ? 63  GLY C C   1 
ATOM   4108 O O   . GLY C 1 72  ? 7.502   -52.316  34.614  1.00 49.96  ? 63  GLY C O   1 
ATOM   4109 N N   . ASN C 1 73  ? 9.272   -52.935  33.405  1.00 48.61  ? 64  ASN C N   1 
ATOM   4110 C CA  . ASN C 1 73  ? 8.521   -53.940  32.703  1.00 52.60  ? 64  ASN C CA  1 
ATOM   4111 C C   . ASN C 1 73  ? 8.049   -54.928  33.765  1.00 57.94  ? 64  ASN C C   1 
ATOM   4112 O O   . ASN C 1 73  ? 8.845   -55.381  34.591  1.00 59.40  ? 64  ASN C O   1 
ATOM   4113 C CB  . ASN C 1 73  ? 9.408   -54.623  31.674  1.00 52.27  ? 64  ASN C CB  1 
ATOM   4114 C CG  . ASN C 1 73  ? 8.651   -55.035  30.443  1.00 58.09  ? 64  ASN C CG  1 
ATOM   4115 O OD1 . ASN C 1 73  ? 7.421   -55.083  30.447  1.00 60.02  ? 64  ASN C OD1 1 
ATOM   4116 N ND2 . ASN C 1 73  ? 9.377   -55.336  29.373  1.00 57.43  ? 64  ASN C ND2 1 
ATOM   4117 N N   . PRO C 1 74  ? 6.750   -55.259  33.763  1.00 59.94  ? 65  PRO C N   1 
ATOM   4118 C CA  . PRO C 1 74  ? 6.172   -56.091  34.825  1.00 61.48  ? 65  PRO C CA  1 
ATOM   4119 C C   . PRO C 1 74  ? 6.806   -57.477  34.939  1.00 63.44  ? 65  PRO C C   1 
ATOM   4120 O O   . PRO C 1 74  ? 6.617   -58.146  35.949  1.00 66.11  ? 65  PRO C O   1 
ATOM   4121 C CB  . PRO C 1 74  ? 4.700   -56.214  34.414  1.00 61.29  ? 65  PRO C CB  1 
ATOM   4122 C CG  . PRO C 1 74  ? 4.452   -55.047  33.545  1.00 55.12  ? 65  PRO C CG  1 
ATOM   4123 C CD  . PRO C 1 74  ? 5.730   -54.844  32.789  1.00 57.34  ? 65  PRO C CD  1 
ATOM   4124 N N   . GLU C 1 75  ? 7.527   -57.916  33.918  1.00 63.70  ? 66  GLU C N   1 
ATOM   4125 C CA  . GLU C 1 75  ? 8.277   -59.158  34.034  1.00 64.57  ? 66  GLU C CA  1 
ATOM   4126 C C   . GLU C 1 75  ? 9.544   -58.927  34.836  1.00 67.81  ? 66  GLU C C   1 
ATOM   4127 O O   . GLU C 1 75  ? 10.163  -59.866  35.328  1.00 70.61  ? 66  GLU C O   1 
ATOM   4128 C CB  . GLU C 1 75  ? 8.630   -59.697  32.662  1.00 63.55  ? 66  GLU C CB  1 
ATOM   4129 C CG  . GLU C 1 75  ? 7.420   -59.946  31.805  1.00 68.36  ? 66  GLU C CG  1 
ATOM   4130 C CD  . GLU C 1 75  ? 6.480   -60.985  32.402  1.00 72.02  ? 66  GLU C CD  1 
ATOM   4131 O OE1 . GLU C 1 75  ? 5.247   -60.767  32.374  1.00 74.77  ? 66  GLU C OE1 1 
ATOM   4132 O OE2 . GLU C 1 75  ? 6.968   -62.029  32.887  1.00 73.86  ? 66  GLU C OE2 1 
ATOM   4133 N N   . CYS C 1 76  ? 9.938   -57.666  34.951  1.00 67.84  ? 67  CYS C N   1 
ATOM   4134 C CA  . CYS C 1 76  ? 11.100  -57.313  35.746  1.00 68.35  ? 67  CYS C CA  1 
ATOM   4135 C C   . CYS C 1 76  ? 10.645  -57.069  37.159  1.00 69.87  ? 67  CYS C C   1 
ATOM   4136 O O   . CYS C 1 76  ? 11.438  -56.719  38.024  1.00 72.24  ? 67  CYS C O   1 
ATOM   4137 C CB  . CYS C 1 76  ? 11.782  -56.074  35.185  1.00 63.05  ? 67  CYS C CB  1 
ATOM   4138 S SG  . CYS C 1 76  ? 12.286  -56.286  33.477  1.00 66.80  ? 67  CYS C SG  1 
ATOM   4139 N N   . GLU C 1 77  ? 9.346   -57.238  37.372  1.00 70.62  ? 68  GLU C N   1 
ATOM   4140 C CA  . GLU C 1 77  ? 8.798   -57.344  38.710  1.00 76.29  ? 68  GLU C CA  1 
ATOM   4141 C C   . GLU C 1 77  ? 9.562   -58.508  39.329  1.00 81.66  ? 68  GLU C C   1 
ATOM   4142 O O   . GLU C 1 77  ? 9.924   -59.462  38.624  1.00 81.14  ? 68  GLU C O   1 
ATOM   4143 C CB  . GLU C 1 77  ? 7.300   -57.671  38.629  1.00 75.84  ? 68  GLU C CB  1 
ATOM   4144 C CG  . GLU C 1 77  ? 6.508   -57.592  39.940  1.00 83.37  ? 68  GLU C CG  1 
ATOM   4145 C CD  . GLU C 1 77  ? 5.032   -58.005  39.778  1.00 84.34  ? 68  GLU C CD  1 
ATOM   4146 O OE1 . GLU C 1 77  ? 4.137   -57.295  40.289  1.00 87.01  ? 68  GLU C OE1 1 
ATOM   4147 O OE2 . GLU C 1 77  ? 4.759   -59.049  39.152  1.00 79.71  ? 68  GLU C OE2 1 
ATOM   4148 N N   . SER C 1 78  ? 9.822   -58.424  40.632  1.00 82.60  ? 69  SER C N   1 
ATOM   4149 C CA  . SER C 1 78  ? 10.536  -59.481  41.358  1.00 83.61  ? 69  SER C CA  1 
ATOM   4150 C C   . SER C 1 78  ? 12.012  -59.694  40.971  1.00 86.48  ? 69  SER C C   1 
ATOM   4151 O O   . SER C 1 78  ? 12.474  -60.833  40.871  1.00 87.08  ? 69  SER C O   1 
ATOM   4152 C CB  . SER C 1 78  ? 9.778   -60.806  41.251  1.00 84.30  ? 69  SER C CB  1 
ATOM   4153 O OG  . SER C 1 78  ? 8.447   -60.670  41.720  1.00 90.72  ? 69  SER C OG  1 
ATOM   4154 N N   . LEU C 1 79  ? 12.740  -58.602  40.747  1.00 86.54  ? 70  LEU C N   1 
ATOM   4155 C CA  . LEU C 1 79  ? 14.191  -58.655  40.536  1.00 86.43  ? 70  LEU C CA  1 
ATOM   4156 C C   . LEU C 1 79  ? 14.952  -58.178  41.786  1.00 92.78  ? 70  LEU C C   1 
ATOM   4157 O O   . LEU C 1 79  ? 14.345  -57.980  42.841  1.00 94.63  ? 70  LEU C O   1 
ATOM   4158 C CB  . LEU C 1 79  ? 14.619  -57.934  39.247  1.00 80.60  ? 70  LEU C CB  1 
ATOM   4159 C CG  . LEU C 1 79  ? 14.757  -58.828  37.997  1.00 77.40  ? 70  LEU C CG  1 
ATOM   4160 C CD1 . LEU C 1 79  ? 13.485  -59.626  37.698  1.00 77.23  ? 70  LEU C CD1 1 
ATOM   4161 C CD2 . LEU C 1 79  ? 15.188  -58.041  36.765  1.00 69.06  ? 70  LEU C CD2 1 
ATOM   4162 N N   . SER C 1 80  ? 16.270  -58.011  41.670  1.00 94.94  ? 71  SER C N   1 
ATOM   4163 C CA  . SER C 1 80  ? 17.177  -58.005  42.830  1.00 92.81  ? 71  SER C CA  1 
ATOM   4164 C C   . SER C 1 80  ? 17.320  -56.708  43.663  1.00 92.94  ? 71  SER C C   1 
ATOM   4165 O O   . SER C 1 80  ? 16.810  -56.621  44.787  1.00 96.00  ? 71  SER C O   1 
ATOM   4166 C CB  . SER C 1 80  ? 18.565  -58.474  42.370  1.00 90.45  ? 71  SER C CB  1 
ATOM   4167 O OG  . SER C 1 80  ? 18.476  -59.343  41.241  1.00 84.01  ? 71  SER C OG  1 
ATOM   4168 N N   . THR C 1 81  ? 18.004  -55.712  43.100  1.00 95.69  ? 72  THR C N   1 
ATOM   4169 C CA  . THR C 1 81  ? 18.392  -54.476  43.814  1.00 96.22  ? 72  THR C CA  1 
ATOM   4170 C C   . THR C 1 81  ? 19.307  -54.564  45.059  1.00 92.81  ? 72  THR C C   1 
ATOM   4171 O O   . THR C 1 81  ? 20.463  -54.990  44.995  1.00 88.01  ? 72  THR C O   1 
ATOM   4172 C CB  . THR C 1 81  ? 17.159  -53.597  44.192  1.00 96.47  ? 72  THR C CB  1 
ATOM   4173 O OG1 . THR C 1 81  ? 16.317  -54.298  45.122  1.00 94.30  ? 72  THR C OG1 1 
ATOM   4174 C CG2 . THR C 1 81  ? 16.360  -53.202  42.945  1.00 94.63  ? 72  THR C CG2 1 
ATOM   4175 N N   . ALA C 1 82  ? 18.735  -54.163  46.186  1.00 93.37  ? 73  ALA C N   1 
ATOM   4176 C CA  . ALA C 1 82  ? 19.419  -53.502  47.299  1.00 95.20  ? 73  ALA C CA  1 
ATOM   4177 C C   . ALA C 1 82  ? 20.098  -52.190  46.866  1.00 90.12  ? 73  ALA C C   1 
ATOM   4178 O O   . ALA C 1 82  ? 19.683  -51.571  45.882  1.00 88.03  ? 73  ALA C O   1 
ATOM   4179 C CB  . ALA C 1 82  ? 20.436  -54.450  47.956  1.00 94.62  ? 73  ALA C CB  1 
ATOM   4180 N N   . SER C 1 83  ? 21.163  -51.788  47.555  1.00 84.16  ? 74  SER C N   1 
ATOM   4181 C CA  . SER C 1 83  ? 21.656  -50.424  47.367  1.00 77.37  ? 74  SER C CA  1 
ATOM   4182 C C   . SER C 1 83  ? 22.896  -50.310  46.494  1.00 71.58  ? 74  SER C C   1 
ATOM   4183 O O   . SER C 1 83  ? 23.287  -49.212  46.102  1.00 68.38  ? 74  SER C O   1 
ATOM   4184 C CB  . SER C 1 83  ? 21.906  -49.770  48.734  1.00 77.82  ? 74  SER C CB  1 
ATOM   4185 O OG  . SER C 1 83  ? 21.906  -48.350  48.651  1.00 78.45  ? 74  SER C OG  1 
ATOM   4186 N N   . SER C 1 84  ? 23.490  -51.449  46.165  1.00 71.07  ? 75  SER C N   1 
ATOM   4187 C CA  . SER C 1 84  ? 24.811  -51.455  45.554  1.00 70.97  ? 75  SER C CA  1 
ATOM   4188 C C   . SER C 1 84  ? 25.041  -52.697  44.716  1.00 68.64  ? 75  SER C C   1 
ATOM   4189 O O   . SER C 1 84  ? 24.513  -53.771  45.006  1.00 69.38  ? 75  SER C O   1 
ATOM   4190 C CB  . SER C 1 84  ? 25.906  -51.352  46.630  1.00 72.50  ? 75  SER C CB  1 
ATOM   4191 O OG  . SER C 1 84  ? 25.812  -52.393  47.592  1.00 69.00  ? 75  SER C OG  1 
ATOM   4192 N N   . TRP C 1 85  ? 25.838  -52.546  43.674  1.00 66.18  ? 76  TRP C N   1 
ATOM   4193 C CA  . TRP C 1 85  ? 26.365  -53.695  42.975  1.00 68.41  ? 76  TRP C CA  1 
ATOM   4194 C C   . TRP C 1 85  ? 27.695  -53.276  42.427  1.00 70.77  ? 76  TRP C C   1 
ATOM   4195 O O   . TRP C 1 85  ? 27.911  -52.102  42.118  1.00 69.60  ? 76  TRP C O   1 
ATOM   4196 C CB  . TRP C 1 85  ? 25.446  -54.145  41.838  1.00 70.73  ? 76  TRP C CB  1 
ATOM   4197 C CG  . TRP C 1 85  ? 25.103  -53.038  40.889  1.00 71.24  ? 76  TRP C CG  1 
ATOM   4198 C CD1 . TRP C 1 85  ? 25.746  -52.722  39.731  1.00 66.78  ? 76  TRP C CD1 1 
ATOM   4199 C CD2 . TRP C 1 85  ? 24.035  -52.089  41.030  1.00 71.23  ? 76  TRP C CD2 1 
ATOM   4200 N NE1 . TRP C 1 85  ? 25.150  -51.634  39.145  1.00 67.83  ? 76  TRP C NE1 1 
ATOM   4201 C CE2 . TRP C 1 85  ? 24.098  -51.225  39.922  1.00 66.44  ? 76  TRP C CE2 1 
ATOM   4202 C CE3 . TRP C 1 85  ? 23.036  -51.885  41.993  1.00 71.58  ? 76  TRP C CE3 1 
ATOM   4203 C CZ2 . TRP C 1 85  ? 23.197  -50.174  39.742  1.00 66.41  ? 76  TRP C CZ2 1 
ATOM   4204 C CZ3 . TRP C 1 85  ? 22.139  -50.841  41.814  1.00 70.79  ? 76  TRP C CZ3 1 
ATOM   4205 C CH2 . TRP C 1 85  ? 22.224  -50.000  40.693  1.00 67.49  ? 76  TRP C CH2 1 
ATOM   4206 N N   . SER C 1 86  ? 28.585  -54.248  42.305  1.00 72.67  ? 77  SER C N   1 
ATOM   4207 C CA  . SER C 1 86  ? 29.889  -54.014  41.735  1.00 73.72  ? 77  SER C CA  1 
ATOM   4208 C C   . SER C 1 86  ? 29.662  -53.804  40.249  1.00 73.87  ? 77  SER C C   1 
ATOM   4209 O O   . SER C 1 86  ? 29.950  -52.736  39.711  1.00 74.50  ? 77  SER C O   1 
ATOM   4210 C CB  . SER C 1 86  ? 30.780  -55.223  41.985  1.00 77.13  ? 77  SER C CB  1 
ATOM   4211 O OG  . SER C 1 86  ? 29.990  -56.394  42.094  1.00 76.62  ? 77  SER C OG  1 
ATOM   4212 N N   . TYR C 1 87  ? 29.140  -54.828  39.584  1.00 71.16  ? 78  TYR C N   1 
ATOM   4213 C CA  . TYR C 1 87  ? 28.806  -54.718  38.169  1.00 69.23  ? 78  TYR C CA  1 
ATOM   4214 C C   . TYR C 1 87  ? 27.379  -55.175  37.896  1.00 67.54  ? 78  TYR C C   1 
ATOM   4215 O O   . TYR C 1 87  ? 26.608  -55.432  38.818  1.00 68.11  ? 78  TYR C O   1 
ATOM   4216 C CB  . TYR C 1 87  ? 29.788  -55.522  37.321  1.00 69.74  ? 78  TYR C CB  1 
ATOM   4217 C CG  . TYR C 1 87  ? 29.863  -56.989  37.696  1.00 72.87  ? 78  TYR C CG  1 
ATOM   4218 C CD1 . TYR C 1 87  ? 30.562  -57.405  38.826  1.00 73.94  ? 78  TYR C CD1 1 
ATOM   4219 C CD2 . TYR C 1 87  ? 29.242  -57.957  36.919  1.00 69.87  ? 78  TYR C CD2 1 
ATOM   4220 C CE1 . TYR C 1 87  ? 30.637  -58.743  39.173  1.00 73.81  ? 78  TYR C CE1 1 
ATOM   4221 C CE2 . TYR C 1 87  ? 29.319  -59.296  37.255  1.00 72.84  ? 78  TYR C CE2 1 
ATOM   4222 C CZ  . TYR C 1 87  ? 30.016  -59.687  38.384  1.00 74.26  ? 78  TYR C CZ  1 
ATOM   4223 O OH  . TYR C 1 87  ? 30.086  -61.024  38.720  1.00 75.02  ? 78  TYR C OH  1 
ATOM   4224 N N   . ILE C 1 88  ? 27.029  -55.250  36.618  1.00 66.05  ? 79  ILE C N   1 
ATOM   4225 C CA  . ILE C 1 88  ? 25.707  -55.699  36.220  1.00 63.59  ? 79  ILE C CA  1 
ATOM   4226 C C   . ILE C 1 88  ? 25.799  -56.875  35.271  1.00 64.28  ? 79  ILE C C   1 
ATOM   4227 O O   . ILE C 1 88  ? 26.608  -56.885  34.341  1.00 66.24  ? 79  ILE C O   1 
ATOM   4228 C CB  . ILE C 1 88  ? 24.917  -54.590  35.528  1.00 60.74  ? 79  ILE C CB  1 
ATOM   4229 C CG1 . ILE C 1 88  ? 25.005  -53.295  36.336  1.00 62.48  ? 79  ILE C CG1 1 
ATOM   4230 C CG2 . ILE C 1 88  ? 23.479  -55.026  35.327  1.00 58.94  ? 79  ILE C CG2 1 
ATOM   4231 C CD1 . ILE C 1 88  ? 23.923  -52.307  36.011  1.00 58.80  ? 79  ILE C CD1 1 
ATOM   4232 N N   . VAL C 1 89  ? 24.958  -57.869  35.502  1.00 64.27  ? 80  VAL C N   1 
ATOM   4233 C CA  . VAL C 1 89  ? 24.957  -59.045  34.657  1.00 63.87  ? 80  VAL C CA  1 
ATOM   4234 C C   . VAL C 1 89  ? 23.648  -59.165  33.899  1.00 65.92  ? 80  VAL C C   1 
ATOM   4235 O O   . VAL C 1 89  ? 22.571  -59.050  34.474  1.00 66.69  ? 80  VAL C O   1 
ATOM   4236 C CB  . VAL C 1 89  ? 25.187  -60.321  35.475  1.00 65.22  ? 80  VAL C CB  1 
ATOM   4237 C CG1 . VAL C 1 89  ? 25.049  -61.553  34.593  1.00 67.25  ? 80  VAL C CG1 1 
ATOM   4238 C CG2 . VAL C 1 89  ? 26.546  -60.277  36.112  1.00 67.29  ? 80  VAL C CG2 1 
ATOM   4239 N N   . GLU C 1 90  ? 23.749  -59.391  32.597  1.00 64.58  ? 81  GLU C N   1 
ATOM   4240 C CA  . GLU C 1 90  ? 22.584  -59.667  31.778  1.00 65.25  ? 81  GLU C CA  1 
ATOM   4241 C C   . GLU C 1 90  ? 22.787  -61.030  31.147  1.00 68.99  ? 81  GLU C C   1 
ATOM   4242 O O   . GLU C 1 90  ? 23.915  -61.522  31.068  1.00 70.74  ? 81  GLU C O   1 
ATOM   4243 C CB  . GLU C 1 90  ? 22.413  -58.605  30.690  1.00 66.37  ? 81  GLU C CB  1 
ATOM   4244 C CG  . GLU C 1 90  ? 21.680  -57.343  31.125  1.00 61.32  ? 81  GLU C CG  1 
ATOM   4245 C CD  . GLU C 1 90  ? 21.584  -56.305  30.011  1.00 60.05  ? 81  GLU C CD  1 
ATOM   4246 O OE1 . GLU C 1 90  ? 21.447  -56.673  28.823  1.00 56.28  ? 81  GLU C OE1 1 
ATOM   4247 O OE2 . GLU C 1 90  ? 21.647  -55.104  30.327  1.00 61.59  ? 81  GLU C OE2 1 
ATOM   4248 N N   . THR C 1 91  ? 21.702  -61.641  30.692  1.00 70.82  ? 82  THR C N   1 
ATOM   4249 C CA  . THR C 1 91  ? 21.767  -62.993  30.154  1.00 74.15  ? 82  THR C CA  1 
ATOM   4250 C C   . THR C 1 91  ? 21.334  -63.076  28.698  1.00 78.26  ? 82  THR C C   1 
ATOM   4251 O O   . THR C 1 91  ? 20.554  -62.251  28.223  1.00 78.82  ? 82  THR C O   1 
ATOM   4252 C CB  . THR C 1 91  ? 20.891  -63.952  30.963  1.00 75.36  ? 82  THR C CB  1 
ATOM   4253 O OG1 . THR C 1 91  ? 20.173  -64.807  30.061  1.00 81.44  ? 82  THR C OG1 1 
ATOM   4254 C CG2 . THR C 1 91  ? 19.904  -63.166  31.816  1.00 74.43  ? 82  THR C CG2 1 
ATOM   4255 N N   . SER C 1 92  ? 21.837  -64.092  28.003  1.00 78.79  ? 83  SER C N   1 
ATOM   4256 C CA  . SER C 1 92  ? 21.527  -64.289  26.594  1.00 84.17  ? 83  SER C CA  1 
ATOM   4257 C C   . SER C 1 92  ? 20.038  -64.559  26.401  1.00 85.32  ? 83  SER C C   1 
ATOM   4258 O O   . SER C 1 92  ? 19.505  -64.424  25.294  1.00 89.03  ? 83  SER C O   1 
ATOM   4259 C CB  . SER C 1 92  ? 22.349  -65.448  26.017  1.00 87.15  ? 83  SER C CB  1 
ATOM   4260 O OG  . SER C 1 92  ? 21.770  -66.704  26.342  1.00 88.40  ? 83  SER C OG  1 
ATOM   4261 N N   . SER C 1 93  ? 19.379  -64.963  27.479  1.00 82.69  ? 84  SER C N   1 
ATOM   4262 C CA  . SER C 1 93  ? 17.954  -65.254  27.436  1.00 83.48  ? 84  SER C CA  1 
ATOM   4263 C C   . SER C 1 93  ? 17.083  -64.100  27.934  1.00 81.40  ? 84  SER C C   1 
ATOM   4264 O O   . SER C 1 93  ? 15.860  -64.239  28.004  1.00 83.36  ? 84  SER C O   1 
ATOM   4265 C CB  . SER C 1 93  ? 17.641  -66.544  28.206  1.00 87.34  ? 84  SER C CB  1 
ATOM   4266 O OG  . SER C 1 93  ? 18.364  -67.645  27.671  1.00 87.37  ? 84  SER C OG  1 
ATOM   4267 N N   . SER C 1 94  ? 17.684  -62.960  28.276  1.00 78.96  ? 85  SER C N   1 
ATOM   4268 C CA  . SER C 1 94  ? 16.871  -61.918  28.888  1.00 74.48  ? 85  SER C CA  1 
ATOM   4269 C C   . SER C 1 94  ? 16.317  -60.974  27.830  1.00 72.51  ? 85  SER C C   1 
ATOM   4270 O O   . SER C 1 94  ? 16.998  -60.085  27.316  1.00 70.54  ? 85  SER C O   1 
ATOM   4271 C CB  . SER C 1 94  ? 17.675  -61.143  29.932  1.00 71.26  ? 85  SER C CB  1 
ATOM   4272 O OG  . SER C 1 94  ? 18.348  -60.045  29.348  1.00 70.13  ? 85  SER C OG  1 
ATOM   4273 N N   . ASP C 1 95  ? 15.033  -61.170  27.566  1.00 71.45  ? 86  ASP C N   1 
ATOM   4274 C CA  . ASP C 1 95  ? 14.342  -60.512  26.477  1.00 71.86  ? 86  ASP C CA  1 
ATOM   4275 C C   . ASP C 1 95  ? 13.484  -59.342  26.891  1.00 69.44  ? 86  ASP C C   1 
ATOM   4276 O O   . ASP C 1 95  ? 12.866  -58.701  26.031  1.00 70.23  ? 86  ASP C O   1 
ATOM   4277 C CB  . ASP C 1 95  ? 13.441  -61.511  25.763  1.00 76.52  ? 86  ASP C CB  1 
ATOM   4278 C CG  . ASP C 1 95  ? 14.170  -62.309  24.723  1.00 79.40  ? 86  ASP C CG  1 
ATOM   4279 O OD1 . ASP C 1 95  ? 15.415  -62.377  24.807  1.00 81.78  ? 86  ASP C OD1 1 
ATOM   4280 O OD2 . ASP C 1 95  ? 13.497  -62.864  23.822  1.00 79.94  ? 86  ASP C OD2 1 
ATOM   4281 N N   . ASN C 1 96  ? 13.404  -59.049  28.182  1.00 65.25  ? 87  ASN C N   1 
ATOM   4282 C CA  . ASN C 1 96  ? 12.335  -58.146  28.559  1.00 62.59  ? 87  ASN C CA  1 
ATOM   4283 C C   . ASN C 1 96  ? 12.786  -56.703  28.696  1.00 61.40  ? 87  ASN C C   1 
ATOM   4284 O O   . ASN C 1 96  ? 13.372  -56.262  29.689  1.00 60.40  ? 87  ASN C O   1 
ATOM   4285 C CB  . ASN C 1 96  ? 11.597  -58.673  29.780  1.00 63.22  ? 87  ASN C CB  1 
ATOM   4286 C CG  . ASN C 1 96  ? 10.678  -59.814  29.421  1.00 64.96  ? 87  ASN C CG  1 
ATOM   4287 O OD1 . ASN C 1 96  ? 10.823  -60.901  29.955  1.00 64.80  ? 87  ASN C OD1 1 
ATOM   4288 N ND2 . ASN C 1 96  ? 9.716   -59.573  28.545  1.00 66.86  ? 87  ASN C ND2 1 
ATOM   4289 N N   . GLY C 1 97  ? 12.464  -56.002  27.616  1.00 60.63  ? 88  GLY C N   1 
ATOM   4290 C CA  . GLY C 1 97  ? 12.820  -54.631  27.321  1.00 59.33  ? 88  GLY C CA  1 
ATOM   4291 C C   . GLY C 1 97  ? 11.656  -53.679  27.378  1.00 56.54  ? 88  GLY C C   1 
ATOM   4292 O O   . GLY C 1 97  ? 10.831  -53.710  28.295  1.00 54.40  ? 88  GLY C O   1 
ATOM   4293 N N   . THR C 1 98  ? 11.647  -52.778  26.397  1.00 54.95  ? 89  THR C N   1 
ATOM   4294 C CA  . THR C 1 98  ? 10.502  -51.932  26.180  1.00 47.99  ? 89  THR C CA  1 
ATOM   4295 C C   . THR C 1 98  ? 9.459   -52.793  25.492  1.00 48.38  ? 89  THR C C   1 
ATOM   4296 O O   . THR C 1 98  ? 9.616   -53.182  24.330  1.00 47.36  ? 89  THR C O   1 
ATOM   4297 C CB  . THR C 1 98  ? 10.877  -50.819  25.206  1.00 47.60  ? 89  THR C CB  1 
ATOM   4298 O OG1 . THR C 1 98  ? 11.221  -51.394  23.929  1.00 47.56  ? 89  THR C OG1 1 
ATOM   4299 C CG2 . THR C 1 98  ? 12.064  -50.036  25.743  1.00 43.62  ? 89  THR C CG2 1 
ATOM   4300 N N   . CYS C 1 99  ? 8.371   -53.048  26.213  1.00 51.21  ? 90  CYS C N   1 
ATOM   4301 C CA  . CYS C 1 99  ? 7.277   -53.863  25.704  1.00 50.64  ? 90  CYS C CA  1 
ATOM   4302 C C   . CYS C 1 99  ? 6.307   -53.047  24.869  1.00 49.41  ? 90  CYS C C   1 
ATOM   4303 O O   . CYS C 1 99  ? 5.628   -53.596  24.009  1.00 52.23  ? 90  CYS C O   1 
ATOM   4304 C CB  . CYS C 1 99  ? 6.557   -54.607  26.832  1.00 52.73  ? 90  CYS C CB  1 
ATOM   4305 S SG  . CYS C 1 99  ? 6.106   -53.595  28.270  1.00 60.80  ? 90  CYS C SG  1 
ATOM   4306 N N   . TYR C 1 100 ? 6.262   -51.737  25.093  1.00 45.84  ? 91  TYR C N   1 
ATOM   4307 C CA  . TYR C 1 100 ? 5.645   -50.862  24.116  1.00 43.95  ? 91  TYR C CA  1 
ATOM   4308 C C   . TYR C 1 100 ? 6.786   -50.420  23.214  1.00 42.46  ? 91  TYR C C   1 
ATOM   4309 O O   . TYR C 1 100 ? 7.769   -49.857  23.689  1.00 43.57  ? 91  TYR C O   1 
ATOM   4310 C CB  . TYR C 1 100 ? 4.941   -49.653  24.749  1.00 42.61  ? 91  TYR C CB  1 
ATOM   4311 C CG  . TYR C 1 100 ? 4.058   -48.932  23.747  1.00 46.82  ? 91  TYR C CG  1 
ATOM   4312 C CD1 . TYR C 1 100 ? 4.611   -48.114  22.765  1.00 44.11  ? 91  TYR C CD1 1 
ATOM   4313 C CD2 . TYR C 1 100 ? 2.679   -49.108  23.747  1.00 47.57  ? 91  TYR C CD2 1 
ATOM   4314 C CE1 . TYR C 1 100 ? 3.814   -47.471  21.832  1.00 44.51  ? 91  TYR C CE1 1 
ATOM   4315 C CE2 . TYR C 1 100 ? 1.877   -48.469  22.814  1.00 44.39  ? 91  TYR C CE2 1 
ATOM   4316 C CZ  . TYR C 1 100 ? 2.446   -47.650  21.863  1.00 46.17  ? 91  TYR C CZ  1 
ATOM   4317 O OH  . TYR C 1 100 ? 1.635   -47.019  20.935  1.00 49.36  ? 91  TYR C OH  1 
ATOM   4318 N N   . PRO C 1 101 ? 6.670   -50.699  21.914  1.00 40.83  ? 92  PRO C N   1 
ATOM   4319 C CA  . PRO C 1 101 ? 7.772   -50.470  20.973  1.00 38.54  ? 92  PRO C CA  1 
ATOM   4320 C C   . PRO C 1 101 ? 8.182   -49.009  20.853  1.00 38.23  ? 92  PRO C C   1 
ATOM   4321 O O   . PRO C 1 101 ? 7.347   -48.112  20.924  1.00 37.25  ? 92  PRO C O   1 
ATOM   4322 C CB  . PRO C 1 101 ? 7.212   -50.966  19.643  1.00 35.94  ? 92  PRO C CB  1 
ATOM   4323 C CG  . PRO C 1 101 ? 5.726   -50.961  19.813  1.00 41.30  ? 92  PRO C CG  1 
ATOM   4324 C CD  . PRO C 1 101 ? 5.459   -51.222  21.257  1.00 40.91  ? 92  PRO C CD  1 
ATOM   4325 N N   . GLY C 1 102 ? 9.478   -48.790  20.673  1.00 36.46  ? 93  GLY C N   1 
ATOM   4326 C CA  . GLY C 1 102 ? 10.028  -47.462  20.576  1.00 35.13  ? 93  GLY C CA  1 
ATOM   4327 C C   . GLY C 1 102 ? 11.520  -47.523  20.809  1.00 39.90  ? 93  GLY C C   1 
ATOM   4328 O O   . GLY C 1 102 ? 12.058  -48.545  21.244  1.00 40.79  ? 93  GLY C O   1 
ATOM   4329 N N   . ASP C 1 103 ? 12.205  -46.423  20.526  1.00 41.51  ? 94  ASP C N   1 
ATOM   4330 C CA  . ASP C 1 103 ? 13.638  -46.382  20.755  1.00 43.71  ? 94  ASP C CA  1 
ATOM   4331 C C   . ASP C 1 103 ? 13.949  -45.791  22.132  1.00 44.34  ? 94  ASP C C   1 
ATOM   4332 O O   . ASP C 1 103 ? 13.362  -44.786  22.556  1.00 41.34  ? 94  ASP C O   1 
ATOM   4333 C CB  . ASP C 1 103 ? 14.354  -45.598  19.655  1.00 41.28  ? 94  ASP C CB  1 
ATOM   4334 C CG  . ASP C 1 103 ? 14.153  -46.202  18.278  1.00 46.07  ? 94  ASP C CG  1 
ATOM   4335 O OD1 . ASP C 1 103 ? 14.172  -47.449  18.148  1.00 46.72  ? 94  ASP C OD1 1 
ATOM   4336 O OD2 . ASP C 1 103 ? 13.964  -45.417  17.319  1.00 46.42  ? 94  ASP C OD2 1 
ATOM   4337 N N   . PHE C 1 104 ? 14.872  -46.441  22.828  1.00 42.56  ? 95  PHE C N   1 
ATOM   4338 C CA  . PHE C 1 104 ? 15.337  -45.955  24.104  1.00 43.02  ? 95  PHE C CA  1 
ATOM   4339 C C   . PHE C 1 104 ? 16.557  -45.064  23.877  1.00 43.79  ? 95  PHE C C   1 
ATOM   4340 O O   . PHE C 1 104 ? 17.615  -45.532  23.452  1.00 43.57  ? 95  PHE C O   1 
ATOM   4341 C CB  . PHE C 1 104 ? 15.722  -47.140  24.956  1.00 44.54  ? 95  PHE C CB  1 
ATOM   4342 C CG  . PHE C 1 104 ? 15.932  -46.803  26.391  1.00 46.37  ? 95  PHE C CG  1 
ATOM   4343 C CD1 . PHE C 1 104 ? 16.828  -45.816  26.758  1.00 47.57  ? 95  PHE C CD1 1 
ATOM   4344 C CD2 . PHE C 1 104 ? 15.239  -47.483  27.382  1.00 45.53  ? 95  PHE C CD2 1 
ATOM   4345 C CE1 . PHE C 1 104 ? 17.021  -45.508  28.089  1.00 45.71  ? 95  PHE C CE1 1 
ATOM   4346 C CE2 . PHE C 1 104 ? 15.430  -47.187  28.708  1.00 42.26  ? 95  PHE C CE2 1 
ATOM   4347 C CZ  . PHE C 1 104 ? 16.323  -46.196  29.064  1.00 43.66  ? 95  PHE C CZ  1 
ATOM   4348 N N   . ILE C 1 105 ? 16.404  -43.780  24.172  1.00 42.74  ? 96  ILE C N   1 
ATOM   4349 C CA  . ILE C 1 105 ? 17.408  -42.783  23.813  1.00 41.58  ? 96  ILE C CA  1 
ATOM   4350 C C   . ILE C 1 105 ? 18.576  -42.735  24.800  1.00 41.84  ? 96  ILE C C   1 
ATOM   4351 O O   . ILE C 1 105 ? 18.369  -42.824  26.011  1.00 43.35  ? 96  ILE C O   1 
ATOM   4352 C CB  . ILE C 1 105 ? 16.746  -41.406  23.710  1.00 43.01  ? 96  ILE C CB  1 
ATOM   4353 C CG1 . ILE C 1 105 ? 15.526  -41.490  22.788  1.00 42.18  ? 96  ILE C CG1 1 
ATOM   4354 C CG2 . ILE C 1 105 ? 17.738  -40.351  23.265  1.00 43.28  ? 96  ILE C CG2 1 
ATOM   4355 C CD1 . ILE C 1 105 ? 15.794  -42.173  21.489  1.00 39.02  ? 96  ILE C CD1 1 
ATOM   4356 N N   . ASP C 1 106 ? 19.800  -42.610  24.285  1.00 41.33  ? 97  ASP C N   1 
ATOM   4357 C CA  . ASP C 1 106 ? 21.007  -42.597  25.132  1.00 42.77  ? 97  ASP C CA  1 
ATOM   4358 C C   . ASP C 1 106 ? 21.157  -43.854  25.980  1.00 45.45  ? 97  ASP C C   1 
ATOM   4359 O O   . ASP C 1 106 ? 21.546  -43.794  27.147  1.00 45.67  ? 97  ASP C O   1 
ATOM   4360 C CB  . ASP C 1 106 ? 20.974  -41.410  26.072  1.00 44.39  ? 97  ASP C CB  1 
ATOM   4361 C CG  . ASP C 1 106 ? 21.017  -40.116  25.350  1.00 45.85  ? 97  ASP C CG  1 
ATOM   4362 O OD1 . ASP C 1 106 ? 21.931  -39.955  24.519  1.00 47.41  ? 97  ASP C OD1 1 
ATOM   4363 O OD2 . ASP C 1 106 ? 20.153  -39.254  25.623  1.00 49.08  ? 97  ASP C OD2 1 
ATOM   4364 N N   . TYR C 1 107 ? 20.862  -44.998  25.395  1.00 42.96  ? 98  TYR C N   1 
ATOM   4365 C CA  . TYR C 1 107 ? 20.752  -46.204  26.180  1.00 45.73  ? 98  TYR C CA  1 
ATOM   4366 C C   . TYR C 1 107 ? 22.117  -46.763  26.537  1.00 47.11  ? 98  TYR C C   1 
ATOM   4367 O O   . TYR C 1 107 ? 22.308  -47.326  27.611  1.00 48.44  ? 98  TYR C O   1 
ATOM   4368 C CB  . TYR C 1 107 ? 19.925  -47.218  25.404  1.00 46.47  ? 98  TYR C CB  1 
ATOM   4369 C CG  . TYR C 1 107 ? 19.749  -48.564  26.065  1.00 47.98  ? 98  TYR C CG  1 
ATOM   4370 C CD1 . TYR C 1 107 ? 19.508  -48.684  27.431  1.00 45.56  ? 98  TYR C CD1 1 
ATOM   4371 C CD2 . TYR C 1 107 ? 19.790  -49.723  25.307  1.00 47.82  ? 98  TYR C CD2 1 
ATOM   4372 C CE1 . TYR C 1 107 ? 19.331  -49.940  28.017  1.00 44.12  ? 98  TYR C CE1 1 
ATOM   4373 C CE2 . TYR C 1 107 ? 19.618  -50.970  25.880  1.00 47.79  ? 98  TYR C CE2 1 
ATOM   4374 C CZ  . TYR C 1 107 ? 19.392  -51.078  27.227  1.00 46.69  ? 98  TYR C CZ  1 
ATOM   4375 O OH  . TYR C 1 107 ? 19.224  -52.339  27.745  1.00 49.37  ? 98  TYR C OH  1 
ATOM   4376 N N   . GLU C 1 108 ? 23.066  -46.615  25.626  1.00 49.24  ? 99  GLU C N   1 
ATOM   4377 C CA  . GLU C 1 108 ? 24.411  -47.090  25.875  1.00 48.85  ? 99  GLU C CA  1 
ATOM   4378 C C   . GLU C 1 108 ? 24.986  -46.249  27.000  1.00 48.54  ? 99  GLU C C   1 
ATOM   4379 O O   . GLU C 1 108 ? 25.677  -46.755  27.878  1.00 51.89  ? 99  GLU C O   1 
ATOM   4380 C CB  . GLU C 1 108 ? 25.265  -46.965  24.606  1.00 51.30  ? 99  GLU C CB  1 
ATOM   4381 C CG  . GLU C 1 108 ? 26.493  -47.880  24.581  1.00 56.81  ? 99  GLU C CG  1 
ATOM   4382 C CD  . GLU C 1 108 ? 26.122  -49.355  24.396  1.00 64.20  ? 99  GLU C CD  1 
ATOM   4383 O OE1 . GLU C 1 108 ? 24.917  -49.659  24.187  1.00 54.26  ? 99  GLU C OE1 1 
ATOM   4384 O OE2 . GLU C 1 108 ? 27.042  -50.208  24.457  1.00 70.05  ? 99  GLU C OE2 1 
ATOM   4385 N N   . GLU C 1 109 ? 24.681  -44.957  26.978  1.00 44.79  ? 100 GLU C N   1 
ATOM   4386 C CA  . GLU C 1 109 ? 25.208  -44.053  27.977  1.00 45.68  ? 100 GLU C CA  1 
ATOM   4387 C C   . GLU C 1 109 ? 24.713  -44.469  29.339  1.00 54.04  ? 100 GLU C C   1 
ATOM   4388 O O   . GLU C 1 109 ? 25.492  -44.659  30.270  1.00 57.90  ? 100 GLU C O   1 
ATOM   4389 C CB  . GLU C 1 109 ? 24.753  -42.624  27.736  1.00 42.73  ? 100 GLU C CB  1 
ATOM   4390 C CG  . GLU C 1 109 ? 25.009  -41.761  28.965  1.00 48.00  ? 100 GLU C CG  1 
ATOM   4391 C CD  . GLU C 1 109 ? 24.968  -40.276  28.684  1.00 49.80  ? 100 GLU C CD  1 
ATOM   4392 O OE1 . GLU C 1 109 ? 24.392  -39.879  27.657  1.00 50.94  ? 100 GLU C OE1 1 
ATOM   4393 O OE2 . GLU C 1 109 ? 25.505  -39.500  29.501  1.00 54.86  ? 100 GLU C OE2 1 
ATOM   4394 N N   . LEU C 1 110 ? 23.396  -44.571  29.453  1.00 50.65  ? 101 LEU C N   1 
ATOM   4395 C CA  . LEU C 1 110 ? 22.776  -44.979  30.686  1.00 49.41  ? 101 LEU C CA  1 
ATOM   4396 C C   . LEU C 1 110 ? 23.406  -46.278  31.169  1.00 53.46  ? 101 LEU C C   1 
ATOM   4397 O O   . LEU C 1 110 ? 23.861  -46.368  32.302  1.00 54.63  ? 101 LEU C O   1 
ATOM   4398 C CB  . LEU C 1 110 ? 21.285  -45.172  30.464  1.00 49.84  ? 101 LEU C CB  1 
ATOM   4399 C CG  . LEU C 1 110 ? 20.530  -45.591  31.721  1.00 49.24  ? 101 LEU C CG  1 
ATOM   4400 C CD1 . LEU C 1 110 ? 20.537  -44.433  32.684  1.00 52.88  ? 101 LEU C CD1 1 
ATOM   4401 C CD2 . LEU C 1 110 ? 19.117  -45.988  31.385  1.00 45.65  ? 101 LEU C CD2 1 
ATOM   4402 N N   . ARG C 1 111 ? 23.461  -47.273  30.295  1.00 51.62  ? 102 ARG C N   1 
ATOM   4403 C CA  . ARG C 1 111 ? 24.029  -48.559  30.663  1.00 53.16  ? 102 ARG C CA  1 
ATOM   4404 C C   . ARG C 1 111 ? 25.362  -48.386  31.367  1.00 57.09  ? 102 ARG C C   1 
ATOM   4405 O O   . ARG C 1 111 ? 25.683  -49.117  32.297  1.00 57.36  ? 102 ARG C O   1 
ATOM   4406 C CB  . ARG C 1 111 ? 24.222  -49.423  29.422  1.00 54.24  ? 102 ARG C CB  1 
ATOM   4407 C CG  . ARG C 1 111 ? 22.966  -50.157  28.992  1.00 51.19  ? 102 ARG C CG  1 
ATOM   4408 C CD  . ARG C 1 111 ? 23.142  -50.807  27.642  1.00 48.83  ? 102 ARG C CD  1 
ATOM   4409 N NE  . ARG C 1 111 ? 23.971  -52.008  27.695  1.00 53.40  ? 102 ARG C NE  1 
ATOM   4410 C CZ  . ARG C 1 111 ? 23.501  -53.247  27.856  1.00 53.71  ? 102 ARG C CZ  1 
ATOM   4411 N NH1 . ARG C 1 111 ? 22.197  -53.470  27.994  1.00 45.93  ? 102 ARG C NH1 1 
ATOM   4412 N NH2 . ARG C 1 111 ? 24.347  -54.273  27.882  1.00 57.57  ? 102 ARG C NH2 1 
ATOM   4413 N N   . GLU C 1 112 ? 26.146  -47.427  30.899  1.00 58.69  ? 103 GLU C N   1 
ATOM   4414 C CA  . GLU C 1 112 ? 27.422  -47.122  31.525  1.00 62.67  ? 103 GLU C CA  1 
ATOM   4415 C C   . GLU C 1 112 ? 27.240  -46.482  32.903  1.00 65.46  ? 103 GLU C C   1 
ATOM   4416 O O   . GLU C 1 112 ? 27.988  -46.777  33.833  1.00 68.42  ? 103 GLU C O   1 
ATOM   4417 C CB  . GLU C 1 112 ? 28.253  -46.200  30.625  1.00 69.45  ? 103 GLU C CB  1 
ATOM   4418 C CG  . GLU C 1 112 ? 29.603  -45.791  31.219  1.00 78.48  ? 103 GLU C CG  1 
ATOM   4419 C CD  . GLU C 1 112 ? 30.604  -46.948  31.292  1.00 86.68  ? 103 GLU C CD  1 
ATOM   4420 O OE1 . GLU C 1 112 ? 31.702  -46.745  31.869  1.00 87.04  ? 103 GLU C OE1 1 
ATOM   4421 O OE2 . GLU C 1 112 ? 30.299  -48.050  30.766  1.00 85.47  ? 103 GLU C OE2 1 
ATOM   4422 N N   . GLN C 1 113 ? 26.254  -45.603  33.038  1.00 62.29  ? 104 GLN C N   1 
ATOM   4423 C CA  . GLN C 1 113 ? 26.035  -44.939  34.316  1.00 64.48  ? 104 GLN C CA  1 
ATOM   4424 C C   . GLN C 1 113 ? 25.764  -45.930  35.438  1.00 64.21  ? 104 GLN C C   1 
ATOM   4425 O O   . GLN C 1 113 ? 26.251  -45.763  36.552  1.00 66.44  ? 104 GLN C O   1 
ATOM   4426 C CB  . GLN C 1 113 ? 24.865  -43.965  34.229  1.00 63.08  ? 104 GLN C CB  1 
ATOM   4427 C CG  . GLN C 1 113 ? 25.130  -42.766  33.359  1.00 65.35  ? 104 GLN C CG  1 
ATOM   4428 C CD  . GLN C 1 113 ? 26.301  -41.946  33.856  1.00 72.50  ? 104 GLN C CD  1 
ATOM   4429 O OE1 . GLN C 1 113 ? 26.135  -41.022  34.659  1.00 74.25  ? 104 GLN C OE1 1 
ATOM   4430 N NE2 . GLN C 1 113 ? 27.499  -42.279  33.377  1.00 72.78  ? 104 GLN C NE2 1 
ATOM   4431 N N   . LEU C 1 114 ? 24.981  -46.959  35.138  1.00 61.18  ? 105 LEU C N   1 
ATOM   4432 C CA  . LEU C 1 114 ? 24.461  -47.838  36.173  1.00 60.86  ? 105 LEU C CA  1 
ATOM   4433 C C   . LEU C 1 114 ? 25.300  -49.077  36.436  1.00 64.03  ? 105 LEU C C   1 
ATOM   4434 O O   . LEU C 1 114 ? 24.950  -49.881  37.288  1.00 68.00  ? 105 LEU C O   1 
ATOM   4435 C CB  . LEU C 1 114 ? 23.040  -48.270  35.822  1.00 58.08  ? 105 LEU C CB  1 
ATOM   4436 C CG  . LEU C 1 114 ? 22.030  -47.140  35.657  1.00 56.66  ? 105 LEU C CG  1 
ATOM   4437 C CD1 . LEU C 1 114 ? 20.630  -47.708  35.592  1.00 54.27  ? 105 LEU C CD1 1 
ATOM   4438 C CD2 . LEU C 1 114 ? 22.149  -46.173  36.804  1.00 60.84  ? 105 LEU C CD2 1 
ATOM   4439 N N   . SER C 1 115 ? 26.393  -49.251  35.707  1.00 64.93  ? 106 SER C N   1 
ATOM   4440 C CA  . SER C 1 115 ? 27.193  -50.464  35.850  1.00 67.28  ? 106 SER C CA  1 
ATOM   4441 C C   . SER C 1 115 ? 27.642  -50.719  37.292  1.00 66.33  ? 106 SER C C   1 
ATOM   4442 O O   . SER C 1 115 ? 27.663  -51.862  37.748  1.00 65.95  ? 106 SER C O   1 
ATOM   4443 C CB  . SER C 1 115 ? 28.397  -50.405  34.914  1.00 65.88  ? 106 SER C CB  1 
ATOM   4444 O OG  . SER C 1 115 ? 29.116  -49.200  35.104  1.00 71.23  ? 106 SER C OG  1 
ATOM   4445 N N   . SER C 1 116 ? 27.992  -49.654  38.005  1.00 65.57  ? 107 SER C N   1 
ATOM   4446 C CA  . SER C 1 116 ? 28.429  -49.786  39.385  1.00 70.48  ? 107 SER C CA  1 
ATOM   4447 C C   . SER C 1 116 ? 27.918  -48.638  40.251  1.00 71.99  ? 107 SER C C   1 
ATOM   4448 O O   . SER C 1 116 ? 28.041  -47.470  39.878  1.00 70.70  ? 107 SER C O   1 
ATOM   4449 C CB  . SER C 1 116 ? 29.958  -49.853  39.441  1.00 75.22  ? 107 SER C CB  1 
ATOM   4450 O OG  . SER C 1 116 ? 30.414  -50.296  40.710  1.00 74.98  ? 107 SER C OG  1 
ATOM   4451 N N   . VAL C 1 117 ? 27.347  -48.974  41.406  1.00 73.85  ? 108 VAL C N   1 
ATOM   4452 C CA  . VAL C 1 117 ? 26.900  -47.962  42.363  1.00 74.70  ? 108 VAL C CA  1 
ATOM   4453 C C   . VAL C 1 117 ? 27.171  -48.387  43.805  1.00 73.56  ? 108 VAL C C   1 
ATOM   4454 O O   . VAL C 1 117 ? 27.167  -49.582  44.125  1.00 73.47  ? 108 VAL C O   1 
ATOM   4455 C CB  . VAL C 1 117 ? 25.382  -47.654  42.229  1.00 73.19  ? 108 VAL C CB  1 
ATOM   4456 C CG1 . VAL C 1 117 ? 25.016  -47.337  40.786  1.00 67.78  ? 108 VAL C CG1 1 
ATOM   4457 C CG2 . VAL C 1 117 ? 24.554  -48.814  42.742  1.00 72.04  ? 108 VAL C CG2 1 
ATOM   4458 N N   . SER C 1 118 ? 27.408  -47.398  44.666  1.00 74.60  ? 109 SER C N   1 
ATOM   4459 C CA  . SER C 1 118 ? 27.457  -47.610  46.112  1.00 74.09  ? 109 SER C CA  1 
ATOM   4460 C C   . SER C 1 118 ? 26.044  -47.603  46.686  1.00 73.36  ? 109 SER C C   1 
ATOM   4461 O O   . SER C 1 118 ? 25.557  -48.623  47.160  1.00 74.06  ? 109 SER C O   1 
ATOM   4462 C CB  . SER C 1 118 ? 28.301  -46.530  46.795  1.00 75.58  ? 109 SER C CB  1 
ATOM   4463 O OG  . SER C 1 118 ? 28.402  -45.367  45.989  1.00 76.96  ? 109 SER C OG  1 
ATOM   4464 N N   . SER C 1 119 ? 25.387  -46.446  46.630  1.00 72.98  ? 110 SER C N   1 
ATOM   4465 C CA  . SER C 1 119 ? 23.998  -46.315  47.074  1.00 74.70  ? 110 SER C CA  1 
ATOM   4466 C C   . SER C 1 119 ? 23.058  -46.023  45.910  1.00 73.17  ? 110 SER C C   1 
ATOM   4467 O O   . SER C 1 119 ? 23.349  -45.187  45.047  1.00 74.05  ? 110 SER C O   1 
ATOM   4468 C CB  . SER C 1 119 ? 23.848  -45.200  48.110  1.00 75.40  ? 110 SER C CB  1 
ATOM   4469 O OG  . SER C 1 119 ? 23.226  -44.058  47.534  1.00 71.47  ? 110 SER C OG  1 
ATOM   4470 N N   . PHE C 1 120 ? 21.931  -46.722  45.888  1.00 70.70  ? 111 PHE C N   1 
ATOM   4471 C CA  . PHE C 1 120 ? 20.956  -46.552  44.823  1.00 69.06  ? 111 PHE C CA  1 
ATOM   4472 C C   . PHE C 1 120 ? 19.551  -46.567  45.418  1.00 65.55  ? 111 PHE C C   1 
ATOM   4473 O O   . PHE C 1 120 ? 19.128  -47.592  45.950  1.00 67.72  ? 111 PHE C O   1 
ATOM   4474 C CB  . PHE C 1 120 ? 21.133  -47.697  43.819  1.00 68.98  ? 111 PHE C CB  1 
ATOM   4475 C CG  . PHE C 1 120 ? 20.289  -47.568  42.597  1.00 67.98  ? 111 PHE C CG  1 
ATOM   4476 C CD1 . PHE C 1 120 ? 20.431  -46.477  41.758  1.00 69.86  ? 111 PHE C CD1 1 
ATOM   4477 C CD2 . PHE C 1 120 ? 19.366  -48.546  42.266  1.00 69.63  ? 111 PHE C CD2 1 
ATOM   4478 C CE1 . PHE C 1 120 ? 19.648  -46.347  40.621  1.00 63.32  ? 111 PHE C CE1 1 
ATOM   4479 C CE2 . PHE C 1 120 ? 18.579  -48.421  41.127  1.00 63.52  ? 111 PHE C CE2 1 
ATOM   4480 C CZ  . PHE C 1 120 ? 18.724  -47.319  40.309  1.00 59.20  ? 111 PHE C CZ  1 
ATOM   4481 N N   . GLU C 1 121 ? 18.807  -45.466  45.300  1.00 61.77  ? 112 GLU C N   1 
ATOM   4482 C CA  . GLU C 1 121 ? 17.491  -45.390  45.960  1.00 58.52  ? 112 GLU C CA  1 
ATOM   4483 C C   . GLU C 1 121 ? 16.300  -45.050  45.068  1.00 55.57  ? 112 GLU C C   1 
ATOM   4484 O O   . GLU C 1 121 ? 16.153  -43.922  44.605  1.00 56.76  ? 112 GLU C O   1 
ATOM   4485 C CB  . GLU C 1 121 ? 17.521  -44.388  47.127  1.00 61.88  ? 112 GLU C CB  1 
ATOM   4486 C CG  . GLU C 1 121 ? 16.172  -44.212  47.846  1.00 62.67  ? 112 GLU C CG  1 
ATOM   4487 C CD  . GLU C 1 121 ? 16.211  -43.207  49.009  1.00 67.09  ? 112 GLU C CD  1 
ATOM   4488 O OE1 . GLU C 1 121 ? 17.280  -43.056  49.663  1.00 60.23  ? 112 GLU C OE1 1 
ATOM   4489 O OE2 . GLU C 1 121 ? 15.153  -42.573  49.265  1.00 63.73  ? 112 GLU C OE2 1 
ATOM   4490 N N   . ARG C 1 122 ? 15.413  -46.017  44.886  1.00 54.35  ? 113 ARG C N   1 
ATOM   4491 C CA  . ARG C 1 122 ? 14.148  -45.768  44.206  1.00 55.23  ? 113 ARG C CA  1 
ATOM   4492 C C   . ARG C 1 122 ? 13.199  -44.885  45.031  1.00 53.98  ? 113 ARG C C   1 
ATOM   4493 O O   . ARG C 1 122 ? 13.250  -44.875  46.256  1.00 57.21  ? 113 ARG C O   1 
ATOM   4494 C CB  . ARG C 1 122 ? 13.469  -47.096  43.896  1.00 54.28  ? 113 ARG C CB  1 
ATOM   4495 C CG  . ARG C 1 122 ? 12.012  -46.951  43.522  1.00 58.81  ? 113 ARG C CG  1 
ATOM   4496 C CD  . ARG C 1 122 ? 11.243  -48.161  43.997  1.00 63.01  ? 113 ARG C CD  1 
ATOM   4497 N NE  . ARG C 1 122 ? 10.674  -48.893  42.875  1.00 67.31  ? 113 ARG C NE  1 
ATOM   4498 C CZ  . ARG C 1 122 ? 9.386   -49.205  42.775  1.00 68.64  ? 113 ARG C CZ  1 
ATOM   4499 N NH1 . ARG C 1 122 ? 8.537   -48.860  43.739  1.00 65.36  ? 113 ARG C NH1 1 
ATOM   4500 N NH2 . ARG C 1 122 ? 8.944   -49.869  41.716  1.00 66.27  ? 113 ARG C NH2 1 
ATOM   4501 N N   . PHE C 1 123 ? 12.300  -44.175  44.367  1.00 53.14  ? 114 PHE C N   1 
ATOM   4502 C CA  . PHE C 1 123 ? 11.333  -43.367  45.098  1.00 53.69  ? 114 PHE C CA  1 
ATOM   4503 C C   . PHE C 1 123 ? 10.316  -42.700  44.186  1.00 54.92  ? 114 PHE C C   1 
ATOM   4504 O O   . PHE C 1 123 ? 10.555  -42.539  42.991  1.00 56.77  ? 114 PHE C O   1 
ATOM   4505 C CB  . PHE C 1 123 ? 12.053  -42.304  45.917  1.00 51.76  ? 114 PHE C CB  1 
ATOM   4506 C CG  . PHE C 1 123 ? 12.587  -41.165  45.112  1.00 50.52  ? 114 PHE C CG  1 
ATOM   4507 C CD1 . PHE C 1 123 ? 13.842  -41.241  44.528  1.00 51.20  ? 114 PHE C CD1 1 
ATOM   4508 C CD2 . PHE C 1 123 ? 11.854  -39.996  44.976  1.00 51.27  ? 114 PHE C CD2 1 
ATOM   4509 C CE1 . PHE C 1 123 ? 14.350  -40.174  43.805  1.00 52.14  ? 114 PHE C CE1 1 
ATOM   4510 C CE2 . PHE C 1 123 ? 12.352  -38.926  44.250  1.00 53.43  ? 114 PHE C CE2 1 
ATOM   4511 C CZ  . PHE C 1 123 ? 13.605  -39.014  43.666  1.00 51.41  ? 114 PHE C CZ  1 
ATOM   4512 N N   . GLU C 1 124 ? 9.187   -42.289  44.752  1.00 52.04  ? 115 GLU C N   1 
ATOM   4513 C CA  . GLU C 1 124 ? 8.122   -41.740  43.937  1.00 54.00  ? 115 GLU C CA  1 
ATOM   4514 C C   . GLU C 1 124 ? 8.284   -40.234  43.879  1.00 54.00  ? 115 GLU C C   1 
ATOM   4515 O O   . GLU C 1 124 ? 8.001   -39.529  44.838  1.00 56.56  ? 115 GLU C O   1 
ATOM   4516 C CB  . GLU C 1 124 ? 6.772   -42.116  44.550  1.00 54.77  ? 115 GLU C CB  1 
ATOM   4517 C CG  . GLU C 1 124 ? 5.544   -41.719  43.758  1.00 54.24  ? 115 GLU C CG  1 
ATOM   4518 C CD  . GLU C 1 124 ? 4.358   -42.612  44.090  1.00 59.84  ? 115 GLU C CD  1 
ATOM   4519 O OE1 . GLU C 1 124 ? 3.310   -42.097  44.541  1.00 63.51  ? 115 GLU C OE1 1 
ATOM   4520 O OE2 . GLU C 1 124 ? 4.476   -43.843  43.905  1.00 60.17  ? 115 GLU C OE2 1 
ATOM   4521 N N   . ILE C 1 125 ? 8.711   -39.742  42.728  1.00 50.82  ? 116 ILE C N   1 
ATOM   4522 C CA  . ILE C 1 125 ? 8.978   -38.328  42.563  1.00 53.94  ? 116 ILE C CA  1 
ATOM   4523 C C   . ILE C 1 125 ? 7.668   -37.569  42.350  1.00 57.70  ? 116 ILE C C   1 
ATOM   4524 O O   . ILE C 1 125 ? 7.523   -36.413  42.759  1.00 57.49  ? 116 ILE C O   1 
ATOM   4525 C CB  . ILE C 1 125 ? 9.933   -38.097  41.388  1.00 56.32  ? 116 ILE C CB  1 
ATOM   4526 C CG1 . ILE C 1 125 ? 9.965   -36.619  41.003  1.00 54.99  ? 116 ILE C CG1 1 
ATOM   4527 C CG2 . ILE C 1 125 ? 9.548   -38.979  40.190  1.00 50.31  ? 116 ILE C CG2 1 
ATOM   4528 C CD1 . ILE C 1 125 ? 11.075  -36.303  40.053  1.00 53.82  ? 116 ILE C CD1 1 
ATOM   4529 N N   . PHE C 1 126 ? 6.717   -38.237  41.711  1.00 55.00  ? 117 PHE C N   1 
ATOM   4530 C CA  . PHE C 1 126 ? 5.388   -37.690  41.519  1.00 56.69  ? 117 PHE C CA  1 
ATOM   4531 C C   . PHE C 1 126 ? 4.339   -38.696  41.953  1.00 56.60  ? 117 PHE C C   1 
ATOM   4532 O O   . PHE C 1 126 ? 3.947   -39.555  41.162  1.00 55.79  ? 117 PHE C O   1 
ATOM   4533 C CB  . PHE C 1 126 ? 5.182   -37.317  40.064  1.00 54.84  ? 117 PHE C CB  1 
ATOM   4534 C CG  . PHE C 1 126 ? 6.143   -36.282  39.571  1.00 56.41  ? 117 PHE C CG  1 
ATOM   4535 C CD1 . PHE C 1 126 ? 6.176   -35.020  40.149  1.00 57.68  ? 117 PHE C CD1 1 
ATOM   4536 C CD2 . PHE C 1 126 ? 7.001   -36.561  38.515  1.00 54.17  ? 117 PHE C CD2 1 
ATOM   4537 C CE1 . PHE C 1 126 ? 7.060   -34.056  39.689  1.00 60.97  ? 117 PHE C CE1 1 
ATOM   4538 C CE2 . PHE C 1 126 ? 7.890   -35.610  38.049  1.00 51.45  ? 117 PHE C CE2 1 
ATOM   4539 C CZ  . PHE C 1 126 ? 7.923   -34.355  38.631  1.00 58.80  ? 117 PHE C CZ  1 
ATOM   4540 N N   . PRO C 1 127 ? 3.889   -38.604  43.215  1.00 56.07  ? 118 PRO C N   1 
ATOM   4541 C CA  . PRO C 1 127 ? 2.896   -39.574  43.670  1.00 56.69  ? 118 PRO C CA  1 
ATOM   4542 C C   . PRO C 1 127 ? 1.761   -39.685  42.666  1.00 55.82  ? 118 PRO C C   1 
ATOM   4543 O O   . PRO C 1 127 ? 1.200   -38.690  42.178  1.00 52.95  ? 118 PRO C O   1 
ATOM   4544 C CB  . PRO C 1 127 ? 2.410   -38.981  44.994  1.00 56.34  ? 118 PRO C CB  1 
ATOM   4545 C CG  . PRO C 1 127 ? 3.596   -38.234  45.503  1.00 56.94  ? 118 PRO C CG  1 
ATOM   4546 C CD  . PRO C 1 127 ? 4.278   -37.667  44.280  1.00 55.25  ? 118 PRO C CD  1 
ATOM   4547 N N   . LYS C 1 128 ? 1.449   -40.930  42.339  1.00 54.25  ? 119 LYS C N   1 
ATOM   4548 C CA  . LYS C 1 128 ? 0.400   -41.220  41.392  1.00 52.31  ? 119 LYS C CA  1 
ATOM   4549 C C   . LYS C 1 128 ? -0.887  -40.483  41.754  1.00 54.47  ? 119 LYS C C   1 
ATOM   4550 O O   . LYS C 1 128 ? -1.546  -39.907  40.882  1.00 51.68  ? 119 LYS C O   1 
ATOM   4551 C CB  . LYS C 1 128 ? 0.168   -42.726  41.345  1.00 51.25  ? 119 LYS C CB  1 
ATOM   4552 C CG  . LYS C 1 128 ? -1.036  -43.144  40.535  1.00 52.80  ? 119 LYS C CG  1 
ATOM   4553 C CD  . LYS C 1 128 ? -0.955  -44.610  40.148  1.00 51.73  ? 119 LYS C CD  1 
ATOM   4554 C CE  . LYS C 1 128 ? -2.105  -44.986  39.212  1.00 51.72  ? 119 LYS C CE  1 
ATOM   4555 N NZ  . LYS C 1 128 ? -1.958  -46.368  38.654  1.00 46.88  ? 119 LYS C NZ  1 
ATOM   4556 N N   . THR C 1 129 ? -1.232  -40.485  43.044  1.00 55.19  ? 120 THR C N   1 
ATOM   4557 C CA  . THR C 1 129 ? -2.542  -39.997  43.483  1.00 55.65  ? 120 THR C CA  1 
ATOM   4558 C C   . THR C 1 129 ? -2.688  -38.477  43.439  1.00 54.76  ? 120 THR C C   1 
ATOM   4559 O O   . THR C 1 129 ? -3.663  -37.940  42.912  1.00 55.94  ? 120 THR C O   1 
ATOM   4560 C CB  . THR C 1 129 ? -2.826  -40.435  44.910  1.00 54.51  ? 120 THR C CB  1 
ATOM   4561 O OG1 . THR C 1 129 ? -2.265  -39.475  45.811  1.00 58.64  ? 120 THR C OG1 1 
ATOM   4562 C CG2 . THR C 1 129 ? -2.214  -41.794  45.175  1.00 53.99  ? 120 THR C CG2 1 
ATOM   4563 N N   . SER C 1 130 ? -1.710  -37.794  44.010  1.00 54.72  ? 121 SER C N   1 
ATOM   4564 C CA  . SER C 1 130 ? -1.810  -36.366  44.253  1.00 56.16  ? 121 SER C CA  1 
ATOM   4565 C C   . SER C 1 130 ? -1.354  -35.494  43.105  1.00 54.80  ? 121 SER C C   1 
ATOM   4566 O O   . SER C 1 130 ? -1.683  -34.307  43.063  1.00 54.02  ? 121 SER C O   1 
ATOM   4567 C CB  . SER C 1 130 ? -0.970  -36.032  45.480  1.00 57.97  ? 121 SER C CB  1 
ATOM   4568 O OG  . SER C 1 130 ? 0.240   -36.773  45.458  1.00 56.70  ? 121 SER C OG  1 
ATOM   4569 N N   . SER C 1 131 ? -0.599  -36.089  42.183  1.00 58.56  ? 122 SER C N   1 
ATOM   4570 C CA  . SER C 1 131 ? 0.133   -35.331  41.163  1.00 54.75  ? 122 SER C CA  1 
ATOM   4571 C C   . SER C 1 131 ? -0.665  -34.900  39.931  1.00 52.16  ? 122 SER C C   1 
ATOM   4572 O O   . SER C 1 131 ? -0.391  -33.843  39.366  1.00 53.23  ? 122 SER C O   1 
ATOM   4573 C CB  . SER C 1 131 ? 1.408   -36.075  40.735  1.00 53.60  ? 122 SER C CB  1 
ATOM   4574 O OG  . SER C 1 131 ? 2.303   -36.259  41.825  1.00 53.23  ? 122 SER C OG  1 
ATOM   4575 N N   . TRP C 1 132 ? -1.647  -35.698  39.514  1.00 53.77  ? 123 TRP C N   1 
ATOM   4576 C CA  . TRP C 1 132 ? -2.299  -35.463  38.216  1.00 55.23  ? 123 TRP C CA  1 
ATOM   4577 C C   . TRP C 1 132 ? -3.802  -35.294  38.341  1.00 55.84  ? 123 TRP C C   1 
ATOM   4578 O O   . TRP C 1 132 ? -4.570  -36.064  37.751  1.00 53.45  ? 123 TRP C O   1 
ATOM   4579 C CB  . TRP C 1 132 ? -2.001  -36.625  37.259  1.00 50.96  ? 123 TRP C CB  1 
ATOM   4580 C CG  . TRP C 1 132 ? -0.572  -37.030  37.327  1.00 49.13  ? 123 TRP C CG  1 
ATOM   4581 C CD1 . TRP C 1 132 ? -0.072  -38.210  37.796  1.00 49.32  ? 123 TRP C CD1 1 
ATOM   4582 C CD2 . TRP C 1 132 ? 0.558   -36.233  36.960  1.00 50.47  ? 123 TRP C CD2 1 
ATOM   4583 N NE1 . TRP C 1 132 ? 1.307   -38.204  37.730  1.00 46.84  ? 123 TRP C NE1 1 
ATOM   4584 C CE2 . TRP C 1 132 ? 1.717   -37.002  37.219  1.00 47.94  ? 123 TRP C CE2 1 
ATOM   4585 C CE3 . TRP C 1 132 ? 0.704   -34.946  36.428  1.00 51.31  ? 123 TRP C CE3 1 
ATOM   4586 C CZ2 . TRP C 1 132 ? 2.997   -36.527  36.967  1.00 46.54  ? 123 TRP C CZ2 1 
ATOM   4587 C CZ3 . TRP C 1 132 ? 1.983   -34.475  36.178  1.00 49.48  ? 123 TRP C CZ3 1 
ATOM   4588 C CH2 . TRP C 1 132 ? 3.110   -35.264  36.452  1.00 47.85  ? 123 TRP C CH2 1 
ATOM   4589 N N   . PRO C 1 133 ? -4.226  -34.263  39.091  1.00 59.03  ? 124 PRO C N   1 
ATOM   4590 C CA  . PRO C 1 133 ? -5.652  -34.005  39.334  1.00 57.90  ? 124 PRO C CA  1 
ATOM   4591 C C   . PRO C 1 133 ? -6.427  -33.906  38.031  1.00 54.62  ? 124 PRO C C   1 
ATOM   4592 O O   . PRO C 1 133 ? -7.477  -34.526  37.873  1.00 53.90  ? 124 PRO C O   1 
ATOM   4593 C CB  . PRO C 1 133 ? -5.647  -32.643  40.040  1.00 52.19  ? 124 PRO C CB  1 
ATOM   4594 C CG  . PRO C 1 133 ? -4.289  -32.065  39.791  1.00 52.27  ? 124 PRO C CG  1 
ATOM   4595 C CD  . PRO C 1 133 ? -3.370  -33.236  39.706  1.00 52.08  ? 124 PRO C CD  1 
ATOM   4596 N N   . ASN C 1 134 ? -5.879  -33.158  37.086  1.00 52.15  ? 125 ASN C N   1 
ATOM   4597 C CA  . ASN C 1 134 ? -6.621  -32.830  35.885  1.00 54.17  ? 125 ASN C CA  1 
ATOM   4598 C C   . ASN C 1 134 ? -6.424  -33.834  34.769  1.00 54.22  ? 125 ASN C C   1 
ATOM   4599 O O   . ASN C 1 134 ? -6.914  -33.641  33.652  1.00 54.59  ? 125 ASN C O   1 
ATOM   4600 C CB  . ASN C 1 134 ? -6.254  -31.433  35.416  1.00 54.10  ? 125 ASN C CB  1 
ATOM   4601 C CG  . ASN C 1 134 ? -6.528  -30.410  36.459  1.00 55.63  ? 125 ASN C CG  1 
ATOM   4602 O OD1 . ASN C 1 134 ? -7.497  -30.532  37.212  1.00 53.51  ? 125 ASN C OD1 1 
ATOM   4603 N ND2 . ASN C 1 134 ? -5.678  -29.389  36.530  1.00 53.73  ? 125 ASN C ND2 1 
ATOM   4604 N N   . HIS C 1 135 ? -5.686  -34.898  35.050  1.00 53.91  ? 126 HIS C N   1 
ATOM   4605 C CA  . HIS C 1 135 ? -5.473  -35.882  34.010  1.00 53.51  ? 126 HIS C CA  1 
ATOM   4606 C C   . HIS C 1 135 ? -5.791  -37.256  34.512  1.00 53.52  ? 126 HIS C C   1 
ATOM   4607 O O   . HIS C 1 135 ? -6.041  -37.451  35.691  1.00 55.10  ? 126 HIS C O   1 
ATOM   4608 C CB  . HIS C 1 135 ? -4.045  -35.792  33.503  1.00 51.72  ? 126 HIS C CB  1 
ATOM   4609 C CG  . HIS C 1 135 ? -3.694  -34.436  32.981  1.00 51.65  ? 126 HIS C CG  1 
ATOM   4610 N ND1 . HIS C 1 135 ? -3.150  -33.444  33.770  1.00 53.22  ? 126 HIS C ND1 1 
ATOM   4611 C CD2 . HIS C 1 135 ? -3.828  -33.903  31.745  1.00 51.21  ? 126 HIS C CD2 1 
ATOM   4612 C CE1 . HIS C 1 135 ? -2.955  -32.361  33.041  1.00 53.30  ? 126 HIS C CE1 1 
ATOM   4613 N NE2 . HIS C 1 135 ? -3.357  -32.612  31.806  1.00 54.30  ? 126 HIS C NE2 1 
ATOM   4614 N N   . ASP C 1 136 ? -5.776  -38.220  33.610  1.00 53.23  ? 127 ASP C N   1 
ATOM   4615 C CA  . ASP C 1 136 ? -6.285  -39.518  33.968  1.00 51.06  ? 127 ASP C CA  1 
ATOM   4616 C C   . ASP C 1 136 ? -5.155  -40.495  34.140  1.00 51.18  ? 127 ASP C C   1 
ATOM   4617 O O   . ASP C 1 136 ? -4.513  -40.937  33.170  1.00 52.06  ? 127 ASP C O   1 
ATOM   4618 C CB  . ASP C 1 136 ? -7.274  -40.022  32.939  1.00 51.72  ? 127 ASP C CB  1 
ATOM   4619 C CG  . ASP C 1 136 ? -7.937  -41.309  33.372  1.00 51.40  ? 127 ASP C CG  1 
ATOM   4620 O OD1 . ASP C 1 136 ? -7.264  -42.125  34.033  1.00 53.82  ? 127 ASP C OD1 1 
ATOM   4621 O OD2 . ASP C 1 136 ? -9.127  -41.508  33.058  1.00 52.08  ? 127 ASP C OD2 1 
ATOM   4622 N N   . SER C 1 137 ? -4.950  -40.847  35.400  1.00 50.63  ? 128 SER C N   1 
ATOM   4623 C CA  . SER C 1 137 ? -3.811  -41.640  35.810  1.00 53.45  ? 128 SER C CA  1 
ATOM   4624 C C   . SER C 1 137 ? -4.104  -43.143  35.731  1.00 53.23  ? 128 SER C C   1 
ATOM   4625 O O   . SER C 1 137 ? -3.186  -43.958  35.802  1.00 54.46  ? 128 SER C O   1 
ATOM   4626 C CB  . SER C 1 137 ? -3.391  -41.227  37.229  1.00 50.74  ? 128 SER C CB  1 
ATOM   4627 O OG  . SER C 1 137 ? -3.430  -39.806  37.380  1.00 48.41  ? 128 SER C OG  1 
ATOM   4628 N N   . ASN C 1 138 ? -5.370  -43.512  35.558  1.00 51.13  ? 129 ASN C N   1 
ATOM   4629 C CA  . ASN C 1 138 ? -5.760  -44.923  35.619  1.00 49.93  ? 129 ASN C CA  1 
ATOM   4630 C C   . ASN C 1 138 ? -5.541  -45.691  34.343  1.00 54.91  ? 129 ASN C C   1 
ATOM   4631 O O   . ASN C 1 138 ? -4.805  -46.677  34.342  1.00 59.64  ? 129 ASN C O   1 
ATOM   4632 C CB  . ASN C 1 138 ? -7.188  -45.067  36.075  1.00 50.39  ? 129 ASN C CB  1 
ATOM   4633 C CG  . ASN C 1 138 ? -7.377  -44.525  37.445  1.00 58.31  ? 129 ASN C CG  1 
ATOM   4634 O OD1 . ASN C 1 138 ? -6.660  -44.910  38.369  1.00 59.26  ? 129 ASN C OD1 1 
ATOM   4635 N ND2 . ASN C 1 138 ? -8.299  -43.578  37.590  1.00 61.87  ? 129 ASN C ND2 1 
ATOM   4636 N N   . LYS C 1 139 ? -6.208  -45.275  33.270  1.00 52.31  ? 130 LYS C N   1 
ATOM   4637 C CA  . LYS C 1 139 ? -5.903  -45.799  31.944  1.00 48.68  ? 130 LYS C CA  1 
ATOM   4638 C C   . LYS C 1 139 ? -4.523  -45.315  31.573  1.00 49.56  ? 130 LYS C C   1 
ATOM   4639 O O   . LYS C 1 139 ? -4.030  -44.328  32.142  1.00 53.00  ? 130 LYS C O   1 
ATOM   4640 C CB  . LYS C 1 139 ? -6.909  -45.309  30.930  1.00 46.67  ? 130 LYS C CB  1 
ATOM   4641 C CG  . LYS C 1 139 ? -8.015  -44.506  31.555  1.00 51.30  ? 130 LYS C CG  1 
ATOM   4642 C CD  . LYS C 1 139 ? -9.075  -44.234  30.510  1.00 59.29  ? 130 LYS C CD  1 
ATOM   4643 C CE  . LYS C 1 139 ? -10.309 -43.524  31.057  1.00 61.70  ? 130 LYS C CE  1 
ATOM   4644 N NZ  . LYS C 1 139 ? -11.253 -43.189  29.928  1.00 65.62  ? 130 LYS C NZ  1 
ATOM   4645 N N   . GLY C 1 140 ? -3.928  -45.927  30.562  1.00 46.54  ? 131 GLY C N   1 
ATOM   4646 C CA  . GLY C 1 140 ? -2.486  -45.977  30.500  1.00 47.65  ? 131 GLY C CA  1 
ATOM   4647 C C   . GLY C 1 140 ? -1.932  -47.382  30.620  1.00 48.50  ? 131 GLY C C   1 
ATOM   4648 O O   . GLY C 1 140 ? -0.803  -47.562  31.073  1.00 46.51  ? 131 GLY C O   1 
ATOM   4649 N N   . VAL C 1 141 ? -2.757  -48.374  30.280  1.00 48.15  ? 132 VAL C N   1 
ATOM   4650 C CA  . VAL C 1 141 ? -2.255  -49.730  30.034  1.00 49.22  ? 132 VAL C CA  1 
ATOM   4651 C C   . VAL C 1 141 ? -2.430  -50.219  28.600  1.00 49.98  ? 132 VAL C C   1 
ATOM   4652 O O   . VAL C 1 141 ? -3.253  -49.722  27.829  1.00 51.52  ? 132 VAL C O   1 
ATOM   4653 C CB  . VAL C 1 141 ? -2.910  -50.771  30.912  1.00 49.04  ? 132 VAL C CB  1 
ATOM   4654 C CG1 . VAL C 1 141 ? -2.590  -50.501  32.359  1.00 48.47  ? 132 VAL C CG1 1 
ATOM   4655 C CG2 . VAL C 1 141 ? -4.400  -50.796  30.648  1.00 48.15  ? 132 VAL C CG2 1 
ATOM   4656 N N   . THR C 1 142 ? -1.642  -51.220  28.257  1.00 49.58  ? 133 THR C N   1 
ATOM   4657 C CA  . THR C 1 142 ? -1.531  -51.619  26.883  1.00 47.07  ? 133 THR C CA  1 
ATOM   4658 C C   . THR C 1 142 ? -1.469  -53.128  26.813  1.00 46.29  ? 133 THR C C   1 
ATOM   4659 O O   . THR C 1 142 ? -1.176  -53.800  27.799  1.00 46.46  ? 133 THR C O   1 
ATOM   4660 C CB  . THR C 1 142 ? -0.256  -51.003  26.281  1.00 47.11  ? 133 THR C CB  1 
ATOM   4661 O OG1 . THR C 1 142 ? -0.120  -51.398  24.910  1.00 50.83  ? 133 THR C OG1 1 
ATOM   4662 C CG2 . THR C 1 142 ? 0.988   -51.421  27.082  1.00 44.80  ? 133 THR C CG2 1 
ATOM   4663 N N   . ALA C 1 143 ? -1.772  -53.665  25.647  1.00 44.81  ? 134 ALA C N   1 
ATOM   4664 C CA  . ALA C 1 143 ? -1.571  -55.084  25.427  1.00 48.01  ? 134 ALA C CA  1 
ATOM   4665 C C   . ALA C 1 143 ? -0.112  -55.369  25.114  1.00 48.75  ? 134 ALA C C   1 
ATOM   4666 O O   . ALA C 1 143 ? 0.340   -56.511  25.192  1.00 51.41  ? 134 ALA C O   1 
ATOM   4667 C CB  . ALA C 1 143 ? -2.436  -55.561  24.312  1.00 49.97  ? 134 ALA C CB  1 
ATOM   4668 N N   . ALA C 1 144 ? 0.617   -54.330  24.733  1.00 46.35  ? 135 ALA C N   1 
ATOM   4669 C CA  . ALA C 1 144 ? 2.042   -54.465  24.504  1.00 48.07  ? 135 ALA C CA  1 
ATOM   4670 C C   . ALA C 1 144 ? 2.727   -54.949  25.775  1.00 50.06  ? 135 ALA C C   1 
ATOM   4671 O O   . ALA C 1 144 ? 3.771   -55.592  25.710  1.00 51.30  ? 135 ALA C O   1 
ATOM   4672 C CB  . ALA C 1 144 ? 2.623   -53.146  24.068  1.00 48.87  ? 135 ALA C CB  1 
ATOM   4673 N N   . CYS C 1 145 ? 2.124   -54.654  26.929  1.00 49.55  ? 136 CYS C N   1 
ATOM   4674 C CA  . CYS C 1 145 ? 2.742   -54.956  28.225  1.00 52.63  ? 136 CYS C CA  1 
ATOM   4675 C C   . CYS C 1 145 ? 1.815   -55.699  29.187  1.00 51.22  ? 136 CYS C C   1 
ATOM   4676 O O   . CYS C 1 145 ? 1.354   -55.119  30.170  1.00 47.78  ? 136 CYS C O   1 
ATOM   4677 C CB  . CYS C 1 145 ? 3.206   -53.663  28.909  1.00 53.05  ? 136 CYS C CB  1 
ATOM   4678 S SG  . CYS C 1 145 ? 4.323   -52.626  27.931  1.00 55.61  ? 136 CYS C SG  1 
ATOM   4679 N N   . PRO C 1 146 ? 1.548   -56.984  28.913  1.00 50.65  ? 137 PRO C N   1 
ATOM   4680 C CA  . PRO C 1 146 ? 0.655   -57.795  29.740  1.00 51.50  ? 137 PRO C CA  1 
ATOM   4681 C C   . PRO C 1 146 ? 1.284   -58.215  31.052  1.00 57.40  ? 137 PRO C C   1 
ATOM   4682 O O   . PRO C 1 146 ? 2.480   -58.490  31.114  1.00 61.36  ? 137 PRO C O   1 
ATOM   4683 C CB  . PRO C 1 146 ? 0.427   -59.030  28.877  1.00 53.29  ? 137 PRO C CB  1 
ATOM   4684 C CG  . PRO C 1 146 ? 1.689   -59.165  28.118  1.00 52.37  ? 137 PRO C CG  1 
ATOM   4685 C CD  . PRO C 1 146 ? 2.086   -57.757  27.783  1.00 53.80  ? 137 PRO C CD  1 
ATOM   4686 N N   . HIS C 1 147 ? 0.472   -58.249  32.098  1.00 61.13  ? 138 HIS C N   1 
ATOM   4687 C CA  . HIS C 1 147 ? 0.861   -58.882  33.348  1.00 65.51  ? 138 HIS C CA  1 
ATOM   4688 C C   . HIS C 1 147 ? -0.360  -59.565  33.922  1.00 64.17  ? 138 HIS C C   1 
ATOM   4689 O O   . HIS C 1 147 ? -1.434  -58.969  33.976  1.00 59.70  ? 138 HIS C O   1 
ATOM   4690 C CB  . HIS C 1 147 ? 1.388   -57.863  34.348  1.00 62.57  ? 138 HIS C CB  1 
ATOM   4691 C CG  . HIS C 1 147 ? 1.951   -58.481  35.590  1.00 66.22  ? 138 HIS C CG  1 
ATOM   4692 N ND1 . HIS C 1 147 ? 3.027   -59.343  35.569  1.00 67.63  ? 138 HIS C ND1 1 
ATOM   4693 C CD2 . HIS C 1 147 ? 1.589   -58.363  36.890  1.00 71.55  ? 138 HIS C CD2 1 
ATOM   4694 C CE1 . HIS C 1 147 ? 3.305   -59.726  36.804  1.00 71.44  ? 138 HIS C CE1 1 
ATOM   4695 N NE2 . HIS C 1 147 ? 2.447   -59.146  37.625  1.00 72.17  ? 138 HIS C NE2 1 
ATOM   4696 N N   . ALA C 1 148 ? -0.185  -60.811  34.346  1.00 67.85  ? 139 ALA C N   1 
ATOM   4697 C CA  . ALA C 1 148 ? -1.265  -61.588  34.946  1.00 68.49  ? 139 ALA C CA  1 
ATOM   4698 C C   . ALA C 1 148 ? -2.451  -61.727  34.003  1.00 67.17  ? 139 ALA C C   1 
ATOM   4699 O O   . ALA C 1 148 ? -3.607  -61.619  34.420  1.00 67.31  ? 139 ALA C O   1 
ATOM   4700 C CB  . ALA C 1 148 ? -1.705  -60.964  36.258  1.00 64.76  ? 139 ALA C CB  1 
ATOM   4701 N N   . GLY C 1 149 ? -2.160  -61.965  32.730  1.00 65.36  ? 140 GLY C N   1 
ATOM   4702 C CA  . GLY C 1 149 ? -3.206  -62.126  31.738  1.00 67.34  ? 140 GLY C CA  1 
ATOM   4703 C C   . GLY C 1 149 ? -4.091  -60.902  31.588  1.00 65.67  ? 140 GLY C C   1 
ATOM   4704 O O   . GLY C 1 149 ? -5.303  -61.028  31.408  1.00 70.63  ? 140 GLY C O   1 
ATOM   4705 N N   . ALA C 1 150 ? -3.491  -59.716  31.663  1.00 63.22  ? 141 ALA C N   1 
ATOM   4706 C CA  . ALA C 1 150 ? -4.231  -58.471  31.473  1.00 61.22  ? 141 ALA C CA  1 
ATOM   4707 C C   . ALA C 1 150 ? -3.325  -57.315  31.049  1.00 57.40  ? 141 ALA C C   1 
ATOM   4708 O O   . ALA C 1 150 ? -2.114  -57.343  31.275  1.00 56.76  ? 141 ALA C O   1 
ATOM   4709 C CB  . ALA C 1 150 ? -4.991  -58.106  32.733  1.00 59.91  ? 141 ALA C CB  1 
ATOM   4710 N N   . LYS C 1 151 ? -3.930  -56.292  30.455  1.00 53.78  ? 142 LYS C N   1 
ATOM   4711 C CA  . LYS C 1 151 ? -3.191  -55.147  29.953  1.00 51.13  ? 142 LYS C CA  1 
ATOM   4712 C C   . LYS C 1 151 ? -2.443  -54.438  31.060  1.00 49.55  ? 142 LYS C C   1 
ATOM   4713 O O   . LYS C 1 151 ? -3.010  -54.141  32.103  1.00 48.08  ? 142 LYS C O   1 
ATOM   4714 C CB  . LYS C 1 151 ? -4.138  -54.169  29.266  1.00 49.48  ? 142 LYS C CB  1 
ATOM   4715 C CG  . LYS C 1 151 ? -4.721  -54.694  27.978  1.00 48.69  ? 142 LYS C CG  1 
ATOM   4716 C CD  . LYS C 1 151 ? -5.465  -53.589  27.228  1.00 53.88  ? 142 LYS C CD  1 
ATOM   4717 C CE  . LYS C 1 151 ? -6.852  -53.307  27.822  1.00 60.63  ? 142 LYS C CE  1 
ATOM   4718 N NZ  . LYS C 1 151 ? -7.611  -52.265  27.041  1.00 59.57  ? 142 LYS C NZ  1 
ATOM   4719 N N   . SER C 1 152 ? -1.165  -54.154  30.836  1.00 50.80  ? 143 SER C N   1 
ATOM   4720 C CA  . SER C 1 152 ? -0.396  -53.437  31.851  1.00 50.62  ? 143 SER C CA  1 
ATOM   4721 C C   . SER C 1 152 ? 0.533   -52.388  31.255  1.00 48.25  ? 143 SER C C   1 
ATOM   4722 O O   . SER C 1 152 ? 0.443   -52.064  30.078  1.00 48.65  ? 143 SER C O   1 
ATOM   4723 C CB  . SER C 1 152 ? 0.391   -54.400  32.736  1.00 53.69  ? 143 SER C CB  1 
ATOM   4724 O OG  . SER C 1 152 ? 1.039   -53.687  33.770  1.00 52.20  ? 143 SER C OG  1 
ATOM   4725 N N   . PHE C 1 153 ? 1.411   -51.843  32.085  1.00 48.89  ? 144 PHE C N   1 
ATOM   4726 C CA  . PHE C 1 153 ? 2.356   -50.837  31.635  1.00 46.35  ? 144 PHE C CA  1 
ATOM   4727 C C   . PHE C 1 153 ? 3.576   -50.844  32.557  1.00 48.32  ? 144 PHE C C   1 
ATOM   4728 O O   . PHE C 1 153 ? 3.612   -51.591  33.539  1.00 45.62  ? 144 PHE C O   1 
ATOM   4729 C CB  . PHE C 1 153 ? 1.677   -49.475  31.654  1.00 40.47  ? 144 PHE C CB  1 
ATOM   4730 C CG  . PHE C 1 153 ? 2.394   -48.436  30.876  1.00 43.28  ? 144 PHE C CG  1 
ATOM   4731 C CD1 . PHE C 1 153 ? 2.496   -48.533  29.503  1.00 44.54  ? 144 PHE C CD1 1 
ATOM   4732 C CD2 . PHE C 1 153 ? 2.954   -47.345  31.509  1.00 42.69  ? 144 PHE C CD2 1 
ATOM   4733 C CE1 . PHE C 1 153 ? 3.156   -47.560  28.785  1.00 43.75  ? 144 PHE C CE1 1 
ATOM   4734 C CE2 . PHE C 1 153 ? 3.614   -46.372  30.792  1.00 41.40  ? 144 PHE C CE2 1 
ATOM   4735 C CZ  . PHE C 1 153 ? 3.716   -46.472  29.439  1.00 39.40  ? 144 PHE C CZ  1 
ATOM   4736 N N   . TYR C 1 154 ? 4.574   -50.019  32.248  1.00 48.46  ? 145 TYR C N   1 
ATOM   4737 C CA  . TYR C 1 154 ? 5.786   -49.975  33.063  1.00 47.42  ? 145 TYR C CA  1 
ATOM   4738 C C   . TYR C 1 154 ? 5.456   -49.388  34.425  1.00 46.95  ? 145 TYR C C   1 
ATOM   4739 O O   . TYR C 1 154 ? 4.704   -48.414  34.514  1.00 46.57  ? 145 TYR C O   1 
ATOM   4740 C CB  . TYR C 1 154 ? 6.858   -49.120  32.391  1.00 45.34  ? 145 TYR C CB  1 
ATOM   4741 C CG  . TYR C 1 154 ? 7.084   -49.457  30.943  1.00 44.50  ? 145 TYR C CG  1 
ATOM   4742 C CD1 . TYR C 1 154 ? 7.787   -50.592  30.579  1.00 45.94  ? 145 TYR C CD1 1 
ATOM   4743 C CD2 . TYR C 1 154 ? 6.593   -48.642  29.940  1.00 43.88  ? 145 TYR C CD2 1 
ATOM   4744 C CE1 . TYR C 1 154 ? 8.001   -50.913  29.256  1.00 47.16  ? 145 TYR C CE1 1 
ATOM   4745 C CE2 . TYR C 1 154 ? 6.802   -48.948  28.606  1.00 45.72  ? 145 TYR C CE2 1 
ATOM   4746 C CZ  . TYR C 1 154 ? 7.507   -50.092  28.264  1.00 47.05  ? 145 TYR C CZ  1 
ATOM   4747 O OH  . TYR C 1 154 ? 7.728   -50.415  26.931  1.00 45.48  ? 145 TYR C OH  1 
ATOM   4748 N N   . LYS C 1 155 ? 6.016   -49.960  35.488  1.00 47.69  ? 146 LYS C N   1 
ATOM   4749 C CA  . LYS C 1 155 ? 5.700   -49.471  36.839  1.00 49.20  ? 146 LYS C CA  1 
ATOM   4750 C C   . LYS C 1 155 ? 6.248   -48.090  37.164  1.00 46.80  ? 146 LYS C C   1 
ATOM   4751 O O   . LYS C 1 155 ? 5.599   -47.306  37.844  1.00 50.77  ? 146 LYS C O   1 
ATOM   4752 C CB  . LYS C 1 155 ? 6.146   -50.437  37.931  1.00 48.89  ? 146 LYS C CB  1 
ATOM   4753 C CG  . LYS C 1 155 ? 6.126   -49.779  39.323  1.00 55.26  ? 146 LYS C CG  1 
ATOM   4754 C CD  . LYS C 1 155 ? 5.955   -50.816  40.451  1.00 64.41  ? 146 LYS C CD  1 
ATOM   4755 C CE  . LYS C 1 155 ? 5.995   -50.176  41.845  1.00 67.16  ? 146 LYS C CE  1 
ATOM   4756 N NZ  . LYS C 1 155 ? 5.968   -51.184  42.948  1.00 67.38  ? 146 LYS C NZ  1 
ATOM   4757 N N   . ASN C 1 156 ? 7.431   -47.787  36.662  1.00 48.04  ? 147 ASN C N   1 
ATOM   4758 C CA  . ASN C 1 156 ? 8.098   -46.545  37.018  1.00 47.67  ? 147 ASN C CA  1 
ATOM   4759 C C   . ASN C 1 156 ? 7.610   -45.339  36.224  1.00 46.30  ? 147 ASN C C   1 
ATOM   4760 O O   . ASN C 1 156 ? 8.129   -44.232  36.377  1.00 45.57  ? 147 ASN C O   1 
ATOM   4761 C CB  . ASN C 1 156 ? 9.612   -46.723  36.904  1.00 47.94  ? 147 ASN C CB  1 
ATOM   4762 C CG  . ASN C 1 156 ? 10.124  -47.790  37.843  1.00 50.77  ? 147 ASN C CG  1 
ATOM   4763 O OD1 . ASN C 1 156 ? 9.461   -48.120  38.831  1.00 52.07  ? 147 ASN C OD1 1 
ATOM   4764 N ND2 . ASN C 1 156 ? 11.297  -48.340  37.546  1.00 51.50  ? 147 ASN C ND2 1 
ATOM   4765 N N   . LEU C 1 157 ? 6.606   -45.569  35.379  1.00 48.28  ? 148 LEU C N   1 
ATOM   4766 C CA  . LEU C 1 157 ? 5.996   -44.511  34.564  1.00 45.52  ? 148 LEU C CA  1 
ATOM   4767 C C   . LEU C 1 157 ? 4.469   -44.560  34.495  1.00 44.72  ? 148 LEU C C   1 
ATOM   4768 O O   . LEU C 1 157 ? 3.858   -45.634  34.548  1.00 47.70  ? 148 LEU C O   1 
ATOM   4769 C CB  . LEU C 1 157 ? 6.510   -44.595  33.140  1.00 47.70  ? 148 LEU C CB  1 
ATOM   4770 C CG  . LEU C 1 157 ? 8.008   -44.496  32.898  1.00 44.41  ? 148 LEU C CG  1 
ATOM   4771 C CD1 . LEU C 1 157 ? 8.232   -44.518  31.390  1.00 38.32  ? 148 LEU C CD1 1 
ATOM   4772 C CD2 . LEU C 1 157 ? 8.557   -43.234  33.555  1.00 40.86  ? 148 LEU C CD2 1 
ATOM   4773 N N   . ILE C 1 158 ? 3.863   -43.387  34.343  1.00 46.57  ? 149 ILE C N   1 
ATOM   4774 C CA  . ILE C 1 158 ? 2.414   -43.275  34.164  1.00 47.33  ? 149 ILE C CA  1 
ATOM   4775 C C   . ILE C 1 158 ? 2.066   -42.691  32.794  1.00 45.81  ? 149 ILE C C   1 
ATOM   4776 O O   . ILE C 1 158 ? 2.549   -41.615  32.406  1.00 43.20  ? 149 ILE C O   1 
ATOM   4777 C CB  . ILE C 1 158 ? 1.757   -42.390  35.244  1.00 45.15  ? 149 ILE C CB  1 
ATOM   4778 C CG1 . ILE C 1 158 ? 2.068   -42.914  36.638  1.00 47.92  ? 149 ILE C CG1 1 
ATOM   4779 C CG2 . ILE C 1 158 ? 0.243   -42.333  35.048  1.00 48.88  ? 149 ILE C CG2 1 
ATOM   4780 C CD1 . ILE C 1 158 ? 1.187   -44.046  37.050  1.00 49.69  ? 149 ILE C CD1 1 
ATOM   4781 N N   . TRP C 1 159 ? 1.214   -43.399  32.064  1.00 44.62  ? 150 TRP C N   1 
ATOM   4782 C CA  . TRP C 1 159 ? 0.794   -42.916  30.773  1.00 40.54  ? 150 TRP C CA  1 
ATOM   4783 C C   . TRP C 1 159 ? -0.488  -42.142  31.017  1.00 44.51  ? 150 TRP C C   1 
ATOM   4784 O O   . TRP C 1 159 ? -1.564  -42.712  31.207  1.00 43.34  ? 150 TRP C O   1 
ATOM   4785 C CB  . TRP C 1 159 ? 0.543   -44.109  29.874  1.00 38.89  ? 150 TRP C CB  1 
ATOM   4786 C CG  . TRP C 1 159 ? 0.241   -43.766  28.453  1.00 46.10  ? 150 TRP C CG  1 
ATOM   4787 C CD1 . TRP C 1 159 ? 0.122   -42.515  27.906  1.00 44.50  ? 150 TRP C CD1 1 
ATOM   4788 C CD2 . TRP C 1 159 ? 0.006   -44.694  27.387  1.00 42.52  ? 150 TRP C CD2 1 
ATOM   4789 N NE1 . TRP C 1 159 ? -0.172  -42.614  26.571  1.00 42.21  ? 150 TRP C NE1 1 
ATOM   4790 C CE2 . TRP C 1 159 ? -0.248  -43.943  26.232  1.00 43.16  ? 150 TRP C CE2 1 
ATOM   4791 C CE3 . TRP C 1 159 ? -0.014  -46.092  27.304  1.00 44.01  ? 150 TRP C CE3 1 
ATOM   4792 C CZ2 . TRP C 1 159 ? -0.516  -44.546  25.002  1.00 46.97  ? 150 TRP C CZ2 1 
ATOM   4793 C CZ3 . TRP C 1 159 ? -0.284  -46.686  26.090  1.00 41.39  ? 150 TRP C CZ3 1 
ATOM   4794 C CH2 . TRP C 1 159 ? -0.532  -45.919  24.957  1.00 43.67  ? 150 TRP C CH2 1 
ATOM   4795 N N   . LEU C 1 160 ? -0.361  -40.823  30.963  1.00 46.03  ? 151 LEU C N   1 
ATOM   4796 C CA  . LEU C 1 160 ? -1.475  -39.925  31.206  1.00 46.49  ? 151 LEU C CA  1 
ATOM   4797 C C   . LEU C 1 160 ? -2.331  -39.762  29.971  1.00 48.52  ? 151 LEU C C   1 
ATOM   4798 O O   . LEU C 1 160 ? -1.855  -39.842  28.842  1.00 46.14  ? 151 LEU C O   1 
ATOM   4799 C CB  . LEU C 1 160 ? -0.976  -38.561  31.642  1.00 46.92  ? 151 LEU C CB  1 
ATOM   4800 C CG  . LEU C 1 160 ? -0.453  -38.506  33.071  1.00 48.06  ? 151 LEU C CG  1 
ATOM   4801 C CD1 . LEU C 1 160 ? -0.130  -37.065  33.397  1.00 48.30  ? 151 LEU C CD1 1 
ATOM   4802 C CD2 . LEU C 1 160 ? -1.489  -39.070  34.042  1.00 49.73  ? 151 LEU C CD2 1 
ATOM   4803 N N   . VAL C 1 161 ? -3.604  -39.507  30.202  1.00 50.21  ? 152 VAL C N   1 
ATOM   4804 C CA  . VAL C 1 161 ? -4.579  -39.528  29.142  1.00 47.54  ? 152 VAL C CA  1 
ATOM   4805 C C   . VAL C 1 161 ? -5.576  -38.468  29.542  1.00 51.26  ? 152 VAL C C   1 
ATOM   4806 O O   . VAL C 1 161 ? -5.673  -38.144  30.732  1.00 54.25  ? 152 VAL C O   1 
ATOM   4807 C CB  . VAL C 1 161 ? -5.250  -40.910  29.091  1.00 47.79  ? 152 VAL C CB  1 
ATOM   4808 C CG1 . VAL C 1 161 ? -6.631  -40.808  28.515  1.00 51.24  ? 152 VAL C CG1 1 
ATOM   4809 C CG2 . VAL C 1 161 ? -4.380  -41.902  28.310  1.00 42.88  ? 152 VAL C CG2 1 
ATOM   4810 N N   . LYS C 1 162 ? -6.302  -37.912  28.575  1.00 49.37  ? 153 LYS C N   1 
ATOM   4811 C CA  . LYS C 1 162 ? -7.268  -36.868  28.878  1.00 52.21  ? 153 LYS C CA  1 
ATOM   4812 C C   . LYS C 1 162 ? -8.198  -37.341  29.983  1.00 54.12  ? 153 LYS C C   1 
ATOM   4813 O O   . LYS C 1 162 ? -8.631  -38.491  29.983  1.00 53.78  ? 153 LYS C O   1 
ATOM   4814 C CB  . LYS C 1 162 ? -8.082  -36.503  27.636  1.00 53.57  ? 153 LYS C CB  1 
ATOM   4815 C CG  . LYS C 1 162 ? -8.980  -37.625  27.100  1.00 49.33  ? 153 LYS C CG  1 
ATOM   4816 C CD  . LYS C 1 162 ? -9.609  -37.216  25.766  1.00 51.28  ? 153 LYS C CD  1 
ATOM   4817 C CE  . LYS C 1 162 ? -10.630 -38.241  25.270  1.00 50.14  ? 153 LYS C CE  1 
ATOM   4818 N NZ  . LYS C 1 162 ? -11.221 -37.875  23.953  1.00 43.75  ? 153 LYS C NZ  1 
ATOM   4819 N N   . LYS C 1 163 ? -8.462  -36.467  30.950  1.00 59.02  ? 154 LYS C N   1 
ATOM   4820 C CA  . LYS C 1 163 ? -9.571  -36.670  31.877  1.00 58.59  ? 154 LYS C CA  1 
ATOM   4821 C C   . LYS C 1 163 ? -10.742 -36.013  31.175  1.00 61.25  ? 154 LYS C C   1 
ATOM   4822 O O   . LYS C 1 163 ? -10.630 -34.872  30.707  1.00 60.02  ? 154 LYS C O   1 
ATOM   4823 C CB  . LYS C 1 163 ? -9.307  -36.018  33.227  1.00 60.36  ? 154 LYS C CB  1 
ATOM   4824 C CG  . LYS C 1 163 ? -10.039 -36.706  34.370  1.00 60.61  ? 154 LYS C CG  1 
ATOM   4825 C CD  . LYS C 1 163 ? -9.536  -36.207  35.706  1.00 59.62  ? 154 LYS C CD  1 
ATOM   4826 C CE  . LYS C 1 163 ? -9.998  -37.097  36.829  1.00 60.66  ? 154 LYS C CE  1 
ATOM   4827 N NZ  . LYS C 1 163 ? -9.221  -36.798  38.058  1.00 63.15  ? 154 LYS C NZ  1 
ATOM   4828 N N   . GLY C 1 164 ? -11.883 -36.693  31.154  1.00 61.45  ? 155 GLY C N   1 
ATOM   4829 C CA  . GLY C 1 164 ? -12.682 -36.719  29.943  1.00 62.33  ? 155 GLY C CA  1 
ATOM   4830 C C   . GLY C 1 164 ? -12.823 -35.390  29.229  1.00 63.56  ? 155 GLY C C   1 
ATOM   4831 O O   . GLY C 1 164 ? -13.140 -34.361  29.830  1.00 67.15  ? 155 GLY C O   1 
ATOM   4832 N N   . ASN C 1 165 ? -12.547 -35.436  27.929  1.00 58.00  ? 156 ASN C N   1 
ATOM   4833 C CA  . ASN C 1 165 ? -12.709 -34.309  27.016  1.00 61.34  ? 156 ASN C CA  1 
ATOM   4834 C C   . ASN C 1 165 ? -11.603 -33.260  27.120  1.00 59.07  ? 156 ASN C C   1 
ATOM   4835 O O   . ASN C 1 165 ? -11.425 -32.442  26.224  1.00 61.17  ? 156 ASN C O   1 
ATOM   4836 C CB  . ASN C 1 165 ? -14.091 -33.662  27.188  1.00 64.47  ? 156 ASN C CB  1 
ATOM   4837 C CG  . ASN C 1 165 ? -14.562 -32.933  25.932  1.00 69.47  ? 156 ASN C CG  1 
ATOM   4838 O OD1 . ASN C 1 165 ? -13.853 -32.885  24.915  1.00 69.42  ? 156 ASN C OD1 1 
ATOM   4839 N ND2 . ASN C 1 165 ? -15.771 -32.372  25.992  1.00 64.74  ? 156 ASN C ND2 1 
ATOM   4840 N N   . SER C 1 166 ? -10.825 -33.303  28.189  1.00 58.93  ? 157 SER C N   1 
ATOM   4841 C CA  . SER C 1 166 ? -9.893  -32.212  28.432  1.00 60.89  ? 157 SER C CA  1 
ATOM   4842 C C   . SER C 1 166 ? -8.486  -32.630  28.799  1.00 59.56  ? 157 SER C C   1 
ATOM   4843 O O   . SER C 1 166 ? -8.249  -33.332  29.791  1.00 59.45  ? 157 SER C O   1 
ATOM   4844 C CB  . SER C 1 166 ? -10.440 -31.270  29.499  1.00 64.34  ? 157 SER C CB  1 
ATOM   4845 O OG  . SER C 1 166 ? -11.591 -30.606  29.009  1.00 69.26  ? 157 SER C OG  1 
ATOM   4846 N N   . TYR C 1 167 ? -7.544  -32.162  27.995  1.00 58.02  ? 158 TYR C N   1 
ATOM   4847 C CA  . TYR C 1 167 ? -6.157  -32.345  28.331  1.00 54.19  ? 158 TYR C CA  1 
ATOM   4848 C C   . TYR C 1 167 ? -5.517  -30.987  28.503  1.00 50.01  ? 158 TYR C C   1 
ATOM   4849 O O   . TYR C 1 167 ? -4.880  -30.474  27.599  1.00 53.50  ? 158 TYR C O   1 
ATOM   4850 C CB  . TYR C 1 167 ? -5.449  -33.159  27.270  1.00 51.82  ? 158 TYR C CB  1 
ATOM   4851 C CG  . TYR C 1 167 ? -4.153  -33.700  27.772  1.00 49.89  ? 158 TYR C CG  1 
ATOM   4852 C CD1 . TYR C 1 167 ? -3.117  -32.843  28.112  1.00 50.00  ? 158 TYR C CD1 1 
ATOM   4853 C CD2 . TYR C 1 167 ? -3.966  -35.064  27.932  1.00 46.11  ? 158 TYR C CD2 1 
ATOM   4854 C CE1 . TYR C 1 167 ? -1.925  -33.328  28.584  1.00 49.57  ? 158 TYR C CE1 1 
ATOM   4855 C CE2 . TYR C 1 167 ? -2.775  -35.561  28.401  1.00 46.58  ? 158 TYR C CE2 1 
ATOM   4856 C CZ  . TYR C 1 167 ? -1.757  -34.687  28.726  1.00 47.60  ? 158 TYR C CZ  1 
ATOM   4857 O OH  . TYR C 1 167 ? -0.557  -35.170  29.196  1.00 47.09  ? 158 TYR C OH  1 
ATOM   4858 N N   . PRO C 1 168 ? -5.703  -30.400  29.685  1.00 54.26  ? 159 PRO C N   1 
ATOM   4859 C CA  . PRO C 1 168 ? -5.238  -29.056  30.025  1.00 55.83  ? 159 PRO C CA  1 
ATOM   4860 C C   . PRO C 1 168 ? -3.721  -29.058  30.063  1.00 57.03  ? 159 PRO C C   1 
ATOM   4861 O O   . PRO C 1 168 ? -3.125  -30.118  30.296  1.00 55.74  ? 159 PRO C O   1 
ATOM   4862 C CB  . PRO C 1 168 ? -5.789  -28.857  31.436  1.00 52.67  ? 159 PRO C CB  1 
ATOM   4863 C CG  . PRO C 1 168 ? -5.791  -30.245  32.020  1.00 52.00  ? 159 PRO C CG  1 
ATOM   4864 C CD  . PRO C 1 168 ? -6.183  -31.135  30.871  1.00 55.83  ? 159 PRO C CD  1 
ATOM   4865 N N   . LYS C 1 169 ? -3.096  -27.906  29.846  1.00 56.06  ? 160 LYS C N   1 
ATOM   4866 C CA  . LYS C 1 169 ? -1.647  -27.888  29.856  1.00 55.96  ? 160 LYS C CA  1 
ATOM   4867 C C   . LYS C 1 169 ? -1.227  -28.484  31.170  1.00 56.94  ? 160 LYS C C   1 
ATOM   4868 O O   . LYS C 1 169 ? -1.901  -28.346  32.186  1.00 60.75  ? 160 LYS C O   1 
ATOM   4869 C CB  . LYS C 1 169 ? -1.051  -26.489  29.699  1.00 57.33  ? 160 LYS C CB  1 
ATOM   4870 C CG  . LYS C 1 169 ? 0.475   -26.520  29.567  1.00 60.08  ? 160 LYS C CG  1 
ATOM   4871 C CD  . LYS C 1 169 ? 1.086   -25.129  29.435  1.00 60.84  ? 160 LYS C CD  1 
ATOM   4872 C CE  . LYS C 1 169 ? 1.041   -24.378  30.749  1.00 65.35  ? 160 LYS C CE  1 
ATOM   4873 N NZ  . LYS C 1 169 ? 1.806   -23.102  30.682  1.00 67.67  ? 160 LYS C NZ  1 
ATOM   4874 N N   . LEU C 1 170 ? -0.120  -29.192  31.140  1.00 56.94  ? 161 LEU C N   1 
ATOM   4875 C CA  . LEU C 1 170 ? 0.295   -29.914  32.306  1.00 53.81  ? 161 LEU C CA  1 
ATOM   4876 C C   . LEU C 1 170 ? 1.642   -29.379  32.696  1.00 55.10  ? 161 LEU C C   1 
ATOM   4877 O O   . LEU C 1 170 ? 2.576   -29.367  31.906  1.00 57.45  ? 161 LEU C O   1 
ATOM   4878 C CB  . LEU C 1 170 ? 0.340   -31.408  32.002  1.00 52.08  ? 161 LEU C CB  1 
ATOM   4879 C CG  . LEU C 1 170 ? 1.103   -32.340  32.936  1.00 51.41  ? 161 LEU C CG  1 
ATOM   4880 C CD1 . LEU C 1 170 ? 0.587   -33.753  32.773  1.00 50.80  ? 161 LEU C CD1 1 
ATOM   4881 C CD2 . LEU C 1 170 ? 2.608   -32.287  32.697  1.00 52.82  ? 161 LEU C CD2 1 
ATOM   4882 N N   . SER C 1 171 ? 1.733   -28.900  33.919  1.00 57.30  ? 162 SER C N   1 
ATOM   4883 C CA  . SER C 1 171 ? 3.020   -28.526  34.439  1.00 60.22  ? 162 SER C CA  1 
ATOM   4884 C C   . SER C 1 171 ? 3.093   -29.045  35.842  1.00 58.83  ? 162 SER C C   1 
ATOM   4885 O O   . SER C 1 171 ? 2.208   -28.800  36.658  1.00 64.54  ? 162 SER C O   1 
ATOM   4886 C CB  . SER C 1 171 ? 3.227   -27.014  34.407  1.00 62.02  ? 162 SER C CB  1 
ATOM   4887 O OG  . SER C 1 171 ? 4.600   -26.701  34.594  1.00 63.75  ? 162 SER C OG  1 
ATOM   4888 N N   . LYS C 1 172 ? 4.125   -29.826  36.094  1.00 56.91  ? 163 LYS C N   1 
ATOM   4889 C CA  . LYS C 1 172 ? 4.465   -30.205  37.439  1.00 56.93  ? 163 LYS C CA  1 
ATOM   4890 C C   . LYS C 1 172 ? 5.971   -30.218  37.415  1.00 59.63  ? 163 LYS C C   1 
ATOM   4891 O O   . LYS C 1 172 ? 6.576   -30.677  36.446  1.00 58.70  ? 163 LYS C O   1 
ATOM   4892 C CB  . LYS C 1 172 ? 3.908   -31.583  37.782  1.00 56.34  ? 163 LYS C CB  1 
ATOM   4893 C CG  . LYS C 1 172 ? 3.780   -31.870  39.292  1.00 64.49  ? 163 LYS C CG  1 
ATOM   4894 C CD  . LYS C 1 172 ? 2.347   -31.607  39.817  1.00 65.00  ? 163 LYS C CD  1 
ATOM   4895 C CE  . LYS C 1 172 ? 2.156   -32.093  41.264  1.00 63.88  ? 163 LYS C CE  1 
ATOM   4896 N NZ  . LYS C 1 172 ? 0.710   -32.159  41.670  1.00 57.19  ? 163 LYS C NZ  1 
ATOM   4897 N N   . SER C 1 173 ? 6.580   -29.666  38.453  1.00 60.82  ? 164 SER C N   1 
ATOM   4898 C CA  . SER C 1 173 ? 8.025   -29.611  38.507  1.00 58.10  ? 164 SER C CA  1 
ATOM   4899 C C   . SER C 1 173 ? 8.518   -30.342  39.754  1.00 56.75  ? 164 SER C C   1 
ATOM   4900 O O   . SER C 1 173 ? 7.724   -30.816  40.563  1.00 58.94  ? 164 SER C O   1 
ATOM   4901 C CB  . SER C 1 173 ? 8.496   -28.154  38.485  1.00 54.33  ? 164 SER C CB  1 
ATOM   4902 O OG  . SER C 1 173 ? 9.337   -27.883  39.592  1.00 52.84  ? 164 SER C OG  1 
ATOM   4903 N N   . TYR C 1 174 ? 9.828   -30.439  39.909  1.00 55.35  ? 165 TYR C N   1 
ATOM   4904 C CA  . TYR C 1 174 ? 10.392  -31.100  41.068  1.00 53.61  ? 165 TYR C CA  1 
ATOM   4905 C C   . TYR C 1 174 ? 11.817  -30.650  41.301  1.00 56.16  ? 165 TYR C C   1 
ATOM   4906 O O   . TYR C 1 174 ? 12.491  -30.175  40.379  1.00 54.71  ? 165 TYR C O   1 
ATOM   4907 C CB  . TYR C 1 174 ? 10.349  -32.611  40.896  1.00 51.26  ? 165 TYR C CB  1 
ATOM   4908 C CG  . TYR C 1 174 ? 11.288  -33.367  41.810  1.00 53.40  ? 165 TYR C CG  1 
ATOM   4909 C CD1 . TYR C 1 174 ? 10.887  -33.781  43.074  1.00 53.18  ? 165 TYR C CD1 1 
ATOM   4910 C CD2 . TYR C 1 174 ? 12.575  -33.670  41.404  1.00 52.32  ? 165 TYR C CD2 1 
ATOM   4911 C CE1 . TYR C 1 174 ? 11.742  -34.486  43.898  1.00 50.90  ? 165 TYR C CE1 1 
ATOM   4912 C CE2 . TYR C 1 174 ? 13.435  -34.373  42.218  1.00 56.58  ? 165 TYR C CE2 1 
ATOM   4913 C CZ  . TYR C 1 174 ? 13.017  -34.781  43.465  1.00 56.08  ? 165 TYR C CZ  1 
ATOM   4914 O OH  . TYR C 1 174 ? 13.890  -35.477  44.271  1.00 55.88  ? 165 TYR C OH  1 
ATOM   4915 N N   . ILE C 1 175 ? 12.272  -30.835  42.535  1.00 55.85  ? 166 ILE C N   1 
ATOM   4916 C CA  . ILE C 1 175 ? 13.572  -30.357  42.965  1.00 55.00  ? 166 ILE C CA  1 
ATOM   4917 C C   . ILE C 1 175 ? 14.359  -31.479  43.612  1.00 58.59  ? 166 ILE C C   1 
ATOM   4918 O O   . ILE C 1 175 ? 13.811  -32.224  44.427  1.00 60.53  ? 166 ILE C O   1 
ATOM   4919 C CB  . ILE C 1 175 ? 13.403  -29.243  43.981  1.00 51.77  ? 166 ILE C CB  1 
ATOM   4920 C CG1 . ILE C 1 175 ? 12.751  -28.035  43.302  1.00 54.20  ? 166 ILE C CG1 1 
ATOM   4921 C CG2 . ILE C 1 175 ? 14.735  -28.900  44.597  1.00 54.96  ? 166 ILE C CG2 1 
ATOM   4922 C CD1 . ILE C 1 175 ? 12.832  -26.734  44.082  1.00 52.01  ? 166 ILE C CD1 1 
ATOM   4923 N N   . ASN C 1 176 ? 15.651  -31.581  43.310  1.00 58.59  ? 167 ASN C N   1 
ATOM   4924 C CA  . ASN C 1 176 ? 16.426  -32.652  43.922  1.00 61.59  ? 167 ASN C CA  1 
ATOM   4925 C C   . ASN C 1 176 ? 16.953  -32.101  45.243  1.00 63.43  ? 167 ASN C C   1 
ATOM   4926 O O   . ASN C 1 176 ? 17.847  -31.265  45.264  1.00 63.87  ? 167 ASN C O   1 
ATOM   4927 C CB  . ASN C 1 176 ? 17.587  -33.078  43.001  1.00 57.02  ? 167 ASN C CB  1 
ATOM   4928 C CG  . ASN C 1 176 ? 18.421  -34.211  43.585  1.00 57.81  ? 167 ASN C CG  1 
ATOM   4929 O OD1 . ASN C 1 176 ? 18.346  -34.493  44.775  1.00 59.91  ? 167 ASN C OD1 1 
ATOM   4930 N ND2 . ASN C 1 176 ? 19.234  -34.851  42.751  1.00 58.96  ? 167 ASN C ND2 1 
ATOM   4931 N N   . ASP C 1 177 ? 16.352  -32.556  46.342  1.00 64.60  ? 168 ASP C N   1 
ATOM   4932 C CA  . ASP C 1 177 ? 16.753  -32.168  47.693  1.00 62.42  ? 168 ASP C CA  1 
ATOM   4933 C C   . ASP C 1 177 ? 17.574  -33.248  48.379  1.00 61.70  ? 168 ASP C C   1 
ATOM   4934 O O   . ASP C 1 177 ? 17.971  -33.107  49.541  1.00 65.16  ? 168 ASP C O   1 
ATOM   4935 C CB  . ASP C 1 177 ? 15.521  -31.820  48.529  1.00 64.36  ? 168 ASP C CB  1 
ATOM   4936 C CG  . ASP C 1 177 ? 14.380  -32.804  48.321  1.00 68.06  ? 168 ASP C CG  1 
ATOM   4937 O OD1 . ASP C 1 177 ? 14.635  -34.031  48.349  1.00 66.62  ? 168 ASP C OD1 1 
ATOM   4938 O OD2 . ASP C 1 177 ? 13.234  -32.348  48.104  1.00 71.11  ? 168 ASP C OD2 1 
ATOM   4939 N N   . LYS C 1 178 ? 17.800  -34.347  47.675  1.00 59.88  ? 169 LYS C N   1 
ATOM   4940 C CA  . LYS C 1 178 ? 18.563  -35.436  48.251  1.00 59.15  ? 169 LYS C CA  1 
ATOM   4941 C C   . LYS C 1 178 ? 20.050  -35.108  48.140  1.00 62.31  ? 169 LYS C C   1 
ATOM   4942 O O   . LYS C 1 178 ? 20.446  -34.065  47.588  1.00 59.80  ? 169 LYS C O   1 
ATOM   4943 C CB  . LYS C 1 178 ? 18.251  -36.748  47.537  1.00 58.47  ? 169 LYS C CB  1 
ATOM   4944 C CG  . LYS C 1 178 ? 16.858  -36.797  46.929  1.00 59.05  ? 169 LYS C CG  1 
ATOM   4945 C CD  . LYS C 1 178 ? 16.368  -38.228  46.759  1.00 58.12  ? 169 LYS C CD  1 
ATOM   4946 C CE  . LYS C 1 178 ? 15.227  -38.536  47.712  1.00 58.96  ? 169 LYS C CE  1 
ATOM   4947 N NZ  . LYS C 1 178 ? 15.628  -39.453  48.815  1.00 60.72  ? 169 LYS C NZ  1 
ATOM   4948 N N   . GLY C 1 179 ? 20.873  -36.010  48.654  1.00 60.00  ? 170 GLY C N   1 
ATOM   4949 C CA  . GLY C 1 179 ? 22.299  -35.774  48.684  1.00 62.82  ? 170 GLY C CA  1 
ATOM   4950 C C   . GLY C 1 179 ? 22.960  -36.112  47.371  1.00 64.23  ? 170 GLY C C   1 
ATOM   4951 O O   . GLY C 1 179 ? 24.071  -35.662  47.104  1.00 64.21  ? 170 GLY C O   1 
ATOM   4952 N N   . LYS C 1 180 ? 22.295  -36.924  46.557  1.00 63.19  ? 171 LYS C N   1 
ATOM   4953 C CA  . LYS C 1 180 ? 22.873  -37.305  45.279  1.00 63.47  ? 171 LYS C CA  1 
ATOM   4954 C C   . LYS C 1 180 ? 22.068  -36.815  44.079  1.00 64.39  ? 171 LYS C C   1 
ATOM   4955 O O   . LYS C 1 180 ? 20.995  -36.204  44.216  1.00 61.31  ? 171 LYS C O   1 
ATOM   4956 C CB  . LYS C 1 180 ? 23.060  -38.825  45.181  1.00 65.53  ? 171 LYS C CB  1 
ATOM   4957 C CG  . LYS C 1 180 ? 23.035  -39.582  46.506  1.00 64.45  ? 171 LYS C CG  1 
ATOM   4958 C CD  . LYS C 1 180 ? 21.605  -39.925  46.917  1.00 63.43  ? 171 LYS C CD  1 
ATOM   4959 C CE  . LYS C 1 180 ? 21.569  -41.044  47.945  1.00 66.93  ? 171 LYS C CE  1 
ATOM   4960 N NZ  . LYS C 1 180 ? 20.775  -40.679  49.154  1.00 64.89  ? 171 LYS C NZ  1 
ATOM   4961 N N   . GLU C 1 181 ? 22.605  -37.100  42.897  1.00 63.51  ? 172 GLU C N   1 
ATOM   4962 C CA  . GLU C 1 181 ? 21.915  -36.805  41.657  1.00 63.49  ? 172 GLU C CA  1 
ATOM   4963 C C   . GLU C 1 181 ? 20.812  -37.834  41.476  1.00 61.40  ? 172 GLU C C   1 
ATOM   4964 O O   . GLU C 1 181 ? 20.952  -38.998  41.878  1.00 61.97  ? 172 GLU C O   1 
ATOM   4965 C CB  . GLU C 1 181 ? 22.887  -36.856  40.486  1.00 62.17  ? 172 GLU C CB  1 
ATOM   4966 C CG  . GLU C 1 181 ? 23.737  -38.112  40.488  1.00 67.53  ? 172 GLU C CG  1 
ATOM   4967 C CD  . GLU C 1 181 ? 24.743  -38.168  39.340  1.00 72.45  ? 172 GLU C CD  1 
ATOM   4968 O OE1 . GLU C 1 181 ? 25.219  -39.287  39.045  1.00 71.80  ? 172 GLU C OE1 1 
ATOM   4969 O OE2 . GLU C 1 181 ? 25.063  -37.106  38.744  1.00 71.34  ? 172 GLU C OE2 1 
ATOM   4970 N N   . VAL C 1 182 ? 19.708  -37.400  40.882  1.00 57.43  ? 173 VAL C N   1 
ATOM   4971 C CA  . VAL C 1 182 ? 18.579  -38.289  40.667  1.00 56.80  ? 173 VAL C CA  1 
ATOM   4972 C C   . VAL C 1 182 ? 18.409  -38.647  39.184  1.00 55.07  ? 173 VAL C C   1 
ATOM   4973 O O   . VAL C 1 182 ? 18.426  -37.780  38.300  1.00 55.06  ? 173 VAL C O   1 
ATOM   4974 C CB  . VAL C 1 182 ? 17.266  -37.683  41.214  1.00 55.44  ? 173 VAL C CB  1 
ATOM   4975 C CG1 . VAL C 1 182 ? 16.115  -38.671  41.032  1.00 51.45  ? 173 VAL C CG1 1 
ATOM   4976 C CG2 . VAL C 1 182 ? 17.430  -37.295  42.673  1.00 56.15  ? 173 VAL C CG2 1 
ATOM   4977 N N   . LEU C 1 183 ? 18.260  -39.937  38.918  1.00 50.58  ? 174 LEU C N   1 
ATOM   4978 C CA  . LEU C 1 183 ? 17.972  -40.394  37.576  1.00 46.96  ? 174 LEU C CA  1 
ATOM   4979 C C   . LEU C 1 183 ? 16.495  -40.250  37.310  1.00 46.82  ? 174 LEU C C   1 
ATOM   4980 O O   . LEU C 1 183 ? 15.668  -40.881  37.953  1.00 48.63  ? 174 LEU C O   1 
ATOM   4981 C CB  . LEU C 1 183 ? 18.368  -41.855  37.420  1.00 48.02  ? 174 LEU C CB  1 
ATOM   4982 C CG  . LEU C 1 183 ? 17.880  -42.500  36.130  1.00 43.25  ? 174 LEU C CG  1 
ATOM   4983 C CD1 . LEU C 1 183 ? 18.295  -41.642  34.971  1.00 46.34  ? 174 LEU C CD1 1 
ATOM   4984 C CD2 . LEU C 1 183 ? 18.440  -43.900  36.005  1.00 49.36  ? 174 LEU C CD2 1 
ATOM   4985 N N   . VAL C 1 184 ? 16.158  -39.438  36.329  1.00 47.05  ? 175 VAL C N   1 
ATOM   4986 C CA  . VAL C 1 184 ? 14.771  -39.160  36.045  1.00 47.33  ? 175 VAL C CA  1 
ATOM   4987 C C   . VAL C 1 184 ? 14.482  -39.662  34.626  1.00 47.58  ? 175 VAL C C   1 
ATOM   4988 O O   . VAL C 1 184 ? 15.260  -39.401  33.704  1.00 46.39  ? 175 VAL C O   1 
ATOM   4989 C CB  . VAL C 1 184 ? 14.501  -37.650  36.174  1.00 48.80  ? 175 VAL C CB  1 
ATOM   4990 C CG1 . VAL C 1 184 ? 13.048  -37.325  35.859  1.00 45.21  ? 175 VAL C CG1 1 
ATOM   4991 C CG2 . VAL C 1 184 ? 14.897  -37.169  37.559  1.00 48.34  ? 175 VAL C CG2 1 
ATOM   4992 N N   . LEU C 1 185 ? 13.373  -40.388  34.464  1.00 47.53  ? 176 LEU C N   1 
ATOM   4993 C CA  . LEU C 1 185 ? 13.007  -40.992  33.180  1.00 46.35  ? 176 LEU C CA  1 
ATOM   4994 C C   . LEU C 1 185 ? 11.560  -40.715  32.768  1.00 44.29  ? 176 LEU C C   1 
ATOM   4995 O O   . LEU C 1 185 ? 10.652  -40.771  33.590  1.00 44.87  ? 176 LEU C O   1 
ATOM   4996 C CB  . LEU C 1 185 ? 13.226  -42.504  33.220  1.00 43.08  ? 176 LEU C CB  1 
ATOM   4997 C CG  . LEU C 1 185 ? 14.628  -42.992  33.560  1.00 43.63  ? 176 LEU C CG  1 
ATOM   4998 C CD1 . LEU C 1 185 ? 14.690  -43.508  34.992  1.00 43.47  ? 176 LEU C CD1 1 
ATOM   4999 C CD2 . LEU C 1 185 ? 15.053  -44.082  32.590  1.00 45.83  ? 176 LEU C CD2 1 
ATOM   5000 N N   . TRP C 1 186 ? 11.336  -40.441  31.490  1.00 42.48  ? 177 TRP C N   1 
ATOM   5001 C CA  . TRP C 1 186 ? 9.971   -40.240  31.014  1.00 44.06  ? 177 TRP C CA  1 
ATOM   5002 C C   . TRP C 1 186 ? 9.845   -40.800  29.621  1.00 43.95  ? 177 TRP C C   1 
ATOM   5003 O O   . TRP C 1 186 ? 10.793  -41.377  29.110  1.00 44.29  ? 177 TRP C O   1 
ATOM   5004 C CB  . TRP C 1 186 ? 9.612   -38.765  31.007  1.00 43.33  ? 177 TRP C CB  1 
ATOM   5005 C CG  . TRP C 1 186 ? 10.448  -37.985  30.068  1.00 45.20  ? 177 TRP C CG  1 
ATOM   5006 C CD1 . TRP C 1 186 ? 10.111  -37.587  28.820  1.00 44.02  ? 177 TRP C CD1 1 
ATOM   5007 C CD2 . TRP C 1 186 ? 11.789  -37.523  30.293  1.00 47.17  ? 177 TRP C CD2 1 
ATOM   5008 N NE1 . TRP C 1 186 ? 11.150  -36.890  28.254  1.00 46.59  ? 177 TRP C NE1 1 
ATOM   5009 C CE2 . TRP C 1 186 ? 12.191  -36.837  29.143  1.00 47.35  ? 177 TRP C CE2 1 
ATOM   5010 C CE3 . TRP C 1 186 ? 12.676  -37.614  31.364  1.00 46.25  ? 177 TRP C CE3 1 
ATOM   5011 C CZ2 . TRP C 1 186 ? 13.446  -36.247  29.033  1.00 48.57  ? 177 TRP C CZ2 1 
ATOM   5012 C CZ3 . TRP C 1 186 ? 13.915  -37.037  31.245  1.00 46.27  ? 177 TRP C CZ3 1 
ATOM   5013 C CH2 . TRP C 1 186 ? 14.290  -36.365  30.096  1.00 45.61  ? 177 TRP C CH2 1 
ATOM   5014 N N   . GLY C 1 187 ? 8.689   -40.607  28.994  1.00 44.15  ? 178 GLY C N   1 
ATOM   5015 C CA  . GLY C 1 187 ? 8.446   -41.163  27.675  1.00 41.58  ? 178 GLY C CA  1 
ATOM   5016 C C   . GLY C 1 187 ? 7.546   -40.291  26.820  1.00 44.22  ? 178 GLY C C   1 
ATOM   5017 O O   . GLY C 1 187 ? 6.798   -39.458  27.344  1.00 46.42  ? 178 GLY C O   1 
ATOM   5018 N N   . ILE C 1 188 ? 7.620   -40.481  25.502  1.00 39.96  ? 179 ILE C N   1 
ATOM   5019 C CA  . ILE C 1 188 ? 6.874   -39.665  24.565  1.00 38.60  ? 179 ILE C CA  1 
ATOM   5020 C C   . ILE C 1 188 ? 6.076   -40.593  23.675  1.00 41.95  ? 179 ILE C C   1 
ATOM   5021 O O   . ILE C 1 188 ? 6.655   -41.475  23.034  1.00 42.68  ? 179 ILE C O   1 
ATOM   5022 C CB  . ILE C 1 188 ? 7.817   -38.875  23.661  1.00 43.38  ? 179 ILE C CB  1 
ATOM   5023 C CG1 . ILE C 1 188 ? 8.919   -38.169  24.475  1.00 44.98  ? 179 ILE C CG1 1 
ATOM   5024 C CG2 . ILE C 1 188 ? 7.015   -37.921  22.777  1.00 43.02  ? 179 ILE C CG2 1 
ATOM   5025 C CD1 . ILE C 1 188 ? 8.484   -36.907  25.186  1.00 43.80  ? 179 ILE C CD1 1 
ATOM   5026 N N   . HIS C 1 189 ? 4.758   -40.402  23.625  1.00 38.88  ? 180 HIS C N   1 
ATOM   5027 C CA  . HIS C 1 189 ? 3.929   -41.238  22.780  1.00 37.65  ? 180 HIS C CA  1 
ATOM   5028 C C   . HIS C 1 189 ? 3.736   -40.639  21.406  1.00 40.39  ? 180 HIS C C   1 
ATOM   5029 O O   . HIS C 1 189 ? 3.348   -39.488  21.276  1.00 43.23  ? 180 HIS C O   1 
ATOM   5030 C CB  . HIS C 1 189 ? 2.565   -41.519  23.407  1.00 38.82  ? 180 HIS C CB  1 
ATOM   5031 C CG  . HIS C 1 189 ? 1.788   -42.587  22.692  1.00 43.52  ? 180 HIS C CG  1 
ATOM   5032 N ND1 . HIS C 1 189 ? 0.460   -42.449  22.351  1.00 45.13  ? 180 HIS C ND1 1 
ATOM   5033 C CD2 . HIS C 1 189 ? 2.168   -43.806  22.230  1.00 41.88  ? 180 HIS C CD2 1 
ATOM   5034 C CE1 . HIS C 1 189 ? 0.052   -43.538  21.719  1.00 45.75  ? 180 HIS C CE1 1 
ATOM   5035 N NE2 . HIS C 1 189 ? 1.069   -44.377  21.633  1.00 42.68  ? 180 HIS C NE2 1 
ATOM   5036 N N   . HIS C 1 190 ? 4.009   -41.427  20.374  1.00 40.48  ? 181 HIS C N   1 
ATOM   5037 C CA  . HIS C 1 190 ? 3.638   -41.047  19.023  1.00 40.12  ? 181 HIS C CA  1 
ATOM   5038 C C   . HIS C 1 190 ? 2.532   -41.984  18.526  1.00 40.70  ? 181 HIS C C   1 
ATOM   5039 O O   . HIS C 1 190 ? 2.776   -43.159  18.226  1.00 39.67  ? 181 HIS C O   1 
ATOM   5040 C CB  . HIS C 1 190 ? 4.842   -41.133  18.099  1.00 40.14  ? 181 HIS C CB  1 
ATOM   5041 C CG  . HIS C 1 190 ? 6.010   -40.307  18.539  1.00 41.65  ? 181 HIS C CG  1 
ATOM   5042 N ND1 . HIS C 1 190 ? 6.183   -38.994  18.154  1.00 42.87  ? 181 HIS C ND1 1 
ATOM   5043 C CD2 . HIS C 1 190 ? 7.080   -40.616  19.306  1.00 43.13  ? 181 HIS C CD2 1 
ATOM   5044 C CE1 . HIS C 1 190 ? 7.303   -38.528  18.673  1.00 43.61  ? 181 HIS C CE1 1 
ATOM   5045 N NE2 . HIS C 1 190 ? 7.870   -39.493  19.377  1.00 45.44  ? 181 HIS C NE2 1 
ATOM   5046 N N   . PRO C 1 191 ? 1.303   -41.468  18.433  1.00 39.73  ? 182 PRO C N   1 
ATOM   5047 C CA  . PRO C 1 191 ? 0.209   -42.336  18.018  1.00 41.84  ? 182 PRO C CA  1 
ATOM   5048 C C   . PRO C 1 191 ? 0.315   -42.650  16.534  1.00 43.05  ? 182 PRO C C   1 
ATOM   5049 O O   . PRO C 1 191 ? 1.030   -41.962  15.792  1.00 40.78  ? 182 PRO C O   1 
ATOM   5050 C CB  . PRO C 1 191 ? -1.039  -41.489  18.310  1.00 43.37  ? 182 PRO C CB  1 
ATOM   5051 C CG  . PRO C 1 191 ? -0.576  -40.403  19.238  1.00 42.58  ? 182 PRO C CG  1 
ATOM   5052 C CD  . PRO C 1 191 ? 0.825   -40.128  18.800  1.00 43.19  ? 182 PRO C CD  1 
ATOM   5053 N N   . SER C 1 192 ? -0.400  -43.688  16.121  1.00 41.69  ? 183 SER C N   1 
ATOM   5054 C CA  . SER C 1 192 ? -0.393  -44.131  14.748  1.00 41.23  ? 183 SER C CA  1 
ATOM   5055 C C   . SER C 1 192 ? -1.171  -43.163  13.863  1.00 42.68  ? 183 SER C C   1 
ATOM   5056 O O   . SER C 1 192 ? -0.809  -42.945  12.702  1.00 41.39  ? 183 SER C O   1 
ATOM   5057 C CB  . SER C 1 192 ? -1.005  -45.517  14.674  1.00 42.69  ? 183 SER C CB  1 
ATOM   5058 O OG  . SER C 1 192 ? -2.280  -45.496  15.278  1.00 46.36  ? 183 SER C OG  1 
ATOM   5059 N N   . THR C 1 193 ? -2.231  -42.578  14.419  1.00 43.47  ? 184 THR C N   1 
ATOM   5060 C CA  . THR C 1 193 ? -3.122  -41.723  13.642  1.00 42.37  ? 184 THR C CA  1 
ATOM   5061 C C   . THR C 1 193 ? -3.533  -40.451  14.372  1.00 44.95  ? 184 THR C C   1 
ATOM   5062 O O   . THR C 1 193 ? -3.250  -40.267  15.556  1.00 46.05  ? 184 THR C O   1 
ATOM   5063 C CB  . THR C 1 193 ? -4.438  -42.431  13.376  1.00 42.87  ? 184 THR C CB  1 
ATOM   5064 O OG1 . THR C 1 193 ? -5.180  -42.509  14.609  1.00 41.27  ? 184 THR C OG1 1 
ATOM   5065 C CG2 . THR C 1 193 ? -4.191  -43.817  12.833  1.00 38.58  ? 184 THR C CG2 1 
ATOM   5066 N N   . SER C 1 194 ? -4.268  -39.601  13.667  1.00 44.51  ? 185 SER C N   1 
ATOM   5067 C CA  . SER C 1 194 ? -4.793  -38.389  14.263  1.00 45.44  ? 185 SER C CA  1 
ATOM   5068 C C   . SER C 1 194 ? -5.988  -38.720  15.136  1.00 45.82  ? 185 SER C C   1 
ATOM   5069 O O   . SER C 1 194 ? -6.233  -38.063  16.151  1.00 47.06  ? 185 SER C O   1 
ATOM   5070 C CB  . SER C 1 194 ? -5.165  -37.376  13.186  1.00 48.80  ? 185 SER C CB  1 
ATOM   5071 O OG  . SER C 1 194 ? -4.125  -36.426  13.035  1.00 48.48  ? 185 SER C OG  1 
ATOM   5072 N N   . ALA C 1 195 ? -6.738  -39.740  14.743  1.00 44.01  ? 186 ALA C N   1 
ATOM   5073 C CA  . ALA C 1 195 ? -7.838  -40.192  15.576  1.00 42.67  ? 186 ALA C CA  1 
ATOM   5074 C C   . ALA C 1 195 ? -7.272  -40.661  16.914  1.00 45.32  ? 186 ALA C C   1 
ATOM   5075 O O   . ALA C 1 195 ? -7.762  -40.295  17.980  1.00 44.19  ? 186 ALA C O   1 
ATOM   5076 C CB  . ALA C 1 195 ? -8.560  -41.301  14.907  1.00 39.65  ? 186 ALA C CB  1 
ATOM   5077 N N   . ASP C 1 196 ? -6.226  -41.474  16.848  1.00 45.30  ? 187 ASP C N   1 
ATOM   5078 C CA  . ASP C 1 196 ? -5.556  -41.920  18.053  1.00 45.34  ? 187 ASP C CA  1 
ATOM   5079 C C   . ASP C 1 196 ? -5.143  -40.710  18.870  1.00 45.30  ? 187 ASP C C   1 
ATOM   5080 O O   . ASP C 1 196 ? -5.495  -40.601  20.037  1.00 45.79  ? 187 ASP C O   1 
ATOM   5081 C CB  . ASP C 1 196 ? -4.321  -42.743  17.703  1.00 48.37  ? 187 ASP C CB  1 
ATOM   5082 C CG  . ASP C 1 196 ? -4.211  -43.991  18.538  1.00 51.08  ? 187 ASP C CG  1 
ATOM   5083 O OD1 . ASP C 1 196 ? -5.260  -44.645  18.731  1.00 53.00  ? 187 ASP C OD1 1 
ATOM   5084 O OD2 . ASP C 1 196 ? -3.089  -44.324  18.988  1.00 50.39  ? 187 ASP C OD2 1 
ATOM   5085 N N   . GLN C 1 197 ? -4.431  -39.779  18.241  1.00 44.72  ? 188 GLN C N   1 
ATOM   5086 C CA  . GLN C 1 197 ? -3.946  -38.604  18.945  1.00 43.18  ? 188 GLN C CA  1 
ATOM   5087 C C   . GLN C 1 197 ? -5.076  -37.923  19.650  1.00 46.85  ? 188 GLN C C   1 
ATOM   5088 O O   . GLN C 1 197 ? -5.028  -37.710  20.853  1.00 48.90  ? 188 GLN C O   1 
ATOM   5089 C CB  . GLN C 1 197 ? -3.365  -37.593  17.982  1.00 41.94  ? 188 GLN C CB  1 
ATOM   5090 C CG  . GLN C 1 197 ? -3.135  -36.253  18.642  1.00 44.29  ? 188 GLN C CG  1 
ATOM   5091 C CD  . GLN C 1 197 ? -2.013  -36.313  19.650  1.00 47.09  ? 188 GLN C CD  1 
ATOM   5092 O OE1 . GLN C 1 197 ? -1.248  -37.272  19.684  1.00 44.96  ? 188 GLN C OE1 1 
ATOM   5093 N NE2 . GLN C 1 197 ? -1.907  -35.288  20.477  1.00 51.25  ? 188 GLN C NE2 1 
ATOM   5094 N N   . GLN C 1 198 ? -6.106  -37.582  18.890  1.00 48.59  ? 189 GLN C N   1 
ATOM   5095 C CA  . GLN C 1 198 ? -7.243  -36.869  19.458  1.00 52.80  ? 189 GLN C CA  1 
ATOM   5096 C C   . GLN C 1 198 ? -7.896  -37.668  20.581  1.00 50.43  ? 189 GLN C C   1 
ATOM   5097 O O   . GLN C 1 198 ? -8.367  -37.107  21.569  1.00 52.36  ? 189 GLN C O   1 
ATOM   5098 C CB  . GLN C 1 198 ? -8.254  -36.506  18.360  1.00 54.12  ? 189 GLN C CB  1 
ATOM   5099 C CG  . GLN C 1 198 ? -9.684  -36.251  18.838  1.00 54.23  ? 189 GLN C CG  1 
ATOM   5100 C CD  . GLN C 1 198 ? -10.442 -37.551  19.096  1.00 60.62  ? 189 GLN C CD  1 
ATOM   5101 O OE1 . GLN C 1 198 ? -9.942  -38.646  18.798  1.00 58.19  ? 189 GLN C OE1 1 
ATOM   5102 N NE2 . GLN C 1 198 ? -11.653 -37.440  19.653  1.00 56.64  ? 189 GLN C NE2 1 
ATOM   5103 N N   . SER C 1 199 ? -7.909  -38.984  20.438  1.00 47.38  ? 190 SER C N   1 
ATOM   5104 C CA  . SER C 1 199 ? -8.550  -39.805  21.444  1.00 48.73  ? 190 SER C CA  1 
ATOM   5105 C C   . SER C 1 199 ? -7.867  -39.695  22.801  1.00 50.99  ? 190 SER C C   1 
ATOM   5106 O O   . SER C 1 199 ? -8.520  -39.499  23.817  1.00 54.50  ? 190 SER C O   1 
ATOM   5107 C CB  . SER C 1 199 ? -8.561  -41.263  21.025  1.00 50.65  ? 190 SER C CB  1 
ATOM   5108 O OG  . SER C 1 199 ? -8.782  -42.061  22.173  1.00 50.98  ? 190 SER C OG  1 
ATOM   5109 N N   . LEU C 1 200 ? -6.550  -39.831  22.819  1.00 48.41  ? 191 LEU C N   1 
ATOM   5110 C CA  . LEU C 1 200 ? -5.820  -39.828  24.071  1.00 46.79  ? 191 LEU C CA  1 
ATOM   5111 C C   . LEU C 1 200 ? -5.746  -38.430  24.667  1.00 47.26  ? 191 LEU C C   1 
ATOM   5112 O O   . LEU C 1 200 ? -6.222  -38.206  25.769  1.00 51.45  ? 191 LEU C O   1 
ATOM   5113 C CB  . LEU C 1 200 ? -4.416  -40.404  23.875  1.00 48.50  ? 191 LEU C CB  1 
ATOM   5114 C CG  . LEU C 1 200 ? -4.407  -41.776  23.188  1.00 47.82  ? 191 LEU C CG  1 
ATOM   5115 C CD1 . LEU C 1 200 ? -2.993  -42.377  23.085  1.00 45.17  ? 191 LEU C CD1 1 
ATOM   5116 C CD2 . LEU C 1 200 ? -5.340  -42.724  23.909  1.00 41.59  ? 191 LEU C CD2 1 
ATOM   5117 N N   . TYR C 1 201 ? -5.112  -37.508  23.958  1.00 46.01  ? 192 TYR C N   1 
ATOM   5118 C CA  . TYR C 1 201 ? -4.826  -36.184  24.494  1.00 45.81  ? 192 TYR C CA  1 
ATOM   5119 C C   . TYR C 1 201 ? -5.765  -35.056  24.058  1.00 48.41  ? 192 TYR C C   1 
ATOM   5120 O O   . TYR C 1 201 ? -5.606  -33.910  24.467  1.00 49.64  ? 192 TYR C O   1 
ATOM   5121 C CB  . TYR C 1 201 ? -3.383  -35.868  24.157  1.00 47.09  ? 192 TYR C CB  1 
ATOM   5122 C CG  . TYR C 1 201 ? -2.574  -37.141  24.175  1.00 46.24  ? 192 TYR C CG  1 
ATOM   5123 C CD1 . TYR C 1 201 ? -2.370  -37.824  25.363  1.00 45.85  ? 192 TYR C CD1 1 
ATOM   5124 C CD2 . TYR C 1 201 ? -2.062  -37.689  23.011  1.00 45.37  ? 192 TYR C CD2 1 
ATOM   5125 C CE1 . TYR C 1 201 ? -1.651  -38.991  25.404  1.00 46.06  ? 192 TYR C CE1 1 
ATOM   5126 C CE2 . TYR C 1 201 ? -1.339  -38.873  23.041  1.00 45.59  ? 192 TYR C CE2 1 
ATOM   5127 C CZ  . TYR C 1 201 ? -1.135  -39.518  24.246  1.00 46.45  ? 192 TYR C CZ  1 
ATOM   5128 O OH  . TYR C 1 201 ? -0.413  -40.694  24.321  1.00 44.64  ? 192 TYR C OH  1 
ATOM   5129 N N   . GLN C 1 202 ? -6.710  -35.381  23.188  1.00 51.95  ? 193 GLN C N   1 
ATOM   5130 C CA  . GLN C 1 202 ? -7.712  -34.430  22.696  1.00 52.88  ? 193 GLN C CA  1 
ATOM   5131 C C   . GLN C 1 202 ? -7.136  -33.303  21.844  1.00 54.67  ? 193 GLN C C   1 
ATOM   5132 O O   . GLN C 1 202 ? -7.848  -32.688  21.049  1.00 57.67  ? 193 GLN C O   1 
ATOM   5133 C CB  . GLN C 1 202 ? -8.483  -33.813  23.860  1.00 52.75  ? 193 GLN C CB  1 
ATOM   5134 C CG  . GLN C 1 202 ? -9.481  -32.753  23.450  1.00 53.28  ? 193 GLN C CG  1 
ATOM   5135 C CD  . GLN C 1 202 ? -10.606 -33.325  22.618  1.00 58.90  ? 193 GLN C CD  1 
ATOM   5136 O OE1 . GLN C 1 202 ? -10.645 -33.150  21.393  1.00 59.64  ? 193 GLN C OE1 1 
ATOM   5137 N NE2 . GLN C 1 202 ? -11.536 -34.020  23.278  1.00 58.86  ? 193 GLN C NE2 1 
ATOM   5138 N N   . ASN C 1 203 ? -5.833  -33.084  21.956  1.00 54.66  ? 194 ASN C N   1 
ATOM   5139 C CA  . ASN C 1 203 ? -5.195  -31.947  21.315  1.00 54.19  ? 194 ASN C CA  1 
ATOM   5140 C C   . ASN C 1 203 ? -4.309  -32.395  20.157  1.00 54.06  ? 194 ASN C C   1 
ATOM   5141 O O   . ASN C 1 203 ? -3.349  -33.141  20.355  1.00 53.56  ? 194 ASN C O   1 
ATOM   5142 C CB  . ASN C 1 203 ? -4.378  -31.165  22.347  1.00 52.66  ? 194 ASN C CB  1 
ATOM   5143 C CG  . ASN C 1 203 ? -5.205  -30.730  23.537  1.00 53.57  ? 194 ASN C CG  1 
ATOM   5144 O OD1 . ASN C 1 203 ? -6.397  -30.452  23.412  1.00 53.90  ? 194 ASN C OD1 1 
ATOM   5145 N ND2 . ASN C 1 203 ? -4.574  -30.654  24.697  1.00 52.03  ? 194 ASN C ND2 1 
ATOM   5146 N N   . ALA C 1 204 ? -4.631  -31.939  18.952  1.00 54.31  ? 195 ALA C N   1 
ATOM   5147 C CA  . ALA C 1 204 ? -3.869  -32.316  17.766  1.00 54.66  ? 195 ALA C CA  1 
ATOM   5148 C C   . ALA C 1 204 ? -2.492  -31.669  17.778  1.00 56.28  ? 195 ALA C C   1 
ATOM   5149 O O   . ALA C 1 204 ? -1.522  -32.200  17.239  1.00 60.21  ? 195 ALA C O   1 
ATOM   5150 C CB  . ALA C 1 204 ? -4.622  -31.904  16.522  1.00 52.70  ? 195 ALA C CB  1 
ATOM   5151 N N   . ASP C 1 205 ? -2.427  -30.516  18.420  1.00 55.54  ? 196 ASP C N   1 
ATOM   5152 C CA  . ASP C 1 205 ? -1.260  -29.655  18.394  1.00 57.42  ? 196 ASP C CA  1 
ATOM   5153 C C   . ASP C 1 205 ? -0.316  -29.944  19.545  1.00 60.72  ? 196 ASP C C   1 
ATOM   5154 O O   . ASP C 1 205 ? 0.668   -29.223  19.737  1.00 61.39  ? 196 ASP C O   1 
ATOM   5155 C CB  . ASP C 1 205 ? -1.743  -28.227  18.535  1.00 61.44  ? 196 ASP C CB  1 
ATOM   5156 C CG  . ASP C 1 205 ? -2.779  -28.092  19.627  1.00 65.14  ? 196 ASP C CG  1 
ATOM   5157 O OD1 . ASP C 1 205 ? -3.131  -29.134  20.233  1.00 62.53  ? 196 ASP C OD1 1 
ATOM   5158 O OD2 . ASP C 1 205 ? -3.250  -26.963  19.875  1.00 73.63  ? 196 ASP C OD2 1 
ATOM   5159 N N   . ALA C 1 206 ? -0.625  -30.983  20.318  1.00 57.45  ? 197 ALA C N   1 
ATOM   5160 C CA  . ALA C 1 206 ? 0.080   -31.236  21.566  1.00 50.91  ? 197 ALA C CA  1 
ATOM   5161 C C   . ALA C 1 206 ? 1.594   -31.202  21.393  1.00 53.85  ? 197 ALA C C   1 
ATOM   5162 O O   . ALA C 1 206 ? 2.136   -31.737  20.428  1.00 60.61  ? 197 ALA C O   1 
ATOM   5163 C CB  . ALA C 1 206 ? -0.349  -32.569  22.153  1.00 50.73  ? 197 ALA C CB  1 
ATOM   5164 N N   . TYR C 1 207 ? 2.264   -30.548  22.336  1.00 54.31  ? 198 TYR C N   1 
ATOM   5165 C CA  . TYR C 1 207 ? 3.716   -30.549  22.432  1.00 54.10  ? 198 TYR C CA  1 
ATOM   5166 C C   . TYR C 1 207 ? 4.103   -30.930  23.854  1.00 52.88  ? 198 TYR C C   1 
ATOM   5167 O O   . TYR C 1 207 ? 3.256   -31.067  24.739  1.00 51.51  ? 198 TYR C O   1 
ATOM   5168 C CB  . TYR C 1 207 ? 4.263   -29.149  22.185  1.00 58.75  ? 198 TYR C CB  1 
ATOM   5169 C CG  . TYR C 1 207 ? 3.946   -28.238  23.348  1.00 61.01  ? 198 TYR C CG  1 
ATOM   5170 C CD1 . TYR C 1 207 ? 2.686   -27.660  23.468  1.00 61.16  ? 198 TYR C CD1 1 
ATOM   5171 C CD2 . TYR C 1 207 ? 4.878   -27.998  24.356  1.00 61.04  ? 198 TYR C CD2 1 
ATOM   5172 C CE1 . TYR C 1 207 ? 2.368   -26.849  24.536  1.00 60.74  ? 198 TYR C CE1 1 
ATOM   5173 C CE2 . TYR C 1 207 ? 4.564   -27.180  25.437  1.00 63.31  ? 198 TYR C CE2 1 
ATOM   5174 C CZ  . TYR C 1 207 ? 3.303   -26.609  25.516  1.00 64.43  ? 198 TYR C CZ  1 
ATOM   5175 O OH  . TYR C 1 207 ? 2.969   -25.796  26.579  1.00 70.12  ? 198 TYR C OH  1 
ATOM   5176 N N   . VAL C 1 208 ? 5.399   -31.058  24.085  1.00 52.46  ? 199 VAL C N   1 
ATOM   5177 C CA  . VAL C 1 208 ? 5.879   -31.485  25.382  1.00 51.36  ? 199 VAL C CA  1 
ATOM   5178 C C   . VAL C 1 208 ? 7.239   -30.906  25.668  1.00 52.62  ? 199 VAL C C   1 
ATOM   5179 O O   . VAL C 1 208 ? 8.067   -30.787  24.771  1.00 54.10  ? 199 VAL C O   1 
ATOM   5180 C CB  . VAL C 1 208 ? 6.005   -32.999  25.452  1.00 51.48  ? 199 VAL C CB  1 
ATOM   5181 C CG1 . VAL C 1 208 ? 6.758   -33.385  26.706  1.00 50.84  ? 199 VAL C CG1 1 
ATOM   5182 C CG2 . VAL C 1 208 ? 4.633   -33.638  25.416  1.00 49.48  ? 199 VAL C CG2 1 
ATOM   5183 N N   . PHE C 1 209 ? 7.489   -30.560  26.923  1.00 55.83  ? 200 PHE C N   1 
ATOM   5184 C CA  . PHE C 1 209 ? 8.758   -29.939  27.255  1.00 55.21  ? 200 PHE C CA  1 
ATOM   5185 C C   . PHE C 1 209 ? 9.310   -30.338  28.618  1.00 55.71  ? 200 PHE C C   1 
ATOM   5186 O O   . PHE C 1 209 ? 8.567   -30.528  29.576  1.00 55.46  ? 200 PHE C O   1 
ATOM   5187 C CB  . PHE C 1 209 ? 8.660   -28.421  27.179  1.00 54.40  ? 200 PHE C CB  1 
ATOM   5188 C CG  . PHE C 1 209 ? 9.865   -27.741  27.727  1.00 57.81  ? 200 PHE C CG  1 
ATOM   5189 C CD1 . PHE C 1 209 ? 10.016  -27.588  29.105  1.00 57.87  ? 200 PHE C CD1 1 
ATOM   5190 C CD2 . PHE C 1 209 ? 10.872  -27.301  26.882  1.00 55.25  ? 200 PHE C CD2 1 
ATOM   5191 C CE1 . PHE C 1 209 ? 11.137  -26.989  29.631  1.00 56.50  ? 200 PHE C CE1 1 
ATOM   5192 C CE2 . PHE C 1 209 ? 12.000  -26.698  27.395  1.00 56.16  ? 200 PHE C CE2 1 
ATOM   5193 C CZ  . PHE C 1 209 ? 12.135  -26.539  28.773  1.00 59.62  ? 200 PHE C CZ  1 
ATOM   5194 N N   . VAL C 1 210 ? 10.634  -30.438  28.689  1.00 56.93  ? 201 VAL C N   1 
ATOM   5195 C CA  . VAL C 1 210 ? 11.335  -30.808  29.910  1.00 53.45  ? 201 VAL C CA  1 
ATOM   5196 C C   . VAL C 1 210 ? 12.589  -29.967  30.037  1.00 55.72  ? 201 VAL C C   1 
ATOM   5197 O O   . VAL C 1 210 ? 13.376  -29.905  29.097  1.00 58.07  ? 201 VAL C O   1 
ATOM   5198 C CB  . VAL C 1 210 ? 11.772  -32.273  29.865  1.00 51.95  ? 201 VAL C CB  1 
ATOM   5199 C CG1 . VAL C 1 210 ? 12.618  -32.610  31.080  1.00 55.40  ? 201 VAL C CG1 1 
ATOM   5200 C CG2 . VAL C 1 210 ? 10.560  -33.192  29.773  1.00 51.49  ? 201 VAL C CG2 1 
ATOM   5201 N N   . GLY C 1 211 ? 12.798  -29.337  31.192  1.00 56.70  ? 202 GLY C N   1 
ATOM   5202 C CA  . GLY C 1 211 ? 13.920  -28.427  31.344  1.00 59.11  ? 202 GLY C CA  1 
ATOM   5203 C C   . GLY C 1 211 ? 14.525  -28.380  32.732  1.00 61.39  ? 202 GLY C C   1 
ATOM   5204 O O   . GLY C 1 211 ? 13.901  -28.803  33.712  1.00 58.64  ? 202 GLY C O   1 
ATOM   5205 N N   . SER C 1 212 ? 15.755  -27.866  32.790  1.00 62.97  ? 203 SER C N   1 
ATOM   5206 C CA  . SER C 1 212 ? 16.588  -27.862  33.990  1.00 63.72  ? 203 SER C CA  1 
ATOM   5207 C C   . SER C 1 212 ? 17.851  -27.036  33.729  1.00 66.39  ? 203 SER C C   1 
ATOM   5208 O O   . SER C 1 212 ? 17.980  -26.395  32.683  1.00 68.82  ? 203 SER C O   1 
ATOM   5209 C CB  . SER C 1 212 ? 16.987  -29.288  34.378  1.00 64.61  ? 203 SER C CB  1 
ATOM   5210 O OG  . SER C 1 212 ? 18.220  -29.651  33.777  1.00 66.15  ? 203 SER C OG  1 
ATOM   5211 N N   . SER C 1 213 ? 18.776  -27.032  34.687  1.00 69.06  ? 204 SER C N   1 
ATOM   5212 C CA  . SER C 1 213 ? 20.074  -26.406  34.461  1.00 67.51  ? 204 SER C CA  1 
ATOM   5213 C C   . SER C 1 213 ? 20.789  -27.136  33.348  1.00 64.78  ? 204 SER C C   1 
ATOM   5214 O O   . SER C 1 213 ? 21.181  -26.541  32.351  1.00 67.99  ? 204 SER C O   1 
ATOM   5215 C CB  . SER C 1 213 ? 20.952  -26.468  35.713  1.00 69.91  ? 204 SER C CB  1 
ATOM   5216 O OG  . SER C 1 213 ? 22.320  -26.664  35.355  1.00 69.15  ? 204 SER C OG  1 
ATOM   5217 N N   . ARG C 1 214 ? 20.939  -28.442  33.541  1.00 65.08  ? 205 ARG C N   1 
ATOM   5218 C CA  . ARG C 1 214 ? 21.798  -29.276  32.711  1.00 66.32  ? 205 ARG C CA  1 
ATOM   5219 C C   . ARG C 1 214 ? 21.071  -29.886  31.508  1.00 67.33  ? 205 ARG C C   1 
ATOM   5220 O O   . ARG C 1 214 ? 21.654  -30.670  30.757  1.00 65.41  ? 205 ARG C O   1 
ATOM   5221 C CB  . ARG C 1 214 ? 22.431  -30.378  33.576  1.00 67.79  ? 205 ARG C CB  1 
ATOM   5222 C CG  . ARG C 1 214 ? 23.378  -31.335  32.845  1.00 69.47  ? 205 ARG C CG  1 
ATOM   5223 C CD  . ARG C 1 214 ? 24.303  -32.089  33.832  1.00 71.05  ? 205 ARG C CD  1 
ATOM   5224 N NE  . ARG C 1 214 ? 23.613  -33.108  34.628  1.00 70.99  ? 205 ARG C NE  1 
ATOM   5225 C CZ  . ARG C 1 214 ? 23.999  -33.504  35.840  1.00 68.99  ? 205 ARG C CZ  1 
ATOM   5226 N NH1 . ARG C 1 214 ? 25.067  -32.962  36.412  1.00 70.58  ? 205 ARG C NH1 1 
ATOM   5227 N NH2 . ARG C 1 214 ? 23.311  -34.437  36.488  1.00 67.61  ? 205 ARG C NH2 1 
ATOM   5228 N N   . TYR C 1 215 ? 19.790  -29.560  31.348  1.00 66.33  ? 206 TYR C N   1 
ATOM   5229 C CA  . TYR C 1 215 ? 18.995  -30.132  30.265  1.00 63.95  ? 206 TYR C CA  1 
ATOM   5230 C C   . TYR C 1 215 ? 17.812  -29.234  29.880  1.00 63.99  ? 206 TYR C C   1 
ATOM   5231 O O   . TYR C 1 215 ? 17.207  -28.602  30.741  1.00 66.77  ? 206 TYR C O   1 
ATOM   5232 C CB  . TYR C 1 215 ? 18.500  -31.501  30.727  1.00 62.96  ? 206 TYR C CB  1 
ATOM   5233 C CG  . TYR C 1 215 ? 17.819  -32.365  29.693  1.00 64.14  ? 206 TYR C CG  1 
ATOM   5234 C CD1 . TYR C 1 215 ? 16.531  -32.082  29.255  1.00 60.27  ? 206 TYR C CD1 1 
ATOM   5235 C CD2 . TYR C 1 215 ? 18.441  -33.510  29.207  1.00 63.39  ? 206 TYR C CD2 1 
ATOM   5236 C CE1 . TYR C 1 215 ? 15.899  -32.898  28.329  1.00 60.81  ? 206 TYR C CE1 1 
ATOM   5237 C CE2 . TYR C 1 215 ? 17.821  -34.328  28.279  1.00 59.44  ? 206 TYR C CE2 1 
ATOM   5238 C CZ  . TYR C 1 215 ? 16.551  -34.020  27.842  1.00 61.21  ? 206 TYR C CZ  1 
ATOM   5239 O OH  . TYR C 1 215 ? 15.934  -34.838  26.915  1.00 60.29  ? 206 TYR C OH  1 
ATOM   5240 N N   . SER C 1 216 ? 17.497  -29.151  28.591  1.00 65.20  ? 207 SER C N   1 
ATOM   5241 C CA  . SER C 1 216 ? 16.181  -28.674  28.144  1.00 63.48  ? 207 SER C CA  1 
ATOM   5242 C C   . SER C 1 216 ? 15.851  -29.255  26.765  1.00 64.01  ? 207 SER C C   1 
ATOM   5243 O O   . SER C 1 216 ? 16.732  -29.350  25.904  1.00 62.59  ? 207 SER C O   1 
ATOM   5244 C CB  . SER C 1 216 ? 16.120  -27.145  28.106  1.00 60.30  ? 207 SER C CB  1 
ATOM   5245 O OG  . SER C 1 216 ? 17.084  -26.634  27.206  1.00 63.90  ? 207 SER C OG  1 
ATOM   5246 N N   . LYS C 1 217 ? 14.595  -29.642  26.550  1.00 59.84  ? 208 LYS C N   1 
ATOM   5247 C CA  . LYS C 1 217 ? 14.191  -30.193  25.257  1.00 56.87  ? 208 LYS C CA  1 
ATOM   5248 C C   . LYS C 1 217 ? 12.699  -30.026  25.010  1.00 55.65  ? 208 LYS C C   1 
ATOM   5249 O O   . LYS C 1 217 ? 11.899  -30.076  25.952  1.00 54.87  ? 208 LYS C O   1 
ATOM   5250 C CB  . LYS C 1 217 ? 14.587  -31.671  25.147  1.00 58.02  ? 208 LYS C CB  1 
ATOM   5251 C CG  . LYS C 1 217 ? 15.047  -32.093  23.740  1.00 66.95  ? 208 LYS C CG  1 
ATOM   5252 C CD  . LYS C 1 217 ? 16.591  -32.200  23.614  1.00 70.29  ? 208 LYS C CD  1 
ATOM   5253 C CE  . LYS C 1 217 ? 17.045  -32.498  22.163  1.00 63.67  ? 208 LYS C CE  1 
ATOM   5254 N NZ  . LYS C 1 217 ? 18.470  -32.968  22.058  1.00 53.47  ? 208 LYS C NZ  1 
ATOM   5255 N N   . LYS C 1 218 ? 12.328  -29.841  23.744  1.00 55.75  ? 209 LYS C N   1 
ATOM   5256 C CA  . LYS C 1 218 ? 10.921  -29.804  23.368  1.00 56.41  ? 209 LYS C CA  1 
ATOM   5257 C C   . LYS C 1 218 ? 10.574  -30.956  22.423  1.00 55.75  ? 209 LYS C C   1 
ATOM   5258 O O   . LYS C 1 218 ? 11.394  -31.381  21.614  1.00 55.72  ? 209 LYS C O   1 
ATOM   5259 C CB  . LYS C 1 218 ? 10.533  -28.457  22.756  1.00 55.39  ? 209 LYS C CB  1 
ATOM   5260 C CG  . LYS C 1 218 ? 9.013   -28.237  22.718  1.00 57.14  ? 209 LYS C CG  1 
ATOM   5261 C CD  . LYS C 1 218 ? 8.616   -26.915  22.055  1.00 63.18  ? 209 LYS C CD  1 
ATOM   5262 C CE  . LYS C 1 218 ? 7.107   -26.635  22.185  1.00 65.86  ? 209 LYS C CE  1 
ATOM   5263 N NZ  . LYS C 1 218 ? 6.655   -25.435  21.389  1.00 55.65  ? 209 LYS C NZ  1 
ATOM   5264 N N   . PHE C 1 219 ? 9.349   -31.456  22.536  1.00 54.53  ? 210 PHE C N   1 
ATOM   5265 C CA  . PHE C 1 219 ? 8.931   -32.626  21.783  1.00 53.95  ? 210 PHE C CA  1 
ATOM   5266 C C   . PHE C 1 219 ? 7.603   -32.387  21.073  1.00 55.44  ? 210 PHE C C   1 
ATOM   5267 O O   . PHE C 1 219 ? 6.696   -31.752  21.622  1.00 53.68  ? 210 PHE C O   1 
ATOM   5268 C CB  . PHE C 1 219 ? 8.770   -33.834  22.712  1.00 54.74  ? 210 PHE C CB  1 
ATOM   5269 C CG  . PHE C 1 219 ? 9.989   -34.145  23.541  1.00 55.75  ? 210 PHE C CG  1 
ATOM   5270 C CD1 . PHE C 1 219 ? 10.160  -33.566  24.780  1.00 53.19  ? 210 PHE C CD1 1 
ATOM   5271 C CD2 . PHE C 1 219 ? 10.949  -35.040  23.090  1.00 53.43  ? 210 PHE C CD2 1 
ATOM   5272 C CE1 . PHE C 1 219 ? 11.275  -33.859  25.541  1.00 53.80  ? 210 PHE C CE1 1 
ATOM   5273 C CE2 . PHE C 1 219 ? 12.063  -35.334  23.854  1.00 51.57  ? 210 PHE C CE2 1 
ATOM   5274 C CZ  . PHE C 1 219 ? 12.225  -34.744  25.073  1.00 52.13  ? 210 PHE C CZ  1 
ATOM   5275 N N   . LYS C 1 220 ? 7.490   -32.923  19.861  1.00 56.06  ? 211 LYS C N   1 
ATOM   5276 C CA  . LYS C 1 220 ? 6.230   -32.952  19.147  1.00 53.21  ? 211 LYS C CA  1 
ATOM   5277 C C   . LYS C 1 220 ? 5.956   -34.412  18.821  1.00 53.00  ? 211 LYS C C   1 
ATOM   5278 O O   . LYS C 1 220 ? 6.848   -35.137  18.376  1.00 53.30  ? 211 LYS C O   1 
ATOM   5279 C CB  . LYS C 1 220 ? 6.374   -32.176  17.835  1.00 58.86  ? 211 LYS C CB  1 
ATOM   5280 C CG  . LYS C 1 220 ? 5.259   -31.169  17.515  1.00 66.00  ? 211 LYS C CG  1 
ATOM   5281 C CD  . LYS C 1 220 ? 5.377   -29.882  18.357  1.00 62.86  ? 211 LYS C CD  1 
ATOM   5282 C CE  . LYS C 1 220 ? 4.405   -28.811  17.869  1.00 61.09  ? 211 LYS C CE  1 
ATOM   5283 N NZ  . LYS C 1 220 ? 4.369   -27.636  18.790  1.00 64.06  ? 211 LYS C NZ  1 
ATOM   5284 N N   . PRO C 1 221 ? 4.709   -34.846  18.995  1.00 49.37  ? 212 PRO C N   1 
ATOM   5285 C CA  . PRO C 1 221 ? 4.368   -36.211  18.606  1.00 46.51  ? 212 PRO C CA  1 
ATOM   5286 C C   . PRO C 1 221 ? 4.365   -36.300  17.091  1.00 48.97  ? 212 PRO C C   1 
ATOM   5287 O O   . PRO C 1 221 ? 3.902   -35.369  16.430  1.00 53.40  ? 212 PRO C O   1 
ATOM   5288 C CB  . PRO C 1 221 ? 2.942   -36.357  19.117  1.00 49.16  ? 212 PRO C CB  1 
ATOM   5289 C CG  . PRO C 1 221 ? 2.385   -34.966  18.999  1.00 52.82  ? 212 PRO C CG  1 
ATOM   5290 C CD  . PRO C 1 221 ? 3.528   -34.074  19.409  1.00 52.97  ? 212 PRO C CD  1 
ATOM   5291 N N   . GLU C 1 222 ? 4.885   -37.393  16.545  1.00 47.64  ? 213 GLU C N   1 
ATOM   5292 C CA  . GLU C 1 222 ? 4.809   -37.639  15.113  1.00 43.63  ? 213 GLU C CA  1 
ATOM   5293 C C   . GLU C 1 222 ? 3.768   -38.723  14.884  1.00 42.14  ? 213 GLU C C   1 
ATOM   5294 O O   . GLU C 1 222 ? 3.998   -39.902  15.183  1.00 41.21  ? 213 GLU C O   1 
ATOM   5295 C CB  . GLU C 1 222 ? 6.167   -38.089  14.594  1.00 41.45  ? 213 GLU C CB  1 
ATOM   5296 C CG  . GLU C 1 222 ? 6.276   -38.340  13.097  1.00 42.36  ? 213 GLU C CG  1 
ATOM   5297 C CD  . GLU C 1 222 ? 7.713   -38.719  12.713  1.00 50.59  ? 213 GLU C CD  1 
ATOM   5298 O OE1 . GLU C 1 222 ? 8.061   -38.646  11.506  1.00 48.28  ? 213 GLU C OE1 1 
ATOM   5299 O OE2 . GLU C 1 222 ? 8.504   -39.085  13.633  1.00 50.91  ? 213 GLU C OE2 1 
ATOM   5300 N N   . ILE C 1 223 ? 2.620   -38.317  14.354  1.00 39.28  ? 214 ILE C N   1 
ATOM   5301 C CA  . ILE C 1 223 ? 1.532   -39.249  14.129  1.00 40.38  ? 214 ILE C CA  1 
ATOM   5302 C C   . ILE C 1 223 ? 1.793   -39.968  12.834  1.00 38.39  ? 214 ILE C C   1 
ATOM   5303 O O   . ILE C 1 223 ? 1.855   -39.357  11.772  1.00 42.39  ? 214 ILE C O   1 
ATOM   5304 C CB  . ILE C 1 223 ? 0.197   -38.520  13.986  1.00 39.79  ? 214 ILE C CB  1 
ATOM   5305 C CG1 . ILE C 1 223 ? -0.301  -38.022  15.332  1.00 41.57  ? 214 ILE C CG1 1 
ATOM   5306 C CG2 . ILE C 1 223 ? -0.839  -39.429  13.396  1.00 39.69  ? 214 ILE C CG2 1 
ATOM   5307 C CD1 . ILE C 1 223 ? -1.610  -37.299  15.211  1.00 46.43  ? 214 ILE C CD1 1 
ATOM   5308 N N   . ALA C 1 224 ? 1.959   -41.273  12.904  1.00 37.14  ? 215 ALA C N   1 
ATOM   5309 C CA  . ALA C 1 224 ? 2.158   -42.017  11.680  1.00 36.84  ? 215 ALA C CA  1 
ATOM   5310 C C   . ALA C 1 224 ? 1.855   -43.464  11.944  1.00 36.49  ? 215 ALA C C   1 
ATOM   5311 O O   . ALA C 1 224 ? 1.911   -43.915  13.081  1.00 40.62  ? 215 ALA C O   1 
ATOM   5312 C CB  . ALA C 1 224 ? 3.565   -41.838  11.180  1.00 36.21  ? 215 ALA C CB  1 
ATOM   5313 N N   . ILE C 1 225 ? 1.557   -44.218  10.906  1.00 36.26  ? 216 ILE C N   1 
ATOM   5314 C CA  . ILE C 1 225 ? 1.308   -45.616  11.155  1.00 38.72  ? 216 ILE C CA  1 
ATOM   5315 C C   . ILE C 1 225 ? 2.590   -46.405  10.943  1.00 39.26  ? 216 ILE C C   1 
ATOM   5316 O O   . ILE C 1 225 ? 3.000   -46.677  9.810   1.00 39.35  ? 216 ILE C O   1 
ATOM   5317 C CB  . ILE C 1 225 ? 0.197   -46.141  10.245  1.00 38.65  ? 216 ILE C CB  1 
ATOM   5318 C CG1 . ILE C 1 225 ? -1.155  -45.673  10.772  1.00 40.86  ? 216 ILE C CG1 1 
ATOM   5319 C CG2 . ILE C 1 225 ? 0.223   -47.639  10.185  1.00 37.12  ? 216 ILE C CG2 1 
ATOM   5320 C CD1 . ILE C 1 225 ? -2.240  -45.712  9.735   1.00 37.33  ? 216 ILE C CD1 1 
ATOM   5321 N N   . ARG C 1 226 ? 3.189   -46.813  12.056  1.00 38.61  ? 217 ARG C N   1 
ATOM   5322 C CA  . ARG C 1 226 ? 4.382   -47.640  12.019  1.00 40.18  ? 217 ARG C CA  1 
ATOM   5323 C C   . ARG C 1 226 ? 3.908   -49.078  11.913  1.00 40.16  ? 217 ARG C C   1 
ATOM   5324 O O   . ARG C 1 226 ? 2.748   -49.369  12.192  1.00 42.94  ? 217 ARG C O   1 
ATOM   5325 C CB  . ARG C 1 226 ? 5.239   -47.447  13.284  1.00 40.65  ? 217 ARG C CB  1 
ATOM   5326 C CG  . ARG C 1 226 ? 5.926   -46.083  13.429  1.00 38.10  ? 217 ARG C CG  1 
ATOM   5327 C CD  . ARG C 1 226 ? 4.975   -44.973  13.869  1.00 35.74  ? 217 ARG C CD  1 
ATOM   5328 N NE  . ARG C 1 226 ? 5.733   -43.777  14.220  1.00 34.60  ? 217 ARG C NE  1 
ATOM   5329 C CZ  . ARG C 1 226 ? 5.209   -42.633  14.642  1.00 36.39  ? 217 ARG C CZ  1 
ATOM   5330 N NH1 . ARG C 1 226 ? 3.895   -42.501  14.780  1.00 38.23  ? 217 ARG C NH1 1 
ATOM   5331 N NH2 . ARG C 1 226 ? 6.014   -41.614  14.932  1.00 38.07  ? 217 ARG C NH2 1 
ATOM   5332 N N   . PRO C 1 227 ? 4.801   -49.985  11.504  1.00 39.99  ? 218 PRO C N   1 
ATOM   5333 C CA  . PRO C 1 227 ? 4.493   -51.417  11.403  1.00 40.13  ? 218 PRO C CA  1 
ATOM   5334 C C   . PRO C 1 227 ? 4.108   -52.021  12.760  1.00 43.04  ? 218 PRO C C   1 
ATOM   5335 O O   . PRO C 1 227 ? 4.757   -51.724  13.767  1.00 44.19  ? 218 PRO C O   1 
ATOM   5336 C CB  . PRO C 1 227 ? 5.813   -52.018  10.915  1.00 38.99  ? 218 PRO C CB  1 
ATOM   5337 C CG  . PRO C 1 227 ? 6.490   -50.895  10.179  1.00 38.97  ? 218 PRO C CG  1 
ATOM   5338 C CD  . PRO C 1 227 ? 6.129   -49.661  10.954  1.00 41.19  ? 218 PRO C CD  1 
ATOM   5339 N N   . LYS C 1 228 ? 3.065   -52.849  12.792  1.00 43.35  ? 219 LYS C N   1 
ATOM   5340 C CA  . LYS C 1 228 ? 2.635   -53.466  14.044  1.00 44.86  ? 219 LYS C CA  1 
ATOM   5341 C C   . LYS C 1 228 ? 3.738   -54.263  14.729  1.00 44.51  ? 219 LYS C C   1 
ATOM   5342 O O   . LYS C 1 228 ? 4.270   -55.218  14.168  1.00 45.15  ? 219 LYS C O   1 
ATOM   5343 C CB  . LYS C 1 228 ? 1.444   -54.397  13.798  1.00 47.78  ? 219 LYS C CB  1 
ATOM   5344 C CG  . LYS C 1 228 ? 0.099   -53.712  13.916  1.00 51.46  ? 219 LYS C CG  1 
ATOM   5345 C CD  . LYS C 1 228 ? -1.050  -54.684  13.744  1.00 54.60  ? 219 LYS C CD  1 
ATOM   5346 C CE  . LYS C 1 228 ? -2.366  -53.975  13.982  1.00 59.29  ? 219 LYS C CE  1 
ATOM   5347 N NZ  . LYS C 1 228 ? -3.477  -54.655  13.280  1.00 64.19  ? 219 LYS C NZ  1 
ATOM   5348 N N   . VAL C 1 229 ? 4.041   -53.892  15.967  1.00 45.96  ? 220 VAL C N   1 
ATOM   5349 C CA  . VAL C 1 229 ? 4.951   -54.665  16.808  1.00 47.51  ? 220 VAL C CA  1 
ATOM   5350 C C   . VAL C 1 229 ? 4.300   -54.856  18.178  1.00 47.97  ? 220 VAL C C   1 
ATOM   5351 O O   . VAL C 1 229 ? 3.822   -53.892  18.790  1.00 46.60  ? 220 VAL C O   1 
ATOM   5352 C CB  . VAL C 1 229 ? 6.332   -53.992  16.954  1.00 42.06  ? 220 VAL C CB  1 
ATOM   5353 C CG1 . VAL C 1 229 ? 7.129   -54.668  18.042  1.00 42.42  ? 220 VAL C CG1 1 
ATOM   5354 C CG2 . VAL C 1 229 ? 7.078   -54.044  15.653  1.00 37.65  ? 220 VAL C CG2 1 
ATOM   5355 N N   . ARG C 1 230 ? 4.258   -56.101  18.643  1.00 48.29  ? 221 ARG C N   1 
ATOM   5356 C CA  . ARG C 1 230 ? 3.482   -56.426  19.825  1.00 49.65  ? 221 ARG C CA  1 
ATOM   5357 C C   . ARG C 1 230 ? 2.122   -55.773  19.612  1.00 51.37  ? 221 ARG C C   1 
ATOM   5358 O O   . ARG C 1 230 ? 1.446   -55.353  20.553  1.00 51.28  ? 221 ARG C O   1 
ATOM   5359 C CB  . ARG C 1 230 ? 4.201   -55.956  21.081  1.00 47.79  ? 221 ARG C CB  1 
ATOM   5360 C CG  . ARG C 1 230 ? 5.447   -56.793  21.357  1.00 52.69  ? 221 ARG C CG  1 
ATOM   5361 C CD  . ARG C 1 230 ? 6.317   -56.239  22.479  1.00 55.42  ? 221 ARG C CD  1 
ATOM   5362 N NE  . ARG C 1 230 ? 5.698   -56.350  23.798  1.00 59.64  ? 221 ARG C NE  1 
ATOM   5363 C CZ  . ARG C 1 230 ? 5.729   -57.442  24.561  1.00 63.09  ? 221 ARG C CZ  1 
ATOM   5364 N NH1 . ARG C 1 230 ? 6.337   -58.543  24.129  1.00 66.04  ? 221 ARG C NH1 1 
ATOM   5365 N NH2 . ARG C 1 230 ? 5.142   -57.435  25.757  1.00 58.65  ? 221 ARG C NH2 1 
ATOM   5366 N N   . ASP C 1 231 ? 1.738   -55.738  18.337  1.00 48.53  ? 222 ASP C N   1 
ATOM   5367 C CA  . ASP C 1 231 ? 0.456   -55.224  17.880  1.00 52.93  ? 222 ASP C CA  1 
ATOM   5368 C C   . ASP C 1 231 ? 0.252   -53.708  18.019  1.00 53.95  ? 222 ASP C C   1 
ATOM   5369 O O   . ASP C 1 231 ? -0.887  -53.227  18.049  1.00 53.52  ? 222 ASP C O   1 
ATOM   5370 C CB  . ASP C 1 231 ? -0.676  -55.974  18.588  1.00 55.49  ? 222 ASP C CB  1 
ATOM   5371 C CG  . ASP C 1 231 ? -2.013  -55.777  17.910  1.00 60.17  ? 222 ASP C CG  1 
ATOM   5372 O OD1 . ASP C 1 231 ? -2.194  -56.310  16.792  1.00 66.68  ? 222 ASP C OD1 1 
ATOM   5373 O OD2 . ASP C 1 231 ? -2.884  -55.094  18.492  1.00 62.07  ? 222 ASP C OD2 1 
ATOM   5374 N N   . GLN C 1 232 ? 1.350   -52.955  18.046  1.00 50.69  ? 223 GLN C N   1 
ATOM   5375 C CA  . GLN C 1 232 ? 1.265   -51.503  18.149  1.00 45.63  ? 223 GLN C CA  1 
ATOM   5376 C C   . GLN C 1 232 ? 1.766   -50.819  16.872  1.00 43.93  ? 223 GLN C C   1 
ATOM   5377 O O   . GLN C 1 232 ? 2.844   -51.141  16.367  1.00 42.42  ? 223 GLN C O   1 
ATOM   5378 C CB  . GLN C 1 232 ? 2.053   -51.014  19.367  1.00 44.72  ? 223 GLN C CB  1 
ATOM   5379 C CG  . GLN C 1 232 ? 1.712   -51.727  20.672  1.00 48.85  ? 223 GLN C CG  1 
ATOM   5380 C CD  . GLN C 1 232 ? 0.267   -51.521  21.079  1.00 49.47  ? 223 GLN C CD  1 
ATOM   5381 O OE1 . GLN C 1 232 ? -0.201  -50.388  21.170  1.00 51.91  ? 223 GLN C OE1 1 
ATOM   5382 N NE2 . GLN C 1 232 ? -0.454  -52.618  21.306  1.00 48.41  ? 223 GLN C NE2 1 
ATOM   5383 N N   . GLU C 1 233 ? 0.974   -49.907  16.316  1.00 42.64  ? 224 GLU C N   1 
ATOM   5384 C CA  . GLU C 1 233 ? 1.483   -49.071  15.224  1.00 42.68  ? 224 GLU C CA  1 
ATOM   5385 C C   . GLU C 1 233 ? 1.930   -47.711  15.735  1.00 42.68  ? 224 GLU C C   1 
ATOM   5386 O O   . GLU C 1 233 ? 2.485   -46.896  14.988  1.00 42.18  ? 224 GLU C O   1 
ATOM   5387 C CB  . GLU C 1 233 ? 0.439   -48.905  14.139  1.00 40.71  ? 224 GLU C CB  1 
ATOM   5388 C CG  . GLU C 1 233 ? -0.147  -50.214  13.705  1.00 44.14  ? 224 GLU C CG  1 
ATOM   5389 C CD  . GLU C 1 233 ? -1.325  -49.998  12.812  1.00 49.17  ? 224 GLU C CD  1 
ATOM   5390 O OE1 . GLU C 1 233 ? -2.198  -49.182  13.191  1.00 51.04  ? 224 GLU C OE1 1 
ATOM   5391 O OE2 . GLU C 1 233 ? -1.357  -50.606  11.719  1.00 52.65  ? 224 GLU C OE2 1 
ATOM   5392 N N   . GLY C 1 234 ? 1.701   -47.480  17.022  1.00 40.32  ? 225 GLY C N   1 
ATOM   5393 C CA  . GLY C 1 234 ? 2.149   -46.259  17.647  1.00 39.91  ? 225 GLY C CA  1 
ATOM   5394 C C   . GLY C 1 234 ? 3.591   -46.474  18.024  1.00 40.07  ? 225 GLY C C   1 
ATOM   5395 O O   . GLY C 1 234 ? 4.139   -47.552  17.796  1.00 39.58  ? 225 GLY C O   1 
ATOM   5396 N N   . ARG C 1 235 ? 4.214   -45.451  18.594  1.00 40.64  ? 226 ARG C N   1 
ATOM   5397 C CA  . ARG C 1 235 ? 5.563   -45.600  19.109  1.00 40.14  ? 226 ARG C CA  1 
ATOM   5398 C C   . ARG C 1 235 ? 5.771   -44.769  20.361  1.00 39.88  ? 226 ARG C C   1 
ATOM   5399 O O   . ARG C 1 235 ? 5.136   -43.724  20.552  1.00 39.45  ? 226 ARG C O   1 
ATOM   5400 C CB  . ARG C 1 235 ? 6.612   -45.234  18.054  1.00 37.25  ? 226 ARG C CB  1 
ATOM   5401 C CG  . ARG C 1 235 ? 6.725   -46.230  16.915  1.00 35.91  ? 226 ARG C CG  1 
ATOM   5402 C CD  . ARG C 1 235 ? 7.109   -47.602  17.420  1.00 36.15  ? 226 ARG C CD  1 
ATOM   5403 N NE  . ARG C 1 235 ? 7.428   -48.518  16.330  1.00 38.09  ? 226 ARG C NE  1 
ATOM   5404 C CZ  . ARG C 1 235 ? 6.587   -49.422  15.837  1.00 37.52  ? 226 ARG C CZ  1 
ATOM   5405 N NH1 . ARG C 1 235 ? 5.364   -49.547  16.332  1.00 38.94  ? 226 ARG C NH1 1 
ATOM   5406 N NH2 . ARG C 1 235 ? 6.975   -50.207  14.848  1.00 37.28  ? 226 ARG C NH2 1 
ATOM   5407 N N   . MET C 1 236 ? 6.674   -45.244  21.209  1.00 38.36  ? 227 MET C N   1 
ATOM   5408 C CA  . MET C 1 236 ? 7.013   -44.533  22.419  1.00 40.41  ? 227 MET C CA  1 
ATOM   5409 C C   . MET C 1 236 ? 8.521   -44.347  22.485  1.00 39.66  ? 227 MET C C   1 
ATOM   5410 O O   . MET C 1 236 ? 9.277   -45.266  22.198  1.00 39.13  ? 227 MET C O   1 
ATOM   5411 C CB  . MET C 1 236 ? 6.491   -45.291  23.638  1.00 41.49  ? 227 MET C CB  1 
ATOM   5412 C CG  . MET C 1 236 ? 6.049   -44.387  24.753  1.00 40.49  ? 227 MET C CG  1 
ATOM   5413 S SD  . MET C 1 236 ? 5.156   -45.313  26.003  1.00 43.25  ? 227 MET C SD  1 
ATOM   5414 C CE  . MET C 1 236 ? 3.445   -45.170  25.479  1.00 40.69  ? 227 MET C CE  1 
ATOM   5415 N N   . ASN C 1 237 ? 8.967   -43.146  22.828  1.00 41.27  ? 228 ASN C N   1 
ATOM   5416 C CA  . ASN C 1 237 ? 10.404  -42.919  22.959  1.00 44.00  ? 228 ASN C CA  1 
ATOM   5417 C C   . ASN C 1 237 ? 10.794  -42.683  24.401  1.00 45.15  ? 228 ASN C C   1 
ATOM   5418 O O   . ASN C 1 237 ? 10.110  -41.964  25.126  1.00 44.67  ? 228 ASN C O   1 
ATOM   5419 C CB  . ASN C 1 237 ? 10.895  -41.782  22.064  1.00 42.24  ? 228 ASN C CB  1 
ATOM   5420 C CG  . ASN C 1 237 ? 11.404  -42.285  20.729  1.00 44.12  ? 228 ASN C CG  1 
ATOM   5421 O OD1 . ASN C 1 237 ? 11.168  -43.440  20.365  1.00 43.61  ? 228 ASN C OD1 1 
ATOM   5422 N ND2 . ASN C 1 237 ? 12.110  -41.432  19.996  1.00 42.46  ? 228 ASN C ND2 1 
ATOM   5423 N N   . TYR C 1 238 ? 11.899  -43.293  24.813  1.00 45.17  ? 229 TYR C N   1 
ATOM   5424 C CA  . TYR C 1 238 ? 12.270  -43.309  26.218  1.00 44.07  ? 229 TYR C CA  1 
ATOM   5425 C C   . TYR C 1 238 ? 13.507  -42.444  26.491  1.00 43.89  ? 229 TYR C C   1 
ATOM   5426 O O   . TYR C 1 238 ? 14.598  -42.730  25.995  1.00 44.90  ? 229 TYR C O   1 
ATOM   5427 C CB  . TYR C 1 238 ? 12.463  -44.760  26.674  1.00 41.97  ? 229 TYR C CB  1 
ATOM   5428 C CG  . TYR C 1 238 ? 11.286  -45.668  26.338  1.00 42.09  ? 229 TYR C CG  1 
ATOM   5429 C CD1 . TYR C 1 238 ? 10.064  -45.499  26.962  1.00 42.27  ? 229 TYR C CD1 1 
ATOM   5430 C CD2 . TYR C 1 238 ? 11.400  -46.695  25.408  1.00 41.93  ? 229 TYR C CD2 1 
ATOM   5431 C CE1 . TYR C 1 238 ? 8.986   -46.321  26.673  1.00 43.13  ? 229 TYR C CE1 1 
ATOM   5432 C CE2 . TYR C 1 238 ? 10.319  -47.522  25.110  1.00 41.66  ? 229 TYR C CE2 1 
ATOM   5433 C CZ  . TYR C 1 238 ? 9.115   -47.327  25.750  1.00 42.73  ? 229 TYR C CZ  1 
ATOM   5434 O OH  . TYR C 1 238 ? 8.025   -48.128  25.489  1.00 40.76  ? 229 TYR C OH  1 
ATOM   5435 N N   . TYR C 1 239 ? 13.316  -41.386  27.280  1.00 43.41  ? 230 TYR C N   1 
ATOM   5436 C CA  . TYR C 1 239 ? 14.350  -40.379  27.552  1.00 46.27  ? 230 TYR C CA  1 
ATOM   5437 C C   . TYR C 1 239 ? 14.721  -40.274  29.042  1.00 45.91  ? 230 TYR C C   1 
ATOM   5438 O O   . TYR C 1 239 ? 13.920  -40.605  29.914  1.00 45.94  ? 230 TYR C O   1 
ATOM   5439 C CB  . TYR C 1 239 ? 13.854  -39.006  27.108  1.00 45.82  ? 230 TYR C CB  1 
ATOM   5440 C CG  . TYR C 1 239 ? 13.524  -38.896  25.649  1.00 46.45  ? 230 TYR C CG  1 
ATOM   5441 C CD1 . TYR C 1 239 ? 12.385  -39.483  25.125  1.00 46.21  ? 230 TYR C CD1 1 
ATOM   5442 C CD2 . TYR C 1 239 ? 14.346  -38.178  24.796  1.00 49.35  ? 230 TYR C CD2 1 
ATOM   5443 C CE1 . TYR C 1 239 ? 12.085  -39.369  23.773  1.00 49.09  ? 230 TYR C CE1 1 
ATOM   5444 C CE2 . TYR C 1 239 ? 14.061  -38.057  23.459  1.00 49.85  ? 230 TYR C CE2 1 
ATOM   5445 C CZ  . TYR C 1 239 ? 12.935  -38.651  22.946  1.00 48.90  ? 230 TYR C CZ  1 
ATOM   5446 O OH  . TYR C 1 239 ? 12.673  -38.516  21.599  1.00 51.21  ? 230 TYR C OH  1 
ATOM   5447 N N   . TRP C 1 240 ? 15.921  -39.780  29.336  1.00 45.44  ? 231 TRP C N   1 
ATOM   5448 C CA  . TRP C 1 240 ? 16.329  -39.594  30.724  1.00 45.03  ? 231 TRP C CA  1 
ATOM   5449 C C   . TRP C 1 240 ? 17.425  -38.558  30.914  1.00 48.58  ? 231 TRP C C   1 
ATOM   5450 O O   . TRP C 1 240 ? 18.132  -38.183  29.980  1.00 50.36  ? 231 TRP C O   1 
ATOM   5451 C CB  . TRP C 1 240 ? 16.813  -40.911  31.313  1.00 46.18  ? 231 TRP C CB  1 
ATOM   5452 C CG  . TRP C 1 240 ? 18.051  -41.403  30.656  1.00 48.71  ? 231 TRP C CG  1 
ATOM   5453 C CD1 . TRP C 1 240 ? 18.124  -42.247  29.594  1.00 47.98  ? 231 TRP C CD1 1 
ATOM   5454 C CD2 . TRP C 1 240 ? 19.402  -41.064  30.993  1.00 51.20  ? 231 TRP C CD2 1 
ATOM   5455 N NE1 . TRP C 1 240 ? 19.435  -42.467  29.249  1.00 50.86  ? 231 TRP C NE1 1 
ATOM   5456 C CE2 . TRP C 1 240 ? 20.241  -41.753  30.094  1.00 51.13  ? 231 TRP C CE2 1 
ATOM   5457 C CE3 . TRP C 1 240 ? 19.984  -40.252  31.966  1.00 50.17  ? 231 TRP C CE3 1 
ATOM   5458 C CZ2 . TRP C 1 240 ? 21.627  -41.656  30.140  1.00 49.91  ? 231 TRP C CZ2 1 
ATOM   5459 C CZ3 . TRP C 1 240 ? 21.365  -40.158  32.009  1.00 49.59  ? 231 TRP C CZ3 1 
ATOM   5460 C CH2 . TRP C 1 240 ? 22.168  -40.856  31.101  1.00 51.02  ? 231 TRP C CH2 1 
ATOM   5461 N N   . THR C 1 241 ? 17.560  -38.098  32.148  1.00 52.20  ? 232 THR C N   1 
ATOM   5462 C CA  . THR C 1 241 ? 18.653  -37.216  32.517  1.00 51.74  ? 232 THR C CA  1 
ATOM   5463 C C   . THR C 1 241 ? 18.918  -37.377  33.992  1.00 52.98  ? 232 THR C C   1 
ATOM   5464 O O   . THR C 1 241 ? 18.004  -37.672  34.760  1.00 53.96  ? 232 THR C O   1 
ATOM   5465 C CB  . THR C 1 241 ? 18.289  -35.760  32.265  1.00 53.72  ? 232 THR C CB  1 
ATOM   5466 O OG1 . THR C 1 241 ? 19.361  -34.920  32.709  1.00 57.18  ? 232 THR C OG1 1 
ATOM   5467 C CG2 . THR C 1 241 ? 17.019  -35.410  33.024  1.00 50.92  ? 232 THR C CG2 1 
ATOM   5468 N N   . LEU C 1 242 ? 20.166  -37.185  34.393  1.00 57.09  ? 233 LEU C N   1 
ATOM   5469 C CA  . LEU C 1 242 ? 20.486  -37.105  35.807  1.00 53.48  ? 233 LEU C CA  1 
ATOM   5470 C C   . LEU C 1 242 ? 20.340  -35.663  36.237  1.00 55.49  ? 233 LEU C C   1 
ATOM   5471 O O   . LEU C 1 242 ? 20.772  -34.743  35.542  1.00 56.04  ? 233 LEU C O   1 
ATOM   5472 C CB  . LEU C 1 242 ? 21.899  -37.604  36.080  1.00 55.68  ? 233 LEU C CB  1 
ATOM   5473 C CG  . LEU C 1 242 ? 22.054  -39.118  35.942  1.00 57.40  ? 233 LEU C CG  1 
ATOM   5474 C CD1 . LEU C 1 242 ? 23.499  -39.537  36.094  1.00 62.27  ? 233 LEU C CD1 1 
ATOM   5475 C CD2 . LEU C 1 242 ? 21.192  -39.833  36.953  1.00 55.06  ? 233 LEU C CD2 1 
ATOM   5476 N N   . VAL C 1 243 ? 19.713  -35.466  37.383  1.00 58.71  ? 234 VAL C N   1 
ATOM   5477 C CA  . VAL C 1 243 ? 19.523  -34.125  37.895  1.00 60.92  ? 234 VAL C CA  1 
ATOM   5478 C C   . VAL C 1 243 ? 20.519  -33.850  39.008  1.00 61.48  ? 234 VAL C C   1 
ATOM   5479 O O   . VAL C 1 243 ? 20.680  -34.655  39.931  1.00 59.68  ? 234 VAL C O   1 
ATOM   5480 C CB  . VAL C 1 243 ? 18.110  -33.945  38.443  1.00 59.93  ? 234 VAL C CB  1 
ATOM   5481 C CG1 . VAL C 1 243 ? 17.816  -32.462  38.654  1.00 60.21  ? 234 VAL C CG1 1 
ATOM   5482 C CG2 . VAL C 1 243 ? 17.117  -34.561  37.489  1.00 56.46  ? 234 VAL C CG2 1 
ATOM   5483 N N   . GLU C 1 244 ? 21.192  -32.710  38.913  1.00 63.97  ? 235 GLU C N   1 
ATOM   5484 C CA  . GLU C 1 244 ? 22.127  -32.307  39.955  1.00 63.07  ? 235 GLU C CA  1 
ATOM   5485 C C   . GLU C 1 244 ? 21.433  -32.203  41.309  1.00 63.88  ? 235 GLU C C   1 
ATOM   5486 O O   . GLU C 1 244 ? 20.251  -31.826  41.395  1.00 62.38  ? 235 GLU C O   1 
ATOM   5487 C CB  . GLU C 1 244 ? 22.781  -30.972  39.616  1.00 63.25  ? 235 GLU C CB  1 
ATOM   5488 C CG  . GLU C 1 244 ? 23.801  -31.036  38.501  1.00 67.43  ? 235 GLU C CG  1 
ATOM   5489 C CD  . GLU C 1 244 ? 24.088  -29.660  37.905  1.00 74.34  ? 235 GLU C CD  1 
ATOM   5490 O OE1 . GLU C 1 244 ? 23.446  -28.674  38.332  1.00 72.69  ? 235 GLU C OE1 1 
ATOM   5491 O OE2 . GLU C 1 244 ? 24.951  -29.559  37.006  1.00 74.37  ? 235 GLU C OE2 1 
ATOM   5492 N N   . PRO C 1 245 ? 22.178  -32.529  42.377  1.00 65.18  ? 236 PRO C N   1 
ATOM   5493 C CA  . PRO C 1 245 ? 21.679  -32.430  43.743  1.00 61.44  ? 236 PRO C CA  1 
ATOM   5494 C C   . PRO C 1 245 ? 20.981  -31.101  44.010  1.00 58.93  ? 236 PRO C C   1 
ATOM   5495 O O   . PRO C 1 245 ? 20.056  -31.062  44.805  1.00 60.93  ? 236 PRO C O   1 
ATOM   5496 C CB  . PRO C 1 245 ? 22.955  -32.551  44.563  1.00 59.24  ? 236 PRO C CB  1 
ATOM   5497 C CG  . PRO C 1 245 ? 23.774  -33.510  43.779  1.00 58.56  ? 236 PRO C CG  1 
ATOM   5498 C CD  . PRO C 1 245 ? 23.512  -33.160  42.338  1.00 64.82  ? 236 PRO C CD  1 
ATOM   5499 N N   . GLY C 1 246 ? 21.409  -30.027  43.368  1.00 58.38  ? 237 GLY C N   1 
ATOM   5500 C CA  . GLY C 1 246 ? 20.743  -28.758  43.593  1.00 59.97  ? 237 GLY C CA  1 
ATOM   5501 C C   . GLY C 1 246 ? 19.579  -28.497  42.661  1.00 59.82  ? 237 GLY C C   1 
ATOM   5502 O O   . GLY C 1 246 ? 18.638  -27.777  42.998  1.00 58.09  ? 237 GLY C O   1 
ATOM   5503 N N   . ASP C 1 247 ? 19.645  -29.117  41.488  1.00 63.59  ? 238 ASP C N   1 
ATOM   5504 C CA  . ASP C 1 247 ? 18.852  -28.717  40.328  1.00 61.80  ? 238 ASP C CA  1 
ATOM   5505 C C   . ASP C 1 247 ? 17.353  -28.963  40.512  1.00 61.18  ? 238 ASP C C   1 
ATOM   5506 O O   . ASP C 1 247 ? 16.943  -29.751  41.371  1.00 60.39  ? 238 ASP C O   1 
ATOM   5507 C CB  . ASP C 1 247 ? 19.360  -29.463  39.083  1.00 62.85  ? 238 ASP C CB  1 
ATOM   5508 C CG  . ASP C 1 247 ? 19.184  -28.666  37.786  1.00 65.40  ? 238 ASP C CG  1 
ATOM   5509 O OD1 . ASP C 1 247 ? 18.497  -27.618  37.784  1.00 62.80  ? 238 ASP C OD1 1 
ATOM   5510 O OD2 . ASP C 1 247 ? 19.737  -29.106  36.752  1.00 66.21  ? 238 ASP C OD2 1 
ATOM   5511 N N   . LYS C 1 248 ? 16.550  -28.263  39.702  1.00 62.78  ? 239 LYS C N   1 
ATOM   5512 C CA  . LYS C 1 248 ? 15.108  -28.506  39.567  1.00 57.40  ? 239 LYS C CA  1 
ATOM   5513 C C   . LYS C 1 248 ? 14.726  -28.909  38.150  1.00 59.62  ? 239 LYS C C   1 
ATOM   5514 O O   . LYS C 1 248 ? 15.172  -28.294  37.174  1.00 61.07  ? 239 LYS C O   1 
ATOM   5515 C CB  . LYS C 1 248 ? 14.303  -27.251  39.885  1.00 57.27  ? 239 LYS C CB  1 
ATOM   5516 C CG  . LYS C 1 248 ? 12.844  -27.353  39.439  1.00 54.83  ? 239 LYS C CG  1 
ATOM   5517 C CD  . LYS C 1 248 ? 12.301  -26.019  38.955  1.00 56.85  ? 239 LYS C CD  1 
ATOM   5518 C CE  . LYS C 1 248 ? 11.545  -25.272  40.048  1.00 56.32  ? 239 LYS C CE  1 
ATOM   5519 N NZ  . LYS C 1 248 ? 10.764  -24.129  39.476  1.00 54.97  ? 239 LYS C NZ  1 
ATOM   5520 N N   . ILE C 1 249 ? 13.859  -29.908  38.039  1.00 57.53  ? 240 ILE C N   1 
ATOM   5521 C CA  . ILE C 1 249 ? 13.368  -30.338  36.739  1.00 55.10  ? 240 ILE C CA  1 
ATOM   5522 C C   . ILE C 1 249 ? 11.884  -30.015  36.557  1.00 54.57  ? 240 ILE C C   1 
ATOM   5523 O O   . ILE C 1 249 ? 11.108  -30.066  37.504  1.00 56.11  ? 240 ILE C O   1 
ATOM   5524 C CB  . ILE C 1 249 ? 13.620  -31.830  36.530  1.00 55.15  ? 240 ILE C CB  1 
ATOM   5525 C CG1 . ILE C 1 249 ? 13.202  -32.242  35.119  1.00 55.65  ? 240 ILE C CG1 1 
ATOM   5526 C CG2 . ILE C 1 249 ? 12.899  -32.654  37.581  1.00 53.00  ? 240 ILE C CG2 1 
ATOM   5527 C CD1 . ILE C 1 249 ? 13.816  -33.529  34.680  1.00 53.74  ? 240 ILE C CD1 1 
ATOM   5528 N N   . THR C 1 250 ? 11.490  -29.669  35.342  1.00 54.65  ? 241 THR C N   1 
ATOM   5529 C CA  . THR C 1 250 ? 10.115  -29.278  35.101  1.00 55.71  ? 241 THR C CA  1 
ATOM   5530 C C   . THR C 1 250 ? 9.552   -29.980  33.873  1.00 57.71  ? 241 THR C C   1 
ATOM   5531 O O   . THR C 1 250 ? 10.273  -30.210  32.909  1.00 55.71  ? 241 THR C O   1 
ATOM   5532 C CB  . THR C 1 250 ? 10.012  -27.777  34.897  1.00 55.99  ? 241 THR C CB  1 
ATOM   5533 O OG1 . THR C 1 250 ? 10.430  -27.116  36.095  1.00 55.31  ? 241 THR C OG1 1 
ATOM   5534 C CG2 . THR C 1 250 ? 8.569   -27.382  34.579  1.00 58.19  ? 241 THR C CG2 1 
ATOM   5535 N N   . PHE C 1 251 ? 8.263   -30.318  33.925  1.00 59.48  ? 242 PHE C N   1 
ATOM   5536 C CA  . PHE C 1 251 ? 7.569   -30.995  32.829  1.00 54.32  ? 242 PHE C CA  1 
ATOM   5537 C C   . PHE C 1 251 ? 6.325   -30.242  32.379  1.00 56.01  ? 242 PHE C C   1 
ATOM   5538 O O   . PHE C 1 251 ? 5.526   -29.776  33.188  1.00 58.14  ? 242 PHE C O   1 
ATOM   5539 C CB  . PHE C 1 251 ? 7.154   -32.403  33.236  1.00 52.77  ? 242 PHE C CB  1 
ATOM   5540 C CG  . PHE C 1 251 ? 8.310   -33.336  33.491  1.00 55.30  ? 242 PHE C CG  1 
ATOM   5541 C CD1 . PHE C 1 251 ? 8.963   -33.330  34.713  1.00 53.57  ? 242 PHE C CD1 1 
ATOM   5542 C CD2 . PHE C 1 251 ? 8.730   -34.235  32.516  1.00 52.86  ? 242 PHE C CD2 1 
ATOM   5543 C CE1 . PHE C 1 251 ? 10.014  -34.191  34.960  1.00 52.51  ? 242 PHE C CE1 1 
ATOM   5544 C CE2 . PHE C 1 251 ? 9.791   -35.096  32.758  1.00 50.71  ? 242 PHE C CE2 1 
ATOM   5545 C CZ  . PHE C 1 251 ? 10.426  -35.076  33.983  1.00 50.71  ? 242 PHE C CZ  1 
ATOM   5546 N N   . GLU C 1 252 ? 6.163   -30.137  31.073  1.00 57.22  ? 243 GLU C N   1 
ATOM   5547 C CA  . GLU C 1 252 ? 5.048   -29.411  30.516  1.00 57.47  ? 243 GLU C CA  1 
ATOM   5548 C C   . GLU C 1 252 ? 4.527   -30.166  29.303  1.00 54.26  ? 243 GLU C C   1 
ATOM   5549 O O   . GLU C 1 252 ? 5.295   -30.534  28.423  1.00 52.49  ? 243 GLU C O   1 
ATOM   5550 C CB  . GLU C 1 252 ? 5.494   -28.006  30.138  1.00 58.17  ? 243 GLU C CB  1 
ATOM   5551 C CG  . GLU C 1 252 ? 4.358   -27.077  29.800  1.00 63.78  ? 243 GLU C CG  1 
ATOM   5552 C CD  . GLU C 1 252 ? 4.810   -25.644  29.776  1.00 70.39  ? 243 GLU C CD  1 
ATOM   5553 O OE1 . GLU C 1 252 ? 4.201   -24.843  29.030  1.00 71.62  ? 243 GLU C OE1 1 
ATOM   5554 O OE2 . GLU C 1 252 ? 5.777   -25.325  30.507  1.00 69.08  ? 243 GLU C OE2 1 
ATOM   5555 N N   . ALA C 1 253 ? 3.231   -30.440  29.277  1.00 53.51  ? 244 ALA C N   1 
ATOM   5556 C CA  . ALA C 1 253 ? 2.668   -31.168  28.153  1.00 54.98  ? 244 ALA C CA  1 
ATOM   5557 C C   . ALA C 1 253 ? 1.203   -30.826  27.864  1.00 56.09  ? 244 ALA C C   1 
ATOM   5558 O O   . ALA C 1 253 ? 0.378   -30.700  28.770  1.00 53.06  ? 244 ALA C O   1 
ATOM   5559 C CB  . ALA C 1 253 ? 2.826   -32.663  28.383  1.00 53.44  ? 244 ALA C CB  1 
ATOM   5560 N N   . THR C 1 254 ? 0.890   -30.685  26.585  1.00 55.46  ? 245 THR C N   1 
ATOM   5561 C CA  . THR C 1 254 ? -0.489  -30.640  26.126  1.00 51.48  ? 245 THR C CA  1 
ATOM   5562 C C   . THR C 1 254 ? -0.926  -31.996  25.556  1.00 52.21  ? 245 THR C C   1 
ATOM   5563 O O   . THR C 1 254 ? -2.002  -32.130  24.961  1.00 53.36  ? 245 THR C O   1 
ATOM   5564 C CB  . THR C 1 254 ? -0.702  -29.492  25.180  1.00 52.76  ? 245 THR C CB  1 
ATOM   5565 O OG1 . THR C 1 254 ? 0.288   -29.557  24.160  1.00 57.83  ? 245 THR C OG1 1 
ATOM   5566 C CG2 . THR C 1 254 ? -0.498  -28.196  25.942  1.00 57.68  ? 245 THR C CG2 1 
ATOM   5567 N N   . GLY C 1 255 ? -0.056  -32.990  25.706  1.00 50.64  ? 246 GLY C N   1 
ATOM   5568 C CA  . GLY C 1 255 ? -0.400  -34.357  25.359  1.00 48.11  ? 246 GLY C CA  1 
ATOM   5569 C C   . GLY C 1 255 ? 0.828   -35.234  25.263  1.00 45.54  ? 246 GLY C C   1 
ATOM   5570 O O   . GLY C 1 255 ? 1.949   -34.739  25.326  1.00 44.63  ? 246 GLY C O   1 
ATOM   5571 N N   . ASN C 1 256 ? 0.612   -36.540  25.138  1.00 44.88  ? 247 ASN C N   1 
ATOM   5572 C CA  . ASN C 1 256 ? 1.669   -37.470  24.735  1.00 43.60  ? 247 ASN C CA  1 
ATOM   5573 C C   . ASN C 1 256 ? 2.798   -37.644  25.748  1.00 43.94  ? 247 ASN C C   1 
ATOM   5574 O O   . ASN C 1 256 ? 3.723   -38.431  25.545  1.00 42.31  ? 247 ASN C O   1 
ATOM   5575 C CB  . ASN C 1 256 ? 2.241   -37.056  23.380  1.00 44.20  ? 247 ASN C CB  1 
ATOM   5576 C CG  . ASN C 1 256 ? 1.162   -36.764  22.361  1.00 44.24  ? 247 ASN C CG  1 
ATOM   5577 O OD1 . ASN C 1 256 ? 0.603   -35.663  22.331  1.00 47.41  ? 247 ASN C OD1 1 
ATOM   5578 N ND2 . ASN C 1 256 ? 0.864   -37.745  21.517  1.00 42.33  ? 247 ASN C ND2 1 
ATOM   5579 N N   . LEU C 1 257 ? 2.744   -36.891  26.836  1.00 48.89  ? 248 LEU C N   1 
ATOM   5580 C CA  . LEU C 1 257 ? 3.735   -37.079  27.880  1.00 45.76  ? 248 LEU C CA  1 
ATOM   5581 C C   . LEU C 1 257 ? 3.415   -38.335  28.658  1.00 43.95  ? 248 LEU C C   1 
ATOM   5582 O O   . LEU C 1 257 ? 2.276   -38.534  29.062  1.00 45.24  ? 248 LEU C O   1 
ATOM   5583 C CB  . LEU C 1 257 ? 3.788   -35.890  28.830  1.00 45.51  ? 248 LEU C CB  1 
ATOM   5584 C CG  . LEU C 1 257 ? 4.762   -36.120  29.991  1.00 47.00  ? 248 LEU C CG  1 
ATOM   5585 C CD1 . LEU C 1 257 ? 6.127   -36.654  29.541  1.00 39.94  ? 248 LEU C CD1 1 
ATOM   5586 C CD2 . LEU C 1 257 ? 4.915   -34.834  30.790  1.00 50.17  ? 248 LEU C CD2 1 
ATOM   5587 N N   . VAL C 1 258 ? 4.421   -39.186  28.843  1.00 42.42  ? 249 VAL C N   1 
ATOM   5588 C CA  . VAL C 1 258 ? 4.294   -40.345  29.702  1.00 40.35  ? 249 VAL C CA  1 
ATOM   5589 C C   . VAL C 1 258 ? 5.138   -40.025  30.913  1.00 45.79  ? 249 VAL C C   1 
ATOM   5590 O O   . VAL C 1 258 ? 6.365   -40.021  30.843  1.00 48.79  ? 249 VAL C O   1 
ATOM   5591 C CB  . VAL C 1 258 ? 4.835   -41.605  29.027  1.00 38.85  ? 249 VAL C CB  1 
ATOM   5592 C CG1 . VAL C 1 258 ? 4.609   -42.818  29.911  1.00 38.75  ? 249 VAL C CG1 1 
ATOM   5593 C CG2 . VAL C 1 258 ? 4.176   -41.801  27.659  1.00 38.74  ? 249 VAL C CG2 1 
ATOM   5594 N N   . VAL C 1 259 ? 4.486   -39.768  32.033  1.00 45.10  ? 250 VAL C N   1 
ATOM   5595 C CA  . VAL C 1 259 ? 5.149   -39.093  33.128  1.00 45.97  ? 250 VAL C CA  1 
ATOM   5596 C C   . VAL C 1 259 ? 5.970   -40.039  33.986  1.00 46.95  ? 250 VAL C C   1 
ATOM   5597 O O   . VAL C 1 259 ? 5.715   -41.248  34.025  1.00 46.33  ? 250 VAL C O   1 
ATOM   5598 C CB  . VAL C 1 259 ? 4.122   -38.380  33.990  1.00 45.22  ? 250 VAL C CB  1 
ATOM   5599 C CG1 . VAL C 1 259 ? 3.370   -37.367  33.145  1.00 47.06  ? 250 VAL C CG1 1 
ATOM   5600 C CG2 . VAL C 1 259 ? 3.163   -39.401  34.560  1.00 45.89  ? 250 VAL C CG2 1 
ATOM   5601 N N   . PRO C 1 260 ? 6.983   -39.487  34.659  1.00 44.70  ? 251 PRO C N   1 
ATOM   5602 C CA  . PRO C 1 260 ? 7.700   -40.235  35.686  1.00 46.75  ? 251 PRO C CA  1 
ATOM   5603 C C   . PRO C 1 260 ? 6.791   -40.465  36.889  1.00 51.62  ? 251 PRO C C   1 
ATOM   5604 O O   . PRO C 1 260 ? 6.022   -39.572  37.288  1.00 51.47  ? 251 PRO C O   1 
ATOM   5605 C CB  . PRO C 1 260 ? 8.858   -39.292  36.072  1.00 45.49  ? 251 PRO C CB  1 
ATOM   5606 C CG  . PRO C 1 260 ? 9.006   -38.365  34.915  1.00 45.71  ? 251 PRO C CG  1 
ATOM   5607 C CD  . PRO C 1 260 ? 7.643   -38.214  34.328  1.00 45.49  ? 251 PRO C CD  1 
ATOM   5608 N N   . ARG C 1 261 ? 6.874   -41.666  37.450  1.00 50.24  ? 252 ARG C N   1 
ATOM   5609 C CA  . ARG C 1 261 ? 6.321   -41.924  38.763  1.00 50.26  ? 252 ARG C CA  1 
ATOM   5610 C C   . ARG C 1 261 ? 7.489   -42.052  39.748  1.00 53.65  ? 252 ARG C C   1 
ATOM   5611 O O   . ARG C 1 261 ? 7.590   -41.290  40.714  1.00 54.96  ? 252 ARG C O   1 
ATOM   5612 C CB  . ARG C 1 261 ? 5.440   -43.171  38.768  1.00 49.95  ? 252 ARG C CB  1 
ATOM   5613 C CG  . ARG C 1 261 ? 4.553   -43.262  39.995  1.00 54.51  ? 252 ARG C CG  1 
ATOM   5614 C CD  . ARG C 1 261 ? 3.686   -44.517  40.017  1.00 56.49  ? 252 ARG C CD  1 
ATOM   5615 N NE  . ARG C 1 261 ? 2.970   -44.642  41.285  1.00 60.26  ? 252 ARG C NE  1 
ATOM   5616 C CZ  . ARG C 1 261 ? 2.335   -45.738  41.691  1.00 61.18  ? 252 ARG C CZ  1 
ATOM   5617 N NH1 . ARG C 1 261 ? 2.318   -46.826  40.932  1.00 62.18  ? 252 ARG C NH1 1 
ATOM   5618 N NH2 . ARG C 1 261 ? 1.720   -45.749  42.868  1.00 64.37  ? 252 ARG C NH2 1 
ATOM   5619 N N   . TYR C 1 262 ? 8.360   -43.029  39.510  1.00 53.66  ? 253 TYR C N   1 
ATOM   5620 C CA  . TYR C 1 262 ? 9.527   -43.239  40.367  1.00 54.86  ? 253 TYR C CA  1 
ATOM   5621 C C   . TYR C 1 262 ? 10.857  -42.784  39.738  1.00 55.08  ? 253 TYR C C   1 
ATOM   5622 O O   . TYR C 1 262 ? 11.209  -43.196  38.635  1.00 57.08  ? 253 TYR C O   1 
ATOM   5623 C CB  . TYR C 1 262 ? 9.651   -44.711  40.772  1.00 54.68  ? 253 TYR C CB  1 
ATOM   5624 C CG  . TYR C 1 262 ? 8.523   -45.248  41.620  1.00 56.49  ? 253 TYR C CG  1 
ATOM   5625 C CD1 . TYR C 1 262 ? 8.382   -44.881  42.955  1.00 57.71  ? 253 TYR C CD1 1 
ATOM   5626 C CD2 . TYR C 1 262 ? 7.608   -46.142  41.089  1.00 57.13  ? 253 TYR C CD2 1 
ATOM   5627 C CE1 . TYR C 1 262 ? 7.345   -45.388  43.729  1.00 58.96  ? 253 TYR C CE1 1 
ATOM   5628 C CE2 . TYR C 1 262 ? 6.579   -46.655  41.851  1.00 60.39  ? 253 TYR C CE2 1 
ATOM   5629 C CZ  . TYR C 1 262 ? 6.450   -46.280  43.164  1.00 60.23  ? 253 TYR C CZ  1 
ATOM   5630 O OH  . TYR C 1 262 ? 5.412   -46.813  43.890  1.00 62.02  ? 253 TYR C OH  1 
ATOM   5631 N N   . ALA C 1 263 ? 11.597  -41.946  40.454  1.00 54.70  ? 254 ALA C N   1 
ATOM   5632 C CA  . ALA C 1 263 ? 12.956  -41.579  40.061  1.00 53.60  ? 254 ALA C CA  1 
ATOM   5633 C C   . ALA C 1 263 ? 13.965  -42.447  40.812  1.00 51.15  ? 254 ALA C C   1 
ATOM   5634 O O   . ALA C 1 263 ? 13.591  -43.443  41.426  1.00 53.06  ? 254 ALA C O   1 
ATOM   5635 C CB  . ALA C 1 263 ? 13.206  -40.109  40.339  1.00 55.37  ? 254 ALA C CB  1 
ATOM   5636 N N   . PHE C 1 264 ? 15.246  -42.109  40.708  1.00 50.32  ? 255 PHE C N   1 
ATOM   5637 C CA  . PHE C 1 264 ? 16.276  -42.783  41.493  1.00 51.04  ? 255 PHE C CA  1 
ATOM   5638 C C   . PHE C 1 264 ? 17.345  -41.812  41.993  1.00 57.19  ? 255 PHE C C   1 
ATOM   5639 O O   . PHE C 1 264 ? 18.029  -41.152  41.196  1.00 52.96  ? 255 PHE C O   1 
ATOM   5640 C CB  . PHE C 1 264 ? 16.946  -43.896  40.693  1.00 51.32  ? 255 PHE C CB  1 
ATOM   5641 C CG  . PHE C 1 264 ? 15.996  -44.952  40.199  1.00 55.93  ? 255 PHE C CG  1 
ATOM   5642 C CD1 . PHE C 1 264 ? 15.328  -44.796  38.989  1.00 53.82  ? 255 PHE C CD1 1 
ATOM   5643 C CD2 . PHE C 1 264 ? 15.779  -46.112  40.933  1.00 56.70  ? 255 PHE C CD2 1 
ATOM   5644 C CE1 . PHE C 1 264 ? 14.452  -45.772  38.523  1.00 53.40  ? 255 PHE C CE1 1 
ATOM   5645 C CE2 . PHE C 1 264 ? 14.907  -47.100  40.468  1.00 56.22  ? 255 PHE C CE2 1 
ATOM   5646 C CZ  . PHE C 1 264 ? 14.242  -46.928  39.259  1.00 53.45  ? 255 PHE C CZ  1 
ATOM   5647 N N   . ALA C 1 265 ? 17.487  -41.756  43.319  1.00 58.45  ? 256 ALA C N   1 
ATOM   5648 C CA  . ALA C 1 265 ? 18.601  -41.095  43.973  1.00 58.02  ? 256 ALA C CA  1 
ATOM   5649 C C   . ALA C 1 265 ? 19.763  -42.084  43.914  1.00 60.63  ? 256 ALA C C   1 
ATOM   5650 O O   . ALA C 1 265 ? 19.586  -43.272  44.196  1.00 57.98  ? 256 ALA C O   1 
ATOM   5651 C CB  . ALA C 1 265 ? 18.238  -40.765  45.414  1.00 59.46  ? 256 ALA C CB  1 
ATOM   5652 N N   . MET C 1 266 ? 20.940  -41.617  43.512  1.00 61.07  ? 257 MET C N   1 
ATOM   5653 C CA  . MET C 1 266 ? 22.049  -42.542  43.374  1.00 66.01  ? 257 MET C CA  1 
ATOM   5654 C C   . MET C 1 266 ? 23.431  -41.920  43.394  1.00 66.66  ? 257 MET C C   1 
ATOM   5655 O O   . MET C 1 266 ? 23.631  -40.727  43.128  1.00 64.62  ? 257 MET C O   1 
ATOM   5656 C CB  . MET C 1 266 ? 21.901  -43.350  42.088  1.00 65.99  ? 257 MET C CB  1 
ATOM   5657 C CG  . MET C 1 266 ? 22.052  -42.488  40.847  1.00 67.14  ? 257 MET C CG  1 
ATOM   5658 S SD  . MET C 1 266 ? 22.128  -43.371  39.277  1.00 72.92  ? 257 MET C SD  1 
ATOM   5659 C CE  . MET C 1 266 ? 23.642  -44.305  39.475  1.00 72.95  ? 257 MET C CE  1 
ATOM   5660 N N   . GLU C 1 267 ? 24.383  -42.788  43.689  1.00 67.32  ? 258 GLU C N   1 
ATOM   5661 C CA  . GLU C 1 267 ? 25.786  -42.464  43.624  1.00 72.95  ? 258 GLU C CA  1 
ATOM   5662 C C   . GLU C 1 267 ? 26.467  -43.586  42.849  1.00 75.27  ? 258 GLU C C   1 
ATOM   5663 O O   . GLU C 1 267 ? 26.267  -44.770  43.141  1.00 74.06  ? 258 GLU C O   1 
ATOM   5664 C CB  . GLU C 1 267 ? 26.361  -42.329  45.039  1.00 77.07  ? 258 GLU C CB  1 
ATOM   5665 C CG  . GLU C 1 267 ? 25.801  -43.348  46.040  1.00 77.25  ? 258 GLU C CG  1 
ATOM   5666 C CD  . GLU C 1 267 ? 26.072  -42.986  47.506  1.00 83.08  ? 258 GLU C CD  1 
ATOM   5667 O OE1 . GLU C 1 267 ? 25.360  -42.102  48.051  1.00 81.15  ? 258 GLU C OE1 1 
ATOM   5668 O OE2 . GLU C 1 267 ? 26.987  -43.601  48.113  1.00 86.69  ? 258 GLU C OE2 1 
ATOM   5669 N N   . ARG C 1 268 ? 27.258  -43.205  41.851  1.00 76.52  ? 259 ARG C N   1 
ATOM   5670 C CA  . ARG C 1 268 ? 27.920  -44.161  40.970  1.00 76.10  ? 259 ARG C CA  1 
ATOM   5671 C C   . ARG C 1 268 ? 29.336  -44.478  41.436  1.00 78.95  ? 259 ARG C C   1 
ATOM   5672 O O   . ARG C 1 268 ? 30.027  -43.616  41.978  1.00 78.10  ? 259 ARG C O   1 
ATOM   5673 C CB  . ARG C 1 268 ? 27.974  -43.626  39.540  1.00 79.30  ? 259 ARG C CB  1 
ATOM   5674 C CG  . ARG C 1 268 ? 26.961  -42.528  39.217  1.00 79.28  ? 259 ARG C CG  1 
ATOM   5675 C CD  . ARG C 1 268 ? 26.899  -42.303  37.704  1.00 78.42  ? 259 ARG C CD  1 
ATOM   5676 N NE  . ARG C 1 268 ? 26.434  -40.964  37.335  1.00 80.23  ? 259 ARG C NE  1 
ATOM   5677 C CZ  . ARG C 1 268 ? 27.229  -39.900  37.221  1.00 81.76  ? 259 ARG C CZ  1 
ATOM   5678 N NH1 . ARG C 1 268 ? 28.530  -40.011  37.465  1.00 82.67  ? 259 ARG C NH1 1 
ATOM   5679 N NH2 . ARG C 1 268 ? 26.725  -38.719  36.876  1.00 79.79  ? 259 ARG C NH2 1 
ATOM   5680 N N   . ASN C 1 269 ? 29.761  -45.720  41.224  1.00 82.86  ? 260 ASN C N   1 
ATOM   5681 C CA  . ASN C 1 269 ? 31.109  -46.156  41.598  1.00 85.32  ? 260 ASN C CA  1 
ATOM   5682 C C   . ASN C 1 269 ? 32.076  -46.206  40.416  1.00 89.78  ? 260 ASN C C   1 
ATOM   5683 O O   . ASN C 1 269 ? 31.744  -46.740  39.351  1.00 87.23  ? 260 ASN C O   1 
ATOM   5684 C CB  . ASN C 1 269 ? 31.075  -47.545  42.248  1.00 82.34  ? 260 ASN C CB  1 
ATOM   5685 C CG  . ASN C 1 269 ? 30.513  -47.525  43.654  1.00 84.75  ? 260 ASN C CG  1 
ATOM   5686 O OD1 . ASN C 1 269 ? 30.512  -46.485  44.324  1.00 88.69  ? 260 ASN C OD1 1 
ATOM   5687 N ND2 . ASN C 1 269 ? 30.036  -48.684  44.117  1.00 81.99  ? 260 ASN C ND2 1 
ATOM   5688 N N   . ALA C 1 270 ? 33.259  -45.619  40.598  1.00 95.45  ? 261 ALA C N   1 
ATOM   5689 C CA  . ALA C 1 270 ? 34.396  -45.878  39.715  1.00 96.94  ? 261 ALA C CA  1 
ATOM   5690 C C   . ALA C 1 270 ? 33.958  -45.913  38.259  1.00 91.73  ? 261 ALA C C   1 
ATOM   5691 O O   . ALA C 1 270 ? 33.352  -44.969  37.750  1.00 92.92  ? 261 ALA C O   1 
ATOM   5692 C CB  . ALA C 1 270 ? 35.086  -47.189  40.101  1.00 97.66  ? 261 ALA C CB  1 
ATOM   5693 N N   . GLY C 1 271 ? 34.260  -47.028  37.606  1.00 89.13  ? 262 GLY C N   1 
ATOM   5694 C CA  . GLY C 1 271 ? 33.740  -47.317  36.286  1.00 87.22  ? 262 GLY C CA  1 
ATOM   5695 C C   . GLY C 1 271 ? 33.675  -48.822  36.141  1.00 86.76  ? 262 GLY C C   1 
ATOM   5696 O O   . GLY C 1 271 ? 34.461  -49.554  36.745  1.00 91.33  ? 262 GLY C O   1 
ATOM   5697 N N   . SER C 1 272 ? 32.750  -49.287  35.315  1.00 81.88  ? 263 SER C N   1 
ATOM   5698 C CA  . SER C 1 272 ? 32.392  -50.698  35.290  1.00 78.41  ? 263 SER C CA  1 
ATOM   5699 C C   . SER C 1 272 ? 31.760  -51.012  33.940  1.00 77.35  ? 263 SER C C   1 
ATOM   5700 O O   . SER C 1 272 ? 31.890  -50.231  32.996  1.00 79.76  ? 263 SER C O   1 
ATOM   5701 C CB  . SER C 1 272 ? 31.437  -51.029  36.446  1.00 75.85  ? 263 SER C CB  1 
ATOM   5702 O OG  . SER C 1 272 ? 31.286  -52.429  36.628  1.00 73.25  ? 263 SER C OG  1 
ATOM   5703 N N   . GLY C 1 273 ? 31.098  -52.160  33.840  1.00 73.69  ? 264 GLY C N   1 
ATOM   5704 C CA  . GLY C 1 273 ? 30.470  -52.561  32.593  1.00 71.30  ? 264 GLY C CA  1 
ATOM   5705 C C   . GLY C 1 273 ? 29.315  -53.529  32.765  1.00 66.37  ? 264 GLY C C   1 
ATOM   5706 O O   . GLY C 1 273 ? 28.842  -53.762  33.875  1.00 64.56  ? 264 GLY C O   1 
ATOM   5707 N N   . ILE C 1 274 ? 28.832  -54.069  31.655  1.00 61.44  ? 265 ILE C N   1 
ATOM   5708 C CA  . ILE C 1 274 ? 27.788  -55.068  31.727  1.00 63.18  ? 265 ILE C CA  1 
ATOM   5709 C C   . ILE C 1 274 ? 28.262  -56.391  31.143  1.00 64.45  ? 265 ILE C C   1 
ATOM   5710 O O   . ILE C 1 274 ? 28.535  -56.498  29.947  1.00 64.72  ? 265 ILE C O   1 
ATOM   5711 C CB  . ILE C 1 274 ? 26.509  -54.612  31.008  1.00 61.66  ? 265 ILE C CB  1 
ATOM   5712 C CG1 . ILE C 1 274 ? 25.862  -53.456  31.772  1.00 58.41  ? 265 ILE C CG1 1 
ATOM   5713 C CG2 . ILE C 1 274 ? 25.531  -55.774  30.893  1.00 59.74  ? 265 ILE C CG2 1 
ATOM   5714 C CD1 . ILE C 1 274 ? 26.653  -52.184  31.736  1.00 59.20  ? 265 ILE C CD1 1 
ATOM   5715 N N   . ILE C 1 275 ? 28.371  -57.401  31.993  1.00 63.62  ? 266 ILE C N   1 
ATOM   5716 C CA  . ILE C 1 275 ? 28.619  -58.742  31.500  1.00 66.37  ? 266 ILE C CA  1 
ATOM   5717 C C   . ILE C 1 275 ? 27.335  -59.311  30.927  1.00 66.67  ? 266 ILE C C   1 
ATOM   5718 O O   . ILE C 1 275 ? 26.295  -59.311  31.582  1.00 66.50  ? 266 ILE C O   1 
ATOM   5719 C CB  . ILE C 1 275 ? 29.092  -59.684  32.613  1.00 68.25  ? 266 ILE C CB  1 
ATOM   5720 C CG1 . ILE C 1 275 ? 30.381  -59.157  33.231  1.00 71.19  ? 266 ILE C CG1 1 
ATOM   5721 C CG2 . ILE C 1 275 ? 29.310  -61.087  32.068  1.00 67.72  ? 266 ILE C CG2 1 
ATOM   5722 C CD1 . ILE C 1 275 ? 31.560  -59.263  32.303  1.00 76.68  ? 266 ILE C CD1 1 
ATOM   5723 N N   . ILE C 1 276 ? 27.401  -59.789  29.696  1.00 66.70  ? 267 ILE C N   1 
ATOM   5724 C CA  . ILE C 1 276 ? 26.319  -60.594  29.182  1.00 68.17  ? 267 ILE C CA  1 
ATOM   5725 C C   . ILE C 1 276 ? 26.810  -62.021  29.274  1.00 69.27  ? 267 ILE C C   1 
ATOM   5726 O O   . ILE C 1 276 ? 27.628  -62.450  28.461  1.00 70.90  ? 267 ILE C O   1 
ATOM   5727 C CB  . ILE C 1 276 ? 26.060  -60.289  27.694  1.00 68.99  ? 267 ILE C CB  1 
ATOM   5728 C CG1 . ILE C 1 276 ? 25.542  -58.856  27.497  1.00 64.67  ? 267 ILE C CG1 1 
ATOM   5729 C CG2 . ILE C 1 276 ? 25.108  -61.310  27.114  1.00 68.69  ? 267 ILE C CG2 1 
ATOM   5730 C CD1 . ILE C 1 276 ? 26.636  -57.821  27.293  1.00 62.66  ? 267 ILE C CD1 1 
ATOM   5731 N N   . SER C 1 277 ? 26.305  -62.775  30.241  1.00 68.17  ? 268 SER C N   1 
ATOM   5732 C CA  . SER C 1 277 ? 26.794  -64.135  30.415  1.00 72.60  ? 268 SER C CA  1 
ATOM   5733 C C   . SER C 1 277 ? 25.757  -65.071  31.010  1.00 74.12  ? 268 SER C C   1 
ATOM   5734 O O   . SER C 1 277 ? 24.960  -64.673  31.854  1.00 76.30  ? 268 SER C O   1 
ATOM   5735 C CB  . SER C 1 277 ? 28.064  -64.146  31.268  1.00 75.25  ? 268 SER C CB  1 
ATOM   5736 O OG  . SER C 1 277 ? 28.634  -65.442  31.298  1.00 76.93  ? 268 SER C OG  1 
ATOM   5737 N N   . ASP C 1 278 ? 25.784  -66.325  30.581  1.00 75.88  ? 269 ASP C N   1 
ATOM   5738 C CA  . ASP C 1 278 ? 24.883  -67.327  31.135  1.00 77.46  ? 269 ASP C CA  1 
ATOM   5739 C C   . ASP C 1 278 ? 25.532  -68.138  32.253  1.00 80.81  ? 269 ASP C C   1 
ATOM   5740 O O   . ASP C 1 278 ? 24.916  -69.054  32.798  1.00 81.77  ? 269 ASP C O   1 
ATOM   5741 C CB  . ASP C 1 278 ? 24.392  -68.257  30.037  1.00 78.56  ? 269 ASP C CB  1 
ATOM   5742 C CG  . ASP C 1 278 ? 23.670  -67.515  28.946  1.00 79.20  ? 269 ASP C CG  1 
ATOM   5743 O OD1 . ASP C 1 278 ? 23.097  -66.447  29.242  1.00 78.62  ? 269 ASP C OD1 1 
ATOM   5744 O OD2 . ASP C 1 278 ? 23.682  -67.994  27.795  1.00 79.30  ? 269 ASP C OD2 1 
ATOM   5745 N N   . THR C 1 279 ? 26.778  -67.806  32.583  1.00 80.89  ? 270 THR C N   1 
ATOM   5746 C CA  . THR C 1 279 ? 27.490  -68.496  33.654  1.00 82.49  ? 270 THR C CA  1 
ATOM   5747 C C   . THR C 1 279 ? 27.017  -67.993  35.008  1.00 84.40  ? 270 THR C C   1 
ATOM   5748 O O   . THR C 1 279 ? 27.004  -66.788  35.255  1.00 84.45  ? 270 THR C O   1 
ATOM   5749 C CB  . THR C 1 279 ? 29.013  -68.304  33.556  1.00 81.94  ? 270 THR C CB  1 
ATOM   5750 O OG1 . THR C 1 279 ? 29.383  -67.023  34.086  1.00 83.36  ? 270 THR C OG1 1 
ATOM   5751 C CG2 . THR C 1 279 ? 29.464  -68.414  32.117  1.00 78.81  ? 270 THR C CG2 1 
ATOM   5752 N N   . PRO C 1 280 ? 26.635  -68.924  35.893  1.00 85.01  ? 271 PRO C N   1 
ATOM   5753 C CA  . PRO C 1 280 ? 26.010  -68.626  37.186  1.00 86.18  ? 271 PRO C CA  1 
ATOM   5754 C C   . PRO C 1 280 ? 26.876  -67.777  38.111  1.00 86.29  ? 271 PRO C C   1 
ATOM   5755 O O   . PRO C 1 280 ? 28.097  -67.702  37.942  1.00 87.56  ? 271 PRO C O   1 
ATOM   5756 C CB  . PRO C 1 280 ? 25.797  -70.015  37.792  1.00 84.77  ? 271 PRO C CB  1 
ATOM   5757 C CG  . PRO C 1 280 ? 25.682  -70.919  36.607  1.00 84.93  ? 271 PRO C CG  1 
ATOM   5758 C CD  . PRO C 1 280 ? 26.663  -70.371  35.620  1.00 84.40  ? 271 PRO C CD  1 
ATOM   5759 N N   . VAL C 1 281 ? 26.227  -67.145  39.083  1.00 83.80  ? 272 VAL C N   1 
ATOM   5760 C CA  . VAL C 1 281 ? 26.909  -66.341  40.085  1.00 85.67  ? 272 VAL C CA  1 
ATOM   5761 C C   . VAL C 1 281 ? 27.161  -67.159  41.351  1.00 90.79  ? 272 VAL C C   1 
ATOM   5762 O O   . VAL C 1 281 ? 26.344  -68.009  41.717  1.00 91.79  ? 272 VAL C O   1 
ATOM   5763 C CB  . VAL C 1 281 ? 26.077  -65.094  40.440  1.00 83.46  ? 272 VAL C CB  1 
ATOM   5764 C CG1 . VAL C 1 281 ? 26.644  -64.389  41.664  1.00 81.96  ? 272 VAL C CG1 1 
ATOM   5765 C CG2 . VAL C 1 281 ? 26.009  -64.150  39.253  1.00 80.88  ? 272 VAL C CG2 1 
ATOM   5766 N N   . HIS C 1 282 ? 28.295  -66.916  42.007  1.00 91.21  ? 273 HIS C N   1 
ATOM   5767 C CA  . HIS C 1 282 ? 28.578  -67.550  43.295  1.00 90.98  ? 273 HIS C CA  1 
ATOM   5768 C C   . HIS C 1 282 ? 29.076  -66.582  44.364  1.00 92.32  ? 273 HIS C C   1 
ATOM   5769 O O   . HIS C 1 282 ? 29.270  -65.395  44.104  1.00 90.89  ? 273 HIS C O   1 
ATOM   5770 C CB  . HIS C 1 282 ? 29.557  -68.699  43.117  1.00 90.96  ? 273 HIS C CB  1 
ATOM   5771 C CG  . HIS C 1 282 ? 28.977  -69.848  42.363  1.00 92.35  ? 273 HIS C CG  1 
ATOM   5772 N ND1 . HIS C 1 282 ? 28.337  -70.895  42.988  1.00 97.48  ? 273 HIS C ND1 1 
ATOM   5773 C CD2 . HIS C 1 282 ? 28.906  -70.097  41.035  1.00 92.42  ? 273 HIS C CD2 1 
ATOM   5774 C CE1 . HIS C 1 282 ? 27.913  -71.753  42.076  1.00 98.38  ? 273 HIS C CE1 1 
ATOM   5775 N NE2 . HIS C 1 282 ? 28.246  -71.293  40.883  1.00 94.05  ? 273 HIS C NE2 1 
ATOM   5776 N N   . ASP C 1 283 ? 29.292  -67.104  45.568  1.00 95.74  ? 274 ASP C N   1 
ATOM   5777 C CA  . ASP C 1 283 ? 29.600  -66.260  46.721  1.00 96.20  ? 274 ASP C CA  1 
ATOM   5778 C C   . ASP C 1 283 ? 31.082  -65.933  46.819  1.00 95.89  ? 274 ASP C C   1 
ATOM   5779 O O   . ASP C 1 283 ? 31.528  -65.254  47.749  1.00 96.57  ? 274 ASP C O   1 
ATOM   5780 C CB  . ASP C 1 283 ? 29.094  -66.898  48.015  1.00 98.09  ? 274 ASP C CB  1 
ATOM   5781 C CG  . ASP C 1 283 ? 27.884  -66.177  48.576  1.00 103.94 ? 274 ASP C CG  1 
ATOM   5782 O OD1 . ASP C 1 283 ? 27.963  -64.942  48.770  1.00 104.55 ? 274 ASP C OD1 1 
ATOM   5783 O OD2 . ASP C 1 283 ? 26.847  -66.839  48.803  1.00 107.24 ? 274 ASP C OD2 1 
ATOM   5784 N N   . CYS C 1 284 ? 31.829  -66.399  45.826  1.00 93.70  ? 275 CYS C N   1 
ATOM   5785 C CA  . CYS C 1 284 ? 33.268  -66.224  45.800  1.00 91.80  ? 275 CYS C CA  1 
ATOM   5786 C C   . CYS C 1 284 ? 33.615  -64.762  45.579  1.00 91.27  ? 275 CYS C C   1 
ATOM   5787 O O   . CYS C 1 284 ? 32.734  -63.913  45.417  1.00 91.76  ? 275 CYS C O   1 
ATOM   5788 C CB  . CYS C 1 284 ? 33.871  -67.069  44.679  1.00 91.53  ? 275 CYS C CB  1 
ATOM   5789 S SG  . CYS C 1 284 ? 33.079  -66.849  43.055  1.00 101.44 ? 275 CYS C SG  1 
ATOM   5790 N N   . ASN C 1 285 ? 34.907  -64.473  45.566  1.00 90.25  ? 276 ASN C N   1 
ATOM   5791 C CA  . ASN C 1 285 ? 35.372  -63.092  45.540  1.00 92.93  ? 276 ASN C CA  1 
ATOM   5792 C C   . ASN C 1 285 ? 36.585  -63.036  44.513  1.00 91.13  ? 276 ASN C C   1 
ATOM   5793 O O   . ASN C 1 285 ? 37.453  -63.904  44.573  1.00 93.15  ? 276 ASN C O   1 
ATOM   5794 C CB  . ASN C 1 285 ? 35.709  -62.499  46.931  1.00 98.31  ? 276 ASN C CB  1 
ATOM   5795 C CG  . ASN C 1 285 ? 34.463  -62.042  47.678  1.00 108.55 ? 276 ASN C CG  1 
ATOM   5796 O OD1 . ASN C 1 285 ? 33.381  -62.106  47.114  1.00 109.51 ? 276 ASN C OD1 1 
ATOM   5797 N ND2 . ASN C 1 285 ? 34.583  -61.582  48.935  1.00 120.60 ? 276 ASN C ND2 1 
ATOM   5798 N N   . THR C 1 286 ? 36.646  -61.995  43.691  1.00 91.44  ? 277 THR C N   1 
ATOM   5799 C CA  . THR C 1 286 ? 37.725  -61.833  42.725  1.00 89.93  ? 277 THR C CA  1 
ATOM   5800 C C   . THR C 1 286 ? 38.199  -60.383  42.653  1.00 89.62  ? 277 THR C C   1 
ATOM   5801 O O   . THR C 1 286 ? 37.464  -59.458  43.005  1.00 87.72  ? 277 THR C O   1 
ATOM   5802 C CB  . THR C 1 286 ? 37.269  -62.287  41.328  1.00 88.00  ? 277 THR C CB  1 
ATOM   5803 O OG1 . THR C 1 286 ? 38.256  -61.927  40.353  1.00 89.63  ? 277 THR C OG1 1 
ATOM   5804 C CG2 . THR C 1 286 ? 35.949  -61.625  40.975  1.00 87.32  ? 277 THR C CG2 1 
ATOM   5805 N N   . THR C 1 287 ? 39.446  -60.197  42.227  1.00 92.35  ? 278 THR C N   1 
ATOM   5806 C CA  . THR C 1 287 ? 39.946  -58.876  41.862  1.00 92.86  ? 278 THR C CA  1 
ATOM   5807 C C   . THR C 1 287 ? 39.440  -58.557  40.458  1.00 92.37  ? 278 THR C C   1 
ATOM   5808 O O   . THR C 1 287 ? 39.209  -57.396  40.112  1.00 91.99  ? 278 THR C O   1 
ATOM   5809 C CB  . THR C 1 287 ? 41.498  -58.805  41.869  1.00 94.03  ? 278 THR C CB  1 
ATOM   5810 O OG1 . THR C 1 287 ? 42.052  -60.007  41.309  1.00 94.71  ? 278 THR C OG1 1 
ATOM   5811 C CG2 . THR C 1 287 ? 42.027  -58.613  43.284  1.00 90.92  ? 278 THR C CG2 1 
ATOM   5812 N N   . CYS C 1 288 ? 39.254  -59.606  39.661  1.00 89.83  ? 279 CYS C N   1 
ATOM   5813 C CA  . CYS C 1 288 ? 38.912  -59.453  38.255  1.00 88.89  ? 279 CYS C CA  1 
ATOM   5814 C C   . CYS C 1 288 ? 37.856  -60.442  37.784  1.00 87.98  ? 279 CYS C C   1 
ATOM   5815 O O   . CYS C 1 288 ? 37.936  -61.638  38.083  1.00 87.22  ? 279 CYS C O   1 
ATOM   5816 C CB  . CYS C 1 288 ? 40.161  -59.609  37.397  1.00 91.27  ? 279 CYS C CB  1 
ATOM   5817 S SG  . CYS C 1 288 ? 39.843  -60.396  35.814  1.00 98.27  ? 279 CYS C SG  1 
ATOM   5818 N N   . GLN C 1 289 ? 36.893  -59.933  37.017  1.00 85.61  ? 280 GLN C N   1 
ATOM   5819 C CA  . GLN C 1 289 ? 35.759  -60.731  36.570  1.00 83.48  ? 280 GLN C CA  1 
ATOM   5820 C C   . GLN C 1 289 ? 35.546  -60.704  35.061  1.00 82.25  ? 280 GLN C C   1 
ATOM   5821 O O   . GLN C 1 289 ? 35.606  -59.658  34.411  1.00 81.08  ? 280 GLN C O   1 
ATOM   5822 C CB  . GLN C 1 289 ? 34.487  -60.297  37.292  1.00 80.15  ? 280 GLN C CB  1 
ATOM   5823 C CG  . GLN C 1 289 ? 33.266  -61.124  36.927  1.00 80.97  ? 280 GLN C CG  1 
ATOM   5824 C CD  . GLN C 1 289 ? 33.446  -62.605  37.206  1.00 83.94  ? 280 GLN C CD  1 
ATOM   5825 O OE1 . GLN C 1 289 ? 33.561  -63.025  38.356  1.00 84.26  ? 280 GLN C OE1 1 
ATOM   5826 N NE2 . GLN C 1 289 ? 33.462  -63.404  36.150  1.00 83.96  ? 280 GLN C NE2 1 
ATOM   5827 N N   . THR C 1 290 ? 35.278  -61.886  34.527  1.00 80.38  ? 281 THR C N   1 
ATOM   5828 C CA  . THR C 1 290 ? 35.150  -62.094  33.105  1.00 80.98  ? 281 THR C CA  1 
ATOM   5829 C C   . THR C 1 290 ? 33.884  -62.889  32.816  1.00 82.53  ? 281 THR C C   1 
ATOM   5830 O O   . THR C 1 290 ? 33.443  -63.680  33.645  1.00 82.16  ? 281 THR C O   1 
ATOM   5831 C CB  . THR C 1 290 ? 36.369  -62.864  32.575  1.00 82.17  ? 281 THR C CB  1 
ATOM   5832 O OG1 . THR C 1 290 ? 37.155  -62.000  31.750  1.00 85.85  ? 281 THR C OG1 1 
ATOM   5833 C CG2 . THR C 1 290 ? 35.939  -64.078  31.771  1.00 82.41  ? 281 THR C CG2 1 
ATOM   5834 N N   . PRO C 1 291 ? 33.288  -62.678  31.633  1.00 83.75  ? 282 PRO C N   1 
ATOM   5835 C CA  . PRO C 1 291 ? 32.068  -63.411  31.275  1.00 80.25  ? 282 PRO C CA  1 
ATOM   5836 C C   . PRO C 1 291 ? 32.215  -64.919  31.473  1.00 82.76  ? 282 PRO C C   1 
ATOM   5837 O O   . PRO C 1 291 ? 31.266  -65.576  31.909  1.00 84.33  ? 282 PRO C O   1 
ATOM   5838 C CB  . PRO C 1 291 ? 31.898  -63.098  29.784  1.00 76.17  ? 282 PRO C CB  1 
ATOM   5839 C CG  . PRO C 1 291 ? 32.575  -61.785  29.599  1.00 80.44  ? 282 PRO C CG  1 
ATOM   5840 C CD  . PRO C 1 291 ? 33.735  -61.782  30.550  1.00 82.09  ? 282 PRO C CD  1 
ATOM   5841 N N   . LYS C 1 292 ? 33.389  -65.459  31.152  1.00 85.21  ? 283 LYS C N   1 
ATOM   5842 C CA  . LYS C 1 292 ? 33.616  -66.904  31.207  1.00 86.23  ? 283 LYS C CA  1 
ATOM   5843 C C   . LYS C 1 292 ? 33.823  -67.385  32.637  1.00 86.72  ? 283 LYS C C   1 
ATOM   5844 O O   . LYS C 1 292 ? 33.510  -68.527  32.975  1.00 86.75  ? 283 LYS C O   1 
ATOM   5845 C CB  . LYS C 1 292 ? 34.821  -67.288  30.346  1.00 88.55  ? 283 LYS C CB  1 
ATOM   5846 C CG  . LYS C 1 292 ? 34.463  -68.084  29.102  1.00 89.71  ? 283 LYS C CG  1 
ATOM   5847 C CD  . LYS C 1 292 ? 35.708  -68.494  28.317  1.00 93.11  ? 283 LYS C CD  1 
ATOM   5848 C CE  . LYS C 1 292 ? 35.412  -69.629  27.332  1.00 90.49  ? 283 LYS C CE  1 
ATOM   5849 N NZ  . LYS C 1 292 ? 34.550  -69.222  26.183  1.00 89.67  ? 283 LYS C NZ  1 
ATOM   5850 N N   . GLY C 1 293 ? 34.356  -66.500  33.469  1.00 86.76  ? 284 GLY C N   1 
ATOM   5851 C CA  . GLY C 1 293 ? 34.583  -66.793  34.870  1.00 87.32  ? 284 GLY C CA  1 
ATOM   5852 C C   . GLY C 1 293 ? 35.459  -65.693  35.423  1.00 87.91  ? 284 GLY C C   1 
ATOM   5853 O O   . GLY C 1 293 ? 35.686  -64.694  34.741  1.00 87.82  ? 284 GLY C O   1 
ATOM   5854 N N   . ALA C 1 294 ? 35.975  -65.871  36.634  1.00 87.80  ? 285 ALA C N   1 
ATOM   5855 C CA  . ALA C 1 294 ? 36.908  -64.900  37.183  1.00 87.57  ? 285 ALA C CA  1 
ATOM   5856 C C   . ALA C 1 294 ? 38.269  -65.556  37.233  1.00 92.90  ? 285 ALA C C   1 
ATOM   5857 O O   . ALA C 1 294 ? 38.404  -66.742  36.914  1.00 89.46  ? 285 ALA C O   1 
ATOM   5858 C CB  . ALA C 1 294 ? 36.478  -64.459  38.573  1.00 86.48  ? 285 ALA C CB  1 
ATOM   5859 N N   . ILE C 1 295 ? 39.276  -64.798  37.652  1.00 96.57  ? 286 ILE C N   1 
ATOM   5860 C CA  . ILE C 1 295 ? 40.647  -65.292  37.565  1.00 101.91 ? 286 ILE C CA  1 
ATOM   5861 C C   . ILE C 1 295 ? 41.614  -64.728  38.597  1.00 106.12 ? 286 ILE C C   1 
ATOM   5862 O O   . ILE C 1 295 ? 41.444  -63.615  39.107  1.00 100.52 ? 286 ILE C O   1 
ATOM   5863 C CB  . ILE C 1 295 ? 41.246  -65.047  36.164  1.00 101.15 ? 286 ILE C CB  1 
ATOM   5864 C CG1 . ILE C 1 295 ? 40.941  -63.624  35.696  1.00 96.68  ? 286 ILE C CG1 1 
ATOM   5865 C CG2 . ILE C 1 295 ? 40.709  -66.052  35.167  1.00 96.21  ? 286 ILE C CG2 1 
ATOM   5866 C CD1 . ILE C 1 295 ? 41.001  -63.451  34.190  1.00 94.72  ? 286 ILE C CD1 1 
ATOM   5867 N N   . ASN C 1 296 ? 42.652  -65.520  38.854  1.00 112.81 ? 287 ASN C N   1 
ATOM   5868 C CA  . ASN C 1 296 ? 43.728  -65.095  39.733  1.00 117.21 ? 287 ASN C CA  1 
ATOM   5869 C C   . ASN C 1 296 ? 44.904  -64.513  38.944  1.00 119.08 ? 287 ASN C C   1 
ATOM   5870 O O   . ASN C 1 296 ? 45.604  -65.221  38.209  1.00 116.98 ? 287 ASN C O   1 
ATOM   5871 C CB  . ASN C 1 296 ? 44.185  -66.248  40.637  1.00 120.37 ? 287 ASN C CB  1 
ATOM   5872 C CG  . ASN C 1 296 ? 43.974  -65.951  42.117  1.00 123.66 ? 287 ASN C CG  1 
ATOM   5873 O OD1 . ASN C 1 296 ? 44.415  -64.917  42.627  1.00 122.70 ? 287 ASN C OD1 1 
ATOM   5874 N ND2 . ASN C 1 296 ? 43.293  -66.860  42.811  1.00 124.87 ? 287 ASN C ND2 1 
ATOM   5875 N N   . THR C 1 297 ? 45.126  -63.217  39.166  1.00 122.22 ? 288 THR C N   1 
ATOM   5876 C CA  . THR C 1 297 ? 46.215  -62.514  38.510  1.00 121.20 ? 288 THR C CA  1 
ATOM   5877 C C   . THR C 1 297 ? 47.476  -63.025  39.191  1.00 123.76 ? 288 THR C C   1 
ATOM   5878 O O   . THR C 1 297 ? 47.412  -64.026  39.910  1.00 124.71 ? 288 THR C O   1 
ATOM   5879 C CB  . THR C 1 297 ? 46.064  -60.978  38.609  1.00 120.20 ? 288 THR C CB  1 
ATOM   5880 O OG1 . THR C 1 297 ? 47.316  -60.347  38.314  1.00 120.66 ? 288 THR C OG1 1 
ATOM   5881 C CG2 . THR C 1 297 ? 45.589  -60.563  40.004  1.00 115.73 ? 288 THR C CG2 1 
ATOM   5882 N N   . SER C 1 298 ? 48.604  -62.353  38.988  1.00 124.09 ? 289 SER C N   1 
ATOM   5883 C CA  . SER C 1 298 ? 49.926  -62.976  39.093  1.00 124.28 ? 289 SER C CA  1 
ATOM   5884 C C   . SER C 1 298 ? 50.324  -63.428  37.701  1.00 120.74 ? 289 SER C C   1 
ATOM   5885 O O   . SER C 1 298 ? 51.433  -63.921  37.484  1.00 121.34 ? 289 SER C O   1 
ATOM   5886 C CB  . SER C 1 298 ? 49.939  -64.174  40.059  1.00 126.70 ? 289 SER C CB  1 
ATOM   5887 O OG  . SER C 1 298 ? 49.183  -65.271  39.557  1.00 124.25 ? 289 SER C OG  1 
ATOM   5888 N N   . LEU C 1 299 ? 49.401  -63.265  36.758  1.00 118.60 ? 290 LEU C N   1 
ATOM   5889 C CA  . LEU C 1 299 ? 49.771  -63.246  35.349  1.00 116.87 ? 290 LEU C CA  1 
ATOM   5890 C C   . LEU C 1 299 ? 49.229  -61.952  34.730  1.00 115.95 ? 290 LEU C C   1 
ATOM   5891 O O   . LEU C 1 299 ? 48.113  -61.525  35.043  1.00 116.14 ? 290 LEU C O   1 
ATOM   5892 C CB  . LEU C 1 299 ? 49.265  -64.502  34.625  1.00 113.09 ? 290 LEU C CB  1 
ATOM   5893 C CG  . LEU C 1 299 ? 49.875  -65.832  35.095  1.00 112.61 ? 290 LEU C CG  1 
ATOM   5894 C CD1 . LEU C 1 299 ? 49.155  -67.034  34.502  1.00 109.59 ? 290 LEU C CD1 1 
ATOM   5895 C CD2 . LEU C 1 299 ? 51.363  -65.896  34.780  1.00 112.54 ? 290 LEU C CD2 1 
ATOM   5896 N N   . PRO C 1 300 ? 50.041  -61.311  33.874  1.00 112.94 ? 291 PRO C N   1 
ATOM   5897 C CA  . PRO C 1 300 ? 49.819  -60.001  33.242  1.00 110.36 ? 291 PRO C CA  1 
ATOM   5898 C C   . PRO C 1 300 ? 48.798  -59.980  32.106  1.00 106.99 ? 291 PRO C C   1 
ATOM   5899 O O   . PRO C 1 300 ? 48.197  -58.935  31.842  1.00 105.34 ? 291 PRO C O   1 
ATOM   5900 C CB  . PRO C 1 300 ? 51.196  -59.660  32.687  1.00 109.45 ? 291 PRO C CB  1 
ATOM   5901 C CG  . PRO C 1 300 ? 51.757  -60.995  32.320  1.00 109.56 ? 291 PRO C CG  1 
ATOM   5902 C CD  . PRO C 1 300 ? 51.275  -61.949  33.380  1.00 111.17 ? 291 PRO C CD  1 
ATOM   5903 N N   . PHE C 1 301 ? 48.636  -61.109  31.424  1.00 104.92 ? 292 PHE C N   1 
ATOM   5904 C CA  . PHE C 1 301 ? 47.806  -61.159  30.231  1.00 103.07 ? 292 PHE C CA  1 
ATOM   5905 C C   . PHE C 1 301 ? 46.871  -62.337  30.276  1.00 102.94 ? 292 PHE C C   1 
ATOM   5906 O O   . PHE C 1 301 ? 47.110  -63.306  30.993  1.00 103.53 ? 292 PHE C O   1 
ATOM   5907 C CB  . PHE C 1 301 ? 48.672  -61.268  28.989  1.00 102.91 ? 292 PHE C CB  1 
ATOM   5908 C CG  . PHE C 1 301 ? 49.492  -60.055  28.727  1.00 104.46 ? 292 PHE C CG  1 
ATOM   5909 C CD1 . PHE C 1 301 ? 48.956  -58.791  28.899  1.00 104.95 ? 292 PHE C CD1 1 
ATOM   5910 C CD2 . PHE C 1 301 ? 50.806  -60.174  28.318  1.00 104.82 ? 292 PHE C CD2 1 
ATOM   5911 C CE1 . PHE C 1 301 ? 49.717  -57.664  28.655  1.00 106.58 ? 292 PHE C CE1 1 
ATOM   5912 C CE2 . PHE C 1 301 ? 51.572  -59.056  28.074  1.00 103.82 ? 292 PHE C CE2 1 
ATOM   5913 C CZ  . PHE C 1 301 ? 51.029  -57.797  28.242  1.00 105.45 ? 292 PHE C CZ  1 
ATOM   5914 N N   . GLN C 1 302 ? 45.807  -62.258  29.492  1.00 98.79  ? 293 GLN C N   1 
ATOM   5915 C CA  . GLN C 1 302 ? 44.818  -63.308  29.509  1.00 97.71  ? 293 GLN C CA  1 
ATOM   5916 C C   . GLN C 1 302 ? 44.269  -63.514  28.119  1.00 96.59  ? 293 GLN C C   1 
ATOM   5917 O O   . GLN C 1 302 ? 44.020  -62.554  27.393  1.00 98.68  ? 293 GLN C O   1 
ATOM   5918 C CB  . GLN C 1 302 ? 43.705  -62.938  30.481  1.00 96.92  ? 293 GLN C CB  1 
ATOM   5919 C CG  . GLN C 1 302 ? 43.143  -61.556  30.247  1.00 94.88  ? 293 GLN C CG  1 
ATOM   5920 C CD  . GLN C 1 302 ? 41.906  -61.591  29.382  1.00 92.79  ? 293 GLN C CD  1 
ATOM   5921 O OE1 . GLN C 1 302 ? 41.511  -62.651  28.891  1.00 90.17  ? 293 GLN C OE1 1 
ATOM   5922 N NE2 . GLN C 1 302 ? 41.275  -60.435  29.199  1.00 92.38  ? 293 GLN C NE2 1 
ATOM   5923 N N   . ASN C 1 303 ? 44.119  -64.780  27.746  1.00 96.23  ? 294 ASN C N   1 
ATOM   5924 C CA  . ASN C 1 303 ? 43.545  -65.148  26.460  1.00 96.09  ? 294 ASN C CA  1 
ATOM   5925 C C   . ASN C 1 303 ? 42.067  -65.501  26.576  1.00 94.92  ? 294 ASN C C   1 
ATOM   5926 O O   . ASN C 1 303 ? 41.431  -65.891  25.592  1.00 94.45  ? 294 ASN C O   1 
ATOM   5927 C CB  . ASN C 1 303 ? 44.315  -66.321  25.854  1.00 100.12 ? 294 ASN C CB  1 
ATOM   5928 C CG  . ASN C 1 303 ? 44.060  -67.629  26.583  1.00 99.37  ? 294 ASN C CG  1 
ATOM   5929 O OD1 . ASN C 1 303 ? 43.601  -67.645  27.727  1.00 96.62  ? 294 ASN C OD1 1 
ATOM   5930 N ND2 . ASN C 1 303 ? 44.363  -68.737  25.918  1.00 99.20  ? 294 ASN C ND2 1 
ATOM   5931 N N   . ILE C 1 304 ? 41.530  -65.371  27.785  1.00 93.79  ? 295 ILE C N   1 
ATOM   5932 C CA  . ILE C 1 304 ? 40.205  -65.899  28.100  1.00 91.86  ? 295 ILE C CA  1 
ATOM   5933 C C   . ILE C 1 304 ? 39.034  -65.133  27.470  1.00 89.70  ? 295 ILE C C   1 
ATOM   5934 O O   . ILE C 1 304 ? 38.077  -65.749  26.990  1.00 85.61  ? 295 ILE C O   1 
ATOM   5935 C CB  . ILE C 1 304 ? 39.991  -66.002  29.626  1.00 92.12  ? 295 ILE C CB  1 
ATOM   5936 C CG1 . ILE C 1 304 ? 39.004  -67.126  29.952  1.00 93.13  ? 295 ILE C CG1 1 
ATOM   5937 C CG2 . ILE C 1 304 ? 39.533  -64.667  30.198  1.00 91.59  ? 295 ILE C CG2 1 
ATOM   5938 C CD1 . ILE C 1 304 ? 39.516  -68.504  29.598  1.00 95.39  ? 295 ILE C CD1 1 
ATOM   5939 N N   . HIS C 1 305 ? 39.115  -63.804  27.461  1.00 89.24  ? 296 HIS C N   1 
ATOM   5940 C CA  . HIS C 1 305 ? 38.020  -62.980  26.960  1.00 86.14  ? 296 HIS C CA  1 
ATOM   5941 C C   . HIS C 1 305 ? 38.355  -61.497  26.981  1.00 84.89  ? 296 HIS C C   1 
ATOM   5942 O O   . HIS C 1 305 ? 38.939  -61.007  27.944  1.00 86.10  ? 296 HIS C O   1 
ATOM   5943 C CB  . HIS C 1 305 ? 36.759  -63.214  27.789  1.00 87.33  ? 296 HIS C CB  1 
ATOM   5944 C CG  . HIS C 1 305 ? 35.523  -62.648  27.168  1.00 86.35  ? 296 HIS C CG  1 
ATOM   5945 N ND1 . HIS C 1 305 ? 35.250  -61.296  27.150  1.00 85.60  ? 296 HIS C ND1 1 
ATOM   5946 C CD2 . HIS C 1 305 ? 34.493  -63.249  26.527  1.00 83.74  ? 296 HIS C CD2 1 
ATOM   5947 C CE1 . HIS C 1 305 ? 34.104  -61.090  26.528  1.00 84.85  ? 296 HIS C CE1 1 
ATOM   5948 N NE2 . HIS C 1 305 ? 33.623  -62.259  26.141  1.00 87.58  ? 296 HIS C NE2 1 
ATOM   5949 N N   . PRO C 1 306 ? 37.962  -60.781  25.916  1.00 84.63  ? 297 PRO C N   1 
ATOM   5950 C CA  . PRO C 1 306 ? 38.205  -59.353  25.675  1.00 83.45  ? 297 PRO C CA  1 
ATOM   5951 C C   . PRO C 1 306 ? 37.552  -58.441  26.703  1.00 83.16  ? 297 PRO C C   1 
ATOM   5952 O O   . PRO C 1 306 ? 38.050  -57.340  26.939  1.00 81.27  ? 297 PRO C O   1 
ATOM   5953 C CB  . PRO C 1 306 ? 37.554  -59.117  24.312  1.00 81.79  ? 297 PRO C CB  1 
ATOM   5954 C CG  . PRO C 1 306 ? 37.543  -60.444  23.664  1.00 84.14  ? 297 PRO C CG  1 
ATOM   5955 C CD  . PRO C 1 306 ? 37.302  -61.419  24.766  1.00 83.87  ? 297 PRO C CD  1 
ATOM   5956 N N   . ILE C 1 307 ? 36.450  -58.880  27.300  1.00 82.83  ? 298 ILE C N   1 
ATOM   5957 C CA  . ILE C 1 307 ? 35.761  -58.054  28.281  1.00 82.31  ? 298 ILE C CA  1 
ATOM   5958 C C   . ILE C 1 307 ? 36.153  -58.445  29.696  1.00 82.82  ? 298 ILE C C   1 
ATOM   5959 O O   . ILE C 1 307 ? 35.963  -59.587  30.108  1.00 83.01  ? 298 ILE C O   1 
ATOM   5960 C CB  . ILE C 1 307 ? 34.245  -58.160  28.156  1.00 82.67  ? 298 ILE C CB  1 
ATOM   5961 C CG1 . ILE C 1 307 ? 33.802  -57.815  26.738  1.00 81.73  ? 298 ILE C CG1 1 
ATOM   5962 C CG2 . ILE C 1 307 ? 33.576  -57.231  29.160  1.00 86.33  ? 298 ILE C CG2 1 
ATOM   5963 C CD1 . ILE C 1 307 ? 32.301  -57.877  26.551  1.00 86.93  ? 298 ILE C CD1 1 
ATOM   5964 N N   . THR C 1 308 ? 36.700  -57.488  30.436  1.00 82.65  ? 299 THR C N   1 
ATOM   5965 C CA  . THR C 1 308 ? 37.217  -57.758  31.771  1.00 84.84  ? 299 THR C CA  1 
ATOM   5966 C C   . THR C 1 308 ? 36.883  -56.631  32.735  1.00 86.09  ? 299 THR C C   1 
ATOM   5967 O O   . THR C 1 308 ? 36.966  -55.450  32.391  1.00 83.43  ? 299 THR C O   1 
ATOM   5968 C CB  . THR C 1 308 ? 38.747  -57.943  31.761  1.00 86.93  ? 299 THR C CB  1 
ATOM   5969 O OG1 . THR C 1 308 ? 39.362  -56.826  31.106  1.00 90.19  ? 299 THR C OG1 1 
ATOM   5970 C CG2 . THR C 1 308 ? 39.130  -59.218  31.037  1.00 85.63  ? 299 THR C CG2 1 
ATOM   5971 N N   . ILE C 1 309 ? 36.513  -57.004  33.951  1.00 85.11  ? 300 ILE C N   1 
ATOM   5972 C CA  . ILE C 1 309 ? 36.146  -56.015  34.944  1.00 84.94  ? 300 ILE C CA  1 
ATOM   5973 C C   . ILE C 1 309 ? 36.937  -56.174  36.221  1.00 86.65  ? 300 ILE C C   1 
ATOM   5974 O O   . ILE C 1 309 ? 37.174  -57.287  36.688  1.00 87.72  ? 300 ILE C O   1 
ATOM   5975 C CB  . ILE C 1 309 ? 34.646  -56.050  35.240  1.00 84.55  ? 300 ILE C CB  1 
ATOM   5976 C CG1 . ILE C 1 309 ? 33.919  -55.222  34.191  1.00 85.35  ? 300 ILE C CG1 1 
ATOM   5977 C CG2 . ILE C 1 309 ? 34.364  -55.493  36.609  1.00 84.07  ? 300 ILE C CG2 1 
ATOM   5978 C CD1 . ILE C 1 309 ? 34.693  -53.977  33.788  1.00 85.52  ? 300 ILE C CD1 1 
ATOM   5979 N N   . GLY C 1 310 ? 37.334  -55.042  36.787  1.00 88.98  ? 301 GLY C N   1 
ATOM   5980 C CA  . GLY C 1 310 ? 38.205  -55.039  37.943  1.00 91.91  ? 301 GLY C CA  1 
ATOM   5981 C C   . GLY C 1 310 ? 39.630  -54.919  37.452  1.00 94.91  ? 301 GLY C C   1 
ATOM   5982 O O   . GLY C 1 310 ? 39.862  -54.843  36.239  1.00 93.55  ? 301 GLY C O   1 
ATOM   5983 N N   . LYS C 1 311 ? 40.587  -54.894  38.378  1.00 95.32  ? 302 LYS C N   1 
ATOM   5984 C CA  . LYS C 1 311 ? 41.988  -54.860  37.982  1.00 96.99  ? 302 LYS C CA  1 
ATOM   5985 C C   . LYS C 1 311 ? 42.303  -56.175  37.287  1.00 96.10  ? 302 LYS C C   1 
ATOM   5986 O O   . LYS C 1 311 ? 42.141  -57.251  37.871  1.00 94.59  ? 302 LYS C O   1 
ATOM   5987 C CB  . LYS C 1 311 ? 42.896  -54.662  39.197  1.00 96.80  ? 302 LYS C CB  1 
ATOM   5988 C CG  . LYS C 1 311 ? 42.741  -53.304  39.875  1.00 97.88  ? 302 LYS C CG  1 
ATOM   5989 C CD  . LYS C 1 311 ? 42.738  -52.162  38.859  1.00 97.41  ? 302 LYS C CD  1 
ATOM   5990 C CE  . LYS C 1 311 ? 42.796  -50.797  39.547  1.00 96.46  ? 302 LYS C CE  1 
ATOM   5991 N NZ  . LYS C 1 311 ? 42.720  -49.673  38.567  1.00 97.66  ? 302 LYS C NZ  1 
ATOM   5992 N N   . CYS C 1 312 ? 42.765  -56.085  36.043  1.00 95.57  ? 303 CYS C N   1 
ATOM   5993 C CA  . CYS C 1 312 ? 42.859  -57.267  35.195  1.00 96.04  ? 303 CYS C CA  1 
ATOM   5994 C C   . CYS C 1 312 ? 44.008  -57.262  34.200  1.00 95.18  ? 303 CYS C C   1 
ATOM   5995 O O   . CYS C 1 312 ? 44.469  -56.203  33.776  1.00 97.22  ? 303 CYS C O   1 
ATOM   5996 C CB  . CYS C 1 312 ? 41.543  -57.479  34.445  1.00 95.56  ? 303 CYS C CB  1 
ATOM   5997 S SG  . CYS C 1 312 ? 40.346  -58.477  35.348  1.00 96.63  ? 303 CYS C SG  1 
ATOM   5998 N N   . PRO C 1 313 ? 44.457  -58.465  33.815  1.00 95.33  ? 304 PRO C N   1 
ATOM   5999 C CA  . PRO C 1 313 ? 45.435  -58.671  32.748  1.00 99.27  ? 304 PRO C CA  1 
ATOM   6000 C C   . PRO C 1 313 ? 44.901  -58.182  31.414  1.00 99.12  ? 304 PRO C C   1 
ATOM   6001 O O   . PRO C 1 313 ? 43.685  -58.145  31.209  1.00 98.71  ? 304 PRO C O   1 
ATOM   6002 C CB  . PRO C 1 313 ? 45.598  -60.199  32.711  1.00 98.95  ? 304 PRO C CB  1 
ATOM   6003 C CG  . PRO C 1 313 ? 44.399  -60.740  33.388  1.00 94.67  ? 304 PRO C CG  1 
ATOM   6004 C CD  . PRO C 1 313 ? 44.073  -59.737  34.446  1.00 95.64  ? 304 PRO C CD  1 
ATOM   6005 N N   . LYS C 1 314 ? 45.803  -57.805  30.516  1.00 99.49  ? 305 LYS C N   1 
ATOM   6006 C CA  . LYS C 1 314 ? 45.395  -57.419  29.179  1.00 98.73  ? 305 LYS C CA  1 
ATOM   6007 C C   . LYS C 1 314 ? 44.974  -58.648  28.397  1.00 98.05  ? 305 LYS C C   1 
ATOM   6008 O O   . LYS C 1 314 ? 45.610  -59.703  28.469  1.00 97.90  ? 305 LYS C O   1 
ATOM   6009 C CB  . LYS C 1 314 ? 46.514  -56.688  28.438  1.00 100.12 ? 305 LYS C CB  1 
ATOM   6010 C CG  . LYS C 1 314 ? 46.228  -56.477  26.946  1.00 102.12 ? 305 LYS C CG  1 
ATOM   6011 C CD  . LYS C 1 314 ? 44.996  -55.591  26.735  1.00 103.74 ? 305 LYS C CD  1 
ATOM   6012 C CE  . LYS C 1 314 ? 44.649  -55.408  25.261  1.00 100.64 ? 305 LYS C CE  1 
ATOM   6013 N NZ  . LYS C 1 314 ? 43.903  -56.575  24.711  1.00 98.80  ? 305 LYS C NZ  1 
ATOM   6014 N N   . TYR C 1 315 ? 43.880  -58.509  27.661  1.00 97.38  ? 306 TYR C N   1 
ATOM   6015 C CA  . TYR C 1 315 ? 43.475  -59.561  26.762  1.00 95.63  ? 306 TYR C CA  1 
ATOM   6016 C C   . TYR C 1 315 ? 44.389  -59.534  25.568  1.00 95.50  ? 306 TYR C C   1 
ATOM   6017 O O   . TYR C 1 315 ? 44.682  -58.474  25.026  1.00 98.19  ? 306 TYR C O   1 
ATOM   6018 C CB  . TYR C 1 315 ? 42.039  -59.380  26.281  1.00 93.01  ? 306 TYR C CB  1 
ATOM   6019 C CG  . TYR C 1 315 ? 41.649  -60.467  25.311  1.00 92.05  ? 306 TYR C CG  1 
ATOM   6020 C CD1 . TYR C 1 315 ? 41.126  -61.669  25.767  1.00 90.48  ? 306 TYR C CD1 1 
ATOM   6021 C CD2 . TYR C 1 315 ? 41.846  -60.313  23.943  1.00 94.08  ? 306 TYR C CD2 1 
ATOM   6022 C CE1 . TYR C 1 315 ? 40.783  -62.680  24.893  1.00 89.56  ? 306 TYR C CE1 1 
ATOM   6023 C CE2 . TYR C 1 315 ? 41.506  -61.322  23.059  1.00 94.27  ? 306 TYR C CE2 1 
ATOM   6024 C CZ  . TYR C 1 315 ? 40.974  -62.505  23.543  1.00 90.90  ? 306 TYR C CZ  1 
ATOM   6025 O OH  . TYR C 1 315 ? 40.628  -63.520  22.682  1.00 89.93  ? 306 TYR C OH  1 
ATOM   6026 N N   . VAL C 1 316 ? 44.843  -60.704  25.155  1.00 94.93  ? 307 VAL C N   1 
ATOM   6027 C CA  . VAL C 1 316 ? 45.536  -60.817  23.891  1.00 97.90  ? 307 VAL C CA  1 
ATOM   6028 C C   . VAL C 1 316 ? 44.943  -61.997  23.154  1.00 97.52  ? 307 VAL C C   1 
ATOM   6029 O O   . VAL C 1 316 ? 44.599  -63.009  23.760  1.00 95.47  ? 307 VAL C O   1 
ATOM   6030 C CB  . VAL C 1 316 ? 47.034  -61.009  24.091  1.00 99.28  ? 307 VAL C CB  1 
ATOM   6031 C CG1 . VAL C 1 316 ? 47.607  -59.829  24.863  1.00 96.79  ? 307 VAL C CG1 1 
ATOM   6032 C CG2 . VAL C 1 316 ? 47.299  -62.313  24.818  1.00 100.79 ? 307 VAL C CG2 1 
ATOM   6033 N N   . LYS C 1 317 ? 44.820  -61.863  21.842  1.00 100.27 ? 308 LYS C N   1 
ATOM   6034 C CA  . LYS C 1 317 ? 44.140  -62.874  21.046  1.00 102.55 ? 308 LYS C CA  1 
ATOM   6035 C C   . LYS C 1 317 ? 44.945  -64.176  20.931  1.00 103.81 ? 308 LYS C C   1 
ATOM   6036 O O   . LYS C 1 317 ? 44.469  -65.157  20.364  1.00 104.00 ? 308 LYS C O   1 
ATOM   6037 C CB  . LYS C 1 317 ? 43.769  -62.316  19.667  1.00 103.78 ? 308 LYS C CB  1 
ATOM   6038 C CG  . LYS C 1 317 ? 42.423  -62.815  19.144  1.00 102.45 ? 308 LYS C CG  1 
ATOM   6039 C CD  . LYS C 1 317 ? 41.827  -61.878  18.094  1.00 106.87 ? 308 LYS C CD  1 
ATOM   6040 C CE  . LYS C 1 317 ? 40.473  -62.388  17.604  1.00 103.29 ? 308 LYS C CE  1 
ATOM   6041 N NZ  . LYS C 1 317 ? 39.771  -61.381  16.756  1.00 106.43 ? 308 LYS C NZ  1 
ATOM   6042 N N   . SER C 1 318 ? 46.154  -64.191  21.485  1.00 104.88 ? 309 SER C N   1 
ATOM   6043 C CA  . SER C 1 318 ? 47.042  -65.345  21.344  1.00 105.70 ? 309 SER C CA  1 
ATOM   6044 C C   . SER C 1 318 ? 46.631  -66.596  22.124  1.00 108.29 ? 309 SER C C   1 
ATOM   6045 O O   . SER C 1 318 ? 45.649  -66.600  22.868  1.00 107.91 ? 309 SER C O   1 
ATOM   6046 C CB  . SER C 1 318 ? 48.460  -64.977  21.755  1.00 107.50 ? 309 SER C CB  1 
ATOM   6047 O OG  . SER C 1 318 ? 49.132  -66.128  22.237  1.00 110.84 ? 309 SER C OG  1 
ATOM   6048 N N   . THR C 1 319 ? 47.432  -67.647  21.965  1.00 108.72 ? 310 THR C N   1 
ATOM   6049 C CA  . THR C 1 319 ? 47.106  -68.976  22.464  1.00 104.95 ? 310 THR C CA  1 
ATOM   6050 C C   . THR C 1 319 ? 47.905  -69.325  23.699  1.00 105.61 ? 310 THR C C   1 
ATOM   6051 O O   . THR C 1 319 ? 47.379  -69.389  24.808  1.00 104.66 ? 310 THR C O   1 
ATOM   6052 C CB  . THR C 1 319 ? 47.455  -70.043  21.417  1.00 104.43 ? 310 THR C CB  1 
ATOM   6053 O OG1 . THR C 1 319 ? 46.834  -69.718  20.166  1.00 107.03 ? 310 THR C OG1 1 
ATOM   6054 C CG2 . THR C 1 319 ? 46.998  -71.413  21.887  1.00 101.89 ? 310 THR C CG2 1 
ATOM   6055 N N   . LYS C 1 320 ? 49.188  -69.576  23.480  1.00 108.06 ? 311 LYS C N   1 
ATOM   6056 C CA  . LYS C 1 320 ? 50.097  -69.952  24.546  1.00 110.51 ? 311 LYS C CA  1 
ATOM   6057 C C   . LYS C 1 320 ? 51.319  -69.059  24.487  1.00 111.02 ? 311 LYS C C   1 
ATOM   6058 O O   . LYS C 1 320 ? 51.973  -68.970  23.456  1.00 111.70 ? 311 LYS C O   1 
ATOM   6059 C CB  . LYS C 1 320 ? 50.528  -71.411  24.385  1.00 108.82 ? 311 LYS C CB  1 
ATOM   6060 C CG  . LYS C 1 320 ? 49.754  -72.402  25.233  1.00 108.69 ? 311 LYS C CG  1 
ATOM   6061 C CD  . LYS C 1 320 ? 50.466  -72.674  26.547  1.00 107.87 ? 311 LYS C CD  1 
ATOM   6062 C CE  . LYS C 1 320 ? 50.465  -71.458  27.454  1.00 106.81 ? 311 LYS C CE  1 
ATOM   6063 N NZ  . LYS C 1 320 ? 51.091  -71.775  28.758  1.00 107.79 ? 311 LYS C NZ  1 
ATOM   6064 N N   . LEU C 1 321 ? 51.620  -68.386  25.589  1.00 111.90 ? 312 LEU C N   1 
ATOM   6065 C CA  . LEU C 1 321 ? 52.853  -67.621  25.673  1.00 115.34 ? 312 LEU C CA  1 
ATOM   6066 C C   . LEU C 1 321 ? 53.654  -68.001  26.908  1.00 119.17 ? 312 LEU C C   1 
ATOM   6067 O O   . LEU C 1 321 ? 53.222  -67.779  28.043  1.00 116.39 ? 312 LEU C O   1 
ATOM   6068 C CB  . LEU C 1 321 ? 52.576  -66.123  25.647  1.00 113.42 ? 312 LEU C CB  1 
ATOM   6069 C CG  . LEU C 1 321 ? 53.176  -65.434  24.425  1.00 111.71 ? 312 LEU C CG  1 
ATOM   6070 C CD1 . LEU C 1 321 ? 52.566  -65.997  23.153  1.00 114.24 ? 312 LEU C CD1 1 
ATOM   6071 C CD2 . LEU C 1 321 ? 52.961  -63.944  24.511  1.00 110.92 ? 312 LEU C CD2 1 
ATOM   6072 N N   . ARG C 1 322 ? 54.829  -68.573  26.657  1.00 125.04 ? 313 ARG C N   1 
ATOM   6073 C CA  . ARG C 1 322 ? 55.724  -69.081  27.693  1.00 127.30 ? 313 ARG C CA  1 
ATOM   6074 C C   . ARG C 1 322 ? 57.173  -68.755  27.306  1.00 127.09 ? 313 ARG C C   1 
ATOM   6075 O O   . ARG C 1 322 ? 57.519  -68.717  26.123  1.00 125.85 ? 313 ARG C O   1 
ATOM   6076 C CB  . ARG C 1 322 ? 55.527  -70.596  27.878  1.00 127.08 ? 313 ARG C CB  1 
ATOM   6077 C CG  . ARG C 1 322 ? 56.467  -71.254  28.878  1.00 124.18 ? 313 ARG C CG  1 
ATOM   6078 C CD  . ARG C 1 322 ? 56.120  -70.880  30.303  1.00 123.26 ? 313 ARG C CD  1 
ATOM   6079 N NE  . ARG C 1 322 ? 55.065  -71.727  30.852  1.00 124.09 ? 313 ARG C NE  1 
ATOM   6080 C CZ  . ARG C 1 322 ? 54.989  -72.074  32.132  1.00 125.29 ? 313 ARG C CZ  1 
ATOM   6081 N NH1 . ARG C 1 322 ? 55.908  -71.646  32.988  1.00 125.86 ? 313 ARG C NH1 1 
ATOM   6082 N NH2 . ARG C 1 322 ? 54.001  -72.850  32.560  1.00 123.74 ? 313 ARG C NH2 1 
ATOM   6083 N N   . LEU C 1 323 ? 58.006  -68.498  28.309  1.00 127.97 ? 314 LEU C N   1 
ATOM   6084 C CA  . LEU C 1 323 ? 59.375  -68.041  28.080  1.00 126.26 ? 314 LEU C CA  1 
ATOM   6085 C C   . LEU C 1 323 ? 60.474  -69.086  28.209  1.00 125.99 ? 314 LEU C C   1 
ATOM   6086 O O   . LEU C 1 323 ? 60.214  -70.281  28.338  1.00 128.29 ? 314 LEU C O   1 
ATOM   6087 C CB  . LEU C 1 323 ? 59.698  -66.844  28.967  1.00 124.97 ? 314 LEU C CB  1 
ATOM   6088 C CG  . LEU C 1 323 ? 59.136  -65.538  28.423  1.00 123.42 ? 314 LEU C CG  1 
ATOM   6089 C CD1 . LEU C 1 323 ? 60.020  -64.393  28.874  1.00 125.36 ? 314 LEU C CD1 1 
ATOM   6090 C CD2 . LEU C 1 323 ? 59.063  -65.608  26.904  1.00 121.55 ? 314 LEU C CD2 1 
ATOM   6091 N N   . ALA C 1 324 ? 61.710  -68.605  28.148  1.00 125.23 ? 315 ALA C N   1 
ATOM   6092 C CA  . ALA C 1 324 ? 62.881  -69.454  28.258  1.00 124.94 ? 315 ALA C CA  1 
ATOM   6093 C C   . ALA C 1 324 ? 63.723  -69.086  29.476  1.00 127.52 ? 315 ALA C C   1 
ATOM   6094 O O   . ALA C 1 324 ? 63.941  -67.909  29.766  1.00 127.41 ? 315 ALA C O   1 
ATOM   6095 C CB  . ALA C 1 324 ? 63.714  -69.352  26.996  1.00 125.13 ? 315 ALA C CB  1 
ATOM   6096 N N   . THR C 1 325 ? 64.174  -70.105  30.200  1.00 128.13 ? 316 THR C N   1 
ATOM   6097 C CA  . THR C 1 325 ? 65.151  -69.924  31.269  1.00 126.37 ? 316 THR C CA  1 
ATOM   6098 C C   . THR C 1 325 ? 66.314  -70.924  31.147  1.00 125.79 ? 316 THR C C   1 
ATOM   6099 O O   . THR C 1 325 ? 67.464  -70.529  30.955  1.00 125.67 ? 316 THR C O   1 
ATOM   6100 C CB  . THR C 1 325 ? 64.489  -69.966  32.659  1.00 126.51 ? 316 THR C CB  1 
ATOM   6101 O OG1 . THR C 1 325 ? 63.324  -70.796  32.608  1.00 125.57 ? 316 THR C OG1 1 
ATOM   6102 C CG2 . THR C 1 325 ? 64.061  -68.571  33.071  1.00 123.43 ? 316 THR C CG2 1 
ATOM   6103 N N   . GLY C 1 326 ? 66.002  -72.212  31.261  1.00 124.23 ? 317 GLY C N   1 
ATOM   6104 C CA  . GLY C 1 326 ? 66.989  -73.274  31.134  1.00 124.03 ? 317 GLY C CA  1 
ATOM   6105 C C   . GLY C 1 326 ? 67.174  -73.774  29.711  1.00 125.16 ? 317 GLY C C   1 
ATOM   6106 O O   . GLY C 1 326 ? 67.088  -73.002  28.760  1.00 126.24 ? 317 GLY C O   1 
ATOM   6107 N N   . LEU C 1 327 ? 67.476  -75.061  29.570  1.00 125.18 ? 318 LEU C N   1 
ATOM   6108 C CA  . LEU C 1 327 ? 67.586  -75.698  28.260  1.00 125.62 ? 318 LEU C CA  1 
ATOM   6109 C C   . LEU C 1 327 ? 66.759  -76.980  28.218  1.00 124.52 ? 318 LEU C C   1 
ATOM   6110 O O   . LEU C 1 327 ? 65.978  -77.262  29.123  1.00 125.08 ? 318 LEU C O   1 
ATOM   6111 C CB  . LEU C 1 327 ? 69.041  -76.028  27.915  1.00 128.51 ? 318 LEU C CB  1 
ATOM   6112 C CG  . LEU C 1 327 ? 70.143  -74.984  28.088  1.00 129.15 ? 318 LEU C CG  1 
ATOM   6113 C CD1 . LEU C 1 327 ? 70.527  -74.825  29.562  1.00 125.14 ? 318 LEU C CD1 1 
ATOM   6114 C CD2 . LEU C 1 327 ? 71.359  -75.379  27.251  1.00 125.63 ? 318 LEU C CD2 1 
ATOM   6115 N N   . ARG C 1 328 ? 66.926  -77.743  27.147  1.00 124.11 ? 319 ARG C N   1 
ATOM   6116 C CA  . ARG C 1 328 ? 66.338  -79.072  27.039  1.00 127.09 ? 319 ARG C CA  1 
ATOM   6117 C C   . ARG C 1 328 ? 67.077  -80.039  27.972  1.00 129.10 ? 319 ARG C C   1 
ATOM   6118 O O   . ARG C 1 328 ? 68.001  -79.630  28.670  1.00 131.06 ? 319 ARG C O   1 
ATOM   6119 C CB  . ARG C 1 328 ? 66.436  -79.522  25.588  1.00 127.48 ? 319 ARG C CB  1 
ATOM   6120 C CG  . ARG C 1 328 ? 67.283  -78.555  24.759  1.00 128.76 ? 319 ARG C CG  1 
ATOM   6121 C CD  . ARG C 1 328 ? 66.694  -78.284  23.384  1.00 131.50 ? 319 ARG C CD  1 
ATOM   6122 N NE  . ARG C 1 328 ? 67.322  -77.123  22.751  1.00 134.16 ? 319 ARG C NE  1 
ATOM   6123 C CZ  . ARG C 1 328 ? 67.104  -76.738  21.494  1.00 135.16 ? 319 ARG C CZ  1 
ATOM   6124 N NH1 . ARG C 1 328 ? 66.275  -77.426  20.717  1.00 135.12 ? 319 ARG C NH1 1 
ATOM   6125 N NH2 . ARG C 1 328 ? 67.722  -75.666  21.009  1.00 135.35 ? 319 ARG C NH2 1 
ATOM   6126 N N   . ASN C 1 329 ? 66.687  -81.313  27.985  1.00 130.44 ? 320 ASN C N   1 
ATOM   6127 C CA  . ASN C 1 329 ? 67.224  -82.263  28.972  1.00 135.20 ? 320 ASN C CA  1 
ATOM   6128 C C   . ASN C 1 329 ? 67.347  -83.707  28.466  1.00 134.91 ? 320 ASN C C   1 
ATOM   6129 O O   . ASN C 1 329 ? 67.269  -83.958  27.265  1.00 133.35 ? 320 ASN C O   1 
ATOM   6130 C CB  . ASN C 1 329 ? 66.360  -82.241  30.241  1.00 135.29 ? 320 ASN C CB  1 
ATOM   6131 C CG  . ASN C 1 329 ? 67.160  -82.518  31.510  1.00 135.11 ? 320 ASN C CG  1 
ATOM   6132 O OD1 . ASN C 1 329 ? 67.627  -81.593  32.178  1.00 135.47 ? 320 ASN C OD1 1 
ATOM   6133 N ND2 . ASN C 1 329 ? 67.307  -83.793  31.854  1.00 133.14 ? 320 ASN C ND2 1 
ATOM   6134 N N   . VAL C 1 330 ? 67.588  -84.636  29.395  1.00 136.17 ? 321 VAL C N   1 
ATOM   6135 C CA  . VAL C 1 330 ? 67.377  -86.078  29.178  1.00 136.28 ? 321 VAL C CA  1 
ATOM   6136 C C   . VAL C 1 330 ? 68.617  -86.889  28.789  1.00 133.83 ? 321 VAL C C   1 
ATOM   6137 O O   . VAL C 1 330 ? 68.765  -88.049  29.190  1.00 130.23 ? 321 VAL C O   1 
ATOM   6138 C CB  . VAL C 1 330 ? 66.235  -86.346  28.164  1.00 135.25 ? 321 VAL C CB  1 
ATOM   6139 C CG1 . VAL C 1 330 ? 66.680  -87.344  27.099  1.00 132.91 ? 321 VAL C CG1 1 
ATOM   6140 C CG2 . VAL C 1 330 ? 64.979  -86.821  28.887  1.00 132.55 ? 321 VAL C CG2 1 
ATOM   6141 N N   . ILE D 2 10  ? 79.414  -81.090  24.561  1.00 125.22 ? 10  ILE D N   1 
ATOM   6142 C CA  . ILE D 2 10  ? 78.217  -81.807  24.135  1.00 127.65 ? 10  ILE D CA  1 
ATOM   6143 C C   . ILE D 2 10  ? 77.552  -82.546  25.288  1.00 129.35 ? 10  ILE D C   1 
ATOM   6144 O O   . ILE D 2 10  ? 78.221  -83.131  26.140  1.00 131.35 ? 10  ILE D O   1 
ATOM   6145 C CB  . ILE D 2 10  ? 78.524  -82.812  23.004  1.00 127.67 ? 10  ILE D CB  1 
ATOM   6146 C CG1 . ILE D 2 10  ? 78.236  -82.184  21.636  1.00 121.43 ? 10  ILE D CG1 1 
ATOM   6147 C CG2 . ILE D 2 10  ? 77.707  -84.092  23.183  1.00 126.44 ? 10  ILE D CG2 1 
ATOM   6148 C CD1 . ILE D 2 10  ? 78.932  -80.858  21.395  1.00 114.25 ? 10  ILE D CD1 1 
ATOM   6149 N N   . GLU D 2 11  ? 76.225  -82.511  25.308  1.00 131.11 ? 11  GLU D N   1 
ATOM   6150 C CA  . GLU D 2 11  ? 75.464  -83.233  26.316  1.00 134.35 ? 11  GLU D CA  1 
ATOM   6151 C C   . GLU D 2 11  ? 74.436  -84.158  25.686  1.00 134.72 ? 11  GLU D C   1 
ATOM   6152 O O   . GLU D 2 11  ? 73.580  -83.719  24.918  1.00 133.43 ? 11  GLU D O   1 
ATOM   6153 C CB  . GLU D 2 11  ? 74.741  -82.268  27.259  1.00 134.49 ? 11  GLU D CB  1 
ATOM   6154 C CG  . GLU D 2 11  ? 73.800  -82.983  28.220  1.00 133.83 ? 11  GLU D CG  1 
ATOM   6155 C CD  . GLU D 2 11  ? 72.802  -82.056  28.879  1.00 134.41 ? 11  GLU D CD  1 
ATOM   6156 O OE1 . GLU D 2 11  ? 72.920  -80.827  28.696  1.00 136.01 ? 11  GLU D OE1 1 
ATOM   6157 O OE2 . GLU D 2 11  ? 71.897  -82.559  29.576  1.00 133.83 ? 11  GLU D OE2 1 
ATOM   6158 N N   . GLY D 2 12  ? 74.530  -85.444  26.007  1.00 136.15 ? 12  GLY D N   1 
ATOM   6159 C CA  . GLY D 2 12  ? 73.457  -86.373  25.710  1.00 136.84 ? 12  GLY D CA  1 
ATOM   6160 C C   . GLY D 2 12  ? 72.255  -86.055  26.581  1.00 136.97 ? 12  GLY D C   1 
ATOM   6161 O O   . GLY D 2 12  ? 71.150  -85.836  26.086  1.00 138.08 ? 12  GLY D O   1 
ATOM   6162 N N   . GLY D 2 13  ? 72.481  -86.022  27.890  1.00 135.86 ? 13  GLY D N   1 
ATOM   6163 C CA  . GLY D 2 13  ? 71.464  -85.587  28.827  1.00 135.01 ? 13  GLY D CA  1 
ATOM   6164 C C   . GLY D 2 13  ? 71.911  -85.797  30.254  1.00 134.28 ? 13  GLY D C   1 
ATOM   6165 O O   . GLY D 2 13  ? 72.808  -86.598  30.519  1.00 133.08 ? 13  GLY D O   1 
ATOM   6166 N N   . TRP D 2 14  ? 71.276  -85.090  31.181  1.00 135.93 ? 14  TRP D N   1 
ATOM   6167 C CA  . TRP D 2 14  ? 71.649  -85.207  32.583  1.00 135.36 ? 14  TRP D CA  1 
ATOM   6168 C C   . TRP D 2 14  ? 70.454  -85.539  33.466  1.00 134.01 ? 14  TRP D C   1 
ATOM   6169 O O   . TRP D 2 14  ? 69.327  -85.122  33.195  1.00 132.89 ? 14  TRP D O   1 
ATOM   6170 C CB  . TRP D 2 14  ? 72.383  -83.947  33.077  1.00 133.70 ? 14  TRP D CB  1 
ATOM   6171 C CG  . TRP D 2 14  ? 71.541  -82.705  33.233  1.00 133.86 ? 14  TRP D CG  1 
ATOM   6172 C CD1 . TRP D 2 14  ? 70.186  -82.636  33.399  1.00 133.52 ? 14  TRP D CD1 1 
ATOM   6173 C CD2 . TRP D 2 14  ? 72.011  -81.350  33.241  1.00 134.99 ? 14  TRP D CD2 1 
ATOM   6174 N NE1 . TRP D 2 14  ? 69.785  -81.327  33.510  1.00 132.66 ? 14  TRP D NE1 1 
ATOM   6175 C CE2 . TRP D 2 14  ? 70.887  -80.517  33.415  1.00 134.23 ? 14  TRP D CE2 1 
ATOM   6176 C CE3 . TRP D 2 14  ? 73.275  -80.762  33.117  1.00 133.62 ? 14  TRP D CE3 1 
ATOM   6177 C CZ2 . TRP D 2 14  ? 70.989  -79.125  33.469  1.00 132.97 ? 14  TRP D CZ2 1 
ATOM   6178 C CZ3 . TRP D 2 14  ? 73.375  -79.380  33.169  1.00 131.53 ? 14  TRP D CZ3 1 
ATOM   6179 C CH2 . TRP D 2 14  ? 72.238  -78.578  33.341  1.00 131.77 ? 14  TRP D CH2 1 
ATOM   6180 N N   . THR D 2 15  ? 70.708  -86.313  34.512  1.00 133.79 ? 15  THR D N   1 
ATOM   6181 C CA  . THR D 2 15  ? 69.686  -86.583  35.510  1.00 133.43 ? 15  THR D CA  1 
ATOM   6182 C C   . THR D 2 15  ? 69.676  -85.447  36.539  1.00 134.46 ? 15  THR D C   1 
ATOM   6183 O O   . THR D 2 15  ? 68.752  -84.628  36.562  1.00 132.32 ? 15  THR D O   1 
ATOM   6184 C CB  . THR D 2 15  ? 69.893  -87.963  36.168  1.00 130.56 ? 15  THR D CB  1 
ATOM   6185 O OG1 . THR D 2 15  ? 69.628  -87.877  37.572  1.00 129.79 ? 15  THR D OG1 1 
ATOM   6186 C CG2 . THR D 2 15  ? 71.319  -88.457  35.944  1.00 131.03 ? 15  THR D CG2 1 
ATOM   6187 N N   . GLY D 2 16  ? 70.699  -85.396  37.386  1.00 133.88 ? 16  GLY D N   1 
ATOM   6188 C CA  . GLY D 2 16  ? 70.941  -84.215  38.193  1.00 130.97 ? 16  GLY D CA  1 
ATOM   6189 C C   . GLY D 2 16  ? 71.900  -83.250  37.519  1.00 131.56 ? 16  GLY D C   1 
ATOM   6190 O O   . GLY D 2 16  ? 72.770  -83.658  36.754  1.00 132.95 ? 16  GLY D O   1 
ATOM   6191 N N   . MET D 2 17  ? 71.722  -81.961  37.779  1.00 132.52 ? 17  MET D N   1 
ATOM   6192 C CA  . MET D 2 17  ? 72.764  -80.975  37.522  1.00 133.76 ? 17  MET D CA  1 
ATOM   6193 C C   . MET D 2 17  ? 73.449  -80.712  38.854  1.00 131.61 ? 17  MET D C   1 
ATOM   6194 O O   . MET D 2 17  ? 74.337  -79.866  38.957  1.00 129.70 ? 17  MET D O   1 
ATOM   6195 C CB  . MET D 2 17  ? 72.181  -79.677  36.951  1.00 134.82 ? 17  MET D CB  1 
ATOM   6196 C CG  . MET D 2 17  ? 73.230  -78.656  36.510  1.00 134.08 ? 17  MET D CG  1 
ATOM   6197 S SD  . MET D 2 17  ? 72.519  -77.064  36.032  1.00 129.73 ? 17  MET D SD  1 
ATOM   6198 C CE  . MET D 2 17  ? 73.972  -76.203  35.435  1.00 128.02 ? 17  MET D CE  1 
ATOM   6199 N N   . VAL D 2 18  ? 73.027  -81.469  39.866  1.00 130.94 ? 18  VAL D N   1 
ATOM   6200 C CA  . VAL D 2 18  ? 73.187  -81.075  41.262  1.00 130.76 ? 18  VAL D CA  1 
ATOM   6201 C C   . VAL D 2 18  ? 72.372  -79.796  41.444  1.00 129.71 ? 18  VAL D C   1 
ATOM   6202 O O   . VAL D 2 18  ? 71.170  -79.790  41.175  1.00 128.30 ? 18  VAL D O   1 
ATOM   6203 C CB  . VAL D 2 18  ? 74.666  -80.878  41.675  1.00 128.79 ? 18  VAL D CB  1 
ATOM   6204 C CG1 . VAL D 2 18  ? 74.784  -80.720  43.189  1.00 126.81 ? 18  VAL D CG1 1 
ATOM   6205 C CG2 . VAL D 2 18  ? 75.500  -82.057  41.215  1.00 128.53 ? 18  VAL D CG2 1 
ATOM   6206 N N   . ASP D 2 19  ? 73.009  -78.718  41.888  1.00 129.73 ? 19  ASP D N   1 
ATOM   6207 C CA  . ASP D 2 19  ? 72.316  -77.445  42.054  1.00 127.92 ? 19  ASP D CA  1 
ATOM   6208 C C   . ASP D 2 19  ? 71.530  -77.089  40.797  1.00 129.98 ? 19  ASP D C   1 
ATOM   6209 O O   . ASP D 2 19  ? 71.121  -75.943  40.612  1.00 132.89 ? 19  ASP D O   1 
ATOM   6210 C CB  . ASP D 2 19  ? 73.315  -76.336  42.383  1.00 126.59 ? 19  ASP D CB  1 
ATOM   6211 C CG  . ASP D 2 19  ? 74.749  -76.830  42.380  1.00 128.96 ? 19  ASP D CG  1 
ATOM   6212 O OD1 . ASP D 2 19  ? 75.034  -77.817  41.667  1.00 129.30 ? 19  ASP D OD1 1 
ATOM   6213 O OD2 . ASP D 2 19  ? 75.590  -76.237  43.088  1.00 126.79 ? 19  ASP D OD2 1 
ATOM   6214 N N   . ALA D 2 35  ? 78.334  -83.143  40.113  1.00 107.73 ? 35  ALA D N   1 
ATOM   6215 C CA  . ALA D 2 35  ? 78.894  -81.944  40.731  1.00 114.40 ? 35  ALA D CA  1 
ATOM   6216 C C   . ALA D 2 35  ? 79.038  -80.797  39.725  1.00 119.07 ? 35  ALA D C   1 
ATOM   6217 O O   . ALA D 2 35  ? 79.780  -80.907  38.745  1.00 116.19 ? 35  ALA D O   1 
ATOM   6218 C CB  . ALA D 2 35  ? 80.231  -82.262  41.382  1.00 113.47 ? 35  ALA D CB  1 
ATOM   6219 N N   . ALA D 2 36  ? 78.337  -79.692  39.984  1.00 124.28 ? 36  ALA D N   1 
ATOM   6220 C CA  . ALA D 2 36  ? 78.258  -78.567  39.042  1.00 125.58 ? 36  ALA D CA  1 
ATOM   6221 C C   . ALA D 2 36  ? 78.682  -77.220  39.651  1.00 125.94 ? 36  ALA D C   1 
ATOM   6222 O O   . ALA D 2 36  ? 79.160  -77.167  40.782  1.00 125.99 ? 36  ALA D O   1 
ATOM   6223 C CB  . ALA D 2 36  ? 76.859  -78.467  38.431  1.00 124.55 ? 36  ALA D CB  1 
ATOM   6224 N N   . ASP D 2 37  ? 78.483  -76.141  38.892  1.00 126.98 ? 37  ASP D N   1 
ATOM   6225 C CA  . ASP D 2 37  ? 79.161  -74.847  39.112  1.00 133.44 ? 37  ASP D CA  1 
ATOM   6226 C C   . ASP D 2 37  ? 78.620  -73.891  40.202  1.00 134.64 ? 37  ASP D C   1 
ATOM   6227 O O   . ASP D 2 37  ? 77.650  -74.201  40.898  1.00 135.18 ? 37  ASP D O   1 
ATOM   6228 C CB  . ASP D 2 37  ? 79.260  -74.097  37.774  1.00 134.42 ? 37  ASP D CB  1 
ATOM   6229 C CG  . ASP D 2 37  ? 80.133  -72.857  37.858  1.00 135.53 ? 37  ASP D CG  1 
ATOM   6230 O OD1 . ASP D 2 37  ? 81.372  -72.990  37.734  1.00 136.66 ? 37  ASP D OD1 1 
ATOM   6231 O OD2 . ASP D 2 37  ? 79.577  -71.752  38.050  1.00 134.18 ? 37  ASP D OD2 1 
ATOM   6232 N N   . LEU D 2 38  ? 79.271  -72.725  40.321  1.00 134.35 ? 38  LEU D N   1 
ATOM   6233 C CA  . LEU D 2 38  ? 78.934  -71.689  41.303  1.00 132.26 ? 38  LEU D CA  1 
ATOM   6234 C C   . LEU D 2 38  ? 78.554  -70.351  40.658  1.00 132.05 ? 38  LEU D C   1 
ATOM   6235 O O   . LEU D 2 38  ? 77.385  -69.977  40.601  1.00 132.71 ? 38  LEU D O   1 
ATOM   6236 C CB  . LEU D 2 38  ? 80.129  -71.401  42.232  1.00 134.18 ? 38  LEU D CB  1 
ATOM   6237 C CG  . LEU D 2 38  ? 81.039  -72.447  42.890  1.00 131.78 ? 38  LEU D CG  1 
ATOM   6238 C CD1 . LEU D 2 38  ? 81.970  -73.091  41.872  1.00 130.09 ? 38  LEU D CD1 1 
ATOM   6239 C CD2 . LEU D 2 38  ? 81.850  -71.797  44.010  1.00 122.12 ? 38  LEU D CD2 1 
ATOM   6240 N N   . LYS D 2 39  ? 79.567  -69.642  40.169  1.00 132.37 ? 39  LYS D N   1 
ATOM   6241 C CA  . LYS D 2 39  ? 79.451  -68.230  39.816  1.00 133.63 ? 39  LYS D CA  1 
ATOM   6242 C C   . LYS D 2 39  ? 78.751  -67.990  38.484  1.00 135.40 ? 39  LYS D C   1 
ATOM   6243 O O   . LYS D 2 39  ? 78.039  -67.001  38.319  1.00 135.75 ? 39  LYS D O   1 
ATOM   6244 C CB  . LYS D 2 39  ? 80.843  -67.600  39.796  1.00 132.57 ? 39  LYS D CB  1 
ATOM   6245 C CG  . LYS D 2 39  ? 81.723  -68.063  40.947  1.00 131.26 ? 39  LYS D CG  1 
ATOM   6246 C CD  . LYS D 2 39  ? 81.218  -67.519  42.271  1.00 131.62 ? 39  LYS D CD  1 
ATOM   6247 C CE  . LYS D 2 39  ? 81.533  -66.037  42.401  1.00 132.65 ? 39  LYS D CE  1 
ATOM   6248 N NZ  . LYS D 2 39  ? 80.527  -65.311  43.225  1.00 130.15 ? 39  LYS D NZ  1 
ATOM   6249 N N   . SER D 2 40  ? 78.968  -68.895  37.535  1.00 135.80 ? 40  SER D N   1 
ATOM   6250 C CA  . SER D 2 40  ? 78.349  -68.801  36.217  1.00 136.20 ? 40  SER D CA  1 
ATOM   6251 C C   . SER D 2 40  ? 76.851  -68.588  36.350  1.00 136.44 ? 40  SER D C   1 
ATOM   6252 O O   . SER D 2 40  ? 76.317  -67.543  35.976  1.00 136.10 ? 40  SER D O   1 
ATOM   6253 C CB  . SER D 2 40  ? 78.591  -70.090  35.438  1.00 134.12 ? 40  SER D CB  1 
ATOM   6254 O OG  . SER D 2 40  ? 77.852  -71.163  35.999  1.00 133.85 ? 40  SER D OG  1 
ATOM   6255 N N   . THR D 2 41  ? 76.183  -69.601  36.889  1.00 136.84 ? 41  THR D N   1 
ATOM   6256 C CA  . THR D 2 41  ? 74.755  -69.549  37.140  1.00 135.93 ? 41  THR D CA  1 
ATOM   6257 C C   . THR D 2 41  ? 74.436  -68.218  37.807  1.00 136.50 ? 41  THR D C   1 
ATOM   6258 O O   . THR D 2 41  ? 73.665  -67.417  37.278  1.00 136.63 ? 41  THR D O   1 
ATOM   6259 C CB  . THR D 2 41  ? 74.305  -70.729  38.018  1.00 135.30 ? 41  THR D CB  1 
ATOM   6260 O OG1 . THR D 2 41  ? 74.874  -71.945  37.515  1.00 134.56 ? 41  THR D OG1 1 
ATOM   6261 C CG2 . THR D 2 41  ? 72.794  -70.849  38.015  1.00 137.23 ? 41  THR D CG2 1 
ATOM   6262 N N   . GLN D 2 42  ? 75.046  -67.989  38.966  1.00 135.38 ? 42  GLN D N   1 
ATOM   6263 C CA  . GLN D 2 42  ? 74.879  -66.745  39.704  1.00 135.57 ? 42  GLN D CA  1 
ATOM   6264 C C   . GLN D 2 42  ? 74.979  -65.547  38.770  1.00 137.08 ? 42  GLN D C   1 
ATOM   6265 O O   . GLN D 2 42  ? 74.240  -64.571  38.911  1.00 136.81 ? 42  GLN D O   1 
ATOM   6266 C CB  . GLN D 2 42  ? 75.958  -66.637  40.782  1.00 134.99 ? 42  GLN D CB  1 
ATOM   6267 C CG  . GLN D 2 42  ? 76.595  -65.256  40.894  1.00 136.78 ? 42  GLN D CG  1 
ATOM   6268 C CD  . GLN D 2 42  ? 77.954  -65.281  41.580  1.00 134.82 ? 42  GLN D CD  1 
ATOM   6269 O OE1 . GLN D 2 42  ? 78.391  -66.316  42.084  1.00 133.21 ? 42  GLN D OE1 1 
ATOM   6270 N NE2 . GLN D 2 42  ? 78.629  -64.136  41.596  1.00 132.18 ? 42  GLN D NE2 1 
ATOM   6271 N N   . ASN D 2 43  ? 75.901  -65.618  37.818  1.00 137.99 ? 43  ASN D N   1 
ATOM   6272 C CA  . ASN D 2 43  ? 76.035  -64.559  36.831  1.00 138.78 ? 43  ASN D CA  1 
ATOM   6273 C C   . ASN D 2 43  ? 74.949  -64.640  35.772  1.00 138.65 ? 43  ASN D C   1 
ATOM   6274 O O   . ASN D 2 43  ? 74.042  -63.809  35.734  1.00 139.41 ? 43  ASN D O   1 
ATOM   6275 C CB  . ASN D 2 43  ? 77.413  -64.604  36.163  1.00 139.27 ? 43  ASN D CB  1 
ATOM   6276 C CG  . ASN D 2 43  ? 78.434  -63.744  36.878  1.00 139.33 ? 43  ASN D CG  1 
ATOM   6277 O OD1 . ASN D 2 43  ? 78.077  -62.849  37.645  1.00 139.48 ? 43  ASN D OD1 1 
ATOM   6278 N ND2 . ASN D 2 43  ? 79.712  -64.001  36.621  1.00 135.11 ? 43  ASN D ND2 1 
ATOM   6279 N N   . ALA D 2 44  ? 75.037  -65.665  34.930  1.00 139.00 ? 44  ALA D N   1 
ATOM   6280 C CA  . ALA D 2 44  ? 74.163  -65.792  33.771  1.00 139.66 ? 44  ALA D CA  1 
ATOM   6281 C C   . ALA D 2 44  ? 72.691  -65.631  34.132  1.00 141.05 ? 44  ALA D C   1 
ATOM   6282 O O   . ALA D 2 44  ? 71.914  -65.078  33.354  1.00 140.86 ? 44  ALA D O   1 
ATOM   6283 C CB  . ALA D 2 44  ? 74.398  -67.123  33.071  1.00 136.46 ? 44  ALA D CB  1 
ATOM   6284 N N   . ILE D 2 45  ? 72.309  -66.102  35.314  1.00 139.94 ? 45  ILE D N   1 
ATOM   6285 C CA  . ILE D 2 45  ? 70.919  -66.010  35.741  1.00 138.97 ? 45  ILE D CA  1 
ATOM   6286 C C   . ILE D 2 45  ? 70.556  -64.576  36.124  1.00 138.22 ? 45  ILE D C   1 
ATOM   6287 O O   . ILE D 2 45  ? 69.383  -64.213  36.167  1.00 139.26 ? 45  ILE D O   1 
ATOM   6288 C CB  . ILE D 2 45  ? 70.621  -66.977  36.899  1.00 136.91 ? 45  ILE D CB  1 
ATOM   6289 C CG1 . ILE D 2 45  ? 70.875  -68.417  36.451  1.00 136.28 ? 45  ILE D CG1 1 
ATOM   6290 C CG2 . ILE D 2 45  ? 69.188  -66.826  37.371  1.00 135.87 ? 45  ILE D CG2 1 
ATOM   6291 C CD1 . ILE D 2 45  ? 70.050  -68.848  35.251  1.00 132.72 ? 45  ILE D CD1 1 
ATOM   6292 N N   . ASP D 2 46  ? 71.570  -63.756  36.370  1.00 135.92 ? 46  ASP D N   1 
ATOM   6293 C CA  . ASP D 2 46  ? 71.339  -62.357  36.702  1.00 137.01 ? 46  ASP D CA  1 
ATOM   6294 C C   . ASP D 2 46  ? 70.925  -61.584  35.456  1.00 139.87 ? 46  ASP D C   1 
ATOM   6295 O O   . ASP D 2 46  ? 69.820  -61.047  35.385  1.00 140.93 ? 46  ASP D O   1 
ATOM   6296 C CB  . ASP D 2 46  ? 72.589  -61.731  37.327  1.00 138.11 ? 46  ASP D CB  1 
ATOM   6297 C CG  . ASP D 2 46  ? 72.377  -60.278  37.727  1.00 138.80 ? 46  ASP D CG  1 
ATOM   6298 O OD1 . ASP D 2 46  ? 71.208  -59.872  37.892  1.00 138.98 ? 46  ASP D OD1 1 
ATOM   6299 O OD2 . ASP D 2 46  ? 73.377  -59.543  37.880  1.00 136.81 ? 46  ASP D OD2 1 
ATOM   6300 N N   . GLU D 2 47  ? 71.823  -61.521  34.479  1.00 141.51 ? 47  GLU D N   1 
ATOM   6301 C CA  . GLU D 2 47  ? 71.559  -60.804  33.235  1.00 142.28 ? 47  GLU D CA  1 
ATOM   6302 C C   . GLU D 2 47  ? 70.350  -61.347  32.464  1.00 141.14 ? 47  GLU D C   1 
ATOM   6303 O O   . GLU D 2 47  ? 69.730  -60.617  31.693  1.00 140.36 ? 47  GLU D O   1 
ATOM   6304 C CB  . GLU D 2 47  ? 72.808  -60.786  32.345  1.00 143.71 ? 47  GLU D CB  1 
ATOM   6305 C CG  . GLU D 2 47  ? 73.902  -59.841  32.830  1.00 142.08 ? 47  GLU D CG  1 
ATOM   6306 C CD  . GLU D 2 47  ? 75.181  -59.966  32.025  1.00 141.68 ? 47  GLU D CD  1 
ATOM   6307 O OE1 . GLU D 2 47  ? 75.288  -60.914  31.215  1.00 139.25 ? 47  GLU D OE1 1 
ATOM   6308 O OE2 . GLU D 2 47  ? 76.079  -59.116  32.206  1.00 141.14 ? 47  GLU D OE2 1 
ATOM   6309 N N   . ILE D 2 48  ? 70.019  -62.622  32.670  1.00 141.08 ? 48  ILE D N   1 
ATOM   6310 C CA  . ILE D 2 48  ? 68.826  -63.210  32.056  1.00 140.84 ? 48  ILE D CA  1 
ATOM   6311 C C   . ILE D 2 48  ? 67.574  -62.500  32.550  1.00 141.20 ? 48  ILE D C   1 
ATOM   6312 O O   . ILE D 2 48  ? 66.602  -62.322  31.815  1.00 139.48 ? 48  ILE D O   1 
ATOM   6313 C CB  . ILE D 2 48  ? 68.686  -64.711  32.381  1.00 140.24 ? 48  ILE D CB  1 
ATOM   6314 C CG1 . ILE D 2 48  ? 69.644  -65.538  31.522  1.00 140.18 ? 48  ILE D CG1 1 
ATOM   6315 C CG2 . ILE D 2 48  ? 67.254  -65.173  32.143  1.00 137.66 ? 48  ILE D CG2 1 
ATOM   6316 C CD1 . ILE D 2 48  ? 68.961  -66.330  30.420  1.00 137.32 ? 48  ILE D CD1 1 
ATOM   6317 N N   . THR D 2 49  ? 67.609  -62.103  33.814  1.00 141.40 ? 49  THR D N   1 
ATOM   6318 C CA  . THR D 2 49  ? 66.516  -61.359  34.410  1.00 140.79 ? 49  THR D CA  1 
ATOM   6319 C C   . THR D 2 49  ? 66.444  -59.946  33.833  1.00 140.92 ? 49  THR D C   1 
ATOM   6320 O O   . THR D 2 49  ? 65.357  -59.431  33.572  1.00 141.61 ? 49  THR D O   1 
ATOM   6321 C CB  . THR D 2 49  ? 66.675  -61.301  35.931  1.00 141.93 ? 49  THR D CB  1 
ATOM   6322 O OG1 . THR D 2 49  ? 67.937  -60.704  36.256  1.00 140.39 ? 49  THR D OG1 1 
ATOM   6323 C CG2 . THR D 2 49  ? 66.629  -62.706  36.508  1.00 141.65 ? 49  THR D CG2 1 
ATOM   6324 N N   . ASN D 2 50  ? 67.608  -59.332  33.627  1.00 141.51 ? 50  ASN D N   1 
ATOM   6325 C CA  . ASN D 2 50  ? 67.695  -57.975  33.084  1.00 142.61 ? 50  ASN D CA  1 
ATOM   6326 C C   . ASN D 2 50  ? 67.013  -57.861  31.722  1.00 143.32 ? 50  ASN D C   1 
ATOM   6327 O O   . ASN D 2 50  ? 66.481  -56.809  31.364  1.00 144.33 ? 50  ASN D O   1 
ATOM   6328 C CB  . ASN D 2 50  ? 69.163  -57.534  32.980  1.00 143.48 ? 50  ASN D CB  1 
ATOM   6329 C CG  . ASN D 2 50  ? 69.345  -56.027  33.146  1.00 143.90 ? 50  ASN D CG  1 
ATOM   6330 O OD1 . ASN D 2 50  ? 69.986  -55.568  34.095  1.00 141.45 ? 50  ASN D OD1 1 
ATOM   6331 N ND2 . ASN D 2 50  ? 68.790  -55.253  32.215  1.00 146.24 ? 50  ASN D ND2 1 
ATOM   6332 N N   . LYS D 2 51  ? 67.030  -58.956  30.969  1.00 143.05 ? 51  LYS D N   1 
ATOM   6333 C CA  . LYS D 2 51  ? 66.411  -59.005  29.646  1.00 142.66 ? 51  LYS D CA  1 
ATOM   6334 C C   . LYS D 2 51  ? 64.898  -59.222  29.720  1.00 142.75 ? 51  LYS D C   1 
ATOM   6335 O O   . LYS D 2 51  ? 64.117  -58.380  29.273  1.00 142.41 ? 51  LYS D O   1 
ATOM   6336 C CB  . LYS D 2 51  ? 67.068  -60.085  28.779  1.00 140.37 ? 51  LYS D CB  1 
ATOM   6337 C CG  . LYS D 2 51  ? 68.339  -59.643  28.051  1.00 138.71 ? 51  LYS D CG  1 
ATOM   6338 C CD  . LYS D 2 51  ? 68.075  -59.408  26.565  1.00 134.31 ? 51  LYS D CD  1 
ATOM   6339 C CE  . LYS D 2 51  ? 69.367  -59.294  25.763  1.00 128.33 ? 51  LYS D CE  1 
ATOM   6340 N NZ  . LYS D 2 51  ? 69.976  -60.626  25.494  1.00 125.96 ? 51  LYS D NZ  1 
ATOM   6341 N N   . VAL D 2 52  ? 64.496  -60.357  30.285  1.00 141.90 ? 52  VAL D N   1 
ATOM   6342 C CA  . VAL D 2 52  ? 63.091  -60.754  30.320  1.00 141.44 ? 52  VAL D CA  1 
ATOM   6343 C C   . VAL D 2 52  ? 62.159  -59.602  30.695  1.00 143.61 ? 52  VAL D C   1 
ATOM   6344 O O   . VAL D 2 52  ? 61.325  -59.189  29.891  1.00 143.49 ? 52  VAL D O   1 
ATOM   6345 C CB  . VAL D 2 52  ? 62.866  -61.944  31.281  1.00 139.49 ? 52  VAL D CB  1 
ATOM   6346 C CG1 . VAL D 2 52  ? 63.598  -61.719  32.595  1.00 139.90 ? 52  VAL D CG1 1 
ATOM   6347 C CG2 . VAL D 2 52  ? 61.380  -62.167  31.515  1.00 136.40 ? 52  VAL D CG2 1 
ATOM   6348 N N   . ASN D 2 53  ? 62.295  -59.086  31.911  1.00 144.58 ? 53  ASN D N   1 
ATOM   6349 C CA  . ASN D 2 53  ? 61.426  -58.005  32.369  1.00 145.46 ? 53  ASN D CA  1 
ATOM   6350 C C   . ASN D 2 53  ? 61.552  -56.742  31.521  1.00 146.30 ? 53  ASN D C   1 
ATOM   6351 O O   . ASN D 2 53  ? 60.731  -55.830  31.633  1.00 147.40 ? 53  ASN D O   1 
ATOM   6352 C CB  . ASN D 2 53  ? 61.677  -57.691  33.845  1.00 148.39 ? 53  ASN D CB  1 
ATOM   6353 C CG  . ASN D 2 53  ? 61.270  -58.831  34.758  1.00 147.55 ? 53  ASN D CG  1 
ATOM   6354 O OD1 . ASN D 2 53  ? 62.066  -59.727  35.040  1.00 145.95 ? 53  ASN D OD1 1 
ATOM   6355 N ND2 . ASN D 2 53  ? 60.025  -58.803  35.225  1.00 144.57 ? 53  ASN D ND2 1 
ATOM   6356 N N   . SER D 2 54  ? 62.578  -56.689  30.676  1.00 145.08 ? 54  SER D N   1 
ATOM   6357 C CA  . SER D 2 54  ? 62.758  -55.553  29.779  1.00 146.21 ? 54  SER D CA  1 
ATOM   6358 C C   . SER D 2 54  ? 62.049  -55.774  28.443  1.00 146.64 ? 54  SER D C   1 
ATOM   6359 O O   . SER D 2 54  ? 62.006  -54.877  27.602  1.00 147.63 ? 54  SER D O   1 
ATOM   6360 C CB  . SER D 2 54  ? 64.245  -55.254  29.559  1.00 145.97 ? 54  SER D CB  1 
ATOM   6361 O OG  . SER D 2 54  ? 64.425  -53.965  28.994  1.00 147.40 ? 54  SER D OG  1 
ATOM   6362 N N   . VAL D 2 55  ? 61.495  -56.969  28.258  1.00 145.91 ? 55  VAL D N   1 
ATOM   6363 C CA  . VAL D 2 55  ? 60.647  -57.258  27.103  1.00 146.09 ? 55  VAL D CA  1 
ATOM   6364 C C   . VAL D 2 55  ? 59.284  -56.610  27.334  1.00 145.65 ? 55  VAL D C   1 
ATOM   6365 O O   . VAL D 2 55  ? 58.580  -56.220  26.398  1.00 142.54 ? 55  VAL D O   1 
ATOM   6366 C CB  . VAL D 2 55  ? 60.473  -58.774  26.901  1.00 143.08 ? 55  VAL D CB  1 
ATOM   6367 C CG1 . VAL D 2 55  ? 59.653  -59.054  25.654  1.00 139.22 ? 55  VAL D CG1 1 
ATOM   6368 C CG2 . VAL D 2 55  ? 61.834  -59.457  26.821  1.00 142.17 ? 55  VAL D CG2 1 
ATOM   6369 N N   . ILE D 2 56  ? 58.938  -56.495  28.609  1.00 145.72 ? 56  ILE D N   1 
ATOM   6370 C CA  . ILE D 2 56  ? 57.742  -55.803  29.051  1.00 144.80 ? 56  ILE D CA  1 
ATOM   6371 C C   . ILE D 2 56  ? 58.002  -54.307  29.110  1.00 146.86 ? 56  ILE D C   1 
ATOM   6372 O O   . ILE D 2 56  ? 57.326  -53.520  28.449  1.00 147.58 ? 56  ILE D O   1 
ATOM   6373 C CB  . ILE D 2 56  ? 57.311  -56.267  30.448  1.00 143.53 ? 56  ILE D CB  1 
ATOM   6374 C CG1 . ILE D 2 56  ? 57.017  -57.770  30.452  1.00 139.22 ? 56  ILE D CG1 1 
ATOM   6375 C CG2 . ILE D 2 56  ? 56.110  -55.465  30.919  1.00 144.00 ? 56  ILE D CG2 1 
ATOM   6376 C CD1 . ILE D 2 56  ? 58.250  -58.639  30.571  1.00 138.26 ? 56  ILE D CD1 1 
ATOM   6377 N N   . GLU D 2 57  ? 58.986  -53.932  29.921  1.00 147.61 ? 57  GLU D N   1 
ATOM   6378 C CA  . GLU D 2 57  ? 59.206  -52.546  30.329  1.00 150.89 ? 57  GLU D CA  1 
ATOM   6379 C C   . GLU D 2 57  ? 59.274  -51.507  29.209  1.00 154.93 ? 57  GLU D C   1 
ATOM   6380 O O   . GLU D 2 57  ? 59.021  -50.325  29.455  1.00 157.14 ? 57  GLU D O   1 
ATOM   6381 C CB  . GLU D 2 57  ? 60.464  -52.443  31.198  1.00 150.65 ? 57  GLU D CB  1 
ATOM   6382 C CG  . GLU D 2 57  ? 60.173  -52.235  32.678  1.00 151.60 ? 57  GLU D CG  1 
ATOM   6383 C CD  . GLU D 2 57  ? 61.437  -52.061  33.504  1.00 149.57 ? 57  GLU D CD  1 
ATOM   6384 O OE1 . GLU D 2 57  ? 62.538  -52.008  32.909  1.00 147.82 ? 57  GLU D OE1 1 
ATOM   6385 O OE2 . GLU D 2 57  ? 61.328  -51.978  34.747  1.00 148.84 ? 57  GLU D OE2 1 
ATOM   6386 N N   . LYS D 2 58  ? 59.626  -51.920  27.995  1.00 153.50 ? 58  LYS D N   1 
ATOM   6387 C CA  . LYS D 2 58  ? 59.610  -50.977  26.871  1.00 154.19 ? 58  LYS D CA  1 
ATOM   6388 C C   . LYS D 2 58  ? 58.329  -51.034  26.018  1.00 154.69 ? 58  LYS D C   1 
ATOM   6389 O O   . LYS D 2 58  ? 58.172  -50.269  25.061  1.00 155.39 ? 58  LYS D O   1 
ATOM   6390 C CB  . LYS D 2 58  ? 60.884  -51.080  26.020  1.00 152.45 ? 58  LYS D CB  1 
ATOM   6391 C CG  . LYS D 2 58  ? 61.391  -52.482  25.808  1.00 149.92 ? 58  LYS D CG  1 
ATOM   6392 C CD  . LYS D 2 58  ? 62.804  -52.469  25.252  1.00 148.26 ? 58  LYS D CD  1 
ATOM   6393 C CE  . LYS D 2 58  ? 63.803  -51.850  26.228  1.00 146.82 ? 58  LYS D CE  1 
ATOM   6394 N NZ  . LYS D 2 58  ? 63.839  -50.357  26.185  1.00 145.80 ? 58  LYS D NZ  1 
ATOM   6395 N N   . MET D 2 59  ? 57.406  -51.912  26.396  1.00 151.76 ? 59  MET D N   1 
ATOM   6396 C CA  . MET D 2 59  ? 56.076  -51.944  25.798  1.00 148.07 ? 59  MET D CA  1 
ATOM   6397 C C   . MET D 2 59  ? 55.221  -50.858  26.411  1.00 148.07 ? 59  MET D C   1 
ATOM   6398 O O   . MET D 2 59  ? 55.733  -49.934  27.042  1.00 149.33 ? 59  MET D O   1 
ATOM   6399 C CB  . MET D 2 59  ? 55.409  -53.293  26.027  1.00 143.60 ? 59  MET D CB  1 
ATOM   6400 C CG  . MET D 2 59  ? 55.976  -54.399  25.176  1.00 142.88 ? 59  MET D CG  1 
ATOM   6401 S SD  . MET D 2 59  ? 55.666  -56.000  25.926  1.00 136.80 ? 59  MET D SD  1 
ATOM   6402 C CE  . MET D 2 59  ? 56.261  -57.082  24.632  1.00 129.05 ? 59  MET D CE  1 
ATOM   6403 N N   . ASN D 2 60  ? 53.915  -50.960  26.207  1.00 145.77 ? 60  ASN D N   1 
ATOM   6404 C CA  . ASN D 2 60  ? 53.006  -49.973  26.752  1.00 148.26 ? 60  ASN D CA  1 
ATOM   6405 C C   . ASN D 2 60  ? 53.280  -48.610  26.132  1.00 148.78 ? 60  ASN D C   1 
ATOM   6406 O O   . ASN D 2 60  ? 53.772  -47.694  26.793  1.00 149.39 ? 60  ASN D O   1 
ATOM   6407 C CB  . ASN D 2 60  ? 53.160  -49.897  28.278  1.00 150.36 ? 60  ASN D CB  1 
ATOM   6408 C CG  . ASN D 2 60  ? 53.716  -51.185  28.883  1.00 147.73 ? 60  ASN D CG  1 
ATOM   6409 O OD1 . ASN D 2 60  ? 53.727  -52.237  28.243  1.00 143.73 ? 60  ASN D OD1 1 
ATOM   6410 N ND2 . ASN D 2 60  ? 54.177  -51.101  30.126  1.00 143.15 ? 60  ASN D ND2 1 
ATOM   6411 N N   . THR D 2 61  ? 52.974  -48.498  24.844  1.00 147.22 ? 61  THR D N   1 
ATOM   6412 C CA  . THR D 2 61  ? 53.137  -47.246  24.118  1.00 147.83 ? 61  THR D CA  1 
ATOM   6413 C C   . THR D 2 61  ? 52.402  -46.103  24.811  1.00 147.14 ? 61  THR D C   1 
ATOM   6414 O O   . THR D 2 61  ? 51.352  -46.307  25.421  1.00 145.14 ? 61  THR D O   1 
ATOM   6415 C CB  . THR D 2 61  ? 52.625  -47.371  22.675  1.00 141.63 ? 61  THR D CB  1 
ATOM   6416 O OG1 . THR D 2 61  ? 52.166  -46.092  22.224  1.00 137.50 ? 61  THR D OG1 1 
ATOM   6417 C CG2 . THR D 2 61  ? 51.472  -48.363  22.602  1.00 136.77 ? 61  THR D CG2 1 
ATOM   6418 N N   . LYS D 2 83  ? 37.627  -51.576  11.353  1.00 140.09 ? 83  LYS D N   1 
ATOM   6419 C CA  . LYS D 2 83  ? 39.006  -51.945  11.662  1.00 143.06 ? 83  LYS D CA  1 
ATOM   6420 C C   . LYS D 2 83  ? 39.499  -51.256  12.935  1.00 140.47 ? 83  LYS D C   1 
ATOM   6421 O O   . LYS D 2 83  ? 40.624  -51.488  13.384  1.00 139.15 ? 83  LYS D O   1 
ATOM   6422 C CB  . LYS D 2 83  ? 39.929  -51.587  10.490  1.00 143.65 ? 83  LYS D CB  1 
ATOM   6423 C CG  . LYS D 2 83  ? 41.384  -52.001  10.685  1.00 143.24 ? 83  LYS D CG  1 
ATOM   6424 C CD  . LYS D 2 83  ? 42.352  -50.863  10.375  1.00 140.67 ? 83  LYS D CD  1 
ATOM   6425 C CE  . LYS D 2 83  ? 43.779  -51.247  10.744  1.00 137.91 ? 83  LYS D CE  1 
ATOM   6426 N NZ  . LYS D 2 83  ? 44.760  -50.171  10.440  1.00 133.53 ? 83  LYS D NZ  1 
ATOM   6427 N N   . VAL D 2 84  ? 38.633  -50.444  13.533  1.00 138.57 ? 84  VAL D N   1 
ATOM   6428 C CA  . VAL D 2 84  ? 39.052  -49.475  14.540  1.00 136.81 ? 84  VAL D CA  1 
ATOM   6429 C C   . VAL D 2 84  ? 40.007  -50.035  15.600  1.00 136.75 ? 84  VAL D C   1 
ATOM   6430 O O   . VAL D 2 84  ? 41.024  -49.410  15.903  1.00 135.67 ? 84  VAL D O   1 
ATOM   6431 C CB  . VAL D 2 84  ? 37.838  -48.809  15.228  1.00 136.15 ? 84  VAL D CB  1 
ATOM   6432 C CG1 . VAL D 2 84  ? 37.066  -47.953  14.231  1.00 132.75 ? 84  VAL D CG1 1 
ATOM   6433 C CG2 . VAL D 2 84  ? 36.932  -49.860  15.857  1.00 131.07 ? 84  VAL D CG2 1 
ATOM   6434 N N   . ASP D 2 85  ? 39.694  -51.209  16.147  1.00 137.04 ? 85  ASP D N   1 
ATOM   6435 C CA  . ASP D 2 85  ? 40.490  -51.779  17.242  1.00 136.23 ? 85  ASP D CA  1 
ATOM   6436 C C   . ASP D 2 85  ? 41.288  -53.023  16.844  1.00 134.16 ? 85  ASP D C   1 
ATOM   6437 O O   . ASP D 2 85  ? 42.516  -53.037  16.936  1.00 132.87 ? 85  ASP D O   1 
ATOM   6438 C CB  . ASP D 2 85  ? 39.627  -52.067  18.480  1.00 135.87 ? 85  ASP D CB  1 
ATOM   6439 C CG  . ASP D 2 85  ? 40.455  -52.166  19.759  1.00 136.46 ? 85  ASP D CG  1 
ATOM   6440 O OD1 . ASP D 2 85  ? 41.656  -51.825  19.712  1.00 137.47 ? 85  ASP D OD1 1 
ATOM   6441 O OD2 . ASP D 2 85  ? 39.908  -52.562  20.813  1.00 135.11 ? 85  ASP D OD2 1 
ATOM   6442 N N   . ASP D 2 86  ? 40.583  -54.069  16.423  1.00 133.54 ? 86  ASP D N   1 
ATOM   6443 C CA  . ASP D 2 86  ? 41.200  -55.355  16.104  1.00 131.75 ? 86  ASP D CA  1 
ATOM   6444 C C   . ASP D 2 86  ? 42.252  -55.261  14.990  1.00 131.89 ? 86  ASP D C   1 
ATOM   6445 O O   . ASP D 2 86  ? 42.978  -56.220  14.729  1.00 130.79 ? 86  ASP D O   1 
ATOM   6446 C CB  . ASP D 2 86  ? 40.121  -56.380  15.754  1.00 132.94 ? 86  ASP D CB  1 
ATOM   6447 C CG  . ASP D 2 86  ? 39.028  -56.451  16.805  1.00 132.73 ? 86  ASP D CG  1 
ATOM   6448 O OD1 . ASP D 2 86  ? 38.882  -55.483  17.582  1.00 131.75 ? 86  ASP D OD1 1 
ATOM   6449 O OD2 . ASP D 2 86  ? 38.313  -57.473  16.853  1.00 131.47 ? 86  ASP D OD2 1 
ATOM   6450 N N   . GLY D 2 87  ? 42.316  -54.111  14.324  1.00 133.48 ? 87  GLY D N   1 
ATOM   6451 C CA  . GLY D 2 87  ? 43.393  -53.826  13.391  1.00 133.04 ? 87  GLY D CA  1 
ATOM   6452 C C   . GLY D 2 87  ? 44.708  -53.541  14.103  1.00 130.93 ? 87  GLY D C   1 
ATOM   6453 O O   . GLY D 2 87  ? 45.788  -53.705  13.533  1.00 129.36 ? 87  GLY D O   1 
ATOM   6454 N N   . PHE D 2 88  ? 44.602  -53.102  15.356  1.00 129.91 ? 88  PHE D N   1 
ATOM   6455 C CA  . PHE D 2 88  ? 45.753  -52.848  16.227  1.00 127.99 ? 88  PHE D CA  1 
ATOM   6456 C C   . PHE D 2 88  ? 46.022  -54.046  17.132  1.00 126.25 ? 88  PHE D C   1 
ATOM   6457 O O   . PHE D 2 88  ? 47.098  -54.642  17.088  1.00 125.30 ? 88  PHE D O   1 
ATOM   6458 C CB  . PHE D 2 88  ? 45.521  -51.600  17.088  1.00 128.64 ? 88  PHE D CB  1 
ATOM   6459 C CG  . PHE D 2 88  ? 46.699  -51.223  17.961  1.00 124.49 ? 88  PHE D CG  1 
ATOM   6460 C CD1 . PHE D 2 88  ? 46.931  -51.870  19.165  1.00 124.98 ? 88  PHE D CD1 1 
ATOM   6461 C CD2 . PHE D 2 88  ? 47.561  -50.206  17.582  1.00 122.73 ? 88  PHE D CD2 1 
ATOM   6462 C CE1 . PHE D 2 88  ? 48.009  -51.515  19.967  1.00 125.11 ? 88  PHE D CE1 1 
ATOM   6463 C CE2 . PHE D 2 88  ? 48.639  -49.847  18.381  1.00 124.95 ? 88  PHE D CE2 1 
ATOM   6464 C CZ  . PHE D 2 88  ? 48.862  -50.503  19.573  1.00 125.73 ? 88  PHE D CZ  1 
ATOM   6465 N N   . LEU D 2 89  ? 45.041  -54.378  17.967  1.00 125.05 ? 89  LEU D N   1 
ATOM   6466 C CA  . LEU D 2 89  ? 45.177  -55.465  18.927  1.00 123.94 ? 89  LEU D CA  1 
ATOM   6467 C C   . LEU D 2 89  ? 45.737  -56.705  18.241  1.00 123.45 ? 89  LEU D C   1 
ATOM   6468 O O   . LEU D 2 89  ? 46.493  -57.469  18.844  1.00 122.22 ? 89  LEU D O   1 
ATOM   6469 C CB  . LEU D 2 89  ? 43.822  -55.779  19.565  1.00 123.58 ? 89  LEU D CB  1 
ATOM   6470 C CG  . LEU D 2 89  ? 43.796  -56.620  20.846  1.00 118.00 ? 89  LEU D CG  1 
ATOM   6471 C CD1 . LEU D 2 89  ? 42.462  -56.441  21.555  1.00 116.67 ? 89  LEU D CD1 1 
ATOM   6472 C CD2 . LEU D 2 89  ? 44.075  -58.098  20.587  1.00 112.27 ? 89  LEU D CD2 1 
ATOM   6473 N N   . ASP D 2 90  ? 45.368  -56.900  16.978  1.00 123.90 ? 90  ASP D N   1 
ATOM   6474 C CA  . ASP D 2 90  ? 45.973  -57.955  16.177  1.00 124.01 ? 90  ASP D CA  1 
ATOM   6475 C C   . ASP D 2 90  ? 47.465  -57.693  16.010  1.00 122.42 ? 90  ASP D C   1 
ATOM   6476 O O   . ASP D 2 90  ? 48.282  -58.584  16.229  1.00 121.44 ? 90  ASP D O   1 
ATOM   6477 C CB  . ASP D 2 90  ? 45.302  -58.074  14.806  1.00 127.23 ? 90  ASP D CB  1 
ATOM   6478 C CG  . ASP D 2 90  ? 44.041  -58.916  14.844  1.00 126.59 ? 90  ASP D CG  1 
ATOM   6479 O OD1 . ASP D 2 90  ? 43.355  -58.906  15.887  1.00 121.64 ? 90  ASP D OD1 1 
ATOM   6480 O OD2 . ASP D 2 90  ? 43.737  -59.586  13.833  1.00 132.44 ? 90  ASP D OD2 1 
ATOM   6481 N N   . ILE D 2 91  ? 47.822  -56.469  15.632  1.00 121.47 ? 91  ILE D N   1 
ATOM   6482 C CA  . ILE D 2 91  ? 49.226  -56.154  15.396  1.00 120.89 ? 91  ILE D CA  1 
ATOM   6483 C C   . ILE D 2 91  ? 50.044  -56.153  16.682  1.00 120.53 ? 91  ILE D C   1 
ATOM   6484 O O   . ILE D 2 91  ? 51.176  -56.625  16.687  1.00 121.23 ? 91  ILE D O   1 
ATOM   6485 C CB  . ILE D 2 91  ? 49.437  -54.804  14.670  1.00 123.52 ? 91  ILE D CB  1 
ATOM   6486 C CG1 . ILE D 2 91  ? 50.665  -54.887  13.756  1.00 122.89 ? 91  ILE D CG1 1 
ATOM   6487 C CG2 . ILE D 2 91  ? 49.616  -53.677  15.673  1.00 124.39 ? 91  ILE D CG2 1 
ATOM   6488 C CD1 . ILE D 2 91  ? 51.287  -53.543  13.399  1.00 121.31 ? 91  ILE D CD1 1 
ATOM   6489 N N   . TRP D 2 92  ? 49.489  -55.622  17.768  1.00 120.08 ? 92  TRP D N   1 
ATOM   6490 C CA  . TRP D 2 92  ? 50.241  -55.590  19.015  1.00 120.24 ? 92  TRP D CA  1 
ATOM   6491 C C   . TRP D 2 92  ? 50.474  -57.009  19.494  1.00 120.09 ? 92  TRP D C   1 
ATOM   6492 O O   . TRP D 2 92  ? 51.575  -57.362  19.915  1.00 119.89 ? 92  TRP D O   1 
ATOM   6493 C CB  . TRP D 2 92  ? 49.530  -54.793  20.106  1.00 121.75 ? 92  TRP D CB  1 
ATOM   6494 C CG  . TRP D 2 92  ? 50.254  -54.890  21.429  1.00 124.31 ? 92  TRP D CG  1 
ATOM   6495 C CD1 . TRP D 2 92  ? 50.260  -55.961  22.278  1.00 122.51 ? 92  TRP D CD1 1 
ATOM   6496 C CD2 . TRP D 2 92  ? 51.088  -53.889  22.041  1.00 127.72 ? 92  TRP D CD2 1 
ATOM   6497 N NE1 . TRP D 2 92  ? 51.039  -55.690  23.378  1.00 123.41 ? 92  TRP D NE1 1 
ATOM   6498 C CE2 . TRP D 2 92  ? 51.557  -54.427  23.260  1.00 128.18 ? 92  TRP D CE2 1 
ATOM   6499 C CE3 . TRP D 2 92  ? 51.478  -52.593  21.682  1.00 129.96 ? 92  TRP D CE3 1 
ATOM   6500 C CZ2 . TRP D 2 92  ? 52.398  -53.713  24.121  1.00 131.70 ? 92  TRP D CZ2 1 
ATOM   6501 C CZ3 . TRP D 2 92  ? 52.313  -51.885  22.541  1.00 132.77 ? 92  TRP D CZ3 1 
ATOM   6502 C CH2 . TRP D 2 92  ? 52.763  -52.449  23.744  1.00 133.64 ? 92  TRP D CH2 1 
ATOM   6503 N N   . THR D 2 93  ? 49.424  -57.819  19.430  1.00 120.66 ? 93  THR D N   1 
ATOM   6504 C CA  . THR D 2 93  ? 49.518  -59.221  19.804  1.00 119.28 ? 93  THR D CA  1 
ATOM   6505 C C   . THR D 2 93  ? 50.585  -59.939  18.972  1.00 120.26 ? 93  THR D C   1 
ATOM   6506 O O   . THR D 2 93  ? 51.506  -60.548  19.522  1.00 118.21 ? 93  THR D O   1 
ATOM   6507 C CB  . THR D 2 93  ? 48.167  -59.938  19.631  1.00 116.83 ? 93  THR D CB  1 
ATOM   6508 O OG1 . THR D 2 93  ? 47.130  -59.167  20.251  1.00 114.60 ? 93  THR D OG1 1 
ATOM   6509 C CG2 . THR D 2 93  ? 48.216  -61.317  20.264  1.00 113.09 ? 93  THR D CG2 1 
ATOM   6510 N N   . TYR D 2 94  ? 50.455  -59.858  17.647  1.00 121.87 ? 94  TYR D N   1 
ATOM   6511 C CA  . TYR D 2 94  ? 51.404  -60.486  16.725  1.00 121.59 ? 94  TYR D CA  1 
ATOM   6512 C C   . TYR D 2 94  ? 52.809  -59.970  17.003  1.00 120.29 ? 94  TYR D C   1 
ATOM   6513 O O   . TYR D 2 94  ? 53.763  -60.742  17.072  1.00 119.62 ? 94  TYR D O   1 
ATOM   6514 C CB  . TYR D 2 94  ? 51.017  -60.189  15.270  1.00 123.73 ? 94  TYR D CB  1 
ATOM   6515 C CG  . TYR D 2 94  ? 51.573  -61.158  14.232  1.00 124.76 ? 94  TYR D CG  1 
ATOM   6516 C CD1 . TYR D 2 94  ? 52.933  -61.206  13.942  1.00 123.61 ? 94  TYR D CD1 1 
ATOM   6517 C CD2 . TYR D 2 94  ? 50.730  -62.016  13.531  1.00 126.20 ? 94  TYR D CD2 1 
ATOM   6518 C CE1 . TYR D 2 94  ? 53.437  -62.090  12.988  1.00 125.30 ? 94  TYR D CE1 1 
ATOM   6519 C CE2 . TYR D 2 94  ? 51.226  -62.898  12.578  1.00 125.99 ? 94  TYR D CE2 1 
ATOM   6520 C CZ  . TYR D 2 94  ? 52.578  -62.932  12.312  1.00 126.03 ? 94  TYR D CZ  1 
ATOM   6521 O OH  . TYR D 2 94  ? 53.071  -63.807  11.367  1.00 128.19 ? 94  TYR D OH  1 
ATOM   6522 N N   . ASN D 2 95  ? 52.925  -58.656  17.163  1.00 119.21 ? 95  ASN D N   1 
ATOM   6523 C CA  . ASN D 2 95  ? 54.199  -58.028  17.474  1.00 117.99 ? 95  ASN D CA  1 
ATOM   6524 C C   . ASN D 2 95  ? 54.861  -58.672  18.687  1.00 119.76 ? 95  ASN D C   1 
ATOM   6525 O O   . ASN D 2 95  ? 56.079  -58.810  18.735  1.00 119.99 ? 95  ASN D O   1 
ATOM   6526 C CB  . ASN D 2 95  ? 53.997  -56.537  17.736  1.00 119.70 ? 95  ASN D CB  1 
ATOM   6527 C CG  . ASN D 2 95  ? 55.244  -55.725  17.468  1.00 120.13 ? 95  ASN D CG  1 
ATOM   6528 O OD1 . ASN D 2 95  ? 55.904  -55.901  16.441  1.00 121.19 ? 95  ASN D OD1 1 
ATOM   6529 N ND2 . ASN D 2 95  ? 55.579  -54.828  18.394  1.00 120.38 ? 95  ASN D ND2 1 
ATOM   6530 N N   . ALA D 2 96  ? 54.049  -59.054  19.670  1.00 119.63 ? 96  ALA D N   1 
ATOM   6531 C CA  . ALA D 2 96  ? 54.559  -59.602  20.924  1.00 116.45 ? 96  ALA D CA  1 
ATOM   6532 C C   . ALA D 2 96  ? 54.984  -61.071  20.867  1.00 116.39 ? 96  ALA D C   1 
ATOM   6533 O O   . ALA D 2 96  ? 56.078  -61.411  21.315  1.00 117.51 ? 96  ALA D O   1 
ATOM   6534 C CB  . ALA D 2 96  ? 53.555  -59.385  22.041  1.00 117.53 ? 96  ALA D CB  1 
ATOM   6535 N N   . GLU D 2 97  ? 54.136  -61.945  20.326  1.00 115.97 ? 97  GLU D N   1 
ATOM   6536 C CA  . GLU D 2 97  ? 54.491  -63.365  20.267  1.00 115.86 ? 97  GLU D CA  1 
ATOM   6537 C C   . GLU D 2 97  ? 55.753  -63.571  19.442  1.00 117.53 ? 97  GLU D C   1 
ATOM   6538 O O   . GLU D 2 97  ? 56.407  -64.609  19.535  1.00 118.94 ? 97  GLU D O   1 
ATOM   6539 C CB  . GLU D 2 97  ? 53.351  -64.227  19.723  1.00 114.54 ? 97  GLU D CB  1 
ATOM   6540 C CG  . GLU D 2 97  ? 52.249  -63.477  19.017  1.00 115.93 ? 97  GLU D CG  1 
ATOM   6541 C CD  . GLU D 2 97  ? 50.957  -64.272  19.002  1.00 117.69 ? 97  GLU D CD  1 
ATOM   6542 O OE1 . GLU D 2 97  ? 51.015  -65.503  19.222  1.00 117.81 ? 97  GLU D OE1 1 
ATOM   6543 O OE2 . GLU D 2 97  ? 49.883  -63.669  18.788  1.00 116.80 ? 97  GLU D OE2 1 
ATOM   6544 N N   . LEU D 2 98  ? 56.074  -62.576  18.621  1.00 117.64 ? 98  LEU D N   1 
ATOM   6545 C CA  . LEU D 2 98  ? 57.347  -62.531  17.913  1.00 116.51 ? 98  LEU D CA  1 
ATOM   6546 C C   . LEU D 2 98  ? 58.490  -62.308  18.896  1.00 117.63 ? 98  LEU D C   1 
ATOM   6547 O O   . LEU D 2 98  ? 59.411  -63.119  18.978  1.00 118.02 ? 98  LEU D O   1 
ATOM   6548 C CB  . LEU D 2 98  ? 57.334  -61.422  16.860  1.00 118.32 ? 98  LEU D CB  1 
ATOM   6549 C CG  . LEU D 2 98  ? 56.967  -61.795  15.420  1.00 119.87 ? 98  LEU D CG  1 
ATOM   6550 C CD1 . LEU D 2 98  ? 55.775  -62.746  15.369  1.00 120.67 ? 98  LEU D CD1 1 
ATOM   6551 C CD2 . LEU D 2 98  ? 56.718  -60.545  14.572  1.00 120.56 ? 98  LEU D CD2 1 
ATOM   6552 N N   . LEU D 2 99  ? 58.400  -61.230  19.673  1.00 117.56 ? 99  LEU D N   1 
ATOM   6553 C CA  . LEU D 2 99  ? 59.423  -60.910  20.663  1.00 116.91 ? 99  LEU D CA  1 
ATOM   6554 C C   . LEU D 2 99  ? 59.777  -62.152  21.470  1.00 117.19 ? 99  LEU D C   1 
ATOM   6555 O O   . LEU D 2 99  ? 60.941  -62.382  21.796  1.00 117.12 ? 99  LEU D O   1 
ATOM   6556 C CB  . LEU D 2 99  ? 58.947  -59.797  21.601  1.00 116.11 ? 99  LEU D CB  1 
ATOM   6557 C CG  . LEU D 2 99  ? 59.127  -58.353  21.130  1.00 116.44 ? 99  LEU D CG  1 
ATOM   6558 C CD1 . LEU D 2 99  ? 60.135  -58.281  19.994  1.00 115.71 ? 99  LEU D CD1 1 
ATOM   6559 C CD2 . LEU D 2 99  ? 57.799  -57.736  20.722  1.00 117.16 ? 99  LEU D CD2 1 
ATOM   6560 N N   . VAL D 2 100 ? 58.760  -62.951  21.779  1.00 116.77 ? 100 VAL D N   1 
ATOM   6561 C CA  . VAL D 2 100 ? 58.935  -64.185  22.536  1.00 117.95 ? 100 VAL D CA  1 
ATOM   6562 C C   . VAL D 2 100 ? 59.937  -65.125  21.882  1.00 118.12 ? 100 VAL D C   1 
ATOM   6563 O O   . VAL D 2 100 ? 60.936  -65.510  22.491  1.00 120.28 ? 100 VAL D O   1 
ATOM   6564 C CB  . VAL D 2 100 ? 57.602  -64.938  22.676  1.00 117.85 ? 100 VAL D CB  1 
ATOM   6565 C CG1 . VAL D 2 100 ? 57.818  -66.262  23.379  1.00 119.68 ? 100 VAL D CG1 1 
ATOM   6566 C CG2 . VAL D 2 100 ? 56.592  -64.089  23.425  1.00 117.54 ? 100 VAL D CG2 1 
ATOM   6567 N N   . LEU D 2 101 ? 59.658  -65.494  20.638  1.00 116.87 ? 101 LEU D N   1 
ATOM   6568 C CA  . LEU D 2 101 ? 60.518  -66.397  19.887  1.00 117.89 ? 101 LEU D CA  1 
ATOM   6569 C C   . LEU D 2 101 ? 61.959  -65.925  19.916  1.00 118.70 ? 101 LEU D C   1 
ATOM   6570 O O   . LEU D 2 101 ? 62.880  -66.709  20.144  1.00 119.81 ? 101 LEU D O   1 
ATOM   6571 C CB  . LEU D 2 101 ? 60.028  -66.487  18.448  1.00 116.75 ? 101 LEU D CB  1 
ATOM   6572 C CG  . LEU D 2 101 ? 58.619  -67.069  18.368  1.00 116.45 ? 101 LEU D CG  1 
ATOM   6573 C CD1 . LEU D 2 101 ? 57.747  -66.291  17.397  1.00 117.72 ? 101 LEU D CD1 1 
ATOM   6574 C CD2 . LEU D 2 101 ? 58.679  -68.544  18.003  1.00 119.12 ? 101 LEU D CD2 1 
ATOM   6575 N N   . LEU D 2 102 ? 62.141  -64.631  19.691  1.00 118.04 ? 102 LEU D N   1 
ATOM   6576 C CA  . LEU D 2 102 ? 63.463  -64.025  19.672  1.00 118.47 ? 102 LEU D CA  1 
ATOM   6577 C C   . LEU D 2 102 ? 64.306  -64.455  20.855  1.00 118.98 ? 102 LEU D C   1 
ATOM   6578 O O   . LEU D 2 102 ? 65.315  -65.143  20.696  1.00 119.61 ? 102 LEU D O   1 
ATOM   6579 C CB  . LEU D 2 102 ? 63.340  -62.504  19.664  1.00 119.00 ? 102 LEU D CB  1 
ATOM   6580 C CG  . LEU D 2 102 ? 63.305  -61.894  18.264  1.00 119.85 ? 102 LEU D CG  1 
ATOM   6581 C CD1 . LEU D 2 102 ? 64.712  -61.543  17.797  1.00 121.12 ? 102 LEU D CD1 1 
ATOM   6582 C CD2 . LEU D 2 102 ? 62.623  -62.847  17.289  1.00 117.93 ? 102 LEU D CD2 1 
ATOM   6583 N N   . GLU D 2 103 ? 63.883  -64.041  22.042  1.00 119.19 ? 103 GLU D N   1 
ATOM   6584 C CA  . GLU D 2 103 ? 64.657  -64.276  23.249  1.00 120.65 ? 103 GLU D CA  1 
ATOM   6585 C C   . GLU D 2 103 ? 64.812  -65.761  23.552  1.00 121.70 ? 103 GLU D C   1 
ATOM   6586 O O   . GLU D 2 103 ? 65.891  -66.208  23.940  1.00 122.50 ? 103 GLU D O   1 
ATOM   6587 C CB  . GLU D 2 103 ? 64.048  -63.528  24.434  1.00 119.95 ? 103 GLU D CB  1 
ATOM   6588 C CG  . GLU D 2 103 ? 64.978  -62.475  25.006  1.00 121.16 ? 103 GLU D CG  1 
ATOM   6589 C CD  . GLU D 2 103 ? 65.904  -61.894  23.953  1.00 122.45 ? 103 GLU D CD  1 
ATOM   6590 O OE1 . GLU D 2 103 ? 67.131  -62.108  24.057  1.00 123.46 ? 103 GLU D OE1 1 
ATOM   6591 O OE2 . GLU D 2 103 ? 65.406  -61.225  23.021  1.00 121.81 ? 103 GLU D OE2 1 
ATOM   6592 N N   . ASN D 2 104 ? 63.740  -66.524  23.369  1.00 120.27 ? 104 ASN D N   1 
ATOM   6593 C CA  . ASN D 2 104 ? 63.830  -67.972  23.484  1.00 120.13 ? 104 ASN D CA  1 
ATOM   6594 C C   . ASN D 2 104 ? 64.993  -68.495  22.658  1.00 120.84 ? 104 ASN D C   1 
ATOM   6595 O O   . ASN D 2 104 ? 65.818  -69.275  23.143  1.00 119.94 ? 104 ASN D O   1 
ATOM   6596 C CB  . ASN D 2 104 ? 62.528  -68.632  23.034  1.00 120.55 ? 104 ASN D CB  1 
ATOM   6597 C CG  . ASN D 2 104 ? 61.448  -68.553  24.087  1.00 122.72 ? 104 ASN D CG  1 
ATOM   6598 O OD1 . ASN D 2 104 ? 61.516  -67.723  24.993  1.00 123.85 ? 104 ASN D OD1 1 
ATOM   6599 N ND2 . ASN D 2 104 ? 60.450  -69.424  23.984  1.00 122.71 ? 104 ASN D ND2 1 
ATOM   6600 N N   . GLU D 2 105 ? 65.054  -68.048  21.406  1.00 121.46 ? 105 GLU D N   1 
ATOM   6601 C CA  . GLU D 2 105 ? 66.148  -68.405  20.514  1.00 120.25 ? 105 GLU D CA  1 
ATOM   6602 C C   . GLU D 2 105 ? 67.444  -67.813  21.050  1.00 120.95 ? 105 GLU D C   1 
ATOM   6603 O O   . GLU D 2 105 ? 68.426  -68.530  21.257  1.00 121.47 ? 105 GLU D O   1 
ATOM   6604 C CB  . GLU D 2 105 ? 65.882  -67.897  19.096  1.00 117.63 ? 105 GLU D CB  1 
ATOM   6605 C CG  . GLU D 2 105 ? 66.732  -68.565  18.035  1.00 117.26 ? 105 GLU D CG  1 
ATOM   6606 C CD  . GLU D 2 105 ? 66.582  -70.073  18.048  1.00 118.17 ? 105 GLU D CD  1 
ATOM   6607 O OE1 . GLU D 2 105 ? 65.755  -70.597  17.272  1.00 119.78 ? 105 GLU D OE1 1 
ATOM   6608 O OE2 . GLU D 2 105 ? 67.287  -70.733  18.840  1.00 117.89 ? 105 GLU D OE2 1 
ATOM   6609 N N   . ARG D 2 106 ? 67.436  -66.502  21.279  1.00 119.75 ? 106 ARG D N   1 
ATOM   6610 C CA  . ARG D 2 106 ? 68.596  -65.813  21.837  1.00 119.34 ? 106 ARG D CA  1 
ATOM   6611 C C   . ARG D 2 106 ? 69.077  -66.491  23.115  1.00 121.39 ? 106 ARG D C   1 
ATOM   6612 O O   . ARG D 2 106 ? 70.276  -66.595  23.366  1.00 123.35 ? 106 ARG D O   1 
ATOM   6613 C CB  . ARG D 2 106 ? 68.282  -64.336  22.103  1.00 117.79 ? 106 ARG D CB  1 
ATOM   6614 C CG  . ARG D 2 106 ? 68.180  -63.487  20.844  1.00 118.02 ? 106 ARG D CG  1 
ATOM   6615 C CD  . ARG D 2 106 ? 68.077  -61.997  21.153  1.00 118.94 ? 106 ARG D CD  1 
ATOM   6616 N NE  . ARG D 2 106 ? 68.135  -61.186  19.938  1.00 119.21 ? 106 ARG D NE  1 
ATOM   6617 C CZ  . ARG D 2 106 ? 69.229  -60.563  19.502  1.00 120.45 ? 106 ARG D CZ  1 
ATOM   6618 N NH1 . ARG D 2 106 ? 70.361  -60.648  20.188  1.00 121.30 ? 106 ARG D NH1 1 
ATOM   6619 N NH2 . ARG D 2 106 ? 69.194  -59.851  18.381  1.00 117.91 ? 106 ARG D NH2 1 
ATOM   6620 N N   . THR D 2 107 ? 68.136  -66.979  23.910  1.00 120.64 ? 107 THR D N   1 
ATOM   6621 C CA  . THR D 2 107 ? 68.480  -67.570  25.191  1.00 120.69 ? 107 THR D CA  1 
ATOM   6622 C C   . THR D 2 107 ? 69.135  -68.927  25.012  1.00 122.15 ? 107 THR D C   1 
ATOM   6623 O O   . THR D 2 107 ? 70.296  -69.110  25.368  1.00 123.74 ? 107 THR D O   1 
ATOM   6624 C CB  . THR D 2 107 ? 67.247  -67.733  26.080  1.00 123.43 ? 107 THR D CB  1 
ATOM   6625 O OG1 . THR D 2 107 ? 66.618  -66.458  26.255  1.00 123.28 ? 107 THR D OG1 1 
ATOM   6626 C CG2 . THR D 2 107 ? 67.645  -68.296  27.436  1.00 124.72 ? 107 THR D CG2 1 
ATOM   6627 N N   . LEU D 2 108 ? 68.391  -69.880  24.465  1.00 120.84 ? 108 LEU D N   1 
ATOM   6628 C CA  . LEU D 2 108 ? 68.905  -71.235  24.362  1.00 122.75 ? 108 LEU D CA  1 
ATOM   6629 C C   . LEU D 2 108 ? 70.272  -71.260  23.683  1.00 124.14 ? 108 LEU D C   1 
ATOM   6630 O O   . LEU D 2 108 ? 71.080  -72.146  23.955  1.00 125.12 ? 108 LEU D O   1 
ATOM   6631 C CB  . LEU D 2 108 ? 67.915  -72.155  23.647  1.00 123.65 ? 108 LEU D CB  1 
ATOM   6632 C CG  . LEU D 2 108 ? 68.018  -73.616  24.103  1.00 125.69 ? 108 LEU D CG  1 
ATOM   6633 C CD1 . LEU D 2 108 ? 66.722  -74.371  23.855  1.00 124.68 ? 108 LEU D CD1 1 
ATOM   6634 C CD2 . LEU D 2 108 ? 69.203  -74.330  23.459  1.00 124.86 ? 108 LEU D CD2 1 
ATOM   6635 N N   . ASP D 2 109 ? 70.534  -70.285  22.813  1.00 124.43 ? 109 ASP D N   1 
ATOM   6636 C CA  . ASP D 2 109 ? 71.851  -70.172  22.178  1.00 125.03 ? 109 ASP D CA  1 
ATOM   6637 C C   . ASP D 2 109 ? 72.793  -69.218  22.920  1.00 125.71 ? 109 ASP D C   1 
ATOM   6638 O O   . ASP D 2 109 ? 73.896  -68.931  22.460  1.00 127.06 ? 109 ASP D O   1 
ATOM   6639 C CB  . ASP D 2 109 ? 71.748  -69.800  20.700  1.00 123.73 ? 109 ASP D CB  1 
ATOM   6640 C CG  . ASP D 2 109 ? 72.982  -70.213  19.915  1.00 127.71 ? 109 ASP D CG  1 
ATOM   6641 O OD1 . ASP D 2 109 ? 73.080  -71.404  19.543  1.00 129.66 ? 109 ASP D OD1 1 
ATOM   6642 O OD2 . ASP D 2 109 ? 73.859  -69.354  19.682  1.00 127.55 ? 109 ASP D OD2 1 
ATOM   6643 N N   . TYR D 2 110 ? 72.328  -68.708  24.053  1.00 124.92 ? 110 TYR D N   1 
ATOM   6644 C CA  . TYR D 2 110 ? 73.196  -68.097  25.053  1.00 125.03 ? 110 TYR D CA  1 
ATOM   6645 C C   . TYR D 2 110 ? 73.746  -69.251  25.876  1.00 126.29 ? 110 TYR D C   1 
ATOM   6646 O O   . TYR D 2 110 ? 74.958  -69.432  25.999  1.00 127.12 ? 110 TYR D O   1 
ATOM   6647 C CB  . TYR D 2 110 ? 72.413  -67.121  25.927  1.00 126.44 ? 110 TYR D CB  1 
ATOM   6648 C CG  . TYR D 2 110 ? 73.228  -66.394  26.978  1.00 127.64 ? 110 TYR D CG  1 
ATOM   6649 C CD1 . TYR D 2 110 ? 74.166  -67.063  27.758  1.00 126.06 ? 110 TYR D CD1 1 
ATOM   6650 C CD2 . TYR D 2 110 ? 73.031  -65.038  27.210  1.00 126.49 ? 110 TYR D CD2 1 
ATOM   6651 C CE1 . TYR D 2 110 ? 74.894  -66.395  28.726  1.00 126.25 ? 110 TYR D CE1 1 
ATOM   6652 C CE2 . TYR D 2 110 ? 73.754  -64.364  28.171  1.00 125.15 ? 110 TYR D CE2 1 
ATOM   6653 C CZ  . TYR D 2 110 ? 74.681  -65.044  28.926  1.00 127.15 ? 110 TYR D CZ  1 
ATOM   6654 O OH  . TYR D 2 110 ? 75.394  -64.359  29.882  1.00 129.16 ? 110 TYR D OH  1 
ATOM   6655 N N   . HIS D 2 111 ? 72.832  -70.006  26.473  1.00 125.97 ? 111 HIS D N   1 
ATOM   6656 C CA  . HIS D 2 111 ? 73.193  -71.229  27.163  1.00 126.05 ? 111 HIS D CA  1 
ATOM   6657 C C   . HIS D 2 111 ? 74.066  -72.096  26.272  1.00 124.45 ? 111 HIS D C   1 
ATOM   6658 O O   . HIS D 2 111 ? 75.197  -72.397  26.623  1.00 124.35 ? 111 HIS D O   1 
ATOM   6659 C CB  . HIS D 2 111 ? 71.930  -72.005  27.525  1.00 128.37 ? 111 HIS D CB  1 
ATOM   6660 C CG  . HIS D 2 111 ? 71.156  -71.403  28.659  1.00 132.20 ? 111 HIS D CG  1 
ATOM   6661 N ND1 . HIS D 2 111 ? 71.632  -70.358  29.414  1.00 133.92 ? 111 HIS D ND1 1 
ATOM   6662 C CD2 . HIS D 2 111 ? 69.934  -71.711  29.160  1.00 131.07 ? 111 HIS D CD2 1 
ATOM   6663 C CE1 . HIS D 2 111 ? 70.737  -70.042  30.339  1.00 132.26 ? 111 HIS D CE1 1 
ATOM   6664 N NE2 . HIS D 2 111 ? 69.703  -70.848  30.206  1.00 131.77 ? 111 HIS D NE2 1 
ATOM   6665 N N   . ASP D 2 112 ? 73.557  -72.461  25.102  1.00 125.04 ? 112 ASP D N   1 
ATOM   6666 C CA  . ASP D 2 112 ? 74.307  -73.317  24.189  1.00 125.75 ? 112 ASP D CA  1 
ATOM   6667 C C   . ASP D 2 112 ? 75.612  -72.662  23.734  1.00 126.70 ? 112 ASP D C   1 
ATOM   6668 O O   . ASP D 2 112 ? 76.492  -73.331  23.198  1.00 128.00 ? 112 ASP D O   1 
ATOM   6669 C CB  . ASP D 2 112 ? 73.459  -73.693  22.969  1.00 126.09 ? 112 ASP D CB  1 
ATOM   6670 C CG  . ASP D 2 112 ? 74.164  -74.675  22.048  1.00 125.69 ? 112 ASP D CG  1 
ATOM   6671 O OD1 . ASP D 2 112 ? 74.604  -75.740  22.540  1.00 126.84 ? 112 ASP D OD1 1 
ATOM   6672 O OD2 . ASP D 2 112 ? 74.289  -74.378  20.839  1.00 124.49 ? 112 ASP D OD2 1 
ATOM   6673 N N   . SER D 2 113 ? 75.739  -71.355  23.945  1.00 126.99 ? 113 SER D N   1 
ATOM   6674 C CA  . SER D 2 113 ? 76.960  -70.649  23.564  1.00 126.47 ? 113 SER D CA  1 
ATOM   6675 C C   . SER D 2 113 ? 77.886  -70.521  24.748  1.00 125.10 ? 113 SER D C   1 
ATOM   6676 O O   . SER D 2 113 ? 78.911  -71.191  24.826  1.00 126.19 ? 113 SER D O   1 
ATOM   6677 C CB  . SER D 2 113 ? 76.653  -69.243  23.042  1.00 126.49 ? 113 SER D CB  1 
ATOM   6678 O OG  . SER D 2 113 ? 76.142  -69.281  21.724  1.00 128.37 ? 113 SER D OG  1 
ATOM   6679 N N   . ASN D 2 114 ? 77.507  -69.660  25.682  1.00 126.22 ? 114 ASN D N   1 
ATOM   6680 C CA  . ASN D 2 114 ? 78.364  -69.361  26.813  1.00 126.84 ? 114 ASN D CA  1 
ATOM   6681 C C   . ASN D 2 114 ? 78.584  -70.599  27.667  1.00 127.47 ? 114 ASN D C   1 
ATOM   6682 O O   . ASN D 2 114 ? 79.349  -70.569  28.626  1.00 129.42 ? 114 ASN D O   1 
ATOM   6683 C CB  . ASN D 2 114 ? 77.846  -68.162  27.608  1.00 125.63 ? 114 ASN D CB  1 
ATOM   6684 C CG  . ASN D 2 114 ? 78.163  -66.839  26.925  1.00 125.21 ? 114 ASN D CG  1 
ATOM   6685 O OD1 . ASN D 2 114 ? 79.087  -66.127  27.319  1.00 121.85 ? 114 ASN D OD1 1 
ATOM   6686 N ND2 . ASN D 2 114 ? 77.412  -66.520  25.878  1.00 125.72 ? 114 ASN D ND2 1 
ATOM   6687 N N   . VAL D 2 115 ? 77.897  -71.684  27.315  1.00 126.48 ? 115 VAL D N   1 
ATOM   6688 C CA  . VAL D 2 115 ? 78.282  -73.001  27.806  1.00 126.68 ? 115 VAL D CA  1 
ATOM   6689 C C   . VAL D 2 115 ? 79.603  -73.410  27.163  1.00 129.96 ? 115 VAL D C   1 
ATOM   6690 O O   . VAL D 2 115 ? 80.481  -73.958  27.825  1.00 132.25 ? 115 VAL D O   1 
ATOM   6691 C CB  . VAL D 2 115 ? 77.244  -74.087  27.475  1.00 125.91 ? 115 VAL D CB  1 
ATOM   6692 C CG1 . VAL D 2 115 ? 77.112  -74.256  25.973  1.00 126.64 ? 115 VAL D CG1 1 
ATOM   6693 C CG2 . VAL D 2 115 ? 77.647  -75.409  28.106  1.00 118.79 ? 115 VAL D CG2 1 
ATOM   6694 N N   . LYS D 2 116 ? 79.750  -73.119  25.872  1.00 129.39 ? 116 LYS D N   1 
ATOM   6695 C CA  . LYS D 2 116 ? 80.921  -73.561  25.119  1.00 128.14 ? 116 LYS D CA  1 
ATOM   6696 C C   . LYS D 2 116 ? 82.182  -72.921  25.688  1.00 129.26 ? 116 LYS D C   1 
ATOM   6697 O O   . LYS D 2 116 ? 83.300  -73.250  25.294  1.00 131.00 ? 116 LYS D O   1 
ATOM   6698 C CB  . LYS D 2 116 ? 80.761  -73.254  23.629  1.00 126.78 ? 116 LYS D CB  1 
ATOM   6699 C CG  . LYS D 2 116 ? 79.484  -73.834  23.005  1.00 129.08 ? 116 LYS D CG  1 
ATOM   6700 C CD  . LYS D 2 116 ? 79.356  -75.354  23.204  1.00 127.61 ? 116 LYS D CD  1 
ATOM   6701 C CE  . LYS D 2 116 ? 78.109  -75.913  22.510  1.00 123.36 ? 116 LYS D CE  1 
ATOM   6702 N NZ  . LYS D 2 116 ? 77.945  -77.389  22.677  1.00 120.22 ? 116 LYS D NZ  1 
ATOM   6703 N N   . ASN D 2 117 ? 81.979  -71.999  26.621  1.00 128.96 ? 117 ASN D N   1 
ATOM   6704 C CA  . ASN D 2 117 ? 83.057  -71.399  27.389  1.00 130.78 ? 117 ASN D CA  1 
ATOM   6705 C C   . ASN D 2 117 ? 83.783  -72.412  28.292  1.00 132.86 ? 117 ASN D C   1 
ATOM   6706 O O   . ASN D 2 117 ? 84.947  -72.218  28.655  1.00 133.50 ? 117 ASN D O   1 
ATOM   6707 C CB  . ASN D 2 117 ? 82.483  -70.249  28.213  1.00 131.41 ? 117 ASN D CB  1 
ATOM   6708 C CG  . ASN D 2 117 ? 83.489  -69.653  29.166  1.00 134.02 ? 117 ASN D CG  1 
ATOM   6709 O OD1 . ASN D 2 117 ? 84.694  -69.845  29.015  1.00 136.43 ? 117 ASN D OD1 1 
ATOM   6710 N ND2 . ASN D 2 117 ? 82.999  -68.917  30.157  1.00 133.19 ? 117 ASN D ND2 1 
ATOM   6711 N N   . LEU D 2 118 ? 83.091  -73.493  28.647  1.00 131.47 ? 118 LEU D N   1 
ATOM   6712 C CA  . LEU D 2 118 ? 83.665  -74.555  29.475  1.00 130.38 ? 118 LEU D CA  1 
ATOM   6713 C C   . LEU D 2 118 ? 84.972  -75.087  28.903  1.00 132.20 ? 118 LEU D C   1 
ATOM   6714 O O   . LEU D 2 118 ? 86.042  -74.908  29.489  1.00 131.92 ? 118 LEU D O   1 
ATOM   6715 C CB  . LEU D 2 118 ? 82.669  -75.712  29.619  1.00 130.19 ? 118 LEU D CB  1 
ATOM   6716 C CG  . LEU D 2 118 ? 83.196  -77.127  29.897  1.00 127.83 ? 118 LEU D CG  1 
ATOM   6717 C CD1 . LEU D 2 118 ? 83.992  -77.172  31.185  1.00 124.55 ? 118 LEU D CD1 1 
ATOM   6718 C CD2 . LEU D 2 118 ? 82.057  -78.146  29.937  1.00 125.92 ? 118 LEU D CD2 1 
ATOM   6719 N N   . TYR D 2 119 ? 84.872  -75.740  27.749  1.00 132.82 ? 119 TYR D N   1 
ATOM   6720 C CA  . TYR D 2 119 ? 86.014  -76.414  27.145  1.00 134.91 ? 119 TYR D CA  1 
ATOM   6721 C C   . TYR D 2 119 ? 87.184  -75.490  26.810  1.00 136.51 ? 119 TYR D C   1 
ATOM   6722 O O   . TYR D 2 119 ? 88.290  -75.965  26.560  1.00 137.60 ? 119 TYR D O   1 
ATOM   6723 C CB  . TYR D 2 119 ? 85.585  -77.202  25.904  1.00 136.85 ? 119 TYR D CB  1 
ATOM   6724 C CG  . TYR D 2 119 ? 85.131  -78.613  26.210  1.00 136.43 ? 119 TYR D CG  1 
ATOM   6725 C CD1 . TYR D 2 119 ? 83.900  -78.854  26.809  1.00 136.50 ? 119 TYR D CD1 1 
ATOM   6726 C CD2 . TYR D 2 119 ? 85.931  -79.706  25.896  1.00 136.95 ? 119 TYR D CD2 1 
ATOM   6727 C CE1 . TYR D 2 119 ? 83.478  -80.148  27.092  1.00 138.17 ? 119 TYR D CE1 1 
ATOM   6728 C CE2 . TYR D 2 119 ? 85.519  -81.003  26.173  1.00 138.88 ? 119 TYR D CE2 1 
ATOM   6729 C CZ  . TYR D 2 119 ? 84.292  -81.219  26.772  1.00 139.23 ? 119 TYR D CZ  1 
ATOM   6730 O OH  . TYR D 2 119 ? 83.879  -82.506  27.050  1.00 138.03 ? 119 TYR D OH  1 
ATOM   6731 N N   . GLU D 2 120 ? 86.952  -74.180  26.811  1.00 136.44 ? 120 GLU D N   1 
ATOM   6732 C CA  . GLU D 2 120 ? 88.045  -73.240  26.570  1.00 136.69 ? 120 GLU D CA  1 
ATOM   6733 C C   . GLU D 2 120 ? 88.841  -72.943  27.833  1.00 135.96 ? 120 GLU D C   1 
ATOM   6734 O O   . GLU D 2 120 ? 89.819  -72.194  27.804  1.00 136.74 ? 120 GLU D O   1 
ATOM   6735 C CB  . GLU D 2 120 ? 87.562  -71.962  25.887  1.00 136.59 ? 120 GLU D CB  1 
ATOM   6736 C CG  . GLU D 2 120 ? 87.338  -72.157  24.395  1.00 138.14 ? 120 GLU D CG  1 
ATOM   6737 C CD  . GLU D 2 120 ? 88.542  -72.787  23.701  1.00 138.88 ? 120 GLU D CD  1 
ATOM   6738 O OE1 . GLU D 2 120 ? 88.349  -73.721  22.891  1.00 137.75 ? 120 GLU D OE1 1 
ATOM   6739 O OE2 . GLU D 2 120 ? 89.684  -72.346  23.961  1.00 139.47 ? 120 GLU D OE2 1 
ATOM   6740 N N   . LYS D 2 121 ? 88.400  -73.510  28.950  1.00 134.69 ? 121 LYS D N   1 
ATOM   6741 C CA  . LYS D 2 121 ? 89.320  -73.735  30.048  1.00 134.40 ? 121 LYS D CA  1 
ATOM   6742 C C   . LYS D 2 121 ? 90.078  -75.039  29.831  1.00 135.07 ? 121 LYS D C   1 
ATOM   6743 O O   . LYS D 2 121 ? 91.269  -75.130  30.115  1.00 136.43 ? 121 LYS D O   1 
ATOM   6744 C CB  . LYS D 2 121 ? 88.623  -73.749  31.399  1.00 131.55 ? 121 LYS D CB  1 
ATOM   6745 C CG  . LYS D 2 121 ? 89.632  -73.763  32.529  1.00 132.62 ? 121 LYS D CG  1 
ATOM   6746 C CD  . LYS D 2 121 ? 90.758  -72.779  32.224  1.00 132.60 ? 121 LYS D CD  1 
ATOM   6747 C CE  . LYS D 2 121 ? 92.069  -73.203  32.856  1.00 130.82 ? 121 LYS D CE  1 
ATOM   6748 N NZ  . LYS D 2 121 ? 93.219  -72.421  32.323  1.00 128.42 ? 121 LYS D NZ  1 
ATOM   6749 N N   . VAL D 2 122 ? 89.377  -76.051  29.332  1.00 133.39 ? 122 VAL D N   1 
ATOM   6750 C CA  . VAL D 2 122 ? 89.994  -77.349  29.089  1.00 134.24 ? 122 VAL D CA  1 
ATOM   6751 C C   . VAL D 2 122 ? 90.888  -77.362  27.845  1.00 137.61 ? 122 VAL D C   1 
ATOM   6752 O O   . VAL D 2 122 ? 92.035  -77.805  27.910  1.00 139.65 ? 122 VAL D O   1 
ATOM   6753 C CB  . VAL D 2 122 ? 88.937  -78.461  28.994  1.00 133.68 ? 122 VAL D CB  1 
ATOM   6754 C CG1 . VAL D 2 122 ? 89.503  -79.683  28.288  1.00 132.70 ? 122 VAL D CG1 1 
ATOM   6755 C CG2 . VAL D 2 122 ? 88.425  -78.814  30.382  1.00 130.83 ? 122 VAL D CG2 1 
ATOM   6756 N N   . ARG D 2 123 ? 90.372  -76.860  26.724  1.00 138.02 ? 123 ARG D N   1 
ATOM   6757 C CA  . ARG D 2 123 ? 91.129  -76.803  25.467  1.00 138.50 ? 123 ARG D CA  1 
ATOM   6758 C C   . ARG D 2 123 ? 92.335  -75.856  25.564  1.00 141.64 ? 123 ARG D C   1 
ATOM   6759 O O   . ARG D 2 123 ? 93.139  -75.764  24.632  1.00 141.57 ? 123 ARG D O   1 
ATOM   6760 C CB  . ARG D 2 123 ? 90.212  -76.437  24.284  1.00 137.16 ? 123 ARG D CB  1 
ATOM   6761 C CG  . ARG D 2 123 ? 90.780  -75.411  23.300  1.00 137.25 ? 123 ARG D CG  1 
ATOM   6762 C CD  . ARG D 2 123 ? 91.372  -76.057  22.051  1.00 136.82 ? 123 ARG D CD  1 
ATOM   6763 N NE  . ARG D 2 123 ? 90.569  -75.798  20.857  1.00 134.89 ? 123 ARG D NE  1 
ATOM   6764 C CZ  . ARG D 2 123 ? 90.694  -74.723  20.082  1.00 134.48 ? 123 ARG D CZ  1 
ATOM   6765 N NH1 . ARG D 2 123 ? 91.592  -73.787  20.369  1.00 133.98 ? 123 ARG D NH1 1 
ATOM   6766 N NH2 . ARG D 2 123 ? 89.915  -74.581  19.017  1.00 132.13 ? 123 ARG D NH2 1 
ATOM   6767 N N   . SER D 2 124 ? 92.451  -75.159  26.695  1.00 141.37 ? 124 SER D N   1 
ATOM   6768 C CA  . SER D 2 124 ? 93.534  -74.193  26.917  1.00 141.85 ? 124 SER D CA  1 
ATOM   6769 C C   . SER D 2 124 ? 94.908  -74.793  27.271  1.00 142.16 ? 124 SER D C   1 
ATOM   6770 O O   . SER D 2 124 ? 95.939  -74.192  26.956  1.00 141.62 ? 124 SER D O   1 
ATOM   6771 C CB  . SER D 2 124 ? 93.129  -73.160  27.978  1.00 137.42 ? 124 SER D CB  1 
ATOM   6772 O OG  . SER D 2 124 ? 92.078  -72.329  27.518  1.00 137.07 ? 124 SER D OG  1 
ATOM   6773 N N   . GLN D 2 125 ? 94.935  -75.952  27.928  1.00 140.34 ? 125 GLN D N   1 
ATOM   6774 C CA  . GLN D 2 125 ? 96.214  -76.539  28.343  1.00 139.70 ? 125 GLN D CA  1 
ATOM   6775 C C   . GLN D 2 125 ? 96.431  -78.004  27.964  1.00 139.89 ? 125 GLN D C   1 
ATOM   6776 O O   . GLN D 2 125 ? 97.246  -78.318  27.096  1.00 138.77 ? 125 GLN D O   1 
ATOM   6777 C CB  . GLN D 2 125 ? 96.418  -76.379  29.854  1.00 138.95 ? 125 GLN D CB  1 
ATOM   6778 C CG  . GLN D 2 125 ? 95.301  -76.963  30.700  1.00 136.91 ? 125 GLN D CG  1 
ATOM   6779 C CD  . GLN D 2 125 ? 94.070  -76.085  30.707  1.00 136.95 ? 125 GLN D CD  1 
ATOM   6780 O OE1 . GLN D 2 125 ? 94.168  -74.863  30.584  1.00 136.73 ? 125 GLN D OE1 1 
ATOM   6781 N NE2 . GLN D 2 125 ? 92.903  -76.702  30.845  1.00 136.14 ? 125 GLN D NE2 1 
ATOM   6782 N N   . LEU D 2 126 ? 95.698  -78.893  28.623  1.00 140.60 ? 126 LEU D N   1 
ATOM   6783 C CA  . LEU D 2 126 ? 96.015  -80.314  28.592  1.00 142.93 ? 126 LEU D CA  1 
ATOM   6784 C C   . LEU D 2 126 ? 94.981  -81.110  27.808  1.00 143.22 ? 126 LEU D C   1 
ATOM   6785 O O   . LEU D 2 126 ? 95.120  -82.320  27.636  1.00 143.61 ? 126 LEU D O   1 
ATOM   6786 C CB  . LEU D 2 126 ? 96.124  -80.845  30.024  1.00 141.70 ? 126 LEU D CB  1 
ATOM   6787 C CG  . LEU D 2 126 ? 97.102  -81.984  30.310  1.00 140.21 ? 126 LEU D CG  1 
ATOM   6788 C CD1 . LEU D 2 126 ? 98.117  -81.552  31.347  1.00 138.18 ? 126 LEU D CD1 1 
ATOM   6789 C CD2 . LEU D 2 126 ? 96.344  -83.207  30.782  1.00 140.04 ? 126 LEU D CD2 1 
ATOM   6790 N N   . ASN D 2 129 ? 96.918  -86.898  26.531  1.00 143.65 ? 129 ASN D N   1 
ATOM   6791 C CA  . ASN D 2 129 ? 96.304  -86.063  27.562  1.00 145.97 ? 129 ASN D CA  1 
ATOM   6792 C C   . ASN D 2 129 ? 94.788  -85.862  27.411  1.00 146.66 ? 129 ASN D C   1 
ATOM   6793 O O   . ASN D 2 129 ? 94.010  -86.341  28.237  1.00 146.55 ? 129 ASN D O   1 
ATOM   6794 C CB  . ASN D 2 129 ? 97.024  -84.713  27.666  1.00 144.61 ? 129 ASN D CB  1 
ATOM   6795 C CG  . ASN D 2 129 ? 98.116  -84.715  28.718  1.00 142.01 ? 129 ASN D CG  1 
ATOM   6796 O OD1 . ASN D 2 129 ? 98.100  -85.529  29.640  1.00 140.71 ? 129 ASN D OD1 1 
ATOM   6797 N ND2 . ASN D 2 129 ? 99.059  -83.787  28.596  1.00 141.14 ? 129 ASN D ND2 1 
ATOM   6798 N N   . ALA D 2 130 ? 94.373  -85.155  26.362  1.00 147.01 ? 130 ALA D N   1 
ATOM   6799 C CA  . ALA D 2 130 ? 92.961  -84.804  26.175  1.00 147.17 ? 130 ALA D CA  1 
ATOM   6800 C C   . ALA D 2 130 ? 92.197  -85.806  25.304  1.00 150.02 ? 130 ALA D C   1 
ATOM   6801 O O   . ALA D 2 130 ? 92.646  -86.150  24.209  1.00 150.15 ? 130 ALA D O   1 
ATOM   6802 C CB  . ALA D 2 130 ? 92.843  -83.402  25.596  1.00 144.86 ? 130 ALA D CB  1 
ATOM   6803 N N   . LYS D 2 131 ? 91.046  -86.274  25.793  1.00 149.86 ? 131 LYS D N   1 
ATOM   6804 C CA  . LYS D 2 131 ? 90.251  -87.265  25.063  1.00 146.14 ? 131 LYS D CA  1 
ATOM   6805 C C   . LYS D 2 131 ? 88.736  -87.019  25.037  1.00 143.62 ? 131 LYS D C   1 
ATOM   6806 O O   . LYS D 2 131 ? 88.083  -87.012  26.079  1.00 142.03 ? 131 LYS D O   1 
ATOM   6807 C CB  . LYS D 2 131 ? 90.519  -88.663  25.631  1.00 143.66 ? 131 LYS D CB  1 
ATOM   6808 C CG  . LYS D 2 131 ? 91.945  -89.153  25.447  1.00 142.41 ? 131 LYS D CG  1 
ATOM   6809 C CD  . LYS D 2 131 ? 92.263  -90.282  26.412  1.00 142.94 ? 131 LYS D CD  1 
ATOM   6810 C CE  . LYS D 2 131 ? 91.215  -91.381  26.345  1.00 139.12 ? 131 LYS D CE  1 
ATOM   6811 N NZ  . LYS D 2 131 ? 91.416  -92.395  27.415  1.00 132.42 ? 131 LYS D NZ  1 
ATOM   6812 N N   . GLU D 2 132 ? 88.183  -86.822  23.842  1.00 144.41 ? 132 GLU D N   1 
ATOM   6813 C CA  . GLU D 2 132 ? 86.747  -87.008  23.631  1.00 145.44 ? 132 GLU D CA  1 
ATOM   6814 C C   . GLU D 2 132 ? 86.471  -87.797  22.348  1.00 148.02 ? 132 GLU D C   1 
ATOM   6815 O O   . GLU D 2 132 ? 86.716  -87.303  21.243  1.00 148.76 ? 132 GLU D O   1 
ATOM   6816 C CB  . GLU D 2 132 ? 86.010  -85.668  23.564  1.00 144.04 ? 132 GLU D CB  1 
ATOM   6817 C CG  . GLU D 2 132 ? 84.495  -85.812  23.388  1.00 141.82 ? 132 GLU D CG  1 
ATOM   6818 C CD  . GLU D 2 132 ? 83.934  -84.959  22.260  1.00 140.30 ? 132 GLU D CD  1 
ATOM   6819 O OE1 . GLU D 2 132 ? 82.692  -84.865  22.143  1.00 138.66 ? 132 GLU D OE1 1 
ATOM   6820 O OE2 . GLU D 2 132 ? 84.731  -84.386  21.489  1.00 140.93 ? 132 GLU D OE2 1 
ATOM   6821 N N   . ILE D 2 133 ? 85.954  -89.014  22.496  1.00 147.16 ? 133 ILE D N   1 
ATOM   6822 C CA  . ILE D 2 133 ? 85.459  -89.784  21.356  1.00 148.35 ? 133 ILE D CA  1 
ATOM   6823 C C   . ILE D 2 133 ? 84.026  -89.362  21.029  1.00 146.75 ? 133 ILE D C   1 
ATOM   6824 O O   . ILE D 2 133 ? 83.635  -89.255  19.865  1.00 148.03 ? 133 ILE D O   1 
ATOM   6825 C CB  . ILE D 2 133 ? 85.552  -91.309  21.607  1.00 149.76 ? 133 ILE D CB  1 
ATOM   6826 C CG1 . ILE D 2 133 ? 86.546  -91.945  20.633  1.00 148.10 ? 133 ILE D CG1 1 
ATOM   6827 C CG2 . ILE D 2 133 ? 84.181  -91.973  21.490  1.00 147.83 ? 133 ILE D CG2 1 
ATOM   6828 C CD1 . ILE D 2 133 ? 87.886  -91.239  20.576  1.00 145.56 ? 133 ILE D CD1 1 
ATOM   6829 N N   . GLY D 2 134 ? 83.256  -89.116  22.083  1.00 144.30 ? 134 GLY D N   1 
ATOM   6830 C CA  . GLY D 2 134 ? 81.895  -88.634  21.964  1.00 141.89 ? 134 GLY D CA  1 
ATOM   6831 C C   . GLY D 2 134 ? 81.376  -88.217  23.327  1.00 142.72 ? 134 GLY D C   1 
ATOM   6832 O O   . GLY D 2 134 ? 81.993  -88.521  24.352  1.00 142.12 ? 134 GLY D O   1 
ATOM   6833 N N   . ASN D 2 135 ? 80.251  -87.509  23.341  1.00 141.67 ? 135 ASN D N   1 
ATOM   6834 C CA  . ASN D 2 135 ? 79.589  -87.143  24.592  1.00 141.71 ? 135 ASN D CA  1 
ATOM   6835 C C   . ASN D 2 135 ? 80.468  -86.296  25.501  1.00 139.14 ? 135 ASN D C   1 
ATOM   6836 O O   . ASN D 2 135 ? 80.308  -86.306  26.723  1.00 137.53 ? 135 ASN D O   1 
ATOM   6837 C CB  . ASN D 2 135 ? 79.150  -88.400  25.343  1.00 142.33 ? 135 ASN D CB  1 
ATOM   6838 C CG  . ASN D 2 135 ? 78.439  -89.391  24.448  1.00 143.27 ? 135 ASN D CG  1 
ATOM   6839 O OD1 . ASN D 2 135 ? 79.072  -90.122  23.684  1.00 143.17 ? 135 ASN D OD1 1 
ATOM   6840 N ND2 . ASN D 2 135 ? 77.116  -89.425  24.539  1.00 142.75 ? 135 ASN D ND2 1 
ATOM   6841 N N   . GLY D 2 136 ? 81.400  -85.565  24.903  1.00 138.32 ? 136 GLY D N   1 
ATOM   6842 C CA  . GLY D 2 136 ? 82.286  -84.722  25.677  1.00 137.34 ? 136 GLY D CA  1 
ATOM   6843 C C   . GLY D 2 136 ? 83.194  -85.537  26.573  1.00 136.69 ? 136 GLY D C   1 
ATOM   6844 O O   . GLY D 2 136 ? 83.505  -86.691  26.276  1.00 135.46 ? 136 GLY D O   1 
ATOM   6845 N N   . CYS D 2 137 ? 83.607  -84.936  27.682  1.00 137.17 ? 137 CYS D N   1 
ATOM   6846 C CA  . CYS D 2 137 ? 84.593  -85.549  28.559  1.00 136.03 ? 137 CYS D CA  1 
ATOM   6847 C C   . CYS D 2 137 ? 84.584  -84.890  29.939  1.00 135.56 ? 137 CYS D C   1 
ATOM   6848 O O   . CYS D 2 137 ? 83.753  -84.023  30.224  1.00 135.25 ? 137 CYS D O   1 
ATOM   6849 C CB  . CYS D 2 137 ? 85.981  -85.441  27.922  1.00 138.11 ? 137 CYS D CB  1 
ATOM   6850 S SG  . CYS D 2 137 ? 87.328  -86.183  28.867  1.00 138.50 ? 137 CYS D SG  1 
ATOM   6851 N N   . CYS D 2 144 ? 92.582  -89.203  38.706  1.00 152.25 ? 144 CYS D N   1 
ATOM   6852 C CA  . CYS D 2 144 ? 92.395  -89.095  40.149  1.00 151.83 ? 144 CYS D CA  1 
ATOM   6853 C C   . CYS D 2 144 ? 91.085  -89.755  40.569  1.00 151.83 ? 144 CYS D C   1 
ATOM   6854 O O   . CYS D 2 144 ? 90.372  -90.326  39.741  1.00 151.82 ? 144 CYS D O   1 
ATOM   6855 C CB  . CYS D 2 144 ? 92.386  -87.623  40.576  1.00 152.41 ? 144 CYS D CB  1 
ATOM   6856 S SG  . CYS D 2 144 ? 93.449  -86.553  39.571  1.00 160.82 ? 144 CYS D SG  1 
ATOM   6857 N N   . ASP D 2 145 ? 90.779  -89.679  41.862  1.00 150.66 ? 145 ASP D N   1 
ATOM   6858 C CA  . ASP D 2 145 ? 89.458  -90.036  42.366  1.00 149.50 ? 145 ASP D CA  1 
ATOM   6859 C C   . ASP D 2 145 ? 88.621  -88.758  42.460  1.00 148.13 ? 145 ASP D C   1 
ATOM   6860 O O   . ASP D 2 145 ? 87.610  -88.611  41.770  1.00 145.87 ? 145 ASP D O   1 
ATOM   6861 C CB  . ASP D 2 145 ? 89.551  -90.744  43.726  1.00 147.44 ? 145 ASP D CB  1 
ATOM   6862 C CG  . ASP D 2 145 ? 90.229  -89.896  44.786  1.00 145.49 ? 145 ASP D CG  1 
ATOM   6863 O OD1 . ASP D 2 145 ? 91.065  -89.042  44.421  1.00 145.32 ? 145 ASP D OD1 1 
ATOM   6864 O OD2 . ASP D 2 145 ? 89.923  -90.082  45.982  1.00 141.32 ? 145 ASP D OD2 1 
ATOM   6865 N N   . ASN D 2 146 ? 89.061  -87.836  43.314  1.00 148.32 ? 146 ASN D N   1 
ATOM   6866 C CA  . ASN D 2 146 ? 88.440  -86.522  43.459  1.00 147.63 ? 146 ASN D CA  1 
ATOM   6867 C C   . ASN D 2 146 ? 89.458  -85.391  43.353  1.00 148.05 ? 146 ASN D C   1 
ATOM   6868 O O   . ASN D 2 146 ? 89.429  -84.580  42.429  1.00 148.73 ? 146 ASN D O   1 
ATOM   6869 C CB  . ASN D 2 146 ? 87.743  -86.401  44.823  1.00 147.33 ? 146 ASN D CB  1 
ATOM   6870 C CG  . ASN D 2 146 ? 86.511  -87.270  44.936  1.00 146.92 ? 146 ASN D CG  1 
ATOM   6871 O OD1 . ASN D 2 146 ? 85.482  -86.993  44.317  1.00 146.60 ? 146 ASN D OD1 1 
ATOM   6872 N ND2 . ASN D 2 146 ? 86.602  -88.321  45.748  1.00 143.63 ? 146 ASN D ND2 1 
ATOM   6873 N N   . THR D 2 147 ? 90.374  -85.387  44.316  1.00 150.10 ? 147 THR D N   1 
ATOM   6874 C CA  . THR D 2 147 ? 91.161  -84.217  44.701  1.00 151.10 ? 147 THR D CA  1 
ATOM   6875 C C   . THR D 2 147 ? 92.244  -83.744  43.717  1.00 151.30 ? 147 THR D C   1 
ATOM   6876 O O   . THR D 2 147 ? 92.857  -82.703  43.940  1.00 151.58 ? 147 THR D O   1 
ATOM   6877 C CB  . THR D 2 147 ? 91.808  -84.453  46.093  1.00 149.72 ? 147 THR D CB  1 
ATOM   6878 O OG1 . THR D 2 147 ? 91.029  -85.406  46.830  1.00 147.79 ? 147 THR D OG1 1 
ATOM   6879 C CG2 . THR D 2 147 ? 91.901  -83.156  46.882  1.00 148.03 ? 147 THR D CG2 1 
ATOM   6880 N N   . CYS D 2 148 ? 92.470  -84.499  42.641  1.00 152.35 ? 148 CYS D N   1 
ATOM   6881 C CA  . CYS D 2 148 ? 93.554  -84.230  41.677  1.00 153.81 ? 148 CYS D CA  1 
ATOM   6882 C C   . CYS D 2 148 ? 93.612  -82.805  41.097  1.00 152.34 ? 148 CYS D C   1 
ATOM   6883 O O   . CYS D 2 148 ? 94.678  -82.192  41.035  1.00 149.74 ? 148 CYS D O   1 
ATOM   6884 C CB  . CYS D 2 148 ? 93.508  -85.265  40.536  1.00 155.10 ? 148 CYS D CB  1 
ATOM   6885 S SG  . CYS D 2 148 ? 94.541  -84.915  39.066  1.00 156.68 ? 148 CYS D SG  1 
ATOM   6886 N N   . MET D 2 149 ? 92.462  -82.293  40.677  1.00 153.86 ? 149 MET D N   1 
ATOM   6887 C CA  . MET D 2 149 ? 92.356  -81.038  39.927  1.00 152.28 ? 149 MET D CA  1 
ATOM   6888 C C   . MET D 2 149 ? 92.081  -79.787  40.764  1.00 149.17 ? 149 MET D C   1 
ATOM   6889 O O   . MET D 2 149 ? 91.819  -78.720  40.221  1.00 146.17 ? 149 MET D O   1 
ATOM   6890 C CB  . MET D 2 149 ? 91.293  -81.172  38.831  1.00 153.12 ? 149 MET D CB  1 
ATOM   6891 C CG  . MET D 2 149 ? 90.100  -82.060  39.202  1.00 154.01 ? 149 MET D CG  1 
ATOM   6892 S SD  . MET D 2 149 ? 90.326  -83.794  38.714  1.00 163.25 ? 149 MET D SD  1 
ATOM   6893 C CE  . MET D 2 149 ? 88.669  -84.470  38.857  1.00 154.16 ? 149 MET D CE  1 
ATOM   6894 N N   . GLU D 2 150 ? 92.171  -79.910  42.081  1.00 150.52 ? 150 GLU D N   1 
ATOM   6895 C CA  . GLU D 2 150 ? 91.289  -79.172  42.980  1.00 150.54 ? 150 GLU D CA  1 
ATOM   6896 C C   . GLU D 2 150 ? 90.968  -77.741  42.560  1.00 148.74 ? 150 GLU D C   1 
ATOM   6897 O O   . GLU D 2 150 ? 89.846  -77.470  42.126  1.00 144.46 ? 150 GLU D O   1 
ATOM   6898 C CB  . GLU D 2 150 ? 91.889  -79.160  44.390  1.00 148.96 ? 150 GLU D CB  1 
ATOM   6899 C CG  . GLU D 2 150 ? 90.852  -79.221  45.485  1.00 146.99 ? 150 GLU D CG  1 
ATOM   6900 C CD  . GLU D 2 150 ? 89.946  -80.421  45.331  1.00 147.20 ? 150 GLU D CD  1 
ATOM   6901 O OE1 . GLU D 2 150 ? 90.303  -81.342  44.568  1.00 146.80 ? 150 GLU D OE1 1 
ATOM   6902 O OE2 . GLU D 2 150 ? 88.871  -80.443  45.961  1.00 148.63 ? 150 GLU D OE2 1 
ATOM   6903 N N   . SER D 2 151 ? 91.923  -76.826  42.646  1.00 150.12 ? 151 SER D N   1 
ATOM   6904 C CA  . SER D 2 151 ? 91.598  -75.474  42.224  1.00 148.45 ? 151 SER D CA  1 
ATOM   6905 C C   . SER D 2 151 ? 92.015  -75.295  40.774  1.00 147.21 ? 151 SER D C   1 
ATOM   6906 O O   . SER D 2 151 ? 93.196  -75.175  40.452  1.00 146.72 ? 151 SER D O   1 
ATOM   6907 C CB  . SER D 2 151 ? 92.245  -74.427  43.137  1.00 147.09 ? 151 SER D CB  1 
ATOM   6908 O OG  . SER D 2 151 ? 93.655  -74.436  43.028  1.00 146.32 ? 151 SER D OG  1 
ATOM   6909 N N   . VAL D 2 152 ? 91.012  -75.255  39.907  1.00 145.80 ? 152 VAL D N   1 
ATOM   6910 C CA  . VAL D 2 152 ? 91.217  -75.126  38.478  1.00 145.41 ? 152 VAL D CA  1 
ATOM   6911 C C   . VAL D 2 152 ? 90.626  -73.790  38.141  1.00 144.32 ? 152 VAL D C   1 
ATOM   6912 O O   . VAL D 2 152 ? 91.312  -72.855  37.728  1.00 143.71 ? 152 VAL D O   1 
ATOM   6913 C CB  . VAL D 2 152 ? 90.396  -76.170  37.703  1.00 144.13 ? 152 VAL D CB  1 
ATOM   6914 C CG1 . VAL D 2 152 ? 90.553  -75.959  36.209  1.00 139.14 ? 152 VAL D CG1 1 
ATOM   6915 C CG2 . VAL D 2 152 ? 90.792  -77.576  38.097  1.00 145.27 ? 152 VAL D CG2 1 
ATOM   6916 N N   . LYS D 2 153 ? 89.317  -73.731  38.334  1.00 144.00 ? 153 LYS D N   1 
ATOM   6917 C CA  . LYS D 2 153 ? 88.554  -72.510  38.231  1.00 145.86 ? 153 LYS D CA  1 
ATOM   6918 C C   . LYS D 2 153 ? 89.066  -71.501  39.259  1.00 147.49 ? 153 LYS D C   1 
ATOM   6919 O O   . LYS D 2 153 ? 89.063  -70.295  39.008  1.00 145.49 ? 153 LYS D O   1 
ATOM   6920 C CB  . LYS D 2 153 ? 87.078  -72.824  38.468  1.00 144.64 ? 153 LYS D CB  1 
ATOM   6921 C CG  . LYS D 2 153 ? 86.691  -74.249  38.084  1.00 141.72 ? 153 LYS D CG  1 
ATOM   6922 C CD  . LYS D 2 153 ? 87.031  -75.233  39.192  1.00 141.34 ? 153 LYS D CD  1 
ATOM   6923 C CE  . LYS D 2 153 ? 87.001  -76.665  38.690  1.00 139.96 ? 153 LYS D CE  1 
ATOM   6924 N NZ  . LYS D 2 153 ? 87.001  -77.645  39.817  1.00 141.98 ? 153 LYS D NZ  1 
ATOM   6925 N N   . ASN D 2 154 ? 89.509  -71.997  40.414  1.00 147.54 ? 154 ASN D N   1 
ATOM   6926 C CA  . ASN D 2 154 ? 90.100  -71.137  41.441  1.00 145.90 ? 154 ASN D CA  1 
ATOM   6927 C C   . ASN D 2 154 ? 91.472  -70.620  41.015  1.00 146.40 ? 154 ASN D C   1 
ATOM   6928 O O   . ASN D 2 154 ? 91.960  -69.610  41.531  1.00 144.56 ? 154 ASN D O   1 
ATOM   6929 C CB  . ASN D 2 154 ? 90.197  -71.864  42.788  1.00 142.62 ? 154 ASN D CB  1 
ATOM   6930 C CG  . ASN D 2 154 ? 91.111  -71.152  43.775  1.00 144.25 ? 154 ASN D CG  1 
ATOM   6931 O OD1 . ASN D 2 154 ? 91.895  -71.787  44.483  1.00 144.93 ? 154 ASN D OD1 1 
ATOM   6932 N ND2 . ASN D 2 154 ? 91.023  -69.826  43.816  1.00 144.41 ? 154 ASN D ND2 1 
ATOM   6933 N N   . GLY D 2 155 ? 92.080  -71.325  40.064  1.00 145.87 ? 155 GLY D N   1 
ATOM   6934 C CA  . GLY D 2 155 ? 93.384  -70.966  39.539  1.00 144.22 ? 155 GLY D CA  1 
ATOM   6935 C C   . GLY D 2 155 ? 94.041  -72.138  38.834  1.00 141.72 ? 155 GLY D C   1 
ATOM   6936 O O   . GLY D 2 155 ? 94.866  -71.960  37.937  1.00 139.14 ? 155 GLY D O   1 
ATOM   6937 N N   . TYR D 2 159 ? 100.598 -80.234  34.611  1.00 146.82 ? 159 TYR D N   1 
ATOM   6938 C CA  . TYR D 2 159 ? 101.275 -80.340  33.321  1.00 148.90 ? 159 TYR D CA  1 
ATOM   6939 C C   . TYR D 2 159 ? 102.651 -81.007  33.433  1.00 148.80 ? 159 TYR D C   1 
ATOM   6940 O O   . TYR D 2 159 ? 102.922 -81.987  32.738  1.00 147.36 ? 159 TYR D O   1 
ATOM   6941 C CB  . TYR D 2 159 ? 101.398 -78.963  32.654  1.00 148.34 ? 159 TYR D CB  1 
ATOM   6942 C CG  . TYR D 2 159 ? 100.853 -78.909  31.247  1.00 144.85 ? 159 TYR D CG  1 
ATOM   6943 C CD1 . TYR D 2 159 ? 100.722 -80.064  30.488  1.00 144.89 ? 159 TYR D CD1 1 
ATOM   6944 C CD2 . TYR D 2 159 ? 100.470 -77.704  30.681  1.00 141.31 ? 159 TYR D CD2 1 
ATOM   6945 C CE1 . TYR D 2 159 ? 100.224 -80.021  29.207  1.00 142.78 ? 159 TYR D CE1 1 
ATOM   6946 C CE2 . TYR D 2 159 ? 99.973  -77.649  29.401  1.00 141.58 ? 159 TYR D CE2 1 
ATOM   6947 C CZ  . TYR D 2 159 ? 99.852  -78.812  28.668  1.00 143.18 ? 159 TYR D CZ  1 
ATOM   6948 O OH  . TYR D 2 159 ? 99.357  -78.769  27.388  1.00 143.54 ? 159 TYR D OH  1 
ATOM   6949 N N   . PRO D 2 160 ? 103.524 -80.478  34.310  1.00 148.70 ? 160 PRO D N   1 
ATOM   6950 C CA  . PRO D 2 160 ? 104.895 -80.995  34.441  1.00 147.34 ? 160 PRO D CA  1 
ATOM   6951 C C   . PRO D 2 160 ? 105.015 -82.522  34.589  1.00 146.18 ? 160 PRO D C   1 
ATOM   6952 O O   . PRO D 2 160 ? 105.999 -83.093  34.123  1.00 145.52 ? 160 PRO D O   1 
ATOM   6953 C CB  . PRO D 2 160 ? 105.407 -80.283  35.694  1.00 146.58 ? 160 PRO D CB  1 
ATOM   6954 C CG  . PRO D 2 160 ? 104.684 -78.975  35.679  1.00 145.65 ? 160 PRO D CG  1 
ATOM   6955 C CD  . PRO D 2 160 ? 103.307 -79.289  35.157  1.00 147.14 ? 160 PRO D CD  1 
ATOM   6956 N N   . LYS D 2 161 ? 104.050 -83.169  35.234  1.00 145.12 ? 161 LYS D N   1 
ATOM   6957 C CA  . LYS D 2 161 ? 104.074 -84.623  35.375  1.00 142.39 ? 161 LYS D CA  1 
ATOM   6958 C C   . LYS D 2 161 ? 103.565 -85.336  34.130  1.00 143.20 ? 161 LYS D C   1 
ATOM   6959 O O   . LYS D 2 161 ? 103.931 -86.477  33.861  1.00 140.81 ? 161 LYS D O   1 
ATOM   6960 C CB  . LYS D 2 161 ? 103.220 -85.055  36.573  1.00 139.86 ? 161 LYS D CB  1 
ATOM   6961 C CG  . LYS D 2 161 ? 102.648 -86.466  36.450  1.00 138.83 ? 161 LYS D CG  1 
ATOM   6962 C CD  . LYS D 2 161 ? 101.655 -86.770  37.562  1.00 135.00 ? 161 LYS D CD  1 
ATOM   6963 C CE  . LYS D 2 161 ? 102.356 -86.993  38.886  1.00 131.07 ? 161 LYS D CE  1 
ATOM   6964 N NZ  . LYS D 2 161 ? 103.233 -88.187  38.827  1.00 128.27 ? 161 LYS D NZ  1 
ATOM   6965 N N   . TYR D 2 162 ? 102.720 -84.647  33.374  1.00 145.06 ? 162 TYR D N   1 
ATOM   6966 C CA  . TYR D 2 162 ? 101.772 -85.319  32.490  1.00 146.17 ? 162 TYR D CA  1 
ATOM   6967 C C   . TYR D 2 162 ? 102.212 -85.561  31.039  1.00 146.98 ? 162 TYR D C   1 
ATOM   6968 O O   . TYR D 2 162 ? 102.487 -86.701  30.668  1.00 145.88 ? 162 TYR D O   1 
ATOM   6969 C CB  . TYR D 2 162 ? 100.408 -84.607  32.556  1.00 145.69 ? 162 TYR D CB  1 
ATOM   6970 C CG  . TYR D 2 162 ? 99.790  -84.639  33.944  1.00 143.72 ? 162 TYR D CG  1 
ATOM   6971 C CD1 . TYR D 2 162 ? 100.288 -83.838  34.968  1.00 143.31 ? 162 TYR D CD1 1 
ATOM   6972 C CD2 . TYR D 2 162 ? 98.730  -85.489  34.238  1.00 141.74 ? 162 TYR D CD2 1 
ATOM   6973 C CE1 . TYR D 2 162 ? 99.739  -83.873  36.240  1.00 140.34 ? 162 TYR D CE1 1 
ATOM   6974 C CE2 . TYR D 2 162 ? 98.176  -85.531  35.506  1.00 140.91 ? 162 TYR D CE2 1 
ATOM   6975 C CZ  . TYR D 2 162 ? 98.684  -84.722  36.501  1.00 139.22 ? 162 TYR D CZ  1 
ATOM   6976 O OH  . TYR D 2 162 ? 98.129  -84.770  37.757  1.00 134.57 ? 162 TYR D OH  1 
ATOM   6977 N N   . SER D 2 163 ? 102.277 -84.508  30.225  1.00 148.39 ? 163 SER D N   1 
ATOM   6978 C CA  . SER D 2 163 ? 102.499 -84.674  28.779  1.00 148.62 ? 163 SER D CA  1 
ATOM   6979 C C   . SER D 2 163 ? 103.756 -85.485  28.447  1.00 147.71 ? 163 SER D C   1 
ATOM   6980 O O   . SER D 2 163 ? 103.804 -86.195  27.440  1.00 145.77 ? 163 SER D O   1 
ATOM   6981 C CB  . SER D 2 163 ? 102.520 -83.322  28.054  1.00 147.15 ? 163 SER D CB  1 
ATOM   6982 O OG  . SER D 2 163 ? 102.343 -83.495  26.656  1.00 144.57 ? 163 SER D OG  1 
ATOM   6983 N N   . GLU D 2 164 ? 104.773 -85.357  29.290  1.00 148.09 ? 164 GLU D N   1 
ATOM   6984 C CA  . GLU D 2 164 ? 105.942 -86.216  29.221  1.00 147.14 ? 164 GLU D CA  1 
ATOM   6985 C C   . GLU D 2 164 ? 105.481 -87.616  29.569  1.00 145.85 ? 164 GLU D C   1 
ATOM   6986 O O   . GLU D 2 164 ? 105.712 -88.573  28.830  1.00 145.45 ? 164 GLU D O   1 
ATOM   6987 C CB  . GLU D 2 164 ? 106.985 -85.751  30.234  1.00 146.38 ? 164 GLU D CB  1 
ATOM   6988 C CG  . GLU D 2 164 ? 106.383 -85.105  31.482  1.00 145.59 ? 164 GLU D CG  1 
ATOM   6989 C CD  . GLU D 2 164 ? 105.867 -83.697  31.223  1.00 145.90 ? 164 GLU D CD  1 
ATOM   6990 O OE1 . GLU D 2 164 ? 106.577 -82.912  30.561  1.00 146.08 ? 164 GLU D OE1 1 
ATOM   6991 O OE2 . GLU D 2 164 ? 104.749 -83.376  31.676  1.00 145.65 ? 164 GLU D OE2 1 
ATOM   6992 N N   . GLU D 2 165 ? 104.808 -87.711  30.708  1.00 145.62 ? 165 GLU D N   1 
ATOM   6993 C CA  . GLU D 2 165 ? 104.232 -88.957  31.172  1.00 145.41 ? 165 GLU D CA  1 
ATOM   6994 C C   . GLU D 2 165 ? 103.167 -89.439  30.192  1.00 145.54 ? 165 GLU D C   1 
ATOM   6995 O O   . GLU D 2 165 ? 102.746 -90.591  30.241  1.00 144.98 ? 165 GLU D O   1 
ATOM   6996 C CB  . GLU D 2 165 ? 103.634 -88.745  32.558  1.00 143.97 ? 165 GLU D CB  1 
ATOM   6997 C CG  . GLU D 2 165 ? 103.228 -90.003  33.268  1.00 144.31 ? 165 GLU D CG  1 
ATOM   6998 C CD  . GLU D 2 165 ? 101.759 -90.290  33.119  1.00 145.71 ? 165 GLU D CD  1 
ATOM   6999 O OE1 . GLU D 2 165 ? 101.126 -89.709  32.212  1.00 146.04 ? 165 GLU D OE1 1 
ATOM   7000 O OE2 . GLU D 2 165 ? 101.236 -91.090  33.920  1.00 144.77 ? 165 GLU D OE2 1 
ATOM   7001 N N   . ALA D 2 166 ? 102.750 -88.551  29.294  1.00 146.19 ? 166 ALA D N   1 
ATOM   7002 C CA  . ALA D 2 166 ? 101.748 -88.880  28.283  1.00 146.65 ? 166 ALA D CA  1 
ATOM   7003 C C   . ALA D 2 166 ? 102.290 -89.929  27.325  1.00 146.92 ? 166 ALA D C   1 
ATOM   7004 O O   . ALA D 2 166 ? 101.586 -90.394  26.429  1.00 145.90 ? 166 ALA D O   1 
ATOM   7005 C CB  . ALA D 2 166 ? 101.314 -87.638  27.522  1.00 145.04 ? 166 ALA D CB  1 
ATOM   7006 N N   . LYS D 2 167 ? 103.561 -90.267  27.498  1.00 146.46 ? 167 LYS D N   1 
ATOM   7007 C CA  . LYS D 2 167 ? 104.186 -91.305  26.695  1.00 147.27 ? 167 LYS D CA  1 
ATOM   7008 C C   . LYS D 2 167 ? 103.709 -92.700  27.090  1.00 148.84 ? 167 LYS D C   1 
ATOM   7009 O O   . LYS D 2 167 ? 103.873 -93.649  26.322  1.00 149.29 ? 167 LYS D O   1 
ATOM   7010 C CB  . LYS D 2 167 ? 105.708 -91.225  26.818  1.00 148.68 ? 167 LYS D CB  1 
ATOM   7011 C CG  . LYS D 2 167 ? 106.457 -92.249  25.975  1.00 151.23 ? 167 LYS D CG  1 
ATOM   7012 C CD  . LYS D 2 167 ? 106.398 -91.898  24.498  1.00 151.92 ? 167 LYS D CD  1 
ATOM   7013 C CE  . LYS D 2 167 ? 106.965 -93.011  23.625  1.00 151.23 ? 167 LYS D CE  1 
ATOM   7014 N NZ  . LYS D 2 167 ? 108.408 -93.240  23.890  1.00 150.37 ? 167 LYS D NZ  1 
ATOM   7015 N N   . LEU D 2 168 ? 103.110 -92.826  28.275  1.00 149.95 ? 168 LEU D N   1 
ATOM   7016 C CA  . LEU D 2 168 ? 102.752 -94.146  28.803  1.00 149.65 ? 168 LEU D CA  1 
ATOM   7017 C C   . LEU D 2 168 ? 102.034 -94.987  27.747  1.00 148.96 ? 168 LEU D C   1 
ATOM   7018 O O   . LEU D 2 168 ? 102.230 -96.201  27.674  1.00 147.56 ? 168 LEU D O   1 
ATOM   7019 C CB  . LEU D 2 168 ? 101.965 -94.061  30.116  1.00 147.02 ? 168 LEU D CB  1 
ATOM   7020 C CG  . LEU D 2 168 ? 100.511 -93.602  30.145  1.00 145.63 ? 168 LEU D CG  1 
ATOM   7021 C CD1 . LEU D 2 168 ? 99.899  -93.995  31.473  1.00 144.57 ? 168 LEU D CD1 1 
ATOM   7022 C CD2 . LEU D 2 168 ? 100.409 -92.108  29.927  1.00 145.33 ? 168 LEU D CD2 1 
ATOM   7023 N N   . ASN D 2 169 ? 101.187 -94.349  26.946  1.00 148.05 ? 169 ASN D N   1 
ATOM   7024 C CA  . ASN D 2 169 ? 101.051 -94.812  25.574  1.00 148.80 ? 169 ASN D CA  1 
ATOM   7025 C C   . ASN D 2 169 ? 101.379 -93.715  24.575  1.00 147.73 ? 169 ASN D C   1 
ATOM   7026 O O   . ASN D 2 169 ? 100.622 -92.762  24.383  1.00 145.11 ? 169 ASN D O   1 
ATOM   7027 C CB  . ASN D 2 169 ? 99.680  -95.412  25.266  1.00 147.28 ? 169 ASN D CB  1 
ATOM   7028 C CG  . ASN D 2 169 ? 99.636  -96.063  23.889  1.00 144.75 ? 169 ASN D CG  1 
ATOM   7029 O OD1 . ASN D 2 169 ? 100.593 -96.715  23.470  1.00 144.55 ? 169 ASN D OD1 1 
ATOM   7030 N ND2 . ASN D 2 169 ? 98.536  -95.874  23.176  1.00 141.02 ? 169 ASN D ND2 1 
ATOM   7031 N N   . ARG D 2 170 ? 102.544 -93.867  23.967  1.00 148.00 ? 170 ARG D N   1 
ATOM   7032 C CA  . ARG D 2 170 ? 102.860 -93.309  22.672  1.00 149.83 ? 170 ARG D CA  1 
ATOM   7033 C C   . ARG D 2 170 ? 103.498 -94.495  21.972  1.00 152.96 ? 170 ARG D C   1 
ATOM   7034 O O   . ARG D 2 170 ? 102.984 -95.006  20.975  1.00 154.83 ? 170 ARG D O   1 
ATOM   7035 C CB  . ARG D 2 170 ? 103.819 -92.128  22.782  1.00 149.07 ? 170 ARG D CB  1 
ATOM   7036 C CG  . ARG D 2 170 ? 103.175 -90.848  23.310  1.00 147.82 ? 170 ARG D CG  1 
ATOM   7037 C CD  . ARG D 2 170 ? 103.060 -89.797  22.213  1.00 147.24 ? 170 ARG D CD  1 
ATOM   7038 N NE  . ARG D 2 170 ? 101.695 -89.301  22.058  1.00 145.68 ? 170 ARG D NE  1 
ATOM   7039 C CZ  . ARG D 2 170 ? 101.278 -88.106  22.463  1.00 144.31 ? 170 ARG D CZ  1 
ATOM   7040 N NH1 . ARG D 2 170 ? 102.122 -87.268  23.051  1.00 142.70 ? 170 ARG D NH1 1 
ATOM   7041 N NH2 . ARG D 2 170 ? 100.015 -87.749  22.274  1.00 142.23 ? 170 ARG D NH2 1 
ATOM   7042 N N   . GLU D 2 171 ? 104.622 -94.938  22.528  1.00 152.78 ? 171 GLU D N   1 
ATOM   7043 C CA  . GLU D 2 171 ? 105.282 -96.159  22.082  1.00 154.31 ? 171 GLU D CA  1 
ATOM   7044 C C   . GLU D 2 171 ? 105.621 -97.091  23.243  1.00 152.52 ? 171 GLU D C   1 
ATOM   7045 O O   . GLU D 2 171 ? 106.248 -98.135  23.052  1.00 149.88 ? 171 GLU D O   1 
ATOM   7046 C CB  . GLU D 2 171 ? 106.545 -95.829  21.292  1.00 152.11 ? 171 GLU D CB  1 
ATOM   7047 C CG  . GLU D 2 171 ? 106.309 -95.655  19.809  1.00 150.24 ? 171 GLU D CG  1 
ATOM   7048 C CD  . GLU D 2 171 ? 107.592 -95.762  19.026  1.00 150.59 ? 171 GLU D CD  1 
ATOM   7049 O OE1 . GLU D 2 171 ? 108.666 -95.720  19.659  1.00 151.08 ? 171 GLU D OE1 1 
ATOM   7050 O OE2 . GLU D 2 171 ? 107.533 -95.897  17.787  1.00 151.63 ? 171 GLU D OE2 1 
HETATM 7051 C C1  . NAG E 3 .   ? 21.124  -56.679  2.185   1.00 65.70  ? 401 NAG A C1  1 
HETATM 7052 C C2  . NAG E 3 .   ? 21.865  -55.694  3.078   1.00 66.16  ? 401 NAG A C2  1 
HETATM 7053 C C3  . NAG E 3 .   ? 23.159  -56.326  3.566   1.00 68.03  ? 401 NAG A C3  1 
HETATM 7054 C C4  . NAG E 3 .   ? 22.797  -57.572  4.348   1.00 70.38  ? 401 NAG A C4  1 
HETATM 7055 C C5  . NAG E 3 .   ? 21.965  -58.497  3.452   1.00 75.04  ? 401 NAG A C5  1 
HETATM 7056 C C6  . NAG E 3 .   ? 21.457  -59.705  4.216   1.00 77.53  ? 401 NAG A C6  1 
HETATM 7057 C C7  . NAG E 3 .   ? 21.377  -53.395  2.594   1.00 61.98  ? 401 NAG A C7  1 
HETATM 7058 C C8  . NAG E 3 .   ? 21.899  -52.061  2.139   1.00 57.37  ? 401 NAG A C8  1 
HETATM 7059 N N2  . NAG E 3 .   ? 22.137  -54.462  2.370   1.00 64.82  ? 401 NAG A N2  1 
HETATM 7060 O O3  . NAG E 3 .   ? 23.902  -55.442  4.376   1.00 67.47  ? 401 NAG A O3  1 
HETATM 7061 O O4  . NAG E 3 .   ? 23.989  -58.183  4.787   1.00 71.89  ? 401 NAG A O4  1 
HETATM 7062 O O5  . NAG E 3 .   ? 20.819  -57.849  2.906   1.00 68.84  ? 401 NAG A O5  1 
HETATM 7063 O O6  . NAG E 3 .   ? 20.069  -59.518  4.364   1.00 78.09  ? 401 NAG A O6  1 
HETATM 7064 O O7  . NAG E 3 .   ? 20.282  -53.484  3.146   1.00 61.88  ? 401 NAG A O7  1 
HETATM 7065 C C1  . NAG F 3 .   ? 24.112  -58.372  6.251   1.00 79.40  ? 402 NAG A C1  1 
HETATM 7066 C C2  . NAG F 3 .   ? 25.337  -59.213  6.529   1.00 80.44  ? 402 NAG A C2  1 
HETATM 7067 C C3  . NAG F 3 .   ? 25.254  -59.640  7.994   1.00 84.30  ? 402 NAG A C3  1 
HETATM 7068 C C4  . NAG F 3 .   ? 25.084  -58.415  8.915   1.00 83.86  ? 402 NAG A C4  1 
HETATM 7069 C C5  . NAG F 3 .   ? 24.221  -57.279  8.314   1.00 81.09  ? 402 NAG A C5  1 
HETATM 7070 C C6  . NAG F 3 .   ? 24.570  -55.908  8.890   1.00 74.80  ? 402 NAG A C6  1 
HETATM 7071 C C7  . NAG F 3 .   ? 25.717  -60.131  4.304   1.00 82.80  ? 402 NAG A C7  1 
HETATM 7072 C C8  . NAG F 3 .   ? 25.183  -61.118  3.301   1.00 77.73  ? 402 NAG A C8  1 
HETATM 7073 N N2  . NAG F 3 .   ? 25.368  -60.315  5.584   1.00 82.75  ? 402 NAG A N2  1 
HETATM 7074 O O3  . NAG F 3 .   ? 26.403  -60.387  8.352   1.00 82.87  ? 402 NAG A O3  1 
HETATM 7075 O O4  . NAG F 3 .   ? 24.541  -58.838  10.157  1.00 78.42  ? 402 NAG A O4  1 
HETATM 7076 O O5  . NAG F 3 .   ? 24.345  -57.153  6.908   1.00 79.52  ? 402 NAG A O5  1 
HETATM 7077 O O6  . NAG F 3 .   ? 24.889  -55.033  7.821   1.00 69.21  ? 402 NAG A O6  1 
HETATM 7078 O O7  . NAG F 3 .   ? 26.446  -59.208  3.929   1.00 83.72  ? 402 NAG A O7  1 
HETATM 7079 C C1  . NAG G 3 .   ? -3.501  -69.218  -18.876 1.00 122.65 ? 403 NAG A C1  1 
HETATM 7080 C C2  . NAG G 3 .   ? -4.911  -68.599  -18.697 1.00 126.67 ? 403 NAG A C2  1 
HETATM 7081 C C3  . NAG G 3 .   ? -5.457  -67.766  -19.880 1.00 121.96 ? 403 NAG A C3  1 
HETATM 7082 C C4  . NAG G 3 .   ? -4.340  -67.318  -20.822 1.00 124.63 ? 403 NAG A C4  1 
HETATM 7083 C C5  . NAG G 3 .   ? -3.612  -68.588  -21.225 1.00 126.44 ? 403 NAG A C5  1 
HETATM 7084 C C6  . NAG G 3 .   ? -2.750  -68.467  -22.485 1.00 120.69 ? 403 NAG A C6  1 
HETATM 7085 C C7  . NAG G 3 .   ? -6.882  -69.581  -17.495 1.00 141.00 ? 403 NAG A C7  1 
HETATM 7086 C C8  . NAG G 3 .   ? -7.247  -68.273  -16.842 1.00 141.66 ? 403 NAG A C8  1 
HETATM 7087 N N2  . NAG G 3 .   ? -5.832  -69.676  -18.321 1.00 133.91 ? 403 NAG A N2  1 
HETATM 7088 O O3  . NAG G 3 .   ? -6.163  -66.638  -19.413 1.00 110.90 ? 403 NAG A O3  1 
HETATM 7089 O O4  . NAG G 3 .   ? -4.815  -66.605  -21.946 1.00 129.95 ? 403 NAG A O4  1 
HETATM 7090 O O5  . NAG G 3 .   ? -2.826  -68.899  -20.095 1.00 127.18 ? 403 NAG A O5  1 
HETATM 7091 O O6  . NAG G 3 .   ? -1.447  -68.072  -22.134 1.00 118.93 ? 403 NAG A O6  1 
HETATM 7092 O O7  . NAG G 3 .   ? -7.568  -70.573  -17.260 1.00 147.46 ? 403 NAG A O7  1 
HETATM 7093 C C1  . NAG H 3 .   ? -6.981  -78.080  -14.503 1.00 113.43 ? 404 NAG A C1  1 
HETATM 7094 C C2  . NAG H 3 .   ? -8.012  -78.954  -15.206 1.00 114.52 ? 404 NAG A C2  1 
HETATM 7095 C C3  . NAG H 3 .   ? -7.658  -79.098  -16.677 1.00 114.42 ? 404 NAG A C3  1 
HETATM 7096 C C4  . NAG H 3 .   ? -7.609  -77.700  -17.279 1.00 114.75 ? 404 NAG A C4  1 
HETATM 7097 C C5  . NAG H 3 .   ? -6.698  -76.764  -16.475 1.00 115.12 ? 404 NAG A C5  1 
HETATM 7098 C C6  . NAG H 3 .   ? -6.832  -75.321  -16.954 1.00 113.07 ? 404 NAG A C6  1 
HETATM 7099 C C7  . NAG H 3 .   ? -9.129  -80.476  -13.711 1.00 116.76 ? 404 NAG A C7  1 
HETATM 7100 C C8  . NAG H 3 .   ? -8.944  -81.598  -12.729 1.00 116.38 ? 404 NAG A C8  1 
HETATM 7101 N N2  . NAG H 3 .   ? -8.125  -80.243  -14.557 1.00 116.29 ? 404 NAG A N2  1 
HETATM 7102 O O3  . NAG H 3 .   ? -8.622  -79.891  -17.337 1.00 112.85 ? 404 NAG A O3  1 
HETATM 7103 O O4  . NAG H 3 .   ? -7.160  -77.790  -18.616 1.00 114.30 ? 404 NAG A O4  1 
HETATM 7104 O O5  . NAG H 3 .   ? -6.979  -76.795  -15.086 1.00 114.13 ? 404 NAG A O5  1 
HETATM 7105 O O6  . NAG H 3 .   ? -6.588  -75.254  -18.341 1.00 114.88 ? 404 NAG A O6  1 
HETATM 7106 O O7  . NAG H 3 .   ? -10.168 -79.815  -13.711 1.00 113.54 ? 404 NAG A O7  1 
HETATM 7107 C C1  . NAG I 3 .   ? 9.012   -60.792  28.366  1.00 69.43  ? 401 NAG C C1  1 
HETATM 7108 C C2  . NAG I 3 .   ? 8.033   -60.327  27.318  1.00 67.84  ? 401 NAG C C2  1 
HETATM 7109 C C3  . NAG I 3 .   ? 7.187   -61.528  26.964  1.00 70.88  ? 401 NAG C C3  1 
HETATM 7110 C C4  . NAG I 3 .   ? 8.119   -62.577  26.385  1.00 74.96  ? 401 NAG C C4  1 
HETATM 7111 C C5  . NAG I 3 .   ? 9.439   -62.732  27.146  1.00 74.00  ? 401 NAG C C5  1 
HETATM 7112 C C6  . NAG I 3 .   ? 10.508  -63.283  26.225  1.00 77.59  ? 401 NAG C C6  1 
HETATM 7113 C C7  . NAG I 3 .   ? 7.807   -58.018  27.807  1.00 65.77  ? 401 NAG C C7  1 
HETATM 7114 C C8  . NAG I 3 .   ? 7.125   -56.973  28.637  1.00 62.26  ? 401 NAG C C8  1 
HETATM 7115 N N2  . NAG I 3 .   ? 7.274   -59.233  27.859  1.00 67.48  ? 401 NAG C N2  1 
HETATM 7116 O O3  . NAG I 3 .   ? 6.216   -61.202  25.999  1.00 73.81  ? 401 NAG C O3  1 
HETATM 7117 O O4  . NAG I 3 .   ? 7.437   -63.801  26.416  1.00 79.32  ? 401 NAG C O4  1 
HETATM 7118 O O5  . NAG I 3 .   ? 9.978   -61.530  27.671  1.00 67.71  ? 401 NAG C O5  1 
HETATM 7119 O O6  . NAG I 3 .   ? 11.181  -64.247  26.994  1.00 74.96  ? 401 NAG C O6  1 
HETATM 7120 O O7  . NAG I 3 .   ? 8.799   -57.749  27.120  1.00 64.74  ? 401 NAG C O7  1 
HETATM 7121 C C1  . NAG J 3 .   ? 7.398   -64.436  24.922  1.00 92.88  ? 402 NAG C C1  1 
HETATM 7122 C C2  . NAG J 3 .   ? 7.330   -65.955  25.021  1.00 95.00  ? 402 NAG C C2  1 
HETATM 7123 C C3  . NAG J 3 .   ? 7.450   -66.582  23.633  1.00 98.95  ? 402 NAG C C3  1 
HETATM 7124 C C4  . NAG J 3 .   ? 6.468   -65.931  22.658  1.00 98.36  ? 402 NAG C C4  1 
HETATM 7125 C C5  . NAG J 3 .   ? 6.499   -64.399  22.743  1.00 98.95  ? 402 NAG C C5  1 
HETATM 7126 C C6  . NAG J 3 .   ? 5.398   -63.760  21.889  1.00 99.71  ? 402 NAG C C6  1 
HETATM 7127 C C7  . NAG J 3 .   ? 8.222   -66.610  27.204  1.00 88.50  ? 402 NAG C C7  1 
HETATM 7128 C C8  . NAG J 3 .   ? 9.485   -66.776  27.998  1.00 85.02  ? 402 NAG C C8  1 
HETATM 7129 N N2  . NAG J 3 .   ? 8.384   -66.442  25.894  1.00 92.56  ? 402 NAG C N2  1 
HETATM 7130 O O3  . NAG J 3 .   ? 7.186   -67.968  23.726  1.00 103.90 ? 402 NAG C O3  1 
HETATM 7131 O O4  . NAG J 3 .   ? 6.754   -66.353  21.339  1.00 96.87  ? 402 NAG C O4  1 
HETATM 7132 O O5  . NAG J 3 .   ? 6.366   -63.961  24.085  1.00 94.90  ? 402 NAG C O5  1 
HETATM 7133 O O6  . NAG J 3 .   ? 4.716   -62.752  22.614  1.00 86.48  ? 402 NAG C O6  1 
HETATM 7134 O O7  . NAG J 3 .   ? 7.118   -66.618  27.756  1.00 87.92  ? 402 NAG C O7  1 
HETATM 7135 C C1  . NAG K 3 .   ? 35.685  -61.404  49.854  1.00 134.57 ? 403 NAG C C1  1 
HETATM 7136 C C2  . NAG K 3 .   ? 36.229  -59.978  50.093  1.00 143.51 ? 403 NAG C C2  1 
HETATM 7137 C C3  . NAG K 3 .   ? 36.079  -59.484  51.533  1.00 143.11 ? 403 NAG C C3  1 
HETATM 7138 C C4  . NAG K 3 .   ? 34.747  -59.925  52.124  1.00 144.87 ? 403 NAG C C4  1 
HETATM 7139 C C5  . NAG K 3 .   ? 34.644  -61.459  52.118  1.00 139.79 ? 403 NAG C C5  1 
HETATM 7140 C C6  . NAG K 3 .   ? 33.196  -61.961  52.157  1.00 134.58 ? 403 NAG C C6  1 
HETATM 7141 C C7  . NAG K 3 .   ? 38.166  -58.956  48.945  1.00 141.65 ? 403 NAG C C7  1 
HETATM 7142 C C8  . NAG K 3 .   ? 39.644  -59.040  48.696  1.00 140.15 ? 403 NAG C C8  1 
HETATM 7143 N N2  . NAG K 3 .   ? 37.644  -59.896  49.737  1.00 145.73 ? 403 NAG C N2  1 
HETATM 7144 O O3  . NAG K 3 .   ? 36.219  -58.075  51.587  1.00 129.29 ? 403 NAG C O3  1 
HETATM 7145 O O4  . NAG K 3 .   ? 34.659  -59.436  53.448  1.00 147.51 ? 403 NAG C O4  1 
HETATM 7146 O O5  . NAG K 3 .   ? 34.670  -61.812  50.653  1.00 136.38 ? 403 NAG C O5  1 
HETATM 7147 O O6  . NAG K 3 .   ? 33.205  -63.337  52.475  1.00 124.34 ? 403 NAG C O6  1 
HETATM 7148 O O7  . NAG K 3 .   ? 37.511  -58.054  48.425  1.00 141.95 ? 403 NAG C O7  1 
HETATM 7149 C C1  . NAG L 3 .   ? 43.373  -67.603  44.008  1.00 135.99 ? 404 NAG C C1  1 
HETATM 7150 C C2  . NAG L 3 .   ? 44.624  -68.483  44.105  1.00 139.11 ? 404 NAG C C2  1 
HETATM 7151 C C3  . NAG L 3 .   ? 44.798  -69.068  45.504  1.00 136.53 ? 404 NAG C C3  1 
HETATM 7152 C C4  . NAG L 3 .   ? 44.689  -67.963  46.544  1.00 133.92 ? 404 NAG C C4  1 
HETATM 7153 C C5  . NAG L 3 .   ? 43.368  -67.215  46.363  1.00 134.30 ? 404 NAG C C5  1 
HETATM 7154 C C6  . NAG L 3 .   ? 43.197  -66.134  47.432  1.00 132.15 ? 404 NAG C C6  1 
HETATM 7155 C C7  . NAG L 3 .   ? 43.484  -70.250  42.839  1.00 137.34 ? 404 NAG C C7  1 
HETATM 7156 C C8  . NAG L 3 .   ? 43.155  -71.422  43.720  1.00 131.15 ? 404 NAG C C8  1 
HETATM 7157 N N2  . NAG L 3 .   ? 44.591  -69.565  43.132  1.00 139.93 ? 404 NAG C N2  1 
HETATM 7158 O O3  . NAG L 3 .   ? 46.036  -69.743  45.613  1.00 135.28 ? 404 NAG C O3  1 
HETATM 7159 O O4  . NAG L 3 .   ? 44.772  -68.520  47.836  1.00 132.28 ? 404 NAG C O4  1 
HETATM 7160 O O5  . NAG L 3 .   ? 43.298  -66.654  45.061  1.00 133.05 ? 404 NAG C O5  1 
HETATM 7161 O O6  . NAG L 3 .   ? 41.828  -65.891  47.688  1.00 129.15 ? 404 NAG C O6  1 
HETATM 7162 O O7  . NAG L 3 .   ? 42.751  -69.968  41.891  1.00 136.66 ? 404 NAG C O7  1 
HETATM 7163 O O   . HOH M 4 .   ? -0.991  -42.460  1.979   1.00 42.65  ? 501 HOH A O   1 
HETATM 7164 O O   . HOH M 4 .   ? 14.980  -25.353  -5.142  1.00 39.25  ? 502 HOH A O   1 
HETATM 7165 O O   . HOH M 4 .   ? 22.477  -21.408  5.937   1.00 57.73  ? 503 HOH A O   1 
HETATM 7166 O O   . HOH M 4 .   ? 23.077  -39.740  11.768  1.00 47.58  ? 504 HOH A O   1 
HETATM 7167 O O   . HOH M 4 .   ? 3.755   -49.022  8.216   1.00 41.24  ? 505 HOH A O   1 
HETATM 7168 O O   . HOH M 4 .   ? 7.413   -35.295  12.370  1.00 39.59  ? 506 HOH A O   1 
HETATM 7169 O O   . HOH M 4 .   ? 18.359  -32.277  2.719   1.00 39.85  ? 507 HOH A O   1 
HETATM 7170 O O   . HOH M 4 .   ? 17.898  -25.330  -5.084  1.00 53.60  ? 508 HOH A O   1 
HETATM 7171 O O   . HOH M 4 .   ? -11.540 -83.968  10.894  1.00 100.64 ? 509 HOH A O   1 
HETATM 7172 O O   . HOH M 4 .   ? 0.387   -81.607  -3.111  1.00 76.67  ? 510 HOH A O   1 
HETATM 7173 O O   . HOH M 4 .   ? -1.841  -42.166  4.804   1.00 42.05  ? 511 HOH A O   1 
HETATM 7174 O O   . HOH M 4 .   ? 10.748  -49.873  15.275  1.00 42.36  ? 512 HOH A O   1 
HETATM 7175 O O   . HOH M 4 .   ? 26.689  -39.244  5.329   1.00 46.11  ? 513 HOH A O   1 
HETATM 7176 O O   . HOH M 4 .   ? 23.532  -53.969  13.087  1.00 42.56  ? 514 HOH A O   1 
HETATM 7177 O O   . HOH M 4 .   ? 26.871  -52.382  8.364   1.00 48.34  ? 515 HOH A O   1 
HETATM 7178 O O   . HOH M 4 .   ? 32.362  -49.727  3.640   1.00 46.98  ? 516 HOH A O   1 
HETATM 7179 O O   . HOH M 4 .   ? 0.633   -72.790  -19.255 1.00 81.06  ? 517 HOH A O   1 
HETATM 7180 O O   . HOH M 4 .   ? 11.824  -53.321  6.157   1.00 40.83  ? 518 HOH A O   1 
HETATM 7181 O O   . HOH M 4 .   ? 10.490  -51.175  7.808   1.00 38.38  ? 519 HOH A O   1 
HETATM 7182 O O   . HOH M 4 .   ? 15.377  -50.379  9.865   1.00 46.11  ? 520 HOH A O   1 
HETATM 7183 O O   . HOH M 4 .   ? 26.817  -51.716  -9.040  1.00 60.13  ? 521 HOH A O   1 
HETATM 7184 O O   . HOH M 4 .   ? -2.018  -41.113  -0.389  1.00 49.16  ? 522 HOH A O   1 
HETATM 7185 O O   . HOH M 4 .   ? 9.351   -49.257  -14.804 1.00 65.01  ? 523 HOH A O   1 
HETATM 7186 O O   . HOH M 4 .   ? 2.034   -51.162  -19.170 1.00 61.89  ? 524 HOH A O   1 
HETATM 7187 O O   . HOH M 4 .   ? 7.637   -70.976  2.564   1.00 67.65  ? 525 HOH A O   1 
HETATM 7188 O O   . HOH M 4 .   ? -5.968  -45.898  5.934   1.00 54.02  ? 526 HOH A O   1 
HETATM 7189 O O   . HOH M 4 .   ? -5.838  -43.529  8.874   1.00 46.06  ? 527 HOH A O   1 
HETATM 7190 O O   . HOH M 4 .   ? -4.753  -42.764  -1.236  1.00 43.31  ? 528 HOH A O   1 
HETATM 7191 O O   . HOH M 4 .   ? 25.763  -32.545  19.710  1.00 46.11  ? 529 HOH A O   1 
HETATM 7192 O O   . HOH M 4 .   ? 13.069  -67.104  -10.517 1.00 62.96  ? 530 HOH A O   1 
HETATM 7193 O O   . HOH N 4 .   ? -45.683 -105.718 -10.065 1.00 103.19 ? 201 HOH B O   1 
HETATM 7194 O O   . HOH N 4 .   ? -30.282 -119.292 -13.875 1.00 112.79 ? 202 HOH B O   1 
HETATM 7195 O O   . HOH N 4 .   ? -29.199 -114.670 10.421  1.00 104.05 ? 203 HOH B O   1 
HETATM 7196 O O   . HOH O 4 .   ? 1.999   -59.062  40.064  1.00 68.61  ? 501 HOH C O   1 
HETATM 7197 O O   . HOH O 4 .   ? 14.686  -48.943  15.281  1.00 44.94  ? 502 HOH C O   1 
HETATM 7198 O O   . HOH O 4 .   ? -0.302  -37.583  28.749  1.00 40.79  ? 503 HOH C O   1 
HETATM 7199 O O   . HOH O 4 .   ? 65.536  -81.565  35.479  1.00 115.85 ? 504 HOH C O   1 
HETATM 7200 O O   . HOH O 4 .   ? 15.183  -49.695  22.643  1.00 40.82  ? 505 HOH C O   1 
HETATM 7201 O O   . HOH O 4 .   ? 10.962  -51.196  20.809  1.00 43.22  ? 506 HOH C O   1 
HETATM 7202 O O   . HOH O 4 .   ? 16.480  -51.643  23.691  1.00 40.57  ? 507 HOH C O   1 
HETATM 7203 O O   . HOH O 4 .   ? 20.223  -45.210  22.922  1.00 39.47  ? 508 HOH C O   1 
HETATM 7204 O O   . HOH O 4 .   ? 26.912  -40.084  42.054  1.00 69.61  ? 509 HOH C O   1 
HETATM 7205 O O   . HOH O 4 .   ? 10.597  -40.526  15.778  1.00 36.30  ? 510 HOH C O   1 
HETATM 7206 O O   . HOH O 4 .   ? 22.011  -35.385  31.911  1.00 54.40  ? 511 HOH C O   1 
HETATM 7207 O O   . HOH O 4 .   ? 20.924  -37.176  29.287  1.00 45.78  ? 512 HOH C O   1 
HETATM 7208 O O   . HOH O 4 .   ? 0.994   -58.678  22.043  1.00 53.83  ? 513 HOH C O   1 
HETATM 7209 O O   . HOH O 4 .   ? 9.973   -56.518  25.241  1.00 54.75  ? 514 HOH C O   1 
HETATM 7210 O O   . HOH O 4 .   ? -1.214  -29.807  36.849  1.00 40.87  ? 515 HOH C O   1 
HETATM 7211 O O   . HOH O 4 .   ? -2.897  -31.195  36.532  1.00 49.17  ? 516 HOH C O   1 
HETATM 7212 O O   . HOH O 4 .   ? 51.805  -80.033  20.720  1.00 90.28  ? 517 HOH C O   1 
HETATM 7213 O O   . HOH O 4 .   ? 53.213  -81.959  18.614  1.00 101.59 ? 518 HOH C O   1 
HETATM 7214 O O   . HOH O 4 .   ? 50.864  -79.557  16.798  1.00 98.15  ? 519 HOH C O   1 
HETATM 7215 O O   . HOH O 4 .   ? -4.488  -46.985  26.308  1.00 38.18  ? 520 HOH C O   1 
HETATM 7216 O O   . HOH O 4 .   ? -1.314  -46.609  18.910  1.00 46.27  ? 521 HOH C O   1 
HETATM 7217 O O   . HOH O 4 .   ? -10.331 -33.507  36.861  1.00 58.64  ? 522 HOH C O   1 
HETATM 7218 O O   . HOH O 4 .   ? 23.934  -34.335  38.862  1.00 62.00  ? 523 HOH C O   1 
HETATM 7219 O O   . HOH O 4 .   ? 18.625  -54.111  26.372  1.00 51.92  ? 524 HOH C O   1 
HETATM 7220 O O   . HOH O 4 .   ? -1.510  -55.070  36.969  1.00 68.22  ? 525 HOH C O   1 
HETATM 7221 O O   . HOH P 4 .   ? 44.997  -59.836  18.518  1.00 115.97 ? 201 HOH D O   1 
HETATM 7222 O O   . HOH P 4 .   ? 81.604  -81.333  31.207  1.00 105.60 ? 202 HOH D O   1 
HETATM 7223 O O   . HOH P 4 .   ? 75.813  -79.184  22.351  1.00 106.79 ? 203 HOH D O   1 
HETATM 7224 O O   . HOH P 4 .   ? 97.537  -87.023  38.494  1.00 131.54 ? 204 HOH D O   1 
HETATM 7225 O O   . HOH P 4 .   ? 80.891  -79.989  36.683  1.00 109.51 ? 205 HOH D O   1 
# 
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   -8  ?   ?   ?   A . n 
A 1 2   ASP 2   -7  ?   ?   ?   A . n 
A 1 3   PRO 3   -6  ?   ?   ?   A . n 
A 1 4   GLY 4   -5  ?   ?   ?   A . n 
A 1 5   TYR 5   -4  ?   ?   ?   A . n 
A 1 6   LEU 6   -3  ?   ?   ?   A . n 
A 1 7   LEU 7   -2  ?   ?   ?   A . n 
A 1 8   GLU 8   -1  ?   ?   ?   A . n 
A 1 9   PHE 9   0   ?   ?   ?   A . n 
A 1 10  ASP 10  1   1   ASP ASP A . n 
A 1 11  THR 11  2   2   THR THR A . n 
A 1 12  LEU 12  3   3   LEU LEU A . n 
A 1 13  CYS 13  4   4   CYS CYS A . n 
A 1 14  ILE 14  5   5   ILE ILE A . n 
A 1 15  GLY 15  6   6   GLY GLY A . n 
A 1 16  TYR 16  7   7   TYR TYR A . n 
A 1 17  HIS 17  8   8   HIS HIS A . n 
A 1 18  ALA 18  9   9   ALA ALA A . n 
A 1 19  ASN 19  10  10  ASN ASN A . n 
A 1 20  ASN 20  11  11  ASN ASN A . n 
A 1 21  SER 21  12  12  SER SER A . n 
A 1 22  THR 22  13  13  THR THR A . n 
A 1 23  ASP 23  14  14  ASP ASP A . n 
A 1 24  THR 24  15  15  THR THR A . n 
A 1 25  VAL 25  16  16  VAL VAL A . n 
A 1 26  ASP 26  17  17  ASP ASP A . n 
A 1 27  THR 27  18  18  THR THR A . n 
A 1 28  VAL 28  19  19  VAL VAL A . n 
A 1 29  LEU 29  20  20  LEU LEU A . n 
A 1 30  GLU 30  21  21  GLU GLU A . n 
A 1 31  LYS 31  22  22  LYS LYS A . n 
A 1 32  ASN 32  23  23  ASN ASN A . n 
A 1 33  VAL 33  24  24  VAL VAL A . n 
A 1 34  THR 34  25  25  THR THR A . n 
A 1 35  VAL 35  26  26  VAL VAL A . n 
A 1 36  THR 36  27  27  THR THR A . n 
A 1 37  HIS 37  28  28  HIS HIS A . n 
A 1 38  SER 38  29  29  SER SER A . n 
A 1 39  VAL 39  30  30  VAL VAL A . n 
A 1 40  ASN 40  31  31  ASN ASN A . n 
A 1 41  LEU 41  32  32  LEU LEU A . n 
A 1 42  LEU 42  33  33  LEU LEU A . n 
A 1 43  GLU 43  34  34  GLU GLU A . n 
A 1 44  ASP 44  35  35  ASP ASP A . n 
A 1 45  LYS 45  36  36  LYS LYS A . n 
A 1 46  HIS 46  37  37  HIS HIS A . n 
A 1 47  ASN 47  38  38  ASN ASN A . n 
A 1 48  GLY 48  39  39  GLY GLY A . n 
A 1 49  LYS 49  40  40  LYS LYS A . n 
A 1 50  LEU 50  41  41  LEU LEU A . n 
A 1 51  CYS 51  42  42  CYS CYS A . n 
A 1 52  LYS 52  43  43  LYS LYS A . n 
A 1 53  LEU 53  44  44  LEU LEU A . n 
A 1 54  ARG 54  45  45  ARG ARG A . n 
A 1 55  GLY 55  46  46  GLY GLY A . n 
A 1 56  VAL 56  47  47  VAL VAL A . n 
A 1 57  ALA 57  48  48  ALA ALA A . n 
A 1 58  PRO 58  49  49  PRO PRO A . n 
A 1 59  LEU 59  50  50  LEU LEU A . n 
A 1 60  HIS 60  51  51  HIS HIS A . n 
A 1 61  LEU 61  52  52  LEU LEU A . n 
A 1 62  GLY 62  53  53  GLY GLY A . n 
A 1 63  LYS 63  54  54  LYS LYS A . n 
A 1 64  CYS 64  55  55  CYS CYS A . n 
A 1 65  ASN 65  56  56  ASN ASN A . n 
A 1 66  ILE 66  57  57  ILE ILE A . n 
A 1 67  ALA 67  58  58  ALA ALA A . n 
A 1 68  GLY 68  59  59  GLY GLY A . n 
A 1 69  TRP 69  60  60  TRP TRP A . n 
A 1 70  ILE 70  61  61  ILE ILE A . n 
A 1 71  LEU 71  62  62  LEU LEU A . n 
A 1 72  GLY 72  63  63  GLY GLY A . n 
A 1 73  ASN 73  64  64  ASN ASN A . n 
A 1 74  PRO 74  65  65  PRO PRO A . n 
A 1 75  GLU 75  66  66  GLU GLU A . n 
A 1 76  CYS 76  67  67  CYS CYS A . n 
A 1 77  GLU 77  68  68  GLU GLU A . n 
A 1 78  SER 78  69  69  SER SER A . n 
A 1 79  LEU 79  70  70  LEU LEU A . n 
A 1 80  SER 80  71  71  SER SER A . n 
A 1 81  THR 81  72  72  THR THR A . n 
A 1 82  ALA 82  73  73  ALA ALA A . n 
A 1 83  SER 83  74  74  SER SER A . n 
A 1 84  SER 84  75  75  SER SER A . n 
A 1 85  TRP 85  76  76  TRP TRP A . n 
A 1 86  SER 86  77  77  SER SER A . n 
A 1 87  TYR 87  78  78  TYR TYR A . n 
A 1 88  ILE 88  79  79  ILE ILE A . n 
A 1 89  VAL 89  80  80  VAL VAL A . n 
A 1 90  GLU 90  81  81  GLU GLU A . n 
A 1 91  THR 91  82  82  THR THR A . n 
A 1 92  SER 92  83  83  SER SER A . n 
A 1 93  SER 93  84  84  SER SER A . n 
A 1 94  SER 94  85  85  SER SER A . n 
A 1 95  ASP 95  86  86  ASP ASP A . n 
A 1 96  ASN 96  87  87  ASN ASN A . n 
A 1 97  GLY 97  88  88  GLY GLY A . n 
A 1 98  THR 98  89  89  THR THR A . n 
A 1 99  CYS 99  90  90  CYS CYS A . n 
A 1 100 TYR 100 91  91  TYR TYR A . n 
A 1 101 PRO 101 92  92  PRO PRO A . n 
A 1 102 GLY 102 93  93  GLY GLY A . n 
A 1 103 ASP 103 94  94  ASP ASP A . n 
A 1 104 PHE 104 95  95  PHE PHE A . n 
A 1 105 ILE 105 96  96  ILE ILE A . n 
A 1 106 ASP 106 97  97  ASP ASP A . n 
A 1 107 TYR 107 98  98  TYR TYR A . n 
A 1 108 GLU 108 99  99  GLU GLU A . n 
A 1 109 GLU 109 100 100 GLU GLU A . n 
A 1 110 LEU 110 101 101 LEU LEU A . n 
A 1 111 ARG 111 102 102 ARG ARG A . n 
A 1 112 GLU 112 103 103 GLU GLU A . n 
A 1 113 GLN 113 104 104 GLN GLN A . n 
A 1 114 LEU 114 105 105 LEU LEU A . n 
A 1 115 SER 115 106 106 SER SER A . n 
A 1 116 SER 116 107 107 SER SER A . n 
A 1 117 VAL 117 108 108 VAL VAL A . n 
A 1 118 SER 118 109 109 SER SER A . n 
A 1 119 SER 119 110 110 SER SER A . n 
A 1 120 PHE 120 111 111 PHE PHE A . n 
A 1 121 GLU 121 112 112 GLU GLU A . n 
A 1 122 ARG 122 113 113 ARG ARG A . n 
A 1 123 PHE 123 114 114 PHE PHE A . n 
A 1 124 GLU 124 115 115 GLU GLU A . n 
A 1 125 ILE 125 116 116 ILE ILE A . n 
A 1 126 PHE 126 117 117 PHE PHE A . n 
A 1 127 PRO 127 118 118 PRO PRO A . n 
A 1 128 LYS 128 119 119 LYS LYS A . n 
A 1 129 THR 129 120 120 THR THR A . n 
A 1 130 SER 130 121 121 SER SER A . n 
A 1 131 SER 131 122 122 SER SER A . n 
A 1 132 TRP 132 123 123 TRP TRP A . n 
A 1 133 PRO 133 124 124 PRO PRO A . n 
A 1 134 ASN 134 125 125 ASN ASN A . n 
A 1 135 HIS 135 126 126 HIS HIS A . n 
A 1 136 ASP 136 127 127 ASP ASP A . n 
A 1 137 SER 137 128 128 SER SER A . n 
A 1 138 ASN 138 129 129 ASN ASN A . n 
A 1 139 LYS 139 130 130 LYS LYS A . n 
A 1 140 GLY 140 131 131 GLY GLY A . n 
A 1 141 VAL 141 132 132 VAL VAL A . n 
A 1 142 THR 142 133 133 THR THR A . n 
A 1 143 ALA 143 134 134 ALA ALA A . n 
A 1 144 ALA 144 135 135 ALA ALA A . n 
A 1 145 CYS 145 136 136 CYS CYS A . n 
A 1 146 PRO 146 137 137 PRO PRO A . n 
A 1 147 HIS 147 138 138 HIS HIS A . n 
A 1 148 ALA 148 139 139 ALA ALA A . n 
A 1 149 GLY 149 140 140 GLY GLY A . n 
A 1 150 ALA 150 141 141 ALA ALA A . n 
A 1 151 LYS 151 142 142 LYS LYS A . n 
A 1 152 SER 152 143 143 SER SER A . n 
A 1 153 PHE 153 144 144 PHE PHE A . n 
A 1 154 TYR 154 145 145 TYR TYR A . n 
A 1 155 LYS 155 146 146 LYS LYS A . n 
A 1 156 ASN 156 147 147 ASN ASN A . n 
A 1 157 LEU 157 148 148 LEU LEU A . n 
A 1 158 ILE 158 149 149 ILE ILE A . n 
A 1 159 TRP 159 150 150 TRP TRP A . n 
A 1 160 LEU 160 151 151 LEU LEU A . n 
A 1 161 VAL 161 152 152 VAL VAL A . n 
A 1 162 LYS 162 153 153 LYS LYS A . n 
A 1 163 LYS 163 154 154 LYS LYS A . n 
A 1 164 GLY 164 155 155 GLY GLY A . n 
A 1 165 ASN 165 156 156 ASN ASN A . n 
A 1 166 SER 166 157 157 SER SER A . n 
A 1 167 TYR 167 158 158 TYR TYR A . n 
A 1 168 PRO 168 159 159 PRO PRO A . n 
A 1 169 LYS 169 160 160 LYS LYS A . n 
A 1 170 LEU 170 161 161 LEU LEU A . n 
A 1 171 SER 171 162 162 SER SER A . n 
A 1 172 LYS 172 163 163 LYS LYS A . n 
A 1 173 SER 173 164 164 SER SER A . n 
A 1 174 TYR 174 165 165 TYR TYR A . n 
A 1 175 ILE 175 166 166 ILE ILE A . n 
A 1 176 ASN 176 167 167 ASN ASN A . n 
A 1 177 ASP 177 168 168 ASP ASP A . n 
A 1 178 LYS 178 169 169 LYS LYS A . n 
A 1 179 GLY 179 170 170 GLY GLY A . n 
A 1 180 LYS 180 171 171 LYS LYS A . n 
A 1 181 GLU 181 172 172 GLU GLU A . n 
A 1 182 VAL 182 173 173 VAL VAL A . n 
A 1 183 LEU 183 174 174 LEU LEU A . n 
A 1 184 VAL 184 175 175 VAL VAL A . n 
A 1 185 LEU 185 176 176 LEU LEU A . n 
A 1 186 TRP 186 177 177 TRP TRP A . n 
A 1 187 GLY 187 178 178 GLY GLY A . n 
A 1 188 ILE 188 179 179 ILE ILE A . n 
A 1 189 HIS 189 180 180 HIS HIS A . n 
A 1 190 HIS 190 181 181 HIS HIS A . n 
A 1 191 PRO 191 182 182 PRO PRO A . n 
A 1 192 SER 192 183 183 SER SER A . n 
A 1 193 THR 193 184 184 THR THR A . n 
A 1 194 SER 194 185 185 SER SER A . n 
A 1 195 ALA 195 186 186 ALA ALA A . n 
A 1 196 ASP 196 187 187 ASP ASP A . n 
A 1 197 GLN 197 188 188 GLN GLN A . n 
A 1 198 GLN 198 189 189 GLN GLN A . n 
A 1 199 SER 199 190 190 SER SER A . n 
A 1 200 LEU 200 191 191 LEU LEU A . n 
A 1 201 TYR 201 192 192 TYR TYR A . n 
A 1 202 GLN 202 193 193 GLN GLN A . n 
A 1 203 ASN 203 194 194 ASN ASN A . n 
A 1 204 ALA 204 195 195 ALA ALA A . n 
A 1 205 ASP 205 196 196 ASP ASP A . n 
A 1 206 ALA 206 197 197 ALA ALA A . n 
A 1 207 TYR 207 198 198 TYR TYR A . n 
A 1 208 VAL 208 199 199 VAL VAL A . n 
A 1 209 PHE 209 200 200 PHE PHE A . n 
A 1 210 VAL 210 201 201 VAL VAL A . n 
A 1 211 GLY 211 202 202 GLY GLY A . n 
A 1 212 SER 212 203 203 SER SER A . n 
A 1 213 SER 213 204 204 SER SER A . n 
A 1 214 ARG 214 205 205 ARG ARG A . n 
A 1 215 TYR 215 206 206 TYR TYR A . n 
A 1 216 SER 216 207 207 SER SER A . n 
A 1 217 LYS 217 208 208 LYS LYS A . n 
A 1 218 LYS 218 209 209 LYS LYS A . n 
A 1 219 PHE 219 210 210 PHE PHE A . n 
A 1 220 LYS 220 211 211 LYS LYS A . n 
A 1 221 PRO 221 212 212 PRO PRO A . n 
A 1 222 GLU 222 213 213 GLU GLU A . n 
A 1 223 ILE 223 214 214 ILE ILE A . n 
A 1 224 ALA 224 215 215 ALA ALA A . n 
A 1 225 ILE 225 216 216 ILE ILE A . n 
A 1 226 ARG 226 217 217 ARG ARG A . n 
A 1 227 PRO 227 218 218 PRO PRO A . n 
A 1 228 LYS 228 219 219 LYS LYS A . n 
A 1 229 VAL 229 220 220 VAL VAL A . n 
A 1 230 ARG 230 221 221 ARG ARG A . n 
A 1 231 ASP 231 222 222 ASP ASP A . n 
A 1 232 GLN 232 223 223 GLN GLN A . n 
A 1 233 GLU 233 224 224 GLU GLU A . n 
A 1 234 GLY 234 225 225 GLY GLY A . n 
A 1 235 ARG 235 226 226 ARG ARG A . n 
A 1 236 MET 236 227 227 MET MET A . n 
A 1 237 ASN 237 228 228 ASN ASN A . n 
A 1 238 TYR 238 229 229 TYR TYR A . n 
A 1 239 TYR 239 230 230 TYR TYR A . n 
A 1 240 TRP 240 231 231 TRP TRP A . n 
A 1 241 THR 241 232 232 THR THR A . n 
A 1 242 LEU 242 233 233 LEU LEU A . n 
A 1 243 VAL 243 234 234 VAL VAL A . n 
A 1 244 GLU 244 235 235 GLU GLU A . n 
A 1 245 PRO 245 236 236 PRO PRO A . n 
A 1 246 GLY 246 237 237 GLY GLY A . n 
A 1 247 ASP 247 238 238 ASP ASP A . n 
A 1 248 LYS 248 239 239 LYS LYS A . n 
A 1 249 ILE 249 240 240 ILE ILE A . n 
A 1 250 THR 250 241 241 THR THR A . n 
A 1 251 PHE 251 242 242 PHE PHE A . n 
A 1 252 GLU 252 243 243 GLU GLU A . n 
A 1 253 ALA 253 244 244 ALA ALA A . n 
A 1 254 THR 254 245 245 THR THR A . n 
A 1 255 GLY 255 246 246 GLY GLY A . n 
A 1 256 ASN 256 247 247 ASN ASN A . n 
A 1 257 LEU 257 248 248 LEU LEU A . n 
A 1 258 VAL 258 249 249 VAL VAL A . n 
A 1 259 VAL 259 250 250 VAL VAL A . n 
A 1 260 PRO 260 251 251 PRO PRO A . n 
A 1 261 ARG 261 252 252 ARG ARG A . n 
A 1 262 TYR 262 253 253 TYR TYR A . n 
A 1 263 ALA 263 254 254 ALA ALA A . n 
A 1 264 PHE 264 255 255 PHE PHE A . n 
A 1 265 ALA 265 256 256 ALA ALA A . n 
A 1 266 MET 266 257 257 MET MET A . n 
A 1 267 GLU 267 258 258 GLU GLU A . n 
A 1 268 ARG 268 259 259 ARG ARG A . n 
A 1 269 ASN 269 260 260 ASN ASN A . n 
A 1 270 ALA 270 261 261 ALA ALA A . n 
A 1 271 GLY 271 262 262 GLY GLY A . n 
A 1 272 SER 272 263 263 SER SER A . n 
A 1 273 GLY 273 264 264 GLY GLY A . n 
A 1 274 ILE 274 265 265 ILE ILE A . n 
A 1 275 ILE 275 266 266 ILE ILE A . n 
A 1 276 ILE 276 267 267 ILE ILE A . n 
A 1 277 SER 277 268 268 SER SER A . n 
A 1 278 ASP 278 269 269 ASP ASP A . n 
A 1 279 THR 279 270 270 THR THR A . n 
A 1 280 PRO 280 271 271 PRO PRO A . n 
A 1 281 VAL 281 272 272 VAL VAL A . n 
A 1 282 HIS 282 273 273 HIS HIS A . n 
A 1 283 ASP 283 274 274 ASP ASP A . n 
A 1 284 CYS 284 275 275 CYS CYS A . n 
A 1 285 ASN 285 276 276 ASN ASN A . n 
A 1 286 THR 286 277 277 THR THR A . n 
A 1 287 THR 287 278 278 THR THR A . n 
A 1 288 CYS 288 279 279 CYS CYS A . n 
A 1 289 GLN 289 280 280 GLN GLN A . n 
A 1 290 THR 290 281 281 THR THR A . n 
A 1 291 PRO 291 282 282 PRO PRO A . n 
A 1 292 LYS 292 283 283 LYS LYS A . n 
A 1 293 GLY 293 284 284 GLY GLY A . n 
A 1 294 ALA 294 285 285 ALA ALA A . n 
A 1 295 ILE 295 286 286 ILE ILE A . n 
A 1 296 ASN 296 287 287 ASN ASN A . n 
A 1 297 THR 297 288 288 THR THR A . n 
A 1 298 SER 298 289 289 SER SER A . n 
A 1 299 LEU 299 290 290 LEU LEU A . n 
A 1 300 PRO 300 291 291 PRO PRO A . n 
A 1 301 PHE 301 292 292 PHE PHE A . n 
A 1 302 GLN 302 293 293 GLN GLN A . n 
A 1 303 ASN 303 294 294 ASN ASN A . n 
A 1 304 ILE 304 295 295 ILE ILE A . n 
A 1 305 HIS 305 296 296 HIS HIS A . n 
A 1 306 PRO 306 297 297 PRO PRO A . n 
A 1 307 ILE 307 298 298 ILE ILE A . n 
A 1 308 THR 308 299 299 THR THR A . n 
A 1 309 ILE 309 300 300 ILE ILE A . n 
A 1 310 GLY 310 301 301 GLY GLY A . n 
A 1 311 LYS 311 302 302 LYS LYS A . n 
A 1 312 CYS 312 303 303 CYS CYS A . n 
A 1 313 PRO 313 304 304 PRO PRO A . n 
A 1 314 LYS 314 305 305 LYS LYS A . n 
A 1 315 TYR 315 306 306 TYR TYR A . n 
A 1 316 VAL 316 307 307 VAL VAL A . n 
A 1 317 LYS 317 308 308 LYS LYS A . n 
A 1 318 SER 318 309 309 SER SER A . n 
A 1 319 THR 319 310 310 THR THR A . n 
A 1 320 LYS 320 311 311 LYS LYS A . n 
A 1 321 LEU 321 312 312 LEU LEU A . n 
A 1 322 ARG 322 313 313 ARG ARG A . n 
A 1 323 LEU 323 314 314 LEU LEU A . n 
A 1 324 ALA 324 315 315 ALA ALA A . n 
A 1 325 THR 325 316 316 THR THR A . n 
A 1 326 GLY 326 317 317 GLY GLY A . n 
A 1 327 LEU 327 318 318 LEU LEU A . n 
A 1 328 ARG 328 319 319 ARG ARG A . n 
A 1 329 ASN 329 320 320 ASN ASN A . n 
A 1 330 VAL 330 321 321 VAL VAL A . n 
A 1 331 PRO 331 322 ?   ?   ?   A . n 
A 1 332 SER 332 323 ?   ?   ?   A . n 
A 1 333 ILE 333 324 ?   ?   ?   A . n 
A 1 334 GLN 334 325 ?   ?   ?   A . n 
A 1 335 SER 335 326 ?   ?   ?   A . n 
A 1 336 ARG 336 327 ?   ?   ?   A . n 
B 2 1   GLY 1   1   ?   ?   ?   B . n 
B 2 2   LEU 2   2   ?   ?   ?   B . n 
B 2 3   PHE 3   3   ?   ?   ?   B . n 
B 2 4   GLY 4   4   ?   ?   ?   B . n 
B 2 5   ALA 5   5   ?   ?   ?   B . n 
B 2 6   ILE 6   6   ?   ?   ?   B . n 
B 2 7   ALA 7   7   ?   ?   ?   B . n 
B 2 8   GLY 8   8   ?   ?   ?   B . n 
B 2 9   PHE 9   9   ?   ?   ?   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  ?   ?   ?   B . n 
B 2 67  GLY 67  67  ?   ?   ?   B . n 
B 2 68  LYS 68  68  ?   ?   ?   B . n 
B 2 69  GLU 69  69  ?   ?   ?   B . n 
B 2 70  PHE 70  70  ?   ?   ?   B . n 
B 2 71  ASN 71  71  ?   ?   ?   B . n 
B 2 72  HIS 72  72  ?   ?   ?   B . n 
B 2 73  LEU 73  73  ?   ?   ?   B . n 
B 2 74  GLU 74  74  ?   ?   ?   B . n 
B 2 75  LYS 75  75  ?   ?   ?   B . n 
B 2 76  ARG 76  76  ?   ?   ?   B . n 
B 2 77  ILE 77  77  ?   ?   ?   B . n 
B 2 78  GLU 78  78  ?   ?   ?   B . n 
B 2 79  ASN 79  79  ?   ?   ?   B . n 
B 2 80  LEU 80  80  ?   ?   ?   B . n 
B 2 81  ASN 81  81  ?   ?   ?   B . n 
B 2 82  LYS 82  82  ?   ?   ?   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 163 163 163 SER SER B . n 
B 2 164 GLU 164 164 164 GLU GLU B . n 
B 2 165 GLU 165 165 165 GLU GLU B . n 
B 2 166 ALA 166 166 166 ALA ALA B . n 
B 2 167 LYS 167 167 167 LYS LYS B . n 
B 2 168 LEU 168 168 168 LEU LEU B . n 
B 2 169 ASN 169 169 169 ASN ASN B . n 
B 2 170 ARG 170 170 170 ARG ARG B . n 
B 2 171 GLU 171 171 171 GLU GLU B . n 
B 2 172 GLU 172 172 172 GLU GLU B . n 
B 2 173 ILE 173 173 173 ILE ILE B . n 
B 2 174 ASP 174 174 174 ASP ASP 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 SER 178 178 ?   ?   ?   B . n 
B 2 179 LEU 179 179 ?   ?   ?   B . n 
B 2 180 VAL 180 180 ?   ?   ?   B . n 
B 2 181 PRO 181 181 ?   ?   ?   B . n 
B 2 182 ARG 182 182 ?   ?   ?   B . n 
C 1 1   ALA 1   -8  ?   ?   ?   C . n 
C 1 2   ASP 2   -7  ?   ?   ?   C . n 
C 1 3   PRO 3   -6  ?   ?   ?   C . n 
C 1 4   GLY 4   -5  ?   ?   ?   C . n 
C 1 5   TYR 5   -4  ?   ?   ?   C . n 
C 1 6   LEU 6   -3  ?   ?   ?   C . n 
C 1 7   LEU 7   -2  ?   ?   ?   C . n 
C 1 8   GLU 8   -1  ?   ?   ?   C . n 
C 1 9   PHE 9   0   ?   ?   ?   C . n 
C 1 10  ASP 10  1   ?   ?   ?   C . n 
C 1 11  THR 11  2   ?   ?   ?   C . n 
C 1 12  LEU 12  3   ?   ?   ?   C . n 
C 1 13  CYS 13  4   ?   ?   ?   C . n 
C 1 14  ILE 14  5   ?   ?   ?   C . n 
C 1 15  GLY 15  6   ?   ?   ?   C . n 
C 1 16  TYR 16  7   ?   ?   ?   C . n 
C 1 17  HIS 17  8   ?   ?   ?   C . n 
C 1 18  ALA 18  9   ?   ?   ?   C . n 
C 1 19  ASN 19  10  ?   ?   ?   C . n 
C 1 20  ASN 20  11  11  ASN ASN C . n 
C 1 21  SER 21  12  12  SER SER C . n 
C 1 22  THR 22  13  13  THR THR C . n 
C 1 23  ASP 23  14  14  ASP ASP C . n 
C 1 24  THR 24  15  15  THR THR C . n 
C 1 25  VAL 25  16  16  VAL VAL C . n 
C 1 26  ASP 26  17  17  ASP ASP C . n 
C 1 27  THR 27  18  18  THR THR C . n 
C 1 28  VAL 28  19  19  VAL VAL C . n 
C 1 29  LEU 29  20  20  LEU LEU C . n 
C 1 30  GLU 30  21  21  GLU GLU C . n 
C 1 31  LYS 31  22  22  LYS LYS C . n 
C 1 32  ASN 32  23  23  ASN ASN C . n 
C 1 33  VAL 33  24  24  VAL VAL C . n 
C 1 34  THR 34  25  25  THR THR C . n 
C 1 35  VAL 35  26  26  VAL VAL C . n 
C 1 36  THR 36  27  27  THR THR C . n 
C 1 37  HIS 37  28  28  HIS HIS C . n 
C 1 38  SER 38  29  29  SER SER C . n 
C 1 39  VAL 39  30  30  VAL VAL C . n 
C 1 40  ASN 40  31  31  ASN ASN C . n 
C 1 41  LEU 41  32  32  LEU LEU C . n 
C 1 42  LEU 42  33  33  LEU LEU C . n 
C 1 43  GLU 43  34  34  GLU GLU C . n 
C 1 44  ASP 44  35  35  ASP ASP C . n 
C 1 45  LYS 45  36  36  LYS LYS C . n 
C 1 46  HIS 46  37  37  HIS HIS C . n 
C 1 47  ASN 47  38  38  ASN ASN C . n 
C 1 48  GLY 48  39  39  GLY GLY C . n 
C 1 49  LYS 49  40  40  LYS LYS C . n 
C 1 50  LEU 50  41  41  LEU LEU C . n 
C 1 51  CYS 51  42  42  CYS CYS C . n 
C 1 52  LYS 52  43  43  LYS LYS C . n 
C 1 53  LEU 53  44  44  LEU LEU C . n 
C 1 54  ARG 54  45  45  ARG ARG C . n 
C 1 55  GLY 55  46  46  GLY GLY C . n 
C 1 56  VAL 56  47  47  VAL VAL C . n 
C 1 57  ALA 57  48  48  ALA ALA C . n 
C 1 58  PRO 58  49  49  PRO PRO C . n 
C 1 59  LEU 59  50  50  LEU LEU C . n 
C 1 60  HIS 60  51  51  HIS HIS C . n 
C 1 61  LEU 61  52  52  LEU LEU C . n 
C 1 62  GLY 62  53  53  GLY GLY C . n 
C 1 63  LYS 63  54  54  LYS LYS C . n 
C 1 64  CYS 64  55  55  CYS CYS C . n 
C 1 65  ASN 65  56  56  ASN ASN C . n 
C 1 66  ILE 66  57  57  ILE ILE C . n 
C 1 67  ALA 67  58  58  ALA ALA C . n 
C 1 68  GLY 68  59  59  GLY GLY C . n 
C 1 69  TRP 69  60  60  TRP TRP C . n 
C 1 70  ILE 70  61  61  ILE ILE C . n 
C 1 71  LEU 71  62  62  LEU LEU C . n 
C 1 72  GLY 72  63  63  GLY GLY C . n 
C 1 73  ASN 73  64  64  ASN ASN C . n 
C 1 74  PRO 74  65  65  PRO PRO C . n 
C 1 75  GLU 75  66  66  GLU GLU C . n 
C 1 76  CYS 76  67  67  CYS CYS C . n 
C 1 77  GLU 77  68  68  GLU GLU C . n 
C 1 78  SER 78  69  69  SER SER C . n 
C 1 79  LEU 79  70  70  LEU LEU C . n 
C 1 80  SER 80  71  71  SER SER C . n 
C 1 81  THR 81  72  72  THR THR C . n 
C 1 82  ALA 82  73  73  ALA ALA C . n 
C 1 83  SER 83  74  74  SER SER C . n 
C 1 84  SER 84  75  75  SER SER C . n 
C 1 85  TRP 85  76  76  TRP TRP C . n 
C 1 86  SER 86  77  77  SER SER C . n 
C 1 87  TYR 87  78  78  TYR TYR C . n 
C 1 88  ILE 88  79  79  ILE ILE C . n 
C 1 89  VAL 89  80  80  VAL VAL C . n 
C 1 90  GLU 90  81  81  GLU GLU C . n 
C 1 91  THR 91  82  82  THR THR C . n 
C 1 92  SER 92  83  83  SER SER C . n 
C 1 93  SER 93  84  84  SER SER C . n 
C 1 94  SER 94  85  85  SER SER C . n 
C 1 95  ASP 95  86  86  ASP ASP C . n 
C 1 96  ASN 96  87  87  ASN ASN C . n 
C 1 97  GLY 97  88  88  GLY GLY C . n 
C 1 98  THR 98  89  89  THR THR C . n 
C 1 99  CYS 99  90  90  CYS CYS C . n 
C 1 100 TYR 100 91  91  TYR TYR C . n 
C 1 101 PRO 101 92  92  PRO PRO C . n 
C 1 102 GLY 102 93  93  GLY GLY C . n 
C 1 103 ASP 103 94  94  ASP ASP C . n 
C 1 104 PHE 104 95  95  PHE PHE C . n 
C 1 105 ILE 105 96  96  ILE ILE C . n 
C 1 106 ASP 106 97  97  ASP ASP C . n 
C 1 107 TYR 107 98  98  TYR TYR C . n 
C 1 108 GLU 108 99  99  GLU GLU C . n 
C 1 109 GLU 109 100 100 GLU GLU C . n 
C 1 110 LEU 110 101 101 LEU LEU C . n 
C 1 111 ARG 111 102 102 ARG ARG C . n 
C 1 112 GLU 112 103 103 GLU GLU C . n 
C 1 113 GLN 113 104 104 GLN GLN C . n 
C 1 114 LEU 114 105 105 LEU LEU C . n 
C 1 115 SER 115 106 106 SER SER C . n 
C 1 116 SER 116 107 107 SER SER C . n 
C 1 117 VAL 117 108 108 VAL VAL C . n 
C 1 118 SER 118 109 109 SER SER C . n 
C 1 119 SER 119 110 110 SER SER C . n 
C 1 120 PHE 120 111 111 PHE PHE C . n 
C 1 121 GLU 121 112 112 GLU GLU C . n 
C 1 122 ARG 122 113 113 ARG ARG C . n 
C 1 123 PHE 123 114 114 PHE PHE C . n 
C 1 124 GLU 124 115 115 GLU GLU C . n 
C 1 125 ILE 125 116 116 ILE ILE C . n 
C 1 126 PHE 126 117 117 PHE PHE C . n 
C 1 127 PRO 127 118 118 PRO PRO C . n 
C 1 128 LYS 128 119 119 LYS LYS C . n 
C 1 129 THR 129 120 120 THR THR C . n 
C 1 130 SER 130 121 121 SER SER C . n 
C 1 131 SER 131 122 122 SER SER C . n 
C 1 132 TRP 132 123 123 TRP TRP C . n 
C 1 133 PRO 133 124 124 PRO PRO C . n 
C 1 134 ASN 134 125 125 ASN ASN C . n 
C 1 135 HIS 135 126 126 HIS HIS C . n 
C 1 136 ASP 136 127 127 ASP ASP C . n 
C 1 137 SER 137 128 128 SER SER C . n 
C 1 138 ASN 138 129 129 ASN ASN C . n 
C 1 139 LYS 139 130 130 LYS LYS C . n 
C 1 140 GLY 140 131 131 GLY GLY C . n 
C 1 141 VAL 141 132 132 VAL VAL C . n 
C 1 142 THR 142 133 133 THR THR C . n 
C 1 143 ALA 143 134 134 ALA ALA C . n 
C 1 144 ALA 144 135 135 ALA ALA C . n 
C 1 145 CYS 145 136 136 CYS CYS C . n 
C 1 146 PRO 146 137 137 PRO PRO C . n 
C 1 147 HIS 147 138 138 HIS HIS C . n 
C 1 148 ALA 148 139 139 ALA ALA C . n 
C 1 149 GLY 149 140 140 GLY GLY C . n 
C 1 150 ALA 150 141 141 ALA ALA C . n 
C 1 151 LYS 151 142 142 LYS LYS C . n 
C 1 152 SER 152 143 143 SER SER C . n 
C 1 153 PHE 153 144 144 PHE PHE C . n 
C 1 154 TYR 154 145 145 TYR TYR C . n 
C 1 155 LYS 155 146 146 LYS LYS C . n 
C 1 156 ASN 156 147 147 ASN ASN C . n 
C 1 157 LEU 157 148 148 LEU LEU C . n 
C 1 158 ILE 158 149 149 ILE ILE C . n 
C 1 159 TRP 159 150 150 TRP TRP C . n 
C 1 160 LEU 160 151 151 LEU LEU C . n 
C 1 161 VAL 161 152 152 VAL VAL C . n 
C 1 162 LYS 162 153 153 LYS LYS C . n 
C 1 163 LYS 163 154 154 LYS LYS C . n 
C 1 164 GLY 164 155 155 GLY GLY C . n 
C 1 165 ASN 165 156 156 ASN ASN C . n 
C 1 166 SER 166 157 157 SER SER C . n 
C 1 167 TYR 167 158 158 TYR TYR C . n 
C 1 168 PRO 168 159 159 PRO PRO C . n 
C 1 169 LYS 169 160 160 LYS LYS C . n 
C 1 170 LEU 170 161 161 LEU LEU C . n 
C 1 171 SER 171 162 162 SER SER C . n 
C 1 172 LYS 172 163 163 LYS LYS C . n 
C 1 173 SER 173 164 164 SER SER C . n 
C 1 174 TYR 174 165 165 TYR TYR C . n 
C 1 175 ILE 175 166 166 ILE ILE C . n 
C 1 176 ASN 176 167 167 ASN ASN C . n 
C 1 177 ASP 177 168 168 ASP ASP C . n 
C 1 178 LYS 178 169 169 LYS LYS C . n 
C 1 179 GLY 179 170 170 GLY GLY C . n 
C 1 180 LYS 180 171 171 LYS LYS C . n 
C 1 181 GLU 181 172 172 GLU GLU C . n 
C 1 182 VAL 182 173 173 VAL VAL C . n 
C 1 183 LEU 183 174 174 LEU LEU C . n 
C 1 184 VAL 184 175 175 VAL VAL C . n 
C 1 185 LEU 185 176 176 LEU LEU C . n 
C 1 186 TRP 186 177 177 TRP TRP C . n 
C 1 187 GLY 187 178 178 GLY GLY C . n 
C 1 188 ILE 188 179 179 ILE ILE C . n 
C 1 189 HIS 189 180 180 HIS HIS C . n 
C 1 190 HIS 190 181 181 HIS HIS C . n 
C 1 191 PRO 191 182 182 PRO PRO C . n 
C 1 192 SER 192 183 183 SER SER C . n 
C 1 193 THR 193 184 184 THR THR C . n 
C 1 194 SER 194 185 185 SER SER C . n 
C 1 195 ALA 195 186 186 ALA ALA C . n 
C 1 196 ASP 196 187 187 ASP ASP C . n 
C 1 197 GLN 197 188 188 GLN GLN C . n 
C 1 198 GLN 198 189 189 GLN GLN C . n 
C 1 199 SER 199 190 190 SER SER C . n 
C 1 200 LEU 200 191 191 LEU LEU C . n 
C 1 201 TYR 201 192 192 TYR TYR C . n 
C 1 202 GLN 202 193 193 GLN GLN C . n 
C 1 203 ASN 203 194 194 ASN ASN C . n 
C 1 204 ALA 204 195 195 ALA ALA C . n 
C 1 205 ASP 205 196 196 ASP ASP C . n 
C 1 206 ALA 206 197 197 ALA ALA C . n 
C 1 207 TYR 207 198 198 TYR TYR C . n 
C 1 208 VAL 208 199 199 VAL VAL C . n 
C 1 209 PHE 209 200 200 PHE PHE C . n 
C 1 210 VAL 210 201 201 VAL VAL C . n 
C 1 211 GLY 211 202 202 GLY GLY C . n 
C 1 212 SER 212 203 203 SER SER C . n 
C 1 213 SER 213 204 204 SER SER C . n 
C 1 214 ARG 214 205 205 ARG ARG C . n 
C 1 215 TYR 215 206 206 TYR TYR C . n 
C 1 216 SER 216 207 207 SER SER C . n 
C 1 217 LYS 217 208 208 LYS LYS C . n 
C 1 218 LYS 218 209 209 LYS LYS C . n 
C 1 219 PHE 219 210 210 PHE PHE C . n 
C 1 220 LYS 220 211 211 LYS LYS C . n 
C 1 221 PRO 221 212 212 PRO PRO C . n 
C 1 222 GLU 222 213 213 GLU GLU C . n 
C 1 223 ILE 223 214 214 ILE ILE C . n 
C 1 224 ALA 224 215 215 ALA ALA C . n 
C 1 225 ILE 225 216 216 ILE ILE C . n 
C 1 226 ARG 226 217 217 ARG ARG C . n 
C 1 227 PRO 227 218 218 PRO PRO C . n 
C 1 228 LYS 228 219 219 LYS LYS C . n 
C 1 229 VAL 229 220 220 VAL VAL C . n 
C 1 230 ARG 230 221 221 ARG ARG C . n 
C 1 231 ASP 231 222 222 ASP ASP C . n 
C 1 232 GLN 232 223 223 GLN GLN C . n 
C 1 233 GLU 233 224 224 GLU GLU C . n 
C 1 234 GLY 234 225 225 GLY GLY C . n 
C 1 235 ARG 235 226 226 ARG ARG C . n 
C 1 236 MET 236 227 227 MET MET C . n 
C 1 237 ASN 237 228 228 ASN ASN C . n 
C 1 238 TYR 238 229 229 TYR TYR C . n 
C 1 239 TYR 239 230 230 TYR TYR C . n 
C 1 240 TRP 240 231 231 TRP TRP C . n 
C 1 241 THR 241 232 232 THR THR C . n 
C 1 242 LEU 242 233 233 LEU LEU C . n 
C 1 243 VAL 243 234 234 VAL VAL C . n 
C 1 244 GLU 244 235 235 GLU GLU C . n 
C 1 245 PRO 245 236 236 PRO PRO C . n 
C 1 246 GLY 246 237 237 GLY GLY C . n 
C 1 247 ASP 247 238 238 ASP ASP C . n 
C 1 248 LYS 248 239 239 LYS LYS C . n 
C 1 249 ILE 249 240 240 ILE ILE C . n 
C 1 250 THR 250 241 241 THR THR C . n 
C 1 251 PHE 251 242 242 PHE PHE C . n 
C 1 252 GLU 252 243 243 GLU GLU C . n 
C 1 253 ALA 253 244 244 ALA ALA C . n 
C 1 254 THR 254 245 245 THR THR C . n 
C 1 255 GLY 255 246 246 GLY GLY C . n 
C 1 256 ASN 256 247 247 ASN ASN C . n 
C 1 257 LEU 257 248 248 LEU LEU C . n 
C 1 258 VAL 258 249 249 VAL VAL C . n 
C 1 259 VAL 259 250 250 VAL VAL C . n 
C 1 260 PRO 260 251 251 PRO PRO C . n 
C 1 261 ARG 261 252 252 ARG ARG C . n 
C 1 262 TYR 262 253 253 TYR TYR C . n 
C 1 263 ALA 263 254 254 ALA ALA C . n 
C 1 264 PHE 264 255 255 PHE PHE C . n 
C 1 265 ALA 265 256 256 ALA ALA C . n 
C 1 266 MET 266 257 257 MET MET C . n 
C 1 267 GLU 267 258 258 GLU GLU C . n 
C 1 268 ARG 268 259 259 ARG ARG C . n 
C 1 269 ASN 269 260 260 ASN ASN C . n 
C 1 270 ALA 270 261 261 ALA ALA C . n 
C 1 271 GLY 271 262 262 GLY GLY C . n 
C 1 272 SER 272 263 263 SER SER C . n 
C 1 273 GLY 273 264 264 GLY GLY C . n 
C 1 274 ILE 274 265 265 ILE ILE C . n 
C 1 275 ILE 275 266 266 ILE ILE C . n 
C 1 276 ILE 276 267 267 ILE ILE C . n 
C 1 277 SER 277 268 268 SER SER C . n 
C 1 278 ASP 278 269 269 ASP ASP C . n 
C 1 279 THR 279 270 270 THR THR C . n 
C 1 280 PRO 280 271 271 PRO PRO C . n 
C 1 281 VAL 281 272 272 VAL VAL C . n 
C 1 282 HIS 282 273 273 HIS HIS C . n 
C 1 283 ASP 283 274 274 ASP ASP C . n 
C 1 284 CYS 284 275 275 CYS CYS C . n 
C 1 285 ASN 285 276 276 ASN ASN C . n 
C 1 286 THR 286 277 277 THR THR C . n 
C 1 287 THR 287 278 278 THR THR C . n 
C 1 288 CYS 288 279 279 CYS CYS C . n 
C 1 289 GLN 289 280 280 GLN GLN C . n 
C 1 290 THR 290 281 281 THR THR C . n 
C 1 291 PRO 291 282 282 PRO PRO C . n 
C 1 292 LYS 292 283 283 LYS LYS C . n 
C 1 293 GLY 293 284 284 GLY GLY C . n 
C 1 294 ALA 294 285 285 ALA ALA C . n 
C 1 295 ILE 295 286 286 ILE ILE C . n 
C 1 296 ASN 296 287 287 ASN ASN C . n 
C 1 297 THR 297 288 288 THR THR C . n 
C 1 298 SER 298 289 289 SER SER C . n 
C 1 299 LEU 299 290 290 LEU LEU C . n 
C 1 300 PRO 300 291 291 PRO PRO C . n 
C 1 301 PHE 301 292 292 PHE PHE C . n 
C 1 302 GLN 302 293 293 GLN GLN C . n 
C 1 303 ASN 303 294 294 ASN ASN C . n 
C 1 304 ILE 304 295 295 ILE ILE C . n 
C 1 305 HIS 305 296 296 HIS HIS C . n 
C 1 306 PRO 306 297 297 PRO PRO C . n 
C 1 307 ILE 307 298 298 ILE ILE C . n 
C 1 308 THR 308 299 299 THR THR C . n 
C 1 309 ILE 309 300 300 ILE ILE C . n 
C 1 310 GLY 310 301 301 GLY GLY C . n 
C 1 311 LYS 311 302 302 LYS LYS C . n 
C 1 312 CYS 312 303 303 CYS CYS C . n 
C 1 313 PRO 313 304 304 PRO PRO C . n 
C 1 314 LYS 314 305 305 LYS LYS C . n 
C 1 315 TYR 315 306 306 TYR TYR C . n 
C 1 316 VAL 316 307 307 VAL VAL C . n 
C 1 317 LYS 317 308 308 LYS LYS C . n 
C 1 318 SER 318 309 309 SER SER C . n 
C 1 319 THR 319 310 310 THR THR C . n 
C 1 320 LYS 320 311 311 LYS LYS C . n 
C 1 321 LEU 321 312 312 LEU LEU C . n 
C 1 322 ARG 322 313 313 ARG ARG C . n 
C 1 323 LEU 323 314 314 LEU LEU C . n 
C 1 324 ALA 324 315 315 ALA ALA C . n 
C 1 325 THR 325 316 316 THR THR C . n 
C 1 326 GLY 326 317 317 GLY GLY C . n 
C 1 327 LEU 327 318 318 LEU LEU C . n 
C 1 328 ARG 328 319 319 ARG ARG C . n 
C 1 329 ASN 329 320 320 ASN ASN C . n 
C 1 330 VAL 330 321 321 VAL VAL C . n 
C 1 331 PRO 331 322 ?   ?   ?   C . n 
C 1 332 SER 332 323 ?   ?   ?   C . n 
C 1 333 ILE 333 324 ?   ?   ?   C . n 
C 1 334 GLN 334 325 ?   ?   ?   C . n 
C 1 335 SER 335 326 ?   ?   ?   C . n 
C 1 336 ARG 336 327 ?   ?   ?   C . n 
D 2 1   GLY 1   1   ?   ?   ?   D . n 
D 2 2   LEU 2   2   ?   ?   ?   D . n 
D 2 3   PHE 3   3   ?   ?   ?   D . n 
D 2 4   GLY 4   4   ?   ?   ?   D . n 
D 2 5   ALA 5   5   ?   ?   ?   D . n 
D 2 6   ILE 6   6   ?   ?   ?   D . n 
D 2 7   ALA 7   7   ?   ?   ?   D . n 
D 2 8   GLY 8   8   ?   ?   ?   D . n 
D 2 9   PHE 9   9   ?   ?   ?   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  ?   ?   ?   D . n 
D 2 21  TRP 21  21  ?   ?   ?   D . n 
D 2 22  TYR 22  22  ?   ?   ?   D . n 
D 2 23  GLY 23  23  ?   ?   ?   D . n 
D 2 24  TYR 24  24  ?   ?   ?   D . n 
D 2 25  HIS 25  25  ?   ?   ?   D . n 
D 2 26  HIS 26  26  ?   ?   ?   D . n 
D 2 27  GLN 27  27  ?   ?   ?   D . n 
D 2 28  ASN 28  28  ?   ?   ?   D . n 
D 2 29  GLU 29  29  ?   ?   ?   D . n 
D 2 30  GLN 30  30  ?   ?   ?   D . n 
D 2 31  GLY 31  31  ?   ?   ?   D . n 
D 2 32  SER 32  32  ?   ?   ?   D . n 
D 2 33  GLY 33  33  ?   ?   ?   D . n 
D 2 34  TYR 34  34  ?   ?   ?   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  ?   ?   ?   D . n 
D 2 63  PHE 63  63  ?   ?   ?   D . n 
D 2 64  THR 64  64  ?   ?   ?   D . n 
D 2 65  ALA 65  65  ?   ?   ?   D . n 
D 2 66  VAL 66  66  ?   ?   ?   D . n 
D 2 67  GLY 67  67  ?   ?   ?   D . n 
D 2 68  LYS 68  68  ?   ?   ?   D . n 
D 2 69  GLU 69  69  ?   ?   ?   D . n 
D 2 70  PHE 70  70  ?   ?   ?   D . n 
D 2 71  ASN 71  71  ?   ?   ?   D . n 
D 2 72  HIS 72  72  ?   ?   ?   D . n 
D 2 73  LEU 73  73  ?   ?   ?   D . n 
D 2 74  GLU 74  74  ?   ?   ?   D . n 
D 2 75  LYS 75  75  ?   ?   ?   D . n 
D 2 76  ARG 76  76  ?   ?   ?   D . n 
D 2 77  ILE 77  77  ?   ?   ?   D . n 
D 2 78  GLU 78  78  ?   ?   ?   D . n 
D 2 79  ASN 79  79  ?   ?   ?   D . n 
D 2 80  LEU 80  80  ?   ?   ?   D . n 
D 2 81  ASN 81  81  ?   ?   ?   D . n 
D 2 82  LYS 82  82  ?   ?   ?   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 ?   ?   ?   D . n 
D 2 128 ASN 128 128 ?   ?   ?   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 ?   ?   ?   D . n 
D 2 139 GLU 139 139 ?   ?   ?   D . n 
D 2 140 PHE 140 140 ?   ?   ?   D . n 
D 2 141 TYR 141 141 ?   ?   ?   D . n 
D 2 142 HIS 142 142 ?   ?   ?   D . n 
D 2 143 LYS 143 143 ?   ?   ?   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 ?   ?   ?   D . n 
D 2 157 TYR 157 157 ?   ?   ?   D . n 
D 2 158 ASP 158 158 ?   ?   ?   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 163 163 163 SER SER D . n 
D 2 164 GLU 164 164 164 GLU GLU D . n 
D 2 165 GLU 165 165 165 GLU GLU D . n 
D 2 166 ALA 166 166 166 ALA ALA D . n 
D 2 167 LYS 167 167 167 LYS LYS D . n 
D 2 168 LEU 168 168 168 LEU LEU D . n 
D 2 169 ASN 169 169 169 ASN ASN D . n 
D 2 170 ARG 170 170 170 ARG ARG D . n 
D 2 171 GLU 171 171 171 GLU GLU 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 SER 178 178 ?   ?   ?   D . n 
D 2 179 LEU 179 179 ?   ?   ?   D . n 
D 2 180 VAL 180 180 ?   ?   ?   D . n 
D 2 181 PRO 181 181 ?   ?   ?   D . n 
D 2 182 ARG 182 182 ?   ?   ?   D . n 
# 
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 
E 3 NAG 1  401 330 NAG NAG A . 
F 3 NAG 2  402 331 NAG NAG A . 
G 3 NAG 1  403 403 NAG NAG A . 
H 3 NAG 1  404 335 NAG NAG A . 
I 3 NAG 1  401 330 NAG NAG C . 
J 3 NAG 2  402 331 NAG NAG C . 
K 3 NAG 1  403 403 NAG NAG C . 
L 3 NAG 1  404 335 NAG NAG C . 
M 4 HOH 1  501 2   HOH HOH A . 
M 4 HOH 2  502 3   HOH HOH A . 
M 4 HOH 3  503 8   HOH HOH A . 
M 4 HOH 4  504 9   HOH HOH A . 
M 4 HOH 5  505 11  HOH HOH A . 
M 4 HOH 6  506 14  HOH HOH A . 
M 4 HOH 7  507 16  HOH HOH A . 
M 4 HOH 8  508 17  HOH HOH A . 
M 4 HOH 9  509 18  HOH HOH A . 
M 4 HOH 10 510 19  HOH HOH A . 
M 4 HOH 11 511 21  HOH HOH A . 
M 4 HOH 12 512 25  HOH HOH A . 
M 4 HOH 13 513 26  HOH HOH A . 
M 4 HOH 14 514 27  HOH HOH A . 
M 4 HOH 15 515 28  HOH HOH A . 
M 4 HOH 16 516 29  HOH HOH A . 
M 4 HOH 17 517 34  HOH HOH A . 
M 4 HOH 18 518 35  HOH HOH A . 
M 4 HOH 19 519 36  HOH HOH A . 
M 4 HOH 20 520 37  HOH HOH A . 
M 4 HOH 21 521 38  HOH HOH A . 
M 4 HOH 22 522 42  HOH HOH A . 
M 4 HOH 23 523 49  HOH HOH A . 
M 4 HOH 24 524 50  HOH HOH A . 
M 4 HOH 25 525 51  HOH HOH A . 
M 4 HOH 26 526 52  HOH HOH A . 
M 4 HOH 27 527 53  HOH HOH A . 
M 4 HOH 28 528 54  HOH HOH A . 
M 4 HOH 29 529 55  HOH HOH A . 
M 4 HOH 30 530 56  HOH HOH A . 
N 4 HOH 1  201 39  HOH HOH B . 
N 4 HOH 2  202 41  HOH HOH B . 
N 4 HOH 3  203 63  HOH HOH B . 
O 4 HOH 1  501 1   HOH HOH C . 
O 4 HOH 2  502 4   HOH HOH C . 
O 4 HOH 3  503 5   HOH HOH C . 
O 4 HOH 4  504 6   HOH HOH C . 
O 4 HOH 5  505 10  HOH HOH C . 
O 4 HOH 6  506 12  HOH HOH C . 
O 4 HOH 7  507 13  HOH HOH C . 
O 4 HOH 8  508 15  HOH HOH C . 
O 4 HOH 9  509 20  HOH HOH C . 
O 4 HOH 10 510 22  HOH HOH C . 
O 4 HOH 11 511 23  HOH HOH C . 
O 4 HOH 12 512 24  HOH HOH C . 
O 4 HOH 13 513 30  HOH HOH C . 
O 4 HOH 14 514 43  HOH HOH C . 
O 4 HOH 15 515 44  HOH HOH C . 
O 4 HOH 16 516 45  HOH HOH C . 
O 4 HOH 17 517 46  HOH HOH C . 
O 4 HOH 18 518 47  HOH HOH C . 
O 4 HOH 19 519 48  HOH HOH C . 
O 4 HOH 20 520 57  HOH HOH C . 
O 4 HOH 21 521 58  HOH HOH C . 
O 4 HOH 22 522 59  HOH HOH C . 
O 4 HOH 23 523 60  HOH HOH C . 
O 4 HOH 24 524 61  HOH HOH C . 
O 4 HOH 25 525 62  HOH HOH C . 
P 4 HOH 1  201 7   HOH HOH D . 
P 4 HOH 2  202 31  HOH HOH D . 
P 4 HOH 3  203 32  HOH HOH D . 
P 4 HOH 4  204 33  HOH HOH D . 
P 4 HOH 5  205 40  HOH HOH D . 
# 
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 A ASN 96  A ASN 87  ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 296 A ASN 287 ? ASN 'GLYCOSYLATION SITE' 
3 C ASN 296 C ASN 287 ? ASN 'GLYCOSYLATION SITE' 
4 C ASN 96  C ASN 87  ? ASN 'GLYCOSYLATION SITE' 
5 A ASN 285 A ASN 276 ? ASN 'GLYCOSYLATION SITE' 
6 C ASN 285 C ASN 276 ? 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 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,M,N 
2 1 C,D,I,J,K,L,O,P 
# 
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)' 4740  ? 
1 MORE         -17   ? 
1 'SSA (A^2)'  24390 ? 
2 'ABSA (A^2)' 2750  ? 
2 MORE         -2    ? 
2 'SSA (A^2)'  24930 ? 
# 
_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 2013-05-22 
2 'Structure model' 1 1 2014-03-12 
3 'Structure model' 1 2 2017-11-15 
# 
_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' 'Database references'    
2 2 'Structure model' 'Derived calculations'   
3 3 'Structure model' 'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    3 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_software.classification'       
2 3 'Structure model' '_software.contact_author'       
3 3 'Structure model' '_software.contact_author_email' 
4 3 'Structure model' '_software.date'                 
5 3 'Structure model' '_software.language'             
6 3 'Structure model' '_software.location'             
7 3 'Structure model' '_software.name'                 
8 3 'Structure model' '_software.type'                 
9 3 'Structure model' '_software.version'              
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 DENZO       .         ?               package 'Zbyszek Otwinowski' hkl@hkl-xray.com         'data reduction'  
http://www.hkl-xray.com/                  ?   ? 
2 SCALEPACK   .         ?               package 'Zbyszek Otwinowski' hkl@hkl-xray.com         'data scaling'    
http://www.hkl-xray.com/                  ?   ? 
3 PHENIX      1.7.1_743 ?               package 'Paul D. Adams'      PDAdams@lbl.gov          refinement        
http://www.phenix-online.org/             C++ ? 
4 PDB_EXTRACT 3.10      'June 10, 2010' package PDB                  deposit@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? 
5 HKL-2000    .         ?               ?       ?                    ?                        'data collection' ? ?   ? 
6 PHASER      .         ?               ?       ?                    ?                        phasing           ? ?   ? 
# 
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 SG  D CYS 144 ? ? CB  D CYS 148 ? ? 1.61 
2  1 ND2 C ASN 276 ? ? O5  C NAG 403 ? ? 1.74 
3  1 O   B CYS 148 ? ? OG  B SER 151 ? ? 1.99 
4  1 OD2 C ASP 14  ? ? OG  C SER 29  ? ? 2.00 
5  1 ND2 A ASN 287 ? ? O5  A NAG 404 ? ? 2.04 
6  1 O   D ASP 46  ? ? OG1 D THR 49  ? ? 2.10 
7  1 O   A LYS 154 ? ? O   A SER 157 ? ? 2.15 
8  1 OD1 A ASP 14  ? ? OG  A SER 29  ? ? 2.16 
9  1 ND2 C ASN 87  ? ? O5  C NAG 401 ? ? 2.16 
10 1 O   D GLN 125 ? ? OH  D TYR 159 ? ? 2.18 
11 1 OG1 A THR 18  ? ? O   A GLU 21  ? ? 2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             N 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASN 
_pdbx_validate_rmsd_angle.auth_seq_id_1              276 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASN 
_pdbx_validate_rmsd_angle.auth_seq_id_2              276 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASN 
_pdbx_validate_rmsd_angle.auth_seq_id_3              276 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                91.75 
_pdbx_validate_rmsd_angle.angle_target_value         110.60 
_pdbx_validate_rmsd_angle.angle_deviation            -18.85 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.80 
_pdbx_validate_rmsd_angle.linker_flag                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 VAL A 19  ? ? -51.46  -70.62  
2  1 LYS A 22  ? ? -90.37  -63.04  
3  1 SER A 69  ? ? -74.51  -73.00  
4  1 LEU A 70  ? ? 44.19   -126.33 
5  1 ALA A 73  ? ? 175.56  166.15  
6  1 SER A 109 ? ? -96.79  -60.54  
7  1 ASN A 156 ? ? 113.66  -6.61   
8  1 GLN A 193 ? ? 66.28   -16.73  
9  1 SER A 203 ? ? -170.73 -174.23 
10 1 ALA A 215 ? ? 178.66  161.44  
11 1 ASN A 247 ? ? 64.48   -2.69   
12 1 ARG A 252 ? ? -120.51 -63.12  
13 1 CYS A 275 ? ? -67.46  -179.15 
14 1 VAL B 18  ? ? -129.58 -68.73  
15 1 ALA B 35  ? ? 175.95  169.36  
16 1 LEU B 38  ? ? -115.02 -72.29  
17 1 GLN B 42  ? ? -58.67  -73.38  
18 1 ASN B 60  ? ? 44.17   -131.57 
19 1 GLN B 62  ? ? -81.95  -153.13 
20 1 PHE B 63  ? ? 73.61   63.47   
21 1 VAL B 84  ? ? -47.64  -81.32  
22 1 LEU B 102 ? ? -91.75  -71.61  
23 1 THR B 107 ? ? -96.94  -60.49  
24 1 LYS B 127 ? ? 46.96   -123.90 
25 1 THR B 147 ? ? 78.85   -19.34  
26 1 LEU C 20  ? ? -93.23  -66.39  
27 1 LEU C 32  ? ? -135.24 -66.83  
28 1 SER C 71  ? ? -81.21  -72.95  
29 1 THR C 72  ? ? 60.64   -115.90 
30 1 ALA C 73  ? ? 58.78   -152.70 
31 1 ASN C 156 ? ? 77.09   -15.38  
32 1 GLN C 193 ? ? 66.21   -18.52  
33 1 SER C 203 ? ? -172.84 -174.13 
34 1 ASN C 247 ? ? 67.29   -3.64   
35 1 ARG C 252 ? ? -106.80 -60.64  
36 1 ALA C 261 ? ? 42.28   -123.83 
37 1 THR C 288 ? ? -72.57  -166.20 
38 1 SER C 289 ? ? 93.68   -4.69   
39 1 HIS C 296 ? ? -177.20 138.90  
40 1 THR C 310 ? ? -104.89 -72.24  
41 1 THR C 316 ? ? -130.96 -63.02  
42 1 THR D 15  ? ? -84.81  -72.13  
43 1 VAL D 18  ? ? 62.94   -122.82 
44 1 LEU D 38  ? ? -120.05 -75.09  
45 1 ASN D 43  ? ? -76.79  -70.02  
46 1 MET D 59  ? ? -79.63  -164.60 
47 1 ASN D 60  ? ? 63.71   68.54   
48 1 PHE D 88  ? ? -96.54  -61.19  
49 1 SER D 113 ? ? -96.23  -72.08  
50 1 GLN D 125 ? ? -129.47 -70.81  
51 1 ASP D 145 ? ? -94.81  -63.33  
52 1 ASN D 146 ? ? -128.56 -63.75  
53 1 GLU D 150 ? ? -38.53  -71.39  
54 1 TYR D 162 ? ? -92.71  -72.25  
55 1 ARG D 170 ? ? -133.47 -62.88  
# 
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 GLY A 155 ? ? ASN A 156 ? ? -116.05 
2 1 GLN B 62  ? ? PHE B 63  ? ? -137.56 
3 1 VAL B 84  ? ? ASP B 85  ? ? 144.95  
4 1 THR C 72  ? ? ALA C 73  ? ? -147.13 
5 1 LYS C 154 ? ? GLY C 155 ? ? -138.58 
6 1 MET D 149 ? ? GLU D 150 ? ? -144.88 
7 1 LEU D 168 ? ? ASN D 169 ? ? 146.67  
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C1 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    A 
_pdbx_validate_chiral.auth_comp_id    NAG 
_pdbx_validate_chiral.auth_seq_id     403 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         PLANAR 
_pdbx_validate_chiral.omega           . 
# 
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 -8  ? A ALA 1   
2   1 Y 1 A ASP -7  ? A ASP 2   
3   1 Y 1 A PRO -6  ? A PRO 3   
4   1 Y 1 A GLY -5  ? A GLY 4   
5   1 Y 1 A TYR -4  ? A TYR 5   
6   1 Y 1 A LEU -3  ? A LEU 6   
7   1 Y 1 A LEU -2  ? A LEU 7   
8   1 Y 1 A GLU -1  ? A GLU 8   
9   1 Y 1 A PHE 0   ? A PHE 9   
10  1 Y 1 A PRO 322 ? A PRO 331 
11  1 Y 1 A SER 323 ? A SER 332 
12  1 Y 1 A ILE 324 ? A ILE 333 
13  1 Y 1 A GLN 325 ? A GLN 334 
14  1 Y 1 A SER 326 ? A SER 335 
15  1 Y 1 A ARG 327 ? A ARG 336 
16  1 Y 1 B GLY 1   ? B GLY 1   
17  1 Y 1 B LEU 2   ? B LEU 2   
18  1 Y 1 B PHE 3   ? B PHE 3   
19  1 Y 1 B GLY 4   ? B GLY 4   
20  1 Y 1 B ALA 5   ? B ALA 5   
21  1 Y 1 B ILE 6   ? B ILE 6   
22  1 Y 1 B ALA 7   ? B ALA 7   
23  1 Y 1 B GLY 8   ? B GLY 8   
24  1 Y 1 B PHE 9   ? B PHE 9   
25  1 Y 1 B VAL 66  ? B VAL 66  
26  1 Y 1 B GLY 67  ? B GLY 67  
27  1 Y 1 B LYS 68  ? B LYS 68  
28  1 Y 1 B GLU 69  ? B GLU 69  
29  1 Y 1 B PHE 70  ? B PHE 70  
30  1 Y 1 B ASN 71  ? B ASN 71  
31  1 Y 1 B HIS 72  ? B HIS 72  
32  1 Y 1 B LEU 73  ? B LEU 73  
33  1 Y 1 B GLU 74  ? B GLU 74  
34  1 Y 1 B LYS 75  ? B LYS 75  
35  1 Y 1 B ARG 76  ? B ARG 76  
36  1 Y 1 B ILE 77  ? B ILE 77  
37  1 Y 1 B GLU 78  ? B GLU 78  
38  1 Y 1 B ASN 79  ? B ASN 79  
39  1 Y 1 B LEU 80  ? B LEU 80  
40  1 Y 1 B ASN 81  ? B ASN 81  
41  1 Y 1 B LYS 82  ? B LYS 82  
42  1 Y 1 B GLY 175 ? B GLY 175 
43  1 Y 1 B VAL 176 ? B VAL 176 
44  1 Y 1 B ARG 177 ? B ARG 177 
45  1 Y 1 B SER 178 ? B SER 178 
46  1 Y 1 B LEU 179 ? B LEU 179 
47  1 Y 1 B VAL 180 ? B VAL 180 
48  1 Y 1 B PRO 181 ? B PRO 181 
49  1 Y 1 B ARG 182 ? B ARG 182 
50  1 Y 1 C ALA -8  ? C ALA 1   
51  1 Y 1 C ASP -7  ? C ASP 2   
52  1 Y 1 C PRO -6  ? C PRO 3   
53  1 Y 1 C GLY -5  ? C GLY 4   
54  1 Y 1 C TYR -4  ? C TYR 5   
55  1 Y 1 C LEU -3  ? C LEU 6   
56  1 Y 1 C LEU -2  ? C LEU 7   
57  1 Y 1 C GLU -1  ? C GLU 8   
58  1 Y 1 C PHE 0   ? C PHE 9   
59  1 Y 1 C ASP 1   ? C ASP 10  
60  1 Y 1 C THR 2   ? C THR 11  
61  1 Y 1 C LEU 3   ? C LEU 12  
62  1 Y 1 C CYS 4   ? C CYS 13  
63  1 Y 1 C ILE 5   ? C ILE 14  
64  1 Y 1 C GLY 6   ? C GLY 15  
65  1 Y 1 C TYR 7   ? C TYR 16  
66  1 Y 1 C HIS 8   ? C HIS 17  
67  1 Y 1 C ALA 9   ? C ALA 18  
68  1 Y 1 C ASN 10  ? C ASN 19  
69  1 Y 1 C PRO 322 ? C PRO 331 
70  1 Y 1 C SER 323 ? C SER 332 
71  1 Y 1 C ILE 324 ? C ILE 333 
72  1 Y 1 C GLN 325 ? C GLN 334 
73  1 Y 1 C SER 326 ? C SER 335 
74  1 Y 1 C ARG 327 ? C ARG 336 
75  1 Y 1 D GLY 1   ? D GLY 1   
76  1 Y 1 D LEU 2   ? D LEU 2   
77  1 Y 1 D PHE 3   ? D PHE 3   
78  1 Y 1 D GLY 4   ? D GLY 4   
79  1 Y 1 D ALA 5   ? D ALA 5   
80  1 Y 1 D ILE 6   ? D ILE 6   
81  1 Y 1 D ALA 7   ? D ALA 7   
82  1 Y 1 D GLY 8   ? D GLY 8   
83  1 Y 1 D PHE 9   ? D PHE 9   
84  1 Y 1 D GLY 20  ? D GLY 20  
85  1 Y 1 D TRP 21  ? D TRP 21  
86  1 Y 1 D TYR 22  ? D TYR 22  
87  1 Y 1 D GLY 23  ? D GLY 23  
88  1 Y 1 D TYR 24  ? D TYR 24  
89  1 Y 1 D HIS 25  ? D HIS 25  
90  1 Y 1 D HIS 26  ? D HIS 26  
91  1 Y 1 D GLN 27  ? D GLN 27  
92  1 Y 1 D ASN 28  ? D ASN 28  
93  1 Y 1 D GLU 29  ? D GLU 29  
94  1 Y 1 D GLN 30  ? D GLN 30  
95  1 Y 1 D GLY 31  ? D GLY 31  
96  1 Y 1 D SER 32  ? D SER 32  
97  1 Y 1 D GLY 33  ? D GLY 33  
98  1 Y 1 D TYR 34  ? D TYR 34  
99  1 Y 1 D GLN 62  ? D GLN 62  
100 1 Y 1 D PHE 63  ? D PHE 63  
101 1 Y 1 D THR 64  ? D THR 64  
102 1 Y 1 D ALA 65  ? D ALA 65  
103 1 Y 1 D VAL 66  ? D VAL 66  
104 1 Y 1 D GLY 67  ? D GLY 67  
105 1 Y 1 D LYS 68  ? D LYS 68  
106 1 Y 1 D GLU 69  ? D GLU 69  
107 1 Y 1 D PHE 70  ? D PHE 70  
108 1 Y 1 D ASN 71  ? D ASN 71  
109 1 Y 1 D HIS 72  ? D HIS 72  
110 1 Y 1 D LEU 73  ? D LEU 73  
111 1 Y 1 D GLU 74  ? D GLU 74  
112 1 Y 1 D LYS 75  ? D LYS 75  
113 1 Y 1 D ARG 76  ? D ARG 76  
114 1 Y 1 D ILE 77  ? D ILE 77  
115 1 Y 1 D GLU 78  ? D GLU 78  
116 1 Y 1 D ASN 79  ? D ASN 79  
117 1 Y 1 D LEU 80  ? D LEU 80  
118 1 Y 1 D ASN 81  ? D ASN 81  
119 1 Y 1 D LYS 82  ? D LYS 82  
120 1 Y 1 D LYS 127 ? D LYS 127 
121 1 Y 1 D ASN 128 ? D ASN 128 
122 1 Y 1 D PHE 138 ? D PHE 138 
123 1 Y 1 D GLU 139 ? D GLU 139 
124 1 Y 1 D PHE 140 ? D PHE 140 
125 1 Y 1 D TYR 141 ? D TYR 141 
126 1 Y 1 D HIS 142 ? D HIS 142 
127 1 Y 1 D LYS 143 ? D LYS 143 
128 1 Y 1 D THR 156 ? D THR 156 
129 1 Y 1 D TYR 157 ? D TYR 157 
130 1 Y 1 D ASP 158 ? D ASP 158 
131 1 Y 1 D GLU 172 ? D GLU 172 
132 1 Y 1 D ILE 173 ? D ILE 173 
133 1 Y 1 D ASP 174 ? D ASP 174 
134 1 Y 1 D GLY 175 ? D GLY 175 
135 1 Y 1 D VAL 176 ? D VAL 176 
136 1 Y 1 D ARG 177 ? D ARG 177 
137 1 Y 1 D SER 178 ? D SER 178 
138 1 Y 1 D LEU 179 ? D LEU 179 
139 1 Y 1 D VAL 180 ? D VAL 180 
140 1 Y 1 D PRO 181 ? D PRO 181 
141 1 Y 1 D ARG 182 ? D ARG 182 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 N-ACETYL-D-GLUCOSAMINE NAG 
4 water                  HOH 
# 
_pdbx_reflns_twin.domain_id                    1 
_pdbx_reflns_twin.crystal_id                   1 
_pdbx_reflns_twin.diffrn_id                    1 
_pdbx_reflns_twin.fraction                     0.085 
_pdbx_reflns_twin.operator                     h,-h-k,-l 
_pdbx_reflns_twin.type                         ? 
_pdbx_reflns_twin.mean_F_square_over_mean_F2   ? 
_pdbx_reflns_twin.mean_I2_over_mean_I_square   ? 
# 
