data_3QQO
# 
_entry.id   3QQO 
# 
_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   3QQO         
RCSB  RCSB063981   
WWPDB D_1000063981 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3QQB . unspecified 
PDB 3QQE . unspecified 
PDB 3QQI . unspecified 
# 
_pdbx_database_status.entry_id                        3QQO 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2011-02-15 
_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 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Xu, R.'       1 
'Wilson, I.A.' 2 
# 
_citation.id                        primary 
_citation.title                     'Structural Characterization of an Early Fusion Intermediate of Influenza Virus Hemagglutinin.' 
_citation.journal_abbrev            J.Virol. 
_citation.journal_volume            85 
_citation.page_first                5172 
_citation.page_last                 5182 
_citation.year                      2011 
_citation.journal_id_ASTM           JOVIAM 
_citation.country                   US 
_citation.journal_id_ISSN           0022-538X 
_citation.journal_id_CSD            0825 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   21367895 
_citation.pdbx_database_id_DOI      10.1128/JVI.02430-10 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Xu, R.'       1 
primary 'Wilson, I.A.' 2 
# 
_cell.entry_id           3QQO 
_cell.length_a           67.999 
_cell.length_b           240.115 
_cell.length_c           70.332 
_cell.angle_alpha        90.00 
_cell.angle_beta         116.52 
_cell.angle_gamma        90.00 
_cell.Z_PDB              6 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3QQO 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_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          36504.227 3  ? ?     'HA1 chain'            ? 
2 polymer     man Hemagglutinin          20120.248 3  ? R106H 'HA2 chain ectodomain' ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   3  ? ?     ?                      ? 
4 water       nat water                  18.015    56 ? ?     ?                      ? 
# 
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 
;PGDQICIGYHANNSTEKVDTILERNVTVTHAKDILEKTHNGKLCKLNGIPPLELGDCSIAGWLLGNPECDRLLSVPEWSY
IMEKENPRDGLCYPGSFNDYEELKHLLSSVKHFEKVKILPKDRWTQHTTTGGSRACAVSGNPSFFRNMVWLTEKGSNYPV
AKGSYNNTSGEQMLIIWGVHHPNDETEQRTLYQNVGTYVSVGTSTLNKRSTPEIATRPKVNGQGGRMEFSWTLLDMWDTI
NFESTGNLIAPEYGFKISKRGSSGIMKTEGTLENCETKCQTPLGAINTTLPFHNVHPLTIGECPKYVKSEKLVLATGLRN
VPQIESR
;
;PGDQICIGYHANNSTEKVDTILERNVTVTHAKDILEKTHNGKLCKLNGIPPLELGDCSIAGWLLGNPECDRLLSVPEWSY
IMEKENPRDGLCYPGSFNDYEELKHLLSSVKHFEKVKILPKDRWTQHTTTGGSRACAVSGNPSFFRNMVWLTEKGSNYPV
AKGSYNNTSGEQMLIIWGVHHPNDETEQRTLYQNVGTYVSVGTSTLNKRSTPEIATRPKVNGQGGRMEFSWTLLDMWDTI
NFESTGNLIAPEYGFKISKRGSSGIMKTEGTLENCETKCQTPLGAINTTLPFHNVHPLTIGECPKYVKSEKLVLATGLRN
VPQIESR
;
A,C,E ? 
2 'polypeptide(L)' no no 
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNDQGSGYAADKESTQKAFDGITNKVNSVIEKMNTQFEAVGKEFSNLERRLENL
NKKMEDGFLDVWTYNAELLVLMENEHTLDFHDSNVKNLYDKVRMQLRDNVKELGNGCFEFYHKCDDECMNSVKNGTYDYP
KYEEESKLNRNEIK
;
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNDQGSGYAADKESTQKAFDGITNKVNSVIEKMNTQFEAVGKEFSNLERRLENL
NKKMEDGFLDVWTYNAELLVLMENEHTLDFHDSNVKNLYDKVRMQLRDNVKELGNGCFEFYHKCDDECMNSVKNGTYDYP
KYEEESKLNRNEIK
;
B,D,F ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   GLY n 
1 3   ASP n 
1 4   GLN n 
1 5   ILE n 
1 6   CYS n 
1 7   ILE n 
1 8   GLY n 
1 9   TYR n 
1 10  HIS n 
1 11  ALA n 
1 12  ASN n 
1 13  ASN n 
1 14  SER n 
1 15  THR n 
1 16  GLU n 
1 17  LYS n 
1 18  VAL n 
1 19  ASP n 
1 20  THR n 
1 21  ILE n 
1 22  LEU n 
1 23  GLU n 
1 24  ARG n 
1 25  ASN n 
1 26  VAL n 
1 27  THR n 
1 28  VAL n 
1 29  THR n 
1 30  HIS n 
1 31  ALA n 
1 32  LYS n 
1 33  ASP n 
1 34  ILE n 
1 35  LEU n 
1 36  GLU n 
1 37  LYS n 
1 38  THR n 
1 39  HIS n 
1 40  ASN n 
1 41  GLY n 
1 42  LYS n 
1 43  LEU n 
1 44  CYS n 
1 45  LYS n 
1 46  LEU n 
1 47  ASN n 
1 48  GLY n 
1 49  ILE n 
1 50  PRO n 
1 51  PRO n 
1 52  LEU n 
1 53  GLU n 
1 54  LEU n 
1 55  GLY n 
1 56  ASP n 
1 57  CYS n 
1 58  SER n 
1 59  ILE n 
1 60  ALA n 
1 61  GLY n 
1 62  TRP n 
1 63  LEU n 
1 64  LEU n 
1 65  GLY n 
1 66  ASN n 
1 67  PRO n 
1 68  GLU n 
1 69  CYS n 
1 70  ASP n 
1 71  ARG n 
1 72  LEU n 
1 73  LEU n 
1 74  SER n 
1 75  VAL n 
1 76  PRO n 
1 77  GLU n 
1 78  TRP n 
1 79  SER n 
1 80  TYR n 
1 81  ILE n 
1 82  MET n 
1 83  GLU n 
1 84  LYS n 
1 85  GLU n 
1 86  ASN n 
1 87  PRO n 
1 88  ARG n 
1 89  ASP n 
1 90  GLY n 
1 91  LEU n 
1 92  CYS n 
1 93  TYR n 
1 94  PRO n 
1 95  GLY n 
1 96  SER n 
1 97  PHE n 
1 98  ASN n 
1 99  ASP n 
1 100 TYR n 
1 101 GLU n 
1 102 GLU n 
1 103 LEU n 
1 104 LYS n 
1 105 HIS n 
1 106 LEU n 
1 107 LEU n 
1 108 SER n 
1 109 SER n 
1 110 VAL n 
1 111 LYS n 
1 112 HIS n 
1 113 PHE n 
1 114 GLU n 
1 115 LYS n 
1 116 VAL n 
1 117 LYS n 
1 118 ILE n 
1 119 LEU n 
1 120 PRO n 
1 121 LYS n 
1 122 ASP n 
1 123 ARG n 
1 124 TRP n 
1 125 THR n 
1 126 GLN n 
1 127 HIS n 
1 128 THR n 
1 129 THR n 
1 130 THR n 
1 131 GLY n 
1 132 GLY n 
1 133 SER n 
1 134 ARG n 
1 135 ALA n 
1 136 CYS n 
1 137 ALA n 
1 138 VAL n 
1 139 SER n 
1 140 GLY n 
1 141 ASN n 
1 142 PRO n 
1 143 SER n 
1 144 PHE n 
1 145 PHE n 
1 146 ARG n 
1 147 ASN n 
1 148 MET n 
1 149 VAL n 
1 150 TRP n 
1 151 LEU n 
1 152 THR n 
1 153 GLU n 
1 154 LYS n 
1 155 GLY n 
1 156 SER n 
1 157 ASN n 
1 158 TYR n 
1 159 PRO n 
1 160 VAL n 
1 161 ALA n 
1 162 LYS n 
1 163 GLY n 
1 164 SER n 
1 165 TYR n 
1 166 ASN n 
1 167 ASN n 
1 168 THR n 
1 169 SER n 
1 170 GLY n 
1 171 GLU n 
1 172 GLN n 
1 173 MET n 
1 174 LEU n 
1 175 ILE n 
1 176 ILE n 
1 177 TRP n 
1 178 GLY n 
1 179 VAL n 
1 180 HIS n 
1 181 HIS n 
1 182 PRO n 
1 183 ASN n 
1 184 ASP n 
1 185 GLU n 
1 186 THR n 
1 187 GLU n 
1 188 GLN n 
1 189 ARG n 
1 190 THR n 
1 191 LEU n 
1 192 TYR n 
1 193 GLN n 
1 194 ASN n 
1 195 VAL n 
1 196 GLY n 
1 197 THR n 
1 198 TYR n 
1 199 VAL n 
1 200 SER n 
1 201 VAL n 
1 202 GLY n 
1 203 THR n 
1 204 SER n 
1 205 THR n 
1 206 LEU n 
1 207 ASN n 
1 208 LYS n 
1 209 ARG n 
1 210 SER n 
1 211 THR n 
1 212 PRO n 
1 213 GLU n 
1 214 ILE n 
1 215 ALA n 
1 216 THR n 
1 217 ARG n 
1 218 PRO n 
1 219 LYS n 
1 220 VAL n 
1 221 ASN n 
1 222 GLY n 
1 223 GLN n 
1 224 GLY n 
1 225 GLY n 
1 226 ARG n 
1 227 MET n 
1 228 GLU n 
1 229 PHE n 
1 230 SER n 
1 231 TRP n 
1 232 THR n 
1 233 LEU n 
1 234 LEU n 
1 235 ASP n 
1 236 MET n 
1 237 TRP n 
1 238 ASP n 
1 239 THR n 
1 240 ILE n 
1 241 ASN n 
1 242 PHE n 
1 243 GLU n 
1 244 SER n 
1 245 THR n 
1 246 GLY n 
1 247 ASN n 
1 248 LEU n 
1 249 ILE n 
1 250 ALA n 
1 251 PRO n 
1 252 GLU n 
1 253 TYR n 
1 254 GLY n 
1 255 PHE n 
1 256 LYS n 
1 257 ILE n 
1 258 SER n 
1 259 LYS n 
1 260 ARG n 
1 261 GLY n 
1 262 SER n 
1 263 SER n 
1 264 GLY n 
1 265 ILE n 
1 266 MET n 
1 267 LYS n 
1 268 THR n 
1 269 GLU n 
1 270 GLY n 
1 271 THR n 
1 272 LEU n 
1 273 GLU n 
1 274 ASN n 
1 275 CYS n 
1 276 GLU n 
1 277 THR n 
1 278 LYS n 
1 279 CYS n 
1 280 GLN n 
1 281 THR n 
1 282 PRO n 
1 283 LEU n 
1 284 GLY n 
1 285 ALA n 
1 286 ILE n 
1 287 ASN n 
1 288 THR n 
1 289 THR n 
1 290 LEU n 
1 291 PRO n 
1 292 PHE n 
1 293 HIS n 
1 294 ASN n 
1 295 VAL n 
1 296 HIS n 
1 297 PRO n 
1 298 LEU n 
1 299 THR n 
1 300 ILE n 
1 301 GLY n 
1 302 GLU n 
1 303 CYS n 
1 304 PRO n 
1 305 LYS n 
1 306 TYR n 
1 307 VAL n 
1 308 LYS n 
1 309 SER n 
1 310 GLU n 
1 311 LYS n 
1 312 LEU n 
1 313 VAL n 
1 314 LEU n 
1 315 ALA n 
1 316 THR n 
1 317 GLY n 
1 318 LEU n 
1 319 ARG n 
1 320 ASN n 
1 321 VAL n 
1 322 PRO n 
1 323 GLN n 
1 324 ILE n 
1 325 GLU n 
1 326 SER n 
1 327 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  GLN 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  SER n 
2 28  ASN n 
2 29  ASP 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  LYS n 
2 39  GLU n 
2 40  SER n 
2 41  THR n 
2 42  GLN n 
2 43  LYS n 
2 44  ALA n 
2 45  PHE n 
2 46  ASP n 
2 47  GLY 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  GLU 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  SER n 
2 72  ASN n 
2 73  LEU n 
2 74  GLU n 
2 75  ARG n 
2 76  ARG n 
2 77  LEU 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  MET n 
2 85  GLU n 
2 86  ASP n 
2 87  GLY n 
2 88  PHE n 
2 89  LEU n 
2 90  ASP n 
2 91  VAL 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 MET n 
2 103 GLU n 
2 104 ASN n 
2 105 GLU n 
2 106 HIS n 
2 107 THR n 
2 108 LEU n 
2 109 ASP n 
2 110 PHE 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 ASP n 
2 121 LYS n 
2 122 VAL n 
2 123 ARG n 
2 124 MET n 
2 125 GLN n 
2 126 LEU n 
2 127 ARG n 
2 128 ASP n 
2 129 ASN n 
2 130 VAL n 
2 131 LYS n 
2 132 GLU n 
2 133 LEU 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 ASP n 
2 147 GLU n 
2 148 CYS n 
2 149 MET n 
2 150 ASN 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 GLU n 
2 164 GLU n 
2 165 GLU n 
2 166 SER n 
2 167 LYS n 
2 168 LEU n 
2 169 ASN n 
2 170 ARG n 
2 171 ASN n 
2 172 GLU n 
2 173 ILE n 
2 174 LYS 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, hemagglutinin' ? 'A/Japan/305/1957 H2N2' ? ? ? ? 'Influenza A virus' 387161 ? ? ? ? ? ? ? ? 
'Trichoplusia ni' 7111 ? ? ? ? ? ? Hi5 ? ? ? ? ? ? ? Baculovirus ? ? ? pFASTbac-HT ? ? 
2 1 sample ? ? ? ? ? 'HA, hemagglutinin' ? 'A/Japan/305/1957 H2N2' ? ? ? ? 'Influenza A virus' 387161 ? ? ? ? ? ? ? ? 
'Trichoplusia ni' 7111 ? ? ? ? ? ? Hi5 ? ? ? ? ? ? ? Baculovirus ? ? ? pFASTbac-HT ? ? 
# 
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 C7S226_I57A0 C7S226 1 
;GDQICIGYHANNSTEKVDTILERNVTVTHAKDILEKTHNGKLCKLNGIPPLELGDCSIAGWLLGNPECDRLLSVPEWSYI
MEKENPRDGLCYPGSFNDYEELKHLLSSVKHFEKVKILPKDRWTQHTTTGGSRACAVSGNPSFFRNMVWLTEKGSNYPVA
KGSYNNTSGEQMLIIWGVHHPNDETEQRTLYQNVGTYVSVGTSTLNKRSTPEIATRPKVNGQGGRMEFSWTLLDMWDTIN
FESTGNLIAPEYGFKISKRGSSGIMKTEGTLENCETKCQTPLGAINTTLPFHNVHPLTIGECPKYVKSEKLVLATGLRNV
PQIESR
;
15  ? 
2 UNP C7S226_I57A0 C7S226 2 
;GLFGAIAGFIEGGWQGMVDGWYGYHHSNDQGSGYAADKESTQKAFDGITNKVNSVIEKMNTQFEAVGKEFSNLERRLENL
NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRMQLRDNVKELGNGCFEFYHKCDDECMNSVKNGTYDYP
KYEEESKLNRNEIK
;
341 ? 
# 
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 3QQO A 2 ? 327 ? C7S226 15  ? 340 ? 10 329 
2 2 3QQO B 1 ? 174 ? C7S226 341 ? 514 ? 1  174 
3 1 3QQO C 2 ? 326 ? C7S226 15  ? 340 ? 10 329 
4 2 3QQO D 1 ? 174 ? C7S226 341 ? 514 ? 1  174 
5 1 3QQO E 2 ? 327 ? C7S226 15  ? 340 ? 10 329 
6 2 3QQO F 1 ? 174 ? C7S226 341 ? 514 ? 1  174 
# 
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 3QQO PRO A 1   ? UNP C7S226 ?   ?   'EXPRESSION TAG'      9   1 
2 3QQO HIS B 106 ? UNP C7S226 ARG 446 'ENGINEERED MUTATION' 106 2 
3 3QQO PRO C 1   ? UNP C7S226 ?   ?   'EXPRESSION TAG'      9   3 
4 3QQO HIS D 106 ? UNP C7S226 ARG 446 'ENGINEERED MUTATION' 106 4 
5 3QQO PRO E 1   ? UNP C7S226 ?   ?   'EXPRESSION TAG'      9   5 
6 3QQO HIS F 106 ? UNP C7S226 ARG 446 'ENGINEERED MUTATION' 106 6 
# 
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.entry_id          3QQO 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.02 
_exptl_crystal.density_percent_sol   59.33 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            295.5 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              5.3 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '16% PEG 3000, 0.1M citric acid, pH 5.3, vapor diffusion, sitting drop, temperature 295.5K' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MARMOSAIC 325 mm CCD' 
_diffrn_detector.pdbx_collection_date   2009-05-21 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Side scattering bent cube-root I-beam single crystal' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97939 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRL BEAMLINE BL11-1' 
_diffrn_source.pdbx_synchrotron_site       SSRL 
_diffrn_source.pdbx_synchrotron_beamline   BL11-1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.97939 
# 
_reflns.entry_id                     3QQO 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             45.000 
_reflns.d_resolution_high            2.900 
_reflns.number_obs                   39294 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         88.400 
_reflns.pdbx_Rmerge_I_obs            0.078 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.300 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              3.400 
_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_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
2.900 3.000  46.900  0.322 ? ? 2.700 ? ? ? ? ? ? ? 1  
3.000 3.120  64.400  0.262 ? ? 2.900 ? ? ? ? ? ? ? 2  
3.120 3.270  81.900  0.217 ? ? 3.100 ? ? ? ? ? ? ? 3  
3.270 3.440  92.500  0.181 ? ? 3.300 ? ? ? ? ? ? ? 4  
3.440 3.650  98.400  0.134 ? ? 3.300 ? ? ? ? ? ? ? 5  
3.650 3.940  99.600  0.104 ? ? 3.500 ? ? ? ? ? ? ? 6  
3.940 4.330  100.000 0.080 ? ? 3.600 ? ? ? ? ? ? ? 7  
4.330 4.960  100.000 0.070 ? ? 3.600 ? ? ? ? ? ? ? 8  
4.960 6.240  100.000 0.065 ? ? 3.700 ? ? ? ? ? ? ? 9  
6.240 45.000 99.600  0.048 ? ? 3.600 ? ? ? ? ? ? ? 10 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 3QQO 
_refine.ls_number_reflns_obs                     39216 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.91 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             43.437 
_refine.ls_d_res_high                            2.900 
_refine.ls_percent_reflns_obs                    88.12 
_refine.ls_R_factor_obs                          0.2252 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2217 
_refine.ls_R_factor_R_free                       0.2896 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.08 
_refine.ls_number_reflns_R_free                  1991 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            0.410 
_refine.occupancy_max                            1.000 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            14.8786 
_refine.aniso_B[2][2]                            -27.5348 
_refine.aniso_B[3][3]                            13.1256 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            9.6520 
_refine.aniso_B[2][3]                            -0.0000 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 0.267 
_refine.solvent_model_param_bsol                 46.863 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.83 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.43 
_refine.pdbx_overall_phase_error                 34.50 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11736 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.number_atoms_solvent             56 
_refine_hist.number_atoms_total               11834 
_refine_hist.d_res_high                       2.900 
_refine_hist.d_res_low                        43.437 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.004  ? ? 12105 'X-RAY DIFFRACTION' ? 
f_angle_d          0.807  ? ? 16359 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 14.572 ? ? 4482  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.055  ? ? 1743  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.003  ? ? 2133  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' . 2.9000 3.0037  1944 0.3595 46.00  0.4689 . . 110 . . . . 
'X-RAY DIFFRACTION' . 3.0037 3.1239  2699 0.3010 64.00  0.4064 . . 128 . . . . 
'X-RAY DIFFRACTION' . 3.1239 3.2660  3434 0.2920 81.00  0.3540 . . 189 . . . . 
'X-RAY DIFFRACTION' . 3.2660 3.4381  3867 0.2855 92.00  0.3546 . . 225 . . . . 
'X-RAY DIFFRACTION' . 3.4381 3.6534  4135 0.2637 98.00  0.3234 . . 225 . . . . 
'X-RAY DIFFRACTION' . 3.6534 3.9354  4224 0.2352 100.00 0.3237 . . 215 . . . . 
'X-RAY DIFFRACTION' . 3.9354 4.3311  4210 0.2012 100.00 0.2749 . . 224 . . . . 
'X-RAY DIFFRACTION' . 4.3311 4.9570  4223 0.1740 100.00 0.2393 . . 229 . . . . 
'X-RAY DIFFRACTION' . 4.9570 6.2424  4234 0.1900 100.00 0.2687 . . 235 . . . . 
'X-RAY DIFFRACTION' . 6.2424 43.4417 4255 0.2090 99.00  0.2490 . . 211 . . . . 
# 
_struct.entry_id                  3QQO 
_struct.title                     'Crystal structure of HA2 R106H mutant of H2 hemagglutinin, acidic pH form' 
_struct.pdbx_descriptor           Hemagglutinin 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3QQO 
_struct_keywords.text            'viral envelope protein, hemagglutinin, viral fusion protein, 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 1 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
O 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  SER A 58  ? GLY A 65  ? SER A 65  GLY A 72  1 ? 8  
HELX_P HELX_P2  2  ASN A 66  ? ASP A 70  ? ASN A 73  ASP A 77  5 ? 5  
HELX_P HELX_P3  3  ASP A 99  ? LEU A 107 ? ASP A 104 LEU A 112 1 ? 9  
HELX_P HELX_P4  4  ASP A 184 ? GLN A 193 ? ASP A 187 GLN A 196 1 ? 10 
HELX_P HELX_P5  5  ASP B 37  ? THR B 49  ? ASP B 37  THR B 49  1 ? 13 
HELX_P HELX_P6  6  LYS B 51  ? ILE B 56  ? LYS B 51  ILE B 56  1 ? 6  
HELX_P HELX_P7  7  GLU B 74  ? ARG B 127 ? GLU B 74  ARG B 127 1 ? 54 
HELX_P HELX_P8  8  ASP B 145 ? ASN B 154 ? ASP B 145 ASN B 154 1 ? 10 
HELX_P HELX_P9  9  ASP B 158 ? GLU B 172 ? ASP B 158 GLU B 172 1 ? 15 
HELX_P HELX_P10 10 SER C 58  ? GLY C 65  ? SER C 65  GLY C 72  1 ? 8  
HELX_P HELX_P11 11 ASN C 66  ? ASP C 70  ? ASN C 73  ASP C 77  5 ? 5  
HELX_P HELX_P12 12 ASP C 99  ? SER C 108 ? ASP C 104 SER C 113 1 ? 10 
HELX_P HELX_P13 13 PRO C 120 ? TRP C 124 ? PRO C 122 TRP C 127 5 ? 5  
HELX_P HELX_P14 14 ASP C 184 ? GLN C 193 ? ASP C 187 GLN C 196 1 ? 10 
HELX_P HELX_P15 15 LYS C 219 ? GLN C 223 ? LYS C 222 GLN C 226 5 ? 5  
HELX_P HELX_P16 16 GLU D 39  ? LYS D 58  ? GLU D 39  LYS D 58  1 ? 20 
HELX_P HELX_P17 17 GLU D 74  ? ARG D 127 ? GLU D 74  ARG D 127 1 ? 54 
HELX_P HELX_P18 18 ASP D 145 ? ASN D 154 ? ASP D 145 ASN D 154 1 ? 10 
HELX_P HELX_P19 19 ASP D 158 ? GLU D 172 ? ASP D 158 GLU D 172 1 ? 15 
HELX_P HELX_P20 20 SER E 58  ? GLY E 65  ? SER E 65  GLY E 72  1 ? 8  
HELX_P HELX_P21 21 ASN E 66  ? ASP E 70  ? ASN E 73  ASP E 77  5 ? 5  
HELX_P HELX_P22 22 ASP E 99  ? LEU E 107 ? ASP E 104 LEU E 112 1 ? 9  
HELX_P HELX_P23 23 PRO E 120 ? TRP E 124 ? PRO E 122 TRP E 127 5 ? 5  
HELX_P HELX_P24 24 ASP E 184 ? GLN E 193 ? ASP E 187 GLN E 196 1 ? 10 
HELX_P HELX_P25 25 ASP F 37  ? LYS F 58  ? ASP F 37  LYS F 58  1 ? 22 
HELX_P HELX_P26 26 GLU F 74  ? ARG F 127 ? GLU F 74  ARG F 127 1 ? 54 
HELX_P HELX_P27 27 ASP F 145 ? ASN F 154 ? ASP F 145 ASN F 154 1 ? 10 
HELX_P HELX_P28 28 TYR F 159 ? LYS F 161 ? TYR F 159 LYS F 161 5 ? 3  
HELX_P HELX_P29 29 TYR F 162 ? ASN F 171 ? TYR F 162 ASN F 171 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 6   SG  ? ? ? 1_555 B CYS 137 SG ? ? A CYS 14  B CYS 137 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf2  disulf ? ? A CYS 44  SG  ? ? ? 1_555 A CYS 275 SG ? ? A CYS 52  A CYS 277 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf3  disulf ? ? A CYS 57  SG  ? ? ? 1_555 A CYS 69  SG ? ? A CYS 64  A CYS 76  1_555 ? ? ? ? ? ? ? 2.023 ? 
disulf4  disulf ? ? A CYS 92  SG  ? ? ? 1_555 A CYS 136 SG ? ? A CYS 97  A CYS 139 1_555 ? ? ? ? ? ? ? 2.062 ? 
disulf5  disulf ? ? A CYS 279 SG  ? ? ? 1_555 A CYS 303 SG ? ? A CYS 281 A CYS 305 1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf6  disulf ? ? B CYS 144 SG  ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf7  disulf ? ? C CYS 6   SG  ? ? ? 1_555 D CYS 137 SG ? ? C CYS 14  D CYS 137 1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf8  disulf ? ? C CYS 44  SG  ? ? ? 1_555 C CYS 275 SG ? ? C CYS 52  C CYS 278 1_555 ? ? ? ? ? ? ? 2.028 ? 
disulf9  disulf ? ? C CYS 57  SG  ? ? ? 1_555 C CYS 69  SG ? ? C CYS 64  C CYS 76  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf10 disulf ? ? C CYS 92  SG  ? ? ? 1_555 C CYS 136 SG ? ? C CYS 97  C CYS 139 1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf11 disulf ? ? C CYS 279 SG  ? ? ? 1_555 C CYS 303 SG ? ? C CYS 282 C CYS 306 1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf12 disulf ? ? D CYS 144 SG  ? ? ? 1_555 D CYS 148 SG ? ? D CYS 144 D CYS 148 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf13 disulf ? ? E CYS 6   SG  ? ? ? 1_555 F CYS 137 SG ? ? E CYS 14  F CYS 137 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf14 disulf ? ? E CYS 44  SG  ? ? ? 1_555 E CYS 275 SG ? ? E CYS 52  E CYS 277 1_555 ? ? ? ? ? ? ? 2.026 ? 
disulf15 disulf ? ? E CYS 57  SG  ? ? ? 1_555 E CYS 69  SG ? ? E CYS 64  E CYS 76  1_555 ? ? ? ? ? ? ? 2.033 ? 
disulf16 disulf ? ? E CYS 92  SG  ? ? ? 1_555 E CYS 136 SG ? ? E CYS 97  E CYS 139 1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf17 disulf ? ? E CYS 279 SG  ? ? ? 1_555 E CYS 303 SG ? ? E CYS 281 E CYS 305 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf18 disulf ? ? F CYS 144 SG  ? ? ? 1_555 F CYS 148 SG ? ? F CYS 144 F CYS 148 1_555 ? ? ? ? ? ? ? 2.031 ? 
covale1  covale ? ? A ASN 13  ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 21  A NAG 330 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale2  covale ? ? A ASN 166 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 169 A NAG 331 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale3  covale ? ? C ASN 287 ND2 ? ? ? 1_555 I NAG .   C1 ? ? C ASN 290 C NAG 331 1_555 ? ? ? ? ? ? ? 1.443 ? 
# 
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  ? 5 ? 
B  ? 2 ? 
C  ? 2 ? 
D  ? 3 ? 
E  ? 3 ? 
F  ? 5 ? 
G  ? 5 ? 
H  ? 2 ? 
I  ? 4 ? 
J  ? 4 ? 
K  ? 5 ? 
L  ? 2 ? 
M  ? 2 ? 
N  ? 3 ? 
O  ? 3 ? 
P  ? 5 ? 
Q  ? 5 ? 
R  ? 2 ? 
S  ? 4 ? 
T  ? 3 ? 
U  ? 5 ? 
V  ? 2 ? 
W  ? 2 ? 
X  ? 3 ? 
Y  ? 2 ? 
Z  ? 5 ? 
AA ? 4 ? 
AB ? 4 ? 
# 
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 
A  3 4 ? anti-parallel 
A  4 5 ? anti-parallel 
B  1 2 ? anti-parallel 
C  1 2 ? anti-parallel 
D  1 2 ? parallel      
D  2 3 ? parallel      
E  1 2 ? parallel      
E  2 3 ? parallel      
F  1 2 ? parallel      
F  2 3 ? anti-parallel 
F  3 4 ? anti-parallel 
F  4 5 ? anti-parallel 
G  1 2 ? parallel      
G  2 3 ? anti-parallel 
G  3 4 ? anti-parallel 
G  4 5 ? anti-parallel 
H  1 2 ? anti-parallel 
I  1 2 ? anti-parallel 
I  2 3 ? anti-parallel 
I  3 4 ? 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 
K  3 4 ? anti-parallel 
K  4 5 ? anti-parallel 
L  1 2 ? anti-parallel 
M  1 2 ? anti-parallel 
N  1 2 ? parallel      
N  2 3 ? parallel      
O  1 2 ? parallel      
O  2 3 ? parallel      
P  1 2 ? parallel      
P  2 3 ? anti-parallel 
P  3 4 ? anti-parallel 
P  4 5 ? anti-parallel 
Q  1 2 ? parallel      
Q  2 3 ? anti-parallel 
Q  3 4 ? anti-parallel 
Q  4 5 ? anti-parallel 
R  1 2 ? anti-parallel 
S  1 2 ? anti-parallel 
S  2 3 ? anti-parallel 
S  3 4 ? anti-parallel 
T  1 2 ? anti-parallel 
T  2 3 ? anti-parallel 
U  1 2 ? anti-parallel 
U  2 3 ? anti-parallel 
U  3 4 ? anti-parallel 
U  4 5 ? anti-parallel 
V  1 2 ? anti-parallel 
W  1 2 ? anti-parallel 
X  1 2 ? parallel      
X  2 3 ? parallel      
Y  1 2 ? parallel      
Z  1 2 ? parallel      
Z  2 3 ? anti-parallel 
Z  3 4 ? anti-parallel 
Z  4 5 ? anti-parallel 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AB 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A  1 GLY B 33  ? ALA B 36  ? GLY B 33  ALA B 36  
A  2 TYR B 22  ? HIS B 26  ? TYR B 22  HIS B 26  
A  3 GLN A 4   ? TYR A 9   ? GLN A 12  TYR A 17  
A  4 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 
A  5 VAL B 130 ? LYS B 131 ? VAL B 130 LYS B 131 
B  1 LYS A 17  ? VAL A 18  ? LYS A 25  VAL A 26  
B  2 VAL A 26  ? THR A 27  ? VAL A 34  THR A 35  
C  1 ALA A 31  ? ASP A 33  ? ALA A 39  ASP A 41  
C  2 VAL A 313 ? ALA A 315 ? VAL A 315 ALA A 317 
D  1 LEU A 35  ? GLU A 36  ? LEU A 43  GLU A 44  
D  2 PHE A 292 ? HIS A 293 ? PHE A 294 HIS A 295 
D  3 LYS A 305 ? TYR A 306 ? LYS A 307 TYR A 308 
E  1 LEU A 52  ? GLU A 53  ? LEU A 59  GLU A 60  
E  2 ILE A 81  ? GLU A 83  ? ILE A 87  GLU A 89  
E  3 ILE A 265 ? LYS A 267 ? ILE A 267 LYS A 269 
F  1 GLY A 95  ? PHE A 97  ? GLY A 100 PHE A 102 
F  2 ARG A 226 ? LEU A 234 ? ARG A 229 LEU A 237 
F  3 MET A 173 ? HIS A 181 ? MET A 176 HIS A 184 
F  4 TYR A 253 ? SER A 258 ? TYR A 256 SER A 261 
F  5 HIS A 112 A LYS A 117 ? HIS A 116 LYS A 119 
G  1 GLY A 95  ? PHE A 97  ? GLY A 100 PHE A 102 
G  2 ARG A 226 ? LEU A 234 ? ARG A 229 LEU A 237 
G  3 MET A 173 ? HIS A 181 ? MET A 176 HIS A 184 
G  4 LEU A 248 ? PRO A 251 ? LEU A 251 PRO A 254 
G  5 MET A 148 ? TRP A 150 ? MET A 151 TRP A 153 
H  1 SER A 133 ? VAL A 138 ? SER A 136 VAL A 141 
H  2 ASN A 141 ? SER A 143 ? ASN A 144 SER A 146 
I  1 ALA A 161 ? ASN A 166 ? ALA A 164 ASN A 169 
I  2 THR A 239 ? SER A 244 ? THR A 242 SER A 247 
I  3 VAL A 199 ? GLY A 202 ? VAL A 202 GLY A 205 
I  4 ASN A 207 ? SER A 210 ? ASN A 210 SER A 213 
J  1 GLY A 284 ? ILE A 286 ? GLY A 286 ILE A 288 
J  2 CYS A 279 ? THR A 281 ? CYS A 281 THR A 283 
J  3 ILE A 300 ? GLU A 302 ? ILE A 302 GLU A 304 
J  4 PHE B 63  ? ALA B 65  ? PHE B 63  ALA B 65  
K  1 GLY D 31  ? ALA D 36  ? GLY D 31  ALA D 36  
K  2 TYR D 22  ? ASN D 28  ? TYR D 22  ASN D 28  
K  3 GLN C 4   ? TYR C 9   ? GLN C 12  TYR C 17  
K  4 CYS D 137 ? PHE D 140 ? CYS D 137 PHE D 140 
K  5 VAL D 130 ? GLU D 132 ? VAL D 130 GLU D 132 
L  1 LYS C 17  ? VAL C 18  ? LYS C 25  VAL C 26  
L  2 VAL C 26  ? THR C 27  ? VAL C 34  THR C 35  
M  1 ALA C 31  ? ASP C 33  ? ALA C 39  ASP C 41  
M  2 VAL C 313 ? ALA C 315 ? VAL C 316 ALA C 318 
N  1 LEU C 35  ? GLU C 36  ? LEU C 43  GLU C 44  
N  2 PHE C 292 ? HIS C 293 ? PHE C 295 HIS C 296 
N  3 LYS C 305 ? TYR C 306 ? LYS C 308 TYR C 309 
O  1 LEU C 52  ? GLU C 53  ? LEU C 59  GLU C 60  
O  2 ILE C 81  ? GLU C 83  ? ILE C 87  GLU C 89  
O  3 ILE C 265 ? LYS C 267 ? ILE C 268 LYS C 270 
P  1 GLY C 95  ? PHE C 97  ? GLY C 100 PHE C 102 
P  2 ARG C 226 ? LEU C 234 ? ARG C 229 LEU C 237 
P  3 MET C 173 ? HIS C 181 ? MET C 176 HIS C 184 
P  4 TYR C 253 ? SER C 258 ? TYR C 256 SER C 261 
P  5 HIS C 112 A LYS C 117 ? HIS C 116 LYS C 119 
Q  1 GLY C 95  ? PHE C 97  ? GLY C 100 PHE C 102 
Q  2 ARG C 226 ? LEU C 234 ? ARG C 229 LEU C 237 
Q  3 MET C 173 ? HIS C 181 ? MET C 176 HIS C 184 
Q  4 LEU C 248 ? PRO C 251 ? LEU C 251 PRO C 254 
Q  5 MET C 148 ? VAL C 149 ? MET C 151 VAL C 152 
R  1 SER C 133 ? VAL C 138 ? SER C 136 VAL C 141 
R  2 ASN C 141 ? SER C 143 ? ASN C 144 SER C 146 
S  1 ALA C 161 ? GLY C 163 ? ALA C 164 GLY C 166 
S  2 ASN C 241 ? SER C 244 ? ASN C 244 SER C 247 
S  3 VAL C 199 ? GLY C 202 ? VAL C 202 GLY C 205 
S  4 ASN C 207 ? SER C 210 ? ASN C 210 SER C 213 
T  1 CYS C 279 ? GLN C 280 ? CYS C 282 GLN C 283 
T  2 ILE C 300 ? GLY C 301 ? ILE C 303 GLY C 304 
T  3 GLU D 64  ? ALA D 65  ? GLU D 64  ALA D 65  
U  1 SER F 32  ? ALA F 36  ? SER F 32  ALA F 36  
U  2 TYR F 22  ? SER F 27  ? TYR F 22  SER F 27  
U  3 GLN E 4   ? TYR E 9   ? GLN E 12  TYR E 17  
U  4 CYS F 137 ? PHE F 140 ? CYS F 137 PHE F 140 
U  5 VAL F 130 ? GLU F 132 ? VAL F 130 GLU F 132 
V  1 LYS E 17  ? VAL E 18  ? LYS E 25  VAL E 26  
V  2 VAL E 26  ? THR E 27  ? VAL E 34  THR E 35  
W  1 ALA E 31  ? ASP E 33  ? ALA E 39  ASP E 41  
W  2 VAL E 313 ? ALA E 315 ? VAL E 315 ALA E 317 
X  1 LEU E 35  ? GLU E 36  ? LEU E 43  GLU E 44  
X  2 PHE E 292 ? HIS E 293 ? PHE E 294 HIS E 295 
X  3 LYS E 305 ? TYR E 306 ? LYS E 307 TYR E 308 
Y  1 ILE E 81  ? MET E 82  ? ILE E 87  MET E 88  
Y  2 ILE E 265 ? MET E 266 ? ILE E 267 MET E 268 
Z  1 GLY E 95  ? PHE E 97  ? GLY E 100 PHE E 102 
Z  2 ARG E 226 ? LEU E 234 ? ARG E 229 LEU E 237 
Z  3 GLN E 172 ? HIS E 181 ? GLN E 175 HIS E 184 
Z  4 TYR E 253 ? SER E 258 ? TYR E 256 SER E 261 
Z  5 HIS E 112 A LYS E 117 ? HIS E 116 LYS E 119 
AA 1 ALA E 161 ? ASN E 166 ? ALA E 164 ASN E 169 
AA 2 THR E 239 ? SER E 244 ? THR E 242 SER E 247 
AA 3 VAL E 199 ? GLY E 202 ? VAL E 202 GLY E 205 
AA 4 ASN E 207 ? SER E 210 ? ASN E 210 SER E 213 
AB 1 GLY E 284 ? ALA E 285 ? GLY E 286 ALA E 287 
AB 2 CYS E 279 ? THR E 281 ? CYS E 281 THR E 283 
AB 3 ILE E 300 ? GLY E 301 ? ILE E 302 GLY E 303 
AB 4 GLU F 64  ? ALA F 65  ? GLU F 64  ALA F 65  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A  1 2 O ALA B 35  ? O ALA B 35  N TYR B 24  ? N TYR B 24  
A  2 3 O GLY B 23  ? O GLY B 23  N GLY A 8   ? N GLY A 16  
A  3 4 N ILE A 5   ? N ILE A 13  O PHE B 138 ? O PHE B 138 
A  4 5 O GLU B 139 ? O GLU B 139 N LYS B 131 ? N LYS B 131 
B  1 2 N VAL A 18  ? N VAL A 26  O VAL A 26  ? O VAL A 34  
C  1 2 N LYS A 32  ? N LYS A 40  O LEU A 314 ? O LEU A 316 
D  1 2 N GLU A 36  ? N GLU A 44  O PHE A 292 ? O PHE A 294 
D  2 3 N HIS A 293 ? N HIS A 295 O LYS A 305 ? O LYS A 307 
E  1 2 N LEU A 52  ? N LEU A 59  O MET A 82  ? O MET A 88  
E  2 3 N ILE A 81  ? N ILE A 87  O MET A 266 ? O MET A 268 
F  1 2 N SER A 96  ? N SER A 101 O PHE A 229 ? O PHE A 232 
F  2 3 O SER A 230 ? O SER A 233 N TRP A 177 ? N TRP A 180 
F  3 4 N LEU A 174 ? N LEU A 177 O PHE A 255 ? O PHE A 258 
F  4 5 O GLY A 254 ? O GLY A 257 N VAL A 116 ? N VAL A 118 
G  1 2 N SER A 96  ? N SER A 101 O PHE A 229 ? O PHE A 232 
G  2 3 O SER A 230 ? O SER A 233 N TRP A 177 ? N TRP A 180 
G  3 4 N GLY A 178 ? N GLY A 181 O ILE A 249 ? O ILE A 252 
G  4 5 O ALA A 250 ? O ALA A 253 N VAL A 149 ? N VAL A 152 
H  1 2 N VAL A 138 ? N VAL A 141 O ASN A 141 ? O ASN A 144 
I  1 2 N GLY A 163 ? N GLY A 166 O PHE A 242 ? O PHE A 245 
I  2 3 O GLU A 243 ? O GLU A 246 N SER A 200 ? N SER A 203 
I  3 4 N VAL A 199 ? N VAL A 202 O SER A 210 ? O SER A 213 
J  1 2 O ILE A 286 ? O ILE A 288 N CYS A 279 ? N CYS A 281 
J  2 3 N GLN A 280 ? N GLN A 282 O ILE A 300 ? O ILE A 302 
J  3 4 N GLY A 301 ? N GLY A 303 O GLU B 64  ? O GLU B 64  
K  1 2 O ALA D 35  ? O ALA D 35  N TYR D 24  ? N TYR D 24  
K  2 3 O HIS D 25  ? O HIS D 25  N CYS C 6   ? N CYS C 14  
K  3 4 N ILE C 5   ? N ILE C 13  O PHE D 138 ? O PHE D 138 
K  4 5 O GLU D 139 ? O GLU D 139 N LYS D 131 ? N LYS D 131 
L  1 2 N VAL C 18  ? N VAL C 26  O VAL C 26  ? O VAL C 34  
M  1 2 N LYS C 32  ? N LYS C 40  O LEU C 314 ? O LEU C 317 
N  1 2 N GLU C 36  ? N GLU C 44  O PHE C 292 ? O PHE C 295 
N  2 3 N HIS C 293 ? N HIS C 296 O LYS C 305 ? O LYS C 308 
O  1 2 N LEU C 52  ? N LEU C 59  O MET C 82  ? O MET C 88  
O  2 3 N ILE C 81  ? N ILE C 87  O MET C 266 ? O MET C 269 
P  1 2 N SER C 96  ? N SER C 101 O PHE C 229 ? O PHE C 232 
P  2 3 O SER C 230 ? O SER C 233 N TRP C 177 ? N TRP C 180 
P  3 4 N LEU C 174 ? N LEU C 177 O PHE C 255 ? O PHE C 258 
P  4 5 O GLY C 254 ? O GLY C 257 N VAL C 116 ? N VAL C 118 
Q  1 2 N SER C 96  ? N SER C 101 O PHE C 229 ? O PHE C 232 
Q  2 3 O SER C 230 ? O SER C 233 N TRP C 177 ? N TRP C 180 
Q  3 4 N GLY C 178 ? N GLY C 181 O ILE C 249 ? O ILE C 252 
Q  4 5 N ALA C 250 ? N ALA C 253 O VAL C 149 ? O VAL C 152 
R  1 2 N SER C 133 ? N SER C 136 O SER C 143 ? O SER C 146 
S  1 2 N GLY C 163 ? N GLY C 166 O PHE C 242 ? O PHE C 245 
S  2 3 O ASN C 241 ? O ASN C 244 N GLY C 202 ? N GLY C 205 
S  3 4 N VAL C 201 ? N VAL C 204 O LYS C 208 ? O LYS C 211 
T  1 2 N GLN C 280 ? N GLN C 283 O ILE C 300 ? O ILE C 303 
T  2 3 N GLY C 301 ? N GLY C 304 O GLU D 64  ? O GLU D 64  
U  1 2 O ALA F 35  ? O ALA F 35  N TYR F 24  ? N TYR F 24  
U  2 3 O GLY F 23  ? O GLY F 23  N GLY E 8   ? N GLY E 16  
U  3 4 N ILE E 5   ? N ILE E 13  O PHE F 138 ? O PHE F 138 
U  4 5 O GLU F 139 ? O GLU F 139 N LYS F 131 ? N LYS F 131 
V  1 2 N VAL E 18  ? N VAL E 26  O VAL E 26  ? O VAL E 34  
W  1 2 N LYS E 32  ? N LYS E 40  O LEU E 314 ? O LEU E 316 
X  1 2 N GLU E 36  ? N GLU E 44  O PHE E 292 ? O PHE E 294 
X  2 3 N HIS E 293 ? N HIS E 295 O LYS E 305 ? O LYS E 307 
Y  1 2 N ILE E 81  ? N ILE E 87  O MET E 266 ? O MET E 268 
Z  1 2 N SER E 96  ? N SER E 101 O PHE E 229 ? O PHE E 232 
Z  2 3 O LEU E 234 ? O LEU E 237 N MET E 173 ? N MET E 176 
Z  3 4 N LEU E 174 ? N LEU E 177 O PHE E 255 ? O PHE E 258 
Z  4 5 O GLY E 254 ? O GLY E 257 N VAL E 116 ? N VAL E 118 
AA 1 2 N GLY E 163 ? N GLY E 166 O PHE E 242 ? O PHE E 245 
AA 2 3 O GLU E 243 ? O GLU E 246 N SER E 200 ? N SER E 203 
AA 3 4 N VAL E 201 ? N VAL E 204 O LYS E 208 ? O LYS E 211 
AB 1 2 O GLY E 284 ? O GLY E 286 N THR E 281 ? N THR E 283 
AB 2 3 N GLN E 280 ? N GLN E 282 O ILE E 300 ? O ILE E 302 
AB 3 4 N GLY E 301 ? N GLY E 303 O GLU F 64  ? O GLU F 64  
# 
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 ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 330' 
AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 331' 
AC3 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG C 331' 
# 
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 1 ASN A 13  ? ASN A 21  . ? 1_555 ? 
2 AC2 2 ASN A 166 ? ASN A 169 . ? 1_555 ? 
3 AC2 2 THR A 239 ? THR A 242 . ? 1_555 ? 
4 AC3 1 ASN C 287 ? ASN C 290 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3QQO 
_atom_sites.fract_transf_matrix[1][1]   0.014706 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007339 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.004165 
_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]   0.015890 
_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   . PRO A 1 1   ? -5.973  53.628  34.118  1.00 144.23 ? 9   PRO A N   1 
ATOM   2     C CA  . PRO A 1 1   ? -6.091  52.166  34.145  1.00 143.00 ? 9   PRO A CA  1 
ATOM   3     C C   . PRO A 1 1   ? -5.645  51.530  32.831  1.00 135.87 ? 9   PRO A C   1 
ATOM   4     O O   . PRO A 1 1   ? -4.706  52.012  32.199  1.00 132.91 ? 9   PRO A O   1 
ATOM   5     C CB  . PRO A 1 1   ? -7.590  51.948  34.355  1.00 151.76 ? 9   PRO A CB  1 
ATOM   6     C CG  . PRO A 1 1   ? -8.034  53.156  35.110  1.00 157.23 ? 9   PRO A CG  1 
ATOM   7     C CD  . PRO A 1 1   ? -7.205  54.293  34.580  1.00 152.06 ? 9   PRO A CD  1 
ATOM   8     N N   . GLY A 1 2   ? -6.319  50.456  32.432  1.00 180.03 ? 10  GLY A N   1 
ATOM   9     C CA  . GLY A 1 2   ? -5.979  49.745  31.212  1.00 168.72 ? 10  GLY A CA  1 
ATOM   10    C C   . GLY A 1 2   ? -6.049  48.239  31.393  1.00 164.68 ? 10  GLY A C   1 
ATOM   11    O O   . GLY A 1 2   ? -5.080  47.610  31.817  1.00 158.05 ? 10  GLY A O   1 
ATOM   12    N N   . ASP A 1 3   ? -7.203  47.663  31.068  1.00 91.84  ? 11  ASP A N   1 
ATOM   13    C CA  . ASP A 1 3   ? -7.431  46.224  31.221  1.00 93.44  ? 11  ASP A CA  1 
ATOM   14    C C   . ASP A 1 3   ? -6.491  45.372  30.363  1.00 85.42  ? 11  ASP A C   1 
ATOM   15    O O   . ASP A 1 3   ? -5.926  45.846  29.377  1.00 76.35  ? 11  ASP A O   1 
ATOM   16    C CB  . ASP A 1 3   ? -8.884  45.879  30.889  1.00 101.12 ? 11  ASP A CB  1 
ATOM   17    C CG  . ASP A 1 3   ? -9.871  46.582  31.798  1.00 110.80 ? 11  ASP A CG  1 
ATOM   18    O OD1 . ASP A 1 3   ? -9.532  46.815  32.978  1.00 113.62 ? 11  ASP A OD1 1 
ATOM   19    O OD2 . ASP A 1 3   ? -10.985 46.900  31.332  1.00 116.66 ? 11  ASP A OD2 1 
ATOM   20    N N   . GLN A 1 4   ? -6.333  44.108  30.745  1.00 139.28 ? 12  GLN A N   1 
ATOM   21    C CA  . GLN A 1 4   ? -5.433  43.206  30.033  1.00 133.21 ? 12  GLN A CA  1 
ATOM   22    C C   . GLN A 1 4   ? -6.034  41.825  29.792  1.00 130.30 ? 12  GLN A C   1 
ATOM   23    O O   . GLN A 1 4   ? -6.973  41.409  30.474  1.00 133.59 ? 12  GLN A O   1 
ATOM   24    C CB  . GLN A 1 4   ? -4.112  43.051  30.791  1.00 129.85 ? 12  GLN A CB  1 
ATOM   25    C CG  . GLN A 1 4   ? -3.217  44.274  30.774  1.00 125.34 ? 12  GLN A CG  1 
ATOM   26    C CD  . GLN A 1 4   ? -1.944  44.062  31.571  1.00 123.21 ? 12  GLN A CD  1 
ATOM   27    O OE1 . GLN A 1 4   ? -1.665  42.955  32.028  1.00 120.60 ? 12  GLN A OE1 1 
ATOM   28    N NE2 . GLN A 1 4   ? -1.168  45.126  31.745  1.00 124.58 ? 12  GLN A NE2 1 
ATOM   29    N N   . ILE A 1 5   ? -5.472  41.127  28.809  1.00 109.34 ? 13  ILE A N   1 
ATOM   30    C CA  . ILE A 1 5   ? -5.772  39.721  28.554  1.00 105.67 ? 13  ILE A CA  1 
ATOM   31    C C   . ILE A 1 5   ? -4.463  39.014  28.212  1.00 98.44  ? 13  ILE A C   1 
ATOM   32    O O   . ILE A 1 5   ? -3.687  39.490  27.383  1.00 94.83  ? 13  ILE A O   1 
ATOM   33    C CB  . ILE A 1 5   ? -6.787  39.543  27.402  1.00 101.53 ? 13  ILE A CB  1 
ATOM   34    C CG1 . ILE A 1 5   ? -7.266  38.096  27.321  1.00 88.32  ? 13  ILE A CG1 1 
ATOM   35    C CG2 . ILE A 1 5   ? -6.186  39.976  26.071  1.00 100.16 ? 13  ILE A CG2 1 
ATOM   36    C CD1 . ILE A 1 5   ? -8.168  37.840  26.137  1.00 85.17  ? 13  ILE A CD1 1 
ATOM   37    N N   . CYS A 1 6   ? -4.204  37.886  28.859  1.00 102.85 ? 14  CYS A N   1 
ATOM   38    C CA  . CYS A 1 6   ? -2.918  37.220  28.686  1.00 95.29  ? 14  CYS A CA  1 
ATOM   39    C C   . CYS A 1 6   ? -3.030  35.801  28.121  1.00 91.83  ? 14  CYS A C   1 
ATOM   40    O O   . CYS A 1 6   ? -4.081  35.167  28.199  1.00 94.62  ? 14  CYS A O   1 
ATOM   41    C CB  . CYS A 1 6   ? -2.133  37.232  30.002  1.00 97.81  ? 14  CYS A CB  1 
ATOM   42    S SG  . CYS A 1 6   ? -1.800  38.900  30.632  1.00 84.84  ? 14  CYS A SG  1 
ATOM   43    N N   . ILE A 1 7   ? -1.934  35.323  27.538  1.00 102.77 ? 15  ILE A N   1 
ATOM   44    C CA  . ILE A 1 7   ? -1.881  33.996  26.939  1.00 99.54  ? 15  ILE A CA  1 
ATOM   45    C C   . ILE A 1 7   ? -0.777  33.189  27.606  1.00 96.30  ? 15  ILE A C   1 
ATOM   46    O O   . ILE A 1 7   ? 0.371   33.630  27.664  1.00 93.51  ? 15  ILE A O   1 
ATOM   47    C CB  . ILE A 1 7   ? -1.583  34.077  25.433  1.00 99.57  ? 15  ILE A CB  1 
ATOM   48    C CG1 . ILE A 1 7   ? -2.410  35.186  24.777  1.00 102.68 ? 15  ILE A CG1 1 
ATOM   49    C CG2 . ILE A 1 7   ? -1.823  32.728  24.770  1.00 102.50 ? 15  ILE A CG2 1 
ATOM   50    C CD1 . ILE A 1 7   ? -3.906  35.006  24.919  1.00 109.56 ? 15  ILE A CD1 1 
ATOM   51    N N   . GLY A 1 8   ? -1.119  32.009  28.112  1.00 123.63 ? 16  GLY A N   1 
ATOM   52    C CA  . GLY A 1 8   ? -0.151  31.187  28.818  1.00 122.25 ? 16  GLY A CA  1 
ATOM   53    C C   . GLY A 1 8   ? -0.383  29.696  28.673  1.00 124.81 ? 16  GLY A C   1 
ATOM   54    O O   . GLY A 1 8   ? -1.287  29.256  27.963  1.00 129.89 ? 16  GLY A O   1 
ATOM   55    N N   . TYR A 1 9   ? 0.441   28.909  29.354  1.00 86.35  ? 17  TYR A N   1 
ATOM   56    C CA  . TYR A 1 9   ? 0.335   27.462  29.268  1.00 84.36  ? 17  TYR A CA  1 
ATOM   57    C C   . TYR A 1 9   ? 0.244   26.804  30.635  1.00 90.06  ? 17  TYR A C   1 
ATOM   58    O O   . TYR A 1 9   ? 0.666   27.372  31.645  1.00 84.96  ? 17  TYR A O   1 
ATOM   59    C CB  . TYR A 1 9   ? 1.501   26.872  28.473  1.00 80.57  ? 17  TYR A CB  1 
ATOM   60    C CG  . TYR A 1 9   ? 2.842   27.498  28.776  1.00 82.85  ? 17  TYR A CG  1 
ATOM   61    C CD1 . TYR A 1 9   ? 3.631   27.042  29.823  1.00 80.46  ? 17  TYR A CD1 1 
ATOM   62    C CD2 . TYR A 1 9   ? 3.324   28.540  28.000  1.00 85.10  ? 17  TYR A CD2 1 
ATOM   63    C CE1 . TYR A 1 9   ? 4.859   27.615  30.088  1.00 80.22  ? 17  TYR A CE1 1 
ATOM   64    C CE2 . TYR A 1 9   ? 4.545   29.121  28.257  1.00 82.75  ? 17  TYR A CE2 1 
ATOM   65    C CZ  . TYR A 1 9   ? 5.310   28.660  29.299  1.00 80.77  ? 17  TYR A CZ  1 
ATOM   66    O OH  . TYR A 1 9   ? 6.528   29.258  29.537  1.00 79.35  ? 17  TYR A OH  1 
ATOM   67    N N   . HIS A 1 10  ? -0.312  25.597  30.646  1.00 76.82  ? 18  HIS A N   1 
ATOM   68    C CA  . HIS A 1 10  ? -0.480  24.814  31.857  1.00 81.08  ? 18  HIS A CA  1 
ATOM   69    C C   . HIS A 1 10  ? 0.848   24.668  32.576  1.00 71.83  ? 18  HIS A C   1 
ATOM   70    O O   . HIS A 1 10  ? 1.909   24.904  32.001  1.00 70.73  ? 18  HIS A O   1 
ATOM   71    C CB  . HIS A 1 10  ? -1.022  23.432  31.495  1.00 96.65  ? 18  HIS A CB  1 
ATOM   72    C CG  . HIS A 1 10  ? -1.435  22.610  32.676  1.00 118.40 ? 18  HIS A CG  1 
ATOM   73    N ND1 . HIS A 1 10  ? -2.689  22.698  33.243  1.00 129.50 ? 18  HIS A ND1 1 
ATOM   74    C CD2 . HIS A 1 10  ? -0.766  21.674  33.390  1.00 126.50 ? 18  HIS A CD2 1 
ATOM   75    C CE1 . HIS A 1 10  ? -2.772  21.857  34.258  1.00 137.38 ? 18  HIS A CE1 1 
ATOM   76    N NE2 . HIS A 1 10  ? -1.618  21.224  34.369  1.00 135.45 ? 18  HIS A NE2 1 
ATOM   77    N N   . ALA A 1 11  ? 0.780   24.286  33.844  1.00 58.78  ? 19  ALA A N   1 
ATOM   78    C CA  . ALA A 1 11  ? 1.963   23.906  34.610  1.00 58.30  ? 19  ALA A CA  1 
ATOM   79    C C   . ALA A 1 11  ? 1.519   23.077  35.811  1.00 66.59  ? 19  ALA A C   1 
ATOM   80    O O   . ALA A 1 11  ? 0.333   23.051  36.146  1.00 74.32  ? 19  ALA A O   1 
ATOM   81    C CB  . ALA A 1 11  ? 2.748   25.132  35.052  1.00 54.06  ? 19  ALA A CB  1 
ATOM   82    N N   . ASN A 1 12  ? 2.458   22.388  36.449  1.00 78.84  ? 20  ASN A N   1 
ATOM   83    C CA  . ASN A 1 12  ? 2.128   21.611  37.640  1.00 90.71  ? 20  ASN A CA  1 
ATOM   84    C C   . ASN A 1 12  ? 3.340   21.231  38.489  1.00 99.48  ? 20  ASN A C   1 
ATOM   85    O O   . ASN A 1 12  ? 4.443   21.734  38.274  1.00 98.21  ? 20  ASN A O   1 
ATOM   86    C CB  . ASN A 1 12  ? 1.280   20.376  37.284  1.00 91.74  ? 20  ASN A CB  1 
ATOM   87    C CG  . ASN A 1 12  ? 1.913   19.509  36.203  1.00 87.11  ? 20  ASN A CG  1 
ATOM   88    O OD1 . ASN A 1 12  ? 3.120   19.263  36.207  1.00 87.20  ? 20  ASN A OD1 1 
ATOM   89    N ND2 . ASN A 1 12  ? 1.091   19.041  35.269  1.00 82.07  ? 20  ASN A ND2 1 
ATOM   90    N N   . ASN A 1 13  ? 3.120   20.352  39.461  1.00 134.90 ? 21  ASN A N   1 
ATOM   91    C CA  . ASN A 1 13  ? 4.181   19.921  40.362  1.00 141.44 ? 21  ASN A CA  1 
ATOM   92    C C   . ASN A 1 13  ? 4.804   18.596  39.934  1.00 133.15 ? 21  ASN A C   1 
ATOM   93    O O   . ASN A 1 13  ? 5.093   17.740  40.767  1.00 135.85 ? 21  ASN A O   1 
ATOM   94    C CB  . ASN A 1 13  ? 3.665   19.837  41.804  1.00 158.01 ? 21  ASN A CB  1 
ATOM   95    C CG  . ASN A 1 13  ? 2.407   18.992  41.932  1.00 172.69 ? 21  ASN A CG  1 
ATOM   96    O OD1 . ASN A 1 13  ? 1.743   18.683  40.942  1.00 168.58 ? 21  ASN A OD1 1 
ATOM   97    N ND2 . ASN A 1 13  ? 2.068   18.624  43.164  1.00 192.36 ? 21  ASN A ND2 1 
ATOM   98    N N   . SER A 1 14  ? 5.018   18.441  38.631  1.00 102.86 ? 22  SER A N   1 
ATOM   99    C CA  . SER A 1 14  ? 5.582   17.211  38.083  1.00 94.92  ? 22  SER A CA  1 
ATOM   100   C C   . SER A 1 14  ? 7.109   17.223  38.059  1.00 86.88  ? 22  SER A C   1 
ATOM   101   O O   . SER A 1 14  ? 7.734   18.279  38.172  1.00 89.91  ? 22  SER A O   1 
ATOM   102   C CB  . SER A 1 14  ? 5.047   16.970  36.672  1.00 93.45  ? 22  SER A CB  1 
ATOM   103   O OG  . SER A 1 14  ? 5.783   15.950  36.022  1.00 92.36  ? 22  SER A OG  1 
ATOM   104   N N   . THR A 1 15  ? 7.701   16.041  37.907  1.00 83.18  ? 23  THR A N   1 
ATOM   105   C CA  . THR A 1 15  ? 9.154   15.908  37.826  1.00 80.79  ? 23  THR A CA  1 
ATOM   106   C C   . THR A 1 15  ? 9.585   14.891  36.760  1.00 80.34  ? 23  THR A C   1 
ATOM   107   O O   . THR A 1 15  ? 10.765  14.536  36.662  1.00 72.27  ? 23  THR A O   1 
ATOM   108   C CB  . THR A 1 15  ? 9.779   15.526  39.190  1.00 80.58  ? 23  THR A CB  1 
ATOM   109   O OG1 . THR A 1 15  ? 9.087   14.395  39.742  1.00 78.69  ? 23  THR A OG1 1 
ATOM   110   C CG2 . THR A 1 15  ? 9.695   16.693  40.159  1.00 79.30  ? 23  THR A CG2 1 
ATOM   111   N N   . GLU A 1 16  ? 8.623   14.425  35.970  1.00 88.58  ? 24  GLU A N   1 
ATOM   112   C CA  . GLU A 1 16  ? 8.919   13.532  34.859  1.00 86.82  ? 24  GLU A CA  1 
ATOM   113   C C   . GLU A 1 16  ? 9.974   14.170  33.959  1.00 80.83  ? 24  GLU A C   1 
ATOM   114   O O   . GLU A 1 16  ? 9.702   15.146  33.264  1.00 82.14  ? 24  GLU A O   1 
ATOM   115   C CB  . GLU A 1 16  ? 7.648   13.236  34.058  1.00 94.78  ? 24  GLU A CB  1 
ATOM   116   C CG  . GLU A 1 16  ? 6.713   12.223  34.698  1.00 105.99 ? 24  GLU A CG  1 
ATOM   117   C CD  . GLU A 1 16  ? 7.183   10.788  34.502  1.00 109.93 ? 24  GLU A CD  1 
ATOM   118   O OE1 . GLU A 1 16  ? 8.295   10.589  33.957  1.00 104.58 ? 24  GLU A OE1 1 
ATOM   119   O OE2 . GLU A 1 16  ? 6.438   9.859   34.890  1.00 113.73 ? 24  GLU A OE2 1 
ATOM   120   N N   . LYS A 1 17  ? 11.184  13.624  33.981  1.00 94.69  ? 25  LYS A N   1 
ATOM   121   C CA  . LYS A 1 17  ? 12.266  14.173  33.175  1.00 84.82  ? 25  LYS A CA  1 
ATOM   122   C C   . LYS A 1 17  ? 12.519  13.379  31.892  1.00 84.36  ? 25  LYS A C   1 
ATOM   123   O O   . LYS A 1 17  ? 13.017  12.255  31.933  1.00 91.39  ? 25  LYS A O   1 
ATOM   124   C CB  . LYS A 1 17  ? 13.550  14.272  33.997  1.00 75.56  ? 25  LYS A CB  1 
ATOM   125   C CG  . LYS A 1 17  ? 13.538  15.390  35.012  1.00 81.67  ? 25  LYS A CG  1 
ATOM   126   C CD  . LYS A 1 17  ? 14.870  15.484  35.736  1.00 81.21  ? 25  LYS A CD  1 
ATOM   127   C CE  . LYS A 1 17  ? 14.904  16.691  36.658  1.00 90.86  ? 25  LYS A CE  1 
ATOM   128   N NZ  . LYS A 1 17  ? 14.674  17.957  35.907  1.00 94.22  ? 25  LYS A NZ  1 
ATOM   129   N N   . VAL A 1 18  ? 12.176  13.984  30.757  1.00 66.30  ? 26  VAL A N   1 
ATOM   130   C CA  . VAL A 1 18  ? 12.444  13.410  29.444  1.00 62.24  ? 26  VAL A CA  1 
ATOM   131   C C   . VAL A 1 18  ? 13.723  13.999  28.847  1.00 65.42  ? 26  VAL A C   1 
ATOM   132   O O   . VAL A 1 18  ? 14.276  14.970  29.373  1.00 64.95  ? 26  VAL A O   1 
ATOM   133   C CB  . VAL A 1 18  ? 11.291  13.696  28.467  1.00 64.50  ? 26  VAL A CB  1 
ATOM   134   C CG1 . VAL A 1 18  ? 9.973   13.242  29.056  1.00 75.82  ? 26  VAL A CG1 1 
ATOM   135   C CG2 . VAL A 1 18  ? 11.237  15.172  28.146  1.00 57.92  ? 26  VAL A CG2 1 
ATOM   136   N N   . ASP A 1 19  ? 14.184  13.416  27.743  1.00 83.40  ? 27  ASP A N   1 
ATOM   137   C CA  . ASP A 1 19  ? 15.365  13.922  27.048  1.00 68.99  ? 27  ASP A CA  1 
ATOM   138   C C   . ASP A 1 19  ? 15.049  14.307  25.607  1.00 65.52  ? 27  ASP A C   1 
ATOM   139   O O   . ASP A 1 19  ? 14.066  13.843  25.033  1.00 73.05  ? 27  ASP A O   1 
ATOM   140   C CB  . ASP A 1 19  ? 16.503  12.896  27.086  1.00 60.92  ? 27  ASP A CB  1 
ATOM   141   C CG  . ASP A 1 19  ? 17.298  12.945  28.390  1.00 65.23  ? 27  ASP A CG  1 
ATOM   142   O OD1 . ASP A 1 19  ? 16.729  13.376  29.418  1.00 76.05  ? 27  ASP A OD1 1 
ATOM   143   O OD2 . ASP A 1 19  ? 18.491  12.559  28.388  1.00 59.46  ? 27  ASP A OD2 1 
ATOM   144   N N   . THR A 1 20  ? 15.884  15.171  25.036  1.00 58.00  ? 28  THR A N   1 
ATOM   145   C CA  . THR A 1 20  ? 15.739  15.592  23.642  1.00 58.95  ? 28  THR A CA  1 
ATOM   146   C C   . THR A 1 20  ? 17.096  15.661  22.938  1.00 59.48  ? 28  THR A C   1 
ATOM   147   O O   . THR A 1 20  ? 18.145  15.652  23.587  1.00 59.30  ? 28  THR A O   1 
ATOM   148   C CB  . THR A 1 20  ? 15.053  16.972  23.520  1.00 56.81  ? 28  THR A CB  1 
ATOM   149   O OG1 . THR A 1 20  ? 15.999  18.013  23.805  1.00 66.10  ? 28  THR A OG1 1 
ATOM   150   C CG2 . THR A 1 20  ? 13.873  17.071  24.468  1.00 54.53  ? 28  THR A CG2 1 
ATOM   151   N N   . ILE A 1 21  ? 17.071  15.731  21.611  1.00 75.62  ? 29  ILE A N   1 
ATOM   152   C CA  . ILE A 1 21  ? 18.300  15.857  20.841  1.00 73.41  ? 29  ILE A CA  1 
ATOM   153   C C   . ILE A 1 21  ? 19.173  16.985  21.380  1.00 72.65  ? 29  ILE A C   1 
ATOM   154   O O   . ILE A 1 21  ? 20.390  16.835  21.494  1.00 78.03  ? 29  ILE A O   1 
ATOM   155   C CB  . ILE A 1 21  ? 18.020  16.124  19.350  1.00 53.90  ? 29  ILE A CB  1 
ATOM   156   C CG1 . ILE A 1 21  ? 17.492  14.867  18.667  1.00 58.37  ? 29  ILE A CG1 1 
ATOM   157   C CG2 . ILE A 1 21  ? 19.293  16.534  18.654  1.00 49.23  ? 29  ILE A CG2 1 
ATOM   158   C CD1 . ILE A 1 21  ? 18.575  13.832  18.390  1.00 47.88  ? 29  ILE A CD1 1 
ATOM   159   N N   . LEU A 1 22  ? 18.545  18.107  21.723  1.00 49.65  ? 30  LEU A N   1 
ATOM   160   C CA  . LEU A 1 22  ? 19.290  19.315  22.073  1.00 46.97  ? 30  LEU A CA  1 
ATOM   161   C C   . LEU A 1 22  ? 19.532  19.518  23.570  1.00 57.69  ? 30  LEU A C   1 
ATOM   162   O O   . LEU A 1 22  ? 20.436  20.256  23.956  1.00 69.16  ? 30  LEU A O   1 
ATOM   163   C CB  . LEU A 1 22  ? 18.615  20.562  21.480  1.00 46.85  ? 30  LEU A CB  1 
ATOM   164   C CG  . LEU A 1 22  ? 18.979  20.949  20.044  1.00 57.27  ? 30  LEU A CG  1 
ATOM   165   C CD1 . LEU A 1 22  ? 18.702  19.809  19.095  1.00 56.24  ? 30  LEU A CD1 1 
ATOM   166   C CD2 . LEU A 1 22  ? 18.219  22.178  19.602  1.00 68.27  ? 30  LEU A CD2 1 
ATOM   167   N N   . GLU A 1 23  ? 18.738  18.865  24.412  1.00 48.40  ? 31  GLU A N   1 
ATOM   168   C CA  . GLU A 1 23  ? 18.730  19.184  25.835  1.00 46.45  ? 31  GLU A CA  1 
ATOM   169   C C   . GLU A 1 23  ? 18.313  17.967  26.652  1.00 56.49  ? 31  GLU A C   1 
ATOM   170   O O   . GLU A 1 23  ? 17.386  17.246  26.273  1.00 60.57  ? 31  GLU A O   1 
ATOM   171   C CB  . GLU A 1 23  ? 17.759  20.341  26.066  1.00 55.23  ? 31  GLU A CB  1 
ATOM   172   C CG  . GLU A 1 23  ? 17.722  20.925  27.465  1.00 68.21  ? 31  GLU A CG  1 
ATOM   173   C CD  . GLU A 1 23  ? 16.796  22.133  27.548  1.00 84.11  ? 31  GLU A CD  1 
ATOM   174   O OE1 . GLU A 1 23  ? 16.034  22.365  26.582  1.00 84.32  ? 31  GLU A OE1 1 
ATOM   175   O OE2 . GLU A 1 23  ? 16.833  22.850  28.570  1.00 85.35  ? 31  GLU A OE2 1 
ATOM   176   N N   . ARG A 1 24  ? 19.002  17.731  27.766  1.00 75.50  ? 32  ARG A N   1 
ATOM   177   C CA  . ARG A 1 24  ? 18.686  16.607  28.647  1.00 78.52  ? 32  ARG A CA  1 
ATOM   178   C C   . ARG A 1 24  ? 18.063  17.095  29.950  1.00 84.26  ? 32  ARG A C   1 
ATOM   179   O O   . ARG A 1 24  ? 18.117  18.284  30.262  1.00 93.12  ? 32  ARG A O   1 
ATOM   180   C CB  . ARG A 1 24  ? 19.951  15.799  28.939  1.00 86.82  ? 32  ARG A CB  1 
ATOM   181   C CG  . ARG A 1 24  ? 20.521  15.080  27.720  1.00 98.38  ? 32  ARG A CG  1 
ATOM   182   C CD  . ARG A 1 24  ? 21.954  14.614  27.948  1.00 111.97 ? 32  ARG A CD  1 
ATOM   183   N NE  . ARG A 1 24  ? 22.504  13.961  26.762  1.00 121.56 ? 32  ARG A NE  1 
ATOM   184   C CZ  . ARG A 1 24  ? 23.800  13.744  26.557  1.00 131.29 ? 32  ARG A CZ  1 
ATOM   185   N NH1 . ARG A 1 24  ? 24.689  14.137  27.459  1.00 138.59 ? 32  ARG A NH1 1 
ATOM   186   N NH2 . ARG A 1 24  ? 24.208  13.142  25.447  1.00 131.53 ? 32  ARG A NH2 1 
ATOM   187   N N   . ASN A 1 25  ? 17.464  16.181  30.706  1.00 82.51  ? 33  ASN A N   1 
ATOM   188   C CA  . ASN A 1 25  ? 16.903  16.522  32.014  1.00 96.32  ? 33  ASN A CA  1 
ATOM   189   C C   . ASN A 1 25  ? 15.840  17.628  31.964  1.00 102.17 ? 33  ASN A C   1 
ATOM   190   O O   . ASN A 1 25  ? 15.691  18.401  32.910  1.00 111.82 ? 33  ASN A O   1 
ATOM   191   C CB  . ASN A 1 25  ? 18.017  16.905  33.001  1.00 105.86 ? 33  ASN A CB  1 
ATOM   192   C CG  . ASN A 1 25  ? 18.308  15.811  34.021  1.00 119.32 ? 33  ASN A CG  1 
ATOM   193   O OD1 . ASN A 1 25  ? 17.468  14.952  34.288  1.00 121.81 ? 33  ASN A OD1 1 
ATOM   194   N ND2 . ASN A 1 25  ? 19.502  15.848  34.603  1.00 128.64 ? 33  ASN A ND2 1 
ATOM   195   N N   . VAL A 1 26  ? 15.108  17.701  30.858  1.00 66.62  ? 34  VAL A N   1 
ATOM   196   C CA  . VAL A 1 26  ? 13.981  18.619  30.742  1.00 63.60  ? 34  VAL A CA  1 
ATOM   197   C C   . VAL A 1 26  ? 12.791  18.172  31.586  1.00 78.73  ? 34  VAL A C   1 
ATOM   198   O O   . VAL A 1 26  ? 12.289  17.061  31.421  1.00 83.97  ? 34  VAL A O   1 
ATOM   199   C CB  . VAL A 1 26  ? 13.492  18.709  29.292  1.00 49.71  ? 34  VAL A CB  1 
ATOM   200   C CG1 . VAL A 1 26  ? 12.065  19.234  29.245  1.00 56.02  ? 34  VAL A CG1 1 
ATOM   201   C CG2 . VAL A 1 26  ? 14.419  19.581  28.472  1.00 38.48  ? 34  VAL A CG2 1 
ATOM   202   N N   . THR A 1 27  ? 12.327  19.038  32.482  1.00 80.65  ? 35  THR A N   1 
ATOM   203   C CA  . THR A 1 27  ? 11.140  18.722  33.269  1.00 84.95  ? 35  THR A CA  1 
ATOM   204   C C   . THR A 1 27  ? 9.892   19.036  32.459  1.00 86.93  ? 35  THR A C   1 
ATOM   205   O O   . THR A 1 27  ? 9.781   20.108  31.871  1.00 92.73  ? 35  THR A O   1 
ATOM   206   C CB  . THR A 1 27  ? 11.099  19.508  34.580  1.00 82.98  ? 35  THR A CB  1 
ATOM   207   O OG1 . THR A 1 27  ? 12.377  19.432  35.222  1.00 80.68  ? 35  THR A OG1 1 
ATOM   208   C CG2 . THR A 1 27  ? 10.029  18.938  35.500  1.00 85.31  ? 35  THR A CG2 1 
ATOM   209   N N   . VAL A 1 28  ? 8.957   18.097  32.418  1.00 67.53  ? 36  VAL A N   1 
ATOM   210   C CA  . VAL A 1 28  ? 7.737   18.287  31.645  1.00 57.41  ? 36  VAL A CA  1 
ATOM   211   C C   . VAL A 1 28  ? 6.525   17.881  32.474  1.00 65.17  ? 36  VAL A C   1 
ATOM   212   O O   . VAL A 1 28  ? 6.671   17.335  33.566  1.00 71.27  ? 36  VAL A O   1 
ATOM   213   C CB  . VAL A 1 28  ? 7.755   17.485  30.326  1.00 48.89  ? 36  VAL A CB  1 
ATOM   214   C CG1 . VAL A 1 28  ? 9.076   17.691  29.592  1.00 42.27  ? 36  VAL A CG1 1 
ATOM   215   C CG2 . VAL A 1 28  ? 7.514   16.010  30.598  1.00 51.18  ? 36  VAL A CG2 1 
ATOM   216   N N   . THR A 1 29  ? 5.331   18.144  31.953  1.00 45.80  ? 37  THR A N   1 
ATOM   217   C CA  . THR A 1 29  ? 4.113   17.979  32.740  1.00 56.29  ? 37  THR A CA  1 
ATOM   218   C C   . THR A 1 29  ? 3.625   16.540  32.755  1.00 61.31  ? 37  THR A C   1 
ATOM   219   O O   . THR A 1 29  ? 3.108   16.065  33.762  1.00 70.11  ? 37  THR A O   1 
ATOM   220   C CB  . THR A 1 29  ? 2.985   18.926  32.270  1.00 62.63  ? 37  THR A CB  1 
ATOM   221   O OG1 . THR A 1 29  ? 2.456   18.485  31.011  1.00 60.07  ? 37  THR A OG1 1 
ATOM   222   C CG2 . THR A 1 29  ? 3.519   20.353  32.137  1.00 63.92  ? 37  THR A CG2 1 
ATOM   223   N N   . HIS A 1 30  ? 3.796   15.842  31.639  1.00 85.95  ? 38  HIS A N   1 
ATOM   224   C CA  . HIS A 1 30  ? 3.374   14.454  31.561  1.00 91.69  ? 38  HIS A CA  1 
ATOM   225   C C   . HIS A 1 30  ? 4.181   13.685  30.527  1.00 87.45  ? 38  HIS A C   1 
ATOM   226   O O   . HIS A 1 30  ? 4.627   14.248  29.528  1.00 76.89  ? 38  HIS A O   1 
ATOM   227   C CB  . HIS A 1 30  ? 1.882   14.363  31.248  1.00 100.96 ? 38  HIS A CB  1 
ATOM   228   C CG  . HIS A 1 30  ? 1.277   13.034  31.582  1.00 111.89 ? 38  HIS A CG  1 
ATOM   229   N ND1 . HIS A 1 30  ? 0.743   12.197  30.626  1.00 114.14 ? 38  HIS A ND1 1 
ATOM   230   C CD2 . HIS A 1 30  ? 1.127   12.397  32.767  1.00 116.92 ? 38  HIS A CD2 1 
ATOM   231   C CE1 . HIS A 1 30  ? 0.286   11.104  31.209  1.00 117.94 ? 38  HIS A CE1 1 
ATOM   232   N NE2 . HIS A 1 30  ? 0.507   11.200  32.507  1.00 119.61 ? 38  HIS A NE2 1 
ATOM   233   N N   . ALA A 1 31  ? 4.356   12.391  30.769  1.00 86.48  ? 39  ALA A N   1 
ATOM   234   C CA  . ALA A 1 31  ? 5.168   11.560  29.897  1.00 76.31  ? 39  ALA A CA  1 
ATOM   235   C C   . ALA A 1 31  ? 4.732   10.104  29.963  1.00 80.13  ? 39  ALA A C   1 
ATOM   236   O O   . ALA A 1 31  ? 4.306   9.624   31.011  1.00 92.53  ? 39  ALA A O   1 
ATOM   237   C CB  . ALA A 1 31  ? 6.634   11.693  30.274  1.00 66.64  ? 39  ALA A CB  1 
ATOM   238   N N   . LYS A 1 32  ? 4.833   9.412   28.833  1.00 79.20  ? 40  LYS A N   1 
ATOM   239   C CA  . LYS A 1 32  ? 4.597   7.976   28.781  1.00 79.69  ? 40  LYS A CA  1 
ATOM   240   C C   . LYS A 1 32  ? 5.932   7.248   28.673  1.00 81.31  ? 40  LYS A C   1 
ATOM   241   O O   . LYS A 1 32  ? 6.857   7.734   28.019  1.00 81.39  ? 40  LYS A O   1 
ATOM   242   C CB  . LYS A 1 32  ? 3.715   7.608   27.584  1.00 76.90  ? 40  LYS A CB  1 
ATOM   243   C CG  . LYS A 1 32  ? 3.319   6.133   27.529  1.00 83.71  ? 40  LYS A CG  1 
ATOM   244   C CD  . LYS A 1 32  ? 2.413   5.772   28.704  1.00 97.55  ? 40  LYS A CD  1 
ATOM   245   C CE  . LYS A 1 32  ? 1.967   4.318   28.668  1.00 96.51  ? 40  LYS A CE  1 
ATOM   246   N NZ  . LYS A 1 32  ? 3.015   3.391   29.177  1.00 90.82  ? 40  LYS A NZ  1 
ATOM   247   N N   . ASP A 1 33  ? 6.041   6.093   29.324  1.00 84.78  ? 41  ASP A N   1 
ATOM   248   C CA  . ASP A 1 33  ? 7.223   5.256   29.168  1.00 79.98  ? 41  ASP A CA  1 
ATOM   249   C C   . ASP A 1 33  ? 6.873   4.121   28.226  1.00 73.70  ? 41  ASP A C   1 
ATOM   250   O O   . ASP A 1 33  ? 5.847   3.465   28.400  1.00 79.93  ? 41  ASP A O   1 
ATOM   251   C CB  . ASP A 1 33  ? 7.690   4.698   30.513  1.00 83.53  ? 41  ASP A CB  1 
ATOM   252   C CG  . ASP A 1 33  ? 9.116   4.174   30.463  1.00 85.50  ? 41  ASP A CG  1 
ATOM   253   O OD1 . ASP A 1 33  ? 9.743   4.045   31.536  1.00 91.52  ? 41  ASP A OD1 1 
ATOM   254   O OD2 . ASP A 1 33  ? 9.617   3.903   29.352  1.00 83.65  ? 41  ASP A OD2 1 
ATOM   255   N N   . ILE A 1 34  ? 7.714   3.898   27.220  1.00 71.17  ? 42  ILE A N   1 
ATOM   256   C CA  . ILE A 1 34  ? 7.479   2.817   26.266  1.00 62.10  ? 42  ILE A CA  1 
ATOM   257   C C   . ILE A 1 34  ? 8.491   1.689   26.411  1.00 58.47  ? 42  ILE A C   1 
ATOM   258   O O   . ILE A 1 34  ? 8.645   0.871   25.508  1.00 64.43  ? 42  ILE A O   1 
ATOM   259   C CB  . ILE A 1 34  ? 7.494   3.309   24.803  1.00 57.49  ? 42  ILE A CB  1 
ATOM   260   C CG1 . ILE A 1 34  ? 8.800   4.046   24.494  1.00 50.87  ? 42  ILE A CG1 1 
ATOM   261   C CG2 . ILE A 1 34  ? 6.279   4.183   24.509  1.00 56.63  ? 42  ILE A CG2 1 
ATOM   262   C CD1 . ILE A 1 34  ? 8.885   4.559   23.073  1.00 43.66  ? 42  ILE A CD1 1 
ATOM   263   N N   . LEU A 1 35  ? 9.181   1.644   27.545  1.00 58.02  ? 43  LEU A N   1 
ATOM   264   C CA  . LEU A 1 35  ? 10.111  0.559   27.810  1.00 51.94  ? 43  LEU A CA  1 
ATOM   265   C C   . LEU A 1 35  ? 9.572   -0.366  28.887  1.00 59.26  ? 43  LEU A C   1 
ATOM   266   O O   . LEU A 1 35  ? 9.746   -0.115  30.080  1.00 71.79  ? 43  LEU A O   1 
ATOM   267   C CB  . LEU A 1 35  ? 11.483  1.088   28.223  1.00 39.95  ? 43  LEU A CB  1 
ATOM   268   C CG  . LEU A 1 35  ? 12.516  0.019   28.590  1.00 39.51  ? 43  LEU A CG  1 
ATOM   269   C CD1 . LEU A 1 35  ? 12.644  -0.991  27.477  1.00 41.38  ? 43  LEU A CD1 1 
ATOM   270   C CD2 . LEU A 1 35  ? 13.870  0.658   28.890  1.00 38.76  ? 43  LEU A CD2 1 
ATOM   271   N N   . GLU A 1 36  ? 8.912   -1.437  28.458  1.00 44.49  ? 44  GLU A N   1 
ATOM   272   C CA  . GLU A 1 36  ? 8.487   -2.479  29.382  1.00 55.44  ? 44  GLU A CA  1 
ATOM   273   C C   . GLU A 1 36  ? 9.699   -3.060  30.096  1.00 66.00  ? 44  GLU A C   1 
ATOM   274   O O   . GLU A 1 36  ? 10.638  -3.525  29.457  1.00 67.61  ? 44  GLU A O   1 
ATOM   275   C CB  . GLU A 1 36  ? 7.737   -3.584  28.640  1.00 51.41  ? 44  GLU A CB  1 
ATOM   276   C CG  . GLU A 1 36  ? 7.013   -4.513  29.573  1.00 59.43  ? 44  GLU A CG  1 
ATOM   277   C CD  . GLU A 1 36  ? 6.436   -3.771  30.757  1.00 74.52  ? 44  GLU A CD  1 
ATOM   278   O OE1 . GLU A 1 36  ? 7.158   -3.612  31.768  1.00 79.96  ? 44  GLU A OE1 1 
ATOM   279   O OE2 . GLU A 1 36  ? 5.267   -3.334  30.672  1.00 78.82  ? 44  GLU A OE2 1 
ATOM   280   N N   . LYS A 1 37  ? 9.690   -3.018  31.421  1.00 74.08  ? 45  LYS A N   1 
ATOM   281   C CA  . LYS A 1 37  ? 10.813  -3.554  32.175  1.00 69.01  ? 45  LYS A CA  1 
ATOM   282   C C   . LYS A 1 37  ? 10.358  -4.243  33.447  1.00 71.03  ? 45  LYS A C   1 
ATOM   283   O O   . LYS A 1 37  ? 11.119  -4.364  34.405  1.00 69.47  ? 45  LYS A O   1 
ATOM   284   C CB  . LYS A 1 37  ? 11.842  -2.463  32.478  1.00 65.84  ? 45  LYS A CB  1 
ATOM   285   C CG  . LYS A 1 37  ? 11.259  -1.099  32.836  1.00 65.96  ? 45  LYS A CG  1 
ATOM   286   C CD  . LYS A 1 37  ? 12.371  -0.068  33.005  1.00 64.78  ? 45  LYS A CD  1 
ATOM   287   C CE  . LYS A 1 37  ? 11.811  1.291   33.373  1.00 73.09  ? 45  LYS A CE  1 
ATOM   288   N NZ  . LYS A 1 37  ? 10.765  1.717   32.406  1.00 77.85  ? 45  LYS A NZ  1 
ATOM   289   N N   . THR A 1 38  ? 9.115   -4.712  33.435  1.00 62.23  ? 46  THR A N   1 
ATOM   290   C CA  . THR A 1 38  ? 8.538   -5.385  34.592  1.00 70.07  ? 46  THR A CA  1 
ATOM   291   C C   . THR A 1 38  ? 7.880   -6.710  34.206  1.00 71.11  ? 46  THR A C   1 
ATOM   292   O O   . THR A 1 38  ? 7.039   -6.761  33.306  1.00 68.87  ? 46  THR A O   1 
ATOM   293   C CB  . THR A 1 38  ? 7.508   -4.479  35.320  1.00 75.83  ? 46  THR A CB  1 
ATOM   294   O OG1 . THR A 1 38  ? 6.324   -4.342  34.521  1.00 74.94  ? 46  THR A OG1 1 
ATOM   295   C CG2 . THR A 1 38  ? 8.102   -3.098  35.593  1.00 72.18  ? 46  THR A CG2 1 
ATOM   296   N N   . HIS A 1 39  ? 8.273   -7.776  34.895  1.00 84.53  ? 47  HIS A N   1 
ATOM   297   C CA  . HIS A 1 39  ? 7.700   -9.103  34.686  1.00 80.77  ? 47  HIS A CA  1 
ATOM   298   C C   . HIS A 1 39  ? 6.919   -9.511  35.932  1.00 88.03  ? 47  HIS A C   1 
ATOM   299   O O   . HIS A 1 39  ? 6.848   -8.747  36.896  1.00 89.28  ? 47  HIS A O   1 
ATOM   300   C CB  . HIS A 1 39  ? 8.810   -10.110 34.422  1.00 69.66  ? 47  HIS A CB  1 
ATOM   301   C CG  . HIS A 1 39  ? 9.894   -10.080 35.451  1.00 73.45  ? 47  HIS A CG  1 
ATOM   302   N ND1 . HIS A 1 39  ? 9.690   -10.473 36.755  1.00 84.58  ? 47  HIS A ND1 1 
ATOM   303   C CD2 . HIS A 1 39  ? 11.186  -9.683  35.375  1.00 72.61  ? 47  HIS A CD2 1 
ATOM   304   C CE1 . HIS A 1 39  ? 10.812  -10.328 37.437  1.00 87.04  ? 47  HIS A CE1 1 
ATOM   305   N NE2 . HIS A 1 39  ? 11.736  -9.850  36.623  1.00 79.01  ? 47  HIS A NE2 1 
ATOM   306   N N   . ASN A 1 40  ? 6.347   -10.714 35.926  1.00 70.53  ? 48  ASN A N   1 
ATOM   307   C CA  . ASN A 1 40  ? 5.553   -11.170 37.068  1.00 75.52  ? 48  ASN A CA  1 
ATOM   308   C C   . ASN A 1 40  ? 6.199   -12.263 37.925  1.00 77.96  ? 48  ASN A C   1 
ATOM   309   O O   . ASN A 1 40  ? 5.612   -12.713 38.905  1.00 86.18  ? 48  ASN A O   1 
ATOM   310   C CB  . ASN A 1 40  ? 4.145   -11.591 36.631  1.00 78.44  ? 48  ASN A CB  1 
ATOM   311   C CG  . ASN A 1 40  ? 4.143   -12.849 35.800  1.00 77.23  ? 48  ASN A CG  1 
ATOM   312   O OD1 . ASN A 1 40  ? 5.136   -13.571 35.742  1.00 75.49  ? 48  ASN A OD1 1 
ATOM   313   N ND2 . ASN A 1 40  ? 3.017   -13.127 35.155  1.00 77.88  ? 48  ASN A ND2 1 
ATOM   314   N N   . GLY A 1 41  ? 7.402   -12.688 37.552  1.00 97.41  ? 49  GLY A N   1 
ATOM   315   C CA  . GLY A 1 41  ? 8.137   -13.674 38.328  1.00 97.71  ? 49  GLY A CA  1 
ATOM   316   C C   . GLY A 1 41  ? 7.666   -15.114 38.175  1.00 100.72 ? 49  GLY A C   1 
ATOM   317   O O   . GLY A 1 41  ? 8.314   -16.038 38.663  1.00 106.47 ? 49  GLY A O   1 
ATOM   318   N N   . LYS A 1 42  ? 6.540   -15.309 37.497  1.00 87.24  ? 50  LYS A N   1 
ATOM   319   C CA  . LYS A 1 42  ? 5.965   -16.641 37.343  1.00 86.64  ? 50  LYS A CA  1 
ATOM   320   C C   . LYS A 1 42  ? 6.126   -17.178 35.921  1.00 81.87  ? 50  LYS A C   1 
ATOM   321   O O   . LYS A 1 42  ? 5.728   -16.522 34.959  1.00 86.26  ? 50  LYS A O   1 
ATOM   322   C CB  . LYS A 1 42  ? 4.473   -16.621 37.693  1.00 91.99  ? 50  LYS A CB  1 
ATOM   323   C CG  . LYS A 1 42  ? 4.119   -16.052 39.063  1.00 95.60  ? 50  LYS A CG  1 
ATOM   324   C CD  . LYS A 1 42  ? 2.599   -16.001 39.242  1.00 95.26  ? 50  LYS A CD  1 
ATOM   325   C CE  . LYS A 1 42  ? 2.186   -15.219 40.481  1.00 99.75  ? 50  LYS A CE  1 
ATOM   326   N NZ  . LYS A 1 42  ? 2.555   -15.907 41.747  1.00 112.26 ? 50  LYS A NZ  1 
ATOM   327   N N   . LEU A 1 43  ? 6.697   -18.373 35.783  1.00 74.83  ? 51  LEU A N   1 
ATOM   328   C CA  . LEU A 1 43  ? 6.693   -19.044 34.488  1.00 68.22  ? 51  LEU A CA  1 
ATOM   329   C C   . LEU A 1 43  ? 5.274   -19.529 34.231  1.00 74.36  ? 51  LEU A C   1 
ATOM   330   O O   . LEU A 1 43  ? 4.697   -20.238 35.054  1.00 81.37  ? 51  LEU A O   1 
ATOM   331   C CB  . LEU A 1 43  ? 7.667   -20.216 34.471  1.00 66.30  ? 51  LEU A CB  1 
ATOM   332   C CG  . LEU A 1 43  ? 9.007   -20.001 35.174  1.00 71.11  ? 51  LEU A CG  1 
ATOM   333   C CD1 . LEU A 1 43  ? 9.915   -21.204 34.938  1.00 68.92  ? 51  LEU A CD1 1 
ATOM   334   C CD2 . LEU A 1 43  ? 9.681   -18.721 34.707  1.00 71.25  ? 51  LEU A CD2 1 
ATOM   335   N N   . CYS A 1 44  ? 4.708   -19.142 33.095  1.00 63.43  ? 52  CYS A N   1 
ATOM   336   C CA  . CYS A 1 44  ? 3.275   -19.302 32.881  1.00 64.28  ? 52  CYS A CA  1 
ATOM   337   C C   . CYS A 1 44  ? 2.971   -20.062 31.608  1.00 55.92  ? 52  CYS A C   1 
ATOM   338   O O   . CYS A 1 44  ? 3.860   -20.305 30.799  1.00 52.34  ? 52  CYS A O   1 
ATOM   339   C CB  . CYS A 1 44  ? 2.595   -17.930 32.825  1.00 69.13  ? 52  CYS A CB  1 
ATOM   340   S SG  . CYS A 1 44  ? 2.891   -16.876 34.265  1.00 93.78  ? 52  CYS A SG  1 
ATOM   341   N N   . LYS A 1 45  ? 1.710   -20.438 31.430  1.00 51.40  ? 53  LYS A N   1 
ATOM   342   C CA  . LYS A 1 45  ? 1.289   -21.067 30.187  1.00 51.68  ? 53  LYS A CA  1 
ATOM   343   C C   . LYS A 1 45  ? 1.442   -20.072 29.049  1.00 51.64  ? 53  LYS A C   1 
ATOM   344   O O   . LYS A 1 45  ? 1.487   -18.869 29.273  1.00 59.53  ? 53  LYS A O   1 
ATOM   345   C CB  . LYS A 1 45  ? -0.152  -21.578 30.283  1.00 65.40  ? 53  LYS A CB  1 
ATOM   346   C CG  . LYS A 1 45  ? -0.314  -22.780 31.214  1.00 75.74  ? 53  LYS A CG  1 
ATOM   347   C CD  . LYS A 1 45  ? -1.718  -23.358 31.157  1.00 80.84  ? 53  LYS A CD  1 
ATOM   348   C CE  . LYS A 1 45  ? -2.690  -22.526 31.961  1.00 90.41  ? 53  LYS A CE  1 
ATOM   349   N NZ  . LYS A 1 45  ? -2.258  -22.432 33.385  1.00 94.76  ? 53  LYS A NZ  1 
ATOM   350   N N   . LEU A 1 46  A 1.523   -20.574 27.828  1.00 61.64  ? 53  LEU A N   1 
ATOM   351   C CA  . LEU A 1 46  A 1.820   -19.730 26.685  1.00 56.82  ? 53  LEU A CA  1 
ATOM   352   C C   . LEU A 1 46  A 0.708   -19.865 25.651  1.00 60.99  ? 53  LEU A C   1 
ATOM   353   O O   . LEU A 1 46  A 0.663   -20.834 24.891  1.00 61.12  ? 53  LEU A O   1 
ATOM   354   C CB  . LEU A 1 46  A 3.182   -20.126 26.098  1.00 53.54  ? 53  LEU A CB  1 
ATOM   355   C CG  . LEU A 1 46  A 3.946   -19.227 25.117  1.00 49.56  ? 53  LEU A CG  1 
ATOM   356   C CD1 . LEU A 1 46  A 3.461   -19.429 23.680  1.00 47.11  ? 53  LEU A CD1 1 
ATOM   357   C CD2 . LEU A 1 46  A 3.871   -17.753 25.531  1.00 44.52  ? 53  LEU A CD2 1 
ATOM   358   N N   . ASN A 1 47  ? -0.186  -18.881 25.630  1.00 75.72  ? 54  ASN A N   1 
ATOM   359   C CA  . ASN A 1 47  ? -1.387  -18.936 24.800  1.00 80.77  ? 54  ASN A CA  1 
ATOM   360   C C   . ASN A 1 47  ? -2.349  -19.990 25.321  1.00 85.48  ? 54  ASN A C   1 
ATOM   361   O O   . ASN A 1 47  ? -3.097  -20.603 24.554  1.00 79.45  ? 54  ASN A O   1 
ATOM   362   C CB  . ASN A 1 47  ? -1.049  -19.211 23.335  1.00 87.38  ? 54  ASN A CB  1 
ATOM   363   C CG  . ASN A 1 47  ? -0.020  -18.242 22.786  1.00 97.80  ? 54  ASN A CG  1 
ATOM   364   O OD1 . ASN A 1 47  ? 0.903   -18.637 22.068  1.00 105.22 ? 54  ASN A OD1 1 
ATOM   365   N ND2 . ASN A 1 47  ? -0.166  -16.963 23.131  1.00 89.35  ? 54  ASN A ND2 1 
ATOM   366   N N   . GLY A 1 48  ? -2.307  -20.200 26.633  1.00 81.35  ? 55  GLY A N   1 
ATOM   367   C CA  . GLY A 1 48  ? -3.213  -21.117 27.300  1.00 90.14  ? 55  GLY A CA  1 
ATOM   368   C C   . GLY A 1 48  ? -2.658  -22.518 27.408  1.00 86.72  ? 55  GLY A C   1 
ATOM   369   O O   . GLY A 1 48  ? -2.894  -23.214 28.396  1.00 91.98  ? 55  GLY A O   1 
ATOM   370   N N   . ILE A 1 49  ? -1.920  -22.927 26.381  1.00 82.67  ? 56  ILE A N   1 
ATOM   371   C CA  . ILE A 1 49  ? -1.333  -24.261 26.321  1.00 80.49  ? 56  ILE A CA  1 
ATOM   372   C C   . ILE A 1 49  ? 0.033   -24.274 27.016  1.00 76.44  ? 56  ILE A C   1 
ATOM   373   O O   . ILE A 1 49  ? 0.917   -23.506 26.666  1.00 78.48  ? 56  ILE A O   1 
ATOM   374   C CB  . ILE A 1 49  ? -1.229  -24.742 24.863  1.00 76.26  ? 56  ILE A CB  1 
ATOM   375   C CG1 . ILE A 1 49  ? -0.607  -26.130 24.800  1.00 82.58  ? 56  ILE A CG1 1 
ATOM   376   C CG2 . ILE A 1 49  ? -0.454  -23.747 24.013  1.00 78.88  ? 56  ILE A CG2 1 
ATOM   377   C CD1 . ILE A 1 49  ? -1.535  -27.215 25.284  1.00 98.48  ? 56  ILE A CD1 1 
ATOM   378   N N   . PRO A 1 50  ? 0.199   -25.146 28.018  1.00 67.73  ? 57  PRO A N   1 
ATOM   379   C CA  . PRO A 1 50  ? 1.320   -25.084 28.963  1.00 62.67  ? 57  PRO A CA  1 
ATOM   380   C C   . PRO A 1 50  ? 2.618   -25.717 28.464  1.00 53.52  ? 57  PRO A C   1 
ATOM   381   O O   . PRO A 1 50  ? 2.627   -26.393 27.438  1.00 52.13  ? 57  PRO A O   1 
ATOM   382   C CB  . PRO A 1 50  ? 0.798   -25.894 30.148  1.00 64.51  ? 57  PRO A CB  1 
ATOM   383   C CG  . PRO A 1 50  ? -0.055  -26.928 29.515  1.00 64.29  ? 57  PRO A CG  1 
ATOM   384   C CD  . PRO A 1 50  ? -0.726  -26.244 28.345  1.00 67.86  ? 57  PRO A CD  1 
ATOM   385   N N   . PRO A 1 51  ? 3.716   -25.506 29.202  1.00 58.53  ? 58  PRO A N   1 
ATOM   386   C CA  . PRO A 1 51  ? 4.984   -26.148 28.872  1.00 52.37  ? 58  PRO A CA  1 
ATOM   387   C C   . PRO A 1 51  ? 5.053   -27.571 29.406  1.00 61.54  ? 58  PRO A C   1 
ATOM   388   O O   . PRO A 1 51  ? 4.539   -27.858 30.488  1.00 79.34  ? 58  PRO A O   1 
ATOM   389   C CB  . PRO A 1 51  ? 6.006   -25.289 29.628  1.00 50.41  ? 58  PRO A CB  1 
ATOM   390   C CG  . PRO A 1 51  ? 5.266   -24.825 30.824  1.00 52.16  ? 58  PRO A CG  1 
ATOM   391   C CD  . PRO A 1 51  ? 3.857   -24.569 30.331  1.00 62.82  ? 58  PRO A CD  1 
ATOM   392   N N   . LEU A 1 52  ? 5.689   -28.454 28.647  1.00 59.90  ? 59  LEU A N   1 
ATOM   393   C CA  . LEU A 1 52  ? 6.112   -29.732 29.179  1.00 59.79  ? 59  LEU A CA  1 
ATOM   394   C C   . LEU A 1 52  ? 7.130   -29.449 30.273  1.00 62.68  ? 59  LEU A C   1 
ATOM   395   O O   . LEU A 1 52  ? 8.013   -28.617 30.089  1.00 58.65  ? 59  LEU A O   1 
ATOM   396   C CB  . LEU A 1 52  ? 6.763   -30.552 28.078  1.00 56.25  ? 59  LEU A CB  1 
ATOM   397   C CG  . LEU A 1 52  ? 7.504   -31.797 28.548  1.00 58.58  ? 59  LEU A CG  1 
ATOM   398   C CD1 . LEU A 1 52  ? 6.532   -32.945 28.635  1.00 62.38  ? 59  LEU A CD1 1 
ATOM   399   C CD2 . LEU A 1 52  ? 8.631   -32.121 27.582  1.00 55.08  ? 59  LEU A CD2 1 
ATOM   400   N N   . GLU A 1 53  ? 7.015   -30.129 31.409  1.00 61.39  ? 60  GLU A N   1 
ATOM   401   C CA  . GLU A 1 53  ? 7.889   -29.846 32.548  1.00 60.88  ? 60  GLU A CA  1 
ATOM   402   C C   . GLU A 1 53  ? 8.778   -31.045 32.868  1.00 62.35  ? 60  GLU A C   1 
ATOM   403   O O   . GLU A 1 53  ? 8.281   -32.136 33.131  1.00 65.69  ? 60  GLU A O   1 
ATOM   404   C CB  . GLU A 1 53  ? 7.043   -29.464 33.757  1.00 60.80  ? 60  GLU A CB  1 
ATOM   405   C CG  . GLU A 1 53  ? 7.723   -28.552 34.753  1.00 63.36  ? 60  GLU A CG  1 
ATOM   406   C CD  . GLU A 1 53  ? 6.714   -27.851 35.650  1.00 73.63  ? 60  GLU A CD  1 
ATOM   407   O OE1 . GLU A 1 53  ? 5.492   -28.059 35.451  1.00 65.37  ? 60  GLU A OE1 1 
ATOM   408   O OE2 . GLU A 1 53  ? 7.142   -27.090 36.546  1.00 87.20  ? 60  GLU A OE2 1 
ATOM   409   N N   . LEU A 1 54  ? 10.092  -30.840 32.846  1.00 73.12  ? 61  LEU A N   1 
ATOM   410   C CA  . LEU A 1 54  ? 11.032  -31.960 32.913  1.00 67.39  ? 61  LEU A CA  1 
ATOM   411   C C   . LEU A 1 54  ? 11.763  -32.114 34.247  1.00 74.93  ? 61  LEU A C   1 
ATOM   412   O O   . LEU A 1 54  ? 12.505  -33.075 34.447  1.00 82.54  ? 61  LEU A O   1 
ATOM   413   C CB  . LEU A 1 54  ? 12.043  -31.886 31.762  1.00 49.48  ? 61  LEU A CB  1 
ATOM   414   C CG  . LEU A 1 54  ? 11.451  -31.941 30.351  1.00 41.82  ? 61  LEU A CG  1 
ATOM   415   C CD1 . LEU A 1 54  ? 12.536  -32.203 29.326  1.00 30.35  ? 61  LEU A CD1 1 
ATOM   416   C CD2 . LEU A 1 54  ? 10.386  -33.005 30.270  1.00 59.51  ? 61  LEU A CD2 1 
ATOM   417   N N   . GLY A 1 55  ? 11.558  -31.172 35.157  1.00 63.63  ? 62  GLY A N   1 
ATOM   418   C CA  . GLY A 1 55  ? 12.176  -31.259 36.467  1.00 68.02  ? 62  GLY A CA  1 
ATOM   419   C C   . GLY A 1 55  ? 13.681  -31.384 36.389  1.00 66.97  ? 62  GLY A C   1 
ATOM   420   O O   . GLY A 1 55  ? 14.335  -30.609 35.687  1.00 66.98  ? 62  GLY A O   1 
ATOM   421   N N   . ASP A 1 56  ? 14.236  -32.354 37.108  1.00 80.21  ? 63  ASP A N   1 
ATOM   422   C CA  . ASP A 1 56  ? 15.680  -32.551 37.111  1.00 73.16  ? 63  ASP A CA  1 
ATOM   423   C C   . ASP A 1 56  ? 16.114  -33.520 36.004  1.00 67.82  ? 63  ASP A C   1 
ATOM   424   O O   . ASP A 1 56  ? 17.216  -34.077 36.042  1.00 62.87  ? 63  ASP A O   1 
ATOM   425   C CB  . ASP A 1 56  ? 16.161  -33.032 38.483  1.00 76.36  ? 63  ASP A CB  1 
ATOM   426   C CG  . ASP A 1 56  ? 17.442  -32.335 38.933  1.00 68.61  ? 63  ASP A CG  1 
ATOM   427   O OD1 . ASP A 1 56  ? 18.239  -31.919 38.059  1.00 59.44  ? 63  ASP A OD1 1 
ATOM   428   O OD2 . ASP A 1 56  ? 17.655  -32.194 40.162  1.00 65.44  ? 63  ASP A OD2 1 
ATOM   429   N N   . CYS A 1 57  ? 15.243  -33.698 35.011  1.00 58.22  ? 64  CYS A N   1 
ATOM   430   C CA  . CYS A 1 57  ? 15.511  -34.595 33.889  1.00 46.86  ? 64  CYS A CA  1 
ATOM   431   C C   . CYS A 1 57  ? 15.855  -33.874 32.586  1.00 50.13  ? 64  CYS A C   1 
ATOM   432   O O   . CYS A 1 57  ? 15.584  -32.677 32.425  1.00 59.68  ? 64  CYS A O   1 
ATOM   433   C CB  . CYS A 1 57  ? 14.319  -35.515 33.644  1.00 45.46  ? 64  CYS A CB  1 
ATOM   434   S SG  . CYS A 1 57  ? 14.237  -36.864 34.789  1.00 69.08  ? 64  CYS A SG  1 
ATOM   435   N N   . SER A 1 58  ? 16.443  -34.624 31.657  1.00 63.89  ? 65  SER A N   1 
ATOM   436   C CA  . SER A 1 58  ? 16.787  -34.108 30.342  1.00 65.12  ? 65  SER A CA  1 
ATOM   437   C C   . SER A 1 58  ? 15.876  -34.738 29.306  1.00 80.37  ? 65  SER A C   1 
ATOM   438   O O   . SER A 1 58  ? 15.375  -35.835 29.515  1.00 87.88  ? 65  SER A O   1 
ATOM   439   C CB  . SER A 1 58  ? 18.243  -34.436 30.015  1.00 42.43  ? 65  SER A CB  1 
ATOM   440   O OG  . SER A 1 58  ? 18.361  -35.665 29.305  1.00 41.37  ? 65  SER A OG  1 
ATOM   441   N N   . ILE A 1 59  ? 15.659  -34.052 28.191  1.00 53.81  ? 66  ILE A N   1 
ATOM   442   C CA  . ILE A 1 59  ? 14.804  -34.598 27.148  1.00 49.22  ? 66  ILE A CA  1 
ATOM   443   C C   . ILE A 1 59  ? 15.103  -36.069 26.948  1.00 54.81  ? 66  ILE A C   1 
ATOM   444   O O   . ILE A 1 59  ? 14.196  -36.900 26.914  1.00 65.76  ? 66  ILE A O   1 
ATOM   445   C CB  . ILE A 1 59  ? 15.008  -33.901 25.801  1.00 46.30  ? 66  ILE A CB  1 
ATOM   446   C CG1 . ILE A 1 59  ? 14.718  -32.406 25.923  1.00 41.35  ? 66  ILE A CG1 1 
ATOM   447   C CG2 . ILE A 1 59  ? 14.108  -34.527 24.741  1.00 47.18  ? 66  ILE A CG2 1 
ATOM   448   C CD1 . ILE A 1 59  ? 13.256  -32.088 25.984  1.00 33.61  ? 66  ILE A CD1 1 
ATOM   449   N N   . ALA A 1 60  ? 16.378  -36.396 26.816  1.00 39.92  ? 67  ALA A N   1 
ATOM   450   C CA  . ALA A 1 60  ? 16.755  -37.769 26.503  1.00 41.30  ? 67  ALA A CA  1 
ATOM   451   C C   . ALA A 1 60  ? 16.308  -38.744 27.595  1.00 47.30  ? 67  ALA A C   1 
ATOM   452   O O   . ALA A 1 60  ? 15.551  -39.674 27.332  1.00 50.33  ? 67  ALA A O   1 
ATOM   453   C CB  . ALA A 1 60  ? 18.258  -37.872 26.264  1.00 33.17  ? 67  ALA A CB  1 
ATOM   454   N N   . GLY A 1 61  ? 16.779  -38.519 28.819  1.00 42.69  ? 68  GLY A N   1 
ATOM   455   C CA  . GLY A 1 61  ? 16.409  -39.353 29.945  1.00 45.04  ? 68  GLY A CA  1 
ATOM   456   C C   . GLY A 1 61  ? 14.906  -39.458 30.050  1.00 47.78  ? 68  GLY A C   1 
ATOM   457   O O   . GLY A 1 61  ? 14.376  -40.419 30.593  1.00 57.83  ? 68  GLY A O   1 
ATOM   458   N N   . TRP A 1 62  ? 14.219  -38.461 29.513  1.00 38.08  ? 69  TRP A N   1 
ATOM   459   C CA  . TRP A 1 62  ? 12.766  -38.422 29.529  1.00 41.81  ? 69  TRP A CA  1 
ATOM   460   C C   . TRP A 1 62  ? 12.169  -39.395 28.504  1.00 44.28  ? 69  TRP A C   1 
ATOM   461   O O   . TRP A 1 62  ? 11.367  -40.257 28.862  1.00 52.68  ? 69  TRP A O   1 
ATOM   462   C CB  . TRP A 1 62  ? 12.274  -36.981 29.298  1.00 46.28  ? 69  TRP A CB  1 
ATOM   463   C CG  . TRP A 1 62  ? 10.818  -36.874 29.014  1.00 55.09  ? 69  TRP A CG  1 
ATOM   464   C CD1 . TRP A 1 62  ? 9.797   -37.249 29.830  1.00 60.49  ? 69  TRP A CD1 1 
ATOM   465   C CD2 . TRP A 1 62  ? 10.213  -36.349 27.826  1.00 56.96  ? 69  TRP A CD2 1 
ATOM   466   N NE1 . TRP A 1 62  ? 8.591   -36.995 29.222  1.00 60.63  ? 69  TRP A NE1 1 
ATOM   467   C CE2 . TRP A 1 62  ? 8.821   -36.445 27.990  1.00 55.44  ? 69  TRP A CE2 1 
ATOM   468   C CE3 . TRP A 1 62  ? 10.716  -35.812 26.638  1.00 48.92  ? 69  TRP A CE3 1 
ATOM   469   C CZ2 . TRP A 1 62  ? 7.927   -36.029 27.012  1.00 52.86  ? 69  TRP A CZ2 1 
ATOM   470   C CZ3 . TRP A 1 62  ? 9.824   -35.395 25.668  1.00 39.54  ? 69  TRP A CZ3 1 
ATOM   471   C CH2 . TRP A 1 62  ? 8.449   -35.503 25.860  1.00 45.03  ? 69  TRP A CH2 1 
ATOM   472   N N   . LEU A 1 63  ? 12.573  -39.262 27.242  1.00 58.61  ? 70  LEU A N   1 
ATOM   473   C CA  . LEU A 1 63  ? 12.075  -40.125 26.173  1.00 46.69  ? 70  LEU A CA  1 
ATOM   474   C C   . LEU A 1 63  ? 12.438  -41.594 26.402  1.00 52.08  ? 70  LEU A C   1 
ATOM   475   O O   . LEU A 1 63  ? 11.607  -42.489 26.255  1.00 58.88  ? 70  LEU A O   1 
ATOM   476   C CB  . LEU A 1 63  ? 12.634  -39.675 24.826  1.00 39.96  ? 70  LEU A CB  1 
ATOM   477   C CG  . LEU A 1 63  ? 12.210  -38.307 24.307  1.00 38.46  ? 70  LEU A CG  1 
ATOM   478   C CD1 . LEU A 1 63  ? 13.336  -37.698 23.488  1.00 37.05  ? 70  LEU A CD1 1 
ATOM   479   C CD2 . LEU A 1 63  ? 10.941  -38.397 23.480  1.00 32.36  ? 70  LEU A CD2 1 
ATOM   480   N N   . LEU A 1 64  ? 13.694  -41.837 26.748  1.00 53.89  ? 71  LEU A N   1 
ATOM   481   C CA  . LEU A 1 64  ? 14.156  -43.184 27.001  1.00 56.02  ? 71  LEU A CA  1 
ATOM   482   C C   . LEU A 1 64  ? 13.470  -43.739 28.236  1.00 65.90  ? 71  LEU A C   1 
ATOM   483   O O   . LEU A 1 64  ? 13.190  -44.932 28.320  1.00 77.50  ? 71  LEU A O   1 
ATOM   484   C CB  . LEU A 1 64  ? 15.670  -43.199 27.202  1.00 50.46  ? 71  LEU A CB  1 
ATOM   485   C CG  . LEU A 1 64  ? 16.551  -42.638 26.083  1.00 47.94  ? 71  LEU A CG  1 
ATOM   486   C CD1 . LEU A 1 64  ? 18.014  -42.820 26.452  1.00 42.98  ? 71  LEU A CD1 1 
ATOM   487   C CD2 . LEU A 1 64  ? 16.253  -43.303 24.745  1.00 44.06  ? 71  LEU A CD2 1 
ATOM   488   N N   . GLY A 1 65  ? 13.202  -42.865 29.198  1.00 53.24  ? 72  GLY A N   1 
ATOM   489   C CA  . GLY A 1 65  ? 12.611  -43.281 30.456  1.00 50.78  ? 72  GLY A CA  1 
ATOM   490   C C   . GLY A 1 65  ? 13.638  -43.644 31.511  1.00 54.47  ? 72  GLY A C   1 
ATOM   491   O O   . GLY A 1 65  ? 13.666  -44.770 31.996  1.00 58.98  ? 72  GLY A O   1 
ATOM   492   N N   . ASN A 1 66  ? 14.501  -42.697 31.854  1.00 56.06  ? 73  ASN A N   1 
ATOM   493   C CA  . ASN A 1 66  ? 15.386  -42.879 32.987  1.00 57.75  ? 73  ASN A CA  1 
ATOM   494   C C   . ASN A 1 66  ? 14.523  -42.857 34.225  1.00 67.83  ? 73  ASN A C   1 
ATOM   495   O O   . ASN A 1 66  ? 13.898  -41.842 34.519  1.00 79.98  ? 73  ASN A O   1 
ATOM   496   C CB  . ASN A 1 66  ? 16.420  -41.762 33.051  1.00 53.20  ? 73  ASN A CB  1 
ATOM   497   C CG  . ASN A 1 66  ? 17.296  -41.844 34.290  1.00 58.81  ? 73  ASN A CG  1 
ATOM   498   O OD1 . ASN A 1 66  ? 17.145  -42.742 35.126  1.00 75.25  ? 73  ASN A OD1 1 
ATOM   499   N ND2 . ASN A 1 66  ? 18.232  -40.904 34.408  1.00 45.23  ? 73  ASN A ND2 1 
ATOM   500   N N   . PRO A 1 67  ? 14.476  -43.987 34.947  1.00 63.34  ? 74  PRO A N   1 
ATOM   501   C CA  . PRO A 1 67  ? 13.619  -44.233 36.111  1.00 70.34  ? 74  PRO A CA  1 
ATOM   502   C C   . PRO A 1 67  ? 13.333  -42.980 36.937  1.00 83.94  ? 74  PRO A C   1 
ATOM   503   O O   . PRO A 1 67  ? 12.181  -42.754 37.312  1.00 97.59  ? 74  PRO A O   1 
ATOM   504   C CB  . PRO A 1 67  ? 14.441  -45.230 36.921  1.00 69.57  ? 74  PRO A CB  1 
ATOM   505   C CG  . PRO A 1 67  ? 15.135  -46.040 35.872  1.00 63.85  ? 74  PRO A CG  1 
ATOM   506   C CD  . PRO A 1 67  ? 15.403  -45.109 34.712  1.00 56.98  ? 74  PRO A CD  1 
ATOM   507   N N   . GLU A 1 68  ? 14.364  -42.181 37.207  1.00 58.33  ? 75  GLU A N   1 
ATOM   508   C CA  . GLU A 1 68  ? 14.208  -40.933 37.961  1.00 60.80  ? 75  GLU A CA  1 
ATOM   509   C C   . GLU A 1 68  ? 13.200  -39.974 37.328  1.00 64.53  ? 75  GLU A C   1 
ATOM   510   O O   . GLU A 1 68  ? 12.874  -38.943 37.909  1.00 76.74  ? 75  GLU A O   1 
ATOM   511   C CB  . GLU A 1 68  ? 15.555  -40.221 38.098  1.00 62.87  ? 75  GLU A CB  1 
ATOM   512   C CG  . GLU A 1 68  ? 16.666  -41.061 38.707  1.00 66.13  ? 75  GLU A CG  1 
ATOM   513   C CD  . GLU A 1 68  ? 16.481  -41.285 40.197  1.00 82.82  ? 75  GLU A CD  1 
ATOM   514   O OE1 . GLU A 1 68  ? 15.550  -40.687 40.783  1.00 94.40  ? 75  GLU A OE1 1 
ATOM   515   O OE2 . GLU A 1 68  ? 17.263  -42.063 40.784  1.00 84.81  ? 75  GLU A OE2 1 
ATOM   516   N N   . CYS A 1 69  ? 12.706  -40.322 36.144  1.00 58.02  ? 76  CYS A N   1 
ATOM   517   C CA  . CYS A 1 69  ? 11.846  -39.438 35.368  1.00 60.80  ? 76  CYS A CA  1 
ATOM   518   C C   . CYS A 1 69  ? 10.403  -39.897 35.295  1.00 77.99  ? 76  CYS A C   1 
ATOM   519   O O   . CYS A 1 69  ? 9.566   -39.235 34.682  1.00 86.49  ? 76  CYS A O   1 
ATOM   520   C CB  . CYS A 1 69  ? 12.382  -39.311 33.944  1.00 41.27  ? 76  CYS A CB  1 
ATOM   521   S SG  . CYS A 1 69  ? 14.046  -38.648 33.854  1.00 52.51  ? 76  CYS A SG  1 
ATOM   522   N N   . ASP A 1 70  ? 10.110  -41.035 35.906  1.00 80.99  ? 77  ASP A N   1 
ATOM   523   C CA  . ASP A 1 70  ? 8.782   -41.620 35.788  1.00 82.90  ? 77  ASP A CA  1 
ATOM   524   C C   . ASP A 1 70  ? 7.735   -40.796 36.530  1.00 81.74  ? 77  ASP A C   1 
ATOM   525   O O   . ASP A 1 70  ? 6.539   -41.068 36.446  1.00 80.92  ? 77  ASP A O   1 
ATOM   526   C CB  . ASP A 1 70  ? 8.795   -43.074 36.261  1.00 101.28 ? 77  ASP A CB  1 
ATOM   527   C CG  . ASP A 1 70  ? 9.710   -43.951 35.412  1.00 119.67 ? 77  ASP A CG  1 
ATOM   528   O OD1 . ASP A 1 70  ? 9.965   -43.591 34.240  1.00 121.43 ? 77  ASP A OD1 1 
ATOM   529   O OD2 . ASP A 1 70  ? 10.175  -44.998 35.914  1.00 127.12 ? 77  ASP A OD2 1 
ATOM   530   N N   . ARG A 1 71  ? 8.191   -39.770 37.239  1.00 100.63 ? 78  ARG A N   1 
ATOM   531   C CA  . ARG A 1 71  ? 7.274   -38.919 37.981  1.00 113.59 ? 78  ARG A CA  1 
ATOM   532   C C   . ARG A 1 71  ? 7.015   -37.590 37.272  1.00 109.28 ? 78  ARG A C   1 
ATOM   533   O O   . ARG A 1 71  ? 6.616   -36.609 37.896  1.00 112.24 ? 78  ARG A O   1 
ATOM   534   C CB  . ARG A 1 71  ? 7.771   -38.693 39.413  1.00 129.72 ? 78  ARG A CB  1 
ATOM   535   C CG  . ARG A 1 71  ? 6.694   -38.185 40.372  1.00 147.85 ? 78  ARG A CG  1 
ATOM   536   C CD  . ARG A 1 71  ? 5.383   -38.958 40.212  1.00 163.77 ? 78  ARG A CD  1 
ATOM   537   N NE  . ARG A 1 71  ? 4.710   -38.659 38.948  1.00 172.82 ? 78  ARG A NE  1 
ATOM   538   C CZ  . ARG A 1 71  ? 3.742   -39.399 38.414  1.00 180.69 ? 78  ARG A CZ  1 
ATOM   539   N NH1 . ARG A 1 71  ? 3.320   -40.493 39.032  1.00 184.82 ? 78  ARG A NH1 1 
ATOM   540   N NH2 . ARG A 1 71  ? 3.197   -39.045 37.258  1.00 182.03 ? 78  ARG A NH2 1 
ATOM   541   N N   . LEU A 1 72  ? 7.236   -37.565 35.963  1.00 83.78  ? 79  LEU A N   1 
ATOM   542   C CA  . LEU A 1 72  ? 6.943   -36.377 35.174  1.00 78.62  ? 79  LEU A CA  1 
ATOM   543   C C   . LEU A 1 72  ? 5.484   -36.380 34.733  1.00 81.33  ? 79  LEU A C   1 
ATOM   544   O O   . LEU A 1 72  ? 4.855   -37.434 34.650  1.00 81.26  ? 79  LEU A O   1 
ATOM   545   C CB  . LEU A 1 72  ? 7.876   -36.284 33.965  1.00 65.14  ? 79  LEU A CB  1 
ATOM   546   C CG  . LEU A 1 72  ? 9.348   -36.033 34.298  1.00 59.21  ? 79  LEU A CG  1 
ATOM   547   C CD1 . LEU A 1 72  ? 10.244  -36.213 33.079  1.00 56.21  ? 79  LEU A CD1 1 
ATOM   548   C CD2 . LEU A 1 72  ? 9.516   -34.647 34.880  1.00 61.29  ? 79  LEU A CD2 1 
ATOM   549   N N   . LEU A 1 73  ? 4.947   -35.195 34.460  1.00 83.48  ? 80  LEU A N   1 
ATOM   550   C CA  . LEU A 1 73  ? 3.561   -35.068 34.027  1.00 88.56  ? 80  LEU A CA  1 
ATOM   551   C C   . LEU A 1 73  ? 3.434   -35.413 32.547  1.00 91.65  ? 80  LEU A C   1 
ATOM   552   O O   . LEU A 1 73  ? 4.260   -35.000 31.736  1.00 86.62  ? 80  LEU A O   1 
ATOM   553   C CB  . LEU A 1 73  ? 3.044   -33.653 34.307  1.00 85.29  ? 80  LEU A CB  1 
ATOM   554   C CG  . LEU A 1 73  ? 1.553   -33.382 34.078  1.00 78.62  ? 80  LEU A CG  1 
ATOM   555   C CD1 . LEU A 1 73  ? 0.710   -34.605 34.428  1.00 76.06  ? 80  LEU A CD1 1 
ATOM   556   C CD2 . LEU A 1 73  ? 1.106   -32.164 34.870  1.00 78.69  ? 80  LEU A CD2 1 
ATOM   557   N N   . SER A 1 74  ? 2.401   -36.172 32.197  1.00 96.42  ? 81  SER A N   1 
ATOM   558   C CA  . SER A 1 74  ? 2.274   -36.695 30.842  1.00 92.47  ? 81  SER A CA  1 
ATOM   559   C C   . SER A 1 74  ? 1.284   -35.918 29.978  1.00 92.44  ? 81  SER A C   1 
ATOM   560   O O   . SER A 1 74  ? 0.308   -36.479 29.480  1.00 100.80 ? 81  SER A O   1 
ATOM   561   C CB  . SER A 1 74  ? 1.890   -38.171 30.880  1.00 93.53  ? 81  SER A CB  1 
ATOM   562   O OG  . SER A 1 74  ? 2.527   -38.875 29.829  1.00 93.55  ? 81  SER A OG  1 
ATOM   563   N N   . VAL A 1 75  A 1.554   -34.629 29.797  1.00 76.30  ? 81  VAL A N   1 
ATOM   564   C CA  . VAL A 1 75  A 0.742   -33.776 28.940  1.00 73.96  ? 81  VAL A CA  1 
ATOM   565   C C   . VAL A 1 75  A 0.787   -34.252 27.494  1.00 68.95  ? 81  VAL A C   1 
ATOM   566   O O   . VAL A 1 75  A 1.819   -34.723 27.026  1.00 65.16  ? 81  VAL A O   1 
ATOM   567   C CB  . VAL A 1 75  A 1.235   -32.324 28.990  1.00 77.44  ? 81  VAL A CB  1 
ATOM   568   C CG1 . VAL A 1 75  A 1.067   -31.756 30.389  1.00 85.90  ? 81  VAL A CG1 1 
ATOM   569   C CG2 . VAL A 1 75  A 2.688   -32.251 28.565  1.00 72.86  ? 81  VAL A CG2 1 
ATOM   570   N N   . PRO A 1 76  ? -0.342  -34.146 26.787  1.00 83.17  ? 82  PRO A N   1 
ATOM   571   C CA  . PRO A 1 76  ? -0.446  -34.546 25.382  1.00 76.65  ? 82  PRO A CA  1 
ATOM   572   C C   . PRO A 1 76  ? -0.280  -33.367 24.438  1.00 73.99  ? 82  PRO A C   1 
ATOM   573   O O   . PRO A 1 76  ? -0.446  -33.526 23.228  1.00 71.52  ? 82  PRO A O   1 
ATOM   574   C CB  . PRO A 1 76  ? -1.887  -35.070 25.270  1.00 79.11  ? 82  PRO A CB  1 
ATOM   575   C CG  . PRO A 1 76  ? -2.471  -34.985 26.670  1.00 92.08  ? 82  PRO A CG  1 
ATOM   576   C CD  . PRO A 1 76  ? -1.665  -33.954 27.385  1.00 87.99  ? 82  PRO A CD  1 
ATOM   577   N N   . GLU A 1 77  ? 0.027   -32.197 24.983  1.00 91.90  ? 83  GLU A N   1 
ATOM   578   C CA  . GLU A 1 77  ? 0.180   -30.995 24.170  1.00 84.36  ? 83  GLU A CA  1 
ATOM   579   C C   . GLU A 1 77  ? 0.851   -29.909 24.991  1.00 77.18  ? 83  GLU A C   1 
ATOM   580   O O   . GLU A 1 77  ? 0.433   -29.633 26.112  1.00 86.89  ? 83  GLU A O   1 
ATOM   581   C CB  . GLU A 1 77  ? -1.184  -30.508 23.667  1.00 91.14  ? 83  GLU A CB  1 
ATOM   582   C CG  . GLU A 1 77  ? -1.119  -29.303 22.733  1.00 86.54  ? 83  GLU A CG  1 
ATOM   583   C CD  . GLU A 1 77  ? -2.496  -28.826 22.281  1.00 88.84  ? 83  GLU A CD  1 
ATOM   584   O OE1 . GLU A 1 77  ? -3.477  -29.028 23.033  1.00 96.19  ? 83  GLU A OE1 1 
ATOM   585   O OE2 . GLU A 1 77  ? -2.593  -28.254 21.170  1.00 81.61  ? 83  GLU A OE2 1 
ATOM   586   N N   . TRP A 1 78  ? 1.901   -29.307 24.444  1.00 76.97  ? 84  TRP A N   1 
ATOM   587   C CA  . TRP A 1 78  ? 2.579   -28.213 25.125  1.00 78.81  ? 84  TRP A CA  1 
ATOM   588   C C   . TRP A 1 78  ? 3.117   -27.196 24.123  1.00 76.19  ? 84  TRP A C   1 
ATOM   589   O O   . TRP A 1 78  ? 3.106   -27.439 22.915  1.00 72.28  ? 84  TRP A O   1 
ATOM   590   C CB  . TRP A 1 78  ? 3.686   -28.738 26.040  1.00 81.93  ? 84  TRP A CB  1 
ATOM   591   C CG  . TRP A 1 78  ? 4.777   -29.444 25.319  1.00 77.33  ? 84  TRP A CG  1 
ATOM   592   C CD1 . TRP A 1 78  ? 5.881   -28.880 24.763  1.00 80.95  ? 84  TRP A CD1 1 
ATOM   593   C CD2 . TRP A 1 78  ? 4.881   -30.851 25.076  1.00 72.65  ? 84  TRP A CD2 1 
ATOM   594   N NE1 . TRP A 1 78  ? 6.669   -29.845 24.184  1.00 75.90  ? 84  TRP A NE1 1 
ATOM   595   C CE2 . TRP A 1 78  ? 6.075   -31.066 24.363  1.00 71.88  ? 84  TRP A CE2 1 
ATOM   596   C CE3 . TRP A 1 78  ? 4.081   -31.952 25.392  1.00 83.32  ? 84  TRP A CE3 1 
ATOM   597   C CZ2 . TRP A 1 78  ? 6.488   -32.330 23.961  1.00 71.13  ? 84  TRP A CZ2 1 
ATOM   598   C CZ3 . TRP A 1 78  ? 4.491   -33.206 24.991  1.00 83.45  ? 84  TRP A CZ3 1 
ATOM   599   C CH2 . TRP A 1 78  ? 5.683   -33.387 24.283  1.00 78.57  ? 84  TRP A CH2 1 
ATOM   600   N N   . SER A 1 79  ? 3.582   -26.058 24.630  1.00 58.13  ? 85  SER A N   1 
ATOM   601   C CA  . SER A 1 79  ? 3.930   -24.919 23.785  1.00 49.95  ? 85  SER A CA  1 
ATOM   602   C C   . SER A 1 79  ? 5.405   -24.565 23.889  1.00 54.08  ? 85  SER A C   1 
ATOM   603   O O   . SER A 1 79  ? 5.952   -23.874 23.029  1.00 46.80  ? 85  SER A O   1 
ATOM   604   C CB  . SER A 1 79  ? 3.112   -23.709 24.201  1.00 61.53  ? 85  SER A CB  1 
ATOM   605   O OG  . SER A 1 79  ? 3.462   -23.335 25.520  1.00 70.62  ? 85  SER A OG  1 
ATOM   606   N N   . TYR A 1 80  ? 6.038   -25.007 24.968  1.00 50.79  ? 86  TYR A N   1 
ATOM   607   C CA  . TYR A 1 80  ? 7.490   -24.934 25.084  1.00 47.42  ? 86  TYR A CA  1 
ATOM   608   C C   . TYR A 1 80  ? 7.974   -25.898 26.160  1.00 48.35  ? 86  TYR A C   1 
ATOM   609   O O   . TYR A 1 80  ? 7.175   -26.496 26.870  1.00 57.81  ? 86  TYR A O   1 
ATOM   610   C CB  . TYR A 1 80  ? 7.981   -23.498 25.328  1.00 46.68  ? 86  TYR A CB  1 
ATOM   611   C CG  . TYR A 1 80  ? 7.573   -22.888 26.651  1.00 55.14  ? 86  TYR A CG  1 
ATOM   612   C CD1 . TYR A 1 80  ? 8.474   -22.802 27.703  1.00 55.11  ? 86  TYR A CD1 1 
ATOM   613   C CD2 . TYR A 1 80  ? 6.291   -22.384 26.843  1.00 65.73  ? 86  TYR A CD2 1 
ATOM   614   C CE1 . TYR A 1 80  ? 8.107   -22.237 28.915  1.00 55.20  ? 86  TYR A CE1 1 
ATOM   615   C CE2 . TYR A 1 80  ? 5.915   -21.819 28.052  1.00 65.49  ? 86  TYR A CE2 1 
ATOM   616   C CZ  . TYR A 1 80  ? 6.826   -21.750 29.083  1.00 63.37  ? 86  TYR A CZ  1 
ATOM   617   O OH  . TYR A 1 80  ? 6.456   -21.190 30.285  1.00 72.13  ? 86  TYR A OH  1 
ATOM   618   N N   . ILE A 1 81  ? 9.282   -26.067 26.262  1.00 56.28  ? 87  ILE A N   1 
ATOM   619   C CA  . ILE A 1 81  ? 9.833   -27.046 27.180  1.00 54.14  ? 87  ILE A CA  1 
ATOM   620   C C   . ILE A 1 81  ? 10.630  -26.368 28.273  1.00 53.92  ? 87  ILE A C   1 
ATOM   621   O O   . ILE A 1 81  ? 11.506  -25.551 27.998  1.00 59.49  ? 87  ILE A O   1 
ATOM   622   C CB  . ILE A 1 81  ? 10.746  -28.030 26.443  1.00 49.47  ? 87  ILE A CB  1 
ATOM   623   C CG1 . ILE A 1 81  ? 9.926   -28.878 25.473  1.00 47.71  ? 87  ILE A CG1 1 
ATOM   624   C CG2 . ILE A 1 81  ? 11.499  -28.899 27.429  1.00 52.72  ? 87  ILE A CG2 1 
ATOM   625   C CD1 . ILE A 1 81  ? 10.717  -29.952 24.793  1.00 42.11  ? 87  ILE A CD1 1 
ATOM   626   N N   . MET A 1 82  ? 10.321  -26.691 29.519  1.00 39.23  ? 88  MET A N   1 
ATOM   627   C CA  . MET A 1 82  ? 11.136  -26.202 30.620  1.00 48.16  ? 88  MET A CA  1 
ATOM   628   C C   . MET A 1 82  ? 12.204  -27.242 30.915  1.00 45.43  ? 88  MET A C   1 
ATOM   629   O O   . MET A 1 82  ? 11.986  -28.424 30.690  1.00 53.08  ? 88  MET A O   1 
ATOM   630   C CB  . MET A 1 82  ? 10.271  -25.920 31.843  1.00 54.82  ? 88  MET A CB  1 
ATOM   631   C CG  . MET A 1 82  ? 9.140   -24.952 31.550  1.00 53.16  ? 88  MET A CG  1 
ATOM   632   S SD  . MET A 1 82  ? 8.113   -24.589 32.977  1.00 55.44  ? 88  MET A SD  1 
ATOM   633   C CE  . MET A 1 82  ? 9.361   -24.494 34.257  1.00 51.98  ? 88  MET A CE  1 
ATOM   634   N N   . GLU A 1 83  ? 13.361  -26.809 31.394  1.00 76.29  ? 89  GLU A N   1 
ATOM   635   C CA  . GLU A 1 83  ? 14.461  -27.730 31.609  1.00 81.33  ? 89  GLU A CA  1 
ATOM   636   C C   . GLU A 1 83  ? 15.599  -27.012 32.288  1.00 82.14  ? 89  GLU A C   1 
ATOM   637   O O   . GLU A 1 83  ? 15.930  -25.895 31.918  1.00 79.87  ? 89  GLU A O   1 
ATOM   638   C CB  . GLU A 1 83  ? 14.942  -28.302 30.276  1.00 70.40  ? 89  GLU A CB  1 
ATOM   639   C CG  . GLU A 1 83  ? 16.338  -28.898 30.343  1.00 58.22  ? 89  GLU A CG  1 
ATOM   640   C CD  . GLU A 1 83  ? 16.728  -29.643 29.086  1.00 51.86  ? 89  GLU A CD  1 
ATOM   641   O OE1 . GLU A 1 83  ? 16.032  -30.612 28.718  1.00 51.44  ? 89  GLU A OE1 1 
ATOM   642   O OE2 . GLU A 1 83  ? 17.742  -29.262 28.466  1.00 51.76  ? 89  GLU A OE2 1 
ATOM   643   N N   . LYS A 1 84  ? 16.205  -27.649 33.278  1.00 70.85  ? 90  LYS A N   1 
ATOM   644   C CA  . LYS A 1 84  ? 17.297  -27.014 34.001  1.00 59.99  ? 90  LYS A CA  1 
ATOM   645   C C   . LYS A 1 84  ? 18.520  -26.843 33.111  1.00 49.05  ? 90  LYS A C   1 
ATOM   646   O O   . LYS A 1 84  ? 18.639  -27.498 32.078  1.00 39.17  ? 90  LYS A O   1 
ATOM   647   C CB  . LYS A 1 84  ? 17.654  -27.803 35.260  1.00 61.16  ? 90  LYS A CB  1 
ATOM   648   C CG  . LYS A 1 84  ? 16.459  -28.088 36.157  1.00 80.97  ? 90  LYS A CG  1 
ATOM   649   C CD  . LYS A 1 84  ? 16.874  -28.283 37.605  1.00 88.16  ? 90  LYS A CD  1 
ATOM   650   C CE  . LYS A 1 84  ? 15.682  -28.684 38.465  1.00 110.14 ? 90  LYS A CE  1 
ATOM   651   N NZ  . LYS A 1 84  ? 14.527  -27.751 38.325  1.00 117.05 ? 90  LYS A NZ  1 
ATOM   652   N N   . GLU A 1 85  ? 19.424  -25.950 33.503  1.00 76.43  ? 91  GLU A N   1 
ATOM   653   C CA  . GLU A 1 85  ? 20.628  -25.720 32.716  1.00 65.24  ? 91  GLU A CA  1 
ATOM   654   C C   . GLU A 1 85  ? 21.406  -27.020 32.515  1.00 69.10  ? 91  GLU A C   1 
ATOM   655   O O   . GLU A 1 85  ? 21.690  -27.406 31.383  1.00 73.90  ? 91  GLU A O   1 
ATOM   656   C CB  . GLU A 1 85  ? 21.515  -24.654 33.362  1.00 62.11  ? 91  GLU A CB  1 
ATOM   657   C CG  . GLU A 1 85  ? 22.712  -24.249 32.505  1.00 68.25  ? 91  GLU A CG  1 
ATOM   658   C CD  . GLU A 1 85  ? 22.306  -23.465 31.269  1.00 76.13  ? 91  GLU A CD  1 
ATOM   659   O OE1 . GLU A 1 85  ? 21.437  -22.572 31.386  1.00 74.73  ? 91  GLU A OE1 1 
ATOM   660   O OE2 . GLU A 1 85  ? 22.852  -23.751 30.179  1.00 78.58  ? 91  GLU A OE2 1 
ATOM   661   N N   . ASN A 1 86  ? 21.741  -27.695 33.611  1.00 76.83  ? 92  ASN A N   1 
ATOM   662   C CA  . ASN A 1 86  ? 22.453  -28.972 33.538  1.00 75.91  ? 92  ASN A CA  1 
ATOM   663   C C   . ASN A 1 86  ? 21.784  -30.101 34.331  1.00 75.24  ? 92  ASN A C   1 
ATOM   664   O O   . ASN A 1 86  ? 22.232  -30.453 35.425  1.00 84.32  ? 92  ASN A O   1 
ATOM   665   C CB  . ASN A 1 86  ? 23.909  -28.800 33.970  1.00 83.00  ? 92  ASN A CB  1 
ATOM   666   C CG  . ASN A 1 86  ? 24.743  -28.104 32.918  1.00 92.15  ? 92  ASN A CG  1 
ATOM   667   O OD1 . ASN A 1 86  ? 24.755  -28.506 31.753  1.00 99.96  ? 92  ASN A OD1 1 
ATOM   668   N ND2 . ASN A 1 86  ? 25.429  -27.039 33.316  1.00 90.01  ? 92  ASN A ND2 1 
ATOM   669   N N   . PRO A 1 87  ? 20.712  -30.676 33.765  1.00 45.09  ? 93  PRO A N   1 
ATOM   670   C CA  . PRO A 1 87  ? 19.901  -31.690 34.437  1.00 53.18  ? 93  PRO A CA  1 
ATOM   671   C C   . PRO A 1 87  ? 20.725  -32.836 35.010  1.00 56.94  ? 93  PRO A C   1 
ATOM   672   O O   . PRO A 1 87  ? 21.820  -33.125 34.528  1.00 62.01  ? 93  PRO A O   1 
ATOM   673   C CB  . PRO A 1 87  ? 18.988  -32.188 33.319  1.00 56.39  ? 93  PRO A CB  1 
ATOM   674   C CG  . PRO A 1 87  ? 18.817  -30.987 32.442  1.00 49.25  ? 93  PRO A CG  1 
ATOM   675   C CD  . PRO A 1 87  ? 20.172  -30.341 32.435  1.00 42.02  ? 93  PRO A CD  1 
ATOM   676   N N   . ARG A 1 88  ? 20.184  -33.474 36.041  1.00 70.98  ? 94  ARG A N   1 
ATOM   677   C CA  . ARG A 1 88  ? 20.866  -34.553 36.740  1.00 70.26  ? 94  ARG A CA  1 
ATOM   678   C C   . ARG A 1 88  ? 20.627  -35.878 36.049  1.00 68.12  ? 94  ARG A C   1 
ATOM   679   O O   . ARG A 1 88  ? 21.537  -36.694 35.898  1.00 69.12  ? 94  ARG A O   1 
ATOM   680   C CB  . ARG A 1 88  ? 20.345  -34.654 38.174  1.00 82.91  ? 94  ARG A CB  1 
ATOM   681   C CG  . ARG A 1 88  ? 20.621  -35.996 38.836  1.00 88.89  ? 94  ARG A CG  1 
ATOM   682   C CD  . ARG A 1 88  ? 19.465  -36.424 39.727  1.00 103.88 ? 94  ARG A CD  1 
ATOM   683   N NE  . ARG A 1 88  ? 19.367  -35.627 40.944  1.00 109.69 ? 94  ARG A NE  1 
ATOM   684   C CZ  . ARG A 1 88  ? 18.286  -35.576 41.713  1.00 120.32 ? 94  ARG A CZ  1 
ATOM   685   N NH1 . ARG A 1 88  ? 17.204  -36.268 41.384  1.00 126.49 ? 94  ARG A NH1 1 
ATOM   686   N NH2 . ARG A 1 88  ? 18.282  -34.826 42.805  1.00 128.41 ? 94  ARG A NH2 1 
ATOM   687   N N   . ASP A 1 89  ? 19.385  -36.080 35.630  1.00 48.53  ? 95  ASP A N   1 
ATOM   688   C CA  . ASP A 1 89  ? 18.944  -37.369 35.128  1.00 50.99  ? 95  ASP A CA  1 
ATOM   689   C C   . ASP A 1 89  ? 18.701  -37.385 33.629  1.00 53.80  ? 95  ASP A C   1 
ATOM   690   O O   . ASP A 1 89  ? 17.680  -36.890 33.140  1.00 63.81  ? 95  ASP A O   1 
ATOM   691   C CB  . ASP A 1 89  ? 17.699  -37.803 35.879  1.00 58.44  ? 95  ASP A CB  1 
ATOM   692   C CG  . ASP A 1 89  ? 17.967  -37.974 37.349  1.00 60.78  ? 95  ASP A CG  1 
ATOM   693   O OD1 . ASP A 1 89  ? 19.047  -38.516 37.687  1.00 51.60  ? 95  ASP A OD1 1 
ATOM   694   O OD2 . ASP A 1 89  ? 17.118  -37.543 38.163  1.00 71.68  ? 95  ASP A OD2 1 
ATOM   695   N N   . GLY A 1 90  A 19.666  -37.960 32.915  1.00 66.97  ? 95  GLY A N   1 
ATOM   696   C CA  . GLY A 1 90  A 19.553  -38.213 31.493  1.00 68.59  ? 95  GLY A CA  1 
ATOM   697   C C   . GLY A 1 90  A 19.926  -39.656 31.207  1.00 64.60  ? 95  GLY A C   1 
ATOM   698   O O   . GLY A 1 90  A 19.318  -40.577 31.747  1.00 70.61  ? 95  GLY A O   1 
ATOM   699   N N   . LEU A 1 91  ? 20.929  -39.850 30.360  1.00 60.39  ? 96  LEU A N   1 
ATOM   700   C CA  . LEU A 1 91  ? 21.407  -41.184 30.045  1.00 56.96  ? 96  LEU A CA  1 
ATOM   701   C C   . LEU A 1 91  ? 22.019  -41.807 31.293  1.00 67.08  ? 96  LEU A C   1 
ATOM   702   O O   . LEU A 1 91  ? 23.226  -41.702 31.516  1.00 65.18  ? 96  LEU A O   1 
ATOM   703   C CB  . LEU A 1 91  ? 22.456  -41.130 28.930  1.00 52.36  ? 96  LEU A CB  1 
ATOM   704   C CG  . LEU A 1 91  ? 22.197  -40.274 27.685  1.00 48.18  ? 96  LEU A CG  1 
ATOM   705   C CD1 . LEU A 1 91  ? 23.274  -40.546 26.652  1.00 42.11  ? 96  LEU A CD1 1 
ATOM   706   C CD2 . LEU A 1 91  ? 20.825  -40.540 27.094  1.00 51.44  ? 96  LEU A CD2 1 
ATOM   707   N N   . CYS A 1 92  ? 21.189  -42.450 32.108  1.00 59.74  ? 97  CYS A N   1 
ATOM   708   C CA  . CYS A 1 92  ? 21.665  -43.050 33.348  1.00 58.05  ? 97  CYS A CA  1 
ATOM   709   C C   . CYS A 1 92  ? 22.792  -44.020 33.059  1.00 54.06  ? 97  CYS A C   1 
ATOM   710   O O   . CYS A 1 92  ? 23.818  -44.001 33.736  1.00 62.57  ? 97  CYS A O   1 
ATOM   711   C CB  . CYS A 1 92  ? 20.525  -43.737 34.092  1.00 62.69  ? 97  CYS A CB  1 
ATOM   712   S SG  . CYS A 1 92  ? 19.526  -44.801 33.070  1.00 64.04  ? 97  CYS A SG  1 
ATOM   713   N N   . TYR A 1 93  ? 22.595  -44.867 32.051  1.00 39.95  ? 98  TYR A N   1 
ATOM   714   C CA  . TYR A 1 93  ? 23.684  -45.658 31.502  1.00 38.25  ? 98  TYR A CA  1 
ATOM   715   C C   . TYR A 1 93  ? 24.344  -44.818 30.420  1.00 36.54  ? 98  TYR A C   1 
ATOM   716   O O   . TYR A 1 93  ? 23.696  -44.474 29.435  1.00 33.51  ? 98  TYR A O   1 
ATOM   717   C CB  . TYR A 1 93  ? 23.166  -46.954 30.900  1.00 35.55  ? 98  TYR A CB  1 
ATOM   718   C CG  . TYR A 1 93  ? 24.278  -47.837 30.380  1.00 38.71  ? 98  TYR A CG  1 
ATOM   719   C CD1 . TYR A 1 93  ? 24.774  -48.882 31.140  1.00 38.81  ? 98  TYR A CD1 1 
ATOM   720   C CD2 . TYR A 1 93  ? 24.846  -47.607 29.146  1.00 45.19  ? 98  TYR A CD2 1 
ATOM   721   C CE1 . TYR A 1 93  ? 25.795  -49.675 30.681  1.00 40.36  ? 98  TYR A CE1 1 
ATOM   722   C CE2 . TYR A 1 93  ? 25.868  -48.395 28.680  1.00 49.10  ? 98  TYR A CE2 1 
ATOM   723   C CZ  . TYR A 1 93  ? 26.337  -49.430 29.449  1.00 45.27  ? 98  TYR A CZ  1 
ATOM   724   O OH  . TYR A 1 93  ? 27.357  -50.213 28.971  1.00 54.58  ? 98  TYR A OH  1 
ATOM   725   N N   . PRO A 1 94  ? 25.638  -44.494 30.590  1.00 50.09  ? 99  PRO A N   1 
ATOM   726   C CA  . PRO A 1 94  ? 26.286  -43.437 29.809  1.00 51.57  ? 99  PRO A CA  1 
ATOM   727   C C   . PRO A 1 94  ? 26.195  -43.688 28.318  1.00 50.94  ? 99  PRO A C   1 
ATOM   728   O O   . PRO A 1 94  ? 25.959  -44.814 27.898  1.00 48.47  ? 99  PRO A O   1 
ATOM   729   C CB  . PRO A 1 94  ? 27.743  -43.520 30.261  1.00 60.86  ? 99  PRO A CB  1 
ATOM   730   C CG  . PRO A 1 94  ? 27.920  -44.920 30.670  1.00 54.15  ? 99  PRO A CG  1 
ATOM   731   C CD  . PRO A 1 94  ? 26.626  -45.301 31.323  1.00 53.87  ? 99  PRO A CD  1 
ATOM   732   N N   . GLY A 1 95  ? 26.388  -42.645 27.523  1.00 49.56  ? 100 GLY A N   1 
ATOM   733   C CA  . GLY A 1 95  ? 26.318  -42.786 26.084  1.00 49.42  ? 100 GLY A CA  1 
ATOM   734   C C   . GLY A 1 95  ? 26.185  -41.472 25.339  1.00 54.32  ? 100 GLY A C   1 
ATOM   735   O O   . GLY A 1 95  ? 26.700  -40.438 25.772  1.00 54.64  ? 100 GLY A O   1 
ATOM   736   N N   . SER A 1 96  ? 25.491  -41.528 24.207  1.00 62.04  ? 101 SER A N   1 
ATOM   737   C CA  . SER A 1 96  ? 25.306  -40.370 23.349  1.00 56.79  ? 101 SER A CA  1 
ATOM   738   C C   . SER A 1 96  ? 24.007  -40.499 22.566  1.00 48.07  ? 101 SER A C   1 
ATOM   739   O O   . SER A 1 96  ? 23.366  -41.552 22.575  1.00 52.32  ? 101 SER A O   1 
ATOM   740   C CB  . SER A 1 96  ? 26.476  -40.231 22.384  1.00 55.50  ? 101 SER A CB  1 
ATOM   741   O OG  . SER A 1 96  ? 26.464  -41.272 21.431  1.00 50.14  ? 101 SER A OG  1 
ATOM   742   N N   . PHE A 1 97  ? 23.631  -39.426 21.876  1.00 32.72  ? 102 PHE A N   1 
ATOM   743   C CA  . PHE A 1 97  ? 22.332  -39.342 21.220  1.00 37.60  ? 102 PHE A CA  1 
ATOM   744   C C   . PHE A 1 97  ? 22.490  -38.549 19.924  1.00 36.50  ? 102 PHE A C   1 
ATOM   745   O O   . PHE A 1 97  ? 22.753  -37.348 19.968  1.00 40.63  ? 102 PHE A O   1 
ATOM   746   C CB  . PHE A 1 97  ? 21.380  -38.607 22.151  1.00 42.34  ? 102 PHE A CB  1 
ATOM   747   C CG  . PHE A 1 97  ? 19.944  -39.006 22.014  1.00 43.85  ? 102 PHE A CG  1 
ATOM   748   C CD1 . PHE A 1 97  ? 19.266  -39.547 23.094  1.00 45.76  ? 102 PHE A CD1 1 
ATOM   749   C CD2 . PHE A 1 97  ? 19.262  -38.809 20.833  1.00 41.71  ? 102 PHE A CD2 1 
ATOM   750   C CE1 . PHE A 1 97  ? 17.944  -39.891 22.995  1.00 51.88  ? 102 PHE A CE1 1 
ATOM   751   C CE2 . PHE A 1 97  ? 17.932  -39.157 20.730  1.00 39.73  ? 102 PHE A CE2 1 
ATOM   752   C CZ  . PHE A 1 97  ? 17.275  -39.698 21.812  1.00 40.08  ? 102 PHE A CZ  1 
ATOM   753   N N   . ASN A 1 98  ? 22.338  -39.204 18.775  1.00 44.84  ? 103 ASN A N   1 
ATOM   754   C CA  . ASN A 1 98  ? 22.608  -38.561 17.489  1.00 37.08  ? 103 ASN A CA  1 
ATOM   755   C C   . ASN A 1 98  ? 21.522  -37.597 17.013  1.00 57.44  ? 103 ASN A C   1 
ATOM   756   O O   . ASN A 1 98  ? 20.330  -37.862 17.181  1.00 59.39  ? 103 ASN A O   1 
ATOM   757   C CB  . ASN A 1 98  ? 22.880  -39.609 16.425  1.00 34.54  ? 103 ASN A CB  1 
ATOM   758   C CG  . ASN A 1 98  ? 24.141  -40.370 16.699  1.00 46.43  ? 103 ASN A CG  1 
ATOM   759   O OD1 . ASN A 1 98  ? 25.165  -39.774 17.023  1.00 61.42  ? 103 ASN A OD1 1 
ATOM   760   N ND2 . ASN A 1 98  ? 24.077  -41.696 16.604  1.00 44.16  ? 103 ASN A ND2 1 
ATOM   761   N N   . ASP A 1 99  ? 21.950  -36.486 16.410  1.00 55.68  ? 104 ASP A N   1 
ATOM   762   C CA  . ASP A 1 99  ? 21.042  -35.420 16.000  1.00 50.16  ? 104 ASP A CA  1 
ATOM   763   C C   . ASP A 1 99  ? 20.128  -35.049 17.159  1.00 48.21  ? 104 ASP A C   1 
ATOM   764   O O   . ASP A 1 99  ? 18.923  -34.864 16.986  1.00 56.73  ? 104 ASP A O   1 
ATOM   765   C CB  . ASP A 1 99  ? 20.221  -35.831 14.777  1.00 53.37  ? 104 ASP A CB  1 
ATOM   766   C CG  . ASP A 1 99  ? 21.069  -35.981 13.528  1.00 58.50  ? 104 ASP A CG  1 
ATOM   767   O OD1 . ASP A 1 99  ? 22.006  -35.178 13.349  1.00 54.82  ? 104 ASP A OD1 1 
ATOM   768   O OD2 . ASP A 1 99  ? 20.801  -36.907 12.727  1.00 53.64  ? 104 ASP A OD2 1 
ATOM   769   N N   . TYR A 1 100 ? 20.721  -34.935 18.343  1.00 40.64  ? 105 TYR A N   1 
ATOM   770   C CA  . TYR A 1 100 ? 19.967  -34.700 19.570  1.00 45.61  ? 105 TYR A CA  1 
ATOM   771   C C   . TYR A 1 100 ? 19.271  -33.338 19.588  1.00 53.34  ? 105 TYR A C   1 
ATOM   772   O O   . TYR A 1 100 ? 18.118  -33.235 20.012  1.00 61.82  ? 105 TYR A O   1 
ATOM   773   C CB  . TYR A 1 100 ? 20.874  -34.876 20.797  1.00 39.39  ? 105 TYR A CB  1 
ATOM   774   C CG  . TYR A 1 100 ? 20.183  -34.702 22.133  1.00 38.28  ? 105 TYR A CG  1 
ATOM   775   C CD1 . TYR A 1 100 ? 19.116  -35.511 22.505  1.00 49.72  ? 105 TYR A CD1 1 
ATOM   776   C CD2 . TYR A 1 100 ? 20.617  -33.745 23.032  1.00 38.93  ? 105 TYR A CD2 1 
ATOM   777   C CE1 . TYR A 1 100 ? 18.489  -35.350 23.737  1.00 52.40  ? 105 TYR A CE1 1 
ATOM   778   C CE2 . TYR A 1 100 ? 19.998  -33.579 24.266  1.00 48.39  ? 105 TYR A CE2 1 
ATOM   779   C CZ  . TYR A 1 100 ? 18.938  -34.380 24.612  1.00 52.35  ? 105 TYR A CZ  1 
ATOM   780   O OH  . TYR A 1 100 ? 18.334  -34.204 25.833  1.00 65.86  ? 105 TYR A OH  1 
ATOM   781   N N   . GLU A 1 101 ? 19.960  -32.298 19.122  1.00 49.67  ? 106 GLU A N   1 
ATOM   782   C CA  . GLU A 1 101 ? 19.394  -30.956 19.182  1.00 44.51  ? 106 GLU A CA  1 
ATOM   783   C C   . GLU A 1 101 ? 18.211  -30.816 18.248  1.00 58.32  ? 106 GLU A C   1 
ATOM   784   O O   . GLU A 1 101 ? 17.198  -30.221 18.606  1.00 74.83  ? 106 GLU A O   1 
ATOM   785   C CB  . GLU A 1 101 ? 20.438  -29.889 18.880  1.00 33.52  ? 106 GLU A CB  1 
ATOM   786   C CG  . GLU A 1 101 ? 21.419  -29.659 20.006  1.00 42.40  ? 106 GLU A CG  1 
ATOM   787   C CD  . GLU A 1 101 ? 22.422  -30.786 20.116  1.00 55.75  ? 106 GLU A CD  1 
ATOM   788   O OE1 . GLU A 1 101 ? 22.524  -31.575 19.148  1.00 63.48  ? 106 GLU A OE1 1 
ATOM   789   O OE2 . GLU A 1 101 ? 23.104  -30.886 21.162  1.00 48.86  ? 106 GLU A OE2 1 
ATOM   790   N N   . GLU A 1 102 ? 18.335  -31.367 17.050  1.00 45.65  ? 107 GLU A N   1 
ATOM   791   C CA  . GLU A 1 102 ? 17.212  -31.363 16.125  1.00 35.42  ? 107 GLU A CA  1 
ATOM   792   C C   . GLU A 1 102 ? 15.989  -31.977 16.789  1.00 44.95  ? 107 GLU A C   1 
ATOM   793   O O   . GLU A 1 102 ? 14.895  -31.424 16.703  1.00 54.63  ? 107 GLU A O   1 
ATOM   794   C CB  . GLU A 1 102 ? 17.558  -32.103 14.839  1.00 35.83  ? 107 GLU A CB  1 
ATOM   795   C CG  . GLU A 1 102 ? 18.571  -31.368 13.970  1.00 41.19  ? 107 GLU A CG  1 
ATOM   796   C CD  . GLU A 1 102 ? 17.973  -30.179 13.251  1.00 52.15  ? 107 GLU A CD  1 
ATOM   797   O OE1 . GLU A 1 102 ? 16.825  -30.283 12.774  1.00 61.95  ? 107 GLU A OE1 1 
ATOM   798   O OE2 . GLU A 1 102 ? 18.653  -29.140 13.166  1.00 52.82  ? 107 GLU A OE2 1 
ATOM   799   N N   . LEU A 1 103 ? 16.179  -33.106 17.466  1.00 44.56  ? 108 LEU A N   1 
ATOM   800   C CA  . LEU A 1 103 ? 15.092  -33.738 18.202  1.00 47.70  ? 108 LEU A CA  1 
ATOM   801   C C   . LEU A 1 103 ? 14.505  -32.745 19.203  1.00 54.61  ? 108 LEU A C   1 
ATOM   802   O O   . LEU A 1 103 ? 13.300  -32.492 19.211  1.00 68.27  ? 108 LEU A O   1 
ATOM   803   C CB  . LEU A 1 103 ? 15.586  -34.997 18.919  1.00 47.60  ? 108 LEU A CB  1 
ATOM   804   C CG  . LEU A 1 103 ? 14.580  -35.885 19.659  1.00 50.08  ? 108 LEU A CG  1 
ATOM   805   C CD1 . LEU A 1 103 ? 13.629  -36.543 18.679  1.00 58.09  ? 108 LEU A CD1 1 
ATOM   806   C CD2 . LEU A 1 103 ? 15.311  -36.936 20.470  1.00 43.76  ? 108 LEU A CD2 1 
ATOM   807   N N   . LYS A 1 104 ? 15.360  -32.172 20.042  1.00 35.56  ? 109 LYS A N   1 
ATOM   808   C CA  . LYS A 1 104 ? 14.916  -31.157 20.994  1.00 39.92  ? 109 LYS A CA  1 
ATOM   809   C C   . LYS A 1 104 ? 14.176  -30.027 20.288  1.00 40.75  ? 109 LYS A C   1 
ATOM   810   O O   . LYS A 1 104 ? 13.268  -29.427 20.853  1.00 55.36  ? 109 LYS A O   1 
ATOM   811   C CB  . LYS A 1 104 ? 16.097  -30.592 21.790  1.00 46.15  ? 109 LYS A CB  1 
ATOM   812   C CG  . LYS A 1 104 ? 16.934  -31.653 22.465  1.00 52.03  ? 109 LYS A CG  1 
ATOM   813   C CD  . LYS A 1 104 ? 17.284  -31.270 23.882  1.00 50.12  ? 109 LYS A CD  1 
ATOM   814   C CE  . LYS A 1 104 ? 18.433  -30.296 23.930  1.00 48.45  ? 109 LYS A CE  1 
ATOM   815   N NZ  . LYS A 1 104 ? 18.753  -29.946 25.341  1.00 55.12  ? 109 LYS A NZ  1 
ATOM   816   N N   . HIS A 1 105 ? 14.557  -29.725 19.054  1.00 51.40  ? 110 HIS A N   1 
ATOM   817   C CA  . HIS A 1 105 ? 13.860  -28.676 18.319  1.00 53.85  ? 110 HIS A CA  1 
ATOM   818   C C   . HIS A 1 105 ? 12.504  -29.184 17.862  1.00 56.74  ? 110 HIS A C   1 
ATOM   819   O O   . HIS A 1 105 ? 11.514  -28.455 17.870  1.00 54.80  ? 110 HIS A O   1 
ATOM   820   C CB  . HIS A 1 105 ? 14.670  -28.219 17.113  1.00 43.87  ? 110 HIS A CB  1 
ATOM   821   C CG  . HIS A 1 105 ? 13.962  -27.215 16.262  1.00 40.67  ? 110 HIS A CG  1 
ATOM   822   N ND1 . HIS A 1 105 ? 14.030  -25.858 16.499  1.00 40.86  ? 110 HIS A ND1 1 
ATOM   823   C CD2 . HIS A 1 105 ? 13.163  -27.370 15.179  1.00 48.73  ? 110 HIS A CD2 1 
ATOM   824   C CE1 . HIS A 1 105 ? 13.310  -25.220 15.594  1.00 45.31  ? 110 HIS A CE1 1 
ATOM   825   N NE2 . HIS A 1 105 ? 12.776  -26.114 14.781  1.00 56.84  ? 110 HIS A NE2 1 
ATOM   826   N N   . LEU A 1 106 ? 12.471  -30.449 17.468  1.00 55.03  ? 111 LEU A N   1 
ATOM   827   C CA  . LEU A 1 106 ? 11.244  -31.075 17.007  1.00 48.59  ? 111 LEU A CA  1 
ATOM   828   C C   . LEU A 1 106 ? 10.231  -31.106 18.134  1.00 56.16  ? 111 LEU A C   1 
ATOM   829   O O   . LEU A 1 106 ? 9.049   -30.850 17.920  1.00 66.88  ? 111 LEU A O   1 
ATOM   830   C CB  . LEU A 1 106 ? 11.529  -32.503 16.520  1.00 40.12  ? 111 LEU A CB  1 
ATOM   831   C CG  . LEU A 1 106 ? 10.335  -33.328 16.050  1.00 45.29  ? 111 LEU A CG  1 
ATOM   832   C CD1 . LEU A 1 106 ? 9.522   -32.541 15.047  1.00 60.98  ? 111 LEU A CD1 1 
ATOM   833   C CD2 . LEU A 1 106 ? 10.795  -34.628 15.449  1.00 41.41  ? 111 LEU A CD2 1 
ATOM   834   N N   . LEU A 1 107 ? 10.714  -31.406 19.336  1.00 43.67  ? 112 LEU A N   1 
ATOM   835   C CA  . LEU A 1 107 ? 9.840   -31.680 20.470  1.00 43.83  ? 112 LEU A CA  1 
ATOM   836   C C   . LEU A 1 107 ? 9.548   -30.451 21.307  1.00 58.29  ? 112 LEU A C   1 
ATOM   837   O O   . LEU A 1 107 ? 8.844   -30.540 22.313  1.00 80.03  ? 112 LEU A O   1 
ATOM   838   C CB  . LEU A 1 107 ? 10.456  -32.752 21.368  1.00 41.97  ? 112 LEU A CB  1 
ATOM   839   C CG  . LEU A 1 107 ? 10.634  -34.150 20.775  1.00 41.37  ? 112 LEU A CG  1 
ATOM   840   C CD1 . LEU A 1 107 ? 11.049  -35.132 21.867  1.00 48.08  ? 112 LEU A CD1 1 
ATOM   841   C CD2 . LEU A 1 107 ? 9.357   -34.617 20.108  1.00 47.19  ? 112 LEU A CD2 1 
ATOM   842   N N   . SER A 1 108 ? 10.090  -29.307 20.898  1.00 38.22  ? 113 SER A N   1 
ATOM   843   C CA  . SER A 1 108 ? 9.966   -28.093 21.704  1.00 47.12  ? 113 SER A CA  1 
ATOM   844   C C   . SER A 1 108 ? 8.501   -27.707 21.885  1.00 54.20  ? 113 SER A C   1 
ATOM   845   O O   . SER A 1 108 ? 8.111   -27.189 22.927  1.00 69.80  ? 113 SER A O   1 
ATOM   846   C CB  . SER A 1 108 ? 10.785  -26.939 21.107  1.00 42.81  ? 113 SER A CB  1 
ATOM   847   O OG  . SER A 1 108 ? 10.340  -26.594 19.810  1.00 38.61  ? 113 SER A OG  1 
ATOM   848   N N   . SER A 1 109 ? 7.695   -27.987 20.869  1.00 50.47  ? 114 SER A N   1 
ATOM   849   C CA  . SER A 1 109 ? 6.264   -27.736 20.934  1.00 50.32  ? 114 SER A CA  1 
ATOM   850   C C   . SER A 1 109 ? 5.500   -28.700 20.034  1.00 51.98  ? 114 SER A C   1 
ATOM   851   O O   . SER A 1 109 ? 5.857   -28.896 18.874  1.00 52.71  ? 114 SER A O   1 
ATOM   852   C CB  . SER A 1 109 ? 5.954   -26.297 20.530  1.00 53.21  ? 114 SER A CB  1 
ATOM   853   O OG  . SER A 1 109 ? 4.978   -26.274 19.500  1.00 62.99  ? 114 SER A OG  1 
ATOM   854   N N   . VAL A 1 110 ? 4.440   -29.290 20.576  1.00 72.16  ? 115 VAL A N   1 
ATOM   855   C CA  . VAL A 1 110 ? 3.655   -30.286 19.854  1.00 68.82  ? 115 VAL A CA  1 
ATOM   856   C C   . VAL A 1 110 ? 2.162   -30.037 20.007  1.00 78.16  ? 115 VAL A C   1 
ATOM   857   O O   . VAL A 1 110 ? 1.712   -29.499 21.020  1.00 90.84  ? 115 VAL A O   1 
ATOM   858   C CB  . VAL A 1 110 ? 3.965   -31.714 20.348  1.00 67.38  ? 115 VAL A CB  1 
ATOM   859   C CG1 . VAL A 1 110 ? 5.423   -32.052 20.100  1.00 64.26  ? 115 VAL A CG1 1 
ATOM   860   C CG2 . VAL A 1 110 ? 3.628   -31.859 21.826  1.00 80.66  ? 115 VAL A CG2 1 
ATOM   861   N N   . LYS A 1 111 ? 1.397   -30.423 18.993  1.00 73.18  ? 116 LYS A N   1 
ATOM   862   C CA  . LYS A 1 111 ? -0.052  -30.356 19.085  1.00 78.07  ? 116 LYS A CA  1 
ATOM   863   C C   . LYS A 1 111 ? -0.539  -31.622 19.762  1.00 73.49  ? 116 LYS A C   1 
ATOM   864   O O   . LYS A 1 111 ? -1.439  -31.587 20.600  1.00 86.60  ? 116 LYS A O   1 
ATOM   865   C CB  . LYS A 1 111 ? -0.693  -30.201 17.705  1.00 89.91  ? 116 LYS A CB  1 
ATOM   866   C CG  . LYS A 1 111 ? -2.102  -29.619 17.754  1.00 96.32  ? 116 LYS A CG  1 
ATOM   867   C CD  . LYS A 1 111 ? -2.299  -28.538 16.695  1.00 106.26 ? 116 LYS A CD  1 
ATOM   868   C CE  . LYS A 1 111 ? -3.343  -27.514 17.132  1.00 110.13 ? 116 LYS A CE  1 
ATOM   869   N NZ  . LYS A 1 111 ? -3.442  -26.383 16.169  1.00 111.91 ? 116 LYS A NZ  1 
ATOM   870   N N   . HIS A 1 112 A 0.073   -32.744 19.402  1.00 62.66  ? 116 HIS A N   1 
ATOM   871   C CA  . HIS A 1 112 A -0.233  -34.006 20.057  1.00 69.12  ? 116 HIS A CA  1 
ATOM   872   C C   . HIS A 1 112 A 0.997   -34.874 20.224  1.00 83.17  ? 116 HIS A C   1 
ATOM   873   O O   . HIS A 1 112 A 1.849   -34.956 19.336  1.00 84.44  ? 116 HIS A O   1 
ATOM   874   C CB  . HIS A 1 112 A -1.310  -34.784 19.302  1.00 66.03  ? 116 HIS A CB  1 
ATOM   875   C CG  . HIS A 1 112 A -1.804  -35.984 20.043  1.00 74.87  ? 116 HIS A CG  1 
ATOM   876   N ND1 . HIS A 1 112 A -1.503  -37.271 19.659  1.00 86.04  ? 116 HIS A ND1 1 
ATOM   877   C CD2 . HIS A 1 112 A -2.559  -36.090 21.161  1.00 75.28  ? 116 HIS A CD2 1 
ATOM   878   C CE1 . HIS A 1 112 A -2.062  -38.121 20.502  1.00 89.40  ? 116 HIS A CE1 1 
ATOM   879   N NE2 . HIS A 1 112 A -2.708  -37.430 21.423  1.00 83.52  ? 116 HIS A NE2 1 
ATOM   880   N N   . PHE A 1 113 B 1.066   -35.535 21.372  1.00 50.23  ? 116 PHE A N   1 
ATOM   881   C CA  . PHE A 1 113 B 2.199   -36.374 21.709  1.00 44.96  ? 116 PHE A CA  1 
ATOM   882   C C   . PHE A 1 113 B 1.736   -37.478 22.648  1.00 56.36  ? 116 PHE A C   1 
ATOM   883   O O   . PHE A 1 113 B 1.358   -37.208 23.785  1.00 77.68  ? 116 PHE A O   1 
ATOM   884   C CB  . PHE A 1 113 B 3.268   -35.524 22.384  1.00 54.12  ? 116 PHE A CB  1 
ATOM   885   C CG  . PHE A 1 113 B 4.505   -36.274 22.722  1.00 59.83  ? 116 PHE A CG  1 
ATOM   886   C CD1 . PHE A 1 113 B 5.437   -36.562 21.745  1.00 43.56  ? 116 PHE A CD1 1 
ATOM   887   C CD2 . PHE A 1 113 B 4.744   -36.687 24.019  1.00 77.46  ? 116 PHE A CD2 1 
ATOM   888   C CE1 . PHE A 1 113 B 6.583   -37.256 22.054  1.00 46.40  ? 116 PHE A CE1 1 
ATOM   889   C CE2 . PHE A 1 113 B 5.889   -37.381 24.339  1.00 76.05  ? 116 PHE A CE2 1 
ATOM   890   C CZ  . PHE A 1 113 B 6.810   -37.671 23.356  1.00 63.93  ? 116 PHE A CZ  1 
ATOM   891   N N   . GLU A 1 114 C 1.756   -38.719 22.176  1.00 55.43  ? 116 GLU A N   1 
ATOM   892   C CA  . GLU A 1 114 C 1.294   -39.837 22.993  1.00 70.27  ? 116 GLU A CA  1 
ATOM   893   C C   . GLU A 1 114 C 2.176   -41.069 22.844  1.00 64.65  ? 116 GLU A C   1 
ATOM   894   O O   . GLU A 1 114 C 2.454   -41.500 21.725  1.00 56.90  ? 116 GLU A O   1 
ATOM   895   C CB  . GLU A 1 114 C -0.146  -40.201 22.632  1.00 80.91  ? 116 GLU A CB  1 
ATOM   896   C CG  . GLU A 1 114 C -0.686  -41.383 23.417  1.00 97.09  ? 116 GLU A CG  1 
ATOM   897   C CD  . GLU A 1 114 C -2.030  -41.864 22.905  1.00 91.69  ? 116 GLU A CD  1 
ATOM   898   O OE1 . GLU A 1 114 C -2.557  -41.254 21.948  1.00 82.96  ? 116 GLU A OE1 1 
ATOM   899   O OE2 . GLU A 1 114 C -2.555  -42.858 23.456  1.00 94.49  ? 116 GLU A OE2 1 
ATOM   900   N N   . LYS A 1 115 ? 2.602   -41.632 23.976  1.00 44.94  ? 117 LYS A N   1 
ATOM   901   C CA  . LYS A 1 115 ? 3.422   -42.850 23.989  1.00 38.42  ? 117 LYS A CA  1 
ATOM   902   C C   . LYS A 1 115 ? 2.606   -44.127 23.695  1.00 43.98  ? 117 LYS A C   1 
ATOM   903   O O   . LYS A 1 115 ? 1.477   -44.283 24.163  1.00 61.49  ? 117 LYS A O   1 
ATOM   904   C CB  . LYS A 1 115 ? 4.179   -42.992 25.315  1.00 39.60  ? 117 LYS A CB  1 
ATOM   905   C CG  . LYS A 1 115 ? 5.057   -44.220 25.381  1.00 44.88  ? 117 LYS A CG  1 
ATOM   906   C CD  . LYS A 1 115 ? 5.103   -44.823 26.776  1.00 58.56  ? 117 LYS A CD  1 
ATOM   907   C CE  . LYS A 1 115 ? 6.092   -44.107 27.683  1.00 67.76  ? 117 LYS A CE  1 
ATOM   908   N NZ  . LYS A 1 115 ? 6.340   -44.873 28.947  1.00 75.31  ? 117 LYS A NZ  1 
ATOM   909   N N   . VAL A 1 116 ? 3.194   -45.043 22.932  1.00 62.96  ? 118 VAL A N   1 
ATOM   910   C CA  . VAL A 1 116 ? 2.442   -46.151 22.361  1.00 61.22  ? 118 VAL A CA  1 
ATOM   911   C C   . VAL A 1 116 ? 3.300   -47.407 22.193  1.00 62.38  ? 118 VAL A C   1 
ATOM   912   O O   . VAL A 1 116 ? 4.366   -47.365 21.583  1.00 69.22  ? 118 VAL A O   1 
ATOM   913   C CB  . VAL A 1 116 ? 1.860   -45.748 20.982  1.00 38.32  ? 118 VAL A CB  1 
ATOM   914   C CG1 . VAL A 1 116 ? 1.200   -46.943 20.294  1.00 43.54  ? 118 VAL A CG1 1 
ATOM   915   C CG2 . VAL A 1 116 ? 0.880   -44.598 21.136  1.00 41.76  ? 118 VAL A CG2 1 
ATOM   916   N N   . LYS A 1 117 ? 2.826   -48.529 22.729  1.00 51.44  ? 119 LYS A N   1 
ATOM   917   C CA  . LYS A 1 117 ? 3.557   -49.792 22.627  1.00 55.07  ? 119 LYS A CA  1 
ATOM   918   C C   . LYS A 1 117 ? 3.532   -50.337 21.198  1.00 53.97  ? 119 LYS A C   1 
ATOM   919   O O   . LYS A 1 117 ? 2.486   -50.360 20.549  1.00 58.41  ? 119 LYS A O   1 
ATOM   920   C CB  . LYS A 1 117 ? 3.000   -50.815 23.616  1.00 58.95  ? 119 LYS A CB  1 
ATOM   921   C CG  . LYS A 1 117 ? 3.815   -52.084 23.717  1.00 61.63  ? 119 LYS A CG  1 
ATOM   922   C CD  . LYS A 1 117 ? 3.439   -52.888 24.955  1.00 79.50  ? 119 LYS A CD  1 
ATOM   923   C CE  . LYS A 1 117 ? 3.767   -52.132 26.234  1.00 85.53  ? 119 LYS A CE  1 
ATOM   924   N NZ  . LYS A 1 117 ? 3.478   -52.933 27.460  1.00 91.15  ? 119 LYS A NZ  1 
ATOM   925   N N   . ILE A 1 118 ? 4.694   -50.765 20.710  1.00 86.18  ? 120 ILE A N   1 
ATOM   926   C CA  . ILE A 1 118 ? 4.833   -51.201 19.321  1.00 80.08  ? 120 ILE A CA  1 
ATOM   927   C C   . ILE A 1 118 ? 5.681   -52.465 19.181  1.00 93.34  ? 120 ILE A C   1 
ATOM   928   O O   . ILE A 1 118 ? 5.554   -53.211 18.209  1.00 100.58 ? 120 ILE A O   1 
ATOM   929   C CB  . ILE A 1 118 ? 5.471   -50.105 18.478  1.00 68.21  ? 120 ILE A CB  1 
ATOM   930   C CG1 . ILE A 1 118 ? 6.672   -49.533 19.228  1.00 70.14  ? 120 ILE A CG1 1 
ATOM   931   C CG2 . ILE A 1 118 ? 4.462   -49.014 18.194  1.00 60.13  ? 120 ILE A CG2 1 
ATOM   932   C CD1 . ILE A 1 118 ? 7.511   -48.577 18.415  1.00 63.67  ? 120 ILE A CD1 1 
ATOM   933   N N   . LEU A 1 119 ? 6.559   -52.681 20.153  1.00 70.89  ? 121 LEU A N   1 
ATOM   934   C CA  . LEU A 1 119 ? 7.389   -53.872 20.203  1.00 63.26  ? 121 LEU A CA  1 
ATOM   935   C C   . LEU A 1 119 ? 7.488   -54.290 21.658  1.00 72.61  ? 121 LEU A C   1 
ATOM   936   O O   . LEU A 1 119 ? 8.447   -53.947 22.342  1.00 84.75  ? 121 LEU A O   1 
ATOM   937   C CB  . LEU A 1 119 ? 8.775   -53.597 19.608  1.00 51.62  ? 121 LEU A CB  1 
ATOM   938   C CG  . LEU A 1 119 ? 8.827   -53.410 18.082  1.00 39.29  ? 121 LEU A CG  1 
ATOM   939   C CD1 . LEU A 1 119 ? 10.063  -52.642 17.647  1.00 37.89  ? 121 LEU A CD1 1 
ATOM   940   C CD2 . LEU A 1 119 ? 8.752   -54.757 17.362  1.00 33.45  ? 121 LEU A CD2 1 
ATOM   941   N N   . PRO A 1 120 ? 6.468   -55.017 22.135  1.00 49.73  ? 122 PRO A N   1 
ATOM   942   C CA  . PRO A 1 120 ? 6.244   -55.442 23.522  1.00 61.63  ? 122 PRO A CA  1 
ATOM   943   C C   . PRO A 1 120 ? 7.368   -56.304 24.081  1.00 67.84  ? 122 PRO A C   1 
ATOM   944   O O   . PRO A 1 120 ? 7.800   -57.263 23.440  1.00 69.09  ? 122 PRO A O   1 
ATOM   945   C CB  . PRO A 1 120 ? 4.957   -56.265 23.430  1.00 65.66  ? 122 PRO A CB  1 
ATOM   946   C CG  . PRO A 1 120 ? 4.268   -55.749 22.224  1.00 63.61  ? 122 PRO A CG  1 
ATOM   947   C CD  . PRO A 1 120 ? 5.358   -55.424 21.257  1.00 53.32  ? 122 PRO A CD  1 
ATOM   948   N N   . LYS A 1 121 ? 7.812   -55.967 25.288  1.00 57.82  ? 123 LYS A N   1 
ATOM   949   C CA  . LYS A 1 121 ? 8.943   -56.624 25.942  1.00 56.84  ? 123 LYS A CA  1 
ATOM   950   C C   . LYS A 1 121 ? 8.874   -58.155 25.952  1.00 65.15  ? 123 LYS A C   1 
ATOM   951   O O   . LYS A 1 121 ? 9.903   -58.824 26.071  1.00 65.69  ? 123 LYS A O   1 
ATOM   952   C CB  . LYS A 1 121 ? 9.074   -56.095 27.369  1.00 51.34  ? 123 LYS A CB  1 
ATOM   953   C CG  . LYS A 1 121 ? 10.379  -56.400 28.076  1.00 49.29  ? 123 LYS A CG  1 
ATOM   954   C CD  . LYS A 1 121 ? 10.456  -55.586 29.372  1.00 72.21  ? 123 LYS A CD  1 
ATOM   955   C CE  . LYS A 1 121 ? 11.741  -55.843 30.142  1.00 74.07  ? 123 LYS A CE  1 
ATOM   956   N NZ  . LYS A 1 121 ? 11.841  -54.963 31.338  1.00 69.25  ? 123 LYS A NZ  1 
ATOM   957   N N   . ASP A 1 122 ? 7.674   -58.714 25.824  1.00 72.60  ? 125 ASP A N   1 
ATOM   958   C CA  . ASP A 1 122 ? 7.508   -60.164 25.921  1.00 71.03  ? 125 ASP A CA  1 
ATOM   959   C C   . ASP A 1 122 ? 7.534   -60.864 24.561  1.00 68.73  ? 125 ASP A C   1 
ATOM   960   O O   . ASP A 1 122 ? 7.500   -62.090 24.490  1.00 73.27  ? 125 ASP A O   1 
ATOM   961   C CB  . ASP A 1 122 ? 6.227   -60.522 26.682  1.00 79.87  ? 125 ASP A CB  1 
ATOM   962   C CG  . ASP A 1 122 ? 4.968   -60.098 25.945  1.00 91.79  ? 125 ASP A CG  1 
ATOM   963   O OD1 . ASP A 1 122 ? 5.000   -60.010 24.697  1.00 90.28  ? 125 ASP A OD1 1 
ATOM   964   O OD2 . ASP A 1 122 ? 3.942   -59.853 26.616  1.00 99.62  ? 125 ASP A OD2 1 
ATOM   965   N N   . ARG A 1 123 ? 7.590   -60.089 23.485  1.00 84.79  ? 126 ARG A N   1 
ATOM   966   C CA  . ARG A 1 123 ? 7.656   -60.664 22.150  1.00 78.62  ? 126 ARG A CA  1 
ATOM   967   C C   . ARG A 1 123 ? 8.972   -61.406 21.946  1.00 72.38  ? 126 ARG A C   1 
ATOM   968   O O   . ARG A 1 123 ? 9.032   -62.383 21.203  1.00 76.32  ? 126 ARG A O   1 
ATOM   969   C CB  . ARG A 1 123 ? 7.517   -59.576 21.087  1.00 84.54  ? 126 ARG A CB  1 
ATOM   970   C CG  . ARG A 1 123 ? 8.649   -58.556 21.121  1.00 92.28  ? 126 ARG A CG  1 
ATOM   971   C CD  . ARG A 1 123 ? 8.589   -57.575 19.965  1.00 84.58  ? 126 ARG A CD  1 
ATOM   972   N NE  . ARG A 1 123 ? 8.927   -58.207 18.694  1.00 83.79  ? 126 ARG A NE  1 
ATOM   973   C CZ  . ARG A 1 123 ? 8.118   -58.243 17.642  1.00 88.40  ? 126 ARG A CZ  1 
ATOM   974   N NH1 . ARG A 1 123 ? 6.921   -57.675 17.707  1.00 89.21  ? 126 ARG A NH1 1 
ATOM   975   N NH2 . ARG A 1 123 ? 8.506   -58.839 16.521  1.00 89.40  ? 126 ARG A NH2 1 
ATOM   976   N N   . TRP A 1 124 ? 10.024  -60.938 22.614  1.00 65.19  ? 127 TRP A N   1 
ATOM   977   C CA  . TRP A 1 124 ? 11.363  -61.493 22.437  1.00 64.24  ? 127 TRP A CA  1 
ATOM   978   C C   . TRP A 1 124 ? 11.524  -62.809 23.186  1.00 78.65  ? 127 TRP A C   1 
ATOM   979   O O   . TRP A 1 124 ? 12.416  -62.952 24.021  1.00 82.56  ? 127 TRP A O   1 
ATOM   980   C CB  . TRP A 1 124 ? 12.424  -60.511 22.931  1.00 62.85  ? 127 TRP A CB  1 
ATOM   981   C CG  . TRP A 1 124 ? 12.310  -59.123 22.384  1.00 64.76  ? 127 TRP A CG  1 
ATOM   982   C CD1 . TRP A 1 124 ? 11.909  -58.003 23.061  1.00 68.83  ? 127 TRP A CD1 1 
ATOM   983   C CD2 . TRP A 1 124 ? 12.613  -58.699 21.051  1.00 56.62  ? 127 TRP A CD2 1 
ATOM   984   N NE1 . TRP A 1 124 ? 11.938  -56.913 22.225  1.00 64.08  ? 127 TRP A NE1 1 
ATOM   985   C CE2 . TRP A 1 124 ? 12.369  -57.316 20.987  1.00 53.29  ? 127 TRP A CE2 1 
ATOM   986   C CE3 . TRP A 1 124 ? 13.065  -59.354 19.906  1.00 43.93  ? 127 TRP A CE3 1 
ATOM   987   C CZ2 . TRP A 1 124 ? 12.567  -56.581 19.824  1.00 37.60  ? 127 TRP A CZ2 1 
ATOM   988   C CZ3 . TRP A 1 124 ? 13.252  -58.622 18.750  1.00 34.52  ? 127 TRP A CZ3 1 
ATOM   989   C CH2 . TRP A 1 124 ? 13.005  -57.253 18.717  1.00 27.00  ? 127 TRP A CH2 1 
ATOM   990   N N   . THR A 1 125 ? 10.657  -63.766 22.877  1.00 64.47  ? 128 THR A N   1 
ATOM   991   C CA  . THR A 1 125 ? 10.666  -65.081 23.516  1.00 63.37  ? 128 THR A CA  1 
ATOM   992   C C   . THR A 1 125 ? 12.001  -65.802 23.346  1.00 60.25  ? 128 THR A C   1 
ATOM   993   O O   . THR A 1 125 ? 12.265  -66.793 24.017  1.00 64.72  ? 128 THR A O   1 
ATOM   994   C CB  . THR A 1 125 ? 9.571   -65.983 22.924  1.00 58.26  ? 128 THR A CB  1 
ATOM   995   O OG1 . THR A 1 125 ? 9.936   -66.370 21.590  1.00 52.92  ? 128 THR A OG1 1 
ATOM   996   C CG2 . THR A 1 125 ? 8.224   -65.249 22.903  1.00 57.91  ? 128 THR A CG2 1 
ATOM   997   N N   . GLN A 1 126 ? 12.837  -65.296 22.447  1.00 81.19  ? 129 GLN A N   1 
ATOM   998   C CA  . GLN A 1 126 ? 14.103  -65.942 22.133  1.00 88.68  ? 129 GLN A CA  1 
ATOM   999   C C   . GLN A 1 126 ? 15.293  -65.286 22.817  1.00 89.18  ? 129 GLN A C   1 
ATOM   1000  O O   . GLN A 1 126 ? 16.430  -65.720 22.635  1.00 84.20  ? 129 GLN A O   1 
ATOM   1001  C CB  . GLN A 1 126 ? 14.326  -65.962 20.621  1.00 94.55  ? 129 GLN A CB  1 
ATOM   1002  C CG  . GLN A 1 126 ? 13.421  -66.924 19.873  1.00 96.51  ? 129 GLN A CG  1 
ATOM   1003  C CD  . GLN A 1 126 ? 13.763  -68.365 20.161  1.00 100.13 ? 129 GLN A CD  1 
ATOM   1004  O OE1 . GLN A 1 126 ? 14.937  -68.724 20.267  1.00 98.30  ? 129 GLN A OE1 1 
ATOM   1005  N NE2 . GLN A 1 126 ? 12.740  -69.202 20.303  1.00 101.41 ? 129 GLN A NE2 1 
ATOM   1006  N N   . HIS A 1 127 ? 15.035  -64.242 23.599  1.00 93.56  ? 130 HIS A N   1 
ATOM   1007  C CA  . HIS A 1 127 ? 16.112  -63.540 24.289  1.00 80.47  ? 130 HIS A CA  1 
ATOM   1008  C C   . HIS A 1 127 ? 15.763  -63.152 25.717  1.00 73.74  ? 130 HIS A C   1 
ATOM   1009  O O   . HIS A 1 127 ? 14.612  -63.221 26.146  1.00 75.96  ? 130 HIS A O   1 
ATOM   1010  C CB  . HIS A 1 127 ? 16.511  -62.273 23.534  1.00 72.11  ? 130 HIS A CB  1 
ATOM   1011  C CG  . HIS A 1 127 ? 16.874  -62.502 22.102  1.00 59.59  ? 130 HIS A CG  1 
ATOM   1012  N ND1 . HIS A 1 127 ? 15.933  -62.750 21.126  1.00 60.76  ? 130 HIS A ND1 1 
ATOM   1013  C CD2 . HIS A 1 127 ? 18.074  -62.501 21.476  1.00 56.65  ? 130 HIS A CD2 1 
ATOM   1014  C CE1 . HIS A 1 127 ? 16.539  -62.904 19.962  1.00 57.05  ? 130 HIS A CE1 1 
ATOM   1015  N NE2 . HIS A 1 127 ? 17.839  -62.756 20.147  1.00 56.68  ? 130 HIS A NE2 1 
ATOM   1016  N N   . THR A 1 128 ? 16.788  -62.723 26.439  1.00 44.79  ? 131 THR A N   1 
ATOM   1017  C CA  . THR A 1 128 ? 16.629  -62.186 27.780  1.00 49.16  ? 131 THR A CA  1 
ATOM   1018  C C   . THR A 1 128 ? 16.455  -60.658 27.762  1.00 53.91  ? 131 THR A C   1 
ATOM   1019  O O   . THR A 1 128 ? 17.299  -59.924 27.247  1.00 54.53  ? 131 THR A O   1 
ATOM   1020  C CB  . THR A 1 128 ? 17.838  -62.543 28.642  1.00 48.85  ? 131 THR A CB  1 
ATOM   1021  O OG1 . THR A 1 128 ? 18.101  -63.944 28.522  1.00 49.54  ? 131 THR A OG1 1 
ATOM   1022  C CG2 . THR A 1 128 ? 17.572  -62.203 30.094  1.00 49.09  ? 131 THR A CG2 1 
ATOM   1023  N N   . THR A 1 129 ? 15.354  -60.192 28.342  1.00 62.56  ? 132 THR A N   1 
ATOM   1024  C CA  . THR A 1 129 ? 14.983  -58.786 28.294  1.00 59.16  ? 132 THR A CA  1 
ATOM   1025  C C   . THR A 1 129 ? 14.913  -58.171 29.686  1.00 70.01  ? 132 THR A C   1 
ATOM   1026  O O   . THR A 1 129 ? 14.564  -57.001 29.844  1.00 71.71  ? 132 THR A O   1 
ATOM   1027  C CB  . THR A 1 129 ? 13.609  -58.616 27.646  1.00 45.94  ? 132 THR A CB  1 
ATOM   1028  O OG1 . THR A 1 129 ? 12.602  -59.119 28.532  1.00 53.03  ? 132 THR A OG1 1 
ATOM   1029  C CG2 . THR A 1 129 ? 13.549  -59.368 26.334  1.00 37.42  ? 132 THR A CG2 1 
ATOM   1030  N N   . THR A 1 130 ? 15.236  -58.966 30.697  1.00 85.08  ? 133 THR A N   1 
ATOM   1031  C CA  . THR A 1 130 ? 15.158  -58.509 32.076  1.00 84.33  ? 133 THR A CA  1 
ATOM   1032  C C   . THR A 1 130 ? 16.489  -57.924 32.512  1.00 91.62  ? 133 THR A C   1 
ATOM   1033  O O   . THR A 1 130 ? 16.698  -57.649 33.689  1.00 92.34  ? 133 THR A O   1 
ATOM   1034  C CB  . THR A 1 130 ? 14.806  -59.663 33.015  1.00 79.29  ? 133 THR A CB  1 
ATOM   1035  O OG1 . THR A 1 130 ? 15.832  -60.659 32.940  1.00 71.82  ? 133 THR A OG1 1 
ATOM   1036  C CG2 . THR A 1 130 ? 13.475  -60.285 32.615  1.00 83.84  ? 133 THR A CG2 1 
ATOM   1037  N N   . GLY A 1 131 ? 17.387  -57.740 31.551  1.00 109.95 ? 134 GLY A N   1 
ATOM   1038  C CA  . GLY A 1 131 ? 18.709  -57.209 31.828  1.00 109.70 ? 134 GLY A CA  1 
ATOM   1039  C C   . GLY A 1 131 ? 18.737  -55.726 32.157  1.00 103.31 ? 134 GLY A C   1 
ATOM   1040  O O   . GLY A 1 131 ? 18.393  -54.877 31.332  1.00 95.79  ? 134 GLY A O   1 
ATOM   1041  N N   . GLY A 1 132 ? 19.151  -55.416 33.379  1.00 99.99  ? 135 GLY A N   1 
ATOM   1042  C CA  . GLY A 1 132 ? 19.337  -54.042 33.789  1.00 92.72  ? 135 GLY A CA  1 
ATOM   1043  C C   . GLY A 1 132 ? 20.811  -53.728 33.965  1.00 75.07  ? 135 GLY A C   1 
ATOM   1044  O O   . GLY A 1 132 ? 21.672  -54.491 33.525  1.00 55.08  ? 135 GLY A O   1 
ATOM   1045  N N   . SER A 1 133 ? 21.102  -52.596 34.599  1.00 66.11  ? 136 SER A N   1 
ATOM   1046  C CA  . SER A 1 133 ? 22.470  -52.227 34.927  1.00 56.25  ? 136 SER A CA  1 
ATOM   1047  C C   . SER A 1 133 ? 22.448  -51.369 36.172  1.00 56.96  ? 136 SER A C   1 
ATOM   1048  O O   . SER A 1 133 ? 21.437  -50.735 36.468  1.00 61.96  ? 136 SER A O   1 
ATOM   1049  C CB  . SER A 1 133 ? 23.127  -51.467 33.777  1.00 51.87  ? 136 SER A CB  1 
ATOM   1050  O OG  . SER A 1 133 ? 24.484  -51.168 34.072  1.00 52.37  ? 136 SER A OG  1 
ATOM   1051  N N   . ARG A 1 134 ? 23.559  -51.350 36.901  1.00 64.55  ? 137 ARG A N   1 
ATOM   1052  C CA  . ARG A 1 134 ? 23.610  -50.658 38.186  1.00 63.10  ? 137 ARG A CA  1 
ATOM   1053  C C   . ARG A 1 134 ? 23.552  -49.137 38.029  1.00 61.81  ? 137 ARG A C   1 
ATOM   1054  O O   . ARG A 1 134 ? 23.078  -48.427 38.917  1.00 65.19  ? 137 ARG A O   1 
ATOM   1055  C CB  . ARG A 1 134 ? 24.854  -51.077 38.971  1.00 68.86  ? 137 ARG A CB  1 
ATOM   1056  C CG  . ARG A 1 134 ? 24.619  -51.185 40.472  1.00 85.02  ? 137 ARG A CG  1 
ATOM   1057  C CD  . ARG A 1 134 ? 25.635  -52.106 41.136  1.00 100.72 ? 137 ARG A CD  1 
ATOM   1058  N NE  . ARG A 1 134 ? 25.319  -52.343 42.542  1.00 110.79 ? 137 ARG A NE  1 
ATOM   1059  C CZ  . ARG A 1 134 ? 24.460  -53.263 42.970  1.00 121.31 ? 137 ARG A CZ  1 
ATOM   1060  N NH1 . ARG A 1 134 ? 23.825  -54.039 42.101  1.00 121.97 ? 137 ARG A NH1 1 
ATOM   1061  N NH2 . ARG A 1 134 ? 24.234  -53.408 44.268  1.00 125.69 ? 137 ARG A NH2 1 
ATOM   1062  N N   . ALA A 1 135 ? 24.032  -48.644 36.893  1.00 86.75  ? 138 ALA A N   1 
ATOM   1063  C CA  . ALA A 1 135 ? 23.983  -47.218 36.606  1.00 77.04  ? 138 ALA A CA  1 
ATOM   1064  C C   . ALA A 1 135 ? 22.540  -46.762 36.423  1.00 81.11  ? 138 ALA A C   1 
ATOM   1065  O O   . ALA A 1 135 ? 22.242  -45.570 36.494  1.00 85.66  ? 138 ALA A O   1 
ATOM   1066  C CB  . ALA A 1 135 ? 24.806  -46.899 35.368  1.00 65.24  ? 138 ALA A CB  1 
ATOM   1067  N N   . CYS A 1 136 ? 21.651  -47.721 36.181  1.00 61.02  ? 139 CYS A N   1 
ATOM   1068  C CA  . CYS A 1 136 ? 20.227  -47.445 36.029  1.00 66.58  ? 139 CYS A CA  1 
ATOM   1069  C C   . CYS A 1 136 ? 19.433  -48.112 37.145  1.00 81.21  ? 139 CYS A C   1 
ATOM   1070  O O   . CYS A 1 136 ? 18.302  -48.557 36.948  1.00 91.82  ? 139 CYS A O   1 
ATOM   1071  C CB  . CYS A 1 136 ? 19.726  -47.916 34.661  1.00 62.36  ? 139 CYS A CB  1 
ATOM   1072  S SG  . CYS A 1 136 ? 20.067  -46.776 33.316  1.00 74.08  ? 139 CYS A SG  1 
ATOM   1073  N N   . ALA A 1 137 ? 20.039  -48.168 38.324  1.00 58.70  ? 140 ALA A N   1 
ATOM   1074  C CA  . ALA A 1 137 ? 19.442  -48.839 39.472  1.00 58.79  ? 140 ALA A CA  1 
ATOM   1075  C C   . ALA A 1 137 ? 18.115  -48.231 39.918  1.00 75.09  ? 140 ALA A C   1 
ATOM   1076  O O   . ALA A 1 137 ? 17.891  -47.030 39.793  1.00 76.14  ? 140 ALA A O   1 
ATOM   1077  C CB  . ALA A 1 137 ? 20.425  -48.869 40.632  1.00 48.68  ? 140 ALA A CB  1 
ATOM   1078  N N   . VAL A 1 138 ? 17.246  -49.087 40.442  1.00 65.74  ? 141 VAL A N   1 
ATOM   1079  C CA  . VAL A 1 138 ? 15.959  -48.690 41.000  1.00 73.27  ? 141 VAL A CA  1 
ATOM   1080  C C   . VAL A 1 138 ? 15.789  -49.367 42.359  1.00 85.61  ? 141 VAL A C   1 
ATOM   1081  O O   . VAL A 1 138 ? 15.682  -50.594 42.449  1.00 88.18  ? 141 VAL A O   1 
ATOM   1082  C CB  . VAL A 1 138 ? 14.788  -49.098 40.075  1.00 61.60  ? 141 VAL A CB  1 
ATOM   1083  C CG1 . VAL A 1 138 ? 13.447  -48.905 40.776  1.00 59.24  ? 141 VAL A CG1 1 
ATOM   1084  C CG2 . VAL A 1 138 ? 14.839  -48.324 38.765  1.00 56.68  ? 141 VAL A CG2 1 
ATOM   1085  N N   . SER A 1 139 ? 15.775  -48.562 43.416  1.00 74.68  ? 142 SER A N   1 
ATOM   1086  C CA  . SER A 1 139 ? 15.703  -49.077 44.782  1.00 77.73  ? 142 SER A CA  1 
ATOM   1087  C C   . SER A 1 139 ? 16.680  -50.227 45.004  1.00 71.54  ? 142 SER A C   1 
ATOM   1088  O O   . SER A 1 139 ? 16.269  -51.354 45.251  1.00 76.39  ? 142 SER A O   1 
ATOM   1089  C CB  . SER A 1 139 ? 14.272  -49.506 45.140  1.00 81.29  ? 142 SER A CB  1 
ATOM   1090  O OG  . SER A 1 139 ? 13.844  -50.605 44.356  1.00 75.28  ? 142 SER A OG  1 
ATOM   1091  N N   . GLY A 1 140 ? 17.973  -49.935 44.899  1.00 61.63  ? 143 GLY A N   1 
ATOM   1092  C CA  . GLY A 1 140 ? 19.008  -50.901 45.232  1.00 59.30  ? 143 GLY A CA  1 
ATOM   1093  C C   . GLY A 1 140 ? 19.382  -51.876 44.129  1.00 59.43  ? 143 GLY A C   1 
ATOM   1094  O O   . GLY A 1 140 ? 20.552  -52.246 43.989  1.00 49.77  ? 143 GLY A O   1 
ATOM   1095  N N   . ASN A 1 141 ? 18.387  -52.283 43.345  1.00 89.95  ? 144 ASN A N   1 
ATOM   1096  C CA  . ASN A 1 141 ? 18.575  -53.279 42.294  1.00 80.47  ? 144 ASN A CA  1 
ATOM   1097  C C   . ASN A 1 141 ? 18.822  -52.660 40.921  1.00 68.37  ? 144 ASN A C   1 
ATOM   1098  O O   . ASN A 1 141 ? 18.317  -51.580 40.627  1.00 67.19  ? 144 ASN A O   1 
ATOM   1099  C CB  . ASN A 1 141 ? 17.360  -54.209 42.232  1.00 88.31  ? 144 ASN A CB  1 
ATOM   1100  C CG  . ASN A 1 141 ? 17.170  -55.003 43.508  1.00 99.62  ? 144 ASN A CG  1 
ATOM   1101  O OD1 . ASN A 1 141 ? 18.140  -55.375 44.168  1.00 97.60  ? 144 ASN A OD1 1 
ATOM   1102  N ND2 . ASN A 1 141 ? 15.916  -55.266 43.864  1.00 108.82 ? 144 ASN A ND2 1 
ATOM   1103  N N   . PRO A 1 142 ? 19.611  -53.345 40.079  1.00 76.31  ? 145 PRO A N   1 
ATOM   1104  C CA  . PRO A 1 142 ? 19.866  -52.941 38.691  1.00 69.26  ? 145 PRO A CA  1 
ATOM   1105  C C   . PRO A 1 142 ? 18.589  -52.857 37.865  1.00 80.36  ? 145 PRO A C   1 
ATOM   1106  O O   . PRO A 1 142 ? 17.701  -53.692 38.013  1.00 90.25  ? 145 PRO A O   1 
ATOM   1107  C CB  . PRO A 1 142 ? 20.752  -54.068 38.161  1.00 60.18  ? 145 PRO A CB  1 
ATOM   1108  C CG  . PRO A 1 142 ? 21.458  -54.592 39.371  1.00 55.61  ? 145 PRO A CG  1 
ATOM   1109  C CD  . PRO A 1 142 ? 20.453  -54.484 40.487  1.00 72.34  ? 145 PRO A CD  1 
ATOM   1110  N N   . SER A 1 143 ? 18.507  -51.852 37.001  1.00 69.33  ? 146 SER A N   1 
ATOM   1111  C CA  . SER A 1 143 ? 17.346  -51.673 36.138  1.00 66.07  ? 146 SER A CA  1 
ATOM   1112  C C   . SER A 1 143 ? 17.770  -51.009 34.830  1.00 55.67  ? 146 SER A C   1 
ATOM   1113  O O   . SER A 1 143 ? 18.952  -51.018 34.488  1.00 50.61  ? 146 SER A O   1 
ATOM   1114  C CB  . SER A 1 143 ? 16.275  -50.846 36.841  1.00 71.67  ? 146 SER A CB  1 
ATOM   1115  O OG  . SER A 1 143 ? 15.105  -50.754 36.047  1.00 75.32  ? 146 SER A OG  1 
ATOM   1116  N N   . PHE A 1 144 ? 16.819  -50.424 34.105  1.00 58.38  ? 147 PHE A N   1 
ATOM   1117  C CA  . PHE A 1 144 ? 17.112  -49.893 32.778  1.00 52.81  ? 147 PHE A CA  1 
ATOM   1118  C C   . PHE A 1 144 ? 16.001  -48.993 32.245  1.00 55.62  ? 147 PHE A C   1 
ATOM   1119  O O   . PHE A 1 144 ? 14.861  -49.067 32.700  1.00 66.81  ? 147 PHE A O   1 
ATOM   1120  C CB  . PHE A 1 144 ? 17.319  -51.067 31.827  1.00 49.88  ? 147 PHE A CB  1 
ATOM   1121  C CG  . PHE A 1 144 ? 17.872  -50.684 30.490  1.00 46.19  ? 147 PHE A CG  1 
ATOM   1122  C CD1 . PHE A 1 144 ? 19.207  -50.353 30.350  1.00 33.10  ? 147 PHE A CD1 1 
ATOM   1123  C CD2 . PHE A 1 144 ? 17.064  -50.695 29.367  1.00 50.36  ? 147 PHE A CD2 1 
ATOM   1124  C CE1 . PHE A 1 144 ? 19.723  -50.022 29.120  1.00 28.43  ? 147 PHE A CE1 1 
ATOM   1125  C CE2 . PHE A 1 144 ? 17.572  -50.362 28.132  1.00 49.99  ? 147 PHE A CE2 1 
ATOM   1126  C CZ  . PHE A 1 144 ? 18.905  -50.028 28.006  1.00 42.93  ? 147 PHE A CZ  1 
ATOM   1127  N N   . PHE A 1 145 ? 16.333  -48.156 31.268  1.00 58.76  ? 148 PHE A N   1 
ATOM   1128  C CA  . PHE A 1 145 ? 15.345  -47.280 30.639  1.00 62.24  ? 148 PHE A CA  1 
ATOM   1129  C C   . PHE A 1 145 ? 13.990  -47.955 30.456  1.00 60.74  ? 148 PHE A C   1 
ATOM   1130  O O   . PHE A 1 145 ? 13.859  -48.919 29.721  1.00 63.64  ? 148 PHE A O   1 
ATOM   1131  C CB  . PHE A 1 145 ? 15.849  -46.781 29.281  1.00 57.61  ? 148 PHE A CB  1 
ATOM   1132  C CG  . PHE A 1 145 ? 17.164  -46.072 29.349  1.00 49.02  ? 148 PHE A CG  1 
ATOM   1133  C CD1 . PHE A 1 145 ? 17.240  -44.772 29.808  1.00 49.71  ? 148 PHE A CD1 1 
ATOM   1134  C CD2 . PHE A 1 145 ? 18.325  -46.707 28.948  1.00 42.04  ? 148 PHE A CD2 1 
ATOM   1135  C CE1 . PHE A 1 145 ? 18.449  -44.115 29.869  1.00 41.18  ? 148 PHE A CE1 1 
ATOM   1136  C CE2 . PHE A 1 145 ? 19.546  -46.057 29.011  1.00 27.14  ? 148 PHE A CE2 1 
ATOM   1137  C CZ  . PHE A 1 145 ? 19.607  -44.759 29.476  1.00 31.99  ? 148 PHE A CZ  1 
ATOM   1138  N N   . ARG A 1 146 ? 12.976  -47.422 31.114  1.00 41.06  ? 149 ARG A N   1 
ATOM   1139  C CA  . ARG A 1 146 ? 11.649  -48.016 31.091  1.00 43.38  ? 149 ARG A CA  1 
ATOM   1140  C C   . ARG A 1 146 ? 10.997  -48.081 29.704  1.00 49.26  ? 149 ARG A C   1 
ATOM   1141  O O   . ARG A 1 146 ? 9.880   -48.584 29.573  1.00 58.29  ? 149 ARG A O   1 
ATOM   1142  C CB  . ARG A 1 146 ? 10.727  -47.261 32.050  1.00 48.19  ? 149 ARG A CB  1 
ATOM   1143  C CG  . ARG A 1 146 ? 11.398  -46.807 33.344  1.00 64.44  ? 149 ARG A CG  1 
ATOM   1144  C CD  . ARG A 1 146 ? 11.730  -47.981 34.246  1.00 84.31  ? 149 ARG A CD  1 
ATOM   1145  N NE  . ARG A 1 146 ? 10.525  -48.670 34.701  1.00 99.73  ? 149 ARG A NE  1 
ATOM   1146  C CZ  . ARG A 1 146 ? 9.914   -48.427 35.856  1.00 116.33 ? 149 ARG A CZ  1 
ATOM   1147  N NH1 . ARG A 1 146 ? 10.399  -47.514 36.688  1.00 119.29 ? 149 ARG A NH1 1 
ATOM   1148  N NH2 . ARG A 1 146 ? 8.820   -49.103 36.180  1.00 125.52 ? 149 ARG A NH2 1 
ATOM   1149  N N   . ASN A 1 147 ? 11.674  -47.588 28.671  1.00 47.76  ? 150 ASN A N   1 
ATOM   1150  C CA  . ASN A 1 147 ? 11.051  -47.537 27.347  1.00 47.69  ? 150 ASN A CA  1 
ATOM   1151  C C   . ASN A 1 147 ? 11.804  -48.305 26.274  1.00 50.50  ? 150 ASN A C   1 
ATOM   1152  O O   . ASN A 1 147 ? 11.319  -48.464 25.151  1.00 52.46  ? 150 ASN A O   1 
ATOM   1153  C CB  . ASN A 1 147 ? 10.855  -46.093 26.885  1.00 48.55  ? 150 ASN A CB  1 
ATOM   1154  C CG  . ASN A 1 147 ? 9.828   -45.348 27.706  1.00 56.19  ? 150 ASN A CG  1 
ATOM   1155  O OD1 . ASN A 1 147 ? 8.960   -45.950 28.341  1.00 63.46  ? 150 ASN A OD1 1 
ATOM   1156  N ND2 . ASN A 1 147 ? 9.916   -44.023 27.691  1.00 51.75  ? 150 ASN A ND2 1 
ATOM   1157  N N   . MET A 1 148 ? 12.993  -48.770 26.623  1.00 58.25  ? 151 MET A N   1 
ATOM   1158  C CA  . MET A 1 148 ? 13.788  -49.573 25.719  1.00 48.15  ? 151 MET A CA  1 
ATOM   1159  C C   . MET A 1 148 ? 13.848  -50.989 26.262  1.00 49.59  ? 151 MET A C   1 
ATOM   1160  O O   . MET A 1 148 ? 13.671  -51.213 27.462  1.00 58.78  ? 151 MET A O   1 
ATOM   1161  C CB  . MET A 1 148 ? 15.201  -49.004 25.633  1.00 54.86  ? 151 MET A CB  1 
ATOM   1162  C CG  . MET A 1 148 ? 15.236  -47.499 25.577  1.00 54.04  ? 151 MET A CG  1 
ATOM   1163  S SD  . MET A 1 148 ? 14.303  -46.904 24.163  1.00 49.94  ? 151 MET A SD  1 
ATOM   1164  C CE  . MET A 1 148 ? 15.360  -47.485 22.843  1.00 36.14  ? 151 MET A CE  1 
ATOM   1165  N N   . VAL A 1 149 ? 14.087  -51.951 25.382  1.00 49.40  ? 152 VAL A N   1 
ATOM   1166  C CA  . VAL A 1 149 ? 14.396  -53.298 25.830  1.00 54.79  ? 152 VAL A CA  1 
ATOM   1167  C C   . VAL A 1 149 ? 15.870  -53.531 25.574  1.00 54.65  ? 152 VAL A C   1 
ATOM   1168  O O   . VAL A 1 149 ? 16.405  -53.125 24.542  1.00 61.81  ? 152 VAL A O   1 
ATOM   1169  C CB  . VAL A 1 149 ? 13.595  -54.377 25.082  1.00 50.15  ? 152 VAL A CB  1 
ATOM   1170  C CG1 . VAL A 1 149 ? 13.791  -55.715 25.755  1.00 58.94  ? 152 VAL A CG1 1 
ATOM   1171  C CG2 . VAL A 1 149 ? 12.121  -54.024 25.027  1.00 43.04  ? 152 VAL A CG2 1 
ATOM   1172  N N   . TRP A 1 150 ? 16.530  -54.179 26.519  1.00 40.02  ? 153 TRP A N   1 
ATOM   1173  C CA  . TRP A 1 150 ? 17.936  -54.480 26.362  1.00 42.83  ? 153 TRP A CA  1 
ATOM   1174  C C   . TRP A 1 150 ? 18.110  -55.961 26.038  1.00 61.08  ? 153 TRP A C   1 
ATOM   1175  O O   . TRP A 1 150 ? 18.417  -56.777 26.910  1.00 71.57  ? 153 TRP A O   1 
ATOM   1176  C CB  . TRP A 1 150 ? 18.691  -54.098 27.623  1.00 37.09  ? 153 TRP A CB  1 
ATOM   1177  C CG  . TRP A 1 150 ? 20.152  -54.210 27.481  1.00 43.58  ? 153 TRP A CG  1 
ATOM   1178  C CD1 . TRP A 1 150 ? 20.837  -54.757 26.437  1.00 50.47  ? 153 TRP A CD1 1 
ATOM   1179  C CD2 . TRP A 1 150 ? 21.133  -53.756 28.411  1.00 50.35  ? 153 TRP A CD2 1 
ATOM   1180  N NE1 . TRP A 1 150 ? 22.193  -54.677 26.664  1.00 50.27  ? 153 TRP A NE1 1 
ATOM   1181  C CE2 . TRP A 1 150 ? 22.398  -54.065 27.873  1.00 45.82  ? 153 TRP A CE2 1 
ATOM   1182  C CE3 . TRP A 1 150 ? 21.066  -53.122 29.651  1.00 51.64  ? 153 TRP A CE3 1 
ATOM   1183  C CZ2 . TRP A 1 150 ? 23.582  -53.760 28.532  1.00 33.55  ? 153 TRP A CZ2 1 
ATOM   1184  C CZ3 . TRP A 1 150 ? 22.243  -52.819 30.303  1.00 38.74  ? 153 TRP A CZ3 1 
ATOM   1185  C CH2 . TRP A 1 150 ? 23.485  -53.134 29.741  1.00 28.42  ? 153 TRP A CH2 1 
ATOM   1186  N N   . LEU A 1 151 ? 17.900  -56.295 24.769  1.00 58.60  ? 154 LEU A N   1 
ATOM   1187  C CA  . LEU A 1 151 ? 18.015  -57.665 24.288  1.00 51.89  ? 154 LEU A CA  1 
ATOM   1188  C C   . LEU A 1 151 ? 19.376  -58.262 24.597  1.00 54.90  ? 154 LEU A C   1 
ATOM   1189  O O   . LEU A 1 151 ? 20.407  -57.714 24.205  1.00 59.17  ? 154 LEU A O   1 
ATOM   1190  C CB  . LEU A 1 151 ? 17.751  -57.718 22.784  1.00 40.08  ? 154 LEU A CB  1 
ATOM   1191  C CG  . LEU A 1 151 ? 16.297  -57.945 22.361  1.00 39.00  ? 154 LEU A CG  1 
ATOM   1192  C CD1 . LEU A 1 151 ? 15.345  -57.313 23.343  1.00 39.88  ? 154 LEU A CD1 1 
ATOM   1193  C CD2 . LEU A 1 151 ? 16.046  -57.411 20.956  1.00 33.99  ? 154 LEU A CD2 1 
ATOM   1194  N N   . THR A 1 152 ? 19.371  -59.387 25.307  1.00 58.31  ? 155 THR A N   1 
ATOM   1195  C CA  . THR A 1 152 ? 20.603  -60.128 25.575  1.00 59.26  ? 155 THR A CA  1 
ATOM   1196  C C   . THR A 1 152 ? 20.483  -61.632 25.357  1.00 62.53  ? 155 THR A C   1 
ATOM   1197  O O   . THR A 1 152 ? 19.395  -62.176 25.155  1.00 68.48  ? 155 THR A O   1 
ATOM   1198  C CB  . THR A 1 152 ? 21.158  -59.878 26.998  1.00 49.78  ? 155 THR A CB  1 
ATOM   1199  O OG1 . THR A 1 152 ? 20.104  -60.006 27.963  1.00 59.90  ? 155 THR A OG1 1 
ATOM   1200  C CG2 . THR A 1 152 ? 21.767  -58.490 27.092  1.00 40.11  ? 155 THR A CG2 1 
ATOM   1201  N N   . GLU A 1 153 ? 21.636  -62.286 25.399  1.00 50.75  ? 156 GLU A N   1 
ATOM   1202  C CA  . GLU A 1 153 ? 21.745  -63.726 25.255  1.00 50.63  ? 156 GLU A CA  1 
ATOM   1203  C C   . GLU A 1 153 ? 20.800  -64.444 26.197  1.00 53.80  ? 156 GLU A C   1 
ATOM   1204  O O   . GLU A 1 153 ? 20.458  -63.928 27.264  1.00 58.20  ? 156 GLU A O   1 
ATOM   1205  C CB  . GLU A 1 153 ? 23.187  -64.160 25.537  1.00 56.53  ? 156 GLU A CB  1 
ATOM   1206  C CG  . GLU A 1 153 ? 23.336  -65.583 26.055  1.00 65.25  ? 156 GLU A CG  1 
ATOM   1207  C CD  . GLU A 1 153 ? 23.262  -65.676 27.570  1.00 66.71  ? 156 GLU A CD  1 
ATOM   1208  O OE1 . GLU A 1 153 ? 24.193  -65.186 28.244  1.00 58.51  ? 156 GLU A OE1 1 
ATOM   1209  O OE2 . GLU A 1 153 ? 22.274  -66.243 28.085  1.00 74.59  ? 156 GLU A OE2 1 
ATOM   1210  N N   . LYS A 1 154 ? 20.373  -65.633 25.783  1.00 52.00  ? 157 LYS A N   1 
ATOM   1211  C CA  . LYS A 1 154 ? 19.606  -66.529 26.636  1.00 54.54  ? 157 LYS A CA  1 
ATOM   1212  C C   . LYS A 1 154 ? 20.028  -67.958 26.341  1.00 54.93  ? 157 LYS A C   1 
ATOM   1213  O O   . LYS A 1 154 ? 20.144  -68.351 25.185  1.00 52.35  ? 157 LYS A O   1 
ATOM   1214  C CB  . LYS A 1 154 ? 18.103  -66.361 26.411  1.00 56.49  ? 157 LYS A CB  1 
ATOM   1215  C CG  . LYS A 1 154 ? 17.272  -67.464 27.048  1.00 60.74  ? 157 LYS A CG  1 
ATOM   1216  C CD  . LYS A 1 154 ? 15.882  -66.992 27.434  1.00 64.69  ? 157 LYS A CD  1 
ATOM   1217  C CE  . LYS A 1 154 ? 14.979  -66.816 26.228  1.00 69.63  ? 157 LYS A CE  1 
ATOM   1218  N NZ  . LYS A 1 154 ? 13.644  -66.277 26.639  1.00 79.54  ? 157 LYS A NZ  1 
ATOM   1219  N N   . GLY A 1 155 ? 20.267  -68.730 27.391  1.00 60.14  ? 158 GLY A N   1 
ATOM   1220  C CA  . GLY A 1 155 ? 20.729  -70.091 27.223  1.00 57.80  ? 158 GLY A CA  1 
ATOM   1221  C C   . GLY A 1 155 ? 21.993  -70.119 26.396  1.00 54.23  ? 158 GLY A C   1 
ATOM   1222  O O   . GLY A 1 155 ? 22.238  -71.060 25.646  1.00 62.50  ? 158 GLY A O   1 
ATOM   1223  N N   . SER A 1 156 ? 22.788  -69.066 26.530  1.00 48.60  ? 159 SER A N   1 
ATOM   1224  C CA  . SER A 1 156 ? 24.066  -68.962 25.837  1.00 62.60  ? 159 SER A CA  1 
ATOM   1225  C C   . SER A 1 156 ? 23.916  -68.856 24.322  1.00 74.46  ? 159 SER A C   1 
ATOM   1226  O O   . SER A 1 156 ? 24.878  -69.046 23.577  1.00 81.22  ? 159 SER A O   1 
ATOM   1227  C CB  . SER A 1 156 ? 24.982  -70.125 26.214  1.00 64.71  ? 159 SER A CB  1 
ATOM   1228  O OG  . SER A 1 156 ? 25.296  -70.085 27.593  1.00 75.14  ? 159 SER A OG  1 
ATOM   1229  N N   . ASN A 1 157 ? 22.707  -68.542 23.871  1.00 87.27  ? 160 ASN A N   1 
ATOM   1230  C CA  . ASN A 1 157 ? 22.472  -68.280 22.456  1.00 79.74  ? 160 ASN A CA  1 
ATOM   1231  C C   . ASN A 1 157 ? 21.744  -66.964 22.211  1.00 75.88  ? 160 ASN A C   1 
ATOM   1232  O O   . ASN A 1 157 ? 20.715  -66.685 22.826  1.00 77.58  ? 160 ASN A O   1 
ATOM   1233  C CB  . ASN A 1 157 ? 21.715  -69.437 21.800  1.00 88.78  ? 160 ASN A CB  1 
ATOM   1234  C CG  . ASN A 1 157 ? 22.642  -70.506 21.268  1.00 105.99 ? 160 ASN A CG  1 
ATOM   1235  O OD1 . ASN A 1 157 ? 23.754  -70.211 20.826  1.00 113.07 ? 160 ASN A OD1 1 
ATOM   1236  N ND2 . ASN A 1 157 ? 22.191  -71.758 21.305  1.00 111.73 ? 160 ASN A ND2 1 
ATOM   1237  N N   . TYR A 1 158 ? 22.295  -66.154 21.317  1.00 68.25  ? 161 TYR A N   1 
ATOM   1238  C CA  . TYR A 1 158 ? 21.631  -64.944 20.864  1.00 64.52  ? 161 TYR A CA  1 
ATOM   1239  C C   . TYR A 1 158 ? 21.235  -65.161 19.409  1.00 53.46  ? 161 TYR A C   1 
ATOM   1240  O O   . TYR A 1 158 ? 21.986  -64.819 18.499  1.00 44.36  ? 161 TYR A O   1 
ATOM   1241  C CB  . TYR A 1 158 ? 22.574  -63.744 20.995  1.00 65.24  ? 161 TYR A CB  1 
ATOM   1242  C CG  . TYR A 1 158 ? 21.931  -62.389 20.778  1.00 59.65  ? 161 TYR A CG  1 
ATOM   1243  C CD1 . TYR A 1 158 ? 21.675  -61.542 21.848  1.00 62.65  ? 161 TYR A CD1 1 
ATOM   1244  C CD2 . TYR A 1 158 ? 21.596  -61.951 19.507  1.00 49.19  ? 161 TYR A CD2 1 
ATOM   1245  C CE1 . TYR A 1 158 ? 21.096  -60.304 21.658  1.00 61.68  ? 161 TYR A CE1 1 
ATOM   1246  C CE2 . TYR A 1 158 ? 21.011  -60.715 19.305  1.00 45.49  ? 161 TYR A CE2 1 
ATOM   1247  C CZ  . TYR A 1 158 ? 20.760  -59.894 20.384  1.00 52.83  ? 161 TYR A CZ  1 
ATOM   1248  O OH  . TYR A 1 158 ? 20.184  -58.652 20.192  1.00 50.30  ? 161 TYR A OH  1 
ATOM   1249  N N   . PRO A 1 159 ? 20.061  -65.767 19.182  1.00 44.72  ? 162 PRO A N   1 
ATOM   1250  C CA  . PRO A 1 159 ? 19.581  -66.007 17.818  1.00 41.33  ? 162 PRO A CA  1 
ATOM   1251  C C   . PRO A 1 159 ? 19.396  -64.688 17.099  1.00 48.20  ? 162 PRO A C   1 
ATOM   1252  O O   . PRO A 1 159 ? 19.171  -63.677 17.761  1.00 51.21  ? 162 PRO A O   1 
ATOM   1253  C CB  . PRO A 1 159 ? 18.216  -66.660 18.039  1.00 51.70  ? 162 PRO A CB  1 
ATOM   1254  C CG  . PRO A 1 159 ? 18.282  -67.229 19.411  1.00 55.95  ? 162 PRO A CG  1 
ATOM   1255  C CD  . PRO A 1 159 ? 19.132  -66.289 20.197  1.00 51.37  ? 162 PRO A CD  1 
ATOM   1256  N N   . VAL A 1 160 ? 19.497  -64.683 15.775  1.00 72.19  ? 163 VAL A N   1 
ATOM   1257  C CA  . VAL A 1 160 ? 19.232  -63.470 15.012  1.00 62.37  ? 163 VAL A CA  1 
ATOM   1258  C C   . VAL A 1 160 ? 17.855  -62.938 15.390  1.00 59.89  ? 163 VAL A C   1 
ATOM   1259  O O   . VAL A 1 160 ? 16.862  -63.660 15.300  1.00 65.20  ? 163 VAL A O   1 
ATOM   1260  C CB  . VAL A 1 160 ? 19.307  -63.725 13.502  1.00 67.28  ? 163 VAL A CB  1 
ATOM   1261  C CG1 . VAL A 1 160 ? 18.695  -65.076 13.163  1.00 81.54  ? 163 VAL A CG1 1 
ATOM   1262  C CG2 . VAL A 1 160 ? 18.622  -62.609 12.740  1.00 63.54  ? 163 VAL A CG2 1 
ATOM   1263  N N   . ALA A 1 161 ? 17.802  -61.682 15.830  1.00 52.21  ? 164 ALA A N   1 
ATOM   1264  C CA  . ALA A 1 161 ? 16.572  -61.100 16.363  1.00 47.83  ? 164 ALA A CA  1 
ATOM   1265  C C   . ALA A 1 161 ? 15.952  -60.064 15.432  1.00 45.25  ? 164 ALA A C   1 
ATOM   1266  O O   . ALA A 1 161 ? 16.593  -59.076 15.073  1.00 42.53  ? 164 ALA A O   1 
ATOM   1267  C CB  . ALA A 1 161 ? 16.826  -60.495 17.741  1.00 51.46  ? 164 ALA A CB  1 
ATOM   1268  N N   . LYS A 1 162 ? 14.699  -60.306 15.051  1.00 59.80  ? 165 LYS A N   1 
ATOM   1269  C CA  . LYS A 1 162 ? 13.958  -59.412 14.165  1.00 54.69  ? 165 LYS A CA  1 
ATOM   1270  C C   . LYS A 1 162 ? 12.735  -58.849 14.880  1.00 56.13  ? 165 LYS A C   1 
ATOM   1271  O O   . LYS A 1 162 ? 12.218  -59.457 15.814  1.00 59.69  ? 165 LYS A O   1 
ATOM   1272  C CB  . LYS A 1 162 ? 13.507  -60.155 12.904  1.00 68.68  ? 165 LYS A CB  1 
ATOM   1273  C CG  . LYS A 1 162 ? 14.634  -60.694 12.026  1.00 77.85  ? 165 LYS A CG  1 
ATOM   1274  C CD  . LYS A 1 162 ? 14.081  -61.511 10.859  1.00 88.13  ? 165 LYS A CD  1 
ATOM   1275  C CE  . LYS A 1 162 ? 15.188  -62.199 10.072  1.00 100.22 ? 165 LYS A CE  1 
ATOM   1276  N NZ  . LYS A 1 162 ? 14.679  -63.342 9.259   1.00 106.34 ? 165 LYS A NZ  1 
ATOM   1277  N N   . GLY A 1 163 ? 12.274  -57.688 14.426  1.00 57.28  ? 166 GLY A N   1 
ATOM   1278  C CA  . GLY A 1 163 ? 11.110  -57.028 14.995  1.00 55.96  ? 166 GLY A CA  1 
ATOM   1279  C C   . GLY A 1 163 ? 10.648  -55.911 14.075  1.00 66.68  ? 166 GLY A C   1 
ATOM   1280  O O   . GLY A 1 163 ? 11.470  -55.233 13.468  1.00 69.55  ? 166 GLY A O   1 
ATOM   1281  N N   . SER A 1 164 ? 9.339   -55.709 13.971  1.00 64.38  ? 167 SER A N   1 
ATOM   1282  C CA  . SER A 1 164 ? 8.808   -54.789 12.975  1.00 64.08  ? 167 SER A CA  1 
ATOM   1283  C C   . SER A 1 164 ? 7.549   -54.046 13.444  1.00 67.67  ? 167 SER A C   1 
ATOM   1284  O O   . SER A 1 164 ? 6.912   -54.445 14.422  1.00 72.79  ? 167 SER A O   1 
ATOM   1285  C CB  . SER A 1 164 ? 8.523   -55.552 11.683  1.00 77.47  ? 167 SER A CB  1 
ATOM   1286  O OG  . SER A 1 164 ? 8.372   -54.670 10.588  1.00 95.19  ? 167 SER A OG  1 
ATOM   1287  N N   . TYR A 1 165 ? 7.198   -52.963 12.750  1.00 67.78  ? 168 TYR A N   1 
ATOM   1288  C CA  . TYR A 1 165 ? 5.969   -52.236 13.053  1.00 63.93  ? 168 TYR A CA  1 
ATOM   1289  C C   . TYR A 1 165 ? 5.404   -51.451 11.865  1.00 86.39  ? 168 TYR A C   1 
ATOM   1290  O O   . TYR A 1 165 ? 6.080   -50.600 11.288  1.00 94.94  ? 168 TYR A O   1 
ATOM   1291  C CB  . TYR A 1 165 ? 6.165   -51.310 14.255  1.00 56.21  ? 168 TYR A CB  1 
ATOM   1292  C CG  . TYR A 1 165 ? 4.915   -50.548 14.628  1.00 65.64  ? 168 TYR A CG  1 
ATOM   1293  C CD1 . TYR A 1 165 ? 3.957   -51.112 15.458  1.00 69.19  ? 168 TYR A CD1 1 
ATOM   1294  C CD2 . TYR A 1 165 ? 4.684   -49.271 14.137  1.00 70.03  ? 168 TYR A CD2 1 
ATOM   1295  C CE1 . TYR A 1 165 ? 2.806   -50.425 15.791  1.00 74.99  ? 168 TYR A CE1 1 
ATOM   1296  C CE2 . TYR A 1 165 ? 3.538   -48.574 14.472  1.00 70.76  ? 168 TYR A CE2 1 
ATOM   1297  C CZ  . TYR A 1 165 ? 2.603   -49.156 15.299  1.00 76.89  ? 168 TYR A CZ  1 
ATOM   1298  O OH  . TYR A 1 165 ? 1.458   -48.470 15.633  1.00 80.50  ? 168 TYR A OH  1 
ATOM   1299  N N   . ASN A 1 166 ? 4.160   -51.760 11.508  1.00 79.66  ? 169 ASN A N   1 
ATOM   1300  C CA  . ASN A 1 166 ? 3.405   -50.994 10.525  1.00 86.56  ? 169 ASN A CA  1 
ATOM   1301  C C   . ASN A 1 166 ? 2.731   -49.833 11.250  1.00 75.71  ? 169 ASN A C   1 
ATOM   1302  O O   . ASN A 1 166 ? 1.845   -50.049 12.078  1.00 67.08  ? 169 ASN A O   1 
ATOM   1303  C CB  . ASN A 1 166 ? 2.346   -51.899 9.886   1.00 99.90  ? 169 ASN A CB  1 
ATOM   1304  C CG  . ASN A 1 166 ? 1.830   -51.372 8.549   1.00 114.63 ? 169 ASN A CG  1 
ATOM   1305  O OD1 . ASN A 1 166 ? 2.301   -50.356 8.047   1.00 115.63 ? 169 ASN A OD1 1 
ATOM   1306  N ND2 . ASN A 1 166 ? 0.860   -52.082 7.964   1.00 124.94 ? 169 ASN A ND2 1 
ATOM   1307  N N   . ASN A 1 167 ? 3.157   -48.604 10.958  1.00 92.81  ? 170 ASN A N   1 
ATOM   1308  C CA  . ASN A 1 167 ? 2.626   -47.427 11.659  1.00 81.45  ? 170 ASN A CA  1 
ATOM   1309  C C   . ASN A 1 167 ? 1.159   -47.171 11.362  1.00 94.15  ? 170 ASN A C   1 
ATOM   1310  O O   . ASN A 1 167 ? 0.805   -46.596 10.338  1.00 117.71 ? 170 ASN A O   1 
ATOM   1311  C CB  . ASN A 1 167 ? 3.450   -46.167 11.374  1.00 80.81  ? 170 ASN A CB  1 
ATOM   1312  C CG  . ASN A 1 167 ? 3.019   -44.981 12.229  1.00 76.02  ? 170 ASN A CG  1 
ATOM   1313  O OD1 . ASN A 1 167 ? 2.216   -45.126 13.150  1.00 77.55  ? 170 ASN A OD1 1 
ATOM   1314  N ND2 . ASN A 1 167 ? 3.561   -43.805 11.933  1.00 69.20  ? 170 ASN A ND2 1 
ATOM   1315  N N   . THR A 1 168 ? 0.313   -47.589 12.289  1.00 62.60  ? 171 THR A N   1 
ATOM   1316  C CA  . THR A 1 168 ? -1.125  -47.554 12.099  1.00 64.28  ? 171 THR A CA  1 
ATOM   1317  C C   . THR A 1 168 ? -1.774  -46.870 13.290  1.00 57.29  ? 171 THR A C   1 
ATOM   1318  O O   . THR A 1 168 ? -2.742  -47.378 13.859  1.00 61.79  ? 171 THR A O   1 
ATOM   1319  C CB  . THR A 1 168 ? -1.678  -48.985 11.993  1.00 65.91  ? 171 THR A CB  1 
ATOM   1320  O OG1 . THR A 1 168 ? -1.345  -49.711 13.183  1.00 49.83  ? 171 THR A OG1 1 
ATOM   1321  C CG2 . THR A 1 168 ? -1.080  -49.696 10.790  1.00 82.21  ? 171 THR A CG2 1 
ATOM   1322  N N   . SER A 1 169 ? -1.229  -45.721 13.671  1.00 85.87  ? 172 SER A N   1 
ATOM   1323  C CA  . SER A 1 169 ? -1.666  -45.038 14.880  1.00 88.89  ? 172 SER A CA  1 
ATOM   1324  C C   . SER A 1 169 ? -2.332  -43.698 14.587  1.00 100.20 ? 172 SER A C   1 
ATOM   1325  O O   . SER A 1 169 ? -2.787  -43.011 15.502  1.00 106.13 ? 172 SER A O   1 
ATOM   1326  C CB  . SER A 1 169 ? -0.483  -44.839 15.822  1.00 89.89  ? 172 SER A CB  1 
ATOM   1327  O OG  . SER A 1 169 ? 0.499   -44.006 15.228  1.00 91.23  ? 172 SER A OG  1 
ATOM   1328  N N   . GLY A 1 170 ? -2.380  -43.328 13.311  1.00 76.52  ? 173 GLY A N   1 
ATOM   1329  C CA  . GLY A 1 170 ? -3.087  -42.131 12.895  1.00 79.27  ? 173 GLY A CA  1 
ATOM   1330  C C   . GLY A 1 170 ? -2.238  -40.875 12.842  1.00 85.70  ? 173 GLY A C   1 
ATOM   1331  O O   . GLY A 1 170 ? -2.769  -39.767 12.753  1.00 89.77  ? 173 GLY A O   1 
ATOM   1332  N N   . GLU A 1 171 ? -0.920  -41.044 12.889  1.00 99.10  ? 174 GLU A N   1 
ATOM   1333  C CA  . GLU A 1 171 ? 0.003   -39.913 12.836  1.00 94.08  ? 174 GLU A CA  1 
ATOM   1334  C C   . GLU A 1 171 ? 1.455   -40.373 12.917  1.00 85.52  ? 174 GLU A C   1 
ATOM   1335  O O   . GLU A 1 171 ? 1.742   -41.436 13.465  1.00 77.54  ? 174 GLU A O   1 
ATOM   1336  C CB  . GLU A 1 171 ? -0.306  -38.913 13.954  1.00 87.09  ? 174 GLU A CB  1 
ATOM   1337  C CG  . GLU A 1 171 ? -0.446  -39.541 15.331  1.00 77.12  ? 174 GLU A CG  1 
ATOM   1338  C CD  . GLU A 1 171 ? -1.094  -38.603 16.335  1.00 73.72  ? 174 GLU A CD  1 
ATOM   1339  O OE1 . GLU A 1 171 ? -1.286  -37.415 16.006  1.00 69.00  ? 174 GLU A OE1 1 
ATOM   1340  O OE2 . GLU A 1 171 ? -1.418  -39.057 17.453  1.00 78.51  ? 174 GLU A OE2 1 
ATOM   1341  N N   . GLN A 1 172 ? 2.362   -39.572 12.361  1.00 75.03  ? 175 GLN A N   1 
ATOM   1342  C CA  . GLN A 1 172 ? 3.790   -39.878 12.398  1.00 68.85  ? 175 GLN A CA  1 
ATOM   1343  C C   . GLN A 1 172 ? 4.219   -40.305 13.799  1.00 54.13  ? 175 GLN A C   1 
ATOM   1344  O O   . GLN A 1 172 ? 3.628   -39.889 14.798  1.00 54.07  ? 175 GLN A O   1 
ATOM   1345  C CB  . GLN A 1 172 ? 4.622   -38.673 11.957  1.00 75.75  ? 175 GLN A CB  1 
ATOM   1346  C CG  . GLN A 1 172 ? 4.452   -38.260 10.504  1.00 98.69  ? 175 GLN A CG  1 
ATOM   1347  C CD  . GLN A 1 172 ? 5.279   -37.029 10.166  1.00 102.90 ? 175 GLN A CD  1 
ATOM   1348  O OE1 . GLN A 1 172 ? 6.470   -36.968 10.466  1.00 91.47  ? 175 GLN A OE1 1 
ATOM   1349  N NE2 . GLN A 1 172 ? 4.644   -36.037 9.549   1.00 106.96 ? 175 GLN A NE2 1 
ATOM   1350  N N   . MET A 1 173 ? 5.246   -41.143 13.873  1.00 74.23  ? 176 MET A N   1 
ATOM   1351  C CA  . MET A 1 173 ? 5.670   -41.682 15.157  1.00 63.97  ? 176 MET A CA  1 
ATOM   1352  C C   . MET A 1 173 ? 7.172   -41.578 15.337  1.00 66.77  ? 176 MET A C   1 
ATOM   1353  O O   . MET A 1 173 ? 7.943   -42.131 14.556  1.00 70.08  ? 176 MET A O   1 
ATOM   1354  C CB  . MET A 1 173 ? 5.235   -43.144 15.301  1.00 60.58  ? 176 MET A CB  1 
ATOM   1355  C CG  . MET A 1 173 ? 5.312   -43.665 16.725  1.00 51.79  ? 176 MET A CG  1 
ATOM   1356  S SD  . MET A 1 173 ? 5.070   -45.443 16.783  1.00 81.06  ? 176 MET A SD  1 
ATOM   1357  C CE  . MET A 1 173 ? 3.546   -45.591 15.860  1.00 169.37 ? 176 MET A CE  1 
ATOM   1358  N N   . LEU A 1 174 ? 7.578   -40.855 16.372  1.00 65.03  ? 177 LEU A N   1 
ATOM   1359  C CA  . LEU A 1 174 ? 8.969   -40.815 16.771  1.00 51.54  ? 177 LEU A CA  1 
ATOM   1360  C C   . LEU A 1 174 ? 9.313   -42.163 17.366  1.00 57.32  ? 177 LEU A C   1 
ATOM   1361  O O   . LEU A 1 174 ? 8.585   -42.673 18.214  1.00 65.05  ? 177 LEU A O   1 
ATOM   1362  C CB  . LEU A 1 174 ? 9.185   -39.727 17.810  1.00 40.39  ? 177 LEU A CB  1 
ATOM   1363  C CG  . LEU A 1 174 ? 10.562  -39.660 18.455  1.00 39.75  ? 177 LEU A CG  1 
ATOM   1364  C CD1 . LEU A 1 174 ? 11.621  -39.462 17.392  1.00 47.74  ? 177 LEU A CD1 1 
ATOM   1365  C CD2 . LEU A 1 174 ? 10.603  -38.521 19.465  1.00 47.63  ? 177 LEU A CD2 1 
ATOM   1366  N N   . ILE A 1 175 ? 10.410  -42.747 16.897  1.00 44.59  ? 178 ILE A N   1 
ATOM   1367  C CA  . ILE A 1 175 ? 10.895  -44.023 17.411  1.00 36.97  ? 178 ILE A CA  1 
ATOM   1368  C C   . ILE A 1 175 ? 12.377  -43.896 17.720  1.00 42.77  ? 178 ILE A C   1 
ATOM   1369  O O   . ILE A 1 175 ? 13.123  -43.276 16.964  1.00 53.33  ? 178 ILE A O   1 
ATOM   1370  C CB  . ILE A 1 175 ? 10.698  -45.146 16.392  1.00 38.84  ? 178 ILE A CB  1 
ATOM   1371  C CG1 . ILE A 1 175 ? 9.210   -45.414 16.171  1.00 35.17  ? 178 ILE A CG1 1 
ATOM   1372  C CG2 . ILE A 1 175 ? 11.411  -46.402 16.846  1.00 46.87  ? 178 ILE A CG2 1 
ATOM   1373  C CD1 . ILE A 1 175 ? 8.928   -46.458 15.117  1.00 35.46  ? 178 ILE A CD1 1 
ATOM   1374  N N   . ILE A 1 176 ? 12.804  -44.470 18.836  1.00 36.80  ? 179 ILE A N   1 
ATOM   1375  C CA  . ILE A 1 176 ? 14.199  -44.373 19.236  1.00 39.38  ? 179 ILE A CA  1 
ATOM   1376  C C   . ILE A 1 176 ? 14.831  -45.747 19.375  1.00 49.23  ? 179 ILE A C   1 
ATOM   1377  O O   . ILE A 1 176 ? 14.202  -46.676 19.880  1.00 64.17  ? 179 ILE A O   1 
ATOM   1378  C CB  . ILE A 1 176 ? 14.338  -43.653 20.572  1.00 44.85  ? 179 ILE A CB  1 
ATOM   1379  C CG1 . ILE A 1 176 ? 13.762  -42.243 20.470  1.00 38.86  ? 179 ILE A CG1 1 
ATOM   1380  C CG2 . ILE A 1 176 ? 15.793  -43.624 20.998  1.00 50.36  ? 179 ILE A CG2 1 
ATOM   1381  C CD1 . ILE A 1 176 ? 14.040  -41.393 21.677  1.00 50.35  ? 179 ILE A CD1 1 
ATOM   1382  N N   . TRP A 1 177 ? 16.071  -45.889 18.924  1.00 54.40  ? 180 TRP A N   1 
ATOM   1383  C CA  . TRP A 1 177 ? 16.792  -47.137 19.152  1.00 54.23  ? 180 TRP A CA  1 
ATOM   1384  C C   . TRP A 1 177 ? 18.222  -46.830 19.525  1.00 55.90  ? 180 TRP A C   1 
ATOM   1385  O O   . TRP A 1 177 ? 18.681  -45.701 19.361  1.00 66.87  ? 180 TRP A O   1 
ATOM   1386  C CB  . TRP A 1 177 ? 16.733  -48.064 17.934  1.00 44.51  ? 180 TRP A CB  1 
ATOM   1387  C CG  . TRP A 1 177 ? 17.563  -47.628 16.772  1.00 44.29  ? 180 TRP A CG  1 
ATOM   1388  C CD1 . TRP A 1 177 ? 18.829  -48.030 16.473  1.00 51.38  ? 180 TRP A CD1 1 
ATOM   1389  C CD2 . TRP A 1 177 ? 17.179  -46.716 15.741  1.00 47.03  ? 180 TRP A CD2 1 
ATOM   1390  N NE1 . TRP A 1 177 ? 19.260  -47.420 15.320  1.00 52.73  ? 180 TRP A NE1 1 
ATOM   1391  C CE2 . TRP A 1 177 ? 18.263  -46.606 14.853  1.00 51.53  ? 180 TRP A CE2 1 
ATOM   1392  C CE3 . TRP A 1 177 ? 16.025  -45.975 15.486  1.00 50.65  ? 180 TRP A CE3 1 
ATOM   1393  C CZ2 . TRP A 1 177 ? 18.225  -45.790 13.730  1.00 62.04  ? 180 TRP A CZ2 1 
ATOM   1394  C CZ3 . TRP A 1 177 ? 15.991  -45.165 14.368  1.00 61.82  ? 180 TRP A CZ3 1 
ATOM   1395  C CH2 . TRP A 1 177 ? 17.080  -45.081 13.503  1.00 68.19  ? 180 TRP A CH2 1 
ATOM   1396  N N   . GLY A 1 178 ? 18.923  -47.827 20.042  1.00 41.56  ? 181 GLY A N   1 
ATOM   1397  C CA  . GLY A 1 178 ? 20.290  -47.621 20.473  1.00 50.46  ? 181 GLY A CA  1 
ATOM   1398  C C   . GLY A 1 178 ? 21.155  -48.836 20.234  1.00 48.66  ? 181 GLY A C   1 
ATOM   1399  O O   . GLY A 1 178 ? 20.654  -49.963 20.165  1.00 51.21  ? 181 GLY A O   1 
ATOM   1400  N N   . VAL A 1 179 ? 22.457  -48.614 20.088  1.00 49.03  ? 182 VAL A N   1 
ATOM   1401  C CA  . VAL A 1 179 ? 23.376  -49.733 20.000  1.00 53.13  ? 182 VAL A CA  1 
ATOM   1402  C C   . VAL A 1 179 ? 24.436  -49.611 21.078  1.00 56.16  ? 182 VAL A C   1 
ATOM   1403  O O   . VAL A 1 179 ? 24.838  -48.509 21.447  1.00 60.23  ? 182 VAL A O   1 
ATOM   1404  C CB  . VAL A 1 179 ? 24.005  -49.883 18.600  1.00 40.98  ? 182 VAL A CB  1 
ATOM   1405  C CG1 . VAL A 1 179 ? 23.244  -49.049 17.593  1.00 50.45  ? 182 VAL A CG1 1 
ATOM   1406  C CG2 . VAL A 1 179 ? 25.473  -49.515 18.627  1.00 26.37  ? 182 VAL A CG2 1 
ATOM   1407  N N   . HIS A 1 180 ? 24.864  -50.759 21.589  1.00 37.64  ? 183 HIS A N   1 
ATOM   1408  C CA  . HIS A 1 180 ? 25.721  -50.802 22.756  1.00 42.45  ? 183 HIS A CA  1 
ATOM   1409  C C   . HIS A 1 180 ? 27.179  -51.009 22.378  1.00 49.56  ? 183 HIS A C   1 
ATOM   1410  O O   . HIS A 1 180 ? 27.513  -51.967 21.687  1.00 49.39  ? 183 HIS A O   1 
ATOM   1411  C CB  . HIS A 1 180 ? 25.265  -51.928 23.674  1.00 44.70  ? 183 HIS A CB  1 
ATOM   1412  C CG  . HIS A 1 180 ? 26.065  -52.041 24.929  1.00 49.02  ? 183 HIS A CG  1 
ATOM   1413  N ND1 . HIS A 1 180 ? 26.178  -53.219 25.636  1.00 57.67  ? 183 HIS A ND1 1 
ATOM   1414  C CD2 . HIS A 1 180 ? 26.790  -51.123 25.608  1.00 51.68  ? 183 HIS A CD2 1 
ATOM   1415  C CE1 . HIS A 1 180 ? 26.943  -53.024 26.693  1.00 68.19  ? 183 HIS A CE1 1 
ATOM   1416  N NE2 . HIS A 1 180 ? 27.327  -51.760 26.700  1.00 68.03  ? 183 HIS A NE2 1 
ATOM   1417  N N   . HIS A 1 181 ? 28.047  -50.114 22.833  1.00 58.68  ? 184 HIS A N   1 
ATOM   1418  C CA  . HIS A 1 181 ? 29.475  -50.277 22.629  1.00 57.44  ? 184 HIS A CA  1 
ATOM   1419  C C   . HIS A 1 181 ? 30.119  -50.669 23.950  1.00 77.03  ? 184 HIS A C   1 
ATOM   1420  O O   . HIS A 1 181 ? 30.327  -49.824 24.811  1.00 81.11  ? 184 HIS A O   1 
ATOM   1421  C CB  . HIS A 1 181 ? 30.105  -48.981 22.121  1.00 45.55  ? 184 HIS A CB  1 
ATOM   1422  C CG  . HIS A 1 181 ? 29.359  -48.331 20.995  1.00 35.64  ? 184 HIS A CG  1 
ATOM   1423  N ND1 . HIS A 1 181 ? 29.011  -49.001 19.842  1.00 34.57  ? 184 HIS A ND1 1 
ATOM   1424  C CD2 . HIS A 1 181 ? 28.916  -47.057 20.838  1.00 31.07  ? 184 HIS A CD2 1 
ATOM   1425  C CE1 . HIS A 1 181 ? 28.374  -48.172 19.028  1.00 32.01  ? 184 HIS A CE1 1 
ATOM   1426  N NE2 . HIS A 1 181 ? 28.303  -46.987 19.609  1.00 28.23  ? 184 HIS A NE2 1 
ATOM   1427  N N   . PRO A 1 182 ? 30.428  -51.960 24.121  1.00 49.35  ? 185 PRO A N   1 
ATOM   1428  C CA  . PRO A 1 182 ? 31.031  -52.495 25.350  1.00 57.50  ? 185 PRO A CA  1 
ATOM   1429  C C   . PRO A 1 182 ? 32.475  -52.042 25.570  1.00 68.68  ? 185 PRO A C   1 
ATOM   1430  O O   . PRO A 1 182 ? 33.132  -51.574 24.641  1.00 67.93  ? 185 PRO A O   1 
ATOM   1431  C CB  . PRO A 1 182 ? 30.999  -54.010 25.126  1.00 59.98  ? 185 PRO A CB  1 
ATOM   1432  C CG  . PRO A 1 182 ? 29.990  -54.230 24.045  1.00 52.16  ? 185 PRO A CG  1 
ATOM   1433  C CD  . PRO A 1 182 ? 30.075  -53.029 23.173  1.00 47.56  ? 185 PRO A CD  1 
ATOM   1434  N N   . ASN A 1 183 ? 32.955  -52.199 26.800  1.00 61.30  ? 186 ASN A N   1 
ATOM   1435  C CA  . ASN A 1 183 ? 34.314  -51.819 27.172  1.00 70.77  ? 186 ASN A CA  1 
ATOM   1436  C C   . ASN A 1 183 ? 35.350  -52.805 26.641  1.00 78.74  ? 186 ASN A C   1 
ATOM   1437  O O   . ASN A 1 183 ? 36.455  -52.415 26.269  1.00 85.59  ? 186 ASN A O   1 
ATOM   1438  C CB  . ASN A 1 183 ? 34.427  -51.725 28.700  1.00 79.37  ? 186 ASN A CB  1 
ATOM   1439  C CG  . ASN A 1 183 ? 35.658  -50.952 29.161  1.00 89.63  ? 186 ASN A CG  1 
ATOM   1440  O OD1 . ASN A 1 183 ? 35.580  -50.133 30.077  1.00 91.13  ? 186 ASN A OD1 1 
ATOM   1441  N ND2 . ASN A 1 183 ? 36.798  -51.212 28.534  1.00 93.30  ? 186 ASN A ND2 1 
ATOM   1442  N N   . ASP A 1 184 ? 34.987  -54.083 26.597  1.00 70.17  ? 187 ASP A N   1 
ATOM   1443  C CA  . ASP A 1 184 ? 35.948  -55.145 26.309  1.00 68.70  ? 187 ASP A CA  1 
ATOM   1444  C C   . ASP A 1 184 ? 35.279  -56.354 25.665  1.00 59.58  ? 187 ASP A C   1 
ATOM   1445  O O   . ASP A 1 184 ? 34.067  -56.527 25.772  1.00 52.53  ? 187 ASP A O   1 
ATOM   1446  C CB  . ASP A 1 184 ? 36.613  -55.573 27.609  1.00 73.25  ? 187 ASP A CB  1 
ATOM   1447  C CG  . ASP A 1 184 ? 35.600  -55.870 28.698  1.00 77.60  ? 187 ASP A CG  1 
ATOM   1448  O OD1 . ASP A 1 184 ? 35.142  -57.031 28.779  1.00 80.92  ? 187 ASP A OD1 1 
ATOM   1449  O OD2 . ASP A 1 184 ? 35.247  -54.939 29.458  1.00 77.26  ? 187 ASP A OD2 1 
ATOM   1450  N N   . GLU A 1 185 ? 36.074  -57.201 25.018  1.00 87.07  ? 188 GLU A N   1 
ATOM   1451  C CA  . GLU A 1 185 ? 35.545  -58.364 24.298  1.00 82.16  ? 188 GLU A CA  1 
ATOM   1452  C C   . GLU A 1 185 ? 34.807  -59.380 25.179  1.00 88.97  ? 188 GLU A C   1 
ATOM   1453  O O   . GLU A 1 185 ? 33.888  -60.054 24.717  1.00 81.05  ? 188 GLU A O   1 
ATOM   1454  C CB  . GLU A 1 185 ? 36.659  -59.065 23.516  1.00 74.24  ? 188 GLU A CB  1 
ATOM   1455  C CG  . GLU A 1 185 ? 36.197  -60.272 22.718  1.00 79.99  ? 188 GLU A CG  1 
ATOM   1456  C CD  . GLU A 1 185 ? 37.323  -60.900 21.919  1.00 99.13  ? 188 GLU A CD  1 
ATOM   1457  O OE1 . GLU A 1 185 ? 38.280  -61.412 22.542  1.00 101.78 ? 188 GLU A OE1 1 
ATOM   1458  O OE2 . GLU A 1 185 ? 37.255  -60.872 20.669  1.00 105.04 ? 188 GLU A OE2 1 
ATOM   1459  N N   . THR A 1 186 ? 35.204  -59.498 26.441  1.00 64.75  ? 189 THR A N   1 
ATOM   1460  C CA  . THR A 1 186 ? 34.536  -60.440 27.335  1.00 65.03  ? 189 THR A CA  1 
ATOM   1461  C C   . THR A 1 186 ? 33.126  -59.967 27.720  1.00 62.59  ? 189 THR A C   1 
ATOM   1462  O O   . THR A 1 186 ? 32.263  -60.783 28.039  1.00 63.94  ? 189 THR A O   1 
ATOM   1463  C CB  . THR A 1 186 ? 35.364  -60.723 28.605  1.00 70.81  ? 189 THR A CB  1 
ATOM   1464  O OG1 . THR A 1 186 ? 35.066  -59.745 29.607  1.00 78.99  ? 189 THR A OG1 1 
ATOM   1465  C CG2 . THR A 1 186 ? 36.849  -60.691 28.289  1.00 72.66  ? 189 THR A CG2 1 
ATOM   1466  N N   . GLU A 1 187 ? 32.896  -58.652 27.689  1.00 66.31  ? 190 GLU A N   1 
ATOM   1467  C CA  . GLU A 1 187 ? 31.560  -58.106 27.931  1.00 53.46  ? 190 GLU A CA  1 
ATOM   1468  C C   . GLU A 1 187 ? 30.661  -58.340 26.724  1.00 51.95  ? 190 GLU A C   1 
ATOM   1469  O O   . GLU A 1 187 ? 29.473  -58.619 26.869  1.00 47.47  ? 190 GLU A O   1 
ATOM   1470  C CB  . GLU A 1 187 ? 31.615  -56.617 28.254  1.00 47.36  ? 190 GLU A CB  1 
ATOM   1471  C CG  . GLU A 1 187 ? 30.256  -55.979 28.570  1.00 47.67  ? 190 GLU A CG  1 
ATOM   1472  C CD  . GLU A 1 187 ? 30.317  -54.441 28.616  1.00 57.42  ? 190 GLU A CD  1 
ATOM   1473  O OE1 . GLU A 1 187 ? 31.410  -53.871 28.371  1.00 59.13  ? 190 GLU A OE1 1 
ATOM   1474  O OE2 . GLU A 1 187 ? 29.270  -53.809 28.895  1.00 56.47  ? 190 GLU A OE2 1 
ATOM   1475  N N   . GLN A 1 188 ? 31.229  -58.235 25.530  1.00 71.26  ? 191 GLN A N   1 
ATOM   1476  C CA  . GLN A 1 188 ? 30.470  -58.521 24.322  1.00 66.68  ? 191 GLN A CA  1 
ATOM   1477  C C   . GLN A 1 188 ? 29.956  -59.949 24.363  1.00 68.00  ? 191 GLN A C   1 
ATOM   1478  O O   . GLN A 1 188 ? 28.795  -60.211 24.062  1.00 65.10  ? 191 GLN A O   1 
ATOM   1479  C CB  . GLN A 1 188 ? 31.337  -58.325 23.080  1.00 59.08  ? 191 GLN A CB  1 
ATOM   1480  C CG  . GLN A 1 188 ? 30.744  -58.909 21.807  1.00 49.19  ? 191 GLN A CG  1 
ATOM   1481  C CD  . GLN A 1 188 ? 29.569  -58.107 21.277  1.00 44.30  ? 191 GLN A CD  1 
ATOM   1482  O OE1 . GLN A 1 188 ? 29.368  -56.940 21.644  1.00 47.59  ? 191 GLN A OE1 1 
ATOM   1483  N NE2 . GLN A 1 188 ? 28.788  -58.726 20.400  1.00 41.54  ? 191 GLN A NE2 1 
ATOM   1484  N N   . ARG A 1 189 ? 30.836  -60.865 24.748  1.00 73.18  ? 192 ARG A N   1 
ATOM   1485  C CA  . ARG A 1 189 ? 30.521  -62.285 24.766  1.00 79.01  ? 192 ARG A CA  1 
ATOM   1486  C C   . ARG A 1 189 ? 29.452  -62.598 25.806  1.00 78.33  ? 192 ARG A C   1 
ATOM   1487  O O   . ARG A 1 189 ? 28.495  -63.320 25.531  1.00 73.14  ? 192 ARG A O   1 
ATOM   1488  C CB  . ARG A 1 189 ? 31.789  -63.090 25.066  1.00 91.80  ? 192 ARG A CB  1 
ATOM   1489  C CG  . ARG A 1 189 ? 31.658  -64.608 24.919  1.00 100.91 ? 192 ARG A CG  1 
ATOM   1490  C CD  . ARG A 1 189 ? 32.121  -65.073 23.544  1.00 101.80 ? 192 ARG A CD  1 
ATOM   1491  N NE  . ARG A 1 189 ? 33.406  -64.481 23.175  1.00 101.38 ? 192 ARG A NE  1 
ATOM   1492  C CZ  . ARG A 1 189 ? 33.995  -64.644 21.994  1.00 96.95  ? 192 ARG A CZ  1 
ATOM   1493  N NH1 . ARG A 1 189 ? 33.416  -65.387 21.056  1.00 86.95  ? 192 ARG A NH1 1 
ATOM   1494  N NH2 . ARG A 1 189 ? 35.163  -64.063 21.752  1.00 93.73  ? 192 ARG A NH2 1 
ATOM   1495  N N   . THR A 1 190 ? 29.619  -62.048 27.004  1.00 66.52  ? 193 THR A N   1 
ATOM   1496  C CA  . THR A 1 190 ? 28.727  -62.343 28.122  1.00 59.00  ? 193 THR A CA  1 
ATOM   1497  C C   . THR A 1 190 ? 27.288  -61.896 27.883  1.00 52.70  ? 193 THR A C   1 
ATOM   1498  O O   . THR A 1 190 ? 26.353  -62.528 28.362  1.00 51.24  ? 193 THR A O   1 
ATOM   1499  C CB  . THR A 1 190 ? 29.224  -61.678 29.413  1.00 51.71  ? 193 THR A CB  1 
ATOM   1500  O OG1 . THR A 1 190 ? 30.629  -61.892 29.553  1.00 63.21  ? 193 THR A OG1 1 
ATOM   1501  C CG2 . THR A 1 190 ? 28.512  -62.256 30.619  1.00 48.65  ? 193 THR A CG2 1 
ATOM   1502  N N   . LEU A 1 191 ? 27.109  -60.801 27.152  1.00 59.82  ? 194 LEU A N   1 
ATOM   1503  C CA  . LEU A 1 191 ? 25.777  -60.242 26.951  1.00 56.11  ? 194 LEU A CA  1 
ATOM   1504  C C   . LEU A 1 191 ? 25.157  -60.654 25.621  1.00 56.30  ? 194 LEU A C   1 
ATOM   1505  O O   . LEU A 1 191 ? 23.938  -60.675 25.483  1.00 56.61  ? 194 LEU A O   1 
ATOM   1506  C CB  . LEU A 1 191 ? 25.827  -58.717 27.024  1.00 48.57  ? 194 LEU A CB  1 
ATOM   1507  C CG  . LEU A 1 191 ? 26.418  -58.044 28.263  1.00 48.32  ? 194 LEU A CG  1 
ATOM   1508  C CD1 . LEU A 1 191 ? 26.913  -56.626 27.930  1.00 51.94  ? 194 LEU A CD1 1 
ATOM   1509  C CD2 . LEU A 1 191 ? 25.406  -58.005 29.384  1.00 40.68  ? 194 LEU A CD2 1 
ATOM   1510  N N   . TYR A 1 192 ? 25.996  -60.977 24.644  1.00 69.26  ? 195 TYR A N   1 
ATOM   1511  C CA  . TYR A 1 192 ? 25.515  -61.192 23.283  1.00 64.25  ? 195 TYR A CA  1 
ATOM   1512  C C   . TYR A 1 192 ? 25.916  -62.548 22.683  1.00 67.84  ? 195 TYR A C   1 
ATOM   1513  O O   . TYR A 1 192 ? 25.215  -63.073 21.821  1.00 57.84  ? 195 TYR A O   1 
ATOM   1514  C CB  . TYR A 1 192 ? 25.969  -60.030 22.390  1.00 52.93  ? 195 TYR A CB  1 
ATOM   1515  C CG  . TYR A 1 192 ? 25.622  -58.690 22.997  1.00 56.88  ? 195 TYR A CG  1 
ATOM   1516  C CD1 . TYR A 1 192 ? 24.379  -58.484 23.584  1.00 61.62  ? 195 TYR A CD1 1 
ATOM   1517  C CD2 . TYR A 1 192 ? 26.542  -57.646 23.022  1.00 55.10  ? 195 TYR A CD2 1 
ATOM   1518  C CE1 . TYR A 1 192 ? 24.056  -57.277 24.164  1.00 59.25  ? 195 TYR A CE1 1 
ATOM   1519  C CE2 . TYR A 1 192 ? 26.225  -56.434 23.602  1.00 51.19  ? 195 TYR A CE2 1 
ATOM   1520  C CZ  . TYR A 1 192 ? 24.978  -56.254 24.173  1.00 53.32  ? 195 TYR A CZ  1 
ATOM   1521  O OH  . TYR A 1 192 ? 24.635  -55.050 24.762  1.00 49.00  ? 195 TYR A OH  1 
ATOM   1522  N N   . GLN A 1 193 ? 27.032  -63.105 23.151  1.00 61.17  ? 196 GLN A N   1 
ATOM   1523  C CA  . GLN A 1 193 ? 27.562  -64.371 22.646  1.00 53.86  ? 196 GLN A CA  1 
ATOM   1524  C C   . GLN A 1 193 ? 28.301  -64.225 21.317  1.00 54.69  ? 196 GLN A C   1 
ATOM   1525  O O   . GLN A 1 193 ? 29.520  -64.380 21.257  1.00 65.80  ? 196 GLN A O   1 
ATOM   1526  C CB  . GLN A 1 193 ? 26.462  -65.426 22.530  1.00 62.66  ? 196 GLN A CB  1 
ATOM   1527  C CG  . GLN A 1 193 ? 26.275  -66.261 23.778  1.00 73.02  ? 196 GLN A CG  1 
ATOM   1528  C CD  . GLN A 1 193 ? 27.453  -67.174 24.039  1.00 85.54  ? 196 GLN A CD  1 
ATOM   1529  O OE1 . GLN A 1 193 ? 28.029  -67.744 23.110  1.00 95.62  ? 196 GLN A OE1 1 
ATOM   1530  N NE2 . GLN A 1 193 ? 27.825  -67.312 25.308  1.00 89.17  ? 196 GLN A NE2 1 
ATOM   1531  N N   . ASN A 1 194 ? 27.561  -63.931 20.255  1.00 74.48  ? 197 ASN A N   1 
ATOM   1532  C CA  . ASN A 1 194 ? 28.144  -63.799 18.925  1.00 71.58  ? 197 ASN A CA  1 
ATOM   1533  C C   . ASN A 1 194 ? 29.147  -62.654 18.862  1.00 78.02  ? 197 ASN A C   1 
ATOM   1534  O O   . ASN A 1 194 ? 29.298  -61.902 19.822  1.00 85.83  ? 197 ASN A O   1 
ATOM   1535  C CB  . ASN A 1 194 ? 27.039  -63.550 17.902  1.00 58.33  ? 197 ASN A CB  1 
ATOM   1536  C CG  . ASN A 1 194 ? 25.738  -64.232 18.275  1.00 62.95  ? 197 ASN A CG  1 
ATOM   1537  O OD1 . ASN A 1 194 ? 25.735  -65.362 18.765  1.00 77.27  ? 197 ASN A OD1 1 
ATOM   1538  N ND2 . ASN A 1 194 ? 24.624  -63.545 18.047  1.00 52.52  ? 197 ASN A ND2 1 
ATOM   1539  N N   . VAL A 1 195 ? 29.836  -62.527 17.732  1.00 82.02  ? 198 VAL A N   1 
ATOM   1540  C CA  . VAL A 1 195 ? 30.662  -61.350 17.474  1.00 76.00  ? 198 VAL A CA  1 
ATOM   1541  C C   . VAL A 1 195 ? 30.540  -60.922 16.005  1.00 73.67  ? 198 VAL A C   1 
ATOM   1542  O O   . VAL A 1 195 ? 29.876  -61.596 15.208  1.00 77.40  ? 198 VAL A O   1 
ATOM   1543  C CB  . VAL A 1 195 ? 32.141  -61.558 17.871  1.00 72.85  ? 198 VAL A CB  1 
ATOM   1544  C CG1 . VAL A 1 195 ? 32.859  -60.209 17.945  1.00 76.92  ? 198 VAL A CG1 1 
ATOM   1545  C CG2 . VAL A 1 195 ? 32.234  -62.264 19.209  1.00 70.11  ? 198 VAL A CG2 1 
ATOM   1546  N N   . GLY A 1 196 ? 31.167  -59.801 15.651  1.00 58.84  ? 199 GLY A N   1 
ATOM   1547  C CA  . GLY A 1 196 ? 30.962  -59.232 14.335  1.00 61.43  ? 199 GLY A CA  1 
ATOM   1548  C C   . GLY A 1 196 ? 29.467  -59.063 14.214  1.00 66.53  ? 199 GLY A C   1 
ATOM   1549  O O   . GLY A 1 196 ? 28.817  -59.612 13.324  1.00 78.40  ? 199 GLY A O   1 
ATOM   1550  N N   . THR A 1 197 ? 28.919  -58.317 15.161  1.00 62.76  ? 200 THR A N   1 
ATOM   1551  C CA  . THR A 1 197 ? 27.486  -58.150 15.273  1.00 53.92  ? 200 THR A CA  1 
ATOM   1552  C C   . THR A 1 197 ? 27.068  -56.928 14.490  1.00 57.21  ? 200 THR A C   1 
ATOM   1553  O O   . THR A 1 197 ? 27.898  -56.080 14.156  1.00 60.38  ? 200 THR A O   1 
ATOM   1554  C CB  . THR A 1 197 ? 27.087  -57.956 16.736  1.00 47.17  ? 200 THR A CB  1 
ATOM   1555  O OG1 . THR A 1 197 ? 27.925  -56.949 17.313  1.00 45.18  ? 200 THR A OG1 1 
ATOM   1556  C CG2 . THR A 1 197 ? 27.277  -59.242 17.518  1.00 46.15  ? 200 THR A CG2 1 
ATOM   1557  N N   . TYR A 1 198 ? 25.778  -56.837 14.195  1.00 56.44  ? 201 TYR A N   1 
ATOM   1558  C CA  . TYR A 1 198 ? 25.258  -55.662 13.513  1.00 55.40  ? 201 TYR A CA  1 
ATOM   1559  C C   . TYR A 1 198 ? 23.923  -55.231 14.091  1.00 52.41  ? 201 TYR A C   1 
ATOM   1560  O O   . TYR A 1 198 ? 23.160  -56.049 14.611  1.00 44.54  ? 201 TYR A O   1 
ATOM   1561  C CB  . TYR A 1 198 ? 25.117  -55.919 12.013  1.00 58.96  ? 201 TYR A CB  1 
ATOM   1562  C CG  . TYR A 1 198 ? 24.172  -57.043 11.663  1.00 62.74  ? 201 TYR A CG  1 
ATOM   1563  C CD1 . TYR A 1 198 ? 22.859  -56.785 11.301  1.00 72.91  ? 201 TYR A CD1 1 
ATOM   1564  C CD2 . TYR A 1 198 ? 24.596  -58.367 11.687  1.00 58.50  ? 201 TYR A CD2 1 
ATOM   1565  C CE1 . TYR A 1 198 ? 21.995  -57.813 10.975  1.00 76.70  ? 201 TYR A CE1 1 
ATOM   1566  C CE2 . TYR A 1 198 ? 23.739  -59.396 11.363  1.00 61.23  ? 201 TYR A CE2 1 
ATOM   1567  C CZ  . TYR A 1 198 ? 22.441  -59.113 11.010  1.00 68.92  ? 201 TYR A CZ  1 
ATOM   1568  O OH  . TYR A 1 198 ? 21.577  -60.127 10.691  1.00 68.16  ? 201 TYR A OH  1 
ATOM   1569  N N   . VAL A 1 199 ? 23.655  -53.936 14.019  1.00 64.58  ? 202 VAL A N   1 
ATOM   1570  C CA  . VAL A 1 199 ? 22.332  -53.438 14.309  1.00 57.47  ? 202 VAL A CA  1 
ATOM   1571  C C   . VAL A 1 199 ? 21.846  -52.804 13.025  1.00 67.13  ? 202 VAL A C   1 
ATOM   1572  O O   . VAL A 1 199 ? 22.457  -51.861 12.525  1.00 75.25  ? 202 VAL A O   1 
ATOM   1573  C CB  . VAL A 1 199 ? 22.350  -52.396 15.426  1.00 43.58  ? 202 VAL A CB  1 
ATOM   1574  C CG1 . VAL A 1 199 ? 20.929  -52.041 15.839  1.00 40.81  ? 202 VAL A CG1 1 
ATOM   1575  C CG2 . VAL A 1 199 ? 23.126  -52.919 16.623  1.00 37.97  ? 202 VAL A CG2 1 
ATOM   1576  N N   . SER A 1 200 ? 20.768  -53.347 12.473  1.00 43.18  ? 203 SER A N   1 
ATOM   1577  C CA  A SER A 1 200 ? 20.204  -52.839 11.229  0.50 53.36  ? 203 SER A CA  1 
ATOM   1578  C CA  B SER A 1 200 ? 20.211  -52.823 11.232  0.50 53.97  ? 203 SER A CA  1 
ATOM   1579  C C   . SER A 1 200 ? 18.797  -52.302 11.446  1.00 58.57  ? 203 SER A C   1 
ATOM   1580  O O   . SER A 1 200 ? 17.972  -52.945 12.093  1.00 66.70  ? 203 SER A O   1 
ATOM   1581  C CB  A SER A 1 200 ? 20.177  -53.936 10.167  0.50 54.89  ? 203 SER A CB  1 
ATOM   1582  C CB  B SER A 1 200 ? 20.214  -53.888 10.137  0.50 55.25  ? 203 SER A CB  1 
ATOM   1583  O OG  A SER A 1 200 ? 19.334  -53.569 9.090   0.50 57.02  ? 203 SER A OG  1 
ATOM   1584  O OG  B SER A 1 200 ? 18.927  -54.459 9.985   0.50 58.59  ? 203 SER A OG  1 
ATOM   1585  N N   . VAL A 1 201 ? 18.532  -51.124 10.898  1.00 68.87  ? 204 VAL A N   1 
ATOM   1586  C CA  . VAL A 1 201 ? 17.227  -50.502 11.012  1.00 63.84  ? 204 VAL A CA  1 
ATOM   1587  C C   . VAL A 1 201 ? 16.827  -49.967 9.652   1.00 72.34  ? 204 VAL A C   1 
ATOM   1588  O O   . VAL A 1 201 ? 17.649  -49.405 8.936   1.00 79.91  ? 204 VAL A O   1 
ATOM   1589  C CB  . VAL A 1 201 ? 17.253  -49.335 11.990  1.00 47.61  ? 204 VAL A CB  1 
ATOM   1590  C CG1 . VAL A 1 201 ? 15.847  -49.037 12.455  1.00 43.99  ? 204 VAL A CG1 1 
ATOM   1591  C CG2 . VAL A 1 201 ? 18.162  -49.647 13.175  1.00 43.57  ? 204 VAL A CG2 1 
ATOM   1592  N N   . GLY A 1 202 ? 15.564  -50.131 9.292   1.00 54.97  ? 205 GLY A N   1 
ATOM   1593  C CA  . GLY A 1 202 ? 15.145  -49.746 7.962   1.00 63.65  ? 205 GLY A CA  1 
ATOM   1594  C C   . GLY A 1 202 ? 13.710  -49.285 7.811   1.00 70.06  ? 205 GLY A C   1 
ATOM   1595  O O   . GLY A 1 202 ? 12.791  -49.802 8.455   1.00 67.16  ? 205 GLY A O   1 
ATOM   1596  N N   . THR A 1 203 ? 13.535  -48.295 6.942   1.00 57.98  ? 206 THR A N   1 
ATOM   1597  C CA  . THR A 1 203 ? 12.219  -47.827 6.540   1.00 59.60  ? 206 THR A CA  1 
ATOM   1598  C C   . THR A 1 203 ? 12.257  -47.472 5.059   1.00 64.34  ? 206 THR A C   1 
ATOM   1599  O O   . THR A 1 203 ? 13.265  -47.675 4.380   1.00 72.74  ? 206 THR A O   1 
ATOM   1600  C CB  . THR A 1 203 ? 11.783  -46.574 7.332   1.00 53.00  ? 206 THR A CB  1 
ATOM   1601  O OG1 . THR A 1 203 ? 12.538  -45.431 6.892   1.00 53.97  ? 206 THR A OG1 1 
ATOM   1602  C CG2 . THR A 1 203 ? 11.983  -46.779 8.824   1.00 49.78  ? 206 THR A CG2 1 
ATOM   1603  N N   . SER A 1 204 ? 11.157  -46.925 4.565   1.00 51.60  ? 207 SER A N   1 
ATOM   1604  C CA  . SER A 1 204 ? 11.078  -46.495 3.182   1.00 58.52  ? 207 SER A CA  1 
ATOM   1605  C C   . SER A 1 204 ? 11.982  -45.293 2.918   1.00 61.39  ? 207 SER A C   1 
ATOM   1606  O O   . SER A 1 204 ? 12.149  -44.871 1.772   1.00 67.58  ? 207 SER A O   1 
ATOM   1607  C CB  . SER A 1 204 ? 9.630   -46.165 2.826   1.00 63.05  ? 207 SER A CB  1 
ATOM   1608  O OG  . SER A 1 204 ? 9.001   -45.475 3.892   1.00 58.05  ? 207 SER A OG  1 
ATOM   1609  N N   . THR A 1 205 ? 12.567  -44.743 3.976   1.00 72.98  ? 208 THR A N   1 
ATOM   1610  C CA  . THR A 1 205 ? 13.446  -43.588 3.817   1.00 84.98  ? 208 THR A CA  1 
ATOM   1611  C C   . THR A 1 205 ? 14.804  -43.788 4.490   1.00 85.86  ? 208 THR A C   1 
ATOM   1612  O O   . THR A 1 205 ? 15.837  -43.371 3.960   1.00 94.07  ? 208 THR A O   1 
ATOM   1613  C CB  . THR A 1 205 ? 12.794  -42.286 4.347   1.00 90.40  ? 208 THR A CB  1 
ATOM   1614  O OG1 . THR A 1 205 ? 13.337  -41.956 5.631   1.00 98.65  ? 208 THR A OG1 1 
ATOM   1615  C CG2 . THR A 1 205 ? 11.283  -42.442 4.459   1.00 87.79  ? 208 THR A CG2 1 
ATOM   1616  N N   . LEU A 1 206 ? 14.800  -44.429 5.653   1.00 65.00  ? 209 LEU A N   1 
ATOM   1617  C CA  . LEU A 1 206 ? 16.018  -44.582 6.436   1.00 54.13  ? 209 LEU A CA  1 
ATOM   1618  C C   . LEU A 1 206 ? 16.638  -45.968 6.278   1.00 61.38  ? 209 LEU A C   1 
ATOM   1619  O O   . LEU A 1 206 ? 15.938  -46.961 6.073   1.00 67.19  ? 209 LEU A O   1 
ATOM   1620  C CB  . LEU A 1 206 ? 15.739  -44.279 7.905   1.00 49.15  ? 209 LEU A CB  1 
ATOM   1621  C CG  . LEU A 1 206 ? 16.797  -44.673 8.939   1.00 41.90  ? 209 LEU A CG  1 
ATOM   1622  C CD1 . LEU A 1 206 ? 17.227  -43.472 9.773   1.00 47.42  ? 209 LEU A CD1 1 
ATOM   1623  C CD2 . LEU A 1 206 ? 16.291  -45.808 9.842   1.00 31.09  ? 209 LEU A CD2 1 
ATOM   1624  N N   . ASN A 1 207 ? 17.960  -46.025 6.378   1.00 80.76  ? 210 ASN A N   1 
ATOM   1625  C CA  . ASN A 1 207 ? 18.692  -47.266 6.179   1.00 80.07  ? 210 ASN A CA  1 
ATOM   1626  C C   . ASN A 1 207 ? 20.061  -47.208 6.850   1.00 61.72  ? 210 ASN A C   1 
ATOM   1627  O O   . ASN A 1 207 ? 21.006  -46.655 6.292   1.00 60.59  ? 210 ASN A O   1 
ATOM   1628  C CB  . ASN A 1 207 ? 18.849  -47.542 4.679   1.00 93.55  ? 210 ASN A CB  1 
ATOM   1629  C CG  . ASN A 1 207 ? 19.806  -48.689 4.387   1.00 107.87 ? 210 ASN A CG  1 
ATOM   1630  O OD1 . ASN A 1 207 ? 19.665  -49.790 4.931   1.00 118.94 ? 210 ASN A OD1 1 
ATOM   1631  N ND2 . ASN A 1 207 ? 20.797  -48.432 3.530   1.00 104.66 ? 210 ASN A ND2 1 
ATOM   1632  N N   . LYS A 1 208 ? 20.169  -47.773 8.047   1.00 63.04  ? 211 LYS A N   1 
ATOM   1633  C CA  . LYS A 1 208 ? 21.453  -47.821 8.733   1.00 44.58  ? 211 LYS A CA  1 
ATOM   1634  C C   . LYS A 1 208 ? 21.860  -49.246 9.140   1.00 54.43  ? 211 LYS A C   1 
ATOM   1635  O O   . LYS A 1 208 ? 21.013  -50.068 9.500   1.00 73.07  ? 211 LYS A O   1 
ATOM   1636  C CB  . LYS A 1 208 ? 21.448  -46.898 9.950   1.00 44.28  ? 211 LYS A CB  1 
ATOM   1637  C CG  . LYS A 1 208 ? 22.784  -46.828 10.685  1.00 56.38  ? 211 LYS A CG  1 
ATOM   1638  C CD  . LYS A 1 208 ? 23.136  -45.403 11.118  1.00 72.78  ? 211 LYS A CD  1 
ATOM   1639  C CE  . LYS A 1 208 ? 22.114  -44.838 12.106  1.00 85.07  ? 211 LYS A CE  1 
ATOM   1640  N NZ  . LYS A 1 208 ? 22.381  -43.408 12.479  1.00 80.57  ? 211 LYS A NZ  1 
ATOM   1641  N N   . ARG A 1 209 ? 23.157  -49.538 9.048   1.00 39.54  ? 212 ARG A N   1 
ATOM   1642  C CA  . ARG A 1 209 ? 23.720  -50.743 9.638   1.00 38.63  ? 212 ARG A CA  1 
ATOM   1643  C C   . ARG A 1 209 ? 24.890  -50.376 10.533  1.00 46.57  ? 212 ARG A C   1 
ATOM   1644  O O   . ARG A 1 209 ? 26.001  -50.167 10.053  1.00 54.64  ? 212 ARG A O   1 
ATOM   1645  C CB  . ARG A 1 209 ? 24.185  -51.724 8.566   1.00 40.96  ? 212 ARG A CB  1 
ATOM   1646  C CG  . ARG A 1 209 ? 25.034  -52.862 9.130   1.00 50.26  ? 212 ARG A CG  1 
ATOM   1647  C CD  . ARG A 1 209 ? 25.496  -53.814 8.049   1.00 58.34  ? 212 ARG A CD  1 
ATOM   1648  N NE  . ARG A 1 209 ? 24.497  -54.841 7.771   1.00 72.36  ? 212 ARG A NE  1 
ATOM   1649  C CZ  . ARG A 1 209 ? 24.684  -56.138 7.992   1.00 80.73  ? 212 ARG A CZ  1 
ATOM   1650  N NH1 . ARG A 1 209 ? 25.841  -56.559 8.488   1.00 81.45  ? 212 ARG A NH1 1 
ATOM   1651  N NH2 . ARG A 1 209 ? 23.722  -57.013 7.712   1.00 77.10  ? 212 ARG A NH2 1 
ATOM   1652  N N   . SER A 1 210 ? 24.635  -50.297 11.834  1.00 61.63  ? 213 SER A N   1 
ATOM   1653  C CA  . SER A 1 210 ? 25.669  -49.928 12.796  1.00 52.57  ? 213 SER A CA  1 
ATOM   1654  C C   . SER A 1 210 ? 26.455  -51.154 13.251  1.00 51.57  ? 213 SER A C   1 
ATOM   1655  O O   . SER A 1 210 ? 25.902  -52.246 13.390  1.00 51.98  ? 213 SER A O   1 
ATOM   1656  C CB  . SER A 1 210 ? 25.053  -49.220 14.010  1.00 49.97  ? 213 SER A CB  1 
ATOM   1657  O OG  . SER A 1 210 ? 24.313  -48.064 13.631  1.00 58.76  ? 213 SER A OG  1 
ATOM   1658  N N   . THR A 1 211 ? 27.750  -50.976 13.478  1.00 48.40  ? 214 THR A N   1 
ATOM   1659  C CA  . THR A 1 211 ? 28.574  -52.066 13.975  1.00 51.75  ? 214 THR A CA  1 
ATOM   1660  C C   . THR A 1 211 ? 29.160  -51.700 15.320  1.00 51.78  ? 214 THR A C   1 
ATOM   1661  O O   . THR A 1 211 ? 30.004  -50.810 15.411  1.00 62.38  ? 214 THR A O   1 
ATOM   1662  C CB  . THR A 1 211 ? 29.733  -52.387 13.030  1.00 61.24  ? 214 THR A CB  1 
ATOM   1663  O OG1 . THR A 1 211 ? 29.240  -53.109 11.897  1.00 70.17  ? 214 THR A OG1 1 
ATOM   1664  C CG2 . THR A 1 211 ? 30.770  -53.234 13.749  1.00 65.09  ? 214 THR A CG2 1 
ATOM   1665  N N   . PRO A 1 212 ? 28.722  -52.397 16.372  1.00 41.03  ? 215 PRO A N   1 
ATOM   1666  C CA  . PRO A 1 212 ? 29.146  -52.125 17.746  1.00 40.72  ? 215 PRO A CA  1 
ATOM   1667  C C   . PRO A 1 212 ? 30.646  -51.906 17.824  1.00 48.14  ? 215 PRO A C   1 
ATOM   1668  O O   . PRO A 1 212 ? 31.413  -52.666 17.242  1.00 51.92  ? 215 PRO A O   1 
ATOM   1669  C CB  . PRO A 1 212 ? 28.774  -53.400 18.481  1.00 38.21  ? 215 PRO A CB  1 
ATOM   1670  C CG  . PRO A 1 212 ? 27.642  -53.957 17.702  1.00 44.54  ? 215 PRO A CG  1 
ATOM   1671  C CD  . PRO A 1 212 ? 27.900  -53.611 16.271  1.00 46.62  ? 215 PRO A CD  1 
ATOM   1672  N N   . GLU A 1 213 ? 31.047  -50.856 18.529  1.00 56.62  ? 216 GLU A N   1 
ATOM   1673  C CA  . GLU A 1 213 ? 32.450  -50.523 18.682  1.00 51.94  ? 216 GLU A CA  1 
ATOM   1674  C C   . GLU A 1 213 ? 32.935  -50.833 20.096  1.00 63.10  ? 216 GLU A C   1 
ATOM   1675  O O   . GLU A 1 213 ? 32.782  -50.022 21.007  1.00 68.96  ? 216 GLU A O   1 
ATOM   1676  C CB  . GLU A 1 213 ? 32.681  -49.049 18.362  1.00 48.24  ? 216 GLU A CB  1 
ATOM   1677  C CG  . GLU A 1 213 ? 32.244  -48.634 16.966  1.00 48.75  ? 216 GLU A CG  1 
ATOM   1678  C CD  . GLU A 1 213 ? 32.286  -47.117 16.769  1.00 55.04  ? 216 GLU A CD  1 
ATOM   1679  O OE1 . GLU A 1 213 ? 32.740  -46.406 17.697  1.00 59.34  ? 216 GLU A OE1 1 
ATOM   1680  O OE2 . GLU A 1 213 ? 31.857  -46.642 15.691  1.00 50.47  ? 216 GLU A OE2 1 
ATOM   1681  N N   . ILE A 1 214 ? 33.519  -52.013 20.268  1.00 55.06  ? 217 ILE A N   1 
ATOM   1682  C CA  . ILE A 1 214 ? 34.129  -52.391 21.534  1.00 62.80  ? 217 ILE A CA  1 
ATOM   1683  C C   . ILE A 1 214 ? 35.452  -51.659 21.772  1.00 67.99  ? 217 ILE A C   1 
ATOM   1684  O O   . ILE A 1 214 ? 36.330  -51.647 20.902  1.00 62.37  ? 217 ILE A O   1 
ATOM   1685  C CB  . ILE A 1 214 ? 34.408  -53.896 21.572  1.00 61.54  ? 217 ILE A CB  1 
ATOM   1686  C CG1 . ILE A 1 214 ? 33.116  -54.683 21.372  1.00 60.24  ? 217 ILE A CG1 1 
ATOM   1687  C CG2 . ILE A 1 214 ? 35.056  -54.278 22.884  1.00 70.45  ? 217 ILE A CG2 1 
ATOM   1688  C CD1 . ILE A 1 214 ? 33.313  -56.173 21.421  1.00 69.65  ? 217 ILE A CD1 1 
ATOM   1689  N N   . ALA A 1 215 ? 35.597  -51.051 22.948  1.00 60.78  ? 218 ALA A N   1 
ATOM   1690  C CA  . ALA A 1 215 ? 36.849  -50.384 23.305  1.00 68.32  ? 218 ALA A CA  1 
ATOM   1691  C C   . ALA A 1 215 ? 36.887  -49.959 24.764  1.00 92.40  ? 218 ALA A C   1 
ATOM   1692  O O   . ALA A 1 215 ? 35.852  -49.842 25.415  1.00 98.74  ? 218 ALA A O   1 
ATOM   1693  C CB  . ALA A 1 215 ? 37.092  -49.190 22.407  1.00 51.19  ? 218 ALA A CB  1 
ATOM   1694  N N   . THR A 1 216 ? 38.094  -49.725 25.268  1.00 58.24  ? 219 THR A N   1 
ATOM   1695  C CA  . THR A 1 216 ? 38.272  -49.331 26.657  1.00 62.75  ? 219 THR A CA  1 
ATOM   1696  C C   . THR A 1 216 ? 37.955  -47.861 26.831  1.00 60.88  ? 219 THR A C   1 
ATOM   1697  O O   . THR A 1 216 ? 38.321  -47.036 25.998  1.00 57.64  ? 219 THR A O   1 
ATOM   1698  C CB  . THR A 1 216 ? 39.703  -49.578 27.144  1.00 65.25  ? 219 THR A CB  1 
ATOM   1699  O OG1 . THR A 1 216 ? 40.011  -50.975 27.049  1.00 66.32  ? 219 THR A OG1 1 
ATOM   1700  C CG2 . THR A 1 216 ? 39.844  -49.128 28.588  1.00 69.09  ? 219 THR A CG2 1 
ATOM   1701  N N   . ARG A 1 217 ? 37.264  -47.537 27.915  1.00 95.86  ? 220 ARG A N   1 
ATOM   1702  C CA  . ARG A 1 217 ? 36.905  -46.157 28.198  1.00 87.38  ? 220 ARG A CA  1 
ATOM   1703  C C   . ARG A 1 217 ? 36.872  -45.922 29.692  1.00 89.49  ? 220 ARG A C   1 
ATOM   1704  O O   . ARG A 1 217 ? 36.791  -46.867 30.473  1.00 102.42 ? 220 ARG A O   1 
ATOM   1705  C CB  . ARG A 1 217 ? 35.534  -45.827 27.612  1.00 79.28  ? 220 ARG A CB  1 
ATOM   1706  C CG  . ARG A 1 217 ? 35.357  -46.258 26.178  1.00 69.80  ? 220 ARG A CG  1 
ATOM   1707  C CD  . ARG A 1 217 ? 34.043  -45.772 25.596  1.00 62.42  ? 220 ARG A CD  1 
ATOM   1708  N NE  . ARG A 1 217 ? 33.900  -46.237 24.221  1.00 50.65  ? 220 ARG A NE  1 
ATOM   1709  C CZ  . ARG A 1 217 ? 33.429  -47.433 23.895  1.00 49.59  ? 220 ARG A CZ  1 
ATOM   1710  N NH1 . ARG A 1 217 ? 33.046  -48.264 24.852  1.00 54.13  ? 220 ARG A NH1 1 
ATOM   1711  N NH2 . ARG A 1 217 ? 33.337  -47.791 22.621  1.00 42.24  ? 220 ARG A NH2 1 
ATOM   1712  N N   . PRO A 1 218 ? 36.936  -44.653 30.098  1.00 61.10  ? 221 PRO A N   1 
ATOM   1713  C CA  . PRO A 1 218 ? 36.798  -44.300 31.510  1.00 64.37  ? 221 PRO A CA  1 
ATOM   1714  C C   . PRO A 1 218 ? 35.393  -44.612 31.998  1.00 61.46  ? 221 PRO A C   1 
ATOM   1715  O O   . PRO A 1 218 ? 34.423  -44.109 31.430  1.00 56.50  ? 221 PRO A O   1 
ATOM   1716  C CB  . PRO A 1 218 ? 37.015  -42.785 31.514  1.00 68.04  ? 221 PRO A CB  1 
ATOM   1717  C CG  . PRO A 1 218 ? 37.764  -42.497 30.253  1.00 71.39  ? 221 PRO A CG  1 
ATOM   1718  C CD  . PRO A 1 218 ? 37.237  -43.480 29.262  1.00 62.90  ? 221 PRO A CD  1 
ATOM   1719  N N   . LYS A 1 219 ? 35.294  -45.447 33.028  1.00 65.99  ? 222 LYS A N   1 
ATOM   1720  C CA  . LYS A 1 219 ? 34.019  -45.729 33.671  1.00 60.56  ? 222 LYS A CA  1 
ATOM   1721  C C   . LYS A 1 219 ? 33.255  -44.422 33.922  1.00 63.18  ? 222 LYS A C   1 
ATOM   1722  O O   . LYS A 1 219 ? 33.799  -43.478 34.504  1.00 68.14  ? 222 LYS A O   1 
ATOM   1723  C CB  . LYS A 1 219 ? 34.249  -46.474 34.993  1.00 63.68  ? 222 LYS A CB  1 
ATOM   1724  C CG  . LYS A 1 219 ? 33.845  -47.955 35.001  1.00 64.78  ? 222 LYS A CG  1 
ATOM   1725  C CD  . LYS A 1 219 ? 35.010  -48.895 34.693  1.00 73.80  ? 222 LYS A CD  1 
ATOM   1726  C CE  . LYS A 1 219 ? 35.386  -48.866 33.219  1.00 81.28  ? 222 LYS A CE  1 
ATOM   1727  N NZ  . LYS A 1 219 ? 36.457  -49.843 32.878  1.00 86.95  ? 222 LYS A NZ  1 
ATOM   1728  N N   . VAL A 1 220 ? 32.006  -44.374 33.460  1.00 71.20  ? 223 VAL A N   1 
ATOM   1729  C CA  . VAL A 1 220 ? 31.105  -43.247 33.704  1.00 60.24  ? 223 VAL A CA  1 
ATOM   1730  C C   . VAL A 1 220 ? 29.812  -43.778 34.301  1.00 64.66  ? 223 VAL A C   1 
ATOM   1731  O O   . VAL A 1 220 ? 29.005  -44.380 33.597  1.00 64.57  ? 223 VAL A O   1 
ATOM   1732  C CB  . VAL A 1 220 ? 30.758  -42.479 32.406  1.00 48.97  ? 223 VAL A CB  1 
ATOM   1733  C CG1 . VAL A 1 220 ? 29.552  -41.576 32.623  1.00 28.43  ? 223 VAL A CG1 1 
ATOM   1734  C CG2 . VAL A 1 220 ? 31.950  -41.672 31.915  1.00 58.19  ? 223 VAL A CG2 1 
ATOM   1735  N N   . ASN A 1 221 ? 29.613  -43.538 35.592  1.00 100.70 ? 224 ASN A N   1 
ATOM   1736  C CA  . ASN A 1 221 ? 28.588  -44.243 36.350  1.00 82.23  ? 224 ASN A CA  1 
ATOM   1737  C C   . ASN A 1 221 ? 28.972  -45.707 36.460  1.00 82.81  ? 224 ASN A C   1 
ATOM   1738  O O   . ASN A 1 221 ? 28.128  -46.594 36.385  1.00 76.77  ? 224 ASN A O   1 
ATOM   1739  C CB  . ASN A 1 221 ? 27.211  -44.086 35.713  1.00 74.16  ? 224 ASN A CB  1 
ATOM   1740  C CG  . ASN A 1 221 ? 26.654  -42.698 35.891  1.00 74.70  ? 224 ASN A CG  1 
ATOM   1741  O OD1 . ASN A 1 221 ? 27.015  -41.998 36.836  1.00 85.91  ? 224 ASN A OD1 1 
ATOM   1742  N ND2 . ASN A 1 221 ? 25.769  -42.288 34.989  1.00 61.73  ? 224 ASN A ND2 1 
ATOM   1743  N N   . GLY A 1 222 ? 30.270  -45.938 36.633  1.00 62.91  ? 225 GLY A N   1 
ATOM   1744  C CA  . GLY A 1 222 ? 30.810  -47.279 36.731  1.00 68.91  ? 225 GLY A CA  1 
ATOM   1745  C C   . GLY A 1 222 ? 30.517  -48.087 35.487  1.00 69.68  ? 225 GLY A C   1 
ATOM   1746  O O   . GLY A 1 222 ? 30.088  -49.229 35.571  1.00 75.38  ? 225 GLY A O   1 
ATOM   1747  N N   . GLN A 1 223 ? 30.741  -47.490 34.325  1.00 70.51  ? 226 GLN A N   1 
ATOM   1748  C CA  . GLN A 1 223 ? 30.447  -48.158 33.065  1.00 61.58  ? 226 GLN A CA  1 
ATOM   1749  C C   . GLN A 1 223 ? 31.446  -47.751 31.997  1.00 66.46  ? 226 GLN A C   1 
ATOM   1750  O O   . GLN A 1 223 ? 31.591  -46.569 31.691  1.00 66.66  ? 226 GLN A O   1 
ATOM   1751  C CB  . GLN A 1 223 ? 29.039  -47.800 32.595  1.00 47.62  ? 226 GLN A CB  1 
ATOM   1752  C CG  . GLN A 1 223 ? 27.973  -47.911 33.664  1.00 44.31  ? 226 GLN A CG  1 
ATOM   1753  C CD  . GLN A 1 223 ? 27.736  -49.343 34.112  1.00 53.91  ? 226 GLN A CD  1 
ATOM   1754  O OE1 . GLN A 1 223 ? 28.188  -50.296 33.471  1.00 58.88  ? 226 GLN A OE1 1 
ATOM   1755  N NE2 . GLN A 1 223 ? 27.024  -49.501 35.222  1.00 51.16  ? 226 GLN A NE2 1 
ATOM   1756  N N   . GLY A 1 224 ? 32.137  -48.730 31.431  1.00 56.21  ? 227 GLY A N   1 
ATOM   1757  C CA  . GLY A 1 224 ? 33.063  -48.461 30.349  1.00 54.06  ? 227 GLY A CA  1 
ATOM   1758  C C   . GLY A 1 224 ? 32.296  -48.441 29.048  1.00 45.62  ? 227 GLY A C   1 
ATOM   1759  O O   . GLY A 1 224 ? 32.692  -47.788 28.081  1.00 45.85  ? 227 GLY A O   1 
ATOM   1760  N N   . GLY A 1 225 ? 31.182  -49.165 29.033  1.00 57.92  ? 228 GLY A N   1 
ATOM   1761  C CA  . GLY A 1 225 ? 30.319  -49.222 27.870  1.00 49.24  ? 228 GLY A CA  1 
ATOM   1762  C C   . GLY A 1 225 ? 29.615  -47.903 27.608  1.00 52.51  ? 228 GLY A C   1 
ATOM   1763  O O   . GLY A 1 225 ? 29.691  -46.969 28.409  1.00 57.95  ? 228 GLY A O   1 
ATOM   1764  N N   . ARG A 1 226 ? 28.929  -47.833 26.472  1.00 50.17  ? 229 ARG A N   1 
ATOM   1765  C CA  . ARG A 1 226 ? 28.216  -46.634 26.051  1.00 36.75  ? 229 ARG A CA  1 
ATOM   1766  C C   . ARG A 1 226 ? 27.027  -47.065 25.217  1.00 35.20  ? 229 ARG A C   1 
ATOM   1767  O O   . ARG A 1 226 ? 27.077  -48.090 24.544  1.00 47.04  ? 229 ARG A O   1 
ATOM   1768  C CB  . ARG A 1 226 ? 29.119  -45.741 25.191  1.00 39.18  ? 229 ARG A CB  1 
ATOM   1769  C CG  . ARG A 1 226 ? 30.416  -45.279 25.857  1.00 52.07  ? 229 ARG A CG  1 
ATOM   1770  C CD  . ARG A 1 226 ? 30.177  -44.129 26.814  1.00 53.75  ? 229 ARG A CD  1 
ATOM   1771  N NE  . ARG A 1 226 ? 31.423  -43.628 27.387  1.00 69.04  ? 229 ARG A NE  1 
ATOM   1772  C CZ  . ARG A 1 226 ? 32.000  -44.137 28.470  1.00 74.87  ? 229 ARG A CZ  1 
ATOM   1773  N NH1 . ARG A 1 226 ? 31.450  -45.168 29.093  1.00 77.39  ? 229 ARG A NH1 1 
ATOM   1774  N NH2 . ARG A 1 226 ? 33.130  -43.625 28.932  1.00 73.01  ? 229 ARG A NH2 1 
ATOM   1775  N N   . MET A 1 227 ? 25.951  -46.293 25.246  1.00 64.85  ? 230 MET A N   1 
ATOM   1776  C CA  . MET A 1 227 ? 24.831  -46.599 24.373  1.00 53.18  ? 230 MET A CA  1 
ATOM   1777  C C   . MET A 1 227 ? 24.585  -45.451 23.415  1.00 54.54  ? 230 MET A C   1 
ATOM   1778  O O   . MET A 1 227 ? 24.331  -44.325 23.834  1.00 57.53  ? 230 MET A O   1 
ATOM   1779  C CB  . MET A 1 227 ? 23.581  -46.948 25.179  1.00 37.20  ? 230 MET A CB  1 
ATOM   1780  C CG  . MET A 1 227 ? 23.791  -48.151 26.087  1.00 38.39  ? 230 MET A CG  1 
ATOM   1781  S SD  . MET A 1 227 ? 22.282  -48.964 26.625  1.00 55.59  ? 230 MET A SD  1 
ATOM   1782  C CE  . MET A 1 227 ? 22.890  -49.903 28.017  1.00 71.96  ? 230 MET A CE  1 
ATOM   1783  N N   . GLU A 1 228 ? 24.684  -45.744 22.124  1.00 58.28  ? 231 GLU A N   1 
ATOM   1784  C CA  . GLU A 1 228 ? 24.516  -44.730 21.103  1.00 54.26  ? 231 GLU A CA  1 
ATOM   1785  C C   . GLU A 1 228 ? 23.103  -44.750 20.550  1.00 54.27  ? 231 GLU A C   1 
ATOM   1786  O O   . GLU A 1 228 ? 22.778  -45.558 19.684  1.00 56.71  ? 231 GLU A O   1 
ATOM   1787  C CB  . GLU A 1 228 ? 25.518  -44.944 19.975  1.00 47.10  ? 231 GLU A CB  1 
ATOM   1788  C CG  . GLU A 1 228 ? 25.454  -43.875 18.903  1.00 50.11  ? 231 GLU A CG  1 
ATOM   1789  C CD  . GLU A 1 228 ? 26.540  -44.034 17.869  1.00 60.28  ? 231 GLU A CD  1 
ATOM   1790  O OE1 . GLU A 1 228 ? 27.714  -44.232 18.261  1.00 66.64  ? 231 GLU A OE1 1 
ATOM   1791  O OE2 . GLU A 1 228 ? 26.214  -43.977 16.664  1.00 61.35  ? 231 GLU A OE2 1 
ATOM   1792  N N   . PHE A 1 229 ? 22.265  -43.852 21.055  1.00 42.31  ? 232 PHE A N   1 
ATOM   1793  C CA  . PHE A 1 229 ? 20.868  -43.797 20.635  1.00 42.50  ? 232 PHE A CA  1 
ATOM   1794  C C   . PHE A 1 229 ? 20.676  -42.924 19.402  1.00 34.47  ? 232 PHE A C   1 
ATOM   1795  O O   . PHE A 1 229 ? 21.321  -41.886 19.253  1.00 34.62  ? 232 PHE A O   1 
ATOM   1796  C CB  . PHE A 1 229 ? 19.976  -43.306 21.775  1.00 50.97  ? 232 PHE A CB  1 
ATOM   1797  C CG  . PHE A 1 229 ? 19.984  -44.204 22.973  1.00 55.00  ? 232 PHE A CG  1 
ATOM   1798  C CD1 . PHE A 1 229 ? 19.138  -45.296 23.040  1.00 58.12  ? 232 PHE A CD1 1 
ATOM   1799  C CD2 . PHE A 1 229 ? 20.847  -43.964 24.026  1.00 57.39  ? 232 PHE A CD2 1 
ATOM   1800  C CE1 . PHE A 1 229 ? 19.146  -46.131 24.138  1.00 62.64  ? 232 PHE A CE1 1 
ATOM   1801  C CE2 . PHE A 1 229 ? 20.860  -44.792 25.127  1.00 57.53  ? 232 PHE A CE2 1 
ATOM   1802  C CZ  . PHE A 1 229 ? 20.008  -45.880 25.184  1.00 57.82  ? 232 PHE A CZ  1 
ATOM   1803  N N   . SER A 1 230 ? 19.790  -43.369 18.519  1.00 43.47  ? 233 SER A N   1 
ATOM   1804  C CA  . SER A 1 230 ? 19.464  -42.653 17.298  1.00 42.32  ? 233 SER A CA  1 
ATOM   1805  C C   . SER A 1 230 ? 17.952  -42.598 17.219  1.00 49.73  ? 233 SER A C   1 
ATOM   1806  O O   . SER A 1 230 ? 17.264  -43.239 18.018  1.00 54.30  ? 233 SER A O   1 
ATOM   1807  C CB  . SER A 1 230 ? 20.010  -43.403 16.079  1.00 47.27  ? 233 SER A CB  1 
ATOM   1808  O OG  . SER A 1 230 ? 21.378  -43.728 16.238  1.00 50.47  ? 233 SER A OG  1 
ATOM   1809  N N   . TRP A 1 231 ? 17.425  -41.857 16.253  1.00 46.82  ? 234 TRP A N   1 
ATOM   1810  C CA  . TRP A 1 231 ? 15.980  -41.768 16.105  1.00 42.19  ? 234 TRP A CA  1 
ATOM   1811  C C   . TRP A 1 231 ? 15.550  -41.485 14.676  1.00 54.41  ? 234 TRP A C   1 
ATOM   1812  O O   . TRP A 1 231 ? 16.383  -41.259 13.796  1.00 67.56  ? 234 TRP A O   1 
ATOM   1813  C CB  . TRP A 1 231 ? 15.430  -40.689 17.026  1.00 29.69  ? 234 TRP A CB  1 
ATOM   1814  C CG  . TRP A 1 231 ? 16.031  -39.343 16.790  1.00 38.42  ? 234 TRP A CG  1 
ATOM   1815  C CD1 . TRP A 1 231 ? 17.191  -38.859 17.316  1.00 45.47  ? 234 TRP A CD1 1 
ATOM   1816  C CD2 . TRP A 1 231 ? 15.499  -38.296 15.966  1.00 38.36  ? 234 TRP A CD2 1 
ATOM   1817  N NE1 . TRP A 1 231 ? 17.412  -37.574 16.873  1.00 37.36  ? 234 TRP A NE1 1 
ATOM   1818  C CE2 . TRP A 1 231 ? 16.384  -37.211 16.043  1.00 34.44  ? 234 TRP A CE2 1 
ATOM   1819  C CE3 . TRP A 1 231 ? 14.355  -38.175 15.173  1.00 37.01  ? 234 TRP A CE3 1 
ATOM   1820  C CZ2 . TRP A 1 231 ? 16.167  -36.030 15.354  1.00 36.54  ? 234 TRP A CZ2 1 
ATOM   1821  C CZ3 . TRP A 1 231 ? 14.141  -36.995 14.494  1.00 27.29  ? 234 TRP A CZ3 1 
ATOM   1822  C CH2 . TRP A 1 231 ? 15.041  -35.946 14.585  1.00 39.03  ? 234 TRP A CH2 1 
ATOM   1823  N N   . THR A 1 232 ? 14.237  -41.490 14.461  1.00 42.11  ? 235 THR A N   1 
ATOM   1824  C CA  . THR A 1 232 ? 13.665  -41.262 13.140  1.00 55.40  ? 235 THR A CA  1 
ATOM   1825  C C   . THR A 1 232 ? 12.192  -40.906 13.294  1.00 56.90  ? 235 THR A C   1 
ATOM   1826  O O   . THR A 1 232 ? 11.634  -41.019 14.385  1.00 50.11  ? 235 THR A O   1 
ATOM   1827  C CB  . THR A 1 232 ? 13.783  -42.528 12.254  1.00 59.55  ? 235 THR A CB  1 
ATOM   1828  O OG1 . THR A 1 232 ? 13.571  -42.194 10.876  1.00 74.59  ? 235 THR A OG1 1 
ATOM   1829  C CG2 . THR A 1 232 ? 12.771  -43.564 12.689  1.00 52.36  ? 235 THR A CG2 1 
ATOM   1830  N N   . LEU A 1 233 ? 11.576  -40.461 12.203  1.00 54.24  ? 236 LEU A N   1 
ATOM   1831  C CA  . LEU A 1 233 ? 10.129  -40.314 12.138  1.00 49.89  ? 236 LEU A CA  1 
ATOM   1832  C C   . LEU A 1 233 ? 9.556   -41.335 11.164  1.00 64.37  ? 236 LEU A C   1 
ATOM   1833  O O   . LEU A 1 233 ? 9.680   -41.192 9.946   1.00 89.27  ? 236 LEU A O   1 
ATOM   1834  C CB  . LEU A 1 233 ? 9.727   -38.912 11.703  1.00 50.68  ? 236 LEU A CB  1 
ATOM   1835  C CG  . LEU A 1 233 ? 9.513   -37.869 12.795  1.00 52.25  ? 236 LEU A CG  1 
ATOM   1836  C CD1 . LEU A 1 233 ? 10.815  -37.566 13.514  1.00 56.13  ? 236 LEU A CD1 1 
ATOM   1837  C CD2 . LEU A 1 233 ? 8.936   -36.608 12.187  1.00 55.15  ? 236 LEU A CD2 1 
ATOM   1838  N N   . LEU A 1 234 ? 8.940   -42.374 11.718  1.00 35.70  ? 237 LEU A N   1 
ATOM   1839  C CA  . LEU A 1 234 ? 8.256   -43.382 10.926  1.00 49.93  ? 237 LEU A CA  1 
ATOM   1840  C C   . LEU A 1 234 ? 6.915   -42.837 10.455  1.00 76.25  ? 237 LEU A C   1 
ATOM   1841  O O   . LEU A 1 234 ? 5.997   -42.629 11.252  1.00 73.02  ? 237 LEU A O   1 
ATOM   1842  C CB  . LEU A 1 234 ? 8.065   -44.655 11.755  1.00 29.97  ? 237 LEU A CB  1 
ATOM   1843  C CG  . LEU A 1 234 ? 7.263   -45.790 11.121  1.00 47.81  ? 237 LEU A CG  1 
ATOM   1844  C CD1 . LEU A 1 234 ? 7.893   -46.237 9.814   1.00 66.95  ? 237 LEU A CD1 1 
ATOM   1845  C CD2 . LEU A 1 234 ? 7.155   -46.941 12.098  1.00 30.69  ? 237 LEU A CD2 1 
ATOM   1846  N N   . ASP A 1 235 ? 6.819   -42.595 9.154   1.00 74.77  ? 238 ASP A N   1 
ATOM   1847  C CA  . ASP A 1 235 ? 5.608   -42.047 8.564   1.00 81.50  ? 238 ASP A CA  1 
ATOM   1848  C C   . ASP A 1 235 ? 4.422   -42.959 8.826   1.00 82.53  ? 238 ASP A C   1 
ATOM   1849  O O   . ASP A 1 235 ? 4.590   -44.097 9.261   1.00 82.72  ? 238 ASP A O   1 
ATOM   1850  C CB  . ASP A 1 235 ? 5.795   -41.839 7.061   1.00 86.15  ? 238 ASP A CB  1 
ATOM   1851  C CG  . ASP A 1 235 ? 6.714   -40.673 6.745   1.00 89.27  ? 238 ASP A CG  1 
ATOM   1852  O OD1 . ASP A 1 235 ? 6.658   -39.659 7.475   1.00 86.02  ? 238 ASP A OD1 1 
ATOM   1853  O OD2 . ASP A 1 235 ? 7.490   -40.768 5.771   1.00 92.60  ? 238 ASP A OD2 1 
ATOM   1854  N N   . MET A 1 236 ? 3.220   -42.455 8.571   1.00 85.72  ? 239 MET A N   1 
ATOM   1855  C CA  . MET A 1 236 ? 2.021   -43.263 8.746   1.00 83.08  ? 239 MET A CA  1 
ATOM   1856  C C   . MET A 1 236 ? 2.000   -44.379 7.708   1.00 88.69  ? 239 MET A C   1 
ATOM   1857  O O   . MET A 1 236 ? 2.372   -44.177 6.549   1.00 93.62  ? 239 MET A O   1 
ATOM   1858  C CB  . MET A 1 236 ? 0.757   -42.401 8.651   1.00 76.44  ? 239 MET A CB  1 
ATOM   1859  C CG  . MET A 1 236 ? 0.673   -41.289 9.695   1.00 64.81  ? 239 MET A CG  1 
ATOM   1860  S SD  . MET A 1 236 ? -0.884  -40.379 9.628   1.00 101.40 ? 239 MET A SD  1 
ATOM   1861  C CE  . MET A 1 236 ? -0.936  -39.957 7.889   1.00 116.60 ? 239 MET A CE  1 
ATOM   1862  N N   . TRP A 1 237 ? 1.589   -45.562 8.147   1.00 80.78  ? 240 TRP A N   1 
ATOM   1863  C CA  . TRP A 1 237 ? 1.453   -46.720 7.269   1.00 89.60  ? 240 TRP A CA  1 
ATOM   1864  C C   . TRP A 1 237 ? 2.796   -47.315 6.876   1.00 91.90  ? 240 TRP A C   1 
ATOM   1865  O O   . TRP A 1 237 ? 2.869   -48.447 6.396   1.00 97.45  ? 240 TRP A O   1 
ATOM   1866  C CB  . TRP A 1 237 ? 0.641   -46.358 6.027   1.00 92.83  ? 240 TRP A CB  1 
ATOM   1867  C CG  . TRP A 1 237 ? -0.600  -45.618 6.365   1.00 95.22  ? 240 TRP A CG  1 
ATOM   1868  C CD1 . TRP A 1 237 ? -1.044  -44.465 5.799   1.00 93.75  ? 240 TRP A CD1 1 
ATOM   1869  C CD2 . TRP A 1 237 ? -1.550  -45.964 7.376   1.00 93.88  ? 240 TRP A CD2 1 
ATOM   1870  N NE1 . TRP A 1 237 ? -2.224  -44.076 6.385   1.00 89.22  ? 240 TRP A NE1 1 
ATOM   1871  C CE2 . TRP A 1 237 ? -2.555  -44.982 7.359   1.00 87.79  ? 240 TRP A CE2 1 
ATOM   1872  C CE3 . TRP A 1 237 ? -1.652  -47.016 8.292   1.00 98.28  ? 240 TRP A CE3 1 
ATOM   1873  C CZ2 . TRP A 1 237 ? -3.646  -45.017 8.218   1.00 90.28  ? 240 TRP A CZ2 1 
ATOM   1874  C CZ3 . TRP A 1 237 ? -2.734  -47.048 9.144   1.00 102.31 ? 240 TRP A CZ3 1 
ATOM   1875  C CH2 . TRP A 1 237 ? -3.716  -46.055 9.104   1.00 97.32  ? 240 TRP A CH2 1 
ATOM   1876  N N   . ASP A 1 238 ? 3.859   -46.551 7.082   1.00 88.69  ? 241 ASP A N   1 
ATOM   1877  C CA  . ASP A 1 238 ? 5.187   -47.051 6.787   1.00 76.32  ? 241 ASP A CA  1 
ATOM   1878  C C   . ASP A 1 238 ? 5.625   -47.982 7.896   1.00 78.33  ? 241 ASP A C   1 
ATOM   1879  O O   . ASP A 1 238 ? 5.295   -47.763 9.058   1.00 84.86  ? 241 ASP A O   1 
ATOM   1880  C CB  . ASP A 1 238 ? 6.178   -45.909 6.654   1.00 70.80  ? 241 ASP A CB  1 
ATOM   1881  C CG  . ASP A 1 238 ? 7.518   -46.376 6.160   1.00 65.17  ? 241 ASP A CG  1 
ATOM   1882  O OD1 . ASP A 1 238 ? 7.557   -47.469 5.558   1.00 52.58  ? 241 ASP A OD1 1 
ATOM   1883  O OD2 . ASP A 1 238 ? 8.521   -45.656 6.365   1.00 67.65  ? 241 ASP A OD2 1 
ATOM   1884  N N   . THR A 1 239 ? 6.369   -49.021 7.533   1.00 65.41  ? 242 THR A N   1 
ATOM   1885  C CA  . THR A 1 239 ? 6.805   -50.024 8.496   1.00 58.15  ? 242 THR A CA  1 
ATOM   1886  C C   . THR A 1 239 ? 8.272   -49.807 8.843   1.00 60.15  ? 242 THR A C   1 
ATOM   1887  O O   . THR A 1 239 ? 9.035   -49.293 8.028   1.00 61.75  ? 242 THR A O   1 
ATOM   1888  C CB  . THR A 1 239 ? 6.614   -51.444 7.933   1.00 61.21  ? 242 THR A CB  1 
ATOM   1889  O OG1 . THR A 1 239 ? 5.272   -51.593 7.455   1.00 78.33  ? 242 THR A OG1 1 
ATOM   1890  C CG2 . THR A 1 239 ? 6.890   -52.492 8.997   1.00 52.53  ? 242 THR A CG2 1 
ATOM   1891  N N   . ILE A 1 240 ? 8.664   -50.186 10.055  1.00 88.80  ? 243 ILE A N   1 
ATOM   1892  C CA  . ILE A 1 240 ? 10.061  -50.087 10.464  1.00 79.11  ? 243 ILE A CA  1 
ATOM   1893  C C   . ILE A 1 240 ? 10.627  -51.480 10.756  1.00 82.80  ? 243 ILE A C   1 
ATOM   1894  O O   . ILE A 1 240 ? 9.935   -52.335 11.305  1.00 77.19  ? 243 ILE A O   1 
ATOM   1895  C CB  . ILE A 1 240 ? 10.236  -49.161 11.683  1.00 54.74  ? 243 ILE A CB  1 
ATOM   1896  C CG1 . ILE A 1 240 ? 11.713  -48.852 11.915  1.00 48.05  ? 243 ILE A CG1 1 
ATOM   1897  C CG2 . ILE A 1 240 ? 9.631   -49.778 12.927  1.00 40.12  ? 243 ILE A CG2 1 
ATOM   1898  C CD1 . ILE A 1 240 ? 12.010  -48.342 13.312  1.00 32.53  ? 243 ILE A CD1 1 
ATOM   1899  N N   . ASN A 1 241 ? 11.886  -51.697 10.386  1.00 65.46  ? 244 ASN A N   1 
ATOM   1900  C CA  . ASN A 1 241 ? 12.480  -53.030 10.407  1.00 57.13  ? 244 ASN A CA  1 
ATOM   1901  C C   . ASN A 1 241 ? 13.750  -53.161 11.239  1.00 51.16  ? 244 ASN A C   1 
ATOM   1902  O O   . ASN A 1 241 ? 14.823  -52.756 10.799  1.00 58.60  ? 244 ASN A O   1 
ATOM   1903  C CB  . ASN A 1 241 ? 12.793  -53.469 8.979   1.00 58.36  ? 244 ASN A CB  1 
ATOM   1904  C CG  . ASN A 1 241 ? 11.555  -53.823 8.196   1.00 62.96  ? 244 ASN A CG  1 
ATOM   1905  O OD1 . ASN A 1 241 ? 10.526  -54.171 8.770   1.00 57.80  ? 244 ASN A OD1 1 
ATOM   1906  N ND2 . ASN A 1 241 ? 11.647  -53.746 6.872   1.00 77.56  ? 244 ASN A ND2 1 
ATOM   1907  N N   . PHE A 1 242 ? 13.638  -53.749 12.426  1.00 77.39  ? 245 PHE A N   1 
ATOM   1908  C CA  . PHE A 1 242 ? 14.817  -54.021 13.246  1.00 65.09  ? 245 PHE A CA  1 
ATOM   1909  C C   . PHE A 1 242 ? 15.396  -55.414 13.009  1.00 70.32  ? 245 PHE A C   1 
ATOM   1910  O O   . PHE A 1 242 ? 14.674  -56.411 12.995  1.00 78.44  ? 245 PHE A O   1 
ATOM   1911  C CB  . PHE A 1 242 ? 14.512  -53.847 14.734  1.00 43.00  ? 245 PHE A CB  1 
ATOM   1912  C CG  . PHE A 1 242 ? 14.233  -52.434 15.129  1.00 37.99  ? 245 PHE A CG  1 
ATOM   1913  C CD1 . PHE A 1 242 ? 15.223  -51.468 15.042  1.00 42.07  ? 245 PHE A CD1 1 
ATOM   1914  C CD2 . PHE A 1 242 ? 12.979  -52.061 15.588  1.00 40.11  ? 245 PHE A CD2 1 
ATOM   1915  C CE1 . PHE A 1 242 ? 14.962  -50.151 15.401  1.00 42.20  ? 245 PHE A CE1 1 
ATOM   1916  C CE2 . PHE A 1 242 ? 12.716  -50.749 15.944  1.00 40.06  ? 245 PHE A CE2 1 
ATOM   1917  C CZ  . PHE A 1 242 ? 13.707  -49.795 15.850  1.00 39.87  ? 245 PHE A CZ  1 
ATOM   1918  N N   . GLU A 1 243 ? 16.709  -55.473 12.821  1.00 41.68  ? 246 GLU A N   1 
ATOM   1919  C CA  . GLU A 1 243 ? 17.410  -56.746 12.773  1.00 44.55  ? 246 GLU A CA  1 
ATOM   1920  C C   . GLU A 1 243 ? 18.782  -56.583 13.406  1.00 42.11  ? 246 GLU A C   1 
ATOM   1921  O O   . GLU A 1 243 ? 19.469  -55.585 13.170  1.00 42.62  ? 246 GLU A O   1 
ATOM   1922  C CB  . GLU A 1 243 ? 17.546  -57.253 11.338  1.00 58.51  ? 246 GLU A CB  1 
ATOM   1923  C CG  . GLU A 1 243 ? 18.257  -58.595 11.229  1.00 68.91  ? 246 GLU A CG  1 
ATOM   1924  C CD  . GLU A 1 243 ? 18.448  -59.038 9.794   1.00 77.21  ? 246 GLU A CD  1 
ATOM   1925  O OE1 . GLU A 1 243 ? 17.981  -58.323 8.886   1.00 77.48  ? 246 GLU A OE1 1 
ATOM   1926  O OE2 . GLU A 1 243 ? 19.065  -60.097 9.573   1.00 81.28  ? 246 GLU A OE2 1 
ATOM   1927  N N   . SER A 1 244 ? 19.175  -57.561 14.213  1.00 47.18  ? 247 SER A N   1 
ATOM   1928  C CA  . SER A 1 244 ? 20.458  -57.503 14.891  1.00 45.03  ? 247 SER A CA  1 
ATOM   1929  C C   . SER A 1 244 ? 20.906  -58.869 15.387  1.00 52.30  ? 247 SER A C   1 
ATOM   1930  O O   . SER A 1 244 ? 20.087  -59.719 15.732  1.00 58.58  ? 247 SER A O   1 
ATOM   1931  C CB  . SER A 1 244 ? 20.402  -56.517 16.055  1.00 43.63  ? 247 SER A CB  1 
ATOM   1932  O OG  . SER A 1 244 ? 21.581  -56.593 16.838  1.00 51.49  ? 247 SER A OG  1 
ATOM   1933  N N   . THR A 1 245 ? 22.217  -59.072 15.412  1.00 51.84  ? 248 THR A N   1 
ATOM   1934  C CA  . THR A 1 245 ? 22.790  -60.286 15.966  1.00 48.86  ? 248 THR A CA  1 
ATOM   1935  C C   . THR A 1 245 ? 23.623  -59.954 17.202  1.00 50.37  ? 248 THR A C   1 
ATOM   1936  O O   . THR A 1 245 ? 24.595  -60.640 17.512  1.00 54.82  ? 248 THR A O   1 
ATOM   1937  C CB  . THR A 1 245 ? 23.654  -61.002 14.932  1.00 51.10  ? 248 THR A CB  1 
ATOM   1938  O OG1 . THR A 1 245 ? 24.692  -60.121 14.488  1.00 57.08  ? 248 THR A OG1 1 
ATOM   1939  C CG2 . THR A 1 245 ? 22.806  -61.405 13.747  1.00 57.46  ? 248 THR A CG2 1 
ATOM   1940  N N   . GLY A 1 246 ? 23.232  -58.893 17.903  1.00 56.59  ? 249 GLY A N   1 
ATOM   1941  C CA  . GLY A 1 246 ? 23.936  -58.452 19.094  1.00 55.32  ? 249 GLY A CA  1 
ATOM   1942  C C   . GLY A 1 246 ? 23.891  -56.949 19.275  1.00 54.32  ? 249 GLY A C   1 
ATOM   1943  O O   . GLY A 1 246 ? 23.702  -56.214 18.315  1.00 46.09  ? 249 GLY A O   1 
ATOM   1944  N N   . ASN A 1 247 ? 24.042  -56.499 20.516  1.00 66.65  ? 250 ASN A N   1 
ATOM   1945  C CA  . ASN A 1 247 ? 24.188  -55.078 20.826  1.00 57.29  ? 250 ASN A CA  1 
ATOM   1946  C C   . ASN A 1 247 ? 22.999  -54.164 20.490  1.00 48.29  ? 250 ASN A C   1 
ATOM   1947  O O   . ASN A 1 247 ? 23.153  -52.943 20.459  1.00 48.06  ? 250 ASN A O   1 
ATOM   1948  C CB  . ASN A 1 247 ? 25.455  -54.531 20.169  1.00 49.83  ? 250 ASN A CB  1 
ATOM   1949  C CG  . ASN A 1 247 ? 26.659  -55.423 20.394  1.00 58.73  ? 250 ASN A CG  1 
ATOM   1950  O OD1 . ASN A 1 247 ? 26.792  -56.467 19.762  1.00 59.23  ? 250 ASN A OD1 1 
ATOM   1951  N ND2 . ASN A 1 247 ? 27.551  -55.007 21.285  1.00 66.81  ? 250 ASN A ND2 1 
ATOM   1952  N N   . LEU A 1 248 ? 21.820  -54.732 20.248  1.00 50.48  ? 251 LEU A N   1 
ATOM   1953  C CA  . LEU A 1 248 ? 20.643  -53.913 19.930  1.00 49.10  ? 251 LEU A CA  1 
ATOM   1954  C C   . LEU A 1 248 ? 19.845  -53.527 21.164  1.00 57.14  ? 251 LEU A C   1 
ATOM   1955  O O   . LEU A 1 248 ? 19.280  -54.381 21.841  1.00 69.52  ? 251 LEU A O   1 
ATOM   1956  C CB  . LEU A 1 248 ? 19.715  -54.619 18.932  1.00 42.05  ? 251 LEU A CB  1 
ATOM   1957  C CG  . LEU A 1 248 ? 18.268  -54.108 18.912  1.00 30.32  ? 251 LEU A CG  1 
ATOM   1958  C CD1 . LEU A 1 248 ? 18.172  -52.691 18.319  1.00 21.53  ? 251 LEU A CD1 1 
ATOM   1959  C CD2 . LEU A 1 248 ? 17.332  -55.064 18.176  1.00 20.33  ? 251 LEU A CD2 1 
ATOM   1960  N N   . ILE A 1 249 ? 19.806  -52.234 21.457  1.00 36.70  ? 252 ILE A N   1 
ATOM   1961  C CA  . ILE A 1 249 ? 18.895  -51.720 22.469  1.00 39.47  ? 252 ILE A CA  1 
ATOM   1962  C C   . ILE A 1 249 ? 17.657  -51.268 21.733  1.00 43.19  ? 252 ILE A C   1 
ATOM   1963  O O   . ILE A 1 249 ? 17.556  -50.111 21.352  1.00 37.36  ? 252 ILE A O   1 
ATOM   1964  C CB  . ILE A 1 249 ? 19.477  -50.504 23.219  1.00 30.39  ? 252 ILE A CB  1 
ATOM   1965  C CG1 . ILE A 1 249 ? 20.879  -50.807 23.738  1.00 31.38  ? 252 ILE A CG1 1 
ATOM   1966  C CG2 . ILE A 1 249 ? 18.579  -50.099 24.372  1.00 32.95  ? 252 ILE A CG2 1 
ATOM   1967  C CD1 . ILE A 1 249 ? 20.975  -52.093 24.502  1.00 40.01  ? 252 ILE A CD1 1 
ATOM   1968  N N   . ALA A 1 250 ? 16.726  -52.184 21.509  1.00 51.09  ? 253 ALA A N   1 
ATOM   1969  C CA  . ALA A 1 250 ? 15.512  -51.867 20.769  1.00 45.38  ? 253 ALA A CA  1 
ATOM   1970  C C   . ALA A 1 250 ? 14.556  -51.069 21.638  1.00 55.22  ? 253 ALA A C   1 
ATOM   1971  O O   . ALA A 1 250 ? 14.765  -50.950 22.841  1.00 75.46  ? 253 ALA A O   1 
ATOM   1972  C CB  . ALA A 1 250 ? 14.840  -53.147 20.284  1.00 47.20  ? 253 ALA A CB  1 
ATOM   1973  N N   . PRO A 1 251 ? 13.498  -50.520 21.030  1.00 54.09  ? 254 PRO A N   1 
ATOM   1974  C CA  . PRO A 1 251 ? 12.506  -49.767 21.790  1.00 51.00  ? 254 PRO A CA  1 
ATOM   1975  C C   . PRO A 1 251 ? 11.264  -50.603 22.044  1.00 61.71  ? 254 PRO A C   1 
ATOM   1976  O O   . PRO A 1 251 ? 10.968  -51.497 21.259  1.00 61.08  ? 254 PRO A O   1 
ATOM   1977  C CB  . PRO A 1 251 ? 12.153  -48.626 20.834  1.00 40.00  ? 254 PRO A CB  1 
ATOM   1978  C CG  . PRO A 1 251 ? 12.365  -49.215 19.439  1.00 43.59  ? 254 PRO A CG  1 
ATOM   1979  C CD  . PRO A 1 251 ? 13.189  -50.494 19.591  1.00 49.41  ? 254 PRO A CD  1 
ATOM   1980  N N   . GLU A 1 252 ? 10.542  -50.310 23.122  1.00 47.51  ? 255 GLU A N   1 
ATOM   1981  C CA  . GLU A 1 252 ? 9.261   -50.962 23.362  1.00 48.88  ? 255 GLU A CA  1 
ATOM   1982  C C   . GLU A 1 252 ? 8.113   -50.067 22.904  1.00 43.14  ? 255 GLU A C   1 
ATOM   1983  O O   . GLU A 1 252 ? 7.144   -50.546 22.307  1.00 36.31  ? 255 GLU A O   1 
ATOM   1984  C CB  . GLU A 1 252 ? 9.092   -51.353 24.834  1.00 57.52  ? 255 GLU A CB  1 
ATOM   1985  C CG  . GLU A 1 252 ? 7.789   -52.095 25.127  1.00 58.93  ? 255 GLU A CG  1 
ATOM   1986  C CD  . GLU A 1 252 ? 7.780   -52.778 26.484  1.00 63.97  ? 255 GLU A CD  1 
ATOM   1987  O OE1 . GLU A 1 252 ? 8.671   -52.491 27.311  1.00 64.60  ? 255 GLU A OE1 1 
ATOM   1988  O OE2 . GLU A 1 252 ? 6.878   -53.606 26.720  1.00 69.37  ? 255 GLU A OE2 1 
ATOM   1989  N N   . TYR A 1 253 ? 8.226   -48.769 23.170  1.00 50.13  ? 256 TYR A N   1 
ATOM   1990  C CA  . TYR A 1 253 ? 7.162   -47.846 22.787  1.00 53.89  ? 256 TYR A CA  1 
ATOM   1991  C C   . TYR A 1 253 ? 7.621   -46.876 21.702  1.00 44.92  ? 256 TYR A C   1 
ATOM   1992  O O   . TYR A 1 253 ? 8.812   -46.594 21.574  1.00 45.70  ? 256 TYR A O   1 
ATOM   1993  C CB  . TYR A 1 253 ? 6.666   -47.037 23.988  1.00 59.84  ? 256 TYR A CB  1 
ATOM   1994  C CG  . TYR A 1 253 ? 6.414   -47.819 25.261  1.00 63.21  ? 256 TYR A CG  1 
ATOM   1995  C CD1 . TYR A 1 253 ? 5.126   -48.180 25.638  1.00 63.70  ? 256 TYR A CD1 1 
ATOM   1996  C CD2 . TYR A 1 253 ? 7.463   -48.167 26.102  1.00 65.05  ? 256 TYR A CD2 1 
ATOM   1997  C CE1 . TYR A 1 253 ? 4.893   -48.879 26.811  1.00 75.29  ? 256 TYR A CE1 1 
ATOM   1998  C CE2 . TYR A 1 253 ? 7.242   -48.869 27.272  1.00 66.89  ? 256 TYR A CE2 1 
ATOM   1999  C CZ  . TYR A 1 253 ? 5.957   -49.222 27.623  1.00 78.42  ? 256 TYR A CZ  1 
ATOM   2000  O OH  . TYR A 1 253 ? 5.748   -49.915 28.793  1.00 84.22  ? 256 TYR A OH  1 
ATOM   2001  N N   . GLY A 1 254 ? 6.667   -46.369 20.928  1.00 64.85  ? 257 GLY A N   1 
ATOM   2002  C CA  . GLY A 1 254 ? 6.906   -45.262 20.022  1.00 54.13  ? 257 GLY A CA  1 
ATOM   2003  C C   . GLY A 1 254 ? 6.142   -44.048 20.532  1.00 60.42  ? 257 GLY A C   1 
ATOM   2004  O O   . GLY A 1 254 ? 5.404   -44.145 21.515  1.00 75.23  ? 257 GLY A O   1 
ATOM   2005  N N   . PHE A 1 255 ? 6.313   -42.904 19.875  1.00 27.56  ? 258 PHE A N   1 
ATOM   2006  C CA  . PHE A 1 255 ? 5.635   -41.682 20.292  1.00 34.97  ? 258 PHE A CA  1 
ATOM   2007  C C   . PHE A 1 255 ? 4.879   -41.058 19.126  1.00 35.52  ? 258 PHE A C   1 
ATOM   2008  O O   . PHE A 1 255 ? 5.497   -40.549 18.194  1.00 37.47  ? 258 PHE A O   1 
ATOM   2009  C CB  . PHE A 1 255 ? 6.638   -40.673 20.831  1.00 36.90  ? 258 PHE A CB  1 
ATOM   2010  C CG  . PHE A 1 255 ? 7.354   -41.120 22.066  1.00 49.31  ? 258 PHE A CG  1 
ATOM   2011  C CD1 . PHE A 1 255 ? 6.720   -41.108 23.291  1.00 67.36  ? 258 PHE A CD1 1 
ATOM   2012  C CD2 . PHE A 1 255 ? 8.673   -41.516 22.008  1.00 44.91  ? 258 PHE A CD2 1 
ATOM   2013  C CE1 . PHE A 1 255 ? 7.384   -41.507 24.434  1.00 69.88  ? 258 PHE A CE1 1 
ATOM   2014  C CE2 . PHE A 1 255 ? 9.345   -41.910 23.146  1.00 57.23  ? 258 PHE A CE2 1 
ATOM   2015  C CZ  . PHE A 1 255 ? 8.700   -41.906 24.360  1.00 68.11  ? 258 PHE A CZ  1 
ATOM   2016  N N   . LYS A 1 256 ? 3.550   -41.098 19.162  1.00 66.77  ? 259 LYS A N   1 
ATOM   2017  C CA  . LYS A 1 256 ? 2.768   -40.453 18.116  1.00 59.13  ? 259 LYS A CA  1 
ATOM   2018  C C   . LYS A 1 256 ? 2.995   -38.955 18.244  1.00 56.91  ? 259 LYS A C   1 
ATOM   2019  O O   . LYS A 1 256 ? 3.017   -38.429 19.355  1.00 69.74  ? 259 LYS A O   1 
ATOM   2020  C CB  . LYS A 1 256 ? 1.283   -40.782 18.266  1.00 68.92  ? 259 LYS A CB  1 
ATOM   2021  C CG  . LYS A 1 256 ? 0.958   -42.270 18.211  1.00 79.12  ? 259 LYS A CG  1 
ATOM   2022  C CD  . LYS A 1 256 ? -0.545  -42.531 18.098  1.00 88.47  ? 259 LYS A CD  1 
ATOM   2023  C CE  . LYS A 1 256 ? -1.284  -42.245 19.396  1.00 98.68  ? 259 LYS A CE  1 
ATOM   2024  N NZ  . LYS A 1 256 ? -2.721  -42.630 19.304  1.00 102.36 ? 259 LYS A NZ  1 
ATOM   2025  N N   . ILE A 1 257 ? 3.172   -38.262 17.124  1.00 54.94  ? 260 ILE A N   1 
ATOM   2026  C CA  . ILE A 1 257 ? 3.473   -36.831 17.190  1.00 61.07  ? 260 ILE A CA  1 
ATOM   2027  C C   . ILE A 1 257 ? 2.777   -35.964 16.130  1.00 70.19  ? 260 ILE A C   1 
ATOM   2028  O O   . ILE A 1 257 ? 2.649   -36.355 14.962  1.00 78.81  ? 260 ILE A O   1 
ATOM   2029  C CB  . ILE A 1 257 ? 4.996   -36.577 17.153  1.00 55.80  ? 260 ILE A CB  1 
ATOM   2030  C CG1 . ILE A 1 257 ? 5.322   -35.188 17.701  1.00 53.61  ? 260 ILE A CG1 1 
ATOM   2031  C CG2 . ILE A 1 257 ? 5.537   -36.750 15.744  1.00 60.24  ? 260 ILE A CG2 1 
ATOM   2032  C CD1 . ILE A 1 257 ? 6.784   -34.992 17.981  1.00 51.42  ? 260 ILE A CD1 1 
ATOM   2033  N N   . SER A 1 258 ? 2.325   -34.787 16.570  1.00 70.42  ? 261 SER A N   1 
ATOM   2034  C CA  . SER A 1 258 ? 1.711   -33.782 15.704  1.00 72.47  ? 261 SER A CA  1 
ATOM   2035  C C   . SER A 1 258 ? 2.309   -32.411 16.010  1.00 73.85  ? 261 SER A C   1 
ATOM   2036  O O   . SER A 1 258 ? 2.492   -32.059 17.177  1.00 77.85  ? 261 SER A O   1 
ATOM   2037  C CB  . SER A 1 258 ? 0.202   -33.735 15.932  1.00 76.00  ? 261 SER A CB  1 
ATOM   2038  O OG  . SER A 1 258 ? -0.395  -34.994 15.688  1.00 87.91  ? 261 SER A OG  1 
ATOM   2039  N N   . LYS A 1 259 ? 2.612   -31.633 14.975  1.00 65.13  ? 262 LYS A N   1 
ATOM   2040  C CA  . LYS A 1 259 ? 3.237   -30.326 15.179  1.00 73.37  ? 262 LYS A CA  1 
ATOM   2041  C C   . LYS A 1 259 ? 2.462   -29.180 14.544  1.00 85.59  ? 262 LYS A C   1 
ATOM   2042  O O   . LYS A 1 259 ? 2.059   -29.260 13.384  1.00 87.47  ? 262 LYS A O   1 
ATOM   2043  C CB  . LYS A 1 259 ? 4.673   -30.312 14.649  1.00 79.94  ? 262 LYS A CB  1 
ATOM   2044  C CG  . LYS A 1 259 ? 5.741   -30.684 15.672  1.00 74.32  ? 262 LYS A CG  1 
ATOM   2045  C CD  . LYS A 1 259 ? 7.102   -30.119 15.274  1.00 78.38  ? 262 LYS A CD  1 
ATOM   2046  C CE  . LYS A 1 259 ? 7.330   -30.218 13.768  1.00 100.87 ? 262 LYS A CE  1 
ATOM   2047  N NZ  . LYS A 1 259 ? 7.160   -31.601 13.242  1.00 113.05 ? 262 LYS A NZ  1 
ATOM   2048  N N   . ARG A 1 260 ? 2.279   -28.110 15.313  1.00 109.07 ? 263 ARG A N   1 
ATOM   2049  C CA  . ARG A 1 260 ? 1.600   -26.912 14.836  1.00 130.05 ? 263 ARG A CA  1 
ATOM   2050  C C   . ARG A 1 260 ? 2.629   -25.893 14.371  1.00 126.64 ? 263 ARG A C   1 
ATOM   2051  O O   . ARG A 1 260 ? 2.287   -24.766 14.014  1.00 135.53 ? 263 ARG A O   1 
ATOM   2052  C CB  . ARG A 1 260 ? 0.781   -26.292 15.966  1.00 143.81 ? 263 ARG A CB  1 
ATOM   2053  C CG  . ARG A 1 260 ? 1.620   -25.466 16.939  1.00 151.96 ? 263 ARG A CG  1 
ATOM   2054  C CD  . ARG A 1 260 ? 0.758   -24.753 17.968  1.00 163.40 ? 263 ARG A CD  1 
ATOM   2055  N NE  . ARG A 1 260 ? 0.251   -25.670 18.984  1.00 174.64 ? 263 ARG A NE  1 
ATOM   2056  C CZ  . ARG A 1 260 ? 0.784   -25.816 20.193  1.00 181.12 ? 263 ARG A CZ  1 
ATOM   2057  N NH1 . ARG A 1 260 ? 1.843   -25.097 20.545  1.00 179.91 ? 263 ARG A NH1 1 
ATOM   2058  N NH2 . ARG A 1 260 ? 0.254   -26.677 21.052  1.00 186.96 ? 263 ARG A NH2 1 
ATOM   2059  N N   . GLY A 1 261 A 3.894   -26.298 14.378  1.00 91.33  ? 263 GLY A N   1 
ATOM   2060  C CA  . GLY A 1 261 A 4.999   -25.372 14.213  1.00 84.62  ? 263 GLY A CA  1 
ATOM   2061  C C   . GLY A 1 261 A 5.807   -25.412 15.493  1.00 78.76  ? 263 GLY A C   1 
ATOM   2062  O O   . GLY A 1 261 A 5.268   -25.732 16.551  1.00 83.84  ? 263 GLY A O   1 
ATOM   2063  N N   . SER A 1 262 ? 7.093   -25.093 15.417  1.00 101.15 ? 264 SER A N   1 
ATOM   2064  C CA  . SER A 1 262 ? 7.973   -25.335 16.554  1.00 93.48  ? 264 SER A CA  1 
ATOM   2065  C C   . SER A 1 262 ? 8.211   -24.123 17.449  1.00 92.86  ? 264 SER A C   1 
ATOM   2066  O O   . SER A 1 262 ? 7.830   -23.001 17.121  1.00 105.95 ? 264 SER A O   1 
ATOM   2067  C CB  . SER A 1 262 ? 9.299   -25.942 16.089  1.00 99.37  ? 264 SER A CB  1 
ATOM   2068  O OG  . SER A 1 262 ? 9.097   -27.241 15.547  1.00 105.14 ? 264 SER A OG  1 
ATOM   2069  N N   . SER A 1 263 ? 8.841   -24.375 18.590  1.00 50.06  ? 265 SER A N   1 
ATOM   2070  C CA  . SER A 1 263 ? 9.092   -23.359 19.602  1.00 44.14  ? 265 SER A CA  1 
ATOM   2071  C C   . SER A 1 263 ? 10.528  -23.473 20.103  1.00 47.58  ? 265 SER A C   1 
ATOM   2072  O O   . SER A 1 263 ? 11.471  -23.387 19.320  1.00 49.72  ? 265 SER A O   1 
ATOM   2073  C CB  . SER A 1 263 ? 8.115   -23.532 20.762  1.00 50.66  ? 265 SER A CB  1 
ATOM   2074  O OG  . SER A 1 263 ? 8.537   -22.813 21.904  1.00 60.97  ? 265 SER A OG  1 
ATOM   2075  N N   . GLY A 1 264 ? 10.695  -23.681 21.404  1.00 41.91  ? 266 GLY A N   1 
ATOM   2076  C CA  . GLY A 1 264 ? 12.021  -23.769 21.986  1.00 47.75  ? 266 GLY A CA  1 
ATOM   2077  C C   . GLY A 1 264 ? 12.042  -24.138 23.457  1.00 56.31  ? 266 GLY A C   1 
ATOM   2078  O O   . GLY A 1 264 ? 11.064  -23.948 24.176  1.00 67.21  ? 266 GLY A O   1 
ATOM   2079  N N   . ILE A 1 265 ? 13.173  -24.676 23.897  1.00 44.15  ? 267 ILE A N   1 
ATOM   2080  C CA  . ILE A 1 265 ? 13.377  -25.064 25.283  1.00 40.20  ? 267 ILE A CA  1 
ATOM   2081  C C   . ILE A 1 265 ? 13.836  -23.851 26.077  1.00 43.88  ? 267 ILE A C   1 
ATOM   2082  O O   . ILE A 1 265 ? 14.662  -23.083 25.601  1.00 45.71  ? 267 ILE A O   1 
ATOM   2083  C CB  . ILE A 1 265 ? 14.467  -26.159 25.393  1.00 44.74  ? 267 ILE A CB  1 
ATOM   2084  C CG1 . ILE A 1 265 ? 13.915  -27.536 25.013  1.00 41.43  ? 267 ILE A CG1 1 
ATOM   2085  C CG2 . ILE A 1 265 ? 15.055  -26.204 26.787  1.00 44.90  ? 267 ILE A CG2 1 
ATOM   2086  C CD1 . ILE A 1 265 ? 13.833  -27.785 23.520  1.00 34.46  ? 267 ILE A CD1 1 
ATOM   2087  N N   . MET A 1 266 ? 13.310  -23.673 27.285  1.00 42.98  ? 268 MET A N   1 
ATOM   2088  C CA  . MET A 1 266 ? 13.775  -22.595 28.146  1.00 41.36  ? 268 MET A CA  1 
ATOM   2089  C C   . MET A 1 266 ? 14.508  -23.097 29.379  1.00 45.25  ? 268 MET A C   1 
ATOM   2090  O O   . MET A 1 266 ? 13.901  -23.676 30.272  1.00 60.50  ? 268 MET A O   1 
ATOM   2091  C CB  . MET A 1 266 ? 12.612  -21.723 28.597  1.00 52.46  ? 268 MET A CB  1 
ATOM   2092  C CG  . MET A 1 266 ? 13.052  -20.559 29.476  1.00 58.60  ? 268 MET A CG  1 
ATOM   2093  S SD  . MET A 1 266 ? 11.672  -19.537 30.000  1.00 74.90  ? 268 MET A SD  1 
ATOM   2094  C CE  . MET A 1 266 ? 10.818  -19.337 28.441  1.00 76.32  ? 268 MET A CE  1 
ATOM   2095  N N   . LYS A 1 267 ? 15.808  -22.853 29.437  1.00 71.47  ? 269 LYS A N   1 
ATOM   2096  C CA  . LYS A 1 267 ? 16.584  -23.191 30.618  1.00 58.98  ? 269 LYS A CA  1 
ATOM   2097  C C   . LYS A 1 267 ? 16.081  -22.415 31.836  1.00 74.39  ? 269 LYS A C   1 
ATOM   2098  O O   . LYS A 1 267 ? 15.931  -21.198 31.780  1.00 79.11  ? 269 LYS A O   1 
ATOM   2099  C CB  . LYS A 1 267 ? 18.066  -22.896 30.380  1.00 40.40  ? 269 LYS A CB  1 
ATOM   2100  C CG  . LYS A 1 267 ? 18.691  -23.660 29.214  1.00 44.13  ? 269 LYS A CG  1 
ATOM   2101  C CD  . LYS A 1 267 ? 18.649  -25.157 29.458  1.00 52.67  ? 269 LYS A CD  1 
ATOM   2102  C CE  . LYS A 1 267 ? 19.487  -25.918 28.448  1.00 52.90  ? 269 LYS A CE  1 
ATOM   2103  N NZ  . LYS A 1 267 ? 19.579  -27.364 28.802  1.00 52.30  ? 269 LYS A NZ  1 
ATOM   2104  N N   . THR A 1 268 ? 15.819  -23.130 32.929  1.00 48.97  ? 270 THR A N   1 
ATOM   2105  C CA  . THR A 1 268 ? 15.341  -22.523 34.175  1.00 60.06  ? 270 THR A CA  1 
ATOM   2106  C C   . THR A 1 268 ? 15.278  -23.542 35.315  1.00 70.24  ? 270 THR A C   1 
ATOM   2107  O O   . THR A 1 268 ? 15.169  -24.742 35.075  1.00 74.83  ? 270 THR A O   1 
ATOM   2108  C CB  . THR A 1 268 ? 13.945  -21.908 34.007  1.00 75.04  ? 270 THR A CB  1 
ATOM   2109  O OG1 . THR A 1 268 ? 13.484  -21.429 35.273  1.00 88.80  ? 270 THR A OG1 1 
ATOM   2110  C CG2 . THR A 1 268 ? 12.969  -22.946 33.490  1.00 73.18  ? 270 THR A CG2 1 
ATOM   2111  N N   . GLU A 1 269 ? 15.336  -23.057 36.551  1.00 97.64  ? 271 GLU A N   1 
ATOM   2112  C CA  . GLU A 1 269 ? 15.258  -23.924 37.723  1.00 99.98  ? 271 GLU A CA  1 
ATOM   2113  C C   . GLU A 1 269 ? 13.926  -23.744 38.445  1.00 113.18 ? 271 GLU A C   1 
ATOM   2114  O O   . GLU A 1 269 ? 13.788  -24.117 39.608  1.00 112.70 ? 271 GLU A O   1 
ATOM   2115  C CB  . GLU A 1 269 ? 16.396  -23.616 38.695  1.00 85.62  ? 271 GLU A CB  1 
ATOM   2116  C CG  . GLU A 1 269 ? 17.699  -23.224 38.031  1.00 74.25  ? 271 GLU A CG  1 
ATOM   2117  C CD  . GLU A 1 269 ? 18.504  -24.417 37.564  1.00 73.13  ? 271 GLU A CD  1 
ATOM   2118  O OE1 . GLU A 1 269 ? 18.787  -25.307 38.399  1.00 80.26  ? 271 GLU A OE1 1 
ATOM   2119  O OE2 . GLU A 1 269 ? 18.858  -24.464 36.363  1.00 61.15  ? 271 GLU A OE2 1 
ATOM   2120  N N   . GLY A 1 270 ? 12.948  -23.176 37.752  1.00 55.32  ? 272 GLY A N   1 
ATOM   2121  C CA  . GLY A 1 270 ? 11.674  -22.844 38.359  1.00 62.14  ? 272 GLY A CA  1 
ATOM   2122  C C   . GLY A 1 270 ? 10.571  -23.790 37.947  1.00 57.90  ? 272 GLY A C   1 
ATOM   2123  O O   . GLY A 1 270 ? 10.844  -24.821 37.337  1.00 55.68  ? 272 GLY A O   1 
ATOM   2124  N N   . THR A 1 271 ? 9.328   -23.443 38.275  1.00 78.13  ? 273 THR A N   1 
ATOM   2125  C CA  . THR A 1 271 ? 8.187   -24.319 38.007  1.00 82.08  ? 273 THR A CA  1 
ATOM   2126  C C   . THR A 1 271 ? 6.977   -23.562 37.468  1.00 78.07  ? 273 THR A C   1 
ATOM   2127  O O   . THR A 1 271 ? 6.840   -22.356 37.676  1.00 81.46  ? 273 THR A O   1 
ATOM   2128  C CB  . THR A 1 271 ? 7.742   -25.045 39.276  1.00 95.44  ? 273 THR A CB  1 
ATOM   2129  O OG1 . THR A 1 271 ? 6.970   -24.153 40.088  1.00 104.92 ? 273 THR A OG1 1 
ATOM   2130  C CG2 . THR A 1 271 ? 8.950   -25.530 40.065  1.00 98.99  ? 273 THR A CG2 1 
ATOM   2131  N N   . LEU A 1 272 ? 6.090   -24.283 36.791  1.00 54.63  ? 274 LEU A N   1 
ATOM   2132  C CA  . LEU A 1 272 ? 4.901   -23.677 36.206  1.00 54.21  ? 274 LEU A CA  1 
ATOM   2133  C C   . LEU A 1 272 ? 3.939   -23.255 37.309  1.00 69.99  ? 274 LEU A C   1 
ATOM   2134  O O   . LEU A 1 272 ? 3.686   -24.019 38.243  1.00 80.37  ? 274 LEU A O   1 
ATOM   2135  C CB  . LEU A 1 272 ? 4.219   -24.661 35.250  1.00 52.72  ? 274 LEU A CB  1 
ATOM   2136  C CG  . LEU A 1 272 ? 3.017   -24.219 34.403  1.00 50.51  ? 274 LEU A CG  1 
ATOM   2137  C CD1 . LEU A 1 272 ? 2.662   -25.270 33.356  1.00 33.81  ? 274 LEU A CD1 1 
ATOM   2138  C CD2 . LEU A 1 272 ? 1.801   -23.936 35.263  1.00 66.18  ? 274 LEU A CD2 1 
ATOM   2139  N N   . GLU A 1 273 ? 3.421   -22.031 37.207  1.00 59.15  ? 275 GLU A N   1 
ATOM   2140  C CA  . GLU A 1 273 ? 2.360   -21.557 38.097  1.00 70.25  ? 275 GLU A CA  1 
ATOM   2141  C C   . GLU A 1 273 ? 1.086   -21.338 37.290  1.00 71.18  ? 275 GLU A C   1 
ATOM   2142  O O   . GLU A 1 273 ? 1.104   -21.433 36.066  1.00 62.30  ? 275 GLU A O   1 
ATOM   2143  C CB  . GLU A 1 273 ? 2.781   -20.276 38.813  1.00 72.02  ? 275 GLU A CB  1 
ATOM   2144  C CG  . GLU A 1 273 ? 4.088   -20.423 39.580  1.00 73.03  ? 275 GLU A CG  1 
ATOM   2145  C CD  . GLU A 1 273 ? 4.327   -19.289 40.555  1.00 80.22  ? 275 GLU A CD  1 
ATOM   2146  O OE1 . GLU A 1 273 ? 3.338   -18.639 40.956  1.00 91.36  ? 275 GLU A OE1 1 
ATOM   2147  O OE2 . GLU A 1 273 ? 5.499   -19.045 40.922  1.00 72.49  ? 275 GLU A OE2 1 
ATOM   2148  N N   . ASN A 1 274 ? -0.031  -21.068 37.950  1.00 86.58  ? 276 ASN A N   1 
ATOM   2149  C CA  . ASN A 1 274 ? -1.259  -20.919 37.185  1.00 93.90  ? 276 ASN A CA  1 
ATOM   2150  C C   . ASN A 1 274 ? -1.458  -19.497 36.687  1.00 92.45  ? 276 ASN A C   1 
ATOM   2151  O O   . ASN A 1 274 ? -2.217  -18.722 37.271  1.00 91.55  ? 276 ASN A O   1 
ATOM   2152  C CB  . ASN A 1 274 ? -2.486  -21.398 37.955  1.00 109.83 ? 276 ASN A CB  1 
ATOM   2153  C CG  . ASN A 1 274 ? -3.697  -21.570 37.054  1.00 120.33 ? 276 ASN A CG  1 
ATOM   2154  O OD1 . ASN A 1 274 ? -3.561  -21.769 35.846  1.00 116.56 ? 276 ASN A OD1 1 
ATOM   2155  N ND2 . ASN A 1 274 ? -4.886  -21.485 37.635  1.00 131.83 ? 276 ASN A ND2 1 
ATOM   2156  N N   . CYS A 1 275 ? -0.762  -19.166 35.602  1.00 105.58 ? 277 CYS A N   1 
ATOM   2157  C CA  . CYS A 1 275 ? -0.872  -17.856 34.972  1.00 102.36 ? 277 CYS A CA  1 
ATOM   2158  C C   . CYS A 1 275 ? -0.684  -17.957 33.460  1.00 95.00  ? 277 CYS A C   1 
ATOM   2159  O O   . CYS A 1 275 ? -0.155  -18.941 32.953  1.00 91.99  ? 277 CYS A O   1 
ATOM   2160  C CB  . CYS A 1 275 ? 0.131   -16.878 35.582  1.00 98.60  ? 277 CYS A CB  1 
ATOM   2161  S SG  . CYS A 1 275 ? 1.783   -17.556 35.825  1.00 99.86  ? 277 CYS A SG  1 
ATOM   2162  N N   . GLU A 1 276 ? -1.132  -16.934 32.747  1.00 78.00  ? 278 GLU A N   1 
ATOM   2163  C CA  . GLU A 1 276 ? -1.117  -16.934 31.292  1.00 73.57  ? 278 GLU A CA  1 
ATOM   2164  C C   . GLU A 1 276 ? -0.148  -15.860 30.798  1.00 72.70  ? 278 GLU A C   1 
ATOM   2165  O O   . GLU A 1 276 ? 0.279   -15.009 31.578  1.00 76.98  ? 278 GLU A O   1 
ATOM   2166  C CB  . GLU A 1 276 ? -2.536  -16.674 30.783  1.00 78.50  ? 278 GLU A CB  1 
ATOM   2167  C CG  . GLU A 1 276 ? -2.641  -16.180 29.357  1.00 82.96  ? 278 GLU A CG  1 
ATOM   2168  C CD  . GLU A 1 276 ? -2.538  -17.296 28.353  1.00 89.06  ? 278 GLU A CD  1 
ATOM   2169  O OE1 . GLU A 1 276 ? -2.182  -18.421 28.759  1.00 93.95  ? 278 GLU A OE1 1 
ATOM   2170  O OE2 . GLU A 1 276 ? -2.817  -17.050 27.159  1.00 89.30  ? 278 GLU A OE2 1 
ATOM   2171  N N   . THR A 1 277 ? 0.215   -15.913 29.517  1.00 95.80  ? 279 THR A N   1 
ATOM   2172  C CA  . THR A 1 277 ? 1.047   -14.874 28.898  1.00 85.20  ? 279 THR A CA  1 
ATOM   2173  C C   . THR A 1 277 ? 1.290   -15.118 27.412  1.00 73.31  ? 279 THR A C   1 
ATOM   2174  O O   . THR A 1 277 ? 1.236   -16.253 26.939  1.00 69.94  ? 279 THR A O   1 
ATOM   2175  C CB  . THR A 1 277 ? 2.416   -14.732 29.590  1.00 84.07  ? 279 THR A CB  1 
ATOM   2176  O OG1 . THR A 1 277 ? 3.190   -13.730 28.919  1.00 84.40  ? 279 THR A OG1 1 
ATOM   2177  C CG2 . THR A 1 277 ? 3.166   -16.046 29.549  1.00 76.70  ? 279 THR A CG2 1 
ATOM   2178  N N   . LYS A 1 278 ? 1.561   -14.038 26.684  1.00 75.44  ? 280 LYS A N   1 
ATOM   2179  C CA  . LYS A 1 278 ? 1.870   -14.114 25.263  1.00 74.96  ? 280 LYS A CA  1 
ATOM   2180  C C   . LYS A 1 278 ? 3.376   -14.174 25.074  1.00 70.99  ? 280 LYS A C   1 
ATOM   2181  O O   . LYS A 1 278 ? 3.868   -14.463 23.986  1.00 72.89  ? 280 LYS A O   1 
ATOM   2182  C CB  . LYS A 1 278 ? 1.325   -12.889 24.530  1.00 79.78  ? 280 LYS A CB  1 
ATOM   2183  C CG  . LYS A 1 278 ? 0.110   -13.144 23.658  1.00 91.03  ? 280 LYS A CG  1 
ATOM   2184  C CD  . LYS A 1 278 ? -0.042  -12.034 22.613  1.00 97.68  ? 280 LYS A CD  1 
ATOM   2185  C CE  . LYS A 1 278 ? -0.222  -10.658 23.251  1.00 101.47 ? 280 LYS A CE  1 
ATOM   2186  N NZ  . LYS A 1 278 ? -1.525  -10.522 23.963  1.00 103.12 ? 280 LYS A NZ  1 
ATOM   2187  N N   . CYS A 1 279 ? 4.103   -13.901 26.148  1.00 65.46  ? 281 CYS A N   1 
ATOM   2188  C CA  . CYS A 1 279 ? 5.545   -13.762 26.071  1.00 57.25  ? 281 CYS A CA  1 
ATOM   2189  C C   . CYS A 1 279 ? 6.183   -14.169 27.389  1.00 57.82  ? 281 CYS A C   1 
ATOM   2190  O O   . CYS A 1 279 ? 5.924   -13.568 28.432  1.00 55.16  ? 281 CYS A O   1 
ATOM   2191  C CB  . CYS A 1 279 ? 5.903   -12.315 25.725  1.00 54.04  ? 281 CYS A CB  1 
ATOM   2192  S SG  . CYS A 1 279 ? 7.635   -11.859 25.959  1.00 58.65  ? 281 CYS A SG  1 
ATOM   2193  N N   . GLN A 1 280 ? 7.016   -15.200 27.348  1.00 46.44  ? 282 GLN A N   1 
ATOM   2194  C CA  . GLN A 1 280 ? 7.616   -15.704 28.574  1.00 44.02  ? 282 GLN A CA  1 
ATOM   2195  C C   . GLN A 1 280 ? 9.115   -15.467 28.576  1.00 46.86  ? 282 GLN A C   1 
ATOM   2196  O O   . GLN A 1 280 ? 9.761   -15.530 27.536  1.00 47.60  ? 282 GLN A O   1 
ATOM   2197  C CB  . GLN A 1 280 ? 7.287   -17.195 28.769  1.00 40.57  ? 282 GLN A CB  1 
ATOM   2198  C CG  . GLN A 1 280 ? 7.871   -17.819 30.034  1.00 45.93  ? 282 GLN A CG  1 
ATOM   2199  C CD  . GLN A 1 280 ? 7.248   -17.272 31.305  1.00 66.59  ? 282 GLN A CD  1 
ATOM   2200  O OE1 . GLN A 1 280 ? 6.027   -17.283 31.463  1.00 79.69  ? 282 GLN A OE1 1 
ATOM   2201  N NE2 . GLN A 1 280 ? 8.087   -16.790 32.220  1.00 69.80  ? 282 GLN A NE2 1 
ATOM   2202  N N   . THR A 1 281 ? 9.659   -15.186 29.752  1.00 47.38  ? 283 THR A N   1 
ATOM   2203  C CA  . THR A 1 281 ? 11.090  -14.977 29.914  1.00 52.46  ? 283 THR A CA  1 
ATOM   2204  C C   . THR A 1 281 ? 11.572  -15.847 31.067  1.00 55.47  ? 283 THR A C   1 
ATOM   2205  O O   . THR A 1 281 ? 10.779  -16.236 31.919  1.00 55.64  ? 283 THR A O   1 
ATOM   2206  C CB  . THR A 1 281 ? 11.406  -13.490 30.225  1.00 54.11  ? 283 THR A CB  1 
ATOM   2207  O OG1 . THR A 1 281 ? 11.231  -13.234 31.628  1.00 62.56  ? 283 THR A OG1 1 
ATOM   2208  C CG2 . THR A 1 281 ? 10.490  -12.571 29.426  1.00 50.59  ? 283 THR A CG2 1 
ATOM   2209  N N   . PRO A 1 282 ? 12.875  -16.151 31.103  1.00 96.94  ? 284 PRO A N   1 
ATOM   2210  C CA  . PRO A 1 282 ? 13.434  -16.977 32.174  1.00 95.91  ? 284 PRO A CA  1 
ATOM   2211  C C   . PRO A 1 282 ? 13.198  -16.377 33.556  1.00 98.37  ? 284 PRO A C   1 
ATOM   2212  O O   . PRO A 1 282 ? 13.318  -17.093 34.551  1.00 106.54 ? 284 PRO A O   1 
ATOM   2213  C CB  . PRO A 1 282 ? 14.932  -16.984 31.858  1.00 82.34  ? 284 PRO A CB  1 
ATOM   2214  C CG  . PRO A 1 282 ? 15.005  -16.742 30.400  1.00 80.09  ? 284 PRO A CG  1 
ATOM   2215  C CD  . PRO A 1 282 ? 13.895  -15.776 30.113  1.00 92.17  ? 284 PRO A CD  1 
ATOM   2216  N N   . LEU A 1 283 ? 12.869  -15.088 33.612  1.00 78.98  ? 285 LEU A N   1 
ATOM   2217  C CA  . LEU A 1 283 ? 12.663  -14.399 34.882  1.00 78.44  ? 285 LEU A CA  1 
ATOM   2218  C C   . LEU A 1 283 ? 11.193  -14.226 35.220  1.00 97.27  ? 285 LEU A C   1 
ATOM   2219  O O   . LEU A 1 283 ? 10.834  -14.070 36.385  1.00 106.34 ? 285 LEU A O   1 
ATOM   2220  C CB  . LEU A 1 283 ? 13.326  -13.025 34.866  1.00 65.74  ? 285 LEU A CB  1 
ATOM   2221  C CG  . LEU A 1 283 ? 14.813  -12.994 34.535  1.00 57.11  ? 285 LEU A CG  1 
ATOM   2222  C CD1 . LEU A 1 283 ? 15.378  -11.598 34.785  1.00 52.81  ? 285 LEU A CD1 1 
ATOM   2223  C CD2 . LEU A 1 283 ? 15.558  -14.036 35.346  1.00 49.63  ? 285 LEU A CD2 1 
ATOM   2224  N N   . GLY A 1 284 ? 10.345  -14.237 34.200  1.00 70.88  ? 286 GLY A N   1 
ATOM   2225  C CA  . GLY A 1 284 ? 8.924   -14.056 34.414  1.00 70.55  ? 286 GLY A CA  1 
ATOM   2226  C C   . GLY A 1 284 ? 8.195   -13.793 33.117  1.00 67.42  ? 286 GLY A C   1 
ATOM   2227  O O   . GLY A 1 284 ? 8.818   -13.719 32.056  1.00 62.82  ? 286 GLY A O   1 
ATOM   2228  N N   . ALA A 1 285 ? 6.874   -13.651 33.197  1.00 48.75  ? 287 ALA A N   1 
ATOM   2229  C CA  . ALA A 1 285 ? 6.066   -13.407 32.006  1.00 41.84  ? 287 ALA A CA  1 
ATOM   2230  C C   . ALA A 1 285 ? 5.898   -11.907 31.725  1.00 54.45  ? 287 ALA A C   1 
ATOM   2231  O O   . ALA A 1 285 ? 6.135   -11.063 32.598  1.00 56.54  ? 287 ALA A O   1 
ATOM   2232  C CB  . ALA A 1 285 ? 4.723   -14.083 32.132  1.00 31.21  ? 287 ALA A CB  1 
ATOM   2233  N N   . ILE A 1 286 ? 5.492   -11.587 30.500  1.00 72.96  ? 288 ILE A N   1 
ATOM   2234  C CA  . ILE A 1 286 ? 5.305   -10.199 30.098  1.00 68.79  ? 288 ILE A CA  1 
ATOM   2235  C C   . ILE A 1 286 ? 3.905   -9.942  29.552  1.00 72.60  ? 288 ILE A C   1 
ATOM   2236  O O   . ILE A 1 286 ? 3.409   -10.673 28.694  1.00 70.08  ? 288 ILE A O   1 
ATOM   2237  C CB  . ILE A 1 286 ? 6.362   -9.747  29.064  1.00 62.65  ? 288 ILE A CB  1 
ATOM   2238  C CG1 . ILE A 1 286 ? 7.733   -9.620  29.731  1.00 56.58  ? 288 ILE A CG1 1 
ATOM   2239  C CG2 . ILE A 1 286 ? 5.968   -8.422  28.445  1.00 67.86  ? 288 ILE A CG2 1 
ATOM   2240  C CD1 . ILE A 1 286 ? 8.747   -8.865  28.903  1.00 44.34  ? 288 ILE A CD1 1 
ATOM   2241  N N   . ASN A 1 287 ? 3.269   -8.902  30.077  1.00 70.72  ? 289 ASN A N   1 
ATOM   2242  C CA  . ASN A 1 287 ? 1.964   -8.475  29.609  1.00 76.15  ? 289 ASN A CA  1 
ATOM   2243  C C   . ASN A 1 287 ? 2.044   -6.995  29.300  1.00 74.47  ? 289 ASN A C   1 
ATOM   2244  O O   . ASN A 1 287 ? 1.957   -6.166  30.205  1.00 79.38  ? 289 ASN A O   1 
ATOM   2245  C CB  . ASN A 1 287 ? 0.909   -8.718  30.685  1.00 85.25  ? 289 ASN A CB  1 
ATOM   2246  C CG  . ASN A 1 287 ? -0.496  -8.432  30.196  1.00 92.73  ? 289 ASN A CG  1 
ATOM   2247  O OD1 . ASN A 1 287 ? -1.453  -8.448  30.975  1.00 91.47  ? 289 ASN A OD1 1 
ATOM   2248  N ND2 . ASN A 1 287 ? -0.630  -8.177  28.897  1.00 98.66  ? 289 ASN A ND2 1 
ATOM   2249  N N   . THR A 1 288 ? 2.220   -6.655  28.029  1.00 82.27  ? 290 THR A N   1 
ATOM   2250  C CA  . THR A 1 288 ? 2.465   -5.263  27.683  1.00 81.25  ? 290 THR A CA  1 
ATOM   2251  C C   . THR A 1 288 ? 2.206   -4.956  26.212  1.00 82.39  ? 290 THR A C   1 
ATOM   2252  O O   . THR A 1 288 ? 2.375   -5.821  25.347  1.00 79.82  ? 290 THR A O   1 
ATOM   2253  C CB  . THR A 1 288 ? 3.908   -4.853  28.055  1.00 74.87  ? 290 THR A CB  1 
ATOM   2254  O OG1 . THR A 1 288 ? 3.968   -3.442  28.300  1.00 76.53  ? 290 THR A OG1 1 
ATOM   2255  C CG2 . THR A 1 288 ? 4.882   -5.235  26.950  1.00 69.65  ? 290 THR A CG2 1 
ATOM   2256  N N   . THR A 1 289 ? 1.786   -3.718  25.945  1.00 87.74  ? 291 THR A N   1 
ATOM   2257  C CA  . THR A 1 289 ? 1.576   -3.241  24.582  1.00 85.47  ? 291 THR A CA  1 
ATOM   2258  C C   . THR A 1 289 ? 2.785   -2.443  24.139  1.00 74.61  ? 291 THR A C   1 
ATOM   2259  O O   . THR A 1 289 ? 2.954   -2.164  22.952  1.00 75.59  ? 291 THR A O   1 
ATOM   2260  C CB  . THR A 1 289 ? 0.349   -2.326  24.469  1.00 94.67  ? 291 THR A CB  1 
ATOM   2261  O OG1 . THR A 1 289 ? -0.692  -2.807  25.322  1.00 102.67 ? 291 THR A OG1 1 
ATOM   2262  C CG2 . THR A 1 289 ? -0.152  -2.276  23.028  1.00 92.58  ? 291 THR A CG2 1 
ATOM   2263  N N   . LEU A 1 290 ? 3.617   -2.069  25.107  1.00 77.78  ? 292 LEU A N   1 
ATOM   2264  C CA  . LEU A 1 290 ? 4.848   -1.339  24.826  1.00 70.70  ? 292 LEU A CA  1 
ATOM   2265  C C   . LEU A 1 290 ? 5.634   -1.997  23.699  1.00 69.41  ? 292 LEU A C   1 
ATOM   2266  O O   . LEU A 1 290 ? 5.560   -3.209  23.499  1.00 75.11  ? 292 LEU A O   1 
ATOM   2267  C CB  . LEU A 1 290 ? 5.716   -1.247  26.081  1.00 64.64  ? 292 LEU A CB  1 
ATOM   2268  C CG  . LEU A 1 290 ? 5.039   -0.665  27.324  1.00 65.13  ? 292 LEU A CG  1 
ATOM   2269  C CD1 . LEU A 1 290 ? 6.085   -0.266  28.350  1.00 65.21  ? 292 LEU A CD1 1 
ATOM   2270  C CD2 . LEU A 1 290 ? 4.178   0.523   26.959  1.00 65.19  ? 292 LEU A CD2 1 
ATOM   2271  N N   . PRO A 1 291 ? 6.380   -1.191  22.946  1.00 71.06  ? 293 PRO A N   1 
ATOM   2272  C CA  . PRO A 1 291 ? 7.152   -1.674  21.799  1.00 63.11  ? 293 PRO A CA  1 
ATOM   2273  C C   . PRO A 1 291 ? 8.460   -2.364  22.187  1.00 68.09  ? 293 PRO A C   1 
ATOM   2274  O O   . PRO A 1 291 ? 8.833   -3.345  21.545  1.00 66.74  ? 293 PRO A O   1 
ATOM   2275  C CB  . PRO A 1 291 ? 7.446   -0.391  21.014  1.00 60.81  ? 293 PRO A CB  1 
ATOM   2276  C CG  . PRO A 1 291 ? 6.492   0.636   21.557  1.00 65.75  ? 293 PRO A CG  1 
ATOM   2277  C CD  . PRO A 1 291 ? 6.308   0.275   22.986  1.00 70.32  ? 293 PRO A CD  1 
ATOM   2278  N N   . PHE A 1 292 ? 9.138   -1.868  23.219  1.00 67.87  ? 294 PHE A N   1 
ATOM   2279  C CA  . PHE A 1 292 ? 10.441  -2.404  23.609  1.00 67.12  ? 294 PHE A CA  1 
ATOM   2280  C C   . PHE A 1 292 ? 10.456  -2.901  25.052  1.00 71.03  ? 294 PHE A C   1 
ATOM   2281  O O   . PHE A 1 292 ? 9.570   -2.567  25.841  1.00 79.74  ? 294 PHE A O   1 
ATOM   2282  C CB  . PHE A 1 292 ? 11.516  -1.333  23.434  1.00 66.41  ? 294 PHE A CB  1 
ATOM   2283  C CG  . PHE A 1 292 ? 11.468  -0.637  22.106  1.00 62.36  ? 294 PHE A CG  1 
ATOM   2284  C CD1 . PHE A 1 292 ? 12.305  -1.026  21.075  1.00 60.10  ? 294 PHE A CD1 1 
ATOM   2285  C CD2 . PHE A 1 292 ? 10.591  0.406   21.891  1.00 58.73  ? 294 PHE A CD2 1 
ATOM   2286  C CE1 . PHE A 1 292 ? 12.262  -0.387  19.855  1.00 56.73  ? 294 PHE A CE1 1 
ATOM   2287  C CE2 . PHE A 1 292 ? 10.547  1.050   20.674  1.00 55.20  ? 294 PHE A CE2 1 
ATOM   2288  C CZ  . PHE A 1 292 ? 11.381  0.652   19.654  1.00 55.04  ? 294 PHE A CZ  1 
ATOM   2289  N N   . HIS A 1 293 ? 11.471  -3.692  25.397  1.00 57.90  ? 295 HIS A N   1 
ATOM   2290  C CA  . HIS A 1 293 ? 11.650  -4.149  26.778  1.00 62.36  ? 295 HIS A CA  1 
ATOM   2291  C C   . HIS A 1 293 ? 13.102  -4.525  27.093  1.00 59.07  ? 295 HIS A C   1 
ATOM   2292  O O   . HIS A 1 293 ? 13.923  -4.672  26.192  1.00 60.31  ? 295 HIS A O   1 
ATOM   2293  C CB  . HIS A 1 293 ? 10.727  -5.328  27.081  1.00 65.13  ? 295 HIS A CB  1 
ATOM   2294  C CG  . HIS A 1 293 ? 11.271  -6.647  26.638  1.00 61.51  ? 295 HIS A CG  1 
ATOM   2295  N ND1 . HIS A 1 293 ? 12.213  -7.343  27.366  1.00 62.39  ? 295 HIS A ND1 1 
ATOM   2296  C CD2 . HIS A 1 293 ? 11.010  -7.397  25.541  1.00 56.12  ? 295 HIS A CD2 1 
ATOM   2297  C CE1 . HIS A 1 293 ? 12.509  -8.465  26.735  1.00 56.27  ? 295 HIS A CE1 1 
ATOM   2298  N NE2 . HIS A 1 293 ? 11.794  -8.522  25.625  1.00 52.81  ? 295 HIS A NE2 1 
ATOM   2299  N N   . ASN A 1 294 ? 13.415  -4.673  28.376  1.00 62.59  ? 296 ASN A N   1 
ATOM   2300  C CA  . ASN A 1 294 ? 14.755  -5.082  28.781  1.00 49.76  ? 296 ASN A CA  1 
ATOM   2301  C C   . ASN A 1 294 ? 14.730  -6.193  29.824  1.00 55.92  ? 296 ASN A C   1 
ATOM   2302  O O   . ASN A 1 294 ? 15.746  -6.470  30.469  1.00 49.33  ? 296 ASN A O   1 
ATOM   2303  C CB  . ASN A 1 294 ? 15.555  -3.901  29.315  1.00 34.57  ? 296 ASN A CB  1 
ATOM   2304  C CG  . ASN A 1 294 ? 14.867  -3.218  30.486  1.00 51.84  ? 296 ASN A CG  1 
ATOM   2305  O OD1 . ASN A 1 294 ? 13.955  -3.779  31.093  1.00 70.18  ? 296 ASN A OD1 1 
ATOM   2306  N ND2 . ASN A 1 294 ? 15.295  -1.996  30.802  1.00 42.41  ? 296 ASN A ND2 1 
ATOM   2307  N N   . VAL A 1 295 ? 13.569  -6.826  29.980  1.00 58.47  ? 297 VAL A N   1 
ATOM   2308  C CA  . VAL A 1 295 ? 13.389  -7.889  30.962  1.00 56.70  ? 297 VAL A CA  1 
ATOM   2309  C C   . VAL A 1 295 ? 14.483  -8.946  30.848  1.00 54.45  ? 297 VAL A C   1 
ATOM   2310  O O   . VAL A 1 295 ? 15.223  -9.198  31.802  1.00 52.78  ? 297 VAL A O   1 
ATOM   2311  C CB  . VAL A 1 295 ? 12.019  -8.567  30.794  1.00 64.36  ? 297 VAL A CB  1 
ATOM   2312  C CG1 . VAL A 1 295 ? 12.026  -9.942  31.435  1.00 73.11  ? 297 VAL A CG1 1 
ATOM   2313  C CG2 . VAL A 1 295 ? 10.925  -7.699  31.381  1.00 70.30  ? 297 VAL A CG2 1 
ATOM   2314  N N   . HIS A 1 296 ? 14.585  -9.552  29.670  1.00 79.94  ? 298 HIS A N   1 
ATOM   2315  C CA  . HIS A 1 296 ? 15.539  -10.629 29.441  1.00 66.40  ? 298 HIS A CA  1 
ATOM   2316  C C   . HIS A 1 296 ? 15.555  -10.995 27.961  1.00 63.21  ? 298 HIS A C   1 
ATOM   2317  O O   . HIS A 1 296 ? 14.509  -11.039 27.315  1.00 78.44  ? 298 HIS A O   1 
ATOM   2318  C CB  . HIS A 1 296 ? 15.165  -11.848 30.290  1.00 73.04  ? 298 HIS A CB  1 
ATOM   2319  C CG  . HIS A 1 296 ? 16.264  -12.856 30.427  1.00 67.41  ? 298 HIS A CG  1 
ATOM   2320  N ND1 . HIS A 1 296 ? 16.510  -13.822 29.477  1.00 64.81  ? 298 HIS A ND1 1 
ATOM   2321  C CD2 . HIS A 1 296 ? 17.174  -13.055 31.410  1.00 63.18  ? 298 HIS A CD2 1 
ATOM   2322  C CE1 . HIS A 1 296 ? 17.531  -14.567 29.864  1.00 57.95  ? 298 HIS A CE1 1 
ATOM   2323  N NE2 . HIS A 1 296 ? 17.949  -14.125 31.036  1.00 56.98  ? 298 HIS A NE2 1 
ATOM   2324  N N   . PRO A 1 297 ? 16.751  -11.254 27.421  1.00 54.05  ? 299 PRO A N   1 
ATOM   2325  C CA  . PRO A 1 297 ? 16.971  -11.613 26.016  1.00 49.07  ? 299 PRO A CA  1 
ATOM   2326  C C   . PRO A 1 297 ? 16.315  -12.934 25.599  1.00 63.39  ? 299 PRO A C   1 
ATOM   2327  O O   . PRO A 1 297 ? 15.727  -12.997 24.520  1.00 74.37  ? 299 PRO A O   1 
ATOM   2328  C CB  . PRO A 1 297 ? 18.499  -11.738 25.924  1.00 42.43  ? 299 PRO A CB  1 
ATOM   2329  C CG  . PRO A 1 297 ? 19.016  -10.925 27.052  1.00 48.51  ? 299 PRO A CG  1 
ATOM   2330  C CD  . PRO A 1 297 ? 18.019  -11.116 28.152  1.00 57.35  ? 299 PRO A CD  1 
ATOM   2331  N N   . LEU A 1 298 ? 16.415  -13.967 26.430  1.00 69.97  ? 300 LEU A N   1 
ATOM   2332  C CA  . LEU A 1 298 ? 15.903  -15.286 26.059  1.00 68.26  ? 300 LEU A CA  1 
ATOM   2333  C C   . LEU A 1 298 ? 14.387  -15.398 26.237  1.00 87.38  ? 300 LEU A C   1 
ATOM   2334  O O   . LEU A 1 298 ? 13.895  -15.921 27.231  1.00 98.17  ? 300 LEU A O   1 
ATOM   2335  C CB  . LEU A 1 298 ? 16.645  -16.385 26.821  1.00 56.72  ? 300 LEU A CB  1 
ATOM   2336  C CG  . LEU A 1 298 ? 18.166  -16.200 26.784  1.00 42.75  ? 300 LEU A CG  1 
ATOM   2337  C CD1 . LEU A 1 298 ? 18.875  -17.231 27.630  1.00 43.48  ? 300 LEU A CD1 1 
ATOM   2338  C CD2 . LEU A 1 298 ? 18.694  -16.212 25.350  1.00 33.77  ? 300 LEU A CD2 1 
ATOM   2339  N N   . THR A 1 299 ? 13.665  -14.906 25.239  1.00 43.51  ? 301 THR A N   1 
ATOM   2340  C CA  . THR A 1 299 ? 12.218  -14.802 25.273  1.00 48.19  ? 301 THR A CA  1 
ATOM   2341  C C   . THR A 1 299 ? 11.566  -15.975 24.537  1.00 44.33  ? 301 THR A C   1 
ATOM   2342  O O   . THR A 1 299 ? 12.226  -16.668 23.764  1.00 45.44  ? 301 THR A O   1 
ATOM   2343  C CB  . THR A 1 299 ? 11.788  -13.491 24.586  1.00 49.89  ? 301 THR A CB  1 
ATOM   2344  O OG1 . THR A 1 299 ? 10.716  -12.881 25.312  1.00 57.42  ? 301 THR A OG1 1 
ATOM   2345  C CG2 . THR A 1 299 ? 11.358  -13.754 23.141  1.00 43.11  ? 301 THR A CG2 1 
ATOM   2346  N N   . ILE A 1 300 ? 10.278  -16.208 24.790  1.00 42.30  ? 302 ILE A N   1 
ATOM   2347  C CA  . ILE A 1 300 ? 9.471   -17.105 23.956  1.00 37.25  ? 302 ILE A CA  1 
ATOM   2348  C C   . ILE A 1 300 ? 8.053   -16.563 23.816  1.00 45.36  ? 302 ILE A C   1 
ATOM   2349  O O   . ILE A 1 300 ? 7.413   -16.229 24.814  1.00 50.60  ? 302 ILE A O   1 
ATOM   2350  C CB  . ILE A 1 300 ? 9.370   -18.533 24.524  1.00 42.89  ? 302 ILE A CB  1 
ATOM   2351  C CG1 . ILE A 1 300 ? 10.749  -19.102 24.845  1.00 42.10  ? 302 ILE A CG1 1 
ATOM   2352  C CG2 . ILE A 1 300 ? 8.641   -19.444 23.539  1.00 37.71  ? 302 ILE A CG2 1 
ATOM   2353  C CD1 . ILE A 1 300 ? 10.708  -20.560 25.239  1.00 44.06  ? 302 ILE A CD1 1 
ATOM   2354  N N   . GLY A 1 301 ? 7.565   -16.482 22.580  1.00 70.20  ? 303 GLY A N   1 
ATOM   2355  C CA  . GLY A 1 301 ? 6.230   -15.971 22.308  1.00 79.45  ? 303 GLY A CA  1 
ATOM   2356  C C   . GLY A 1 301 ? 6.233   -14.787 21.358  1.00 78.27  ? 303 GLY A C   1 
ATOM   2357  O O   . GLY A 1 301 ? 7.158   -14.635 20.559  1.00 84.68  ? 303 GLY A O   1 
ATOM   2358  N N   . GLU A 1 302 ? 5.187   -13.966 21.421  1.00 56.22  ? 304 GLU A N   1 
ATOM   2359  C CA  . GLU A 1 302 ? 5.203   -12.656 20.767  1.00 60.89  ? 304 GLU A CA  1 
ATOM   2360  C C   . GLU A 1 302 ? 5.682   -11.649 21.797  1.00 61.15  ? 304 GLU A C   1 
ATOM   2361  O O   . GLU A 1 302 ? 5.051   -11.457 22.833  1.00 66.10  ? 304 GLU A O   1 
ATOM   2362  C CB  . GLU A 1 302 ? 3.817   -12.243 20.258  1.00 73.46  ? 304 GLU A CB  1 
ATOM   2363  C CG  . GLU A 1 302 ? 3.070   -13.303 19.468  1.00 78.35  ? 304 GLU A CG  1 
ATOM   2364  C CD  . GLU A 1 302 ? 2.395   -14.327 20.365  1.00 90.89  ? 304 GLU A CD  1 
ATOM   2365  O OE1 . GLU A 1 302 ? 2.031   -15.415 19.864  1.00 87.48  ? 304 GLU A OE1 1 
ATOM   2366  O OE2 . GLU A 1 302 ? 2.226   -14.042 21.571  1.00 105.16 ? 304 GLU A OE2 1 
ATOM   2367  N N   . CYS A 1 303 ? 6.809   -11.012 21.525  1.00 55.15  ? 305 CYS A N   1 
ATOM   2368  C CA  . CYS A 1 303 ? 7.398   -10.127 22.518  1.00 58.31  ? 305 CYS A CA  1 
ATOM   2369  C C   . CYS A 1 303 ? 7.816   -8.779  21.943  1.00 51.64  ? 305 CYS A C   1 
ATOM   2370  O O   . CYS A 1 303 ? 8.084   -8.652  20.748  1.00 49.90  ? 305 CYS A O   1 
ATOM   2371  C CB  . CYS A 1 303 ? 8.581   -10.814 23.200  1.00 57.74  ? 305 CYS A CB  1 
ATOM   2372  S SG  . CYS A 1 303 ? 8.132   -12.337 24.042  1.00 61.26  ? 305 CYS A SG  1 
ATOM   2373  N N   . PRO A 1 304 ? 7.855   -7.759  22.800  1.00 48.17  ? 306 PRO A N   1 
ATOM   2374  C CA  . PRO A 1 304 ? 8.294   -6.456  22.318  1.00 44.67  ? 306 PRO A CA  1 
ATOM   2375  C C   . PRO A 1 304 ? 9.767   -6.565  21.951  1.00 41.95  ? 306 PRO A C   1 
ATOM   2376  O O   . PRO A 1 304 ? 10.433  -7.482  22.449  1.00 40.87  ? 306 PRO A O   1 
ATOM   2377  C CB  . PRO A 1 304 ? 8.108   -5.554  23.544  1.00 55.42  ? 306 PRO A CB  1 
ATOM   2378  C CG  . PRO A 1 304 ? 7.188   -6.314  24.458  1.00 55.33  ? 306 PRO A CG  1 
ATOM   2379  C CD  . PRO A 1 304 ? 7.521   -7.738  24.230  1.00 51.90  ? 306 PRO A CD  1 
ATOM   2380  N N   . LYS A 1 305 ? 10.261  -5.665  21.101  1.00 41.99  ? 307 LYS A N   1 
ATOM   2381  C CA  . LYS A 1 305 ? 11.675  -5.668  20.724  1.00 39.61  ? 307 LYS A CA  1 
ATOM   2382  C C   . LYS A 1 305 ? 12.588  -5.452  21.929  1.00 47.55  ? 307 LYS A C   1 
ATOM   2383  O O   . LYS A 1 305 ? 12.371  -4.537  22.720  1.00 62.77  ? 307 LYS A O   1 
ATOM   2384  C CB  . LYS A 1 305 ? 11.947  -4.627  19.634  1.00 40.23  ? 307 LYS A CB  1 
ATOM   2385  C CG  . LYS A 1 305 ? 11.493  -5.069  18.245  1.00 45.96  ? 307 LYS A CG  1 
ATOM   2386  C CD  . LYS A 1 305 ? 12.149  -6.394  17.842  1.00 55.92  ? 307 LYS A CD  1 
ATOM   2387  C CE  . LYS A 1 305 ? 11.127  -7.394  17.336  1.00 63.35  ? 307 LYS A CE  1 
ATOM   2388  N NZ  . LYS A 1 305 ? 10.347  -6.856  16.192  1.00 66.11  ? 307 LYS A NZ  1 
ATOM   2389  N N   . TYR A 1 306 ? 13.603  -6.298  22.070  1.00 77.06  ? 308 TYR A N   1 
ATOM   2390  C CA  . TYR A 1 306 ? 14.508  -6.220  23.209  1.00 73.31  ? 308 TYR A CA  1 
ATOM   2391  C C   . TYR A 1 306 ? 15.627  -5.232  22.960  1.00 67.10  ? 308 TYR A C   1 
ATOM   2392  O O   . TYR A 1 306 ? 16.267  -5.275  21.921  1.00 68.56  ? 308 TYR A O   1 
ATOM   2393  C CB  . TYR A 1 306 ? 15.110  -7.588  23.503  1.00 59.06  ? 308 TYR A CB  1 
ATOM   2394  C CG  . TYR A 1 306 ? 16.072  -7.597  24.667  1.00 63.20  ? 308 TYR A CG  1 
ATOM   2395  C CD1 . TYR A 1 306 ? 15.624  -7.371  25.961  1.00 75.44  ? 308 TYR A CD1 1 
ATOM   2396  C CD2 . TYR A 1 306 ? 17.422  -7.854  24.477  1.00 59.91  ? 308 TYR A CD2 1 
ATOM   2397  C CE1 . TYR A 1 306 ? 16.493  -7.388  27.033  1.00 67.76  ? 308 TYR A CE1 1 
ATOM   2398  C CE2 . TYR A 1 306 ? 18.302  -7.876  25.546  1.00 59.52  ? 308 TYR A CE2 1 
ATOM   2399  C CZ  . TYR A 1 306 ? 17.829  -7.639  26.822  1.00 57.81  ? 308 TYR A CZ  1 
ATOM   2400  O OH  . TYR A 1 306 ? 18.695  -7.652  27.893  1.00 50.48  ? 308 TYR A OH  1 
ATOM   2401  N N   . VAL A 1 307 ? 15.873  -4.350  23.920  1.00 66.48  ? 309 VAL A N   1 
ATOM   2402  C CA  . VAL A 1 307 ? 16.926  -3.346  23.780  1.00 56.14  ? 309 VAL A CA  1 
ATOM   2403  C C   . VAL A 1 307 ? 17.857  -3.321  24.979  1.00 54.67  ? 309 VAL A C   1 
ATOM   2404  O O   . VAL A 1 307 ? 17.495  -3.756  26.074  1.00 66.47  ? 309 VAL A O   1 
ATOM   2405  C CB  . VAL A 1 307 ? 16.355  -1.934  23.599  1.00 57.40  ? 309 VAL A CB  1 
ATOM   2406  C CG1 . VAL A 1 307 ? 15.819  -1.754  22.190  1.00 64.67  ? 309 VAL A CG1 1 
ATOM   2407  C CG2 . VAL A 1 307 ? 15.277  -1.659  24.638  1.00 66.31  ? 309 VAL A CG2 1 
ATOM   2408  N N   . LYS A 1 308 ? 19.065  -2.820  24.760  1.00 65.32  ? 310 LYS A N   1 
ATOM   2409  C CA  . LYS A 1 308 ? 20.021  -2.654  25.838  1.00 71.34  ? 310 LYS A CA  1 
ATOM   2410  C C   . LYS A 1 308 ? 19.861  -1.234  26.367  1.00 74.80  ? 310 LYS A C   1 
ATOM   2411  O O   . LYS A 1 308 ? 20.801  -0.442  26.357  1.00 84.99  ? 310 LYS A O   1 
ATOM   2412  C CB  . LYS A 1 308 ? 21.443  -2.918  25.333  1.00 72.04  ? 310 LYS A CB  1 
ATOM   2413  C CG  . LYS A 1 308 ? 22.515  -2.963  26.417  1.00 82.32  ? 310 LYS A CG  1 
ATOM   2414  C CD  . LYS A 1 308 ? 23.375  -1.698  26.397  1.00 93.85  ? 310 LYS A CD  1 
ATOM   2415  C CE  . LYS A 1 308 ? 24.418  -1.689  27.510  1.00 99.62  ? 310 LYS A CE  1 
ATOM   2416  N NZ  . LYS A 1 308 ? 25.200  -0.418  27.524  1.00 104.30 ? 310 LYS A NZ  1 
ATOM   2417  N N   . SER A 1 309 ? 18.650  -0.913  26.817  1.00 56.58  ? 311 SER A N   1 
ATOM   2418  C CA  . SER A 1 309 ? 18.331  0.444   27.261  1.00 54.92  ? 311 SER A CA  1 
ATOM   2419  C C   . SER A 1 309 ? 17.749  0.483   28.669  1.00 61.18  ? 311 SER A C   1 
ATOM   2420  O O   . SER A 1 309 ? 17.154  -0.488  29.129  1.00 68.74  ? 311 SER A O   1 
ATOM   2421  C CB  . SER A 1 309 ? 17.360  1.104   26.284  1.00 61.06  ? 311 SER A CB  1 
ATOM   2422  O OG  . SER A 1 309 ? 16.795  2.268   26.849  1.00 81.46  ? 311 SER A OG  1 
ATOM   2423  N N   . GLU A 1 310 ? 17.912  1.618   29.342  1.00 74.55  ? 312 GLU A N   1 
ATOM   2424  C CA  . GLU A 1 310 ? 17.469  1.753   30.727  1.00 87.04  ? 312 GLU A CA  1 
ATOM   2425  C C   . GLU A 1 310 ? 16.072  2.353   30.844  1.00 95.30  ? 312 GLU A C   1 
ATOM   2426  O O   . GLU A 1 310 ? 15.221  1.818   31.549  1.00 98.38  ? 312 GLU A O   1 
ATOM   2427  C CB  . GLU A 1 310 ? 18.468  2.581   31.536  1.00 92.91  ? 312 GLU A CB  1 
ATOM   2428  C CG  . GLU A 1 310 ? 18.635  2.084   32.958  1.00 105.77 ? 312 GLU A CG  1 
ATOM   2429  C CD  . GLU A 1 310 ? 19.030  0.615   33.011  1.00 111.25 ? 312 GLU A CD  1 
ATOM   2430  O OE1 . GLU A 1 310 ? 20.042  0.244   32.373  1.00 110.28 ? 312 GLU A OE1 1 
ATOM   2431  O OE2 . GLU A 1 310 ? 18.321  -0.171  33.678  1.00 113.13 ? 312 GLU A OE2 1 
ATOM   2432  N N   . LYS A 1 311 ? 15.845  3.471   30.163  1.00 69.57  ? 313 LYS A N   1 
ATOM   2433  C CA  . LYS A 1 311 ? 14.525  4.095   30.138  1.00 85.22  ? 313 LYS A CA  1 
ATOM   2434  C C   . LYS A 1 311 ? 14.258  4.711   28.774  1.00 83.67  ? 313 LYS A C   1 
ATOM   2435  O O   . LYS A 1 311 ? 15.170  5.224   28.133  1.00 75.79  ? 313 LYS A O   1 
ATOM   2436  C CB  . LYS A 1 311 ? 14.408  5.166   31.225  1.00 93.37  ? 313 LYS A CB  1 
ATOM   2437  C CG  . LYS A 1 311 ? 15.413  6.308   31.085  1.00 88.58  ? 313 LYS A CG  1 
ATOM   2438  C CD  . LYS A 1 311 ? 15.300  7.328   32.219  1.00 95.69  ? 313 LYS A CD  1 
ATOM   2439  C CE  . LYS A 1 311 ? 14.055  8.182   32.074  1.00 111.33 ? 313 LYS A CE  1 
ATOM   2440  N NZ  . LYS A 1 311 ? 14.058  8.936   30.793  1.00 109.26 ? 313 LYS A NZ  1 
ATOM   2441  N N   . LEU A 1 312 ? 13.010  4.645   28.326  1.00 80.21  ? 314 LEU A N   1 
ATOM   2442  C CA  . LEU A 1 312 ? 12.621  5.293   27.080  1.00 69.18  ? 314 LEU A CA  1 
ATOM   2443  C C   . LEU A 1 312 ? 11.347  6.086   27.301  1.00 67.94  ? 314 LEU A C   1 
ATOM   2444  O O   . LEU A 1 312 ? 10.245  5.556   27.175  1.00 69.06  ? 314 LEU A O   1 
ATOM   2445  C CB  . LEU A 1 312 ? 12.422  4.269   25.962  1.00 60.29  ? 314 LEU A CB  1 
ATOM   2446  C CG  . LEU A 1 312 ? 13.636  3.400   25.620  1.00 53.73  ? 314 LEU A CG  1 
ATOM   2447  C CD1 . LEU A 1 312 ? 13.308  2.383   24.530  1.00 52.19  ? 314 LEU A CD1 1 
ATOM   2448  C CD2 . LEU A 1 312 ? 14.807  4.270   25.203  1.00 47.92  ? 314 LEU A CD2 1 
ATOM   2449  N N   . VAL A 1 313 ? 11.509  7.363   27.631  1.00 56.26  ? 315 VAL A N   1 
ATOM   2450  C CA  . VAL A 1 313 ? 10.387  8.196   28.042  1.00 60.29  ? 315 VAL A CA  1 
ATOM   2451  C C   . VAL A 1 313 ? 9.989   9.225   27.000  1.00 60.44  ? 315 VAL A C   1 
ATOM   2452  O O   . VAL A 1 313 ? 10.658  10.244  26.849  1.00 71.13  ? 315 VAL A O   1 
ATOM   2453  C CB  . VAL A 1 313 ? 10.715  8.956   29.337  1.00 62.65  ? 315 VAL A CB  1 
ATOM   2454  C CG1 . VAL A 1 313 ? 9.541   9.815   29.750  1.00 64.76  ? 315 VAL A CG1 1 
ATOM   2455  C CG2 . VAL A 1 313 ? 11.085  7.983   30.444  1.00 66.14  ? 315 VAL A CG2 1 
ATOM   2456  N N   . LEU A 1 314 ? 8.896   8.963   26.289  1.00 45.37  ? 316 LEU A N   1 
ATOM   2457  C CA  . LEU A 1 314 ? 8.301   9.971   25.418  1.00 44.23  ? 316 LEU A CA  1 
ATOM   2458  C C   . LEU A 1 314 ? 7.739   11.105  26.260  1.00 63.36  ? 316 LEU A C   1 
ATOM   2459  O O   . LEU A 1 314 ? 7.394   10.914  27.424  1.00 73.07  ? 316 LEU A O   1 
ATOM   2460  C CB  . LEU A 1 314 ? 7.176   9.380   24.574  1.00 36.58  ? 316 LEU A CB  1 
ATOM   2461  C CG  . LEU A 1 314 ? 7.554   8.665   23.280  1.00 42.54  ? 316 LEU A CG  1 
ATOM   2462  C CD1 . LEU A 1 314 ? 6.306   8.420   22.450  1.00 49.79  ? 316 LEU A CD1 1 
ATOM   2463  C CD2 . LEU A 1 314 ? 8.568   9.471   22.483  1.00 40.11  ? 316 LEU A CD2 1 
ATOM   2464  N N   . ALA A 1 315 ? 7.651   12.289  25.672  1.00 66.67  ? 317 ALA A N   1 
ATOM   2465  C CA  . ALA A 1 315 ? 6.998   13.401  26.341  1.00 66.82  ? 317 ALA A CA  1 
ATOM   2466  C C   . ALA A 1 315 ? 5.594   13.553  25.770  1.00 71.04  ? 317 ALA A C   1 
ATOM   2467  O O   . ALA A 1 315 ? 5.409   13.553  24.552  1.00 73.44  ? 317 ALA A O   1 
ATOM   2468  C CB  . ALA A 1 315 ? 7.796   14.674  26.164  1.00 53.28  ? 317 ALA A CB  1 
ATOM   2469  N N   . THR A 1 316 ? 4.606   13.653  26.653  1.00 78.06  ? 318 THR A N   1 
ATOM   2470  C CA  . THR A 1 316 ? 3.224   13.824  26.230  1.00 85.84  ? 318 THR A CA  1 
ATOM   2471  C C   . THR A 1 316 ? 2.818   15.289  26.340  1.00 97.62  ? 318 THR A C   1 
ATOM   2472  O O   . THR A 1 316 ? 2.239   15.852  25.413  1.00 101.86 ? 318 THR A O   1 
ATOM   2473  C CB  . THR A 1 316 ? 2.262   12.966  27.068  1.00 89.04  ? 318 THR A CB  1 
ATOM   2474  O OG1 . THR A 1 316 ? 2.063   13.577  28.348  1.00 95.15  ? 318 THR A OG1 1 
ATOM   2475  C CG2 . THR A 1 316 ? 2.825   11.571  27.259  1.00 87.00  ? 318 THR A CG2 1 
ATOM   2476  N N   . GLY A 1 317 ? 3.138   15.904  27.475  1.00 110.78 ? 319 GLY A N   1 
ATOM   2477  C CA  . GLY A 1 317 ? 2.780   17.289  27.715  1.00 112.34 ? 319 GLY A CA  1 
ATOM   2478  C C   . GLY A 1 317 ? 3.829   18.276  27.240  1.00 107.91 ? 319 GLY A C   1 
ATOM   2479  O O   . GLY A 1 317 ? 4.600   17.991  26.324  1.00 105.37 ? 319 GLY A O   1 
ATOM   2480  N N   . LEU A 1 318 ? 3.850   19.446  27.870  1.00 85.09  ? 320 LEU A N   1 
ATOM   2481  C CA  . LEU A 1 318 ? 4.797   20.500  27.524  1.00 73.76  ? 320 LEU A CA  1 
ATOM   2482  C C   . LEU A 1 318 ? 5.848   20.696  28.617  1.00 74.47  ? 320 LEU A C   1 
ATOM   2483  O O   . LEU A 1 318 ? 5.908   19.932  29.582  1.00 82.30  ? 320 LEU A O   1 
ATOM   2484  C CB  . LEU A 1 318 ? 4.052   21.807  27.246  1.00 68.49  ? 320 LEU A CB  1 
ATOM   2485  C CG  . LEU A 1 318 ? 3.010   22.236  28.286  1.00 71.30  ? 320 LEU A CG  1 
ATOM   2486  C CD1 . LEU A 1 318 ? 3.638   23.129  29.351  1.00 75.91  ? 320 LEU A CD1 1 
ATOM   2487  C CD2 . LEU A 1 318 ? 1.830   22.939  27.622  1.00 64.79  ? 320 LEU A CD2 1 
ATOM   2488  N N   . ARG A 1 319 ? 6.679   21.721  28.464  1.00 65.97  ? 321 ARG A N   1 
ATOM   2489  C CA  . ARG A 1 319 ? 7.777   21.930  29.398  1.00 61.81  ? 321 ARG A CA  1 
ATOM   2490  C C   . ARG A 1 319 ? 7.307   22.595  30.686  1.00 78.06  ? 321 ARG A C   1 
ATOM   2491  O O   . ARG A 1 319 ? 6.712   23.670  30.661  1.00 89.56  ? 321 ARG A O   1 
ATOM   2492  C CB  . ARG A 1 319 ? 8.899   22.747  28.752  1.00 61.69  ? 321 ARG A CB  1 
ATOM   2493  C CG  . ARG A 1 319 ? 10.162  22.816  29.601  1.00 75.47  ? 321 ARG A CG  1 
ATOM   2494  C CD  . ARG A 1 319 ? 11.248  23.618  28.918  1.00 75.12  ? 321 ARG A CD  1 
ATOM   2495  N NE  . ARG A 1 319 ? 11.526  23.121  27.575  1.00 74.64  ? 321 ARG A NE  1 
ATOM   2496  C CZ  . ARG A 1 319 ? 12.736  22.780  27.145  1.00 72.18  ? 321 ARG A CZ  1 
ATOM   2497  N NH1 . ARG A 1 319 ? 13.780  22.886  27.959  1.00 77.34  ? 321 ARG A NH1 1 
ATOM   2498  N NH2 . ARG A 1 319 ? 12.904  22.340  25.903  1.00 59.89  ? 321 ARG A NH2 1 
ATOM   2499  N N   . ASN A 1 320 ? 7.578   21.946  31.812  1.00 82.06  ? 322 ASN A N   1 
ATOM   2500  C CA  . ASN A 1 320 ? 7.186   22.482  33.107  1.00 87.27  ? 322 ASN A CA  1 
ATOM   2501  C C   . ASN A 1 320 ? 8.117   23.602  33.549  1.00 98.92  ? 322 ASN A C   1 
ATOM   2502  O O   . ASN A 1 320 ? 9.292   23.367  33.842  1.00 104.17 ? 322 ASN A O   1 
ATOM   2503  C CB  . ASN A 1 320 ? 7.159   21.373  34.157  1.00 82.44  ? 322 ASN A CB  1 
ATOM   2504  C CG  . ASN A 1 320 ? 6.087   21.588  35.204  1.00 87.29  ? 322 ASN A CG  1 
ATOM   2505  O OD1 . ASN A 1 320 ? 5.251   22.483  35.079  1.00 95.52  ? 322 ASN A OD1 1 
ATOM   2506  N ND2 . ASN A 1 320 ? 6.098   20.758  36.242  1.00 85.91  ? 322 ASN A ND2 1 
ATOM   2507  N N   . VAL A 1 321 ? 7.582   24.820  33.585  1.00 121.74 ? 323 VAL A N   1 
ATOM   2508  C CA  . VAL A 1 321 ? 8.337   25.996  34.014  1.00 123.51 ? 323 VAL A CA  1 
ATOM   2509  C C   . VAL A 1 321 ? 7.608   26.766  35.114  1.00 135.98 ? 323 VAL A C   1 
ATOM   2510  O O   . VAL A 1 321 ? 6.400   26.985  35.028  1.00 144.83 ? 323 VAL A O   1 
ATOM   2511  C CB  . VAL A 1 321 ? 8.608   26.956  32.839  1.00 110.47 ? 323 VAL A CB  1 
ATOM   2512  C CG1 . VAL A 1 321 ? 9.754   26.443  31.980  1.00 106.51 ? 323 VAL A CG1 1 
ATOM   2513  C CG2 . VAL A 1 321 ? 7.352   27.145  32.012  1.00 105.87 ? 323 VAL A CG2 1 
ATOM   2514  N N   . PRO A 1 322 ? 8.350   27.176  36.155  1.00 115.39 ? 324 PRO A N   1 
ATOM   2515  C CA  . PRO A 1 322 ? 7.840   27.959  37.290  1.00 119.98 ? 324 PRO A CA  1 
ATOM   2516  C C   . PRO A 1 322 ? 7.092   29.225  36.857  1.00 115.29 ? 324 PRO A C   1 
ATOM   2517  O O   . PRO A 1 322 ? 6.454   29.884  37.686  1.00 115.76 ? 324 PRO A O   1 
ATOM   2518  C CB  . PRO A 1 322 ? 9.118   28.334  38.046  1.00 123.88 ? 324 PRO A CB  1 
ATOM   2519  C CG  . PRO A 1 322 ? 10.063  27.215  37.744  1.00 118.69 ? 324 PRO A CG  1 
ATOM   2520  C CD  . PRO A 1 322 ? 9.770   26.818  36.325  1.00 110.23 ? 324 PRO A CD  1 
ATOM   2521  N N   . GLY B 2 1   ? 11.990  28.482  23.523  1.00 98.55  ? 1   GLY B N   1 
ATOM   2522  C CA  . GLY B 2 1   ? 12.163  27.207  22.855  1.00 96.47  ? 1   GLY B CA  1 
ATOM   2523  C C   . GLY B 2 1   ? 12.565  27.369  21.402  1.00 82.95  ? 1   GLY B C   1 
ATOM   2524  O O   . GLY B 2 1   ? 13.666  27.832  21.108  1.00 76.93  ? 1   GLY B O   1 
ATOM   2525  N N   . LEU B 2 2   ? 11.670  26.990  20.494  1.00 57.81  ? 2   LEU B N   1 
ATOM   2526  C CA  . LEU B 2 2   ? 11.949  27.044  19.062  1.00 47.87  ? 2   LEU B CA  1 
ATOM   2527  C C   . LEU B 2 2   ? 10.891  27.857  18.349  1.00 48.78  ? 2   LEU B C   1 
ATOM   2528  O O   . LEU B 2 2   ? 11.017  28.160  17.165  1.00 58.14  ? 2   LEU B O   1 
ATOM   2529  C CB  . LEU B 2 2   ? 12.001  25.638  18.461  1.00 48.90  ? 2   LEU B CB  1 
ATOM   2530  C CG  . LEU B 2 2   ? 12.169  25.584  16.937  1.00 49.63  ? 2   LEU B CG  1 
ATOM   2531  C CD1 . LEU B 2 2   ? 13.610  25.283  16.540  1.00 56.04  ? 2   LEU B CD1 1 
ATOM   2532  C CD2 . LEU B 2 2   ? 11.223  24.577  16.316  1.00 41.77  ? 2   LEU B CD2 1 
ATOM   2533  N N   . PHE B 2 3   ? 9.836   28.200  19.074  1.00 60.14  ? 3   PHE B N   1 
ATOM   2534  C CA  . PHE B 2 3   ? 8.846   29.143  18.570  1.00 70.24  ? 3   PHE B CA  1 
ATOM   2535  C C   . PHE B 2 3   ? 8.756   30.320  19.528  1.00 82.14  ? 3   PHE B C   1 
ATOM   2536  O O   . PHE B 2 3   ? 7.904   31.193  19.388  1.00 89.58  ? 3   PHE B O   1 
ATOM   2537  C CB  . PHE B 2 3   ? 7.489   28.470  18.364  1.00 72.80  ? 3   PHE B CB  1 
ATOM   2538  C CG  . PHE B 2 3   ? 7.412   27.650  17.108  1.00 70.89  ? 3   PHE B CG  1 
ATOM   2539  C CD1 . PHE B 2 3   ? 7.101   28.245  15.898  1.00 65.30  ? 3   PHE B CD1 1 
ATOM   2540  C CD2 . PHE B 2 3   ? 7.659   26.292  17.134  1.00 67.92  ? 3   PHE B CD2 1 
ATOM   2541  C CE1 . PHE B 2 3   ? 7.035   27.503  14.743  1.00 64.73  ? 3   PHE B CE1 1 
ATOM   2542  C CE2 . PHE B 2 3   ? 7.596   25.542  15.979  1.00 68.54  ? 3   PHE B CE2 1 
ATOM   2543  C CZ  . PHE B 2 3   ? 7.284   26.151  14.782  1.00 68.08  ? 3   PHE B CZ  1 
ATOM   2544  N N   . GLY B 2 4   ? 9.655   30.319  20.507  1.00 83.17  ? 4   GLY B N   1 
ATOM   2545  C CA  . GLY B 2 4   ? 9.875   31.469  21.359  1.00 79.18  ? 4   GLY B CA  1 
ATOM   2546  C C   . GLY B 2 4   ? 8.806   31.730  22.394  1.00 81.85  ? 4   GLY B C   1 
ATOM   2547  O O   . GLY B 2 4   ? 9.004   32.541  23.300  1.00 84.30  ? 4   GLY B O   1 
ATOM   2548  N N   . ALA B 2 5   ? 7.671   31.057  22.268  1.00 51.83  ? 5   ALA B N   1 
ATOM   2549  C CA  . ALA B 2 5   ? 6.585   31.285  23.209  1.00 55.19  ? 5   ALA B CA  1 
ATOM   2550  C C   . ALA B 2 5   ? 6.910   30.740  24.605  1.00 61.30  ? 5   ALA B C   1 
ATOM   2551  O O   . ALA B 2 5   ? 7.129   31.513  25.545  1.00 65.56  ? 5   ALA B O   1 
ATOM   2552  C CB  . ALA B 2 5   ? 5.286   30.702  22.682  1.00 57.63  ? 5   ALA B CB  1 
ATOM   2553  N N   . ILE B 2 6   ? 6.951   29.414  24.731  1.00 58.77  ? 6   ILE B N   1 
ATOM   2554  C CA  . ILE B 2 6   ? 7.178   28.753  26.019  1.00 61.75  ? 6   ILE B CA  1 
ATOM   2555  C C   . ILE B 2 6   ? 8.602   28.931  26.527  1.00 66.36  ? 6   ILE B C   1 
ATOM   2556  O O   . ILE B 2 6   ? 9.565   28.700  25.795  1.00 72.24  ? 6   ILE B O   1 
ATOM   2557  C CB  . ILE B 2 6   ? 6.884   27.247  25.939  1.00 55.52  ? 6   ILE B CB  1 
ATOM   2558  C CG1 . ILE B 2 6   ? 5.451   27.014  25.467  1.00 49.02  ? 6   ILE B CG1 1 
ATOM   2559  C CG2 . ILE B 2 6   ? 7.125   26.588  27.287  1.00 59.46  ? 6   ILE B CG2 1 
ATOM   2560  C CD1 . ILE B 2 6   ? 5.158   25.583  25.154  1.00 43.69  ? 6   ILE B CD1 1 
ATOM   2561  N N   . ALA B 2 7   ? 8.722   29.329  27.790  1.00 60.32  ? 7   ALA B N   1 
ATOM   2562  C CA  . ALA B 2 7   ? 10.016  29.619  28.398  1.00 61.76  ? 7   ALA B CA  1 
ATOM   2563  C C   . ALA B 2 7   ? 10.749  30.691  27.601  1.00 65.72  ? 7   ALA B C   1 
ATOM   2564  O O   . ALA B 2 7   ? 11.983  30.746  27.604  1.00 70.75  ? 7   ALA B O   1 
ATOM   2565  C CB  . ALA B 2 7   ? 10.855  28.356  28.502  1.00 63.24  ? 7   ALA B CB  1 
ATOM   2566  N N   . GLY B 2 8   ? 9.978   31.539  26.920  1.00 80.12  ? 8   GLY B N   1 
ATOM   2567  C CA  . GLY B 2 8   ? 10.529  32.587  26.079  1.00 76.98  ? 8   GLY B CA  1 
ATOM   2568  C C   . GLY B 2 8   ? 9.957   33.946  26.429  1.00 79.08  ? 8   GLY B C   1 
ATOM   2569  O O   . GLY B 2 8   ? 10.177  34.443  27.534  1.00 79.77  ? 8   GLY B O   1 
ATOM   2570  N N   . PHE B 2 9   ? 9.217   34.552  25.501  1.00 71.17  ? 9   PHE B N   1 
ATOM   2571  C CA  . PHE B 2 9   ? 8.570   35.827  25.800  1.00 73.14  ? 9   PHE B CA  1 
ATOM   2572  C C   . PHE B 2 9   ? 7.472   35.671  26.848  1.00 79.72  ? 9   PHE B C   1 
ATOM   2573  O O   . PHE B 2 9   ? 7.164   36.613  27.579  1.00 91.43  ? 9   PHE B O   1 
ATOM   2574  C CB  . PHE B 2 9   ? 8.085   36.563  24.537  1.00 75.80  ? 9   PHE B CB  1 
ATOM   2575  C CG  . PHE B 2 9   ? 6.880   35.948  23.861  1.00 73.56  ? 9   PHE B CG  1 
ATOM   2576  C CD1 . PHE B 2 9   ? 5.648   35.916  24.489  1.00 73.91  ? 9   PHE B CD1 1 
ATOM   2577  C CD2 . PHE B 2 9   ? 6.969   35.468  22.563  1.00 69.57  ? 9   PHE B CD2 1 
ATOM   2578  C CE1 . PHE B 2 9   ? 4.543   35.383  23.854  1.00 70.93  ? 9   PHE B CE1 1 
ATOM   2579  C CE2 . PHE B 2 9   ? 5.864   34.935  21.923  1.00 67.76  ? 9   PHE B CE2 1 
ATOM   2580  C CZ  . PHE B 2 9   ? 4.652   34.895  22.572  1.00 67.83  ? 9   PHE B CZ  1 
ATOM   2581  N N   . ILE B 2 10  ? 6.890   34.477  26.920  1.00 49.26  ? 10  ILE B N   1 
ATOM   2582  C CA  . ILE B 2 10  ? 6.061   34.095  28.058  1.00 48.22  ? 10  ILE B CA  1 
ATOM   2583  C C   . ILE B 2 10  ? 6.942   33.355  29.057  1.00 59.73  ? 10  ILE B C   1 
ATOM   2584  O O   . ILE B 2 10  ? 7.253   32.179  28.863  1.00 71.50  ? 10  ILE B O   1 
ATOM   2585  C CB  . ILE B 2 10  ? 4.901   33.191  27.644  1.00 40.77  ? 10  ILE B CB  1 
ATOM   2586  C CG1 . ILE B 2 10  ? 4.045   33.874  26.590  1.00 35.36  ? 10  ILE B CG1 1 
ATOM   2587  C CG2 . ILE B 2 10  ? 4.036   32.867  28.836  1.00 52.68  ? 10  ILE B CG2 1 
ATOM   2588  C CD1 . ILE B 2 10  ? 2.814   33.098  26.232  1.00 34.62  ? 10  ILE B CD1 1 
ATOM   2589  N N   . GLU B 2 11  ? 7.343   34.045  30.121  1.00 61.41  ? 11  GLU B N   1 
ATOM   2590  C CA  . GLU B 2 11  ? 8.373   33.540  31.028  1.00 55.51  ? 11  GLU B CA  1 
ATOM   2591  C C   . GLU B 2 11  ? 8.044   32.201  31.681  1.00 63.51  ? 11  GLU B C   1 
ATOM   2592  O O   . GLU B 2 11  ? 8.916   31.340  31.801  1.00 70.16  ? 11  GLU B O   1 
ATOM   2593  C CB  . GLU B 2 11  ? 8.687   34.566  32.117  1.00 62.50  ? 11  GLU B CB  1 
ATOM   2594  C CG  . GLU B 2 11  ? 9.348   35.834  31.615  1.00 70.56  ? 11  GLU B CG  1 
ATOM   2595  C CD  . GLU B 2 11  ? 9.362   36.935  32.659  1.00 82.44  ? 11  GLU B CD  1 
ATOM   2596  O OE1 . GLU B 2 11  ? 8.977   38.075  32.324  1.00 86.51  ? 11  GLU B OE1 1 
ATOM   2597  O OE2 . GLU B 2 11  ? 9.758   36.662  33.812  1.00 86.33  ? 11  GLU B OE2 1 
ATOM   2598  N N   . GLY B 2 12  ? 6.797   32.030  32.114  1.00 63.39  ? 12  GLY B N   1 
ATOM   2599  C CA  . GLY B 2 12  ? 6.439   30.859  32.889  1.00 67.68  ? 12  GLY B CA  1 
ATOM   2600  C C   . GLY B 2 12  ? 5.027   30.337  32.713  1.00 79.34  ? 12  GLY B C   1 
ATOM   2601  O O   . GLY B 2 12  ? 4.222   30.895  31.962  1.00 81.49  ? 12  GLY B O   1 
ATOM   2602  N N   . GLY B 2 13  ? 4.733   29.250  33.422  1.00 76.73  ? 13  GLY B N   1 
ATOM   2603  C CA  . GLY B 2 13  ? 3.439   28.603  33.332  1.00 80.78  ? 13  GLY B CA  1 
ATOM   2604  C C   . GLY B 2 13  ? 2.494   29.007  34.445  1.00 90.17  ? 13  GLY B C   1 
ATOM   2605  O O   . GLY B 2 13  ? 2.901   29.627  35.429  1.00 93.90  ? 13  GLY B O   1 
ATOM   2606  N N   . TRP B 2 14  ? 1.226   28.638  34.289  1.00 82.25  ? 14  TRP B N   1 
ATOM   2607  C CA  . TRP B 2 14  ? 0.190   28.989  35.251  1.00 85.83  ? 14  TRP B CA  1 
ATOM   2608  C C   . TRP B 2 14  ? -0.324  27.787  36.032  1.00 88.99  ? 14  TRP B C   1 
ATOM   2609  O O   . TRP B 2 14  ? -1.228  27.081  35.573  1.00 83.10  ? 14  TRP B O   1 
ATOM   2610  C CB  . TRP B 2 14  ? -0.986  29.639  34.532  1.00 85.01  ? 14  TRP B CB  1 
ATOM   2611  C CG  . TRP B 2 14  ? -0.643  30.917  33.851  1.00 74.70  ? 14  TRP B CG  1 
ATOM   2612  C CD1 . TRP B 2 14  ? 0.394   31.753  34.142  1.00 75.39  ? 14  TRP B CD1 1 
ATOM   2613  C CD2 . TRP B 2 14  ? -1.338  31.504  32.751  1.00 68.89  ? 14  TRP B CD2 1 
ATOM   2614  N NE1 . TRP B 2 14  ? 0.382   32.826  33.290  1.00 74.22  ? 14  TRP B NE1 1 
ATOM   2615  C CE2 . TRP B 2 14  ? -0.673  32.694  32.425  1.00 69.99  ? 14  TRP B CE2 1 
ATOM   2616  C CE3 . TRP B 2 14  ? -2.463  31.134  32.008  1.00 68.93  ? 14  TRP B CE3 1 
ATOM   2617  C CZ2 . TRP B 2 14  ? -1.093  33.520  31.390  1.00 69.37  ? 14  TRP B CZ2 1 
ATOM   2618  C CZ3 . TRP B 2 14  ? -2.880  31.950  30.983  1.00 68.86  ? 14  TRP B CZ3 1 
ATOM   2619  C CH2 . TRP B 2 14  ? -2.198  33.130  30.682  1.00 70.67  ? 14  TRP B CH2 1 
ATOM   2620  N N   . GLN B 2 15  ? 0.238   27.565  37.215  1.00 91.58  ? 15  GLN B N   1 
ATOM   2621  C CA  . GLN B 2 15  ? -0.245  26.503  38.086  1.00 102.69 ? 15  GLN B CA  1 
ATOM   2622  C C   . GLN B 2 15  ? -1.763  26.591  38.209  1.00 111.07 ? 15  GLN B C   1 
ATOM   2623  O O   . GLN B 2 15  ? -2.463  25.586  38.100  1.00 117.77 ? 15  GLN B O   1 
ATOM   2624  C CB  . GLN B 2 15  ? 0.400   26.605  39.468  1.00 109.11 ? 15  GLN B CB  1 
ATOM   2625  C CG  . GLN B 2 15  ? 1.914   26.465  39.463  1.00 106.98 ? 15  GLN B CG  1 
ATOM   2626  C CD  . GLN B 2 15  ? 2.374   25.065  39.096  1.00 107.19 ? 15  GLN B CD  1 
ATOM   2627  O OE1 . GLN B 2 15  ? 1.908   24.073  39.663  1.00 109.65 ? 15  GLN B OE1 1 
ATOM   2628  N NE2 . GLN B 2 15  ? 3.292   24.978  38.137  1.00 104.00 ? 15  GLN B NE2 1 
ATOM   2629  N N   . GLY B 2 16  ? -2.259  27.807  38.423  1.00 156.94 ? 16  GLY B N   1 
ATOM   2630  C CA  . GLY B 2 16  ? -3.680  28.049  38.604  1.00 165.10 ? 16  GLY B CA  1 
ATOM   2631  C C   . GLY B 2 16  ? -4.566  27.339  37.600  1.00 164.42 ? 16  GLY B C   1 
ATOM   2632  O O   . GLY B 2 16  ? -5.535  26.680  37.975  1.00 174.74 ? 16  GLY B O   1 
ATOM   2633  N N   . MET B 2 17  ? -4.240  27.477  36.319  1.00 116.04 ? 17  MET B N   1 
ATOM   2634  C CA  . MET B 2 17  ? -4.997  26.819  35.263  1.00 116.41 ? 17  MET B CA  1 
ATOM   2635  C C   . MET B 2 17  ? -4.920  25.305  35.428  1.00 125.04 ? 17  MET B C   1 
ATOM   2636  O O   . MET B 2 17  ? -3.843  24.763  35.677  1.00 126.73 ? 17  MET B O   1 
ATOM   2637  C CB  . MET B 2 17  ? -4.458  27.235  33.897  1.00 103.65 ? 17  MET B CB  1 
ATOM   2638  C CG  . MET B 2 17  ? -5.214  26.655  32.724  1.00 101.65 ? 17  MET B CG  1 
ATOM   2639  S SD  . MET B 2 17  ? -4.912  27.604  31.224  1.00 84.32  ? 17  MET B SD  1 
ATOM   2640  C CE  . MET B 2 17  ? -3.193  28.039  31.456  1.00 83.65  ? 17  MET B CE  1 
ATOM   2641  N N   . VAL B 2 18  ? -6.058  24.625  35.302  1.00 102.35 ? 18  VAL B N   1 
ATOM   2642  C CA  . VAL B 2 18  ? -6.105  23.178  35.515  1.00 101.62 ? 18  VAL B CA  1 
ATOM   2643  C C   . VAL B 2 18  ? -6.926  22.443  34.455  1.00 104.74 ? 18  VAL B C   1 
ATOM   2644  O O   . VAL B 2 18  ? -6.856  21.217  34.342  1.00 107.32 ? 18  VAL B O   1 
ATOM   2645  C CB  . VAL B 2 18  ? -6.673  22.830  36.907  1.00 103.69 ? 18  VAL B CB  1 
ATOM   2646  C CG1 . VAL B 2 18  ? -5.836  23.473  38.000  1.00 100.18 ? 18  VAL B CG1 1 
ATOM   2647  C CG2 . VAL B 2 18  ? -8.123  23.268  37.011  1.00 110.20 ? 18  VAL B CG2 1 
ATOM   2648  N N   . ASP B 2 19  ? -7.697  23.197  33.680  1.00 127.05 ? 19  ASP B N   1 
ATOM   2649  C CA  . ASP B 2 19  ? -8.620  22.611  32.716  1.00 129.02 ? 19  ASP B CA  1 
ATOM   2650  C C   . ASP B 2 19  ? -8.051  22.542  31.301  1.00 120.84 ? 19  ASP B C   1 
ATOM   2651  O O   . ASP B 2 19  ? -8.801  22.401  30.335  1.00 120.66 ? 19  ASP B O   1 
ATOM   2652  C CB  . ASP B 2 19  ? -9.930  23.400  32.700  1.00 135.89 ? 19  ASP B CB  1 
ATOM   2653  C CG  . ASP B 2 19  ? -9.723  24.865  32.353  1.00 132.32 ? 19  ASP B CG  1 
ATOM   2654  O OD1 . ASP B 2 19  ? -8.716  25.448  32.810  1.00 129.77 ? 19  ASP B OD1 1 
ATOM   2655  O OD2 . ASP B 2 19  ? -10.562 25.432  31.618  1.00 130.41 ? 19  ASP B OD2 1 
ATOM   2656  N N   . GLY B 2 20  ? -6.733  22.644  31.173  1.00 152.17 ? 20  GLY B N   1 
ATOM   2657  C CA  . GLY B 2 20  ? -6.108  22.585  29.863  1.00 145.23 ? 20  GLY B CA  1 
ATOM   2658  C C   . GLY B 2 20  ? -4.624  22.895  29.862  1.00 132.79 ? 20  GLY B C   1 
ATOM   2659  O O   . GLY B 2 20  ? -4.027  23.139  30.910  1.00 135.51 ? 20  GLY B O   1 
ATOM   2660  N N   . TRP B 2 21  ? -4.030  22.886  28.672  1.00 106.86 ? 21  TRP B N   1 
ATOM   2661  C CA  . TRP B 2 21  ? -2.606  23.158  28.514  1.00 98.26  ? 21  TRP B CA  1 
ATOM   2662  C C   . TRP B 2 21  ? -2.363  24.585  28.037  1.00 97.80  ? 21  TRP B C   1 
ATOM   2663  O O   . TRP B 2 21  ? -1.359  25.199  28.384  1.00 97.66  ? 21  TRP B O   1 
ATOM   2664  C CB  . TRP B 2 21  ? -1.981  22.175  27.523  1.00 97.44  ? 21  TRP B CB  1 
ATOM   2665  C CG  . TRP B 2 21  ? -1.671  20.816  28.091  1.00 102.11 ? 21  TRP B CG  1 
ATOM   2666  C CD1 . TRP B 2 21  ? -1.224  20.526  29.351  1.00 106.20 ? 21  TRP B CD1 1 
ATOM   2667  C CD2 . TRP B 2 21  ? -1.784  19.561  27.408  1.00 102.53 ? 21  TRP B CD2 1 
ATOM   2668  N NE1 . TRP B 2 21  ? -1.048  19.167  29.491  1.00 109.24 ? 21  TRP B NE1 1 
ATOM   2669  C CE2 . TRP B 2 21  ? -1.387  18.554  28.313  1.00 104.86 ? 21  TRP B CE2 1 
ATOM   2670  C CE3 . TRP B 2 21  ? -2.180  19.193  26.115  1.00 98.58  ? 21  TRP B CE3 1 
ATOM   2671  C CZ2 . TRP B 2 21  ? -1.378  17.205  27.968  1.00 98.30  ? 21  TRP B CZ2 1 
ATOM   2672  C CZ3 . TRP B 2 21  ? -2.170  17.858  25.773  1.00 95.26  ? 21  TRP B CZ3 1 
ATOM   2673  C CH2 . TRP B 2 21  ? -1.772  16.877  26.695  1.00 96.08  ? 21  TRP B CH2 1 
ATOM   2674  N N   . TYR B 2 22  ? -3.280  25.102  27.226  1.00 111.53 ? 22  TYR B N   1 
ATOM   2675  C CA  . TYR B 2 22  ? -3.179  26.466  26.717  1.00 109.51 ? 22  TYR B CA  1 
ATOM   2676  C C   . TYR B 2 22  ? -4.387  27.278  27.186  1.00 122.05 ? 22  TYR B C   1 
ATOM   2677  O O   . TYR B 2 22  ? -5.518  26.792  27.154  1.00 130.73 ? 22  TYR B O   1 
ATOM   2678  C CB  . TYR B 2 22  ? -3.122  26.460  25.188  1.00 100.63 ? 22  TYR B CB  1 
ATOM   2679  C CG  . TYR B 2 22  ? -2.281  25.351  24.599  1.00 95.05  ? 22  TYR B CG  1 
ATOM   2680  C CD1 . TYR B 2 22  ? -1.101  24.945  25.209  1.00 92.34  ? 22  TYR B CD1 1 
ATOM   2681  C CD2 . TYR B 2 22  ? -2.674  24.703  23.436  1.00 97.78  ? 22  TYR B CD2 1 
ATOM   2682  C CE1 . TYR B 2 22  ? -0.334  23.924  24.672  1.00 87.31  ? 22  TYR B CE1 1 
ATOM   2683  C CE2 . TYR B 2 22  ? -1.916  23.684  22.893  1.00 92.54  ? 22  TYR B CE2 1 
ATOM   2684  C CZ  . TYR B 2 22  ? -0.747  23.299  23.513  1.00 89.63  ? 22  TYR B CZ  1 
ATOM   2685  O OH  . TYR B 2 22  ? 0.007   22.285  22.968  1.00 92.26  ? 22  TYR B OH  1 
ATOM   2686  N N   . GLY B 2 23  ? -4.160  28.516  27.613  1.00 114.64 ? 23  GLY B N   1 
ATOM   2687  C CA  . GLY B 2 23  ? -5.249  29.305  28.155  1.00 121.34 ? 23  GLY B CA  1 
ATOM   2688  C C   . GLY B 2 23  ? -5.156  30.812  28.010  1.00 118.36 ? 23  GLY B C   1 
ATOM   2689  O O   . GLY B 2 23  ? -4.439  31.334  27.155  1.00 114.87 ? 23  GLY B O   1 
ATOM   2690  N N   . TYR B 2 24  ? -5.907  31.503  28.864  1.00 94.38  ? 24  TYR B N   1 
ATOM   2691  C CA  . TYR B 2 24  ? -5.990  32.956  28.861  1.00 92.05  ? 24  TYR B CA  1 
ATOM   2692  C C   . TYR B 2 24  ? -5.892  33.498  30.290  1.00 95.65  ? 24  TYR B C   1 
ATOM   2693  O O   . TYR B 2 24  ? -5.838  32.730  31.252  1.00 94.58  ? 24  TYR B O   1 
ATOM   2694  C CB  . TYR B 2 24  ? -7.317  33.411  28.250  1.00 93.81  ? 24  TYR B CB  1 
ATOM   2695  C CG  . TYR B 2 24  ? -7.573  32.977  26.820  1.00 87.05  ? 24  TYR B CG  1 
ATOM   2696  C CD1 . TYR B 2 24  ? -7.085  33.720  25.748  1.00 80.56  ? 24  TYR B CD1 1 
ATOM   2697  C CD2 . TYR B 2 24  ? -8.338  31.850  26.542  1.00 87.10  ? 24  TYR B CD2 1 
ATOM   2698  C CE1 . TYR B 2 24  ? -7.334  33.340  24.436  1.00 79.14  ? 24  TYR B CE1 1 
ATOM   2699  C CE2 . TYR B 2 24  ? -8.592  31.460  25.234  1.00 86.62  ? 24  TYR B CE2 1 
ATOM   2700  C CZ  . TYR B 2 24  ? -8.085  32.209  24.185  1.00 83.19  ? 24  TYR B CZ  1 
ATOM   2701  O OH  . TYR B 2 24  ? -8.331  31.832  22.882  1.00 84.86  ? 24  TYR B OH  1 
ATOM   2702  N N   . HIS B 2 25  ? -5.881  34.823  30.419  1.00 127.91 ? 25  HIS B N   1 
ATOM   2703  C CA  . HIS B 2 25  ? -5.847  35.482  31.727  1.00 140.26 ? 25  HIS B CA  1 
ATOM   2704  C C   . HIS B 2 25  ? -6.448  36.892  31.666  1.00 144.42 ? 25  HIS B C   1 
ATOM   2705  O O   . HIS B 2 25  ? -5.941  37.765  30.958  1.00 139.89 ? 25  HIS B O   1 
ATOM   2706  C CB  . HIS B 2 25  ? -4.416  35.538  32.265  1.00 141.38 ? 25  HIS B CB  1 
ATOM   2707  C CG  . HIS B 2 25  ? -4.302  36.166  33.620  1.00 152.91 ? 25  HIS B CG  1 
ATOM   2708  N ND1 . HIS B 2 25  ? -5.018  35.721  34.710  1.00 162.28 ? 25  HIS B ND1 1 
ATOM   2709  C CD2 . HIS B 2 25  ? -3.552  37.204  34.060  1.00 156.06 ? 25  HIS B CD2 1 
ATOM   2710  C CE1 . HIS B 2 25  ? -4.715  36.458  35.764  1.00 166.78 ? 25  HIS B CE1 1 
ATOM   2711  N NE2 . HIS B 2 25  ? -3.828  37.365  35.396  1.00 163.96 ? 25  HIS B NE2 1 
ATOM   2712  N N   . HIS B 2 26  ? -7.527  37.107  32.415  1.00 111.13 ? 26  HIS B N   1 
ATOM   2713  C CA  . HIS B 2 26  ? -8.243  38.380  32.386  1.00 113.59 ? 26  HIS B CA  1 
ATOM   2714  C C   . HIS B 2 26  ? -8.007  39.192  33.654  1.00 118.97 ? 26  HIS B C   1 
ATOM   2715  O O   . HIS B 2 26  ? -7.899  38.636  34.749  1.00 122.76 ? 26  HIS B O   1 
ATOM   2716  C CB  . HIS B 2 26  ? -9.747  38.150  32.206  1.00 118.01 ? 26  HIS B CB  1 
ATOM   2717  C CG  . HIS B 2 26  ? -10.453 37.756  33.467  1.00 123.22 ? 26  HIS B CG  1 
ATOM   2718  N ND1 . HIS B 2 26  ? -10.792 36.452  33.755  1.00 124.05 ? 26  HIS B ND1 1 
ATOM   2719  C CD2 . HIS B 2 26  ? -10.884 38.495  34.517  1.00 129.72 ? 26  HIS B CD2 1 
ATOM   2720  C CE1 . HIS B 2 26  ? -11.402 36.405  34.925  1.00 131.00 ? 26  HIS B CE1 1 
ATOM   2721  N NE2 . HIS B 2 26  ? -11.470 37.631  35.410  1.00 134.84 ? 26  HIS B NE2 1 
ATOM   2722  N N   . SER B 2 27  ? -7.937  40.511  33.496  1.00 110.13 ? 27  SER B N   1 
ATOM   2723  C CA  . SER B 2 27  ? -7.822  41.414  34.634  1.00 116.40 ? 27  SER B CA  1 
ATOM   2724  C C   . SER B 2 27  ? -8.625  42.688  34.375  1.00 125.70 ? 27  SER B C   1 
ATOM   2725  O O   . SER B 2 27  ? -8.095  43.798  34.455  1.00 127.56 ? 27  SER B O   1 
ATOM   2726  C CB  . SER B 2 27  ? -6.356  41.747  34.918  1.00 105.47 ? 27  SER B CB  1 
ATOM   2727  O OG  . SER B 2 27  ? -6.147  41.994  36.298  1.00 105.84 ? 27  SER B OG  1 
ATOM   2728  N N   . ASN B 2 28  ? -9.905  42.513  34.052  1.00 119.90 ? 28  ASN B N   1 
ATOM   2729  C CA  . ASN B 2 28  ? -10.805 43.639  33.828  1.00 118.29 ? 28  ASN B CA  1 
ATOM   2730  C C   . ASN B 2 28  ? -11.342 44.194  35.143  1.00 121.88 ? 28  ASN B C   1 
ATOM   2731  O O   . ASN B 2 28  ? -10.719 44.030  36.193  1.00 124.02 ? 28  ASN B O   1 
ATOM   2732  C CB  . ASN B 2 28  ? -11.962 43.240  32.909  1.00 120.03 ? 28  ASN B CB  1 
ATOM   2733  C CG  . ASN B 2 28  ? -12.797 42.109  33.478  1.00 126.30 ? 28  ASN B CG  1 
ATOM   2734  O OD1 . ASN B 2 28  ? -12.540 41.622  34.581  1.00 126.39 ? 28  ASN B OD1 1 
ATOM   2735  N ND2 . ASN B 2 28  ? -13.810 41.689  32.729  1.00 130.96 ? 28  ASN B ND2 1 
ATOM   2736  N N   . ASP B 2 29  ? -12.500 44.845  35.083  1.00 130.74 ? 29  ASP B N   1 
ATOM   2737  C CA  . ASP B 2 29  ? -13.098 45.447  36.271  1.00 134.09 ? 29  ASP B CA  1 
ATOM   2738  C C   . ASP B 2 29  ? -13.905 44.439  37.093  1.00 141.84 ? 29  ASP B C   1 
ATOM   2739  O O   . ASP B 2 29  ? -14.492 44.790  38.117  1.00 147.32 ? 29  ASP B O   1 
ATOM   2740  C CB  . ASP B 2 29  ? -13.968 46.650  35.890  1.00 134.10 ? 29  ASP B CB  1 
ATOM   2741  C CG  . ASP B 2 29  ? -13.147 47.846  35.427  1.00 125.18 ? 29  ASP B CG  1 
ATOM   2742  O OD1 . ASP B 2 29  ? -12.043 48.064  35.972  1.00 119.57 ? 29  ASP B OD1 1 
ATOM   2743  O OD2 . ASP B 2 29  ? -13.608 48.571  34.519  1.00 124.00 ? 29  ASP B OD2 1 
ATOM   2744  N N   . GLN B 2 30  ? -13.930 43.188  36.639  1.00 135.84 ? 30  GLN B N   1 
ATOM   2745  C CA  . GLN B 2 30  ? -14.605 42.119  37.369  1.00 146.61 ? 30  GLN B CA  1 
ATOM   2746  C C   . GLN B 2 30  ? -13.616 41.063  37.856  1.00 153.63 ? 30  GLN B C   1 
ATOM   2747  O O   . GLN B 2 30  ? -13.792 39.872  37.601  1.00 155.45 ? 30  GLN B O   1 
ATOM   2748  C CB  . GLN B 2 30  ? -15.686 41.461  36.508  1.00 143.46 ? 30  GLN B CB  1 
ATOM   2749  C CG  . GLN B 2 30  ? -16.882 42.349  36.220  1.00 145.12 ? 30  GLN B CG  1 
ATOM   2750  C CD  . GLN B 2 30  ? -16.530 43.535  35.346  1.00 134.80 ? 30  GLN B CD  1 
ATOM   2751  O OE1 . GLN B 2 30  ? -16.094 43.374  34.207  1.00 131.60 ? 30  GLN B OE1 1 
ATOM   2752  N NE2 . GLN B 2 30  ? -16.711 44.737  35.879  1.00 129.11 ? 30  GLN B NE2 1 
ATOM   2753  N N   . GLY B 2 31  ? -12.573 41.509  38.550  1.00 189.48 ? 31  GLY B N   1 
ATOM   2754  C CA  . GLY B 2 31  ? -11.613 40.606  39.158  1.00 186.75 ? 31  GLY B CA  1 
ATOM   2755  C C   . GLY B 2 31  ? -10.652 39.944  38.188  1.00 176.01 ? 31  GLY B C   1 
ATOM   2756  O O   . GLY B 2 31  ? -10.240 40.546  37.195  1.00 164.18 ? 31  GLY B O   1 
ATOM   2757  N N   . SER B 2 32  ? -10.294 38.697  38.487  1.00 145.70 ? 32  SER B N   1 
ATOM   2758  C CA  . SER B 2 32  ? -9.340  37.942  37.682  1.00 137.80 ? 32  SER B CA  1 
ATOM   2759  C C   . SER B 2 32  ? -9.551  36.435  37.822  1.00 141.27 ? 32  SER B C   1 
ATOM   2760  O O   . SER B 2 32  ? -10.173 35.969  38.779  1.00 147.48 ? 32  SER B O   1 
ATOM   2761  C CB  . SER B 2 32  ? -7.906  38.307  38.073  1.00 130.50 ? 32  SER B CB  1 
ATOM   2762  O OG  . SER B 2 32  ? -7.662  38.023  39.440  1.00 132.47 ? 32  SER B OG  1 
ATOM   2763  N N   . GLY B 2 33  ? -9.025  35.679  36.862  1.00 192.14 ? 33  GLY B N   1 
ATOM   2764  C CA  . GLY B 2 33  ? -9.147  34.232  36.864  1.00 189.01 ? 33  GLY B CA  1 
ATOM   2765  C C   . GLY B 2 33  ? -8.460  33.597  35.667  1.00 177.04 ? 33  GLY B C   1 
ATOM   2766  O O   . GLY B 2 33  ? -7.892  34.299  34.828  1.00 168.93 ? 33  GLY B O   1 
ATOM   2767  N N   . TYR B 2 34  ? -8.510  32.268  35.590  1.00 122.12 ? 34  TYR B N   1 
ATOM   2768  C CA  . TYR B 2 34  ? -7.889  31.531  34.488  1.00 109.18 ? 34  TYR B CA  1 
ATOM   2769  C C   . TYR B 2 34  ? -8.922  30.771  33.664  1.00 111.58 ? 34  TYR B C   1 
ATOM   2770  O O   . TYR B 2 34  ? -9.982  30.400  34.171  1.00 119.79 ? 34  TYR B O   1 
ATOM   2771  C CB  . TYR B 2 34  ? -6.836  30.556  35.013  1.00 97.88  ? 34  TYR B CB  1 
ATOM   2772  C CG  . TYR B 2 34  ? -5.677  31.221  35.716  1.00 94.26  ? 34  TYR B CG  1 
ATOM   2773  C CD1 . TYR B 2 34  ? -4.568  31.659  35.007  1.00 91.22  ? 34  TYR B CD1 1 
ATOM   2774  C CD2 . TYR B 2 34  ? -5.691  31.409  37.092  1.00 100.53 ? 34  TYR B CD2 1 
ATOM   2775  C CE1 . TYR B 2 34  ? -3.501  32.268  35.650  1.00 91.37  ? 34  TYR B CE1 1 
ATOM   2776  C CE2 . TYR B 2 34  ? -4.631  32.016  37.742  1.00 100.74 ? 34  TYR B CE2 1 
ATOM   2777  C CZ  . TYR B 2 34  ? -3.541  32.443  37.017  1.00 95.46  ? 34  TYR B CZ  1 
ATOM   2778  O OH  . TYR B 2 34  ? -2.487  33.044  37.662  1.00 93.76  ? 34  TYR B OH  1 
ATOM   2779  N N   . ALA B 2 35  ? -8.603  30.539  32.393  1.00 148.31 ? 35  ALA B N   1 
ATOM   2780  C CA  . ALA B 2 35  ? -9.501  29.819  31.497  1.00 152.36 ? 35  ALA B CA  1 
ATOM   2781  C C   . ALA B 2 35  ? -8.764  29.247  30.290  1.00 145.73 ? 35  ALA B C   1 
ATOM   2782  O O   . ALA B 2 35  ? -8.294  29.993  29.430  1.00 144.32 ? 35  ALA B O   1 
ATOM   2783  C CB  . ALA B 2 35  ? -10.638 30.722  31.044  1.00 159.13 ? 35  ALA B CB  1 
ATOM   2784  N N   . ALA B 2 36  ? -8.675  27.921  30.229  1.00 107.03 ? 36  ALA B N   1 
ATOM   2785  C CA  . ALA B 2 36  ? -8.006  27.242  29.123  1.00 97.83  ? 36  ALA B CA  1 
ATOM   2786  C C   . ALA B 2 36  ? -8.796  27.377  27.825  1.00 96.82  ? 36  ALA B C   1 
ATOM   2787  O O   . ALA B 2 36  ? -9.938  27.834  27.826  1.00 105.98 ? 36  ALA B O   1 
ATOM   2788  C CB  . ALA B 2 36  ? -7.790  25.776  29.460  1.00 96.17  ? 36  ALA B CB  1 
ATOM   2789  N N   . ASP B 2 37  ? -8.184  26.973  26.718  1.00 108.33 ? 37  ASP B N   1 
ATOM   2790  C CA  . ASP B 2 37  ? -8.845  27.039  25.422  1.00 108.06 ? 37  ASP B CA  1 
ATOM   2791  C C   . ASP B 2 37  ? -9.176  25.644  24.891  1.00 114.95 ? 37  ASP B C   1 
ATOM   2792  O O   . ASP B 2 37  ? -8.283  24.836  24.641  1.00 110.38 ? 37  ASP B O   1 
ATOM   2793  C CB  . ASP B 2 37  ? -7.975  27.792  24.416  1.00 97.88  ? 37  ASP B CB  1 
ATOM   2794  C CG  . ASP B 2 37  ? -8.705  28.080  23.121  1.00 99.85  ? 37  ASP B CG  1 
ATOM   2795  O OD1 . ASP B 2 37  ? -9.897  28.453  23.182  1.00 109.58 ? 37  ASP B OD1 1 
ATOM   2796  O OD2 . ASP B 2 37  ? -8.092  27.928  22.043  1.00 91.16  ? 37  ASP B OD2 1 
ATOM   2797  N N   . LYS B 2 38  ? -10.464 25.370  24.714  1.00 120.48 ? 38  LYS B N   1 
ATOM   2798  C CA  . LYS B 2 38  ? -10.915 24.068  24.233  1.00 121.59 ? 38  LYS B CA  1 
ATOM   2799  C C   . LYS B 2 38  ? -10.366 23.745  22.840  1.00 116.54 ? 38  LYS B C   1 
ATOM   2800  O O   . LYS B 2 38  ? -9.606  22.793  22.676  1.00 114.68 ? 38  LYS B O   1 
ATOM   2801  C CB  . LYS B 2 38  ? -12.447 24.003  24.236  1.00 134.72 ? 38  LYS B CB  1 
ATOM   2802  C CG  . LYS B 2 38  ? -13.027 22.616  23.989  1.00 139.80 ? 38  LYS B CG  1 
ATOM   2803  C CD  . LYS B 2 38  ? -14.541 22.599  24.191  1.00 146.46 ? 38  LYS B CD  1 
ATOM   2804  C CE  . LYS B 2 38  ? -15.106 21.192  24.032  1.00 149.63 ? 38  LYS B CE  1 
ATOM   2805  N NZ  . LYS B 2 38  ? -16.577 21.137  24.263  1.00 160.22 ? 38  LYS B NZ  1 
ATOM   2806  N N   . GLU B 2 39  ? -10.743 24.552  21.850  1.00 149.21 ? 39  GLU B N   1 
ATOM   2807  C CA  . GLU B 2 39  ? -10.400 24.299  20.445  1.00 148.23 ? 39  GLU B CA  1 
ATOM   2808  C C   . GLU B 2 39  ? -8.927  23.996  20.161  1.00 142.36 ? 39  GLU B C   1 
ATOM   2809  O O   . GLU B 2 39  ? -8.608  23.365  19.154  1.00 146.09 ? 39  GLU B O   1 
ATOM   2810  C CB  . GLU B 2 39  ? -10.852 25.465  19.555  1.00 152.53 ? 39  GLU B CB  1 
ATOM   2811  C CG  . GLU B 2 39  ? -12.343 25.496  19.259  1.00 166.41 ? 39  GLU B CG  1 
ATOM   2812  C CD  . GLU B 2 39  ? -13.098 26.454  20.157  1.00 177.62 ? 39  GLU B CD  1 
ATOM   2813  O OE1 . GLU B 2 39  ? -12.475 27.409  20.669  1.00 175.24 ? 39  GLU B OE1 1 
ATOM   2814  O OE2 . GLU B 2 39  ? -14.316 26.254  20.350  1.00 185.47 ? 39  GLU B OE2 1 
ATOM   2815  N N   . SER B 2 40  ? -8.030  24.452  21.028  1.00 144.96 ? 40  SER B N   1 
ATOM   2816  C CA  . SER B 2 40  ? -6.600  24.283  20.779  1.00 133.62 ? 40  SER B CA  1 
ATOM   2817  C C   . SER B 2 40  ? -5.922  23.351  21.779  1.00 127.90 ? 40  SER B C   1 
ATOM   2818  O O   . SER B 2 40  ? -4.800  22.902  21.550  1.00 124.72 ? 40  SER B O   1 
ATOM   2819  C CB  . SER B 2 40  ? -5.889  25.635  20.770  1.00 127.03 ? 40  SER B CB  1 
ATOM   2820  O OG  . SER B 2 40  ? -5.802  26.170  22.078  1.00 125.07 ? 40  SER B OG  1 
ATOM   2821  N N   . THR B 2 41  ? -6.595  23.072  22.890  1.00 90.85  ? 41  THR B N   1 
ATOM   2822  C CA  . THR B 2 41  ? -6.056  22.152  23.880  1.00 81.93  ? 41  THR B CA  1 
ATOM   2823  C C   . THR B 2 41  ? -6.546  20.743  23.572  1.00 82.54  ? 41  THR B C   1 
ATOM   2824  O O   . THR B 2 41  ? -6.178  19.784  24.251  1.00 81.54  ? 41  THR B O   1 
ATOM   2825  C CB  . THR B 2 41  ? -6.466  22.546  25.313  1.00 83.66  ? 41  THR B CB  1 
ATOM   2826  O OG1 . THR B 2 41  ? -5.505  22.046  26.253  1.00 76.09  ? 41  THR B OG1 1 
ATOM   2827  C CG2 . THR B 2 41  ? -7.845  21.994  25.649  1.00 100.00 ? 41  THR B CG2 1 
ATOM   2828  N N   . GLN B 2 42  ? -7.379  20.628  22.542  1.00 96.40  ? 42  GLN B N   1 
ATOM   2829  C CA  . GLN B 2 42  ? -7.904  19.334  22.121  1.00 100.52 ? 42  GLN B CA  1 
ATOM   2830  C C   . GLN B 2 42  ? -7.277  18.917  20.799  1.00 91.09  ? 42  GLN B C   1 
ATOM   2831  O O   . GLN B 2 42  ? -7.093  17.729  20.541  1.00 87.05  ? 42  GLN B O   1 
ATOM   2832  C CB  . GLN B 2 42  ? -9.431  19.370  22.004  1.00 109.90 ? 42  GLN B CB  1 
ATOM   2833  C CG  . GLN B 2 42  ? -10.081 18.007  21.779  1.00 116.94 ? 42  GLN B CG  1 
ATOM   2834  C CD  . GLN B 2 42  ? -9.989  17.095  22.995  1.00 117.59 ? 42  GLN B CD  1 
ATOM   2835  O OE1 . GLN B 2 42  ? -9.458  17.477  24.038  1.00 121.22 ? 42  GLN B OE1 1 
ATOM   2836  N NE2 . GLN B 2 42  ? -10.513 15.881  22.862  1.00 111.93 ? 42  GLN B NE2 1 
ATOM   2837  N N   . LYS B 2 43  ? -6.955  19.897  19.960  1.00 93.17  ? 43  LYS B N   1 
ATOM   2838  C CA  . LYS B 2 43  ? -6.174  19.623  18.762  1.00 93.50  ? 43  LYS B CA  1 
ATOM   2839  C C   . LYS B 2 43  ? -4.823  19.058  19.195  1.00 89.04  ? 43  LYS B C   1 
ATOM   2840  O O   . LYS B 2 43  ? -4.265  18.166  18.550  1.00 87.90  ? 43  LYS B O   1 
ATOM   2841  C CB  . LYS B 2 43  ? -5.981  20.891  17.928  1.00 97.08  ? 43  LYS B CB  1 
ATOM   2842  C CG  . LYS B 2 43  ? -4.903  20.762  16.856  1.00 99.30  ? 43  LYS B CG  1 
ATOM   2843  C CD  . LYS B 2 43  ? -4.700  22.065  16.092  1.00 103.24 ? 43  LYS B CD  1 
ATOM   2844  C CE  . LYS B 2 43  ? -3.440  22.019  15.229  1.00 97.84  ? 43  LYS B CE  1 
ATOM   2845  N NZ  . LYS B 2 43  ? -3.450  20.901  14.240  1.00 96.84  ? 43  LYS B NZ  1 
ATOM   2846  N N   . ALA B 2 44  ? -4.313  19.579  20.306  1.00 110.37 ? 44  ALA B N   1 
ATOM   2847  C CA  . ALA B 2 44  ? -3.048  19.119  20.860  1.00 106.64 ? 44  ALA B CA  1 
ATOM   2848  C C   . ALA B 2 44  ? -3.151  17.662  21.267  1.00 105.56 ? 44  ALA B C   1 
ATOM   2849  O O   . ALA B 2 44  ? -2.615  16.780  20.595  1.00 97.55  ? 44  ALA B O   1 
ATOM   2850  C CB  . ALA B 2 44  ? -2.658  19.971  22.057  1.00 108.76 ? 44  ALA B CB  1 
ATOM   2851  N N   . PHE B 2 45  ? -3.856  17.425  22.369  1.00 98.75  ? 45  PHE B N   1 
ATOM   2852  C CA  . PHE B 2 45  ? -4.011  16.089  22.937  1.00 101.69 ? 45  PHE B CA  1 
ATOM   2853  C C   . PHE B 2 45  ? -4.310  15.010  21.893  1.00 99.31  ? 45  PHE B C   1 
ATOM   2854  O O   . PHE B 2 45  ? -3.848  13.878  22.022  1.00 96.30  ? 45  PHE B O   1 
ATOM   2855  C CB  . PHE B 2 45  ? -5.104  16.097  24.008  1.00 110.95 ? 45  PHE B CB  1 
ATOM   2856  C CG  . PHE B 2 45  ? -5.213  14.811  24.775  1.00 112.36 ? 45  PHE B CG  1 
ATOM   2857  C CD1 . PHE B 2 45  ? -4.489  14.625  25.941  1.00 109.19 ? 45  PHE B CD1 1 
ATOM   2858  C CD2 . PHE B 2 45  ? -6.040  13.793  24.334  1.00 118.37 ? 45  PHE B CD2 1 
ATOM   2859  C CE1 . PHE B 2 45  ? -4.586  13.447  26.652  1.00 111.53 ? 45  PHE B CE1 1 
ATOM   2860  C CE2 . PHE B 2 45  ? -6.141  12.612  25.040  1.00 120.63 ? 45  PHE B CE2 1 
ATOM   2861  C CZ  . PHE B 2 45  ? -5.412  12.438  26.202  1.00 118.43 ? 45  PHE B CZ  1 
ATOM   2862  N N   . ASP B 2 46  ? -5.084  15.356  20.869  1.00 90.26  ? 46  ASP B N   1 
ATOM   2863  C CA  . ASP B 2 46  ? -5.432  14.403  19.818  1.00 92.06  ? 46  ASP B CA  1 
ATOM   2864  C C   . ASP B 2 46  ? -4.206  13.955  19.029  1.00 93.86  ? 46  ASP B C   1 
ATOM   2865  O O   . ASP B 2 46  ? -3.956  12.759  18.880  1.00 100.37 ? 46  ASP B O   1 
ATOM   2866  C CB  . ASP B 2 46  ? -6.475  14.999  18.871  1.00 95.58  ? 46  ASP B CB  1 
ATOM   2867  C CG  . ASP B 2 46  ? -7.889  14.838  19.387  1.00 101.49 ? 46  ASP B CG  1 
ATOM   2868  O OD1 . ASP B 2 46  ? -8.052  14.379  20.539  1.00 102.67 ? 46  ASP B OD1 1 
ATOM   2869  O OD2 . ASP B 2 46  ? -8.835  15.175  18.642  1.00 104.95 ? 46  ASP B OD2 1 
ATOM   2870  N N   . GLY B 2 47  ? -3.442  14.920  18.528  1.00 97.32  ? 47  GLY B N   1 
ATOM   2871  C CA  . GLY B 2 47  ? -2.271  14.624  17.721  1.00 85.87  ? 47  GLY B CA  1 
ATOM   2872  C C   . GLY B 2 47  ? -1.057  14.209  18.529  1.00 71.58  ? 47  GLY B C   1 
ATOM   2873  O O   . GLY B 2 47  ? -0.020  13.870  17.969  1.00 74.38  ? 47  GLY B O   1 
ATOM   2874  N N   . ILE B 2 48  ? -1.177  14.258  19.849  1.00 69.66  ? 48  ILE B N   1 
ATOM   2875  C CA  . ILE B 2 48  ? -0.120  13.793  20.734  1.00 70.76  ? 48  ILE B CA  1 
ATOM   2876  C C   . ILE B 2 48  ? -0.460  12.377  21.199  1.00 83.85  ? 48  ILE B C   1 
ATOM   2877  O O   . ILE B 2 48  ? 0.428   11.545  21.399  1.00 86.60  ? 48  ILE B O   1 
ATOM   2878  C CB  . ILE B 2 48  ? 0.074   14.750  21.940  1.00 65.32  ? 48  ILE B CB  1 
ATOM   2879  C CG1 . ILE B 2 48  ? 1.061   15.862  21.589  1.00 66.92  ? 48  ILE B CG1 1 
ATOM   2880  C CG2 . ILE B 2 48  ? 0.595   14.012  23.159  1.00 57.07  ? 48  ILE B CG2 1 
ATOM   2881  C CD1 . ILE B 2 48  ? 2.497   15.393  21.488  1.00 61.42  ? 48  ILE B CD1 1 
ATOM   2882  N N   . THR B 2 49  ? -1.755  12.104  21.355  1.00 94.80  ? 49  THR B N   1 
ATOM   2883  C CA  . THR B 2 49  ? -2.221  10.760  21.675  1.00 90.04  ? 49  THR B CA  1 
ATOM   2884  C C   . THR B 2 49  ? -2.409  9.985   20.378  1.00 91.15  ? 49  THR B C   1 
ATOM   2885  O O   . THR B 2 49  ? -2.894  8.857   20.374  1.00 94.72  ? 49  THR B O   1 
ATOM   2886  C CB  . THR B 2 49  ? -3.534  10.778  22.487  1.00 95.29  ? 49  THR B CB  1 
ATOM   2887  O OG1 . THR B 2 49  ? -3.414  11.709  23.570  1.00 104.84 ? 49  THR B OG1 1 
ATOM   2888  C CG2 . THR B 2 49  ? -3.839  9.392   23.053  1.00 88.13  ? 49  THR B CG2 1 
ATOM   2889  N N   . ASN B 2 50  ? -2.037  10.613  19.269  1.00 74.31  ? 50  ASN B N   1 
ATOM   2890  C CA  . ASN B 2 50  ? -1.889  9.901   18.010  1.00 71.38  ? 50  ASN B CA  1 
ATOM   2891  C C   . ASN B 2 50  ? -0.418  9.845   17.639  1.00 69.57  ? 50  ASN B C   1 
ATOM   2892  O O   . ASN B 2 50  ? -0.054  9.339   16.584  1.00 71.52  ? 50  ASN B O   1 
ATOM   2893  C CB  . ASN B 2 50  ? -2.689  10.555  16.888  1.00 76.53  ? 50  ASN B CB  1 
ATOM   2894  C CG  . ASN B 2 50  ? -2.611  9.772   15.590  1.00 77.89  ? 50  ASN B CG  1 
ATOM   2895  O OD1 . ASN B 2 50  ? -3.338  8.799   15.399  1.00 84.85  ? 50  ASN B OD1 1 
ATOM   2896  N ND2 . ASN B 2 50  ? -1.720  10.188  14.695  1.00 73.15  ? 50  ASN B ND2 1 
ATOM   2897  N N   . LYS B 2 51  ? 0.427   10.384  18.512  1.00 91.99  ? 51  LYS B N   1 
ATOM   2898  C CA  . LYS B 2 51  ? 1.864   10.221  18.361  1.00 82.81  ? 51  LYS B CA  1 
ATOM   2899  C C   . LYS B 2 51  ? 2.314   8.986   19.125  1.00 79.44  ? 51  LYS B C   1 
ATOM   2900  O O   . LYS B 2 51  ? 3.092   8.186   18.613  1.00 86.54  ? 51  LYS B O   1 
ATOM   2901  C CB  . LYS B 2 51  ? 2.635   11.451  18.841  1.00 76.26  ? 51  LYS B CB  1 
ATOM   2902  C CG  . LYS B 2 51  ? 4.145   11.229  18.895  1.00 68.19  ? 51  LYS B CG  1 
ATOM   2903  C CD  . LYS B 2 51  ? 4.918   12.450  19.384  1.00 65.13  ? 51  LYS B CD  1 
ATOM   2904  C CE  . LYS B 2 51  ? 5.016   13.510  18.306  1.00 58.81  ? 51  LYS B CE  1 
ATOM   2905  N NZ  . LYS B 2 51  ? 5.991   14.585  18.638  1.00 53.29  ? 51  LYS B NZ  1 
ATOM   2906  N N   . VAL B 2 52  ? 1.821   8.820   20.348  1.00 69.24  ? 52  VAL B N   1 
ATOM   2907  C CA  . VAL B 2 52  ? 2.148   7.623   21.111  1.00 68.50  ? 52  VAL B CA  1 
ATOM   2908  C C   . VAL B 2 52  ? 1.482   6.398   20.495  1.00 68.16  ? 52  VAL B C   1 
ATOM   2909  O O   . VAL B 2 52  ? 2.055   5.310   20.490  1.00 66.86  ? 52  VAL B O   1 
ATOM   2910  C CB  . VAL B 2 52  ? 1.763   7.742   22.601  1.00 79.52  ? 52  VAL B CB  1 
ATOM   2911  C CG1 . VAL B 2 52  ? 2.534   8.875   23.260  1.00 74.29  ? 52  VAL B CG1 1 
ATOM   2912  C CG2 . VAL B 2 52  ? 0.264   7.939   22.762  1.00 95.79  ? 52  VAL B CG2 1 
ATOM   2913  N N   . ASN B 2 53  ? 0.275   6.579   19.968  1.00 90.08  ? 53  ASN B N   1 
ATOM   2914  C CA  . ASN B 2 53  ? -0.437  5.491   19.303  1.00 96.58  ? 53  ASN B CA  1 
ATOM   2915  C C   . ASN B 2 53  ? 0.088   5.271   17.889  1.00 100.68 ? 53  ASN B C   1 
ATOM   2916  O O   . ASN B 2 53  ? -0.548  4.601   17.078  1.00 110.75 ? 53  ASN B O   1 
ATOM   2917  C CB  . ASN B 2 53  ? -1.949  5.751   19.268  1.00 98.98  ? 53  ASN B CB  1 
ATOM   2918  C CG  . ASN B 2 53  ? -2.568  5.831   20.655  1.00 102.75 ? 53  ASN B CG  1 
ATOM   2919  O OD1 . ASN B 2 53  ? -1.929  5.504   21.656  1.00 98.18  ? 53  ASN B OD1 1 
ATOM   2920  N ND2 . ASN B 2 53  ? -3.825  6.261   20.716  1.00 104.22 ? 53  ASN B ND2 1 
ATOM   2921  N N   . SER B 2 54  ? 1.247   5.847   17.596  1.00 71.12  ? 54  SER B N   1 
ATOM   2922  C CA  . SER B 2 54  ? 1.901   5.626   16.316  1.00 61.87  ? 54  SER B CA  1 
ATOM   2923  C C   . SER B 2 54  ? 3.212   4.877   16.521  1.00 60.59  ? 54  SER B C   1 
ATOM   2924  O O   . SER B 2 54  ? 3.472   3.879   15.847  1.00 69.63  ? 54  SER B O   1 
ATOM   2925  C CB  . SER B 2 54  ? 2.143   6.947   15.587  1.00 63.96  ? 54  SER B CB  1 
ATOM   2926  O OG  . SER B 2 54  ? 1.595   6.912   14.281  1.00 74.06  ? 54  SER B OG  1 
ATOM   2927  N N   . VAL B 2 55  ? 4.030   5.347   17.461  1.00 61.64  ? 55  VAL B N   1 
ATOM   2928  C CA  . VAL B 2 55  ? 5.286   4.670   17.771  1.00 58.46  ? 55  VAL B CA  1 
ATOM   2929  C C   . VAL B 2 55  ? 5.025   3.292   18.360  1.00 59.84  ? 55  VAL B C   1 
ATOM   2930  O O   . VAL B 2 55  ? 5.869   2.406   18.266  1.00 53.69  ? 55  VAL B O   1 
ATOM   2931  C CB  . VAL B 2 55  ? 6.152   5.447   18.786  1.00 59.74  ? 55  VAL B CB  1 
ATOM   2932  C CG1 . VAL B 2 55  ? 6.240   6.916   18.413  1.00 52.32  ? 55  VAL B CG1 1 
ATOM   2933  C CG2 . VAL B 2 55  ? 5.606   5.273   20.195  1.00 68.02  ? 55  VAL B CG2 1 
ATOM   2934  N N   . ILE B 2 56  ? 3.854   3.123   18.966  1.00 64.09  ? 56  ILE B N   1 
ATOM   2935  C CA  . ILE B 2 56  ? 3.521   1.889   19.666  1.00 56.90  ? 56  ILE B CA  1 
ATOM   2936  C C   . ILE B 2 56  ? 2.911   0.828   18.754  1.00 63.80  ? 56  ILE B C   1 
ATOM   2937  O O   . ILE B 2 56  ? 3.245   -0.353  18.856  1.00 67.98  ? 56  ILE B O   1 
ATOM   2938  C CB  . ILE B 2 56  ? 2.550   2.149   20.827  1.00 63.78  ? 56  ILE B CB  1 
ATOM   2939  C CG1 . ILE B 2 56  ? 3.318   2.580   22.078  1.00 70.39  ? 56  ILE B CG1 1 
ATOM   2940  C CG2 . ILE B 2 56  ? 1.731   0.908   21.121  1.00 65.03  ? 56  ILE B CG2 1 
ATOM   2941  C CD1 . ILE B 2 56  ? 2.427   2.896   23.260  1.00 71.77  ? 56  ILE B CD1 1 
ATOM   2942  N N   . GLU B 2 57  ? 2.024   1.255   17.862  1.00 78.93  ? 57  GLU B N   1 
ATOM   2943  C CA  . GLU B 2 57  ? 1.239   0.328   17.055  1.00 79.99  ? 57  GLU B CA  1 
ATOM   2944  C C   . GLU B 2 57  ? 1.936   -0.113  15.762  1.00 81.52  ? 57  GLU B C   1 
ATOM   2945  O O   . GLU B 2 57  ? 1.581   -1.134  15.173  1.00 82.27  ? 57  GLU B O   1 
ATOM   2946  C CB  . GLU B 2 57  ? -0.128  0.940   16.734  1.00 86.87  ? 57  GLU B CB  1 
ATOM   2947  C CG  . GLU B 2 57  ? -0.948  1.310   17.963  1.00 101.61 ? 57  GLU B CG  1 
ATOM   2948  C CD  . GLU B 2 57  ? -2.322  1.857   17.610  1.00 119.01 ? 57  GLU B CD  1 
ATOM   2949  O OE1 . GLU B 2 57  ? -2.627  1.979   16.403  1.00 121.64 ? 57  GLU B OE1 1 
ATOM   2950  O OE2 . GLU B 2 57  ? -3.097  2.165   18.542  1.00 127.17 ? 57  GLU B OE2 1 
ATOM   2951  N N   . LYS B 2 58  ? 2.926   0.655   15.322  1.00 60.83  ? 58  LYS B N   1 
ATOM   2952  C CA  . LYS B 2 58  ? 3.592   0.369   14.051  1.00 64.58  ? 58  LYS B CA  1 
ATOM   2953  C C   . LYS B 2 58  ? 4.675   -0.698  14.203  1.00 69.34  ? 58  LYS B C   1 
ATOM   2954  O O   . LYS B 2 58  ? 5.322   -1.074  13.229  1.00 78.80  ? 58  LYS B O   1 
ATOM   2955  C CB  . LYS B 2 58  ? 4.184   1.654   13.443  1.00 63.80  ? 58  LYS B CB  1 
ATOM   2956  C CG  . LYS B 2 58  ? 3.641   2.013   12.057  1.00 64.72  ? 58  LYS B CG  1 
ATOM   2957  C CD  . LYS B 2 58  ? 2.189   2.474   12.126  1.00 69.99  ? 58  LYS B CD  1 
ATOM   2958  C CE  . LYS B 2 58  ? 1.575   2.632   10.737  1.00 75.68  ? 58  LYS B CE  1 
ATOM   2959  N NZ  . LYS B 2 58  ? 2.164   3.763   9.974   1.00 71.36  ? 58  LYS B NZ  1 
ATOM   2960  N N   . MET B 2 59  ? 4.867   -1.176  15.429  1.00 76.60  ? 59  MET B N   1 
ATOM   2961  C CA  . MET B 2 59  ? 5.832   -2.236  15.708  1.00 75.22  ? 59  MET B CA  1 
ATOM   2962  C C   . MET B 2 59  ? 5.296   -3.597  15.287  1.00 80.07  ? 59  MET B C   1 
ATOM   2963  O O   . MET B 2 59  ? 4.122   -3.898  15.496  1.00 85.09  ? 59  MET B O   1 
ATOM   2964  C CB  . MET B 2 59  ? 6.163   -2.274  17.199  1.00 76.82  ? 59  MET B CB  1 
ATOM   2965  C CG  . MET B 2 59  ? 7.519   -1.701  17.562  1.00 80.06  ? 59  MET B CG  1 
ATOM   2966  S SD  . MET B 2 59  ? 8.872   -2.695  16.921  1.00 63.07  ? 59  MET B SD  1 
ATOM   2967  C CE  . MET B 2 59  ? 8.298   -4.330  17.368  1.00 126.01 ? 59  MET B CE  1 
ATOM   2968  N N   . ASN B 2 60  ? 6.160   -4.420  14.701  1.00 77.75  ? 60  ASN B N   1 
ATOM   2969  C CA  . ASN B 2 60  ? 5.778   -5.773  14.306  1.00 84.93  ? 60  ASN B CA  1 
ATOM   2970  C C   . ASN B 2 60  ? 6.287   -6.787  15.327  1.00 78.80  ? 60  ASN B C   1 
ATOM   2971  O O   . ASN B 2 60  ? 7.478   -6.823  15.618  1.00 80.48  ? 60  ASN B O   1 
ATOM   2972  C CB  . ASN B 2 60  ? 6.324   -6.085  12.911  1.00 95.04  ? 60  ASN B CB  1 
ATOM   2973  C CG  . ASN B 2 60  ? 5.486   -7.105  12.168  1.00 104.09 ? 60  ASN B CG  1 
ATOM   2974  O OD1 . ASN B 2 60  ? 4.424   -7.517  12.638  1.00 110.66 ? 60  ASN B OD1 1 
ATOM   2975  N ND2 . ASN B 2 60  ? 5.954   -7.511  10.992  1.00 104.54 ? 60  ASN B ND2 1 
ATOM   2976  N N   . THR B 2 61  ? 5.391   -7.603  15.873  1.00 122.25 ? 61  THR B N   1 
ATOM   2977  C CA  . THR B 2 61  ? 5.757   -8.509  16.964  1.00 119.25 ? 61  THR B CA  1 
ATOM   2978  C C   . THR B 2 61  ? 6.385   -9.830  16.504  1.00 119.03 ? 61  THR B C   1 
ATOM   2979  O O   . THR B 2 61  ? 7.561   -10.083 16.762  1.00 125.16 ? 61  THR B O   1 
ATOM   2980  C CB  . THR B 2 61  ? 4.558   -8.799  17.890  1.00 113.87 ? 61  THR B CB  1 
ATOM   2981  O OG1 . THR B 2 61  ? 3.513   -9.448  17.148  1.00 119.31 ? 61  THR B OG1 1 
ATOM   2982  C CG2 . THR B 2 61  ? 4.031   -7.506  18.493  1.00 108.33 ? 61  THR B CG2 1 
ATOM   2983  N N   . GLN B 2 62  ? 5.593   -10.674 15.846  1.00 99.82  ? 62  GLN B N   1 
ATOM   2984  C CA  . GLN B 2 62  ? 6.082   -11.948 15.308  1.00 103.59 ? 62  GLN B CA  1 
ATOM   2985  C C   . GLN B 2 62  ? 6.551   -12.933 16.391  1.00 95.80  ? 62  GLN B C   1 
ATOM   2986  O O   . GLN B 2 62  ? 7.473   -12.644 17.152  1.00 111.29 ? 62  GLN B O   1 
ATOM   2987  C CB  . GLN B 2 62  ? 7.208   -11.705 14.295  1.00 104.54 ? 62  GLN B CB  1 
ATOM   2988  C CG  . GLN B 2 62  ? 7.341   -12.785 13.231  1.00 109.57 ? 62  GLN B CG  1 
ATOM   2989  C CD  . GLN B 2 62  ? 6.514   -12.491 11.990  1.00 122.55 ? 62  GLN B CD  1 
ATOM   2990  O OE1 . GLN B 2 62  ? 6.596   -11.400 11.420  1.00 122.14 ? 62  GLN B OE1 1 
ATOM   2991  N NE2 . GLN B 2 62  ? 5.711   -13.464 11.568  1.00 129.04 ? 62  GLN B NE2 1 
ATOM   2992  N N   . PHE B 2 63  ? 5.916   -14.099 16.441  1.00 74.89  ? 63  PHE B N   1 
ATOM   2993  C CA  . PHE B 2 63  ? 6.224   -15.112 17.449  1.00 64.85  ? 63  PHE B CA  1 
ATOM   2994  C C   . PHE B 2 63  ? 7.597   -15.738 17.224  1.00 63.61  ? 63  PHE B C   1 
ATOM   2995  O O   . PHE B 2 63  ? 7.908   -16.196 16.124  1.00 60.42  ? 63  PHE B O   1 
ATOM   2996  C CB  . PHE B 2 63  ? 5.144   -16.200 17.441  1.00 64.09  ? 63  PHE B CB  1 
ATOM   2997  C CG  . PHE B 2 63  ? 5.442   -17.372 18.338  1.00 62.66  ? 63  PHE B CG  1 
ATOM   2998  C CD1 . PHE B 2 63  ? 4.967   -17.405 19.639  1.00 67.79  ? 63  PHE B CD1 1 
ATOM   2999  C CD2 . PHE B 2 63  ? 6.177   -18.443 17.875  1.00 53.58  ? 63  PHE B CD2 1 
ATOM   3000  C CE1 . PHE B 2 63  ? 5.232   -18.485 20.466  1.00 56.71  ? 63  PHE B CE1 1 
ATOM   3001  C CE2 . PHE B 2 63  ? 6.446   -19.520 18.693  1.00 50.59  ? 63  PHE B CE2 1 
ATOM   3002  C CZ  . PHE B 2 63  ? 5.974   -19.538 19.992  1.00 49.41  ? 63  PHE B CZ  1 
ATOM   3003  N N   . GLU B 2 64  ? 8.415   -15.771 18.270  1.00 59.87  ? 64  GLU B N   1 
ATOM   3004  C CA  . GLU B 2 64  ? 9.780   -16.261 18.131  1.00 52.95  ? 64  GLU B CA  1 
ATOM   3005  C C   . GLU B 2 64  ? 10.263  -17.022 19.353  1.00 46.80  ? 64  GLU B C   1 
ATOM   3006  O O   . GLU B 2 64  ? 9.844   -16.758 20.477  1.00 51.95  ? 64  GLU B O   1 
ATOM   3007  C CB  . GLU B 2 64  ? 10.746  -15.100 17.849  1.00 59.83  ? 64  GLU B CB  1 
ATOM   3008  C CG  . GLU B 2 64  ? 10.483  -14.348 16.551  1.00 64.06  ? 64  GLU B CG  1 
ATOM   3009  C CD  . GLU B 2 64  ? 10.765  -15.176 15.302  1.00 75.15  ? 64  GLU B CD  1 
ATOM   3010  O OE1 . GLU B 2 64  ? 11.032  -16.392 15.427  1.00 82.05  ? 64  GLU B OE1 1 
ATOM   3011  O OE2 . GLU B 2 64  ? 10.722  -14.607 14.187  1.00 77.01  ? 64  GLU B OE2 1 
ATOM   3012  N N   . ALA B 2 65  ? 11.168  -17.961 19.120  1.00 39.98  ? 65  ALA B N   1 
ATOM   3013  C CA  . ALA B 2 65  ? 11.853  -18.640 20.203  1.00 37.82  ? 65  ALA B CA  1 
ATOM   3014  C C   . ALA B 2 65  ? 13.332  -18.268 20.192  1.00 40.87  ? 65  ALA B C   1 
ATOM   3015  O O   . ALA B 2 65  ? 14.080  -18.618 19.270  1.00 47.94  ? 65  ALA B O   1 
ATOM   3016  C CB  . ALA B 2 65  ? 11.681  -20.145 20.080  1.00 35.80  ? 65  ALA B CB  1 
ATOM   3017  N N   . VAL B 2 66  ? 13.747  -17.551 21.223  1.00 47.83  ? 66  VAL B N   1 
ATOM   3018  C CA  . VAL B 2 66  ? 15.127  -17.136 21.354  1.00 54.80  ? 66  VAL B CA  1 
ATOM   3019  C C   . VAL B 2 66  ? 15.814  -18.042 22.364  1.00 60.00  ? 66  VAL B C   1 
ATOM   3020  O O   . VAL B 2 66  ? 15.585  -17.927 23.566  1.00 63.67  ? 66  VAL B O   1 
ATOM   3021  C CB  . VAL B 2 66  ? 15.193  -15.687 21.842  1.00 58.18  ? 66  VAL B CB  1 
ATOM   3022  C CG1 . VAL B 2 66  ? 16.628  -15.285 22.133  1.00 37.72  ? 66  VAL B CG1 1 
ATOM   3023  C CG2 . VAL B 2 66  ? 14.549  -14.764 20.822  1.00 66.34  ? 66  VAL B CG2 1 
ATOM   3024  N N   . GLY B 2 67  ? 16.640  -18.961 21.885  1.00 85.54  ? 67  GLY B N   1 
ATOM   3025  C CA  . GLY B 2 67  ? 17.266  -19.918 22.776  1.00 84.45  ? 67  GLY B CA  1 
ATOM   3026  C C   . GLY B 2 67  ? 18.501  -20.547 22.174  1.00 82.01  ? 67  GLY B C   1 
ATOM   3027  O O   . GLY B 2 67  ? 18.816  -20.325 21.007  1.00 82.14  ? 67  GLY B O   1 
ATOM   3028  N N   . LYS B 2 68  ? 19.201  -21.344 22.970  1.00 97.95  ? 68  LYS B N   1 
ATOM   3029  C CA  . LYS B 2 68  ? 20.439  -21.962 22.513  1.00 86.84  ? 68  LYS B CA  1 
ATOM   3030  C C   . LYS B 2 68  ? 20.227  -22.875 21.308  1.00 84.29  ? 68  LYS B C   1 
ATOM   3031  O O   . LYS B 2 68  ? 20.099  -22.391 20.183  1.00 91.41  ? 68  LYS B O   1 
ATOM   3032  C CB  . LYS B 2 68  ? 21.140  -22.692 23.660  1.00 83.91  ? 68  LYS B CB  1 
ATOM   3033  C CG  . LYS B 2 68  ? 22.093  -21.789 24.429  1.00 88.75  ? 68  LYS B CG  1 
ATOM   3034  C CD  . LYS B 2 68  ? 21.626  -20.335 24.368  1.00 93.05  ? 68  LYS B CD  1 
ATOM   3035  C CE  . LYS B 2 68  ? 22.746  -19.356 24.693  1.00 97.84  ? 68  LYS B CE  1 
ATOM   3036  N NZ  . LYS B 2 68  ? 23.149  -19.411 26.123  1.00 103.11 ? 68  LYS B NZ  1 
ATOM   3037  N N   . GLU B 2 69  ? 20.200  -24.185 21.544  1.00 56.60  ? 69  GLU B N   1 
ATOM   3038  C CA  . GLU B 2 69  ? 20.020  -25.161 20.470  1.00 61.02  ? 69  GLU B CA  1 
ATOM   3039  C C   . GLU B 2 69  ? 21.307  -25.492 19.716  1.00 50.12  ? 69  GLU B C   1 
ATOM   3040  O O   . GLU B 2 69  ? 21.261  -25.804 18.531  1.00 53.00  ? 69  GLU B O   1 
ATOM   3041  C CB  . GLU B 2 69  ? 18.962  -24.688 19.467  1.00 81.01  ? 69  GLU B CB  1 
ATOM   3042  C CG  . GLU B 2 69  ? 17.556  -25.204 19.716  1.00 100.53 ? 69  GLU B CG  1 
ATOM   3043  C CD  . GLU B 2 69  ? 16.564  -24.657 18.708  1.00 97.49  ? 69  GLU B CD  1 
ATOM   3044  O OE1 . GLU B 2 69  ? 16.965  -23.798 17.893  1.00 84.53  ? 69  GLU B OE1 1 
ATOM   3045  O OE2 . GLU B 2 69  ? 15.389  -25.081 18.731  1.00 101.54 ? 69  GLU B OE2 1 
ATOM   3046  N N   . PHE B 2 70  ? 22.450  -25.432 20.387  1.00 42.23  ? 70  PHE B N   1 
ATOM   3047  C CA  . PHE B 2 70  ? 23.703  -25.782 19.728  1.00 41.13  ? 70  PHE B CA  1 
ATOM   3048  C C   . PHE B 2 70  ? 24.653  -26.563 20.621  1.00 50.45  ? 70  PHE B C   1 
ATOM   3049  O O   . PHE B 2 70  ? 24.853  -26.225 21.789  1.00 60.74  ? 70  PHE B O   1 
ATOM   3050  C CB  . PHE B 2 70  ? 24.399  -24.545 19.165  1.00 45.97  ? 70  PHE B CB  1 
ATOM   3051  C CG  . PHE B 2 70  ? 23.635  -23.878 18.062  1.00 54.89  ? 70  PHE B CG  1 
ATOM   3052  C CD1 . PHE B 2 70  ? 23.489  -24.494 16.830  1.00 61.55  ? 70  PHE B CD1 1 
ATOM   3053  C CD2 . PHE B 2 70  ? 23.066  -22.629 18.252  1.00 57.09  ? 70  PHE B CD2 1 
ATOM   3054  C CE1 . PHE B 2 70  ? 22.785  -23.881 15.807  1.00 53.13  ? 70  PHE B CE1 1 
ATOM   3055  C CE2 . PHE B 2 70  ? 22.358  -22.014 17.237  1.00 55.76  ? 70  PHE B CE2 1 
ATOM   3056  C CZ  . PHE B 2 70  ? 22.217  -22.643 16.011  1.00 47.67  ? 70  PHE B CZ  1 
ATOM   3057  N N   . SER B 2 71  ? 25.235  -27.615 20.054  1.00 42.47  ? 71  SER B N   1 
ATOM   3058  C CA  . SER B 2 71  ? 26.197  -28.444 20.761  1.00 50.51  ? 71  SER B CA  1 
ATOM   3059  C C   . SER B 2 71  ? 27.500  -27.695 20.978  1.00 63.11  ? 71  SER B C   1 
ATOM   3060  O O   . SER B 2 71  ? 27.586  -26.495 20.739  1.00 72.59  ? 71  SER B O   1 
ATOM   3061  C CB  . SER B 2 71  ? 26.480  -29.706 19.957  1.00 51.88  ? 71  SER B CB  1 
ATOM   3062  O OG  . SER B 2 71  ? 27.132  -29.376 18.745  1.00 60.67  ? 71  SER B OG  1 
ATOM   3063  N N   . ASN B 2 72  ? 28.515  -28.420 21.429  1.00 77.57  ? 72  ASN B N   1 
ATOM   3064  C CA  . ASN B 2 72  ? 29.835  -27.850 21.636  1.00 89.42  ? 72  ASN B CA  1 
ATOM   3065  C C   . ASN B 2 72  ? 30.696  -28.005 20.384  1.00 74.05  ? 72  ASN B C   1 
ATOM   3066  O O   . ASN B 2 72  ? 31.855  -27.583 20.352  1.00 81.13  ? 72  ASN B O   1 
ATOM   3067  C CB  . ASN B 2 72  ? 30.511  -28.508 22.840  1.00 110.30 ? 72  ASN B CB  1 
ATOM   3068  C CG  . ASN B 2 72  ? 30.507  -30.023 22.753  1.00 123.16 ? 72  ASN B CG  1 
ATOM   3069  O OD1 . ASN B 2 72  ? 30.262  -30.596 21.689  1.00 112.94 ? 72  ASN B OD1 1 
ATOM   3070  N ND2 . ASN B 2 72  ? 30.779  -30.681 23.875  1.00 138.39 ? 72  ASN B ND2 1 
ATOM   3071  N N   . LEU B 2 73  ? 30.119  -28.620 19.358  1.00 62.64  ? 73  LEU B N   1 
ATOM   3072  C CA  . LEU B 2 73  ? 30.797  -28.784 18.084  1.00 65.82  ? 73  LEU B CA  1 
ATOM   3073  C C   . LEU B 2 73  ? 30.161  -27.872 17.044  1.00 66.42  ? 73  LEU B C   1 
ATOM   3074  O O   . LEU B 2 73  ? 30.460  -27.952 15.854  1.00 67.49  ? 73  LEU B O   1 
ATOM   3075  C CB  . LEU B 2 73  ? 30.724  -30.237 17.633  1.00 72.92  ? 73  LEU B CB  1 
ATOM   3076  C CG  . LEU B 2 73  ? 31.993  -30.749 16.953  1.00 81.64  ? 73  LEU B CG  1 
ATOM   3077  C CD1 . LEU B 2 73  ? 33.216  -30.385 17.786  1.00 80.72  ? 73  LEU B CD1 1 
ATOM   3078  C CD2 . LEU B 2 73  ? 31.922  -32.258 16.706  1.00 80.66  ? 73  LEU B CD2 1 
ATOM   3079  N N   . GLU B 2 74  ? 29.279  -26.997 17.512  1.00 64.92  ? 74  GLU B N   1 
ATOM   3080  C CA  . GLU B 2 74  ? 28.586  -26.057 16.643  1.00 61.08  ? 74  GLU B CA  1 
ATOM   3081  C C   . GLU B 2 74  ? 28.803  -24.627 17.136  1.00 66.04  ? 74  GLU B C   1 
ATOM   3082  O O   . GLU B 2 74  ? 27.959  -23.747 16.951  1.00 73.87  ? 74  GLU B O   1 
ATOM   3083  C CB  . GLU B 2 74  ? 27.097  -26.388 16.592  1.00 54.69  ? 74  GLU B CB  1 
ATOM   3084  C CG  . GLU B 2 74  ? 26.810  -27.766 16.060  1.00 49.14  ? 74  GLU B CG  1 
ATOM   3085  C CD  . GLU B 2 74  ? 25.359  -28.161 16.208  1.00 49.13  ? 74  GLU B CD  1 
ATOM   3086  O OE1 . GLU B 2 74  ? 24.705  -27.690 17.159  1.00 52.39  ? 74  GLU B OE1 1 
ATOM   3087  O OE2 . GLU B 2 74  ? 24.874  -28.955 15.373  1.00 42.14  ? 74  GLU B OE2 1 
ATOM   3088  N N   . ARG B 2 75  ? 29.953  -24.412 17.759  1.00 42.43  ? 75  ARG B N   1 
ATOM   3089  C CA  . ARG B 2 75  ? 30.288  -23.127 18.340  1.00 45.89  ? 75  ARG B CA  1 
ATOM   3090  C C   . ARG B 2 75  ? 30.341  -22.008 17.293  1.00 43.83  ? 75  ARG B C   1 
ATOM   3091  O O   . ARG B 2 75  ? 30.061  -20.847 17.602  1.00 44.25  ? 75  ARG B O   1 
ATOM   3092  C CB  . ARG B 2 75  ? 31.603  -23.234 19.114  1.00 61.25  ? 75  ARG B CB  1 
ATOM   3093  C CG  . ARG B 2 75  ? 31.480  -23.997 20.426  1.00 75.04  ? 75  ARG B CG  1 
ATOM   3094  C CD  . ARG B 2 75  ? 30.573  -23.253 21.394  1.00 98.59  ? 75  ARG B CD  1 
ATOM   3095  N NE  . ARG B 2 75  ? 30.481  -23.910 22.694  1.00 127.84 ? 75  ARG B NE  1 
ATOM   3096  C CZ  . ARG B 2 75  ? 30.015  -23.323 23.793  1.00 148.49 ? 75  ARG B CZ  1 
ATOM   3097  N NH1 . ARG B 2 75  ? 29.607  -22.062 23.752  1.00 149.78 ? 75  ARG B NH1 1 
ATOM   3098  N NH2 . ARG B 2 75  ? 29.965  -23.994 24.936  1.00 152.86 ? 75  ARG B NH2 1 
ATOM   3099  N N   . ARG B 2 76  ? 30.694  -22.347 16.057  1.00 42.91  ? 76  ARG B N   1 
ATOM   3100  C CA  . ARG B 2 76  ? 30.626  -21.359 14.980  1.00 45.63  ? 76  ARG B CA  1 
ATOM   3101  C C   . ARG B 2 76  ? 29.180  -20.912 14.813  1.00 47.53  ? 76  ARG B C   1 
ATOM   3102  O O   . ARG B 2 76  ? 28.908  -19.736 14.602  1.00 55.12  ? 76  ARG B O   1 
ATOM   3103  C CB  . ARG B 2 76  ? 31.148  -21.927 13.659  1.00 53.91  ? 76  ARG B CB  1 
ATOM   3104  C CG  . ARG B 2 76  ? 32.658  -22.039 13.564  1.00 55.04  ? 76  ARG B CG  1 
ATOM   3105  C CD  . ARG B 2 76  ? 33.074  -22.733 12.271  1.00 62.08  ? 76  ARG B CD  1 
ATOM   3106  N NE  . ARG B 2 76  ? 32.558  -24.096 12.197  1.00 66.30  ? 76  ARG B NE  1 
ATOM   3107  C CZ  . ARG B 2 76  ? 31.942  -24.609 11.138  1.00 79.09  ? 76  ARG B CZ  1 
ATOM   3108  N NH1 . ARG B 2 76  ? 31.759  -23.878 10.050  1.00 87.73  ? 76  ARG B NH1 1 
ATOM   3109  N NH2 . ARG B 2 76  ? 31.510  -25.859 11.170  1.00 76.95  ? 76  ARG B NH2 1 
ATOM   3110  N N   . LEU B 2 77  ? 28.254  -21.861 14.918  1.00 62.89  ? 77  LEU B N   1 
ATOM   3111  C CA  . LEU B 2 77  ? 26.836  -21.557 14.753  1.00 57.70  ? 77  LEU B CA  1 
ATOM   3112  C C   . LEU B 2 77  ? 26.303  -20.696 15.887  1.00 50.50  ? 77  LEU B C   1 
ATOM   3113  O O   . LEU B 2 77  ? 25.780  -19.609 15.648  1.00 43.27  ? 77  LEU B O   1 
ATOM   3114  C CB  . LEU B 2 77  ? 26.004  -22.829 14.593  1.00 53.96  ? 77  LEU B CB  1 
ATOM   3115  C CG  . LEU B 2 77  ? 25.964  -23.355 13.161  1.00 64.23  ? 77  LEU B CG  1 
ATOM   3116  C CD1 . LEU B 2 77  ? 27.234  -24.121 12.846  1.00 76.09  ? 77  LEU B CD1 1 
ATOM   3117  C CD2 . LEU B 2 77  ? 24.741  -24.223 12.957  1.00 62.38  ? 77  LEU B CD2 1 
ATOM   3118  N N   . GLU B 2 78  ? 26.427  -21.188 17.116  1.00 43.74  ? 78  GLU B N   1 
ATOM   3119  C CA  . GLU B 2 78  ? 26.135  -20.381 18.291  1.00 44.14  ? 78  GLU B CA  1 
ATOM   3120  C C   . GLU B 2 78  ? 26.594  -18.929 18.024  1.00 43.15  ? 78  GLU B C   1 
ATOM   3121  O O   . GLU B 2 78  ? 25.788  -17.995 18.023  1.00 48.61  ? 78  GLU B O   1 
ATOM   3122  C CB  . GLU B 2 78  ? 26.855  -20.973 19.504  1.00 62.94  ? 78  GLU B CB  1 
ATOM   3123  C CG  . GLU B 2 78  ? 26.369  -20.493 20.860  1.00 74.91  ? 78  GLU B CG  1 
ATOM   3124  C CD  . GLU B 2 78  ? 27.033  -21.249 22.007  1.00 91.18  ? 78  GLU B CD  1 
ATOM   3125  O OE1 . GLU B 2 78  ? 27.229  -22.478 21.877  1.00 94.60  ? 78  GLU B OE1 1 
ATOM   3126  O OE2 . GLU B 2 78  ? 27.365  -20.615 23.032  1.00 91.63  ? 78  GLU B OE2 1 
ATOM   3127  N N   . ASN B 2 79  ? 27.887  -18.759 17.765  1.00 39.76  ? 79  ASN B N   1 
ATOM   3128  C CA  . ASN B 2 79  ? 28.454  -17.451 17.467  1.00 48.71  ? 79  ASN B CA  1 
ATOM   3129  C C   . ASN B 2 79  ? 27.669  -16.679 16.412  1.00 56.60  ? 79  ASN B C   1 
ATOM   3130  O O   . ASN B 2 79  ? 27.413  -15.487 16.569  1.00 65.23  ? 79  ASN B O   1 
ATOM   3131  C CB  . ASN B 2 79  ? 29.904  -17.593 17.011  1.00 58.89  ? 79  ASN B CB  1 
ATOM   3132  C CG  . ASN B 2 79  ? 30.549  -16.257 16.713  1.00 67.96  ? 79  ASN B CG  1 
ATOM   3133  O OD1 . ASN B 2 79  ? 30.447  -15.315 17.501  1.00 68.03  ? 79  ASN B OD1 1 
ATOM   3134  N ND2 . ASN B 2 79  ? 31.201  -16.161 15.562  1.00 75.57  ? 79  ASN B ND2 1 
ATOM   3135  N N   . LEU B 2 80  ? 27.305  -17.356 15.329  1.00 56.29  ? 80  LEU B N   1 
ATOM   3136  C CA  . LEU B 2 80  ? 26.539  -16.728 14.263  1.00 43.84  ? 80  LEU B CA  1 
ATOM   3137  C C   . LEU B 2 80  ? 25.253  -16.183 14.845  1.00 46.85  ? 80  LEU B C   1 
ATOM   3138  O O   . LEU B 2 80  ? 24.950  -14.995 14.713  1.00 55.99  ? 80  LEU B O   1 
ATOM   3139  C CB  . LEU B 2 80  ? 26.212  -17.736 13.170  1.00 36.48  ? 80  LEU B CB  1 
ATOM   3140  C CG  . LEU B 2 80  ? 26.293  -17.160 11.767  1.00 43.70  ? 80  LEU B CG  1 
ATOM   3141  C CD1 . LEU B 2 80  ? 25.607  -18.066 10.770  1.00 45.22  ? 80  LEU B CD1 1 
ATOM   3142  C CD2 . LEU B 2 80  ? 25.669  -15.783 11.760  1.00 39.64  ? 80  LEU B CD2 1 
ATOM   3143  N N   . ASN B 2 81  ? 24.501  -17.061 15.504  1.00 52.60  ? 81  ASN B N   1 
ATOM   3144  C CA  . ASN B 2 81  ? 23.275  -16.660 16.185  1.00 43.12  ? 81  ASN B CA  1 
ATOM   3145  C C   . ASN B 2 81  ? 23.512  -15.421 17.053  1.00 45.99  ? 81  ASN B C   1 
ATOM   3146  O O   . ASN B 2 81  ? 22.727  -14.475 17.027  1.00 53.03  ? 81  ASN B O   1 
ATOM   3147  C CB  . ASN B 2 81  ? 22.717  -17.807 17.035  1.00 44.19  ? 81  ASN B CB  1 
ATOM   3148  C CG  . ASN B 2 81  ? 21.246  -17.634 17.350  1.00 62.68  ? 81  ASN B CG  1 
ATOM   3149  O OD1 . ASN B 2 81  ? 20.384  -17.914 16.517  1.00 68.90  ? 81  ASN B OD1 1 
ATOM   3150  N ND2 . ASN B 2 81  ? 20.949  -17.172 18.556  1.00 68.23  ? 81  ASN B ND2 1 
ATOM   3151  N N   . LYS B 2 82  ? 24.607  -15.434 17.809  1.00 37.80  ? 82  LYS B N   1 
ATOM   3152  C CA  . LYS B 2 82  ? 24.943  -14.332 18.701  1.00 35.21  ? 82  LYS B CA  1 
ATOM   3153  C C   . LYS B 2 82  ? 25.199  -13.042 17.918  1.00 41.62  ? 82  LYS B C   1 
ATOM   3154  O O   . LYS B 2 82  ? 24.668  -11.988 18.265  1.00 47.47  ? 82  LYS B O   1 
ATOM   3155  C CB  . LYS B 2 82  ? 26.143  -14.693 19.577  1.00 44.22  ? 82  LYS B CB  1 
ATOM   3156  C CG  . LYS B 2 82  ? 26.563  -13.603 20.541  1.00 60.47  ? 82  LYS B CG  1 
ATOM   3157  C CD  . LYS B 2 82  ? 27.846  -13.976 21.270  1.00 84.98  ? 82  LYS B CD  1 
ATOM   3158  C CE  . LYS B 2 82  ? 28.373  -12.824 22.116  1.00 105.11 ? 82  LYS B CE  1 
ATOM   3159  N NZ  . LYS B 2 82  ? 28.827  -11.677 21.283  1.00 112.08 ? 82  LYS B NZ  1 
ATOM   3160  N N   . LYS B 2 83  ? 25.998  -13.120 16.859  1.00 51.17  ? 83  LYS B N   1 
ATOM   3161  C CA  . LYS B 2 83  ? 26.214  -11.953 16.011  1.00 60.44  ? 83  LYS B CA  1 
ATOM   3162  C C   . LYS B 2 83  ? 24.877  -11.380 15.562  1.00 50.79  ? 83  LYS B C   1 
ATOM   3163  O O   . LYS B 2 83  ? 24.689  -10.166 15.553  1.00 59.60  ? 83  LYS B O   1 
ATOM   3164  C CB  . LYS B 2 83  ? 27.085  -12.290 14.798  1.00 79.05  ? 83  LYS B CB  1 
ATOM   3165  C CG  . LYS B 2 83  ? 28.563  -11.997 15.005  1.00 108.28 ? 83  LYS B CG  1 
ATOM   3166  C CD  . LYS B 2 83  ? 29.277  -11.736 13.684  1.00 131.78 ? 83  LYS B CD  1 
ATOM   3167  C CE  . LYS B 2 83  ? 29.671  -13.027 12.976  1.00 142.79 ? 83  LYS B CE  1 
ATOM   3168  N NZ  . LYS B 2 83  ? 30.846  -13.685 13.615  1.00 137.12 ? 83  LYS B NZ  1 
ATOM   3169  N N   . MET B 2 84  ? 23.944  -12.257 15.207  1.00 47.34  ? 84  MET B N   1 
ATOM   3170  C CA  . MET B 2 84  ? 22.624  -11.824 14.762  1.00 49.08  ? 84  MET B CA  1 
ATOM   3171  C C   . MET B 2 84  ? 21.858  -11.089 15.861  1.00 51.47  ? 84  MET B C   1 
ATOM   3172  O O   . MET B 2 84  ? 21.409  -9.964  15.663  1.00 58.06  ? 84  MET B O   1 
ATOM   3173  C CB  . MET B 2 84  ? 21.791  -13.010 14.264  1.00 44.91  ? 84  MET B CB  1 
ATOM   3174  C CG  . MET B 2 84  ? 20.460  -12.588 13.658  1.00 37.87  ? 84  MET B CG  1 
ATOM   3175  S SD  . MET B 2 84  ? 19.325  -13.941 13.304  1.00 80.36  ? 84  MET B SD  1 
ATOM   3176  C CE  . MET B 2 84  ? 18.879  -14.454 14.961  1.00 71.64  ? 84  MET B CE  1 
ATOM   3177  N N   . GLU B 2 85  ? 21.695  -11.733 17.012  1.00 45.05  ? 85  GLU B N   1 
ATOM   3178  C CA  . GLU B 2 85  ? 20.938  -11.152 18.114  1.00 42.15  ? 85  GLU B CA  1 
ATOM   3179  C C   . GLU B 2 85  ? 21.574  -9.836  18.531  1.00 49.63  ? 85  GLU B C   1 
ATOM   3180  O O   . GLU B 2 85  ? 20.894  -8.811  18.631  1.00 52.95  ? 85  GLU B O   1 
ATOM   3181  C CB  . GLU B 2 85  ? 20.867  -12.115 19.308  1.00 47.32  ? 85  GLU B CB  1 
ATOM   3182  C CG  . GLU B 2 85  ? 20.098  -13.412 19.055  1.00 56.59  ? 85  GLU B CG  1 
ATOM   3183  C CD  . GLU B 2 85  ? 18.617  -13.182 18.793  1.00 81.10  ? 85  GLU B CD  1 
ATOM   3184  O OE1 . GLU B 2 85  ? 17.982  -14.060 18.164  1.00 83.23  ? 85  GLU B OE1 1 
ATOM   3185  O OE2 . GLU B 2 85  ? 18.089  -12.130 19.218  1.00 78.59  ? 85  GLU B OE2 1 
ATOM   3186  N N   . ASP B 2 86  ? 22.883  -9.873  18.773  1.00 44.19  ? 86  ASP B N   1 
ATOM   3187  C CA  . ASP B 2 86  ? 23.646  -8.663  19.061  1.00 46.06  ? 86  ASP B CA  1 
ATOM   3188  C C   . ASP B 2 86  ? 23.317  -7.609  18.006  1.00 57.86  ? 86  ASP B C   1 
ATOM   3189  O O   . ASP B 2 86  ? 23.066  -6.447  18.330  1.00 63.10  ? 86  ASP B O   1 
ATOM   3190  C CB  . ASP B 2 86  ? 25.151  -8.959  19.052  1.00 54.99  ? 86  ASP B CB  1 
ATOM   3191  C CG  . ASP B 2 86  ? 25.614  -9.709  20.291  1.00 64.73  ? 86  ASP B CG  1 
ATOM   3192  O OD1 . ASP B 2 86  ? 24.758  -10.181 21.063  1.00 59.39  ? 86  ASP B OD1 1 
ATOM   3193  O OD2 . ASP B 2 86  ? 26.840  -9.831  20.489  1.00 79.81  ? 86  ASP B OD2 1 
ATOM   3194  N N   . GLY B 2 87  ? 23.313  -8.034  16.744  1.00 63.25  ? 87  GLY B N   1 
ATOM   3195  C CA  . GLY B 2 87  ? 23.038  -7.153  15.626  1.00 56.43  ? 87  GLY B CA  1 
ATOM   3196  C C   . GLY B 2 87  ? 21.725  -6.416  15.768  1.00 46.27  ? 87  GLY B C   1 
ATOM   3197  O O   . GLY B 2 87  ? 21.684  -5.185  15.704  1.00 54.55  ? 87  GLY B O   1 
ATOM   3198  N N   . PHE B 2 88  ? 20.645  -7.164  15.964  1.00 41.66  ? 88  PHE B N   1 
ATOM   3199  C CA  . PHE B 2 88  ? 19.321  -6.561  16.079  1.00 48.22  ? 88  PHE B CA  1 
ATOM   3200  C C   . PHE B 2 88  ? 19.148  -5.789  17.389  1.00 53.09  ? 88  PHE B C   1 
ATOM   3201  O O   . PHE B 2 88  ? 18.264  -4.946  17.517  1.00 66.33  ? 88  PHE B O   1 
ATOM   3202  C CB  . PHE B 2 88  ? 18.237  -7.623  15.910  1.00 50.70  ? 88  PHE B CB  1 
ATOM   3203  C CG  . PHE B 2 88  ? 18.099  -8.116  14.502  1.00 48.13  ? 88  PHE B CG  1 
ATOM   3204  C CD1 . PHE B 2 88  ? 17.967  -7.221  13.453  1.00 47.25  ? 88  PHE B CD1 1 
ATOM   3205  C CD2 . PHE B 2 88  ? 18.119  -9.475  14.219  1.00 46.31  ? 88  PHE B CD2 1 
ATOM   3206  C CE1 . PHE B 2 88  ? 17.844  -7.669  12.144  1.00 49.74  ? 88  PHE B CE1 1 
ATOM   3207  C CE2 . PHE B 2 88  ? 17.995  -9.931  12.916  1.00 48.16  ? 88  PHE B CE2 1 
ATOM   3208  C CZ  . PHE B 2 88  ? 17.858  -9.026  11.874  1.00 49.18  ? 88  PHE B CZ  1 
ATOM   3209  N N   . LEU B 2 89  ? 20.007  -6.083  18.357  1.00 45.98  ? 89  LEU B N   1 
ATOM   3210  C CA  . LEU B 2 89  ? 20.002  -5.378  19.625  1.00 50.86  ? 89  LEU B CA  1 
ATOM   3211  C C   . LEU B 2 89  ? 20.542  -3.973  19.413  1.00 52.12  ? 89  LEU B C   1 
ATOM   3212  O O   . LEU B 2 89  ? 19.900  -2.987  19.770  1.00 49.58  ? 89  LEU B O   1 
ATOM   3213  C CB  . LEU B 2 89  ? 20.874  -6.116  20.637  1.00 57.01  ? 89  LEU B CB  1 
ATOM   3214  C CG  . LEU B 2 89  ? 20.989  -5.470  22.014  1.00 59.12  ? 89  LEU B CG  1 
ATOM   3215  C CD1 . LEU B 2 89  ? 19.666  -5.596  22.738  1.00 63.06  ? 89  LEU B CD1 1 
ATOM   3216  C CD2 . LEU B 2 89  ? 22.108  -6.111  22.815  1.00 57.94  ? 89  LEU B CD2 1 
ATOM   3217  N N   . ASP B 2 90  ? 21.728  -3.886  18.824  1.00 44.24  ? 90  ASP B N   1 
ATOM   3218  C CA  . ASP B 2 90  ? 22.367  -2.601  18.589  1.00 40.43  ? 90  ASP B CA  1 
ATOM   3219  C C   . ASP B 2 90  ? 21.502  -1.694  17.715  1.00 42.84  ? 90  ASP B C   1 
ATOM   3220  O O   . ASP B 2 90  ? 21.424  -0.488  17.947  1.00 52.38  ? 90  ASP B O   1 
ATOM   3221  C CB  . ASP B 2 90  ? 23.749  -2.797  17.961  1.00 52.71  ? 90  ASP B CB  1 
ATOM   3222  C CG  . ASP B 2 90  ? 24.716  -3.503  18.890  1.00 62.51  ? 90  ASP B CG  1 
ATOM   3223  O OD1 . ASP B 2 90  ? 24.462  -3.515  20.113  1.00 63.83  ? 90  ASP B OD1 1 
ATOM   3224  O OD2 . ASP B 2 90  ? 25.733  -4.039  18.401  1.00 72.59  ? 90  ASP B OD2 1 
ATOM   3225  N N   . VAL B 2 91  ? 20.855  -2.286  16.716  1.00 37.64  ? 91  VAL B N   1 
ATOM   3226  C CA  . VAL B 2 91  ? 19.951  -1.566  15.820  1.00 33.79  ? 91  VAL B CA  1 
ATOM   3227  C C   . VAL B 2 91  ? 18.739  -0.969  16.552  1.00 42.50  ? 91  VAL B C   1 
ATOM   3228  O O   . VAL B 2 91  ? 18.503  0.235   16.498  1.00 50.86  ? 91  VAL B O   1 
ATOM   3229  C CB  . VAL B 2 91  ? 19.470  -2.490  14.677  1.00 31.11  ? 91  VAL B CB  1 
ATOM   3230  C CG1 . VAL B 2 91  ? 18.305  -1.877  13.913  1.00 29.56  ? 91  VAL B CG1 1 
ATOM   3231  C CG2 . VAL B 2 91  ? 20.624  -2.806  13.753  1.00 33.49  ? 91  VAL B CG2 1 
ATOM   3232  N N   . TRP B 2 92  ? 17.971  -1.811  17.238  1.00 27.31  ? 92  TRP B N   1 
ATOM   3233  C CA  . TRP B 2 92  ? 16.774  -1.345  17.931  1.00 33.44  ? 92  TRP B CA  1 
ATOM   3234  C C   . TRP B 2 92  ? 17.132  -0.386  19.051  1.00 44.46  ? 92  TRP B C   1 
ATOM   3235  O O   . TRP B 2 92  ? 16.442  0.610   19.273  1.00 61.02  ? 92  TRP B O   1 
ATOM   3236  C CB  . TRP B 2 92  ? 15.964  -2.517  18.482  1.00 40.06  ? 92  TRP B CB  1 
ATOM   3237  C CG  . TRP B 2 92  ? 15.243  -3.285  17.426  1.00 44.47  ? 92  TRP B CG  1 
ATOM   3238  C CD1 . TRP B 2 92  ? 15.500  -4.558  17.022  1.00 36.61  ? 92  TRP B CD1 1 
ATOM   3239  C CD2 . TRP B 2 92  ? 14.150  -2.823  16.625  1.00 51.81  ? 92  TRP B CD2 1 
ATOM   3240  N NE1 . TRP B 2 92  ? 14.634  -4.921  16.022  1.00 55.62  ? 92  TRP B NE1 1 
ATOM   3241  C CE2 . TRP B 2 92  ? 13.794  -3.872  15.761  1.00 57.75  ? 92  TRP B CE2 1 
ATOM   3242  C CE3 . TRP B 2 92  ? 13.440  -1.624  16.555  1.00 62.29  ? 92  TRP B CE3 1 
ATOM   3243  C CZ2 . TRP B 2 92  ? 12.760  -3.761  14.839  1.00 65.89  ? 92  TRP B CZ2 1 
ATOM   3244  C CZ3 . TRP B 2 92  ? 12.410  -1.516  15.643  1.00 72.07  ? 92  TRP B CZ3 1 
ATOM   3245  C CH2 . TRP B 2 92  ? 12.081  -2.577  14.797  1.00 75.99  ? 92  TRP B CH2 1 
ATOM   3246  N N   . THR B 2 93  ? 18.215  -0.684  19.756  1.00 42.87  ? 93  THR B N   1 
ATOM   3247  C CA  . THR B 2 93  ? 18.667  0.196   20.822  1.00 46.39  ? 93  THR B CA  1 
ATOM   3248  C C   . THR B 2 93  ? 18.916  1.599   20.267  1.00 60.31  ? 93  THR B C   1 
ATOM   3249  O O   . THR B 2 93  ? 18.336  2.570   20.740  1.00 76.34  ? 93  THR B O   1 
ATOM   3250  C CB  . THR B 2 93  ? 19.918  -0.356  21.520  1.00 45.58  ? 93  THR B CB  1 
ATOM   3251  O OG1 . THR B 2 93  ? 19.595  -1.615  22.131  1.00 55.67  ? 93  THR B OG1 1 
ATOM   3252  C CG2 . THR B 2 93  ? 20.409  0.611   22.586  1.00 44.65  ? 93  THR B CG2 1 
ATOM   3253  N N   . TYR B 2 94  ? 19.746  1.697   19.236  1.00 62.42  ? 94  TYR B N   1 
ATOM   3254  C CA  . TYR B 2 94  ? 20.019  2.983   18.611  1.00 58.49  ? 94  TYR B CA  1 
ATOM   3255  C C   . TYR B 2 94  ? 18.739  3.657   18.133  1.00 68.02  ? 94  TYR B C   1 
ATOM   3256  O O   . TYR B 2 94  ? 18.383  4.723   18.617  1.00 76.07  ? 94  TYR B O   1 
ATOM   3257  C CB  . TYR B 2 94  ? 20.987  2.815   17.446  1.00 47.18  ? 94  TYR B CB  1 
ATOM   3258  C CG  . TYR B 2 94  ? 21.632  4.103   17.022  1.00 53.68  ? 94  TYR B CG  1 
ATOM   3259  C CD1 . TYR B 2 94  ? 22.511  4.766   17.870  1.00 59.20  ? 94  TYR B CD1 1 
ATOM   3260  C CD2 . TYR B 2 94  ? 21.367  4.661   15.779  1.00 56.95  ? 94  TYR B CD2 1 
ATOM   3261  C CE1 . TYR B 2 94  ? 23.105  5.949   17.497  1.00 61.89  ? 94  TYR B CE1 1 
ATOM   3262  C CE2 . TYR B 2 94  ? 21.959  5.846   15.393  1.00 61.76  ? 94  TYR B CE2 1 
ATOM   3263  C CZ  . TYR B 2 94  ? 22.828  6.487   16.258  1.00 66.84  ? 94  TYR B CZ  1 
ATOM   3264  O OH  . TYR B 2 94  ? 23.430  7.670   15.889  1.00 68.96  ? 94  TYR B OH  1 
ATOM   3265  N N   . ASN B 2 95  ? 18.052  3.033   17.182  1.00 61.72  ? 95  ASN B N   1 
ATOM   3266  C CA  . ASN B 2 95  ? 16.796  3.566   16.658  1.00 63.19  ? 95  ASN B CA  1 
ATOM   3267  C C   . ASN B 2 95  ? 15.855  4.086   17.741  1.00 59.13  ? 95  ASN B C   1 
ATOM   3268  O O   . ASN B 2 95  ? 15.429  5.245   17.705  1.00 61.59  ? 95  ASN B O   1 
ATOM   3269  C CB  . ASN B 2 95  ? 16.070  2.511   15.831  1.00 69.93  ? 95  ASN B CB  1 
ATOM   3270  C CG  . ASN B 2 95  ? 16.706  2.292   14.478  1.00 67.53  ? 95  ASN B CG  1 
ATOM   3271  O OD1 . ASN B 2 95  ? 17.790  2.809   14.196  1.00 52.65  ? 95  ASN B OD1 1 
ATOM   3272  N ND2 . ASN B 2 95  ? 16.035  1.518   13.629  1.00 71.36  ? 95  ASN B ND2 1 
ATOM   3273  N N   . ALA B 2 96  ? 15.526  3.223   18.698  1.00 37.00  ? 96  ALA B N   1 
ATOM   3274  C CA  . ALA B 2 96  ? 14.614  3.588   19.783  1.00 36.88  ? 96  ALA B CA  1 
ATOM   3275  C C   . ALA B 2 96  ? 15.056  4.867   20.497  1.00 45.42  ? 96  ALA B C   1 
ATOM   3276  O O   . ALA B 2 96  ? 14.278  5.800   20.638  1.00 54.70  ? 96  ALA B O   1 
ATOM   3277  C CB  . ALA B 2 96  ? 14.486  2.438   20.776  1.00 25.59  ? 96  ALA B CB  1 
ATOM   3278  N N   . GLU B 2 97  ? 16.306  4.901   20.943  1.00 52.82  ? 97  GLU B N   1 
ATOM   3279  C CA  . GLU B 2 97  ? 16.825  6.050   21.664  1.00 50.21  ? 97  GLU B CA  1 
ATOM   3280  C C   . GLU B 2 97  ? 16.701  7.344   20.859  1.00 57.27  ? 97  GLU B C   1 
ATOM   3281  O O   . GLU B 2 97  ? 16.220  8.361   21.371  1.00 78.95  ? 97  GLU B O   1 
ATOM   3282  C CB  . GLU B 2 97  ? 18.283  5.825   22.055  1.00 46.29  ? 97  GLU B CB  1 
ATOM   3283  C CG  . GLU B 2 97  ? 18.529  4.563   22.844  1.00 50.45  ? 97  GLU B CG  1 
ATOM   3284  C CD  . GLU B 2 97  ? 18.483  4.775   24.338  1.00 52.29  ? 97  GLU B CD  1 
ATOM   3285  O OE1 . GLU B 2 97  ? 18.247  5.922   24.783  1.00 64.63  ? 97  GLU B OE1 1 
ATOM   3286  O OE2 . GLU B 2 97  ? 18.694  3.784   25.068  1.00 41.65  ? 97  GLU B OE2 1 
ATOM   3287  N N   . LEU B 2 98  ? 17.138  7.315   19.603  1.00 42.19  ? 98  LEU B N   1 
ATOM   3288  C CA  . LEU B 2 98  ? 17.088  8.515   18.772  1.00 42.87  ? 98  LEU B CA  1 
ATOM   3289  C C   . LEU B 2 98  ? 15.658  8.864   18.355  1.00 56.68  ? 98  LEU B C   1 
ATOM   3290  O O   . LEU B 2 98  ? 15.355  10.012  18.046  1.00 65.57  ? 98  LEU B O   1 
ATOM   3291  C CB  . LEU B 2 98  ? 18.017  8.396   17.556  1.00 42.29  ? 98  LEU B CB  1 
ATOM   3292  C CG  . LEU B 2 98  ? 19.389  9.063   17.716  1.00 44.71  ? 98  LEU B CG  1 
ATOM   3293  C CD1 . LEU B 2 98  ? 20.114  8.541   18.945  1.00 46.69  ? 98  LEU B CD1 1 
ATOM   3294  C CD2 . LEU B 2 98  ? 20.234  8.853   16.486  1.00 49.16  ? 98  LEU B CD2 1 
ATOM   3295  N N   . LEU B 2 99  ? 14.780  7.870   18.349  1.00 43.54  ? 99  LEU B N   1 
ATOM   3296  C CA  . LEU B 2 99  ? 13.360  8.119   18.128  1.00 43.53  ? 99  LEU B CA  1 
ATOM   3297  C C   . LEU B 2 99  ? 12.817  8.931   19.297  1.00 50.87  ? 99  LEU B C   1 
ATOM   3298  O O   . LEU B 2 99  ? 12.171  9.960   19.113  1.00 66.42  ? 99  LEU B O   1 
ATOM   3299  C CB  . LEU B 2 99  ? 12.590  6.799   18.025  1.00 42.02  ? 99  LEU B CB  1 
ATOM   3300  C CG  . LEU B 2 99  ? 11.091  6.957   17.798  1.00 51.91  ? 99  LEU B CG  1 
ATOM   3301  C CD1 . LEU B 2 99  ? 10.860  7.378   16.362  1.00 61.03  ? 99  LEU B CD1 1 
ATOM   3302  C CD2 . LEU B 2 99  ? 10.314  5.683   18.128  1.00 51.06  ? 99  LEU B CD2 1 
ATOM   3303  N N   . VAL B 2 100 ? 13.075  8.446   20.506  1.00 46.22  ? 100 VAL B N   1 
ATOM   3304  C CA  . VAL B 2 100 ? 12.601  9.112   21.703  1.00 48.64  ? 100 VAL B CA  1 
ATOM   3305  C C   . VAL B 2 100 ? 12.985  10.576  21.647  1.00 49.03  ? 100 VAL B C   1 
ATOM   3306  O O   . VAL B 2 100 ? 12.128  11.449  21.747  1.00 59.35  ? 100 VAL B O   1 
ATOM   3307  C CB  . VAL B 2 100 ? 13.169  8.455   22.980  1.00 56.05  ? 100 VAL B CB  1 
ATOM   3308  C CG1 . VAL B 2 100 ? 13.136  9.429   24.147  1.00 60.56  ? 100 VAL B CG1 1 
ATOM   3309  C CG2 . VAL B 2 100 ? 12.390  7.198   23.313  1.00 50.53  ? 100 VAL B CG2 1 
ATOM   3310  N N   . LEU B 2 101 ? 14.274  10.836  21.457  1.00 59.35  ? 101 LEU B N   1 
ATOM   3311  C CA  . LEU B 2 101 ? 14.780  12.204  21.395  1.00 66.98  ? 101 LEU B CA  1 
ATOM   3312  C C   . LEU B 2 101 ? 14.119  13.013  20.278  1.00 73.02  ? 101 LEU B C   1 
ATOM   3313  O O   . LEU B 2 101 ? 13.417  13.983  20.545  1.00 84.14  ? 101 LEU B O   1 
ATOM   3314  C CB  . LEU B 2 101 ? 16.303  12.213  21.228  1.00 62.65  ? 101 LEU B CB  1 
ATOM   3315  C CG  . LEU B 2 101 ? 17.128  11.456  22.277  1.00 49.65  ? 101 LEU B CG  1 
ATOM   3316  C CD1 . LEU B 2 101 ? 18.622  11.786  22.137  1.00 35.20  ? 101 LEU B CD1 1 
ATOM   3317  C CD2 . LEU B 2 101 ? 16.644  11.771  23.683  1.00 47.22  ? 101 LEU B CD2 1 
ATOM   3318  N N   . MET B 2 102 ? 14.349  12.617  19.030  1.00 50.13  ? 102 MET B N   1 
ATOM   3319  C CA  . MET B 2 102 ? 13.746  13.299  17.893  1.00 54.12  ? 102 MET B CA  1 
ATOM   3320  C C   . MET B 2 102 ? 12.283  13.633  18.146  1.00 60.56  ? 102 MET B C   1 
ATOM   3321  O O   . MET B 2 102 ? 11.871  14.782  18.019  1.00 75.88  ? 102 MET B O   1 
ATOM   3322  C CB  . MET B 2 102 ? 13.871  12.460  16.624  1.00 62.02  ? 102 MET B CB  1 
ATOM   3323  C CG  . MET B 2 102 ? 15.212  12.569  15.910  1.00 62.78  ? 102 MET B CG  1 
ATOM   3324  S SD  . MET B 2 102 ? 15.350  11.317  14.610  1.00 119.20 ? 102 MET B SD  1 
ATOM   3325  C CE  . MET B 2 102 ? 16.779  11.905  13.701  1.00 56.32  ? 102 MET B CE  1 
ATOM   3326  N N   . GLU B 2 103 ? 11.500  12.633  18.520  1.00 50.16  ? 103 GLU B N   1 
ATOM   3327  C CA  . GLU B 2 103 ? 10.071  12.832  18.731  1.00 60.42  ? 103 GLU B CA  1 
ATOM   3328  C C   . GLU B 2 103 ? 9.752   13.689  19.957  1.00 66.33  ? 103 GLU B C   1 
ATOM   3329  O O   . GLU B 2 103 ? 8.633   14.178  20.101  1.00 74.29  ? 103 GLU B O   1 
ATOM   3330  C CB  . GLU B 2 103 ? 9.340   11.488  18.810  1.00 62.74  ? 103 GLU B CB  1 
ATOM   3331  C CG  . GLU B 2 103 ? 9.126   10.828  17.456  1.00 72.84  ? 103 GLU B CG  1 
ATOM   3332  C CD  . GLU B 2 103 ? 8.298   11.687  16.514  1.00 89.00  ? 103 GLU B CD  1 
ATOM   3333  O OE1 . GLU B 2 103 ? 7.337   12.326  16.986  1.00 96.38  ? 103 GLU B OE1 1 
ATOM   3334  O OE2 . GLU B 2 103 ? 8.609   11.728  15.303  1.00 93.35  ? 103 GLU B OE2 1 
ATOM   3335  N N   . ASN B 2 104 ? 10.728  13.869  20.841  1.00 61.08  ? 104 ASN B N   1 
ATOM   3336  C CA  . ASN B 2 104 ? 10.541  14.742  21.998  1.00 55.85  ? 104 ASN B CA  1 
ATOM   3337  C C   . ASN B 2 104 ? 10.854  16.200  21.680  1.00 56.68  ? 104 ASN B C   1 
ATOM   3338  O O   . ASN B 2 104 ? 10.111  17.103  22.069  1.00 68.18  ? 104 ASN B O   1 
ATOM   3339  C CB  . ASN B 2 104 ? 11.371  14.264  23.186  1.00 46.49  ? 104 ASN B CB  1 
ATOM   3340  C CG  . ASN B 2 104 ? 10.753  13.069  23.869  1.00 55.75  ? 104 ASN B CG  1 
ATOM   3341  O OD1 . ASN B 2 104 ? 9.700   12.585  23.448  1.00 59.43  ? 104 ASN B OD1 1 
ATOM   3342  N ND2 . ASN B 2 104 ? 11.401  12.581  24.926  1.00 55.92  ? 104 ASN B ND2 1 
ATOM   3343  N N   . GLU B 2 105 ? 11.956  16.427  20.971  1.00 46.73  ? 105 GLU B N   1 
ATOM   3344  C CA  . GLU B 2 105 ? 12.289  17.766  20.528  1.00 48.65  ? 105 GLU B CA  1 
ATOM   3345  C C   . GLU B 2 105 ? 11.082  18.290  19.763  1.00 58.91  ? 105 GLU B C   1 
ATOM   3346  O O   . GLU B 2 105 ? 10.693  19.444  19.920  1.00 63.65  ? 105 GLU B O   1 
ATOM   3347  C CB  . GLU B 2 105 ? 13.532  17.754  19.638  1.00 40.96  ? 105 GLU B CB  1 
ATOM   3348  C CG  . GLU B 2 105 ? 14.215  19.113  19.466  1.00 56.24  ? 105 GLU B CG  1 
ATOM   3349  C CD  . GLU B 2 105 ? 15.199  19.444  20.588  1.00 70.95  ? 105 GLU B CD  1 
ATOM   3350  O OE1 . GLU B 2 105 ? 15.209  20.608  21.049  1.00 70.37  ? 105 GLU B OE1 1 
ATOM   3351  O OE2 . GLU B 2 105 ? 15.972  18.549  20.998  1.00 77.25  ? 105 GLU B OE2 1 
ATOM   3352  N N   . HIS B 2 106 ? 10.471  17.432  18.951  1.00 52.68  ? 106 HIS B N   1 
ATOM   3353  C CA  A HIS B 2 106 ? 9.286   17.822  18.190  0.60 53.52  ? 106 HIS B CA  1 
ATOM   3354  C CA  B HIS B 2 106 ? 9.295   17.829  18.190  0.40 53.37  ? 106 HIS B CA  1 
ATOM   3355  C C   . HIS B 2 106 ? 8.105   18.074  19.115  1.00 56.95  ? 106 HIS B C   1 
ATOM   3356  O O   . HIS B 2 106 ? 7.536   19.162  19.123  1.00 66.35  ? 106 HIS B O   1 
ATOM   3357  C CB  A HIS B 2 106 ? 8.917   16.760  17.150  0.60 54.32  ? 106 HIS B CB  1 
ATOM   3358  C CB  B HIS B 2 106 ? 8.955   16.776  17.135  0.40 50.85  ? 106 HIS B CB  1 
ATOM   3359  C CG  A HIS B 2 106 ? 7.675   17.078  16.372  0.60 57.25  ? 106 HIS B CG  1 
ATOM   3360  C CG  B HIS B 2 106 ? 10.020  16.591  16.098  0.40 38.17  ? 106 HIS B CG  1 
ATOM   3361  N ND1 A HIS B 2 106 ? 6.411   16.772  16.829  0.60 55.52  ? 106 HIS B ND1 1 
ATOM   3362  N ND1 B HIS B 2 106 ? 11.362  16.541  16.408  0.40 32.18  ? 106 HIS B ND1 1 
ATOM   3363  C CD2 A HIS B 2 106 ? 7.505   17.668  15.163  0.60 54.81  ? 106 HIS B CD2 1 
ATOM   3364  C CD2 B HIS B 2 106 ? 9.940   16.440  14.755  0.40 37.37  ? 106 HIS B CD2 1 
ATOM   3365  C CE1 A HIS B 2 106 ? 5.517   17.163  15.938  0.60 57.26  ? 106 HIS B CE1 1 
ATOM   3366  C CE1 B HIS B 2 106 ? 12.062  16.362  15.303  0.40 28.27  ? 106 HIS B CE1 1 
ATOM   3367  N NE2 A HIS B 2 106 ? 6.155   17.709  14.918  0.60 54.03  ? 106 HIS B NE2 1 
ATOM   3368  N NE2 B HIS B 2 106 ? 11.222  16.299  14.285  0.40 32.61  ? 106 HIS B NE2 1 
ATOM   3369  N N   . THR B 2 107 ? 7.742   17.060  19.895  1.00 52.78  ? 107 THR B N   1 
ATOM   3370  C CA  . THR B 2 107 ? 6.627   17.179  20.828  1.00 54.22  ? 107 THR B CA  1 
ATOM   3371  C C   . THR B 2 107 ? 6.683   18.506  21.563  1.00 60.40  ? 107 THR B C   1 
ATOM   3372  O O   . THR B 2 107 ? 5.720   19.275  21.549  1.00 67.36  ? 107 THR B O   1 
ATOM   3373  C CB  . THR B 2 107 ? 6.615   16.048  21.874  1.00 56.12  ? 107 THR B CB  1 
ATOM   3374  O OG1 . THR B 2 107 ? 6.281   14.800  21.244  1.00 54.31  ? 107 THR B OG1 1 
ATOM   3375  C CG2 . THR B 2 107 ? 5.592   16.352  22.963  1.00 59.83  ? 107 THR B CG2 1 
ATOM   3376  N N   . LEU B 2 108 ? 7.817   18.771  22.202  1.00 51.75  ? 108 LEU B N   1 
ATOM   3377  C CA  . LEU B 2 108 ? 8.001   20.021  22.933  1.00 48.08  ? 108 LEU B CA  1 
ATOM   3378  C C   . LEU B 2 108 ? 7.807   21.269  22.046  1.00 48.22  ? 108 LEU B C   1 
ATOM   3379  O O   . LEU B 2 108 ? 7.058   22.169  22.408  1.00 56.54  ? 108 LEU B O   1 
ATOM   3380  C CB  . LEU B 2 108 ? 9.364   20.052  23.643  1.00 39.69  ? 108 LEU B CB  1 
ATOM   3381  C CG  . LEU B 2 108 ? 9.572   19.090  24.815  1.00 40.82  ? 108 LEU B CG  1 
ATOM   3382  C CD1 . LEU B 2 108 ? 10.794  19.490  25.637  1.00 35.75  ? 108 LEU B CD1 1 
ATOM   3383  C CD2 . LEU B 2 108 ? 8.341   19.041  25.691  1.00 47.20  ? 108 LEU B CD2 1 
ATOM   3384  N N   . ASP B 2 109 ? 8.474   21.314  20.894  1.00 56.85  ? 109 ASP B N   1 
ATOM   3385  C CA  . ASP B 2 109 ? 8.328   22.445  19.980  1.00 60.16  ? 109 ASP B CA  1 
ATOM   3386  C C   . ASP B 2 109 ? 6.898   22.558  19.460  1.00 64.17  ? 109 ASP B C   1 
ATOM   3387  O O   . ASP B 2 109 ? 6.398   23.657  19.221  1.00 65.20  ? 109 ASP B O   1 
ATOM   3388  C CB  . ASP B 2 109 ? 9.311   22.350  18.811  1.00 62.08  ? 109 ASP B CB  1 
ATOM   3389  C CG  . ASP B 2 109 ? 10.747  22.539  19.245  1.00 64.97  ? 109 ASP B CG  1 
ATOM   3390  O OD1 . ASP B 2 109 ? 10.971  23.012  20.379  1.00 62.51  ? 109 ASP B OD1 1 
ATOM   3391  O OD2 . ASP B 2 109 ? 11.654  22.215  18.449  1.00 66.89  ? 109 ASP B OD2 1 
ATOM   3392  N N   . PHE B 2 110 ? 6.250   21.414  19.276  1.00 52.55  ? 110 PHE B N   1 
ATOM   3393  C CA  . PHE B 2 110 ? 4.839   21.372  18.917  1.00 56.15  ? 110 PHE B CA  1 
ATOM   3394  C C   . PHE B 2 110 ? 4.061   22.228  19.907  1.00 69.80  ? 110 PHE B C   1 
ATOM   3395  O O   . PHE B 2 110 ? 3.311   23.120  19.512  1.00 83.75  ? 110 PHE B O   1 
ATOM   3396  C CB  . PHE B 2 110 ? 4.339   19.922  18.950  1.00 59.97  ? 110 PHE B CB  1 
ATOM   3397  C CG  . PHE B 2 110 ? 2.858   19.769  18.719  1.00 66.93  ? 110 PHE B CG  1 
ATOM   3398  C CD1 . PHE B 2 110 ? 2.252   20.313  17.598  1.00 75.27  ? 110 PHE B CD1 1 
ATOM   3399  C CD2 . PHE B 2 110 ? 2.078   19.046  19.609  1.00 65.20  ? 110 PHE B CD2 1 
ATOM   3400  C CE1 . PHE B 2 110 ? 0.891   20.159  17.383  1.00 81.16  ? 110 PHE B CE1 1 
ATOM   3401  C CE2 . PHE B 2 110 ? 0.721   18.888  19.398  1.00 71.74  ? 110 PHE B CE2 1 
ATOM   3402  C CZ  . PHE B 2 110 ? 0.127   19.446  18.285  1.00 79.50  ? 110 PHE B CZ  1 
ATOM   3403  N N   . HIS B 2 111 ? 4.254   21.959  21.197  1.00 72.26  ? 111 HIS B N   1 
ATOM   3404  C CA  . HIS B 2 111 ? 3.584   22.714  22.253  1.00 69.43  ? 111 HIS B CA  1 
ATOM   3405  C C   . HIS B 2 111 ? 3.857   24.215  22.144  1.00 68.59  ? 111 HIS B C   1 
ATOM   3406  O O   . HIS B 2 111 ? 2.977   25.038  22.398  1.00 74.97  ? 111 HIS B O   1 
ATOM   3407  C CB  . HIS B 2 111 ? 4.008   22.199  23.631  1.00 69.03  ? 111 HIS B CB  1 
ATOM   3408  C CG  . HIS B 2 111 ? 3.250   20.991  24.084  1.00 71.78  ? 111 HIS B CG  1 
ATOM   3409  N ND1 . HIS B 2 111 ? 1.883   20.993  24.255  1.00 74.14  ? 111 HIS B ND1 1 
ATOM   3410  C CD2 . HIS B 2 111 ? 3.668   19.744  24.410  1.00 70.15  ? 111 HIS B CD2 1 
ATOM   3411  C CE1 . HIS B 2 111 ? 1.491   19.800  24.664  1.00 75.24  ? 111 HIS B CE1 1 
ATOM   3412  N NE2 . HIS B 2 111 ? 2.554   19.025  24.768  1.00 69.27  ? 111 HIS B NE2 1 
ATOM   3413  N N   . ASP B 2 112 ? 5.083   24.565  21.768  1.00 64.42  ? 112 ASP B N   1 
ATOM   3414  C CA  . ASP B 2 112 ? 5.448   25.959  21.571  1.00 61.79  ? 112 ASP B CA  1 
ATOM   3415  C C   . ASP B 2 112 ? 4.591   26.527  20.457  1.00 68.73  ? 112 ASP B C   1 
ATOM   3416  O O   . ASP B 2 112 ? 3.792   27.430  20.681  1.00 72.28  ? 112 ASP B O   1 
ATOM   3417  C CB  . ASP B 2 112 ? 6.927   26.086  21.214  1.00 57.10  ? 112 ASP B CB  1 
ATOM   3418  C CG  . ASP B 2 112 ? 7.589   27.259  21.900  1.00 64.82  ? 112 ASP B CG  1 
ATOM   3419  O OD1 . ASP B 2 112 ? 7.080   27.682  22.952  1.00 69.64  ? 112 ASP B OD1 1 
ATOM   3420  O OD2 . ASP B 2 112 ? 8.619   27.755  21.399  1.00 70.48  ? 112 ASP B OD2 1 
ATOM   3421  N N   . SER B 2 113 ? 4.745   25.976  19.258  1.00 56.55  ? 113 SER B N   1 
ATOM   3422  C CA  . SER B 2 113 ? 3.971   26.426  18.108  1.00 56.59  ? 113 SER B CA  1 
ATOM   3423  C C   . SER B 2 113 ? 2.482   26.498  18.403  1.00 59.50  ? 113 SER B C   1 
ATOM   3424  O O   . SER B 2 113 ? 1.794   27.388  17.913  1.00 63.80  ? 113 SER B O   1 
ATOM   3425  C CB  . SER B 2 113 ? 4.200   25.521  16.906  1.00 57.41  ? 113 SER B CB  1 
ATOM   3426  O OG  . SER B 2 113 ? 3.170   25.704  15.949  1.00 61.73  ? 113 SER B OG  1 
ATOM   3427  N N   . ASN B 2 114 ? 1.977   25.558  19.191  1.00 69.60  ? 114 ASN B N   1 
ATOM   3428  C CA  . ASN B 2 114 ? 0.562   25.569  19.559  1.00 75.89  ? 114 ASN B CA  1 
ATOM   3429  C C   . ASN B 2 114 ? 0.175   26.839  20.324  1.00 73.60  ? 114 ASN B C   1 
ATOM   3430  O O   . ASN B 2 114 ? -0.862  27.449  20.054  1.00 73.57  ? 114 ASN B O   1 
ATOM   3431  C CB  . ASN B 2 114 ? 0.200   24.312  20.362  1.00 78.15  ? 114 ASN B CB  1 
ATOM   3432  C CG  . ASN B 2 114 ? -0.400  23.220  19.496  1.00 78.78  ? 114 ASN B CG  1 
ATOM   3433  O OD1 . ASN B 2 114 ? -0.271  23.239  18.271  1.00 76.02  ? 114 ASN B OD1 1 
ATOM   3434  N ND2 . ASN B 2 114 ? -1.071  22.268  20.128  1.00 83.70  ? 114 ASN B ND2 1 
ATOM   3435  N N   . VAL B 2 115 ? 1.025   27.229  21.272  1.00 62.43  ? 115 VAL B N   1 
ATOM   3436  C CA  . VAL B 2 115 ? 0.849   28.468  22.028  1.00 59.42  ? 115 VAL B CA  1 
ATOM   3437  C C   . VAL B 2 115 ? 1.072   29.707  21.157  1.00 62.77  ? 115 VAL B C   1 
ATOM   3438  O O   . VAL B 2 115 ? 0.158   30.503  20.969  1.00 71.47  ? 115 VAL B O   1 
ATOM   3439  C CB  . VAL B 2 115 ? 1.784   28.522  23.256  1.00 49.33  ? 115 VAL B CB  1 
ATOM   3440  C CG1 . VAL B 2 115 ? 1.780   29.906  23.870  1.00 44.44  ? 115 VAL B CG1 1 
ATOM   3441  C CG2 . VAL B 2 115 ? 1.375   27.478  24.283  1.00 52.25  ? 115 VAL B CG2 1 
ATOM   3442  N N   . LYS B 2 116 ? 2.282   29.868  20.629  1.00 66.64  ? 116 LYS B N   1 
ATOM   3443  C CA  . LYS B 2 116 ? 2.595   31.007  19.768  1.00 66.43  ? 116 LYS B CA  1 
ATOM   3444  C C   . LYS B 2 116 ? 1.545   31.210  18.681  1.00 73.92  ? 116 LYS B C   1 
ATOM   3445  O O   . LYS B 2 116 ? 1.290   32.339  18.263  1.00 81.77  ? 116 LYS B O   1 
ATOM   3446  C CB  . LYS B 2 116 ? 3.970   30.852  19.114  1.00 62.94  ? 116 LYS B CB  1 
ATOM   3447  C CG  . LYS B 2 116 ? 4.375   32.044  18.247  1.00 70.36  ? 116 LYS B CG  1 
ATOM   3448  C CD  . LYS B 2 116 ? 5.548   31.707  17.334  1.00 72.53  ? 116 LYS B CD  1 
ATOM   3449  C CE  . LYS B 2 116 ? 6.109   32.950  16.649  1.00 70.98  ? 116 LYS B CE  1 
ATOM   3450  N NZ  . LYS B 2 116 ? 5.081   33.695  15.865  1.00 69.92  ? 116 LYS B NZ  1 
ATOM   3451  N N   . ASN B 2 117 ? 0.946   30.119  18.215  1.00 75.20  ? 117 ASN B N   1 
ATOM   3452  C CA  . ASN B 2 117 ? -0.084  30.202  17.185  1.00 77.36  ? 117 ASN B CA  1 
ATOM   3453  C C   . ASN B 2 117 ? -1.420  30.675  17.733  1.00 86.16  ? 117 ASN B C   1 
ATOM   3454  O O   . ASN B 2 117 ? -2.274  31.143  16.979  1.00 86.02  ? 117 ASN B O   1 
ATOM   3455  C CB  . ASN B 2 117 ? -0.259  28.859  16.483  1.00 77.91  ? 117 ASN B CB  1 
ATOM   3456  C CG  . ASN B 2 117 ? 0.707   28.673  15.328  1.00 77.76  ? 117 ASN B CG  1 
ATOM   3457  O OD1 . ASN B 2 117 ? 1.577   29.516  15.084  1.00 74.57  ? 117 ASN B OD1 1 
ATOM   3458  N ND2 . ASN B 2 117 ? 0.560   27.561  14.610  1.00 75.52  ? 117 ASN B ND2 1 
ATOM   3459  N N   . LEU B 2 118 ? -1.594  30.540  19.046  1.00 56.28  ? 118 LEU B N   1 
ATOM   3460  C CA  . LEU B 2 118 ? -2.786  31.052  19.729  1.00 62.69  ? 118 LEU B CA  1 
ATOM   3461  C C   . LEU B 2 118 ? -2.645  32.537  20.088  1.00 68.21  ? 118 LEU B C   1 
ATOM   3462  O O   . LEU B 2 118 ? -3.556  33.330  19.852  1.00 76.13  ? 118 LEU B O   1 
ATOM   3463  C CB  . LEU B 2 118 ? -3.090  30.244  20.997  1.00 64.80  ? 118 LEU B CB  1 
ATOM   3464  C CG  . LEU B 2 118 ? -4.398  30.625  21.699  1.00 73.35  ? 118 LEU B CG  1 
ATOM   3465  C CD1 . LEU B 2 118 ? -5.587  30.062  20.930  1.00 82.24  ? 118 LEU B CD1 1 
ATOM   3466  C CD2 . LEU B 2 118 ? -4.410  30.145  23.144  1.00 71.35  ? 118 LEU B CD2 1 
ATOM   3467  N N   . TYR B 2 119 ? -1.505  32.893  20.674  1.00 106.62 ? 119 TYR B N   1 
ATOM   3468  C CA  . TYR B 2 119 ? -1.183  34.283  20.971  1.00 105.11 ? 119 TYR B CA  1 
ATOM   3469  C C   . TYR B 2 119 ? -1.412  35.137  19.736  1.00 102.33 ? 119 TYR B C   1 
ATOM   3470  O O   . TYR B 2 119 ? -2.000  36.212  19.814  1.00 112.95 ? 119 TYR B O   1 
ATOM   3471  C CB  . TYR B 2 119 ? 0.272   34.405  21.429  1.00 102.49 ? 119 TYR B CB  1 
ATOM   3472  C CG  . TYR B 2 119 ? 0.766   35.828  21.570  1.00 99.35  ? 119 TYR B CG  1 
ATOM   3473  C CD1 . TYR B 2 119 ? 0.507   36.562  22.720  1.00 101.53 ? 119 TYR B CD1 1 
ATOM   3474  C CD2 . TYR B 2 119 ? 1.500   36.433  20.557  1.00 96.28  ? 119 TYR B CD2 1 
ATOM   3475  C CE1 . TYR B 2 119 ? 0.957   37.861  22.858  1.00 103.75 ? 119 TYR B CE1 1 
ATOM   3476  C CE2 . TYR B 2 119 ? 1.955   37.731  20.684  1.00 98.31  ? 119 TYR B CE2 1 
ATOM   3477  C CZ  . TYR B 2 119 ? 1.679   38.444  21.838  1.00 102.17 ? 119 TYR B CZ  1 
ATOM   3478  O OH  . TYR B 2 119 ? 2.127   39.740  21.974  1.00 103.70 ? 119 TYR B OH  1 
ATOM   3479  N N   . ASP B 2 120 ? -0.947  34.647  18.595  1.00 69.75  ? 120 ASP B N   1 
ATOM   3480  C CA  . ASP B 2 120 ? -1.142  35.348  17.335  1.00 78.24  ? 120 ASP B CA  1 
ATOM   3481  C C   . ASP B 2 120 ? -2.608  35.357  16.901  1.00 86.76  ? 120 ASP B C   1 
ATOM   3482  O O   . ASP B 2 120 ? -3.099  36.354  16.373  1.00 85.74  ? 120 ASP B O   1 
ATOM   3483  C CB  . ASP B 2 120 ? -0.258  34.749  16.237  1.00 76.76  ? 120 ASP B CB  1 
ATOM   3484  C CG  . ASP B 2 120 ? 1.217   35.052  16.443  1.00 70.62  ? 120 ASP B CG  1 
ATOM   3485  O OD1 . ASP B 2 120 ? 1.537   36.064  17.116  1.00 73.02  ? 120 ASP B OD1 1 
ATOM   3486  O OD2 . ASP B 2 120 ? 2.057   34.282  15.925  1.00 64.76  ? 120 ASP B OD2 1 
ATOM   3487  N N   . LYS B 2 121 ? -3.306  34.247  17.119  1.00 92.13  ? 121 LYS B N   1 
ATOM   3488  C CA  . LYS B 2 121 ? -4.729  34.181  16.806  1.00 99.13  ? 121 LYS B CA  1 
ATOM   3489  C C   . LYS B 2 121 ? -5.437  35.373  17.436  1.00 101.93 ? 121 LYS B C   1 
ATOM   3490  O O   . LYS B 2 121 ? -6.299  35.997  16.818  1.00 110.94 ? 121 LYS B O   1 
ATOM   3491  C CB  . LYS B 2 121 ? -5.334  32.868  17.314  1.00 104.02 ? 121 LYS B CB  1 
ATOM   3492  C CG  . LYS B 2 121 ? -6.856  32.790  17.225  1.00 115.03 ? 121 LYS B CG  1 
ATOM   3493  C CD  . LYS B 2 121 ? -7.370  31.465  17.771  1.00 113.87 ? 121 LYS B CD  1 
ATOM   3494  C CE  . LYS B 2 121 ? -8.890  31.424  17.806  1.00 116.61 ? 121 LYS B CE  1 
ATOM   3495  N NZ  . LYS B 2 121 ? -9.462  32.383  18.792  1.00 116.22 ? 121 LYS B NZ  1 
ATOM   3496  N N   . VAL B 2 122 ? -5.044  35.686  18.669  1.00 81.89  ? 122 VAL B N   1 
ATOM   3497  C CA  . VAL B 2 122 ? -5.629  36.785  19.434  1.00 76.44  ? 122 VAL B CA  1 
ATOM   3498  C C   . VAL B 2 122 ? -5.078  38.153  19.013  1.00 69.91  ? 122 VAL B C   1 
ATOM   3499  O O   . VAL B 2 122 ? -5.842  39.075  18.731  1.00 75.40  ? 122 VAL B O   1 
ATOM   3500  C CB  . VAL B 2 122 ? -5.416  36.589  20.956  1.00 74.85  ? 122 VAL B CB  1 
ATOM   3501  C CG1 . VAL B 2 122 ? -5.636  37.898  21.703  1.00 75.16  ? 122 VAL B CG1 1 
ATOM   3502  C CG2 . VAL B 2 122 ? -6.330  35.492  21.493  1.00 78.88  ? 122 VAL B CG2 1 
ATOM   3503  N N   . ARG B 2 123 ? -3.755  38.280  18.980  1.00 78.39  ? 123 ARG B N   1 
ATOM   3504  C CA  . ARG B 2 123 ? -3.116  39.513  18.537  1.00 81.29  ? 123 ARG B CA  1 
ATOM   3505  C C   . ARG B 2 123 ? -3.703  40.024  17.224  1.00 89.17  ? 123 ARG B C   1 
ATOM   3506  O O   . ARG B 2 123 ? -4.069  41.193  17.114  1.00 93.15  ? 123 ARG B O   1 
ATOM   3507  C CB  . ARG B 2 123 ? -1.607  39.316  18.373  1.00 80.63  ? 123 ARG B CB  1 
ATOM   3508  C CG  . ARG B 2 123 ? -0.931  40.441  17.596  1.00 84.72  ? 123 ARG B CG  1 
ATOM   3509  C CD  . ARG B 2 123 ? 0.556   40.202  17.409  1.00 88.27  ? 123 ARG B CD  1 
ATOM   3510  N NE  . ARG B 2 123 ? 0.830   39.030  16.578  1.00 93.67  ? 123 ARG B NE  1 
ATOM   3511  C CZ  . ARG B 2 123 ? 1.014   39.066  15.260  1.00 97.61  ? 123 ARG B CZ  1 
ATOM   3512  N NH1 . ARG B 2 123 ? 0.950   40.222  14.608  1.00 96.68  ? 123 ARG B NH1 1 
ATOM   3513  N NH2 . ARG B 2 123 ? 1.262   37.942  14.593  1.00 97.72  ? 123 ARG B NH2 1 
ATOM   3514  N N   . MET B 2 124 ? -3.790  39.144  16.231  1.00 106.59 ? 124 MET B N   1 
ATOM   3515  C CA  . MET B 2 124 ? -4.200  39.544  14.886  1.00 111.02 ? 124 MET B CA  1 
ATOM   3516  C C   . MET B 2 124 ? -5.673  39.939  14.805  1.00 117.84 ? 124 MET B C   1 
ATOM   3517  O O   . MET B 2 124 ? -6.134  40.430  13.775  1.00 120.67 ? 124 MET B O   1 
ATOM   3518  C CB  . MET B 2 124 ? -3.885  38.433  13.879  1.00 107.80 ? 124 MET B CB  1 
ATOM   3519  C CG  . MET B 2 124 ? -2.430  37.981  13.907  1.00 100.55 ? 124 MET B CG  1 
ATOM   3520  S SD  . MET B 2 124 ? -2.044  36.641  12.760  1.00 169.19 ? 124 MET B SD  1 
ATOM   3521  C CE  . MET B 2 124 ? -2.093  37.505  11.192  1.00 117.92 ? 124 MET B CE  1 
ATOM   3522  N N   . GLN B 2 125 ? -6.403  39.723  15.896  1.00 87.39  ? 125 GLN B N   1 
ATOM   3523  C CA  . GLN B 2 125 ? -7.811  40.105  15.977  1.00 94.47  ? 125 GLN B CA  1 
ATOM   3524  C C   . GLN B 2 125 ? -7.974  41.484  16.603  1.00 97.89  ? 125 GLN B C   1 
ATOM   3525  O O   . GLN B 2 125 ? -8.902  42.222  16.273  1.00 106.04 ? 125 GLN B O   1 
ATOM   3526  C CB  . GLN B 2 125 ? -8.604  39.084  16.798  1.00 99.70  ? 125 GLN B CB  1 
ATOM   3527  C CG  . GLN B 2 125 ? -9.443  38.121  15.975  1.00 105.72 ? 125 GLN B CG  1 
ATOM   3528  C CD  . GLN B 2 125 ? -10.358 37.278  16.837  1.00 112.64 ? 125 GLN B CD  1 
ATOM   3529  O OE1 . GLN B 2 125 ? -10.975 37.775  17.779  1.00 119.30 ? 125 GLN B OE1 1 
ATOM   3530  N NE2 . GLN B 2 125 ? -10.441 35.988  16.528  1.00 110.85 ? 125 GLN B NE2 1 
ATOM   3531  N N   . LEU B 2 126 ? -7.065  41.822  17.513  1.00 83.23  ? 126 LEU B N   1 
ATOM   3532  C CA  . LEU B 2 126 ? -7.148  43.074  18.254  1.00 79.04  ? 126 LEU B CA  1 
ATOM   3533  C C   . LEU B 2 126 ? -6.457  44.230  17.535  1.00 76.73  ? 126 LEU B C   1 
ATOM   3534  O O   . LEU B 2 126 ? -7.067  45.268  17.296  1.00 78.41  ? 126 LEU B O   1 
ATOM   3535  C CB  . LEU B 2 126 ? -6.564  42.898  19.653  1.00 74.25  ? 126 LEU B CB  1 
ATOM   3536  C CG  . LEU B 2 126 ? -7.072  41.685  20.429  1.00 78.08  ? 126 LEU B CG  1 
ATOM   3537  C CD1 . LEU B 2 126 ? -6.701  41.800  21.900  1.00 78.98  ? 126 LEU B CD1 1 
ATOM   3538  C CD2 . LEU B 2 126 ? -8.575  41.530  20.263  1.00 84.05  ? 126 LEU B CD2 1 
ATOM   3539  N N   . ARG B 2 127 ? -5.186  44.049  17.195  1.00 100.97 ? 127 ARG B N   1 
ATOM   3540  C CA  . ARG B 2 127 ? -4.414  45.091  16.523  1.00 97.51  ? 127 ARG B CA  1 
ATOM   3541  C C   . ARG B 2 127 ? -4.181  46.301  17.420  1.00 103.96 ? 127 ARG B C   1 
ATOM   3542  O O   . ARG B 2 127 ? -3.638  46.181  18.519  1.00 106.62 ? 127 ARG B O   1 
ATOM   3543  C CB  . ARG B 2 127 ? -5.102  45.535  15.230  1.00 92.17  ? 127 ARG B CB  1 
ATOM   3544  C CG  . ARG B 2 127 ? -4.804  44.666  14.032  1.00 86.50  ? 127 ARG B CG  1 
ATOM   3545  C CD  . ARG B 2 127 ? -5.449  45.232  12.786  1.00 96.70  ? 127 ARG B CD  1 
ATOM   3546  N NE  . ARG B 2 127 ? -6.863  44.885  12.695  1.00 115.20 ? 127 ARG B NE  1 
ATOM   3547  C CZ  . ARG B 2 127 ? -7.726  45.484  11.881  1.00 127.58 ? 127 ARG B CZ  1 
ATOM   3548  N NH1 . ARG B 2 127 ? -7.320  46.473  11.094  1.00 129.06 ? 127 ARG B NH1 1 
ATOM   3549  N NH2 . ARG B 2 127 ? -8.996  45.102  11.859  1.00 133.29 ? 127 ARG B NH2 1 
ATOM   3550  N N   . ASP B 2 128 ? -4.605  47.467  16.939  1.00 120.92 ? 128 ASP B N   1 
ATOM   3551  C CA  . ASP B 2 128 ? -4.378  48.732  17.635  1.00 117.30 ? 128 ASP B CA  1 
ATOM   3552  C C   . ASP B 2 128 ? -5.305  48.943  18.831  1.00 113.62 ? 128 ASP B C   1 
ATOM   3553  O O   . ASP B 2 128 ? -5.043  49.793  19.680  1.00 107.88 ? 128 ASP B O   1 
ATOM   3554  C CB  . ASP B 2 128 ? -4.499  49.903  16.660  1.00 120.79 ? 128 ASP B CB  1 
ATOM   3555  C CG  . ASP B 2 128 ? -5.725  49.799  15.777  1.00 132.10 ? 128 ASP B CG  1 
ATOM   3556  O OD1 . ASP B 2 128 ? -6.707  49.146  16.191  1.00 137.43 ? 128 ASP B OD1 1 
ATOM   3557  O OD2 . ASP B 2 128 ? -5.705  50.372  14.666  1.00 135.51 ? 128 ASP B OD2 1 
ATOM   3558  N N   . ASN B 2 129 ? -6.385  48.171  18.900  1.00 81.27  ? 129 ASN B N   1 
ATOM   3559  C CA  . ASN B 2 129 ? -7.306  48.256  20.031  1.00 87.39  ? 129 ASN B CA  1 
ATOM   3560  C C   . ASN B 2 129 ? -6.659  47.822  21.348  1.00 91.04  ? 129 ASN B C   1 
ATOM   3561  O O   . ASN B 2 129 ? -7.324  47.771  22.385  1.00 98.22  ? 129 ASN B O   1 
ATOM   3562  C CB  . ASN B 2 129 ? -8.567  47.425  19.776  1.00 88.13  ? 129 ASN B CB  1 
ATOM   3563  C CG  . ASN B 2 129 ? -9.378  47.934  18.596  1.00 85.38  ? 129 ASN B CG  1 
ATOM   3564  O OD1 . ASN B 2 129 ? -8.902  48.747  17.799  1.00 85.54  ? 129 ASN B OD1 1 
ATOM   3565  N ND2 . ASN B 2 129 ? -10.612 47.449  18.477  1.00 82.13  ? 129 ASN B ND2 1 
ATOM   3566  N N   . VAL B 2 130 ? -5.364  47.513  21.301  1.00 96.74  ? 130 VAL B N   1 
ATOM   3567  C CA  . VAL B 2 130 ? -4.638  47.044  22.481  1.00 91.42  ? 130 VAL B CA  1 
ATOM   3568  C C   . VAL B 2 130 ? -3.134  47.341  22.448  1.00 82.70  ? 130 VAL B C   1 
ATOM   3569  O O   . VAL B 2 130 ? -2.523  47.453  21.382  1.00 75.37  ? 130 VAL B O   1 
ATOM   3570  C CB  . VAL B 2 130 ? -4.827  45.525  22.698  1.00 91.86  ? 130 VAL B CB  1 
ATOM   3571  C CG1 . VAL B 2 130 ? -6.199  45.223  23.280  1.00 97.38  ? 130 VAL B CG1 1 
ATOM   3572  C CG2 . VAL B 2 130 ? -4.616  44.777  21.395  1.00 87.90  ? 130 VAL B CG2 1 
ATOM   3573  N N   . LYS B 2 131 ? -2.553  47.465  23.637  1.00 126.11 ? 131 LYS B N   1 
ATOM   3574  C CA  . LYS B 2 131 ? -1.122  47.664  23.810  1.00 120.25 ? 131 LYS B CA  1 
ATOM   3575  C C   . LYS B 2 131 ? -0.463  46.296  23.901  1.00 120.93 ? 131 LYS B C   1 
ATOM   3576  O O   . LYS B 2 131 ? -0.673  45.570  24.872  1.00 130.33 ? 131 LYS B O   1 
ATOM   3577  C CB  . LYS B 2 131 ? -0.867  48.427  25.112  1.00 119.28 ? 131 LYS B CB  1 
ATOM   3578  C CG  . LYS B 2 131 ? -0.070  49.716  24.989  1.00 117.09 ? 131 LYS B CG  1 
ATOM   3579  C CD  . LYS B 2 131 ? -0.132  50.492  26.304  1.00 123.22 ? 131 LYS B CD  1 
ATOM   3580  C CE  . LYS B 2 131 ? 0.603   51.821  26.225  1.00 124.27 ? 131 LYS B CE  1 
ATOM   3581  N NZ  . LYS B 2 131 ? 2.085   51.669  26.250  1.00 120.61 ? 131 LYS B NZ  1 
ATOM   3582  N N   . GLU B 2 132 ? 0.324   45.935  22.894  1.00 93.18  ? 132 GLU B N   1 
ATOM   3583  C CA  . GLU B 2 132 ? 1.016   44.650  22.907  1.00 84.24  ? 132 GLU B CA  1 
ATOM   3584  C C   . GLU B 2 132 ? 2.161   44.684  23.913  1.00 84.67  ? 132 GLU B C   1 
ATOM   3585  O O   . GLU B 2 132 ? 3.325   44.802  23.535  1.00 84.42  ? 132 GLU B O   1 
ATOM   3586  C CB  . GLU B 2 132 ? 1.532   44.299  21.506  1.00 78.62  ? 132 GLU B CB  1 
ATOM   3587  C CG  . GLU B 2 132 ? 2.172   42.918  21.382  1.00 78.62  ? 132 GLU B CG  1 
ATOM   3588  C CD  . GLU B 2 132 ? 2.280   42.450  19.934  1.00 79.15  ? 132 GLU B CD  1 
ATOM   3589  O OE1 . GLU B 2 132 ? 1.878   43.217  19.029  1.00 87.32  ? 132 GLU B OE1 1 
ATOM   3590  O OE2 . GLU B 2 132 ? 2.757   41.312  19.701  1.00 69.86  ? 132 GLU B OE2 1 
ATOM   3591  N N   . LEU B 2 133 ? 1.817   44.581  25.195  1.00 73.11  ? 133 LEU B N   1 
ATOM   3592  C CA  . LEU B 2 133 ? 2.795   44.681  26.282  1.00 68.37  ? 133 LEU B CA  1 
ATOM   3593  C C   . LEU B 2 133 ? 4.150   44.058  25.949  1.00 71.33  ? 133 LEU B C   1 
ATOM   3594  O O   . LEU B 2 133 ? 5.196   44.636  26.248  1.00 72.45  ? 133 LEU B O   1 
ATOM   3595  C CB  . LEU B 2 133 ? 2.235   44.084  27.574  1.00 62.93  ? 133 LEU B CB  1 
ATOM   3596  C CG  . LEU B 2 133 ? 1.256   44.981  28.330  1.00 65.14  ? 133 LEU B CG  1 
ATOM   3597  C CD1 . LEU B 2 133 ? 0.808   44.331  29.629  1.00 63.88  ? 133 LEU B CD1 1 
ATOM   3598  C CD2 . LEU B 2 133 ? 1.898   46.332  28.608  1.00 69.50  ? 133 LEU B CD2 1 
ATOM   3599  N N   . GLY B 2 134 ? 4.124   42.882  25.326  1.00 98.16  ? 134 GLY B N   1 
ATOM   3600  C CA  . GLY B 2 134 ? 5.338   42.210  24.903  1.00 95.30  ? 134 GLY B CA  1 
ATOM   3601  C C   . GLY B 2 134 ? 5.723   41.067  25.820  1.00 98.62  ? 134 GLY B C   1 
ATOM   3602  O O   . GLY B 2 134 ? 6.892   40.693  25.893  1.00 104.50 ? 134 GLY B O   1 
ATOM   3603  N N   . ASN B 2 135 ? 4.738   40.505  26.517  1.00 73.00  ? 135 ASN B N   1 
ATOM   3604  C CA  . ASN B 2 135 ? 4.999   39.438  27.478  1.00 66.83  ? 135 ASN B CA  1 
ATOM   3605  C C   . ASN B 2 135 ? 3.879   38.402  27.529  1.00 68.74  ? 135 ASN B C   1 
ATOM   3606  O O   . ASN B 2 135 ? 3.754   37.656  28.503  1.00 66.64  ? 135 ASN B O   1 
ATOM   3607  C CB  . ASN B 2 135 ? 5.208   40.022  28.872  1.00 71.16  ? 135 ASN B CB  1 
ATOM   3608  C CG  . ASN B 2 135 ? 3.906   40.445  29.523  1.00 82.06  ? 135 ASN B CG  1 
ATOM   3609  O OD1 . ASN B 2 135 ? 2.876   40.580  28.856  1.00 85.23  ? 135 ASN B OD1 1 
ATOM   3610  N ND2 . ASN B 2 135 ? 3.942   40.657  30.835  1.00 87.86  ? 135 ASN B ND2 1 
ATOM   3611  N N   . GLY B 2 136 ? 3.063   38.364  26.479  1.00 72.90  ? 136 GLY B N   1 
ATOM   3612  C CA  . GLY B 2 136 ? 1.943   37.443  26.419  1.00 77.10  ? 136 GLY B CA  1 
ATOM   3613  C C   . GLY B 2 136 ? 0.629   38.115  26.764  1.00 91.58  ? 136 GLY B C   1 
ATOM   3614  O O   . GLY B 2 136 ? -0.442  37.534  26.589  1.00 98.40  ? 136 GLY B O   1 
ATOM   3615  N N   . CYS B 2 137 ? 0.717   39.347  27.258  1.00 81.81  ? 137 CYS B N   1 
ATOM   3616  C CA  . CYS B 2 137 ? -0.464  40.129  27.602  1.00 86.02  ? 137 CYS B CA  1 
ATOM   3617  C C   . CYS B 2 137 ? -0.768  41.164  26.529  1.00 92.23  ? 137 CYS B C   1 
ATOM   3618  O O   . CYS B 2 137 ? 0.086   41.485  25.703  1.00 92.16  ? 137 CYS B O   1 
ATOM   3619  C CB  . CYS B 2 137 ? -0.262  40.841  28.937  1.00 87.12  ? 137 CYS B CB  1 
ATOM   3620  S SG  . CYS B 2 137 ? 0.027   39.756  30.340  1.00 79.99  ? 137 CYS B SG  1 
ATOM   3621  N N   . PHE B 2 138 ? -1.996  41.670  26.548  1.00 138.67 ? 138 PHE B N   1 
ATOM   3622  C CA  . PHE B 2 138 ? -2.387  42.818  25.738  1.00 140.69 ? 138 PHE B CA  1 
ATOM   3623  C C   . PHE B 2 138 ? -3.116  43.799  26.652  1.00 150.43 ? 138 PHE B C   1 
ATOM   3624  O O   . PHE B 2 138 ? -4.004  43.401  27.404  1.00 159.09 ? 138 PHE B O   1 
ATOM   3625  C CB  . PHE B 2 138 ? -3.323  42.404  24.596  1.00 138.07 ? 138 PHE B CB  1 
ATOM   3626  C CG  . PHE B 2 138 ? -2.732  41.398  23.641  1.00 128.57 ? 138 PHE B CG  1 
ATOM   3627  C CD1 . PHE B 2 138 ? -1.897  41.801  22.615  1.00 119.59 ? 138 PHE B CD1 1 
ATOM   3628  C CD2 . PHE B 2 138 ? -3.038  40.051  23.756  1.00 130.73 ? 138 PHE B CD2 1 
ATOM   3629  C CE1 . PHE B 2 138 ? -1.364  40.878  21.732  1.00 118.80 ? 138 PHE B CE1 1 
ATOM   3630  C CE2 . PHE B 2 138 ? -2.509  39.124  22.875  1.00 126.92 ? 138 PHE B CE2 1 
ATOM   3631  C CZ  . PHE B 2 138 ? -1.672  39.538  21.862  1.00 121.60 ? 138 PHE B CZ  1 
ATOM   3632  N N   . GLU B 2 139 ? -2.743  45.075  26.602  1.00 124.73 ? 139 GLU B N   1 
ATOM   3633  C CA  . GLU B 2 139 ? -3.455  46.083  27.381  1.00 127.88 ? 139 GLU B CA  1 
ATOM   3634  C C   . GLU B 2 139 ? -4.514  46.750  26.515  1.00 127.55 ? 139 GLU B C   1 
ATOM   3635  O O   . GLU B 2 139 ? -4.243  47.140  25.385  1.00 117.79 ? 139 GLU B O   1 
ATOM   3636  C CB  . GLU B 2 139 ? -2.498  47.127  27.961  1.00 130.00 ? 139 GLU B CB  1 
ATOM   3637  C CG  . GLU B 2 139 ? -3.142  48.019  29.018  1.00 138.53 ? 139 GLU B CG  1 
ATOM   3638  C CD  . GLU B 2 139 ? -2.224  49.128  29.499  1.00 139.12 ? 139 GLU B CD  1 
ATOM   3639  O OE1 . GLU B 2 139 ? -1.014  49.080  29.191  1.00 134.51 ? 139 GLU B OE1 1 
ATOM   3640  O OE2 . GLU B 2 139 ? -2.717  50.053  30.180  1.00 146.10 ? 139 GLU B OE2 1 
ATOM   3641  N N   . PHE B 2 140 ? -5.723  46.874  27.052  1.00 128.47 ? 140 PHE B N   1 
ATOM   3642  C CA  . PHE B 2 140 ? -6.847  47.406  26.293  1.00 134.96 ? 140 PHE B CA  1 
ATOM   3643  C C   . PHE B 2 140 ? -6.958  48.923  26.378  1.00 138.46 ? 140 PHE B C   1 
ATOM   3644  O O   . PHE B 2 140 ? -6.863  49.511  27.457  1.00 142.67 ? 140 PHE B O   1 
ATOM   3645  C CB  . PHE B 2 140 ? -8.155  46.762  26.755  1.00 142.98 ? 140 PHE B CB  1 
ATOM   3646  C CG  . PHE B 2 140 ? -8.262  45.308  26.413  1.00 145.68 ? 140 PHE B CG  1 
ATOM   3647  C CD1 . PHE B 2 140 ? -8.842  44.906  25.223  1.00 147.12 ? 140 PHE B CD1 1 
ATOM   3648  C CD2 . PHE B 2 140 ? -7.778  44.341  27.278  1.00 146.06 ? 140 PHE B CD2 1 
ATOM   3649  C CE1 . PHE B 2 140 ? -8.941  43.569  24.901  1.00 146.54 ? 140 PHE B CE1 1 
ATOM   3650  C CE2 . PHE B 2 140 ? -7.873  43.000  26.961  1.00 145.72 ? 140 PHE B CE2 1 
ATOM   3651  C CZ  . PHE B 2 140 ? -8.457  42.615  25.771  1.00 145.99 ? 140 PHE B CZ  1 
ATOM   3652  N N   . TYR B 2 141 ? -7.161  49.548  25.224  1.00 130.12 ? 141 TYR B N   1 
ATOM   3653  C CA  . TYR B 2 141 ? -7.424  50.976  25.164  1.00 127.78 ? 141 TYR B CA  1 
ATOM   3654  C C   . TYR B 2 141 ? -8.905  51.242  25.405  1.00 134.43 ? 141 TYR B C   1 
ATOM   3655  O O   . TYR B 2 141 ? -9.449  52.249  24.950  1.00 139.10 ? 141 TYR B O   1 
ATOM   3656  C CB  . TYR B 2 141 ? -6.982  51.545  23.816  1.00 122.83 ? 141 TYR B CB  1 
ATOM   3657  C CG  . TYR B 2 141 ? -5.485  51.709  23.699  1.00 116.41 ? 141 TYR B CG  1 
ATOM   3658  C CD1 . TYR B 2 141 ? -4.732  52.152  24.779  1.00 117.08 ? 141 TYR B CD1 1 
ATOM   3659  C CD2 . TYR B 2 141 ? -4.824  51.415  22.516  1.00 114.12 ? 141 TYR B CD2 1 
ATOM   3660  C CE1 . TYR B 2 141 ? -3.364  52.304  24.682  1.00 114.19 ? 141 TYR B CE1 1 
ATOM   3661  C CE2 . TYR B 2 141 ? -3.455  51.562  22.410  1.00 113.11 ? 141 TYR B CE2 1 
ATOM   3662  C CZ  . TYR B 2 141 ? -2.731  52.007  23.496  1.00 114.05 ? 141 TYR B CZ  1 
ATOM   3663  O OH  . TYR B 2 141 ? -1.367  52.155  23.395  1.00 113.71 ? 141 TYR B OH  1 
ATOM   3664  N N   . HIS B 2 142 ? -9.547  50.323  26.121  1.00 119.67 ? 142 HIS B N   1 
ATOM   3665  C CA  . HIS B 2 142 ? -10.943 50.470  26.515  1.00 125.59 ? 142 HIS B CA  1 
ATOM   3666  C C   . HIS B 2 142 ? -11.348 49.357  27.475  1.00 130.26 ? 142 HIS B C   1 
ATOM   3667  O O   . HIS B 2 142 ? -10.888 48.224  27.348  1.00 124.51 ? 142 HIS B O   1 
ATOM   3668  C CB  . HIS B 2 142 ? -11.862 50.471  25.292  1.00 125.42 ? 142 HIS B CB  1 
ATOM   3669  C CG  . HIS B 2 142 ? -11.892 49.169  24.556  1.00 119.27 ? 142 HIS B CG  1 
ATOM   3670  N ND1 . HIS B 2 142 ? -11.205 48.965  23.379  1.00 111.94 ? 142 HIS B ND1 1 
ATOM   3671  C CD2 . HIS B 2 142 ? -12.529 48.006  24.826  1.00 123.67 ? 142 HIS B CD2 1 
ATOM   3672  C CE1 . HIS B 2 142 ? -11.413 47.730  22.959  1.00 112.20 ? 142 HIS B CE1 1 
ATOM   3673  N NE2 . HIS B 2 142 ? -12.215 47.127  23.818  1.00 119.43 ? 142 HIS B NE2 1 
ATOM   3674  N N   . LYS B 2 143 ? -12.203 49.686  28.437  1.00 118.01 ? 143 LYS B N   1 
ATOM   3675  C CA  . LYS B 2 143 ? -12.689 48.699  29.395  1.00 127.83 ? 143 LYS B CA  1 
ATOM   3676  C C   . LYS B 2 143 ? -13.331 47.513  28.682  1.00 131.80 ? 143 LYS B C   1 
ATOM   3677  O O   . LYS B 2 143 ? -14.241 47.680  27.870  1.00 134.12 ? 143 LYS B O   1 
ATOM   3678  C CB  . LYS B 2 143 ? -13.689 49.334  30.365  1.00 138.32 ? 143 LYS B CB  1 
ATOM   3679  C CG  . LYS B 2 143 ? -13.090 50.393  31.275  1.00 139.55 ? 143 LYS B CG  1 
ATOM   3680  C CD  . LYS B 2 143 ? -12.015 49.805  32.176  1.00 139.88 ? 143 LYS B CD  1 
ATOM   3681  C CE  . LYS B 2 143 ? -11.414 50.862  33.090  1.00 141.97 ? 143 LYS B CE  1 
ATOM   3682  N NZ  . LYS B 2 143 ? -10.387 50.294  34.011  1.00 140.58 ? 143 LYS B NZ  1 
ATOM   3683  N N   . CYS B 2 144 ? -12.849 46.314  28.985  1.00 181.50 ? 144 CYS B N   1 
ATOM   3684  C CA  . CYS B 2 144 ? -13.378 45.106  28.366  1.00 189.60 ? 144 CYS B CA  1 
ATOM   3685  C C   . CYS B 2 144 ? -13.948 44.177  29.434  1.00 197.84 ? 144 CYS B C   1 
ATOM   3686  O O   . CYS B 2 144 ? -13.202 43.578  30.210  1.00 193.90 ? 144 CYS B O   1 
ATOM   3687  C CB  . CYS B 2 144 ? -12.286 44.393  27.563  1.00 182.18 ? 144 CYS B CB  1 
ATOM   3688  S SG  . CYS B 2 144 ? -12.895 43.382  26.189  1.00 195.20 ? 144 CYS B SG  1 
ATOM   3689  N N   . ASP B 2 145 ? -15.273 44.067  29.475  1.00 159.08 ? 145 ASP B N   1 
ATOM   3690  C CA  . ASP B 2 145 ? -15.939 43.247  30.483  1.00 163.43 ? 145 ASP B CA  1 
ATOM   3691  C C   . ASP B 2 145 ? -15.918 41.761  30.127  1.00 156.34 ? 145 ASP B C   1 
ATOM   3692  O O   . ASP B 2 145 ? -15.215 41.343  29.209  1.00 150.15 ? 145 ASP B O   1 
ATOM   3693  C CB  . ASP B 2 145 ? -17.373 43.732  30.727  1.00 175.13 ? 145 ASP B CB  1 
ATOM   3694  C CG  . ASP B 2 145 ? -18.252 43.619  29.494  1.00 177.96 ? 145 ASP B CG  1 
ATOM   3695  O OD1 . ASP B 2 145 ? -19.479 43.461  29.659  1.00 184.02 ? 145 ASP B OD1 1 
ATOM   3696  O OD2 . ASP B 2 145 ? -17.723 43.690  28.364  1.00 174.33 ? 145 ASP B OD2 1 
ATOM   3697  N N   . ASP B 2 146 ? -16.694 40.970  30.860  1.00 124.38 ? 146 ASP B N   1 
ATOM   3698  C CA  . ASP B 2 146 ? -16.695 39.523  30.686  1.00 117.33 ? 146 ASP B CA  1 
ATOM   3699  C C   . ASP B 2 146 ? -17.227 39.077  29.323  1.00 122.08 ? 146 ASP B C   1 
ATOM   3700  O O   . ASP B 2 146 ? -16.617 38.235  28.667  1.00 119.04 ? 146 ASP B O   1 
ATOM   3701  C CB  . ASP B 2 146 ? -17.467 38.842  31.821  1.00 117.73 ? 146 ASP B CB  1 
ATOM   3702  C CG  . ASP B 2 146 ? -16.774 38.988  33.166  1.00 106.15 ? 146 ASP B CG  1 
ATOM   3703  O OD1 . ASP B 2 146 ? -15.946 39.916  33.313  1.00 92.21  ? 146 ASP B OD1 1 
ATOM   3704  O OD2 . ASP B 2 146 ? -17.058 38.178  34.075  1.00 107.72 ? 146 ASP B OD2 1 
ATOM   3705  N N   . GLU B 2 147 ? -18.354 39.640  28.896  1.00 161.80 ? 147 GLU B N   1 
ATOM   3706  C CA  . GLU B 2 147 ? -18.956 39.256  27.618  1.00 161.39 ? 147 GLU B CA  1 
ATOM   3707  C C   . GLU B 2 147 ? -18.046 39.563  26.430  1.00 155.27 ? 147 GLU B C   1 
ATOM   3708  O O   . GLU B 2 147 ? -18.162 38.942  25.371  1.00 152.25 ? 147 GLU B O   1 
ATOM   3709  C CB  . GLU B 2 147 ? -20.328 39.915  27.436  1.00 166.03 ? 147 GLU B CB  1 
ATOM   3710  C CG  . GLU B 2 147 ? -20.363 41.404  27.758  1.00 168.00 ? 147 GLU B CG  1 
ATOM   3711  C CD  . GLU B 2 147 ? -20.352 42.286  26.521  1.00 161.85 ? 147 GLU B CD  1 
ATOM   3712  O OE1 . GLU B 2 147 ? -20.159 43.512  26.670  1.00 162.94 ? 147 GLU B OE1 1 
ATOM   3713  O OE2 . GLU B 2 147 ? -20.544 41.760  25.404  1.00 154.88 ? 147 GLU B OE2 1 
ATOM   3714  N N   . CYS B 2 148 ? -17.140 40.520  26.618  1.00 163.43 ? 148 CYS B N   1 
ATOM   3715  C CA  . CYS B 2 148 ? -16.179 40.897  25.585  1.00 154.02 ? 148 CYS B CA  1 
ATOM   3716  C C   . CYS B 2 148 ? -15.048 39.879  25.484  1.00 142.12 ? 148 CYS B C   1 
ATOM   3717  O O   . CYS B 2 148 ? -14.835 39.275  24.433  1.00 137.73 ? 148 CYS B O   1 
ATOM   3718  C CB  . CYS B 2 148 ? -15.605 42.288  25.870  1.00 150.94 ? 148 CYS B CB  1 
ATOM   3719  S SG  . CYS B 2 148 ? -14.237 42.782  24.787  1.00 197.22 ? 148 CYS B SG  1 
ATOM   3720  N N   . MET B 2 149 ? -14.324 39.702  26.585  1.00 130.94 ? 149 MET B N   1 
ATOM   3721  C CA  . MET B 2 149 ? -13.245 38.726  26.651  1.00 119.48 ? 149 MET B CA  1 
ATOM   3722  C C   . MET B 2 149 ? -13.659 37.428  25.967  1.00 123.21 ? 149 MET B C   1 
ATOM   3723  O O   . MET B 2 149 ? -12.955 36.913  25.099  1.00 122.38 ? 149 MET B O   1 
ATOM   3724  C CB  . MET B 2 149 ? -12.880 38.438  28.110  1.00 113.92 ? 149 MET B CB  1 
ATOM   3725  C CG  . MET B 2 149 ? -12.497 39.663  28.921  1.00 111.16 ? 149 MET B CG  1 
ATOM   3726  S SD  . MET B 2 149 ? -11.007 40.477  28.314  1.00 125.59 ? 149 MET B SD  1 
ATOM   3727  C CE  . MET B 2 149 ? -10.765 41.728  29.574  1.00 175.29 ? 149 MET B CE  1 
ATOM   3728  N N   . ASN B 2 150 ? -14.818 36.913  26.364  1.00 97.88  ? 150 ASN B N   1 
ATOM   3729  C CA  . ASN B 2 150 ? -15.320 35.645  25.854  1.00 95.74  ? 150 ASN B CA  1 
ATOM   3730  C C   . ASN B 2 150 ? -15.702 35.705  24.376  1.00 88.28  ? 150 ASN B C   1 
ATOM   3731  O O   . ASN B 2 150 ? -16.272 34.758  23.835  1.00 82.99  ? 150 ASN B O   1 
ATOM   3732  C CB  . ASN B 2 150 ? -16.501 35.168  26.702  1.00 106.38 ? 150 ASN B CB  1 
ATOM   3733  C CG  . ASN B 2 150 ? -16.196 35.197  28.193  1.00 106.19 ? 150 ASN B CG  1 
ATOM   3734  O OD1 . ASN B 2 150 ? -15.035 35.243  28.599  1.00 99.17  ? 150 ASN B OD1 1 
ATOM   3735  N ND2 . ASN B 2 150 ? -17.241 35.170  29.014  1.00 113.33 ? 150 ASN B ND2 1 
ATOM   3736  N N   . SER B 2 151 ? -15.390 36.825  23.730  1.00 107.42 ? 151 SER B N   1 
ATOM   3737  C CA  . SER B 2 151 ? -15.547 36.945  22.287  1.00 102.67 ? 151 SER B CA  1 
ATOM   3738  C C   . SER B 2 151 ? -14.171 37.066  21.639  1.00 99.44  ? 151 SER B C   1 
ATOM   3739  O O   . SER B 2 151 ? -14.015 36.843  20.441  1.00 100.18 ? 151 SER B O   1 
ATOM   3740  C CB  . SER B 2 151 ? -16.416 38.143  21.921  1.00 98.95  ? 151 SER B CB  1 
ATOM   3741  O OG  . SER B 2 151 ? -15.679 39.345  22.018  1.00 93.91  ? 151 SER B OG  1 
ATOM   3742  N N   . VAL B 2 152 ? -13.175 37.434  22.439  1.00 129.28 ? 152 VAL B N   1 
ATOM   3743  C CA  . VAL B 2 152 ? -11.785 37.348  22.009  1.00 112.24 ? 152 VAL B CA  1 
ATOM   3744  C C   . VAL B 2 152 ? -11.408 35.877  22.035  1.00 107.81 ? 152 VAL B C   1 
ATOM   3745  O O   . VAL B 2 152 ? -10.726 35.377  21.138  1.00 103.82 ? 152 VAL B O   1 
ATOM   3746  C CB  . VAL B 2 152 ? -10.844 38.110  22.962  1.00 100.02 ? 152 VAL B CB  1 
ATOM   3747  C CG1 . VAL B 2 152 ? -9.403  38.000  22.494  1.00 87.53  ? 152 VAL B CG1 1 
ATOM   3748  C CG2 . VAL B 2 152 ? -11.260 39.565  23.073  1.00 99.94  ? 152 VAL B CG2 1 
ATOM   3749  N N   . LYS B 2 153 ? -11.881 35.194  23.077  1.00 88.63  ? 153 LYS B N   1 
ATOM   3750  C CA  . LYS B 2 153 ? -11.619 33.774  23.293  1.00 91.09  ? 153 LYS B CA  1 
ATOM   3751  C C   . LYS B 2 153 ? -12.260 32.887  22.233  1.00 102.10 ? 153 LYS B C   1 
ATOM   3752  O O   . LYS B 2 153 ? -11.560 32.234  21.458  1.00 103.14 ? 153 LYS B O   1 
ATOM   3753  C CB  . LYS B 2 153 ? -12.112 33.350  24.675  1.00 89.75  ? 153 LYS B CB  1 
ATOM   3754  C CG  . LYS B 2 153 ? -11.407 34.041  25.819  1.00 87.15  ? 153 LYS B CG  1 
ATOM   3755  C CD  . LYS B 2 153 ? -11.981 33.591  27.142  1.00 94.59  ? 153 LYS B CD  1 
ATOM   3756  C CE  . LYS B 2 153 ? -11.277 34.264  28.299  1.00 97.45  ? 153 LYS B CE  1 
ATOM   3757  N NZ  . LYS B 2 153 ? -11.894 33.898  29.601  1.00 106.42 ? 153 LYS B NZ  1 
ATOM   3758  N N   . ASN B 2 154 ? -13.589 32.857  22.207  1.00 106.54 ? 154 ASN B N   1 
ATOM   3759  C CA  . ASN B 2 154 ? -14.310 32.018  21.254  1.00 111.78 ? 154 ASN B CA  1 
ATOM   3760  C C   . ASN B 2 154 ? -14.040 32.405  19.799  1.00 112.50 ? 154 ASN B C   1 
ATOM   3761  O O   . ASN B 2 154 ? -14.573 31.787  18.877  1.00 120.75 ? 154 ASN B O   1 
ATOM   3762  C CB  . ASN B 2 154 ? -15.815 32.012  21.547  1.00 124.61 ? 154 ASN B CB  1 
ATOM   3763  C CG  . ASN B 2 154 ? -16.448 33.381  21.396  1.00 133.85 ? 154 ASN B CG  1 
ATOM   3764  O OD1 . ASN B 2 154 ? -15.825 34.314  20.891  1.00 131.60 ? 154 ASN B OD1 1 
ATOM   3765  N ND2 . ASN B 2 154 ? -17.698 33.506  21.831  1.00 143.37 ? 154 ASN B ND2 1 
ATOM   3766  N N   . GLY B 2 155 ? -13.212 33.429  19.604  1.00 131.56 ? 155 GLY B N   1 
ATOM   3767  C CA  . GLY B 2 155 ? -12.750 33.806  18.280  1.00 126.46 ? 155 GLY B CA  1 
ATOM   3768  C C   . GLY B 2 155 ? -13.716 34.679  17.505  1.00 133.53 ? 155 GLY B C   1 
ATOM   3769  O O   . GLY B 2 155 ? -13.725 34.658  16.273  1.00 134.07 ? 155 GLY B O   1 
ATOM   3770  N N   . THR B 2 156 ? -14.530 35.446  18.225  1.00 150.38 ? 156 THR B N   1 
ATOM   3771  C CA  . THR B 2 156 ? -15.486 36.356  17.599  1.00 154.87 ? 156 THR B CA  1 
ATOM   3772  C C   . THR B 2 156 ? -15.430 37.752  18.227  1.00 158.88 ? 156 THR B C   1 
ATOM   3773  O O   . THR B 2 156 ? -16.390 38.204  18.852  1.00 161.22 ? 156 THR B O   1 
ATOM   3774  C CB  . THR B 2 156 ? -16.926 35.807  17.670  1.00 157.34 ? 156 THR B CB  1 
ATOM   3775  O OG1 . THR B 2 156 ? -17.233 35.432  19.019  1.00 156.80 ? 156 THR B OG1 1 
ATOM   3776  C CG2 . THR B 2 156 ? -17.077 34.592  16.769  1.00 152.99 ? 156 THR B CG2 1 
ATOM   3777  N N   . TYR B 2 157 ? -14.293 38.422  18.058  1.00 166.73 ? 157 TYR B N   1 
ATOM   3778  C CA  . TYR B 2 157 ? -14.093 39.767  18.589  1.00 166.44 ? 157 TYR B CA  1 
ATOM   3779  C C   . TYR B 2 157 ? -14.549 40.815  17.578  1.00 173.46 ? 157 TYR B C   1 
ATOM   3780  O O   . TYR B 2 157 ? -14.253 40.708  16.386  1.00 170.66 ? 157 TYR B O   1 
ATOM   3781  C CB  . TYR B 2 157 ? -12.620 39.977  18.958  1.00 156.28 ? 157 TYR B CB  1 
ATOM   3782  C CG  . TYR B 2 157 ? -12.244 41.402  19.318  1.00 153.37 ? 157 TYR B CG  1 
ATOM   3783  C CD1 . TYR B 2 157 ? -12.484 41.908  20.590  1.00 152.14 ? 157 TYR B CD1 1 
ATOM   3784  C CD2 . TYR B 2 157 ? -11.629 42.233  18.388  1.00 150.36 ? 157 TYR B CD2 1 
ATOM   3785  C CE1 . TYR B 2 157 ? -12.134 43.208  20.922  1.00 151.13 ? 157 TYR B CE1 1 
ATOM   3786  C CE2 . TYR B 2 157 ? -11.277 43.533  18.710  1.00 148.46 ? 157 TYR B CE2 1 
ATOM   3787  C CZ  . TYR B 2 157 ? -11.531 44.015  19.977  1.00 148.24 ? 157 TYR B CZ  1 
ATOM   3788  O OH  . TYR B 2 157 ? -11.179 45.308  20.295  1.00 143.85 ? 157 TYR B OH  1 
ATOM   3789  N N   . ASP B 2 158 ? -15.272 41.824  18.061  1.00 143.19 ? 158 ASP B N   1 
ATOM   3790  C CA  . ASP B 2 158 ? -15.815 42.874  17.199  1.00 147.97 ? 158 ASP B CA  1 
ATOM   3791  C C   . ASP B 2 158 ? -14.912 44.107  17.183  1.00 143.32 ? 158 ASP B C   1 
ATOM   3792  O O   . ASP B 2 158 ? -15.026 44.988  18.036  1.00 146.65 ? 158 ASP B O   1 
ATOM   3793  C CB  . ASP B 2 158 ? -17.228 43.258  17.650  1.00 157.88 ? 158 ASP B CB  1 
ATOM   3794  C CG  . ASP B 2 158 ? -18.093 43.751  16.504  1.00 161.58 ? 158 ASP B CG  1 
ATOM   3795  O OD1 . ASP B 2 158 ? -17.534 44.165  15.466  1.00 157.07 ? 158 ASP B OD1 1 
ATOM   3796  O OD2 . ASP B 2 158 ? -19.334 43.724  16.641  1.00 168.95 ? 158 ASP B OD2 1 
ATOM   3797  N N   . TYR B 2 159 ? -14.018 44.162  16.200  1.00 144.91 ? 159 TYR B N   1 
ATOM   3798  C CA  . TYR B 2 159 ? -13.038 45.240  16.098  1.00 135.49 ? 159 TYR B CA  1 
ATOM   3799  C C   . TYR B 2 159 ? -13.675 46.619  15.943  1.00 137.91 ? 159 TYR B C   1 
ATOM   3800  O O   . TYR B 2 159 ? -13.443 47.500  16.773  1.00 140.13 ? 159 TYR B O   1 
ATOM   3801  C CB  . TYR B 2 159 ? -12.057 44.964  14.952  1.00 129.59 ? 159 TYR B CB  1 
ATOM   3802  C CG  . TYR B 2 159 ? -11.080 46.086  14.670  1.00 122.94 ? 159 TYR B CG  1 
ATOM   3803  C CD1 . TYR B 2 159 ? -10.155 46.485  15.623  1.00 115.30 ? 159 TYR B CD1 1 
ATOM   3804  C CD2 . TYR B 2 159 ? -11.070 46.731  13.439  1.00 123.41 ? 159 TYR B CD2 1 
ATOM   3805  C CE1 . TYR B 2 159 ? -9.256  47.503  15.365  1.00 109.99 ? 159 TYR B CE1 1 
ATOM   3806  C CE2 . TYR B 2 159 ? -10.173 47.750  13.172  1.00 119.67 ? 159 TYR B CE2 1 
ATOM   3807  C CZ  . TYR B 2 159 ? -9.268  48.132  14.138  1.00 113.75 ? 159 TYR B CZ  1 
ATOM   3808  O OH  . TYR B 2 159 ? -8.374  49.145  13.875  1.00 109.92 ? 159 TYR B OH  1 
ATOM   3809  N N   . PRO B 2 160 ? -14.483 46.812  14.884  1.00 112.96 ? 160 PRO B N   1 
ATOM   3810  C CA  . PRO B 2 160 ? -15.080 48.130  14.636  1.00 111.87 ? 160 PRO B CA  1 
ATOM   3811  C C   . PRO B 2 160 ? -15.784 48.694  15.871  1.00 115.15 ? 160 PRO B C   1 
ATOM   3812  O O   . PRO B 2 160 ? -15.650 49.884  16.165  1.00 110.23 ? 160 PRO B O   1 
ATOM   3813  C CB  . PRO B 2 160 ? -16.096 47.843  13.527  1.00 115.81 ? 160 PRO B CB  1 
ATOM   3814  C CG  . PRO B 2 160 ? -15.543 46.663  12.814  1.00 115.61 ? 160 PRO B CG  1 
ATOM   3815  C CD  . PRO B 2 160 ? -14.917 45.818  13.884  1.00 112.85 ? 160 PRO B CD  1 
ATOM   3816  N N   . LYS B 2 161 ? -16.514 47.838  16.581  1.00 118.84 ? 161 LYS B N   1 
ATOM   3817  C CA  . LYS B 2 161 ? -17.258 48.237  17.776  1.00 126.92 ? 161 LYS B CA  1 
ATOM   3818  C C   . LYS B 2 161 ? -16.432 49.103  18.730  1.00 125.53 ? 161 LYS B C   1 
ATOM   3819  O O   . LYS B 2 161 ? -16.949 50.048  19.330  1.00 129.65 ? 161 LYS B O   1 
ATOM   3820  C CB  . LYS B 2 161 ? -17.780 46.998  18.514  1.00 129.61 ? 161 LYS B CB  1 
ATOM   3821  C CG  . LYS B 2 161 ? -18.684 47.303  19.703  1.00 140.36 ? 161 LYS B CG  1 
ATOM   3822  C CD  . LYS B 2 161 ? -18.907 46.068  20.570  1.00 145.32 ? 161 LYS B CD  1 
ATOM   3823  C CE  . LYS B 2 161 ? -19.633 44.964  19.814  1.00 153.00 ? 161 LYS B CE  1 
ATOM   3824  N NZ  . LYS B 2 161 ? -21.061 45.297  19.560  1.00 166.84 ? 161 LYS B NZ  1 
ATOM   3825  N N   . TYR B 2 162 ? -15.151 48.778  18.868  1.00 128.91 ? 162 TYR B N   1 
ATOM   3826  C CA  . TYR B 2 162 ? -14.286 49.487  19.802  1.00 125.61 ? 162 TYR B CA  1 
ATOM   3827  C C   . TYR B 2 162 ? -13.267 50.372  19.092  1.00 120.75 ? 162 TYR B C   1 
ATOM   3828  O O   . TYR B 2 162 ? -12.496 51.087  19.737  1.00 117.49 ? 162 TYR B O   1 
ATOM   3829  C CB  . TYR B 2 162 ? -13.571 48.493  20.716  1.00 123.17 ? 162 TYR B CB  1 
ATOM   3830  C CG  . TYR B 2 162 ? -14.508 47.694  21.589  1.00 130.07 ? 162 TYR B CG  1 
ATOM   3831  C CD1 . TYR B 2 162 ? -14.987 48.217  22.783  1.00 136.67 ? 162 TYR B CD1 1 
ATOM   3832  C CD2 . TYR B 2 162 ? -14.914 46.418  21.222  1.00 131.37 ? 162 TYR B CD2 1 
ATOM   3833  C CE1 . TYR B 2 162 ? -15.844 47.492  23.589  1.00 145.56 ? 162 TYR B CE1 1 
ATOM   3834  C CE2 . TYR B 2 162 ? -15.771 45.684  22.023  1.00 140.41 ? 162 TYR B CE2 1 
ATOM   3835  C CZ  . TYR B 2 162 ? -16.234 46.228  23.205  1.00 148.93 ? 162 TYR B CZ  1 
ATOM   3836  O OH  . TYR B 2 162 ? -17.088 45.511  24.011  1.00 157.55 ? 162 TYR B OH  1 
ATOM   3837  N N   . GLU B 2 163 ? -13.273 50.328  17.764  1.00 113.39 ? 163 GLU B N   1 
ATOM   3838  C CA  . GLU B 2 163 ? -12.292 51.057  16.968  1.00 111.35 ? 163 GLU B CA  1 
ATOM   3839  C C   . GLU B 2 163 ? -12.251 52.540  17.312  1.00 118.94 ? 163 GLU B C   1 
ATOM   3840  O O   . GLU B 2 163 ? -11.177 53.144  17.356  1.00 115.31 ? 163 GLU B O   1 
ATOM   3841  C CB  . GLU B 2 163 ? -12.576 50.887  15.475  1.00 109.78 ? 163 GLU B CB  1 
ATOM   3842  C CG  . GLU B 2 163 ? -11.534 51.533  14.578  1.00 102.60 ? 163 GLU B CG  1 
ATOM   3843  C CD  . GLU B 2 163 ? -11.973 51.590  13.127  1.00 103.70 ? 163 GLU B CD  1 
ATOM   3844  O OE1 . GLU B 2 163 ? -13.174 51.365  12.860  1.00 110.11 ? 163 GLU B OE1 1 
ATOM   3845  O OE2 . GLU B 2 163 ? -11.118 51.861  12.253  1.00 98.24  ? 163 GLU B OE2 1 
ATOM   3846  N N   . GLU B 2 164 ? -13.420 53.124  17.558  1.00 149.24 ? 164 GLU B N   1 
ATOM   3847  C CA  . GLU B 2 164 ? -13.522 54.570  17.749  1.00 152.81 ? 164 GLU B CA  1 
ATOM   3848  C C   . GLU B 2 164 ? -13.332 55.019  19.198  1.00 147.84 ? 164 GLU B C   1 
ATOM   3849  O O   . GLU B 2 164 ? -12.852 56.124  19.446  1.00 144.40 ? 164 GLU B O   1 
ATOM   3850  C CB  . GLU B 2 164 ? -14.843 55.103  17.181  1.00 163.76 ? 164 GLU B CB  1 
ATOM   3851  C CG  . GLU B 2 164 ? -15.009 54.883  15.678  1.00 163.23 ? 164 GLU B CG  1 
ATOM   3852  C CD  . GLU B 2 164 ? -13.925 55.564  14.854  1.00 154.78 ? 164 GLU B CD  1 
ATOM   3853  O OE1 . GLU B 2 164 ? -13.190 56.408  15.408  1.00 151.13 ? 164 GLU B OE1 1 
ATOM   3854  O OE2 . GLU B 2 164 ? -13.807 55.252  13.649  1.00 150.29 ? 164 GLU B OE2 1 
ATOM   3855  N N   . GLU B 2 165 ? -13.705 54.172  20.152  1.00 128.92 ? 165 GLU B N   1 
ATOM   3856  C CA  . GLU B 2 165 ? -13.458 54.487  21.555  1.00 124.25 ? 165 GLU B CA  1 
ATOM   3857  C C   . GLU B 2 165 ? -11.971 54.395  21.864  1.00 121.90 ? 165 GLU B C   1 
ATOM   3858  O O   . GLU B 2 165 ? -11.457 55.102  22.735  1.00 120.17 ? 165 GLU B O   1 
ATOM   3859  C CB  . GLU B 2 165 ? -14.220 53.542  22.485  1.00 119.08 ? 165 GLU B CB  1 
ATOM   3860  C CG  . GLU B 2 165 ? -13.811 53.708  23.945  1.00 108.84 ? 165 GLU B CG  1 
ATOM   3861  C CD  . GLU B 2 165 ? -14.432 52.677  24.869  1.00 104.33 ? 165 GLU B CD  1 
ATOM   3862  O OE1 . GLU B 2 165 ? -15.314 51.912  24.419  1.00 101.20 ? 165 GLU B OE1 1 
ATOM   3863  O OE2 . GLU B 2 165 ? -14.032 52.635  26.053  1.00 102.16 ? 165 GLU B OE2 1 
ATOM   3864  N N   . SER B 2 166 ? -11.282 53.521  21.138  1.00 152.64 ? 166 SER B N   1 
ATOM   3865  C CA  . SER B 2 166 ? -9.892  53.205  21.438  1.00 146.83 ? 166 SER B CA  1 
ATOM   3866  C C   . SER B 2 166 ? -8.891  54.179  20.824  1.00 146.44 ? 166 SER B C   1 
ATOM   3867  O O   . SER B 2 166 ? -7.916  54.554  21.476  1.00 146.95 ? 166 SER B O   1 
ATOM   3868  C CB  . SER B 2 166 ? -9.568  51.771  21.021  1.00 141.66 ? 166 SER B CB  1 
ATOM   3869  O OG  . SER B 2 166 ? -10.310 50.851  21.801  1.00 143.82 ? 166 SER B OG  1 
ATOM   3870  N N   . LYS B 2 167 ? -9.122  54.591  19.581  1.00 136.65 ? 167 LYS B N   1 
ATOM   3871  C CA  . LYS B 2 167 ? -8.215  55.539  18.940  1.00 132.07 ? 167 LYS B CA  1 
ATOM   3872  C C   . LYS B 2 167 ? -8.135  56.818  19.767  1.00 133.09 ? 167 LYS B C   1 
ATOM   3873  O O   . LYS B 2 167 ? -7.281  57.672  19.533  1.00 132.00 ? 167 LYS B O   1 
ATOM   3874  C CB  . LYS B 2 167 ? -8.629  55.840  17.494  1.00 134.93 ? 167 LYS B CB  1 
ATOM   3875  C CG  . LYS B 2 167 ? -9.931  56.604  17.339  1.00 145.22 ? 167 LYS B CG  1 
ATOM   3876  C CD  . LYS B 2 167 ? -10.090 57.122  15.912  1.00 147.62 ? 167 LYS B CD  1 
ATOM   3877  C CE  . LYS B 2 167 ? -10.012 55.993  14.893  1.00 148.02 ? 167 LYS B CE  1 
ATOM   3878  N NZ  . LYS B 2 167 ? -10.149 56.489  13.494  1.00 149.46 ? 167 LYS B NZ  1 
ATOM   3879  N N   . LEU B 2 168 ? -9.033  56.936  20.740  1.00 114.51 ? 168 LEU B N   1 
ATOM   3880  C CA  . LEU B 2 168 ? -8.989  58.027  21.699  1.00 117.20 ? 168 LEU B CA  1 
ATOM   3881  C C   . LEU B 2 168 ? -7.796  57.834  22.630  1.00 113.29 ? 168 LEU B C   1 
ATOM   3882  O O   . LEU B 2 168 ? -6.704  58.340  22.368  1.00 110.23 ? 168 LEU B O   1 
ATOM   3883  C CB  . LEU B 2 168 ? -10.290 58.082  22.508  1.00 123.09 ? 168 LEU B CB  1 
ATOM   3884  C CG  . LEU B 2 168 ? -10.989 59.439  22.661  1.00 124.48 ? 168 LEU B CG  1 
ATOM   3885  C CD1 . LEU B 2 168 ? -12.361 59.268  23.302  1.00 131.75 ? 168 LEU B CD1 1 
ATOM   3886  C CD2 . LEU B 2 168 ? -10.135 60.420  23.459  1.00 118.61 ? 168 LEU B CD2 1 
ATOM   3887  N N   . ASN B 2 169 ? -8.010  57.075  23.703  1.00 105.67 ? 169 ASN B N   1 
ATOM   3888  C CA  . ASN B 2 169 ? -7.003  56.890  24.746  1.00 99.88  ? 169 ASN B CA  1 
ATOM   3889  C C   . ASN B 2 169 ? -5.604  56.600  24.205  1.00 94.15  ? 169 ASN B C   1 
ATOM   3890  O O   . ASN B 2 169 ? -4.604  56.882  24.868  1.00 89.55  ? 169 ASN B O   1 
ATOM   3891  C CB  . ASN B 2 169 ? -7.429  55.785  25.718  1.00 101.78 ? 169 ASN B CB  1 
ATOM   3892  C CG  . ASN B 2 169 ? -8.911  55.836  26.054  1.00 110.44 ? 169 ASN B CG  1 
ATOM   3893  O OD1 . ASN B 2 169 ? -9.623  56.756  25.655  1.00 115.94 ? 169 ASN B OD1 1 
ATOM   3894  N ND2 . ASN B 2 169 ? -9.380  54.843  26.799  1.00 110.61 ? 169 ASN B ND2 1 
ATOM   3895  N N   . ARG B 2 170 ? -5.543  56.035  23.002  1.00 159.80 ? 170 ARG B N   1 
ATOM   3896  C CA  . ARG B 2 170 ? -4.274  55.687  22.370  1.00 159.53 ? 170 ARG B CA  1 
ATOM   3897  C C   . ARG B 2 170 ? -3.421  56.920  22.103  1.00 158.66 ? 170 ARG B C   1 
ATOM   3898  O O   . ARG B 2 170 ? -2.299  57.029  22.600  1.00 155.65 ? 170 ARG B O   1 
ATOM   3899  C CB  . ARG B 2 170 ? -4.514  54.918  21.067  1.00 160.43 ? 170 ARG B CB  1 
ATOM   3900  C CG  . ARG B 2 170 ? -3.242  54.577  20.305  1.00 154.05 ? 170 ARG B CG  1 
ATOM   3901  C CD  . ARG B 2 170 ? -3.431  53.383  19.368  1.00 154.47 ? 170 ARG B CD  1 
ATOM   3902  N NE  . ARG B 2 170 ? -4.090  53.729  18.109  1.00 157.01 ? 170 ARG B NE  1 
ATOM   3903  C CZ  . ARG B 2 170 ? -5.333  53.381  17.787  1.00 160.25 ? 170 ARG B CZ  1 
ATOM   3904  N NH1 . ARG B 2 170 ? -6.070  52.672  18.631  1.00 162.67 ? 170 ARG B NH1 1 
ATOM   3905  N NH2 . ARG B 2 170 ? -5.841  53.741  16.616  1.00 161.09 ? 170 ARG B NH2 1 
ATOM   3906  N N   . ASN B 2 171 ? -3.960  57.845  21.316  1.00 123.84 ? 171 ASN B N   1 
ATOM   3907  C CA  . ASN B 2 171 ? -3.249  59.071  20.965  1.00 118.36 ? 171 ASN B CA  1 
ATOM   3908  C C   . ASN B 2 171 ? -2.897  59.938  22.178  1.00 122.57 ? 171 ASN B C   1 
ATOM   3909  O O   . ASN B 2 171 ? -1.759  59.927  22.652  1.00 121.96 ? 171 ASN B O   1 
ATOM   3910  C CB  . ASN B 2 171 ? -4.067  59.884  19.957  1.00 110.84 ? 171 ASN B CB  1 
ATOM   3911  C CG  . ASN B 2 171 ? -4.144  59.220  18.597  1.00 99.97  ? 171 ASN B CG  1 
ATOM   3912  O OD1 . ASN B 2 171 ? -3.122  58.971  17.958  1.00 93.94  ? 171 ASN B OD1 1 
ATOM   3913  N ND2 . ASN B 2 171 ? -5.361  58.931  18.146  1.00 98.18  ? 171 ASN B ND2 1 
ATOM   3914  N N   . GLU B 2 172 ? -3.885  60.682  22.670  1.00 127.12 ? 172 GLU B N   1 
ATOM   3915  C CA  . GLU B 2 172 ? -3.699  61.618  23.780  1.00 125.79 ? 172 GLU B CA  1 
ATOM   3916  C C   . GLU B 2 172 ? -2.438  62.475  23.659  1.00 116.30 ? 172 GLU B C   1 
ATOM   3917  O O   . GLU B 2 172 ? -2.468  63.679  23.929  1.00 113.53 ? 172 GLU B O   1 
ATOM   3918  C CB  . GLU B 2 172 ? -3.729  60.889  25.126  1.00 129.29 ? 172 GLU B CB  1 
ATOM   3919  C CG  . GLU B 2 172 ? -5.093  60.321  25.479  1.00 138.54 ? 172 GLU B CG  1 
ATOM   3920  C CD  . GLU B 2 172 ? -6.212  61.339  25.320  1.00 148.14 ? 172 GLU B CD  1 
ATOM   3921  O OE1 . GLU B 2 172 ? -7.392  60.932  25.306  1.00 155.49 ? 172 GLU B OE1 1 
ATOM   3922  O OE2 . GLU B 2 172 ? -5.916  62.547  25.208  1.00 146.40 ? 172 GLU B OE2 1 
ATOM   3923  N N   . PRO C 1 1   ? 19.656  61.856  10.619  1.00 143.21 ? 9   PRO C N   1 
ATOM   3924  C CA  . PRO C 1 1   ? 20.045  61.064  11.791  1.00 138.13 ? 9   PRO C CA  1 
ATOM   3925  C C   . PRO C 1 1   ? 19.113  59.876  11.997  1.00 129.35 ? 9   PRO C C   1 
ATOM   3926  O O   . PRO C 1 1   ? 18.476  59.426  11.046  1.00 131.88 ? 9   PRO C O   1 
ATOM   3927  C CB  . PRO C 1 1   ? 19.895  62.057  12.949  1.00 141.91 ? 9   PRO C CB  1 
ATOM   3928  C CG  . PRO C 1 1   ? 20.019  63.404  12.315  1.00 144.66 ? 9   PRO C CG  1 
ATOM   3929  C CD  . PRO C 1 1   ? 19.387  63.263  10.966  1.00 145.52 ? 9   PRO C CD  1 
ATOM   3930  N N   . GLY C 1 2   ? 19.039  59.379  13.229  1.00 77.78  ? 10  GLY C N   1 
ATOM   3931  C CA  . GLY C 1 2   ? 18.205  58.232  13.550  1.00 64.13  ? 10  GLY C CA  1 
ATOM   3932  C C   . GLY C 1 2   ? 19.014  57.020  13.996  1.00 64.09  ? 10  GLY C C   1 
ATOM   3933  O O   . GLY C 1 2   ? 19.483  56.236  13.170  1.00 67.65  ? 10  GLY C O   1 
ATOM   3934  N N   . ASP C 1 3   ? 19.184  56.862  15.304  1.00 83.77  ? 11  ASP C N   1 
ATOM   3935  C CA  . ASP C 1 3   ? 19.964  55.752  15.834  1.00 84.47  ? 11  ASP C CA  1 
ATOM   3936  C C   . ASP C 1 3   ? 19.329  54.405  15.502  1.00 85.68  ? 11  ASP C C   1 
ATOM   3937  O O   . ASP C 1 3   ? 18.110  54.260  15.551  1.00 87.55  ? 11  ASP C O   1 
ATOM   3938  C CB  . ASP C 1 3   ? 20.142  55.904  17.341  1.00 81.64  ? 11  ASP C CB  1 
ATOM   3939  C CG  . ASP C 1 3   ? 20.984  57.102  17.699  1.00 84.22  ? 11  ASP C CG  1 
ATOM   3940  O OD1 . ASP C 1 3   ? 21.732  57.566  16.817  1.00 84.59  ? 11  ASP C OD1 1 
ATOM   3941  O OD2 . ASP C 1 3   ? 20.904  57.576  18.851  1.00 89.17  ? 11  ASP C OD2 1 
ATOM   3942  N N   . GLN C 1 4   ? 20.163  53.429  15.155  1.00 85.09  ? 12  GLN C N   1 
ATOM   3943  C CA  . GLN C 1 4   ? 19.691  52.103  14.768  1.00 73.51  ? 12  GLN C CA  1 
ATOM   3944  C C   . GLN C 1 4   ? 20.350  51.024  15.606  1.00 74.29  ? 12  GLN C C   1 
ATOM   3945  O O   . GLN C 1 4   ? 21.429  51.228  16.162  1.00 77.88  ? 12  GLN C O   1 
ATOM   3946  C CB  . GLN C 1 4   ? 20.017  51.818  13.299  1.00 66.50  ? 12  GLN C CB  1 
ATOM   3947  C CG  . GLN C 1 4   ? 19.043  52.376  12.278  1.00 70.99  ? 12  GLN C CG  1 
ATOM   3948  C CD  . GLN C 1 4   ? 19.443  52.029  10.847  1.00 74.68  ? 12  GLN C CD  1 
ATOM   3949  O OE1 . GLN C 1 4   ? 20.169  51.059  10.605  1.00 80.84  ? 12  GLN C OE1 1 
ATOM   3950  N NE2 . GLN C 1 4   ? 18.974  52.826  9.892   1.00 67.77  ? 12  GLN C NE2 1 
ATOM   3951  N N   . ILE C 1 5   ? 19.693  49.872  15.690  1.00 61.55  ? 13  ILE C N   1 
ATOM   3952  C CA  . ILE C 1 5   ? 20.341  48.642  16.149  1.00 63.65  ? 13  ILE C CA  1 
ATOM   3953  C C   . ILE C 1 5   ? 19.849  47.483  15.305  1.00 60.75  ? 13  ILE C C   1 
ATOM   3954  O O   . ILE C 1 5   ? 18.707  47.472  14.851  1.00 62.16  ? 13  ILE C O   1 
ATOM   3955  C CB  . ILE C 1 5   ? 20.074  48.332  17.627  1.00 61.38  ? 13  ILE C CB  1 
ATOM   3956  C CG1 . ILE C 1 5   ? 21.046  47.256  18.113  1.00 55.81  ? 13  ILE C CG1 1 
ATOM   3957  C CG2 . ILE C 1 5   ? 18.634  47.893  17.823  1.00 56.01  ? 13  ILE C CG2 1 
ATOM   3958  C CD1 . ILE C 1 5   ? 20.998  47.017  19.608  1.00 52.59  ? 13  ILE C CD1 1 
ATOM   3959  N N   . CYS C 1 6   ? 20.713  46.505  15.095  1.00 58.69  ? 14  CYS C N   1 
ATOM   3960  C CA  . CYS C 1 6   ? 20.396  45.435  14.169  1.00 59.91  ? 14  CYS C CA  1 
ATOM   3961  C C   . CYS C 1 6   ? 20.749  44.076  14.748  1.00 66.96  ? 14  CYS C C   1 
ATOM   3962  O O   . CYS C 1 6   ? 21.631  43.961  15.604  1.00 75.13  ? 14  CYS C O   1 
ATOM   3963  C CB  . CYS C 1 6   ? 21.127  45.668  12.849  1.00 57.48  ? 14  CYS C CB  1 
ATOM   3964  S SG  . CYS C 1 6   ? 20.733  47.256  12.078  1.00 72.67  ? 14  CYS C SG  1 
ATOM   3965  N N   . ILE C 1 7   ? 20.046  43.050  14.275  1.00 67.07  ? 15  ILE C N   1 
ATOM   3966  C CA  . ILE C 1 7   ? 20.232  41.684  14.758  1.00 64.42  ? 15  ILE C CA  1 
ATOM   3967  C C   . ILE C 1 7   ? 20.615  40.782  13.591  1.00 77.84  ? 15  ILE C C   1 
ATOM   3968  O O   . ILE C 1 7   ? 19.932  40.759  12.569  1.00 82.44  ? 15  ILE C O   1 
ATOM   3969  C CB  . ILE C 1 7   ? 18.943  41.155  15.398  1.00 55.85  ? 15  ILE C CB  1 
ATOM   3970  C CG1 . ILE C 1 7   ? 18.296  42.231  16.275  1.00 46.24  ? 15  ILE C CG1 1 
ATOM   3971  C CG2 . ILE C 1 7   ? 19.227  39.902  16.202  1.00 65.99  ? 15  ILE C CG2 1 
ATOM   3972  C CD1 . ILE C 1 7   ? 19.110  42.588  17.486  1.00 37.76  ? 15  ILE C CD1 1 
ATOM   3973  N N   . GLY C 1 8   ? 21.707  40.040  13.741  1.00 90.22  ? 16  GLY C N   1 
ATOM   3974  C CA  . GLY C 1 8   ? 22.210  39.217  12.653  1.00 91.84  ? 16  GLY C CA  1 
ATOM   3975  C C   . GLY C 1 8   ? 23.113  38.095  13.119  1.00 82.55  ? 16  GLY C C   1 
ATOM   3976  O O   . GLY C 1 8   ? 23.350  37.938  14.316  1.00 79.61  ? 16  GLY C O   1 
ATOM   3977  N N   . TYR C 1 9   ? 23.636  37.321  12.174  1.00 61.72  ? 17  TYR C N   1 
ATOM   3978  C CA  . TYR C 1 9   ? 24.359  36.105  12.527  1.00 57.27  ? 17  TYR C CA  1 
ATOM   3979  C C   . TYR C 1 9   ? 25.817  36.073  12.120  1.00 59.05  ? 17  TYR C C   1 
ATOM   3980  O O   . TYR C 1 9   ? 26.294  36.921  11.374  1.00 61.08  ? 17  TYR C O   1 
ATOM   3981  C CB  . TYR C 1 9   ? 23.652  34.873  11.968  1.00 59.19  ? 17  TYR C CB  1 
ATOM   3982  C CG  . TYR C 1 9   ? 23.056  35.058  10.593  1.00 62.94  ? 17  TYR C CG  1 
ATOM   3983  C CD1 . TYR C 1 9   ? 23.791  34.790  9.446   1.00 62.62  ? 17  TYR C CD1 1 
ATOM   3984  C CD2 . TYR C 1 9   ? 21.743  35.482  10.446  1.00 68.87  ? 17  TYR C CD2 1 
ATOM   3985  C CE1 . TYR C 1 9   ? 23.230  34.953  8.191   1.00 68.04  ? 17  TYR C CE1 1 
ATOM   3986  C CE2 . TYR C 1 9   ? 21.177  35.647  9.203   1.00 70.97  ? 17  TYR C CE2 1 
ATOM   3987  C CZ  . TYR C 1 9   ? 21.919  35.383  8.081   1.00 73.38  ? 17  TYR C CZ  1 
ATOM   3988  O OH  . TYR C 1 9   ? 21.336  35.557  6.849   1.00 81.61  ? 17  TYR C OH  1 
ATOM   3989  N N   . HIS C 1 10  ? 26.513  35.064  12.625  1.00 63.10  ? 18  HIS C N   1 
ATOM   3990  C CA  . HIS C 1 10  ? 27.919  34.866  12.334  1.00 71.42  ? 18  HIS C CA  1 
ATOM   3991  C C   . HIS C 1 10  ? 28.101  34.505  10.871  1.00 73.35  ? 18  HIS C C   1 
ATOM   3992  O O   . HIS C 1 10  ? 27.159  34.092  10.193  1.00 72.50  ? 18  HIS C O   1 
ATOM   3993  C CB  . HIS C 1 10  ? 28.475  33.750  13.214  1.00 82.50  ? 18  HIS C CB  1 
ATOM   3994  C CG  . HIS C 1 10  ? 29.964  33.630  13.166  1.00 98.75  ? 18  HIS C CG  1 
ATOM   3995  N ND1 . HIS C 1 10  ? 30.795  34.726  13.088  1.00 107.29 ? 18  HIS C ND1 1 
ATOM   3996  C CD2 . HIS C 1 10  ? 30.773  32.545  13.196  1.00 105.14 ? 18  HIS C CD2 1 
ATOM   3997  C CE1 . HIS C 1 10  ? 32.053  34.323  13.066  1.00 113.73 ? 18  HIS C CE1 1 
ATOM   3998  N NE2 . HIS C 1 10  ? 32.067  33.004  13.131  1.00 114.36 ? 18  HIS C NE2 1 
ATOM   3999  N N   . ALA C 1 11  ? 29.323  34.676  10.388  1.00 61.85  ? 19  ALA C N   1 
ATOM   4000  C CA  . ALA C 1 11  ? 29.680  34.280  9.032   1.00 61.13  ? 19  ALA C CA  1 
ATOM   4001  C C   . ALA C 1 11  ? 31.194  34.243  8.924   1.00 73.22  ? 19  ALA C C   1 
ATOM   4002  O O   . ALA C 1 11  ? 31.894  34.886  9.705   1.00 79.73  ? 19  ALA C O   1 
ATOM   4003  C CB  . ALA C 1 11  ? 29.092  35.233  8.018   1.00 53.86  ? 19  ALA C CB  1 
ATOM   4004  N N   . ASN C 1 12  ? 31.703  33.483  7.963   1.00 62.48  ? 20  ASN C N   1 
ATOM   4005  C CA  . ASN C 1 12  ? 33.143  33.318  7.851   1.00 66.63  ? 20  ASN C CA  1 
ATOM   4006  C C   . ASN C 1 12  ? 33.618  32.825  6.486   1.00 78.84  ? 20  ASN C C   1 
ATOM   4007  O O   . ASN C 1 12  ? 32.853  32.786  5.517   1.00 74.90  ? 20  ASN C O   1 
ATOM   4008  C CB  . ASN C 1 12  ? 33.674  32.418  8.981   1.00 54.88  ? 20  ASN C CB  1 
ATOM   4009  C CG  . ASN C 1 12  ? 32.888  31.099  9.125   1.00 48.02  ? 20  ASN C CG  1 
ATOM   4010  O OD1 . ASN C 1 12  ? 32.113  30.717  8.242   1.00 51.21  ? 20  ASN C OD1 1 
ATOM   4011  N ND2 . ASN C 1 12  ? 33.097  30.404  10.247  1.00 35.44  ? 20  ASN C ND2 1 
ATOM   4012  N N   . ASN C 1 13  ? 34.899  32.473  6.426   1.00 108.78 ? 21  ASN C N   1 
ATOM   4013  C CA  . ASN C 1 13  ? 35.520  31.975  5.209   1.00 116.93 ? 21  ASN C CA  1 
ATOM   4014  C C   . ASN C 1 13  ? 35.522  30.448  5.208   1.00 115.52 ? 21  ASN C C   1 
ATOM   4015  O O   . ASN C 1 13  ? 36.582  29.823  5.203   1.00 119.58 ? 21  ASN C O   1 
ATOM   4016  C CB  . ASN C 1 13  ? 36.960  32.502  5.092   1.00 129.20 ? 21  ASN C CB  1 
ATOM   4017  C CG  . ASN C 1 13  ? 37.049  34.025  5.206   1.00 135.09 ? 21  ASN C CG  1 
ATOM   4018  O OD1 . ASN C 1 13  ? 37.703  34.556  6.108   1.00 130.18 ? 21  ASN C OD1 1 
ATOM   4019  N ND2 . ASN C 1 13  ? 36.404  34.728  4.283   1.00 145.80 ? 21  ASN C ND2 1 
ATOM   4020  N N   . SER C 1 14  ? 34.332  29.853  5.216   1.00 124.39 ? 22  SER C N   1 
ATOM   4021  C CA  . SER C 1 14  ? 34.207  28.402  5.339   1.00 120.09 ? 22  SER C CA  1 
ATOM   4022  C C   . SER C 1 14  ? 33.670  27.728  4.078   1.00 117.81 ? 22  SER C C   1 
ATOM   4023  O O   . SER C 1 14  ? 32.618  28.104  3.563   1.00 118.60 ? 22  SER C O   1 
ATOM   4024  C CB  . SER C 1 14  ? 33.325  28.038  6.536   1.00 117.32 ? 22  SER C CB  1 
ATOM   4025  O OG  . SER C 1 14  ? 33.241  26.632  6.702   1.00 117.86 ? 22  SER C OG  1 
ATOM   4026  N N   . THR C 1 15  ? 34.399  26.722  3.599   1.00 89.38  ? 23  THR C N   1 
ATOM   4027  C CA  . THR C 1 15  ? 34.011  25.960  2.413   1.00 84.87  ? 23  THR C CA  1 
ATOM   4028  C C   . THR C 1 15  ? 33.165  24.742  2.783   1.00 80.29  ? 23  THR C C   1 
ATOM   4029  O O   . THR C 1 15  ? 32.386  24.242  1.968   1.00 74.84  ? 23  THR C O   1 
ATOM   4030  C CB  . THR C 1 15  ? 35.252  25.476  1.626   1.00 91.49  ? 23  THR C CB  1 
ATOM   4031  O OG1 . THR C 1 15  ? 36.450  25.815  2.342   1.00 93.80  ? 23  THR C OG1 1 
ATOM   4032  C CG2 . THR C 1 15  ? 35.290  26.101  0.239   1.00 95.91  ? 23  THR C CG2 1 
ATOM   4033  N N   . GLU C 1 16  ? 33.336  24.273  4.018   1.00 100.69 ? 24  GLU C N   1 
ATOM   4034  C CA  . GLU C 1 16  ? 32.614  23.118  4.553   1.00 97.86  ? 24  GLU C CA  1 
ATOM   4035  C C   . GLU C 1 16  ? 31.169  23.027  4.073   1.00 93.46  ? 24  GLU C C   1 
ATOM   4036  O O   . GLU C 1 16  ? 30.373  23.943  4.283   1.00 94.14  ? 24  GLU C O   1 
ATOM   4037  C CB  . GLU C 1 16  ? 32.624  23.167  6.081   1.00 96.69  ? 24  GLU C CB  1 
ATOM   4038  C CG  . GLU C 1 16  ? 34.004  23.259  6.701   1.00 105.27 ? 24  GLU C CG  1 
ATOM   4039  C CD  . GLU C 1 16  ? 34.778  21.962  6.589   1.00 118.03 ? 24  GLU C CD  1 
ATOM   4040  O OE1 . GLU C 1 16  ? 34.150  20.914  6.310   1.00 118.01 ? 24  GLU C OE1 1 
ATOM   4041  O OE2 . GLU C 1 16  ? 36.015  21.990  6.776   1.00 128.86 ? 24  GLU C OE2 1 
ATOM   4042  N N   . LYS C 1 17  ? 30.821  21.912  3.443   1.00 77.44  ? 25  LYS C N   1 
ATOM   4043  C CA  . LYS C 1 17  ? 29.453  21.732  2.978   1.00 71.70  ? 25  LYS C CA  1 
ATOM   4044  C C   . LYS C 1 17  ? 28.761  20.490  3.566   1.00 70.06  ? 25  LYS C C   1 
ATOM   4045  O O   . LYS C 1 17  ? 29.412  19.506  3.917   1.00 76.20  ? 25  LYS C O   1 
ATOM   4046  C CB  . LYS C 1 17  ? 29.390  21.751  1.446   1.00 70.58  ? 25  LYS C CB  1 
ATOM   4047  C CG  . LYS C 1 17  ? 29.758  23.103  0.843   1.00 75.37  ? 25  LYS C CG  1 
ATOM   4048  C CD  . LYS C 1 17  ? 29.555  23.124  -0.669  1.00 89.56  ? 25  LYS C CD  1 
ATOM   4049  C CE  . LYS C 1 17  ? 30.722  23.791  -1.388  1.00 99.56  ? 25  LYS C CE  1 
ATOM   4050  N NZ  . LYS C 1 17  ? 30.999  25.158  -0.878  1.00 102.06 ? 25  LYS C NZ  1 
ATOM   4051  N N   . VAL C 1 18  ? 27.438  20.572  3.688   1.00 78.89  ? 26  VAL C N   1 
ATOM   4052  C CA  . VAL C 1 18  ? 26.621  19.495  4.229   1.00 69.71  ? 26  VAL C CA  1 
ATOM   4053  C C   . VAL C 1 18  ? 25.367  19.337  3.379   1.00 63.15  ? 26  VAL C C   1 
ATOM   4054  O O   . VAL C 1 18  ? 24.976  20.257  2.661   1.00 64.50  ? 26  VAL C O   1 
ATOM   4055  C CB  . VAL C 1 18  ? 26.184  19.781  5.688   1.00 66.05  ? 26  VAL C CB  1 
ATOM   4056  C CG1 . VAL C 1 18  ? 27.253  20.573  6.432   1.00 69.45  ? 26  VAL C CG1 1 
ATOM   4057  C CG2 . VAL C 1 18  ? 24.855  20.516  5.715   1.00 60.51  ? 26  VAL C CG2 1 
ATOM   4058  N N   . ASP C 1 19  ? 24.733  18.174  3.459   1.00 74.22  ? 27  ASP C N   1 
ATOM   4059  C CA  . ASP C 1 19  ? 23.470  17.971  2.767   1.00 66.99  ? 27  ASP C CA  1 
ATOM   4060  C C   . ASP C 1 19  ? 22.340  17.895  3.777   1.00 56.73  ? 27  ASP C C   1 
ATOM   4061  O O   . ASP C 1 19  ? 22.567  17.627  4.955   1.00 55.48  ? 27  ASP C O   1 
ATOM   4062  C CB  . ASP C 1 19  ? 23.510  16.698  1.923   1.00 70.63  ? 27  ASP C CB  1 
ATOM   4063  C CG  . ASP C 1 19  ? 24.531  16.773  0.800   1.00 89.27  ? 27  ASP C CG  1 
ATOM   4064  O OD1 . ASP C 1 19  ? 24.639  17.844  0.170   1.00 98.89  ? 27  ASP C OD1 1 
ATOM   4065  O OD2 . ASP C 1 19  ? 25.223  15.761  0.547   1.00 88.98  ? 27  ASP C OD2 1 
ATOM   4066  N N   . THR C 1 20  ? 21.125  18.146  3.313   1.00 70.17  ? 28  THR C N   1 
ATOM   4067  C CA  . THR C 1 20  ? 19.950  18.084  4.164   1.00 67.51  ? 28  THR C CA  1 
ATOM   4068  C C   . THR C 1 20  ? 18.849  17.381  3.391   1.00 72.87  ? 28  THR C C   1 
ATOM   4069  O O   . THR C 1 20  ? 19.023  17.059  2.215   1.00 80.22  ? 28  THR C O   1 
ATOM   4070  C CB  . THR C 1 20  ? 19.447  19.492  4.556   1.00 63.89  ? 28  THR C CB  1 
ATOM   4071  O OG1 . THR C 1 20  ? 18.761  20.081  3.446   1.00 66.96  ? 28  THR C OG1 1 
ATOM   4072  C CG2 . THR C 1 20  ? 20.599  20.390  4.975   1.00 68.18  ? 28  THR C CG2 1 
ATOM   4073  N N   . ILE C 1 21  ? 17.716  17.147  4.043   1.00 60.20  ? 29  ILE C N   1 
ATOM   4074  C CA  . ILE C 1 21  ? 16.592  16.513  3.371   1.00 61.31  ? 29  ILE C CA  1 
ATOM   4075  C C   . ILE C 1 21  ? 16.208  17.314  2.138   1.00 67.57  ? 29  ILE C C   1 
ATOM   4076  O O   . ILE C 1 21  ? 15.969  16.749  1.069   1.00 74.63  ? 29  ILE C O   1 
ATOM   4077  C CB  . ILE C 1 21  ? 15.357  16.409  4.284   1.00 68.14  ? 29  ILE C CB  1 
ATOM   4078  C CG1 . ILE C 1 21  ? 15.652  15.537  5.507   1.00 69.36  ? 29  ILE C CG1 1 
ATOM   4079  C CG2 . ILE C 1 21  ? 14.179  15.832  3.510   1.00 67.57  ? 29  ILE C CG2 1 
ATOM   4080  C CD1 . ILE C 1 21  ? 15.246  14.090  5.330   1.00 67.19  ? 29  ILE C CD1 1 
ATOM   4081  N N   . LEU C 1 22  ? 16.165  18.636  2.293   1.00 55.92  ? 30  LEU C N   1 
ATOM   4082  C CA  . LEU C 1 22  ? 15.633  19.514  1.254   1.00 57.92  ? 30  LEU C CA  1 
ATOM   4083  C C   . LEU C 1 22  ? 16.684  20.086  0.312   1.00 52.87  ? 30  LEU C C   1 
ATOM   4084  O O   . LEU C 1 22  ? 16.376  20.408  -0.831  1.00 62.24  ? 30  LEU C O   1 
ATOM   4085  C CB  . LEU C 1 22  ? 14.827  20.647  1.883   1.00 63.88  ? 30  LEU C CB  1 
ATOM   4086  C CG  . LEU C 1 22  ? 13.511  20.231  2.540   1.00 76.37  ? 30  LEU C CG  1 
ATOM   4087  C CD1 . LEU C 1 22  ? 13.296  20.958  3.862   1.00 81.66  ? 30  LEU C CD1 1 
ATOM   4088  C CD2 . LEU C 1 22  ? 12.335  20.458  1.596   1.00 83.67  ? 30  LEU C CD2 1 
ATOM   4089  N N   . GLU C 1 23  ? 17.921  20.204  0.780   1.00 55.61  ? 31  GLU C N   1 
ATOM   4090  C CA  . GLU C 1 23  ? 18.931  20.923  0.017   1.00 61.63  ? 31  GLU C CA  1 
ATOM   4091  C C   . GLU C 1 23  ? 20.272  20.208  0.039   1.00 64.32  ? 31  GLU C C   1 
ATOM   4092  O O   . GLU C 1 23  ? 20.552  19.432  0.951   1.00 68.55  ? 31  GLU C O   1 
ATOM   4093  C CB  . GLU C 1 23  ? 19.080  22.352  0.557   1.00 74.54  ? 31  GLU C CB  1 
ATOM   4094  C CG  . GLU C 1 23  ? 19.851  23.293  -0.362  1.00 86.91  ? 31  GLU C CG  1 
ATOM   4095  C CD  . GLU C 1 23  ? 19.757  24.749  0.069   1.00 92.36  ? 31  GLU C CD  1 
ATOM   4096  O OE1 . GLU C 1 23  ? 18.877  25.078  0.899   1.00 82.58  ? 31  GLU C OE1 1 
ATOM   4097  O OE2 . GLU C 1 23  ? 20.566  25.564  -0.423  1.00 97.91  ? 31  GLU C OE2 1 
ATOM   4098  N N   . ARG C 1 24  ? 21.104  20.474  -0.965  1.00 74.10  ? 32  ARG C N   1 
ATOM   4099  C CA  . ARG C 1 24  ? 22.403  19.819  -1.068  1.00 83.91  ? 32  ARG C CA  1 
ATOM   4100  C C   . ARG C 1 24  ? 23.554  20.800  -1.296  1.00 103.20 ? 32  ARG C C   1 
ATOM   4101  O O   . ARG C 1 24  ? 23.337  21.968  -1.613  1.00 105.54 ? 32  ARG C O   1 
ATOM   4102  C CB  . ARG C 1 24  ? 22.373  18.758  -2.171  1.00 77.93  ? 32  ARG C CB  1 
ATOM   4103  C CG  . ARG C 1 24  ? 21.471  17.576  -1.854  1.00 79.41  ? 32  ARG C CG  1 
ATOM   4104  C CD  . ARG C 1 24  ? 21.422  16.573  -3.002  1.00 93.55  ? 32  ARG C CD  1 
ATOM   4105  N NE  . ARG C 1 24  ? 20.794  15.315  -2.599  1.00 92.42  ? 32  ARG C NE  1 
ATOM   4106  C CZ  . ARG C 1 24  ? 20.396  14.369  -3.444  1.00 92.55  ? 32  ARG C CZ  1 
ATOM   4107  N NH1 . ARG C 1 24  ? 20.550  14.537  -4.751  1.00 90.03  ? 32  ARG C NH1 1 
ATOM   4108  N NH2 . ARG C 1 24  ? 19.838  13.257  -2.981  1.00 93.74  ? 32  ARG C NH2 1 
ATOM   4109  N N   . ASN C 1 25  ? 24.778  20.311  -1.126  1.00 103.00 ? 33  ASN C N   1 
ATOM   4110  C CA  . ASN C 1 25  ? 25.976  21.120  -1.318  1.00 114.65 ? 33  ASN C CA  1 
ATOM   4111  C C   . ASN C 1 25  ? 25.907  22.426  -0.530  1.00 107.72 ? 33  ASN C C   1 
ATOM   4112  O O   . ASN C 1 25  ? 26.483  23.439  -0.927  1.00 117.86 ? 33  ASN C O   1 
ATOM   4113  C CB  . ASN C 1 25  ? 26.201  21.390  -2.810  1.00 131.58 ? 33  ASN C CB  1 
ATOM   4114  C CG  . ASN C 1 25  ? 27.589  21.935  -3.109  1.00 151.55 ? 33  ASN C CG  1 
ATOM   4115  O OD1 . ASN C 1 25  ? 27.744  23.087  -3.520  1.00 150.00 ? 33  ASN C OD1 1 
ATOM   4116  N ND2 . ASN C 1 25  ? 28.606  21.106  -2.903  1.00 166.57 ? 33  ASN C ND2 1 
ATOM   4117  N N   . VAL C 1 26  ? 25.202  22.388  0.596   1.00 67.09  ? 34  VAL C N   1 
ATOM   4118  C CA  . VAL C 1 26  ? 24.984  23.572  1.417   1.00 63.53  ? 34  VAL C CA  1 
ATOM   4119  C C   . VAL C 1 26  ? 26.192  23.965  2.255   1.00 70.46  ? 34  VAL C C   1 
ATOM   4120  O O   . VAL C 1 26  ? 26.739  23.157  2.991   1.00 68.86  ? 34  VAL C O   1 
ATOM   4121  C CB  . VAL C 1 26  ? 23.798  23.375  2.361   1.00 52.33  ? 34  VAL C CB  1 
ATOM   4122  C CG1 . VAL C 1 26  ? 23.883  24.349  3.524   1.00 49.49  ? 34  VAL C CG1 1 
ATOM   4123  C CG2 . VAL C 1 26  ? 22.492  23.542  1.606   1.00 44.60  ? 34  VAL C CG2 1 
ATOM   4124  N N   . THR C 1 27  ? 26.592  25.224  2.155   1.00 79.75  ? 35  THR C N   1 
ATOM   4125  C CA  . THR C 1 27  ? 27.717  25.709  2.934   1.00 78.97  ? 35  THR C CA  1 
ATOM   4126  C C   . THR C 1 27  ? 27.280  26.083  4.344   1.00 83.02  ? 35  THR C C   1 
ATOM   4127  O O   . THR C 1 27  ? 26.239  26.711  4.537   1.00 92.83  ? 35  THR C O   1 
ATOM   4128  C CB  . THR C 1 27  ? 28.360  26.925  2.268   1.00 75.84  ? 35  THR C CB  1 
ATOM   4129  O OG1 . THR C 1 27  ? 28.336  26.754  0.845   1.00 83.53  ? 35  THR C OG1 1 
ATOM   4130  C CG2 . THR C 1 27  ? 29.796  27.083  2.738   1.00 74.45  ? 35  THR C CG2 1 
ATOM   4131  N N   . VAL C 1 28  ? 28.080  25.691  5.327   1.00 69.52  ? 36  VAL C N   1 
ATOM   4132  C CA  . VAL C 1 28  ? 27.775  25.988  6.720   1.00 53.85  ? 36  VAL C CA  1 
ATOM   4133  C C   . VAL C 1 28  ? 29.027  26.534  7.389   1.00 56.00  ? 36  VAL C C   1 
ATOM   4134  O O   . VAL C 1 28  ? 30.136  26.339  6.895   1.00 63.67  ? 36  VAL C O   1 
ATOM   4135  C CB  . VAL C 1 28  ? 27.250  24.728  7.489   1.00 42.58  ? 36  VAL C CB  1 
ATOM   4136  C CG1 . VAL C 1 28  ? 26.027  24.111  6.780   1.00 41.04  ? 36  VAL C CG1 1 
ATOM   4137  C CG2 . VAL C 1 28  ? 28.353  23.694  7.677   1.00 35.31  ? 36  VAL C CG2 1 
ATOM   4138  N N   . THR C 1 29  ? 28.848  27.220  8.510   1.00 63.70  ? 37  THR C N   1 
ATOM   4139  C CA  . THR C 1 29  ? 29.953  27.907  9.169   1.00 71.89  ? 37  THR C CA  1 
ATOM   4140  C C   . THR C 1 29  ? 31.000  26.948  9.707   1.00 78.33  ? 37  THR C C   1 
ATOM   4141  O O   . THR C 1 29  ? 32.149  27.328  9.925   1.00 85.05  ? 37  THR C O   1 
ATOM   4142  C CB  . THR C 1 29  ? 29.456  28.796  10.323  1.00 72.30  ? 37  THR C CB  1 
ATOM   4143  O OG1 . THR C 1 29  ? 28.508  28.065  11.110  1.00 72.02  ? 37  THR C OG1 1 
ATOM   4144  C CG2 . THR C 1 29  ? 28.789  30.059  9.782   1.00 65.91  ? 37  THR C CG2 1 
ATOM   4145  N N   . HIS C 1 30  ? 30.595  25.703  9.913   1.00 66.92  ? 38  HIS C N   1 
ATOM   4146  C CA  . HIS C 1 30  ? 31.450  24.710  10.542  1.00 72.26  ? 38  HIS C CA  1 
ATOM   4147  C C   . HIS C 1 30  ? 30.638  23.438  10.674  1.00 64.15  ? 38  HIS C C   1 
ATOM   4148  O O   . HIS C 1 30  ? 29.411  23.479  10.647  1.00 53.69  ? 38  HIS C O   1 
ATOM   4149  C CB  . HIS C 1 30  ? 31.897  25.192  11.924  1.00 82.07  ? 38  HIS C CB  1 
ATOM   4150  C CG  . HIS C 1 30  ? 32.889  24.292  12.592  1.00 92.68  ? 38  HIS C CG  1 
ATOM   4151  N ND1 . HIS C 1 30  ? 32.524  23.128  13.233  1.00 94.61  ? 38  HIS C ND1 1 
ATOM   4152  C CD2 . HIS C 1 30  ? 34.232  24.393  12.730  1.00 101.23 ? 38  HIS C CD2 1 
ATOM   4153  C CE1 . HIS C 1 30  ? 33.601  22.545  13.728  1.00 101.78 ? 38  HIS C CE1 1 
ATOM   4154  N NE2 . HIS C 1 30  ? 34.650  23.293  13.438  1.00 104.75 ? 38  HIS C NE2 1 
ATOM   4155  N N   . ALA C 1 31  ? 31.315  22.306  10.813  1.00 68.36  ? 39  ALA C N   1 
ATOM   4156  C CA  . ALA C 1 31  ? 30.619  21.032  10.852  1.00 56.70  ? 39  ALA C CA  1 
ATOM   4157  C C   . ALA C 1 31  ? 31.460  19.956  11.525  1.00 58.02  ? 39  ALA C C   1 
ATOM   4158  O O   . ALA C 1 31  ? 32.668  20.120  11.712  1.00 70.00  ? 39  ALA C O   1 
ATOM   4159  C CB  . ALA C 1 31  ? 30.229  20.607  9.444   1.00 50.38  ? 39  ALA C CB  1 
ATOM   4160  N N   . LYS C 1 32  ? 30.798  18.863  11.897  1.00 53.84  ? 40  LYS C N   1 
ATOM   4161  C CA  . LYS C 1 32  ? 31.458  17.699  12.467  1.00 56.54  ? 40  LYS C CA  1 
ATOM   4162  C C   . LYS C 1 32  ? 31.225  16.522  11.537  1.00 62.54  ? 40  LYS C C   1 
ATOM   4163  O O   . LYS C 1 32  ? 30.125  16.348  11.016  1.00 65.37  ? 40  LYS C O   1 
ATOM   4164  C CB  . LYS C 1 32  ? 30.891  17.384  13.855  1.00 57.45  ? 40  LYS C CB  1 
ATOM   4165  C CG  . LYS C 1 32  ? 31.531  16.184  14.547  1.00 67.63  ? 40  LYS C CG  1 
ATOM   4166  C CD  . LYS C 1 32  ? 32.799  16.581  15.287  1.00 80.78  ? 40  LYS C CD  1 
ATOM   4167  C CE  . LYS C 1 32  ? 33.589  15.367  15.759  1.00 90.06  ? 40  LYS C CE  1 
ATOM   4168  N NZ  . LYS C 1 32  ? 34.273  14.670  14.627  1.00 94.12  ? 40  LYS C NZ  1 
ATOM   4169  N N   . ASP C 1 33  ? 32.267  15.728  11.318  1.00 60.23  ? 41  ASP C N   1 
ATOM   4170  C CA  . ASP C 1 33  ? 32.169  14.535  10.487  1.00 64.43  ? 41  ASP C CA  1 
ATOM   4171  C C   . ASP C 1 33  ? 32.227  13.323  11.411  1.00 66.08  ? 41  ASP C C   1 
ATOM   4172  O O   . ASP C 1 33  ? 33.159  13.189  12.207  1.00 74.63  ? 41  ASP C O   1 
ATOM   4173  C CB  . ASP C 1 33  ? 33.307  14.512  9.454   1.00 73.92  ? 41  ASP C CB  1 
ATOM   4174  C CG  . ASP C 1 33  ? 33.244  13.307  8.521   1.00 76.29  ? 41  ASP C CG  1 
ATOM   4175  O OD1 . ASP C 1 33  ? 33.432  13.474  7.293   1.00 72.78  ? 41  ASP C OD1 1 
ATOM   4176  O OD2 . ASP C 1 33  ? 33.021  12.186  9.016   1.00 77.58  ? 41  ASP C OD2 1 
ATOM   4177  N N   . ILE C 1 34  ? 31.219  12.457  11.319  1.00 62.98  ? 42  ILE C N   1 
ATOM   4178  C CA  . ILE C 1 34  ? 31.129  11.298  12.205  1.00 60.86  ? 42  ILE C CA  1 
ATOM   4179  C C   . ILE C 1 34  ? 31.481  9.962   11.545  1.00 69.58  ? 42  ILE C C   1 
ATOM   4180  O O   . ILE C 1 34  ? 31.144  8.910   12.083  1.00 67.56  ? 42  ILE C O   1 
ATOM   4181  C CB  . ILE C 1 34  ? 29.719  11.155  12.839  1.00 53.20  ? 42  ILE C CB  1 
ATOM   4182  C CG1 . ILE C 1 34  ? 28.629  11.231  11.769  1.00 49.94  ? 42  ILE C CG1 1 
ATOM   4183  C CG2 . ILE C 1 34  ? 29.489  12.205  13.915  1.00 53.62  ? 42  ILE C CG2 1 
ATOM   4184  C CD1 . ILE C 1 34  ? 27.243  11.458  12.349  1.00 45.35  ? 42  ILE C CD1 1 
ATOM   4185  N N   . LEU C 1 35  ? 32.152  9.999   10.395  1.00 63.52  ? 43  LEU C N   1 
ATOM   4186  C CA  . LEU C 1 35  ? 32.511  8.774   9.681   1.00 61.01  ? 43  LEU C CA  1 
ATOM   4187  C C   . LEU C 1 35  ? 34.010  8.497   9.696   1.00 71.70  ? 43  LEU C C   1 
ATOM   4188  O O   . LEU C 1 35  ? 34.773  9.108   8.949   1.00 82.36  ? 43  LEU C O   1 
ATOM   4189  C CB  . LEU C 1 35  ? 32.002  8.805   8.237   1.00 53.36  ? 43  LEU C CB  1 
ATOM   4190  C CG  . LEU C 1 35  ? 32.439  7.625   7.362   1.00 53.57  ? 43  LEU C CG  1 
ATOM   4191  C CD1 . LEU C 1 35  ? 32.213  6.314   8.082   1.00 44.91  ? 43  LEU C CD1 1 
ATOM   4192  C CD2 . LEU C 1 35  ? 31.720  7.617   6.023   1.00 60.94  ? 43  LEU C CD2 1 
ATOM   4193  N N   . GLU C 1 36  ? 34.424  7.558   10.538  1.00 66.33  ? 44  GLU C N   1 
ATOM   4194  C CA  . GLU C 1 36  ? 35.830  7.203   10.640  1.00 71.68  ? 44  GLU C CA  1 
ATOM   4195  C C   . GLU C 1 36  ? 36.268  6.510   9.364   1.00 71.51  ? 44  GLU C C   1 
ATOM   4196  O O   . GLU C 1 36  ? 35.570  5.625   8.873   1.00 72.41  ? 44  GLU C O   1 
ATOM   4197  C CB  . GLU C 1 36  ? 36.062  6.287   11.834  1.00 74.86  ? 44  GLU C CB  1 
ATOM   4198  C CG  . GLU C 1 36  ? 37.506  5.892   11.992  1.00 79.93  ? 44  GLU C CG  1 
ATOM   4199  C CD  . GLU C 1 36  ? 38.395  7.094   12.173  1.00 82.79  ? 44  GLU C CD  1 
ATOM   4200  O OE1 . GLU C 1 36  ? 38.085  7.920   13.052  1.00 75.70  ? 44  GLU C OE1 1 
ATOM   4201  O OE2 . GLU C 1 36  ? 39.392  7.221   11.432  1.00 95.35  ? 44  GLU C OE2 1 
ATOM   4202  N N   . LYS C 1 37  ? 37.411  6.914   8.816   1.00 59.76  ? 45  LYS C N   1 
ATOM   4203  C CA  . LYS C 1 37  ? 37.902  6.303   7.577   1.00 66.75  ? 45  LYS C CA  1 
ATOM   4204  C C   . LYS C 1 37  ? 39.427  6.214   7.475   1.00 72.61  ? 45  LYS C C   1 
ATOM   4205  O O   . LYS C 1 37  ? 39.967  5.828   6.439   1.00 74.02  ? 45  LYS C O   1 
ATOM   4206  C CB  . LYS C 1 37  ? 37.301  6.996   6.344   1.00 72.46  ? 45  LYS C CB  1 
ATOM   4207  C CG  . LYS C 1 37  ? 36.973  8.479   6.520   1.00 74.46  ? 45  LYS C CG  1 
ATOM   4208  C CD  . LYS C 1 37  ? 35.774  8.864   5.651   1.00 74.32  ? 45  LYS C CD  1 
ATOM   4209  C CE  . LYS C 1 37  ? 35.789  10.337  5.248   1.00 76.53  ? 45  LYS C CE  1 
ATOM   4210  N NZ  . LYS C 1 37  ? 35.607  11.283  6.391   1.00 72.45  ? 45  LYS C NZ  1 
ATOM   4211  N N   . THR C 1 38  ? 40.111  6.559   8.561   1.00 70.37  ? 46  THR C N   1 
ATOM   4212  C CA  . THR C 1 38  ? 41.566  6.487   8.605   1.00 86.03  ? 46  THR C CA  1 
ATOM   4213  C C   . THR C 1 38  ? 42.037  5.477   9.646   1.00 85.37  ? 46  THR C C   1 
ATOM   4214  O O   . THR C 1 38  ? 41.718  5.593   10.831  1.00 74.41  ? 46  THR C O   1 
ATOM   4215  C CB  . THR C 1 38  ? 42.203  7.865   8.917   1.00 96.14  ? 46  THR C CB  1 
ATOM   4216  O OG1 . THR C 1 38  ? 41.780  8.313   10.212  1.00 93.15  ? 46  THR C OG1 1 
ATOM   4217  C CG2 . THR C 1 38  ? 41.807  8.895   7.866   1.00 100.73 ? 46  THR C CG2 1 
ATOM   4218  N N   . HIS C 1 39  ? 42.792  4.481   9.192   1.00 79.69  ? 47  HIS C N   1 
ATOM   4219  C CA  . HIS C 1 39  ? 43.398  3.503   10.088  1.00 74.48  ? 47  HIS C CA  1 
ATOM   4220  C C   . HIS C 1 39  ? 44.783  3.993   10.495  1.00 82.32  ? 47  HIS C C   1 
ATOM   4221  O O   . HIS C 1 39  ? 44.975  5.185   10.728  1.00 89.47  ? 47  HIS C O   1 
ATOM   4222  C CB  . HIS C 1 39  ? 43.478  2.135   9.410   1.00 72.39  ? 47  HIS C CB  1 
ATOM   4223  C CG  . HIS C 1 39  ? 44.007  2.180   8.010   1.00 75.61  ? 47  HIS C CG  1 
ATOM   4224  N ND1 . HIS C 1 39  ? 45.350  2.069   7.717   1.00 83.42  ? 47  HIS C ND1 1 
ATOM   4225  C CD2 . HIS C 1 39  ? 43.373  2.324   6.821   1.00 70.98  ? 47  HIS C CD2 1 
ATOM   4226  C CE1 . HIS C 1 39  ? 45.520  2.137   6.409   1.00 85.95  ? 47  HIS C CE1 1 
ATOM   4227  N NE2 . HIS C 1 39  ? 44.336  2.292   5.842   1.00 78.72  ? 47  HIS C NE2 1 
ATOM   4228  N N   . ASN C 1 40  ? 45.745  3.082   10.589  1.00 84.32  ? 48  ASN C N   1 
ATOM   4229  C CA  . ASN C 1 40  ? 47.131  3.485   10.802  1.00 85.70  ? 48  ASN C CA  1 
ATOM   4230  C C   . ASN C 1 40  ? 48.121  2.503   10.193  1.00 92.12  ? 48  ASN C C   1 
ATOM   4231  O O   . ASN C 1 40  ? 49.299  2.489   10.551  1.00 103.73 ? 48  ASN C O   1 
ATOM   4232  C CB  . ASN C 1 40  ? 47.436  3.748   12.286  1.00 78.42  ? 48  ASN C CB  1 
ATOM   4233  C CG  . ASN C 1 40  ? 47.568  2.474   13.103  1.00 72.94  ? 48  ASN C CG  1 
ATOM   4234  O OD1 . ASN C 1 40  ? 47.556  1.363   12.566  1.00 66.39  ? 48  ASN C OD1 1 
ATOM   4235  N ND2 . ASN C 1 40  ? 47.708  2.632   14.417  1.00 68.71  ? 48  ASN C ND2 1 
ATOM   4236  N N   . GLY C 1 41  ? 47.626  1.689   9.265   1.00 88.85  ? 49  GLY C N   1 
ATOM   4237  C CA  . GLY C 1 41  ? 48.452  0.744   8.529   1.00 101.44 ? 49  GLY C CA  1 
ATOM   4238  C C   . GLY C 1 41  ? 49.338  -0.151  9.379   1.00 102.41 ? 49  GLY C C   1 
ATOM   4239  O O   . GLY C 1 41  ? 50.419  -0.548  8.946   1.00 109.15 ? 49  GLY C O   1 
ATOM   4240  N N   . LYS C 1 42  ? 48.886  -0.475  10.585  1.00 90.78  ? 50  LYS C N   1 
ATOM   4241  C CA  . LYS C 1 42  ? 49.691  -1.273  11.499  1.00 85.61  ? 50  LYS C CA  1 
ATOM   4242  C C   . LYS C 1 42  ? 48.866  -2.351  12.186  1.00 74.09  ? 50  LYS C C   1 
ATOM   4243  O O   . LYS C 1 42  ? 47.810  -2.067  12.750  1.00 66.26  ? 50  LYS C O   1 
ATOM   4244  C CB  . LYS C 1 42  ? 50.348  -0.381  12.550  1.00 79.67  ? 50  LYS C CB  1 
ATOM   4245  C CG  . LYS C 1 42  ? 51.253  0.691   11.964  1.00 100.85 ? 50  LYS C CG  1 
ATOM   4246  C CD  . LYS C 1 42  ? 51.766  1.650   13.032  1.00 96.07  ? 50  LYS C CD  1 
ATOM   4247  C CE  . LYS C 1 42  ? 52.476  2.840   12.402  1.00 97.46  ? 50  LYS C CE  1 
ATOM   4248  N NZ  . LYS C 1 42  ? 53.550  2.424   11.453  1.00 91.89  ? 50  LYS C NZ  1 
ATOM   4249  N N   . LEU C 1 43  ? 49.355  -3.588  12.133  1.00 105.61 ? 51  LEU C N   1 
ATOM   4250  C CA  . LEU C 1 43  ? 48.714  -4.707  12.817  1.00 91.67  ? 51  LEU C CA  1 
ATOM   4251  C C   . LEU C 1 43  ? 49.177  -4.742  14.272  1.00 79.35  ? 51  LEU C C   1 
ATOM   4252  O O   . LEU C 1 43  ? 50.343  -5.021  14.549  1.00 81.77  ? 51  LEU C O   1 
ATOM   4253  C CB  . LEU C 1 43  ? 49.060  -6.017  12.111  1.00 93.18  ? 51  LEU C CB  1 
ATOM   4254  C CG  . LEU C 1 43  ? 48.815  -6.028  10.599  1.00 107.34 ? 51  LEU C CG  1 
ATOM   4255  C CD1 . LEU C 1 43  ? 49.489  -7.227  9.951   1.00 115.03 ? 51  LEU C CD1 1 
ATOM   4256  C CD2 . LEU C 1 43  ? 47.326  -6.004  10.282  1.00 99.43  ? 51  LEU C CD2 1 
ATOM   4257  N N   . CYS C 1 44  ? 48.267  -4.464  15.201  1.00 81.44  ? 52  CYS C N   1 
ATOM   4258  C CA  . CYS C 1 44  ? 48.667  -4.190  16.579  1.00 80.45  ? 52  CYS C CA  1 
ATOM   4259  C C   . CYS C 1 44  ? 48.106  -5.163  17.607  1.00 73.62  ? 52  CYS C C   1 
ATOM   4260  O O   . CYS C 1 44  ? 47.154  -5.891  17.336  1.00 74.15  ? 52  CYS C O   1 
ATOM   4261  C CB  . CYS C 1 44  ? 48.273  -2.759  16.970  1.00 88.01  ? 52  CYS C CB  1 
ATOM   4262  S SG  . CYS C 1 44  ? 48.844  -1.479  15.828  1.00 92.86  ? 52  CYS C SG  1 
ATOM   4263  N N   . LYS C 1 45  ? 48.709  -5.155  18.794  1.00 72.92  ? 53  LYS C N   1 
ATOM   4264  C CA  . LYS C 1 45  ? 48.207  -5.911  19.936  1.00 69.68  ? 53  LYS C CA  1 
ATOM   4265  C C   . LYS C 1 45  ? 46.796  -5.453  20.252  1.00 66.39  ? 53  LYS C C   1 
ATOM   4266  O O   . LYS C 1 45  ? 46.431  -4.315  19.966  1.00 66.28  ? 53  LYS C O   1 
ATOM   4267  C CB  . LYS C 1 45  ? 49.107  -5.713  21.159  1.00 84.19  ? 53  LYS C CB  1 
ATOM   4268  C CG  . LYS C 1 45  ? 50.587  -5.993  20.902  1.00 92.13  ? 53  LYS C CG  1 
ATOM   4269  C CD  . LYS C 1 45  ? 51.382  -6.038  22.203  1.00 110.60 ? 53  LYS C CD  1 
ATOM   4270  C CE  . LYS C 1 45  ? 51.476  -4.672  22.868  1.00 122.57 ? 53  LYS C CE  1 
ATOM   4271  N NZ  . LYS C 1 45  ? 52.400  -3.760  22.138  1.00 120.40 ? 53  LYS C NZ  1 
ATOM   4272  N N   . LEU C 1 46  A 46.011  -6.340  20.851  1.00 88.04  ? 53  LEU C N   1 
ATOM   4273  C CA  . LEU C 1 46  A 44.587  -6.096  21.050  1.00 89.04  ? 53  LEU C CA  1 
ATOM   4274  C C   . LEU C 1 46  A 44.254  -6.037  22.533  1.00 109.97 ? 53  LEU C C   1 
ATOM   4275  O O   . LEU C 1 46  A 44.557  -6.966  23.278  1.00 114.05 ? 53  LEU C O   1 
ATOM   4276  C CB  . LEU C 1 46  A 43.778  -7.200  20.361  1.00 78.29  ? 53  LEU C CB  1 
ATOM   4277  C CG  . LEU C 1 46  A 42.279  -7.043  20.093  1.00 70.06  ? 53  LEU C CG  1 
ATOM   4278  C CD1 . LEU C 1 46  A 41.465  -7.152  21.371  1.00 72.91  ? 53  LEU C CD1 1 
ATOM   4279  C CD2 . LEU C 1 46  A 41.996  -5.735  19.367  1.00 70.74  ? 53  LEU C CD2 1 
ATOM   4280  N N   . ASN C 1 47  ? 43.630  -4.941  22.956  1.00 106.40 ? 54  ASN C N   1 
ATOM   4281  C CA  . ASN C 1 47  ? 43.313  -4.730  24.367  1.00 119.20 ? 54  ASN C CA  1 
ATOM   4282  C C   . ASN C 1 47  ? 44.506  -4.994  25.280  1.00 131.79 ? 54  ASN C C   1 
ATOM   4283  O O   . ASN C 1 47  ? 44.337  -5.306  26.459  1.00 136.58 ? 54  ASN C O   1 
ATOM   4284  C CB  . ASN C 1 47  ? 42.115  -5.583  24.797  1.00 115.48 ? 54  ASN C CB  1 
ATOM   4285  C CG  . ASN C 1 47  ? 40.804  -5.092  24.207  1.00 111.83 ? 54  ASN C CG  1 
ATOM   4286  O OD1 . ASN C 1 47  ? 40.607  -3.895  24.012  1.00 105.12 ? 54  ASN C OD1 1 
ATOM   4287  N ND2 . ASN C 1 47  ? 39.898  -6.019  23.924  1.00 114.57 ? 54  ASN C ND2 1 
ATOM   4288  N N   . GLY C 1 48  ? 45.709  -4.870  24.725  1.00 113.83 ? 55  GLY C N   1 
ATOM   4289  C CA  . GLY C 1 48  ? 46.929  -5.047  25.490  1.00 123.80 ? 55  GLY C CA  1 
ATOM   4290  C C   . GLY C 1 48  ? 47.662  -6.346  25.206  1.00 124.38 ? 55  GLY C C   1 
ATOM   4291  O O   . GLY C 1 48  ? 48.873  -6.348  24.981  1.00 129.84 ? 55  GLY C O   1 
ATOM   4292  N N   . ILE C 1 49  ? 46.927  -7.453  25.217  1.00 120.09 ? 56  ILE C N   1 
ATOM   4293  C CA  . ILE C 1 49  ? 47.527  -8.774  25.039  1.00 117.53 ? 56  ILE C CA  1 
ATOM   4294  C C   . ILE C 1 49  ? 47.689  -9.141  23.559  1.00 95.62  ? 56  ILE C C   1 
ATOM   4295  O O   . ILE C 1 49  ? 46.714  -9.206  22.813  1.00 81.66  ? 56  ILE C O   1 
ATOM   4296  C CB  . ILE C 1 49  ? 46.729  -9.862  25.801  1.00 124.23 ? 56  ILE C CB  1 
ATOM   4297  C CG1 . ILE C 1 49  ? 47.463  -11.203 25.752  1.00 136.12 ? 56  ILE C CG1 1 
ATOM   4298  C CG2 . ILE C 1 49  ? 45.304  -9.973  25.270  1.00 106.59 ? 56  ILE C CG2 1 
ATOM   4299  C CD1 . ILE C 1 49  ? 48.695  -11.257 26.636  1.00 156.33 ? 56  ILE C CD1 1 
ATOM   4300  N N   . PRO C 1 50  ? 48.935  -9.389  23.134  1.00 115.97 ? 57  PRO C N   1 
ATOM   4301  C CA  . PRO C 1 50  ? 49.289  -9.589  21.724  1.00 101.43 ? 57  PRO C CA  1 
ATOM   4302  C C   . PRO C 1 50  ? 48.420  -10.621 21.014  1.00 88.60  ? 57  PRO C C   1 
ATOM   4303  O O   . PRO C 1 50  ? 47.618  -11.289 21.658  1.00 88.91  ? 57  PRO C O   1 
ATOM   4304  C CB  . PRO C 1 50  ? 50.742  -10.082 21.795  1.00 103.49 ? 57  PRO C CB  1 
ATOM   4305  C CG  . PRO C 1 50  ? 50.936  -10.539 23.207  1.00 117.92 ? 57  PRO C CG  1 
ATOM   4306  C CD  . PRO C 1 50  ? 50.086  -9.620  24.020  1.00 129.20 ? 57  PRO C CD  1 
ATOM   4307  N N   . PRO C 1 51  ? 48.563  -10.723 19.685  1.00 112.88 ? 58  PRO C N   1 
ATOM   4308  C CA  . PRO C 1 51  ? 47.963  -11.767 18.846  1.00 99.91  ? 58  PRO C CA  1 
ATOM   4309  C C   . PRO C 1 51  ? 48.837  -13.014 18.790  1.00 98.69  ? 58  PRO C C   1 
ATOM   4310  O O   . PRO C 1 51  ? 49.764  -13.167 19.585  1.00 113.83 ? 58  PRO C O   1 
ATOM   4311  C CB  . PRO C 1 51  ? 47.940  -11.130 17.448  1.00 98.89  ? 58  PRO C CB  1 
ATOM   4312  C CG  . PRO C 1 51  ? 48.304  -9.692  17.641  1.00 107.61 ? 58  PRO C CG  1 
ATOM   4313  C CD  . PRO C 1 51  ? 49.133  -9.642  18.873  1.00 115.35 ? 58  PRO C CD  1 
ATOM   4314  N N   . LEU C 1 52  ? 48.536  -13.893 17.841  1.00 71.18  ? 59  LEU C N   1 
ATOM   4315  C CA  . LEU C 1 52  ? 49.369  -15.047 17.562  1.00 66.15  ? 59  LEU C CA  1 
ATOM   4316  C C   . LEU C 1 52  ? 49.715  -14.955 16.088  1.00 73.42  ? 59  LEU C C   1 
ATOM   4317  O O   . LEU C 1 52  ? 48.861  -14.618 15.268  1.00 82.03  ? 59  LEU C O   1 
ATOM   4318  C CB  . LEU C 1 52  ? 48.614  -16.348 17.860  1.00 58.80  ? 59  LEU C CB  1 
ATOM   4319  C CG  . LEU C 1 52  ? 49.389  -17.677 17.973  1.00 60.68  ? 59  LEU C CG  1 
ATOM   4320  C CD1 . LEU C 1 52  ? 48.456  -18.831 18.331  1.00 61.37  ? 59  LEU C CD1 1 
ATOM   4321  C CD2 . LEU C 1 52  ? 50.163  -18.015 16.706  1.00 57.44  ? 59  LEU C CD2 1 
ATOM   4322  N N   . GLU C 1 53  ? 50.967  -15.245 15.753  1.00 62.35  ? 60  GLU C N   1 
ATOM   4323  C CA  . GLU C 1 53  ? 51.439  -15.104 14.382  1.00 69.96  ? 60  GLU C CA  1 
ATOM   4324  C C   . GLU C 1 53  ? 52.077  -16.397 13.879  1.00 77.31  ? 60  GLU C C   1 
ATOM   4325  O O   . GLU C 1 53  ? 53.240  -16.677 14.161  1.00 83.70  ? 60  GLU C O   1 
ATOM   4326  C CB  . GLU C 1 53  ? 52.433  -13.945 14.301  1.00 71.03  ? 60  GLU C CB  1 
ATOM   4327  C CG  . GLU C 1 53  ? 52.775  -13.474 12.895  1.00 85.72  ? 60  GLU C CG  1 
ATOM   4328  C CD  . GLU C 1 53  ? 53.728  -12.286 12.914  1.00 91.74  ? 60  GLU C CD  1 
ATOM   4329  O OE1 . GLU C 1 53  ? 53.814  -11.616 13.968  1.00 79.12  ? 60  GLU C OE1 1 
ATOM   4330  O OE2 . GLU C 1 53  ? 54.394  -12.033 11.888  1.00 106.22 ? 60  GLU C OE2 1 
ATOM   4331  N N   . LEU C 1 54  ? 51.300  -17.189 13.146  1.00 75.72  ? 61  LEU C N   1 
ATOM   4332  C CA  . LEU C 1 54  ? 51.786  -18.437 12.569  1.00 79.65  ? 61  LEU C CA  1 
ATOM   4333  C C   . LEU C 1 54  ? 52.650  -18.136 11.353  1.00 100.10 ? 61  LEU C C   1 
ATOM   4334  O O   . LEU C 1 54  ? 53.269  -19.033 10.777  1.00 110.45 ? 61  LEU C O   1 
ATOM   4335  C CB  . LEU C 1 54  ? 50.617  -19.320 12.139  1.00 77.11  ? 61  LEU C CB  1 
ATOM   4336  C CG  . LEU C 1 54  ? 49.272  -19.061 12.818  1.00 64.90  ? 61  LEU C CG  1 
ATOM   4337  C CD1 . LEU C 1 54  ? 48.134  -19.657 12.002  1.00 68.04  ? 61  LEU C CD1 1 
ATOM   4338  C CD2 . LEU C 1 54  ? 49.256  -19.594 14.235  1.00 56.85  ? 61  LEU C CD2 1 
ATOM   4339  N N   . GLY C 1 55  ? 52.675  -16.868 10.957  1.00 76.61  ? 62  GLY C N   1 
ATOM   4340  C CA  . GLY C 1 55  ? 53.443  -16.448 9.805   1.00 92.98  ? 62  GLY C CA  1 
ATOM   4341  C C   . GLY C 1 55  ? 53.037  -17.172 8.536   1.00 114.08 ? 62  GLY C C   1 
ATOM   4342  O O   . GLY C 1 55  ? 52.047  -16.812 7.897   1.00 129.36 ? 62  GLY C O   1 
ATOM   4343  N N   . ASP C 1 56  ? 53.801  -18.197 8.170   1.00 62.76  ? 63  ASP C N   1 
ATOM   4344  C CA  . ASP C 1 56  ? 53.558  -18.908 6.919   1.00 85.58  ? 63  ASP C CA  1 
ATOM   4345  C C   . ASP C 1 56  ? 53.000  -20.318 7.135   1.00 81.37  ? 63  ASP C C   1 
ATOM   4346  O O   . ASP C 1 56  ? 53.032  -21.151 6.229   1.00 91.19  ? 63  ASP C O   1 
ATOM   4347  C CB  . ASP C 1 56  ? 54.832  -18.964 6.078   1.00 107.65 ? 63  ASP C CB  1 
ATOM   4348  C CG  . ASP C 1 56  ? 54.560  -18.764 4.601   1.00 123.07 ? 63  ASP C CG  1 
ATOM   4349  O OD1 . ASP C 1 56  ? 53.375  -18.807 4.204   1.00 116.83 ? 63  ASP C OD1 1 
ATOM   4350  O OD2 . ASP C 1 56  ? 55.528  -18.564 3.837   1.00 133.04 ? 63  ASP C OD2 1 
ATOM   4351  N N   . CYS C 1 57  ? 52.480  -20.574 8.332   1.00 128.09 ? 64  CYS C N   1 
ATOM   4352  C CA  . CYS C 1 57  ? 51.905  -21.874 8.655   1.00 114.75 ? 64  CYS C CA  1 
ATOM   4353  C C   . CYS C 1 57  ? 50.417  -21.776 8.991   1.00 104.28 ? 64  CYS C C   1 
ATOM   4354  O O   . CYS C 1 57  ? 49.896  -20.686 9.220   1.00 98.07  ? 64  CYS C O   1 
ATOM   4355  C CB  . CYS C 1 57  ? 52.667  -22.517 9.815   1.00 96.85  ? 64  CYS C CB  1 
ATOM   4356  S SG  . CYS C 1 57  ? 54.074  -23.552 9.315   1.00 140.47 ? 64  CYS C SG  1 
ATOM   4357  N N   . SER C 1 58  ? 49.738  -22.920 9.013   1.00 98.07  ? 65  SER C N   1 
ATOM   4358  C CA  . SER C 1 58  ? 48.324  -22.975 9.377   1.00 87.51  ? 65  SER C CA  1 
ATOM   4359  C C   . SER C 1 58  ? 48.141  -23.430 10.827  1.00 66.59  ? 65  SER C C   1 
ATOM   4360  O O   . SER C 1 58  ? 49.105  -23.787 11.501  1.00 64.32  ? 65  SER C O   1 
ATOM   4361  C CB  . SER C 1 58  ? 47.562  -23.905 8.431   1.00 98.54  ? 65  SER C CB  1 
ATOM   4362  O OG  . SER C 1 58  ? 48.095  -25.215 8.466   1.00 94.97  ? 65  SER C OG  1 
ATOM   4363  N N   . ILE C 1 59  ? 46.904  -23.403 11.310  1.00 87.12  ? 66  ILE C N   1 
ATOM   4364  C CA  . ILE C 1 59  ? 46.623  -23.865 12.663  1.00 72.51  ? 66  ILE C CA  1 
ATOM   4365  C C   . ILE C 1 59  ? 46.808  -25.379 12.733  1.00 74.83  ? 66  ILE C C   1 
ATOM   4366  O O   . ILE C 1 59  ? 47.196  -25.924 13.765  1.00 71.43  ? 66  ILE C O   1 
ATOM   4367  C CB  . ILE C 1 59  ? 45.199  -23.501 13.101  1.00 71.21  ? 66  ILE C CB  1 
ATOM   4368  C CG1 . ILE C 1 59  ? 44.857  -22.077 12.662  1.00 73.78  ? 66  ILE C CG1 1 
ATOM   4369  C CG2 . ILE C 1 59  ? 45.054  -23.648 14.609  1.00 56.27  ? 66  ILE C CG2 1 
ATOM   4370  C CD1 . ILE C 1 59  ? 44.973  -21.050 13.770  1.00 64.34  ? 66  ILE C CD1 1 
ATOM   4371  N N   . ALA C 1 60  ? 46.527  -26.055 11.624  1.00 68.50  ? 67  ALA C N   1 
ATOM   4372  C CA  . ALA C 1 60  ? 46.796  -27.479 11.510  1.00 68.04  ? 67  ALA C CA  1 
ATOM   4373  C C   . ALA C 1 60  ? 48.295  -27.715 11.638  1.00 78.64  ? 67  ALA C C   1 
ATOM   4374  O O   . ALA C 1 60  ? 48.755  -28.350 12.587  1.00 72.08  ? 67  ALA C O   1 
ATOM   4375  C CB  . ALA C 1 60  ? 46.291  -28.004 10.179  1.00 84.38  ? 67  ALA C CB  1 
ATOM   4376  N N   . GLY C 1 61  ? 49.050  -27.183 10.681  1.00 94.84  ? 68  GLY C N   1 
ATOM   4377  C CA  . GLY C 1 61  ? 50.495  -27.309 10.675  1.00 93.21  ? 68  GLY C CA  1 
ATOM   4378  C C   . GLY C 1 61  ? 51.142  -26.866 11.975  1.00 77.50  ? 68  GLY C C   1 
ATOM   4379  O O   . GLY C 1 61  ? 52.095  -27.484 12.445  1.00 75.09  ? 68  GLY C O   1 
ATOM   4380  N N   . TRP C 1 62  ? 50.629  -25.792 12.565  1.00 89.04  ? 69  TRP C N   1 
ATOM   4381  C CA  . TRP C 1 62  ? 51.181  -25.304 13.822  1.00 77.68  ? 69  TRP C CA  1 
ATOM   4382  C C   . TRP C 1 62  ? 51.014  -26.336 14.938  1.00 63.63  ? 69  TRP C C   1 
ATOM   4383  O O   . TRP C 1 62  ? 51.992  -26.748 15.563  1.00 60.93  ? 69  TRP C O   1 
ATOM   4384  C CB  . TRP C 1 62  ? 50.562  -23.955 14.228  1.00 73.00  ? 69  TRP C CB  1 
ATOM   4385  C CG  . TRP C 1 62  ? 50.891  -23.584 15.645  1.00 67.72  ? 69  TRP C CG  1 
ATOM   4386  C CD1 . TRP C 1 62  ? 52.133  -23.526 16.204  1.00 66.54  ? 69  TRP C CD1 1 
ATOM   4387  C CD2 . TRP C 1 62  ? 49.967  -23.243 16.689  1.00 68.33  ? 69  TRP C CD2 1 
ATOM   4388  N NE1 . TRP C 1 62  ? 52.042  -23.170 17.530  1.00 65.24  ? 69  TRP C NE1 1 
ATOM   4389  C CE2 . TRP C 1 62  ? 50.722  -22.988 17.852  1.00 64.20  ? 69  TRP C CE2 1 
ATOM   4390  C CE3 . TRP C 1 62  ? 48.576  -23.124 16.753  1.00 68.52  ? 69  TRP C CE3 1 
ATOM   4391  C CZ2 . TRP C 1 62  ? 50.136  -22.622 19.061  1.00 66.83  ? 69  TRP C CZ2 1 
ATOM   4392  C CZ3 . TRP C 1 62  ? 47.996  -22.764 17.954  1.00 64.21  ? 69  TRP C CZ3 1 
ATOM   4393  C CH2 . TRP C 1 62  ? 48.775  -22.518 19.093  1.00 67.23  ? 69  TRP C CH2 1 
ATOM   4394  N N   . LEU C 1 63  ? 49.771  -26.751 15.172  1.00 71.94  ? 70  LEU C N   1 
ATOM   4395  C CA  . LEU C 1 63  ? 49.436  -27.658 16.269  1.00 63.72  ? 70  LEU C CA  1 
ATOM   4396  C C   . LEU C 1 63  ? 50.135  -29.003 16.159  1.00 70.64  ? 70  LEU C C   1 
ATOM   4397  O O   . LEU C 1 63  ? 50.819  -29.439 17.086  1.00 79.60  ? 70  LEU C O   1 
ATOM   4398  C CB  . LEU C 1 63  ? 47.928  -27.877 16.322  1.00 60.45  ? 70  LEU C CB  1 
ATOM   4399  C CG  . LEU C 1 63  ? 47.119  -26.707 16.872  1.00 63.07  ? 70  LEU C CG  1 
ATOM   4400  C CD1 . LEU C 1 63  ? 45.693  -26.731 16.347  1.00 52.41  ? 70  LEU C CD1 1 
ATOM   4401  C CD2 . LEU C 1 63  ? 47.149  -26.709 18.401  1.00 69.38  ? 70  LEU C CD2 1 
ATOM   4402  N N   . LEU C 1 64  ? 49.932  -29.666 15.027  1.00 52.45  ? 71  LEU C N   1 
ATOM   4403  C CA  . LEU C 1 64  ? 50.571  -30.940 14.760  1.00 56.07  ? 71  LEU C CA  1 
ATOM   4404  C C   . LEU C 1 64  ? 52.057  -30.820 15.059  1.00 70.30  ? 71  LEU C C   1 
ATOM   4405  O O   . LEU C 1 64  ? 52.657  -31.698 15.683  1.00 74.99  ? 71  LEU C O   1 
ATOM   4406  C CB  . LEU C 1 64  ? 50.369  -31.312 13.294  1.00 61.34  ? 71  LEU C CB  1 
ATOM   4407  C CG  . LEU C 1 64  ? 48.906  -31.387 12.872  1.00 62.39  ? 71  LEU C CG  1 
ATOM   4408  C CD1 . LEU C 1 64  ? 48.758  -31.320 11.368  1.00 75.45  ? 71  LEU C CD1 1 
ATOM   4409  C CD2 . LEU C 1 64  ? 48.291  -32.649 13.430  1.00 61.03  ? 71  LEU C CD2 1 
ATOM   4410  N N   . GLY C 1 65  ? 52.644  -29.714 14.612  1.00 93.46  ? 72  GLY C N   1 
ATOM   4411  C CA  . GLY C 1 65  ? 54.066  -29.485 14.762  1.00 94.91  ? 72  GLY C CA  1 
ATOM   4412  C C   . GLY C 1 65  ? 54.832  -29.774 13.486  1.00 97.85  ? 72  GLY C C   1 
ATOM   4413  O O   . GLY C 1 65  ? 55.779  -30.556 13.493  1.00 100.55 ? 72  GLY C O   1 
ATOM   4414  N N   . ASN C 1 66  ? 54.416  -29.160 12.381  1.00 55.53  ? 73  ASN C N   1 
ATOM   4415  C CA  . ASN C 1 66  ? 55.192  -29.232 11.150  1.00 73.91  ? 73  ASN C CA  1 
ATOM   4416  C C   . ASN C 1 66  ? 56.576  -28.690 11.453  1.00 82.58  ? 73  ASN C C   1 
ATOM   4417  O O   . ASN C 1 66  ? 56.705  -27.635 12.079  1.00 75.78  ? 73  ASN C O   1 
ATOM   4418  C CB  . ASN C 1 66  ? 54.530  -28.427 10.032  1.00 90.43  ? 73  ASN C CB  1 
ATOM   4419  C CG  . ASN C 1 66  ? 55.277  -28.526 8.710   1.00 124.18 ? 73  ASN C CG  1 
ATOM   4420  O OD1 . ASN C 1 66  ? 56.500  -28.415 8.662   1.00 131.71 ? 73  ASN C OD1 1 
ATOM   4421  N ND2 . ASN C 1 66  ? 54.535  -28.732 7.628   1.00 146.99 ? 73  ASN C ND2 1 
ATOM   4422  N N   . PRO C 1 67  ? 57.619  -29.423 11.033  1.00 96.17  ? 74  PRO C N   1 
ATOM   4423  C CA  . PRO C 1 67  ? 59.009  -29.059 11.334  1.00 96.45  ? 74  PRO C CA  1 
ATOM   4424  C C   . PRO C 1 67  ? 59.275  -27.583 11.049  1.00 98.64  ? 74  PRO C C   1 
ATOM   4425  O O   . PRO C 1 67  ? 60.004  -26.912 11.784  1.00 93.72  ? 74  PRO C O   1 
ATOM   4426  C CB  . PRO C 1 67  ? 59.807  -29.934 10.365  1.00 110.72 ? 74  PRO C CB  1 
ATOM   4427  C CG  . PRO C 1 67  ? 58.953  -31.129 10.159  1.00 104.92 ? 74  PRO C CG  1 
ATOM   4428  C CD  . PRO C 1 67  ? 57.533  -30.637 10.202  1.00 102.32 ? 74  PRO C CD  1 
ATOM   4429  N N   . GLU C 1 68  ? 58.661  -27.092 9.980   1.00 67.32  ? 75  GLU C N   1 
ATOM   4430  C CA  . GLU C 1 68  ? 58.835  -25.724 9.537   1.00 79.80  ? 75  GLU C CA  1 
ATOM   4431  C C   . GLU C 1 68  ? 58.174  -24.728 10.486  1.00 68.81  ? 75  GLU C C   1 
ATOM   4432  O O   . GLU C 1 68  ? 58.052  -23.547 10.163  1.00 72.79  ? 75  GLU C O   1 
ATOM   4433  C CB  . GLU C 1 68  ? 58.248  -25.565 8.135   1.00 102.92 ? 75  GLU C CB  1 
ATOM   4434  C CG  . GLU C 1 68  ? 58.735  -26.602 7.131   1.00 125.98 ? 75  GLU C CG  1 
ATOM   4435  C CD  . GLU C 1 68  ? 60.132  -26.311 6.615   1.00 151.40 ? 75  GLU C CD  1 
ATOM   4436  O OE1 . GLU C 1 68  ? 60.618  -25.178 6.816   1.00 150.58 ? 75  GLU C OE1 1 
ATOM   4437  O OE2 . GLU C 1 68  ? 60.742  -27.213 6.004   1.00 168.55 ? 75  GLU C OE2 1 
ATOM   4438  N N   . CYS C 1 69  ? 57.761  -25.190 11.661  1.00 95.11  ? 76  CYS C N   1 
ATOM   4439  C CA  . CYS C 1 69  ? 57.005  -24.338 12.575  1.00 89.98  ? 76  CYS C CA  1 
ATOM   4440  C C   . CYS C 1 69  ? 57.510  -24.406 14.021  1.00 83.37  ? 76  CYS C C   1 
ATOM   4441  O O   . CYS C 1 69  ? 56.811  -23.998 14.956  1.00 69.60  ? 76  CYS C O   1 
ATOM   4442  C CB  . CYS C 1 69  ? 55.512  -24.684 12.499  1.00 87.33  ? 76  CYS C CB  1 
ATOM   4443  S SG  . CYS C 1 69  ? 54.844  -24.700 10.805  1.00 105.62 ? 76  CYS C SG  1 
ATOM   4444  N N   . ASP C 1 70  ? 58.728  -24.914 14.192  1.00 127.06 ? 77  ASP C N   1 
ATOM   4445  C CA  . ASP C 1 70  ? 59.329  -25.064 15.515  1.00 125.62 ? 77  ASP C CA  1 
ATOM   4446  C C   . ASP C 1 70  ? 59.896  -23.740 16.014  1.00 128.61 ? 77  ASP C C   1 
ATOM   4447  O O   . ASP C 1 70  ? 60.167  -23.575 17.205  1.00 126.97 ? 77  ASP C O   1 
ATOM   4448  C CB  . ASP C 1 70  ? 60.450  -26.106 15.474  1.00 135.06 ? 77  ASP C CB  1 
ATOM   4449  C CG  . ASP C 1 70  ? 60.062  -27.355 14.706  1.00 141.83 ? 77  ASP C CG  1 
ATOM   4450  O OD1 . ASP C 1 70  ? 58.855  -27.677 14.652  1.00 141.90 ? 77  ASP C OD1 1 
ATOM   4451  O OD2 . ASP C 1 70  ? 60.968  -28.016 14.154  1.00 144.74 ? 77  ASP C OD2 1 
ATOM   4452  N N   . ARG C 1 71  ? 60.069  -22.802 15.088  1.00 141.34 ? 78  ARG C N   1 
ATOM   4453  C CA  . ARG C 1 71  ? 60.758  -21.547 15.362  1.00 145.76 ? 78  ARG C CA  1 
ATOM   4454  C C   . ARG C 1 71  ? 59.791  -20.424 15.743  1.00 138.78 ? 78  ARG C C   1 
ATOM   4455  O O   . ARG C 1 71  ? 60.200  -19.279 15.931  1.00 144.63 ? 78  ARG C O   1 
ATOM   4456  C CB  . ARG C 1 71  ? 61.589  -21.143 14.139  1.00 166.11 ? 78  ARG C CB  1 
ATOM   4457  C CG  . ARG C 1 71  ? 62.512  -19.946 14.340  1.00 181.97 ? 78  ARG C CG  1 
ATOM   4458  C CD  . ARG C 1 71  ? 63.941  -20.361 14.666  1.00 191.44 ? 78  ARG C CD  1 
ATOM   4459  N NE  . ARG C 1 71  ? 64.091  -20.812 16.046  1.00 188.31 ? 78  ARG C NE  1 
ATOM   4460  C CZ  . ARG C 1 71  ? 65.263  -21.005 16.642  1.00 191.96 ? 78  ARG C CZ  1 
ATOM   4461  N NH1 . ARG C 1 71  ? 66.390  -20.784 15.981  1.00 196.07 ? 78  ARG C NH1 1 
ATOM   4462  N NH2 . ARG C 1 71  ? 65.308  -21.415 17.901  1.00 192.83 ? 78  ARG C NH2 1 
ATOM   4463  N N   . LEU C 1 72  ? 58.509  -20.753 15.863  1.00 104.79 ? 79  LEU C N   1 
ATOM   4464  C CA  . LEU C 1 72  ? 57.496  -19.752 16.199  1.00 96.53  ? 79  LEU C CA  1 
ATOM   4465  C C   . LEU C 1 72  ? 57.623  -19.283 17.643  1.00 94.72  ? 79  LEU C C   1 
ATOM   4466  O O   . LEU C 1 72  ? 58.343  -19.880 18.439  1.00 93.64  ? 79  LEU C O   1 
ATOM   4467  C CB  . LEU C 1 72  ? 56.097  -20.298 15.930  1.00 87.07  ? 79  LEU C CB  1 
ATOM   4468  C CG  . LEU C 1 72  ? 55.935  -20.837 14.508  1.00 88.04  ? 79  LEU C CG  1 
ATOM   4469  C CD1 . LEU C 1 72  ? 54.545  -21.414 14.294  1.00 76.03  ? 79  LEU C CD1 1 
ATOM   4470  C CD2 . LEU C 1 72  ? 56.238  -19.753 13.483  1.00 97.18  ? 79  LEU C CD2 1 
ATOM   4471  N N   . LEU C 1 73  ? 56.927  -18.206 17.979  1.00 123.08 ? 80  LEU C N   1 
ATOM   4472  C CA  . LEU C 1 73  ? 57.050  -17.620 19.305  1.00 135.90 ? 80  LEU C CA  1 
ATOM   4473  C C   . LEU C 1 73  ? 55.923  -18.099 20.213  1.00 144.84 ? 80  LEU C C   1 
ATOM   4474  O O   . LEU C 1 73  ? 54.769  -17.717 20.035  1.00 143.32 ? 80  LEU C O   1 
ATOM   4475  C CB  . LEU C 1 73  ? 57.053  -16.093 19.205  1.00 135.53 ? 80  LEU C CB  1 
ATOM   4476  C CG  . LEU C 1 73  ? 57.805  -15.332 20.298  1.00 141.60 ? 80  LEU C CG  1 
ATOM   4477  C CD1 . LEU C 1 73  ? 59.178  -15.948 20.529  1.00 149.07 ? 80  LEU C CD1 1 
ATOM   4478  C CD2 . LEU C 1 73  ? 57.924  -13.860 19.932  1.00 133.99 ? 80  LEU C CD2 1 
ATOM   4479  N N   . SER C 1 74  ? 56.262  -18.944 21.182  1.00 135.79 ? 81  SER C N   1 
ATOM   4480  C CA  . SER C 1 74  ? 55.267  -19.500 22.096  1.00 135.85 ? 81  SER C CA  1 
ATOM   4481  C C   . SER C 1 74  ? 54.594  -18.415 22.935  1.00 146.62 ? 81  SER C C   1 
ATOM   4482  O O   . SER C 1 74  ? 55.231  -17.787 23.780  1.00 170.28 ? 81  SER C O   1 
ATOM   4483  C CB  . SER C 1 74  ? 55.906  -20.551 23.007  1.00 133.85 ? 81  SER C CB  1 
ATOM   4484  O OG  . SER C 1 74  ? 56.465  -21.609 22.248  1.00 117.23 ? 81  SER C OG  1 
ATOM   4485  N N   . VAL C 1 75  A 53.304  -18.204 22.700  1.00 91.32  ? 81  VAL C N   1 
ATOM   4486  C CA  . VAL C 1 75  A 52.558  -17.170 23.405  1.00 95.26  ? 81  VAL C CA  1 
ATOM   4487  C C   . VAL C 1 75  A 51.495  -17.772 24.317  1.00 100.21 ? 81  VAL C C   1 
ATOM   4488  O O   . VAL C 1 75  A 50.435  -18.183 23.853  1.00 91.04  ? 81  VAL C O   1 
ATOM   4489  C CB  . VAL C 1 75  A 51.857  -16.222 22.417  1.00 88.09  ? 81  VAL C CB  1 
ATOM   4490  C CG1 . VAL C 1 75  A 51.736  -14.825 23.016  1.00 101.24 ? 81  VAL C CG1 1 
ATOM   4491  C CG2 . VAL C 1 75  A 52.615  -16.171 21.104  1.00 79.96  ? 81  VAL C CG2 1 
ATOM   4492  N N   . PRO C 1 76  ? 51.772  -17.820 25.626  1.00 99.24  ? 82  PRO C N   1 
ATOM   4493  C CA  . PRO C 1 76  ? 50.830  -18.370 26.607  1.00 105.71 ? 82  PRO C CA  1 
ATOM   4494  C C   . PRO C 1 76  ? 49.446  -17.718 26.552  1.00 96.34  ? 82  PRO C C   1 
ATOM   4495  O O   . PRO C 1 76  ? 48.460  -18.358 26.914  1.00 92.65  ? 82  PRO C O   1 
ATOM   4496  C CB  . PRO C 1 76  ? 51.509  -18.063 27.944  1.00 121.49 ? 82  PRO C CB  1 
ATOM   4497  C CG  . PRO C 1 76  ? 52.963  -18.054 27.618  1.00 130.10 ? 82  PRO C CG  1 
ATOM   4498  C CD  . PRO C 1 76  ? 53.056  -17.448 26.243  1.00 114.13 ? 82  PRO C CD  1 
ATOM   4499  N N   . GLU C 1 77  ? 49.375  -16.469 26.104  1.00 102.02 ? 83  GLU C N   1 
ATOM   4500  C CA  . GLU C 1 77  ? 48.102  -15.756 26.030  1.00 94.39  ? 83  GLU C CA  1 
ATOM   4501  C C   . GLU C 1 77  ? 47.977  -14.995 24.713  1.00 75.08  ? 83  GLU C C   1 
ATOM   4502  O O   . GLU C 1 77  ? 48.964  -14.482 24.192  1.00 68.61  ? 83  GLU C O   1 
ATOM   4503  C CB  . GLU C 1 77  ? 47.972  -14.786 27.208  1.00 101.84 ? 83  GLU C CB  1 
ATOM   4504  C CG  . GLU C 1 77  ? 46.613  -14.119 27.331  1.00 101.05 ? 83  GLU C CG  1 
ATOM   4505  C CD  . GLU C 1 77  ? 46.491  -13.284 28.592  1.00 116.12 ? 83  GLU C CD  1 
ATOM   4506  O OE1 . GLU C 1 77  ? 47.538  -12.965 29.194  1.00 125.80 ? 83  GLU C OE1 1 
ATOM   4507  O OE2 . GLU C 1 77  ? 45.350  -12.953 28.986  1.00 112.33 ? 83  GLU C OE2 1 
ATOM   4508  N N   . TRP C 1 78  ? 46.768  -14.938 24.163  1.00 119.16 ? 84  TRP C N   1 
ATOM   4509  C CA  . TRP C 1 78  ? 46.512  -14.072 23.015  1.00 106.68 ? 84  TRP C CA  1 
ATOM   4510  C C   . TRP C 1 78  ? 45.035  -13.725 22.845  1.00 99.97  ? 84  TRP C C   1 
ATOM   4511  O O   . TRP C 1 78  ? 44.185  -14.172 23.616  1.00 99.57  ? 84  TRP C O   1 
ATOM   4512  C CB  . TRP C 1 78  ? 47.125  -14.627 21.719  1.00 99.40  ? 84  TRP C CB  1 
ATOM   4513  C CG  . TRP C 1 78  ? 46.445  -15.827 21.125  1.00 101.22 ? 84  TRP C CG  1 
ATOM   4514  C CD1 . TRP C 1 78  ? 45.360  -15.831 20.297  1.00 94.02  ? 84  TRP C CD1 1 
ATOM   4515  C CD2 . TRP C 1 78  ? 46.833  -17.199 21.280  1.00 106.89 ? 84  TRP C CD2 1 
ATOM   4516  N NE1 . TRP C 1 78  ? 45.037  -17.122 19.940  1.00 88.67  ? 84  TRP C NE1 1 
ATOM   4517  C CE2 . TRP C 1 78  ? 45.928  -17.979 20.531  1.00 93.95  ? 84  TRP C CE2 1 
ATOM   4518  C CE3 . TRP C 1 78  ? 47.852  -17.844 21.987  1.00 118.38 ? 84  TRP C CE3 1 
ATOM   4519  C CZ2 . TRP C 1 78  ? 46.013  -19.365 20.470  1.00 91.51  ? 84  TRP C CZ2 1 
ATOM   4520  C CZ3 . TRP C 1 78  ? 47.932  -19.222 21.925  1.00 113.43 ? 84  TRP C CZ3 1 
ATOM   4521  C CH2 . TRP C 1 78  ? 47.020  -19.967 21.174  1.00 97.28  ? 84  TRP C CH2 1 
ATOM   4522  N N   . SER C 1 79  ? 44.746  -12.908 21.838  1.00 96.41  ? 85  SER C N   1 
ATOM   4523  C CA  . SER C 1 79  ? 43.410  -12.354 21.658  1.00 93.06  ? 85  SER C CA  1 
ATOM   4524  C C   . SER C 1 79  ? 42.978  -12.407 20.200  1.00 81.44  ? 85  SER C C   1 
ATOM   4525  O O   . SER C 1 79  ? 41.880  -11.968 19.861  1.00 75.90  ? 85  SER C O   1 
ATOM   4526  C CB  . SER C 1 79  ? 43.366  -10.910 22.148  1.00 99.69  ? 85  SER C CB  1 
ATOM   4527  O OG  . SER C 1 79  ? 44.236  -10.106 21.374  1.00 102.94 ? 85  SER C OG  1 
ATOM   4528  N N   . TYR C 1 80  ? 43.855  -12.917 19.339  1.00 58.48  ? 86  TYR C N   1 
ATOM   4529  C CA  . TYR C 1 80  ? 43.459  -13.283 17.984  1.00 47.46  ? 86  TYR C CA  1 
ATOM   4530  C C   . TYR C 1 80  ? 44.589  -13.909 17.183  1.00 50.78  ? 86  TYR C C   1 
ATOM   4531  O O   . TYR C 1 80  ? 45.715  -14.009 17.658  1.00 60.91  ? 86  TYR C O   1 
ATOM   4532  C CB  . TYR C 1 80  ? 42.816  -12.119 17.231  1.00 51.88  ? 86  TYR C CB  1 
ATOM   4533  C CG  . TYR C 1 80  ? 43.756  -11.045 16.734  1.00 61.23  ? 86  TYR C CG  1 
ATOM   4534  C CD1 . TYR C 1 80  ? 44.212  -11.048 15.419  1.00 63.20  ? 86  TYR C CD1 1 
ATOM   4535  C CD2 . TYR C 1 80  ? 44.155  -10.006 17.567  1.00 65.68  ? 86  TYR C CD2 1 
ATOM   4536  C CE1 . TYR C 1 80  ? 45.053  -10.058 14.955  1.00 65.28  ? 86  TYR C CE1 1 
ATOM   4537  C CE2 . TYR C 1 80  ? 44.994  -9.009  17.111  1.00 66.48  ? 86  TYR C CE2 1 
ATOM   4538  C CZ  . TYR C 1 80  ? 45.440  -9.039  15.806  1.00 69.54  ? 86  TYR C CZ  1 
ATOM   4539  O OH  . TYR C 1 80  ? 46.277  -8.043  15.360  1.00 79.62  ? 86  TYR C OH  1 
ATOM   4540  N N   . ILE C 1 81  ? 44.280  -14.342 15.970  1.00 60.64  ? 87  ILE C N   1 
ATOM   4541  C CA  . ILE C 1 81  ? 45.204  -15.164 15.219  1.00 60.91  ? 87  ILE C CA  1 
ATOM   4542  C C   . ILE C 1 81  ? 45.497  -14.559 13.859  1.00 73.24  ? 87  ILE C C   1 
ATOM   4543  O O   . ILE C 1 81  ? 44.588  -14.142 13.140  1.00 85.49  ? 87  ILE C O   1 
ATOM   4544  C CB  . ILE C 1 81  ? 44.662  -16.602 15.069  1.00 58.00  ? 87  ILE C CB  1 
ATOM   4545  C CG1 . ILE C 1 81  ? 44.352  -17.192 16.448  1.00 48.94  ? 87  ILE C CG1 1 
ATOM   4546  C CG2 . ILE C 1 81  ? 45.650  -17.479 14.312  1.00 72.50  ? 87  ILE C CG2 1 
ATOM   4547  C CD1 . ILE C 1 81  ? 44.290  -18.700 16.464  1.00 47.48  ? 87  ILE C CD1 1 
ATOM   4548  N N   . MET C 1 82  ? 46.780  -14.503 13.523  1.00 52.46  ? 88  MET C N   1 
ATOM   4549  C CA  . MET C 1 82  ? 47.218  -13.945 12.256  1.00 67.35  ? 88  MET C CA  1 
ATOM   4550  C C   . MET C 1 82  ? 47.708  -15.067 11.370  1.00 81.18  ? 88  MET C C   1 
ATOM   4551  O O   . MET C 1 82  ? 48.615  -15.804 11.743  1.00 86.67  ? 88  MET C O   1 
ATOM   4552  C CB  . MET C 1 82  ? 48.327  -12.917 12.483  1.00 71.86  ? 88  MET C CB  1 
ATOM   4553  C CG  . MET C 1 82  ? 47.873  -11.683 13.266  1.00 73.18  ? 88  MET C CG  1 
ATOM   4554  S SD  . MET C 1 82  ? 49.229  -10.558 13.664  1.00 85.03  ? 88  MET C SD  1 
ATOM   4555  C CE  . MET C 1 82  ? 49.970  -10.326 12.044  1.00 73.76  ? 88  MET C CE  1 
ATOM   4556  N N   . GLU C 1 83  ? 47.100  -15.188 10.196  1.00 41.72  ? 89  GLU C N   1 
ATOM   4557  C CA  . GLU C 1 83  ? 47.365  -16.302 9.299   1.00 61.76  ? 89  GLU C CA  1 
ATOM   4558  C C   . GLU C 1 83  ? 47.222  -15.851 7.862   1.00 80.69  ? 89  GLU C C   1 
ATOM   4559  O O   . GLU C 1 83  ? 46.232  -15.227 7.502   1.00 84.71  ? 89  GLU C O   1 
ATOM   4560  C CB  . GLU C 1 83  ? 46.390  -17.444 9.592   1.00 58.52  ? 89  GLU C CB  1 
ATOM   4561  C CG  . GLU C 1 83  ? 46.305  -18.514 8.519   1.00 69.02  ? 89  GLU C CG  1 
ATOM   4562  C CD  . GLU C 1 83  ? 45.590  -19.758 9.012   1.00 77.72  ? 89  GLU C CD  1 
ATOM   4563  O OE1 . GLU C 1 83  ? 45.693  -20.053 10.221  1.00 79.22  ? 89  GLU C OE1 1 
ATOM   4564  O OE2 . GLU C 1 83  ? 44.922  -20.440 8.201   1.00 81.82  ? 89  GLU C OE2 1 
ATOM   4565  N N   . LYS C 1 84  ? 48.217  -16.159 7.042   1.00 60.94  ? 90  LYS C N   1 
ATOM   4566  C CA  . LYS C 1 84  ? 48.174  -15.780 5.637   1.00 74.56  ? 90  LYS C CA  1 
ATOM   4567  C C   . LYS C 1 84  ? 46.957  -16.386 4.949   1.00 76.73  ? 90  LYS C C   1 
ATOM   4568  O O   . LYS C 1 84  ? 46.282  -17.245 5.506   1.00 67.43  ? 90  LYS C O   1 
ATOM   4569  C CB  . LYS C 1 84  ? 49.467  -16.185 4.926   1.00 84.61  ? 90  LYS C CB  1 
ATOM   4570  C CG  . LYS C 1 84  ? 50.702  -15.452 5.444   1.00 93.22  ? 90  LYS C CG  1 
ATOM   4571  C CD  . LYS C 1 84  ? 51.874  -15.576 4.481   1.00 106.56 ? 90  LYS C CD  1 
ATOM   4572  C CE  . LYS C 1 84  ? 53.029  -14.675 4.893   1.00 113.18 ? 90  LYS C CE  1 
ATOM   4573  N NZ  . LYS C 1 84  ? 54.115  -14.671 3.871   1.00 122.22 ? 90  LYS C NZ  1 
ATOM   4574  N N   . GLU C 1 85  ? 46.666  -15.920 3.742   1.00 116.22 ? 91  GLU C N   1 
ATOM   4575  C CA  . GLU C 1 85  ? 45.508  -16.415 3.018   1.00 118.50 ? 91  GLU C CA  1 
ATOM   4576  C C   . GLU C 1 85  ? 45.654  -17.905 2.731   1.00 123.57 ? 91  GLU C C   1 
ATOM   4577  O O   . GLU C 1 85  ? 44.763  -18.690 3.045   1.00 122.58 ? 91  GLU C O   1 
ATOM   4578  C CB  . GLU C 1 85  ? 45.303  -15.630 1.723   1.00 127.33 ? 91  GLU C CB  1 
ATOM   4579  C CG  . GLU C 1 85  ? 44.050  -16.020 0.964   1.00 125.28 ? 91  GLU C CG  1 
ATOM   4580  C CD  . GLU C 1 85  ? 42.797  -15.875 1.799   1.00 114.78 ? 91  GLU C CD  1 
ATOM   4581  O OE1 . GLU C 1 85  ? 42.764  -14.986 2.680   1.00 112.55 ? 91  GLU C OE1 1 
ATOM   4582  O OE2 . GLU C 1 85  ? 41.847  -16.654 1.576   1.00 107.41 ? 91  GLU C OE2 1 
ATOM   4583  N N   . ASN C 1 86  ? 46.781  -18.292 2.141   1.00 109.42 ? 92  ASN C N   1 
ATOM   4584  C CA  . ASN C 1 86  ? 47.049  -19.694 1.835   1.00 110.95 ? 92  ASN C CA  1 
ATOM   4585  C C   . ASN C 1 86  ? 48.430  -20.138 2.302   1.00 107.64 ? 92  ASN C C   1 
ATOM   4586  O O   . ASN C 1 86  ? 49.348  -20.258 1.491   1.00 114.38 ? 92  ASN C O   1 
ATOM   4587  C CB  . ASN C 1 86  ? 46.925  -19.953 0.333   1.00 122.20 ? 92  ASN C CB  1 
ATOM   4588  C CG  . ASN C 1 86  ? 45.530  -19.689 -0.195  1.00 123.14 ? 92  ASN C CG  1 
ATOM   4589  O OD1 . ASN C 1 86  ? 44.908  -18.676 0.131   1.00 120.52 ? 92  ASN C OD1 1 
ATOM   4590  N ND2 . ASN C 1 86  ? 45.026  -20.607 -1.016  1.00 123.15 ? 92  ASN C ND2 1 
ATOM   4591  N N   . PRO C 1 87  ? 48.580  -20.387 3.611   1.00 82.72  ? 93  PRO C N   1 
ATOM   4592  C CA  . PRO C 1 87  ? 49.866  -20.793 4.184   1.00 87.56  ? 93  PRO C CA  1 
ATOM   4593  C C   . PRO C 1 87  ? 50.549  -21.877 3.363   1.00 105.80 ? 93  PRO C C   1 
ATOM   4594  O O   . PRO C 1 87  ? 49.884  -22.712 2.751   1.00 108.14 ? 93  PRO C O   1 
ATOM   4595  C CB  . PRO C 1 87  ? 49.474  -21.333 5.559   1.00 67.54  ? 93  PRO C CB  1 
ATOM   4596  C CG  . PRO C 1 87  ? 48.301  -20.509 5.935   1.00 59.81  ? 93  PRO C CG  1 
ATOM   4597  C CD  . PRO C 1 87  ? 47.537  -20.272 4.644   1.00 66.17  ? 93  PRO C CD  1 
ATOM   4598  N N   . ARG C 1 88  ? 51.876  -21.846 3.357   1.00 127.08 ? 94  ARG C N   1 
ATOM   4599  C CA  . ARG C 1 88  ? 52.680  -22.783 2.586   1.00 129.37 ? 94  ARG C CA  1 
ATOM   4600  C C   . ARG C 1 88  ? 52.861  -24.091 3.341   1.00 114.81 ? 94  ARG C C   1 
ATOM   4601  O O   . ARG C 1 88  ? 52.742  -25.175 2.767   1.00 111.55 ? 94  ARG C O   1 
ATOM   4602  C CB  . ARG C 1 88  ? 54.048  -22.160 2.306   1.00 143.56 ? 94  ARG C CB  1 
ATOM   4603  C CG  . ARG C 1 88  ? 55.110  -23.134 1.832   1.00 157.76 ? 94  ARG C CG  1 
ATOM   4604  C CD  . ARG C 1 88  ? 56.496  -22.592 2.143   1.00 170.65 ? 94  ARG C CD  1 
ATOM   4605  N NE  . ARG C 1 88  ? 56.675  -21.237 1.630   1.00 172.98 ? 94  ARG C NE  1 
ATOM   4606  C CZ  . ARG C 1 88  ? 57.570  -20.374 2.096   1.00 175.38 ? 94  ARG C CZ  1 
ATOM   4607  N NH1 . ARG C 1 88  ? 58.370  -20.721 3.096   1.00 177.02 ? 94  ARG C NH1 1 
ATOM   4608  N NH2 . ARG C 1 88  ? 57.662  -19.160 1.567   1.00 176.71 ? 94  ARG C NH2 1 
ATOM   4609  N N   . ASP C 1 89  ? 53.149  -23.974 4.633   1.00 122.05 ? 95  ASP C N   1 
ATOM   4610  C CA  . ASP C 1 89  ? 53.472  -25.125 5.464   1.00 123.40 ? 95  ASP C CA  1 
ATOM   4611  C C   . ASP C 1 89  ? 52.329  -25.484 6.406   1.00 113.62 ? 95  ASP C C   1 
ATOM   4612  O O   . ASP C 1 89  ? 52.132  -24.828 7.428   1.00 100.56 ? 95  ASP C O   1 
ATOM   4613  C CB  . ASP C 1 89  ? 54.737  -24.843 6.275   1.00 122.48 ? 95  ASP C CB  1 
ATOM   4614  C CG  . ASP C 1 89  ? 55.930  -24.517 5.399   1.00 132.22 ? 95  ASP C CG  1 
ATOM   4615  O OD1 . ASP C 1 89  ? 56.161  -25.247 4.408   1.00 136.07 ? 95  ASP C OD1 1 
ATOM   4616  O OD2 . ASP C 1 89  ? 56.631  -23.527 5.701   1.00 132.96 ? 95  ASP C OD2 1 
ATOM   4617  N N   . GLY C 1 90  A 51.585  -26.532 6.062   1.00 141.67 ? 95  GLY C N   1 
ATOM   4618  C CA  . GLY C 1 90  A 50.483  -26.992 6.890   1.00 131.52 ? 95  GLY C CA  1 
ATOM   4619  C C   . GLY C 1 90  A 50.571  -28.477 7.186   1.00 127.10 ? 95  GLY C C   1 
ATOM   4620  O O   . GLY C 1 90  A 51.329  -28.902 8.060   1.00 110.06 ? 95  GLY C O   1 
ATOM   4621  N N   . LEU C 1 91  ? 49.785  -29.268 6.462   1.00 111.43 ? 96  LEU C N   1 
ATOM   4622  C CA  . LEU C 1 91  ? 49.854  -30.721 6.560   1.00 101.99 ? 96  LEU C CA  1 
ATOM   4623  C C   . LEU C 1 91  ? 50.910  -31.233 5.590   1.00 118.57 ? 96  LEU C C   1 
ATOM   4624  O O   . LEU C 1 91  ? 50.602  -31.543 4.437   1.00 126.17 ? 96  LEU C O   1 
ATOM   4625  C CB  . LEU C 1 91  ? 48.498  -31.349 6.221   1.00 95.11  ? 96  LEU C CB  1 
ATOM   4626  C CG  . LEU C 1 91  ? 47.300  -31.066 7.136   1.00 77.04  ? 96  LEU C CG  1 
ATOM   4627  C CD1 . LEU C 1 91  ? 45.989  -31.361 6.418   1.00 73.36  ? 96  LEU C CD1 1 
ATOM   4628  C CD2 . LEU C 1 91  ? 47.393  -31.857 8.427   1.00 51.51  ? 96  LEU C CD2 1 
ATOM   4629  N N   . CYS C 1 92  ? 52.156  -31.309 6.052   1.00 91.26  ? 97  CYS C N   1 
ATOM   4630  C CA  . CYS C 1 92  ? 53.257  -31.728 5.188   1.00 95.91  ? 97  CYS C CA  1 
ATOM   4631  C C   . CYS C 1 92  ? 53.026  -33.124 4.613   1.00 106.12 ? 97  CYS C C   1 
ATOM   4632  O O   . CYS C 1 92  ? 53.268  -33.360 3.430   1.00 121.18 ? 97  CYS C O   1 
ATOM   4633  C CB  . CYS C 1 92  ? 54.605  -31.625 5.908   1.00 89.36  ? 97  CYS C CB  1 
ATOM   4634  S SG  . CYS C 1 92  ? 54.761  -32.583 7.420   1.00 95.18  ? 97  CYS C SG  1 
ATOM   4635  N N   . TYR C 1 93  ? 52.558  -34.048 5.450   1.00 89.19  ? 98  TYR C N   1 
ATOM   4636  C CA  . TYR C 1 93  ? 52.000  -35.293 4.944   1.00 87.45  ? 98  TYR C CA  1 
ATOM   4637  C C   . TYR C 1 93  ? 50.546  -34.997 4.623   1.00 74.87  ? 98  TYR C C   1 
ATOM   4638  O O   . TYR C 1 93  ? 49.786  -34.608 5.510   1.00 59.41  ? 98  TYR C O   1 
ATOM   4639  C CB  . TYR C 1 93  ? 52.091  -36.414 5.980   1.00 81.57  ? 98  TYR C CB  1 
ATOM   4640  C CG  . TYR C 1 93  ? 51.862  -37.792 5.393   1.00 89.25  ? 98  TYR C CG  1 
ATOM   4641  C CD1 . TYR C 1 93  ? 52.914  -38.684 5.236   1.00 99.56  ? 98  TYR C CD1 1 
ATOM   4642  C CD2 . TYR C 1 93  ? 50.598  -38.195 4.983   1.00 87.78  ? 98  TYR C CD2 1 
ATOM   4643  C CE1 . TYR C 1 93  ? 52.716  -39.944 4.695   1.00 102.86 ? 98  TYR C CE1 1 
ATOM   4644  C CE2 . TYR C 1 93  ? 50.389  -39.456 4.441   1.00 91.00  ? 98  TYR C CE2 1 
ATOM   4645  C CZ  . TYR C 1 93  ? 51.452  -40.325 4.300   1.00 98.17  ? 98  TYR C CZ  1 
ATOM   4646  O OH  . TYR C 1 93  ? 51.256  -41.576 3.758   1.00 99.85  ? 98  TYR C OH  1 
ATOM   4647  N N   . PRO C 1 94  ? 50.155  -35.174 3.354   1.00 83.63  ? 99  PRO C N   1 
ATOM   4648  C CA  . PRO C 1 94  ? 48.843  -34.764 2.840   1.00 80.38  ? 99  PRO C CA  1 
ATOM   4649  C C   . PRO C 1 94  ? 47.675  -35.456 3.541   1.00 80.33  ? 99  PRO C C   1 
ATOM   4650  O O   . PRO C 1 94  ? 47.813  -36.597 3.992   1.00 85.24  ? 99  PRO C O   1 
ATOM   4651  C CB  . PRO C 1 94  ? 48.898  -35.195 1.372   1.00 82.50  ? 99  PRO C CB  1 
ATOM   4652  C CG  . PRO C 1 94  ? 49.870  -36.314 1.349   1.00 89.63  ? 99  PRO C CG  1 
ATOM   4653  C CD  . PRO C 1 94  ? 50.918  -35.940 2.357   1.00 94.01  ? 99  PRO C CD  1 
ATOM   4654  N N   . GLY C 1 95  ? 46.534  -34.774 3.622   1.00 95.57  ? 100 GLY C N   1 
ATOM   4655  C CA  . GLY C 1 95  ? 45.349  -35.365 4.216   1.00 85.51  ? 100 GLY C CA  1 
ATOM   4656  C C   . GLY C 1 95  ? 44.200  -34.406 4.459   1.00 76.74  ? 100 GLY C C   1 
ATOM   4657  O O   . GLY C 1 95  ? 43.883  -33.564 3.623   1.00 75.44  ? 100 GLY C O   1 
ATOM   4658  N N   . SER C 1 96  ? 43.558  -34.555 5.610   1.00 87.93  ? 101 SER C N   1 
ATOM   4659  C CA  . SER C 1 96  ? 42.432  -33.709 5.969   1.00 77.88  ? 101 SER C CA  1 
ATOM   4660  C C   . SER C 1 96  ? 42.426  -33.458 7.468   1.00 64.98  ? 101 SER C C   1 
ATOM   4661  O O   . SER C 1 96  ? 43.296  -33.935 8.202   1.00 54.30  ? 101 SER C O   1 
ATOM   4662  C CB  . SER C 1 96  ? 41.110  -34.349 5.541   1.00 69.76  ? 101 SER C CB  1 
ATOM   4663  O OG  . SER C 1 96  ? 40.929  -35.611 6.167   1.00 68.41  ? 101 SER C OG  1 
ATOM   4664  N N   . PHE C 1 97  ? 41.440  -32.702 7.921   1.00 102.96 ? 102 PHE C N   1 
ATOM   4665  C CA  . PHE C 1 97  ? 41.312  -32.409 9.331   1.00 83.88  ? 102 PHE C CA  1 
ATOM   4666  C C   . PHE C 1 97  ? 39.833  -32.272 9.612   1.00 77.26  ? 102 PHE C C   1 
ATOM   4667  O O   . PHE C 1 97  ? 39.121  -31.565 8.901   1.00 88.57  ? 102 PHE C O   1 
ATOM   4668  C CB  . PHE C 1 97  ? 42.045  -31.114 9.654   1.00 85.77  ? 102 PHE C CB  1 
ATOM   4669  C CG  . PHE C 1 97  ? 42.572  -31.042 11.053  1.00 65.43  ? 102 PHE C CG  1 
ATOM   4670  C CD1 . PHE C 1 97  ? 43.878  -30.642 11.291  1.00 57.10  ? 102 PHE C CD1 1 
ATOM   4671  C CD2 . PHE C 1 97  ? 41.763  -31.339 12.130  1.00 57.96  ? 102 PHE C CD2 1 
ATOM   4672  C CE1 . PHE C 1 97  ? 44.377  -30.563 12.583  1.00 43.79  ? 102 PHE C CE1 1 
ATOM   4673  C CE2 . PHE C 1 97  ? 42.252  -31.257 13.428  1.00 47.52  ? 102 PHE C CE2 1 
ATOM   4674  C CZ  . PHE C 1 97  ? 43.563  -30.867 13.656  1.00 40.50  ? 102 PHE C CZ  1 
ATOM   4675  N N   . ASN C 1 98  ? 39.363  -32.966 10.639  1.00 64.99  ? 103 ASN C N   1 
ATOM   4676  C CA  . ASN C 1 98  ? 37.942  -32.967 10.948  1.00 49.63  ? 103 ASN C CA  1 
ATOM   4677  C C   . ASN C 1 98  ? 37.514  -31.847 11.892  1.00 44.06  ? 103 ASN C C   1 
ATOM   4678  O O   . ASN C 1 98  ? 38.183  -31.570 12.886  1.00 43.24  ? 103 ASN C O   1 
ATOM   4679  C CB  . ASN C 1 98  ? 37.528  -34.320 11.507  1.00 35.48  ? 103 ASN C CB  1 
ATOM   4680  C CG  . ASN C 1 98  ? 37.498  -35.377 10.452  1.00 54.85  ? 103 ASN C CG  1 
ATOM   4681  O OD1 . ASN C 1 98  ? 37.101  -35.118 9.320   1.00 85.06  ? 103 ASN C OD1 1 
ATOM   4682  N ND2 . ASN C 1 98  ? 37.935  -36.578 10.802  1.00 48.31  ? 103 ASN C ND2 1 
ATOM   4683  N N   . ASP C 1 99  ? 36.391  -31.212 11.583  1.00 65.43  ? 104 ASP C N   1 
ATOM   4684  C CA  . ASP C 1 99  ? 35.924  -30.133 12.428  1.00 66.02  ? 104 ASP C CA  1 
ATOM   4685  C C   . ASP C 1 99  ? 37.081  -29.161 12.627  1.00 70.84  ? 104 ASP C C   1 
ATOM   4686  O O   . ASP C 1 99  ? 37.300  -28.643 13.720  1.00 71.31  ? 104 ASP C O   1 
ATOM   4687  C CB  . ASP C 1 99  ? 35.420  -30.689 13.765  1.00 60.80  ? 104 ASP C CB  1 
ATOM   4688  C CG  . ASP C 1 99  ? 34.114  -31.474 13.617  1.00 66.65  ? 104 ASP C CG  1 
ATOM   4689  O OD1 . ASP C 1 99  ? 33.229  -30.999 12.870  1.00 61.88  ? 104 ASP C OD1 1 
ATOM   4690  O OD2 . ASP C 1 99  ? 33.973  -32.559 14.233  1.00 72.80  ? 104 ASP C OD2 1 
ATOM   4691  N N   . TYR C 1 100 ? 37.829  -28.947 11.550  1.00 51.69  ? 105 TYR C N   1 
ATOM   4692  C CA  . TYR C 1 100 ? 38.982  -28.054 11.556  1.00 54.95  ? 105 TYR C CA  1 
ATOM   4693  C C   . TYR C 1 100 ? 38.527  -26.636 11.838  1.00 56.47  ? 105 TYR C C   1 
ATOM   4694  O O   . TYR C 1 100 ? 39.036  -25.977 12.742  1.00 57.19  ? 105 TYR C O   1 
ATOM   4695  C CB  . TYR C 1 100 ? 39.694  -28.100 10.201  1.00 72.53  ? 105 TYR C CB  1 
ATOM   4696  C CG  . TYR C 1 100 ? 40.967  -27.288 10.138  1.00 72.92  ? 105 TYR C CG  1 
ATOM   4697  C CD1 . TYR C 1 100 ? 41.649  -26.938 11.294  1.00 62.18  ? 105 TYR C CD1 1 
ATOM   4698  C CD2 . TYR C 1 100 ? 41.480  -26.866 8.922   1.00 89.74  ? 105 TYR C CD2 1 
ATOM   4699  C CE1 . TYR C 1 100 ? 42.812  -26.198 11.240  1.00 58.89  ? 105 TYR C CE1 1 
ATOM   4700  C CE2 . TYR C 1 100 ? 42.640  -26.121 8.858   1.00 98.87  ? 105 TYR C CE2 1 
ATOM   4701  C CZ  . TYR C 1 100 ? 43.302  -25.790 10.021  1.00 86.63  ? 105 TYR C CZ  1 
ATOM   4702  O OH  . TYR C 1 100 ? 44.458  -25.046 9.959   1.00 107.33 ? 105 TYR C OH  1 
ATOM   4703  N N   . GLU C 1 101 ? 37.567  -26.167 11.047  1.00 57.75  ? 106 GLU C N   1 
ATOM   4704  C CA  . GLU C 1 101 ? 37.021  -24.836 11.238  1.00 50.63  ? 106 GLU C CA  1 
ATOM   4705  C C   . GLU C 1 101 ? 36.583  -24.673 12.688  1.00 38.32  ? 106 GLU C C   1 
ATOM   4706  O O   . GLU C 1 101 ? 36.986  -23.729 13.355  1.00 48.59  ? 106 GLU C O   1 
ATOM   4707  C CB  . GLU C 1 101 ? 35.861  -24.588 10.276  1.00 57.92  ? 106 GLU C CB  1 
ATOM   4708  C CG  . GLU C 1 101 ? 36.254  -24.667 8.804   1.00 76.00  ? 106 GLU C CG  1 
ATOM   4709  C CD  . GLU C 1 101 ? 36.228  -26.081 8.257   1.00 88.99  ? 106 GLU C CD  1 
ATOM   4710  O OE1 . GLU C 1 101 ? 35.429  -26.897 8.758   1.00 84.69  ? 106 GLU C OE1 1 
ATOM   4711  O OE2 . GLU C 1 101 ? 37.002  -26.380 7.325   1.00 104.91 ? 106 GLU C OE2 1 
ATOM   4712  N N   . GLU C 1 102 ? 35.782  -25.607 13.186  1.00 58.59  ? 107 GLU C N   1 
ATOM   4713  C CA  . GLU C 1 102 ? 35.327  -25.546 14.571  1.00 50.01  ? 107 GLU C CA  1 
ATOM   4714  C C   . GLU C 1 102 ? 36.490  -25.413 15.537  1.00 57.62  ? 107 GLU C C   1 
ATOM   4715  O O   . GLU C 1 102 ? 36.372  -24.772 16.578  1.00 57.52  ? 107 GLU C O   1 
ATOM   4716  C CB  . GLU C 1 102 ? 34.502  -26.780 14.927  1.00 42.89  ? 107 GLU C CB  1 
ATOM   4717  C CG  . GLU C 1 102 ? 33.022  -26.620 14.660  1.00 49.02  ? 107 GLU C CG  1 
ATOM   4718  C CD  . GLU C 1 102 ? 32.377  -25.640 15.620  1.00 49.38  ? 107 GLU C CD  1 
ATOM   4719  O OE1 . GLU C 1 102 ? 32.693  -25.709 16.831  1.00 39.87  ? 107 GLU C OE1 1 
ATOM   4720  O OE2 . GLU C 1 102 ? 31.568  -24.796 15.163  1.00 59.75  ? 107 GLU C OE2 1 
ATOM   4721  N N   . LEU C 1 103 ? 37.614  -26.028 15.190  1.00 70.32  ? 108 LEU C N   1 
ATOM   4722  C CA  . LEU C 1 103 ? 38.798  -25.989 16.040  1.00 61.85  ? 108 LEU C CA  1 
ATOM   4723  C C   . LEU C 1 103 ? 39.455  -24.615 15.981  1.00 68.12  ? 108 LEU C C   1 
ATOM   4724  O O   . LEU C 1 103 ? 39.739  -24.007 17.014  1.00 74.99  ? 108 LEU C O   1 
ATOM   4725  C CB  . LEU C 1 103 ? 39.792  -27.076 15.626  1.00 52.85  ? 108 LEU C CB  1 
ATOM   4726  C CG  . LEU C 1 103 ? 41.146  -27.104 16.334  1.00 52.92  ? 108 LEU C CG  1 
ATOM   4727  C CD1 . LEU C 1 103 ? 40.964  -27.133 17.837  1.00 54.68  ? 108 LEU C CD1 1 
ATOM   4728  C CD2 . LEU C 1 103 ? 41.967  -28.301 15.868  1.00 55.32  ? 108 LEU C CD2 1 
ATOM   4729  N N   . LYS C 1 104 ? 39.694  -24.130 14.766  1.00 50.70  ? 109 LYS C N   1 
ATOM   4730  C CA  . LYS C 1 104 ? 40.268  -22.807 14.589  1.00 43.63  ? 109 LYS C CA  1 
ATOM   4731  C C   . LYS C 1 104 ? 39.521  -21.835 15.498  1.00 45.56  ? 109 LYS C C   1 
ATOM   4732  O O   . LYS C 1 104 ? 40.129  -21.127 16.297  1.00 52.09  ? 109 LYS C O   1 
ATOM   4733  C CB  . LYS C 1 104 ? 40.187  -22.364 13.126  1.00 47.72  ? 109 LYS C CB  1 
ATOM   4734  C CG  . LYS C 1 104 ? 41.008  -23.218 12.168  1.00 61.85  ? 109 LYS C CG  1 
ATOM   4735  C CD  . LYS C 1 104 ? 41.595  -22.402 11.013  1.00 87.71  ? 109 LYS C CD  1 
ATOM   4736  C CE  . LYS C 1 104 ? 40.766  -22.513 9.744   1.00 105.20 ? 109 LYS C CE  1 
ATOM   4737  N NZ  . LYS C 1 104 ? 41.299  -21.636 8.661   1.00 125.69 ? 109 LYS C NZ  1 
ATOM   4738  N N   . HIS C 1 105 ? 38.198  -21.825 15.397  1.00 59.62  ? 110 HIS C N   1 
ATOM   4739  C CA  . HIS C 1 105 ? 37.385  -20.950 16.231  1.00 57.63  ? 110 HIS C CA  1 
ATOM   4740  C C   . HIS C 1 105 ? 37.703  -21.080 17.719  1.00 58.55  ? 110 HIS C C   1 
ATOM   4741  O O   . HIS C 1 105 ? 37.865  -20.080 18.413  1.00 64.52  ? 110 HIS C O   1 
ATOM   4742  C CB  . HIS C 1 105 ? 35.902  -21.228 16.016  1.00 55.22  ? 110 HIS C CB  1 
ATOM   4743  C CG  . HIS C 1 105 ? 35.012  -20.495 16.971  1.00 52.15  ? 110 HIS C CG  1 
ATOM   4744  N ND1 . HIS C 1 105 ? 34.396  -19.306 16.650  1.00 51.95  ? 110 HIS C ND1 1 
ATOM   4745  C CD2 . HIS C 1 105 ? 34.646  -20.780 18.244  1.00 52.73  ? 110 HIS C CD2 1 
ATOM   4746  C CE1 . HIS C 1 105 ? 33.681  -18.895 17.682  1.00 54.49  ? 110 HIS C CE1 1 
ATOM   4747  N NE2 . HIS C 1 105 ? 33.814  -19.773 18.661  1.00 53.63  ? 110 HIS C NE2 1 
ATOM   4748  N N   . LEU C 1 106 ? 37.766  -22.311 18.212  1.00 57.44  ? 111 LEU C N   1 
ATOM   4749  C CA  . LEU C 1 106 ? 38.034  -22.532 19.629  1.00 57.75  ? 111 LEU C CA  1 
ATOM   4750  C C   . LEU C 1 106 ? 39.271  -21.760 20.053  1.00 62.18  ? 111 LEU C C   1 
ATOM   4751  O O   . LEU C 1 106 ? 39.296  -21.149 21.122  1.00 75.91  ? 111 LEU C O   1 
ATOM   4752  C CB  . LEU C 1 106 ? 38.228  -24.023 19.931  1.00 49.47  ? 111 LEU C CB  1 
ATOM   4753  C CG  . LEU C 1 106 ? 38.819  -24.339 21.311  1.00 55.86  ? 111 LEU C CG  1 
ATOM   4754  C CD1 . LEU C 1 106 ? 37.893  -23.861 22.416  1.00 73.97  ? 111 LEU C CD1 1 
ATOM   4755  C CD2 . LEU C 1 106 ? 39.087  -25.811 21.466  1.00 45.37  ? 111 LEU C CD2 1 
ATOM   4756  N N   . LEU C 1 107 ? 40.285  -21.780 19.189  1.00 59.77  ? 112 LEU C N   1 
ATOM   4757  C CA  . LEU C 1 107 ? 41.616  -21.274 19.529  1.00 57.92  ? 112 LEU C CA  1 
ATOM   4758  C C   . LEU C 1 107 ? 41.827  -19.782 19.302  1.00 75.10  ? 112 LEU C C   1 
ATOM   4759  O O   . LEU C 1 107 ? 42.775  -19.204 19.834  1.00 89.06  ? 112 LEU C O   1 
ATOM   4760  C CB  . LEU C 1 107 ? 42.696  -22.056 18.772  1.00 42.72  ? 112 LEU C CB  1 
ATOM   4761  C CG  . LEU C 1 107 ? 42.969  -23.482 19.252  1.00 48.65  ? 112 LEU C CG  1 
ATOM   4762  C CD1 . LEU C 1 107 ? 44.089  -24.095 18.424  1.00 46.38  ? 112 LEU C CD1 1 
ATOM   4763  C CD2 . LEU C 1 107 ? 43.307  -23.515 20.737  1.00 58.24  ? 112 LEU C CD2 1 
ATOM   4764  N N   . SER C 1 108 ? 40.957  -19.163 18.513  1.00 59.67  ? 113 SER C N   1 
ATOM   4765  C CA  . SER C 1 108 ? 41.108  -17.751 18.177  1.00 56.06  ? 113 SER C CA  1 
ATOM   4766  C C   . SER C 1 108 ? 41.541  -16.882 19.373  1.00 62.05  ? 113 SER C C   1 
ATOM   4767  O O   . SER C 1 108 ? 42.196  -15.861 19.187  1.00 75.16  ? 113 SER C O   1 
ATOM   4768  C CB  . SER C 1 108 ? 39.823  -17.204 17.540  1.00 56.32  ? 113 SER C CB  1 
ATOM   4769  O OG  . SER C 1 108 ? 38.748  -17.191 18.465  1.00 55.72  ? 113 SER C OG  1 
ATOM   4770  N N   . SER C 1 109 ? 41.189  -17.298 20.590  1.00 48.99  ? 114 SER C N   1 
ATOM   4771  C CA  . SER C 1 109 ? 41.532  -16.549 21.802  1.00 60.38  ? 114 SER C CA  1 
ATOM   4772  C C   . SER C 1 109 ? 41.594  -17.440 23.050  1.00 82.42  ? 114 SER C C   1 
ATOM   4773  O O   . SER C 1 109 ? 40.722  -18.279 23.262  1.00 92.02  ? 114 SER C O   1 
ATOM   4774  C CB  . SER C 1 109 ? 40.534  -15.405 22.015  1.00 58.70  ? 114 SER C CB  1 
ATOM   4775  O OG  . SER C 1 109 ? 40.370  -15.119 23.395  1.00 81.28  ? 114 SER C OG  1 
ATOM   4776  N N   . VAL C 1 110 ? 42.610  -17.234 23.886  1.00 51.64  ? 115 VAL C N   1 
ATOM   4777  C CA  . VAL C 1 110 ? 42.880  -18.133 25.001  1.00 71.68  ? 115 VAL C CA  1 
ATOM   4778  C C   . VAL C 1 110 ? 43.527  -17.466 26.209  1.00 95.55  ? 115 VAL C C   1 
ATOM   4779  O O   . VAL C 1 110 ? 44.679  -17.047 26.145  1.00 96.08  ? 115 VAL C O   1 
ATOM   4780  C CB  . VAL C 1 110 ? 43.823  -19.247 24.552  1.00 62.22  ? 115 VAL C CB  1 
ATOM   4781  C CG1 . VAL C 1 110 ? 43.039  -20.512 24.187  1.00 44.92  ? 115 VAL C CG1 1 
ATOM   4782  C CG2 . VAL C 1 110 ? 44.654  -18.763 23.376  1.00 56.44  ? 115 VAL C CG2 1 
ATOM   4783  N N   . LYS C 1 111 ? 42.788  -17.408 27.315  1.00 83.48  ? 116 LYS C N   1 
ATOM   4784  C CA  . LYS C 1 111 ? 43.283  -16.852 28.576  1.00 81.80  ? 116 LYS C CA  1 
ATOM   4785  C C   . LYS C 1 111 ? 44.597  -17.495 29.004  1.00 82.87  ? 116 LYS C C   1 
ATOM   4786  O O   . LYS C 1 111 ? 45.407  -16.865 29.684  1.00 89.56  ? 116 LYS C O   1 
ATOM   4787  C CB  . LYS C 1 111 ? 42.248  -17.041 29.689  1.00 79.17  ? 116 LYS C CB  1 
ATOM   4788  C CG  . LYS C 1 111 ? 42.431  -16.123 30.891  1.00 86.45  ? 116 LYS C CG  1 
ATOM   4789  C CD  . LYS C 1 111 ? 41.696  -14.798 30.673  1.00 87.03  ? 116 LYS C CD  1 
ATOM   4790  C CE  . LYS C 1 111 ? 42.228  -13.682 31.571  1.00 91.56  ? 116 LYS C CE  1 
ATOM   4791  N NZ  . LYS C 1 111 ? 41.598  -12.361 31.279  1.00 83.59  ? 116 LYS C NZ  1 
ATOM   4792  N N   . HIS C 1 112 A 44.791  -18.757 28.624  1.00 94.80  ? 116 HIS C N   1 
ATOM   4793  C CA  . HIS C 1 112 A 46.031  -19.476 28.925  1.00 106.10 ? 116 HIS C CA  1 
ATOM   4794  C C   . HIS C 1 112 A 46.283  -20.614 27.942  1.00 95.73  ? 116 HIS C C   1 
ATOM   4795  O O   . HIS C 1 112 A 45.365  -21.087 27.277  1.00 87.76  ? 116 HIS C O   1 
ATOM   4796  C CB  . HIS C 1 112 A 46.025  -20.013 30.359  1.00 113.46 ? 116 HIS C CB  1 
ATOM   4797  C CG  . HIS C 1 112 A 47.305  -20.682 30.756  1.00 117.69 ? 116 HIS C CG  1 
ATOM   4798  N ND1 . HIS C 1 112 A 47.343  -21.914 31.371  1.00 116.58 ? 116 HIS C ND1 1 
ATOM   4799  C CD2 . HIS C 1 112 A 48.595  -20.293 30.615  1.00 122.44 ? 116 HIS C CD2 1 
ATOM   4800  C CE1 . HIS C 1 112 A 48.599  -22.254 31.596  1.00 122.94 ? 116 HIS C CE1 1 
ATOM   4801  N NE2 . HIS C 1 112 A 49.379  -21.288 31.147  1.00 129.02 ? 116 HIS C NE2 1 
ATOM   4802  N N   . PHE C 1 113 B 47.531  -21.060 27.867  1.00 127.04 ? 116 PHE C N   1 
ATOM   4803  C CA  . PHE C 1 113 B 47.915  -22.044 26.872  1.00 123.24 ? 116 PHE C CA  1 
ATOM   4804  C C   . PHE C 1 113 B 49.347  -22.506 27.108  1.00 140.25 ? 116 PHE C C   1 
ATOM   4805  O O   . PHE C 1 113 B 50.204  -21.715 27.500  1.00 152.85 ? 116 PHE C O   1 
ATOM   4806  C CB  . PHE C 1 113 B 47.774  -21.431 25.485  1.00 92.47  ? 116 PHE C CB  1 
ATOM   4807  C CG  . PHE C 1 113 B 47.844  -22.423 24.371  1.00 75.21  ? 116 PHE C CG  1 
ATOM   4808  C CD1 . PHE C 1 113 B 46.826  -23.340 24.176  1.00 72.26  ? 116 PHE C CD1 1 
ATOM   4809  C CD2 . PHE C 1 113 B 48.918  -22.426 23.498  1.00 67.43  ? 116 PHE C CD2 1 
ATOM   4810  C CE1 . PHE C 1 113 B 46.888  -24.253 23.138  1.00 60.72  ? 116 PHE C CE1 1 
ATOM   4811  C CE2 . PHE C 1 113 B 48.987  -23.331 22.454  1.00 57.74  ? 116 PHE C CE2 1 
ATOM   4812  C CZ  . PHE C 1 113 B 47.972  -24.245 22.272  1.00 56.52  ? 116 PHE C CZ  1 
ATOM   4813  N N   . GLU C 1 114 C 49.604  -23.786 26.857  1.00 83.72  ? 116 GLU C N   1 
ATOM   4814  C CA  . GLU C 1 114 C 50.893  -24.394 27.180  1.00 88.54  ? 116 GLU C CA  1 
ATOM   4815  C C   . GLU C 1 114 C 50.955  -25.869 26.775  1.00 71.02  ? 116 GLU C C   1 
ATOM   4816  O O   . GLU C 1 114 C 50.321  -26.721 27.401  1.00 80.16  ? 116 GLU C O   1 
ATOM   4817  C CB  . GLU C 1 114 C 51.160  -24.272 28.682  1.00 108.11 ? 116 GLU C CB  1 
ATOM   4818  C CG  . GLU C 1 114 C 52.296  -25.143 29.188  1.00 123.01 ? 116 GLU C CG  1 
ATOM   4819  C CD  . GLU C 1 114 C 52.337  -25.215 30.699  1.00 130.17 ? 116 GLU C CD  1 
ATOM   4820  O OE1 . GLU C 1 114 C 51.543  -24.505 31.347  1.00 123.70 ? 116 GLU C OE1 1 
ATOM   4821  O OE2 . GLU C 1 114 C 53.157  -25.982 31.242  1.00 138.04 ? 116 GLU C OE2 1 
ATOM   4822  N N   . LYS C 1 115 ? 51.729  -26.168 25.736  1.00 102.31 ? 117 LYS C N   1 
ATOM   4823  C CA  . LYS C 1 115 ? 51.900  -27.544 25.290  1.00 96.24  ? 117 LYS C CA  1 
ATOM   4824  C C   . LYS C 1 115 ? 52.460  -28.411 26.403  1.00 130.74 ? 117 LYS C C   1 
ATOM   4825  O O   . LYS C 1 115 ? 53.353  -27.995 27.137  1.00 161.82 ? 117 LYS C O   1 
ATOM   4826  C CB  . LYS C 1 115 ? 52.821  -27.603 24.078  1.00 71.72  ? 117 LYS C CB  1 
ATOM   4827  C CG  . LYS C 1 115 ? 53.124  -29.008 23.603  1.00 67.36  ? 117 LYS C CG  1 
ATOM   4828  C CD  . LYS C 1 115 ? 53.932  -28.978 22.311  1.00 66.77  ? 117 LYS C CD  1 
ATOM   4829  C CE  . LYS C 1 115 ? 53.253  -28.092 21.263  1.00 69.24  ? 117 LYS C CE  1 
ATOM   4830  N NZ  . LYS C 1 115 ? 54.158  -27.696 20.131  1.00 70.23  ? 117 LYS C NZ  1 
ATOM   4831  N N   . VAL C 1 116 ? 51.927  -29.621 26.521  1.00 83.42  ? 118 VAL C N   1 
ATOM   4832  C CA  . VAL C 1 116 ? 52.333  -30.552 27.566  1.00 103.62 ? 118 VAL C CA  1 
ATOM   4833  C C   . VAL C 1 116 ? 52.604  -31.934 26.975  1.00 99.96  ? 118 VAL C C   1 
ATOM   4834  O O   . VAL C 1 116 ? 51.973  -32.324 25.995  1.00 85.91  ? 118 VAL C O   1 
ATOM   4835  C CB  . VAL C 1 116 ? 51.248  -30.663 28.654  1.00 95.22  ? 118 VAL C CB  1 
ATOM   4836  C CG1 . VAL C 1 116 ? 51.471  -31.894 29.516  1.00 102.83 ? 118 VAL C CG1 1 
ATOM   4837  C CG2 . VAL C 1 116 ? 51.217  -29.401 29.501  1.00 95.14  ? 118 VAL C CG2 1 
ATOM   4838  N N   . LYS C 1 117 ? 53.556  -32.660 27.559  1.00 114.59 ? 119 LYS C N   1 
ATOM   4839  C CA  . LYS C 1 117 ? 53.819  -34.044 27.168  1.00 104.02 ? 119 LYS C CA  1 
ATOM   4840  C C   . LYS C 1 117 ? 52.847  -34.966 27.897  1.00 114.53 ? 119 LYS C C   1 
ATOM   4841  O O   . LYS C 1 117 ? 52.644  -34.830 29.104  1.00 125.18 ? 119 LYS C O   1 
ATOM   4842  C CB  . LYS C 1 117 ? 55.267  -34.438 27.482  1.00 111.76 ? 119 LYS C CB  1 
ATOM   4843  C CG  . LYS C 1 117 ? 55.643  -35.838 27.016  1.00 98.67  ? 119 LYS C CG  1 
ATOM   4844  C CD  . LYS C 1 117 ? 56.963  -36.308 27.621  1.00 118.93 ? 119 LYS C CD  1 
ATOM   4845  C CE  . LYS C 1 117 ? 58.167  -35.600 27.010  1.00 122.88 ? 119 LYS C CE  1 
ATOM   4846  N NZ  . LYS C 1 117 ? 59.462  -36.178 27.489  1.00 141.33 ? 119 LYS C NZ  1 
ATOM   4847  N N   . ILE C 1 118 ? 52.239  -35.893 27.162  1.00 99.74  ? 120 ILE C N   1 
ATOM   4848  C CA  . ILE C 1 118 ? 51.231  -36.787 27.739  1.00 105.78 ? 120 ILE C CA  1 
ATOM   4849  C C   . ILE C 1 118 ? 51.556  -38.273 27.536  1.00 101.04 ? 120 ILE C C   1 
ATOM   4850  O O   . ILE C 1 118 ? 51.423  -39.081 28.457  1.00 102.32 ? 120 ILE C O   1 
ATOM   4851  C CB  . ILE C 1 118 ? 49.830  -36.504 27.153  1.00 100.66 ? 120 ILE C CB  1 
ATOM   4852  C CG1 . ILE C 1 118 ? 49.953  -36.113 25.677  1.00 75.47  ? 120 ILE C CG1 1 
ATOM   4853  C CG2 . ILE C 1 118 ? 49.124  -35.412 27.941  1.00 104.46 ? 120 ILE C CG2 1 
ATOM   4854  C CD1 . ILE C 1 118 ? 48.629  -35.972 24.967  1.00 60.46  ? 120 ILE C CD1 1 
ATOM   4855  N N   . LEU C 1 119 ? 51.977  -38.622 26.325  1.00 105.73 ? 121 LEU C N   1 
ATOM   4856  C CA  . LEU C 1 119 ? 52.228  -40.009 25.965  1.00 103.24 ? 121 LEU C CA  1 
ATOM   4857  C C   . LEU C 1 119 ? 53.598  -40.157 25.312  1.00 103.14 ? 121 LEU C C   1 
ATOM   4858  O O   . LEU C 1 119 ? 53.694  -40.305 24.088  1.00 89.95  ? 121 LEU C O   1 
ATOM   4859  C CB  . LEU C 1 119 ? 51.138  -40.505 25.017  1.00 87.32  ? 121 LEU C CB  1 
ATOM   4860  C CG  . LEU C 1 119 ? 49.705  -40.240 25.488  1.00 93.65  ? 121 LEU C CG  1 
ATOM   4861  C CD1 . LEU C 1 119 ? 48.698  -40.766 24.476  1.00 73.82  ? 121 LEU C CD1 1 
ATOM   4862  C CD2 . LEU C 1 119 ? 49.469  -40.852 26.857  1.00 113.67 ? 121 LEU C CD2 1 
ATOM   4863  N N   . PRO C 1 120 ? 54.661  -40.131 26.135  1.00 88.62  ? 122 PRO C N   1 
ATOM   4864  C CA  . PRO C 1 120 ? 56.064  -40.116 25.701  1.00 78.52  ? 122 PRO C CA  1 
ATOM   4865  C C   . PRO C 1 120 ? 56.347  -41.116 24.590  1.00 59.41  ? 122 PRO C C   1 
ATOM   4866  O O   . PRO C 1 120 ? 56.007  -42.290 24.722  1.00 60.08  ? 122 PRO C O   1 
ATOM   4867  C CB  . PRO C 1 120 ? 56.817  -40.503 26.971  1.00 106.99 ? 122 PRO C CB  1 
ATOM   4868  C CG  . PRO C 1 120 ? 55.954  -39.990 28.071  1.00 124.90 ? 122 PRO C CG  1 
ATOM   4869  C CD  . PRO C 1 120 ? 54.541  -40.182 27.604  1.00 115.91 ? 122 PRO C CD  1 
ATOM   4870  N N   . LYS C 1 121 ? 56.976  -40.647 23.517  1.00 104.80 ? 123 LYS C N   1 
ATOM   4871  C CA  . LYS C 1 121 ? 57.213  -41.448 22.317  1.00 94.81  ? 123 LYS C CA  1 
ATOM   4872  C C   . LYS C 1 121 ? 57.763  -42.856 22.579  1.00 107.74 ? 123 LYS C C   1 
ATOM   4873  O O   . LYS C 1 121 ? 57.429  -43.796 21.861  1.00 98.92  ? 123 LYS C O   1 
ATOM   4874  C CB  . LYS C 1 121 ? 58.146  -40.689 21.368  1.00 85.80  ? 123 LYS C CB  1 
ATOM   4875  C CG  . LYS C 1 121 ? 58.089  -41.121 19.910  1.00 71.52  ? 123 LYS C CG  1 
ATOM   4876  C CD  . LYS C 1 121 ? 58.711  -40.046 19.025  1.00 69.87  ? 123 LYS C CD  1 
ATOM   4877  C CE  . LYS C 1 121 ? 58.294  -40.203 17.565  1.00 68.33  ? 123 LYS C CE  1 
ATOM   4878  N NZ  . LYS C 1 121 ? 58.443  -38.932 16.794  1.00 70.78  ? 123 LYS C NZ  1 
ATOM   4879  N N   . ASP C 1 122 ? 58.603  -43.008 23.598  1.00 108.36 ? 125 ASP C N   1 
ATOM   4880  C CA  . ASP C 1 122 ? 59.253  -44.295 23.843  1.00 126.46 ? 125 ASP C CA  1 
ATOM   4881  C C   . ASP C 1 122 ? 58.496  -45.209 24.813  1.00 138.58 ? 125 ASP C C   1 
ATOM   4882  O O   . ASP C 1 122 ? 58.945  -46.321 25.092  1.00 143.91 ? 125 ASP C O   1 
ATOM   4883  C CB  . ASP C 1 122 ? 60.709  -44.106 24.292  1.00 150.08 ? 125 ASP C CB  1 
ATOM   4884  C CG  . ASP C 1 122 ? 60.833  -43.276 25.554  1.00 174.22 ? 125 ASP C CG  1 
ATOM   4885  O OD1 . ASP C 1 122 ? 59.839  -43.171 26.304  1.00 190.26 ? 125 ASP C OD1 1 
ATOM   4886  O OD2 . ASP C 1 122 ? 61.931  -42.735 25.800  1.00 176.01 ? 125 ASP C OD2 1 
ATOM   4887  N N   . ARG C 1 123 ? 57.355  -44.748 25.320  1.00 97.81  ? 126 ARG C N   1 
ATOM   4888  C CA  . ARG C 1 123 ? 56.504  -45.595 26.155  1.00 103.04 ? 126 ARG C CA  1 
ATOM   4889  C C   . ARG C 1 123 ? 55.849  -46.672 25.298  1.00 75.46  ? 126 ARG C C   1 
ATOM   4890  O O   . ARG C 1 123 ? 55.398  -47.699 25.809  1.00 80.98  ? 126 ARG C O   1 
ATOM   4891  C CB  . ARG C 1 123 ? 55.429  -44.777 26.871  1.00 118.83 ? 126 ARG C CB  1 
ATOM   4892  C CG  . ARG C 1 123 ? 55.963  -43.749 27.855  1.00 147.74 ? 126 ARG C CG  1 
ATOM   4893  C CD  . ARG C 1 123 ? 56.776  -44.398 28.967  1.00 168.15 ? 126 ARG C CD  1 
ATOM   4894  N NE  . ARG C 1 123 ? 57.241  -43.418 29.948  1.00 176.56 ? 126 ARG C NE  1 
ATOM   4895  C CZ  . ARG C 1 123 ? 58.424  -42.813 29.903  1.00 181.86 ? 126 ARG C CZ  1 
ATOM   4896  N NH1 . ARG C 1 123 ? 59.277  -43.086 28.925  1.00 176.32 ? 126 ARG C NH1 1 
ATOM   4897  N NH2 . ARG C 1 123 ? 58.757  -41.935 30.840  1.00 188.83 ? 126 ARG C NH2 1 
ATOM   4898  N N   . TRP C 1 124 ? 55.799  -46.427 23.989  1.00 117.42 ? 127 TRP C N   1 
ATOM   4899  C CA  . TRP C 1 124 ? 55.296  -47.415 23.042  1.00 109.66 ? 127 TRP C CA  1 
ATOM   4900  C C   . TRP C 1 124 ? 56.341  -48.489 22.783  1.00 116.14 ? 127 TRP C C   1 
ATOM   4901  O O   . TRP C 1 124 ? 56.995  -48.511 21.735  1.00 107.68 ? 127 TRP C O   1 
ATOM   4902  C CB  . TRP C 1 124 ? 54.844  -46.758 21.734  1.00 95.73  ? 127 TRP C CB  1 
ATOM   4903  C CG  . TRP C 1 124 ? 53.606  -45.948 21.902  1.00 95.44  ? 127 TRP C CG  1 
ATOM   4904  C CD1 . TRP C 1 124 ? 53.478  -44.607 21.726  1.00 94.60  ? 127 TRP C CD1 1 
ATOM   4905  C CD2 . TRP C 1 124 ? 52.321  -46.425 22.316  1.00 94.67  ? 127 TRP C CD2 1 
ATOM   4906  N NE1 . TRP C 1 124 ? 52.190  -44.218 21.991  1.00 93.26  ? 127 TRP C NE1 1 
ATOM   4907  C CE2 . TRP C 1 124 ? 51.460  -45.317 22.358  1.00 91.77  ? 127 TRP C CE2 1 
ATOM   4908  C CE3 . TRP C 1 124 ? 51.814  -47.683 22.651  1.00 102.04 ? 127 TRP C CE3 1 
ATOM   4909  C CZ2 . TRP C 1 124 ? 50.119  -45.426 22.721  1.00 91.65  ? 127 TRP C CZ2 1 
ATOM   4910  C CZ3 . TRP C 1 124 ? 50.483  -47.790 23.011  1.00 104.25 ? 127 TRP C CZ3 1 
ATOM   4911  C CH2 . TRP C 1 124 ? 49.651  -46.669 23.042  1.00 96.60  ? 127 TRP C CH2 1 
ATOM   4912  N N   . THR C 1 125 ? 56.493  -49.375 23.763  1.00 96.82  ? 128 THR C N   1 
ATOM   4913  C CA  . THR C 1 125 ? 57.444  -50.476 23.677  1.00 103.91 ? 128 THR C CA  1 
ATOM   4914  C C   . THR C 1 125 ? 56.970  -51.534 22.692  1.00 98.66  ? 128 THR C C   1 
ATOM   4915  O O   . THR C 1 125 ? 57.770  -52.110 21.957  1.00 92.82  ? 128 THR C O   1 
ATOM   4916  C CB  . THR C 1 125 ? 57.662  -51.134 25.050  1.00 117.93 ? 128 THR C CB  1 
ATOM   4917  O OG1 . THR C 1 125 ? 56.454  -51.045 25.815  1.00 119.92 ? 128 THR C OG1 1 
ATOM   4918  C CG2 . THR C 1 125 ? 58.777  -50.433 25.803  1.00 131.98 ? 128 THR C CG2 1 
ATOM   4919  N N   . GLN C 1 126 ? 55.663  -51.774 22.678  1.00 142.31 ? 129 GLN C N   1 
ATOM   4920  C CA  . GLN C 1 126 ? 55.081  -52.814 21.838  1.00 132.79 ? 129 GLN C CA  1 
ATOM   4921  C C   . GLN C 1 126 ? 55.331  -52.563 20.351  1.00 111.90 ? 129 GLN C C   1 
ATOM   4922  O O   . GLN C 1 126 ? 55.457  -53.512 19.573  1.00 100.69 ? 129 GLN C O   1 
ATOM   4923  C CB  . GLN C 1 126 ? 53.580  -52.946 22.110  1.00 138.32 ? 129 GLN C CB  1 
ATOM   4924  C CG  . GLN C 1 126 ? 53.205  -52.952 23.590  1.00 155.90 ? 129 GLN C CG  1 
ATOM   4925  C CD  . GLN C 1 126 ? 52.893  -51.562 24.125  1.00 149.70 ? 129 GLN C CD  1 
ATOM   4926  O OE1 . GLN C 1 126 ? 52.653  -50.628 23.359  1.00 142.08 ? 129 GLN C OE1 1 
ATOM   4927  N NE2 . GLN C 1 126 ? 52.891  -51.423 25.446  1.00 150.15 ? 129 GLN C NE2 1 
ATOM   4928  N N   . HIS C 1 127 ? 55.401  -51.287 19.962  1.00 101.44 ? 130 HIS C N   1 
ATOM   4929  C CA  . HIS C 1 127 ? 55.625  -50.921 18.561  1.00 86.96  ? 130 HIS C CA  1 
ATOM   4930  C C   . HIS C 1 127 ? 56.781  -49.933 18.374  1.00 89.10  ? 130 HIS C C   1 
ATOM   4931  O O   . HIS C 1 127 ? 57.284  -49.348 19.338  1.00 95.18  ? 130 HIS C O   1 
ATOM   4932  C CB  . HIS C 1 127 ? 54.366  -50.309 17.936  1.00 73.05  ? 130 HIS C CB  1 
ATOM   4933  C CG  . HIS C 1 127 ? 53.084  -50.942 18.382  1.00 69.68  ? 130 HIS C CG  1 
ATOM   4934  N ND1 . HIS C 1 127 ? 52.670  -50.939 19.698  1.00 78.76  ? 130 HIS C ND1 1 
ATOM   4935  C CD2 . HIS C 1 127 ? 52.111  -51.569 17.680  1.00 67.23  ? 130 HIS C CD2 1 
ATOM   4936  C CE1 . HIS C 1 127 ? 51.503  -51.554 19.790  1.00 82.25  ? 130 HIS C CE1 1 
ATOM   4937  N NE2 . HIS C 1 127 ? 51.142  -51.945 18.579  1.00 74.90  ? 130 HIS C NE2 1 
ATOM   4938  N N   . THR C 1 128 ? 57.178  -49.746 17.115  1.00 90.96  ? 131 THR C N   1 
ATOM   4939  C CA  . THR C 1 128 ? 58.181  -48.753 16.746  1.00 94.26  ? 131 THR C CA  1 
ATOM   4940  C C   . THR C 1 128 ? 57.633  -47.354 16.971  1.00 91.86  ? 131 THR C C   1 
ATOM   4941  O O   . THR C 1 128 ? 56.419  -47.151 16.977  1.00 92.02  ? 131 THR C O   1 
ATOM   4942  C CB  . THR C 1 128 ? 58.542  -48.851 15.260  1.00 98.90  ? 131 THR C CB  1 
ATOM   4943  O OG1 . THR C 1 128 ? 58.430  -50.209 14.823  1.00 103.61 ? 131 THR C OG1 1 
ATOM   4944  C CG2 . THR C 1 128 ? 59.956  -48.337 15.020  1.00 103.81 ? 131 THR C CG2 1 
ATOM   4945  N N   . THR C 1 129 ? 58.524  -46.381 17.131  1.00 107.45 ? 132 THR C N   1 
ATOM   4946  C CA  . THR C 1 129 ? 58.101  -45.002 17.339  1.00 103.35 ? 132 THR C CA  1 
ATOM   4947  C C   . THR C 1 129 ? 58.995  -44.015 16.596  1.00 106.15 ? 132 THR C C   1 
ATOM   4948  O O   . THR C 1 129 ? 59.216  -42.900 17.061  1.00 103.74 ? 132 THR C O   1 
ATOM   4949  C CB  . THR C 1 129 ? 58.066  -44.645 18.842  1.00 104.09 ? 132 THR C CB  1 
ATOM   4950  O OG1 . THR C 1 129 ? 59.363  -44.844 19.416  1.00 112.91 ? 132 THR C OG1 1 
ATOM   4951  C CG2 . THR C 1 129 ? 57.060  -45.519 19.573  1.00 100.26 ? 132 THR C CG2 1 
ATOM   4952  N N   . THR C 1 130 ? 59.502  -44.425 15.437  1.00 102.26 ? 133 THR C N   1 
ATOM   4953  C CA  . THR C 1 130 ? 60.434  -43.593 14.677  1.00 107.97 ? 133 THR C CA  1 
ATOM   4954  C C   . THR C 1 130 ? 60.189  -43.656 13.173  1.00 110.65 ? 133 THR C C   1 
ATOM   4955  O O   . THR C 1 130 ? 61.092  -43.401 12.378  1.00 119.81 ? 133 THR C O   1 
ATOM   4956  C CB  . THR C 1 130 ? 61.902  -43.985 14.953  1.00 101.37 ? 133 THR C CB  1 
ATOM   4957  O OG1 . THR C 1 130 ? 62.086  -45.381 14.679  1.00 105.88 ? 133 THR C OG1 1 
ATOM   4958  C CG2 . THR C 1 130 ? 62.274  -43.699 16.405  1.00 95.35  ? 133 THR C CG2 1 
ATOM   4959  N N   . GLY C 1 131 ? 58.970  -44.007 12.788  1.00 73.78  ? 134 GLY C N   1 
ATOM   4960  C CA  . GLY C 1 131 ? 58.593  -43.984 11.389  1.00 85.19  ? 134 GLY C CA  1 
ATOM   4961  C C   . GLY C 1 131 ? 58.353  -42.551 10.965  1.00 91.53  ? 134 GLY C C   1 
ATOM   4962  O O   . GLY C 1 131 ? 58.000  -41.708 11.789  1.00 86.58  ? 134 GLY C O   1 
ATOM   4963  N N   . GLY C 1 132 ? 58.550  -42.267 9.684   1.00 72.61  ? 135 GLY C N   1 
ATOM   4964  C CA  . GLY C 1 132 ? 58.367  -40.918 9.179   1.00 75.53  ? 135 GLY C CA  1 
ATOM   4965  C C   . GLY C 1 132 ? 58.227  -40.930 7.671   1.00 106.41 ? 135 GLY C C   1 
ATOM   4966  O O   . GLY C 1 132 ? 58.147  -42.001 7.061   1.00 114.49 ? 135 GLY C O   1 
ATOM   4967  N N   . SER C 1 133 ? 58.196  -39.747 7.061   1.00 68.55  ? 136 SER C N   1 
ATOM   4968  C CA  . SER C 1 133 ? 58.084  -39.671 5.607   1.00 112.33 ? 136 SER C CA  1 
ATOM   4969  C C   . SER C 1 133 ? 58.897  -38.544 4.967   1.00 145.53 ? 136 SER C C   1 
ATOM   4970  O O   . SER C 1 133 ? 59.401  -37.643 5.645   1.00 134.25 ? 136 SER C O   1 
ATOM   4971  C CB  . SER C 1 133 ? 56.618  -39.595 5.168   1.00 113.52 ? 136 SER C CB  1 
ATOM   4972  O OG  . SER C 1 133 ? 56.478  -39.972 3.808   1.00 123.69 ? 136 SER C OG  1 
ATOM   4973  N N   . ARG C 1 134 ? 59.003  -38.622 3.645   1.00 143.83 ? 137 ARG C N   1 
ATOM   4974  C CA  . ARG C 1 134 ? 59.851  -37.745 2.853   1.00 151.14 ? 137 ARG C CA  1 
ATOM   4975  C C   . ARG C 1 134 ? 59.213  -36.369 2.680   1.00 144.03 ? 137 ARG C C   1 
ATOM   4976  O O   . ARG C 1 134 ? 59.907  -35.383 2.430   1.00 156.61 ? 137 ARG C O   1 
ATOM   4977  C CB  . ARG C 1 134 ? 60.093  -38.395 1.488   1.00 158.20 ? 137 ARG C CB  1 
ATOM   4978  C CG  . ARG C 1 134 ? 61.355  -37.964 0.768   1.00 173.29 ? 137 ARG C CG  1 
ATOM   4979  C CD  . ARG C 1 134 ? 61.603  -38.873 -0.429  1.00 183.82 ? 137 ARG C CD  1 
ATOM   4980  N NE  . ARG C 1 134 ? 62.672  -38.389 -1.297  1.00 202.80 ? 137 ARG C NE  1 
ATOM   4981  C CZ  . ARG C 1 134 ? 63.949  -38.735 -1.176  1.00 212.47 ? 137 ARG C CZ  1 
ATOM   4982  N NH1 . ARG C 1 134 ? 64.324  -39.568 -0.215  1.00 210.35 ? 137 ARG C NH1 1 
ATOM   4983  N NH2 . ARG C 1 134 ? 64.852  -38.245 -2.014  1.00 223.28 ? 137 ARG C NH2 1 
ATOM   4984  N N   . ALA C 1 135 ? 57.891  -36.308 2.816   1.00 101.85 ? 138 ALA C N   1 
ATOM   4985  C CA  . ALA C 1 135 ? 57.158  -35.052 2.656   1.00 92.82  ? 138 ALA C CA  1 
ATOM   4986  C C   . ALA C 1 135 ? 57.202  -34.192 3.917   1.00 85.88  ? 138 ALA C C   1 
ATOM   4987  O O   . ALA C 1 135 ? 56.705  -33.067 3.927   1.00 81.42  ? 138 ALA C O   1 
ATOM   4988  C CB  . ALA C 1 135 ? 55.720  -35.317 2.236   1.00 81.10  ? 138 ALA C CB  1 
ATOM   4989  N N   . CYS C 1 136 ? 57.788  -34.731 4.980   1.00 151.09 ? 139 CYS C N   1 
ATOM   4990  C CA  . CYS C 1 136 ? 58.079  -33.948 6.175   1.00 131.15 ? 139 CYS C CA  1 
ATOM   4991  C C   . CYS C 1 136 ? 59.589  -33.816 6.302   1.00 133.31 ? 139 CYS C C   1 
ATOM   4992  O O   . CYS C 1 136 ? 60.148  -33.877 7.400   1.00 107.33 ? 139 CYS C O   1 
ATOM   4993  C CB  . CYS C 1 136 ? 57.478  -34.598 7.422   1.00 103.80 ? 139 CYS C CB  1 
ATOM   4994  S SG  . CYS C 1 136 ? 55.682  -34.409 7.566   1.00 84.89  ? 139 CYS C SG  1 
ATOM   4995  N N   . ALA C 1 137 ? 60.233  -33.627 5.154   1.00 138.29 ? 140 ALA C N   1 
ATOM   4996  C CA  . ALA C 1 137 ? 61.688  -33.595 5.053   1.00 143.78 ? 140 ALA C CA  1 
ATOM   4997  C C   . ALA C 1 137 ? 62.340  -32.541 5.942   1.00 124.10 ? 140 ALA C C   1 
ATOM   4998  O O   . ALA C 1 137 ? 62.030  -31.352 5.854   1.00 121.69 ? 140 ALA C O   1 
ATOM   4999  C CB  . ALA C 1 137 ? 62.114  -33.400 3.602   1.00 166.54 ? 140 ALA C CB  1 
ATOM   5000  N N   . VAL C 1 138 ? 63.248  -32.998 6.797   1.00 150.49 ? 141 VAL C N   1 
ATOM   5001  C CA  . VAL C 1 138 ? 64.042  -32.116 7.637   1.00 134.03 ? 141 VAL C CA  1 
ATOM   5002  C C   . VAL C 1 138 ? 65.475  -32.094 7.111   1.00 154.28 ? 141 VAL C C   1 
ATOM   5003  O O   . VAL C 1 138 ? 66.334  -32.838 7.588   1.00 152.15 ? 141 VAL C O   1 
ATOM   5004  C CB  . VAL C 1 138 ? 64.031  -32.585 9.101   1.00 96.65  ? 141 VAL C CB  1 
ATOM   5005  C CG1 . VAL C 1 138 ? 64.786  -31.608 9.980   1.00 79.44  ? 141 VAL C CG1 1 
ATOM   5006  C CG2 . VAL C 1 138 ? 62.606  -32.741 9.588   1.00 87.16  ? 141 VAL C CG2 1 
ATOM   5007  N N   . SER C 1 139 ? 65.717  -31.243 6.118   1.00 145.70 ? 142 SER C N   1 
ATOM   5008  C CA  . SER C 1 139 ? 67.013  -31.156 5.441   1.00 165.37 ? 142 SER C CA  1 
ATOM   5009  C C   . SER C 1 139 ? 67.501  -32.499 4.887   1.00 181.50 ? 142 SER C C   1 
ATOM   5010  O O   . SER C 1 139 ? 68.468  -33.075 5.387   1.00 169.56 ? 142 SER C O   1 
ATOM   5011  C CB  . SER C 1 139 ? 68.076  -30.509 6.342   1.00 142.13 ? 142 SER C CB  1 
ATOM   5012  O OG  . SER C 1 139 ? 68.158  -31.143 7.606   1.00 112.13 ? 142 SER C OG  1 
ATOM   5013  N N   . GLY C 1 140 ? 66.823  -32.984 3.848   1.00 116.83 ? 143 GLY C N   1 
ATOM   5014  C CA  . GLY C 1 140 ? 67.220  -34.200 3.158   1.00 137.13 ? 143 GLY C CA  1 
ATOM   5015  C C   . GLY C 1 140 ? 66.929  -35.481 3.918   1.00 117.11 ? 143 GLY C C   1 
ATOM   5016  O O   . GLY C 1 140 ? 66.946  -36.571 3.346   1.00 131.70 ? 143 GLY C O   1 
ATOM   5017  N N   . ASN C 1 141 ? 66.661  -35.348 5.213   1.00 206.96 ? 144 ASN C N   1 
ATOM   5018  C CA  . ASN C 1 141 ? 66.407  -36.499 6.071   1.00 176.48 ? 144 ASN C CA  1 
ATOM   5019  C C   . ASN C 1 141 ? 64.957  -36.555 6.538   1.00 150.73 ? 144 ASN C C   1 
ATOM   5020  O O   . ASN C 1 141 ? 64.501  -35.656 7.240   1.00 131.60 ? 144 ASN C O   1 
ATOM   5021  C CB  . ASN C 1 141 ? 67.335  -36.465 7.285   1.00 157.33 ? 144 ASN C CB  1 
ATOM   5022  C CG  . ASN C 1 141 ? 68.797  -36.360 6.899   1.00 176.88 ? 144 ASN C CG  1 
ATOM   5023  O OD1 . ASN C 1 141 ? 69.209  -36.841 5.842   1.00 198.05 ? 144 ASN C OD1 1 
ATOM   5024  N ND2 . ASN C 1 141 ? 69.592  -35.728 7.757   1.00 172.48 ? 144 ASN C ND2 1 
ATOM   5025  N N   . PRO C 1 142 ? 64.231  -37.618 6.152   1.00 139.64 ? 145 PRO C N   1 
ATOM   5026  C CA  . PRO C 1 142 ? 62.819  -37.842 6.495   1.00 124.32 ? 145 PRO C CA  1 
ATOM   5027  C C   . PRO C 1 142 ? 62.503  -37.740 7.999   1.00 90.80  ? 145 PRO C C   1 
ATOM   5028  O O   . PRO C 1 142 ? 63.323  -38.118 8.843   1.00 82.10  ? 145 PRO C O   1 
ATOM   5029  C CB  . PRO C 1 142 ? 62.567  -39.261 5.983   1.00 128.72 ? 145 PRO C CB  1 
ATOM   5030  C CG  . PRO C 1 142 ? 63.511  -39.405 4.838   1.00 160.01 ? 145 PRO C CG  1 
ATOM   5031  C CD  . PRO C 1 142 ? 64.749  -38.665 5.253   1.00 162.69 ? 145 PRO C CD  1 
ATOM   5032  N N   . SER C 1 143 ? 61.312  -37.230 8.317   1.00 125.50 ? 146 SER C N   1 
ATOM   5033  C CA  . SER C 1 143 ? 60.895  -37.010 9.703   1.00 102.63 ? 146 SER C CA  1 
ATOM   5034  C C   . SER C 1 143 ? 59.368  -36.906 9.820   1.00 98.88  ? 146 SER C C   1 
ATOM   5035  O O   . SER C 1 143 ? 58.648  -37.364 8.929   1.00 109.88 ? 146 SER C O   1 
ATOM   5036  C CB  . SER C 1 143 ? 61.562  -35.755 10.269  1.00 99.34  ? 146 SER C CB  1 
ATOM   5037  O OG  . SER C 1 143 ? 61.328  -35.629 11.659  1.00 80.43  ? 146 SER C OG  1 
ATOM   5038  N N   . PHE C 1 144 ? 58.886  -36.295 10.907  1.00 123.08 ? 147 PHE C N   1 
ATOM   5039  C CA  . PHE C 1 144 ? 57.451  -36.266 11.226  1.00 113.76 ? 147 PHE C CA  1 
ATOM   5040  C C   . PHE C 1 144 ? 57.054  -35.074 12.114  1.00 107.02 ? 147 PHE C C   1 
ATOM   5041  O O   . PHE C 1 144 ? 57.909  -34.441 12.733  1.00 111.59 ? 147 PHE C O   1 
ATOM   5042  C CB  . PHE C 1 144 ? 57.057  -37.579 11.914  1.00 95.93  ? 147 PHE C CB  1 
ATOM   5043  C CG  . PHE C 1 144 ? 55.618  -37.983 11.700  1.00 89.40  ? 147 PHE C CG  1 
ATOM   5044  C CD1 . PHE C 1 144 ? 55.137  -38.254 10.425  1.00 105.80 ? 147 PHE C CD1 1 
ATOM   5045  C CD2 . PHE C 1 144 ? 54.757  -38.123 12.778  1.00 78.78  ? 147 PHE C CD2 1 
ATOM   5046  C CE1 . PHE C 1 144 ? 53.822  -38.634 10.227  1.00 109.14 ? 147 PHE C CE1 1 
ATOM   5047  C CE2 . PHE C 1 144 ? 53.440  -38.506 12.587  1.00 80.25  ? 147 PHE C CE2 1 
ATOM   5048  C CZ  . PHE C 1 144 ? 52.972  -38.761 11.307  1.00 92.88  ? 147 PHE C CZ  1 
ATOM   5049  N N   . PHE C 1 145 ? 55.755  -34.781 12.174  1.00 65.49  ? 148 PHE C N   1 
ATOM   5050  C CA  . PHE C 1 145 ? 55.216  -33.726 13.040  1.00 54.14  ? 148 PHE C CA  1 
ATOM   5051  C C   . PHE C 1 145 ? 55.779  -33.785 14.464  1.00 46.72  ? 148 PHE C C   1 
ATOM   5052  O O   . PHE C 1 145 ? 55.553  -34.746 15.162  1.00 43.57  ? 148 PHE C O   1 
ATOM   5053  C CB  . PHE C 1 145 ? 53.682  -33.824 13.105  1.00 53.10  ? 148 PHE C CB  1 
ATOM   5054  C CG  . PHE C 1 145 ? 53.003  -33.841 11.753  1.00 67.57  ? 148 PHE C CG  1 
ATOM   5055  C CD1 . PHE C 1 145 ? 52.613  -32.660 11.138  1.00 72.05  ? 148 PHE C CD1 1 
ATOM   5056  C CD2 . PHE C 1 145 ? 52.740  -35.038 11.106  1.00 68.96  ? 148 PHE C CD2 1 
ATOM   5057  C CE1 . PHE C 1 145 ? 51.979  -32.677 9.899   1.00 78.15  ? 148 PHE C CE1 1 
ATOM   5058  C CE2 . PHE C 1 145 ? 52.109  -35.058 9.866   1.00 76.49  ? 148 PHE C CE2 1 
ATOM   5059  C CZ  . PHE C 1 145 ? 51.728  -33.878 9.265   1.00 81.58  ? 148 PHE C CZ  1 
ATOM   5060  N N   . ARG C 1 146 ? 56.477  -32.749 14.911  1.00 104.57 ? 149 ARG C N   1 
ATOM   5061  C CA  . ARG C 1 146 ? 57.172  -32.799 16.205  1.00 108.93 ? 149 ARG C CA  1 
ATOM   5062  C C   . ARG C 1 146 ? 56.332  -33.216 17.429  1.00 102.03 ? 149 ARG C C   1 
ATOM   5063  O O   . ARG C 1 146 ? 56.884  -33.436 18.514  1.00 108.59 ? 149 ARG C O   1 
ATOM   5064  C CB  . ARG C 1 146 ? 57.876  -31.467 16.488  1.00 120.87 ? 149 ARG C CB  1 
ATOM   5065  C CG  . ARG C 1 146 ? 58.756  -30.970 15.349  1.00 135.07 ? 149 ARG C CG  1 
ATOM   5066  C CD  . ARG C 1 146 ? 59.781  -32.013 14.936  1.00 149.13 ? 149 ARG C CD  1 
ATOM   5067  N NE  . ARG C 1 146 ? 60.812  -32.222 15.950  1.00 158.13 ? 149 ARG C NE  1 
ATOM   5068  C CZ  . ARG C 1 146 ? 61.950  -31.536 16.013  1.00 171.13 ? 149 ARG C CZ  1 
ATOM   5069  N NH1 . ARG C 1 146 ? 62.208  -30.586 15.123  1.00 180.70 ? 149 ARG C NH1 1 
ATOM   5070  N NH2 . ARG C 1 146 ? 62.831  -31.801 16.970  1.00 174.47 ? 149 ARG C NH2 1 
ATOM   5071  N N   . ASN C 1 147 ? 55.015  -33.327 17.265  1.00 98.22  ? 150 ASN C N   1 
ATOM   5072  C CA  . ASN C 1 147 ? 54.132  -33.686 18.383  1.00 91.26  ? 150 ASN C CA  1 
ATOM   5073  C C   . ASN C 1 147 ? 53.309  -34.958 18.164  1.00 89.03  ? 150 ASN C C   1 
ATOM   5074  O O   . ASN C 1 147 ? 52.399  -35.255 18.944  1.00 90.95  ? 150 ASN C O   1 
ATOM   5075  C CB  . ASN C 1 147 ? 53.175  -32.537 18.705  1.00 91.49  ? 150 ASN C CB  1 
ATOM   5076  C CG  . ASN C 1 147 ? 53.892  -31.266 19.122  1.00 92.67  ? 150 ASN C CG  1 
ATOM   5077  O OD1 . ASN C 1 147 ? 54.826  -31.293 19.922  1.00 99.88  ? 150 ASN C OD1 1 
ATOM   5078  N ND2 . ASN C 1 147 ? 53.445  -30.140 18.581  1.00 83.81  ? 150 ASN C ND2 1 
ATOM   5079  N N   . MET C 1 148 ? 53.632  -35.701 17.107  1.00 97.39  ? 151 MET C N   1 
ATOM   5080  C CA  . MET C 1 148 ? 52.875  -36.895 16.722  1.00 97.23  ? 151 MET C CA  1 
ATOM   5081  C C   . MET C 1 148 ? 53.764  -38.143 16.549  1.00 100.42 ? 151 MET C C   1 
ATOM   5082  O O   . MET C 1 148 ? 54.927  -38.046 16.143  1.00 102.22 ? 151 MET C O   1 
ATOM   5083  C CB  . MET C 1 148 ? 52.089  -36.623 15.434  1.00 98.59  ? 151 MET C CB  1 
ATOM   5084  C CG  . MET C 1 148 ? 51.309  -35.320 15.451  1.00 97.65  ? 151 MET C CG  1 
ATOM   5085  S SD  . MET C 1 148 ? 49.912  -35.350 16.590  1.00 75.96  ? 151 MET C SD  1 
ATOM   5086  C CE  . MET C 1 148 ? 48.753  -36.324 15.640  1.00 91.81  ? 151 MET C CE  1 
ATOM   5087  N N   . VAL C 1 149 ? 53.201  -39.314 16.841  1.00 84.04  ? 152 VAL C N   1 
ATOM   5088  C CA  . VAL C 1 149 ? 53.971  -40.551 16.883  1.00 85.53  ? 152 VAL C CA  1 
ATOM   5089  C C   . VAL C 1 149 ? 53.413  -41.601 15.935  1.00 85.97  ? 152 VAL C C   1 
ATOM   5090  O O   . VAL C 1 149 ? 52.451  -42.287 16.266  1.00 88.33  ? 152 VAL C O   1 
ATOM   5091  C CB  . VAL C 1 149 ? 53.954  -41.158 18.296  1.00 87.37  ? 152 VAL C CB  1 
ATOM   5092  C CG1 . VAL C 1 149 ? 55.074  -42.165 18.445  1.00 87.07  ? 152 VAL C CG1 1 
ATOM   5093  C CG2 . VAL C 1 149 ? 54.072  -40.071 19.352  1.00 92.86  ? 152 VAL C CG2 1 
ATOM   5094  N N   . TRP C 1 150 ? 54.036  -41.744 14.769  1.00 36.45  ? 153 TRP C N   1 
ATOM   5095  C CA  . TRP C 1 150 ? 53.560  -42.663 13.732  1.00 41.17  ? 153 TRP C CA  1 
ATOM   5096  C C   . TRP C 1 150 ? 53.813  -44.135 14.061  1.00 46.28  ? 153 TRP C C   1 
ATOM   5097  O O   . TRP C 1 150 ? 54.460  -44.838 13.283  1.00 57.86  ? 153 TRP C O   1 
ATOM   5098  C CB  . TRP C 1 150 ? 54.206  -42.316 12.387  1.00 53.15  ? 153 TRP C CB  1 
ATOM   5099  C CG  . TRP C 1 150 ? 53.578  -43.002 11.211  1.00 58.61  ? 153 TRP C CG  1 
ATOM   5100  C CD1 . TRP C 1 150 ? 52.629  -43.979 11.242  1.00 53.86  ? 153 TRP C CD1 1 
ATOM   5101  C CD2 . TRP C 1 150 ? 53.847  -42.751 9.826   1.00 77.03  ? 153 TRP C CD2 1 
ATOM   5102  N NE1 . TRP C 1 150 ? 52.291  -44.357 9.962   1.00 71.73  ? 153 TRP C NE1 1 
ATOM   5103  C CE2 . TRP C 1 150 ? 53.025  -43.614 9.075   1.00 84.52  ? 153 TRP C CE2 1 
ATOM   5104  C CE3 . TRP C 1 150 ? 54.703  -41.881 9.149   1.00 93.05  ? 153 TRP C CE3 1 
ATOM   5105  C CZ2 . TRP C 1 150 ? 53.037  -43.633 7.684   1.00 105.71 ? 153 TRP C CZ2 1 
ATOM   5106  C CZ3 . TRP C 1 150 ? 54.712  -41.902 7.767   1.00 112.37 ? 153 TRP C CZ3 1 
ATOM   5107  C CH2 . TRP C 1 150 ? 53.884  -42.771 7.050   1.00 119.07 ? 153 TRP C CH2 1 
ATOM   5108  N N   . LEU C 1 151 ? 53.291  -44.601 15.198  1.00 66.04  ? 154 LEU C N   1 
ATOM   5109  C CA  . LEU C 1 151 ? 53.381  -46.016 15.600  1.00 61.10  ? 154 LEU C CA  1 
ATOM   5110  C C   . LEU C 1 151 ? 53.326  -46.990 14.423  1.00 72.81  ? 154 LEU C C   1 
ATOM   5111  O O   . LEU C 1 151 ? 52.333  -47.042 13.695  1.00 80.03  ? 154 LEU C O   1 
ATOM   5112  C CB  . LEU C 1 151 ? 52.272  -46.362 16.603  1.00 52.95  ? 154 LEU C CB  1 
ATOM   5113  C CG  . LEU C 1 151 ? 52.560  -46.178 18.104  1.00 57.67  ? 154 LEU C CG  1 
ATOM   5114  C CD1 . LEU C 1 151 ? 53.465  -44.982 18.347  1.00 67.69  ? 154 LEU C CD1 1 
ATOM   5115  C CD2 . LEU C 1 151 ? 51.277  -46.063 18.946  1.00 57.57  ? 154 LEU C CD2 1 
ATOM   5116  N N   . THR C 1 152 ? 54.399  -47.759 14.241  1.00 75.36  ? 155 THR C N   1 
ATOM   5117  C CA  . THR C 1 152 ? 54.451  -48.788 13.194  1.00 90.37  ? 155 THR C CA  1 
ATOM   5118  C C   . THR C 1 152 ? 54.829  -50.179 13.713  1.00 96.99  ? 155 THR C C   1 
ATOM   5119  O O   . THR C 1 152 ? 55.136  -50.358 14.895  1.00 95.31  ? 155 THR C O   1 
ATOM   5120  C CB  . THR C 1 152 ? 55.417  -48.411 12.054  1.00 102.56 ? 155 THR C CB  1 
ATOM   5121  O OG1 . THR C 1 152 ? 56.443  -47.548 12.561  1.00 102.09 ? 155 THR C OG1 1 
ATOM   5122  C CG2 . THR C 1 152 ? 54.672  -47.703 10.940  1.00 108.95 ? 155 THR C CG2 1 
ATOM   5123  N N   . GLU C 1 153 ? 54.808  -51.152 12.805  1.00 116.09 ? 156 GLU C N   1 
ATOM   5124  C CA  . GLU C 1 153 ? 55.054  -52.557 13.132  1.00 115.46 ? 156 GLU C CA  1 
ATOM   5125  C C   . GLU C 1 153 ? 56.448  -52.821 13.706  1.00 120.05 ? 156 GLU C C   1 
ATOM   5126  O O   . GLU C 1 153 ? 57.414  -52.151 13.341  1.00 128.94 ? 156 GLU C O   1 
ATOM   5127  C CB  . GLU C 1 153 ? 54.812  -53.430 11.894  1.00 127.08 ? 156 GLU C CB  1 
ATOM   5128  C CG  . GLU C 1 153 ? 55.609  -54.722 11.859  1.00 135.81 ? 156 GLU C CG  1 
ATOM   5129  C CD  . GLU C 1 153 ? 56.946  -54.561 11.158  1.00 146.07 ? 156 GLU C CD  1 
ATOM   5130  O OE1 . GLU C 1 153 ? 56.978  -53.920 10.086  1.00 163.43 ? 156 GLU C OE1 1 
ATOM   5131  O OE2 . GLU C 1 153 ? 57.962  -55.070 11.679  1.00 136.91 ? 156 GLU C OE2 1 
ATOM   5132  N N   . LYS C 1 154 ? 56.539  -53.794 14.612  1.00 104.99 ? 157 LYS C N   1 
ATOM   5133  C CA  . LYS C 1 154 ? 57.824  -54.225 15.166  1.00 103.66 ? 157 LYS C CA  1 
ATOM   5134  C C   . LYS C 1 154 ? 57.959  -55.750 15.244  1.00 102.45 ? 157 LYS C C   1 
ATOM   5135  O O   . LYS C 1 154 ? 57.388  -56.393 16.126  1.00 95.09  ? 157 LYS C O   1 
ATOM   5136  C CB  . LYS C 1 154 ? 58.070  -53.609 16.548  1.00 101.81 ? 157 LYS C CB  1 
ATOM   5137  C CG  . LYS C 1 154 ? 59.291  -54.198 17.252  1.00 107.41 ? 157 LYS C CG  1 
ATOM   5138  C CD  . LYS C 1 154 ? 60.040  -53.174 18.099  1.00 108.97 ? 157 LYS C CD  1 
ATOM   5139  C CE  . LYS C 1 154 ? 59.362  -52.935 19.441  1.00 110.00 ? 157 LYS C CE  1 
ATOM   5140  N NZ  . LYS C 1 154 ? 60.204  -52.096 20.344  1.00 114.65 ? 157 LYS C NZ  1 
ATOM   5141  N N   . GLY C 1 155 ? 58.730  -56.322 14.324  1.00 96.88  ? 158 GLY C N   1 
ATOM   5142  C CA  . GLY C 1 155 ? 58.961  -57.755 14.308  1.00 100.94 ? 158 GLY C CA  1 
ATOM   5143  C C   . GLY C 1 155 ? 57.832  -58.500 13.628  1.00 103.58 ? 158 GLY C C   1 
ATOM   5144  O O   . GLY C 1 155 ? 57.388  -59.545 14.104  1.00 97.47  ? 158 GLY C O   1 
ATOM   5145  N N   . SER C 1 156 ? 57.370  -57.953 12.509  1.00 126.13 ? 159 SER C N   1 
ATOM   5146  C CA  . SER C 1 156 ? 56.241  -58.515 11.775  1.00 133.56 ? 159 SER C CA  1 
ATOM   5147  C C   . SER C 1 156 ? 55.041  -58.721 12.693  1.00 124.30 ? 159 SER C C   1 
ATOM   5148  O O   . SER C 1 156 ? 54.216  -59.606 12.466  1.00 124.60 ? 159 SER C O   1 
ATOM   5149  C CB  . SER C 1 156 ? 56.638  -59.828 11.098  1.00 143.35 ? 159 SER C CB  1 
ATOM   5150  O OG  . SER C 1 156 ? 57.638  -59.608 10.118  1.00 157.24 ? 159 SER C OG  1 
ATOM   5151  N N   . ASN C 1 157 ? 54.947  -57.887 13.724  1.00 137.09 ? 160 ASN C N   1 
ATOM   5152  C CA  . ASN C 1 157 ? 53.896  -58.012 14.725  1.00 127.83 ? 160 ASN C CA  1 
ATOM   5153  C C   . ASN C 1 157 ? 53.365  -56.652 15.187  1.00 118.35 ? 160 ASN C C   1 
ATOM   5154  O O   . ASN C 1 157 ? 54.124  -55.813 15.674  1.00 118.86 ? 160 ASN C O   1 
ATOM   5155  C CB  . ASN C 1 157 ? 54.414  -58.811 15.925  1.00 126.39 ? 160 ASN C CB  1 
ATOM   5156  C CG  . ASN C 1 157 ? 53.303  -59.274 16.845  1.00 122.68 ? 160 ASN C CG  1 
ATOM   5157  O OD1 . ASN C 1 157 ? 52.255  -59.732 16.391  1.00 126.49 ? 160 ASN C OD1 1 
ATOM   5158  N ND2 . ASN C 1 157 ? 53.526  -59.152 18.148  1.00 120.23 ? 160 ASN C ND2 1 
ATOM   5159  N N   . TYR C 1 158 ? 52.061  -56.438 15.026  1.00 117.11 ? 161 TYR C N   1 
ATOM   5160  C CA  . TYR C 1 158 ? 51.421  -55.220 15.513  1.00 103.52 ? 161 TYR C CA  1 
ATOM   5161  C C   . TYR C 1 158 ? 50.430  -55.568 16.612  1.00 100.93 ? 161 TYR C C   1 
ATOM   5162  O O   . TYR C 1 158 ? 49.283  -55.902 16.329  1.00 100.52 ? 161 TYR C O   1 
ATOM   5163  C CB  . TYR C 1 158 ? 50.695  -54.488 14.379  1.00 96.76  ? 161 TYR C CB  1 
ATOM   5164  C CG  . TYR C 1 158 ? 50.330  -53.045 14.691  1.00 85.16  ? 161 TYR C CG  1 
ATOM   5165  C CD1 . TYR C 1 158 ? 50.749  -52.012 13.866  1.00 84.58  ? 161 TYR C CD1 1 
ATOM   5166  C CD2 . TYR C 1 158 ? 49.571  -52.720 15.810  1.00 83.07  ? 161 TYR C CD2 1 
ATOM   5167  C CE1 . TYR C 1 158 ? 50.419  -50.697 14.142  1.00 85.00  ? 161 TYR C CE1 1 
ATOM   5168  C CE2 . TYR C 1 158 ? 49.238  -51.406 16.097  1.00 80.04  ? 161 TYR C CE2 1 
ATOM   5169  C CZ  . TYR C 1 158 ? 49.664  -50.396 15.260  1.00 81.62  ? 161 TYR C CZ  1 
ATOM   5170  O OH  . TYR C 1 158 ? 49.336  -49.084 15.533  1.00 77.72  ? 161 TYR C OH  1 
ATOM   5171  N N   . PRO C 1 159 ? 50.878  -55.498 17.874  1.00 74.18  ? 162 PRO C N   1 
ATOM   5172  C CA  . PRO C 1 159 ? 50.050  -55.758 19.060  1.00 77.13  ? 162 PRO C CA  1 
ATOM   5173  C C   . PRO C 1 159 ? 48.826  -54.845 19.164  1.00 76.24  ? 162 PRO C C   1 
ATOM   5174  O O   . PRO C 1 159 ? 48.450  -54.182 18.198  1.00 72.96  ? 162 PRO C O   1 
ATOM   5175  C CB  . PRO C 1 159 ? 51.007  -55.470 20.223  1.00 82.40  ? 162 PRO C CB  1 
ATOM   5176  C CG  . PRO C 1 159 ? 52.363  -55.713 19.661  1.00 83.11  ? 162 PRO C CG  1 
ATOM   5177  C CD  . PRO C 1 159 ? 52.290  -55.266 18.226  1.00 77.02  ? 162 PRO C CD  1 
ATOM   5178  N N   . VAL C 1 160 ? 48.207  -54.821 20.338  1.00 100.20 ? 163 VAL C N   1 
ATOM   5179  C CA  . VAL C 1 160 ? 47.068  -53.946 20.567  1.00 98.96  ? 163 VAL C CA  1 
ATOM   5180  C C   . VAL C 1 160 ? 47.534  -52.667 21.251  1.00 104.41 ? 163 VAL C C   1 
ATOM   5181  O O   . VAL C 1 160 ? 47.891  -52.673 22.428  1.00 122.92 ? 163 VAL C O   1 
ATOM   5182  C CB  . VAL C 1 160 ? 45.981  -54.637 21.410  1.00 104.28 ? 163 VAL C CB  1 
ATOM   5183  C CG1 . VAL C 1 160 ? 46.588  -55.257 22.664  1.00 125.52 ? 163 VAL C CG1 1 
ATOM   5184  C CG2 . VAL C 1 160 ? 44.870  -53.655 21.760  1.00 100.13 ? 163 VAL C CG2 1 
ATOM   5185  N N   . ALA C 1 161 ? 47.540  -51.573 20.497  1.00 78.23  ? 164 ALA C N   1 
ATOM   5186  C CA  . ALA C 1 161 ? 48.021  -50.295 21.005  1.00 75.09  ? 164 ALA C CA  1 
ATOM   5187  C C   . ALA C 1 161 ? 47.097  -49.724 22.073  1.00 85.32  ? 164 ALA C C   1 
ATOM   5188  O O   . ALA C 1 161 ? 46.073  -49.127 21.757  1.00 81.45  ? 164 ALA C O   1 
ATOM   5189  C CB  . ALA C 1 161 ? 48.176  -49.308 19.861  1.00 60.29  ? 164 ALA C CB  1 
ATOM   5190  N N   . LYS C 1 162 ? 47.457  -49.907 23.337  1.00 70.73  ? 165 LYS C N   1 
ATOM   5191  C CA  . LYS C 1 162 ? 46.666  -49.341 24.423  1.00 80.02  ? 165 LYS C CA  1 
ATOM   5192  C C   . LYS C 1 162 ? 47.425  -48.229 25.135  1.00 83.69  ? 165 LYS C C   1 
ATOM   5193  O O   . LYS C 1 162 ? 48.544  -48.429 25.608  1.00 94.91  ? 165 LYS C O   1 
ATOM   5194  C CB  . LYS C 1 162 ? 46.234  -50.419 25.419  1.00 97.56  ? 165 LYS C CB  1 
ATOM   5195  C CG  . LYS C 1 162 ? 45.191  -51.385 24.880  1.00 84.29  ? 165 LYS C CG  1 
ATOM   5196  C CD  . LYS C 1 162 ? 44.822  -52.433 25.926  1.00 102.71 ? 165 LYS C CD  1 
ATOM   5197  C CE  . LYS C 1 162 ? 44.155  -53.651 25.291  1.00 104.09 ? 165 LYS C CE  1 
ATOM   5198  N NZ  . LYS C 1 162 ? 43.855  -54.709 26.293  1.00 101.45 ? 165 LYS C NZ  1 
ATOM   5199  N N   . GLY C 1 163 ? 46.800  -47.057 25.200  1.00 72.85  ? 166 GLY C N   1 
ATOM   5200  C CA  . GLY C 1 163 ? 47.396  -45.887 25.819  1.00 76.07  ? 166 GLY C CA  1 
ATOM   5201  C C   . GLY C 1 163 ? 46.354  -44.979 26.441  1.00 90.55  ? 166 GLY C C   1 
ATOM   5202  O O   . GLY C 1 163 ? 45.298  -44.735 25.864  1.00 86.57  ? 166 GLY C O   1 
ATOM   5203  N N   . SER C 1 164 ? 46.661  -44.470 27.627  1.00 61.32  ? 167 SER C N   1 
ATOM   5204  C CA  . SER C 1 164 ? 45.716  -43.664 28.381  1.00 66.88  ? 167 SER C CA  1 
ATOM   5205  C C   . SER C 1 164 ? 46.338  -42.345 28.830  1.00 73.38  ? 167 SER C C   1 
ATOM   5206  O O   . SER C 1 164 ? 47.539  -42.131 28.677  1.00 87.61  ? 167 SER C O   1 
ATOM   5207  C CB  . SER C 1 164 ? 45.224  -44.444 29.602  1.00 75.27  ? 167 SER C CB  1 
ATOM   5208  O OG  . SER C 1 164 ? 44.617  -43.585 30.552  1.00 77.29  ? 167 SER C OG  1 
ATOM   5209  N N   . TYR C 1 165 ? 45.511  -41.459 29.376  1.00 83.18  ? 168 TYR C N   1 
ATOM   5210  C CA  . TYR C 1 165 ? 46.009  -40.269 30.052  1.00 82.52  ? 168 TYR C CA  1 
ATOM   5211  C C   . TYR C 1 165 ? 44.954  -39.652 30.961  1.00 84.75  ? 168 TYR C C   1 
ATOM   5212  O O   . TYR C 1 165 ? 43.837  -39.376 30.531  1.00 86.85  ? 168 TYR C O   1 
ATOM   5213  C CB  . TYR C 1 165 ? 46.503  -39.223 29.056  1.00 73.70  ? 168 TYR C CB  1 
ATOM   5214  C CG  . TYR C 1 165 ? 46.784  -37.891 29.716  1.00 80.84  ? 168 TYR C CG  1 
ATOM   5215  C CD1 . TYR C 1 165 ? 47.993  -37.650 30.350  1.00 96.65  ? 168 TYR C CD1 1 
ATOM   5216  C CD2 . TYR C 1 165 ? 45.832  -36.883 29.725  1.00 81.29  ? 168 TYR C CD2 1 
ATOM   5217  C CE1 . TYR C 1 165 ? 48.248  -36.442 30.965  1.00 101.51 ? 168 TYR C CE1 1 
ATOM   5218  C CE2 . TYR C 1 165 ? 46.079  -35.674 30.334  1.00 92.87  ? 168 TYR C CE2 1 
ATOM   5219  C CZ  . TYR C 1 165 ? 47.288  -35.456 30.955  1.00 102.90 ? 168 TYR C CZ  1 
ATOM   5220  O OH  . TYR C 1 165 ? 47.535  -34.247 31.566  1.00 111.50 ? 168 TYR C OH  1 
ATOM   5221  N N   . ASN C 1 166 ? 45.310  -39.446 32.223  1.00 76.76  ? 169 ASN C N   1 
ATOM   5222  C CA  . ASN C 1 166 ? 44.442  -38.729 33.139  1.00 76.77  ? 169 ASN C CA  1 
ATOM   5223  C C   . ASN C 1 166 ? 44.770  -37.235 33.030  1.00 82.15  ? 169 ASN C C   1 
ATOM   5224  O O   . ASN C 1 166 ? 45.932  -36.832 33.154  1.00 89.16  ? 169 ASN C O   1 
ATOM   5225  C CB  . ASN C 1 166 ? 44.631  -39.242 34.573  1.00 89.09  ? 169 ASN C CB  1 
ATOM   5226  C CG  . ASN C 1 166 ? 43.398  -39.040 35.439  1.00 90.12  ? 169 ASN C CG  1 
ATOM   5227  O OD1 . ASN C 1 166 ? 43.205  -39.730 36.445  1.00 88.36  ? 169 ASN C OD1 1 
ATOM   5228  N ND2 . ASN C 1 166 ? 42.551  -38.100 35.045  1.00 90.53  ? 169 ASN C ND2 1 
ATOM   5229  N N   . ASN C 1 167 ? 43.756  -36.417 32.761  1.00 102.06 ? 170 ASN C N   1 
ATOM   5230  C CA  . ASN C 1 167 ? 43.983  -34.985 32.585  1.00 106.83 ? 170 ASN C CA  1 
ATOM   5231  C C   . ASN C 1 167 ? 44.025  -34.232 33.901  1.00 109.19 ? 170 ASN C C   1 
ATOM   5232  O O   . ASN C 1 167 ? 43.010  -33.730 34.381  1.00 104.58 ? 170 ASN C O   1 
ATOM   5233  C CB  . ASN C 1 167 ? 42.942  -34.353 31.662  1.00 104.70 ? 170 ASN C CB  1 
ATOM   5234  C CG  . ASN C 1 167 ? 43.185  -32.870 31.449  1.00 106.74 ? 170 ASN C CG  1 
ATOM   5235  O OD1 . ASN C 1 167 ? 44.328  -32.429 31.325  1.00 115.62 ? 170 ASN C OD1 1 
ATOM   5236  N ND2 . ASN C 1 167 ? 42.112  -32.092 31.420  1.00 98.94  ? 170 ASN C ND2 1 
ATOM   5237  N N   . THR C 1 168 ? 45.217  -34.144 34.472  1.00 99.81  ? 171 THR C N   1 
ATOM   5238  C CA  . THR C 1 168 ? 45.393  -33.514 35.767  1.00 103.32 ? 171 THR C CA  1 
ATOM   5239  C C   . THR C 1 168 ? 46.173  -32.216 35.635  1.00 108.18 ? 171 THR C C   1 
ATOM   5240  O O   . THR C 1 168 ? 46.613  -31.647 36.631  1.00 112.96 ? 171 THR C O   1 
ATOM   5241  C CB  . THR C 1 168 ? 46.138  -34.455 36.714  1.00 110.93 ? 171 THR C CB  1 
ATOM   5242  O OG1 . THR C 1 168 ? 47.430  -34.748 36.168  1.00 121.06 ? 171 THR C OG1 1 
ATOM   5243  C CG2 . THR C 1 168 ? 45.365  -35.752 36.867  1.00 106.49 ? 171 THR C CG2 1 
ATOM   5244  N N   . SER C 1 169 ? 46.331  -31.754 34.399  1.00 126.59 ? 172 SER C N   1 
ATOM   5245  C CA  . SER C 1 169 ? 47.162  -30.591 34.101  1.00 135.26 ? 172 SER C CA  1 
ATOM   5246  C C   . SER C 1 169 ? 46.539  -29.274 34.562  1.00 132.59 ? 172 SER C C   1 
ATOM   5247  O O   . SER C 1 169 ? 47.034  -28.195 34.233  1.00 144.71 ? 172 SER C O   1 
ATOM   5248  C CB  . SER C 1 169 ? 47.477  -30.534 32.607  1.00 140.42 ? 172 SER C CB  1 
ATOM   5249  O OG  . SER C 1 169 ? 46.293  -30.369 31.847  1.00 137.31 ? 172 SER C OG  1 
ATOM   5250  N N   . GLY C 1 170 ? 45.448  -29.369 35.315  1.00 101.76 ? 173 GLY C N   1 
ATOM   5251  C CA  . GLY C 1 170 ? 44.857  -28.210 35.961  1.00 98.27  ? 173 GLY C CA  1 
ATOM   5252  C C   . GLY C 1 170 ? 43.838  -27.460 35.128  1.00 94.22  ? 173 GLY C C   1 
ATOM   5253  O O   . GLY C 1 170 ? 43.325  -26.429 35.560  1.00 92.65  ? 173 GLY C O   1 
ATOM   5254  N N   . GLU C 1 171 ? 43.542  -27.974 33.939  1.00 105.21 ? 174 GLU C N   1 
ATOM   5255  C CA  . GLU C 1 171 ? 42.596  -27.324 33.037  1.00 99.57  ? 174 GLU C CA  1 
ATOM   5256  C C   . GLU C 1 171 ? 42.441  -28.107 31.739  1.00 93.90  ? 174 GLU C C   1 
ATOM   5257  O O   . GLU C 1 171 ? 43.289  -28.932 31.403  1.00 95.55  ? 174 GLU C O   1 
ATOM   5258  C CB  . GLU C 1 171 ? 43.045  -25.896 32.736  1.00 102.45 ? 174 GLU C CB  1 
ATOM   5259  C CG  . GLU C 1 171 ? 44.446  -25.813 32.171  1.00 106.16 ? 174 GLU C CG  1 
ATOM   5260  C CD  . GLU C 1 171 ? 44.978  -24.397 32.140  1.00 112.76 ? 174 GLU C CD  1 
ATOM   5261  O OE1 . GLU C 1 171 ? 44.318  -23.496 32.708  1.00 106.52 ? 174 GLU C OE1 1 
ATOM   5262  O OE2 . GLU C 1 171 ? 46.060  -24.189 31.549  1.00 120.58 ? 174 GLU C OE2 1 
ATOM   5263  N N   . GLN C 1 172 ? 41.357  -27.841 31.015  1.00 97.73  ? 175 GLN C N   1 
ATOM   5264  C CA  . GLN C 1 172 ? 41.070  -28.536 29.764  1.00 91.17  ? 175 GLN C CA  1 
ATOM   5265  C C   . GLN C 1 172 ? 42.306  -28.640 28.882  1.00 96.62  ? 175 GLN C C   1 
ATOM   5266  O O   . GLN C 1 172 ? 43.223  -27.826 28.984  1.00 101.01 ? 175 GLN C O   1 
ATOM   5267  C CB  . GLN C 1 172 ? 39.950  -27.836 28.999  1.00 90.48  ? 175 GLN C CB  1 
ATOM   5268  C CG  . GLN C 1 172 ? 38.627  -27.789 29.732  1.00 97.22  ? 175 GLN C CG  1 
ATOM   5269  C CD  . GLN C 1 172 ? 37.535  -27.160 28.896  1.00 97.60  ? 175 GLN C CD  1 
ATOM   5270  O OE1 . GLN C 1 172 ? 37.479  -27.357 27.682  1.00 99.16  ? 175 GLN C OE1 1 
ATOM   5271  N NE2 . GLN C 1 172 ? 36.663  -26.389 29.541  1.00 92.56  ? 175 GLN C NE2 1 
ATOM   5272  N N   . MET C 1 173 ? 42.321  -29.642 28.008  1.00 76.31  ? 176 MET C N   1 
ATOM   5273  C CA  . MET C 1 173 ? 43.491  -29.923 27.187  1.00 74.92  ? 176 MET C CA  1 
ATOM   5274  C C   . MET C 1 173 ? 43.110  -30.355 25.780  1.00 60.23  ? 176 MET C C   1 
ATOM   5275  O O   . MET C 1 173 ? 42.416  -31.349 25.593  1.00 52.03  ? 176 MET C O   1 
ATOM   5276  C CB  . MET C 1 173 ? 44.339  -31.019 27.836  1.00 85.97  ? 176 MET C CB  1 
ATOM   5277  C CG  . MET C 1 173 ? 45.527  -31.455 26.993  1.00 90.26  ? 176 MET C CG  1 
ATOM   5278  S SD  . MET C 1 173 ? 46.462  -32.805 27.728  1.00 97.92  ? 176 MET C SD  1 
ATOM   5279  C CE  . MET C 1 173 ? 46.659  -32.199 29.400  1.00 98.28  ? 176 MET C CE  1 
ATOM   5280  N N   . LEU C 1 174 ? 43.571  -29.611 24.787  1.00 107.61 ? 177 LEU C N   1 
ATOM   5281  C CA  . LEU C 1 174 ? 43.352  -30.002 23.411  1.00 85.18  ? 177 LEU C CA  1 
ATOM   5282  C C   . LEU C 1 174 ? 44.218  -31.217 23.113  1.00 87.78  ? 177 LEU C C   1 
ATOM   5283  O O   . LEU C 1 174 ? 45.411  -31.218 23.409  1.00 105.95 ? 177 LEU C O   1 
ATOM   5284  C CB  . LEU C 1 174 ? 43.710  -28.851 22.477  1.00 71.34  ? 177 LEU C CB  1 
ATOM   5285  C CG  . LEU C 1 174 ? 43.370  -29.057 21.004  1.00 64.49  ? 177 LEU C CG  1 
ATOM   5286  C CD1 . LEU C 1 174 ? 41.918  -29.471 20.876  1.00 65.47  ? 177 LEU C CD1 1 
ATOM   5287  C CD2 . LEU C 1 174 ? 43.654  -27.794 20.191  1.00 59.39  ? 177 LEU C CD2 1 
ATOM   5288  N N   . ILE C 1 175 ? 43.615  -32.258 22.548  1.00 67.04  ? 178 ILE C N   1 
ATOM   5289  C CA  . ILE C 1 175 ? 44.347  -33.468 22.176  1.00 56.83  ? 178 ILE C CA  1 
ATOM   5290  C C   . ILE C 1 175 ? 44.004  -33.856 20.742  1.00 52.54  ? 178 ILE C C   1 
ATOM   5291  O O   . ILE C 1 175 ? 42.871  -33.672 20.301  1.00 52.14  ? 178 ILE C O   1 
ATOM   5292  C CB  . ILE C 1 175 ? 44.010  -34.632 23.109  1.00 55.98  ? 178 ILE C CB  1 
ATOM   5293  C CG1 . ILE C 1 175 ? 44.366  -34.272 24.553  1.00 79.91  ? 178 ILE C CG1 1 
ATOM   5294  C CG2 . ILE C 1 175 ? 44.731  -35.896 22.661  1.00 50.08  ? 178 ILE C CG2 1 
ATOM   5295  C CD1 . ILE C 1 175 ? 43.867  -35.262 25.579  1.00 102.29 ? 178 ILE C CD1 1 
ATOM   5296  N N   . ILE C 1 176 ? 44.974  -34.390 20.009  1.00 61.27  ? 179 ILE C N   1 
ATOM   5297  C CA  . ILE C 1 176 ? 44.783  -34.652 18.585  1.00 49.25  ? 179 ILE C CA  1 
ATOM   5298  C C   . ILE C 1 176 ? 45.279  -36.034 18.191  1.00 53.18  ? 179 ILE C C   1 
ATOM   5299  O O   . ILE C 1 176 ? 46.222  -36.547 18.787  1.00 71.47  ? 179 ILE C O   1 
ATOM   5300  C CB  . ILE C 1 176 ? 45.536  -33.612 17.728  1.00 44.05  ? 179 ILE C CB  1 
ATOM   5301  C CG1 . ILE C 1 176 ? 44.920  -32.235 17.901  1.00 35.86  ? 179 ILE C CG1 1 
ATOM   5302  C CG2 . ILE C 1 176 ? 45.531  -34.002 16.255  1.00 51.05  ? 179 ILE C CG2 1 
ATOM   5303  C CD1 . ILE C 1 176 ? 45.377  -31.231 16.853  1.00 42.94  ? 179 ILE C CD1 1 
ATOM   5304  N N   . TRP C 1 177 ? 44.654  -36.634 17.184  1.00 58.15  ? 180 TRP C N   1 
ATOM   5305  C CA  . TRP C 1 177 ? 45.131  -37.903 16.648  1.00 62.07  ? 180 TRP C CA  1 
ATOM   5306  C C   . TRP C 1 177 ? 44.734  -38.008 15.191  1.00 71.59  ? 180 TRP C C   1 
ATOM   5307  O O   . TRP C 1 177 ? 44.103  -37.099 14.650  1.00 84.35  ? 180 TRP C O   1 
ATOM   5308  C CB  . TRP C 1 177 ? 44.561  -39.090 17.425  1.00 55.95  ? 180 TRP C CB  1 
ATOM   5309  C CG  . TRP C 1 177 ? 43.078  -39.221 17.295  1.00 59.60  ? 180 TRP C CG  1 
ATOM   5310  C CD1 . TRP C 1 177 ? 42.395  -39.983 16.393  1.00 60.57  ? 180 TRP C CD1 1 
ATOM   5311  C CD2 . TRP C 1 177 ? 42.090  -38.559 18.092  1.00 59.02  ? 180 TRP C CD2 1 
ATOM   5312  N NE1 . TRP C 1 177 ? 41.041  -39.839 16.584  1.00 59.26  ? 180 TRP C NE1 1 
ATOM   5313  C CE2 . TRP C 1 177 ? 40.831  -38.967 17.620  1.00 52.27  ? 180 TRP C CE2 1 
ATOM   5314  C CE3 . TRP C 1 177 ? 42.150  -37.659 19.157  1.00 66.09  ? 180 TRP C CE3 1 
ATOM   5315  C CZ2 . TRP C 1 177 ? 39.644  -38.507 18.180  1.00 48.51  ? 180 TRP C CZ2 1 
ATOM   5316  C CZ3 . TRP C 1 177 ? 40.970  -37.203 19.709  1.00 60.38  ? 180 TRP C CZ3 1 
ATOM   5317  C CH2 . TRP C 1 177 ? 39.735  -37.627 19.223  1.00 52.54  ? 180 TRP C CH2 1 
ATOM   5318  N N   . GLY C 1 178 ? 45.103  -39.118 14.559  1.00 36.50  ? 181 GLY C N   1 
ATOM   5319  C CA  . GLY C 1 178 ? 44.794  -39.329 13.157  1.00 47.80  ? 181 GLY C CA  1 
ATOM   5320  C C   . GLY C 1 178 ? 44.840  -40.786 12.737  1.00 57.70  ? 181 GLY C C   1 
ATOM   5321  O O   . GLY C 1 178 ? 45.132  -41.682 13.537  1.00 54.34  ? 181 GLY C O   1 
ATOM   5322  N N   . VAL C 1 179 ? 44.541  -41.028 11.469  1.00 52.84  ? 182 VAL C N   1 
ATOM   5323  C CA  . VAL C 1 179 ? 44.640  -42.371 10.938  1.00 62.13  ? 182 VAL C CA  1 
ATOM   5324  C C   . VAL C 1 179 ? 45.251  -42.330 9.555   1.00 78.97  ? 182 VAL C C   1 
ATOM   5325  O O   . VAL C 1 179 ? 44.881  -41.501 8.722   1.00 96.12  ? 182 VAL C O   1 
ATOM   5326  C CB  . VAL C 1 179 ? 43.271  -43.081 10.894  1.00 62.92  ? 182 VAL C CB  1 
ATOM   5327  C CG1 . VAL C 1 179 ? 42.655  -43.129 12.288  1.00 45.67  ? 182 VAL C CG1 1 
ATOM   5328  C CG2 . VAL C 1 179 ? 42.339  -42.386 9.927   1.00 76.72  ? 182 VAL C CG2 1 
ATOM   5329  N N   . HIS C 1 180 ? 46.202  -43.226 9.321   1.00 35.97  ? 183 HIS C N   1 
ATOM   5330  C CA  . HIS C 1 180 ? 46.899  -43.268 8.047   1.00 61.95  ? 183 HIS C CA  1 
ATOM   5331  C C   . HIS C 1 180 ? 46.036  -44.003 7.043   1.00 73.50  ? 183 HIS C C   1 
ATOM   5332  O O   . HIS C 1 180 ? 45.500  -45.065 7.343   1.00 58.63  ? 183 HIS C O   1 
ATOM   5333  C CB  . HIS C 1 180 ? 48.257  -43.957 8.212   1.00 67.23  ? 183 HIS C CB  1 
ATOM   5334  C CG  . HIS C 1 180 ? 49.010  -44.140 6.933   1.00 96.64  ? 183 HIS C CG  1 
ATOM   5335  N ND1 . HIS C 1 180 ? 50.386  -44.178 6.883   1.00 102.94 ? 183 HIS C ND1 1 
ATOM   5336  C CD2 . HIS C 1 180 ? 48.582  -44.309 5.660   1.00 116.43 ? 183 HIS C CD2 1 
ATOM   5337  C CE1 . HIS C 1 180 ? 50.773  -44.353 5.632   1.00 131.70 ? 183 HIS C CE1 1 
ATOM   5338  N NE2 . HIS C 1 180 ? 49.698  -44.436 4.871   1.00 132.80 ? 183 HIS C NE2 1 
ATOM   5339  N N   . HIS C 1 181 ? 45.883  -43.424 5.860   1.00 76.01  ? 184 HIS C N   1 
ATOM   5340  C CA  . HIS C 1 181 ? 45.154  -44.083 4.792   1.00 79.19  ? 184 HIS C CA  1 
ATOM   5341  C C   . HIS C 1 181 ? 46.094  -44.461 3.666   1.00 97.07  ? 184 HIS C C   1 
ATOM   5342  O O   . HIS C 1 181 ? 46.336  -43.662 2.763   1.00 105.46 ? 184 HIS C O   1 
ATOM   5343  C CB  . HIS C 1 181 ? 44.044  -43.190 4.264   1.00 73.45  ? 184 HIS C CB  1 
ATOM   5344  C CG  . HIS C 1 181 ? 43.002  -42.863 5.285   1.00 66.55  ? 184 HIS C CG  1 
ATOM   5345  N ND1 . HIS C 1 181 ? 41.656  -42.835 4.989   1.00 64.36  ? 184 HIS C ND1 1 
ATOM   5346  C CD2 . HIS C 1 181 ? 43.108  -42.539 6.596   1.00 66.31  ? 184 HIS C CD2 1 
ATOM   5347  C CE1 . HIS C 1 181 ? 40.978  -42.513 6.076   1.00 62.09  ? 184 HIS C CE1 1 
ATOM   5348  N NE2 . HIS C 1 181 ? 41.834  -42.330 7.065   1.00 60.27  ? 184 HIS C NE2 1 
ATOM   5349  N N   . PRO C 1 182 ? 46.620  -45.694 3.719   1.00 72.35  ? 185 PRO C N   1 
ATOM   5350  C CA  . PRO C 1 182 ? 47.626  -46.204 2.789   1.00 83.30  ? 185 PRO C CA  1 
ATOM   5351  C C   . PRO C 1 182 ? 47.066  -46.312 1.381   1.00 91.89  ? 185 PRO C C   1 
ATOM   5352  O O   . PRO C 1 182 ? 45.848  -46.232 1.200   1.00 86.18  ? 185 PRO C O   1 
ATOM   5353  C CB  . PRO C 1 182 ? 47.930  -47.597 3.345   1.00 82.76  ? 185 PRO C CB  1 
ATOM   5354  C CG  . PRO C 1 182 ? 47.458  -47.560 4.768   1.00 73.43  ? 185 PRO C CG  1 
ATOM   5355  C CD  . PRO C 1 182 ? 46.249  -46.707 4.718   1.00 67.16  ? 185 PRO C CD  1 
ATOM   5356  N N   . ASN C 1 183 ? 47.946  -46.506 0.403   1.00 89.65  ? 186 ASN C N   1 
ATOM   5357  C CA  . ASN C 1 183 ? 47.556  -46.438 -1.000  1.00 88.23  ? 186 ASN C CA  1 
ATOM   5358  C C   . ASN C 1 183 ? 46.987  -47.751 -1.529  1.00 81.09  ? 186 ASN C C   1 
ATOM   5359  O O   . ASN C 1 183 ? 46.075  -47.751 -2.361  1.00 69.66  ? 186 ASN C O   1 
ATOM   5360  C CB  . ASN C 1 183 ? 48.735  -45.979 -1.867  1.00 95.67  ? 186 ASN C CB  1 
ATOM   5361  C CG  . ASN C 1 183 ? 48.286  -45.280 -3.140  1.00 102.80 ? 186 ASN C CG  1 
ATOM   5362  O OD1 . ASN C 1 183 ? 47.420  -44.404 -3.107  1.00 92.72  ? 186 ASN C OD1 1 
ATOM   5363  N ND2 . ASN C 1 183 ? 48.867  -45.671 -4.270  1.00 122.57 ? 186 ASN C ND2 1 
ATOM   5364  N N   . ASP C 1 184 ? 47.526  -48.866 -1.047  1.00 77.62  ? 187 ASP C N   1 
ATOM   5365  C CA  . ASP C 1 184 ? 47.046  -50.184 -1.473  1.00 81.92  ? 187 ASP C CA  1 
ATOM   5366  C C   . ASP C 1 184 ? 46.995  -51.189 -0.331  1.00 86.14  ? 187 ASP C C   1 
ATOM   5367  O O   . ASP C 1 184 ? 47.479  -50.923 0.774   1.00 78.02  ? 187 ASP C O   1 
ATOM   5368  C CB  . ASP C 1 184 ? 47.889  -50.743 -2.629  1.00 90.12  ? 187 ASP C CB  1 
ATOM   5369  C CG  . ASP C 1 184 ? 49.371  -50.778 -2.310  1.00 94.68  ? 187 ASP C CG  1 
ATOM   5370  O OD1 . ASP C 1 184 ? 49.735  -50.968 -1.129  1.00 95.07  ? 187 ASP C OD1 1 
ATOM   5371  O OD2 . ASP C 1 184 ? 50.175  -50.608 -3.248  1.00 92.95  ? 187 ASP C OD2 1 
ATOM   5372  N N   . GLU C 1 185 ? 46.404  -52.345 -0.617  1.00 111.83 ? 188 GLU C N   1 
ATOM   5373  C CA  . GLU C 1 185 ? 46.276  -53.413 0.361   1.00 112.04 ? 188 GLU C CA  1 
ATOM   5374  C C   . GLU C 1 185 ? 47.646  -53.775 0.925   1.00 113.83 ? 188 GLU C C   1 
ATOM   5375  O O   . GLU C 1 185 ? 47.832  -53.851 2.142   1.00 112.35 ? 188 GLU C O   1 
ATOM   5376  C CB  . GLU C 1 185 ? 45.615  -54.635 -0.280  1.00 117.96 ? 188 GLU C CB  1 
ATOM   5377  C CG  . GLU C 1 185 ? 45.366  -55.783 0.679   1.00 122.03 ? 188 GLU C CG  1 
ATOM   5378  C CD  . GLU C 1 185 ? 44.645  -56.950 0.024   1.00 129.61 ? 188 GLU C CD  1 
ATOM   5379  O OE1 . GLU C 1 185 ? 44.876  -58.102 0.451   1.00 126.04 ? 188 GLU C OE1 1 
ATOM   5380  O OE2 . GLU C 1 185 ? 43.844  -56.716 -0.909  1.00 137.53 ? 188 GLU C OE2 1 
ATOM   5381  N N   . THR C 1 186 ? 48.607  -53.974 0.028   1.00 71.55  ? 189 THR C N   1 
ATOM   5382  C CA  . THR C 1 186 ? 49.968  -54.337 0.415   1.00 71.92  ? 189 THR C CA  1 
ATOM   5383  C C   . THR C 1 186 ? 50.605  -53.366 1.425   1.00 74.26  ? 189 THR C C   1 
ATOM   5384  O O   . THR C 1 186 ? 51.193  -53.798 2.420   1.00 77.83  ? 189 THR C O   1 
ATOM   5385  C CB  . THR C 1 186 ? 50.873  -54.512 -0.825  1.00 79.45  ? 189 THR C CB  1 
ATOM   5386  O OG1 . THR C 1 186 ? 52.093  -53.781 -0.646  1.00 90.75  ? 189 THR C OG1 1 
ATOM   5387  C CG2 . THR C 1 186 ? 50.157  -54.018 -2.073  1.00 71.65  ? 189 THR C CG2 1 
ATOM   5388  N N   . GLU C 1 187 ? 50.485  -52.064 1.180   1.00 86.14  ? 190 GLU C N   1 
ATOM   5389  C CA  . GLU C 1 187 ? 51.082  -51.078 2.077   1.00 83.47  ? 190 GLU C CA  1 
ATOM   5390  C C   . GLU C 1 187 ? 50.551  -51.206 3.499   1.00 75.73  ? 190 GLU C C   1 
ATOM   5391  O O   . GLU C 1 187 ? 51.314  -51.153 4.467   1.00 76.09  ? 190 GLU C O   1 
ATOM   5392  C CB  . GLU C 1 187 ? 50.863  -49.653 1.573   1.00 82.30  ? 190 GLU C CB  1 
ATOM   5393  C CG  . GLU C 1 187 ? 51.409  -48.606 2.535   1.00 81.93  ? 190 GLU C CG  1 
ATOM   5394  C CD  . GLU C 1 187 ? 51.423  -47.208 1.955   1.00 88.89  ? 190 GLU C CD  1 
ATOM   5395  O OE1 . GLU C 1 187 ? 50.853  -46.998 0.861   1.00 93.75  ? 190 GLU C OE1 1 
ATOM   5396  O OE2 . GLU C 1 187 ? 52.015  -46.319 2.599   1.00 86.81  ? 190 GLU C OE2 1 
ATOM   5397  N N   . GLN C 1 188 ? 49.239  -51.363 3.624   1.00 122.33 ? 191 GLN C N   1 
ATOM   5398  C CA  . GLN C 1 188 ? 48.632  -51.549 4.932   1.00 120.07 ? 191 GLN C CA  1 
ATOM   5399  C C   . GLN C 1 188 ? 49.356  -52.682 5.632   1.00 130.06 ? 191 GLN C C   1 
ATOM   5400  O O   . GLN C 1 188 ? 49.718  -52.577 6.805   1.00 127.45 ? 191 GLN C O   1 
ATOM   5401  C CB  . GLN C 1 188 ? 47.143  -51.869 4.793   1.00 106.49 ? 191 GLN C CB  1 
ATOM   5402  C CG  . GLN C 1 188 ? 46.472  -52.298 6.088   1.00 95.06  ? 191 GLN C CG  1 
ATOM   5403  C CD  . GLN C 1 188 ? 46.610  -51.268 7.191   1.00 88.87  ? 191 GLN C CD  1 
ATOM   5404  O OE1 . GLN C 1 188 ? 46.425  -50.072 6.967   1.00 94.74  ? 191 GLN C OE1 1 
ATOM   5405  N NE2 . GLN C 1 188 ? 46.942  -51.729 8.393   1.00 63.60  ? 191 GLN C NE2 1 
ATOM   5406  N N   . ARG C 1 189 ? 49.584  -53.756 4.882   1.00 100.24 ? 192 ARG C N   1 
ATOM   5407  C CA  . ARG C 1 189 ? 50.235  -54.950 5.403   1.00 105.66 ? 192 ARG C CA  1 
ATOM   5408  C C   . ARG C 1 189 ? 51.683  -54.660 5.800   1.00 110.54 ? 192 ARG C C   1 
ATOM   5409  O O   . ARG C 1 189 ? 52.159  -55.127 6.837   1.00 108.58 ? 192 ARG C O   1 
ATOM   5410  C CB  . ARG C 1 189 ? 50.178  -56.071 4.359   1.00 116.53 ? 192 ARG C CB  1 
ATOM   5411  C CG  . ARG C 1 189 ? 50.442  -57.465 4.908   1.00 127.18 ? 192 ARG C CG  1 
ATOM   5412  C CD  . ARG C 1 189 ? 49.163  -58.141 5.391   1.00 123.24 ? 192 ARG C CD  1 
ATOM   5413  N NE  . ARG C 1 189 ? 48.208  -58.367 4.304   1.00 122.84 ? 192 ARG C NE  1 
ATOM   5414  C CZ  . ARG C 1 189 ? 47.237  -59.278 4.333   1.00 118.21 ? 192 ARG C CZ  1 
ATOM   5415  N NH1 . ARG C 1 189 ? 47.091  -60.067 5.393   1.00 118.90 ? 192 ARG C NH1 1 
ATOM   5416  N NH2 . ARG C 1 189 ? 46.414  -59.408 3.298   1.00 109.29 ? 192 ARG C NH2 1 
ATOM   5417  N N   . THR C 1 190 ? 52.376  -53.883 4.974   1.00 87.43  ? 193 THR C N   1 
ATOM   5418  C CA  . THR C 1 190 ? 53.774  -53.555 5.223   1.00 89.75  ? 193 THR C CA  1 
ATOM   5419  C C   . THR C 1 190 ? 53.954  -52.785 6.530   1.00 71.31  ? 193 THR C C   1 
ATOM   5420  O O   . THR C 1 190 ? 54.818  -53.110 7.347   1.00 56.64  ? 193 THR C O   1 
ATOM   5421  C CB  . THR C 1 190 ? 54.365  -52.712 4.072   1.00 101.73 ? 193 THR C CB  1 
ATOM   5422  O OG1 . THR C 1 190 ? 54.099  -53.348 2.817   1.00 111.05 ? 193 THR C OG1 1 
ATOM   5423  C CG2 . THR C 1 190 ? 55.869  -52.538 4.243   1.00 101.23 ? 193 THR C CG2 1 
ATOM   5424  N N   . LEU C 1 191 ? 53.131  -51.762 6.726   1.00 131.01 ? 194 LEU C N   1 
ATOM   5425  C CA  . LEU C 1 191 ? 53.332  -50.835 7.833   1.00 105.77 ? 194 LEU C CA  1 
ATOM   5426  C C   . LEU C 1 191 ? 52.765  -51.318 9.167   1.00 86.03  ? 194 LEU C C   1 
ATOM   5427  O O   . LEU C 1 191 ? 53.344  -51.049 10.224  1.00 70.19  ? 194 LEU C O   1 
ATOM   5428  C CB  . LEU C 1 191 ? 52.758  -49.460 7.478   1.00 100.27 ? 194 LEU C CB  1 
ATOM   5429  C CG  . LEU C 1 191 ? 53.592  -48.598 6.527   1.00 113.57 ? 194 LEU C CG  1 
ATOM   5430  C CD1 . LEU C 1 191 ? 52.713  -47.849 5.543   1.00 123.51 ? 194 LEU C CD1 1 
ATOM   5431  C CD2 . LEU C 1 191 ? 54.465  -47.637 7.319   1.00 103.09 ? 194 LEU C CD2 1 
ATOM   5432  N N   . TYR C 1 192 ? 51.642  -52.032 9.114   1.00 109.37 ? 195 TYR C N   1 
ATOM   5433  C CA  . TYR C 1 192 ? 50.903  -52.385 10.326  1.00 89.00  ? 195 TYR C CA  1 
ATOM   5434  C C   . TYR C 1 192 ? 50.609  -53.882 10.447  1.00 94.50  ? 195 TYR C C   1 
ATOM   5435  O O   . TYR C 1 192 ? 50.091  -54.338 11.469  1.00 81.59  ? 195 TYR C O   1 
ATOM   5436  C CB  . TYR C 1 192 ? 49.604  -51.576 10.395  1.00 75.18  ? 195 TYR C CB  1 
ATOM   5437  C CG  . TYR C 1 192 ? 49.789  -50.138 9.963   1.00 77.02  ? 195 TYR C CG  1 
ATOM   5438  C CD1 . TYR C 1 192 ? 50.409  -49.219 10.800  1.00 65.87  ? 195 TYR C CD1 1 
ATOM   5439  C CD2 . TYR C 1 192 ? 49.363  -49.704 8.717   1.00 94.55  ? 195 TYR C CD2 1 
ATOM   5440  C CE1 . TYR C 1 192 ? 50.593  -47.906 10.413  1.00 64.60  ? 195 TYR C CE1 1 
ATOM   5441  C CE2 . TYR C 1 192 ? 49.540  -48.393 8.320   1.00 96.10  ? 195 TYR C CE2 1 
ATOM   5442  C CZ  . TYR C 1 192 ? 50.158  -47.499 9.174   1.00 80.52  ? 195 TYR C CZ  1 
ATOM   5443  O OH  . TYR C 1 192 ? 50.345  -46.188 8.797   1.00 92.00  ? 195 TYR C OH  1 
ATOM   5444  N N   . GLN C 1 193 ? 50.951  -54.638 9.404   1.00 112.32 ? 196 GLN C N   1 
ATOM   5445  C CA  . GLN C 1 193 ? 50.715  -56.084 9.361   1.00 119.60 ? 196 GLN C CA  1 
ATOM   5446  C C   . GLN C 1 193 ? 49.240  -56.418 9.206   1.00 123.31 ? 196 GLN C C   1 
ATOM   5447  O O   . GLN C 1 193 ? 48.780  -56.763 8.119   1.00 141.61 ? 196 GLN C O   1 
ATOM   5448  C CB  . GLN C 1 193 ? 51.275  -56.777 10.609  1.00 105.88 ? 196 GLN C CB  1 
ATOM   5449  C CG  . GLN C 1 193 ? 52.773  -57.055 10.555  1.00 117.17 ? 196 GLN C CG  1 
ATOM   5450  C CD  . GLN C 1 193 ? 53.119  -58.235 9.665   1.00 134.79 ? 196 GLN C CD  1 
ATOM   5451  O OE1 . GLN C 1 193 ? 52.265  -59.067 9.360   1.00 141.48 ? 196 GLN C OE1 1 
ATOM   5452  N NE2 . GLN C 1 193 ? 54.375  -58.311 9.243   1.00 140.95 ? 196 GLN C NE2 1 
ATOM   5453  N N   . ASN C 1 194 ? 48.507  -56.311 10.308  1.00 139.64 ? 197 ASN C N   1 
ATOM   5454  C CA  . ASN C 1 194 ? 47.094  -56.651 10.338  1.00 132.19 ? 197 ASN C CA  1 
ATOM   5455  C C   . ASN C 1 194 ? 46.292  -55.877 9.308   1.00 136.81 ? 197 ASN C C   1 
ATOM   5456  O O   . ASN C 1 194 ? 46.488  -54.679 9.133   1.00 141.49 ? 197 ASN C O   1 
ATOM   5457  C CB  . ASN C 1 194 ? 46.518  -56.362 11.722  1.00 118.70 ? 197 ASN C CB  1 
ATOM   5458  C CG  . ASN C 1 194 ? 47.543  -56.523 12.825  1.00 111.90 ? 197 ASN C CG  1 
ATOM   5459  O OD1 . ASN C 1 194 ? 48.355  -57.450 12.807  1.00 121.96 ? 197 ASN C OD1 1 
ATOM   5460  N ND2 . ASN C 1 194 ? 47.515  -55.613 13.795  1.00 96.73  ? 197 ASN C ND2 1 
ATOM   5461  N N   . VAL C 1 195 ? 45.388  -56.568 8.628   1.00 89.45  ? 198 VAL C N   1 
ATOM   5462  C CA  . VAL C 1 195 ? 44.394  -55.910 7.791   1.00 96.97  ? 198 VAL C CA  1 
ATOM   5463  C C   . VAL C 1 195 ? 43.087  -55.787 8.578   1.00 81.48  ? 198 VAL C C   1 
ATOM   5464  O O   . VAL C 1 195 ? 42.881  -56.491 9.571   1.00 66.18  ? 198 VAL C O   1 
ATOM   5465  C CB  . VAL C 1 195 ? 44.189  -56.656 6.452   1.00 101.34 ? 198 VAL C CB  1 
ATOM   5466  C CG1 . VAL C 1 195 ? 42.753  -56.533 5.956   1.00 94.06  ? 198 VAL C CG1 1 
ATOM   5467  C CG2 . VAL C 1 195 ? 45.166  -56.140 5.408   1.00 107.82 ? 198 VAL C CG2 1 
ATOM   5468  N N   . GLY C 1 196 ? 42.213  -54.882 8.155   1.00 122.14 ? 199 GLY C N   1 
ATOM   5469  C CA  . GLY C 1 196 ? 40.993  -54.636 8.894   1.00 103.76 ? 199 GLY C CA  1 
ATOM   5470  C C   . GLY C 1 196 ? 41.348  -54.074 10.253  1.00 80.29  ? 199 GLY C C   1 
ATOM   5471  O O   . GLY C 1 196 ? 40.918  -54.588 11.290  1.00 65.06  ? 199 GLY C O   1 
ATOM   5472  N N   . THR C 1 197 ? 42.163  -53.023 10.244  1.00 78.97  ? 200 THR C N   1 
ATOM   5473  C CA  . THR C 1 197 ? 42.535  -52.339 11.471  1.00 61.73  ? 200 THR C CA  1 
ATOM   5474  C C   . THR C 1 197 ? 41.495  -51.286 11.792  1.00 56.07  ? 200 THR C C   1 
ATOM   5475  O O   . THR C 1 197 ? 40.635  -50.973 10.963  1.00 65.46  ? 200 THR C O   1 
ATOM   5476  C CB  . THR C 1 197 ? 43.900  -51.640 11.349  1.00 67.47  ? 200 THR C CB  1 
ATOM   5477  O OG1 . THR C 1 197 ? 43.912  -50.822 10.169  1.00 83.92  ? 200 THR C OG1 1 
ATOM   5478  C CG2 . THR C 1 197 ? 45.019  -52.655 11.266  1.00 71.68  ? 200 THR C CG2 1 
ATOM   5479  N N   . TYR C 1 198 ? 41.585  -50.738 12.998  1.00 87.60  ? 201 TYR C N   1 
ATOM   5480  C CA  . TYR C 1 198 ? 40.711  -49.652 13.412  1.00 73.88  ? 201 TYR C CA  1 
ATOM   5481  C C   . TYR C 1 198 ? 41.404  -48.773 14.453  1.00 66.99  ? 201 TYR C C   1 
ATOM   5482  O O   . TYR C 1 198 ? 42.413  -49.162 15.036  1.00 71.02  ? 201 TYR C O   1 
ATOM   5483  C CB  . TYR C 1 198 ? 39.395  -50.208 13.960  1.00 70.41  ? 201 TYR C CB  1 
ATOM   5484  C CG  . TYR C 1 198 ? 39.521  -50.908 15.288  1.00 65.45  ? 201 TYR C CG  1 
ATOM   5485  C CD1 . TYR C 1 198 ? 39.585  -50.185 16.469  1.00 64.52  ? 201 TYR C CD1 1 
ATOM   5486  C CD2 . TYR C 1 198 ? 39.560  -52.289 15.365  1.00 69.28  ? 201 TYR C CD2 1 
ATOM   5487  C CE1 . TYR C 1 198 ? 39.698  -50.820 17.687  1.00 70.31  ? 201 TYR C CE1 1 
ATOM   5488  C CE2 . TYR C 1 198 ? 39.671  -52.934 16.577  1.00 73.75  ? 201 TYR C CE2 1 
ATOM   5489  C CZ  . TYR C 1 198 ? 39.738  -52.198 17.736  1.00 77.98  ? 201 TYR C CZ  1 
ATOM   5490  O OH  . TYR C 1 198 ? 39.848  -52.838 18.948  1.00 89.10  ? 201 TYR C OH  1 
ATOM   5491  N N   . VAL C 1 199 ? 40.857  -47.589 14.691  1.00 60.18  ? 202 VAL C N   1 
ATOM   5492  C CA  . VAL C 1 199 ? 41.468  -46.662 15.626  1.00 54.61  ? 202 VAL C CA  1 
ATOM   5493  C C   . VAL C 1 199 ? 40.393  -46.087 16.531  1.00 53.50  ? 202 VAL C C   1 
ATOM   5494  O O   . VAL C 1 199 ? 39.620  -45.228 16.112  1.00 52.21  ? 202 VAL C O   1 
ATOM   5495  C CB  . VAL C 1 199 ? 42.183  -45.507 14.878  1.00 56.89  ? 202 VAL C CB  1 
ATOM   5496  C CG1 . VAL C 1 199 ? 42.994  -44.657 15.846  1.00 51.28  ? 202 VAL C CG1 1 
ATOM   5497  C CG2 . VAL C 1 199 ? 43.079  -46.059 13.777  1.00 60.26  ? 202 VAL C CG2 1 
ATOM   5498  N N   . SER C 1 200 ? 40.338  -46.553 17.771  1.00 57.57  ? 203 SER C N   1 
ATOM   5499  C CA  A SER C 1 200 ? 39.313  -46.089 18.696  0.57 59.54  ? 203 SER C CA  1 
ATOM   5500  C CA  B SER C 1 200 ? 39.314  -46.102 18.708  0.43 61.02  ? 203 SER C CA  1 
ATOM   5501  C C   . SER C 1 200 ? 39.871  -45.107 19.715  1.00 59.32  ? 203 SER C C   1 
ATOM   5502  O O   . SER C 1 200 ? 40.992  -45.255 20.185  1.00 56.81  ? 203 SER C O   1 
ATOM   5503  C CB  A SER C 1 200 ? 38.641  -47.270 19.403  0.57 63.80  ? 203 SER C CB  1 
ATOM   5504  C CB  B SER C 1 200 ? 38.709  -47.292 19.453  0.43 70.54  ? 203 SER C CB  1 
ATOM   5505  O OG  A SER C 1 200 ? 37.967  -48.108 18.476  0.57 51.87  ? 203 SER C OG  1 
ATOM   5506  O OG  B SER C 1 200 ? 39.605  -47.769 20.443  0.43 86.72  ? 203 SER C OG  1 
ATOM   5507  N N   . VAL C 1 201 ? 39.071  -44.099 20.044  1.00 70.94  ? 204 VAL C N   1 
ATOM   5508  C CA  . VAL C 1 201 ? 39.435  -43.093 21.032  1.00 77.53  ? 204 VAL C CA  1 
ATOM   5509  C C   . VAL C 1 201 ? 38.242  -42.885 21.951  1.00 93.53  ? 204 VAL C C   1 
ATOM   5510  O O   . VAL C 1 201 ? 37.094  -42.916 21.503  1.00 92.78  ? 204 VAL C O   1 
ATOM   5511  C CB  . VAL C 1 201 ? 39.779  -41.748 20.375  1.00 65.55  ? 204 VAL C CB  1 
ATOM   5512  C CG1 . VAL C 1 201 ? 40.247  -40.758 21.425  1.00 73.51  ? 204 VAL C CG1 1 
ATOM   5513  C CG2 . VAL C 1 201 ? 40.837  -41.931 19.301  1.00 69.11  ? 204 VAL C CG2 1 
ATOM   5514  N N   . GLY C 1 202 ? 38.506  -42.665 23.233  1.00 47.19  ? 205 GLY C N   1 
ATOM   5515  C CA  . GLY C 1 202 ? 37.431  -42.547 24.194  1.00 50.93  ? 205 GLY C CA  1 
ATOM   5516  C C   . GLY C 1 202 ? 37.739  -41.688 25.397  1.00 63.97  ? 205 GLY C C   1 
ATOM   5517  O O   . GLY C 1 202 ? 38.801  -41.786 26.003  1.00 80.00  ? 205 GLY C O   1 
ATOM   5518  N N   . THR C 1 203 ? 36.794  -40.825 25.729  1.00 44.15  ? 206 THR C N   1 
ATOM   5519  C CA  . THR C 1 203 ? 36.835  -40.092 26.976  1.00 53.75  ? 206 THR C CA  1 
ATOM   5520  C C   . THR C 1 203 ? 35.475  -40.308 27.626  1.00 62.45  ? 206 THR C C   1 
ATOM   5521  O O   . THR C 1 203 ? 34.744  -41.209 27.224  1.00 68.92  ? 206 THR C O   1 
ATOM   5522  C CB  . THR C 1 203 ? 37.103  -38.599 26.750  1.00 57.21  ? 206 THR C CB  1 
ATOM   5523  O OG1 . THR C 1 203 ? 35.917  -37.962 26.264  1.00 56.94  ? 206 THR C OG1 1 
ATOM   5524  C CG2 . THR C 1 203 ? 38.214  -38.419 25.746  1.00 52.30  ? 206 THR C CG2 1 
ATOM   5525  N N   . SER C 1 204 ? 35.125  -39.502 28.620  1.00 56.50  ? 207 SER C N   1 
ATOM   5526  C CA  . SER C 1 204 ? 33.850  -39.689 29.298  1.00 57.34  ? 207 SER C CA  1 
ATOM   5527  C C   . SER C 1 204 ? 32.686  -39.306 28.398  1.00 53.89  ? 207 SER C C   1 
ATOM   5528  O O   . SER C 1 204 ? 31.561  -39.772 28.591  1.00 56.48  ? 207 SER C O   1 
ATOM   5529  C CB  . SER C 1 204 ? 33.791  -38.885 30.598  1.00 61.70  ? 207 SER C CB  1 
ATOM   5530  O OG  . SER C 1 204 ? 34.601  -39.465 31.604  1.00 71.36  ? 207 SER C OG  1 
ATOM   5531  N N   . THR C 1 205 ? 32.956  -38.454 27.416  1.00 54.41  ? 208 THR C N   1 
ATOM   5532  C CA  . THR C 1 205 ? 31.894  -37.935 26.564  1.00 40.85  ? 208 THR C CA  1 
ATOM   5533  C C   . THR C 1 205 ? 32.123  -38.281 25.108  1.00 48.83  ? 208 THR C C   1 
ATOM   5534  O O   . THR C 1 205 ? 31.190  -38.260 24.309  1.00 51.01  ? 208 THR C O   1 
ATOM   5535  C CB  . THR C 1 205 ? 31.746  -36.393 26.674  1.00 40.02  ? 208 THR C CB  1 
ATOM   5536  O OG1 . THR C 1 205 ? 32.862  -35.743 26.041  1.00 55.80  ? 208 THR C OG1 1 
ATOM   5537  C CG2 . THR C 1 205 ? 31.660  -35.946 28.125  1.00 30.96  ? 208 THR C CG2 1 
ATOM   5538  N N   . LEU C 1 206 ? 33.362  -38.590 24.758  1.00 84.16  ? 209 LEU C N   1 
ATOM   5539  C CA  . LEU C 1 206 ? 33.677  -38.871 23.371  1.00 62.23  ? 209 LEU C CA  1 
ATOM   5540  C C   . LEU C 1 206 ? 33.949  -40.335 23.117  1.00 71.86  ? 209 LEU C C   1 
ATOM   5541  O O   . LEU C 1 206 ? 34.734  -40.972 23.817  1.00 88.81  ? 209 LEU C O   1 
ATOM   5542  C CB  . LEU C 1 206 ? 34.885  -38.066 22.915  1.00 51.60  ? 209 LEU C CB  1 
ATOM   5543  C CG  . LEU C 1 206 ? 35.324  -38.424 21.496  1.00 33.44  ? 209 LEU C CG  1 
ATOM   5544  C CD1 . LEU C 1 206 ? 34.384  -37.787 20.486  1.00 27.57  ? 209 LEU C CD1 1 
ATOM   5545  C CD2 . LEU C 1 206 ? 36.762  -38.002 21.245  1.00 42.50  ? 209 LEU C CD2 1 
ATOM   5546  N N   . ASN C 1 207 ? 33.282  -40.859 22.102  1.00 79.86  ? 210 ASN C N   1 
ATOM   5547  C CA  . ASN C 1 207 ? 33.618  -42.158 21.557  1.00 69.82  ? 210 ASN C CA  1 
ATOM   5548  C C   . ASN C 1 207 ? 33.609  -42.076 20.044  1.00 59.93  ? 210 ASN C C   1 
ATOM   5549  O O   . ASN C 1 207 ? 32.551  -41.972 19.426  1.00 63.72  ? 210 ASN C O   1 
ATOM   5550  C CB  . ASN C 1 207 ? 32.639  -43.224 22.035  1.00 68.62  ? 210 ASN C CB  1 
ATOM   5551  C CG  . ASN C 1 207 ? 32.631  -44.435 21.143  1.00 65.37  ? 210 ASN C CG  1 
ATOM   5552  O OD1 . ASN C 1 207 ? 33.608  -45.180 21.082  1.00 81.17  ? 210 ASN C OD1 1 
ATOM   5553  N ND2 . ASN C 1 207 ? 31.525  -44.643 20.439  1.00 50.36  ? 210 ASN C ND2 1 
ATOM   5554  N N   . LYS C 1 208 ? 34.794  -42.095 19.451  1.00 59.18  ? 211 LYS C N   1 
ATOM   5555  C CA  . LYS C 1 208 ? 34.911  -42.047 18.004  1.00 55.41  ? 211 LYS C CA  1 
ATOM   5556  C C   . LYS C 1 208 ? 35.763  -43.200 17.533  1.00 60.38  ? 211 LYS C C   1 
ATOM   5557  O O   . LYS C 1 208 ? 36.688  -43.618 18.223  1.00 73.37  ? 211 LYS C O   1 
ATOM   5558  C CB  . LYS C 1 208 ? 35.514  -40.709 17.550  1.00 53.24  ? 211 LYS C CB  1 
ATOM   5559  C CG  . LYS C 1 208 ? 36.015  -40.688 16.104  1.00 55.73  ? 211 LYS C CG  1 
ATOM   5560  C CD  . LYS C 1 208 ? 35.637  -39.400 15.385  1.00 61.30  ? 211 LYS C CD  1 
ATOM   5561  C CE  . LYS C 1 208 ? 36.109  -38.173 16.147  1.00 69.95  ? 211 LYS C CE  1 
ATOM   5562  N NZ  . LYS C 1 208 ? 35.775  -36.909 15.430  1.00 75.68  ? 211 LYS C NZ  1 
ATOM   5563  N N   . ARG C 1 209 ? 35.436  -43.729 16.363  1.00 58.46  ? 212 ARG C N   1 
ATOM   5564  C CA  . ARG C 1 209 ? 36.239  -44.774 15.755  1.00 60.88  ? 212 ARG C CA  1 
ATOM   5565  C C   . ARG C 1 209 ? 36.463  -44.444 14.297  1.00 80.82  ? 212 ARG C C   1 
ATOM   5566  O O   . ARG C 1 209 ? 35.529  -44.064 13.587  1.00 91.50  ? 212 ARG C O   1 
ATOM   5567  C CB  . ARG C 1 209 ? 35.567  -46.141 15.869  1.00 51.57  ? 212 ARG C CB  1 
ATOM   5568  C CG  . ARG C 1 209 ? 36.191  -47.161 14.937  1.00 62.80  ? 212 ARG C CG  1 
ATOM   5569  C CD  . ARG C 1 209 ? 35.739  -48.574 15.236  1.00 63.31  ? 212 ARG C CD  1 
ATOM   5570  N NE  . ARG C 1 209 ? 36.004  -48.947 16.621  1.00 63.25  ? 212 ARG C NE  1 
ATOM   5571  C CZ  . ARG C 1 209 ? 36.139  -50.199 17.043  1.00 72.99  ? 212 ARG C CZ  1 
ATOM   5572  N NH1 . ARG C 1 209 ? 36.047  -51.209 16.180  1.00 66.28  ? 212 ARG C NH1 1 
ATOM   5573  N NH2 . ARG C 1 209 ? 36.376  -50.441 18.329  1.00 83.14  ? 212 ARG C NH2 1 
ATOM   5574  N N   . SER C 1 210 ? 37.708  -44.583 13.858  1.00 68.42  ? 213 SER C N   1 
ATOM   5575  C CA  . SER C 1 210 ? 38.053  -44.379 12.461  1.00 67.65  ? 213 SER C CA  1 
ATOM   5576  C C   . SER C 1 210 ? 38.480  -45.703 11.838  1.00 75.39  ? 213 SER C C   1 
ATOM   5577  O O   . SER C 1 210 ? 38.968  -46.598 12.529  1.00 72.67  ? 213 SER C O   1 
ATOM   5578  C CB  . SER C 1 210 ? 39.159  -43.329 12.332  1.00 65.90  ? 213 SER C CB  1 
ATOM   5579  O OG  . SER C 1 210 ? 38.701  -42.038 12.730  1.00 64.64  ? 213 SER C OG  1 
ATOM   5580  N N   . THR C 1 211 ? 38.276  -45.833 10.533  1.00 60.24  ? 214 THR C N   1 
ATOM   5581  C CA  . THR C 1 211 ? 38.672  -47.040 9.829   1.00 77.63  ? 214 THR C CA  1 
ATOM   5582  C C   . THR C 1 211 ? 39.245  -46.679 8.472   1.00 104.84 ? 214 THR C C   1 
ATOM   5583  O O   . THR C 1 211 ? 38.556  -46.087 7.643   1.00 116.99 ? 214 THR C O   1 
ATOM   5584  C CB  . THR C 1 211 ? 37.488  -47.988 9.641   1.00 78.88  ? 214 THR C CB  1 
ATOM   5585  O OG1 . THR C 1 211 ? 36.566  -47.805 10.719  1.00 62.72  ? 214 THR C OG1 1 
ATOM   5586  C CG2 . THR C 1 211 ? 37.962  -49.439 9.620   1.00 81.36  ? 214 THR C CG2 1 
ATOM   5587  N N   . PRO C 1 212 ? 40.515  -47.040 8.246   1.00 52.79  ? 215 PRO C N   1 
ATOM   5588  C CA  . PRO C 1 212 ? 41.226  -46.686 7.019   1.00 63.46  ? 215 PRO C CA  1 
ATOM   5589  C C   . PRO C 1 212 ? 40.401  -47.026 5.796   1.00 70.44  ? 215 PRO C C   1 
ATOM   5590  O O   . PRO C 1 212 ? 40.047  -48.182 5.596   1.00 75.52  ? 215 PRO C O   1 
ATOM   5591  C CB  . PRO C 1 212 ? 42.464  -47.579 7.070   1.00 66.38  ? 215 PRO C CB  1 
ATOM   5592  C CG  . PRO C 1 212 ? 42.694  -47.818 8.514   1.00 44.86  ? 215 PRO C CG  1 
ATOM   5593  C CD  . PRO C 1 212 ? 41.336  -47.877 9.138   1.00 36.90  ? 215 PRO C CD  1 
ATOM   5594  N N   . GLU C 1 213 ? 40.085  -46.019 4.996   1.00 104.37 ? 216 GLU C N   1 
ATOM   5595  C CA  . GLU C 1 213 ? 39.442  -46.251 3.717   1.00 111.44 ? 216 GLU C CA  1 
ATOM   5596  C C   . GLU C 1 213 ? 40.513  -46.168 2.638   1.00 120.39 ? 216 GLU C C   1 
ATOM   5597  O O   . GLU C 1 213 ? 41.043  -45.094 2.358   1.00 129.89 ? 216 GLU C O   1 
ATOM   5598  C CB  . GLU C 1 213 ? 38.331  -45.229 3.472   1.00 109.26 ? 216 GLU C CB  1 
ATOM   5599  C CG  . GLU C 1 213 ? 37.143  -45.375 4.412   1.00 108.69 ? 216 GLU C CG  1 
ATOM   5600  C CD  . GLU C 1 213 ? 36.159  -44.224 4.304   1.00 110.63 ? 216 GLU C CD  1 
ATOM   5601  O OE1 . GLU C 1 213 ? 36.298  -43.402 3.376   1.00 113.92 ? 216 GLU C OE1 1 
ATOM   5602  O OE2 . GLU C 1 213 ? 35.247  -44.139 5.152   1.00 108.49 ? 216 GLU C OE2 1 
ATOM   5603  N N   . ILE C 1 214 ? 40.842  -47.310 2.049   1.00 89.19  ? 217 ILE C N   1 
ATOM   5604  C CA  . ILE C 1 214 ? 41.921  -47.380 1.072   1.00 102.19 ? 217 ILE C CA  1 
ATOM   5605  C C   . ILE C 1 214 ? 41.471  -47.010 -0.340  1.00 109.14 ? 217 ILE C C   1 
ATOM   5606  O O   . ILE C 1 214 ? 40.680  -47.720 -0.961  1.00 111.20 ? 217 ILE C O   1 
ATOM   5607  C CB  . ILE C 1 214 ? 42.585  -48.770 1.078   1.00 85.59  ? 217 ILE C CB  1 
ATOM   5608  C CG1 . ILE C 1 214 ? 43.494  -48.903 2.303   1.00 79.58  ? 217 ILE C CG1 1 
ATOM   5609  C CG2 . ILE C 1 214 ? 43.376  -48.991 -0.198  1.00 94.38  ? 217 ILE C CG2 1 
ATOM   5610  C CD1 . ILE C 1 214 ? 44.116  -50.274 2.463   1.00 77.66  ? 217 ILE C CD1 1 
ATOM   5611  N N   . ALA C 1 215 ? 41.985  -45.887 -0.834  1.00 104.21 ? 218 ALA C N   1 
ATOM   5612  C CA  . ALA C 1 215 ? 41.703  -45.426 -2.189  1.00 105.73 ? 218 ALA C CA  1 
ATOM   5613  C C   . ALA C 1 215 ? 43.004  -45.031 -2.874  1.00 110.50 ? 218 ALA C C   1 
ATOM   5614  O O   . ALA C 1 215 ? 44.018  -44.818 -2.210  1.00 117.83 ? 218 ALA C O   1 
ATOM   5615  C CB  . ALA C 1 215 ? 40.739  -44.249 -2.163  1.00 101.80 ? 218 ALA C CB  1 
ATOM   5616  N N   . THR C 1 216 ? 42.975  -44.932 -4.200  1.00 68.99  ? 219 THR C N   1 
ATOM   5617  C CA  . THR C 1 216 ? 44.172  -44.574 -4.958  1.00 74.78  ? 219 THR C CA  1 
ATOM   5618  C C   . THR C 1 216 ? 44.225  -43.069 -5.245  1.00 84.28  ? 219 THR C C   1 
ATOM   5619  O O   . THR C 1 216 ? 43.279  -42.499 -5.790  1.00 87.00  ? 219 THR C O   1 
ATOM   5620  C CB  . THR C 1 216 ? 44.279  -45.389 -6.259  1.00 81.56  ? 219 THR C CB  1 
ATOM   5621  O OG1 . THR C 1 216 ? 44.446  -46.776 -5.935  1.00 81.66  ? 219 THR C OG1 1 
ATOM   5622  C CG2 . THR C 1 216 ? 45.471  -44.927 -7.082  1.00 92.08  ? 219 THR C CG2 1 
ATOM   5623  N N   . ARG C 1 217 ? 45.344  -42.440 -4.882  1.00 118.71 ? 220 ARG C N   1 
ATOM   5624  C CA  . ARG C 1 217 ? 45.441  -40.982 -4.840  1.00 116.15 ? 220 ARG C CA  1 
ATOM   5625  C C   . ARG C 1 217 ? 46.695  -40.425 -5.516  1.00 121.63 ? 220 ARG C C   1 
ATOM   5626  O O   . ARG C 1 217 ? 47.765  -41.028 -5.434  1.00 123.91 ? 220 ARG C O   1 
ATOM   5627  C CB  . ARG C 1 217 ? 45.437  -40.525 -3.381  1.00 102.38 ? 220 ARG C CB  1 
ATOM   5628  C CG  . ARG C 1 217 ? 44.564  -41.367 -2.476  1.00 86.74  ? 220 ARG C CG  1 
ATOM   5629  C CD  . ARG C 1 217 ? 44.840  -41.062 -1.019  1.00 89.18  ? 220 ARG C CD  1 
ATOM   5630  N NE  . ARG C 1 217 ? 44.001  -41.849 -0.120  1.00 83.16  ? 220 ARG C NE  1 
ATOM   5631  C CZ  . ARG C 1 217 ? 44.357  -43.019 0.400   1.00 80.87  ? 220 ARG C CZ  1 
ATOM   5632  N NH1 . ARG C 1 217 ? 45.539  -43.545 0.111   1.00 94.69  ? 220 ARG C NH1 1 
ATOM   5633  N NH2 . ARG C 1 217 ? 43.532  -43.665 1.209   1.00 59.70  ? 220 ARG C NH2 1 
ATOM   5634  N N   . PRO C 1 218 ? 46.563  -39.254 -6.170  1.00 75.44  ? 221 PRO C N   1 
ATOM   5635  C CA  . PRO C 1 218 ? 47.673  -38.475 -6.739  1.00 87.21  ? 221 PRO C CA  1 
ATOM   5636  C C   . PRO C 1 218 ? 48.751  -38.165 -5.703  1.00 88.99  ? 221 PRO C C   1 
ATOM   5637  O O   . PRO C 1 218 ? 48.431  -37.824 -4.570  1.00 80.81  ? 221 PRO C O   1 
ATOM   5638  C CB  . PRO C 1 218 ? 46.995  -37.177 -7.174  1.00 83.42  ? 221 PRO C CB  1 
ATOM   5639  C CG  . PRO C 1 218 ? 45.589  -37.570 -7.461  1.00 75.60  ? 221 PRO C CG  1 
ATOM   5640  C CD  . PRO C 1 218 ? 45.256  -38.632 -6.454  1.00 69.28  ? 221 PRO C CD  1 
ATOM   5641  N N   . LYS C 1 219 ? 50.014  -38.273 -6.097  1.00 124.09 ? 222 LYS C N   1 
ATOM   5642  C CA  . LYS C 1 219 ? 51.123  -38.132 -5.155  1.00 131.58 ? 222 LYS C CA  1 
ATOM   5643  C C   . LYS C 1 219 ? 51.370  -36.692 -4.711  1.00 132.86 ? 222 LYS C C   1 
ATOM   5644  O O   . LYS C 1 219 ? 52.424  -36.123 -4.995  1.00 143.24 ? 222 LYS C O   1 
ATOM   5645  C CB  . LYS C 1 219 ? 52.412  -38.728 -5.735  1.00 148.38 ? 222 LYS C CB  1 
ATOM   5646  C CG  . LYS C 1 219 ? 52.457  -40.251 -5.736  1.00 158.30 ? 222 LYS C CG  1 
ATOM   5647  C CD  . LYS C 1 219 ? 51.396  -40.846 -6.651  1.00 159.86 ? 222 LYS C CD  1 
ATOM   5648  C CE  . LYS C 1 219 ? 51.183  -42.326 -6.365  1.00 146.64 ? 222 LYS C CE  1 
ATOM   5649  N NZ  . LYS C 1 219 ? 50.044  -42.887 -7.146  1.00 136.88 ? 222 LYS C NZ  1 
ATOM   5650  N N   . VAL C 1 220 ? 50.403  -36.107 -4.012  1.00 88.45  ? 223 VAL C N   1 
ATOM   5651  C CA  . VAL C 1 220 ? 50.591  -34.782 -3.434  1.00 86.69  ? 223 VAL C CA  1 
ATOM   5652  C C   . VAL C 1 220 ? 51.738  -34.831 -2.430  1.00 88.50  ? 223 VAL C C   1 
ATOM   5653  O O   . VAL C 1 220 ? 51.706  -35.624 -1.490  1.00 83.73  ? 223 VAL C O   1 
ATOM   5654  C CB  . VAL C 1 220 ? 49.315  -34.276 -2.735  1.00 78.99  ? 223 VAL C CB  1 
ATOM   5655  C CG1 . VAL C 1 220 ? 49.646  -33.131 -1.790  1.00 72.53  ? 223 VAL C CG1 1 
ATOM   5656  C CG2 . VAL C 1 220 ? 48.272  -33.855 -3.768  1.00 81.18  ? 223 VAL C CG2 1 
ATOM   5657  N N   . ASN C 1 221 ? 52.746  -33.987 -2.635  1.00 89.66  ? 224 ASN C N   1 
ATOM   5658  C CA  . ASN C 1 221 ? 53.978  -34.045 -1.848  1.00 93.24  ? 224 ASN C CA  1 
ATOM   5659  C C   . ASN C 1 221 ? 54.704  -35.372 -2.032  1.00 94.63  ? 224 ASN C C   1 
ATOM   5660  O O   . ASN C 1 221 ? 55.337  -35.881 -1.103  1.00 92.76  ? 224 ASN C O   1 
ATOM   5661  C CB  . ASN C 1 221 ? 53.701  -33.814 -0.364  1.00 87.00  ? 224 ASN C CB  1 
ATOM   5662  C CG  . ASN C 1 221 ? 53.093  -32.466 -0.096  1.00 86.57  ? 224 ASN C CG  1 
ATOM   5663  O OD1 . ASN C 1 221 ? 52.437  -31.889 -0.963  1.00 89.45  ? 224 ASN C OD1 1 
ATOM   5664  N ND2 . ASN C 1 221 ? 53.306  -31.948 1.107   1.00 81.45  ? 224 ASN C ND2 1 
ATOM   5665  N N   . GLY C 1 222 ? 54.606  -35.926 -3.236  1.00 178.93 ? 225 GLY C N   1 
ATOM   5666  C CA  . GLY C 1 222 ? 55.215  -37.207 -3.541  1.00 185.18 ? 225 GLY C CA  1 
ATOM   5667  C C   . GLY C 1 222 ? 54.664  -38.324 -2.678  1.00 170.58 ? 225 GLY C C   1 
ATOM   5668  O O   . GLY C 1 222 ? 55.282  -39.380 -2.542  1.00 171.10 ? 225 GLY C O   1 
ATOM   5669  N N   . GLN C 1 223 ? 53.494  -38.088 -2.094  1.00 100.85 ? 226 GLN C N   1 
ATOM   5670  C CA  . GLN C 1 223 ? 52.862  -39.067 -1.217  1.00 90.15  ? 226 GLN C CA  1 
ATOM   5671  C C   . GLN C 1 223 ? 51.462  -39.413 -1.715  1.00 79.65  ? 226 GLN C C   1 
ATOM   5672  O O   . GLN C 1 223 ? 50.704  -38.533 -2.129  1.00 82.75  ? 226 GLN C O   1 
ATOM   5673  C CB  . GLN C 1 223 ? 52.792  -38.537 0.215   1.00 86.15  ? 226 GLN C CB  1 
ATOM   5674  C CG  . GLN C 1 223 ? 54.123  -38.055 0.776   1.00 100.45 ? 226 GLN C CG  1 
ATOM   5675  C CD  . GLN C 1 223 ? 55.026  -39.184 1.232   1.00 111.19 ? 226 GLN C CD  1 
ATOM   5676  O OE1 . GLN C 1 223 ? 56.215  -38.979 1.479   1.00 113.65 ? 226 GLN C OE1 1 
ATOM   5677  N NE2 . GLN C 1 223 ? 54.465  -40.381 1.355   1.00 113.26 ? 226 GLN C NE2 1 
ATOM   5678  N N   . GLY C 1 224 ? 51.131  -40.701 -1.678  1.00 76.36  ? 227 GLY C N   1 
ATOM   5679  C CA  . GLY C 1 224 ? 49.827  -41.171 -2.109  1.00 74.87  ? 227 GLY C CA  1 
ATOM   5680  C C   . GLY C 1 224 ? 48.905  -41.403 -0.928  1.00 76.16  ? 227 GLY C C   1 
ATOM   5681  O O   . GLY C 1 224 ? 47.684  -41.395 -1.077  1.00 70.27  ? 227 GLY C O   1 
ATOM   5682  N N   . GLY C 1 225 ? 49.494  -41.605 0.248   1.00 101.95 ? 228 GLY C N   1 
ATOM   5683  C CA  . GLY C 1 225 ? 48.726  -41.790 1.465   1.00 91.94  ? 228 GLY C CA  1 
ATOM   5684  C C   . GLY C 1 225 ? 48.182  -40.480 2.000   1.00 83.48  ? 228 GLY C C   1 
ATOM   5685  O O   . GLY C 1 225 ? 48.627  -39.411 1.591   1.00 85.80  ? 228 GLY C O   1 
ATOM   5686  N N   . ARG C 1 226 ? 47.213  -40.562 2.910   1.00 76.60  ? 229 ARG C N   1 
ATOM   5687  C CA  . ARG C 1 226 ? 46.628  -39.371 3.530   1.00 64.33  ? 229 ARG C CA  1 
ATOM   5688  C C   . ARG C 1 226 ? 46.352  -39.612 5.000   1.00 55.72  ? 229 ARG C C   1 
ATOM   5689  O O   . ARG C 1 226 ? 46.031  -40.720 5.396   1.00 52.87  ? 229 ARG C O   1 
ATOM   5690  C CB  . ARG C 1 226 ? 45.343  -38.970 2.813   1.00 58.70  ? 229 ARG C CB  1 
ATOM   5691  C CG  . ARG C 1 226 ? 45.597  -38.291 1.488   1.00 68.88  ? 229 ARG C CG  1 
ATOM   5692  C CD  . ARG C 1 226 ? 44.363  -38.272 0.603   1.00 69.44  ? 229 ARG C CD  1 
ATOM   5693  N NE  . ARG C 1 226 ? 44.634  -37.915 -0.795  1.00 79.98  ? 229 ARG C NE  1 
ATOM   5694  C CZ  . ARG C 1 226 ? 45.832  -37.639 -1.321  1.00 80.03  ? 229 ARG C CZ  1 
ATOM   5695  N NH1 . ARG C 1 226 ? 46.942  -37.659 -0.591  1.00 73.23  ? 229 ARG C NH1 1 
ATOM   5696  N NH2 . ARG C 1 226 ? 45.918  -37.333 -2.607  1.00 84.83  ? 229 ARG C NH2 1 
ATOM   5697  N N   . MET C 1 227 ? 46.486  -38.584 5.820   1.00 94.02  ? 230 MET C N   1 
ATOM   5698  C CA  . MET C 1 227 ? 46.266  -38.777 7.242   1.00 81.02  ? 230 MET C CA  1 
ATOM   5699  C C   . MET C 1 227 ? 45.138  -37.903 7.773   1.00 75.37  ? 230 MET C C   1 
ATOM   5700  O O   . MET C 1 227 ? 45.320  -36.713 8.014   1.00 85.39  ? 230 MET C O   1 
ATOM   5701  C CB  . MET C 1 227 ? 47.553  -38.543 8.030   1.00 62.06  ? 230 MET C CB  1 
ATOM   5702  C CG  . MET C 1 227 ? 48.679  -39.505 7.684   1.00 66.10  ? 230 MET C CG  1 
ATOM   5703  S SD  . MET C 1 227 ? 50.076  -39.326 8.816   1.00 79.06  ? 230 MET C SD  1 
ATOM   5704  C CE  . MET C 1 227 ? 51.340  -40.218 7.918   1.00 102.18 ? 230 MET C CE  1 
ATOM   5705  N N   . GLU C 1 228 ? 43.974  -38.519 7.953   1.00 109.23 ? 231 GLU C N   1 
ATOM   5706  C CA  . GLU C 1 228 ? 42.779  -37.847 8.458   1.00 101.51 ? 231 GLU C CA  1 
ATOM   5707  C C   . GLU C 1 228 ? 42.877  -37.582 9.961   1.00 72.67  ? 231 GLU C C   1 
ATOM   5708  O O   . GLU C 1 228 ? 42.923  -38.520 10.754  1.00 64.39  ? 231 GLU C O   1 
ATOM   5709  C CB  . GLU C 1 228 ? 41.559  -38.717 8.149   1.00 110.40 ? 231 GLU C CB  1 
ATOM   5710  C CG  . GLU C 1 228 ? 40.284  -38.334 8.861   1.00 96.60  ? 231 GLU C CG  1 
ATOM   5711  C CD  . GLU C 1 228 ? 39.130  -39.232 8.464   1.00 105.20 ? 231 GLU C CD  1 
ATOM   5712  O OE1 . GLU C 1 228 ? 39.274  -39.978 7.471   1.00 115.94 ? 231 GLU C OE1 1 
ATOM   5713  O OE2 . GLU C 1 228 ? 38.081  -39.197 9.141   1.00 94.76  ? 231 GLU C OE2 1 
ATOM   5714  N N   . PHE C 1 229 ? 42.903  -36.309 10.349  1.00 79.66  ? 232 PHE C N   1 
ATOM   5715  C CA  . PHE C 1 229 ? 43.123  -35.932 11.747  1.00 64.71  ? 232 PHE C CA  1 
ATOM   5716  C C   . PHE C 1 229 ? 41.847  -35.549 12.503  1.00 51.68  ? 232 PHE C C   1 
ATOM   5717  O O   . PHE C 1 229 ? 40.914  -34.984 11.931  1.00 64.19  ? 232 PHE C O   1 
ATOM   5718  C CB  . PHE C 1 229 ? 44.128  -34.781 11.834  1.00 65.22  ? 232 PHE C CB  1 
ATOM   5719  C CG  . PHE C 1 229 ? 45.550  -35.203 11.634  1.00 71.84  ? 232 PHE C CG  1 
ATOM   5720  C CD1 . PHE C 1 229 ? 46.356  -35.507 12.721  1.00 63.89  ? 232 PHE C CD1 1 
ATOM   5721  C CD2 . PHE C 1 229 ? 46.083  -35.297 10.363  1.00 90.49  ? 232 PHE C CD2 1 
ATOM   5722  C CE1 . PHE C 1 229 ? 47.669  -35.899 12.540  1.00 62.65  ? 232 PHE C CE1 1 
ATOM   5723  C CE2 . PHE C 1 229 ? 47.391  -35.686 10.175  1.00 90.73  ? 232 PHE C CE2 1 
ATOM   5724  C CZ  . PHE C 1 229 ? 48.186  -35.986 11.266  1.00 76.36  ? 232 PHE C CZ  1 
ATOM   5725  N N   . SER C 1 230 ? 41.824  -35.838 13.799  1.00 55.26  ? 233 SER C N   1 
ATOM   5726  C CA  . SER C 1 230 ? 40.653  -35.564 14.624  1.00 54.24  ? 233 SER C CA  1 
ATOM   5727  C C   . SER C 1 230 ? 41.066  -35.152 16.033  1.00 51.51  ? 233 SER C C   1 
ATOM   5728  O O   . SER C 1 230 ? 42.130  -35.552 16.507  1.00 61.43  ? 233 SER C O   1 
ATOM   5729  C CB  . SER C 1 230 ? 39.736  -36.792 14.677  1.00 57.00  ? 233 SER C CB  1 
ATOM   5730  O OG  . SER C 1 230 ? 39.080  -36.994 13.436  1.00 68.22  ? 233 SER C OG  1 
ATOM   5731  N N   . TRP C 1 231 ? 40.219  -34.373 16.707  1.00 43.17  ? 234 TRP C N   1 
ATOM   5732  C CA  . TRP C 1 231 ? 40.582  -33.794 18.001  1.00 48.28  ? 234 TRP C CA  1 
ATOM   5733  C C   . TRP C 1 231 ? 39.438  -33.738 19.030  1.00 54.80  ? 234 TRP C C   1 
ATOM   5734  O O   . TRP C 1 231 ? 38.275  -33.989 18.705  1.00 54.11  ? 234 TRP C O   1 
ATOM   5735  C CB  . TRP C 1 231 ? 41.084  -32.384 17.764  1.00 47.79  ? 234 TRP C CB  1 
ATOM   5736  C CG  . TRP C 1 231 ? 40.020  -31.522 17.204  1.00 45.08  ? 234 TRP C CG  1 
ATOM   5737  C CD1 . TRP C 1 231 ? 39.650  -31.422 15.897  1.00 46.87  ? 234 TRP C CD1 1 
ATOM   5738  C CD2 . TRP C 1 231 ? 39.159  -30.655 17.938  1.00 42.17  ? 234 TRP C CD2 1 
ATOM   5739  N NE1 . TRP C 1 231 ? 38.614  -30.531 15.769  1.00 45.01  ? 234 TRP C NE1 1 
ATOM   5740  C CE2 . TRP C 1 231 ? 38.294  -30.045 17.009  1.00 36.15  ? 234 TRP C CE2 1 
ATOM   5741  C CE3 . TRP C 1 231 ? 39.041  -30.326 19.289  1.00 49.45  ? 234 TRP C CE3 1 
ATOM   5742  C CZ2 . TRP C 1 231 ? 37.323  -29.121 17.388  1.00 32.28  ? 234 TRP C CZ2 1 
ATOM   5743  C CZ3 . TRP C 1 231 ? 38.076  -29.408 19.667  1.00 48.94  ? 234 TRP C CZ3 1 
ATOM   5744  C CH2 . TRP C 1 231 ? 37.226  -28.820 18.720  1.00 36.75  ? 234 TRP C CH2 1 
ATOM   5745  N N   . THR C 1 232 ? 39.784  -33.386 20.269  1.00 42.47  ? 235 THR C N   1 
ATOM   5746  C CA  . THR C 1 232 ? 38.805  -33.221 21.354  1.00 40.83  ? 235 THR C CA  1 
ATOM   5747  C C   . THR C 1 232 ? 39.356  -32.403 22.525  1.00 56.78  ? 235 THR C C   1 
ATOM   5748  O O   . THR C 1 232 ? 40.557  -32.164 22.619  1.00 75.84  ? 235 THR C O   1 
ATOM   5749  C CB  . THR C 1 232 ? 38.319  -34.578 21.895  1.00 43.86  ? 235 THR C CB  1 
ATOM   5750  O OG1 . THR C 1 232 ? 37.864  -34.424 23.245  1.00 55.27  ? 235 THR C OG1 1 
ATOM   5751  C CG2 . THR C 1 232 ? 39.449  -35.586 21.879  1.00 50.59  ? 235 THR C CG2 1 
ATOM   5752  N N   . LEU C 1 233 ? 38.467  -31.971 23.413  1.00 38.53  ? 236 LEU C N   1 
ATOM   5753  C CA  . LEU C 1 233 ? 38.868  -31.326 24.659  1.00 59.83  ? 236 LEU C CA  1 
ATOM   5754  C C   . LEU C 1 233 ? 38.615  -32.221 25.864  1.00 80.95  ? 236 LEU C C   1 
ATOM   5755  O O   . LEU C 1 233 ? 37.466  -32.478 26.229  1.00 78.95  ? 236 LEU C O   1 
ATOM   5756  C CB  . LEU C 1 233 ? 38.131  -30.009 24.855  1.00 63.32  ? 236 LEU C CB  1 
ATOM   5757  C CG  . LEU C 1 233 ? 38.858  -28.813 24.264  1.00 62.30  ? 236 LEU C CG  1 
ATOM   5758  C CD1 . LEU C 1 233 ? 39.036  -29.026 22.763  1.00 46.11  ? 236 LEU C CD1 1 
ATOM   5759  C CD2 . LEU C 1 233 ? 38.110  -27.524 24.563  1.00 61.98  ? 236 LEU C CD2 1 
ATOM   5760  N N   . LEU C 1 234 ? 39.696  -32.672 26.489  1.00 56.55  ? 237 LEU C N   1 
ATOM   5761  C CA  . LEU C 1 234 ? 39.600  -33.585 27.615  1.00 63.91  ? 237 LEU C CA  1 
ATOM   5762  C C   . LEU C 1 234 ? 39.515  -32.825 28.923  1.00 66.82  ? 237 LEU C C   1 
ATOM   5763  O O   . LEU C 1 234 ? 40.461  -32.149 29.314  1.00 66.45  ? 237 LEU C O   1 
ATOM   5764  C CB  . LEU C 1 234 ? 40.797  -34.534 27.631  1.00 73.33  ? 237 LEU C CB  1 
ATOM   5765  C CG  . LEU C 1 234 ? 40.720  -35.602 28.722  1.00 80.91  ? 237 LEU C CG  1 
ATOM   5766  C CD1 . LEU C 1 234 ? 39.297  -36.128 28.857  1.00 75.33  ? 237 LEU C CD1 1 
ATOM   5767  C CD2 . LEU C 1 234 ? 41.691  -36.721 28.427  1.00 83.69  ? 237 LEU C CD2 1 
ATOM   5768  N N   . ASP C 1 235 ? 38.378  -32.952 29.597  1.00 63.58  ? 238 ASP C N   1 
ATOM   5769  C CA  . ASP C 1 235 ? 38.102  -32.159 30.790  1.00 72.15  ? 238 ASP C CA  1 
ATOM   5770  C C   . ASP C 1 235 ? 39.100  -32.438 31.893  1.00 75.47  ? 238 ASP C C   1 
ATOM   5771  O O   . ASP C 1 235 ? 39.801  -33.443 31.870  1.00 76.36  ? 238 ASP C O   1 
ATOM   5772  C CB  . ASP C 1 235 ? 36.695  -32.436 31.311  1.00 78.35  ? 238 ASP C CB  1 
ATOM   5773  C CG  . ASP C 1 235 ? 35.635  -32.251 30.252  1.00 85.94  ? 238 ASP C CG  1 
ATOM   5774  O OD1 . ASP C 1 235 ? 35.987  -32.176 29.053  1.00 91.54  ? 238 ASP C OD1 1 
ATOM   5775  O OD2 . ASP C 1 235 ? 34.442  -32.197 30.621  1.00 88.17  ? 238 ASP C OD2 1 
ATOM   5776  N N   . MET C 1 236 ? 39.159  -31.537 32.863  1.00 79.99  ? 239 MET C N   1 
ATOM   5777  C CA  . MET C 1 236 ? 39.995  -31.758 34.026  1.00 87.73  ? 239 MET C CA  1 
ATOM   5778  C C   . MET C 1 236 ? 39.561  -33.055 34.693  1.00 87.35  ? 239 MET C C   1 
ATOM   5779  O O   . MET C 1 236 ? 38.381  -33.242 34.983  1.00 82.98  ? 239 MET C O   1 
ATOM   5780  C CB  . MET C 1 236 ? 39.877  -30.583 35.002  1.00 93.87  ? 239 MET C CB  1 
ATOM   5781  C CG  . MET C 1 236 ? 40.253  -29.240 34.395  1.00 91.90  ? 239 MET C CG  1 
ATOM   5782  S SD  . MET C 1 236 ? 40.539  -27.939 35.613  1.00 128.16 ? 239 MET C SD  1 
ATOM   5783  C CE  . MET C 1 236 ? 38.865  -27.537 36.115  1.00 51.88  ? 239 MET C CE  1 
ATOM   5784  N N   . TRP C 1 237 ? 40.515  -33.955 34.903  1.00 105.28 ? 240 TRP C N   1 
ATOM   5785  C CA  . TRP C 1 237 ? 40.288  -35.197 35.645  1.00 102.92 ? 240 TRP C CA  1 
ATOM   5786  C C   . TRP C 1 237 ? 39.749  -36.355 34.806  1.00 105.26 ? 240 TRP C C   1 
ATOM   5787  O O   . TRP C 1 237 ? 39.798  -37.508 35.231  1.00 106.97 ? 240 TRP C O   1 
ATOM   5788  C CB  . TRP C 1 237 ? 39.378  -34.963 36.856  1.00 99.42  ? 240 TRP C CB  1 
ATOM   5789  C CG  . TRP C 1 237 ? 39.788  -33.800 37.708  1.00 99.05  ? 240 TRP C CG  1 
ATOM   5790  C CD1 . TRP C 1 237 ? 38.964  -32.888 38.295  1.00 90.29  ? 240 TRP C CD1 1 
ATOM   5791  C CD2 . TRP C 1 237 ? 41.125  -33.416 38.055  1.00 109.95 ? 240 TRP C CD2 1 
ATOM   5792  N NE1 . TRP C 1 237 ? 39.703  -31.966 38.994  1.00 100.30 ? 240 TRP C NE1 1 
ATOM   5793  C CE2 . TRP C 1 237 ? 41.032  -32.269 38.861  1.00 114.54 ? 240 TRP C CE2 1 
ATOM   5794  C CE3 . TRP C 1 237 ? 42.390  -33.935 37.765  1.00 114.93 ? 240 TRP C CE3 1 
ATOM   5795  C CZ2 . TRP C 1 237 ? 42.154  -31.632 39.379  1.00 129.84 ? 240 TRP C CZ2 1 
ATOM   5796  C CZ3 . TRP C 1 237 ? 43.500  -33.301 38.282  1.00 122.96 ? 240 TRP C CZ3 1 
ATOM   5797  C CH2 . TRP C 1 237 ? 43.377  -32.162 39.077  1.00 135.86 ? 240 TRP C CH2 1 
ATOM   5798  N N   . ASP C 1 238 ? 39.227  -36.058 33.623  1.00 94.41  ? 241 ASP C N   1 
ATOM   5799  C CA  . ASP C 1 238 ? 38.762  -37.123 32.750  1.00 85.67  ? 241 ASP C CA  1 
ATOM   5800  C C   . ASP C 1 238 ? 39.952  -37.758 32.049  1.00 82.28  ? 241 ASP C C   1 
ATOM   5801  O O   . ASP C 1 238 ? 41.024  -37.169 31.971  1.00 81.50  ? 241 ASP C O   1 
ATOM   5802  C CB  . ASP C 1 238 ? 37.739  -36.608 31.738  1.00 77.98  ? 241 ASP C CB  1 
ATOM   5803  C CG  . ASP C 1 238 ? 37.064  -37.731 30.967  1.00 77.11  ? 241 ASP C CG  1 
ATOM   5804  O OD1 . ASP C 1 238 ? 37.081  -38.884 31.453  1.00 85.74  ? 241 ASP C OD1 1 
ATOM   5805  O OD2 . ASP C 1 238 ? 36.515  -37.461 29.877  1.00 67.93  ? 241 ASP C OD2 1 
ATOM   5806  N N   . THR C 1 239 ? 39.755  -38.967 31.546  1.00 61.58  ? 242 THR C N   1 
ATOM   5807  C CA  . THR C 1 239 ? 40.845  -39.744 30.985  1.00 68.34  ? 242 THR C CA  1 
ATOM   5808  C C   . THR C 1 239 ? 40.565  -40.065 29.523  1.00 60.60  ? 242 THR C C   1 
ATOM   5809  O O   . THR C 1 239 ? 39.415  -40.079 29.096  1.00 57.25  ? 242 THR C O   1 
ATOM   5810  C CB  . THR C 1 239 ? 41.020  -41.037 31.786  1.00 80.81  ? 242 THR C CB  1 
ATOM   5811  O OG1 . THR C 1 239 ? 41.107  -40.715 33.179  1.00 88.28  ? 242 THR C OG1 1 
ATOM   5812  C CG2 . THR C 1 239 ? 42.272  -41.773 31.360  1.00 90.47  ? 242 THR C CG2 1 
ATOM   5813  N N   . ILE C 1 240 ? 41.613  -40.306 28.748  1.00 76.20  ? 243 ILE C N   1 
ATOM   5814  C CA  . ILE C 1 240 ? 41.435  -40.601 27.335  1.00 70.70  ? 243 ILE C CA  1 
ATOM   5815  C C   . ILE C 1 240 ? 42.158  -41.875 26.938  1.00 77.06  ? 243 ILE C C   1 
ATOM   5816  O O   . ILE C 1 240 ? 43.376  -41.983 27.070  1.00 94.44  ? 243 ILE C O   1 
ATOM   5817  C CB  . ILE C 1 240 ? 41.923  -39.452 26.444  1.00 69.13  ? 243 ILE C CB  1 
ATOM   5818  C CG1 . ILE C 1 240 ? 41.798  -39.838 24.971  1.00 56.24  ? 243 ILE C CG1 1 
ATOM   5819  C CG2 . ILE C 1 240 ? 43.362  -39.103 26.767  1.00 72.18  ? 243 ILE C CG2 1 
ATOM   5820  C CD1 . ILE C 1 240 ? 42.314  -38.776 24.031  1.00 38.08  ? 243 ILE C CD1 1 
ATOM   5821  N N   . ASN C 1 241 ? 41.397  -42.840 26.443  1.00 68.35  ? 244 ASN C N   1 
ATOM   5822  C CA  . ASN C 1 241 ? 41.951  -44.141 26.123  1.00 72.08  ? 244 ASN C CA  1 
ATOM   5823  C C   . ASN C 1 241 ? 42.038  -44.385 24.630  1.00 52.02  ? 244 ASN C C   1 
ATOM   5824  O O   . ASN C 1 241 ? 41.020  -44.492 23.945  1.00 45.21  ? 244 ASN C O   1 
ATOM   5825  C CB  . ASN C 1 241 ? 41.133  -45.244 26.787  1.00 74.37  ? 244 ASN C CB  1 
ATOM   5826  C CG  . ASN C 1 241 ? 41.253  -45.224 28.294  1.00 84.06  ? 244 ASN C CG  1 
ATOM   5827  O OD1 . ASN C 1 241 ? 42.197  -45.775 28.858  1.00 94.94  ? 244 ASN C OD1 1 
ATOM   5828  N ND2 . ASN C 1 241 ? 40.294  -44.587 28.957  1.00 80.90  ? 244 ASN C ND2 1 
ATOM   5829  N N   . PHE C 1 242 ? 43.262  -44.466 24.125  1.00 85.64  ? 245 PHE C N   1 
ATOM   5830  C CA  . PHE C 1 242 ? 43.480  -44.886 22.753  1.00 69.78  ? 245 PHE C CA  1 
ATOM   5831  C C   . PHE C 1 242 ? 43.533  -46.410 22.706  1.00 78.88  ? 245 PHE C C   1 
ATOM   5832  O O   . PHE C 1 242 ? 43.875  -47.064 23.694  1.00 90.90  ? 245 PHE C O   1 
ATOM   5833  C CB  . PHE C 1 242 ? 44.777  -44.292 22.202  1.00 61.68  ? 245 PHE C CB  1 
ATOM   5834  C CG  . PHE C 1 242 ? 44.744  -42.799 22.044  1.00 59.33  ? 245 PHE C CG  1 
ATOM   5835  C CD1 . PHE C 1 242 ? 44.566  -42.223 20.794  1.00 52.16  ? 245 PHE C CD1 1 
ATOM   5836  C CD2 . PHE C 1 242 ? 44.890  -41.970 23.143  1.00 70.77  ? 245 PHE C CD2 1 
ATOM   5837  C CE1 . PHE C 1 242 ? 44.536  -40.840 20.650  1.00 51.02  ? 245 PHE C CE1 1 
ATOM   5838  C CE2 . PHE C 1 242 ? 44.860  -40.593 23.004  1.00 74.81  ? 245 PHE C CE2 1 
ATOM   5839  C CZ  . PHE C 1 242 ? 44.682  -40.029 21.757  1.00 60.52  ? 245 PHE C CZ  1 
ATOM   5840  N N   . GLU C 1 243 ? 43.183  -46.970 21.556  1.00 85.44  ? 246 GLU C N   1 
ATOM   5841  C CA  . GLU C 1 243 ? 43.192  -48.410 21.363  1.00 88.92  ? 246 GLU C CA  1 
ATOM   5842  C C   . GLU C 1 243 ? 43.039  -48.693 19.879  1.00 77.71  ? 246 GLU C C   1 
ATOM   5843  O O   . GLU C 1 243 ? 41.960  -48.507 19.319  1.00 75.83  ? 246 GLU C O   1 
ATOM   5844  C CB  . GLU C 1 243 ? 42.053  -49.069 22.148  1.00 89.83  ? 246 GLU C CB  1 
ATOM   5845  C CG  . GLU C 1 243 ? 41.906  -50.567 21.896  1.00 98.22  ? 246 GLU C CG  1 
ATOM   5846  C CD  . GLU C 1 243 ? 40.961  -51.244 22.870  1.00 109.66 ? 246 GLU C CD  1 
ATOM   5847  O OE1 . GLU C 1 243 ? 40.435  -50.560 23.771  1.00 106.99 ? 246 GLU C OE1 1 
ATOM   5848  O OE2 . GLU C 1 243 ? 40.748  -52.466 22.738  1.00 120.68 ? 246 GLU C OE2 1 
ATOM   5849  N N   . SER C 1 244 ? 44.115  -49.131 19.233  1.00 62.54  ? 247 SER C N   1 
ATOM   5850  C CA  . SER C 1 244 ? 44.053  -49.402 17.801  1.00 57.03  ? 247 SER C CA  1 
ATOM   5851  C C   . SER C 1 244 ? 44.779  -50.671 17.369  1.00 60.49  ? 247 SER C C   1 
ATOM   5852  O O   . SER C 1 244 ? 45.755  -51.093 17.992  1.00 66.01  ? 247 SER C O   1 
ATOM   5853  C CB  . SER C 1 244 ? 44.591  -48.215 17.007  1.00 59.16  ? 247 SER C CB  1 
ATOM   5854  O OG  . SER C 1 244 ? 44.924  -48.619 15.689  1.00 64.12  ? 247 SER C OG  1 
ATOM   5855  N N   . THR C 1 245 ? 44.292  -51.263 16.283  1.00 70.95  ? 248 THR C N   1 
ATOM   5856  C CA  . THR C 1 245 ? 44.921  -52.434 15.691  1.00 76.37  ? 248 THR C CA  1 
ATOM   5857  C C   . THR C 1 245 ? 45.783  -52.042 14.492  1.00 76.41  ? 248 THR C C   1 
ATOM   5858  O O   . THR C 1 245 ? 46.364  -52.899 13.833  1.00 78.66  ? 248 THR C O   1 
ATOM   5859  C CB  . THR C 1 245 ? 43.872  -53.488 15.256  1.00 85.86  ? 248 THR C CB  1 
ATOM   5860  O OG1 . THR C 1 245 ? 42.918  -52.885 14.371  1.00 89.46  ? 248 THR C OG1 1 
ATOM   5861  C CG2 . THR C 1 245 ? 43.141  -54.050 16.466  1.00 83.74  ? 248 THR C CG2 1 
ATOM   5862  N N   . GLY C 1 246 ? 45.867  -50.743 14.216  1.00 75.95  ? 249 GLY C N   1 
ATOM   5863  C CA  . GLY C 1 246 ? 46.689  -50.257 13.123  1.00 84.34  ? 249 GLY C CA  1 
ATOM   5864  C C   . GLY C 1 246 ? 46.263  -48.914 12.565  1.00 88.89  ? 249 GLY C C   1 
ATOM   5865  O O   . GLY C 1 246 ? 45.110  -48.509 12.700  1.00 90.82  ? 249 GLY C O   1 
ATOM   5866  N N   . ASN C 1 247 ? 47.209  -48.231 11.928  1.00 54.96  ? 250 ASN C N   1 
ATOM   5867  C CA  . ASN C 1 247 ? 46.987  -46.915 11.332  1.00 54.18  ? 250 ASN C CA  1 
ATOM   5868  C C   . ASN C 1 247 ? 46.841  -45.798 12.359  1.00 42.09  ? 250 ASN C C   1 
ATOM   5869  O O   . ASN C 1 247 ? 46.684  -44.635 11.988  1.00 46.61  ? 250 ASN C O   1 
ATOM   5870  C CB  . ASN C 1 247 ? 45.779  -46.912 10.393  1.00 61.03  ? 250 ASN C CB  1 
ATOM   5871  C CG  . ASN C 1 247 ? 45.810  -48.047 9.397   1.00 77.33  ? 250 ASN C CG  1 
ATOM   5872  O OD1 . ASN C 1 247 ? 45.982  -49.207 9.763   1.00 68.28  ? 250 ASN C OD1 1 
ATOM   5873  N ND2 . ASN C 1 247 ? 45.650  -47.716 8.123   1.00 96.99  ? 250 ASN C ND2 1 
ATOM   5874  N N   . LEU C 1 248 ? 46.879  -46.136 13.643  1.00 75.39  ? 251 LEU C N   1 
ATOM   5875  C CA  . LEU C 1 248 ? 46.746  -45.115 14.674  1.00 64.13  ? 251 LEU C CA  1 
ATOM   5876  C C   . LEU C 1 248 ? 47.969  -44.220 14.694  1.00 66.50  ? 251 LEU C C   1 
ATOM   5877  O O   . LEU C 1 248 ? 49.074  -44.693 14.950  1.00 73.89  ? 251 LEU C O   1 
ATOM   5878  C CB  . LEU C 1 248 ? 46.559  -45.740 16.052  1.00 48.51  ? 251 LEU C CB  1 
ATOM   5879  C CG  . LEU C 1 248 ? 47.047  -44.886 17.225  1.00 44.01  ? 251 LEU C CG  1 
ATOM   5880  C CD1 . LEU C 1 248 ? 46.191  -43.640 17.423  1.00 36.63  ? 251 LEU C CD1 1 
ATOM   5881  C CD2 . LEU C 1 248 ? 47.101  -45.704 18.507  1.00 53.12  ? 251 LEU C CD2 1 
ATOM   5882  N N   . ILE C 1 249 ? 47.766  -42.933 14.409  1.00 63.19  ? 252 ILE C N   1 
ATOM   5883  C CA  . ILE C 1 249 ? 48.815  -41.922 14.553  1.00 62.07  ? 252 ILE C CA  1 
ATOM   5884  C C   . ILE C 1 249 ? 48.640  -41.209 15.881  1.00 55.38  ? 252 ILE C C   1 
ATOM   5885  O O   . ILE C 1 249 ? 47.710  -40.426 16.059  1.00 46.05  ? 252 ILE C O   1 
ATOM   5886  C CB  . ILE C 1 249 ? 48.769  -40.868 13.445  1.00 61.36  ? 252 ILE C CB  1 
ATOM   5887  C CG1 . ILE C 1 249 ? 49.378  -41.415 12.154  1.00 71.65  ? 252 ILE C CG1 1 
ATOM   5888  C CG2 . ILE C 1 249 ? 49.523  -39.631 13.887  1.00 57.03  ? 252 ILE C CG2 1 
ATOM   5889  C CD1 . ILE C 1 249 ? 48.562  -42.497 11.495  1.00 78.00  ? 252 ILE C CD1 1 
ATOM   5890  N N   . ALA C 1 250 ? 49.546  -41.475 16.811  1.00 53.85  ? 253 ALA C N   1 
ATOM   5891  C CA  . ALA C 1 250 ? 49.349  -41.075 18.195  1.00 57.89  ? 253 ALA C CA  1 
ATOM   5892  C C   . ALA C 1 250 ? 49.717  -39.631 18.462  1.00 61.88  ? 253 ALA C C   1 
ATOM   5893  O O   . ALA C 1 250 ? 50.324  -38.970 17.619  1.00 70.50  ? 253 ALA C O   1 
ATOM   5894  C CB  . ALA C 1 250 ? 50.141  -41.986 19.118  1.00 67.56  ? 253 ALA C CB  1 
ATOM   5895  N N   . PRO C 1 251 ? 49.328  -39.135 19.642  1.00 72.19  ? 254 PRO C N   1 
ATOM   5896  C CA  . PRO C 1 251 ? 49.850  -37.889 20.196  1.00 79.52  ? 254 PRO C CA  1 
ATOM   5897  C C   . PRO C 1 251 ? 51.050  -38.177 21.096  1.00 99.96  ? 254 PRO C C   1 
ATOM   5898  O O   . PRO C 1 251 ? 51.164  -39.276 21.649  1.00 107.15 ? 254 PRO C O   1 
ATOM   5899  C CB  . PRO C 1 251 ? 48.686  -37.368 21.057  1.00 77.80  ? 254 PRO C CB  1 
ATOM   5900  C CG  . PRO C 1 251 ? 47.549  -38.338 20.863  1.00 69.79  ? 254 PRO C CG  1 
ATOM   5901  C CD  . PRO C 1 251 ? 48.164  -39.611 20.400  1.00 70.80  ? 254 PRO C CD  1 
ATOM   5902  N N   . GLU C 1 252 ? 51.939  -37.197 21.222  1.00 78.02  ? 255 GLU C N   1 
ATOM   5903  C CA  . GLU C 1 252 ? 53.002  -37.231 22.214  1.00 90.43  ? 255 GLU C CA  1 
ATOM   5904  C C   . GLU C 1 252 ? 52.670  -36.114 23.184  1.00 102.77 ? 255 GLU C C   1 
ATOM   5905  O O   . GLU C 1 252 ? 52.934  -36.205 24.383  1.00 118.94 ? 255 GLU C O   1 
ATOM   5906  C CB  . GLU C 1 252 ? 54.363  -36.987 21.551  1.00 89.65  ? 255 GLU C CB  1 
ATOM   5907  C CG  . GLU C 1 252 ? 55.576  -37.071 22.486  1.00 111.65 ? 255 GLU C CG  1 
ATOM   5908  C CD  . GLU C 1 252 ? 56.901  -36.794 21.770  1.00 118.46 ? 255 GLU C CD  1 
ATOM   5909  O OE1 . GLU C 1 252 ? 56.950  -36.900 20.523  1.00 104.42 ? 255 GLU C OE1 1 
ATOM   5910  O OE2 . GLU C 1 252 ? 57.894  -36.464 22.459  1.00 138.50 ? 255 GLU C OE2 1 
ATOM   5911  N N   . TYR C 1 253 ? 52.053  -35.065 22.645  1.00 82.09  ? 256 TYR C N   1 
ATOM   5912  C CA  . TYR C 1 253 ? 51.726  -33.882 23.430  1.00 90.05  ? 256 TYR C CA  1 
ATOM   5913  C C   . TYR C 1 253 ? 50.251  -33.499 23.373  1.00 81.86  ? 256 TYR C C   1 
ATOM   5914  O O   . TYR C 1 253 ? 49.544  -33.800 22.407  1.00 68.71  ? 256 TYR C O   1 
ATOM   5915  C CB  . TYR C 1 253 ? 52.575  -32.688 22.983  1.00 83.25  ? 256 TYR C CB  1 
ATOM   5916  C CG  . TYR C 1 253 ? 54.064  -32.896 23.127  1.00 90.50  ? 256 TYR C CG  1 
ATOM   5917  C CD1 . TYR C 1 253 ? 54.685  -32.784 24.364  1.00 106.14 ? 256 TYR C CD1 1 
ATOM   5918  C CD2 . TYR C 1 253 ? 54.851  -33.195 22.021  1.00 84.29  ? 256 TYR C CD2 1 
ATOM   5919  C CE1 . TYR C 1 253 ? 56.047  -32.972 24.499  1.00 110.58 ? 256 TYR C CE1 1 
ATOM   5920  C CE2 . TYR C 1 253 ? 56.216  -33.382 22.144  1.00 89.86  ? 256 TYR C CE2 1 
ATOM   5921  C CZ  . TYR C 1 253 ? 56.808  -33.269 23.386  1.00 101.59 ? 256 TYR C CZ  1 
ATOM   5922  O OH  . TYR C 1 253 ? 58.165  -33.457 23.513  1.00 107.79 ? 256 TYR C OH  1 
ATOM   5923  N N   . GLY C 1 254 ? 49.805  -32.839 24.436  1.00 84.82  ? 257 GLY C N   1 
ATOM   5924  C CA  . GLY C 1 254 ? 48.511  -32.193 24.469  1.00 81.72  ? 257 GLY C CA  1 
ATOM   5925  C C   . GLY C 1 254 ? 48.727  -30.697 24.600  1.00 91.81  ? 257 GLY C C   1 
ATOM   5926  O O   . GLY C 1 254 ? 49.840  -30.201 24.426  1.00 114.14 ? 257 GLY C O   1 
ATOM   5927  N N   . PHE C 1 255 ? 47.661  -29.971 24.906  1.00 85.71  ? 258 PHE C N   1 
ATOM   5928  C CA  . PHE C 1 255 ? 47.757  -28.539 25.110  1.00 93.09  ? 258 PHE C CA  1 
ATOM   5929  C C   . PHE C 1 255 ? 46.817  -28.119 26.219  1.00 115.80 ? 258 PHE C C   1 
ATOM   5930  O O   . PHE C 1 255 ? 45.607  -28.078 26.021  1.00 107.21 ? 258 PHE C O   1 
ATOM   5931  C CB  . PHE C 1 255 ? 47.356  -27.780 23.847  1.00 68.72  ? 258 PHE C CB  1 
ATOM   5932  C CG  . PHE C 1 255 ? 48.201  -28.086 22.649  1.00 61.94  ? 258 PHE C CG  1 
ATOM   5933  C CD1 . PHE C 1 255 ? 49.275  -27.281 22.318  1.00 58.91  ? 258 PHE C CD1 1 
ATOM   5934  C CD2 . PHE C 1 255 ? 47.909  -29.170 21.837  1.00 59.70  ? 258 PHE C CD2 1 
ATOM   5935  C CE1 . PHE C 1 255 ? 50.053  -27.552 21.204  1.00 49.17  ? 258 PHE C CE1 1 
ATOM   5936  C CE2 . PHE C 1 255 ? 48.680  -29.449 20.718  1.00 53.43  ? 258 PHE C CE2 1 
ATOM   5937  C CZ  . PHE C 1 255 ? 49.753  -28.632 20.396  1.00 48.15  ? 258 PHE C CZ  1 
ATOM   5938  N N   . LYS C 1 256 ? 47.360  -27.809 27.389  1.00 66.23  ? 259 LYS C N   1 
ATOM   5939  C CA  . LYS C 1 256 ? 46.558  -27.148 28.397  1.00 63.50  ? 259 LYS C CA  1 
ATOM   5940  C C   . LYS C 1 256 ? 46.010  -25.906 27.710  1.00 66.07  ? 259 LYS C C   1 
ATOM   5941  O O   . LYS C 1 256 ? 46.634  -25.391 26.780  1.00 71.04  ? 259 LYS C O   1 
ATOM   5942  C CB  . LYS C 1 256 ? 47.406  -26.759 29.601  1.00 62.38  ? 259 LYS C CB  1 
ATOM   5943  C CG  . LYS C 1 256 ? 48.051  -27.926 30.302  1.00 76.44  ? 259 LYS C CG  1 
ATOM   5944  C CD  . LYS C 1 256 ? 48.497  -27.533 31.689  1.00 89.73  ? 259 LYS C CD  1 
ATOM   5945  C CE  . LYS C 1 256 ? 49.309  -26.267 31.646  1.00 95.49  ? 259 LYS C CE  1 
ATOM   5946  N NZ  . LYS C 1 256 ? 49.678  -25.814 33.008  1.00 96.90  ? 259 LYS C NZ  1 
ATOM   5947  N N   . ILE C 1 257 ? 44.851  -25.423 28.147  1.00 86.45  ? 260 ILE C N   1 
ATOM   5948  C CA  . ILE C 1 257 ? 44.190  -24.351 27.415  1.00 76.22  ? 260 ILE C CA  1 
ATOM   5949  C C   . ILE C 1 257 ? 42.953  -23.836 28.135  1.00 81.40  ? 260 ILE C C   1 
ATOM   5950  O O   . ILE C 1 257 ? 42.080  -24.610 28.512  1.00 80.68  ? 260 ILE C O   1 
ATOM   5951  C CB  . ILE C 1 257 ? 43.811  -24.826 26.002  1.00 61.98  ? 260 ILE C CB  1 
ATOM   5952  C CG1 . ILE C 1 257 ? 43.337  -23.665 25.145  1.00 58.39  ? 260 ILE C CG1 1 
ATOM   5953  C CG2 . ILE C 1 257 ? 42.732  -25.872 26.065  1.00 54.80  ? 260 ILE C CG2 1 
ATOM   5954  C CD1 . ILE C 1 257 ? 41.922  -23.840 24.667  1.00 44.10  ? 260 ILE C CD1 1 
ATOM   5955  N N   . SER C 1 258 ? 42.898  -22.521 28.334  1.00 79.59  ? 261 SER C N   1 
ATOM   5956  C CA  . SER C 1 258 ? 41.766  -21.876 29.002  1.00 79.72  ? 261 SER C CA  1 
ATOM   5957  C C   . SER C 1 258 ? 41.177  -20.772 28.129  1.00 75.28  ? 261 SER C C   1 
ATOM   5958  O O   . SER C 1 258 ? 41.905  -20.075 27.427  1.00 68.08  ? 261 SER C O   1 
ATOM   5959  C CB  . SER C 1 258 ? 42.189  -21.300 30.355  1.00 89.53  ? 261 SER C CB  1 
ATOM   5960  O OG  . SER C 1 258 ? 41.111  -20.634 30.989  1.00 86.67  ? 261 SER C OG  1 
ATOM   5961  N N   . LYS C 1 259 ? 39.856  -20.619 28.178  1.00 106.64 ? 262 LYS C N   1 
ATOM   5962  C CA  . LYS C 1 259 ? 39.160  -19.646 27.341  1.00 103.55 ? 262 LYS C CA  1 
ATOM   5963  C C   . LYS C 1 259 ? 38.618  -18.480 28.155  1.00 115.34 ? 262 LYS C C   1 
ATOM   5964  O O   . LYS C 1 259 ? 38.335  -18.618 29.344  1.00 117.64 ? 262 LYS C O   1 
ATOM   5965  C CB  . LYS C 1 259 ? 38.005  -20.319 26.600  1.00 90.79  ? 262 LYS C CB  1 
ATOM   5966  C CG  . LYS C 1 259 ? 38.418  -21.257 25.477  1.00 80.27  ? 262 LYS C CG  1 
ATOM   5967  C CD  . LYS C 1 259 ? 38.816  -20.497 24.223  1.00 66.43  ? 262 LYS C CD  1 
ATOM   5968  C CE  . LYS C 1 259 ? 37.828  -19.382 23.902  1.00 62.27  ? 262 LYS C CE  1 
ATOM   5969  N NZ  . LYS C 1 259 ? 36.398  -19.820 23.924  1.00 53.99  ? 262 LYS C NZ  1 
ATOM   5970  N N   . ARG C 1 260 ? 38.470  -17.331 27.504  1.00 154.00 ? 263 ARG C N   1 
ATOM   5971  C CA  . ARG C 1 260 ? 37.890  -16.158 28.144  1.00 163.27 ? 263 ARG C CA  1 
ATOM   5972  C C   . ARG C 1 260 ? 36.814  -15.549 27.252  1.00 157.66 ? 263 ARG C C   1 
ATOM   5973  O O   . ARG C 1 260 ? 36.130  -14.600 27.639  1.00 160.82 ? 263 ARG C O   1 
ATOM   5974  C CB  . ARG C 1 260 ? 38.969  -15.117 28.445  1.00 174.40 ? 263 ARG C CB  1 
ATOM   5975  C CG  . ARG C 1 260 ? 38.975  -13.935 27.490  1.00 176.73 ? 263 ARG C CG  1 
ATOM   5976  C CD  . ARG C 1 260 ? 39.963  -12.874 27.937  1.00 188.64 ? 263 ARG C CD  1 
ATOM   5977  N NE  . ARG C 1 260 ? 41.342  -13.326 27.786  1.00 197.90 ? 263 ARG C NE  1 
ATOM   5978  C CZ  . ARG C 1 260 ? 42.067  -13.146 26.688  1.00 192.82 ? 263 ARG C CZ  1 
ATOM   5979  N NH1 . ARG C 1 260 ? 41.544  -12.518 25.643  1.00 181.50 ? 263 ARG C NH1 1 
ATOM   5980  N NH2 . ARG C 1 260 ? 43.314  -13.591 26.634  1.00 195.26 ? 263 ARG C NH2 1 
ATOM   5981  N N   . GLY C 1 261 A 36.670  -16.104 26.054  1.00 99.77  ? 263 GLY C N   1 
ATOM   5982  C CA  . GLY C 1 261 A 35.704  -15.605 25.094  1.00 85.49  ? 263 GLY C CA  1 
ATOM   5983  C C   . GLY C 1 261 A 36.252  -15.669 23.683  1.00 77.08  ? 263 GLY C C   1 
ATOM   5984  O O   . GLY C 1 261 A 37.432  -15.404 23.449  1.00 81.92  ? 263 GLY C O   1 
ATOM   5985  N N   . SER C 1 262 ? 35.391  -16.020 22.738  1.00 104.92 ? 265 SER C N   1 
ATOM   5986  C CA  . SER C 1 262 ? 35.816  -16.198 21.360  1.00 87.79  ? 265 SER C CA  1 
ATOM   5987  C C   . SER C 1 262 ? 36.440  -14.936 20.784  1.00 77.43  ? 265 SER C C   1 
ATOM   5988  O O   . SER C 1 262 ? 36.366  -13.860 21.373  1.00 89.83  ? 265 SER C O   1 
ATOM   5989  C CB  . SER C 1 262 ? 34.641  -16.644 20.491  1.00 93.17  ? 265 SER C CB  1 
ATOM   5990  O OG  . SER C 1 262 ? 34.168  -17.913 20.903  1.00 104.40 ? 265 SER C OG  1 
ATOM   5991  N N   . SER C 1 263 ? 37.061  -15.096 19.622  1.00 53.06  ? 266 SER C N   1 
ATOM   5992  C CA  . SER C 1 263 ? 37.677  -14.007 18.888  1.00 47.32  ? 266 SER C CA  1 
ATOM   5993  C C   . SER C 1 263 ? 37.490  -14.278 17.402  1.00 46.14  ? 266 SER C C   1 
ATOM   5994  O O   . SER C 1 263 ? 36.367  -14.514 16.941  1.00 57.01  ? 266 SER C O   1 
ATOM   5995  C CB  . SER C 1 263 ? 39.162  -13.927 19.223  1.00 66.52  ? 266 SER C CB  1 
ATOM   5996  O OG  . SER C 1 263 ? 39.833  -13.022 18.367  1.00 76.77  ? 266 SER C OG  1 
ATOM   5997  N N   . GLY C 1 264 ? 38.589  -14.262 16.656  1.00 46.51  ? 267 GLY C N   1 
ATOM   5998  C CA  . GLY C 1 264 ? 38.534  -14.541 15.235  1.00 56.45  ? 267 GLY C CA  1 
ATOM   5999  C C   . GLY C 1 264 ? 39.900  -14.639 14.600  1.00 63.36  ? 267 GLY C C   1 
ATOM   6000  O O   . GLY C 1 264 ? 40.890  -14.220 15.188  1.00 70.41  ? 267 GLY C O   1 
ATOM   6001  N N   . ILE C 1 265 ? 39.946  -15.204 13.399  1.00 55.00  ? 268 ILE C N   1 
ATOM   6002  C CA  . ILE C 1 265 ? 41.175  -15.254 12.623  1.00 70.35  ? 268 ILE C CA  1 
ATOM   6003  C C   . ILE C 1 265 ? 41.172  -14.130 11.598  1.00 88.66  ? 268 ILE C C   1 
ATOM   6004  O O   . ILE C 1 265 ? 40.149  -13.871 10.956  1.00 106.30 ? 268 ILE C O   1 
ATOM   6005  C CB  . ILE C 1 265 ? 41.340  -16.605 11.889  1.00 58.74  ? 268 ILE C CB  1 
ATOM   6006  C CG1 . ILE C 1 265 ? 42.055  -17.624 12.782  1.00 48.91  ? 268 ILE C CG1 1 
ATOM   6007  C CG2 . ILE C 1 265 ? 42.120  -16.426 10.593  1.00 71.45  ? 268 ILE C CG2 1 
ATOM   6008  C CD1 . ILE C 1 265 ? 41.300  -17.971 14.044  1.00 41.89  ? 268 ILE C CD1 1 
ATOM   6009  N N   . MET C 1 266 ? 42.315  -13.460 11.453  1.00 55.79  ? 269 MET C N   1 
ATOM   6010  C CA  . MET C 1 266 ? 42.473  -12.433 10.425  1.00 77.53  ? 269 MET C CA  1 
ATOM   6011  C C   . MET C 1 266 ? 43.494  -12.837 9.379   1.00 94.83  ? 269 MET C C   1 
ATOM   6012  O O   . MET C 1 266 ? 44.664  -13.050 9.688   1.00 103.97 ? 269 MET C O   1 
ATOM   6013  C CB  . MET C 1 266 ? 42.865  -11.091 11.039  1.00 79.70  ? 269 MET C CB  1 
ATOM   6014  C CG  . MET C 1 266 ? 43.157  -10.022 10.003  1.00 96.85  ? 269 MET C CG  1 
ATOM   6015  S SD  . MET C 1 266 ? 43.387  -8.381  10.710  1.00 102.44 ? 269 MET C SD  1 
ATOM   6016  C CE  . MET C 1 266 ? 41.719  -7.996  11.229  1.00 76.99  ? 269 MET C CE  1 
ATOM   6017  N N   . LYS C 1 267 ? 43.036  -12.939 8.138   1.00 55.45  ? 270 LYS C N   1 
ATOM   6018  C CA  . LYS C 1 267 ? 43.900  -13.295 7.023   1.00 69.09  ? 270 LYS C CA  1 
ATOM   6019  C C   . LYS C 1 267 ? 44.739  -12.098 6.575   1.00 92.78  ? 270 LYS C C   1 
ATOM   6020  O O   . LYS C 1 267 ? 44.284  -11.273 5.781   1.00 100.47 ? 270 LYS C O   1 
ATOM   6021  C CB  . LYS C 1 267 ? 43.069  -13.816 5.847   1.00 65.13  ? 270 LYS C CB  1 
ATOM   6022  C CG  . LYS C 1 267 ? 42.227  -15.050 6.152   1.00 61.91  ? 270 LYS C CG  1 
ATOM   6023  C CD  . LYS C 1 267 ? 43.092  -16.259 6.466   1.00 72.97  ? 270 LYS C CD  1 
ATOM   6024  C CE  . LYS C 1 267 ? 42.545  -17.516 5.806   1.00 68.06  ? 270 LYS C CE  1 
ATOM   6025  N NZ  . LYS C 1 267 ? 43.365  -18.723 6.136   1.00 68.52  ? 270 LYS C NZ  1 
ATOM   6026  N N   . THR C 1 268 ? 45.965  -12.012 7.084   1.00 91.71  ? 271 THR C N   1 
ATOM   6027  C CA  . THR C 1 268 ? 46.873  -10.929 6.721   1.00 99.37  ? 271 THR C CA  1 
ATOM   6028  C C   . THR C 1 268 ? 48.213  -11.454 6.211   1.00 107.28 ? 271 THR C C   1 
ATOM   6029  O O   . THR C 1 268 ? 48.595  -12.593 6.490   1.00 105.97 ? 271 THR C O   1 
ATOM   6030  C CB  . THR C 1 268 ? 47.142  -10.000 7.917   1.00 101.51 ? 271 THR C CB  1 
ATOM   6031  O OG1 . THR C 1 268 ? 47.906  -8.866  7.485   1.00 113.30 ? 271 THR C OG1 1 
ATOM   6032  C CG2 . THR C 1 268 ? 47.910  -10.742 9.003   1.00 98.28  ? 271 THR C CG2 1 
ATOM   6033  N N   . GLU C 1 269 ? 48.923  -10.617 5.461   1.00 89.66  ? 272 GLU C N   1 
ATOM   6034  C CA  . GLU C 1 269 ? 50.265  -10.951 5.001   1.00 103.01 ? 272 GLU C CA  1 
ATOM   6035  C C   . GLU C 1 269 ? 51.286  -10.249 5.882   1.00 99.58  ? 272 GLU C C   1 
ATOM   6036  O O   . GLU C 1 269 ? 52.380  -10.760 6.113   1.00 103.28 ? 272 GLU C O   1 
ATOM   6037  C CB  . GLU C 1 269 ? 50.458  -10.539 3.539   1.00 117.05 ? 272 GLU C CB  1 
ATOM   6038  C CG  . GLU C 1 269 ? 49.604  -11.315 2.546   1.00 118.50 ? 272 GLU C CG  1 
ATOM   6039  C CD  . GLU C 1 269 ? 50.100  -12.736 2.327   1.00 122.21 ? 272 GLU C CD  1 
ATOM   6040  O OE1 . GLU C 1 269 ? 51.279  -13.012 2.643   1.00 127.07 ? 272 GLU C OE1 1 
ATOM   6041  O OE2 . GLU C 1 269 ? 49.311  -13.578 1.840   1.00 117.32 ? 272 GLU C OE2 1 
ATOM   6042  N N   . GLY C 1 270 ? 50.909  -9.078  6.382   1.00 98.56  ? 273 GLY C N   1 
ATOM   6043  C CA  . GLY C 1 270 ? 51.794  -8.266  7.195   1.00 98.24  ? 273 GLY C CA  1 
ATOM   6044  C C   . GLY C 1 270 ? 52.214  -8.950  8.476   1.00 91.63  ? 273 GLY C C   1 
ATOM   6045  O O   . GLY C 1 270 ? 51.833  -10.089 8.731   1.00 94.56  ? 273 GLY C O   1 
ATOM   6046  N N   . THR C 1 271 ? 53.003  -8.249  9.280   1.00 107.18 ? 274 THR C N   1 
ATOM   6047  C CA  . THR C 1 271 ? 53.496  -8.789  10.539  1.00 85.85  ? 274 THR C CA  1 
ATOM   6048  C C   . THR C 1 271 ? 53.101  -7.865  11.683  1.00 71.72  ? 274 THR C C   1 
ATOM   6049  O O   . THR C 1 271 ? 52.459  -6.842  11.459  1.00 76.15  ? 274 THR C O   1 
ATOM   6050  C CB  . THR C 1 271 ? 55.028  -8.958  10.515  1.00 72.07  ? 274 THR C CB  1 
ATOM   6051  O OG1 . THR C 1 271 ? 55.657  -7.687  10.711  1.00 93.38  ? 274 THR C OG1 1 
ATOM   6052  C CG2 . THR C 1 271 ? 55.485  -9.547  9.182   1.00 80.11  ? 274 THR C CG2 1 
ATOM   6053  N N   . LEU C 1 272 ? 53.487  -8.213  12.904  1.00 100.61 ? 275 LEU C N   1 
ATOM   6054  C CA  . LEU C 1 272 ? 53.052  -7.452  14.072  1.00 87.99  ? 275 LEU C CA  1 
ATOM   6055  C C   . LEU C 1 272 ? 54.031  -6.361  14.497  1.00 96.80  ? 275 LEU C C   1 
ATOM   6056  O O   . LEU C 1 272 ? 55.234  -6.606  14.601  1.00 102.02 ? 275 LEU C O   1 
ATOM   6057  C CB  . LEU C 1 272 ? 52.780  -8.385  15.252  1.00 71.87  ? 275 LEU C CB  1 
ATOM   6058  C CG  . LEU C 1 272 ? 52.460  -7.679  16.575  1.00 70.22  ? 275 LEU C CG  1 
ATOM   6059  C CD1 . LEU C 1 272 ? 51.696  -8.595  17.495  1.00 68.74  ? 275 LEU C CD1 1 
ATOM   6060  C CD2 . LEU C 1 272 ? 53.722  -7.165  17.267  1.00 80.15  ? 275 LEU C CD2 1 
ATOM   6061  N N   . GLU C 1 273 ? 53.500  -5.168  14.774  1.00 81.11  ? 276 GLU C N   1 
ATOM   6062  C CA  . GLU C 1 273 ? 54.310  -4.044  15.256  1.00 83.60  ? 276 GLU C CA  1 
ATOM   6063  C C   . GLU C 1 273 ? 54.018  -3.744  16.726  1.00 81.56  ? 276 GLU C C   1 
ATOM   6064  O O   . GLU C 1 273 ? 53.067  -4.282  17.294  1.00 73.74  ? 276 GLU C O   1 
ATOM   6065  C CB  . GLU C 1 273 ? 54.089  -2.803  14.387  1.00 87.86  ? 276 GLU C CB  1 
ATOM   6066  C CG  . GLU C 1 273 ? 54.366  -3.050  12.912  1.00 105.82 ? 276 GLU C CG  1 
ATOM   6067  C CD  . GLU C 1 273 ? 54.273  -1.794  12.078  1.00 128.68 ? 276 GLU C CD  1 
ATOM   6068  O OE1 . GLU C 1 273 ? 54.359  -0.690  12.657  1.00 127.49 ? 276 GLU C OE1 1 
ATOM   6069  O OE2 . GLU C 1 273 ? 54.111  -1.913  10.844  1.00 149.32 ? 276 GLU C OE2 1 
ATOM   6070  N N   . ASN C 1 274 ? 54.843  -2.903  17.347  1.00 87.97  ? 277 ASN C N   1 
ATOM   6071  C CA  . ASN C 1 274 ? 54.671  -2.604  18.769  1.00 94.23  ? 277 ASN C CA  1 
ATOM   6072  C C   . ASN C 1 274 ? 53.706  -1.447  19.014  1.00 96.72  ? 277 ASN C C   1 
ATOM   6073  O O   . ASN C 1 274 ? 54.117  -0.294  19.128  1.00 102.81 ? 277 ASN C O   1 
ATOM   6074  C CB  . ASN C 1 274 ? 56.017  -2.339  19.455  1.00 102.21 ? 277 ASN C CB  1 
ATOM   6075  C CG  . ASN C 1 274 ? 55.882  -2.155  20.965  1.00 110.48 ? 277 ASN C CG  1 
ATOM   6076  O OD1 . ASN C 1 274 ? 54.787  -2.243  21.521  1.00 113.20 ? 277 ASN C OD1 1 
ATOM   6077  N ND2 . ASN C 1 274 ? 57.003  -1.909  21.631  1.00 119.38 ? 277 ASN C ND2 1 
ATOM   6078  N N   . CYS C 1 275 ? 52.421  -1.773  19.103  1.00 111.18 ? 278 CYS C N   1 
ATOM   6079  C CA  . CYS C 1 275 ? 51.380  -0.771  19.291  1.00 111.28 ? 278 CYS C CA  1 
ATOM   6080  C C   . CYS C 1 275 ? 50.166  -1.339  20.019  1.00 107.83 ? 278 CYS C C   1 
ATOM   6081  O O   . CYS C 1 275 ? 50.119  -2.520  20.356  1.00 106.24 ? 278 CYS C O   1 
ATOM   6082  C CB  . CYS C 1 275 ? 50.960  -0.178  17.945  1.00 112.63 ? 278 CYS C CB  1 
ATOM   6083  S SG  . CYS C 1 275 ? 50.701  -1.396  16.639  1.00 114.33 ? 278 CYS C SG  1 
ATOM   6084  N N   . GLU C 1 276 ? 49.187  -0.479  20.260  1.00 99.79  ? 279 GLU C N   1 
ATOM   6085  C CA  . GLU C 1 276 ? 47.981  -0.849  20.984  1.00 97.55  ? 279 GLU C CA  1 
ATOM   6086  C C   . GLU C 1 276 ? 46.766  -0.520  20.122  1.00 95.24  ? 279 GLU C C   1 
ATOM   6087  O O   . GLU C 1 276 ? 46.896  0.144   19.093  1.00 103.09 ? 279 GLU C O   1 
ATOM   6088  C CB  . GLU C 1 276 ? 47.933  -0.100  22.318  1.00 107.09 ? 279 GLU C CB  1 
ATOM   6089  C CG  . GLU C 1 276 ? 46.546  0.128   22.883  1.00 109.52 ? 279 GLU C CG  1 
ATOM   6090  C CD  . GLU C 1 276 ? 45.892  -1.147  23.357  1.00 111.16 ? 279 GLU C CD  1 
ATOM   6091  O OE1 . GLU C 1 276 ? 46.618  -2.138  23.582  1.00 117.70 ? 279 GLU C OE1 1 
ATOM   6092  O OE2 . GLU C 1 276 ? 44.650  -1.161  23.502  1.00 103.30 ? 279 GLU C OE2 1 
ATOM   6093  N N   . THR C 1 277 ? 45.595  -1.003  20.523  1.00 83.18  ? 280 THR C N   1 
ATOM   6094  C CA  . THR C 1 277 ? 44.366  -0.723  19.790  1.00 76.63  ? 280 THR C CA  1 
ATOM   6095  C C   . THR C 1 277 ? 43.148  -1.424  20.382  1.00 70.57  ? 280 THR C C   1 
ATOM   6096  O O   . THR C 1 277 ? 43.242  -2.516  20.938  1.00 66.82  ? 280 THR C O   1 
ATOM   6097  C CB  . THR C 1 277 ? 44.478  -1.096  18.299  1.00 77.61  ? 280 THR C CB  1 
ATOM   6098  O OG1 . THR C 1 277 ? 43.267  -0.738  17.625  1.00 83.51  ? 280 THR C OG1 1 
ATOM   6099  C CG2 . THR C 1 277 ? 44.724  -2.586  18.132  1.00 71.33  ? 280 THR C CG2 1 
ATOM   6100  N N   . LYS C 1 278 ? 42.002  -0.774  20.243  1.00 96.31  ? 281 LYS C N   1 
ATOM   6101  C CA  . LYS C 1 278 ? 40.744  -1.268  20.775  1.00 105.47 ? 281 LYS C CA  1 
ATOM   6102  C C   . LYS C 1 278 ? 39.950  -1.945  19.664  1.00 91.43  ? 281 LYS C C   1 
ATOM   6103  O O   . LYS C 1 278 ? 39.003  -2.690  19.918  1.00 90.41  ? 281 LYS C O   1 
ATOM   6104  C CB  . LYS C 1 278 ? 39.961  -0.095  21.370  1.00 122.16 ? 281 LYS C CB  1 
ATOM   6105  C CG  . LYS C 1 278 ? 38.454  -0.256  21.376  1.00 132.21 ? 281 LYS C CG  1 
ATOM   6106  C CD  . LYS C 1 278 ? 37.783  1.018   21.860  1.00 142.90 ? 281 LYS C CD  1 
ATOM   6107  C CE  . LYS C 1 278 ? 38.384  1.470   23.176  1.00 152.17 ? 281 LYS C CE  1 
ATOM   6108  N NZ  . LYS C 1 278 ? 38.403  0.359   24.166  1.00 154.28 ? 281 LYS C NZ  1 
ATOM   6109  N N   . CYS C 1 279 ? 40.361  -1.687  18.428  1.00 70.59  ? 282 CYS C N   1 
ATOM   6110  C CA  . CYS C 1 279 ? 39.677  -2.209  17.255  1.00 60.74  ? 282 CYS C CA  1 
ATOM   6111  C C   . CYS C 1 279 ? 40.672  -2.371  16.108  1.00 67.19  ? 282 CYS C C   1 
ATOM   6112  O O   . CYS C 1 279 ? 41.489  -1.486  15.866  1.00 71.64  ? 282 CYS C O   1 
ATOM   6113  C CB  . CYS C 1 279 ? 38.543  -1.272  16.852  1.00 60.31  ? 282 CYS C CB  1 
ATOM   6114  S SG  . CYS C 1 279 ? 37.981  -1.496  15.164  1.00 75.37  ? 282 CYS C SG  1 
ATOM   6115  N N   . GLN C 1 280 ? 40.601  -3.496  15.400  1.00 53.95  ? 283 GLN C N   1 
ATOM   6116  C CA  . GLN C 1 280 ? 41.645  -3.848  14.444  1.00 56.49  ? 283 GLN C CA  1 
ATOM   6117  C C   . GLN C 1 280 ? 41.130  -4.293  13.078  1.00 64.68  ? 283 GLN C C   1 
ATOM   6118  O O   . GLN C 1 280 ? 40.075  -4.913  12.976  1.00 67.13  ? 283 GLN C O   1 
ATOM   6119  C CB  . GLN C 1 280 ? 42.526  -4.941  15.031  1.00 47.93  ? 283 GLN C CB  1 
ATOM   6120  C CG  . GLN C 1 280 ? 43.517  -5.518  14.040  1.00 60.02  ? 283 GLN C CG  1 
ATOM   6121  C CD  . GLN C 1 280 ? 44.626  -4.556  13.719  1.00 73.49  ? 283 GLN C CD  1 
ATOM   6122  O OE1 . GLN C 1 280 ? 45.254  -4.000  14.618  1.00 74.21  ? 283 GLN C OE1 1 
ATOM   6123  N NE2 . GLN C 1 280 ? 44.874  -4.345  12.435  1.00 86.51  ? 283 GLN C NE2 1 
ATOM   6124  N N   . THR C 1 281 ? 41.896  -3.987  12.033  1.00 36.09  ? 284 THR C N   1 
ATOM   6125  C CA  . THR C 1 281 ? 41.512  -4.322  10.663  1.00 46.92  ? 284 THR C CA  1 
ATOM   6126  C C   . THR C 1 281 ? 42.717  -4.809  9.863   1.00 62.34  ? 284 THR C C   1 
ATOM   6127  O O   . THR C 1 281 ? 43.859  -4.573  10.248  1.00 67.91  ? 284 THR C O   1 
ATOM   6128  C CB  . THR C 1 281 ? 40.876  -3.108  9.914   1.00 58.20  ? 284 THR C CB  1 
ATOM   6129  O OG1 . THR C 1 281 ? 41.889  -2.382  9.205   1.00 64.58  ? 284 THR C OG1 1 
ATOM   6130  C CG2 . THR C 1 281 ? 40.168  -2.174  10.880  1.00 50.90  ? 284 THR C CG2 1 
ATOM   6131  N N   . PRO C 1 282 ? 42.461  -5.489  8.738   1.00 66.21  ? 285 PRO C N   1 
ATOM   6132  C CA  . PRO C 1 282 ? 43.534  -5.938  7.851   1.00 74.05  ? 285 PRO C CA  1 
ATOM   6133  C C   . PRO C 1 282 ? 44.442  -4.787  7.417   1.00 85.42  ? 285 PRO C C   1 
ATOM   6134  O O   . PRO C 1 282 ? 45.658  -4.975  7.335   1.00 100.42 ? 285 PRO C O   1 
ATOM   6135  C CB  . PRO C 1 282 ? 42.772  -6.489  6.644   1.00 73.89  ? 285 PRO C CB  1 
ATOM   6136  C CG  . PRO C 1 282 ? 41.463  -6.906  7.194   1.00 63.26  ? 285 PRO C CG  1 
ATOM   6137  C CD  . PRO C 1 282 ? 41.136  -5.902  8.249   1.00 58.33  ? 285 PRO C CD  1 
ATOM   6138  N N   . LEU C 1 283 ? 43.860  -3.620  7.148   1.00 69.33  ? 286 LEU C N   1 
ATOM   6139  C CA  . LEU C 1 283 ? 44.628  -2.447  6.716   1.00 75.77  ? 286 LEU C CA  1 
ATOM   6140  C C   . LEU C 1 283 ? 45.420  -1.818  7.860   1.00 77.62  ? 286 LEU C C   1 
ATOM   6141  O O   . LEU C 1 283 ? 46.537  -1.342  7.665   1.00 86.02  ? 286 LEU C O   1 
ATOM   6142  C CB  . LEU C 1 283 ? 43.712  -1.391  6.096   1.00 62.48  ? 286 LEU C CB  1 
ATOM   6143  C CG  . LEU C 1 283 ? 42.635  -1.932  5.162   1.00 53.73  ? 286 LEU C CG  1 
ATOM   6144  C CD1 . LEU C 1 283 ? 42.014  -0.814  4.345   1.00 44.66  ? 286 LEU C CD1 1 
ATOM   6145  C CD2 . LEU C 1 283 ? 43.214  -3.016  4.257   1.00 57.62  ? 286 LEU C CD2 1 
ATOM   6146  N N   . GLY C 1 284 ? 44.831  -1.807  9.049   1.00 69.88  ? 287 GLY C N   1 
ATOM   6147  C CA  . GLY C 1 284 ? 45.491  -1.253  10.213  1.00 60.80  ? 287 GLY C CA  1 
ATOM   6148  C C   . GLY C 1 284 ? 44.490  -0.992  11.315  1.00 50.11  ? 287 GLY C C   1 
ATOM   6149  O O   . GLY C 1 284 ? 43.281  -1.079  11.096  1.00 53.16  ? 287 GLY C O   1 
ATOM   6150  N N   . ALA C 1 285 ? 44.988  -0.662  12.501  1.00 76.33  ? 288 ALA C N   1 
ATOM   6151  C CA  . ALA C 1 285 ? 44.128  -0.480  13.663  1.00 66.31  ? 288 ALA C CA  1 
ATOM   6152  C C   . ALA C 1 285 ? 43.346  0.829   13.634  1.00 74.51  ? 288 ALA C C   1 
ATOM   6153  O O   . ALA C 1 285 ? 43.741  1.799   12.989  1.00 93.32  ? 288 ALA C O   1 
ATOM   6154  C CB  . ALA C 1 285 ? 44.939  -0.579  14.941  1.00 65.13  ? 288 ALA C CB  1 
ATOM   6155  N N   . ILE C 1 286 ? 42.230  0.844   14.350  1.00 60.34  ? 289 ILE C N   1 
ATOM   6156  C CA  . ILE C 1 286 ? 41.374  2.013   14.402  1.00 65.69  ? 289 ILE C CA  1 
ATOM   6157  C C   . ILE C 1 286 ? 41.336  2.581   15.809  1.00 70.12  ? 289 ILE C C   1 
ATOM   6158  O O   . ILE C 1 286 ? 41.230  1.844   16.791  1.00 66.13  ? 289 ILE C O   1 
ATOM   6159  C CB  . ILE C 1 286 ? 39.940  1.691   13.961  1.00 63.80  ? 289 ILE C CB  1 
ATOM   6160  C CG1 . ILE C 1 286 ? 39.853  1.610   12.437  1.00 66.89  ? 289 ILE C CG1 1 
ATOM   6161  C CG2 . ILE C 1 286 ? 38.986  2.746   14.474  1.00 62.61  ? 289 ILE C CG2 1 
ATOM   6162  C CD1 . ILE C 1 286 ? 38.480  1.240   11.935  1.00 56.28  ? 289 ILE C CD1 1 
ATOM   6163  N N   . ASN C 1 287 ? 41.451  3.900   15.896  1.00 82.43  ? 290 ASN C N   1 
ATOM   6164  C CA  . ASN C 1 287 ? 41.300  4.610   17.151  1.00 85.96  ? 290 ASN C CA  1 
ATOM   6165  C C   . ASN C 1 287 ? 40.361  5.762   16.896  1.00 82.11  ? 290 ASN C C   1 
ATOM   6166  O O   . ASN C 1 287 ? 40.741  6.751   16.268  1.00 84.91  ? 290 ASN C O   1 
ATOM   6167  C CB  . ASN C 1 287 ? 42.639  5.132   17.652  1.00 101.14 ? 290 ASN C CB  1 
ATOM   6168  C CG  . ASN C 1 287 ? 42.578  5.577   19.087  1.00 109.26 ? 290 ASN C CG  1 
ATOM   6169  O OD1 . ASN C 1 287 ? 41.567  5.384   19.765  1.00 109.48 ? 290 ASN C OD1 1 
ATOM   6170  N ND2 . ASN C 1 287 ? 43.671  6.162   19.572  1.00 113.13 ? 290 ASN C ND2 1 
ATOM   6171  N N   . THR C 1 288 ? 39.129  5.626   17.372  1.00 73.79  ? 291 THR C N   1 
ATOM   6172  C CA  . THR C 1 288 ? 38.076  6.563   17.022  1.00 77.01  ? 291 THR C CA  1 
ATOM   6173  C C   . THR C 1 288 ? 36.989  6.526   18.087  1.00 76.23  ? 291 THR C C   1 
ATOM   6174  O O   . THR C 1 288 ? 37.121  5.830   19.093  1.00 77.19  ? 291 THR C O   1 
ATOM   6175  C CB  . THR C 1 288 ? 37.476  6.215   15.635  1.00 77.51  ? 291 THR C CB  1 
ATOM   6176  O OG1 . THR C 1 288 ? 36.513  7.204   15.244  1.00 72.28  ? 291 THR C OG1 1 
ATOM   6177  C CG2 . THR C 1 288 ? 36.810  4.844   15.669  1.00 75.60  ? 291 THR C CG2 1 
ATOM   6178  N N   . THR C 1 289 ? 35.924  7.287   17.869  1.00 97.30  ? 292 THR C N   1 
ATOM   6179  C CA  . THR C 1 289 ? 34.784  7.275   18.770  1.00 94.24  ? 292 THR C CA  1 
ATOM   6180  C C   . THR C 1 289 ? 33.512  7.447   17.961  1.00 93.69  ? 292 THR C C   1 
ATOM   6181  O O   . THR C 1 289 ? 32.414  7.180   18.447  1.00 98.46  ? 292 THR C O   1 
ATOM   6182  C CB  . THR C 1 289 ? 34.864  8.402   19.809  1.00 95.71  ? 292 THR C CB  1 
ATOM   6183  O OG1 . THR C 1 289 ? 36.236  8.729   20.062  1.00 100.51 ? 292 THR C OG1 1 
ATOM   6184  C CG2 . THR C 1 289 ? 34.189  7.973   21.106  1.00 95.62  ? 292 THR C CG2 1 
ATOM   6185  N N   . LEU C 1 290 ? 33.669  7.894   16.720  1.00 74.65  ? 293 LEU C N   1 
ATOM   6186  C CA  . LEU C 1 290 ? 32.531  8.101   15.837  1.00 65.13  ? 293 LEU C CA  1 
ATOM   6187  C C   . LEU C 1 290 ? 31.644  6.863   15.812  1.00 60.19  ? 293 LEU C C   1 
ATOM   6188  O O   . LEU C 1 290 ? 32.114  5.751   16.038  1.00 61.58  ? 293 LEU C O   1 
ATOM   6189  C CB  . LEU C 1 290 ? 33.006  8.431   14.423  1.00 61.97  ? 293 LEU C CB  1 
ATOM   6190  C CG  . LEU C 1 290 ? 34.089  9.504   14.294  1.00 60.58  ? 293 LEU C CG  1 
ATOM   6191  C CD1 . LEU C 1 290 ? 34.458  9.709   12.835  1.00 73.98  ? 293 LEU C CD1 1 
ATOM   6192  C CD2 . LEU C 1 290 ? 33.626  10.802  14.908  1.00 52.95  ? 293 LEU C CD2 1 
ATOM   6193  N N   . PRO C 1 291 ? 30.347  7.056   15.561  1.00 81.43  ? 294 PRO C N   1 
ATOM   6194  C CA  . PRO C 1 291 ? 29.420  5.927   15.462  1.00 79.70  ? 294 PRO C CA  1 
ATOM   6195  C C   . PRO C 1 291 ? 29.782  4.960   14.343  1.00 77.42  ? 294 PRO C C   1 
ATOM   6196  O O   . PRO C 1 291 ? 29.610  3.760   14.526  1.00 78.69  ? 294 PRO C O   1 
ATOM   6197  C CB  . PRO C 1 291 ? 28.087  6.606   15.153  1.00 75.85  ? 294 PRO C CB  1 
ATOM   6198  C CG  . PRO C 1 291 ? 28.211  7.953   15.793  1.00 81.51  ? 294 PRO C CG  1 
ATOM   6199  C CD  . PRO C 1 291 ? 29.646  8.349   15.587  1.00 87.85  ? 294 PRO C CD  1 
ATOM   6200  N N   . PHE C 1 292 ? 30.283  5.461   13.219  1.00 69.13  ? 295 PHE C N   1 
ATOM   6201  C CA  . PHE C 1 292 ? 30.482  4.618   12.044  1.00 69.35  ? 295 PHE C CA  1 
ATOM   6202  C C   . PHE C 1 292 ? 31.880  4.685   11.438  1.00 82.87  ? 295 PHE C C   1 
ATOM   6203  O O   . PHE C 1 292 ? 32.639  5.624   11.689  1.00 87.02  ? 295 PHE C O   1 
ATOM   6204  C CB  . PHE C 1 292 ? 29.476  4.990   10.961  1.00 61.00  ? 295 PHE C CB  1 
ATOM   6205  C CG  . PHE C 1 292 ? 28.092  5.227   11.476  1.00 53.20  ? 295 PHE C CG  1 
ATOM   6206  C CD1 . PHE C 1 292 ? 27.270  4.163   11.814  1.00 47.55  ? 295 PHE C CD1 1 
ATOM   6207  C CD2 . PHE C 1 292 ? 27.604  6.513   11.605  1.00 50.65  ? 295 PHE C CD2 1 
ATOM   6208  C CE1 . PHE C 1 292 ? 25.989  4.381   12.283  1.00 34.74  ? 295 PHE C CE1 1 
ATOM   6209  C CE2 . PHE C 1 292 ? 26.328  6.743   12.067  1.00 38.41  ? 295 PHE C CE2 1 
ATOM   6210  C CZ  . PHE C 1 292 ? 25.514  5.675   12.406  1.00 31.92  ? 295 PHE C CZ  1 
ATOM   6211  N N   . HIS C 1 293 ? 32.202  3.682   10.622  1.00 71.58  ? 296 HIS C N   1 
ATOM   6212  C CA  . HIS C 1 293 ? 33.437  3.688   9.843   1.00 75.22  ? 296 HIS C CA  1 
ATOM   6213  C C   . HIS C 1 293 ? 33.251  2.970   8.507   1.00 73.60  ? 296 HIS C C   1 
ATOM   6214  O O   . HIS C 1 293 ? 32.167  2.464   8.215   1.00 65.36  ? 296 HIS C O   1 
ATOM   6215  C CB  . HIS C 1 293 ? 34.594  3.079   10.637  1.00 73.09  ? 296 HIS C CB  1 
ATOM   6216  C CG  . HIS C 1 293 ? 34.740  1.602   10.462  1.00 74.02  ? 296 HIS C CG  1 
ATOM   6217  N ND1 . HIS C 1 293 ? 35.911  1.020   10.028  1.00 73.77  ? 296 HIS C ND1 1 
ATOM   6218  C CD2 . HIS C 1 293 ? 33.867  0.587   10.667  1.00 70.78  ? 296 HIS C CD2 1 
ATOM   6219  C CE1 . HIS C 1 293 ? 35.751  -0.290  9.964   1.00 74.27  ? 296 HIS C CE1 1 
ATOM   6220  N NE2 . HIS C 1 293 ? 34.518  -0.579  10.344  1.00 67.62  ? 296 HIS C NE2 1 
ATOM   6221  N N   . ASN C 1 294 ? 34.308  2.941   7.697   1.00 47.89  ? 297 ASN C N   1 
ATOM   6222  C CA  . ASN C 1 294 ? 34.256  2.307   6.377   1.00 40.74  ? 297 ASN C CA  1 
ATOM   6223  C C   . ASN C 1 294 ? 35.618  1.872   5.850   1.00 51.44  ? 297 ASN C C   1 
ATOM   6224  O O   . ASN C 1 294 ? 35.824  1.790   4.637   1.00 62.94  ? 297 ASN C O   1 
ATOM   6225  C CB  . ASN C 1 294 ? 33.581  3.218   5.348   1.00 43.64  ? 297 ASN C CB  1 
ATOM   6226  C CG  . ASN C 1 294 ? 34.335  4.538   5.132   1.00 58.14  ? 297 ASN C CG  1 
ATOM   6227  O OD1 . ASN C 1 294 ? 35.454  4.730   5.619   1.00 66.82  ? 297 ASN C OD1 1 
ATOM   6228  N ND2 . ASN C 1 294 ? 33.715  5.450   4.391   1.00 56.83  ? 297 ASN C ND2 1 
ATOM   6229  N N   . VAL C 1 295 ? 36.540  1.595   6.764   1.00 45.45  ? 298 VAL C N   1 
ATOM   6230  C CA  . VAL C 1 295 ? 37.846  1.062   6.396   1.00 52.08  ? 298 VAL C CA  1 
ATOM   6231  C C   . VAL C 1 295 ? 37.728  -0.338  5.780   1.00 59.86  ? 298 VAL C C   1 
ATOM   6232  O O   . VAL C 1 295 ? 37.805  -0.500  4.562   1.00 68.60  ? 298 VAL C O   1 
ATOM   6233  C CB  . VAL C 1 295 ? 38.777  0.980   7.613   1.00 48.47  ? 298 VAL C CB  1 
ATOM   6234  C CG1 . VAL C 1 295 ? 40.196  0.697   7.164   1.00 59.84  ? 298 VAL C CG1 1 
ATOM   6235  C CG2 . VAL C 1 295 ? 38.708  2.261   8.422   1.00 44.47  ? 298 VAL C CG2 1 
ATOM   6236  N N   . HIS C 1 296 ? 37.530  -1.346  6.625   1.00 74.59  ? 299 HIS C N   1 
ATOM   6237  C CA  . HIS C 1 296 ? 37.501  -2.735  6.175   1.00 69.57  ? 299 HIS C CA  1 
ATOM   6238  C C   . HIS C 1 296 ? 36.420  -3.520  6.912   1.00 73.25  ? 299 HIS C C   1 
ATOM   6239  O O   . HIS C 1 296 ? 36.303  -3.424  8.140   1.00 73.84  ? 299 HIS C O   1 
ATOM   6240  C CB  . HIS C 1 296 ? 38.867  -3.391  6.408   1.00 69.94  ? 299 HIS C CB  1 
ATOM   6241  C CG  . HIS C 1 296 ? 39.163  -4.530  5.480   1.00 79.02  ? 299 HIS C CG  1 
ATOM   6242  N ND1 . HIS C 1 296 ? 38.277  -5.562  5.258   1.00 79.69  ? 299 HIS C ND1 1 
ATOM   6243  C CD2 . HIS C 1 296 ? 40.253  -4.803  4.724   1.00 84.36  ? 299 HIS C CD2 1 
ATOM   6244  C CE1 . HIS C 1 296 ? 38.804  -6.418  4.401   1.00 80.37  ? 299 HIS C CE1 1 
ATOM   6245  N NE2 . HIS C 1 296 ? 40.002  -5.981  4.061   1.00 88.05  ? 299 HIS C NE2 1 
ATOM   6246  N N   . PRO C 1 297 ? 35.625  -4.304  6.165   1.00 70.42  ? 300 PRO C N   1 
ATOM   6247  C CA  . PRO C 1 297 ? 34.574  -5.132  6.766   1.00 64.81  ? 300 PRO C CA  1 
ATOM   6248  C C   . PRO C 1 297 ? 35.128  -6.094  7.822   1.00 66.84  ? 300 PRO C C   1 
ATOM   6249  O O   . PRO C 1 297 ? 34.748  -6.001  8.989   1.00 58.89  ? 300 PRO C O   1 
ATOM   6250  C CB  . PRO C 1 297 ? 34.021  -5.910  5.570   1.00 60.54  ? 300 PRO C CB  1 
ATOM   6251  C CG  . PRO C 1 297 ? 34.310  -5.049  4.402   1.00 69.46  ? 300 PRO C CG  1 
ATOM   6252  C CD  . PRO C 1 297 ? 35.631  -4.407  4.697   1.00 73.58  ? 300 PRO C CD  1 
ATOM   6253  N N   . LEU C 1 298 ? 36.017  -6.998  7.413   1.00 80.48  ? 301 LEU C N   1 
ATOM   6254  C CA  . LEU C 1 298 ? 36.629  -7.957  8.332   1.00 77.03  ? 301 LEU C CA  1 
ATOM   6255  C C   . LEU C 1 298 ? 37.310  -7.250  9.492   1.00 71.37  ? 301 LEU C C   1 
ATOM   6256  O O   . LEU C 1 298 ? 38.454  -6.821  9.386   1.00 83.98  ? 301 LEU C O   1 
ATOM   6257  C CB  . LEU C 1 298 ? 37.648  -8.828  7.608   1.00 82.55  ? 301 LEU C CB  1 
ATOM   6258  C CG  . LEU C 1 298 ? 37.197  -9.441  6.286   1.00 87.86  ? 301 LEU C CG  1 
ATOM   6259  C CD1 . LEU C 1 298 ? 38.012  -10.698 6.023   1.00 95.12  ? 301 LEU C CD1 1 
ATOM   6260  C CD2 . LEU C 1 298 ? 35.711  -9.762  6.302   1.00 77.91  ? 301 LEU C CD2 1 
ATOM   6261  N N   . THR C 1 299 ? 36.606  -7.158  10.609  1.00 60.68  ? 302 THR C N   1 
ATOM   6262  C CA  . THR C 1 299 ? 37.025  -6.324  11.720  1.00 53.34  ? 302 THR C CA  1 
ATOM   6263  C C   . THR C 1 299 ? 37.156  -7.187  12.973  1.00 56.32  ? 302 THR C C   1 
ATOM   6264  O O   . THR C 1 299 ? 36.562  -8.265  13.037  1.00 57.97  ? 302 THR C O   1 
ATOM   6265  C CB  . THR C 1 299 ? 35.973  -5.212  11.939  1.00 53.96  ? 302 THR C CB  1 
ATOM   6266  O OG1 . THR C 1 299 ? 36.488  -3.947  11.491  1.00 60.75  ? 302 THR C OG1 1 
ATOM   6267  C CG2 . THR C 1 299 ? 35.545  -5.136  13.400  1.00 38.56  ? 302 THR C CG2 1 
ATOM   6268  N N   . ILE C 1 300 ? 37.935  -6.740  13.957  1.00 75.12  ? 303 ILE C N   1 
ATOM   6269  C CA  . ILE C 1 300 ? 38.050  -7.480  15.216  1.00 63.05  ? 303 ILE C CA  1 
ATOM   6270  C C   . ILE C 1 300 ? 38.215  -6.593  16.441  1.00 63.22  ? 303 ILE C C   1 
ATOM   6271  O O   . ILE C 1 300 ? 39.265  -5.980  16.623  1.00 75.74  ? 303 ILE C O   1 
ATOM   6272  C CB  . ILE C 1 300 ? 39.235  -8.455  15.208  1.00 60.76  ? 303 ILE C CB  1 
ATOM   6273  C CG1 . ILE C 1 300 ? 39.125  -9.430  14.040  1.00 64.65  ? 303 ILE C CG1 1 
ATOM   6274  C CG2 . ILE C 1 300 ? 39.305  -9.217  16.530  1.00 51.67  ? 303 ILE C CG2 1 
ATOM   6275  C CD1 . ILE C 1 300 ? 40.138  -10.534 14.100  1.00 59.62  ? 303 ILE C CD1 1 
ATOM   6276  N N   . GLY C 1 301 ? 37.188  -6.550  17.288  1.00 73.50  ? 304 GLY C N   1 
ATOM   6277  C CA  . GLY C 1 301 ? 37.230  -5.778  18.520  1.00 86.36  ? 304 GLY C CA  1 
ATOM   6278  C C   . GLY C 1 301 ? 35.980  -4.944  18.745  1.00 99.05  ? 304 GLY C C   1 
ATOM   6279  O O   . GLY C 1 301 ? 34.880  -5.353  18.370  1.00 102.80 ? 304 GLY C O   1 
ATOM   6280  N N   . GLU C 1 302 ? 36.148  -3.780  19.369  1.00 65.62  ? 305 GLU C N   1 
ATOM   6281  C CA  . GLU C 1 302 ? 35.043  -2.839  19.551  1.00 63.43  ? 305 GLU C CA  1 
ATOM   6282  C C   . GLU C 1 302 ? 35.064  -1.776  18.450  1.00 58.39  ? 305 GLU C C   1 
ATOM   6283  O O   . GLU C 1 302 ? 35.813  -0.796  18.522  1.00 54.35  ? 305 GLU C O   1 
ATOM   6284  C CB  . GLU C 1 302 ? 35.095  -2.180  20.936  1.00 74.21  ? 305 GLU C CB  1 
ATOM   6285  C CG  . GLU C 1 302 ? 34.688  -3.077  22.102  1.00 84.73  ? 305 GLU C CG  1 
ATOM   6286  C CD  . GLU C 1 302 ? 35.874  -3.586  22.911  1.00 101.87 ? 305 GLU C CD  1 
ATOM   6287  O OE1 . GLU C 1 302 ? 35.737  -3.704  24.149  1.00 109.27 ? 305 GLU C OE1 1 
ATOM   6288  O OE2 . GLU C 1 302 ? 36.936  -3.873  22.314  1.00 104.61 ? 305 GLU C OE2 1 
ATOM   6289  N N   . CYS C 1 303 ? 34.238  -1.962  17.429  1.00 69.41  ? 306 CYS C N   1 
ATOM   6290  C CA  . CYS C 1 303 ? 34.320  -1.109  16.255  1.00 69.07  ? 306 CYS C CA  1 
ATOM   6291  C C   . CYS C 1 303 ? 33.013  -0.415  15.934  1.00 63.54  ? 306 CYS C C   1 
ATOM   6292  O O   . CYS C 1 303 ? 31.941  -0.911  16.270  1.00 58.88  ? 306 CYS C O   1 
ATOM   6293  C CB  . CYS C 1 303 ? 34.782  -1.925  15.053  1.00 72.86  ? 306 CYS C CB  1 
ATOM   6294  S SG  . CYS C 1 303 ? 36.369  -2.714  15.332  1.00 61.70  ? 306 CYS C SG  1 
ATOM   6295  N N   . PRO C 1 304 ? 33.107  0.750   15.286  1.00 54.39  ? 307 PRO C N   1 
ATOM   6296  C CA  . PRO C 1 304 ? 31.946  1.508   14.819  1.00 52.56  ? 307 PRO C CA  1 
ATOM   6297  C C   . PRO C 1 304 ? 31.210  0.726   13.743  1.00 48.93  ? 307 PRO C C   1 
ATOM   6298  O O   . PRO C 1 304 ? 31.815  -0.134  13.115  1.00 56.39  ? 307 PRO C O   1 
ATOM   6299  C CB  . PRO C 1 304 ? 32.576  2.765   14.209  1.00 61.52  ? 307 PRO C CB  1 
ATOM   6300  C CG  . PRO C 1 304 ? 33.923  2.874   14.844  1.00 61.81  ? 307 PRO C CG  1 
ATOM   6301  C CD  . PRO C 1 304 ? 34.372  1.465   15.043  1.00 59.67  ? 307 PRO C CD  1 
ATOM   6302  N N   . LYS C 1 305 ? 29.934  1.023   13.530  1.00 50.25  ? 308 LYS C N   1 
ATOM   6303  C CA  . LYS C 1 305 ? 29.148  0.303   12.535  1.00 49.14  ? 308 LYS C CA  1 
ATOM   6304  C C   . LYS C 1 305 ? 29.645  0.537   11.107  1.00 54.53  ? 308 LYS C C   1 
ATOM   6305  O O   . LYS C 1 305 ? 29.529  1.636   10.571  1.00 64.48  ? 308 LYS C O   1 
ATOM   6306  C CB  . LYS C 1 305 ? 27.660  0.644   12.661  1.00 45.80  ? 308 LYS C CB  1 
ATOM   6307  C CG  . LYS C 1 305 ? 26.926  -0.145  13.747  1.00 49.94  ? 308 LYS C CG  1 
ATOM   6308  C CD  . LYS C 1 305 ? 27.846  -0.442  14.926  1.00 57.89  ? 308 LYS C CD  1 
ATOM   6309  C CE  . LYS C 1 305 ? 27.085  -0.927  16.155  1.00 60.44  ? 308 LYS C CE  1 
ATOM   6310  N NZ  . LYS C 1 305 ? 26.373  -2.213  15.945  1.00 49.76  ? 308 LYS C NZ  1 
ATOM   6311  N N   . TYR C 1 306 ? 30.200  -0.507  10.497  1.00 47.61  ? 309 TYR C N   1 
ATOM   6312  C CA  . TYR C 1 306 ? 30.681  -0.424  9.125   1.00 60.16  ? 309 TYR C CA  1 
ATOM   6313  C C   . TYR C 1 306 ? 29.550  0.016   8.213   1.00 55.79  ? 309 TYR C C   1 
ATOM   6314  O O   . TYR C 1 306 ? 28.439  -0.485  8.316   1.00 51.34  ? 309 TYR C O   1 
ATOM   6315  C CB  . TYR C 1 306 ? 31.229  -1.777  8.664   1.00 67.17  ? 309 TYR C CB  1 
ATOM   6316  C CG  . TYR C 1 306 ? 31.838  -1.758  7.275   1.00 74.25  ? 309 TYR C CG  1 
ATOM   6317  C CD1 . TYR C 1 306 ? 33.061  -1.141  7.041   1.00 83.73  ? 309 TYR C CD1 1 
ATOM   6318  C CD2 . TYR C 1 306 ? 31.197  -2.367  6.202   1.00 71.63  ? 309 TYR C CD2 1 
ATOM   6319  C CE1 . TYR C 1 306 ? 33.624  -1.122  5.776   1.00 88.40  ? 309 TYR C CE1 1 
ATOM   6320  C CE2 . TYR C 1 306 ? 31.753  -2.349  4.932   1.00 78.78  ? 309 TYR C CE2 1 
ATOM   6321  C CZ  . TYR C 1 306 ? 32.966  -1.726  4.726   1.00 82.32  ? 309 TYR C CZ  1 
ATOM   6322  O OH  . TYR C 1 306 ? 33.526  -1.702  3.468   1.00 77.38  ? 309 TYR C OH  1 
ATOM   6323  N N   . VAL C 1 307 ? 29.829  0.957   7.320   1.00 64.57  ? 310 VAL C N   1 
ATOM   6324  C CA  . VAL C 1 307 ? 28.798  1.434   6.410   1.00 64.27  ? 310 VAL C CA  1 
ATOM   6325  C C   . VAL C 1 307 ? 29.294  1.630   4.977   1.00 85.30  ? 310 VAL C C   1 
ATOM   6326  O O   . VAL C 1 307 ? 30.413  2.091   4.747   1.00 94.74  ? 310 VAL C O   1 
ATOM   6327  C CB  . VAL C 1 307 ? 28.149  2.736   6.923   1.00 59.01  ? 310 VAL C CB  1 
ATOM   6328  C CG1 . VAL C 1 307 ? 27.246  2.445   8.115   1.00 42.91  ? 310 VAL C CG1 1 
ATOM   6329  C CG2 . VAL C 1 307 ? 29.215  3.759   7.283   1.00 63.94  ? 310 VAL C CG2 1 
ATOM   6330  N N   . LYS C 1 308 ? 28.453  1.254   4.017   1.00 111.51 ? 311 LYS C N   1 
ATOM   6331  C CA  . LYS C 1 308 ? 28.728  1.498   2.610   1.00 116.00 ? 311 LYS C CA  1 
ATOM   6332  C C   . LYS C 1 308 ? 28.423  2.960   2.348   1.00 113.94 ? 311 LYS C C   1 
ATOM   6333  O O   . LYS C 1 308 ? 27.371  3.297   1.803   1.00 110.39 ? 311 LYS C O   1 
ATOM   6334  C CB  . LYS C 1 308 ? 27.844  0.613   1.731   1.00 111.83 ? 311 LYS C CB  1 
ATOM   6335  C CG  . LYS C 1 308 ? 28.474  0.223   0.405   1.00 129.26 ? 311 LYS C CG  1 
ATOM   6336  C CD  . LYS C 1 308 ? 28.877  1.446   -0.404  1.00 135.10 ? 311 LYS C CD  1 
ATOM   6337  C CE  . LYS C 1 308 ? 29.789  1.070   -1.565  1.00 148.55 ? 311 LYS C CE  1 
ATOM   6338  N NZ  . LYS C 1 308 ? 30.318  2.272   -2.272  1.00 142.66 ? 311 LYS C NZ  1 
ATOM   6339  N N   . SER C 1 309 ? 29.343  3.831   2.747   1.00 68.95  ? 312 SER C N   1 
ATOM   6340  C CA  . SER C 1 309 ? 29.065  5.255   2.755   1.00 60.24  ? 312 SER C CA  1 
ATOM   6341  C C   . SER C 1 309 ? 30.331  6.056   2.529   1.00 70.62  ? 312 SER C C   1 
ATOM   6342  O O   . SER C 1 309 ? 31.398  5.693   3.019   1.00 64.82  ? 312 SER C O   1 
ATOM   6343  C CB  . SER C 1 309 ? 28.424  5.652   4.087   1.00 52.96  ? 312 SER C CB  1 
ATOM   6344  O OG  . SER C 1 309 ? 27.921  6.977   4.040   1.00 52.89  ? 312 SER C OG  1 
ATOM   6345  N N   . GLU C 1 310 ? 30.192  7.159   1.797   1.00 68.52  ? 313 GLU C N   1 
ATOM   6346  C CA  . GLU C 1 310 ? 31.328  7.963   1.356   1.00 73.09  ? 313 GLU C CA  1 
ATOM   6347  C C   . GLU C 1 310 ? 31.747  8.991   2.404   1.00 65.79  ? 313 GLU C C   1 
ATOM   6348  O O   . GLU C 1 310 ? 32.914  9.056   2.796   1.00 62.41  ? 313 GLU C O   1 
ATOM   6349  C CB  . GLU C 1 310 ? 30.978  8.665   0.044   1.00 84.85  ? 313 GLU C CB  1 
ATOM   6350  C CG  . GLU C 1 310 ? 32.170  9.226   -0.716  1.00 106.72 ? 313 GLU C CG  1 
ATOM   6351  C CD  . GLU C 1 310 ? 32.973  8.156   -1.442  1.00 119.35 ? 313 GLU C CD  1 
ATOM   6352  O OE1 . GLU C 1 310 ? 33.689  8.507   -2.406  1.00 125.03 ? 313 GLU C OE1 1 
ATOM   6353  O OE2 . GLU C 1 310 ? 32.892  6.970   -1.054  1.00 118.49 ? 313 GLU C OE2 1 
ATOM   6354  N N   . LYS C 1 311 ? 30.782  9.791   2.849   1.00 86.73  ? 314 LYS C N   1 
ATOM   6355  C CA  . LYS C 1 311 ? 31.015  10.809  3.866   1.00 85.72  ? 314 LYS C CA  1 
ATOM   6356  C C   . LYS C 1 311 ? 29.800  10.905  4.775   1.00 72.84  ? 314 LYS C C   1 
ATOM   6357  O O   . LYS C 1 311 ? 28.665  10.779  4.318   1.00 66.71  ? 314 LYS C O   1 
ATOM   6358  C CB  . LYS C 1 311 ? 31.265  12.171  3.206   1.00 98.08  ? 314 LYS C CB  1 
ATOM   6359  C CG  . LYS C 1 311 ? 30.070  12.710  2.402   1.00 99.30  ? 314 LYS C CG  1 
ATOM   6360  C CD  . LYS C 1 311 ? 30.472  13.821  1.429   1.00 104.31 ? 314 LYS C CD  1 
ATOM   6361  C CE  . LYS C 1 311 ? 30.618  15.180  2.115   1.00 107.17 ? 314 LYS C CE  1 
ATOM   6362  N NZ  . LYS C 1 311 ? 29.446  16.088  1.888   1.00 103.26 ? 314 LYS C NZ  1 
ATOM   6363  N N   . LEU C 1 312 ? 30.032  11.117  6.064   1.00 73.81  ? 315 LEU C N   1 
ATOM   6364  C CA  . LEU C 1 312 ? 28.935  11.431  6.971   1.00 72.86  ? 315 LEU C CA  1 
ATOM   6365  C C   . LEU C 1 312 ? 29.245  12.742  7.678   1.00 81.42  ? 315 LEU C C   1 
ATOM   6366  O O   . LEU C 1 312 ? 29.985  12.769  8.663   1.00 88.92  ? 315 LEU C O   1 
ATOM   6367  C CB  . LEU C 1 312 ? 28.692  10.304  7.979   1.00 64.61  ? 315 LEU C CB  1 
ATOM   6368  C CG  . LEU C 1 312 ? 28.075  9.014   7.420   1.00 55.71  ? 315 LEU C CG  1 
ATOM   6369  C CD1 . LEU C 1 312 ? 28.179  7.872   8.415   1.00 54.38  ? 315 LEU C CD1 1 
ATOM   6370  C CD2 . LEU C 1 312 ? 26.630  9.230   6.991   1.00 47.94  ? 315 LEU C CD2 1 
ATOM   6371  N N   . VAL C 1 313 ? 28.678  13.829  7.159   1.00 80.07  ? 316 VAL C N   1 
ATOM   6372  C CA  . VAL C 1 313 ? 28.983  15.166  7.652   1.00 74.40  ? 316 VAL C CA  1 
ATOM   6373  C C   . VAL C 1 313 ? 27.801  15.855  8.328   1.00 71.70  ? 316 VAL C C   1 
ATOM   6374  O O   . VAL C 1 313 ? 26.827  16.238  7.675   1.00 71.01  ? 316 VAL C O   1 
ATOM   6375  C CB  . VAL C 1 313 ? 29.503  16.063  6.524   1.00 73.89  ? 316 VAL C CB  1 
ATOM   6376  C CG1 . VAL C 1 313 ? 29.860  17.437  7.065   1.00 74.93  ? 316 VAL C CG1 1 
ATOM   6377  C CG2 . VAL C 1 313 ? 30.707  15.412  5.867   1.00 80.34  ? 316 VAL C CG2 1 
ATOM   6378  N N   . LEU C 1 314 ? 27.912  16.011  9.645   1.00 70.26  ? 317 LEU C N   1 
ATOM   6379  C CA  . LEU C 1 314 ? 26.919  16.721  10.442  1.00 63.87  ? 317 LEU C CA  1 
ATOM   6380  C C   . LEU C 1 314 ? 27.215  18.209  10.467  1.00 72.80  ? 317 LEU C C   1 
ATOM   6381  O O   . LEU C 1 314 ? 28.333  18.625  10.767  1.00 78.51  ? 317 LEU C O   1 
ATOM   6382  C CB  . LEU C 1 314 ? 26.899  16.197  11.881  1.00 52.48  ? 317 LEU C CB  1 
ATOM   6383  C CG  . LEU C 1 314 ? 25.969  15.034  12.218  1.00 41.63  ? 317 LEU C CG  1 
ATOM   6384  C CD1 . LEU C 1 314 ? 26.043  14.710  13.700  1.00 31.10  ? 317 LEU C CD1 1 
ATOM   6385  C CD2 . LEU C 1 314 ? 24.538  15.342  11.805  1.00 40.83  ? 317 LEU C CD2 1 
ATOM   6386  N N   . ALA C 1 315 ? 26.196  19.002  10.162  1.00 69.04  ? 318 ALA C N   1 
ATOM   6387  C CA  . ALA C 1 315 ? 26.306  20.453  10.193  1.00 65.10  ? 318 ALA C CA  1 
ATOM   6388  C C   . ALA C 1 315 ? 26.104  20.981  11.610  1.00 60.21  ? 318 ALA C C   1 
ATOM   6389  O O   . ALA C 1 315 ? 24.988  20.992  12.117  1.00 55.46  ? 318 ALA C O   1 
ATOM   6390  C CB  . ALA C 1 315 ? 25.284  21.061  9.261   1.00 58.11  ? 318 ALA C CB  1 
ATOM   6391  N N   . THR C 1 316 ? 27.186  21.415  12.247  1.00 56.81  ? 319 THR C N   1 
ATOM   6392  C CA  . THR C 1 316 ? 27.102  22.010  13.579  1.00 51.94  ? 319 THR C CA  1 
ATOM   6393  C C   . THR C 1 316 ? 26.796  23.509  13.524  1.00 58.15  ? 319 THR C C   1 
ATOM   6394  O O   . THR C 1 316 ? 25.809  23.975  14.101  1.00 65.16  ? 319 THR C O   1 
ATOM   6395  C CB  . THR C 1 316 ? 28.394  21.792  14.372  1.00 50.62  ? 319 THR C CB  1 
ATOM   6396  O OG1 . THR C 1 316 ? 29.514  22.235  13.593  1.00 58.84  ? 319 THR C OG1 1 
ATOM   6397  C CG2 . THR C 1 316 ? 28.553  20.317  14.718  1.00 47.29  ? 319 THR C CG2 1 
ATOM   6398  N N   . GLY C 1 317 ? 27.648  24.260  12.829  1.00 60.98  ? 320 GLY C N   1 
ATOM   6399  C CA  . GLY C 1 317 ? 27.440  25.685  12.635  1.00 66.04  ? 320 GLY C CA  1 
ATOM   6400  C C   . GLY C 1 317 ? 26.140  26.000  11.913  1.00 70.57  ? 320 GLY C C   1 
ATOM   6401  O O   . GLY C 1 317 ? 25.224  25.178  11.879  1.00 74.18  ? 320 GLY C O   1 
ATOM   6402  N N   . LEU C 1 318 ? 26.051  27.193  11.332  1.00 74.39  ? 321 LEU C N   1 
ATOM   6403  C CA  . LEU C 1 318 ? 24.835  27.599  10.635  1.00 71.06  ? 321 LEU C CA  1 
ATOM   6404  C C   . LEU C 1 318 ? 25.116  27.898  9.170   1.00 67.33  ? 321 LEU C C   1 
ATOM   6405  O O   . LEU C 1 318 ? 26.273  27.928  8.756   1.00 71.56  ? 321 LEU C O   1 
ATOM   6406  C CB  . LEU C 1 318 ? 24.192  28.805  11.319  1.00 73.89  ? 321 LEU C CB  1 
ATOM   6407  C CG  . LEU C 1 318 ? 24.978  30.113  11.318  1.00 75.16  ? 321 LEU C CG  1 
ATOM   6408  C CD1 . LEU C 1 318 ? 24.399  31.057  10.285  1.00 77.40  ? 321 LEU C CD1 1 
ATOM   6409  C CD2 . LEU C 1 318 ? 24.924  30.738  12.696  1.00 73.50  ? 321 LEU C CD2 1 
ATOM   6410  N N   . ARG C 1 319 ? 24.057  28.104  8.388   1.00 63.11  ? 322 ARG C N   1 
ATOM   6411  C CA  . ARG C 1 319 ? 24.211  28.369  6.961   1.00 64.01  ? 322 ARG C CA  1 
ATOM   6412  C C   . ARG C 1 319 ? 25.074  29.606  6.760   1.00 78.14  ? 322 ARG C C   1 
ATOM   6413  O O   . ARG C 1 319 ? 24.728  30.692  7.219   1.00 82.05  ? 322 ARG C O   1 
ATOM   6414  C CB  . ARG C 1 319 ? 22.850  28.555  6.292   1.00 54.81  ? 322 ARG C CB  1 
ATOM   6415  C CG  . ARG C 1 319 ? 22.897  28.434  4.774   1.00 68.92  ? 322 ARG C CG  1 
ATOM   6416  C CD  . ARG C 1 319 ? 21.521  28.632  4.146   1.00 78.70  ? 322 ARG C CD  1 
ATOM   6417  N NE  . ARG C 1 319 ? 20.524  27.700  4.673   1.00 84.19  ? 322 ARG C NE  1 
ATOM   6418  C CZ  . ARG C 1 319 ? 20.139  26.579  4.066   1.00 82.13  ? 322 ARG C CZ  1 
ATOM   6419  N NH1 . ARG C 1 319 ? 20.666  26.237  2.896   1.00 81.40  ? 322 ARG C NH1 1 
ATOM   6420  N NH2 . ARG C 1 319 ? 19.220  25.805  4.631   1.00 74.98  ? 322 ARG C NH2 1 
ATOM   6421  N N   . ASN C 1 320 ? 26.200  29.436  6.074   1.00 62.05  ? 323 ASN C N   1 
ATOM   6422  C CA  . ASN C 1 320 ? 27.194  30.500  5.951   1.00 62.33  ? 323 ASN C CA  1 
ATOM   6423  C C   . ASN C 1 320 ? 27.007  31.346  4.700   1.00 66.26  ? 323 ASN C C   1 
ATOM   6424  O O   . ASN C 1 320 ? 27.276  30.884  3.590   1.00 64.14  ? 323 ASN C O   1 
ATOM   6425  C CB  . ASN C 1 320 ? 28.600  29.908  5.973   1.00 61.31  ? 323 ASN C CB  1 
ATOM   6426  C CG  . ASN C 1 320 ? 29.675  30.961  5.906   1.00 63.24  ? 323 ASN C CG  1 
ATOM   6427  O OD1 . ASN C 1 320 ? 29.472  32.101  6.331   1.00 63.55  ? 323 ASN C OD1 1 
ATOM   6428  N ND2 . ASN C 1 320 ? 30.834  30.590  5.370   1.00 67.06  ? 323 ASN C ND2 1 
ATOM   6429  N N   . VAL C 1 321 ? 26.557  32.585  4.894   1.00 115.54 ? 324 VAL C N   1 
ATOM   6430  C CA  . VAL C 1 321 ? 26.241  33.493  3.791   1.00 124.65 ? 324 VAL C CA  1 
ATOM   6431  C C   . VAL C 1 321 ? 27.127  34.744  3.793   1.00 131.68 ? 324 VAL C C   1 
ATOM   6432  O O   . VAL C 1 321 ? 27.453  35.279  4.853   1.00 131.80 ? 324 VAL C O   1 
ATOM   6433  C CB  . VAL C 1 321 ? 24.755  33.925  3.826   1.00 131.47 ? 324 VAL C CB  1 
ATOM   6434  C CG1 . VAL C 1 321 ? 23.844  32.705  3.878   1.00 126.42 ? 324 VAL C CG1 1 
ATOM   6435  C CG2 . VAL C 1 321 ? 24.490  34.832  5.013   1.00 133.13 ? 324 VAL C CG2 1 
ATOM   6436  N N   . PRO C 1 322 ? 27.517  35.214  2.596   1.00 118.51 ? 325 PRO C N   1 
ATOM   6437  C CA  . PRO C 1 322 ? 28.386  36.386  2.416   1.00 117.11 ? 325 PRO C CA  1 
ATOM   6438  C C   . PRO C 1 322 ? 27.797  37.668  3.003   1.00 111.78 ? 325 PRO C C   1 
ATOM   6439  O O   . PRO C 1 322 ? 28.444  38.716  2.923   1.00 111.76 ? 325 PRO C O   1 
ATOM   6440  C CB  . PRO C 1 322 ? 28.490  36.510  0.892   1.00 125.37 ? 325 PRO C CB  1 
ATOM   6441  C CG  . PRO C 1 322 ? 28.213  35.137  0.380   1.00 125.46 ? 325 PRO C CG  1 
ATOM   6442  C CD  . PRO C 1 322 ? 27.189  34.569  1.313   1.00 119.51 ? 325 PRO C CD  1 
ATOM   6443  N N   . GLY D 2 1   ? 15.240  30.897  6.390   1.00 71.27  ? 1   GLY D N   1 
ATOM   6444  C CA  . GLY D 2 1   ? 15.217  29.503  5.981   1.00 71.27  ? 1   GLY D CA  1 
ATOM   6445  C C   . GLY D 2 1   ? 13.841  28.895  6.157   1.00 71.17  ? 1   GLY D C   1 
ATOM   6446  O O   . GLY D 2 1   ? 13.013  28.929  5.247   1.00 79.31  ? 1   GLY D O   1 
ATOM   6447  N N   . LEU D 2 2   ? 13.593  28.336  7.334   1.00 70.72  ? 2   LEU D N   1 
ATOM   6448  C CA  . LEU D 2 2   ? 12.269  27.825  7.648   1.00 71.62  ? 2   LEU D CA  1 
ATOM   6449  C C   . LEU D 2 2   ? 11.562  28.820  8.546   1.00 78.40  ? 2   LEU D C   1 
ATOM   6450  O O   . LEU D 2 2   ? 10.334  28.860  8.608   1.00 85.48  ? 2   LEU D O   1 
ATOM   6451  C CB  . LEU D 2 2   ? 12.353  26.465  8.344   1.00 63.88  ? 2   LEU D CB  1 
ATOM   6452  C CG  . LEU D 2 2   ? 10.992  25.807  8.593   1.00 58.98  ? 2   LEU D CG  1 
ATOM   6453  C CD1 . LEU D 2 2   ? 10.483  25.174  7.312   1.00 70.21  ? 2   LEU D CD1 1 
ATOM   6454  C CD2 . LEU D 2 2   ? 11.075  24.781  9.691   1.00 43.81  ? 2   LEU D CD2 1 
ATOM   6455  N N   . PHE D 2 3   ? 12.352  29.621  9.249   1.00 92.08  ? 3   PHE D N   1 
ATOM   6456  C CA  . PHE D 2 3   ? 11.814  30.644  10.133  1.00 91.18  ? 3   PHE D CA  1 
ATOM   6457  C C   . PHE D 2 3   ? 11.975  32.040  9.535   1.00 97.14  ? 3   PHE D C   1 
ATOM   6458  O O   . PHE D 2 3   ? 11.618  33.039  10.157  1.00 96.34  ? 3   PHE D O   1 
ATOM   6459  C CB  . PHE D 2 3   ? 12.444  30.546  11.526  1.00 85.04  ? 3   PHE D CB  1 
ATOM   6460  C CG  . PHE D 2 3   ? 11.878  29.436  12.359  1.00 79.85  ? 3   PHE D CG  1 
ATOM   6461  C CD1 . PHE D 2 3   ? 10.757  29.645  13.141  1.00 81.26  ? 3   PHE D CD1 1 
ATOM   6462  C CD2 . PHE D 2 3   ? 12.453  28.178  12.347  1.00 75.54  ? 3   PHE D CD2 1 
ATOM   6463  C CE1 . PHE D 2 3   ? 10.222  28.618  13.905  1.00 77.39  ? 3   PHE D CE1 1 
ATOM   6464  C CE2 . PHE D 2 3   ? 11.922  27.143  13.106  1.00 72.55  ? 3   PHE D CE2 1 
ATOM   6465  C CZ  . PHE D 2 3   ? 10.806  27.364  13.886  1.00 75.46  ? 3   PHE D CZ  1 
ATOM   6466  N N   . GLY D 2 4   ? 12.513  32.098  8.321   1.00 73.33  ? 4   GLY D N   1 
ATOM   6467  C CA  . GLY D 2 4   ? 12.516  33.328  7.552   1.00 69.79  ? 4   GLY D CA  1 
ATOM   6468  C C   . GLY D 2 4   ? 13.692  34.252  7.788   1.00 64.75  ? 4   GLY D C   1 
ATOM   6469  O O   . GLY D 2 4   ? 13.987  35.104  6.953   1.00 66.94  ? 4   GLY D O   1 
ATOM   6470  N N   . ALA D 2 5   ? 14.370  34.083  8.916   1.00 59.53  ? 5   ALA D N   1 
ATOM   6471  C CA  . ALA D 2 5   ? 15.449  34.991  9.295   1.00 58.78  ? 5   ALA D CA  1 
ATOM   6472  C C   . ALA D 2 5   ? 16.716  34.799  8.471   1.00 55.75  ? 5   ALA D C   1 
ATOM   6473  O O   . ALA D 2 5   ? 17.040  35.618  7.612   1.00 55.44  ? 5   ALA D O   1 
ATOM   6474  C CB  . ALA D 2 5   ? 15.760  34.856  10.778  1.00 59.78  ? 5   ALA D CB  1 
ATOM   6475  N N   . ILE D 2 6   ? 17.435  33.719  8.749   1.00 57.76  ? 6   ILE D N   1 
ATOM   6476  C CA  . ILE D 2 6   ? 18.716  33.476  8.105   1.00 56.38  ? 6   ILE D CA  1 
ATOM   6477  C C   . ILE D 2 6   ? 18.561  33.305  6.601   1.00 55.42  ? 6   ILE D C   1 
ATOM   6478  O O   . ILE D 2 6   ? 17.808  32.447  6.137   1.00 54.97  ? 6   ILE D O   1 
ATOM   6479  C CB  . ILE D 2 6   ? 19.429  32.264  8.709   1.00 55.99  ? 6   ILE D CB  1 
ATOM   6480  C CG1 . ILE D 2 6   ? 19.831  32.568  10.153  1.00 59.09  ? 6   ILE D CG1 1 
ATOM   6481  C CG2 . ILE D 2 6   ? 20.647  31.901  7.883   1.00 54.28  ? 6   ILE D CG2 1 
ATOM   6482  C CD1 . ILE D 2 6   ? 20.650  31.485  10.800  1.00 60.57  ? 6   ILE D CD1 1 
ATOM   6483  N N   . ALA D 2 7   ? 19.286  34.136  5.853   1.00 54.44  ? 7   ALA D N   1 
ATOM   6484  C CA  . ALA D 2 7   ? 19.160  34.212  4.398   1.00 58.89  ? 7   ALA D CA  1 
ATOM   6485  C C   . ALA D 2 7   ? 17.704  34.412  4.000   1.00 64.63  ? 7   ALA D C   1 
ATOM   6486  O O   . ALA D 2 7   ? 17.181  33.707  3.135   1.00 64.35  ? 7   ALA D O   1 
ATOM   6487  C CB  . ALA D 2 7   ? 19.741  32.978  3.739   1.00 49.72  ? 7   ALA D CB  1 
ATOM   6488  N N   . GLY D 2 8   ? 17.062  35.382  4.648   1.00 77.44  ? 8   GLY D N   1 
ATOM   6489  C CA  . GLY D 2 8   ? 15.662  35.694  4.418   1.00 79.71  ? 8   GLY D CA  1 
ATOM   6490  C C   . GLY D 2 8   ? 15.399  37.183  4.546   1.00 84.59  ? 8   GLY D C   1 
ATOM   6491  O O   . GLY D 2 8   ? 15.677  37.942  3.620   1.00 91.08  ? 8   GLY D O   1 
ATOM   6492  N N   . PHE D 2 9   ? 14.868  37.612  5.689   1.00 85.04  ? 9   PHE D N   1 
ATOM   6493  C CA  . PHE D 2 9   ? 14.659  39.039  5.917   1.00 81.91  ? 9   PHE D CA  1 
ATOM   6494  C C   . PHE D 2 9   ? 15.939  39.717  6.405   1.00 81.53  ? 9   PHE D C   1 
ATOM   6495  O O   . PHE D 2 9   ? 16.079  40.936  6.331   1.00 96.48  ? 9   PHE D O   1 
ATOM   6496  C CB  . PHE D 2 9   ? 13.457  39.317  6.836   1.00 79.81  ? 9   PHE D CB  1 
ATOM   6497  C CG  . PHE D 2 9   ? 13.714  39.065  8.298   1.00 73.89  ? 9   PHE D CG  1 
ATOM   6498  C CD1 . PHE D 2 9   ? 14.656  39.805  8.996   1.00 74.04  ? 9   PHE D CD1 1 
ATOM   6499  C CD2 . PHE D 2 9   ? 12.970  38.120  8.987   1.00 68.00  ? 9   PHE D CD2 1 
ATOM   6500  C CE1 . PHE D 2 9   ? 14.876  39.580  10.346  1.00 68.89  ? 9   PHE D CE1 1 
ATOM   6501  C CE2 . PHE D 2 9   ? 13.185  37.894  10.335  1.00 66.80  ? 9   PHE D CE2 1 
ATOM   6502  C CZ  . PHE D 2 9   ? 14.139  38.627  11.015  1.00 64.23  ? 9   PHE D CZ  1 
ATOM   6503  N N   . ILE D 2 10  ? 16.870  38.912  6.900   1.00 65.93  ? 10  ILE D N   1 
ATOM   6504  C CA  . ILE D 2 10  ? 18.236  39.362  7.127   1.00 67.44  ? 10  ILE D CA  1 
ATOM   6505  C C   . ILE D 2 10  ? 19.111  38.755  6.038   1.00 77.16  ? 10  ILE D C   1 
ATOM   6506  O O   . ILE D 2 10  ? 19.614  37.640  6.184   1.00 77.73  ? 10  ILE D O   1 
ATOM   6507  C CB  . ILE D 2 10  ? 18.751  38.921  8.504   1.00 64.27  ? 10  ILE D CB  1 
ATOM   6508  C CG1 . ILE D 2 10  ? 17.923  39.571  9.607   1.00 62.73  ? 10  ILE D CG1 1 
ATOM   6509  C CG2 . ILE D 2 10  ? 20.222  39.276  8.677   1.00 63.32  ? 10  ILE D CG2 1 
ATOM   6510  C CD1 . ILE D 2 10  ? 18.141  38.962  10.968  1.00 60.68  ? 10  ILE D CD1 1 
ATOM   6511  N N   . GLU D 2 11  ? 19.284  39.492  4.944   1.00 73.67  ? 11  GLU D N   1 
ATOM   6512  C CA  . GLU D 2 11  ? 19.946  38.972  3.746   1.00 79.61  ? 11  GLU D CA  1 
ATOM   6513  C C   . GLU D 2 11  ? 21.232  38.177  4.008   1.00 75.89  ? 11  GLU D C   1 
ATOM   6514  O O   . GLU D 2 11  ? 21.358  37.034  3.574   1.00 73.14  ? 11  GLU D O   1 
ATOM   6515  C CB  . GLU D 2 11  ? 20.214  40.106  2.750   1.00 88.67  ? 11  GLU D CB  1 
ATOM   6516  C CG  . GLU D 2 11  ? 18.952  40.715  2.156   1.00 97.35  ? 11  GLU D CG  1 
ATOM   6517  C CD  . GLU D 2 11  ? 19.202  42.053  1.475   1.00 103.09 ? 11  GLU D CD  1 
ATOM   6518  O OE1 . GLU D 2 11  ? 18.244  42.610  0.897   1.00 101.39 ? 11  GLU D OE1 1 
ATOM   6519  O OE2 . GLU D 2 11  ? 20.350  42.548  1.521   1.00 104.92 ? 11  GLU D OE2 1 
ATOM   6520  N N   . GLY D 2 12  ? 22.180  38.779  4.716   1.00 66.51  ? 12  GLY D N   1 
ATOM   6521  C CA  . GLY D 2 12  ? 23.477  38.155  4.911   1.00 63.84  ? 12  GLY D CA  1 
ATOM   6522  C C   . GLY D 2 12  ? 23.913  38.048  6.358   1.00 56.98  ? 12  GLY D C   1 
ATOM   6523  O O   . GLY D 2 12  ? 23.115  38.233  7.279   1.00 59.37  ? 12  GLY D O   1 
ATOM   6524  N N   . GLY D 2 13  ? 25.192  37.745  6.557   1.00 49.91  ? 13  GLY D N   1 
ATOM   6525  C CA  . GLY D 2 13  ? 25.741  37.593  7.891   1.00 52.32  ? 13  GLY D CA  1 
ATOM   6526  C C   . GLY D 2 13  ? 26.987  38.430  8.104   1.00 62.90  ? 13  GLY D C   1 
ATOM   6527  O O   . GLY D 2 13  ? 27.766  38.657  7.182   1.00 76.34  ? 13  GLY D O   1 
ATOM   6528  N N   . TRP D 2 14  ? 27.184  38.883  9.333   1.00 65.61  ? 14  TRP D N   1 
ATOM   6529  C CA  . TRP D 2 14  ? 28.296  39.764  9.641   1.00 70.54  ? 14  TRP D CA  1 
ATOM   6530  C C   . TRP D 2 14  ? 29.593  39.021  9.879   1.00 80.27  ? 14  TRP D C   1 
ATOM   6531  O O   . TRP D 2 14  ? 29.756  38.362  10.904  1.00 79.94  ? 14  TRP D O   1 
ATOM   6532  C CB  . TRP D 2 14  ? 27.976  40.579  10.881  1.00 70.31  ? 14  TRP D CB  1 
ATOM   6533  C CG  . TRP D 2 14  ? 26.664  41.234  10.802  1.00 70.26  ? 14  TRP D CG  1 
ATOM   6534  C CD1 . TRP D 2 14  ? 26.044  41.702  9.679   1.00 62.27  ? 14  TRP D CD1 1 
ATOM   6535  C CD2 . TRP D 2 14  ? 25.779  41.488  11.888  1.00 70.39  ? 14  TRP D CD2 1 
ATOM   6536  N NE1 . TRP D 2 14  ? 24.825  42.242  10.004  1.00 58.99  ? 14  TRP D NE1 1 
ATOM   6537  C CE2 . TRP D 2 14  ? 24.639  42.123  11.357  1.00 62.73  ? 14  TRP D CE2 1 
ATOM   6538  C CE3 . TRP D 2 14  ? 25.839  41.241  13.264  1.00 68.28  ? 14  TRP D CE3 1 
ATOM   6539  C CZ2 . TRP D 2 14  ? 23.569  42.508  12.152  1.00 59.01  ? 14  TRP D CZ2 1 
ATOM   6540  C CZ3 . TRP D 2 14  ? 24.779  41.625  14.051  1.00 63.35  ? 14  TRP D CZ3 1 
ATOM   6541  C CH2 . TRP D 2 14  ? 23.659  42.253  13.495  1.00 60.96  ? 14  TRP D CH2 1 
ATOM   6542  N N   . GLN D 2 15  ? 30.524  39.144  8.942   1.00 69.80  ? 15  GLN D N   1 
ATOM   6543  C CA  . GLN D 2 15  ? 31.872  38.647  9.170   1.00 73.12  ? 15  GLN D CA  1 
ATOM   6544  C C   . GLN D 2 15  ? 32.515  39.440  10.306  1.00 68.49  ? 15  GLN D C   1 
ATOM   6545  O O   . GLN D 2 15  ? 33.454  38.973  10.955  1.00 63.80  ? 15  GLN D O   1 
ATOM   6546  C CB  . GLN D 2 15  ? 32.706  38.753  7.896   1.00 78.89  ? 15  GLN D CB  1 
ATOM   6547  C CG  . GLN D 2 15  ? 32.187  37.901  6.758   1.00 78.74  ? 15  GLN D CG  1 
ATOM   6548  C CD  . GLN D 2 15  ? 33.254  36.989  6.191   1.00 79.98  ? 15  GLN D CD  1 
ATOM   6549  O OE1 . GLN D 2 15  ? 34.212  36.630  6.879   1.00 76.71  ? 15  GLN D OE1 1 
ATOM   6550  N NE2 . GLN D 2 15  ? 33.100  36.615  4.926   1.00 81.65  ? 15  GLN D NE2 1 
ATOM   6551  N N   . GLY D 2 16  ? 31.993  40.642  10.542  1.00 74.91  ? 16  GLY D N   1 
ATOM   6552  C CA  . GLY D 2 16  ? 32.480  41.498  11.608  1.00 77.66  ? 16  GLY D CA  1 
ATOM   6553  C C   . GLY D 2 16  ? 32.315  40.848  12.966  1.00 84.97  ? 16  GLY D C   1 
ATOM   6554  O O   . GLY D 2 16  ? 33.242  40.835  13.773  1.00 95.89  ? 16  GLY D O   1 
ATOM   6555  N N   . MET D 2 17  ? 31.129  40.304  13.220  1.00 94.08  ? 17  MET D N   1 
ATOM   6556  C CA  . MET D 2 17  ? 30.867  39.595  14.465  1.00 88.36  ? 17  MET D CA  1 
ATOM   6557  C C   . MET D 2 17  ? 31.805  38.410  14.566  1.00 91.17  ? 17  MET D C   1 
ATOM   6558  O O   . MET D 2 17  ? 31.845  37.571  13.670  1.00 92.82  ? 17  MET D O   1 
ATOM   6559  C CB  . MET D 2 17  ? 29.419  39.124  14.519  1.00 80.06  ? 17  MET D CB  1 
ATOM   6560  C CG  . MET D 2 17  ? 28.998  38.612  15.878  1.00 71.42  ? 17  MET D CG  1 
ATOM   6561  S SD  . MET D 2 17  ? 27.258  38.947  16.208  1.00 71.54  ? 17  MET D SD  1 
ATOM   6562  C CE  . MET D 2 17  ? 26.485  38.101  14.829  1.00 56.46  ? 17  MET D CE  1 
ATOM   6563  N N   . VAL D 2 18  ? 32.564  38.347  15.654  1.00 97.40  ? 18  VAL D N   1 
ATOM   6564  C CA  . VAL D 2 18  ? 33.630  37.357  15.780  1.00 101.79 ? 18  VAL D CA  1 
ATOM   6565  C C   . VAL D 2 18  ? 33.631  36.669  17.140  1.00 97.43  ? 18  VAL D C   1 
ATOM   6566  O O   . VAL D 2 18  ? 34.581  35.974  17.495  1.00 107.98 ? 18  VAL D O   1 
ATOM   6567  C CB  . VAL D 2 18  ? 35.008  38.017  15.577  1.00 111.98 ? 18  VAL D CB  1 
ATOM   6568  C CG1 . VAL D 2 18  ? 35.169  38.480  14.137  1.00 110.73 ? 18  VAL D CG1 1 
ATOM   6569  C CG2 . VAL D 2 18  ? 35.186  39.182  16.544  1.00 117.11 ? 18  VAL D CG2 1 
ATOM   6570  N N   . ASP D 2 19  ? 32.554  36.859  17.891  1.00 69.05  ? 19  ASP D N   1 
ATOM   6571  C CA  . ASP D 2 19  ? 32.527  36.491  19.300  1.00 74.76  ? 19  ASP D CA  1 
ATOM   6572  C C   . ASP D 2 19  ? 31.267  35.711  19.664  1.00 74.01  ? 19  ASP D C   1 
ATOM   6573  O O   . ASP D 2 19  ? 30.923  35.576  20.841  1.00 70.50  ? 19  ASP D O   1 
ATOM   6574  C CB  . ASP D 2 19  ? 32.629  37.753  20.161  1.00 79.55  ? 19  ASP D CB  1 
ATOM   6575  C CG  . ASP D 2 19  ? 31.748  38.891  19.643  1.00 81.85  ? 19  ASP D CG  1 
ATOM   6576  O OD1 . ASP D 2 19  ? 31.570  39.014  18.408  1.00 82.20  ? 19  ASP D OD1 1 
ATOM   6577  O OD2 . ASP D 2 19  ? 31.232  39.669  20.476  1.00 80.68  ? 19  ASP D OD2 1 
ATOM   6578  N N   . GLY D 2 20  ? 30.583  35.199  18.646  1.00 76.25  ? 20  GLY D N   1 
ATOM   6579  C CA  . GLY D 2 20  ? 29.342  34.484  18.861  1.00 64.81  ? 20  GLY D CA  1 
ATOM   6580  C C   . GLY D 2 20  ? 28.612  34.190  17.568  1.00 55.29  ? 20  GLY D C   1 
ATOM   6581  O O   . GLY D 2 20  ? 29.042  34.601  16.490  1.00 60.95  ? 20  GLY D O   1 
ATOM   6582  N N   . TRP D 2 21  ? 27.500  33.476  17.684  1.00 70.19  ? 21  TRP D N   1 
ATOM   6583  C CA  . TRP D 2 21  ? 26.750  33.012  16.527  1.00 75.96  ? 21  TRP D CA  1 
ATOM   6584  C C   . TRP D 2 21  ? 25.681  34.014  16.113  1.00 73.44  ? 21  TRP D C   1 
ATOM   6585  O O   . TRP D 2 21  ? 25.425  34.198  14.927  1.00 69.85  ? 21  TRP D O   1 
ATOM   6586  C CB  . TRP D 2 21  ? 26.102  31.651  16.821  1.00 79.88  ? 21  TRP D CB  1 
ATOM   6587  C CG  . TRP D 2 21  ? 26.984  30.453  16.551  1.00 78.04  ? 21  TRP D CG  1 
ATOM   6588  C CD1 . TRP D 2 21  ? 28.078  30.401  15.736  1.00 83.38  ? 21  TRP D CD1 1 
ATOM   6589  C CD2 . TRP D 2 21  ? 26.833  29.138  17.099  1.00 73.51  ? 21  TRP D CD2 1 
ATOM   6590  N NE1 . TRP D 2 21  ? 28.615  29.137  15.744  1.00 82.63  ? 21  TRP D NE1 1 
ATOM   6591  C CE2 . TRP D 2 21  ? 27.870  28.345  16.575  1.00 74.65  ? 21  TRP D CE2 1 
ATOM   6592  C CE3 . TRP D 2 21  ? 25.919  28.554  17.981  1.00 71.01  ? 21  TRP D CE3 1 
ATOM   6593  C CZ2 . TRP D 2 21  ? 28.017  27.001  16.906  1.00 70.72  ? 21  TRP D CZ2 1 
ATOM   6594  C CZ3 . TRP D 2 21  ? 26.070  27.221  18.309  1.00 66.36  ? 21  TRP D CZ3 1 
ATOM   6595  C CH2 . TRP D 2 21  ? 27.109  26.460  17.774  1.00 69.53  ? 21  TRP D CH2 1 
ATOM   6596  N N   . TYR D 2 22  ? 25.044  34.647  17.092  1.00 76.27  ? 22  TYR D N   1 
ATOM   6597  C CA  . TYR D 2 22  ? 24.038  35.663  16.800  1.00 73.68  ? 22  TYR D CA  1 
ATOM   6598  C C   . TYR D 2 22  ? 24.131  36.848  17.759  1.00 81.00  ? 22  TYR D C   1 
ATOM   6599  O O   . TYR D 2 22  ? 23.960  36.696  18.968  1.00 94.18  ? 22  TYR D O   1 
ATOM   6600  C CB  . TYR D 2 22  ? 22.629  35.076  16.855  1.00 64.41  ? 22  TYR D CB  1 
ATOM   6601  C CG  . TYR D 2 22  ? 22.555  33.566  16.919  1.00 74.55  ? 22  TYR D CG  1 
ATOM   6602  C CD1 . TYR D 2 22  ? 22.396  32.808  15.767  1.00 79.88  ? 22  TYR D CD1 1 
ATOM   6603  C CD2 . TYR D 2 22  ? 22.618  32.899  18.132  1.00 74.86  ? 22  TYR D CD2 1 
ATOM   6604  C CE1 . TYR D 2 22  ? 22.316  31.427  15.821  1.00 72.87  ? 22  TYR D CE1 1 
ATOM   6605  C CE2 . TYR D 2 22  ? 22.539  31.519  18.193  1.00 69.58  ? 22  TYR D CE2 1 
ATOM   6606  C CZ  . TYR D 2 22  ? 22.386  30.791  17.035  1.00 67.95  ? 22  TYR D CZ  1 
ATOM   6607  O OH  . TYR D 2 22  ? 22.304  29.421  17.092  1.00 64.76  ? 22  TYR D OH  1 
ATOM   6608  N N   . GLY D 2 23  ? 24.390  38.032  17.215  1.00 56.00  ? 23  GLY D N   1 
ATOM   6609  C CA  . GLY D 2 23  ? 24.509  39.229  18.030  1.00 50.54  ? 23  GLY D CA  1 
ATOM   6610  C C   . GLY D 2 23  ? 23.937  40.481  17.386  1.00 60.28  ? 23  GLY D C   1 
ATOM   6611  O O   . GLY D 2 23  ? 23.122  40.407  16.462  1.00 62.79  ? 23  GLY D O   1 
ATOM   6612  N N   . TYR D 2 24  ? 24.376  41.639  17.876  1.00 63.41  ? 24  TYR D N   1 
ATOM   6613  C CA  . TYR D 2 24  ? 23.848  42.924  17.423  1.00 56.69  ? 24  TYR D CA  1 
ATOM   6614  C C   . TYR D 2 24  ? 24.894  43.791  16.724  1.00 61.97  ? 24  TYR D C   1 
ATOM   6615  O O   . TYR D 2 24  ? 26.103  43.617  16.912  1.00 68.10  ? 24  TYR D O   1 
ATOM   6616  C CB  . TYR D 2 24  ? 23.280  43.717  18.602  1.00 57.66  ? 24  TYR D CB  1 
ATOM   6617  C CG  . TYR D 2 24  ? 22.647  42.886  19.696  1.00 62.51  ? 24  TYR D CG  1 
ATOM   6618  C CD1 . TYR D 2 24  ? 21.270  42.721  19.762  1.00 58.42  ? 24  TYR D CD1 1 
ATOM   6619  C CD2 . TYR D 2 24  ? 23.426  42.289  20.678  1.00 62.75  ? 24  TYR D CD2 1 
ATOM   6620  C CE1 . TYR D 2 24  ? 20.686  41.971  20.768  1.00 53.26  ? 24  TYR D CE1 1 
ATOM   6621  C CE2 . TYR D 2 24  ? 22.856  41.540  21.688  1.00 55.22  ? 24  TYR D CE2 1 
ATOM   6622  C CZ  . TYR D 2 24  ? 21.484  41.380  21.730  1.00 53.12  ? 24  TYR D CZ  1 
ATOM   6623  O OH  . TYR D 2 24  ? 20.914  40.627  22.739  1.00 61.15  ? 24  TYR D OH  1 
ATOM   6624  N N   . HIS D 2 25  ? 24.406  44.724  15.911  1.00 73.04  ? 25  HIS D N   1 
ATOM   6625  C CA  . HIS D 2 25  ? 25.209  45.844  15.436  1.00 78.12  ? 25  HIS D CA  1 
ATOM   6626  C C   . HIS D 2 25  ? 24.431  47.123  15.688  1.00 89.26  ? 25  HIS D C   1 
ATOM   6627  O O   . HIS D 2 25  ? 23.273  47.235  15.283  1.00 92.39  ? 25  HIS D O   1 
ATOM   6628  C CB  . HIS D 2 25  ? 25.521  45.731  13.948  1.00 75.85  ? 25  HIS D CB  1 
ATOM   6629  C CG  . HIS D 2 25  ? 26.328  46.877  13.419  1.00 84.52  ? 25  HIS D CG  1 
ATOM   6630  N ND1 . HIS D 2 25  ? 27.694  46.962  13.581  1.00 93.95  ? 25  HIS D ND1 1 
ATOM   6631  C CD2 . HIS D 2 25  ? 25.959  47.995  12.751  1.00 86.44  ? 25  HIS D CD2 1 
ATOM   6632  C CE1 . HIS D 2 25  ? 28.134  48.076  13.025  1.00 96.30  ? 25  HIS D CE1 1 
ATOM   6633  N NE2 . HIS D 2 25  ? 27.100  48.723  12.515  1.00 95.71  ? 25  HIS D NE2 1 
ATOM   6634  N N   . HIS D 2 26  ? 25.058  48.081  16.365  1.00 82.75  ? 26  HIS D N   1 
ATOM   6635  C CA  . HIS D 2 26  ? 24.411  49.360  16.638  1.00 76.06  ? 26  HIS D CA  1 
ATOM   6636  C C   . HIS D 2 26  ? 25.129  50.495  15.935  1.00 80.63  ? 26  HIS D C   1 
ATOM   6637  O O   . HIS D 2 26  ? 26.274  50.349  15.502  1.00 83.14  ? 26  HIS D O   1 
ATOM   6638  C CB  . HIS D 2 26  ? 24.383  49.652  18.137  1.00 73.83  ? 26  HIS D CB  1 
ATOM   6639  C CG  . HIS D 2 26  ? 25.739  49.869  18.731  1.00 78.57  ? 26  HIS D CG  1 
ATOM   6640  N ND1 . HIS D 2 26  ? 26.279  49.031  19.682  1.00 82.68  ? 26  HIS D ND1 1 
ATOM   6641  C CD2 . HIS D 2 26  ? 26.670  50.823  18.502  1.00 82.89  ? 26  HIS D CD2 1 
ATOM   6642  C CE1 . HIS D 2 26  ? 27.481  49.462  20.018  1.00 86.18  ? 26  HIS D CE1 1 
ATOM   6643  N NE2 . HIS D 2 26  ? 27.742  50.548  19.314  1.00 89.18  ? 26  HIS D NE2 1 
ATOM   6644  N N   . SER D 2 27  ? 24.436  51.625  15.831  1.00 80.29  ? 27  SER D N   1 
ATOM   6645  C CA  . SER D 2 27  ? 25.032  52.883  15.397  1.00 77.51  ? 27  SER D CA  1 
ATOM   6646  C C   . SER D 2 27  ? 24.298  54.034  16.076  1.00 78.66  ? 27  SER D C   1 
ATOM   6647  O O   . SER D 2 27  ? 23.185  54.387  15.688  1.00 83.50  ? 27  SER D O   1 
ATOM   6648  C CB  . SER D 2 27  ? 24.967  53.034  13.877  1.00 77.17  ? 27  SER D CB  1 
ATOM   6649  O OG  . SER D 2 27  ? 25.668  54.191  13.455  1.00 86.57  ? 27  SER D OG  1 
ATOM   6650  N N   . ASN D 2 28  ? 24.913  54.594  17.110  1.00 65.74  ? 28  ASN D N   1 
ATOM   6651  C CA  . ASN D 2 28  ? 24.363  55.761  17.789  1.00 70.97  ? 28  ASN D CA  1 
ATOM   6652  C C   . ASN D 2 28  ? 25.289  56.977  17.638  1.00 84.63  ? 28  ASN D C   1 
ATOM   6653  O O   . ASN D 2 28  ? 26.287  56.912  16.916  1.00 90.76  ? 28  ASN D O   1 
ATOM   6654  C CB  . ASN D 2 28  ? 24.091  55.453  19.265  1.00 65.03  ? 28  ASN D CB  1 
ATOM   6655  C CG  . ASN D 2 28  ? 25.329  54.971  20.004  1.00 66.99  ? 28  ASN D CG  1 
ATOM   6656  O OD1 . ASN D 2 28  ? 26.416  54.864  19.426  1.00 73.52  ? 28  ASN D OD1 1 
ATOM   6657  N ND2 . ASN D 2 28  ? 25.170  54.678  21.295  1.00 65.20  ? 28  ASN D ND2 1 
ATOM   6658  N N   . ASP D 2 29  ? 24.964  58.081  18.310  1.00 98.03  ? 29  ASP D N   1 
ATOM   6659  C CA  . ASP D 2 29  ? 25.794  59.284  18.238  1.00 94.25  ? 29  ASP D CA  1 
ATOM   6660  C C   . ASP D 2 29  ? 27.215  59.041  18.758  1.00 96.16  ? 29  ASP D C   1 
ATOM   6661  O O   . ASP D 2 29  ? 28.100  59.875  18.568  1.00 101.43 ? 29  ASP D O   1 
ATOM   6662  C CB  . ASP D 2 29  ? 25.152  60.449  19.004  1.00 90.51  ? 29  ASP D CB  1 
ATOM   6663  C CG  . ASP D 2 29  ? 24.123  61.211  18.176  1.00 87.01  ? 29  ASP D CG  1 
ATOM   6664  O OD1 . ASP D 2 29  ? 24.151  61.101  16.933  1.00 87.13  ? 29  ASP D OD1 1 
ATOM   6665  O OD2 . ASP D 2 29  ? 23.293  61.935  18.772  1.00 85.67  ? 29  ASP D OD2 1 
ATOM   6666  N N   . GLN D 2 30  ? 27.431  57.899  19.410  1.00 73.02  ? 30  GLN D N   1 
ATOM   6667  C CA  . GLN D 2 30  ? 28.726  57.602  20.022  1.00 76.78  ? 30  GLN D CA  1 
ATOM   6668  C C   . GLN D 2 30  ? 29.623  56.721  19.153  1.00 80.23  ? 30  GLN D C   1 
ATOM   6669  O O   . GLN D 2 30  ? 30.823  56.610  19.406  1.00 85.44  ? 30  GLN D O   1 
ATOM   6670  C CB  . GLN D 2 30  ? 28.541  56.950  21.392  1.00 77.11  ? 30  GLN D CB  1 
ATOM   6671  C CG  . GLN D 2 30  ? 27.574  57.677  22.306  1.00 79.02  ? 30  GLN D CG  1 
ATOM   6672  C CD  . GLN D 2 30  ? 27.706  57.237  23.753  1.00 86.50  ? 30  GLN D CD  1 
ATOM   6673  O OE1 . GLN D 2 30  ? 28.814  57.090  24.272  1.00 97.69  ? 30  GLN D OE1 1 
ATOM   6674  N NE2 . GLN D 2 30  ? 26.575  57.021  24.410  1.00 77.92  ? 30  GLN D NE2 1 
ATOM   6675  N N   . GLY D 2 31  ? 29.045  56.091  18.136  1.00 93.26  ? 31  GLY D N   1 
ATOM   6676  C CA  . GLY D 2 31  ? 29.816  55.236  17.252  1.00 94.33  ? 31  GLY D CA  1 
ATOM   6677  C C   . GLY D 2 31  ? 29.097  53.963  16.843  1.00 93.34  ? 31  GLY D C   1 
ATOM   6678  O O   . GLY D 2 31  ? 27.895  53.817  17.069  1.00 93.32  ? 31  GLY D O   1 
ATOM   6679  N N   . SER D 2 32  ? 29.842  53.040  16.241  1.00 95.40  ? 32  SER D N   1 
ATOM   6680  C CA  . SER D 2 32  ? 29.262  51.819  15.703  1.00 94.44  ? 32  SER D CA  1 
ATOM   6681  C C   . SER D 2 32  ? 30.106  50.597  16.042  1.00 100.74 ? 32  SER D C   1 
ATOM   6682  O O   . SER D 2 32  ? 31.252  50.723  16.483  1.00 105.92 ? 32  SER D O   1 
ATOM   6683  C CB  . SER D 2 32  ? 29.113  51.933  14.186  1.00 98.86  ? 32  SER D CB  1 
ATOM   6684  O OG  . SER D 2 32  ? 30.377  52.097  13.565  1.00 110.59 ? 32  SER D OG  1 
ATOM   6685  N N   . GLY D 2 33  ? 29.533  49.415  15.830  1.00 91.50  ? 33  GLY D N   1 
ATOM   6686  C CA  . GLY D 2 33  ? 30.252  48.173  16.043  1.00 86.70  ? 33  GLY D CA  1 
ATOM   6687  C C   . GLY D 2 33  ? 29.370  46.958  16.267  1.00 80.21  ? 33  GLY D C   1 
ATOM   6688  O O   . GLY D 2 33  ? 28.149  47.066  16.402  1.00 72.78  ? 33  GLY D O   1 
ATOM   6689  N N   . TYR D 2 34  ? 30.003  45.791  16.306  1.00 80.96  ? 34  TYR D N   1 
ATOM   6690  C CA  . TYR D 2 34  ? 29.297  44.542  16.558  1.00 76.14  ? 34  TYR D CA  1 
ATOM   6691  C C   . TYR D 2 34  ? 29.463  44.111  18.012  1.00 81.43  ? 34  TYR D C   1 
ATOM   6692  O O   . TYR D 2 34  ? 30.213  44.729  18.773  1.00 89.00  ? 34  TYR D O   1 
ATOM   6693  C CB  . TYR D 2 34  ? 29.801  43.434  15.627  1.00 77.75  ? 34  TYR D CB  1 
ATOM   6694  C CG  . TYR D 2 34  ? 29.600  43.703  14.146  1.00 79.07  ? 34  TYR D CG  1 
ATOM   6695  C CD1 . TYR D 2 34  ? 28.339  43.626  13.571  1.00 76.48  ? 34  TYR D CD1 1 
ATOM   6696  C CD2 . TYR D 2 34  ? 30.677  44.009  13.321  1.00 83.51  ? 34  TYR D CD2 1 
ATOM   6697  C CE1 . TYR D 2 34  ? 28.152  43.863  12.218  1.00 78.35  ? 34  TYR D CE1 1 
ATOM   6698  C CE2 . TYR D 2 34  ? 30.498  44.244  11.966  1.00 84.38  ? 34  TYR D CE2 1 
ATOM   6699  C CZ  . TYR D 2 34  ? 29.233  44.172  11.421  1.00 78.76  ? 34  TYR D CZ  1 
ATOM   6700  O OH  . TYR D 2 34  ? 29.038  44.404  10.078  1.00 75.18  ? 34  TYR D OH  1 
ATOM   6701  N N   . ALA D 2 35  ? 28.756  43.047  18.382  1.00 99.44  ? 35  ALA D N   1 
ATOM   6702  C CA  . ALA D 2 35  ? 28.800  42.490  19.732  1.00 101.53 ? 35  ALA D CA  1 
ATOM   6703  C C   . ALA D 2 35  ? 27.723  41.420  19.871  1.00 100.13 ? 35  ALA D C   1 
ATOM   6704  O O   . ALA D 2 35  ? 26.536  41.733  19.930  1.00 106.61 ? 35  ALA D O   1 
ATOM   6705  C CB  . ALA D 2 35  ? 28.603  43.580  20.775  1.00 98.75  ? 35  ALA D CB  1 
ATOM   6706  N N   . ALA D 2 36  ? 28.142  40.159  19.928  1.00 63.21  ? 36  ALA D N   1 
ATOM   6707  C CA  . ALA D 2 36  ? 27.211  39.033  19.928  1.00 57.85  ? 36  ALA D CA  1 
ATOM   6708  C C   . ALA D 2 36  ? 26.507  38.818  21.272  1.00 58.52  ? 36  ALA D C   1 
ATOM   6709  O O   . ALA D 2 36  ? 27.023  39.205  22.321  1.00 64.87  ? 36  ALA D O   1 
ATOM   6710  C CB  . ALA D 2 36  ? 27.925  37.768  19.493  1.00 56.02  ? 36  ALA D CB  1 
ATOM   6711  N N   . ASP D 2 37  ? 25.330  38.194  21.227  1.00 65.95  ? 37  ASP D N   1 
ATOM   6712  C CA  . ASP D 2 37  ? 24.538  37.934  22.430  1.00 65.26  ? 37  ASP D CA  1 
ATOM   6713  C C   . ASP D 2 37  ? 25.043  36.715  23.201  1.00 76.82  ? 37  ASP D C   1 
ATOM   6714  O O   . ASP D 2 37  ? 24.922  35.582  22.740  1.00 77.61  ? 37  ASP D O   1 
ATOM   6715  C CB  . ASP D 2 37  ? 23.061  37.749  22.070  1.00 64.67  ? 37  ASP D CB  1 
ATOM   6716  C CG  . ASP D 2 37  ? 22.152  37.777  23.290  1.00 75.38  ? 37  ASP D CG  1 
ATOM   6717  O OD1 . ASP D 2 37  ? 22.614  38.198  24.375  1.00 78.02  ? 37  ASP D OD1 1 
ATOM   6718  O OD2 . ASP D 2 37  ? 20.969  37.392  23.162  1.00 76.76  ? 37  ASP D OD2 1 
ATOM   6719  N N   . LYS D 2 38  ? 25.601  36.964  24.381  1.00 92.17  ? 38  LYS D N   1 
ATOM   6720  C CA  . LYS D 2 38  ? 26.166  35.916  25.231  1.00 96.17  ? 38  LYS D CA  1 
ATOM   6721  C C   . LYS D 2 38  ? 25.227  34.720  25.463  1.00 89.89  ? 38  LYS D C   1 
ATOM   6722  O O   . LYS D 2 38  ? 25.644  33.570  25.332  1.00 84.37  ? 38  LYS D O   1 
ATOM   6723  C CB  . LYS D 2 38  ? 26.604  36.524  26.572  1.00 109.73 ? 38  LYS D CB  1 
ATOM   6724  C CG  . LYS D 2 38  ? 26.872  35.517  27.688  1.00 122.65 ? 38  LYS D CG  1 
ATOM   6725  C CD  . LYS D 2 38  ? 26.867  36.198  29.060  1.00 130.50 ? 38  LYS D CD  1 
ATOM   6726  C CE  . LYS D 2 38  ? 26.943  35.178  30.191  1.00 132.72 ? 38  LYS D CE  1 
ATOM   6727  N NZ  . LYS D 2 38  ? 26.771  35.793  31.535  1.00 132.81 ? 38  LYS D NZ  1 
ATOM   6728  N N   . GLU D 2 39  ? 23.970  34.992  25.808  1.00 90.86  ? 39  GLU D N   1 
ATOM   6729  C CA  . GLU D 2 39  ? 23.009  33.935  26.129  1.00 91.38  ? 39  GLU D CA  1 
ATOM   6730  C C   . GLU D 2 39  ? 22.648  33.061  24.932  1.00 86.02  ? 39  GLU D C   1 
ATOM   6731  O O   . GLU D 2 39  ? 23.034  31.896  24.872  1.00 87.04  ? 39  GLU D O   1 
ATOM   6732  C CB  . GLU D 2 39  ? 21.737  34.519  26.751  1.00 100.15 ? 39  GLU D CB  1 
ATOM   6733  C CG  . GLU D 2 39  ? 21.752  34.546  28.268  1.00 112.48 ? 39  GLU D CG  1 
ATOM   6734  C CD  . GLU D 2 39  ? 22.911  35.352  28.819  1.00 126.25 ? 39  GLU D CD  1 
ATOM   6735  O OE1 . GLU D 2 39  ? 23.218  36.416  28.241  1.00 133.17 ? 39  GLU D OE1 1 
ATOM   6736  O OE2 . GLU D 2 39  ? 23.519  34.919  29.822  1.00 127.97 ? 39  GLU D OE2 1 
ATOM   6737  N N   . SER D 2 40  ? 21.899  33.622  23.988  1.00 86.59  ? 40  SER D N   1 
ATOM   6738  C CA  . SER D 2 40  ? 21.492  32.891  22.788  1.00 83.98  ? 40  SER D CA  1 
ATOM   6739  C C   . SER D 2 40  ? 22.640  32.080  22.188  1.00 81.45  ? 40  SER D C   1 
ATOM   6740  O O   . SER D 2 40  ? 22.501  30.889  21.932  1.00 74.29  ? 40  SER D O   1 
ATOM   6741  C CB  . SER D 2 40  ? 20.938  33.858  21.739  1.00 76.39  ? 40  SER D CB  1 
ATOM   6742  O OG  . SER D 2 40  ? 21.879  34.878  21.445  1.00 73.73  ? 40  SER D OG  1 
ATOM   6743  N N   . THR D 2 41  ? 23.775  32.733  21.969  1.00 74.52  ? 41  THR D N   1 
ATOM   6744  C CA  . THR D 2 41  ? 24.928  32.088  21.354  1.00 70.78  ? 41  THR D CA  1 
ATOM   6745  C C   . THR D 2 41  ? 25.452  30.939  22.209  1.00 70.77  ? 41  THR D C   1 
ATOM   6746  O O   . THR D 2 41  ? 26.208  30.096  21.735  1.00 68.34  ? 41  THR D O   1 
ATOM   6747  C CB  . THR D 2 41  ? 26.070  33.086  21.135  1.00 76.12  ? 41  THR D CB  1 
ATOM   6748  O OG1 . THR D 2 41  ? 26.916  32.621  20.080  1.00 81.47  ? 41  THR D OG1 1 
ATOM   6749  C CG2 . THR D 2 41  ? 26.890  33.236  22.407  1.00 84.72  ? 41  THR D CG2 1 
ATOM   6750  N N   . GLN D 2 42  ? 25.054  30.911  23.474  1.00 66.47  ? 42  GLN D N   1 
ATOM   6751  C CA  . GLN D 2 42  ? 25.514  29.880  24.391  1.00 72.00  ? 42  GLN D CA  1 
ATOM   6752  C C   . GLN D 2 42  ? 24.466  28.780  24.518  1.00 64.74  ? 42  GLN D C   1 
ATOM   6753  O O   . GLN D 2 42  ? 24.796  27.599  24.603  1.00 68.81  ? 42  GLN D O   1 
ATOM   6754  C CB  . GLN D 2 42  ? 25.816  30.486  25.761  1.00 80.09  ? 42  GLN D CB  1 
ATOM   6755  C CG  . GLN D 2 42  ? 26.374  29.495  26.752  1.00 87.10  ? 42  GLN D CG  1 
ATOM   6756  C CD  . GLN D 2 42  ? 27.574  28.766  26.201  1.00 95.86  ? 42  GLN D CD  1 
ATOM   6757  O OE1 . GLN D 2 42  ? 28.319  29.307  25.382  1.00 100.06 ? 42  GLN D OE1 1 
ATOM   6758  N NE2 . GLN D 2 42  ? 27.765  27.526  26.636  1.00 96.40  ? 42  GLN D NE2 1 
ATOM   6759  N N   . LYS D 2 43  ? 23.201  29.188  24.535  1.00 73.48  ? 43  LYS D N   1 
ATOM   6760  C CA  . LYS D 2 43  ? 22.074  28.266  24.576  1.00 68.88  ? 43  LYS D CA  1 
ATOM   6761  C C   . LYS D 2 43  ? 22.109  27.361  23.347  1.00 62.43  ? 43  LYS D C   1 
ATOM   6762  O O   . LYS D 2 43  ? 21.755  26.182  23.410  1.00 66.17  ? 43  LYS D O   1 
ATOM   6763  C CB  . LYS D 2 43  ? 20.762  29.060  24.643  1.00 73.42  ? 43  LYS D CB  1 
ATOM   6764  C CG  . LYS D 2 43  ? 19.484  28.247  24.461  1.00 80.49  ? 43  LYS D CG  1 
ATOM   6765  C CD  . LYS D 2 43  ? 18.248  29.074  24.830  1.00 89.75  ? 43  LYS D CD  1 
ATOM   6766  C CE  . LYS D 2 43  ? 16.959  28.467  24.282  1.00 94.60  ? 43  LYS D CE  1 
ATOM   6767  N NZ  . LYS D 2 43  ? 16.771  27.050  24.689  1.00 94.16  ? 43  LYS D NZ  1 
ATOM   6768  N N   . ALA D 2 44  ? 22.562  27.922  22.234  1.00 51.00  ? 44  ALA D N   1 
ATOM   6769  C CA  . ALA D 2 44  ? 22.667  27.197  20.977  1.00 48.10  ? 44  ALA D CA  1 
ATOM   6770  C C   . ALA D 2 44  ? 23.836  26.222  21.004  1.00 64.40  ? 44  ALA D C   1 
ATOM   6771  O O   . ALA D 2 44  ? 23.677  25.038  20.717  1.00 67.25  ? 44  ALA D O   1 
ATOM   6772  C CB  . ALA D 2 44  ? 22.838  28.177  19.824  1.00 40.71  ? 44  ALA D CB  1 
ATOM   6773  N N   . PHE D 2 45  ? 25.016  26.736  21.334  1.00 61.49  ? 45  PHE D N   1 
ATOM   6774  C CA  . PHE D 2 45  ? 26.223  25.928  21.366  1.00 57.27  ? 45  PHE D CA  1 
ATOM   6775  C C   . PHE D 2 45  ? 26.061  24.757  22.309  1.00 58.58  ? 45  PHE D C   1 
ATOM   6776  O O   . PHE D 2 45  ? 26.584  23.678  22.052  1.00 68.17  ? 45  PHE D O   1 
ATOM   6777  C CB  . PHE D 2 45  ? 27.422  26.767  21.786  1.00 65.18  ? 45  PHE D CB  1 
ATOM   6778  C CG  . PHE D 2 45  ? 28.696  25.990  21.879  1.00 70.09  ? 45  PHE D CG  1 
ATOM   6779  C CD1 . PHE D 2 45  ? 29.441  25.721  20.744  1.00 67.82  ? 45  PHE D CD1 1 
ATOM   6780  C CD2 . PHE D 2 45  ? 29.151  25.525  23.102  1.00 74.34  ? 45  PHE D CD2 1 
ATOM   6781  C CE1 . PHE D 2 45  ? 30.618  25.002  20.826  1.00 72.63  ? 45  PHE D CE1 1 
ATOM   6782  C CE2 . PHE D 2 45  ? 30.329  24.804  23.191  1.00 76.31  ? 45  PHE D CE2 1 
ATOM   6783  C CZ  . PHE D 2 45  ? 31.064  24.541  22.052  1.00 75.66  ? 45  PHE D CZ  1 
ATOM   6784  N N   . ASP D 2 46  ? 25.344  24.968  23.407  1.00 61.70  ? 46  ASP D N   1 
ATOM   6785  C CA  . ASP D 2 46  ? 25.030  23.864  24.304  1.00 65.89  ? 46  ASP D CA  1 
ATOM   6786  C C   . ASP D 2 46  ? 24.199  22.821  23.554  1.00 56.42  ? 46  ASP D C   1 
ATOM   6787  O O   . ASP D 2 46  ? 24.576  21.650  23.477  1.00 55.44  ? 46  ASP D O   1 
ATOM   6788  C CB  . ASP D 2 46  ? 24.303  24.353  25.561  1.00 68.79  ? 46  ASP D CB  1 
ATOM   6789  C CG  . ASP D 2 46  ? 25.255  24.896  26.614  1.00 75.23  ? 46  ASP D CG  1 
ATOM   6790  O OD1 . ASP D 2 46  ? 26.479  24.666  26.491  1.00 80.28  ? 46  ASP D OD1 1 
ATOM   6791  O OD2 . ASP D 2 46  ? 24.774  25.543  27.572  1.00 69.75  ? 46  ASP D OD2 1 
ATOM   6792  N N   . GLY D 2 47  ? 23.082  23.258  22.982  1.00 60.62  ? 47  GLY D N   1 
ATOM   6793  C CA  . GLY D 2 47  ? 22.256  22.394  22.165  1.00 53.04  ? 47  GLY D CA  1 
ATOM   6794  C C   . GLY D 2 47  ? 23.086  21.576  21.198  1.00 52.68  ? 47  GLY D C   1 
ATOM   6795  O O   . GLY D 2 47  ? 23.251  20.376  21.385  1.00 55.21  ? 47  GLY D O   1 
ATOM   6796  N N   . ILE D 2 48  ? 23.619  22.223  20.169  1.00 55.87  ? 48  ILE D N   1 
ATOM   6797  C CA  . ILE D 2 48  ? 24.406  21.530  19.155  1.00 55.57  ? 48  ILE D CA  1 
ATOM   6798  C C   . ILE D 2 48  ? 25.427  20.565  19.762  1.00 68.91  ? 48  ILE D C   1 
ATOM   6799  O O   . ILE D 2 48  ? 25.526  19.413  19.330  1.00 75.02  ? 48  ILE D O   1 
ATOM   6800  C CB  . ILE D 2 48  ? 25.115  22.519  18.220  1.00 56.21  ? 48  ILE D CB  1 
ATOM   6801  C CG1 . ILE D 2 48  ? 24.094  23.458  17.583  1.00 57.63  ? 48  ILE D CG1 1 
ATOM   6802  C CG2 . ILE D 2 48  ? 25.870  21.771  17.141  1.00 63.28  ? 48  ILE D CG2 1 
ATOM   6803  C CD1 . ILE D 2 48  ? 23.132  22.754  16.661  1.00 56.21  ? 48  ILE D CD1 1 
ATOM   6804  N N   . THR D 2 49  ? 26.177  21.027  20.762  1.00 63.37  ? 49  THR D N   1 
ATOM   6805  C CA  . THR D 2 49  ? 27.107  20.153  21.474  1.00 67.17  ? 49  THR D CA  1 
ATOM   6806  C C   . THR D 2 49  ? 26.392  18.888  21.943  1.00 65.92  ? 49  THR D C   1 
ATOM   6807  O O   . THR D 2 49  ? 26.855  17.773  21.720  1.00 69.54  ? 49  THR D O   1 
ATOM   6808  C CB  . THR D 2 49  ? 27.733  20.848  22.693  1.00 67.14  ? 49  THR D CB  1 
ATOM   6809  O OG1 . THR D 2 49  ? 28.884  21.594  22.280  1.00 76.16  ? 49  THR D OG1 1 
ATOM   6810  C CG2 . THR D 2 49  ? 28.159  19.818  23.726  1.00 56.38  ? 49  THR D CG2 1 
ATOM   6811  N N   . ASN D 2 50  ? 25.249  19.073  22.586  1.00 83.30  ? 50  ASN D N   1 
ATOM   6812  C CA  . ASN D 2 50  ? 24.455  17.956  23.057  1.00 72.64  ? 50  ASN D CA  1 
ATOM   6813  C C   . ASN D 2 50  ? 23.980  17.073  21.907  1.00 73.67  ? 50  ASN D C   1 
ATOM   6814  O O   . ASN D 2 50  ? 23.886  15.855  22.052  1.00 79.10  ? 50  ASN D O   1 
ATOM   6815  C CB  . ASN D 2 50  ? 23.261  18.469  23.852  1.00 67.18  ? 50  ASN D CB  1 
ATOM   6816  C CG  . ASN D 2 50  ? 22.762  17.465  24.852  1.00 78.75  ? 50  ASN D CG  1 
ATOM   6817  O OD1 . ASN D 2 50  ? 21.969  16.583  24.517  1.00 79.60  ? 50  ASN D OD1 1 
ATOM   6818  N ND2 . ASN D 2 50  ? 23.228  17.581  26.091  1.00 86.62  ? 50  ASN D ND2 1 
ATOM   6819  N N   . LYS D 2 51  ? 23.683  17.681  20.763  1.00 59.11  ? 51  LYS D N   1 
ATOM   6820  C CA  . LYS D 2 51  ? 23.188  16.922  19.621  1.00 48.42  ? 51  LYS D CA  1 
ATOM   6821  C C   . LYS D 2 51  ? 24.237  15.960  19.074  1.00 57.26  ? 51  LYS D C   1 
ATOM   6822  O O   . LYS D 2 51  ? 23.925  14.808  18.797  1.00 61.58  ? 51  LYS D O   1 
ATOM   6823  C CB  . LYS D 2 51  ? 22.685  17.840  18.508  1.00 43.97  ? 51  LYS D CB  1 
ATOM   6824  C CG  . LYS D 2 51  ? 22.410  17.109  17.196  1.00 42.54  ? 51  LYS D CG  1 
ATOM   6825  C CD  . LYS D 2 51  ? 21.912  18.037  16.080  1.00 42.82  ? 51  LYS D CD  1 
ATOM   6826  C CE  . LYS D 2 51  ? 20.577  18.684  16.437  1.00 46.86  ? 51  LYS D CE  1 
ATOM   6827  N NZ  . LYS D 2 51  ? 19.720  18.984  15.253  1.00 51.93  ? 51  LYS D NZ  1 
ATOM   6828  N N   . VAL D 2 52  ? 25.480  16.408  18.921  1.00 47.25  ? 52  VAL D N   1 
ATOM   6829  C CA  . VAL D 2 52  ? 26.497  15.497  18.395  1.00 51.75  ? 52  VAL D CA  1 
ATOM   6830  C C   . VAL D 2 52  ? 26.801  14.380  19.386  1.00 63.17  ? 52  VAL D C   1 
ATOM   6831  O O   . VAL D 2 52  ? 27.169  13.273  18.989  1.00 76.47  ? 52  VAL D O   1 
ATOM   6832  C CB  . VAL D 2 52  ? 27.814  16.194  17.986  1.00 62.19  ? 52  VAL D CB  1 
ATOM   6833  C CG1 . VAL D 2 52  ? 27.564  17.650  17.628  1.00 58.01  ? 52  VAL D CG1 1 
ATOM   6834  C CG2 . VAL D 2 52  ? 28.866  16.054  19.084  1.00 66.44  ? 52  VAL D CG2 1 
ATOM   6835  N N   . ASN D 2 53  ? 26.650  14.660  20.674  1.00 65.41  ? 53  ASN D N   1 
ATOM   6836  C CA  . ASN D 2 53  ? 26.894  13.632  21.675  1.00 70.60  ? 53  ASN D CA  1 
ATOM   6837  C C   . ASN D 2 53  ? 25.794  12.577  21.652  1.00 66.49  ? 53  ASN D C   1 
ATOM   6838  O O   . ASN D 2 53  ? 26.073  11.382  21.687  1.00 67.00  ? 53  ASN D O   1 
ATOM   6839  C CB  . ASN D 2 53  ? 27.055  14.234  23.070  1.00 78.23  ? 53  ASN D CB  1 
ATOM   6840  C CG  . ASN D 2 53  ? 28.248  15.166  23.166  1.00 90.06  ? 53  ASN D CG  1 
ATOM   6841  O OD1 . ASN D 2 53  ? 29.116  15.177  22.290  1.00 88.67  ? 53  ASN D OD1 1 
ATOM   6842  N ND2 . ASN D 2 53  ? 28.299  15.954  24.235  1.00 95.01  ? 53  ASN D ND2 1 
ATOM   6843  N N   . SER D 2 54  ? 24.544  13.016  21.575  1.00 77.02  ? 54  SER D N   1 
ATOM   6844  C CA  . SER D 2 54  ? 23.434  12.080  21.487  1.00 64.47  ? 54  SER D CA  1 
ATOM   6845  C C   . SER D 2 54  ? 23.636  11.071  20.365  1.00 64.37  ? 54  SER D C   1 
ATOM   6846  O O   . SER D 2 54  ? 23.361  9.886   20.535  1.00 66.49  ? 54  SER D O   1 
ATOM   6847  C CB  . SER D 2 54  ? 22.110  12.817  21.297  1.00 64.31  ? 54  SER D CB  1 
ATOM   6848  O OG  . SER D 2 54  ? 21.471  13.029  22.544  1.00 72.87  ? 54  SER D OG  1 
ATOM   6849  N N   . VAL D 2 55  ? 24.124  11.539  19.222  1.00 65.69  ? 55  VAL D N   1 
ATOM   6850  C CA  . VAL D 2 55  ? 24.281  10.680  18.049  1.00 64.76  ? 55  VAL D CA  1 
ATOM   6851  C C   . VAL D 2 55  ? 25.544  9.807   18.108  1.00 75.99  ? 55  VAL D C   1 
ATOM   6852  O O   . VAL D 2 55  ? 25.650  8.802   17.407  1.00 72.61  ? 55  VAL D O   1 
ATOM   6853  C CB  . VAL D 2 55  ? 24.221  11.508  16.737  1.00 58.26  ? 55  VAL D CB  1 
ATOM   6854  C CG1 . VAL D 2 55  ? 24.928  12.832  16.910  1.00 62.92  ? 55  VAL D CG1 1 
ATOM   6855  C CG2 . VAL D 2 55  ? 24.801  10.730  15.565  1.00 59.40  ? 55  VAL D CG2 1 
ATOM   6856  N N   . ILE D 2 56  ? 26.490  10.180  18.961  1.00 58.48  ? 56  ILE D N   1 
ATOM   6857  C CA  . ILE D 2 56  ? 27.693  9.376   19.147  1.00 60.65  ? 56  ILE D CA  1 
ATOM   6858  C C   . ILE D 2 56  ? 27.587  8.449   20.355  1.00 64.15  ? 56  ILE D C   1 
ATOM   6859  O O   . ILE D 2 56  ? 27.730  7.237   20.229  1.00 71.06  ? 56  ILE D O   1 
ATOM   6860  C CB  . ILE D 2 56  ? 28.938  10.254  19.320  1.00 59.26  ? 56  ILE D CB  1 
ATOM   6861  C CG1 . ILE D 2 56  ? 29.261  10.984  18.016  1.00 54.81  ? 56  ILE D CG1 1 
ATOM   6862  C CG2 . ILE D 2 56  ? 30.120  9.410   19.770  1.00 66.07  ? 56  ILE D CG2 1 
ATOM   6863  C CD1 . ILE D 2 56  ? 30.465  11.895  18.112  1.00 55.29  ? 56  ILE D CD1 1 
ATOM   6864  N N   . GLU D 2 57  ? 27.337  9.025   21.525  1.00 79.62  ? 57  GLU D N   1 
ATOM   6865  C CA  . GLU D 2 57  ? 27.294  8.259   22.766  1.00 84.12  ? 57  GLU D CA  1 
ATOM   6866  C C   . GLU D 2 57  ? 26.235  7.156   22.766  1.00 71.33  ? 57  GLU D C   1 
ATOM   6867  O O   . GLU D 2 57  ? 26.424  6.112   23.389  1.00 75.52  ? 57  GLU D O   1 
ATOM   6868  C CB  . GLU D 2 57  ? 27.072  9.188   23.959  1.00 93.24  ? 57  GLU D CB  1 
ATOM   6869  C CG  . GLU D 2 57  ? 28.169  10.218  24.149  1.00 111.16 ? 57  GLU D CG  1 
ATOM   6870  C CD  . GLU D 2 57  ? 27.771  11.326  25.109  1.00 124.37 ? 57  GLU D CD  1 
ATOM   6871  O OE1 . GLU D 2 57  ? 26.732  11.187  25.795  1.00 126.47 ? 57  GLU D OE1 1 
ATOM   6872  O OE2 . GLU D 2 57  ? 28.500  12.339  25.170  1.00 130.15 ? 57  GLU D OE2 1 
ATOM   6873  N N   . LYS D 2 58  ? 25.129  7.385   22.067  1.00 71.53  ? 58  LYS D N   1 
ATOM   6874  C CA  . LYS D 2 58  ? 24.000  6.463   22.110  1.00 59.83  ? 58  LYS D CA  1 
ATOM   6875  C C   . LYS D 2 58  ? 24.229  5.195   21.304  1.00 71.35  ? 58  LYS D C   1 
ATOM   6876  O O   . LYS D 2 58  ? 23.325  4.368   21.178  1.00 60.32  ? 58  LYS D O   1 
ATOM   6877  C CB  . LYS D 2 58  ? 22.726  7.145   21.624  1.00 53.24  ? 58  LYS D CB  1 
ATOM   6878  C CG  . LYS D 2 58  ? 21.615  7.180   22.654  1.00 56.28  ? 58  LYS D CG  1 
ATOM   6879  C CD  . LYS D 2 58  ? 22.018  8.008   23.866  1.00 63.19  ? 58  LYS D CD  1 
ATOM   6880  C CE  . LYS D 2 58  ? 20.874  8.126   24.865  1.00 64.05  ? 58  LYS D CE  1 
ATOM   6881  N NZ  . LYS D 2 58  ? 20.890  9.444   25.575  1.00 67.97  ? 58  LYS D NZ  1 
ATOM   6882  N N   . MET D 2 59  ? 25.434  5.039   20.766  1.00 72.80  ? 59  MET D N   1 
ATOM   6883  C CA  . MET D 2 59  ? 25.759  3.876   19.939  1.00 73.59  ? 59  MET D CA  1 
ATOM   6884  C C   . MET D 2 59  ? 26.390  2.755   20.751  1.00 82.76  ? 59  MET D C   1 
ATOM   6885  O O   . MET D 2 59  ? 27.351  2.980   21.486  1.00 89.48  ? 59  MET D O   1 
ATOM   6886  C CB  . MET D 2 59  ? 26.696  4.280   18.798  1.00 80.68  ? 59  MET D CB  1 
ATOM   6887  C CG  . MET D 2 59  ? 26.066  4.207   17.415  1.00 79.94  ? 59  MET D CG  1 
ATOM   6888  S SD  . MET D 2 59  ? 26.231  2.574   16.679  1.00 60.30  ? 59  MET D SD  1 
ATOM   6889  C CE  . MET D 2 59  ? 28.009  2.376   16.769  1.00 173.00 ? 59  MET D CE  1 
ATOM   6890  N N   . ASN D 2 60  ? 25.851  1.546   20.606  1.00 108.79 ? 60  ASN D N   1 
ATOM   6891  C CA  . ASN D 2 60  ? 26.382  0.380   21.306  1.00 113.24 ? 60  ASN D CA  1 
ATOM   6892  C C   . ASN D 2 60  ? 27.410  -0.370  20.462  1.00 117.16 ? 60  ASN D C   1 
ATOM   6893  O O   . ASN D 2 60  ? 27.127  -0.775  19.336  1.00 110.61 ? 60  ASN D O   1 
ATOM   6894  C CB  . ASN D 2 60  ? 25.247  -0.558  21.723  1.00 104.21 ? 60  ASN D CB  1 
ATOM   6895  C CG  . ASN D 2 60  ? 25.546  -1.297  23.015  1.00 105.29 ? 60  ASN D CG  1 
ATOM   6896  O OD1 . ASN D 2 60  ? 25.834  -0.681  24.044  1.00 106.63 ? 60  ASN D OD1 1 
ATOM   6897  N ND2 . ASN D 2 60  ? 25.484  -2.626  22.967  1.00 103.86 ? 60  ASN D ND2 1 
ATOM   6898  N N   . THR D 2 61  ? 28.605  -0.555  21.015  1.00 118.97 ? 61  THR D N   1 
ATOM   6899  C CA  . THR D 2 61  ? 29.712  -1.142  20.267  1.00 128.19 ? 61  THR D CA  1 
ATOM   6900  C C   . THR D 2 61  ? 29.754  -2.667  20.367  1.00 131.98 ? 61  THR D C   1 
ATOM   6901  O O   . THR D 2 61  ? 29.768  -3.360  19.348  1.00 135.94 ? 61  THR D O   1 
ATOM   6902  C CB  . THR D 2 61  ? 31.065  -0.570  20.727  1.00 133.28 ? 61  THR D CB  1 
ATOM   6903  O OG1 . THR D 2 61  ? 31.296  -0.924  22.097  1.00 141.32 ? 61  THR D OG1 1 
ATOM   6904  C CG2 . THR D 2 61  ? 31.079  0.945   20.587  1.00 132.23 ? 61  THR D CG2 1 
ATOM   6905  N N   . GLN D 2 62  ? 29.788  -3.176  21.597  1.00 116.40 ? 62  GLN D N   1 
ATOM   6906  C CA  . GLN D 2 62  ? 29.814  -4.616  21.856  1.00 114.52 ? 62  GLN D CA  1 
ATOM   6907  C C   . GLN D 2 62  ? 31.224  -5.203  21.772  1.00 116.96 ? 62  GLN D C   1 
ATOM   6908  O O   . GLN D 2 62  ? 32.064  -4.956  22.637  1.00 124.84 ? 62  GLN D O   1 
ATOM   6909  C CB  . GLN D 2 62  ? 28.884  -5.358  20.894  1.00 107.36 ? 62  GLN D CB  1 
ATOM   6910  C CG  . GLN D 2 62  ? 28.101  -6.489  21.529  1.00 108.41 ? 62  GLN D CG  1 
ATOM   6911  C CD  . GLN D 2 62  ? 26.607  -6.225  21.529  1.00 98.75  ? 62  GLN D CD  1 
ATOM   6912  O OE1 . GLN D 2 62  ? 26.101  -5.467  20.701  1.00 103.39 ? 62  GLN D OE1 1 
ATOM   6913  N NE2 . GLN D 2 62  ? 25.892  -6.850  22.463  1.00 85.83  ? 62  GLN D NE2 1 
ATOM   6914  N N   . PHE D 2 63  ? 31.454  -5.990  20.724  1.00 88.57  ? 63  PHE D N   1 
ATOM   6915  C CA  . PHE D 2 63  ? 32.733  -6.646  20.438  1.00 78.55  ? 63  PHE D CA  1 
ATOM   6916  C C   . PHE D 2 63  ? 32.465  -7.797  19.491  1.00 69.59  ? 63  PHE D C   1 
ATOM   6917  O O   . PHE D 2 63  ? 31.952  -8.838  19.904  1.00 59.28  ? 63  PHE D O   1 
ATOM   6918  C CB  . PHE D 2 63  ? 33.406  -7.214  21.694  1.00 76.15  ? 63  PHE D CB  1 
ATOM   6919  C CG  . PHE D 2 63  ? 34.624  -8.065  21.398  1.00 70.82  ? 63  PHE D CG  1 
ATOM   6920  C CD1 . PHE D 2 63  ? 35.896  -7.600  21.678  1.00 69.37  ? 63  PHE D CD1 1 
ATOM   6921  C CD2 . PHE D 2 63  ? 34.494  -9.324  20.830  1.00 69.10  ? 63  PHE D CD2 1 
ATOM   6922  C CE1 . PHE D 2 63  ? 37.011  -8.375  21.401  1.00 58.76  ? 63  PHE D CE1 1 
ATOM   6923  C CE2 . PHE D 2 63  ? 35.604  -10.100 20.546  1.00 54.67  ? 63  PHE D CE2 1 
ATOM   6924  C CZ  . PHE D 2 63  ? 36.863  -9.627  20.832  1.00 47.54  ? 63  PHE D CZ  1 
ATOM   6925  N N   . GLU D 2 64  ? 32.811  -7.631  18.225  1.00 99.53  ? 64  GLU D N   1 
ATOM   6926  C CA  . GLU D 2 64  ? 32.606  -8.715  17.285  1.00 94.35  ? 64  GLU D CA  1 
ATOM   6927  C C   . GLU D 2 64  ? 33.900  -9.155  16.641  1.00 89.27  ? 64  GLU D C   1 
ATOM   6928  O O   . GLU D 2 64  ? 34.940  -8.517  16.795  1.00 88.21  ? 64  GLU D O   1 
ATOM   6929  C CB  . GLU D 2 64  ? 31.592  -8.325  16.207  1.00 94.06  ? 64  GLU D CB  1 
ATOM   6930  C CG  . GLU D 2 64  ? 30.161  -8.291  16.695  1.00 96.09  ? 64  GLU D CG  1 
ATOM   6931  C CD  . GLU D 2 64  ? 29.749  -9.581  17.383  1.00 99.57  ? 64  GLU D CD  1 
ATOM   6932  O OE1 . GLU D 2 64  ? 30.370  -10.638 17.115  1.00 106.09 ? 64  GLU D OE1 1 
ATOM   6933  O OE2 . GLU D 2 64  ? 28.805  -9.533  18.203  1.00 88.11  ? 64  GLU D OE2 1 
ATOM   6934  N N   . ALA D 2 65  ? 33.821  -10.271 15.930  1.00 56.14  ? 65  ALA D N   1 
ATOM   6935  C CA  . ALA D 2 65  ? 34.872  -10.673 15.022  1.00 57.60  ? 65  ALA D CA  1 
ATOM   6936  C C   . ALA D 2 65  ? 34.221  -11.284 13.796  1.00 71.13  ? 65  ALA D C   1 
ATOM   6937  O O   . ALA D 2 65  ? 33.639  -12.362 13.868  1.00 70.92  ? 65  ALA D O   1 
ATOM   6938  C CB  . ALA D 2 65  ? 35.791  -11.660 15.682  1.00 53.01  ? 65  ALA D CB  1 
ATOM   6939  N N   . VAL D 2 66  ? 34.294  -10.571 12.679  1.00 62.65  ? 66  VAL D N   1 
ATOM   6940  C CA  . VAL D 2 66  ? 33.840  -11.102 11.403  1.00 66.17  ? 66  VAL D CA  1 
ATOM   6941  C C   . VAL D 2 66  ? 34.955  -11.956 10.816  1.00 79.63  ? 66  VAL D C   1 
ATOM   6942  O O   . VAL D 2 66  ? 36.128  -11.610 10.929  1.00 85.95  ? 66  VAL D O   1 
ATOM   6943  C CB  . VAL D 2 66  ? 33.530  -9.970  10.416  1.00 63.71  ? 66  VAL D CB  1 
ATOM   6944  C CG1 . VAL D 2 66  ? 32.591  -10.472 9.329   1.00 79.63  ? 66  VAL D CG1 1 
ATOM   6945  C CG2 . VAL D 2 66  ? 32.930  -8.787  11.143  1.00 34.12  ? 66  VAL D CG2 1 
ATOM   6946  N N   . GLY D 2 67  ? 34.600  -13.072 10.191  1.00 82.27  ? 67  GLY D N   1 
ATOM   6947  C CA  . GLY D 2 67  ? 35.608  -13.947 9.625   1.00 86.72  ? 67  GLY D CA  1 
ATOM   6948  C C   . GLY D 2 67  ? 35.038  -15.214 9.028   1.00 88.47  ? 67  GLY D C   1 
ATOM   6949  O O   . GLY D 2 67  ? 33.885  -15.561 9.275   1.00 85.74  ? 67  GLY D O   1 
ATOM   6950  N N   . LYS D 2 68  ? 35.863  -15.913 8.253   1.00 98.10  ? 68  LYS D N   1 
ATOM   6951  C CA  . LYS D 2 68  ? 35.450  -17.133 7.559   1.00 100.92 ? 68  LYS D CA  1 
ATOM   6952  C C   . LYS D 2 68  ? 35.085  -18.277 8.501   1.00 97.55  ? 68  LYS D C   1 
ATOM   6953  O O   . LYS D 2 68  ? 34.068  -18.223 9.193   1.00 99.02  ? 68  LYS D O   1 
ATOM   6954  C CB  . LYS D 2 68  ? 36.534  -17.585 6.571   1.00 111.21 ? 68  LYS D CB  1 
ATOM   6955  C CG  . LYS D 2 68  ? 36.772  -16.602 5.426   1.00 111.96 ? 68  LYS D CG  1 
ATOM   6956  C CD  . LYS D 2 68  ? 37.901  -17.051 4.514   1.00 115.88 ? 68  LYS D CD  1 
ATOM   6957  C CE  . LYS D 2 68  ? 38.096  -16.068 3.374   1.00 124.87 ? 68  LYS D CE  1 
ATOM   6958  N NZ  . LYS D 2 68  ? 39.243  -16.443 2.509   1.00 130.48 ? 68  LYS D NZ  1 
ATOM   6959  N N   . GLU D 2 69  ? 35.917  -19.313 8.517   1.00 130.64 ? 69  GLU D N   1 
ATOM   6960  C CA  . GLU D 2 69  ? 35.596  -20.531 9.244   1.00 133.35 ? 69  GLU D CA  1 
ATOM   6961  C C   . GLU D 2 69  ? 34.389  -21.214 8.609   1.00 133.34 ? 69  GLU D C   1 
ATOM   6962  O O   . GLU D 2 69  ? 33.405  -21.495 9.286   1.00 135.70 ? 69  GLU D O   1 
ATOM   6963  C CB  . GLU D 2 69  ? 35.302  -20.227 10.712  1.00 133.59 ? 69  GLU D CB  1 
ATOM   6964  C CG  . GLU D 2 69  ? 36.472  -19.654 11.487  1.00 143.91 ? 69  GLU D CG  1 
ATOM   6965  C CD  . GLU D 2 69  ? 36.061  -19.156 12.861  1.00 143.66 ? 69  GLU D CD  1 
ATOM   6966  O OE1 . GLU D 2 69  ? 34.847  -18.933 13.073  1.00 147.39 ? 69  GLU D OE1 1 
ATOM   6967  O OE2 . GLU D 2 69  ? 36.948  -18.991 13.727  1.00 139.47 ? 69  GLU D OE2 1 
ATOM   6968  N N   . PHE D 2 70  ? 34.468  -21.464 7.305   1.00 89.46  ? 70  PHE D N   1 
ATOM   6969  C CA  . PHE D 2 70  ? 33.413  -22.167 6.583   1.00 74.55  ? 70  PHE D CA  1 
ATOM   6970  C C   . PHE D 2 70  ? 33.980  -23.073 5.495   1.00 82.65  ? 70  PHE D C   1 
ATOM   6971  O O   . PHE D 2 70  ? 34.286  -22.613 4.397   1.00 86.26  ? 70  PHE D O   1 
ATOM   6972  C CB  . PHE D 2 70  ? 32.432  -21.180 5.970   1.00 67.79  ? 70  PHE D CB  1 
ATOM   6973  C CG  . PHE D 2 70  ? 31.516  -20.535 6.972   1.00 65.41  ? 70  PHE D CG  1 
ATOM   6974  C CD1 . PHE D 2 70  ? 30.903  -21.289 7.961   1.00 60.16  ? 70  PHE D CD1 1 
ATOM   6975  C CD2 . PHE D 2 70  ? 31.264  -19.170 6.924   1.00 65.55  ? 70  PHE D CD2 1 
ATOM   6976  C CE1 . PHE D 2 70  ? 30.052  -20.696 8.889   1.00 45.61  ? 70  PHE D CE1 1 
ATOM   6977  C CE2 . PHE D 2 70  ? 30.421  -18.573 7.843   1.00 59.71  ? 70  PHE D CE2 1 
ATOM   6978  C CZ  . PHE D 2 70  ? 29.814  -19.339 8.826   1.00 51.18  ? 70  PHE D CZ  1 
ATOM   6979  N N   . SER D 2 71  ? 34.115  -24.361 5.814   1.00 62.26  ? 71  SER D N   1 
ATOM   6980  C CA  . SER D 2 71  ? 34.630  -25.359 4.881   1.00 66.88  ? 71  SER D CA  1 
ATOM   6981  C C   . SER D 2 71  ? 33.887  -25.310 3.554   1.00 78.54  ? 71  SER D C   1 
ATOM   6982  O O   . SER D 2 71  ? 32.776  -24.786 3.472   1.00 84.47  ? 71  SER D O   1 
ATOM   6983  C CB  . SER D 2 71  ? 34.512  -26.764 5.476   1.00 65.19  ? 71  SER D CB  1 
ATOM   6984  O OG  . SER D 2 71  ? 33.287  -27.375 5.100   1.00 60.32  ? 71  SER D OG  1 
ATOM   6985  N N   . ASN D 2 72  ? 34.498  -25.877 2.519   1.00 85.00  ? 72  ASN D N   1 
ATOM   6986  C CA  . ASN D 2 72  ? 33.920  -25.846 1.181   1.00 86.06  ? 72  ASN D CA  1 
ATOM   6987  C C   . ASN D 2 72  ? 32.660  -26.687 1.071   1.00 69.63  ? 72  ASN D C   1 
ATOM   6988  O O   . ASN D 2 72  ? 32.045  -26.766 0.007   1.00 70.41  ? 72  ASN D O   1 
ATOM   6989  C CB  . ASN D 2 72  ? 34.941  -26.284 0.126   1.00 97.12  ? 72  ASN D CB  1 
ATOM   6990  C CG  . ASN D 2 72  ? 36.267  -26.700 0.730   1.00 98.33  ? 72  ASN D CG  1 
ATOM   6991  O OD1 . ASN D 2 72  ? 36.317  -27.515 1.653   1.00 99.34  ? 72  ASN D OD1 1 
ATOM   6992  N ND2 . ASN D 2 72  ? 37.351  -26.131 0.215   1.00 98.88  ? 72  ASN D ND2 1 
ATOM   6993  N N   . LEU D 2 73  ? 32.276  -27.316 2.174   1.00 75.26  ? 73  LEU D N   1 
ATOM   6994  C CA  . LEU D 2 73  ? 31.051  -28.095 2.187   1.00 67.30  ? 73  LEU D CA  1 
ATOM   6995  C C   . LEU D 2 73  ? 30.007  -27.457 3.100   1.00 54.62  ? 73  LEU D C   1 
ATOM   6996  O O   . LEU D 2 73  ? 28.974  -28.056 3.414   1.00 44.15  ? 73  LEU D O   1 
ATOM   6997  C CB  . LEU D 2 73  ? 31.336  -29.535 2.591   1.00 69.87  ? 73  LEU D CB  1 
ATOM   6998  C CG  . LEU D 2 73  ? 30.378  -30.558 1.978   1.00 63.15  ? 73  LEU D CG  1 
ATOM   6999  C CD1 . LEU D 2 73  ? 29.895  -30.088 0.613   1.00 69.62  ? 73  LEU D CD1 1 
ATOM   7000  C CD2 . LEU D 2 73  ? 31.048  -31.927 1.886   1.00 61.90  ? 73  LEU D CD2 1 
ATOM   7001  N N   . GLU D 2 74  ? 30.295  -26.231 3.523   1.00 50.99  ? 74  GLU D N   1 
ATOM   7002  C CA  . GLU D 2 74  ? 29.355  -25.425 4.283   1.00 28.52  ? 74  GLU D CA  1 
ATOM   7003  C C   . GLU D 2 74  ? 29.201  -24.106 3.564   1.00 41.87  ? 74  GLU D C   1 
ATOM   7004  O O   . GLU D 2 74  ? 29.405  -23.040 4.149   1.00 43.83  ? 74  GLU D O   1 
ATOM   7005  C CB  . GLU D 2 74  ? 29.891  -25.136 5.682   1.00 34.49  ? 74  GLU D CB  1 
ATOM   7006  C CG  . GLU D 2 74  ? 29.970  -26.318 6.603   1.00 37.28  ? 74  GLU D CG  1 
ATOM   7007  C CD  . GLU D 2 74  ? 30.858  -26.036 7.792   1.00 47.37  ? 74  GLU D CD  1 
ATOM   7008  O OE1 . GLU D 2 74  ? 31.777  -25.208 7.659   1.00 59.15  ? 74  GLU D OE1 1 
ATOM   7009  O OE2 . GLU D 2 74  ? 30.639  -26.638 8.861   1.00 45.25  ? 74  GLU D OE2 1 
ATOM   7010  N N   . ARG D 2 75  ? 28.871  -24.163 2.284   1.00 65.53  ? 75  ARG D N   1 
ATOM   7011  C CA  . ARG D 2 75  ? 28.696  -22.935 1.538   1.00 63.70  ? 75  ARG D CA  1 
ATOM   7012  C C   . ARG D 2 75  ? 27.442  -22.207 2.015   1.00 50.83  ? 75  ARG D C   1 
ATOM   7013  O O   . ARG D 2 75  ? 27.451  -20.989 2.169   1.00 46.51  ? 75  ARG D O   1 
ATOM   7014  C CB  . ARG D 2 75  ? 28.651  -23.204 0.033   1.00 71.94  ? 75  ARG D CB  1 
ATOM   7015  C CG  . ARG D 2 75  ? 29.961  -23.732 -0.536  1.00 107.31 ? 75  ARG D CG  1 
ATOM   7016  C CD  . ARG D 2 75  ? 31.138  -22.856 -0.131  1.00 135.92 ? 75  ARG D CD  1 
ATOM   7017  N NE  . ARG D 2 75  ? 32.377  -23.252 -0.796  1.00 157.80 ? 75  ARG D NE  1 
ATOM   7018  C CZ  . ARG D 2 75  ? 33.563  -22.703 -0.554  1.00 161.59 ? 75  ARG D CZ  1 
ATOM   7019  N NH1 . ARG D 2 75  ? 33.681  -21.734 0.342   1.00 159.58 ? 75  ARG D NH1 1 
ATOM   7020  N NH2 . ARG D 2 75  ? 34.636  -23.128 -1.207  1.00 162.51 ? 75  ARG D NH2 1 
ATOM   7021  N N   . ARG D 2 76  ? 26.376  -22.955 2.278   1.00 73.57  ? 76  ARG D N   1 
ATOM   7022  C CA  . ARG D 2 76  ? 25.111  -22.355 2.689   1.00 58.92  ? 76  ARG D CA  1 
ATOM   7023  C C   . ARG D 2 76  ? 25.238  -21.494 3.936   1.00 60.51  ? 76  ARG D C   1 
ATOM   7024  O O   . ARG D 2 76  ? 24.547  -20.486 4.059   1.00 63.28  ? 76  ARG D O   1 
ATOM   7025  C CB  . ARG D 2 76  ? 24.059  -23.427 2.921   1.00 51.42  ? 76  ARG D CB  1 
ATOM   7026  C CG  . ARG D 2 76  ? 23.464  -23.994 1.663   1.00 45.56  ? 76  ARG D CG  1 
ATOM   7027  C CD  . ARG D 2 76  ? 22.673  -25.230 2.001   1.00 45.34  ? 76  ARG D CD  1 
ATOM   7028  N NE  . ARG D 2 76  ? 23.508  -26.198 2.709   1.00 41.88  ? 76  ARG D NE  1 
ATOM   7029  C CZ  . ARG D 2 76  ? 23.031  -27.139 3.518   1.00 35.17  ? 76  ARG D CZ  1 
ATOM   7030  N NH1 . ARG D 2 76  ? 21.723  -27.236 3.729   1.00 34.46  ? 76  ARG D NH1 1 
ATOM   7031  N NH2 . ARG D 2 76  ? 23.863  -27.978 4.124   1.00 37.38  ? 76  ARG D NH2 1 
ATOM   7032  N N   . LEU D 2 77  ? 26.097  -21.899 4.867   1.00 43.12  ? 77  LEU D N   1 
ATOM   7033  C CA  . LEU D 2 77  ? 26.390  -21.070 6.029   1.00 46.59  ? 77  LEU D CA  1 
ATOM   7034  C C   . LEU D 2 77  ? 27.108  -19.813 5.592   1.00 58.68  ? 77  LEU D C   1 
ATOM   7035  O O   . LEU D 2 77  ? 26.681  -18.700 5.899   1.00 54.10  ? 77  LEU D O   1 
ATOM   7036  C CB  . LEU D 2 77  ? 27.268  -21.804 7.025   1.00 52.32  ? 77  LEU D CB  1 
ATOM   7037  C CG  . LEU D 2 77  ? 26.523  -22.540 8.122   1.00 53.87  ? 77  LEU D CG  1 
ATOM   7038  C CD1 . LEU D 2 77  ? 25.894  -23.798 7.547   1.00 63.87  ? 77  LEU D CD1 1 
ATOM   7039  C CD2 . LEU D 2 77  ? 27.494  -22.872 9.241   1.00 59.47  ? 77  LEU D CD2 1 
ATOM   7040  N N   . GLU D 2 78  ? 28.214  -19.997 4.882   1.00 42.42  ? 78  GLU D N   1 
ATOM   7041  C CA  . GLU D 2 78  ? 28.928  -18.871 4.312   1.00 57.33  ? 78  GLU D CA  1 
ATOM   7042  C C   . GLU D 2 78  ? 27.892  -17.850 3.844   1.00 51.74  ? 78  GLU D C   1 
ATOM   7043  O O   . GLU D 2 78  ? 28.017  -16.654 4.110   1.00 57.33  ? 78  GLU D O   1 
ATOM   7044  C CB  . GLU D 2 78  ? 29.803  -19.339 3.149   1.00 80.05  ? 78  GLU D CB  1 
ATOM   7045  C CG  . GLU D 2 78  ? 30.945  -18.403 2.805   1.00 102.08 ? 78  GLU D CG  1 
ATOM   7046  C CD  . GLU D 2 78  ? 32.073  -19.108 2.076   1.00 120.21 ? 78  GLU D CD  1 
ATOM   7047  O OE1 . GLU D 2 78  ? 33.004  -18.422 1.605   1.00 121.90 ? 78  GLU D OE1 1 
ATOM   7048  O OE2 . GLU D 2 78  ? 32.032  -20.352 1.982   1.00 126.91 ? 78  GLU D OE2 1 
ATOM   7049  N N   . ASN D 2 79  ? 26.846  -18.341 3.187   1.00 78.09  ? 79  ASN D N   1 
ATOM   7050  C CA  . ASN D 2 79  ? 25.819  -17.479 2.614   1.00 71.97  ? 79  ASN D CA  1 
ATOM   7051  C C   . ASN D 2 79  ? 24.922  -16.794 3.649   1.00 61.87  ? 79  ASN D C   1 
ATOM   7052  O O   . ASN D 2 79  ? 24.667  -15.589 3.565   1.00 62.95  ? 79  ASN D O   1 
ATOM   7053  C CB  . ASN D 2 79  ? 24.968  -18.266 1.622   1.00 71.00  ? 79  ASN D CB  1 
ATOM   7054  C CG  . ASN D 2 79  ? 24.359  -17.386 0.562   1.00 67.45  ? 79  ASN D CG  1 
ATOM   7055  O OD1 . ASN D 2 79  ? 25.053  -16.920 -0.342  1.00 72.27  ? 79  ASN D OD1 1 
ATOM   7056  N ND2 . ASN D 2 79  ? 23.054  -17.152 0.662   1.00 63.90  ? 79  ASN D ND2 1 
ATOM   7057  N N   . LEU D 2 80  ? 24.437  -17.566 4.616   1.00 53.27  ? 80  LEU D N   1 
ATOM   7058  C CA  . LEU D 2 80  ? 23.634  -17.023 5.704   1.00 41.82  ? 80  LEU D CA  1 
ATOM   7059  C C   . LEU D 2 80  ? 24.381  -15.865 6.366   1.00 57.87  ? 80  LEU D C   1 
ATOM   7060  O O   . LEU D 2 80  ? 23.811  -14.810 6.630   1.00 63.43  ? 80  LEU D O   1 
ATOM   7061  C CB  . LEU D 2 80  ? 23.350  -18.107 6.738   1.00 33.40  ? 80  LEU D CB  1 
ATOM   7062  C CG  . LEU D 2 80  ? 21.983  -18.038 7.413   1.00 30.90  ? 80  LEU D CG  1 
ATOM   7063  C CD1 . LEU D 2 80  ? 21.906  -19.027 8.566   1.00 30.79  ? 80  LEU D CD1 1 
ATOM   7064  C CD2 . LEU D 2 80  ? 21.690  -16.636 7.901   1.00 27.20  ? 80  LEU D CD2 1 
ATOM   7065  N N   . ASN D 2 81  ? 25.665  -16.077 6.631   1.00 43.14  ? 81  ASN D N   1 
ATOM   7066  C CA  . ASN D 2 81  ? 26.519  -15.045 7.197   1.00 45.23  ? 81  ASN D CA  1 
ATOM   7067  C C   . ASN D 2 81  ? 26.579  -13.839 6.270   1.00 54.61  ? 81  ASN D C   1 
ATOM   7068  O O   . ASN D 2 81  ? 26.419  -12.708 6.709   1.00 66.16  ? 81  ASN D O   1 
ATOM   7069  C CB  . ASN D 2 81  ? 27.922  -15.598 7.437   1.00 62.63  ? 81  ASN D CB  1 
ATOM   7070  C CG  . ASN D 2 81  ? 28.763  -14.695 8.303   1.00 84.33  ? 81  ASN D CG  1 
ATOM   7071  O OD1 . ASN D 2 81  ? 28.247  -13.821 8.990   1.00 101.38 ? 81  ASN D OD1 1 
ATOM   7072  N ND2 . ASN D 2 81  ? 30.068  -14.907 8.282   1.00 91.99  ? 81  ASN D ND2 1 
ATOM   7073  N N   . LYS D 2 82  ? 26.801  -14.080 4.982   1.00 56.08  ? 82  LYS D N   1 
ATOM   7074  C CA  . LYS D 2 82  ? 26.819  -12.993 4.015   1.00 49.26  ? 82  LYS D CA  1 
ATOM   7075  C C   . LYS D 2 82  ? 25.491  -12.254 4.078   1.00 39.29  ? 82  LYS D C   1 
ATOM   7076  O O   . LYS D 2 82  ? 25.455  -11.076 4.408   1.00 52.57  ? 82  LYS D O   1 
ATOM   7077  C CB  . LYS D 2 82  ? 27.071  -13.513 2.600   1.00 65.55  ? 82  LYS D CB  1 
ATOM   7078  C CG  . LYS D 2 82  ? 27.324  -12.413 1.574   1.00 78.86  ? 82  LYS D CG  1 
ATOM   7079  C CD  . LYS D 2 82  ? 27.537  -12.988 0.183   1.00 91.68  ? 82  LYS D CD  1 
ATOM   7080  C CE  . LYS D 2 82  ? 28.045  -11.933 -0.787  1.00 105.78 ? 82  LYS D CE  1 
ATOM   7081  N NZ  . LYS D 2 82  ? 27.048  -10.858 -1.027  1.00 95.03  ? 82  LYS D NZ  1 
ATOM   7082  N N   . LYS D 2 83  ? 24.396  -12.947 3.780   1.00 60.26  ? 83  LYS D N   1 
ATOM   7083  C CA  . LYS D 2 83  ? 23.068  -12.341 3.877   1.00 65.06  ? 83  LYS D CA  1 
ATOM   7084  C C   . LYS D 2 83  ? 22.890  -11.526 5.168   1.00 60.49  ? 83  LYS D C   1 
ATOM   7085  O O   . LYS D 2 83  ? 22.186  -10.514 5.183   1.00 61.24  ? 83  LYS D O   1 
ATOM   7086  C CB  . LYS D 2 83  ? 21.968  -13.405 3.762   1.00 74.21  ? 83  LYS D CB  1 
ATOM   7087  C CG  . LYS D 2 83  ? 21.650  -13.821 2.335   1.00 87.72  ? 83  LYS D CG  1 
ATOM   7088  C CD  . LYS D 2 83  ? 20.150  -13.991 2.134   1.00 95.95  ? 83  LYS D CD  1 
ATOM   7089  C CE  . LYS D 2 83  ? 19.615  -15.233 2.838   1.00 101.85 ? 83  LYS D CE  1 
ATOM   7090  N NZ  . LYS D 2 83  ? 19.931  -16.496 2.100   1.00 101.88 ? 83  LYS D NZ  1 
ATOM   7091  N N   . MET D 2 84  ? 23.533  -11.973 6.245   1.00 40.60  ? 84  MET D N   1 
ATOM   7092  C CA  . MET D 2 84  ? 23.457  -11.291 7.533   1.00 41.75  ? 84  MET D CA  1 
ATOM   7093  C C   . MET D 2 84  ? 24.257  -9.992  7.522   1.00 57.14  ? 84  MET D C   1 
ATOM   7094  O O   . MET D 2 84  ? 23.709  -8.920  7.755   1.00 60.32  ? 84  MET D O   1 
ATOM   7095  C CB  . MET D 2 84  ? 23.978  -12.190 8.651   1.00 36.05  ? 84  MET D CB  1 
ATOM   7096  C CG  . MET D 2 84  ? 23.565  -11.746 10.039  1.00 39.49  ? 84  MET D CG  1 
ATOM   7097  S SD  . MET D 2 84  ? 24.652  -12.351 11.340  1.00 66.75  ? 84  MET D SD  1 
ATOM   7098  C CE  . MET D 2 84  ? 26.192  -11.598 10.840  1.00 56.35  ? 84  MET D CE  1 
ATOM   7099  N N   . GLU D 2 85  ? 25.558  -10.095 7.269   1.00 48.51  ? 85  GLU D N   1 
ATOM   7100  C CA  . GLU D 2 85  ? 26.429  -8.927  7.226   1.00 46.93  ? 85  GLU D CA  1 
ATOM   7101  C C   . GLU D 2 85  ? 25.925  -7.938  6.184   1.00 49.55  ? 85  GLU D C   1 
ATOM   7102  O O   . GLU D 2 85  ? 25.971  -6.723  6.389   1.00 54.29  ? 85  GLU D O   1 
ATOM   7103  C CB  . GLU D 2 85  ? 27.873  -9.326  6.905   1.00 69.48  ? 85  GLU D CB  1 
ATOM   7104  C CG  . GLU D 2 85  ? 28.447  -10.445 7.766   1.00 98.18  ? 85  GLU D CG  1 
ATOM   7105  C CD  . GLU D 2 85  ? 28.752  -10.010 9.187   1.00 116.75 ? 85  GLU D CD  1 
ATOM   7106  O OE1 . GLU D 2 85  ? 29.244  -10.851 9.970   1.00 123.55 ? 85  GLU D OE1 1 
ATOM   7107  O OE2 . GLU D 2 85  ? 28.506  -8.831  9.521   1.00 117.90 ? 85  GLU D OE2 1 
ATOM   7108  N N   . ASP D 2 86  ? 25.438  -8.458  5.064   1.00 55.81  ? 86  ASP D N   1 
ATOM   7109  C CA  . ASP D 2 86  ? 24.979  -7.602  3.981   1.00 51.53  ? 86  ASP D CA  1 
ATOM   7110  C C   . ASP D 2 86  ? 23.649  -6.940  4.310   1.00 45.15  ? 86  ASP D C   1 
ATOM   7111  O O   . ASP D 2 86  ? 23.357  -5.852  3.815   1.00 57.48  ? 86  ASP D O   1 
ATOM   7112  C CB  . ASP D 2 86  ? 24.889  -8.372  2.662   1.00 50.07  ? 86  ASP D CB  1 
ATOM   7113  C CG  . ASP D 2 86  ? 26.246  -8.650  2.062   1.00 72.33  ? 86  ASP D CG  1 
ATOM   7114  O OD1 . ASP D 2 86  ? 27.253  -8.126  2.584   1.00 86.55  ? 86  ASP D OD1 1 
ATOM   7115  O OD2 . ASP D 2 86  ? 26.306  -9.388  1.060   1.00 83.21  ? 86  ASP D OD2 1 
ATOM   7116  N N   . GLY D 2 87  ? 22.845  -7.587  5.146   1.00 52.43  ? 87  GLY D N   1 
ATOM   7117  C CA  . GLY D 2 87  ? 21.556  -7.033  5.523   1.00 51.67  ? 87  GLY D CA  1 
ATOM   7118  C C   . GLY D 2 87  ? 21.700  -5.918  6.538   1.00 61.41  ? 87  GLY D C   1 
ATOM   7119  O O   . GLY D 2 87  ? 20.888  -4.992  6.575   1.00 69.39  ? 87  GLY D O   1 
ATOM   7120  N N   . PHE D 2 88  ? 22.743  -6.010  7.361   1.00 52.14  ? 88  PHE D N   1 
ATOM   7121  C CA  . PHE D 2 88  ? 23.004  -5.032  8.415   1.00 49.03  ? 88  PHE D CA  1 
ATOM   7122  C C   . PHE D 2 88  ? 23.681  -3.781  7.869   1.00 71.52  ? 88  PHE D C   1 
ATOM   7123  O O   . PHE D 2 88  ? 23.285  -2.661  8.190   1.00 78.56  ? 88  PHE D O   1 
ATOM   7124  C CB  . PHE D 2 88  ? 23.859  -5.652  9.527   1.00 40.28  ? 88  PHE D CB  1 
ATOM   7125  C CG  . PHE D 2 88  ? 23.068  -6.430  10.541  1.00 31.44  ? 88  PHE D CG  1 
ATOM   7126  C CD1 . PHE D 2 88  ? 21.949  -5.877  11.139  1.00 33.32  ? 88  PHE D CD1 1 
ATOM   7127  C CD2 . PHE D 2 88  ? 23.431  -7.719  10.884  1.00 35.29  ? 88  PHE D CD2 1 
ATOM   7128  C CE1 . PHE D 2 88  ? 21.215  -6.593  12.065  1.00 33.73  ? 88  PHE D CE1 1 
ATOM   7129  C CE2 . PHE D 2 88  ? 22.704  -8.435  11.808  1.00 34.77  ? 88  PHE D CE2 1 
ATOM   7130  C CZ  . PHE D 2 88  ? 21.597  -7.872  12.401  1.00 34.74  ? 88  PHE D CZ  1 
ATOM   7131  N N   . LEU D 2 89  ? 24.712  -3.980  7.055   1.00 67.55  ? 89  LEU D N   1 
ATOM   7132  C CA  . LEU D 2 89  ? 25.389  -2.870  6.401   1.00 68.42  ? 89  LEU D CA  1 
ATOM   7133  C C   . LEU D 2 89  ? 24.359  -1.958  5.759   1.00 57.77  ? 89  LEU D C   1 
ATOM   7134  O O   . LEU D 2 89  ? 24.380  -0.747  5.965   1.00 61.21  ? 89  LEU D O   1 
ATOM   7135  C CB  . LEU D 2 89  ? 26.347  -3.378  5.332   1.00 74.78  ? 89  LEU D CB  1 
ATOM   7136  C CG  . LEU D 2 89  ? 27.113  -2.274  4.612   1.00 81.32  ? 89  LEU D CG  1 
ATOM   7137  C CD1 . LEU D 2 89  ? 28.125  -1.685  5.561   1.00 101.22 ? 89  LEU D CD1 1 
ATOM   7138  C CD2 . LEU D 2 89  ? 27.796  -2.803  3.368   1.00 86.16  ? 89  LEU D CD2 1 
ATOM   7139  N N   . ASP D 2 90  ? 23.455  -2.549  4.982   1.00 58.73  ? 90  ASP D N   1 
ATOM   7140  C CA  . ASP D 2 90  ? 22.377  -1.799  4.353   1.00 53.11  ? 90  ASP D CA  1 
ATOM   7141  C C   . ASP D 2 90  ? 21.600  -0.979  5.375   1.00 55.19  ? 90  ASP D C   1 
ATOM   7142  O O   . ASP D 2 90  ? 21.498  0.243   5.253   1.00 60.31  ? 90  ASP D O   1 
ATOM   7143  C CB  . ASP D 2 90  ? 21.430  -2.741  3.623   1.00 52.12  ? 90  ASP D CB  1 
ATOM   7144  C CG  . ASP D 2 90  ? 21.981  -3.200  2.301   1.00 63.54  ? 90  ASP D CG  1 
ATOM   7145  O OD1 . ASP D 2 90  ? 23.189  -2.993  2.060   1.00 78.98  ? 90  ASP D OD1 1 
ATOM   7146  O OD2 . ASP D 2 90  ? 21.203  -3.770  1.506   1.00 54.96  ? 90  ASP D OD2 1 
ATOM   7147  N N   . VAL D 2 91  ? 21.054  -1.657  6.380   1.00 46.97  ? 91  VAL D N   1 
ATOM   7148  C CA  . VAL D 2 91  ? 20.344  -0.985  7.457   1.00 40.85  ? 91  VAL D CA  1 
ATOM   7149  C C   . VAL D 2 91  ? 21.170  0.152   8.063   1.00 45.53  ? 91  VAL D C   1 
ATOM   7150  O O   . VAL D 2 91  ? 20.724  1.294   8.072   1.00 51.04  ? 91  VAL D O   1 
ATOM   7151  C CB  . VAL D 2 91  ? 19.899  -1.980  8.556   1.00 41.48  ? 91  VAL D CB  1 
ATOM   7152  C CG1 . VAL D 2 91  ? 19.870  -1.309  9.922   1.00 38.60  ? 91  VAL D CG1 1 
ATOM   7153  C CG2 . VAL D 2 91  ? 18.534  -2.569  8.219   1.00 44.31  ? 91  VAL D CG2 1 
ATOM   7154  N N   . TRP D 2 92  ? 22.373  -0.146  8.549   1.00 39.00  ? 92  TRP D N   1 
ATOM   7155  C CA  . TRP D 2 92  ? 23.203  0.892   9.160   1.00 48.22  ? 92  TRP D CA  1 
ATOM   7156  C C   . TRP D 2 92  ? 23.575  2.011   8.181   1.00 56.21  ? 92  TRP D C   1 
ATOM   7157  O O   . TRP D 2 92  ? 23.656  3.181   8.558   1.00 65.37  ? 92  TRP D O   1 
ATOM   7158  C CB  . TRP D 2 92  ? 24.460  0.311   9.826   1.00 59.33  ? 92  TRP D CB  1 
ATOM   7159  C CG  . TRP D 2 92  ? 24.209  -0.308  11.176  1.00 48.27  ? 92  TRP D CG  1 
ATOM   7160  C CD1 . TRP D 2 92  ? 24.466  -1.593  11.543  1.00 46.96  ? 92  TRP D CD1 1 
ATOM   7161  C CD2 . TRP D 2 92  ? 23.639  0.327   12.327  1.00 49.45  ? 92  TRP D CD2 1 
ATOM   7162  N NE1 . TRP D 2 92  ? 24.105  -1.799  12.848  1.00 52.61  ? 92  TRP D NE1 1 
ATOM   7163  C CE2 . TRP D 2 92  ? 23.589  -0.637  13.354  1.00 50.56  ? 92  TRP D CE2 1 
ATOM   7164  C CE3 . TRP D 2 92  ? 23.163  1.620   12.591  1.00 53.32  ? 92  TRP D CE3 1 
ATOM   7165  C CZ2 . TRP D 2 92  ? 23.084  -0.357  14.622  1.00 45.97  ? 92  TRP D CZ2 1 
ATOM   7166  C CZ3 . TRP D 2 92  ? 22.669  1.901   13.848  1.00 50.42  ? 92  TRP D CZ3 1 
ATOM   7167  C CH2 . TRP D 2 92  ? 22.632  0.916   14.851  1.00 46.93  ? 92  TRP D CH2 1 
ATOM   7168  N N   . THR D 2 93  ? 23.797  1.659   6.922   1.00 49.98  ? 93  THR D N   1 
ATOM   7169  C CA  . THR D 2 93  ? 24.156  2.666   5.932   1.00 53.98  ? 93  THR D CA  1 
ATOM   7170  C C   . THR D 2 93  ? 22.992  3.631   5.692   1.00 51.80  ? 93  THR D C   1 
ATOM   7171  O O   . THR D 2 93  ? 23.164  4.840   5.746   1.00 61.40  ? 93  THR D O   1 
ATOM   7172  C CB  . THR D 2 93  ? 24.647  2.029   4.606   1.00 59.90  ? 93  THR D CB  1 
ATOM   7173  O OG1 . THR D 2 93  ? 26.015  1.632   4.750   1.00 71.41  ? 93  THR D OG1 1 
ATOM   7174  C CG2 . THR D 2 93  ? 24.547  3.024   3.459   1.00 66.41  ? 93  THR D CG2 1 
ATOM   7175  N N   . TYR D 2 94  ? 21.804  3.089   5.457   1.00 51.24  ? 94  TYR D N   1 
ATOM   7176  C CA  . TYR D 2 94  ? 20.637  3.911   5.170   1.00 48.47  ? 94  TYR D CA  1 
ATOM   7177  C C   . TYR D 2 94  ? 20.219  4.699   6.391   1.00 55.70  ? 94  TYR D C   1 
ATOM   7178  O O   . TYR D 2 94  ? 19.705  5.804   6.275   1.00 60.70  ? 94  TYR D O   1 
ATOM   7179  C CB  . TYR D 2 94  ? 19.478  3.033   4.724   1.00 45.57  ? 94  TYR D CB  1 
ATOM   7180  C CG  . TYR D 2 94  ? 18.237  3.776   4.282   1.00 48.41  ? 94  TYR D CG  1 
ATOM   7181  C CD1 . TYR D 2 94  ? 18.209  4.467   3.076   1.00 51.32  ? 94  TYR D CD1 1 
ATOM   7182  C CD2 . TYR D 2 94  ? 17.081  3.750   5.048   1.00 60.32  ? 94  TYR D CD2 1 
ATOM   7183  C CE1 . TYR D 2 94  ? 17.072  5.129   2.660   1.00 67.13  ? 94  TYR D CE1 1 
ATOM   7184  C CE2 . TYR D 2 94  ? 15.939  4.409   4.639   1.00 73.82  ? 94  TYR D CE2 1 
ATOM   7185  C CZ  . TYR D 2 94  ? 15.941  5.098   3.444   1.00 79.48  ? 94  TYR D CZ  1 
ATOM   7186  O OH  . TYR D 2 94  ? 14.806  5.758   3.033   1.00 94.32  ? 94  TYR D OH  1 
ATOM   7187  N N   . ASN D 2 95  ? 20.431  4.130   7.569   1.00 70.77  ? 95  ASN D N   1 
ATOM   7188  C CA  . ASN D 2 95  ? 20.090  4.829   8.798   1.00 66.68  ? 95  ASN D CA  1 
ATOM   7189  C C   . ASN D 2 95  ? 21.010  6.013   9.065   1.00 65.18  ? 95  ASN D C   1 
ATOM   7190  O O   . ASN D 2 95  ? 20.538  7.103   9.385   1.00 67.27  ? 95  ASN D O   1 
ATOM   7191  C CB  . ASN D 2 95  ? 20.066  3.869   9.983   1.00 63.44  ? 95  ASN D CB  1 
ATOM   7192  C CG  . ASN D 2 95  ? 18.804  3.023   10.016  1.00 73.60  ? 95  ASN D CG  1 
ATOM   7193  O OD1 . ASN D 2 95  ? 18.002  3.046   9.077   1.00 76.40  ? 95  ASN D OD1 1 
ATOM   7194  N ND2 . ASN D 2 95  ? 18.620  2.272   11.100  1.00 77.62  ? 95  ASN D ND2 1 
ATOM   7195  N N   . ALA D 2 96  ? 22.318  5.809   8.926   1.00 38.71  ? 96  ALA D N   1 
ATOM   7196  C CA  . ALA D 2 96  ? 23.261  6.918   9.065   1.00 38.22  ? 96  ALA D CA  1 
ATOM   7197  C C   . ALA D 2 96  ? 22.886  8.041   8.104   1.00 48.66  ? 96  ALA D C   1 
ATOM   7198  O O   . ALA D 2 96  ? 22.496  9.125   8.534   1.00 57.97  ? 96  ALA D O   1 
ATOM   7199  C CB  . ALA D 2 96  ? 24.693  6.458   8.828   1.00 45.99  ? 96  ALA D CB  1 
ATOM   7200  N N   . GLU D 2 97  ? 22.983  7.770   6.804   1.00 45.29  ? 97  GLU D N   1 
ATOM   7201  C CA  . GLU D 2 97  ? 22.646  8.758   5.778   1.00 51.15  ? 97  GLU D CA  1 
ATOM   7202  C C   . GLU D 2 97  ? 21.427  9.608   6.170   1.00 48.02  ? 97  GLU D C   1 
ATOM   7203  O O   . GLU D 2 97  ? 21.503  10.841  6.208   1.00 58.57  ? 97  GLU D O   1 
ATOM   7204  C CB  . GLU D 2 97  ? 22.379  8.090   4.416   1.00 51.00  ? 97  GLU D CB  1 
ATOM   7205  C CG  . GLU D 2 97  ? 23.419  7.093   3.921   1.00 54.59  ? 97  GLU D CG  1 
ATOM   7206  C CD  . GLU D 2 97  ? 24.757  7.711   3.605   1.00 69.91  ? 97  GLU D CD  1 
ATOM   7207  O OE1 . GLU D 2 97  ? 25.125  8.710   4.254   1.00 72.61  ? 97  GLU D OE1 1 
ATOM   7208  O OE2 . GLU D 2 97  ? 25.445  7.178   2.707   1.00 81.24  ? 97  GLU D OE2 1 
ATOM   7209  N N   . LEU D 2 98  ? 20.307  8.949   6.459   1.00 55.16  ? 98  LEU D N   1 
ATOM   7210  C CA  . LEU D 2 98  ? 19.072  9.675   6.730   1.00 61.58  ? 98  LEU D CA  1 
ATOM   7211  C C   . LEU D 2 98  ? 19.086  10.388  8.074   1.00 67.20  ? 98  LEU D C   1 
ATOM   7212  O O   . LEU D 2 98  ? 18.419  11.412  8.243   1.00 77.73  ? 98  LEU D O   1 
ATOM   7213  C CB  . LEU D 2 98  ? 17.840  8.779   6.599   1.00 62.19  ? 98  LEU D CB  1 
ATOM   7214  C CG  . LEU D 2 98  ? 17.100  8.920   5.266   1.00 71.76  ? 98  LEU D CG  1 
ATOM   7215  C CD1 . LEU D 2 98  ? 17.934  8.367   4.127   1.00 67.65  ? 98  LEU D CD1 1 
ATOM   7216  C CD2 . LEU D 2 98  ? 15.753  8.230   5.319   1.00 82.68  ? 98  LEU D CD2 1 
ATOM   7217  N N   . LEU D 2 99  ? 19.841  9.854   9.027   1.00 57.86  ? 99  LEU D N   1 
ATOM   7218  C CA  . LEU D 2 99  ? 20.016  10.542  10.301  1.00 56.94  ? 99  LEU D CA  1 
ATOM   7219  C C   . LEU D 2 99  ? 20.620  11.912  10.028  1.00 65.32  ? 99  LEU D C   1 
ATOM   7220  O O   . LEU D 2 99  ? 20.037  12.943  10.359  1.00 65.00  ? 99  LEU D O   1 
ATOM   7221  C CB  . LEU D 2 99  ? 20.936  9.752   11.234  1.00 58.19  ? 99  LEU D CB  1 
ATOM   7222  C CG  . LEU D 2 99  ? 21.000  10.325  12.649  1.00 54.33  ? 99  LEU D CG  1 
ATOM   7223  C CD1 . LEU D 2 99  ? 19.667  10.086  13.328  1.00 54.33  ? 99  LEU D CD1 1 
ATOM   7224  C CD2 . LEU D 2 99  ? 22.137  9.730   13.459  1.00 45.93  ? 99  LEU D CD2 1 
ATOM   7225  N N   . VAL D 2 100 ? 21.795  11.906  9.410   1.00 60.21  ? 100 VAL D N   1 
ATOM   7226  C CA  . VAL D 2 100 ? 22.448  13.134  8.982   1.00 56.26  ? 100 VAL D CA  1 
ATOM   7227  C C   . VAL D 2 100 ? 21.451  14.063  8.300   1.00 53.53  ? 100 VAL D C   1 
ATOM   7228  O O   . VAL D 2 100 ? 21.114  15.113  8.837   1.00 65.87  ? 100 VAL D O   1 
ATOM   7229  C CB  . VAL D 2 100 ? 23.603  12.841  8.022   1.00 61.81  ? 100 VAL D CB  1 
ATOM   7230  C CG1 . VAL D 2 100 ? 24.024  14.110  7.305   1.00 71.25  ? 100 VAL D CG1 1 
ATOM   7231  C CG2 . VAL D 2 100 ? 24.769  12.221  8.778   1.00 69.63  ? 100 VAL D CG2 1 
ATOM   7232  N N   . LEU D 2 101 ? 20.963  13.666  7.130   1.00 46.94  ? 101 LEU D N   1 
ATOM   7233  C CA  . LEU D 2 101 ? 20.008  14.486  6.394   1.00 48.85  ? 101 LEU D CA  1 
ATOM   7234  C C   . LEU D 2 101 ? 18.958  15.129  7.301   1.00 58.79  ? 101 LEU D C   1 
ATOM   7235  O O   . LEU D 2 101 ? 18.769  16.348  7.268   1.00 62.06  ? 101 LEU D O   1 
ATOM   7236  C CB  . LEU D 2 101 ? 19.339  13.689  5.274   1.00 43.45  ? 101 LEU D CB  1 
ATOM   7237  C CG  . LEU D 2 101 ? 20.247  13.226  4.130   1.00 47.91  ? 101 LEU D CG  1 
ATOM   7238  C CD1 . LEU D 2 101 ? 19.467  13.166  2.813   1.00 53.43  ? 101 LEU D CD1 1 
ATOM   7239  C CD2 . LEU D 2 101 ? 21.476  14.122  3.989   1.00 51.19  ? 101 LEU D CD2 1 
ATOM   7240  N N   . MET D 2 102 ? 18.287  14.322  8.119   1.00 50.25  ? 102 MET D N   1 
ATOM   7241  C CA  . MET D 2 102 ? 17.283  14.864  9.029   1.00 60.40  ? 102 MET D CA  1 
ATOM   7242  C C   . MET D 2 102 ? 17.918  15.789  10.067  1.00 61.13  ? 102 MET D C   1 
ATOM   7243  O O   . MET D 2 102 ? 17.531  16.951  10.187  1.00 72.32  ? 102 MET D O   1 
ATOM   7244  C CB  . MET D 2 102 ? 16.485  13.750  9.711   1.00 70.48  ? 102 MET D CB  1 
ATOM   7245  C CG  . MET D 2 102 ? 15.614  12.937  8.763   1.00 86.03  ? 102 MET D CG  1 
ATOM   7246  S SD  . MET D 2 102 ? 14.534  11.779  9.632   1.00 132.59 ? 102 MET D SD  1 
ATOM   7247  C CE  . MET D 2 102 ? 14.795  10.295  8.670   1.00 92.21  ? 102 MET D CE  1 
ATOM   7248  N N   . GLU D 2 103 ? 18.900  15.271  10.800  1.00 56.57  ? 103 GLU D N   1 
ATOM   7249  C CA  . GLU D 2 103 ? 19.587  16.046  11.831  1.00 53.83  ? 103 GLU D CA  1 
ATOM   7250  C C   . GLU D 2 103 ? 20.191  17.347  11.298  1.00 66.36  ? 103 GLU D C   1 
ATOM   7251  O O   . GLU D 2 103 ? 20.476  18.276  12.058  1.00 72.46  ? 103 GLU D O   1 
ATOM   7252  C CB  . GLU D 2 103 ? 20.670  15.208  12.512  1.00 49.13  ? 103 GLU D CB  1 
ATOM   7253  C CG  . GLU D 2 103 ? 20.132  14.344  13.620  1.00 55.09  ? 103 GLU D CG  1 
ATOM   7254  C CD  . GLU D 2 103 ? 19.233  15.132  14.548  1.00 72.90  ? 103 GLU D CD  1 
ATOM   7255  O OE1 . GLU D 2 103 ? 19.565  16.302  14.835  1.00 78.38  ? 103 GLU D OE1 1 
ATOM   7256  O OE2 . GLU D 2 103 ? 18.188  14.593  14.975  1.00 82.47  ? 103 GLU D OE2 1 
ATOM   7257  N N   . ASN D 2 104 ? 20.389  17.405  9.988   1.00 47.88  ? 104 ASN D N   1 
ATOM   7258  C CA  . ASN D 2 104 ? 20.987  18.573  9.372   1.00 45.65  ? 104 ASN D CA  1 
ATOM   7259  C C   . ASN D 2 104 ? 19.920  19.610  9.056   1.00 50.86  ? 104 ASN D C   1 
ATOM   7260  O O   . ASN D 2 104 ? 20.091  20.803  9.328   1.00 61.49  ? 104 ASN D O   1 
ATOM   7261  C CB  . ASN D 2 104 ? 21.778  18.176  8.124   1.00 51.51  ? 104 ASN D CB  1 
ATOM   7262  C CG  . ASN D 2 104 ? 23.185  17.694  8.455   1.00 61.01  ? 104 ASN D CG  1 
ATOM   7263  O OD1 . ASN D 2 104 ? 23.600  17.699  9.618   1.00 62.07  ? 104 ASN D OD1 1 
ATOM   7264  N ND2 . ASN D 2 104 ? 23.925  17.274  7.431   1.00 62.05  ? 104 ASN D ND2 1 
ATOM   7265  N N   . GLU D 2 105 ? 18.808  19.148  8.499   1.00 57.86  ? 105 GLU D N   1 
ATOM   7266  C CA  . GLU D 2 105 ? 17.678  20.023  8.250   1.00 56.29  ? 105 GLU D CA  1 
ATOM   7267  C C   . GLU D 2 105 ? 17.276  20.722  9.551   1.00 54.85  ? 105 GLU D C   1 
ATOM   7268  O O   . GLU D 2 105 ? 16.974  21.913  9.559   1.00 61.12  ? 105 GLU D O   1 
ATOM   7269  C CB  . GLU D 2 105 ? 16.498  19.224  7.689   1.00 67.27  ? 105 GLU D CB  1 
ATOM   7270  C CG  . GLU D 2 105 ? 15.447  20.067  6.986   1.00 85.24  ? 105 GLU D CG  1 
ATOM   7271  C CD  . GLU D 2 105 ? 15.960  20.690  5.701   1.00 96.64  ? 105 GLU D CD  1 
ATOM   7272  O OE1 . GLU D 2 105 ? 15.732  21.901  5.493   1.00 99.55  ? 105 GLU D OE1 1 
ATOM   7273  O OE2 . GLU D 2 105 ? 16.580  19.967  4.894   1.00 97.81  ? 105 GLU D OE2 1 
ATOM   7274  N N   . HIS D 2 106 ? 17.297  19.983  10.653  1.00 56.59  ? 106 HIS D N   1 
ATOM   7275  C CA  A HIS D 2 106 ? 16.861  20.523  11.939  0.56 57.34  ? 106 HIS D CA  1 
ATOM   7276  C CA  B HIS D 2 106 ? 16.854  20.516  11.935  0.44 57.56  ? 106 HIS D CA  1 
ATOM   7277  C C   . HIS D 2 106 ? 17.880  21.458  12.574  1.00 56.53  ? 106 HIS D C   1 
ATOM   7278  O O   . HIS D 2 106 ? 17.512  22.422  13.240  1.00 59.02  ? 106 HIS D O   1 
ATOM   7279  C CB  A HIS D 2 106 ? 16.521  19.405  12.929  0.56 58.04  ? 106 HIS D CB  1 
ATOM   7280  C CB  B HIS D 2 106 ? 16.495  19.373  12.896  0.44 56.72  ? 106 HIS D CB  1 
ATOM   7281  C CG  A HIS D 2 106 ? 16.234  19.898  14.315  0.56 60.58  ? 106 HIS D CG  1 
ATOM   7282  C CG  B HIS D 2 106 ? 15.340  18.531  12.439  0.44 55.81  ? 106 HIS D CG  1 
ATOM   7283  N ND1 A HIS D 2 106 ? 17.220  20.069  15.262  0.56 53.51  ? 106 HIS D ND1 1 
ATOM   7284  N ND1 B HIS D 2 106 ? 15.306  17.162  12.600  0.44 52.27  ? 106 HIS D ND1 1 
ATOM   7285  C CD2 A HIS D 2 106 ? 15.073  20.265  14.908  0.56 60.03  ? 106 HIS D CD2 1 
ATOM   7286  C CD2 B HIS D 2 106 ? 14.174  18.866  11.836  0.44 59.45  ? 106 HIS D CD2 1 
ATOM   7287  C CE1 A HIS D 2 106 ? 16.678  20.518  16.381  0.56 54.07  ? 106 HIS D CE1 1 
ATOM   7288  C CE1 B HIS D 2 106 ? 14.173  16.690  12.112  0.44 56.23  ? 106 HIS D CE1 1 
ATOM   7289  N NE2 A HIS D 2 106 ? 15.377  20.644  16.193  0.56 55.82  ? 106 HIS D NE2 1 
ATOM   7290  N NE2 B HIS D 2 106 ? 13.467  17.703  11.642  0.44 62.01  ? 106 HIS D NE2 1 
ATOM   7291  N N   . THR D 2 107 ? 19.165  21.178  12.387  1.00 47.55  ? 107 THR D N   1 
ATOM   7292  C CA  . THR D 2 107 ? 20.176  22.042  12.993  1.00 52.21  ? 107 THR D CA  1 
ATOM   7293  C C   . THR D 2 107 ? 20.120  23.434  12.379  1.00 56.70  ? 107 THR D C   1 
ATOM   7294  O O   . THR D 2 107 ? 20.002  24.437  13.089  1.00 63.91  ? 107 THR D O   1 
ATOM   7295  C CB  . THR D 2 107 ? 21.603  21.480  12.871  1.00 53.67  ? 107 THR D CB  1 
ATOM   7296  O OG1 . THR D 2 107 ? 21.732  20.327  13.704  1.00 52.25  ? 107 THR D OG1 1 
ATOM   7297  C CG2 . THR D 2 107 ? 22.616  22.517  13.324  1.00 59.03  ? 107 THR D CG2 1 
ATOM   7298  N N   . LEU D 2 108 ? 20.197  23.490  11.053  1.00 38.60  ? 108 LEU D N   1 
ATOM   7299  C CA  . LEU D 2 108 ? 20.115  24.759  10.344  1.00 31.39  ? 108 LEU D CA  1 
ATOM   7300  C C   . LEU D 2 108 ? 18.888  25.576  10.778  1.00 41.11  ? 108 LEU D C   1 
ATOM   7301  O O   . LEU D 2 108 ? 18.992  26.773  11.004  1.00 51.80  ? 108 LEU D O   1 
ATOM   7302  C CB  . LEU D 2 108 ? 20.118  24.537  8.826   1.00 31.93  ? 108 LEU D CB  1 
ATOM   7303  C CG  . LEU D 2 108 ? 21.336  23.871  8.175   1.00 42.59  ? 108 LEU D CG  1 
ATOM   7304  C CD1 . LEU D 2 108 ? 21.313  24.147  6.683   1.00 51.72  ? 108 LEU D CD1 1 
ATOM   7305  C CD2 . LEU D 2 108 ? 22.654  24.353  8.780   1.00 43.78  ? 108 LEU D CD2 1 
ATOM   7306  N N   . ASP D 2 109 ? 17.737  24.926  10.908  1.00 53.57  ? 109 ASP D N   1 
ATOM   7307  C CA  . ASP D 2 109 ? 16.525  25.623  11.328  1.00 54.01  ? 109 ASP D CA  1 
ATOM   7308  C C   . ASP D 2 109 ? 16.568  26.053  12.797  1.00 60.19  ? 109 ASP D C   1 
ATOM   7309  O O   . ASP D 2 109 ? 15.969  27.063  13.166  1.00 66.10  ? 109 ASP D O   1 
ATOM   7310  C CB  . ASP D 2 109 ? 15.279  24.774  11.065  1.00 55.40  ? 109 ASP D CB  1 
ATOM   7311  C CG  . ASP D 2 109 ? 15.062  24.499  9.591   1.00 69.17  ? 109 ASP D CG  1 
ATOM   7312  O OD1 . ASP D 2 109 ? 15.853  25.009  8.770   1.00 78.73  ? 109 ASP D OD1 1 
ATOM   7313  O OD2 . ASP D 2 109 ? 14.093  23.787  9.251   1.00 74.80  ? 109 ASP D OD2 1 
ATOM   7314  N N   . PHE D 2 110 ? 17.258  25.280  13.633  1.00 53.49  ? 110 PHE D N   1 
ATOM   7315  C CA  . PHE D 2 110 ? 17.459  25.655  15.031  1.00 48.87  ? 110 PHE D CA  1 
ATOM   7316  C C   . PHE D 2 110 ? 18.132  27.017  15.044  1.00 64.15  ? 110 PHE D C   1 
ATOM   7317  O O   . PHE D 2 110 ? 17.691  27.942  15.731  1.00 76.68  ? 110 PHE D O   1 
ATOM   7318  C CB  . PHE D 2 110 ? 18.329  24.621  15.752  1.00 40.89  ? 110 PHE D CB  1 
ATOM   7319  C CG  . PHE D 2 110 ? 18.678  24.986  17.177  1.00 41.19  ? 110 PHE D CG  1 
ATOM   7320  C CD1 . PHE D 2 110 ? 17.688  25.270  18.104  1.00 43.92  ? 110 PHE D CD1 1 
ATOM   7321  C CD2 . PHE D 2 110 ? 20.002  25.008  17.598  1.00 41.76  ? 110 PHE D CD2 1 
ATOM   7322  C CE1 . PHE D 2 110 ? 18.010  25.587  19.415  1.00 43.04  ? 110 PHE D CE1 1 
ATOM   7323  C CE2 . PHE D 2 110 ? 20.327  25.331  18.908  1.00 40.96  ? 110 PHE D CE2 1 
ATOM   7324  C CZ  . PHE D 2 110 ? 19.330  25.617  19.813  1.00 38.36  ? 110 PHE D CZ  1 
ATOM   7325  N N   . HIS D 2 111 ? 19.198  27.137  14.263  1.00 56.17  ? 111 HIS D N   1 
ATOM   7326  C CA  . HIS D 2 111 ? 19.886  28.407  14.125  1.00 58.10  ? 111 HIS D CA  1 
ATOM   7327  C C   . HIS D 2 111 ? 18.930  29.488  13.608  1.00 64.65  ? 111 HIS D C   1 
ATOM   7328  O O   . HIS D 2 111 ? 19.049  30.659  13.968  1.00 72.61  ? 111 HIS D O   1 
ATOM   7329  C CB  . HIS D 2 111 ? 21.099  28.259  13.200  1.00 60.43  ? 111 HIS D CB  1 
ATOM   7330  C CG  . HIS D 2 111 ? 22.265  27.572  13.840  1.00 59.96  ? 111 HIS D CG  1 
ATOM   7331  N ND1 . HIS D 2 111 ? 22.849  28.027  15.002  1.00 56.81  ? 111 HIS D ND1 1 
ATOM   7332  C CD2 . HIS D 2 111 ? 22.961  26.469  13.477  1.00 63.16  ? 111 HIS D CD2 1 
ATOM   7333  C CE1 . HIS D 2 111 ? 23.855  27.234  15.327  1.00 60.47  ? 111 HIS D CE1 1 
ATOM   7334  N NE2 . HIS D 2 111 ? 23.944  26.280  14.418  1.00 65.47  ? 111 HIS D NE2 1 
ATOM   7335  N N   . ASP D 2 112 ? 17.978  29.093  12.770  1.00 64.83  ? 112 ASP D N   1 
ATOM   7336  C CA  . ASP D 2 112 ? 17.015  30.042  12.228  1.00 64.38  ? 112 ASP D CA  1 
ATOM   7337  C C   . ASP D 2 112 ? 16.139  30.546  13.368  1.00 66.94  ? 112 ASP D C   1 
ATOM   7338  O O   . ASP D 2 112 ? 16.174  31.725  13.712  1.00 68.25  ? 112 ASP D O   1 
ATOM   7339  C CB  . ASP D 2 112 ? 16.167  29.392  11.131  1.00 66.59  ? 112 ASP D CB  1 
ATOM   7340  C CG  . ASP D 2 112 ? 15.724  30.384  10.067  1.00 72.55  ? 112 ASP D CG  1 
ATOM   7341  O OD1 . ASP D 2 112 ? 16.339  31.463  9.963   1.00 78.37  ? 112 ASP D OD1 1 
ATOM   7342  O OD2 . ASP D 2 112 ? 14.770  30.079  9.321   1.00 78.09  ? 112 ASP D OD2 1 
ATOM   7343  N N   . SER D 2 113 ? 15.363  29.643  13.956  1.00 66.28  ? 113 SER D N   1 
ATOM   7344  C CA  . SER D 2 113 ? 14.590  29.957  15.148  1.00 68.50  ? 113 SER D CA  1 
ATOM   7345  C C   . SER D 2 113 ? 15.386  30.870  16.077  1.00 70.20  ? 113 SER D C   1 
ATOM   7346  O O   . SER D 2 113 ? 14.928  31.952  16.445  1.00 76.85  ? 113 SER D O   1 
ATOM   7347  C CB  . SER D 2 113 ? 14.214  28.668  15.883  1.00 67.15  ? 113 SER D CB  1 
ATOM   7348  O OG  . SER D 2 113 ? 13.806  28.917  17.219  1.00 65.62  ? 113 SER D OG  1 
ATOM   7349  N N   . ASN D 2 114 ? 16.585  30.428  16.445  1.00 58.53  ? 114 ASN D N   1 
ATOM   7350  C CA  . ASN D 2 114 ? 17.428  31.156  17.393  1.00 49.67  ? 114 ASN D CA  1 
ATOM   7351  C C   . ASN D 2 114 ? 17.582  32.631  17.059  1.00 56.66  ? 114 ASN D C   1 
ATOM   7352  O O   . ASN D 2 114 ? 17.438  33.493  17.927  1.00 62.24  ? 114 ASN D O   1 
ATOM   7353  C CB  . ASN D 2 114 ? 18.803  30.498  17.489  1.00 42.62  ? 114 ASN D CB  1 
ATOM   7354  C CG  . ASN D 2 114 ? 18.795  29.266  18.368  1.00 49.09  ? 114 ASN D CG  1 
ATOM   7355  O OD1 . ASN D 2 114 ? 17.743  28.830  18.839  1.00 58.76  ? 114 ASN D OD1 1 
ATOM   7356  N ND2 . ASN D 2 114 ? 19.971  28.700  18.598  1.00 51.98  ? 114 ASN D ND2 1 
ATOM   7357  N N   . VAL D 2 115 ? 17.886  32.908  15.797  1.00 49.81  ? 115 VAL D N   1 
ATOM   7358  C CA  . VAL D 2 115 ? 17.977  34.280  15.311  1.00 47.12  ? 115 VAL D CA  1 
ATOM   7359  C C   . VAL D 2 115 ? 16.636  35.015  15.423  1.00 55.67  ? 115 VAL D C   1 
ATOM   7360  O O   . VAL D 2 115 ? 16.532  36.013  16.131  1.00 65.35  ? 115 VAL D O   1 
ATOM   7361  C CB  . VAL D 2 115 ? 18.484  34.332  13.858  1.00 44.04  ? 115 VAL D CB  1 
ATOM   7362  C CG1 . VAL D 2 115 ? 18.038  35.619  13.199  1.00 43.70  ? 115 VAL D CG1 1 
ATOM   7363  C CG2 . VAL D 2 115 ? 20.004  34.187  13.812  1.00 44.19  ? 115 VAL D CG2 1 
ATOM   7364  N N   . LYS D 2 116 ? 15.611  34.517  14.735  1.00 56.34  ? 116 LYS D N   1 
ATOM   7365  C CA  . LYS D 2 116 ? 14.290  35.138  14.784  1.00 57.79  ? 116 LYS D CA  1 
ATOM   7366  C C   . LYS D 2 116 ? 13.804  35.372  16.210  1.00 56.61  ? 116 LYS D C   1 
ATOM   7367  O O   . LYS D 2 116 ? 13.122  36.356  16.482  1.00 53.55  ? 116 LYS D O   1 
ATOM   7368  C CB  . LYS D 2 116 ? 13.253  34.314  14.027  1.00 60.52  ? 116 LYS D CB  1 
ATOM   7369  C CG  . LYS D 2 116 ? 11.824  34.748  14.315  1.00 69.24  ? 116 LYS D CG  1 
ATOM   7370  C CD  . LYS D 2 116 ? 10.866  34.252  13.254  1.00 75.91  ? 116 LYS D CD  1 
ATOM   7371  C CE  . LYS D 2 116 ? 9.903   35.349  12.833  1.00 79.70  ? 116 LYS D CE  1 
ATOM   7372  N NZ  . LYS D 2 116 ? 9.112   35.876  13.983  1.00 82.80  ? 116 LYS D NZ  1 
ATOM   7373  N N   . ASN D 2 117 ? 14.143  34.464  17.117  1.00 57.80  ? 117 ASN D N   1 
ATOM   7374  C CA  . ASN D 2 117 ? 13.794  34.648  18.519  1.00 55.56  ? 117 ASN D CA  1 
ATOM   7375  C C   . ASN D 2 117 ? 14.465  35.892  19.089  1.00 56.19  ? 117 ASN D C   1 
ATOM   7376  O O   . ASN D 2 117 ? 13.817  36.723  19.729  1.00 58.31  ? 117 ASN D O   1 
ATOM   7377  C CB  . ASN D 2 117 ? 14.169  33.420  19.342  1.00 47.44  ? 117 ASN D CB  1 
ATOM   7378  C CG  . ASN D 2 117 ? 13.251  32.250  19.086  1.00 58.96  ? 117 ASN D CG  1 
ATOM   7379  O OD1 . ASN D 2 117 ? 12.385  32.301  18.213  1.00 69.83  ? 117 ASN D OD1 1 
ATOM   7380  N ND2 . ASN D 2 117 ? 13.440  31.181  19.846  1.00 60.59  ? 117 ASN D ND2 1 
ATOM   7381  N N   . LEU D 2 118 ? 15.766  36.019  18.849  1.00 40.54  ? 118 LEU D N   1 
ATOM   7382  C CA  . LEU D 2 118 ? 16.501  37.198  19.288  1.00 43.97  ? 118 LEU D CA  1 
ATOM   7383  C C   . LEU D 2 118 ? 15.836  38.439  18.714  1.00 46.16  ? 118 LEU D C   1 
ATOM   7384  O O   . LEU D 2 118 ? 15.499  39.365  19.448  1.00 57.23  ? 118 LEU D O   1 
ATOM   7385  C CB  . LEU D 2 118 ? 17.963  37.122  18.843  1.00 46.98  ? 118 LEU D CB  1 
ATOM   7386  C CG  . LEU D 2 118 ? 18.904  38.103  19.535  1.00 45.45  ? 118 LEU D CG  1 
ATOM   7387  C CD1 . LEU D 2 118 ? 18.491  38.261  20.978  1.00 39.82  ? 118 LEU D CD1 1 
ATOM   7388  C CD2 . LEU D 2 118 ? 20.335  37.625  19.431  1.00 47.70  ? 118 LEU D CD2 1 
ATOM   7389  N N   . TYR D 2 119 ? 15.629  38.447  17.400  1.00 52.07  ? 119 TYR D N   1 
ATOM   7390  C CA  . TYR D 2 119 ? 14.958  39.569  16.758  1.00 52.33  ? 119 TYR D CA  1 
ATOM   7391  C C   . TYR D 2 119 ? 13.624  39.873  17.440  1.00 53.49  ? 119 TYR D C   1 
ATOM   7392  O O   . TYR D 2 119 ? 13.354  41.011  17.783  1.00 62.04  ? 119 TYR D O   1 
ATOM   7393  C CB  . TYR D 2 119 ? 14.750  39.298  15.268  1.00 54.31  ? 119 TYR D CB  1 
ATOM   7394  C CG  . TYR D 2 119 ? 14.106  40.444  14.512  1.00 63.22  ? 119 TYR D CG  1 
ATOM   7395  C CD1 . TYR D 2 119 ? 14.860  41.525  14.071  1.00 72.95  ? 119 TYR D CD1 1 
ATOM   7396  C CD2 . TYR D 2 119 ? 12.747  40.441  14.234  1.00 68.36  ? 119 TYR D CD2 1 
ATOM   7397  C CE1 . TYR D 2 119 ? 14.279  42.572  13.373  1.00 77.09  ? 119 TYR D CE1 1 
ATOM   7398  C CE2 . TYR D 2 119 ? 12.157  41.483  13.539  1.00 74.67  ? 119 TYR D CE2 1 
ATOM   7399  C CZ  . TYR D 2 119 ? 12.928  42.545  13.112  1.00 76.30  ? 119 TYR D CZ  1 
ATOM   7400  O OH  . TYR D 2 119 ? 12.347  43.582  12.419  1.00 76.41  ? 119 TYR D OH  1 
ATOM   7401  N N   . ASP D 2 120 ? 12.800  38.852  17.642  1.00 59.10  ? 120 ASP D N   1 
ATOM   7402  C CA  . ASP D 2 120 ? 11.514  39.036  18.307  1.00 69.49  ? 120 ASP D CA  1 
ATOM   7403  C C   . ASP D 2 120 ? 11.683  39.497  19.753  1.00 68.48  ? 120 ASP D C   1 
ATOM   7404  O O   . ASP D 2 120 ? 10.897  40.305  20.244  1.00 67.22  ? 120 ASP D O   1 
ATOM   7405  C CB  . ASP D 2 120 ? 10.680  37.747  18.270  1.00 75.10  ? 120 ASP D CB  1 
ATOM   7406  C CG  . ASP D 2 120 ? 9.989   37.530  16.933  1.00 73.02  ? 120 ASP D CG  1 
ATOM   7407  O OD1 . ASP D 2 120 ? 9.735   38.522  16.216  1.00 70.10  ? 120 ASP D OD1 1 
ATOM   7408  O OD2 . ASP D 2 120 ? 9.695   36.361  16.601  1.00 73.89  ? 120 ASP D OD2 1 
ATOM   7409  N N   . LYS D 2 121 ? 12.699  38.975  20.437  1.00 70.86  ? 121 LYS D N   1 
ATOM   7410  C CA  . LYS D 2 121 ? 12.912  39.292  21.849  1.00 72.24  ? 121 LYS D CA  1 
ATOM   7411  C C   . LYS D 2 121 ? 13.264  40.764  22.037  1.00 72.60  ? 121 LYS D C   1 
ATOM   7412  O O   . LYS D 2 121 ? 12.954  41.363  23.069  1.00 81.66  ? 121 LYS D O   1 
ATOM   7413  C CB  . LYS D 2 121 ? 14.000  38.402  22.456  1.00 74.30  ? 121 LYS D CB  1 
ATOM   7414  C CG  . LYS D 2 121 ? 14.455  38.845  23.840  1.00 88.69  ? 121 LYS D CG  1 
ATOM   7415  C CD  . LYS D 2 121 ? 15.599  37.986  24.361  1.00 92.69  ? 121 LYS D CD  1 
ATOM   7416  C CE  . LYS D 2 121 ? 16.396  38.707  25.449  1.00 94.34  ? 121 LYS D CE  1 
ATOM   7417  N NZ  . LYS D 2 121 ? 17.140  39.899  24.929  1.00 92.88  ? 121 LYS D NZ  1 
ATOM   7418  N N   . VAL D 2 122 ? 13.915  41.341  21.033  1.00 53.07  ? 122 VAL D N   1 
ATOM   7419  C CA  . VAL D 2 122 ? 14.268  42.759  21.053  1.00 50.24  ? 122 VAL D CA  1 
ATOM   7420  C C   . VAL D 2 122 ? 13.090  43.623  20.606  1.00 61.14  ? 122 VAL D C   1 
ATOM   7421  O O   . VAL D 2 122 ? 12.638  44.504  21.332  1.00 61.84  ? 122 VAL D O   1 
ATOM   7422  C CB  . VAL D 2 122 ? 15.476  43.048  20.146  1.00 38.97  ? 122 VAL D CB  1 
ATOM   7423  C CG1 . VAL D 2 122 ? 15.455  44.494  19.679  1.00 40.57  ? 122 VAL D CG1 1 
ATOM   7424  C CG2 . VAL D 2 122 ? 16.765  42.729  20.872  1.00 47.39  ? 122 VAL D CG2 1 
ATOM   7425  N N   . ARG D 2 123 ? 12.612  43.359  19.396  1.00 80.47  ? 123 ARG D N   1 
ATOM   7426  C CA  . ARG D 2 123 ? 11.438  44.017  18.852  1.00 76.67  ? 123 ARG D CA  1 
ATOM   7427  C C   . ARG D 2 123 ? 10.374  44.243  19.926  1.00 76.45  ? 123 ARG D C   1 
ATOM   7428  O O   . ARG D 2 123 ? 9.973   45.378  20.186  1.00 80.65  ? 123 ARG D O   1 
ATOM   7429  C CB  . ARG D 2 123 ? 10.861  43.174  17.713  1.00 76.26  ? 123 ARG D CB  1 
ATOM   7430  C CG  . ARG D 2 123 ? 9.630   43.757  17.049  1.00 82.47  ? 123 ARG D CG  1 
ATOM   7431  C CD  . ARG D 2 123 ? 9.049   42.801  16.013  1.00 85.28  ? 123 ARG D CD  1 
ATOM   7432  N NE  . ARG D 2 123 ? 8.320   41.689  16.621  1.00 84.42  ? 123 ARG D NE  1 
ATOM   7433  C CZ  . ARG D 2 123 ? 7.052   41.753  17.020  1.00 84.88  ? 123 ARG D CZ  1 
ATOM   7434  N NH1 . ARG D 2 123 ? 6.367   42.885  16.886  1.00 81.72  ? 123 ARG D NH1 1 
ATOM   7435  N NH2 . ARG D 2 123 ? 6.470   40.688  17.561  1.00 87.02  ? 123 ARG D NH2 1 
ATOM   7436  N N   . MET D 2 124 ? 9.931   43.160  20.557  1.00 59.94  ? 124 MET D N   1 
ATOM   7437  C CA  . MET D 2 124 ? 8.807   43.214  21.491  1.00 60.33  ? 124 MET D CA  1 
ATOM   7438  C C   . MET D 2 124 ? 9.115   44.061  22.715  1.00 69.26  ? 124 MET D C   1 
ATOM   7439  O O   . MET D 2 124 ? 8.218   44.383  23.487  1.00 77.47  ? 124 MET D O   1 
ATOM   7440  C CB  . MET D 2 124 ? 8.393   41.803  21.940  1.00 48.76  ? 124 MET D CB  1 
ATOM   7441  C CG  . MET D 2 124 ? 8.041   40.837  20.807  1.00 44.25  ? 124 MET D CG  1 
ATOM   7442  S SD  . MET D 2 124 ? 7.277   39.322  21.413  1.00 74.43  ? 124 MET D SD  1 
ATOM   7443  C CE  . MET D 2 124 ? 5.628   39.891  21.803  1.00 76.28  ? 124 MET D CE  1 
ATOM   7444  N N   . GLN D 2 125 ? 10.386  44.401  22.900  1.00 56.44  ? 125 GLN D N   1 
ATOM   7445  C CA  . GLN D 2 125 ? 10.800  45.219  24.037  1.00 56.78  ? 125 GLN D CA  1 
ATOM   7446  C C   . GLN D 2 125 ? 10.838  46.705  23.655  1.00 56.14  ? 125 GLN D C   1 
ATOM   7447  O O   . GLN D 2 125 ? 10.746  47.580  24.517  1.00 63.63  ? 125 GLN D O   1 
ATOM   7448  C CB  . GLN D 2 125 ? 12.172  44.766  24.548  1.00 66.68  ? 125 GLN D CB  1 
ATOM   7449  C CG  . GLN D 2 125 ? 12.339  44.828  26.059  1.00 70.49  ? 125 GLN D CG  1 
ATOM   7450  C CD  . GLN D 2 125 ? 13.767  44.541  26.499  1.00 65.65  ? 125 GLN D CD  1 
ATOM   7451  O OE1 . GLN D 2 125 ? 14.062  44.489  27.697  1.00 75.41  ? 125 GLN D OE1 1 
ATOM   7452  N NE2 . GLN D 2 125 ? 14.664  44.357  25.529  1.00 42.66  ? 125 GLN D NE2 1 
ATOM   7453  N N   . LEU D 2 126 ? 10.968  46.983  22.358  1.00 64.69  ? 126 LEU D N   1 
ATOM   7454  C CA  . LEU D 2 126 ? 11.065  48.355  21.867  1.00 58.28  ? 126 LEU D CA  1 
ATOM   7455  C C   . LEU D 2 126 ? 9.704   48.936  21.512  1.00 63.10  ? 126 LEU D C   1 
ATOM   7456  O O   . LEU D 2 126 ? 9.367   50.041  21.930  1.00 59.01  ? 126 LEU D O   1 
ATOM   7457  C CB  . LEU D 2 126 ? 11.986  48.428  20.656  1.00 46.18  ? 126 LEU D CB  1 
ATOM   7458  C CG  . LEU D 2 126 ? 13.390  47.888  20.897  1.00 43.21  ? 126 LEU D CG  1 
ATOM   7459  C CD1 . LEU D 2 126 ? 14.298  48.179  19.704  1.00 41.33  ? 126 LEU D CD1 1 
ATOM   7460  C CD2 . LEU D 2 126 ? 13.951  48.492  22.165  1.00 53.46  ? 126 LEU D CD2 1 
ATOM   7461  N N   . ARG D 2 127 ? 8.927   48.194  20.733  1.00 53.04  ? 127 ARG D N   1 
ATOM   7462  C CA  . ARG D 2 127 ? 7.577   48.621  20.390  1.00 56.93  ? 127 ARG D CA  1 
ATOM   7463  C C   . ARG D 2 127 ? 7.575   49.864  19.518  1.00 61.92  ? 127 ARG D C   1 
ATOM   7464  O O   . ARG D 2 127 ? 8.480   50.071  18.705  1.00 69.66  ? 127 ARG D O   1 
ATOM   7465  C CB  . ARG D 2 127 ? 6.777   48.917  21.655  1.00 54.86  ? 127 ARG D CB  1 
ATOM   7466  C CG  . ARG D 2 127 ? 6.556   47.739  22.559  1.00 48.77  ? 127 ARG D CG  1 
ATOM   7467  C CD  . ARG D 2 127 ? 5.302   47.976  23.374  1.00 57.13  ? 127 ARG D CD  1 
ATOM   7468  N NE  . ARG D 2 127 ? 5.590   48.227  24.780  1.00 67.16  ? 127 ARG D NE  1 
ATOM   7469  C CZ  . ARG D 2 127 ? 4.676   48.602  25.666  1.00 74.47  ? 127 ARG D CZ  1 
ATOM   7470  N NH1 . ARG D 2 127 ? 3.418   48.780  25.283  1.00 77.57  ? 127 ARG D NH1 1 
ATOM   7471  N NH2 . ARG D 2 127 ? 5.021   48.800  26.931  1.00 77.94  ? 127 ARG D NH2 1 
ATOM   7472  N N   . ASP D 2 128 ? 6.550   50.695  19.711  1.00 50.99  ? 128 ASP D N   1 
ATOM   7473  C CA  . ASP D 2 128 ? 6.407   51.960  18.970  1.00 43.11  ? 128 ASP D CA  1 
ATOM   7474  C C   . ASP D 2 128 ? 7.509   52.967  19.266  1.00 43.94  ? 128 ASP D C   1 
ATOM   7475  O O   . ASP D 2 128 ? 7.460   54.084  18.783  1.00 50.25  ? 128 ASP D O   1 
ATOM   7476  C CB  . ASP D 2 128 ? 5.035   52.598  19.209  1.00 43.76  ? 128 ASP D CB  1 
ATOM   7477  C CG  . ASP D 2 128 ? 4.672   52.651  20.675  1.00 60.07  ? 128 ASP D CG  1 
ATOM   7478  O OD1 . ASP D 2 128 ? 5.583   52.527  21.527  1.00 64.20  ? 128 ASP D OD1 1 
ATOM   7479  O OD2 . ASP D 2 128 ? 3.471   52.815  20.976  1.00 69.32  ? 128 ASP D OD2 1 
ATOM   7480  N N   . ASN D 2 129 ? 8.506   52.579  20.050  1.00 52.52  ? 129 ASN D N   1 
ATOM   7481  C CA  . ASN D 2 129 ? 9.646   53.456  20.270  1.00 53.53  ? 129 ASN D CA  1 
ATOM   7482  C C   . ASN D 2 129 ? 10.619  53.448  19.106  1.00 53.57  ? 129 ASN D C   1 
ATOM   7483  O O   . ASN D 2 129 ? 11.584  54.204  19.114  1.00 54.38  ? 129 ASN D O   1 
ATOM   7484  C CB  . ASN D 2 129 ? 10.394  53.081  21.546  1.00 51.78  ? 129 ASN D CB  1 
ATOM   7485  C CG  . ASN D 2 129 ? 10.064  53.992  22.705  1.00 57.63  ? 129 ASN D CG  1 
ATOM   7486  O OD1 . ASN D 2 129 ? 9.018   54.645  22.722  1.00 62.88  ? 129 ASN D OD1 1 
ATOM   7487  N ND2 . ASN D 2 129 ? 10.959  54.044  23.686  1.00 57.22  ? 129 ASN D ND2 1 
ATOM   7488  N N   . VAL D 2 130 ? 10.385  52.590  18.114  1.00 65.85  ? 130 VAL D N   1 
ATOM   7489  C CA  . VAL D 2 130 ? 11.313  52.493  16.982  1.00 61.68  ? 130 VAL D CA  1 
ATOM   7490  C C   . VAL D 2 130 ? 10.690  52.103  15.643  1.00 64.69  ? 130 VAL D C   1 
ATOM   7491  O O   . VAL D 2 130 ? 9.613   51.510  15.579  1.00 63.91  ? 130 VAL D O   1 
ATOM   7492  C CB  . VAL D 2 130 ? 12.478  51.527  17.267  1.00 55.27  ? 130 VAL D CB  1 
ATOM   7493  C CG1 . VAL D 2 130 ? 13.279  51.987  18.482  1.00 54.36  ? 130 VAL D CG1 1 
ATOM   7494  C CG2 . VAL D 2 130 ? 11.962  50.109  17.462  1.00 61.51  ? 130 VAL D CG2 1 
ATOM   7495  N N   . LYS D 2 131 ? 11.405  52.446  14.578  1.00 83.73  ? 131 LYS D N   1 
ATOM   7496  C CA  . LYS D 2 131 ? 10.976  52.202  13.212  1.00 92.78  ? 131 LYS D CA  1 
ATOM   7497  C C   . LYS D 2 131 ? 11.505  50.839  12.806  1.00 94.39  ? 131 LYS D C   1 
ATOM   7498  O O   . LYS D 2 131 ? 12.715  50.640  12.735  1.00 101.01 ? 131 LYS D O   1 
ATOM   7499  C CB  . LYS D 2 131 ? 11.568  53.283  12.302  1.00 99.82  ? 131 LYS D CB  1 
ATOM   7500  C CG  . LYS D 2 131 ? 10.790  53.591  11.029  1.00 111.81 ? 131 LYS D CG  1 
ATOM   7501  C CD  . LYS D 2 131 ? 11.306  54.893  10.405  1.00 121.55 ? 131 LYS D CD  1 
ATOM   7502  C CE  . LYS D 2 131 ? 10.611  55.221  9.092   1.00 124.93 ? 131 LYS D CE  1 
ATOM   7503  N NZ  . LYS D 2 131 ? 11.579  55.318  7.961   1.00 125.53 ? 131 LYS D NZ  1 
ATOM   7504  N N   . GLU D 2 132 ? 10.605  49.894  12.557  1.00 65.07  ? 132 GLU D N   1 
ATOM   7505  C CA  . GLU D 2 132 ? 11.014  48.546  12.166  1.00 64.65  ? 132 GLU D CA  1 
ATOM   7506  C C   . GLU D 2 132 ? 11.354  48.491  10.675  1.00 79.23  ? 132 GLU D C   1 
ATOM   7507  O O   . GLU D 2 132 ? 10.469  48.335  9.832   1.00 90.24  ? 132 GLU D O   1 
ATOM   7508  C CB  . GLU D 2 132 ? 9.920   47.535  12.506  1.00 59.82  ? 132 GLU D CB  1 
ATOM   7509  C CG  . GLU D 2 132 ? 10.454  46.152  12.841  1.00 64.64  ? 132 GLU D CG  1 
ATOM   7510  C CD  . GLU D 2 132 ? 9.357   45.114  13.011  1.00 70.46  ? 132 GLU D CD  1 
ATOM   7511  O OE1 . GLU D 2 132 ? 8.281   45.451  13.555  1.00 80.83  ? 132 GLU D OE1 1 
ATOM   7512  O OE2 . GLU D 2 132 ? 9.574   43.956  12.593  1.00 68.22  ? 132 GLU D OE2 1 
ATOM   7513  N N   . LEU D 2 133 ? 12.641  48.619  10.359  1.00 73.14  ? 133 LEU D N   1 
ATOM   7514  C CA  . LEU D 2 133 ? 13.100  48.726  8.973   1.00 67.80  ? 133 LEU D CA  1 
ATOM   7515  C C   . LEU D 2 133 ? 12.834  47.478  8.130   1.00 78.02  ? 133 LEU D C   1 
ATOM   7516  O O   . LEU D 2 133 ? 12.917  47.532  6.902   1.00 81.03  ? 133 LEU D O   1 
ATOM   7517  C CB  . LEU D 2 133 ? 14.588  49.073  8.927   1.00 54.24  ? 133 LEU D CB  1 
ATOM   7518  C CG  . LEU D 2 133 ? 14.975  50.393  9.597   1.00 53.21  ? 133 LEU D CG  1 
ATOM   7519  C CD1 . LEU D 2 133 ? 16.434  50.735  9.310   1.00 55.85  ? 133 LEU D CD1 1 
ATOM   7520  C CD2 . LEU D 2 133 ? 14.053  51.524  9.152   1.00 52.70  ? 133 LEU D CD2 1 
ATOM   7521  N N   . GLY D 2 134 ? 12.528  46.360  8.789   1.00 71.73  ? 134 GLY D N   1 
ATOM   7522  C CA  . GLY D 2 134 ? 12.191  45.128  8.098   1.00 65.90  ? 134 GLY D CA  1 
ATOM   7523  C C   . GLY D 2 134 ? 13.386  44.444  7.462   1.00 61.40  ? 134 GLY D C   1 
ATOM   7524  O O   . GLY D 2 134 ? 13.238  43.437  6.773   1.00 60.64  ? 134 GLY D O   1 
ATOM   7525  N N   . ASN D 2 135 ? 14.573  44.994  7.689   1.00 55.18  ? 135 ASN D N   1 
ATOM   7526  C CA  . ASN D 2 135 ? 15.796  44.401  7.171   1.00 53.53  ? 135 ASN D CA  1 
ATOM   7527  C C   . ASN D 2 135 ? 16.609  43.788  8.304   1.00 51.94  ? 135 ASN D C   1 
ATOM   7528  O O   . ASN D 2 135 ? 17.764  43.391  8.120   1.00 51.45  ? 135 ASN D O   1 
ATOM   7529  C CB  . ASN D 2 135 ? 16.632  45.445  6.433   1.00 59.86  ? 135 ASN D CB  1 
ATOM   7530  C CG  . ASN D 2 135 ? 17.473  46.286  7.373   1.00 59.86  ? 135 ASN D CG  1 
ATOM   7531  O OD1 . ASN D 2 135 ? 17.056  46.593  8.492   1.00 56.79  ? 135 ASN D OD1 1 
ATOM   7532  N ND2 . ASN D 2 135 ? 18.672  46.657  6.924   1.00 61.25  ? 135 ASN D ND2 1 
ATOM   7533  N N   . GLY D 2 136 ? 15.993  43.713  9.480   1.00 72.87  ? 136 GLY D N   1 
ATOM   7534  C CA  . GLY D 2 136 ? 16.656  43.184  10.654  1.00 75.34  ? 136 GLY D CA  1 
ATOM   7535  C C   . GLY D 2 136 ? 17.267  44.288  11.490  1.00 79.53  ? 136 GLY D C   1 
ATOM   7536  O O   . GLY D 2 136 ? 18.241  44.067  12.211  1.00 85.32  ? 136 GLY D O   1 
ATOM   7537  N N   . CYS D 2 137 ? 16.695  45.484  11.380  1.00 65.30  ? 137 CYS D N   1 
ATOM   7538  C CA  . CYS D 2 137 ? 17.153  46.640  12.138  1.00 57.86  ? 137 CYS D CA  1 
ATOM   7539  C C   . CYS D 2 137 ? 15.973  47.451  12.643  1.00 61.91  ? 137 CYS D C   1 
ATOM   7540  O O   . CYS D 2 137 ? 14.873  47.389  12.085  1.00 68.64  ? 137 CYS D O   1 
ATOM   7541  C CB  . CYS D 2 137 ? 18.022  47.539  11.274  1.00 57.15  ? 137 CYS D CB  1 
ATOM   7542  S SG  . CYS D 2 137 ? 19.459  46.752  10.575  1.00 64.69  ? 137 CYS D SG  1 
ATOM   7543  N N   . PHE D 2 138 ? 16.216  48.213  13.704  1.00 71.04  ? 138 PHE D N   1 
ATOM   7544  C CA  . PHE D 2 138 ? 15.235  49.147  14.234  1.00 66.49  ? 138 PHE D CA  1 
ATOM   7545  C C   . PHE D 2 138 ? 15.826  50.554  14.204  1.00 67.54  ? 138 PHE D C   1 
ATOM   7546  O O   . PHE D 2 138 ? 16.971  50.761  14.605  1.00 75.49  ? 138 PHE D O   1 
ATOM   7547  C CB  . PHE D 2 138 ? 14.859  48.765  15.666  1.00 65.32  ? 138 PHE D CB  1 
ATOM   7548  C CG  . PHE D 2 138 ? 14.452  47.326  15.825  1.00 62.13  ? 138 PHE D CG  1 
ATOM   7549  C CD1 . PHE D 2 138 ? 13.133  46.941  15.654  1.00 62.36  ? 138 PHE D CD1 1 
ATOM   7550  C CD2 . PHE D 2 138 ? 15.388  46.359  16.149  1.00 58.67  ? 138 PHE D CD2 1 
ATOM   7551  C CE1 . PHE D 2 138 ? 12.756  45.614  15.801  1.00 62.11  ? 138 PHE D CE1 1 
ATOM   7552  C CE2 . PHE D 2 138 ? 15.020  45.033  16.298  1.00 56.99  ? 138 PHE D CE2 1 
ATOM   7553  C CZ  . PHE D 2 138 ? 13.703  44.661  16.126  1.00 60.30  ? 138 PHE D CZ  1 
ATOM   7554  N N   . GLU D 2 139 ? 15.059  51.519  13.712  1.00 69.21  ? 139 GLU D N   1 
ATOM   7555  C CA  . GLU D 2 139 ? 15.493  52.910  13.747  1.00 71.16  ? 139 GLU D CA  1 
ATOM   7556  C C   . GLU D 2 139 ? 14.839  53.587  14.943  1.00 71.44  ? 139 GLU D C   1 
ATOM   7557  O O   . GLU D 2 139 ? 13.624  53.528  15.112  1.00 70.35  ? 139 GLU D O   1 
ATOM   7558  C CB  . GLU D 2 139 ? 15.133  53.643  12.452  1.00 80.07  ? 139 GLU D CB  1 
ATOM   7559  C CG  . GLU D 2 139 ? 15.899  54.950  12.263  1.00 85.63  ? 139 GLU D CG  1 
ATOM   7560  C CD  . GLU D 2 139 ? 15.381  55.790  11.111  1.00 82.83  ? 139 GLU D CD  1 
ATOM   7561  O OE1 . GLU D 2 139 ? 14.343  55.427  10.519  1.00 83.36  ? 139 GLU D OE1 1 
ATOM   7562  O OE2 . GLU D 2 139 ? 16.013  56.823  10.803  1.00 81.90  ? 139 GLU D OE2 1 
ATOM   7563  N N   . PHE D 2 140 ? 15.652  54.218  15.779  1.00 72.53  ? 140 PHE D N   1 
ATOM   7564  C CA  . PHE D 2 140 ? 15.161  54.788  17.026  1.00 72.70  ? 140 PHE D CA  1 
ATOM   7565  C C   . PHE D 2 140 ? 14.399  56.099  16.842  1.00 77.37  ? 140 PHE D C   1 
ATOM   7566  O O   . PHE D 2 140 ? 14.851  57.008  16.140  1.00 78.47  ? 140 PHE D O   1 
ATOM   7567  C CB  . PHE D 2 140 ? 16.313  54.985  18.016  1.00 72.94  ? 140 PHE D CB  1 
ATOM   7568  C CG  . PHE D 2 140 ? 16.733  53.726  18.716  1.00 67.25  ? 140 PHE D CG  1 
ATOM   7569  C CD1 . PHE D 2 140 ? 16.093  53.318  19.873  1.00 62.93  ? 140 PHE D CD1 1 
ATOM   7570  C CD2 . PHE D 2 140 ? 17.769  52.951  18.220  1.00 68.55  ? 140 PHE D CD2 1 
ATOM   7571  C CE1 . PHE D 2 140 ? 16.475  52.161  20.523  1.00 64.87  ? 140 PHE D CE1 1 
ATOM   7572  C CE2 . PHE D 2 140 ? 18.157  51.792  18.867  1.00 70.48  ? 140 PHE D CE2 1 
ATOM   7573  C CZ  . PHE D 2 140 ? 17.509  51.396  20.020  1.00 67.07  ? 140 PHE D CZ  1 
ATOM   7574  N N   . TYR D 2 141 ? 13.236  56.176  17.481  1.00 72.46  ? 141 TYR D N   1 
ATOM   7575  C CA  . TYR D 2 141 ? 12.481  57.413  17.575  1.00 73.15  ? 141 TYR D CA  1 
ATOM   7576  C C   . TYR D 2 141 ? 12.909  58.160  18.825  1.00 76.38  ? 141 TYR D C   1 
ATOM   7577  O O   . TYR D 2 141 ? 12.120  58.883  19.431  1.00 83.57  ? 141 TYR D O   1 
ATOM   7578  C CB  . TYR D 2 141 ? 10.983  57.132  17.624  1.00 73.60  ? 141 TYR D CB  1 
ATOM   7579  C CG  . TYR D 2 141 ? 10.365  56.928  16.265  1.00 76.71  ? 141 TYR D CG  1 
ATOM   7580  C CD1 . TYR D 2 141 ? 10.969  57.445  15.127  1.00 83.22  ? 141 TYR D CD1 1 
ATOM   7581  C CD2 . TYR D 2 141 ? 9.176   56.223  16.117  1.00 75.63  ? 141 TYR D CD2 1 
ATOM   7582  C CE1 . TYR D 2 141 ? 10.409  57.267  13.881  1.00 90.37  ? 141 TYR D CE1 1 
ATOM   7583  C CE2 . TYR D 2 141 ? 8.608   56.036  14.874  1.00 79.65  ? 141 TYR D CE2 1 
ATOM   7584  C CZ  . TYR D 2 141 ? 9.228   56.559  13.759  1.00 90.01  ? 141 TYR D CZ  1 
ATOM   7585  O OH  . TYR D 2 141 ? 8.664   56.373  12.517  1.00 96.80  ? 141 TYR D OH  1 
ATOM   7586  N N   . HIS D 2 142 ? 14.163  57.961  19.211  1.00 63.61  ? 142 HIS D N   1 
ATOM   7587  C CA  . HIS D 2 142 ? 14.758  58.690  20.314  1.00 55.33  ? 142 HIS D CA  1 
ATOM   7588  C C   . HIS D 2 142 ? 16.245  58.396  20.357  1.00 59.02  ? 142 HIS D C   1 
ATOM   7589  O O   . HIS D 2 142 ? 16.722  57.500  19.671  1.00 65.34  ? 142 HIS D O   1 
ATOM   7590  C CB  . HIS D 2 142 ? 14.079  58.340  21.638  1.00 50.68  ? 142 HIS D CB  1 
ATOM   7591  C CG  . HIS D 2 142 ? 14.542  57.054  22.245  1.00 49.89  ? 142 HIS D CG  1 
ATOM   7592  N ND1 . HIS D 2 142 ? 15.836  56.858  22.678  1.00 51.82  ? 142 HIS D ND1 1 
ATOM   7593  C CD2 . HIS D 2 142 ? 13.877  55.905  22.516  1.00 51.98  ? 142 HIS D CD2 1 
ATOM   7594  C CE1 . HIS D 2 142 ? 15.952  55.640  23.178  1.00 51.39  ? 142 HIS D CE1 1 
ATOM   7595  N NE2 . HIS D 2 142 ? 14.777  55.041  23.093  1.00 46.15  ? 142 HIS D NE2 1 
ATOM   7596  N N   . LYS D 2 143 ? 16.984  59.163  21.147  1.00 63.59  ? 143 LYS D N   1 
ATOM   7597  C CA  . LYS D 2 143 ? 18.429  59.004  21.208  1.00 58.75  ? 143 LYS D CA  1 
ATOM   7598  C C   . LYS D 2 143 ? 18.832  57.897  22.176  1.00 63.66  ? 143 LYS D C   1 
ATOM   7599  O O   . LYS D 2 143 ? 18.318  57.807  23.291  1.00 71.36  ? 143 LYS D O   1 
ATOM   7600  C CB  . LYS D 2 143 ? 19.107  60.332  21.559  1.00 60.47  ? 143 LYS D CB  1 
ATOM   7601  C CG  . LYS D 2 143 ? 19.356  61.236  20.346  1.00 65.83  ? 143 LYS D CG  1 
ATOM   7602  C CD  . LYS D 2 143 ? 20.432  60.647  19.427  1.00 70.61  ? 143 LYS D CD  1 
ATOM   7603  C CE  . LYS D 2 143 ? 20.502  61.363  18.086  1.00 79.43  ? 143 LYS D CE  1 
ATOM   7604  N NZ  . LYS D 2 143 ? 19.312  61.086  17.226  1.00 82.99  ? 143 LYS D NZ  1 
ATOM   7605  N N   . CYS D 2 144 ? 19.758  57.053  21.741  1.00 59.44  ? 144 CYS D N   1 
ATOM   7606  C CA  . CYS D 2 144 ? 20.121  55.879  22.516  1.00 63.03  ? 144 CYS D CA  1 
ATOM   7607  C C   . CYS D 2 144 ? 21.624  55.795  22.695  1.00 66.15  ? 144 CYS D C   1 
ATOM   7608  O O   . CYS D 2 144 ? 22.325  55.266  21.831  1.00 72.67  ? 144 CYS D O   1 
ATOM   7609  C CB  . CYS D 2 144 ? 19.611  54.618  21.814  1.00 65.73  ? 144 CYS D CB  1 
ATOM   7610  S SG  . CYS D 2 144 ? 19.349  53.198  22.889  1.00 70.28  ? 144 CYS D SG  1 
ATOM   7611  N N   . ASP D 2 145 ? 22.118  56.317  23.815  1.00 54.38  ? 145 ASP D N   1 
ATOM   7612  C CA  . ASP D 2 145 ? 23.545  56.236  24.113  1.00 54.35  ? 145 ASP D CA  1 
ATOM   7613  C C   . ASP D 2 145 ? 23.986  54.775  24.294  1.00 54.58  ? 145 ASP D C   1 
ATOM   7614  O O   . ASP D 2 145 ? 23.298  53.852  23.856  1.00 56.34  ? 145 ASP D O   1 
ATOM   7615  C CB  . ASP D 2 145 ? 23.922  57.101  25.329  1.00 62.98  ? 145 ASP D CB  1 
ATOM   7616  C CG  . ASP D 2 145 ? 23.186  56.708  26.595  1.00 74.79  ? 145 ASP D CG  1 
ATOM   7617  O OD1 . ASP D 2 145 ? 23.302  57.439  27.600  1.00 78.37  ? 145 ASP D OD1 1 
ATOM   7618  O OD2 . ASP D 2 145 ? 22.493  55.675  26.596  1.00 80.22  ? 145 ASP D OD2 1 
ATOM   7619  N N   . ASP D 2 146 ? 25.132  54.568  24.933  1.00 53.16  ? 146 ASP D N   1 
ATOM   7620  C CA  . ASP D 2 146 ? 25.642  53.220  25.137  1.00 57.17  ? 146 ASP D CA  1 
ATOM   7621  C C   . ASP D 2 146 ? 24.981  52.537  26.332  1.00 62.19  ? 146 ASP D C   1 
ATOM   7622  O O   . ASP D 2 146 ? 24.530  51.398  26.222  1.00 64.11  ? 146 ASP D O   1 
ATOM   7623  C CB  . ASP D 2 146 ? 27.168  53.224  25.263  1.00 62.28  ? 146 ASP D CB  1 
ATOM   7624  C CG  . ASP D 2 146 ? 27.855  53.584  23.957  1.00 66.45  ? 146 ASP D CG  1 
ATOM   7625  O OD1 . ASP D 2 146 ? 27.161  54.069  23.038  1.00 64.35  ? 146 ASP D OD1 1 
ATOM   7626  O OD2 . ASP D 2 146 ? 29.084  53.385  23.848  1.00 72.52  ? 146 ASP D OD2 1 
ATOM   7627  N N   . GLU D 2 147 ? 24.900  53.223  27.468  1.00 96.39  ? 147 GLU D N   1 
ATOM   7628  C CA  . GLU D 2 147 ? 24.233  52.631  28.622  1.00 102.84 ? 147 GLU D CA  1 
ATOM   7629  C C   . GLU D 2 147 ? 22.796  52.289  28.238  1.00 107.13 ? 147 GLU D C   1 
ATOM   7630  O O   . GLU D 2 147 ? 22.123  51.523  28.926  1.00 111.07 ? 147 GLU D O   1 
ATOM   7631  C CB  . GLU D 2 147 ? 24.269  53.558  29.840  1.00 102.15 ? 147 GLU D CB  1 
ATOM   7632  C CG  . GLU D 2 147 ? 22.975  54.314  30.089  1.00 108.94 ? 147 GLU D CG  1 
ATOM   7633  C CD  . GLU D 2 147 ? 22.964  55.040  31.425  1.00 120.56 ? 147 GLU D CD  1 
ATOM   7634  O OE1 . GLU D 2 147 ? 22.501  56.203  31.472  1.00 120.60 ? 147 GLU D OE1 1 
ATOM   7635  O OE2 . GLU D 2 147 ? 23.414  54.443  32.429  1.00 124.95 ? 147 GLU D OE2 1 
ATOM   7636  N N   . CYS D 2 148 ? 22.344  52.857  27.123  1.00 89.28  ? 148 CYS D N   1 
ATOM   7637  C CA  . CYS D 2 148 ? 21.021  52.569  26.576  1.00 82.90  ? 148 CYS D CA  1 
ATOM   7638  C C   . CYS D 2 148 ? 21.055  51.330  25.691  1.00 77.56  ? 148 CYS D C   1 
ATOM   7639  O O   . CYS D 2 148 ? 20.294  50.391  25.908  1.00 80.62  ? 148 CYS D O   1 
ATOM   7640  C CB  . CYS D 2 148 ? 20.497  53.763  25.771  1.00 81.29  ? 148 CYS D CB  1 
ATOM   7641  S SG  . CYS D 2 148 ? 18.954  53.461  24.864  1.00 59.09  ? 148 CYS D SG  1 
ATOM   7642  N N   . MET D 2 149 ? 21.934  51.346  24.689  1.00 67.39  ? 149 MET D N   1 
ATOM   7643  C CA  . MET D 2 149 ? 22.110  50.211  23.786  1.00 60.79  ? 149 MET D CA  1 
ATOM   7644  C C   . MET D 2 149 ? 22.293  48.930  24.586  1.00 61.69  ? 149 MET D C   1 
ATOM   7645  O O   . MET D 2 149 ? 21.659  47.911  24.307  1.00 66.27  ? 149 MET D O   1 
ATOM   7646  C CB  . MET D 2 149 ? 23.310  50.425  22.863  1.00 57.58  ? 149 MET D CB  1 
ATOM   7647  C CG  . MET D 2 149 ? 23.068  51.436  21.759  1.00 58.88  ? 149 MET D CG  1 
ATOM   7648  S SD  . MET D 2 149 ? 21.697  50.946  20.703  1.00 57.40  ? 149 MET D SD  1 
ATOM   7649  C CE  . MET D 2 149 ? 21.333  52.464  19.836  1.00 39.63  ? 149 MET D CE  1 
ATOM   7650  N N   . ASN D 2 150 ? 23.157  48.985  25.591  1.00 51.48  ? 150 ASN D N   1 
ATOM   7651  C CA  . ASN D 2 150 ? 23.336  47.848  26.467  1.00 56.41  ? 150 ASN D CA  1 
ATOM   7652  C C   . ASN D 2 150 ? 22.004  47.345  27.004  1.00 59.45  ? 150 ASN D C   1 
ATOM   7653  O O   . ASN D 2 150 ? 21.700  46.166  26.887  1.00 58.70  ? 150 ASN D O   1 
ATOM   7654  C CB  . ASN D 2 150 ? 24.299  48.180  27.604  1.00 64.98  ? 150 ASN D CB  1 
ATOM   7655  C CG  . ASN D 2 150 ? 25.630  48.709  27.100  1.00 68.85  ? 150 ASN D CG  1 
ATOM   7656  O OD1 . ASN D 2 150 ? 26.203  49.634  27.681  1.00 72.78  ? 150 ASN D OD1 1 
ATOM   7657  N ND2 . ASN D 2 150 ? 26.120  48.138  26.000  1.00 66.83  ? 150 ASN D ND2 1 
ATOM   7658  N N   . SER D 2 151 ? 21.195  48.235  27.567  1.00 74.18  ? 151 SER D N   1 
ATOM   7659  C CA  . SER D 2 151 ? 19.911  47.823  28.133  1.00 75.05  ? 151 SER D CA  1 
ATOM   7660  C C   . SER D 2 151 ? 19.120  46.932  27.175  1.00 73.81  ? 151 SER D C   1 
ATOM   7661  O O   . SER D 2 151 ? 18.372  46.059  27.607  1.00 77.65  ? 151 SER D O   1 
ATOM   7662  C CB  . SER D 2 151 ? 19.068  49.032  28.552  1.00 77.69  ? 151 SER D CB  1 
ATOM   7663  O OG  . SER D 2 151 ? 18.284  49.518  27.476  1.00 75.40  ? 151 SER D OG  1 
ATOM   7664  N N   . VAL D 2 152 ? 19.291  47.148  25.876  1.00 84.16  ? 152 VAL D N   1 
ATOM   7665  C CA  . VAL D 2 152 ? 18.599  46.344  24.876  1.00 78.25  ? 152 VAL D CA  1 
ATOM   7666  C C   . VAL D 2 152 ? 19.204  44.952  24.776  1.00 76.69  ? 152 VAL D C   1 
ATOM   7667  O O   . VAL D 2 152 ? 18.503  43.942  24.889  1.00 86.92  ? 152 VAL D O   1 
ATOM   7668  C CB  . VAL D 2 152 ? 18.667  46.997  23.487  1.00 66.97  ? 152 VAL D CB  1 
ATOM   7669  C CG1 . VAL D 2 152 ? 18.337  45.981  22.404  1.00 59.44  ? 152 VAL D CG1 1 
ATOM   7670  C CG2 . VAL D 2 152 ? 17.730  48.199  23.411  1.00 60.81  ? 152 VAL D CG2 1 
ATOM   7671  N N   . LYS D 2 153 ? 20.514  44.912  24.554  1.00 76.75  ? 153 LYS D N   1 
ATOM   7672  C CA  . LYS D 2 153 ? 21.251  43.662  24.447  1.00 74.84  ? 153 LYS D CA  1 
ATOM   7673  C C   . LYS D 2 153 ? 21.100  42.824  25.710  1.00 79.28  ? 153 LYS D C   1 
ATOM   7674  O O   . LYS D 2 153 ? 21.001  41.596  25.646  1.00 72.00  ? 153 LYS D O   1 
ATOM   7675  C CB  . LYS D 2 153 ? 22.730  43.949  24.203  1.00 71.88  ? 153 LYS D CB  1 
ATOM   7676  C CG  . LYS D 2 153 ? 23.013  44.853  23.014  1.00 72.01  ? 153 LYS D CG  1 
ATOM   7677  C CD  . LYS D 2 153 ? 24.504  45.115  22.911  1.00 80.16  ? 153 LYS D CD  1 
ATOM   7678  C CE  . LYS D 2 153 ? 24.875  45.799  21.616  1.00 85.79  ? 153 LYS D CE  1 
ATOM   7679  N NZ  . LYS D 2 153 ? 26.353  45.952  21.518  1.00 90.34  ? 153 LYS D NZ  1 
ATOM   7680  N N   . ASN D 2 154 ? 21.088  43.498  26.857  1.00 68.51  ? 154 ASN D N   1 
ATOM   7681  C CA  . ASN D 2 154 ? 20.995  42.831  28.150  1.00 71.64  ? 154 ASN D CA  1 
ATOM   7682  C C   . ASN D 2 154 ? 19.555  42.481  28.556  1.00 66.34  ? 154 ASN D C   1 
ATOM   7683  O O   . ASN D 2 154 ? 19.328  41.739  29.515  1.00 65.06  ? 154 ASN D O   1 
ATOM   7684  C CB  . ASN D 2 154 ? 21.697  43.669  29.222  1.00 83.26  ? 154 ASN D CB  1 
ATOM   7685  C CG  . ASN D 2 154 ? 21.337  43.245  30.633  1.00 107.22 ? 154 ASN D CG  1 
ATOM   7686  O OD1 . ASN D 2 154 ? 20.404  43.784  31.232  1.00 112.02 ? 154 ASN D OD1 1 
ATOM   7687  N ND2 . ASN D 2 154 ? 22.081  42.287  31.177  1.00 125.83 ? 154 ASN D ND2 1 
ATOM   7688  N N   . GLY D 2 155 ? 18.587  43.008  27.814  1.00 56.29  ? 155 GLY D N   1 
ATOM   7689  C CA  . GLY D 2 155 ? 17.190  42.688  28.048  1.00 54.89  ? 155 GLY D CA  1 
ATOM   7690  C C   . GLY D 2 155 ? 16.493  43.583  29.059  1.00 58.61  ? 155 GLY D C   1 
ATOM   7691  O O   . GLY D 2 155 ? 15.450  43.222  29.604  1.00 62.97  ? 155 GLY D O   1 
ATOM   7692  N N   . THR D 2 156 ? 17.060  44.758  29.307  1.00 65.47  ? 156 THR D N   1 
ATOM   7693  C CA  . THR D 2 156 ? 16.497  45.676  30.292  1.00 74.31  ? 156 THR D CA  1 
ATOM   7694  C C   . THR D 2 156 ? 16.241  47.066  29.724  1.00 76.35  ? 156 THR D C   1 
ATOM   7695  O O   . THR D 2 156 ? 16.687  48.061  30.289  1.00 85.37  ? 156 THR D O   1 
ATOM   7696  C CB  . THR D 2 156 ? 17.406  45.798  31.525  1.00 78.81  ? 156 THR D CB  1 
ATOM   7697  O OG1 . THR D 2 156 ? 18.738  46.139  31.110  1.00 81.37  ? 156 THR D OG1 1 
ATOM   7698  C CG2 . THR D 2 156 ? 17.430  44.474  32.288  1.00 65.43  ? 156 THR D CG2 1 
ATOM   7699  N N   . TYR D 2 157 ? 15.518  47.126  28.609  1.00 65.07  ? 157 TYR D N   1 
ATOM   7700  C CA  . TYR D 2 157 ? 15.184  48.393  27.967  1.00 56.72  ? 157 TYR D CA  1 
ATOM   7701  C C   . TYR D 2 157 ? 14.016  49.054  28.691  1.00 65.25  ? 157 TYR D C   1 
ATOM   7702  O O   . TYR D 2 157 ? 13.022  48.391  29.007  1.00 66.49  ? 157 TYR D O   1 
ATOM   7703  C CB  . TYR D 2 157 ? 14.837  48.172  26.491  1.00 50.00  ? 157 TYR D CB  1 
ATOM   7704  C CG  . TYR D 2 157 ? 14.482  49.439  25.735  1.00 51.82  ? 157 TYR D CG  1 
ATOM   7705  C CD1 . TYR D 2 157 ? 15.467  50.278  25.235  1.00 46.15  ? 157 TYR D CD1 1 
ATOM   7706  C CD2 . TYR D 2 157 ? 13.156  49.791  25.517  1.00 65.05  ? 157 TYR D CD2 1 
ATOM   7707  C CE1 . TYR D 2 157 ? 15.141  51.426  24.540  1.00 48.88  ? 157 TYR D CE1 1 
ATOM   7708  C CE2 . TYR D 2 157 ? 12.824  50.940  24.830  1.00 66.92  ? 157 TYR D CE2 1 
ATOM   7709  C CZ  . TYR D 2 157 ? 13.818  51.753  24.341  1.00 55.14  ? 157 TYR D CZ  1 
ATOM   7710  O OH  . TYR D 2 157 ? 13.484  52.900  23.651  1.00 54.52  ? 157 TYR D OH  1 
ATOM   7711  N N   . ASP D 2 158 ? 14.137  50.361  28.943  1.00 73.44  ? 158 ASP D N   1 
ATOM   7712  C CA  . ASP D 2 158 ? 13.134  51.091  29.722  1.00 75.22  ? 158 ASP D CA  1 
ATOM   7713  C C   . ASP D 2 158 ? 12.190  51.914  28.851  1.00 74.94  ? 158 ASP D C   1 
ATOM   7714  O O   . ASP D 2 158 ? 12.179  53.139  28.916  1.00 78.65  ? 158 ASP D O   1 
ATOM   7715  C CB  . ASP D 2 158 ? 13.808  51.981  30.768  1.00 73.91  ? 158 ASP D CB  1 
ATOM   7716  C CG  . ASP D 2 158 ? 12.824  52.538  31.779  1.00 81.07  ? 158 ASP D CG  1 
ATOM   7717  O OD1 . ASP D 2 158 ? 11.696  52.008  31.870  1.00 79.71  ? 158 ASP D OD1 1 
ATOM   7718  O OD2 . ASP D 2 158 ? 13.179  53.500  32.489  1.00 86.22  ? 158 ASP D OD2 1 
ATOM   7719  N N   . TYR D 2 159 ? 11.396  51.225  28.041  1.00 57.20  ? 159 TYR D N   1 
ATOM   7720  C CA  . TYR D 2 159 ? 10.415  51.861  27.172  1.00 53.26  ? 159 TYR D CA  1 
ATOM   7721  C C   . TYR D 2 159 ? 9.702   53.000  27.868  1.00 54.52  ? 159 TYR D C   1 
ATOM   7722  O O   . TYR D 2 159 ? 9.658   54.115  27.353  1.00 63.21  ? 159 TYR D O   1 
ATOM   7723  C CB  . TYR D 2 159 ? 9.403   50.825  26.701  1.00 56.08  ? 159 TYR D CB  1 
ATOM   7724  C CG  . TYR D 2 159 ? 8.170   51.365  26.005  1.00 62.84  ? 159 TYR D CG  1 
ATOM   7725  C CD1 . TYR D 2 159 ? 8.215   51.778  24.677  1.00 66.00  ? 159 TYR D CD1 1 
ATOM   7726  C CD2 . TYR D 2 159 ? 6.950   51.416  26.662  1.00 67.44  ? 159 TYR D CD2 1 
ATOM   7727  C CE1 . TYR D 2 159 ? 7.080   52.239  24.036  1.00 65.68  ? 159 TYR D CE1 1 
ATOM   7728  C CE2 . TYR D 2 159 ? 5.816   51.881  26.031  1.00 73.26  ? 159 TYR D CE2 1 
ATOM   7729  C CZ  . TYR D 2 159 ? 5.886   52.286  24.722  1.00 68.31  ? 159 TYR D CZ  1 
ATOM   7730  O OH  . TYR D 2 159 ? 4.750   52.737  24.106  1.00 64.75  ? 159 TYR D OH  1 
ATOM   7731  N N   . PRO D 2 160 ? 9.147   52.732  29.053  1.00 55.66  ? 160 PRO D N   1 
ATOM   7732  C CA  . PRO D 2 160 ? 8.408   53.800  29.735  1.00 58.45  ? 160 PRO D CA  1 
ATOM   7733  C C   . PRO D 2 160 ? 9.202   55.101  29.751  1.00 60.14  ? 160 PRO D C   1 
ATOM   7734  O O   . PRO D 2 160 ? 8.643   56.168  29.514  1.00 65.49  ? 160 PRO D O   1 
ATOM   7735  C CB  . PRO D 2 160 ? 8.251   53.254  31.155  1.00 61.49  ? 160 PRO D CB  1 
ATOM   7736  C CG  . PRO D 2 160 ? 8.267   51.773  30.980  1.00 59.12  ? 160 PRO D CG  1 
ATOM   7737  C CD  . PRO D 2 160 ? 9.222   51.503  29.861  1.00 56.53  ? 160 PRO D CD  1 
ATOM   7738  N N   . LYS D 2 161 ? 10.497  54.992  30.018  1.00 64.18  ? 161 LYS D N   1 
ATOM   7739  C CA  . LYS D 2 161 ? 11.391  56.143  30.073  1.00 69.16  ? 161 LYS D CA  1 
ATOM   7740  C C   . LYS D 2 161 ? 11.364  56.976  28.798  1.00 67.75  ? 161 LYS D C   1 
ATOM   7741  O O   . LYS D 2 161 ? 11.103  58.181  28.839  1.00 71.88  ? 161 LYS D O   1 
ATOM   7742  C CB  . LYS D 2 161 ? 12.818  55.675  30.357  1.00 65.66  ? 161 LYS D CB  1 
ATOM   7743  C CG  . LYS D 2 161 ? 13.885  56.707  30.095  1.00 50.09  ? 161 LYS D CG  1 
ATOM   7744  C CD  . LYS D 2 161 ? 15.163  56.345  30.839  1.00 47.32  ? 161 LYS D CD  1 
ATOM   7745  C CE  . LYS D 2 161 ? 14.920  56.240  32.342  1.00 56.12  ? 161 LYS D CE  1 
ATOM   7746  N NZ  . LYS D 2 161 ? 14.233  57.443  32.899  1.00 63.74  ? 161 LYS D NZ  1 
ATOM   7747  N N   . TYR D 2 162 ? 11.635  56.328  27.671  1.00 54.63  ? 162 TYR D N   1 
ATOM   7748  C CA  . TYR D 2 162 ? 11.702  57.007  26.383  1.00 51.60  ? 162 TYR D CA  1 
ATOM   7749  C C   . TYR D 2 162 ? 10.365  56.962  25.652  1.00 52.20  ? 162 TYR D C   1 
ATOM   7750  O O   . TYR D 2 162 ? 10.298  57.227  24.455  1.00 53.88  ? 162 TYR D O   1 
ATOM   7751  C CB  . TYR D 2 162 ? 12.777  56.372  25.503  1.00 48.43  ? 162 TYR D CB  1 
ATOM   7752  C CG  . TYR D 2 162 ? 14.073  56.079  26.220  1.00 53.54  ? 162 TYR D CG  1 
ATOM   7753  C CD1 . TYR D 2 162 ? 15.180  56.898  26.062  1.00 54.87  ? 162 TYR D CD1 1 
ATOM   7754  C CD2 . TYR D 2 162 ? 14.192  54.975  27.052  1.00 61.28  ? 162 TYR D CD2 1 
ATOM   7755  C CE1 . TYR D 2 162 ? 16.369  56.632  26.718  1.00 59.64  ? 162 TYR D CE1 1 
ATOM   7756  C CE2 . TYR D 2 162 ? 15.375  54.701  27.712  1.00 66.74  ? 162 TYR D CE2 1 
ATOM   7757  C CZ  . TYR D 2 162 ? 16.460  55.531  27.541  1.00 67.59  ? 162 TYR D CZ  1 
ATOM   7758  O OH  . TYR D 2 162 ? 17.639  55.262  28.195  1.00 74.28  ? 162 TYR D OH  1 
ATOM   7759  N N   . GLU D 2 163 ? 9.300   56.617  26.364  1.00 58.48  ? 163 GLU D N   1 
ATOM   7760  C CA  . GLU D 2 163 ? 8.002   56.507  25.718  1.00 55.45  ? 163 GLU D CA  1 
ATOM   7761  C C   . GLU D 2 163 ? 7.564   57.850  25.177  1.00 63.13  ? 163 GLU D C   1 
ATOM   7762  O O   . GLU D 2 163 ? 7.273   57.986  23.991  1.00 60.32  ? 163 GLU D O   1 
ATOM   7763  C CB  . GLU D 2 163 ? 6.940   55.969  26.677  1.00 56.43  ? 163 GLU D CB  1 
ATOM   7764  C CG  . GLU D 2 163 ? 5.562   55.857  26.038  1.00 55.70  ? 163 GLU D CG  1 
ATOM   7765  C CD  . GLU D 2 163 ? 4.490   55.406  27.014  1.00 64.24  ? 163 GLU D CD  1 
ATOM   7766  O OE1 . GLU D 2 163 ? 3.454   54.875  26.555  1.00 66.39  ? 163 GLU D OE1 1 
ATOM   7767  O OE2 . GLU D 2 163 ? 4.679   55.588  28.238  1.00 73.42  ? 163 GLU D OE2 1 
ATOM   7768  N N   . GLU D 2 164 ? 7.533   58.845  26.057  1.00 80.19  ? 164 GLU D N   1 
ATOM   7769  C CA  . GLU D 2 164 ? 6.991   60.156  25.711  1.00 88.92  ? 164 GLU D CA  1 
ATOM   7770  C C   . GLU D 2 164 ? 7.848   60.913  24.696  1.00 85.25  ? 164 GLU D C   1 
ATOM   7771  O O   . GLU D 2 164 ? 7.319   61.479  23.737  1.00 84.17  ? 164 GLU D O   1 
ATOM   7772  C CB  . GLU D 2 164 ? 6.759   60.997  26.970  1.00 94.70  ? 164 GLU D CB  1 
ATOM   7773  C CG  . GLU D 2 164 ? 5.608   60.512  27.842  1.00 102.20 ? 164 GLU D CG  1 
ATOM   7774  C CD  . GLU D 2 164 ? 4.254   60.646  27.163  1.00 108.86 ? 164 GLU D CD  1 
ATOM   7775  O OE1 . GLU D 2 164 ? 4.130   61.468  26.229  1.00 109.06 ? 164 GLU D OE1 1 
ATOM   7776  O OE2 . GLU D 2 164 ? 3.312   59.926  27.563  1.00 111.20 ? 164 GLU D OE2 1 
ATOM   7777  N N   . GLU D 2 165 ? 9.163   60.920  24.902  1.00 84.74  ? 165 GLU D N   1 
ATOM   7778  C CA  . GLU D 2 165 ? 10.060  61.614  23.985  1.00 79.80  ? 165 GLU D CA  1 
ATOM   7779  C C   . GLU D 2 165 ? 9.874   61.097  22.574  1.00 76.69  ? 165 GLU D C   1 
ATOM   7780  O O   . GLU D 2 165 ? 10.083  61.822  21.603  1.00 77.19  ? 165 GLU D O   1 
ATOM   7781  C CB  . GLU D 2 165 ? 11.519  61.424  24.390  1.00 78.45  ? 165 GLU D CB  1 
ATOM   7782  C CG  . GLU D 2 165 ? 12.498  61.972  23.361  1.00 80.21  ? 165 GLU D CG  1 
ATOM   7783  C CD  . GLU D 2 165 ? 13.928  61.510  23.591  1.00 85.97  ? 165 GLU D CD  1 
ATOM   7784  O OE1 . GLU D 2 165 ? 14.243  61.037  24.710  1.00 83.05  ? 165 GLU D OE1 1 
ATOM   7785  O OE2 . GLU D 2 165 ? 14.736  61.619  22.642  1.00 89.80  ? 165 GLU D OE2 1 
ATOM   7786  N N   . SER D 2 166 ? 9.474   59.836  22.471  1.00 75.44  ? 166 SER D N   1 
ATOM   7787  C CA  . SER D 2 166 ? 9.394   59.159  21.188  1.00 73.72  ? 166 SER D CA  1 
ATOM   7788  C C   . SER D 2 166 ? 8.083   59.433  20.458  1.00 83.38  ? 166 SER D C   1 
ATOM   7789  O O   . SER D 2 166 ? 8.100   59.792  19.282  1.00 91.46  ? 166 SER D O   1 
ATOM   7790  C CB  . SER D 2 166 ? 9.611   57.651  21.363  1.00 71.53  ? 166 SER D CB  1 
ATOM   7791  O OG  . SER D 2 166 ? 10.935  57.370  21.793  1.00 68.90  ? 166 SER D OG  1 
ATOM   7792  N N   . LYS D 2 167 ? 6.953   59.267  21.145  1.00 81.88  ? 167 LYS D N   1 
ATOM   7793  C CA  . LYS D 2 167 ? 5.657   59.487  20.503  1.00 79.36  ? 167 LYS D CA  1 
ATOM   7794  C C   . LYS D 2 167 ? 5.617   60.904  19.956  1.00 78.55  ? 167 LYS D C   1 
ATOM   7795  O O   . LYS D 2 167 ? 4.893   61.204  19.005  1.00 79.50  ? 167 LYS D O   1 
ATOM   7796  C CB  . LYS D 2 167 ? 4.486   59.242  21.462  1.00 82.28  ? 167 LYS D CB  1 
ATOM   7797  C CG  . LYS D 2 167 ? 4.152   60.414  22.367  1.00 94.89  ? 167 LYS D CG  1 
ATOM   7798  C CD  . LYS D 2 167 ? 2.682   60.396  22.783  1.00 104.94 ? 167 LYS D CD  1 
ATOM   7799  C CE  . LYS D 2 167 ? 2.304   59.099  23.491  1.00 105.67 ? 167 LYS D CE  1 
ATOM   7800  N NZ  . LYS D 2 167 ? 0.870   59.077  23.897  1.00 111.48 ? 167 LYS D NZ  1 
ATOM   7801  N N   . LEU D 2 168 ? 6.417   61.769  20.570  1.00 87.63  ? 168 LEU D N   1 
ATOM   7802  C CA  . LEU D 2 168 ? 6.609   63.125  20.090  1.00 87.46  ? 168 LEU D CA  1 
ATOM   7803  C C   . LEU D 2 168 ? 7.221   63.056  18.696  1.00 90.35  ? 168 LEU D C   1 
ATOM   7804  O O   . LEU D 2 168 ? 6.542   63.296  17.696  1.00 93.84  ? 168 LEU D O   1 
ATOM   7805  C CB  . LEU D 2 168 ? 7.527   63.884  21.050  1.00 83.32  ? 168 LEU D CB  1 
ATOM   7806  C CG  . LEU D 2 168 ? 7.506   65.415  21.076  1.00 91.74  ? 168 LEU D CG  1 
ATOM   7807  C CD1 . LEU D 2 168 ? 8.216   65.921  22.321  1.00 92.19  ? 168 LEU D CD1 1 
ATOM   7808  C CD2 . LEU D 2 168 ? 8.138   66.013  19.819  1.00 94.23  ? 168 LEU D CD2 1 
ATOM   7809  N N   . ASN D 2 169 ? 8.502   62.706  18.635  1.00 86.51  ? 169 ASN D N   1 
ATOM   7810  C CA  . ASN D 2 169 ? 9.204   62.572  17.362  1.00 83.12  ? 169 ASN D CA  1 
ATOM   7811  C C   . ASN D 2 169 ? 8.425   61.753  16.341  1.00 81.93  ? 169 ASN D C   1 
ATOM   7812  O O   . ASN D 2 169 ? 8.476   62.024  15.142  1.00 82.16  ? 169 ASN D O   1 
ATOM   7813  C CB  . ASN D 2 169 ? 10.580  61.945  17.579  1.00 77.90  ? 169 ASN D CB  1 
ATOM   7814  C CG  . ASN D 2 169 ? 11.562  62.905  18.213  1.00 88.94  ? 169 ASN D CG  1 
ATOM   7815  O OD1 . ASN D 2 169 ? 11.690  64.051  17.783  1.00 94.07  ? 169 ASN D OD1 1 
ATOM   7816  N ND2 . ASN D 2 169 ? 12.260  62.446  19.245  1.00 94.33  ? 169 ASN D ND2 1 
ATOM   7817  N N   . ARG D 2 170 ? 7.697   60.758  16.832  1.00 74.78  ? 170 ARG D N   1 
ATOM   7818  C CA  . ARG D 2 170 ? 7.001   59.804  15.980  1.00 74.96  ? 170 ARG D CA  1 
ATOM   7819  C C   . ARG D 2 170 ? 5.870   60.444  15.173  1.00 83.67  ? 170 ARG D C   1 
ATOM   7820  O O   . ARG D 2 170 ? 5.600   60.038  14.043  1.00 87.02  ? 170 ARG D O   1 
ATOM   7821  C CB  . ARG D 2 170 ? 6.469   58.644  16.834  1.00 68.73  ? 170 ARG D CB  1 
ATOM   7822  C CG  . ARG D 2 170 ? 5.999   57.422  16.048  1.00 62.84  ? 170 ARG D CG  1 
ATOM   7823  C CD  . ARG D 2 170 ? 5.772   56.223  16.957  1.00 61.61  ? 170 ARG D CD  1 
ATOM   7824  N NE  . ARG D 2 170 ? 4.565   56.340  17.773  1.00 67.75  ? 170 ARG D NE  1 
ATOM   7825  C CZ  . ARG D 2 170 ? 4.548   56.305  19.105  1.00 69.55  ? 170 ARG D CZ  1 
ATOM   7826  N NH1 . ARG D 2 170 ? 5.679   56.158  19.787  1.00 69.06  ? 170 ARG D NH1 1 
ATOM   7827  N NH2 . ARG D 2 170 ? 3.397   56.409  19.762  1.00 68.49  ? 170 ARG D NH2 1 
ATOM   7828  N N   . ASN D 2 171 ? 5.219   61.452  15.744  1.00 102.54 ? 171 ASN D N   1 
ATOM   7829  C CA  . ASN D 2 171 ? 4.071   62.069  15.082  1.00 111.32 ? 171 ASN D CA  1 
ATOM   7830  C C   . ASN D 2 171 ? 4.419   63.251  14.171  1.00 119.95 ? 171 ASN D C   1 
ATOM   7831  O O   . ASN D 2 171 ? 4.576   63.081  12.961  1.00 118.84 ? 171 ASN D O   1 
ATOM   7832  C CB  . ASN D 2 171 ? 2.994   62.445  16.102  1.00 104.11 ? 171 ASN D CB  1 
ATOM   7833  C CG  . ASN D 2 171 ? 2.409   61.228  16.799  1.00 90.74  ? 171 ASN D CG  1 
ATOM   7834  O OD1 . ASN D 2 171 ? 2.495   60.109  16.291  1.00 79.32  ? 171 ASN D OD1 1 
ATOM   7835  N ND2 . ASN D 2 171 ? 1.810   61.440  17.966  1.00 88.96  ? 171 ASN D ND2 1 
ATOM   7836  N N   . GLU D 2 172 ? 4.533   64.443  14.748  1.00 131.30 ? 172 GLU D N   1 
ATOM   7837  C CA  . GLU D 2 172 ? 4.885   65.632  13.977  1.00 137.09 ? 172 GLU D CA  1 
ATOM   7838  C C   . GLU D 2 172 ? 3.805   65.988  12.955  1.00 147.97 ? 172 GLU D C   1 
ATOM   7839  O O   . GLU D 2 172 ? 3.999   66.859  12.104  1.00 151.29 ? 172 GLU D O   1 
ATOM   7840  C CB  . GLU D 2 172 ? 6.230   65.434  13.271  1.00 133.31 ? 172 GLU D CB  1 
ATOM   7841  C CG  . GLU D 2 172 ? 7.337   64.905  14.171  1.00 131.14 ? 172 GLU D CG  1 
ATOM   7842  C CD  . GLU D 2 172 ? 7.703   65.865  15.293  1.00 128.64 ? 172 GLU D CD  1 
ATOM   7843  O OE1 . GLU D 2 172 ? 8.856   65.802  15.772  1.00 123.94 ? 172 GLU D OE1 1 
ATOM   7844  O OE2 . GLU D 2 172 ? 6.844   66.680  15.701  1.00 127.82 ? 172 GLU D OE2 1 
ATOM   7845  N N   . PRO E 1 1   ? -12.993 52.915  -1.052  1.00 173.56 ? 9   PRO E N   1 
ATOM   7846  C CA  . PRO E 1 1   ? -12.932 51.469  -1.292  1.00 171.88 ? 9   PRO E CA  1 
ATOM   7847  C C   . PRO E 1 1   ? -11.750 50.830  -0.571  1.00 160.47 ? 9   PRO E C   1 
ATOM   7848  O O   . PRO E 1 1   ? -11.934 50.166  0.450   1.00 160.41 ? 9   PRO E O   1 
ATOM   7849  C CB  . PRO E 1 1   ? -12.737 51.378  -2.807  1.00 175.63 ? 9   PRO E CB  1 
ATOM   7850  C CG  . PRO E 1 1   ? -13.365 52.620  -3.335  1.00 182.99 ? 9   PRO E CG  1 
ATOM   7851  C CD  . PRO E 1 1   ? -13.090 53.680  -2.307  1.00 179.82 ? 9   PRO E CD  1 
ATOM   7852  N N   . GLY E 1 2   ? -10.549 51.035  -1.100  1.00 144.14 ? 10  GLY E N   1 
ATOM   7853  C CA  . GLY E 1 2   ? -9.350  50.474  -0.507  1.00 125.07 ? 10  GLY E CA  1 
ATOM   7854  C C   . GLY E 1 2   ? -8.899  49.203  -1.201  1.00 117.50 ? 10  GLY E C   1 
ATOM   7855  O O   . GLY E 1 2   ? -9.396  48.113  -0.912  1.00 110.92 ? 10  GLY E O   1 
ATOM   7856  N N   . ASP E 1 3   ? -7.955  49.343  -2.125  1.00 122.27 ? 11  ASP E N   1 
ATOM   7857  C CA  . ASP E 1 3   ? -7.395  48.195  -2.824  1.00 120.44 ? 11  ASP E CA  1 
ATOM   7858  C C   . ASP E 1 3   ? -6.803  47.197  -1.829  1.00 110.69 ? 11  ASP E C   1 
ATOM   7859  O O   . ASP E 1 3   ? -6.179  47.588  -0.840  1.00 102.91 ? 11  ASP E O   1 
ATOM   7860  C CB  . ASP E 1 3   ? -6.324  48.647  -3.819  1.00 124.77 ? 11  ASP E CB  1 
ATOM   7861  C CG  . ASP E 1 3   ? -6.844  49.670  -4.808  1.00 138.33 ? 11  ASP E CG  1 
ATOM   7862  O OD1 . ASP E 1 3   ? -8.078  49.836  -4.905  1.00 145.94 ? 11  ASP E OD1 1 
ATOM   7863  O OD2 . ASP E 1 3   ? -6.017  50.302  -5.496  1.00 139.77 ? 11  ASP E OD2 1 
ATOM   7864  N N   . GLN E 1 4   ? -7.003  45.908  -2.092  1.00 114.74 ? 12  GLN E N   1 
ATOM   7865  C CA  . GLN E 1 4   ? -6.485  44.864  -1.213  1.00 102.70 ? 12  GLN E CA  1 
ATOM   7866  C C   . GLN E 1 4   ? -5.455  43.978  -1.905  1.00 99.33  ? 12  GLN E C   1 
ATOM   7867  O O   . GLN E 1 4   ? -5.283  44.034  -3.125  1.00 107.54 ? 12  GLN E O   1 
ATOM   7868  C CB  . GLN E 1 4   ? -7.623  43.994  -0.675  1.00 101.73 ? 12  GLN E CB  1 
ATOM   7869  C CG  . GLN E 1 4   ? -8.522  44.682  0.335   1.00 100.75 ? 12  GLN E CG  1 
ATOM   7870  C CD  . GLN E 1 4   ? -9.533  43.730  0.945   1.00 101.46 ? 12  GLN E CD  1 
ATOM   7871  O OE1 . GLN E 1 4   ? -9.618  42.566  0.556   1.00 103.22 ? 12  GLN E OE1 1 
ATOM   7872  N NE2 . GLN E 1 4   ? -10.303 44.219  1.909   1.00 100.65 ? 12  GLN E NE2 1 
ATOM   7873  N N   . ILE E 1 5   ? -4.766  43.167  -1.108  1.00 125.54 ? 13  ILE E N   1 
ATOM   7874  C CA  . ILE E 1 5   ? -3.877  42.132  -1.628  1.00 125.26 ? 13  ILE E CA  1 
ATOM   7875  C C   . ILE E 1 5   ? -3.836  40.944  -0.668  1.00 118.82 ? 13  ILE E C   1 
ATOM   7876  O O   . ILE E 1 5   ? -3.213  41.000  0.390   1.00 117.13 ? 13  ILE E O   1 
ATOM   7877  C CB  . ILE E 1 5   ? -2.451  42.656  -1.896  1.00 124.69 ? 13  ILE E CB  1 
ATOM   7878  C CG1 . ILE E 1 5   ? -1.605  41.571  -2.563  1.00 124.17 ? 13  ILE E CG1 1 
ATOM   7879  C CG2 . ILE E 1 5   ? -1.795  43.141  -0.610  1.00 118.17 ? 13  ILE E CG2 1 
ATOM   7880  C CD1 . ILE E 1 5   ? -0.194  42.008  -2.861  1.00 120.19 ? 13  ILE E CD1 1 
ATOM   7881  N N   . CYS E 1 6   ? -4.523  39.872  -1.037  1.00 103.76 ? 14  CYS E N   1 
ATOM   7882  C CA  . CYS E 1 6   ? -4.620  38.709  -0.175  1.00 103.97 ? 14  CYS E CA  1 
ATOM   7883  C C   . CYS E 1 6   ? -3.553  37.677  -0.545  1.00 104.63 ? 14  CYS E C   1 
ATOM   7884  O O   . CYS E 1 6   ? -3.157  37.572  -1.709  1.00 109.72 ? 14  CYS E O   1 
ATOM   7885  C CB  . CYS E 1 6   ? -6.019  38.101  -0.282  1.00 108.80 ? 14  CYS E CB  1 
ATOM   7886  S SG  . CYS E 1 6   ? -7.357  39.320  -0.279  1.00 273.93 ? 14  CYS E SG  1 
ATOM   7887  N N   . ILE E 1 7   ? -3.083  36.927  0.449   1.00 112.92 ? 15  ILE E N   1 
ATOM   7888  C CA  . ILE E 1 7   ? -2.116  35.855  0.211   1.00 109.90 ? 15  ILE E CA  1 
ATOM   7889  C C   . ILE E 1 7   ? -2.690  34.499  0.616   1.00 110.60 ? 15  ILE E C   1 
ATOM   7890  O O   . ILE E 1 7   ? -3.377  34.377  1.630   1.00 113.67 ? 15  ILE E O   1 
ATOM   7891  C CB  . ILE E 1 7   ? -0.780  36.093  0.948   1.00 96.95  ? 15  ILE E CB  1 
ATOM   7892  C CG1 . ILE E 1 7   ? -0.255  37.505  0.663   1.00 93.83  ? 15  ILE E CG1 1 
ATOM   7893  C CG2 . ILE E 1 7   ? 0.244   35.029  0.552   1.00 90.41  ? 15  ILE E CG2 1 
ATOM   7894  C CD1 . ILE E 1 7   ? -0.040  37.794  -0.808  1.00 95.34  ? 15  ILE E CD1 1 
ATOM   7895  N N   . GLY E 1 8   ? -2.406  33.484  -0.192  1.00 70.90  ? 16  GLY E N   1 
ATOM   7896  C CA  . GLY E 1 8   ? -2.952  32.157  0.025   1.00 74.01  ? 16  GLY E CA  1 
ATOM   7897  C C   . GLY E 1 8   ? -2.194  31.079  -0.726  1.00 78.76  ? 16  GLY E C   1 
ATOM   7898  O O   . GLY E 1 8   ? -1.220  31.355  -1.439  1.00 79.11  ? 16  GLY E O   1 
ATOM   7899  N N   . TYR E 1 9   ? -2.649  29.841  -0.575  1.00 87.12  ? 17  TYR E N   1 
ATOM   7900  C CA  . TYR E 1 9   ? -1.926  28.700  -1.125  1.00 83.27  ? 17  TYR E CA  1 
ATOM   7901  C C   . TYR E 1 9   ? -2.762  27.846  -2.066  1.00 89.85  ? 17  TYR E C   1 
ATOM   7902  O O   . TYR E 1 9   ? -3.992  27.821  -1.985  1.00 89.03  ? 17  TYR E O   1 
ATOM   7903  C CB  . TYR E 1 9   ? -1.377  27.839  0.006   1.00 72.79  ? 17  TYR E CB  1 
ATOM   7904  C CG  . TYR E 1 9   ? -2.359  27.650  1.140   1.00 73.95  ? 17  TYR E CG  1 
ATOM   7905  C CD1 . TYR E 1 9   ? -3.287  26.617  1.119   1.00 82.44  ? 17  TYR E CD1 1 
ATOM   7906  C CD2 . TYR E 1 9   ? -2.356  28.505  2.231   1.00 74.74  ? 17  TYR E CD2 1 
ATOM   7907  C CE1 . TYR E 1 9   ? -4.181  26.443  2.154   1.00 85.27  ? 17  TYR E CE1 1 
ATOM   7908  C CE2 . TYR E 1 9   ? -3.247  28.338  3.267   1.00 78.17  ? 17  TYR E CE2 1 
ATOM   7909  C CZ  . TYR E 1 9   ? -4.155  27.308  3.225   1.00 81.97  ? 17  TYR E CZ  1 
ATOM   7910  O OH  . TYR E 1 9   ? -5.040  27.145  4.262   1.00 85.16  ? 17  TYR E OH  1 
ATOM   7911  N N   . HIS E 1 10  ? -2.064  27.144  -2.951  1.00 90.17  ? 18  HIS E N   1 
ATOM   7912  C CA  . HIS E 1 10  ? -2.672  26.270  -3.947  1.00 99.95  ? 18  HIS E CA  1 
ATOM   7913  C C   . HIS E 1 10  ? -3.644  25.263  -3.332  1.00 96.03  ? 18  HIS E C   1 
ATOM   7914  O O   . HIS E 1 10  ? -3.456  24.797  -2.207  1.00 87.37  ? 18  HIS E O   1 
ATOM   7915  C CB  . HIS E 1 10  ? -1.572  25.524  -4.708  1.00 109.28 ? 18  HIS E CB  1 
ATOM   7916  C CG  . HIS E 1 10  ? -1.984  25.055  -6.068  1.00 127.57 ? 18  HIS E CG  1 
ATOM   7917  N ND1 . HIS E 1 10  ? -2.468  23.786  -6.303  1.00 135.36 ? 18  HIS E ND1 1 
ATOM   7918  C CD2 . HIS E 1 10  ? -1.977  25.684  -7.267  1.00 137.89 ? 18  HIS E CD2 1 
ATOM   7919  C CE1 . HIS E 1 10  ? -2.746  23.655  -7.588  1.00 144.28 ? 18  HIS E CE1 1 
ATOM   7920  N NE2 . HIS E 1 10  ? -2.455  24.792  -8.195  1.00 146.89 ? 18  HIS E NE2 1 
ATOM   7921  N N   . ALA E 1 11  ? -4.688  24.933  -4.082  1.00 95.85  ? 19  ALA E N   1 
ATOM   7922  C CA  . ALA E 1 11  ? -5.631  23.905  -3.666  1.00 95.17  ? 19  ALA E CA  1 
ATOM   7923  C C   . ALA E 1 11  ? -6.265  23.254  -4.895  1.00 98.55  ? 19  ALA E C   1 
ATOM   7924  O O   . ALA E 1 11  ? -6.298  23.855  -5.971  1.00 100.60 ? 19  ALA E O   1 
ATOM   7925  C CB  . ALA E 1 11  ? -6.695  24.486  -2.741  1.00 99.02  ? 19  ALA E CB  1 
ATOM   7926  N N   . ASN E 1 12  ? -6.748  22.023  -4.735  1.00 86.70  ? 20  ASN E N   1 
ATOM   7927  C CA  . ASN E 1 12  ? -7.382  21.293  -5.834  1.00 98.78  ? 20  ASN E CA  1 
ATOM   7928  C C   . ASN E 1 12  ? -8.343  20.188  -5.379  1.00 109.17 ? 20  ASN E C   1 
ATOM   7929  O O   . ASN E 1 12  ? -8.665  20.080  -4.195  1.00 104.15 ? 20  ASN E O   1 
ATOM   7930  C CB  . ASN E 1 12  ? -6.330  20.739  -6.805  1.00 95.28  ? 20  ASN E CB  1 
ATOM   7931  C CG  . ASN E 1 12  ? -5.178  20.050  -6.094  1.00 90.18  ? 20  ASN E CG  1 
ATOM   7932  O OD1 . ASN E 1 12  ? -5.306  19.614  -4.948  1.00 90.57  ? 20  ASN E OD1 1 
ATOM   7933  N ND2 . ASN E 1 12  ? -4.040  19.950  -6.776  1.00 88.85  ? 20  ASN E ND2 1 
ATOM   7934  N N   . ASN E 1 13  ? -8.797  19.377  -6.331  1.00 141.97 ? 21  ASN E N   1 
ATOM   7935  C CA  . ASN E 1 13  ? -9.798  18.342  -6.067  1.00 146.48 ? 21  ASN E CA  1 
ATOM   7936  C C   . ASN E 1 13  ? -9.195  16.975  -5.748  1.00 133.04 ? 21  ASN E C   1 
ATOM   7937  O O   . ASN E 1 13  ? -9.804  15.941  -6.024  1.00 130.42 ? 21  ASN E O   1 
ATOM   7938  C CB  . ASN E 1 13  ? -10.765 18.221  -7.251  1.00 163.31 ? 21  ASN E CB  1 
ATOM   7939  C CG  . ASN E 1 13  ? -10.066 17.821  -8.544  1.00 169.28 ? 21  ASN E CG  1 
ATOM   7940  O OD1 . ASN E 1 13  ? -8.935  17.334  -8.530  1.00 160.58 ? 21  ASN E OD1 1 
ATOM   7941  N ND2 . ASN E 1 13  ? -10.744 18.023  -9.669  1.00 180.57 ? 21  ASN E ND2 1 
ATOM   7942  N N   . SER E 1 14  ? -8.001  16.980  -5.166  1.00 111.76 ? 22  SER E N   1 
ATOM   7943  C CA  . SER E 1 14  ? -7.281  15.752  -4.855  1.00 104.05 ? 22  SER E CA  1 
ATOM   7944  C C   . SER E 1 14  ? -7.841  15.096  -3.595  1.00 94.00  ? 22  SER E C   1 
ATOM   7945  O O   . SER E 1 14  ? -8.204  15.782  -2.641  1.00 84.99  ? 22  SER E O   1 
ATOM   7946  C CB  . SER E 1 14  ? -5.788  16.052  -4.685  1.00 102.13 ? 22  SER E CB  1 
ATOM   7947  O OG  . SER E 1 14  ? -5.013  14.868  -4.720  1.00 102.03 ? 22  SER E OG  1 
ATOM   7948  N N   . THR E 1 15  ? -7.921  13.769  -3.602  1.00 115.64 ? 23  THR E N   1 
ATOM   7949  C CA  . THR E 1 15  ? -8.401  13.033  -2.440  1.00 116.13 ? 23  THR E CA  1 
ATOM   7950  C C   . THR E 1 15  ? -7.263  12.250  -1.803  1.00 114.84 ? 23  THR E C   1 
ATOM   7951  O O   . THR E 1 15  ? -7.389  11.765  -0.678  1.00 111.60 ? 23  THR E O   1 
ATOM   7952  C CB  . THR E 1 15  ? -9.530  12.059  -2.803  1.00 117.64 ? 23  THR E CB  1 
ATOM   7953  O OG1 . THR E 1 15  ? -9.000  10.983  -3.587  1.00 119.70 ? 23  THR E OG1 1 
ATOM   7954  C CG2 . THR E 1 15  ? -10.618 12.775  -3.586  1.00 124.37 ? 23  THR E CG2 1 
ATOM   7955  N N   . GLU E 1 16  ? -6.159  12.124  -2.537  1.00 117.08 ? 24  GLU E N   1 
ATOM   7956  C CA  . GLU E 1 16  ? -4.948  11.501  -2.016  1.00 103.87 ? 24  GLU E CA  1 
ATOM   7957  C C   . GLU E 1 16  ? -4.768  11.842  -0.545  1.00 95.86  ? 24  GLU E C   1 
ATOM   7958  O O   . GLU E 1 16  ? -4.916  12.995  -0.145  1.00 99.25  ? 24  GLU E O   1 
ATOM   7959  C CB  . GLU E 1 16  ? -3.725  11.976  -2.804  1.00 99.65  ? 24  GLU E CB  1 
ATOM   7960  C CG  . GLU E 1 16  ? -3.619  11.398  -4.199  1.00 106.44 ? 24  GLU E CG  1 
ATOM   7961  C CD  . GLU E 1 16  ? -3.415  9.893   -4.184  1.00 121.35 ? 24  GLU E CD  1 
ATOM   7962  O OE1 . GLU E 1 16  ? -2.388  9.434   -3.633  1.00 117.62 ? 24  GLU E OE1 1 
ATOM   7963  O OE2 . GLU E 1 16  ? -4.286  9.170   -4.715  1.00 134.09 ? 24  GLU E OE2 1 
ATOM   7964  N N   . LYS E 1 17  ? -4.458  10.842  0.269   1.00 97.10  ? 25  LYS E N   1 
ATOM   7965  C CA  . LYS E 1 17  ? -4.237  11.094  1.686   1.00 93.96  ? 25  LYS E CA  1 
ATOM   7966  C C   . LYS E 1 17  ? -2.909  10.523  2.165   1.00 87.16  ? 25  LYS E C   1 
ATOM   7967  O O   . LYS E 1 17  ? -2.438  9.498   1.670   1.00 86.92  ? 25  LYS E O   1 
ATOM   7968  C CB  . LYS E 1 17  ? -5.403  10.567  2.526   1.00 99.07  ? 25  LYS E CB  1 
ATOM   7969  C CG  . LYS E 1 17  ? -6.738  11.171  2.127   1.00 111.34 ? 25  LYS E CG  1 
ATOM   7970  C CD  . LYS E 1 17  ? -7.839  10.843  3.116   1.00 117.89 ? 25  LYS E CD  1 
ATOM   7971  C CE  . LYS E 1 17  ? -9.202  11.067  2.484   1.00 125.23 ? 25  LYS E CE  1 
ATOM   7972  N NZ  . LYS E 1 17  ? -9.158  12.149  1.461   1.00 126.11 ? 25  LYS E NZ  1 
ATOM   7973  N N   . VAL E 1 18  ? -2.305  11.215  3.123   1.00 81.39  ? 26  VAL E N   1 
ATOM   7974  C CA  . VAL E 1 18  ? -1.042  10.803  3.706   1.00 76.41  ? 26  VAL E CA  1 
ATOM   7975  C C   . VAL E 1 18  ? -1.190  10.858  5.220   1.00 73.54  ? 26  VAL E C   1 
ATOM   7976  O O   . VAL E 1 18  ? -2.084  11.532  5.730   1.00 76.05  ? 26  VAL E O   1 
ATOM   7977  C CB  . VAL E 1 18  ? 0.093   11.745  3.277   1.00 71.50  ? 26  VAL E CB  1 
ATOM   7978  C CG1 . VAL E 1 18  ? 0.214   11.780  1.757   1.00 69.37  ? 26  VAL E CG1 1 
ATOM   7979  C CG2 . VAL E 1 18  ? -0.154  13.140  3.823   1.00 67.90  ? 26  VAL E CG2 1 
ATOM   7980  N N   . ASP E 1 19  ? -0.328  10.151  5.942   1.00 97.52  ? 27  ASP E N   1 
ATOM   7981  C CA  . ASP E 1 19  ? -0.382  10.187  7.401   1.00 103.65 ? 27  ASP E CA  1 
ATOM   7982  C C   . ASP E 1 19  ? 0.831   10.891  7.995   1.00 96.60  ? 27  ASP E C   1 
ATOM   7983  O O   . ASP E 1 19  ? 1.940   10.792  7.471   1.00 101.61 ? 27  ASP E O   1 
ATOM   7984  C CB  . ASP E 1 19  ? -0.521  8.779   7.990   1.00 109.03 ? 27  ASP E CB  1 
ATOM   7985  C CG  . ASP E 1 19  ? -1.935  8.229   7.873   1.00 119.71 ? 27  ASP E CG  1 
ATOM   7986  O OD1 . ASP E 1 19  ? -2.620  8.549   6.877   1.00 126.64 ? 27  ASP E OD1 1 
ATOM   7987  O OD2 . ASP E 1 19  ? -2.363  7.477   8.778   1.00 118.75 ? 27  ASP E OD2 1 
ATOM   7988  N N   . THR E 1 20  ? 0.601   11.607  9.091   1.00 71.48  ? 28  THR E N   1 
ATOM   7989  C CA  . THR E 1 20  ? 1.665   12.281  9.818   1.00 62.94  ? 28  THR E CA  1 
ATOM   7990  C C   . THR E 1 20  ? 1.708   11.774  11.250  1.00 65.92  ? 28  THR E C   1 
ATOM   7991  O O   . THR E 1 20  ? 0.768   11.127  11.710  1.00 76.82  ? 28  THR E O   1 
ATOM   7992  C CB  . THR E 1 20  ? 1.408   13.780  9.872   1.00 66.91  ? 28  THR E CB  1 
ATOM   7993  O OG1 . THR E 1 20  ? 0.079   14.011  10.360  1.00 70.60  ? 28  THR E OG1 1 
ATOM   7994  C CG2 . THR E 1 20  ? 1.557   14.396  8.491   1.00 75.41  ? 28  THR E CG2 1 
ATOM   7995  N N   . ILE E 1 21  ? 2.791   12.081  11.959  1.00 71.73  ? 29  ILE E N   1 
ATOM   7996  C CA  . ILE E 1 21  ? 2.930   11.690  13.362  1.00 70.14  ? 29  ILE E CA  1 
ATOM   7997  C C   . ILE E 1 21  ? 1.776   12.188  14.242  1.00 79.55  ? 29  ILE E C   1 
ATOM   7998  O O   . ILE E 1 21  ? 1.457   11.575  15.262  1.00 86.96  ? 29  ILE E O   1 
ATOM   7999  C CB  . ILE E 1 21  ? 4.265   12.189  13.963  1.00 64.40  ? 29  ILE E CB  1 
ATOM   8000  C CG1 . ILE E 1 21  ? 5.455   11.493  13.305  1.00 72.85  ? 29  ILE E CG1 1 
ATOM   8001  C CG2 . ILE E 1 21  ? 4.305   11.929  15.459  1.00 59.26  ? 29  ILE E CG2 1 
ATOM   8002  C CD1 . ILE E 1 21  ? 5.819   10.172  13.957  1.00 76.33  ? 29  ILE E CD1 1 
ATOM   8003  N N   . LEU E 1 22  ? 1.149   13.293  13.845  1.00 68.43  ? 30  LEU E N   1 
ATOM   8004  C CA  . LEU E 1 22  ? 0.124   13.926  14.678  1.00 72.38  ? 30  LEU E CA  1 
ATOM   8005  C C   . LEU E 1 22  ? -1.292  13.796  14.114  1.00 80.60  ? 30  LEU E C   1 
ATOM   8006  O O   . LEU E 1 22  ? -2.268  13.839  14.860  1.00 78.11  ? 30  LEU E O   1 
ATOM   8007  C CB  . LEU E 1 22  ? 0.454   15.409  14.906  1.00 67.98  ? 30  LEU E CB  1 
ATOM   8008  C CG  . LEU E 1 22  ? 1.635   15.799  15.804  1.00 64.62  ? 30  LEU E CG  1 
ATOM   8009  C CD1 . LEU E 1 22  ? 2.908   15.103  15.372  1.00 62.86  ? 30  LEU E CD1 1 
ATOM   8010  C CD2 . LEU E 1 22  ? 1.835   17.300  15.791  1.00 67.80  ? 30  LEU E CD2 1 
ATOM   8011  N N   . GLU E 1 23  ? -1.401  13.638  12.798  1.00 88.94  ? 31  GLU E N   1 
ATOM   8012  C CA  . GLU E 1 23  ? -2.704  13.635  12.142  1.00 96.31  ? 31  GLU E CA  1 
ATOM   8013  C C   . GLU E 1 23  ? -2.818  12.508  11.110  1.00 99.68  ? 31  GLU E C   1 
ATOM   8014  O O   . GLU E 1 23  ? -1.957  12.363  10.240  1.00 96.98  ? 31  GLU E O   1 
ATOM   8015  C CB  . GLU E 1 23  ? -2.952  14.994  11.480  1.00 96.22  ? 31  GLU E CB  1 
ATOM   8016  C CG  . GLU E 1 23  ? -4.416  15.339  11.219  1.00 106.14 ? 31  GLU E CG  1 
ATOM   8017  C CD  . GLU E 1 23  ? -4.592  16.736  10.622  1.00 110.68 ? 31  GLU E CD  1 
ATOM   8018  O OE1 . GLU E 1 23  ? -3.587  17.476  10.515  1.00 97.95  ? 31  GLU E OE1 1 
ATOM   8019  O OE2 . GLU E 1 23  ? -5.732  17.096  10.256  1.00 120.35 ? 31  GLU E OE2 1 
ATOM   8020  N N   . ARG E 1 24  ? -3.880  11.712  11.219  1.00 98.18  ? 32  ARG E N   1 
ATOM   8021  C CA  . ARG E 1 24  ? -4.143  10.639  10.262  1.00 108.40 ? 32  ARG E CA  1 
ATOM   8022  C C   . ARG E 1 24  ? -5.206  11.043  9.244   1.00 117.92 ? 32  ARG E C   1 
ATOM   8023  O O   . ARG E 1 24  ? -6.061  11.880  9.527   1.00 127.14 ? 32  ARG E O   1 
ATOM   8024  C CB  . ARG E 1 24  ? -4.582  9.366   10.985  1.00 114.76 ? 32  ARG E CB  1 
ATOM   8025  C CG  . ARG E 1 24  ? -3.521  8.756   11.878  1.00 114.61 ? 32  ARG E CG  1 
ATOM   8026  C CD  . ARG E 1 24  ? -4.058  7.524   12.582  1.00 121.58 ? 32  ARG E CD  1 
ATOM   8027  N NE  . ARG E 1 24  ? -3.089  6.964   13.517  1.00 123.17 ? 32  ARG E NE  1 
ATOM   8028  C CZ  . ARG E 1 24  ? -3.357  5.977   14.367  1.00 123.53 ? 32  ARG E CZ  1 
ATOM   8029  N NH1 . ARG E 1 24  ? -4.571  5.441   14.402  1.00 130.45 ? 32  ARG E NH1 1 
ATOM   8030  N NH2 . ARG E 1 24  ? -2.414  5.531   15.184  1.00 112.74 ? 32  ARG E NH2 1 
ATOM   8031  N N   . ASN E 1 25  ? -5.153  10.433  8.065   1.00 151.39 ? 33  ASN E N   1 
ATOM   8032  C CA  . ASN E 1 25  ? -6.085  10.757  6.990   1.00 159.32 ? 33  ASN E CA  1 
ATOM   8033  C C   . ASN E 1 25  ? -6.049  12.244  6.657   1.00 154.94 ? 33  ASN E C   1 
ATOM   8034  O O   . ASN E 1 25  ? -6.906  13.009  7.098   1.00 164.09 ? 33  ASN E O   1 
ATOM   8035  C CB  . ASN E 1 25  ? -7.511  10.327  7.353   1.00 174.49 ? 33  ASN E CB  1 
ATOM   8036  C CG  . ASN E 1 25  ? -7.676  8.815   7.398   1.00 182.39 ? 33  ASN E CG  1 
ATOM   8037  O OD1 . ASN E 1 25  ? -6.703  8.067   7.295   1.00 177.84 ? 33  ASN E OD1 1 
ATOM   8038  N ND2 . ASN E 1 25  ? -8.914  8.360   7.558   1.00 189.31 ? 33  ASN E ND2 1 
ATOM   8039  N N   . VAL E 1 26  ? -5.051  12.648  5.878   1.00 68.89  ? 34  VAL E N   1 
ATOM   8040  C CA  . VAL E 1 26  ? -4.871  14.055  5.539   1.00 65.80  ? 34  VAL E CA  1 
ATOM   8041  C C   . VAL E 1 26  ? -4.700  14.293  4.037   1.00 68.16  ? 34  VAL E C   1 
ATOM   8042  O O   . VAL E 1 26  ? -3.667  13.962  3.451   1.00 68.38  ? 34  VAL E O   1 
ATOM   8043  C CB  . VAL E 1 26  ? -3.677  14.670  6.300   1.00 57.84  ? 34  VAL E CB  1 
ATOM   8044  C CG1 . VAL E 1 26  ? -3.292  16.012  5.701   1.00 60.37  ? 34  VAL E CG1 1 
ATOM   8045  C CG2 . VAL E 1 26  ? -4.006  14.805  7.784   1.00 51.99  ? 34  VAL E CG2 1 
ATOM   8046  N N   . THR E 1 27  ? -5.719  14.889  3.426   1.00 76.55  ? 35  THR E N   1 
ATOM   8047  C CA  . THR E 1 27  ? -5.719  15.146  1.992   1.00 77.29  ? 35  THR E CA  1 
ATOM   8048  C C   . THR E 1 27  ? -4.557  16.051  1.612   1.00 79.48  ? 35  THR E C   1 
ATOM   8049  O O   . THR E 1 27  ? -4.200  16.953  2.365   1.00 78.42  ? 35  THR E O   1 
ATOM   8050  C CB  . THR E 1 27  ? -7.032  15.815  1.551   1.00 77.06  ? 35  THR E CB  1 
ATOM   8051  O OG1 . THR E 1 27  ? -8.127  15.288  2.315   1.00 76.15  ? 35  THR E OG1 1 
ATOM   8052  C CG2 . THR E 1 27  ? -7.277  15.579  0.073   1.00 81.40  ? 35  THR E CG2 1 
ATOM   8053  N N   . VAL E 1 28  ? -3.960  15.798  0.451   1.00 83.82  ? 36  VAL E N   1 
ATOM   8054  C CA  . VAL E 1 28  ? -2.907  16.661  -0.077  1.00 78.61  ? 36  VAL E CA  1 
ATOM   8055  C C   . VAL E 1 28  ? -3.140  16.865  -1.562  1.00 81.72  ? 36  VAL E C   1 
ATOM   8056  O O   . VAL E 1 28  ? -4.048  16.267  -2.135  1.00 86.39  ? 36  VAL E O   1 
ATOM   8057  C CB  . VAL E 1 28  ? -1.500  16.059  0.119   1.00 67.84  ? 36  VAL E CB  1 
ATOM   8058  C CG1 . VAL E 1 28  ? -1.319  15.575  1.557   1.00 59.02  ? 36  VAL E CG1 1 
ATOM   8059  C CG2 . VAL E 1 28  ? -1.254  14.929  -0.875  1.00 66.24  ? 36  VAL E CG2 1 
ATOM   8060  N N   . THR E 1 29  ? -2.322  17.704  -2.189  1.00 85.12  ? 37  THR E N   1 
ATOM   8061  C CA  . THR E 1 29  ? -2.485  17.967  -3.613  1.00 94.40  ? 37  THR E CA  1 
ATOM   8062  C C   . THR E 1 29  ? -1.841  16.860  -4.437  1.00 102.35 ? 37  THR E C   1 
ATOM   8063  O O   . THR E 1 29  ? -2.505  16.204  -5.241  1.00 111.40 ? 37  THR E O   1 
ATOM   8064  C CB  . THR E 1 29  ? -1.907  19.348  -4.028  1.00 86.20  ? 37  THR E CB  1 
ATOM   8065  O OG1 . THR E 1 29  ? -0.497  19.244  -4.271  1.00 82.34  ? 37  THR E OG1 1 
ATOM   8066  C CG2 . THR E 1 29  ? -2.172  20.393  -2.950  1.00 79.03  ? 37  THR E CG2 1 
ATOM   8067  N N   . HIS E 1 30  ? -0.546  16.651  -4.225  1.00 108.56 ? 38  HIS E N   1 
ATOM   8068  C CA  . HIS E 1 30  ? 0.200   15.649  -4.973  1.00 110.30 ? 38  HIS E CA  1 
ATOM   8069  C C   . HIS E 1 30  ? 0.974   14.743  -4.021  1.00 100.09 ? 38  HIS E C   1 
ATOM   8070  O O   . HIS E 1 30  ? 1.567   15.209  -3.047  1.00 88.53  ? 38  HIS E O   1 
ATOM   8071  C CB  . HIS E 1 30  ? 1.155   16.322  -5.964  1.00 115.51 ? 38  HIS E CB  1 
ATOM   8072  C CG  . HIS E 1 30  ? 1.452   15.497  -7.180  1.00 122.07 ? 38  HIS E CG  1 
ATOM   8073  N ND1 . HIS E 1 30  ? 2.576   14.707  -7.289  1.00 115.32 ? 38  HIS E ND1 1 
ATOM   8074  C CD2 . HIS E 1 30  ? 0.774   15.348  -8.343  1.00 132.13 ? 38  HIS E CD2 1 
ATOM   8075  C CE1 . HIS E 1 30  ? 2.576   14.105  -8.465  1.00 120.81 ? 38  HIS E CE1 1 
ATOM   8076  N NE2 . HIS E 1 30  ? 1.494   14.477  -9.124  1.00 132.15 ? 38  HIS E NE2 1 
ATOM   8077  N N   . ALA E 1 31  ? 0.956   13.445  -4.307  1.00 144.70 ? 39  ALA E N   1 
ATOM   8078  C CA  . ALA E 1 31  ? 1.645   12.464  -3.478  1.00 137.88 ? 39  ALA E CA  1 
ATOM   8079  C C   . ALA E 1 31  ? 2.389   11.449  -4.336  1.00 135.18 ? 39  ALA E C   1 
ATOM   8080  O O   . ALA E 1 31  ? 1.877   10.994  -5.358  1.00 143.16 ? 39  ALA E O   1 
ATOM   8081  C CB  . ALA E 1 31  ? 0.659   11.759  -2.557  1.00 138.51 ? 39  ALA E CB  1 
ATOM   8082  N N   . LYS E 1 32  ? 3.602   11.107  -3.917  1.00 101.33 ? 40  LYS E N   1 
ATOM   8083  C CA  . LYS E 1 32  ? 4.393   10.076  -4.581  1.00 101.87 ? 40  LYS E CA  1 
ATOM   8084  C C   . LYS E 1 32  ? 4.436   8.836   -3.694  1.00 97.45  ? 40  LYS E C   1 
ATOM   8085  O O   . LYS E 1 32  ? 4.949   8.891   -2.579  1.00 90.01  ? 40  LYS E O   1 
ATOM   8086  C CB  . LYS E 1 32  ? 5.814   10.579  -4.837  1.00 99.03  ? 40  LYS E CB  1 
ATOM   8087  C CG  . LYS E 1 32  ? 6.732   9.571   -5.507  1.00 102.16 ? 40  LYS E CG  1 
ATOM   8088  C CD  . LYS E 1 32  ? 6.716   9.725   -7.019  1.00 112.20 ? 40  LYS E CD  1 
ATOM   8089  C CE  . LYS E 1 32  ? 7.755   8.830   -7.674  1.00 110.70 ? 40  LYS E CE  1 
ATOM   8090  N NZ  . LYS E 1 32  ? 7.486   7.392   -7.398  1.00 106.51 ? 40  LYS E NZ  1 
ATOM   8091  N N   . ASP E 1 33  ? 3.882   7.725   -4.172  1.00 100.03 ? 41  ASP E N   1 
ATOM   8092  C CA  . ASP E 1 33  ? 3.934   6.480   -3.409  1.00 99.09  ? 41  ASP E CA  1 
ATOM   8093  C C   . ASP E 1 33  ? 5.250   5.775   -3.703  1.00 92.33  ? 41  ASP E C   1 
ATOM   8094  O O   . ASP E 1 33  ? 5.732   5.790   -4.836  1.00 97.87  ? 41  ASP E O   1 
ATOM   8095  C CB  . ASP E 1 33  ? 2.742   5.573   -3.735  1.00 108.57 ? 41  ASP E CB  1 
ATOM   8096  C CG  . ASP E 1 33  ? 2.608   4.407   -2.762  1.00 110.67 ? 41  ASP E CG  1 
ATOM   8097  O OD1 . ASP E 1 33  ? 1.717   3.554   -2.965  1.00 114.57 ? 41  ASP E OD1 1 
ATOM   8098  O OD2 . ASP E 1 33  ? 3.393   4.340   -1.793  1.00 108.29 ? 41  ASP E OD2 1 
ATOM   8099  N N   . ILE E 1 34  ? 5.835   5.170   -2.677  1.00 71.86  ? 42  ILE E N   1 
ATOM   8100  C CA  . ILE E 1 34  ? 7.143   4.544   -2.821  1.00 67.81  ? 42  ILE E CA  1 
ATOM   8101  C C   . ILE E 1 34  ? 7.134   3.038   -2.544  1.00 72.48  ? 42  ILE E C   1 
ATOM   8102  O O   . ILE E 1 34  ? 8.189   2.415   -2.450  1.00 74.67  ? 42  ILE E O   1 
ATOM   8103  C CB  . ILE E 1 34  ? 8.172   5.204   -1.898  1.00 55.13  ? 42  ILE E CB  1 
ATOM   8104  C CG1 . ILE E 1 34  ? 7.552   5.450   -0.519  1.00 51.89  ? 42  ILE E CG1 1 
ATOM   8105  C CG2 . ILE E 1 34  ? 8.675   6.502   -2.507  1.00 46.86  ? 42  ILE E CG2 1 
ATOM   8106  C CD1 . ILE E 1 34  ? 8.549   5.949   0.513   1.00 45.26  ? 42  ILE E CD1 1 
ATOM   8107  N N   . LEU E 1 35  ? 5.947   2.458   -2.412  1.00 76.71  ? 43  LEU E N   1 
ATOM   8108  C CA  . LEU E 1 35  ? 5.834   1.036   -2.128  1.00 69.48  ? 43  LEU E CA  1 
ATOM   8109  C C   . LEU E 1 35  ? 5.420   0.272   -3.376  1.00 82.74  ? 43  LEU E C   1 
ATOM   8110  O O   . LEU E 1 35  ? 4.235   0.208   -3.711  1.00 90.24  ? 43  LEU E O   1 
ATOM   8111  C CB  . LEU E 1 35  ? 4.830   0.784   -1.002  1.00 57.55  ? 43  LEU E CB  1 
ATOM   8112  C CG  . LEU E 1 35  ? 4.725   -0.685  -0.583  1.00 54.61  ? 43  LEU E CG  1 
ATOM   8113  C CD1 . LEU E 1 35  ? 6.120   -1.240  -0.302  1.00 40.72  ? 43  LEU E CD1 1 
ATOM   8114  C CD2 . LEU E 1 35  ? 3.805   -0.873  0.618   1.00 54.92  ? 43  LEU E CD2 1 
ATOM   8115  N N   . GLU E 1 36  ? 6.401   -0.304  -4.064  1.00 71.79  ? 44  GLU E N   1 
ATOM   8116  C CA  . GLU E 1 36  ? 6.140   -1.088  -5.264  1.00 69.82  ? 44  GLU E CA  1 
ATOM   8117  C C   . GLU E 1 36  ? 5.334   -2.325  -4.900  1.00 67.73  ? 44  GLU E C   1 
ATOM   8118  O O   . GLU E 1 36  ? 5.728   -3.092  -4.027  1.00 57.60  ? 44  GLU E O   1 
ATOM   8119  C CB  . GLU E 1 36  ? 7.455   -1.477  -5.940  1.00 64.80  ? 44  GLU E CB  1 
ATOM   8120  C CG  . GLU E 1 36  ? 7.281   -2.242  -7.230  1.00 73.73  ? 44  GLU E CG  1 
ATOM   8121  C CD  . GLU E 1 36  ? 6.407   -1.511  -8.231  1.00 91.23  ? 44  GLU E CD  1 
ATOM   8122  O OE1 . GLU E 1 36  ? 6.804   -0.427  -8.708  1.00 92.00  ? 44  GLU E OE1 1 
ATOM   8123  O OE2 . GLU E 1 36  ? 5.311   -2.025  -8.538  1.00 100.95 ? 44  GLU E OE2 1 
ATOM   8124  N N   . LYS E 1 37  ? 4.198   -2.512  -5.559  1.00 71.05  ? 45  LYS E N   1 
ATOM   8125  C CA  . LYS E 1 37  ? 3.312   -3.614  -5.207  1.00 74.74  ? 45  LYS E CA  1 
ATOM   8126  C C   . LYS E 1 37  ? 2.741   -4.373  -6.415  1.00 84.27  ? 45  LYS E C   1 
ATOM   8127  O O   . LYS E 1 37  ? 1.877   -5.240  -6.261  1.00 81.49  ? 45  LYS E O   1 
ATOM   8128  C CB  . LYS E 1 37  ? 2.197   -3.126  -4.272  1.00 73.22  ? 45  LYS E CB  1 
ATOM   8129  C CG  . LYS E 1 37  ? 1.808   -1.665  -4.452  1.00 76.53  ? 45  LYS E CG  1 
ATOM   8130  C CD  . LYS E 1 37  ? 1.568   -0.979  -3.101  1.00 71.49  ? 45  LYS E CD  1 
ATOM   8131  C CE  . LYS E 1 37  ? 0.626   0.221   -3.219  1.00 74.87  ? 45  LYS E CE  1 
ATOM   8132  N NZ  . LYS E 1 37  ? 1.027   1.182   -4.286  1.00 75.63  ? 45  LYS E NZ  1 
ATOM   8133  N N   . THR E 1 38  ? 3.242   -4.057  -7.608  1.00 104.75 ? 46  THR E N   1 
ATOM   8134  C CA  . THR E 1 38  ? 2.772   -4.699  -8.837  1.00 117.91 ? 46  THR E CA  1 
ATOM   8135  C C   . THR E 1 38  ? 3.904   -5.364  -9.621  1.00 118.14 ? 46  THR E C   1 
ATOM   8136  O O   . THR E 1 38  ? 4.898   -4.721  -9.963  1.00 115.06 ? 46  THR E O   1 
ATOM   8137  C CB  . THR E 1 38  ? 2.037   -3.700  -9.759  1.00 127.89 ? 46  THR E CB  1 
ATOM   8138  O OG1 . THR E 1 38  ? 2.898   -2.591  -10.050 1.00 126.89 ? 46  THR E OG1 1 
ATOM   8139  C CG2 . THR E 1 38  ? 0.765   -3.189  -9.095  1.00 129.25 ? 46  THR E CG2 1 
ATOM   8140  N N   . HIS E 1 39  ? 3.735   -6.654  -9.903  1.00 121.07 ? 47  HIS E N   1 
ATOM   8141  C CA  . HIS E 1 39  ? 4.711   -7.439  -10.660 1.00 121.98 ? 47  HIS E CA  1 
ATOM   8142  C C   . HIS E 1 39  ? 4.381   -7.424  -12.150 1.00 133.28 ? 47  HIS E C   1 
ATOM   8143  O O   . HIS E 1 39  ? 4.035   -6.380  -12.704 1.00 144.64 ? 47  HIS E O   1 
ATOM   8144  C CB  . HIS E 1 39  ? 4.732   -8.878  -10.146 1.00 116.94 ? 47  HIS E CB  1 
ATOM   8145  C CG  . HIS E 1 39  ? 3.371   -9.437  -9.866  1.00 114.95 ? 47  HIS E CG  1 
ATOM   8146  N ND1 . HIS E 1 39  ? 2.503   -9.823  -10.865 1.00 120.52 ? 47  HIS E ND1 1 
ATOM   8147  C CD2 . HIS E 1 39  ? 2.725   -9.667  -8.698  1.00 107.92 ? 47  HIS E CD2 1 
ATOM   8148  C CE1 . HIS E 1 39  ? 1.384   -10.273 -10.325 1.00 119.77 ? 47  HIS E CE1 1 
ATOM   8149  N NE2 . HIS E 1 39  ? 1.493   -10.189 -9.011  1.00 110.59 ? 47  HIS E NE2 1 
ATOM   8150  N N   . ASN E 1 40  ? 4.497   -8.579  -12.799 1.00 79.85  ? 48  ASN E N   1 
ATOM   8151  C CA  . ASN E 1 40  ? 4.025   -8.719  -14.177 1.00 87.35  ? 48  ASN E CA  1 
ATOM   8152  C C   . ASN E 1 40  ? 3.640   -10.149 -14.550 1.00 93.12  ? 48  ASN E C   1 
ATOM   8153  O O   . ASN E 1 40  ? 3.179   -10.403 -15.662 1.00 103.54 ? 48  ASN E O   1 
ATOM   8154  C CB  . ASN E 1 40  ? 5.015   -8.112  -15.190 1.00 88.93  ? 48  ASN E CB  1 
ATOM   8155  C CG  . ASN E 1 40  ? 6.236   -8.985  -15.435 1.00 85.24  ? 48  ASN E CG  1 
ATOM   8156  O OD1 . ASN E 1 40  ? 6.197   -10.199 -15.265 1.00 81.47  ? 48  ASN E OD1 1 
ATOM   8157  N ND2 . ASN E 1 40  ? 7.331   -8.360  -15.854 1.00 87.39  ? 48  ASN E ND2 1 
ATOM   8158  N N   . GLY E 1 41  ? 3.832   -11.075 -13.613 1.00 105.26 ? 49  GLY E N   1 
ATOM   8159  C CA  . GLY E 1 41  ? 3.436   -12.464 -13.794 1.00 105.60 ? 49  GLY E CA  1 
ATOM   8160  C C   . GLY E 1 41  ? 4.343   -13.261 -14.711 1.00 106.24 ? 49  GLY E C   1 
ATOM   8161  O O   . GLY E 1 41  ? 4.188   -14.474 -14.845 1.00 105.24 ? 49  GLY E O   1 
ATOM   8162  N N   . LYS E 1 42  ? 5.296   -12.576 -15.335 1.00 100.70 ? 50  LYS E N   1 
ATOM   8163  C CA  . LYS E 1 42  ? 6.187   -13.189 -16.315 1.00 102.74 ? 50  LYS E CA  1 
ATOM   8164  C C   . LYS E 1 42  ? 7.595   -13.407 -15.772 1.00 96.19  ? 50  LYS E C   1 
ATOM   8165  O O   . LYS E 1 42  ? 8.361   -12.456 -15.624 1.00 91.73  ? 50  LYS E O   1 
ATOM   8166  C CB  . LYS E 1 42  ? 6.262   -12.322 -17.571 1.00 101.95 ? 50  LYS E CB  1 
ATOM   8167  C CG  . LYS E 1 42  ? 4.926   -12.113 -18.248 1.00 107.40 ? 50  LYS E CG  1 
ATOM   8168  C CD  . LYS E 1 42  ? 5.082   -11.302 -19.519 1.00 113.75 ? 50  LYS E CD  1 
ATOM   8169  C CE  . LYS E 1 42  ? 3.739   -11.073 -20.192 1.00 121.38 ? 50  LYS E CE  1 
ATOM   8170  N NZ  . LYS E 1 42  ? 3.090   -12.354 -20.580 1.00 127.60 ? 50  LYS E NZ  1 
ATOM   8171  N N   . LEU E 1 43  ? 7.942   -14.660 -15.490 1.00 74.18  ? 51  LEU E N   1 
ATOM   8172  C CA  . LEU E 1 43  ? 9.287   -14.972 -15.027 1.00 68.94  ? 51  LEU E CA  1 
ATOM   8173  C C   . LEU E 1 43  ? 10.275  -14.760 -16.165 1.00 71.20  ? 51  LEU E C   1 
ATOM   8174  O O   . LEU E 1 43  ? 10.396  -15.591 -17.062 1.00 69.56  ? 51  LEU E O   1 
ATOM   8175  C CB  . LEU E 1 43  ? 9.384   -16.402 -14.489 1.00 73.33  ? 51  LEU E CB  1 
ATOM   8176  C CG  . LEU E 1 43  ? 8.103   -17.203 -14.230 1.00 77.03  ? 51  LEU E CG  1 
ATOM   8177  C CD1 . LEU E 1 43  ? 8.453   -18.481 -13.484 1.00 70.93  ? 51  LEU E CD1 1 
ATOM   8178  C CD2 . LEU E 1 43  ? 7.038   -16.419 -13.459 1.00 79.42  ? 51  LEU E CD2 1 
ATOM   8179  N N   . CYS E 1 44  ? 10.970  -13.628 -16.124 1.00 110.64 ? 52  CYS E N   1 
ATOM   8180  C CA  . CYS E 1 44  ? 11.885  -13.234 -17.186 1.00 106.96 ? 52  CYS E CA  1 
ATOM   8181  C C   . CYS E 1 44  ? 13.308  -13.648 -16.847 1.00 83.03  ? 52  CYS E C   1 
ATOM   8182  O O   . CYS E 1 44  ? 13.580  -14.088 -15.737 1.00 79.57  ? 52  CYS E O   1 
ATOM   8183  C CB  . CYS E 1 44  ? 11.831  -11.720 -17.374 1.00 102.80 ? 52  CYS E CB  1 
ATOM   8184  S SG  . CYS E 1 44  ? 10.160  -11.054 -17.465 1.00 159.43 ? 52  CYS E SG  1 
ATOM   8185  N N   . LYS E 1 45  ? 14.219  -13.500 -17.801 1.00 119.21 ? 53  LYS E N   1 
ATOM   8186  C CA  . LYS E 1 45  ? 15.624  -13.749 -17.520 1.00 98.99  ? 53  LYS E CA  1 
ATOM   8187  C C   . LYS E 1 45  ? 16.095  -12.777 -16.443 1.00 85.26  ? 53  LYS E C   1 
ATOM   8188  O O   . LYS E 1 45  ? 15.290  -12.066 -15.847 1.00 90.76  ? 53  LYS E O   1 
ATOM   8189  C CB  . LYS E 1 45  ? 16.467  -13.605 -18.786 1.00 100.37 ? 53  LYS E CB  1 
ATOM   8190  C CG  . LYS E 1 45  ? 16.029  -14.518 -19.922 1.00 112.12 ? 53  LYS E CG  1 
ATOM   8191  C CD  . LYS E 1 45  ? 16.978  -14.431 -21.107 1.00 114.87 ? 53  LYS E CD  1 
ATOM   8192  C CE  . LYS E 1 45  ? 17.081  -13.009 -21.631 1.00 130.74 ? 53  LYS E CE  1 
ATOM   8193  N NZ  . LYS E 1 45  ? 15.764  -12.478 -22.081 1.00 151.96 ? 53  LYS E NZ  1 
ATOM   8194  N N   . LEU E 1 46  A 17.398  -12.747 -16.194 1.00 86.90  ? 53  LEU E N   1 
ATOM   8195  C CA  . LEU E 1 46  A 17.946  -11.900 -15.143 1.00 81.02  ? 53  LEU E CA  1 
ATOM   8196  C C   . LEU E 1 46  A 19.280  -11.301 -15.568 1.00 87.18  ? 53  LEU E C   1 
ATOM   8197  O O   . LEU E 1 46  A 20.228  -12.026 -15.870 1.00 91.64  ? 53  LEU E O   1 
ATOM   8198  C CB  . LEU E 1 46  A 18.105  -12.701 -13.847 1.00 66.24  ? 53  LEU E CB  1 
ATOM   8199  C CG  . LEU E 1 46  A 18.725  -12.027 -12.614 1.00 60.88  ? 53  LEU E CG  1 
ATOM   8200  C CD1 . LEU E 1 46  A 18.341  -12.767 -11.331 1.00 49.84  ? 53  LEU E CD1 1 
ATOM   8201  C CD2 . LEU E 1 46  A 20.246  -11.911 -12.726 1.00 67.00  ? 53  LEU E CD2 1 
ATOM   8202  N N   . ASN E 1 47  ? 19.350  -9.975  -15.587 1.00 117.64 ? 54  ASN E N   1 
ATOM   8203  C CA  . ASN E 1 47  ? 20.565  -9.278  -15.995 1.00 121.16 ? 54  ASN E CA  1 
ATOM   8204  C C   . ASN E 1 47  ? 21.015  -9.667  -17.398 1.00 123.46 ? 54  ASN E C   1 
ATOM   8205  O O   . ASN E 1 47  ? 22.156  -9.420  -17.783 1.00 127.84 ? 54  ASN E O   1 
ATOM   8206  C CB  . ASN E 1 47  ? 21.692  -9.522  -14.990 1.00 122.49 ? 54  ASN E CB  1 
ATOM   8207  C CG  . ASN E 1 47  ? 21.406  -8.906  -13.635 1.00 123.57 ? 54  ASN E CG  1 
ATOM   8208  O OD1 . ASN E 1 47  ? 20.256  -8.608  -13.307 1.00 123.79 ? 54  ASN E OD1 1 
ATOM   8209  N ND2 . ASN E 1 47  ? 22.452  -8.708  -12.841 1.00 124.64 ? 54  ASN E ND2 1 
ATOM   8210  N N   . GLY E 1 48  ? 20.111  -10.282 -18.155 1.00 106.13 ? 55  GLY E N   1 
ATOM   8211  C CA  . GLY E 1 48  ? 20.385  -10.637 -19.533 1.00 110.26 ? 55  GLY E CA  1 
ATOM   8212  C C   . GLY E 1 48  ? 20.624  -12.117 -19.755 1.00 112.40 ? 55  GLY E C   1 
ATOM   8213  O O   . GLY E 1 48  ? 20.523  -12.602 -20.883 1.00 120.53 ? 55  GLY E O   1 
ATOM   8214  N N   . ILE E 1 49  ? 20.944  -12.836 -18.683 1.00 106.65 ? 56  ILE E N   1 
ATOM   8215  C CA  . ILE E 1 49  ? 21.221  -14.269 -18.771 1.00 104.27 ? 56  ILE E CA  1 
ATOM   8216  C C   . ILE E 1 49  ? 20.120  -15.102 -18.107 1.00 102.44 ? 56  ILE E C   1 
ATOM   8217  O O   . ILE E 1 49  ? 19.802  -14.901 -16.937 1.00 96.91  ? 56  ILE E O   1 
ATOM   8218  C CB  . ILE E 1 49  ? 22.611  -14.612 -18.184 1.00 101.90 ? 56  ILE E CB  1 
ATOM   8219  C CG1 . ILE E 1 49  ? 22.793  -16.124 -18.067 1.00 105.58 ? 56  ILE E CG1 1 
ATOM   8220  C CG2 . ILE E 1 49  ? 22.809  -13.941 -16.842 1.00 98.19  ? 56  ILE E CG2 1 
ATOM   8221  C CD1 . ILE E 1 49  ? 23.096  -16.806 -19.382 1.00 114.92 ? 56  ILE E CD1 1 
ATOM   8222  N N   . PRO E 1 50  ? 19.529  -16.038 -18.866 1.00 115.62 ? 57  PRO E N   1 
ATOM   8223  C CA  . PRO E 1 50  ? 18.372  -16.859 -18.478 1.00 124.11 ? 57  PRO E CA  1 
ATOM   8224  C C   . PRO E 1 50  ? 18.570  -17.739 -17.237 1.00 119.96 ? 57  PRO E C   1 
ATOM   8225  O O   . PRO E 1 50  ? 19.699  -17.930 -16.785 1.00 119.65 ? 57  PRO E O   1 
ATOM   8226  C CB  . PRO E 1 50  ? 18.143  -17.744 -19.714 1.00 131.70 ? 57  PRO E CB  1 
ATOM   8227  C CG  . PRO E 1 50  ? 19.439  -17.719 -20.458 1.00 127.14 ? 57  PRO E CG  1 
ATOM   8228  C CD  . PRO E 1 50  ? 19.973  -16.341 -20.236 1.00 122.70 ? 57  PRO E CD  1 
ATOM   8229  N N   . PRO E 1 51  ? 17.461  -18.271 -16.692 1.00 95.39  ? 58  PRO E N   1 
ATOM   8230  C CA  . PRO E 1 51  ? 17.415  -19.208 -15.564 1.00 78.87  ? 58  PRO E CA  1 
ATOM   8231  C C   . PRO E 1 51  ? 17.960  -20.572 -15.952 1.00 71.56  ? 58  PRO E C   1 
ATOM   8232  O O   . PRO E 1 51  ? 18.990  -20.678 -16.619 1.00 77.28  ? 58  PRO E O   1 
ATOM   8233  C CB  . PRO E 1 51  ? 15.913  -19.360 -15.283 1.00 94.75  ? 58  PRO E CB  1 
ATOM   8234  C CG  . PRO E 1 51  ? 15.250  -18.247 -15.995 1.00 112.62 ? 58  PRO E CG  1 
ATOM   8235  C CD  . PRO E 1 51  ? 16.113  -17.909 -17.158 1.00 109.66 ? 58  PRO E CD  1 
ATOM   8236  N N   . LEU E 1 52  ? 17.247  -21.611 -15.529 1.00 92.76  ? 59  LEU E N   1 
ATOM   8237  C CA  . LEU E 1 52  ? 17.568  -22.982 -15.899 1.00 95.33  ? 59  LEU E CA  1 
ATOM   8238  C C   . LEU E 1 52  ? 16.395  -23.907 -15.590 1.00 120.36 ? 59  LEU E C   1 
ATOM   8239  O O   . LEU E 1 52  ? 16.505  -24.825 -14.779 1.00 126.19 ? 59  LEU E O   1 
ATOM   8240  C CB  . LEU E 1 52  ? 18.829  -23.463 -15.189 1.00 70.27  ? 59  LEU E CB  1 
ATOM   8241  C CG  . LEU E 1 52  ? 19.226  -24.863 -15.648 1.00 68.50  ? 59  LEU E CG  1 
ATOM   8242  C CD1 . LEU E 1 52  ? 19.173  -24.947 -17.163 1.00 70.40  ? 59  LEU E CD1 1 
ATOM   8243  C CD2 . LEU E 1 52  ? 20.597  -25.223 -15.133 1.00 61.43  ? 59  LEU E CD2 1 
ATOM   8244  N N   . GLU E 1 53  ? 15.274  -23.646 -16.253 1.00 61.40  ? 60  GLU E N   1 
ATOM   8245  C CA  . GLU E 1 53  ? 14.026  -24.382 -16.041 1.00 85.44  ? 60  GLU E CA  1 
ATOM   8246  C C   . GLU E 1 53  ? 14.199  -25.906 -16.087 1.00 85.83  ? 60  GLU E C   1 
ATOM   8247  O O   . GLU E 1 53  ? 14.818  -26.442 -17.004 1.00 89.21  ? 60  GLU E O   1 
ATOM   8248  C CB  . GLU E 1 53  ? 12.997  -23.936 -17.081 1.00 108.36 ? 60  GLU E CB  1 
ATOM   8249  C CG  . GLU E 1 53  ? 11.588  -24.406 -16.818 1.00 127.62 ? 60  GLU E CG  1 
ATOM   8250  C CD  . GLU E 1 53  ? 10.600  -23.794 -17.786 1.00 137.73 ? 60  GLU E CD  1 
ATOM   8251  O OE1 . GLU E 1 53  ? 11.042  -23.141 -18.757 1.00 133.07 ? 60  GLU E OE1 1 
ATOM   8252  O OE2 . GLU E 1 53  ? 9.384   -23.961 -17.571 1.00 143.58 ? 60  GLU E OE2 1 
ATOM   8253  N N   . LEU E 1 54  ? 13.640  -26.596 -15.097 1.00 111.94 ? 61  LEU E N   1 
ATOM   8254  C CA  . LEU E 1 54  ? 13.810  -28.044 -14.990 1.00 117.03 ? 61  LEU E CA  1 
ATOM   8255  C C   . LEU E 1 54  ? 12.513  -28.807 -15.248 1.00 147.15 ? 61  LEU E C   1 
ATOM   8256  O O   . LEU E 1 54  ? 12.537  -29.948 -15.711 1.00 154.63 ? 61  LEU E O   1 
ATOM   8257  C CB  . LEU E 1 54  ? 14.372  -28.425 -13.615 1.00 98.65  ? 61  LEU E CB  1 
ATOM   8258  C CG  . LEU E 1 54  ? 15.720  -27.832 -13.193 1.00 69.78  ? 61  LEU E CG  1 
ATOM   8259  C CD1 . LEU E 1 54  ? 16.146  -28.408 -11.854 1.00 67.31  ? 61  LEU E CD1 1 
ATOM   8260  C CD2 . LEU E 1 54  ? 16.785  -28.088 -14.244 1.00 53.84  ? 61  LEU E CD2 1 
ATOM   8261  N N   . GLY E 1 55  ? 11.386  -28.177 -14.935 1.00 162.98 ? 62  GLY E N   1 
ATOM   8262  C CA  . GLY E 1 55  ? 10.087  -28.782 -15.171 1.00 165.52 ? 62  GLY E CA  1 
ATOM   8263  C C   . GLY E 1 55  ? 9.587   -29.626 -14.015 1.00 157.65 ? 62  GLY E C   1 
ATOM   8264  O O   . GLY E 1 55  ? 9.496   -29.152 -12.882 1.00 150.39 ? 62  GLY E O   1 
ATOM   8265  N N   . ASP E 1 56  ? 9.256   -30.882 -14.308 1.00 106.31 ? 63  ASP E N   1 
ATOM   8266  C CA  . ASP E 1 56  ? 8.732   -31.804 -13.299 1.00 103.67 ? 63  ASP E CA  1 
ATOM   8267  C C   . ASP E 1 56  ? 9.868   -32.583 -12.636 1.00 98.95  ? 63  ASP E C   1 
ATOM   8268  O O   . ASP E 1 56  ? 9.637   -33.423 -11.766 1.00 95.08  ? 63  ASP E O   1 
ATOM   8269  C CB  . ASP E 1 56  ? 7.711   -32.765 -13.923 1.00 112.37 ? 63  ASP E CB  1 
ATOM   8270  C CG  . ASP E 1 56  ? 6.498   -32.994 -13.032 1.00 110.53 ? 63  ASP E CG  1 
ATOM   8271  O OD1 . ASP E 1 56  ? 6.620   -32.821 -11.801 1.00 101.76 ? 63  ASP E OD1 1 
ATOM   8272  O OD2 . ASP E 1 56  ? 5.421   -33.348 -13.563 1.00 114.90 ? 63  ASP E OD2 1 
ATOM   8273  N N   . CYS E 1 57  ? 11.096  -32.283 -13.050 1.00 139.74 ? 64  CYS E N   1 
ATOM   8274  C CA  . CYS E 1 57  ? 12.279  -32.951 -12.525 1.00 127.48 ? 64  CYS E CA  1 
ATOM   8275  C C   . CYS E 1 57  ? 12.813  -32.293 -11.259 1.00 115.57 ? 64  CYS E C   1 
ATOM   8276  O O   . CYS E 1 57  ? 12.486  -31.149 -10.948 1.00 118.58 ? 64  CYS E O   1 
ATOM   8277  C CB  . CYS E 1 57  ? 13.390  -32.968 -13.577 1.00 121.44 ? 64  CYS E CB  1 
ATOM   8278  S SG  . CYS E 1 57  ? 13.058  -33.997 -15.015 1.00 179.79 ? 64  CYS E SG  1 
ATOM   8279  N N   . SER E 1 58  ? 13.637  -33.039 -10.534 1.00 95.12  ? 65  SER E N   1 
ATOM   8280  C CA  . SER E 1 58  ? 14.427  -32.505 -9.439  1.00 77.59  ? 65  SER E CA  1 
ATOM   8281  C C   . SER E 1 58  ? 15.821  -32.282 -9.998  1.00 53.14  ? 65  SER E C   1 
ATOM   8282  O O   . SER E 1 58  ? 16.115  -32.730 -11.103 1.00 49.15  ? 65  SER E O   1 
ATOM   8283  C CB  . SER E 1 58  ? 14.503  -33.523 -8.312  1.00 80.85  ? 65  SER E CB  1 
ATOM   8284  O OG  . SER E 1 58  ? 15.278  -34.640 -8.718  1.00 73.29  ? 65  SER E OG  1 
ATOM   8285  N N   . ILE E 1 59  ? 16.684  -31.596 -9.254  1.00 82.72  ? 66  ILE E N   1 
ATOM   8286  C CA  . ILE E 1 59  ? 18.049  -31.388 -9.732  1.00 68.66  ? 66  ILE E CA  1 
ATOM   8287  C C   . ILE E 1 59  ? 18.803  -32.708 -9.780  1.00 67.29  ? 66  ILE E C   1 
ATOM   8288  O O   . ILE E 1 59  ? 19.691  -32.901 -10.615 1.00 63.50  ? 66  ILE E O   1 
ATOM   8289  C CB  . ILE E 1 59  ? 18.827  -30.365 -8.888  1.00 55.31  ? 66  ILE E CB  1 
ATOM   8290  C CG1 . ILE E 1 59  ? 18.148  -28.998 -8.970  1.00 56.18  ? 66  ILE E CG1 1 
ATOM   8291  C CG2 . ILE E 1 59  ? 20.278  -30.257 -9.364  1.00 45.56  ? 66  ILE E CG2 1 
ATOM   8292  C CD1 . ILE E 1 59  ? 19.119  -27.839 -8.896  1.00 56.46  ? 66  ILE E CD1 1 
ATOM   8293  N N   . ALA E 1 60  ? 18.444  -33.618 -8.881  1.00 96.08  ? 67  ALA E N   1 
ATOM   8294  C CA  . ALA E 1 60  ? 19.000  -34.962 -8.910  1.00 94.24  ? 67  ALA E CA  1 
ATOM   8295  C C   . ALA E 1 60  ? 18.683  -35.603 -10.257 1.00 101.88 ? 67  ALA E C   1 
ATOM   8296  O O   . ALA E 1 60  ? 19.578  -36.091 -10.947 1.00 99.90  ? 67  ALA E O   1 
ATOM   8297  C CB  . ALA E 1 60  ? 18.438  -35.793 -7.773  1.00 94.63  ? 67  ALA E CB  1 
ATOM   8298  N N   . GLY E 1 61  ? 17.405  -35.586 -10.629 1.00 93.12  ? 68  GLY E N   1 
ATOM   8299  C CA  . GLY E 1 61  ? 16.981  -36.091 -11.921 1.00 95.94  ? 68  GLY E CA  1 
ATOM   8300  C C   . GLY E 1 61  ? 17.849  -35.561 -13.048 1.00 84.72  ? 68  GLY E C   1 
ATOM   8301  O O   . GLY E 1 61  ? 18.288  -36.317 -13.911 1.00 86.55  ? 68  GLY E O   1 
ATOM   8302  N N   . TRP E 1 62  ? 18.109  -34.258 -13.032 1.00 90.59  ? 69  TRP E N   1 
ATOM   8303  C CA  . TRP E 1 62  ? 18.906  -33.624 -14.076 1.00 90.86  ? 69  TRP E CA  1 
ATOM   8304  C C   . TRP E 1 62  ? 20.301  -34.241 -14.187 1.00 91.66  ? 69  TRP E C   1 
ATOM   8305  O O   . TRP E 1 62  ? 20.562  -35.039 -15.087 1.00 94.05  ? 69  TRP E O   1 
ATOM   8306  C CB  . TRP E 1 62  ? 19.000  -32.106 -13.839 1.00 82.13  ? 69  TRP E CB  1 
ATOM   8307  C CG  . TRP E 1 62  ? 19.590  -31.342 -14.992 1.00 82.71  ? 69  TRP E CG  1 
ATOM   8308  C CD1 . TRP E 1 62  ? 19.148  -31.343 -16.281 1.00 97.45  ? 69  TRP E CD1 1 
ATOM   8309  C CD2 . TRP E 1 62  ? 20.722  -30.460 -14.958 1.00 84.60  ? 69  TRP E CD2 1 
ATOM   8310  N NE1 . TRP E 1 62  ? 19.937  -30.527 -17.054 1.00 98.99  ? 69  TRP E NE1 1 
ATOM   8311  C CE2 . TRP E 1 62  ? 20.911  -29.972 -16.265 1.00 91.08  ? 69  TRP E CE2 1 
ATOM   8312  C CE3 . TRP E 1 62  ? 21.594  -30.040 -13.951 1.00 89.03  ? 69  TRP E CE3 1 
ATOM   8313  C CZ2 . TRP E 1 62  ? 21.935  -29.082 -16.594 1.00 94.38  ? 69  TRP E CZ2 1 
ATOM   8314  C CZ3 . TRP E 1 62  ? 22.614  -29.156 -14.279 1.00 90.70  ? 69  TRP E CZ3 1 
ATOM   8315  C CH2 . TRP E 1 62  ? 22.774  -28.687 -15.589 1.00 93.49  ? 69  TRP E CH2 1 
ATOM   8316  N N   . LEU E 1 63  ? 21.180  -33.874 -13.258 1.00 116.23 ? 70  LEU E N   1 
ATOM   8317  C CA  . LEU E 1 63  ? 22.601  -34.224 -13.319 1.00 108.72 ? 70  LEU E CA  1 
ATOM   8318  C C   . LEU E 1 63  ? 22.908  -35.644 -13.809 1.00 112.96 ? 70  LEU E C   1 
ATOM   8319  O O   . LEU E 1 63  ? 23.608  -35.821 -14.807 1.00 120.61 ? 70  LEU E O   1 
ATOM   8320  C CB  . LEU E 1 63  ? 23.268  -33.975 -11.960 1.00 100.29 ? 70  LEU E CB  1 
ATOM   8321  C CG  . LEU E 1 63  ? 23.413  -32.519 -11.505 1.00 96.17  ? 70  LEU E CG  1 
ATOM   8322  C CD1 . LEU E 1 63  ? 24.028  -32.438 -10.117 1.00 93.81  ? 70  LEU E CD1 1 
ATOM   8323  C CD2 . LEU E 1 63  ? 24.255  -31.745 -12.498 1.00 101.04 ? 70  LEU E CD2 1 
ATOM   8324  N N   . LEU E 1 64  ? 22.392  -36.644 -13.098 1.00 71.03  ? 71  LEU E N   1 
ATOM   8325  C CA  . LEU E 1 64  ? 22.630  -38.049 -13.432 1.00 83.69  ? 71  LEU E CA  1 
ATOM   8326  C C   . LEU E 1 64  ? 22.325  -38.360 -14.894 1.00 96.70  ? 71  LEU E C   1 
ATOM   8327  O O   . LEU E 1 64  ? 23.225  -38.636 -15.691 1.00 96.06  ? 71  LEU E O   1 
ATOM   8328  C CB  . LEU E 1 64  ? 21.774  -38.956 -12.541 1.00 84.13  ? 71  LEU E CB  1 
ATOM   8329  C CG  . LEU E 1 64  ? 21.913  -38.767 -11.028 1.00 83.60  ? 71  LEU E CG  1 
ATOM   8330  C CD1 . LEU E 1 64  ? 20.788  -39.474 -10.284 1.00 85.37  ? 71  LEU E CD1 1 
ATOM   8331  C CD2 . LEU E 1 64  ? 23.275  -39.250 -10.552 1.00 84.23  ? 71  LEU E CD2 1 
ATOM   8332  N N   . GLY E 1 65  ? 21.043  -38.322 -15.233 1.00 100.94 ? 72  GLY E N   1 
ATOM   8333  C CA  . GLY E 1 65  ? 20.605  -38.628 -16.576 1.00 109.33 ? 72  GLY E CA  1 
ATOM   8334  C C   . GLY E 1 65  ? 19.353  -39.474 -16.559 1.00 120.11 ? 72  GLY E C   1 
ATOM   8335  O O   . GLY E 1 65  ? 19.185  -40.350 -17.409 1.00 132.41 ? 72  GLY E O   1 
ATOM   8336  N N   . ASN E 1 66  ? 18.479  -39.231 -15.584 1.00 54.71  ? 73  ASN E N   1 
ATOM   8337  C CA  . ASN E 1 66  ? 17.178  -39.890 -15.578 1.00 68.60  ? 73  ASN E CA  1 
ATOM   8338  C C   . ASN E 1 66  ? 16.528  -39.639 -16.927 1.00 83.55  ? 73  ASN E C   1 
ATOM   8339  O O   . ASN E 1 66  ? 16.229  -38.495 -17.265 1.00 85.32  ? 73  ASN E O   1 
ATOM   8340  C CB  . ASN E 1 66  ? 16.285  -39.371 -14.448 1.00 75.95  ? 73  ASN E CB  1 
ATOM   8341  C CG  . ASN E 1 66  ? 14.910  -40.027 -14.443 1.00 101.32 ? 73  ASN E CG  1 
ATOM   8342  O OD1 . ASN E 1 66  ? 14.649  -40.953 -15.212 1.00 114.92 ? 73  ASN E OD1 1 
ATOM   8343  N ND2 . ASN E 1 66  ? 14.028  -39.556 -13.566 1.00 101.07 ? 73  ASN E ND2 1 
ATOM   8344  N N   . PRO E 1 67  ? 16.334  -40.706 -17.717 1.00 163.16 ? 74  PRO E N   1 
ATOM   8345  C CA  . PRO E 1 67  ? 15.847  -40.594 -19.096 1.00 176.58 ? 74  PRO E CA  1 
ATOM   8346  C C   . PRO E 1 67  ? 14.624  -39.688 -19.249 1.00 201.62 ? 74  PRO E C   1 
ATOM   8347  O O   . PRO E 1 67  ? 14.351  -39.217 -20.354 1.00 210.66 ? 74  PRO E O   1 
ATOM   8348  C CB  . PRO E 1 67  ? 15.499  -42.038 -19.450 1.00 185.19 ? 74  PRO E CB  1 
ATOM   8349  C CG  . PRO E 1 67  ? 16.462  -42.841 -18.649 1.00 170.67 ? 74  PRO E CG  1 
ATOM   8350  C CD  . PRO E 1 67  ? 16.602  -42.106 -17.344 1.00 163.42 ? 74  PRO E CD  1 
ATOM   8351  N N   . GLU E 1 68  ? 13.905  -39.445 -18.157 1.00 141.97 ? 75  GLU E N   1 
ATOM   8352  C CA  . GLU E 1 68  ? 12.752  -38.549 -18.179 1.00 143.57 ? 75  GLU E CA  1 
ATOM   8353  C C   . GLU E 1 68  ? 13.177  -37.077 -18.214 1.00 130.43 ? 75  GLU E C   1 
ATOM   8354  O O   . GLU E 1 68  ? 12.334  -36.182 -18.259 1.00 127.78 ? 75  GLU E O   1 
ATOM   8355  C CB  . GLU E 1 68  ? 11.862  -38.804 -16.960 1.00 141.58 ? 75  GLU E CB  1 
ATOM   8356  C CG  . GLU E 1 68  ? 11.450  -40.257 -16.782 1.00 143.65 ? 75  GLU E CG  1 
ATOM   8357  C CD  . GLU E 1 68  ? 10.449  -40.718 -17.825 1.00 152.43 ? 75  GLU E CD  1 
ATOM   8358  O OE1 . GLU E 1 68  ? 9.912   -39.862 -18.560 1.00 161.11 ? 75  GLU E OE1 1 
ATOM   8359  O OE2 . GLU E 1 68  ? 10.199  -41.939 -17.907 1.00 147.99 ? 75  GLU E OE2 1 
ATOM   8360  N N   . CYS E 1 69  ? 14.485  -36.837 -18.193 1.00 143.32 ? 76  CYS E N   1 
ATOM   8361  C CA  . CYS E 1 69  ? 15.026  -35.481 -18.163 1.00 134.08 ? 76  CYS E CA  1 
ATOM   8362  C C   . CYS E 1 69  ? 15.904  -35.188 -19.377 1.00 124.75 ? 76  CYS E C   1 
ATOM   8363  O O   . CYS E 1 69  ? 16.581  -34.160 -19.428 1.00 118.39 ? 76  CYS E O   1 
ATOM   8364  C CB  . CYS E 1 69  ? 15.826  -35.242 -16.874 1.00 117.00 ? 76  CYS E CB  1 
ATOM   8365  S SG  . CYS E 1 69  ? 14.836  -34.910 -15.385 1.00 150.99 ? 76  CYS E SG  1 
ATOM   8366  N N   . ASP E 1 70  ? 15.891  -36.087 -20.354 1.00 153.95 ? 77  ASP E N   1 
ATOM   8367  C CA  . ASP E 1 70  ? 16.711  -35.924 -21.551 1.00 143.14 ? 77  ASP E CA  1 
ATOM   8368  C C   . ASP E 1 70  ? 16.335  -34.665 -22.319 1.00 145.53 ? 77  ASP E C   1 
ATOM   8369  O O   . ASP E 1 70  ? 17.143  -34.118 -23.072 1.00 134.24 ? 77  ASP E O   1 
ATOM   8370  C CB  . ASP E 1 70  ? 16.563  -37.138 -22.470 1.00 153.35 ? 77  ASP E CB  1 
ATOM   8371  C CG  . ASP E 1 70  ? 17.047  -38.418 -21.828 1.00 148.83 ? 77  ASP E CG  1 
ATOM   8372  O OD1 . ASP E 1 70  ? 17.123  -38.463 -20.583 1.00 146.42 ? 77  ASP E OD1 1 
ATOM   8373  O OD2 . ASP E 1 70  ? 17.350  -39.380 -22.566 1.00 149.04 ? 77  ASP E OD2 1 
ATOM   8374  N N   . ARG E 1 71  ? 15.104  -34.208 -22.119 1.00 119.95 ? 78  ARG E N   1 
ATOM   8375  C CA  . ARG E 1 71  ? 14.550  -33.132 -22.928 1.00 140.63 ? 78  ARG E CA  1 
ATOM   8376  C C   . ARG E 1 71  ? 14.986  -31.731 -22.490 1.00 130.51 ? 78  ARG E C   1 
ATOM   8377  O O   . ARG E 1 71  ? 14.706  -30.746 -23.173 1.00 133.87 ? 78  ARG E O   1 
ATOM   8378  C CB  . ARG E 1 71  ? 13.022  -33.226 -22.954 1.00 174.85 ? 78  ARG E CB  1 
ATOM   8379  C CG  . ARG E 1 71  ? 12.365  -32.409 -24.055 1.00 198.21 ? 78  ARG E CG  1 
ATOM   8380  C CD  . ARG E 1 71  ? 12.897  -32.787 -25.437 1.00 200.59 ? 78  ARG E CD  1 
ATOM   8381  N NE  . ARG E 1 71  ? 14.297  -32.407 -25.620 1.00 179.69 ? 78  ARG E NE  1 
ATOM   8382  C CZ  . ARG E 1 71  ? 14.982  -32.572 -26.747 1.00 173.70 ? 78  ARG E CZ  1 
ATOM   8383  N NH1 . ARG E 1 71  ? 14.397  -33.110 -27.810 1.00 183.98 ? 78  ARG E NH1 1 
ATOM   8384  N NH2 . ARG E 1 71  ? 16.253  -32.195 -26.812 1.00 158.56 ? 78  ARG E NH2 1 
ATOM   8385  N N   . LEU E 1 72  ? 15.678  -31.642 -21.360 1.00 120.42 ? 79  LEU E N   1 
ATOM   8386  C CA  . LEU E 1 72  ? 16.034  -30.341 -20.800 1.00 112.75 ? 79  LEU E CA  1 
ATOM   8387  C C   . LEU E 1 72  ? 17.056  -29.566 -21.641 1.00 109.33 ? 79  LEU E C   1 
ATOM   8388  O O   . LEU E 1 72  ? 17.874  -30.152 -22.354 1.00 101.54 ? 79  LEU E O   1 
ATOM   8389  C CB  . LEU E 1 72  ? 16.501  -30.485 -19.346 1.00 93.53  ? 79  LEU E CB  1 
ATOM   8390  C CG  . LEU E 1 72  ? 15.420  -30.978 -18.376 1.00 98.62  ? 79  LEU E CG  1 
ATOM   8391  C CD1 . LEU E 1 72  ? 15.942  -31.060 -16.950 1.00 86.80  ? 79  LEU E CD1 1 
ATOM   8392  C CD2 . LEU E 1 72  ? 14.187  -30.089 -18.444 1.00 111.75 ? 79  LEU E CD2 1 
ATOM   8393  N N   . LEU E 1 73  ? 16.983  -28.239 -21.552 1.00 181.25 ? 80  LEU E N   1 
ATOM   8394  C CA  . LEU E 1 73  ? 17.872  -27.346 -22.293 1.00 180.65 ? 80  LEU E CA  1 
ATOM   8395  C C   . LEU E 1 73  ? 19.198  -27.162 -21.568 1.00 172.38 ? 80  LEU E C   1 
ATOM   8396  O O   . LEU E 1 73  ? 19.241  -26.641 -20.456 1.00 165.89 ? 80  LEU E O   1 
ATOM   8397  C CB  . LEU E 1 73  ? 17.204  -25.985 -22.505 1.00 182.75 ? 80  LEU E CB  1 
ATOM   8398  C CG  . LEU E 1 73  ? 18.103  -24.843 -22.989 1.00 177.86 ? 80  LEU E CG  1 
ATOM   8399  C CD1 . LEU E 1 73  ? 18.768  -25.193 -24.312 1.00 184.74 ? 80  LEU E CD1 1 
ATOM   8400  C CD2 . LEU E 1 73  ? 17.312  -23.549 -23.111 1.00 181.22 ? 80  LEU E CD2 1 
ATOM   8401  N N   . SER E 1 74  ? 20.281  -27.577 -22.215 1.00 127.77 ? 81  SER E N   1 
ATOM   8402  C CA  . SER E 1 74  ? 21.599  -27.580 -21.591 1.00 121.90 ? 81  SER E CA  1 
ATOM   8403  C C   . SER E 1 74  ? 22.339  -26.250 -21.721 1.00 120.27 ? 81  SER E C   1 
ATOM   8404  O O   . SER E 1 74  ? 23.481  -26.223 -22.178 1.00 128.67 ? 81  SER E O   1 
ATOM   8405  C CB  . SER E 1 74  ? 22.457  -28.691 -22.200 1.00 122.99 ? 81  SER E CB  1 
ATOM   8406  O OG  . SER E 1 74  ? 21.714  -29.889 -22.337 1.00 121.97 ? 81  SER E OG  1 
ATOM   8407  N N   . VAL E 1 75  A 21.702  -25.154 -21.318 1.00 152.07 ? 81  VAL E N   1 
ATOM   8408  C CA  . VAL E 1 75  A 22.361  -23.849 -21.341 1.00 147.87 ? 81  VAL E CA  1 
ATOM   8409  C C   . VAL E 1 75  A 23.647  -23.873 -20.515 1.00 145.04 ? 81  VAL E C   1 
ATOM   8410  O O   . VAL E 1 75  A 23.632  -24.267 -19.352 1.00 142.68 ? 81  VAL E O   1 
ATOM   8411  C CB  . VAL E 1 75  A 21.434  -22.721 -20.841 1.00 104.47 ? 81  VAL E CB  1 
ATOM   8412  C CG1 . VAL E 1 75  A 20.577  -22.192 -21.980 1.00 109.51 ? 81  VAL E CG1 1 
ATOM   8413  C CG2 . VAL E 1 75  A 20.564  -23.211 -19.697 1.00 99.85  ? 81  VAL E CG2 1 
ATOM   8414  N N   . PRO E 1 76  ? 24.771  -23.465 -21.127 1.00 92.41  ? 82  PRO E N   1 
ATOM   8415  C CA  . PRO E 1 76  ? 26.105  -23.511 -20.509 1.00 97.63  ? 82  PRO E CA  1 
ATOM   8416  C C   . PRO E 1 76  ? 26.310  -22.456 -19.420 1.00 93.12  ? 82  PRO E C   1 
ATOM   8417  O O   . PRO E 1 76  ? 27.244  -22.563 -18.621 1.00 94.32  ? 82  PRO E O   1 
ATOM   8418  C CB  . PRO E 1 76  ? 27.048  -23.236 -21.689 1.00 112.70 ? 82  PRO E CB  1 
ATOM   8419  C CG  . PRO E 1 76  ? 26.228  -23.494 -22.922 1.00 110.10 ? 82  PRO E CG  1 
ATOM   8420  C CD  . PRO E 1 76  ? 24.842  -23.084 -22.546 1.00 97.69  ? 82  PRO E CD  1 
ATOM   8421  N N   . GLU E 1 77  ? 25.445  -21.447 -19.403 1.00 138.91 ? 83  GLU E N   1 
ATOM   8422  C CA  . GLU E 1 77  ? 25.515  -20.373 -18.418 1.00 135.32 ? 83  GLU E CA  1 
ATOM   8423  C C   . GLU E 1 77  ? 24.105  -19.961 -18.005 1.00 120.51 ? 83  GLU E C   1 
ATOM   8424  O O   . GLU E 1 77  ? 23.214  -19.841 -18.847 1.00 121.10 ? 83  GLU E O   1 
ATOM   8425  C CB  . GLU E 1 77  ? 26.270  -19.171 -18.992 1.00 146.66 ? 83  GLU E CB  1 
ATOM   8426  C CG  . GLU E 1 77  ? 26.269  -17.938 -18.097 1.00 145.74 ? 83  GLU E CG  1 
ATOM   8427  C CD  . GLU E 1 77  ? 26.955  -16.737 -18.738 1.00 157.26 ? 83  GLU E CD  1 
ATOM   8428  O OE1 . GLU E 1 77  ? 27.767  -16.932 -19.667 1.00 161.90 ? 83  GLU E OE1 1 
ATOM   8429  O OE2 . GLU E 1 77  ? 26.677  -15.596 -18.312 1.00 159.02 ? 83  GLU E OE2 1 
ATOM   8430  N N   . TRP E 1 78  ? 23.900  -19.753 -16.710 1.00 119.24 ? 84  TRP E N   1 
ATOM   8431  C CA  . TRP E 1 78  ? 22.594  -19.338 -16.219 1.00 100.24 ? 84  TRP E CA  1 
ATOM   8432  C C   . TRP E 1 78  ? 22.704  -18.544 -14.923 1.00 88.85  ? 84  TRP E C   1 
ATOM   8433  O O   . TRP E 1 78  ? 23.732  -18.589 -14.242 1.00 84.58  ? 84  TRP E O   1 
ATOM   8434  C CB  . TRP E 1 78  ? 21.686  -20.545 -16.020 1.00 95.60  ? 84  TRP E CB  1 
ATOM   8435  C CG  . TRP E 1 78  ? 22.241  -21.540 -15.068 1.00 92.76  ? 84  TRP E CG  1 
ATOM   8436  C CD1 . TRP E 1 78  ? 22.298  -21.430 -13.712 1.00 90.39  ? 84  TRP E CD1 1 
ATOM   8437  C CD2 . TRP E 1 78  ? 22.819  -22.805 -15.393 1.00 96.89  ? 84  TRP E CD2 1 
ATOM   8438  N NE1 . TRP E 1 78  ? 22.879  -22.546 -13.171 1.00 87.05  ? 84  TRP E NE1 1 
ATOM   8439  C CE2 . TRP E 1 78  ? 23.208  -23.408 -14.183 1.00 91.89  ? 84  TRP E CE2 1 
ATOM   8440  C CE3 . TRP E 1 78  ? 23.047  -23.488 -16.590 1.00 108.51 ? 84  TRP E CE3 1 
ATOM   8441  C CZ2 . TRP E 1 78  ? 23.814  -24.662 -14.134 1.00 98.25  ? 84  TRP E CZ2 1 
ATOM   8442  C CZ3 . TRP E 1 78  ? 23.646  -24.735 -16.539 1.00 113.19 ? 84  TRP E CZ3 1 
ATOM   8443  C CH2 . TRP E 1 78  ? 24.022  -25.309 -15.321 1.00 108.39 ? 84  TRP E CH2 1 
ATOM   8444  N N   . SER E 1 79  ? 21.627  -17.832 -14.589 1.00 108.23 ? 85  SER E N   1 
ATOM   8445  C CA  . SER E 1 79  ? 21.607  -16.897 -13.462 1.00 107.57 ? 85  SER E CA  1 
ATOM   8446  C C   . SER E 1 79  ? 20.892  -17.452 -12.229 1.00 109.96 ? 85  SER E C   1 
ATOM   8447  O O   . SER E 1 79  ? 21.190  -17.054 -11.102 1.00 100.11 ? 85  SER E O   1 
ATOM   8448  C CB  . SER E 1 79  ? 20.944  -15.584 -13.881 1.00 104.43 ? 85  SER E CB  1 
ATOM   8449  O OG  . SER E 1 79  ? 19.570  -15.785 -14.172 1.00 105.42 ? 85  SER E OG  1 
ATOM   8450  N N   . TYR E 1 80  ? 19.935  -18.351 -12.450 1.00 80.30  ? 86  TYR E N   1 
ATOM   8451  C CA  . TYR E 1 80  ? 19.239  -19.017 -11.349 1.00 76.78  ? 86  TYR E CA  1 
ATOM   8452  C C   . TYR E 1 80  ? 18.519  -20.280 -11.825 1.00 85.76  ? 86  TYR E C   1 
ATOM   8453  O O   . TYR E 1 80  ? 18.643  -20.666 -12.987 1.00 99.45  ? 86  TYR E O   1 
ATOM   8454  C CB  . TYR E 1 80  ? 18.265  -18.058 -10.656 1.00 74.90  ? 86  TYR E CB  1 
ATOM   8455  C CG  . TYR E 1 80  ? 17.051  -17.677 -11.476 1.00 75.81  ? 86  TYR E CG  1 
ATOM   8456  C CD1 . TYR E 1 80  ? 15.794  -18.169 -11.154 1.00 79.18  ? 86  TYR E CD1 1 
ATOM   8457  C CD2 . TYR E 1 80  ? 17.160  -16.817 -12.564 1.00 74.44  ? 86  TYR E CD2 1 
ATOM   8458  C CE1 . TYR E 1 80  ? 14.680  -17.822 -11.888 1.00 89.37  ? 86  TYR E CE1 1 
ATOM   8459  C CE2 . TYR E 1 80  ? 16.046  -16.463 -13.306 1.00 84.46  ? 86  TYR E CE2 1 
ATOM   8460  C CZ  . TYR E 1 80  ? 14.809  -16.971 -12.960 1.00 96.57  ? 86  TYR E CZ  1 
ATOM   8461  O OH  . TYR E 1 80  ? 13.692  -16.633 -13.687 1.00 119.66 ? 86  TYR E OH  1 
ATOM   8462  N N   . ILE E 1 81  ? 17.772  -20.922 -10.930 1.00 71.14  ? 87  ILE E N   1 
ATOM   8463  C CA  . ILE E 1 81  ? 17.091  -22.169 -11.261 1.00 76.08  ? 87  ILE E CA  1 
ATOM   8464  C C   . ILE E 1 81  ? 15.623  -22.187 -10.850 1.00 93.63  ? 87  ILE E C   1 
ATOM   8465  O O   . ILE E 1 81  ? 15.257  -21.702 -9.782  1.00 99.03  ? 87  ILE E O   1 
ATOM   8466  C CB  . ILE E 1 81  ? 17.778  -23.379 -10.601 1.00 69.29  ? 87  ILE E CB  1 
ATOM   8467  C CG1 . ILE E 1 81  ? 19.247  -23.470 -11.024 1.00 59.53  ? 87  ILE E CG1 1 
ATOM   8468  C CG2 . ILE E 1 81  ? 17.037  -24.676 -10.933 1.00 80.00  ? 87  ILE E CG2 1 
ATOM   8469  C CD1 . ILE E 1 81  ? 19.939  -24.728 -10.515 1.00 58.00  ? 87  ILE E CD1 1 
ATOM   8470  N N   . MET E 1 82  ? 14.797  -22.779 -11.706 1.00 53.80  ? 88  MET E N   1 
ATOM   8471  C CA  . MET E 1 82  ? 13.377  -22.968 -11.436 1.00 79.70  ? 88  MET E CA  1 
ATOM   8472  C C   . MET E 1 82  ? 13.121  -24.463 -11.218 1.00 86.80  ? 88  MET E C   1 
ATOM   8473  O O   . MET E 1 82  ? 13.733  -25.296 -11.885 1.00 92.14  ? 88  MET E O   1 
ATOM   8474  C CB  . MET E 1 82  ? 12.562  -22.429 -12.615 1.00 97.46  ? 88  MET E CB  1 
ATOM   8475  C CG  . MET E 1 82  ? 13.006  -21.025 -13.051 1.00 92.17  ? 88  MET E CG  1 
ATOM   8476  S SD  . MET E 1 82  ? 12.325  -20.436 -14.618 1.00 100.61 ? 88  MET E SD  1 
ATOM   8477  C CE  . MET E 1 82  ? 10.604  -20.909 -14.413 1.00 86.68  ? 88  MET E CE  1 
ATOM   8478  N N   . GLU E 1 83  ? 12.238  -24.804 -10.280 1.00 98.65  ? 89  GLU E N   1 
ATOM   8479  C CA  . GLU E 1 83  ? 12.020  -26.205 -9.901  1.00 102.02 ? 89  GLU E CA  1 
ATOM   8480  C C   . GLU E 1 83  ? 10.804  -26.377 -8.998  1.00 101.77 ? 89  GLU E C   1 
ATOM   8481  O O   . GLU E 1 83  ? 10.743  -25.798 -7.918  1.00 101.75 ? 89  GLU E O   1 
ATOM   8482  C CB  . GLU E 1 83  ? 13.259  -26.765 -9.192  1.00 91.96  ? 89  GLU E CB  1 
ATOM   8483  C CG  . GLU E 1 83  ? 13.040  -28.115 -8.511  1.00 92.01  ? 89  GLU E CG  1 
ATOM   8484  C CD  . GLU E 1 83  ? 14.148  -28.468 -7.519  1.00 78.88  ? 89  GLU E CD  1 
ATOM   8485  O OE1 . GLU E 1 83  ? 15.313  -28.653 -7.949  1.00 76.57  ? 89  GLU E OE1 1 
ATOM   8486  O OE2 . GLU E 1 83  ? 13.847  -28.555 -6.303  1.00 63.03  ? 89  GLU E OE2 1 
ATOM   8487  N N   . LYS E 1 84  ? 9.844   -27.187 -9.435  1.00 90.84  ? 90  LYS E N   1 
ATOM   8488  C CA  . LYS E 1 84  ? 8.625   -27.424 -8.664  1.00 91.14  ? 90  LYS E CA  1 
ATOM   8489  C C   . LYS E 1 84  ? 8.919   -27.782 -7.207  1.00 83.40  ? 90  LYS E C   1 
ATOM   8490  O O   . LYS E 1 84  ? 10.026  -28.206 -6.870  1.00 80.92  ? 90  LYS E O   1 
ATOM   8491  C CB  . LYS E 1 84  ? 7.789   -28.534 -9.308  1.00 101.64 ? 90  LYS E CB  1 
ATOM   8492  C CG  . LYS E 1 84  ? 7.445   -28.300 -10.770 1.00 114.36 ? 90  LYS E CG  1 
ATOM   8493  C CD  . LYS E 1 84  ? 6.717   -29.497 -11.356 1.00 124.08 ? 90  LYS E CD  1 
ATOM   8494  C CE  . LYS E 1 84  ? 6.435   -29.310 -12.835 1.00 136.38 ? 90  LYS E CE  1 
ATOM   8495  N NZ  . LYS E 1 84  ? 5.513   -28.174 -13.079 1.00 139.13 ? 90  LYS E NZ  1 
ATOM   8496  N N   . GLU E 1 85  ? 7.920   -27.613 -6.346  1.00 102.13 ? 91  GLU E N   1 
ATOM   8497  C CA  . GLU E 1 85  ? 8.060   -27.957 -4.936  1.00 99.76  ? 91  GLU E CA  1 
ATOM   8498  C C   . GLU E 1 85  ? 8.302   -29.455 -4.770  1.00 104.27 ? 91  GLU E C   1 
ATOM   8499  O O   . GLU E 1 85  ? 9.272   -29.863 -4.132  1.00 107.20 ? 91  GLU E O   1 
ATOM   8500  C CB  . GLU E 1 85  ? 6.814   -27.537 -4.156  1.00 98.04  ? 91  GLU E CB  1 
ATOM   8501  C CG  . GLU E 1 85  ? 6.950   -27.667 -2.648  1.00 94.38  ? 91  GLU E CG  1 
ATOM   8502  C CD  . GLU E 1 85  ? 7.811   -26.575 -2.036  1.00 100.07 ? 91  GLU E CD  1 
ATOM   8503  O OE1 . GLU E 1 85  ? 8.086   -25.568 -2.724  1.00 101.74 ? 91  GLU E OE1 1 
ATOM   8504  O OE2 . GLU E 1 85  ? 8.209   -26.721 -0.862  1.00 102.00 ? 91  GLU E OE2 1 
ATOM   8505  N N   . ASN E 1 86  ? 7.416   -30.264 -5.351  1.00 94.28  ? 92  ASN E N   1 
ATOM   8506  C CA  . ASN E 1 86  ? 7.518   -31.725 -5.300  1.00 93.88  ? 92  ASN E CA  1 
ATOM   8507  C C   . ASN E 1 86  ? 7.535   -32.381 -6.684  1.00 99.79  ? 92  ASN E C   1 
ATOM   8508  O O   . ASN E 1 86  ? 6.534   -32.959 -7.110  1.00 104.85 ? 92  ASN E O   1 
ATOM   8509  C CB  . ASN E 1 86  ? 6.370   -32.320 -4.475  1.00 94.04  ? 92  ASN E CB  1 
ATOM   8510  C CG  . ASN E 1 86  ? 6.496   -32.025 -2.989  1.00 91.80  ? 92  ASN E CG  1 
ATOM   8511  O OD1 . ASN E 1 86  ? 7.264   -31.154 -2.577  1.00 88.10  ? 92  ASN E OD1 1 
ATOM   8512  N ND2 . ASN E 1 86  ? 5.735   -32.750 -2.177  1.00 91.75  ? 92  ASN E ND2 1 
ATOM   8513  N N   . PRO E 1 87  ? 8.677   -32.291 -7.389  1.00 99.62  ? 93  PRO E N   1 
ATOM   8514  C CA  . PRO E 1 87  ? 8.864   -32.929 -8.699  1.00 107.87 ? 93  PRO E CA  1 
ATOM   8515  C C   . PRO E 1 87  ? 8.619   -34.436 -8.649  1.00 116.99 ? 93  PRO E C   1 
ATOM   8516  O O   . PRO E 1 87  ? 8.521   -35.006 -7.560  1.00 113.52 ? 93  PRO E O   1 
ATOM   8517  C CB  . PRO E 1 87  ? 10.339  -32.659 -9.010  1.00 99.37  ? 93  PRO E CB  1 
ATOM   8518  C CG  . PRO E 1 87  ? 10.655  -31.421 -8.266  1.00 93.25  ? 93  PRO E CG  1 
ATOM   8519  C CD  . PRO E 1 87  ? 9.848   -31.488 -6.999  1.00 91.01  ? 93  PRO E CD  1 
ATOM   8520  N N   . ARG E 1 88  ? 8.530   -35.065 -9.819  1.00 139.14 ? 94  ARG E N   1 
ATOM   8521  C CA  . ARG E 1 88  ? 8.288   -36.503 -9.920  1.00 141.25 ? 94  ARG E CA  1 
ATOM   8522  C C   . ARG E 1 88  ? 9.495   -37.209 -10.525 1.00 134.98 ? 94  ARG E C   1 
ATOM   8523  O O   . ARG E 1 88  ? 9.753   -38.379 -10.236 1.00 123.85 ? 94  ARG E O   1 
ATOM   8524  C CB  . ARG E 1 88  ? 7.052   -36.774 -10.786 1.00 155.79 ? 94  ARG E CB  1 
ATOM   8525  C CG  . ARG E 1 88  ? 6.656   -38.244 -10.879 1.00 161.88 ? 94  ARG E CG  1 
ATOM   8526  C CD  . ARG E 1 88  ? 6.046   -38.599 -12.238 1.00 171.40 ? 94  ARG E CD  1 
ATOM   8527  N NE  . ARG E 1 88  ? 4.926   -37.735 -12.609 1.00 173.42 ? 94  ARG E NE  1 
ATOM   8528  C CZ  . ARG E 1 88  ? 4.062   -38.006 -13.584 1.00 177.08 ? 94  ARG E CZ  1 
ATOM   8529  N NH1 . ARG E 1 88  ? 4.178   -39.126 -14.286 1.00 179.82 ? 94  ARG E NH1 1 
ATOM   8530  N NH2 . ARG E 1 88  ? 3.076   -37.162 -13.854 1.00 180.09 ? 94  ARG E NH2 1 
ATOM   8531  N N   . ASP E 1 89  ? 10.233  -36.487 -11.363 1.00 115.01 ? 95  ASP E N   1 
ATOM   8532  C CA  . ASP E 1 89  ? 11.340  -37.067 -12.121 1.00 122.78 ? 95  ASP E CA  1 
ATOM   8533  C C   . ASP E 1 89  ? 12.695  -36.903 -11.433 1.00 117.50 ? 95  ASP E C   1 
ATOM   8534  O O   . ASP E 1 89  ? 13.609  -36.282 -11.980 1.00 119.48 ? 95  ASP E O   1 
ATOM   8535  C CB  . ASP E 1 89  ? 11.397  -36.466 -13.528 1.00 133.33 ? 95  ASP E CB  1 
ATOM   8536  C CG  . ASP E 1 89  ? 10.110  -36.675 -14.303 1.00 145.65 ? 95  ASP E CG  1 
ATOM   8537  O OD1 . ASP E 1 89  ? 9.372   -37.632 -13.984 1.00 148.50 ? 95  ASP E OD1 1 
ATOM   8538  O OD2 . ASP E 1 89  ? 9.837   -35.885 -15.232 1.00 151.33 ? 95  ASP E OD2 1 
ATOM   8539  N N   . GLY E 1 90  A 12.820  -37.473 -10.240 1.00 120.85 ? 95  GLY E N   1 
ATOM   8540  C CA  . GLY E 1 90  A 14.066  -37.421 -9.500  1.00 109.10 ? 95  GLY E CA  1 
ATOM   8541  C C   . GLY E 1 90  A 14.782  -38.756 -9.499  1.00 106.65 ? 95  GLY E C   1 
ATOM   8542  O O   . GLY E 1 90  A 15.464  -39.110 -10.462 1.00 99.76  ? 95  GLY E O   1 
ATOM   8543  N N   . LEU E 1 91  ? 14.627  -39.502 -8.411  1.00 129.67 ? 96  LEU E N   1 
ATOM   8544  C CA  . LEU E 1 91  ? 15.255  -40.812 -8.290  1.00 128.86 ? 96  LEU E CA  1 
ATOM   8545  C C   . LEU E 1 91  ? 14.275  -41.928 -8.627  1.00 137.32 ? 96  LEU E C   1 
ATOM   8546  O O   . LEU E 1 91  ? 13.486  -42.357 -7.782  1.00 136.03 ? 96  LEU E O   1 
ATOM   8547  C CB  . LEU E 1 91  ? 15.824  -41.009 -6.885  1.00 114.41 ? 96  LEU E CB  1 
ATOM   8548  C CG  . LEU E 1 91  ? 17.002  -40.093 -6.555  1.00 87.39  ? 96  LEU E CG  1 
ATOM   8549  C CD1 . LEU E 1 91  ? 17.436  -40.253 -5.106  1.00 74.29  ? 96  LEU E CD1 1 
ATOM   8550  C CD2 . LEU E 1 91  ? 18.159  -40.361 -7.506  1.00 75.76  ? 96  LEU E CD2 1 
ATOM   8551  N N   . CYS E 1 92  ? 14.324  -42.382 -9.875  1.00 115.39 ? 97  CYS E N   1 
ATOM   8552  C CA  . CYS E 1 92  ? 13.510  -43.504 -10.317 1.00 119.47 ? 97  CYS E CA  1 
ATOM   8553  C C   . CYS E 1 92  ? 13.887  -44.744 -9.522  1.00 117.05 ? 97  CYS E C   1 
ATOM   8554  O O   . CYS E 1 92  ? 13.026  -45.443 -8.989  1.00 116.90 ? 97  CYS E O   1 
ATOM   8555  C CB  . CYS E 1 92  ? 13.705  -43.740 -11.814 1.00 128.55 ? 97  CYS E CB  1 
ATOM   8556  S SG  . CYS E 1 92  ? 15.348  -43.292 -12.429 1.00 92.53  ? 97  CYS E SG  1 
ATOM   8557  N N   . TYR E 1 93  ? 15.186  -45.007 -9.442  1.00 141.67 ? 98  TYR E N   1 
ATOM   8558  C CA  . TYR E 1 93  ? 15.695  -46.056 -8.577  1.00 132.98 ? 98  TYR E CA  1 
ATOM   8559  C C   . TYR E 1 93  ? 15.908  -45.455 -7.199  1.00 120.44 ? 98  TYR E C   1 
ATOM   8560  O O   . TYR E 1 93  ? 16.785  -44.614 -7.020  1.00 111.79 ? 98  TYR E O   1 
ATOM   8561  C CB  . TYR E 1 93  ? 17.015  -46.607 -9.115  1.00 127.41 ? 98  TYR E CB  1 
ATOM   8562  C CG  . TYR E 1 93  ? 17.444  -47.881 -8.429  1.00 130.01 ? 98  TYR E CG  1 
ATOM   8563  C CD1 . TYR E 1 93  ? 17.363  -49.103 -9.079  1.00 132.13 ? 98  TYR E CD1 1 
ATOM   8564  C CD2 . TYR E 1 93  ? 17.907  -47.864 -7.123  1.00 130.99 ? 98  TYR E CD2 1 
ATOM   8565  C CE1 . TYR E 1 93  ? 17.743  -50.271 -8.451  1.00 134.34 ? 98  TYR E CE1 1 
ATOM   8566  C CE2 . TYR E 1 93  ? 18.288  -49.026 -6.486  1.00 131.51 ? 98  TYR E CE2 1 
ATOM   8567  C CZ  . TYR E 1 93  ? 18.204  -50.225 -7.154  1.00 134.02 ? 98  TYR E CZ  1 
ATOM   8568  O OH  . TYR E 1 93  ? 18.583  -51.383 -6.519  1.00 134.62 ? 98  TYR E OH  1 
ATOM   8569  N N   . PRO E 1 94  ? 15.108  -45.883 -6.215  1.00 110.46 ? 99  PRO E N   1 
ATOM   8570  C CA  . PRO E 1 94  ? 15.142  -45.292 -4.872  1.00 108.55 ? 99  PRO E CA  1 
ATOM   8571  C C   . PRO E 1 94  ? 16.560  -45.178 -4.323  1.00 106.19 ? 99  PRO E C   1 
ATOM   8572  O O   . PRO E 1 94  ? 17.441  -45.944 -4.716  1.00 106.91 ? 99  PRO E O   1 
ATOM   8573  C CB  . PRO E 1 94  ? 14.318  -46.274 -4.030  1.00 107.06 ? 99  PRO E CB  1 
ATOM   8574  C CG  . PRO E 1 94  ? 14.242  -47.525 -4.843  1.00 112.37 ? 99  PRO E CG  1 
ATOM   8575  C CD  . PRO E 1 94  ? 14.245  -47.070 -6.267  1.00 114.82 ? 99  PRO E CD  1 
ATOM   8576  N N   . GLY E 1 95  ? 16.780  -44.223 -3.427  1.00 114.95 ? 100 GLY E N   1 
ATOM   8577  C CA  . GLY E 1 95  ? 18.094  -44.047 -2.841  1.00 91.22  ? 100 GLY E CA  1 
ATOM   8578  C C   . GLY E 1 95  ? 18.270  -42.758 -2.064  1.00 83.41  ? 100 GLY E C   1 
ATOM   8579  O O   . GLY E 1 95  ? 17.415  -42.365 -1.267  1.00 90.03  ? 100 GLY E O   1 
ATOM   8580  N N   . SER E 1 96  ? 19.391  -42.091 -2.305  1.00 91.29  ? 101 SER E N   1 
ATOM   8581  C CA  . SER E 1 96  ? 19.763  -40.933 -1.516  1.00 76.18  ? 101 SER E CA  1 
ATOM   8582  C C   . SER E 1 96  ? 20.898  -40.157 -2.180  1.00 62.41  ? 101 SER E C   1 
ATOM   8583  O O   . SER E 1 96  ? 21.608  -40.691 -3.042  1.00 55.14  ? 101 SER E O   1 
ATOM   8584  C CB  . SER E 1 96  ? 20.192  -41.386 -0.123  1.00 77.36  ? 101 SER E CB  1 
ATOM   8585  O OG  . SER E 1 96  ? 21.281  -42.287 -0.207  1.00 77.95  ? 101 SER E OG  1 
ATOM   8586  N N   . PHE E 1 97  ? 21.078  -38.905 -1.755  1.00 67.08  ? 102 PHE E N   1 
ATOM   8587  C CA  . PHE E 1 97  ? 22.054  -38.009 -2.366  1.00 62.09  ? 102 PHE E CA  1 
ATOM   8588  C C   . PHE E 1 97  ? 22.797  -37.174 -1.326  1.00 56.02  ? 102 PHE E C   1 
ATOM   8589  O O   . PHE E 1 97  ? 22.236  -36.242 -0.751  1.00 58.35  ? 102 PHE E O   1 
ATOM   8590  C CB  . PHE E 1 97  ? 21.350  -37.087 -3.360  1.00 69.24  ? 102 PHE E CB  1 
ATOM   8591  C CG  . PHE E 1 97  ? 22.196  -36.713 -4.537  1.00 77.21  ? 102 PHE E CG  1 
ATOM   8592  C CD1 . PHE E 1 97  ? 21.647  -36.634 -5.806  1.00 76.39  ? 102 PHE E CD1 1 
ATOM   8593  C CD2 . PHE E 1 97  ? 23.545  -36.443 -4.376  1.00 83.18  ? 102 PHE E CD2 1 
ATOM   8594  C CE1 . PHE E 1 97  ? 22.427  -36.296 -6.892  1.00 73.74  ? 102 PHE E CE1 1 
ATOM   8595  C CE2 . PHE E 1 97  ? 24.333  -36.100 -5.461  1.00 85.77  ? 102 PHE E CE2 1 
ATOM   8596  C CZ  . PHE E 1 97  ? 23.774  -36.028 -6.721  1.00 80.02  ? 102 PHE E CZ  1 
ATOM   8597  N N   . ASN E 1 98  ? 24.066  -37.494 -1.101  1.00 46.57  ? 103 ASN E N   1 
ATOM   8598  C CA  . ASN E 1 98  ? 24.843  -36.842 -0.050  1.00 46.51  ? 103 ASN E CA  1 
ATOM   8599  C C   . ASN E 1 98  ? 25.277  -35.421 -0.363  1.00 49.71  ? 103 ASN E C   1 
ATOM   8600  O O   . ASN E 1 98  ? 25.728  -35.132 -1.468  1.00 59.12  ? 103 ASN E O   1 
ATOM   8601  C CB  . ASN E 1 98  ? 26.060  -37.685 0.299   1.00 58.87  ? 103 ASN E CB  1 
ATOM   8602  C CG  . ASN E 1 98  ? 25.678  -39.015 0.887   1.00 66.60  ? 103 ASN E CG  1 
ATOM   8603  O OD1 . ASN E 1 98  ? 24.594  -39.164 1.457   1.00 65.26  ? 103 ASN E OD1 1 
ATOM   8604  N ND2 . ASN E 1 98  ? 26.562  -39.996 0.753   1.00 74.17  ? 103 ASN E ND2 1 
ATOM   8605  N N   . ASP E 1 99  ? 25.156  -34.551 0.637   1.00 42.02  ? 104 ASP E N   1 
ATOM   8606  C CA  . ASP E 1 99  ? 25.444  -33.125 0.494   1.00 42.65  ? 104 ASP E CA  1 
ATOM   8607  C C   . ASP E 1 99  ? 24.661  -32.545 -0.675  1.00 46.76  ? 104 ASP E C   1 
ATOM   8608  O O   . ASP E 1 99  ? 25.123  -31.638 -1.366  1.00 60.42  ? 104 ASP E O   1 
ATOM   8609  C CB  . ASP E 1 99  ? 26.941  -32.882 0.324   1.00 61.22  ? 104 ASP E CB  1 
ATOM   8610  C CG  . ASP E 1 99  ? 27.738  -33.331 1.525   1.00 80.39  ? 104 ASP E CG  1 
ATOM   8611  O OD1 . ASP E 1 99  ? 27.277  -33.116 2.663   1.00 73.45  ? 104 ASP E OD1 1 
ATOM   8612  O OD2 . ASP E 1 99  ? 28.826  -33.907 1.329   1.00 102.41 ? 104 ASP E OD2 1 
ATOM   8613  N N   . TYR E 1 100 ? 23.467  -33.091 -0.881  1.00 42.46  ? 105 TYR E N   1 
ATOM   8614  C CA  . TYR E 1 100 ? 22.569  -32.655 -1.942  1.00 44.10  ? 105 TYR E CA  1 
ATOM   8615  C C   . TYR E 1 100 ? 22.292  -31.165 -1.820  1.00 49.31  ? 105 TYR E C   1 
ATOM   8616  O O   . TYR E 1 100 ? 22.434  -30.417 -2.787  1.00 56.07  ? 105 TYR E O   1 
ATOM   8617  C CB  . TYR E 1 100 ? 21.265  -33.443 -1.850  1.00 51.62  ? 105 TYR E CB  1 
ATOM   8618  C CG  . TYR E 1 100 ? 20.266  -33.168 -2.948  1.00 52.21  ? 105 TYR E CG  1 
ATOM   8619  C CD1 . TYR E 1 100 ? 20.658  -33.123 -4.278  1.00 49.52  ? 105 TYR E CD1 1 
ATOM   8620  C CD2 . TYR E 1 100 ? 18.919  -32.992 -2.654  1.00 61.20  ? 105 TYR E CD2 1 
ATOM   8621  C CE1 . TYR E 1 100 ? 19.738  -32.884 -5.282  1.00 57.53  ? 105 TYR E CE1 1 
ATOM   8622  C CE2 . TYR E 1 100 ? 17.994  -32.757 -3.650  1.00 74.38  ? 105 TYR E CE2 1 
ATOM   8623  C CZ  . TYR E 1 100 ? 18.409  -32.704 -4.962  1.00 70.79  ? 105 TYR E CZ  1 
ATOM   8624  O OH  . TYR E 1 100 ? 17.488  -32.465 -5.956  1.00 82.45  ? 105 TYR E OH  1 
ATOM   8625  N N   . GLU E 1 101 ? 21.903  -30.730 -0.626  1.00 48.46  ? 106 GLU E N   1 
ATOM   8626  C CA  . GLU E 1 101 ? 21.630  -29.319 -0.415  1.00 43.52  ? 106 GLU E CA  1 
ATOM   8627  C C   . GLU E 1 101 ? 22.819  -28.458 -0.840  1.00 43.18  ? 106 GLU E C   1 
ATOM   8628  O O   . GLU E 1 101 ? 22.689  -27.608 -1.721  1.00 40.29  ? 106 GLU E O   1 
ATOM   8629  C CB  . GLU E 1 101 ? 21.226  -29.037 1.034   1.00 39.15  ? 106 GLU E CB  1 
ATOM   8630  C CG  . GLU E 1 101 ? 19.740  -29.248 1.316   1.00 43.45  ? 106 GLU E CG  1 
ATOM   8631  C CD  . GLU E 1 101 ? 19.368  -30.714 1.502   1.00 58.49  ? 106 GLU E CD  1 
ATOM   8632  O OE1 . GLU E 1 101 ? 20.281  -31.565 1.619   1.00 51.62  ? 106 GLU E OE1 1 
ATOM   8633  O OE2 . GLU E 1 101 ? 18.154  -31.007 1.533   1.00 74.87  ? 106 GLU E OE2 1 
ATOM   8634  N N   . GLU E 1 102 ? 23.976  -28.683 -0.227  1.00 48.64  ? 107 GLU E N   1 
ATOM   8635  C CA  . GLU E 1 102 ? 25.174  -27.930 -0.594  1.00 51.25  ? 107 GLU E CA  1 
ATOM   8636  C C   . GLU E 1 102 ? 25.368  -27.941 -2.105  1.00 60.96  ? 107 GLU E C   1 
ATOM   8637  O O   . GLU E 1 102 ? 25.747  -26.934 -2.695  1.00 68.62  ? 107 GLU E O   1 
ATOM   8638  C CB  . GLU E 1 102 ? 26.410  -28.502 0.098   1.00 54.61  ? 107 GLU E CB  1 
ATOM   8639  C CG  . GLU E 1 102 ? 26.554  -28.083 1.542   1.00 59.99  ? 107 GLU E CG  1 
ATOM   8640  C CD  . GLU E 1 102 ? 26.994  -26.643 1.678   1.00 64.26  ? 107 GLU E CD  1 
ATOM   8641  O OE1 . GLU E 1 102 ? 28.010  -26.273 1.051   1.00 73.93  ? 107 GLU E OE1 1 
ATOM   8642  O OE2 . GLU E 1 102 ? 26.321  -25.881 2.409   1.00 60.78  ? 107 GLU E OE2 1 
ATOM   8643  N N   . LEU E 1 103 ? 25.094  -29.086 -2.725  1.00 61.02  ? 108 LEU E N   1 
ATOM   8644  C CA  . LEU E 1 103 ? 25.194  -29.223 -4.174  1.00 62.95  ? 108 LEU E CA  1 
ATOM   8645  C C   . LEU E 1 103 ? 24.202  -28.305 -4.894  1.00 61.62  ? 108 LEU E C   1 
ATOM   8646  O O   . LEU E 1 103 ? 24.606  -27.455 -5.690  1.00 70.72  ? 108 LEU E O   1 
ATOM   8647  C CB  . LEU E 1 103 ? 24.988  -30.681 -4.593  1.00 62.17  ? 108 LEU E CB  1 
ATOM   8648  C CG  . LEU E 1 103 ? 25.246  -31.064 -6.052  1.00 64.04  ? 108 LEU E CG  1 
ATOM   8649  C CD1 . LEU E 1 103 ? 26.639  -30.658 -6.476  1.00 71.59  ? 108 LEU E CD1 1 
ATOM   8650  C CD2 . LEU E 1 103 ? 25.049  -32.568 -6.231  1.00 60.66  ? 108 LEU E CD2 1 
ATOM   8651  N N   . LYS E 1 104 ? 22.913  -28.470 -4.611  1.00 58.35  ? 109 LYS E N   1 
ATOM   8652  C CA  . LYS E 1 104 ? 21.901  -27.607 -5.204  1.00 54.24  ? 109 LYS E CA  1 
ATOM   8653  C C   . LYS E 1 104 ? 22.389  -26.162 -5.173  1.00 56.52  ? 109 LYS E C   1 
ATOM   8654  O O   . LYS E 1 104 ? 22.093  -25.367 -6.067  1.00 66.03  ? 109 LYS E O   1 
ATOM   8655  C CB  . LYS E 1 104 ? 20.570  -27.706 -4.449  1.00 56.47  ? 109 LYS E CB  1 
ATOM   8656  C CG  . LYS E 1 104 ? 19.808  -29.011 -4.633  1.00 68.44  ? 109 LYS E CG  1 
ATOM   8657  C CD  . LYS E 1 104 ? 18.296  -28.778 -4.723  1.00 78.12  ? 109 LYS E CD  1 
ATOM   8658  C CE  . LYS E 1 104 ? 17.728  -28.203 -3.437  1.00 77.72  ? 109 LYS E CE  1 
ATOM   8659  N NZ  . LYS E 1 104 ? 16.335  -27.694 -3.613  1.00 93.95  ? 109 LYS E NZ  1 
ATOM   8660  N N   . HIS E 1 105 ? 23.138  -25.819 -4.131  1.00 56.67  ? 110 HIS E N   1 
ATOM   8661  C CA  . HIS E 1 105 ? 23.620  -24.456 -3.961  1.00 58.90  ? 110 HIS E CA  1 
ATOM   8662  C C   . HIS E 1 105 ? 24.704  -24.153 -4.984  1.00 73.93  ? 110 HIS E C   1 
ATOM   8663  O O   . HIS E 1 105 ? 24.607  -23.181 -5.731  1.00 72.79  ? 110 HIS E O   1 
ATOM   8664  C CB  . HIS E 1 105 ? 24.161  -24.264 -2.548  1.00 48.08  ? 110 HIS E CB  1 
ATOM   8665  C CG  . HIS E 1 105 ? 24.527  -22.851 -2.225  1.00 50.83  ? 110 HIS E CG  1 
ATOM   8666  N ND1 . HIS E 1 105 ? 23.587  -21.895 -1.909  1.00 54.30  ? 110 HIS E ND1 1 
ATOM   8667  C CD2 . HIS E 1 105 ? 25.731  -22.235 -2.156  1.00 64.08  ? 110 HIS E CD2 1 
ATOM   8668  C CE1 . HIS E 1 105 ? 24.197  -20.749 -1.660  1.00 61.45  ? 110 HIS E CE1 1 
ATOM   8669  N NE2 . HIS E 1 105 ? 25.498  -20.929 -1.802  1.00 70.48  ? 110 HIS E NE2 1 
ATOM   8670  N N   . LEU E 1 106 ? 25.734  -24.994 -5.017  1.00 58.96  ? 111 LEU E N   1 
ATOM   8671  C CA  . LEU E 1 106 ? 26.839  -24.820 -5.956  1.00 63.71  ? 111 LEU E CA  1 
ATOM   8672  C C   . LEU E 1 106 ? 26.314  -24.460 -7.334  1.00 67.59  ? 111 LEU E C   1 
ATOM   8673  O O   . LEU E 1 106 ? 26.791  -23.523 -7.973  1.00 82.37  ? 111 LEU E O   1 
ATOM   8674  C CB  . LEU E 1 106 ? 27.662  -26.103 -6.058  1.00 73.18  ? 111 LEU E CB  1 
ATOM   8675  C CG  . LEU E 1 106 ? 28.871  -26.016 -6.988  1.00 90.16  ? 111 LEU E CG  1 
ATOM   8676  C CD1 . LEU E 1 106 ? 29.891  -25.058 -6.408  1.00 111.48 ? 111 LEU E CD1 1 
ATOM   8677  C CD2 . LEU E 1 106 ? 29.488  -27.384 -7.211  1.00 84.73  ? 111 LEU E CD2 1 
ATOM   8678  N N   . LEU E 1 107 ? 25.314  -25.210 -7.776  1.00 81.99  ? 112 LEU E N   1 
ATOM   8679  C CA  . LEU E 1 107 ? 24.789  -25.071 -9.124  1.00 81.03  ? 112 LEU E CA  1 
ATOM   8680  C C   . LEU E 1 107 ? 23.559  -24.174 -9.153  1.00 85.28  ? 112 LEU E C   1 
ATOM   8681  O O   . LEU E 1 107 ? 22.616  -24.426 -9.895  1.00 95.51  ? 112 LEU E O   1 
ATOM   8682  C CB  . LEU E 1 107 ? 24.457  -26.451 -9.697  1.00 75.07  ? 112 LEU E CB  1 
ATOM   8683  C CG  . LEU E 1 107 ? 25.540  -27.514 -9.469  1.00 84.91  ? 112 LEU E CG  1 
ATOM   8684  C CD1 . LEU E 1 107 ? 25.032  -28.908 -9.819  1.00 80.48  ? 112 LEU E CD1 1 
ATOM   8685  C CD2 . LEU E 1 107 ? 26.807  -27.186 -10.244 1.00 100.16 ? 112 LEU E CD2 1 
ATOM   8686  N N   . SER E 1 108 ? 23.570  -23.129 -8.333  1.00 95.19  ? 113 SER E N   1 
ATOM   8687  C CA  . SER E 1 108 ? 22.513  -22.126 -8.369  1.00 92.24  ? 113 SER E CA  1 
ATOM   8688  C C   . SER E 1 108 ? 22.867  -21.092 -9.425  1.00 102.57 ? 113 SER E C   1 
ATOM   8689  O O   . SER E 1 108 ? 22.012  -20.637 -10.189 1.00 105.66 ? 113 SER E O   1 
ATOM   8690  C CB  . SER E 1 108 ? 22.377  -21.442 -7.007  1.00 82.48  ? 113 SER E CB  1 
ATOM   8691  O OG  . SER E 1 108 ? 23.576  -20.766 -6.654  1.00 81.77  ? 113 SER E OG  1 
ATOM   8692  N N   . SER E 1 109 ? 24.145  -20.735 -9.452  1.00 90.34  ? 114 SER E N   1 
ATOM   8693  C CA  . SER E 1 109 ? 24.671  -19.762 -10.391 1.00 97.94  ? 114 SER E CA  1 
ATOM   8694  C C   . SER E 1 109 ? 26.002  -20.266 -10.918 1.00 109.94 ? 114 SER E C   1 
ATOM   8695  O O   . SER E 1 109 ? 26.820  -20.786 -10.159 1.00 115.73 ? 114 SER E O   1 
ATOM   8696  C CB  . SER E 1 109 ? 24.860  -18.406 -9.707  1.00 100.94 ? 114 SER E CB  1 
ATOM   8697  O OG  . SER E 1 109 ? 25.736  -17.574 -10.450 1.00 114.97 ? 114 SER E OG  1 
ATOM   8698  N N   . VAL E 1 110 ? 26.210  -20.114 -12.221 1.00 97.89  ? 115 VAL E N   1 
ATOM   8699  C CA  . VAL E 1 110 ? 27.440  -20.562 -12.858 1.00 106.36 ? 115 VAL E CA  1 
ATOM   8700  C C   . VAL E 1 110 ? 27.818  -19.643 -14.009 1.00 114.25 ? 115 VAL E C   1 
ATOM   8701  O O   . VAL E 1 110 ? 26.964  -19.242 -14.801 1.00 106.72 ? 115 VAL E O   1 
ATOM   8702  C CB  . VAL E 1 110 ? 27.304  -22.001 -13.405 1.00 103.17 ? 115 VAL E CB  1 
ATOM   8703  C CG1 . VAL E 1 110 ? 27.074  -22.995 -12.269 1.00 92.33  ? 115 VAL E CG1 1 
ATOM   8704  C CG2 . VAL E 1 110 ? 26.179  -22.078 -14.427 1.00 94.59  ? 115 VAL E CG2 1 
ATOM   8705  N N   . LYS E 1 111 ? 29.099  -19.302 -14.089 1.00 88.83  ? 116 LYS E N   1 
ATOM   8706  C CA  . LYS E 1 111 ? 29.619  -18.604 -15.254 1.00 106.73 ? 116 LYS E CA  1 
ATOM   8707  C C   . LYS E 1 111 ? 29.683  -19.597 -16.410 1.00 109.30 ? 116 LYS E C   1 
ATOM   8708  O O   . LYS E 1 111 ? 28.821  -19.587 -17.290 1.00 104.28 ? 116 LYS E O   1 
ATOM   8709  C CB  . LYS E 1 111 ? 31.001  -18.013 -14.973 1.00 136.27 ? 116 LYS E CB  1 
ATOM   8710  C CG  . LYS E 1 111 ? 31.536  -17.135 -16.095 1.00 154.71 ? 116 LYS E CG  1 
ATOM   8711  C CD  . LYS E 1 111 ? 30.624  -15.942 -16.346 1.00 145.15 ? 116 LYS E CD  1 
ATOM   8712  C CE  . LYS E 1 111 ? 31.162  -15.055 -17.459 1.00 165.04 ? 116 LYS E CE  1 
ATOM   8713  N NZ  . LYS E 1 111 ? 30.323  -13.839 -17.651 1.00 149.87 ? 116 LYS E NZ  1 
ATOM   8714  N N   . HIS E 1 112 A 30.689  -20.468 -16.397 1.00 99.43  ? 116 HIS E N   1 
ATOM   8715  C CA  . HIS E 1 112 A 30.789  -21.515 -17.412 1.00 102.98 ? 116 HIS E CA  1 
ATOM   8716  C C   . HIS E 1 112 A 30.320  -22.877 -16.896 1.00 91.85  ? 116 HIS E C   1 
ATOM   8717  O O   . HIS E 1 112 A 30.282  -23.122 -15.687 1.00 85.74  ? 116 HIS E O   1 
ATOM   8718  C CB  . HIS E 1 112 A 32.212  -21.620 -17.969 1.00 132.93 ? 116 HIS E CB  1 
ATOM   8719  C CG  . HIS E 1 112 A 32.306  -22.431 -19.225 1.00 140.05 ? 116 HIS E CG  1 
ATOM   8720  N ND1 . HIS E 1 112 A 32.509  -23.794 -19.217 1.00 134.72 ? 116 HIS E ND1 1 
ATOM   8721  C CD2 . HIS E 1 112 A 32.212  -22.073 -20.528 1.00 154.31 ? 116 HIS E CD2 1 
ATOM   8722  C CE1 . HIS E 1 112 A 32.542  -24.239 -20.461 1.00 145.13 ? 116 HIS E CE1 1 
ATOM   8723  N NE2 . HIS E 1 112 A 32.364  -23.215 -21.275 1.00 155.01 ? 116 HIS E NE2 1 
ATOM   8724  N N   . PHE E 1 113 B 29.974  -23.759 -17.827 1.00 147.44 ? 116 PHE E N   1 
ATOM   8725  C CA  . PHE E 1 113 B 29.449  -25.073 -17.487 1.00 136.60 ? 116 PHE E CA  1 
ATOM   8726  C C   . PHE E 1 113 B 29.223  -25.879 -18.760 1.00 142.75 ? 116 PHE E C   1 
ATOM   8727  O O   . PHE E 1 113 B 28.680  -25.363 -19.737 1.00 149.41 ? 116 PHE E O   1 
ATOM   8728  C CB  . PHE E 1 113 B 28.135  -24.917 -16.728 1.00 112.74 ? 116 PHE E CB  1 
ATOM   8729  C CG  . PHE E 1 113 B 27.662  -26.173 -16.065 1.00 104.07 ? 116 PHE E CG  1 
ATOM   8730  C CD1 . PHE E 1 113 B 28.201  -26.574 -14.855 1.00 99.87  ? 116 PHE E CD1 1 
ATOM   8731  C CD2 . PHE E 1 113 B 26.666  -26.944 -16.642 1.00 101.19 ? 116 PHE E CD2 1 
ATOM   8732  C CE1 . PHE E 1 113 B 27.764  -27.721 -14.237 1.00 93.56  ? 116 PHE E CE1 1 
ATOM   8733  C CE2 . PHE E 1 113 B 26.223  -28.096 -16.026 1.00 96.14  ? 116 PHE E CE2 1 
ATOM   8734  C CZ  . PHE E 1 113 B 26.774  -28.486 -14.823 1.00 91.41  ? 116 PHE E CZ  1 
ATOM   8735  N N   . GLU E 1 114 C 29.643  -27.141 -18.752 1.00 113.88 ? 116 GLU E N   1 
ATOM   8736  C CA  . GLU E 1 114 C 29.483  -27.995 -19.927 1.00 114.52 ? 116 GLU E CA  1 
ATOM   8737  C C   . GLU E 1 114 C 29.634  -29.479 -19.598 1.00 115.62 ? 116 GLU E C   1 
ATOM   8738  O O   . GLU E 1 114 C 30.594  -29.880 -18.938 1.00 129.42 ? 116 GLU E O   1 
ATOM   8739  C CB  . GLU E 1 114 C 30.481  -27.594 -21.018 1.00 139.95 ? 116 GLU E CB  1 
ATOM   8740  C CG  . GLU E 1 114 C 30.235  -28.262 -22.360 1.00 154.78 ? 116 GLU E CG  1 
ATOM   8741  C CD  . GLU E 1 114 C 31.146  -27.734 -23.450 1.00 188.65 ? 116 GLU E CD  1 
ATOM   8742  O OE1 . GLU E 1 114 C 31.883  -26.759 -23.190 1.00 200.65 ? 116 GLU E OE1 1 
ATOM   8743  O OE2 . GLU E 1 114 C 31.126  -28.292 -24.566 1.00 204.42 ? 116 GLU E OE2 1 
ATOM   8744  N N   . LYS E 1 115 ? 28.679  -30.284 -20.064 1.00 118.21 ? 117 LYS E N   1 
ATOM   8745  C CA  . LYS E 1 115 ? 28.712  -31.735 -19.874 1.00 119.98 ? 117 LYS E CA  1 
ATOM   8746  C C   . LYS E 1 115 ? 29.755  -32.389 -20.781 1.00 145.88 ? 117 LYS E C   1 
ATOM   8747  O O   . LYS E 1 115 ? 29.586  -32.432 -21.998 1.00 150.60 ? 117 LYS E O   1 
ATOM   8748  C CB  . LYS E 1 115 ? 27.335  -32.347 -20.147 1.00 102.24 ? 117 LYS E CB  1 
ATOM   8749  C CG  . LYS E 1 115 ? 27.343  -33.865 -20.149 1.00 104.92 ? 117 LYS E CG  1 
ATOM   8750  C CD  . LYS E 1 115 ? 26.082  -34.452 -20.769 1.00 101.49 ? 117 LYS E CD  1 
ATOM   8751  C CE  . LYS E 1 115 ? 24.844  -34.192 -19.919 1.00 95.09  ? 117 LYS E CE  1 
ATOM   8752  N NZ  . LYS E 1 115 ? 23.722  -35.116 -20.283 1.00 90.20  ? 117 LYS E NZ  1 
ATOM   8753  N N   . VAL E 1 116 ? 30.826  -32.903 -20.186 1.00 99.92  ? 118 VAL E N   1 
ATOM   8754  C CA  . VAL E 1 116 ? 31.925  -33.475 -20.958 1.00 124.03 ? 118 VAL E CA  1 
ATOM   8755  C C   . VAL E 1 116 ? 32.351  -34.856 -20.450 1.00 126.39 ? 118 VAL E C   1 
ATOM   8756  O O   . VAL E 1 116 ? 33.007  -34.967 -19.415 1.00 107.41 ? 118 VAL E O   1 
ATOM   8757  C CB  . VAL E 1 116 ? 33.149  -32.541 -20.954 1.00 150.91 ? 118 VAL E CB  1 
ATOM   8758  C CG1 . VAL E 1 116 ? 34.276  -33.140 -21.777 1.00 175.57 ? 118 VAL E CG1 1 
ATOM   8759  C CG2 . VAL E 1 116 ? 32.769  -31.171 -21.487 1.00 147.87 ? 118 VAL E CG2 1 
ATOM   8760  N N   . LYS E 1 117 ? 31.988  -35.899 -21.193 1.00 162.62 ? 119 LYS E N   1 
ATOM   8761  C CA  . LYS E 1 117 ? 32.324  -37.277 -20.832 1.00 168.85 ? 119 LYS E CA  1 
ATOM   8762  C C   . LYS E 1 117 ? 33.802  -37.426 -20.443 1.00 182.97 ? 119 LYS E C   1 
ATOM   8763  O O   . LYS E 1 117 ? 34.669  -36.771 -21.021 1.00 191.79 ? 119 LYS E O   1 
ATOM   8764  C CB  . LYS E 1 117 ? 31.971  -38.222 -21.987 1.00 172.48 ? 119 LYS E CB  1 
ATOM   8765  C CG  . LYS E 1 117 ? 31.917  -39.693 -21.599 1.00 172.73 ? 119 LYS E CG  1 
ATOM   8766  C CD  . LYS E 1 117 ? 31.743  -40.613 -22.811 1.00 184.02 ? 119 LYS E CD  1 
ATOM   8767  C CE  . LYS E 1 117 ? 30.340  -40.538 -23.403 1.00 168.16 ? 119 LYS E CE  1 
ATOM   8768  N NZ  . LYS E 1 117 ? 30.134  -41.548 -24.485 1.00 170.64 ? 119 LYS E NZ  1 
ATOM   8769  N N   . ILE E 1 118 ? 34.080  -38.285 -19.463 1.00 169.53 ? 120 ILE E N   1 
ATOM   8770  C CA  . ILE E 1 118 ? 35.443  -38.466 -18.949 1.00 166.15 ? 120 ILE E CA  1 
ATOM   8771  C C   . ILE E 1 118 ? 35.868  -39.931 -18.792 1.00 166.41 ? 120 ILE E C   1 
ATOM   8772  O O   . ILE E 1 118 ? 37.061  -40.240 -18.808 1.00 170.27 ? 120 ILE E O   1 
ATOM   8773  C CB  . ILE E 1 118 ? 35.628  -37.770 -17.591 1.00 154.03 ? 120 ILE E CB  1 
ATOM   8774  C CG1 . ILE E 1 118 ? 34.389  -37.987 -16.721 1.00 138.60 ? 120 ILE E CG1 1 
ATOM   8775  C CG2 . ILE E 1 118 ? 35.891  -36.289 -17.785 1.00 153.43 ? 120 ILE E CG2 1 
ATOM   8776  C CD1 . ILE E 1 118 ? 34.548  -37.501 -15.307 1.00 123.89 ? 120 ILE E CD1 1 
ATOM   8777  N N   . LEU E 1 119 ? 34.895  -40.821 -18.615 1.00 96.66  ? 121 LEU E N   1 
ATOM   8778  C CA  . LEU E 1 119 ? 35.165  -42.255 -18.527 1.00 99.59  ? 121 LEU E CA  1 
ATOM   8779  C C   . LEU E 1 119 ? 34.144  -43.027 -19.362 1.00 110.42 ? 121 LEU E C   1 
ATOM   8780  O O   . LEU E 1 119 ? 33.026  -43.292 -18.905 1.00 102.55 ? 121 LEU E O   1 
ATOM   8781  C CB  . LEU E 1 119 ? 35.145  -42.731 -17.071 1.00 84.12  ? 121 LEU E CB  1 
ATOM   8782  C CG  . LEU E 1 119 ? 36.168  -42.121 -16.105 1.00 79.66  ? 121 LEU E CG  1 
ATOM   8783  C CD1 . LEU E 1 119 ? 35.716  -42.323 -14.668 1.00 72.18  ? 121 LEU E CD1 1 
ATOM   8784  C CD2 . LEU E 1 119 ? 37.574  -42.676 -16.312 1.00 78.43  ? 121 LEU E CD2 1 
ATOM   8785  N N   . PRO E 1 120 ? 34.535  -43.388 -20.596 1.00 117.67 ? 122 PRO E N   1 
ATOM   8786  C CA  . PRO E 1 120 ? 33.686  -44.001 -21.627 1.00 113.89 ? 122 PRO E CA  1 
ATOM   8787  C C   . PRO E 1 120 ? 33.006  -45.304 -21.198 1.00 106.36 ? 122 PRO E C   1 
ATOM   8788  O O   . PRO E 1 120 ? 33.617  -46.162 -20.553 1.00 111.58 ? 122 PRO E O   1 
ATOM   8789  C CB  . PRO E 1 120 ? 34.670  -44.277 -22.768 1.00 128.82 ? 122 PRO E CB  1 
ATOM   8790  C CG  . PRO E 1 120 ? 35.780  -43.309 -22.555 1.00 131.62 ? 122 PRO E CG  1 
ATOM   8791  C CD  . PRO E 1 120 ? 35.914  -43.183 -21.073 1.00 126.51 ? 122 PRO E CD  1 
ATOM   8792  N N   . LYS E 1 121 ? 31.741  -45.441 -21.582 1.00 138.45 ? 123 LYS E N   1 
ATOM   8793  C CA  . LYS E 1 121 ? 30.937  -46.615 -21.253 1.00 125.59 ? 123 LYS E CA  1 
ATOM   8794  C C   . LYS E 1 121 ? 31.537  -47.899 -21.830 1.00 150.30 ? 123 LYS E C   1 
ATOM   8795  O O   . LYS E 1 121 ? 31.426  -48.970 -21.230 1.00 147.91 ? 123 LYS E O   1 
ATOM   8796  C CB  . LYS E 1 121 ? 29.508  -46.421 -21.768 1.00 100.37 ? 123 LYS E CB  1 
ATOM   8797  C CG  . LYS E 1 121 ? 28.445  -47.236 -21.057 1.00 83.84  ? 123 LYS E CG  1 
ATOM   8798  C CD  . LYS E 1 121 ? 27.051  -46.900 -21.588 1.00 74.62  ? 123 LYS E CD  1 
ATOM   8799  C CE  . LYS E 1 121 ? 25.968  -47.687 -20.844 1.00 69.82  ? 123 LYS E CE  1 
ATOM   8800  N NZ  . LYS E 1 121 ? 24.591  -47.459 -21.382 1.00 66.19  ? 123 LYS E NZ  1 
ATOM   8801  N N   . ASP E 1 122 ? 32.169  -47.789 -22.995 1.00 145.83 ? 125 ASP E N   1 
ATOM   8802  C CA  . ASP E 1 122 ? 32.756  -48.951 -23.660 1.00 163.34 ? 125 ASP E CA  1 
ATOM   8803  C C   . ASP E 1 122 ? 34.203  -49.192 -23.239 1.00 188.81 ? 125 ASP E C   1 
ATOM   8804  O O   . ASP E 1 122 ? 34.909  -50.004 -23.837 1.00 202.02 ? 125 ASP E O   1 
ATOM   8805  C CB  . ASP E 1 122 ? 32.642  -48.831 -25.184 1.00 164.66 ? 125 ASP E CB  1 
ATOM   8806  C CG  . ASP E 1 122 ? 33.177  -47.514 -25.710 1.00 172.80 ? 125 ASP E CG  1 
ATOM   8807  O OD1 . ASP E 1 122 ? 34.181  -47.014 -25.161 1.00 182.85 ? 125 ASP E OD1 1 
ATOM   8808  O OD2 . ASP E 1 122 ? 32.589  -46.978 -26.674 1.00 170.61 ? 125 ASP E OD2 1 
ATOM   8809  N N   . ARG E 1 123 ? 34.640  -48.475 -22.209 1.00 169.65 ? 126 ARG E N   1 
ATOM   8810  C CA  . ARG E 1 123 ? 35.922  -48.755 -21.580 1.00 178.58 ? 126 ARG E CA  1 
ATOM   8811  C C   . ARG E 1 123 ? 35.737  -49.888 -20.586 1.00 171.34 ? 126 ARG E C   1 
ATOM   8812  O O   . ARG E 1 123 ? 36.691  -50.576 -20.223 1.00 179.33 ? 126 ARG E O   1 
ATOM   8813  C CB  . ARG E 1 123 ? 36.467  -47.517 -20.870 1.00 183.51 ? 126 ARG E CB  1 
ATOM   8814  C CG  . ARG E 1 123 ? 37.303  -46.612 -21.754 1.00 197.52 ? 126 ARG E CG  1 
ATOM   8815  C CD  . ARG E 1 123 ? 38.479  -47.370 -22.349 1.00 211.39 ? 126 ARG E CD  1 
ATOM   8816  N NE  . ARG E 1 123 ? 39.502  -46.471 -22.874 1.00 222.34 ? 126 ARG E NE  1 
ATOM   8817  C CZ  . ARG E 1 123 ? 39.505  -45.974 -24.106 1.00 230.33 ? 126 ARG E CZ  1 
ATOM   8818  N NH1 . ARG E 1 123 ? 38.533  -46.285 -24.954 1.00 232.55 ? 126 ARG E NH1 1 
ATOM   8819  N NH2 . ARG E 1 123 ? 40.482  -45.165 -24.490 1.00 235.07 ? 126 ARG E NH2 1 
ATOM   8820  N N   . TRP E 1 124 ? 34.495  -50.069 -20.144 1.00 156.24 ? 127 TRP E N   1 
ATOM   8821  C CA  . TRP E 1 124 ? 34.144  -51.191 -19.284 1.00 143.70 ? 127 TRP E CA  1 
ATOM   8822  C C   . TRP E 1 124 ? 33.923  -52.435 -20.144 1.00 139.30 ? 127 TRP E C   1 
ATOM   8823  O O   . TRP E 1 124 ? 32.787  -52.818 -20.440 1.00 128.67 ? 127 TRP E O   1 
ATOM   8824  C CB  . TRP E 1 124 ? 32.903  -50.872 -18.444 1.00 134.18 ? 127 TRP E CB  1 
ATOM   8825  C CG  . TRP E 1 124 ? 33.034  -49.613 -17.628 1.00 135.95 ? 127 TRP E CG  1 
ATOM   8826  C CD1 . TRP E 1 124 ? 32.171  -48.556 -17.607 1.00 130.84 ? 127 TRP E CD1 1 
ATOM   8827  C CD2 . TRP E 1 124 ? 34.099  -49.279 -16.727 1.00 136.40 ? 127 TRP E CD2 1 
ATOM   8828  N NE1 . TRP E 1 124 ? 32.627  -47.591 -16.744 1.00 130.15 ? 127 TRP E NE1 1 
ATOM   8829  C CE2 . TRP E 1 124 ? 33.811  -48.011 -16.193 1.00 133.21 ? 127 TRP E CE2 1 
ATOM   8830  C CE3 . TRP E 1 124 ? 35.266  -49.931 -16.319 1.00 137.26 ? 127 TRP E CE3 1 
ATOM   8831  C CZ2 . TRP E 1 124 ? 34.647  -47.382 -15.274 1.00 129.73 ? 127 TRP E CZ2 1 
ATOM   8832  C CZ3 . TRP E 1 124 ? 36.092  -49.305 -15.405 1.00 132.66 ? 127 TRP E CZ3 1 
ATOM   8833  C CH2 . TRP E 1 124 ? 35.780  -48.046 -14.893 1.00 129.02 ? 127 TRP E CH2 1 
ATOM   8834  N N   . THR E 1 125 ? 35.033  -53.047 -20.547 1.00 118.66 ? 128 THR E N   1 
ATOM   8835  C CA  . THR E 1 125 ? 35.019  -54.204 -21.434 1.00 118.50 ? 128 THR E CA  1 
ATOM   8836  C C   . THR E 1 125 ? 35.015  -55.500 -20.633 1.00 108.51 ? 128 THR E C   1 
ATOM   8837  O O   . THR E 1 125 ? 34.696  -56.566 -21.156 1.00 108.07 ? 128 THR E O   1 
ATOM   8838  C CB  . THR E 1 125 ? 36.241  -54.192 -22.381 1.00 114.87 ? 128 THR E CB  1 
ATOM   8839  O OG1 . THR E 1 125 ? 37.449  -54.261 -21.611 1.00 124.83 ? 128 THR E OG1 1 
ATOM   8840  C CG2 . THR E 1 125 ? 36.256  -52.921 -23.225 1.00 104.69 ? 128 THR E CG2 1 
ATOM   8841  N N   . GLN E 1 126 ? 35.374  -55.397 -19.358 1.00 169.08 ? 129 GLN E N   1 
ATOM   8842  C CA  . GLN E 1 126 ? 35.402  -56.555 -18.478 1.00 170.23 ? 129 GLN E CA  1 
ATOM   8843  C C   . GLN E 1 126 ? 34.063  -56.719 -17.765 1.00 164.92 ? 129 GLN E C   1 
ATOM   8844  O O   . GLN E 1 126 ? 33.825  -57.732 -17.104 1.00 159.19 ? 129 GLN E O   1 
ATOM   8845  C CB  . GLN E 1 126 ? 36.528  -56.421 -17.449 1.00 167.44 ? 129 GLN E CB  1 
ATOM   8846  C CG  . GLN E 1 126 ? 37.811  -55.811 -17.994 1.00 171.81 ? 129 GLN E CG  1 
ATOM   8847  C CD  . GLN E 1 126 ? 37.826  -54.291 -17.909 1.00 157.14 ? 129 GLN E CD  1 
ATOM   8848  O OE1 . GLN E 1 126 ? 37.306  -53.700 -16.957 1.00 133.51 ? 129 GLN E OE1 1 
ATOM   8849  N NE2 . GLN E 1 126 ? 38.426  -53.650 -18.909 1.00 161.64 ? 129 GLN E NE2 1 
ATOM   8850  N N   . HIS E 1 127 ? 33.190  -55.723 -17.908 1.00 137.01 ? 130 HIS E N   1 
ATOM   8851  C CA  . HIS E 1 127 ? 31.901  -55.720 -17.213 1.00 115.43 ? 130 HIS E CA  1 
ATOM   8852  C C   . HIS E 1 127 ? 30.719  -55.450 -18.144 1.00 104.55 ? 130 HIS E C   1 
ATOM   8853  O O   . HIS E 1 127 ? 30.885  -54.921 -19.246 1.00 112.13 ? 130 HIS E O   1 
ATOM   8854  C CB  . HIS E 1 127 ? 31.896  -54.676 -16.092 1.00 100.35 ? 130 HIS E CB  1 
ATOM   8855  C CG  . HIS E 1 127 ? 33.075  -54.760 -15.172 1.00 100.04 ? 130 HIS E CG  1 
ATOM   8856  N ND1 . HIS E 1 127 ? 34.299  -54.205 -15.478 1.00 98.26  ? 130 HIS E ND1 1 
ATOM   8857  C CD2 . HIS E 1 127 ? 33.212  -55.326 -13.949 1.00 99.47  ? 130 HIS E CD2 1 
ATOM   8858  C CE1 . HIS E 1 127 ? 35.142  -54.429 -14.485 1.00 100.28 ? 130 HIS E CE1 1 
ATOM   8859  N NE2 . HIS E 1 127 ? 34.507  -55.108 -13.545 1.00 102.58 ? 130 HIS E NE2 1 
ATOM   8860  N N   . THR E 1 128 ? 29.525  -55.810 -17.683 1.00 130.33 ? 131 THR E N   1 
ATOM   8861  C CA  . THR E 1 128 ? 28.295  -55.500 -18.398 1.00 122.47 ? 131 THR E CA  1 
ATOM   8862  C C   . THR E 1 128 ? 27.875  -54.070 -18.082 1.00 118.42 ? 131 THR E C   1 
ATOM   8863  O O   . THR E 1 128 ? 27.778  -53.689 -16.915 1.00 112.11 ? 131 THR E O   1 
ATOM   8864  C CB  . THR E 1 128 ? 27.150  -56.438 -17.987 1.00 115.66 ? 131 THR E CB  1 
ATOM   8865  O OG1 . THR E 1 128 ? 27.588  -57.799 -18.072 1.00 124.40 ? 131 THR E OG1 1 
ATOM   8866  C CG2 . THR E 1 128 ? 25.940  -56.235 -18.888 1.00 110.75 ? 131 THR E CG2 1 
ATOM   8867  N N   . THR E 1 129 ? 27.624  -53.280 -19.120 1.00 127.38 ? 132 THR E N   1 
ATOM   8868  C CA  . THR E 1 129 ? 27.259  -51.881 -18.934 1.00 118.25 ? 132 THR E CA  1 
ATOM   8869  C C   . THR E 1 129 ? 25.862  -51.598 -19.475 1.00 110.23 ? 132 THR E C   1 
ATOM   8870  O O   . THR E 1 129 ? 25.664  -50.655 -20.239 1.00 112.86 ? 132 THR E O   1 
ATOM   8871  C CB  . THR E 1 129 ? 28.284  -50.931 -19.608 1.00 113.49 ? 132 THR E CB  1 
ATOM   8872  O OG1 . THR E 1 129 ? 28.150  -50.993 -21.035 1.00 118.59 ? 132 THR E OG1 1 
ATOM   8873  C CG2 . THR E 1 129 ? 29.705  -51.311 -19.219 1.00 128.57 ? 132 THR E CG2 1 
ATOM   8874  N N   . THR E 1 130 ? 24.891  -52.413 -19.074 1.00 102.39 ? 133 THR E N   1 
ATOM   8875  C CA  . THR E 1 130 ? 23.530  -52.273 -19.585 1.00 102.77 ? 133 THR E CA  1 
ATOM   8876  C C   . THR E 1 130 ? 22.470  -52.767 -18.604 1.00 101.12 ? 133 THR E C   1 
ATOM   8877  O O   . THR E 1 130 ? 21.273  -52.680 -18.880 1.00 108.36 ? 133 THR E O   1 
ATOM   8878  C CB  . THR E 1 130 ? 23.343  -53.033 -20.916 1.00 123.17 ? 133 THR E CB  1 
ATOM   8879  O OG1 . THR E 1 130 ? 23.876  -54.359 -20.792 1.00 126.63 ? 133 THR E OG1 1 
ATOM   8880  C CG2 . THR E 1 130 ? 24.042  -52.311 -22.056 1.00 124.85 ? 133 THR E CG2 1 
ATOM   8881  N N   . GLY E 1 131 ? 22.908  -53.294 -17.466 1.00 128.42 ? 134 GLY E N   1 
ATOM   8882  C CA  . GLY E 1 131 ? 21.984  -53.807 -16.471 1.00 131.10 ? 134 GLY E CA  1 
ATOM   8883  C C   . GLY E 1 131 ? 21.154  -52.704 -15.847 1.00 132.70 ? 134 GLY E C   1 
ATOM   8884  O O   . GLY E 1 131 ? 21.423  -52.279 -14.727 1.00 127.65 ? 134 GLY E O   1 
ATOM   8885  N N   . GLY E 1 132 ? 20.144  -52.239 -16.578 1.00 130.31 ? 135 GLY E N   1 
ATOM   8886  C CA  . GLY E 1 132 ? 19.291  -51.160 -16.114 1.00 125.05 ? 135 GLY E CA  1 
ATOM   8887  C C   . GLY E 1 132 ? 18.304  -51.621 -15.062 1.00 129.85 ? 135 GLY E C   1 
ATOM   8888  O O   . GLY E 1 132 ? 18.592  -52.536 -14.292 1.00 125.95 ? 135 GLY E O   1 
ATOM   8889  N N   . SER E 1 133 ? 17.137  -50.988 -15.024 1.00 81.49  ? 136 SER E N   1 
ATOM   8890  C CA  . SER E 1 133 ? 16.108  -51.371 -14.065 1.00 96.54  ? 136 SER E CA  1 
ATOM   8891  C C   . SER E 1 133 ? 14.725  -50.919 -14.501 1.00 108.15 ? 136 SER E C   1 
ATOM   8892  O O   . SER E 1 133 ? 14.589  -50.054 -15.367 1.00 112.18 ? 136 SER E O   1 
ATOM   8893  C CB  . SER E 1 133 ? 16.424  -50.812 -12.676 1.00 94.55  ? 136 SER E CB  1 
ATOM   8894  O OG  . SER E 1 133 ? 15.379  -51.103 -11.761 1.00 97.19  ? 136 SER E OG  1 
ATOM   8895  N N   . ARG E 1 134 ? 13.706  -51.509 -13.883 1.00 142.50 ? 137 ARG E N   1 
ATOM   8896  C CA  . ARG E 1 134 ? 12.316  -51.234 -14.228 1.00 149.02 ? 137 ARG E CA  1 
ATOM   8897  C C   . ARG E 1 134 ? 11.861  -49.845 -13.795 1.00 145.03 ? 137 ARG E C   1 
ATOM   8898  O O   . ARG E 1 134 ? 11.334  -49.076 -14.600 1.00 151.34 ? 137 ARG E O   1 
ATOM   8899  C CB  . ARG E 1 134 ? 11.394  -52.288 -13.614 1.00 149.71 ? 137 ARG E CB  1 
ATOM   8900  C CG  . ARG E 1 134 ? 9.939   -52.126 -14.010 1.00 162.30 ? 137 ARG E CG  1 
ATOM   8901  C CD  . ARG E 1 134 ? 9.115   -53.329 -13.602 1.00 174.00 ? 137 ARG E CD  1 
ATOM   8902  N NE  . ARG E 1 134 ? 7.991   -53.543 -14.509 1.00 190.71 ? 137 ARG E NE  1 
ATOM   8903  C CZ  . ARG E 1 134 ? 8.062   -54.262 -15.625 1.00 200.59 ? 137 ARG E CZ  1 
ATOM   8904  N NH1 . ARG E 1 134 ? 9.205   -54.838 -15.974 1.00 201.08 ? 137 ARG E NH1 1 
ATOM   8905  N NH2 . ARG E 1 134 ? 6.991   -54.406 -16.394 1.00 208.02 ? 137 ARG E NH2 1 
ATOM   8906  N N   . ALA E 1 135 ? 12.054  -49.529 -12.520 1.00 152.65 ? 138 ALA E N   1 
ATOM   8907  C CA  . ALA E 1 135 ? 11.643  -48.231 -11.998 1.00 143.83 ? 138 ALA E CA  1 
ATOM   8908  C C   . ALA E 1 135 ? 12.298  -47.086 -12.770 1.00 140.30 ? 138 ALA E C   1 
ATOM   8909  O O   . ALA E 1 135 ? 11.806  -45.960 -12.755 1.00 139.73 ? 138 ALA E O   1 
ATOM   8910  C CB  . ALA E 1 135 ? 11.955  -48.130 -10.514 1.00 134.56 ? 138 ALA E CB  1 
ATOM   8911  N N   . CYS E 1 136 ? 13.405  -47.386 -13.445 1.00 109.69 ? 139 CYS E N   1 
ATOM   8912  C CA  . CYS E 1 136 ? 14.114  -46.411 -14.271 1.00 110.51 ? 139 CYS E CA  1 
ATOM   8913  C C   . CYS E 1 136 ? 14.124  -46.834 -15.738 1.00 125.06 ? 139 CYS E C   1 
ATOM   8914  O O   . CYS E 1 136 ? 15.054  -46.508 -16.480 1.00 128.23 ? 139 CYS E O   1 
ATOM   8915  C CB  . CYS E 1 136 ? 15.558  -46.242 -13.789 1.00 99.66  ? 139 CYS E CB  1 
ATOM   8916  S SG  . CYS E 1 136 ? 15.757  -45.276 -12.279 1.00 186.61 ? 139 CYS E SG  1 
ATOM   8917  N N   . ALA E 1 137 ? 13.089  -47.557 -16.153 1.00 124.64 ? 140 ALA E N   1 
ATOM   8918  C CA  . ALA E 1 137 ? 13.049  -48.128 -17.496 1.00 134.60 ? 140 ALA E CA  1 
ATOM   8919  C C   . ALA E 1 137 ? 12.399  -47.205 -18.523 1.00 140.09 ? 140 ALA E C   1 
ATOM   8920  O O   . ALA E 1 137 ? 11.348  -46.615 -18.269 1.00 132.75 ? 140 ALA E O   1 
ATOM   8921  C CB  . ALA E 1 137 ? 12.341  -49.475 -17.473 1.00 135.63 ? 140 ALA E CB  1 
ATOM   8922  N N   . VAL E 1 138 ? 13.032  -47.096 -19.688 1.00 156.55 ? 141 VAL E N   1 
ATOM   8923  C CA  . VAL E 1 138 ? 12.494  -46.308 -20.793 1.00 175.63 ? 141 VAL E CA  1 
ATOM   8924  C C   . VAL E 1 138 ? 11.591  -47.152 -21.687 1.00 189.96 ? 141 VAL E C   1 
ATOM   8925  O O   . VAL E 1 138 ? 12.042  -48.121 -22.300 1.00 194.21 ? 141 VAL E O   1 
ATOM   8926  C CB  . VAL E 1 138 ? 13.618  -45.724 -21.667 1.00 178.31 ? 141 VAL E CB  1 
ATOM   8927  C CG1 . VAL E 1 138 ? 13.031  -44.929 -22.822 1.00 188.78 ? 141 VAL E CG1 1 
ATOM   8928  C CG2 . VAL E 1 138 ? 14.539  -44.858 -20.837 1.00 165.09 ? 141 VAL E CG2 1 
ATOM   8929  N N   . SER E 1 139 ? 10.317  -46.775 -21.762 1.00 176.85 ? 142 SER E N   1 
ATOM   8930  C CA  . SER E 1 139 ? 9.352   -47.475 -22.604 1.00 183.75 ? 142 SER E CA  1 
ATOM   8931  C C   . SER E 1 139 ? 9.439   -48.987 -22.414 1.00 182.55 ? 142 SER E C   1 
ATOM   8932  O O   . SER E 1 139 ? 9.786   -49.718 -23.342 1.00 188.73 ? 142 SER E O   1 
ATOM   8933  C CB  . SER E 1 139 ? 9.566   -47.118 -24.078 1.00 191.18 ? 142 SER E CB  1 
ATOM   8934  O OG  . SER E 1 139 ? 10.826  -47.576 -24.541 1.00 191.96 ? 142 SER E OG  1 
ATOM   8935  N N   . GLY E 1 140 ? 9.125   -49.447 -21.207 1.00 126.79 ? 143 GLY E N   1 
ATOM   8936  C CA  . GLY E 1 140 ? 9.182   -50.863 -20.885 1.00 126.28 ? 143 GLY E CA  1 
ATOM   8937  C C   . GLY E 1 140 ? 10.584  -51.339 -20.547 1.00 125.71 ? 143 GLY E C   1 
ATOM   8938  O O   . GLY E 1 140 ? 10.875  -51.666 -19.393 1.00 120.46 ? 143 GLY E O   1 
ATOM   8939  N N   . ASN E 1 141 ? 11.448  -51.375 -21.560 1.00 181.09 ? 144 ASN E N   1 
ATOM   8940  C CA  . ASN E 1 141 ? 12.831  -51.823 -21.405 1.00 178.15 ? 144 ASN E CA  1 
ATOM   8941  C C   . ASN E 1 141 ? 13.572  -51.136 -20.269 1.00 168.00 ? 144 ASN E C   1 
ATOM   8942  O O   . ASN E 1 141 ? 13.577  -49.910 -20.179 1.00 168.43 ? 144 ASN E O   1 
ATOM   8943  C CB  . ASN E 1 141 ? 13.615  -51.610 -22.703 1.00 182.94 ? 144 ASN E CB  1 
ATOM   8944  C CG  . ASN E 1 141 ? 13.234  -52.594 -23.786 1.00 192.94 ? 144 ASN E CG  1 
ATOM   8945  O OD1 . ASN E 1 141 ? 12.675  -53.656 -23.510 1.00 194.59 ? 144 ASN E OD1 1 
ATOM   8946  N ND2 . ASN E 1 141 ? 13.546  -52.252 -25.031 1.00 197.65 ? 144 ASN E ND2 1 
ATOM   8947  N N   . PRO E 1 142 ? 14.212  -51.930 -19.400 1.00 156.37 ? 145 PRO E N   1 
ATOM   8948  C CA  . PRO E 1 142 ? 15.043  -51.383 -18.325 1.00 140.73 ? 145 PRO E CA  1 
ATOM   8949  C C   . PRO E 1 142 ? 16.083  -50.416 -18.881 1.00 125.80 ? 145 PRO E C   1 
ATOM   8950  O O   . PRO E 1 142 ? 16.642  -50.649 -19.957 1.00 120.67 ? 145 PRO E O   1 
ATOM   8951  C CB  . PRO E 1 142 ? 15.720  -52.627 -17.746 1.00 138.20 ? 145 PRO E CB  1 
ATOM   8952  C CG  . PRO E 1 142 ? 14.763  -53.731 -18.029 1.00 144.53 ? 145 PRO E CG  1 
ATOM   8953  C CD  . PRO E 1 142 ? 14.160  -53.401 -19.365 1.00 156.22 ? 145 PRO E CD  1 
ATOM   8954  N N   . SER E 1 143 ? 16.330  -49.333 -18.154 1.00 159.61 ? 146 SER E N   1 
ATOM   8955  C CA  . SER E 1 143 ? 17.261  -48.311 -18.610 1.00 134.53 ? 146 SER E CA  1 
ATOM   8956  C C   . SER E 1 143 ? 17.903  -47.610 -17.423 1.00 118.65 ? 146 SER E C   1 
ATOM   8957  O O   . SER E 1 143 ? 17.470  -47.782 -16.284 1.00 115.69 ? 146 SER E O   1 
ATOM   8958  C CB  . SER E 1 143 ? 16.538  -47.297 -19.494 1.00 135.06 ? 146 SER E CB  1 
ATOM   8959  O OG  . SER E 1 143 ? 17.465  -46.518 -20.222 1.00 117.21 ? 146 SER E OG  1 
ATOM   8960  N N   . PHE E 1 144 ? 18.932  -46.812 -17.687 1.00 122.57 ? 147 PHE E N   1 
ATOM   8961  C CA  . PHE E 1 144 ? 19.661  -46.173 -16.599 1.00 103.90 ? 147 PHE E CA  1 
ATOM   8962  C C   . PHE E 1 144 ? 20.091  -44.731 -16.868 1.00 98.02  ? 147 PHE E C   1 
ATOM   8963  O O   . PHE E 1 144 ? 20.086  -44.266 -18.007 1.00 107.77 ? 147 PHE E O   1 
ATOM   8964  C CB  . PHE E 1 144 ? 20.876  -47.013 -16.219 1.00 91.24  ? 147 PHE E CB  1 
ATOM   8965  C CG  . PHE E 1 144 ? 21.180  -46.995 -14.753 1.00 83.47  ? 147 PHE E CG  1 
ATOM   8966  C CD1 . PHE E 1 144 ? 20.177  -47.249 -13.826 1.00 87.24  ? 147 PHE E CD1 1 
ATOM   8967  C CD2 . PHE E 1 144 ? 22.462  -46.732 -14.298 1.00 77.22  ? 147 PHE E CD2 1 
ATOM   8968  C CE1 . PHE E 1 144 ? 20.446  -47.236 -12.471 1.00 82.83  ? 147 PHE E CE1 1 
ATOM   8969  C CE2 . PHE E 1 144 ? 22.741  -46.722 -12.943 1.00 76.71  ? 147 PHE E CE2 1 
ATOM   8970  C CZ  . PHE E 1 144 ? 21.731  -46.974 -12.027 1.00 76.72  ? 147 PHE E CZ  1 
ATOM   8971  N N   . PHE E 1 145 ? 20.464  -44.040 -15.795 1.00 111.26 ? 148 PHE E N   1 
ATOM   8972  C CA  . PHE E 1 145 ? 20.920  -42.659 -15.865 1.00 101.94 ? 148 PHE E CA  1 
ATOM   8973  C C   . PHE E 1 145 ? 21.898  -42.473 -17.009 1.00 100.03 ? 148 PHE E C   1 
ATOM   8974  O O   . PHE E 1 145 ? 22.998  -43.016 -16.984 1.00 103.51 ? 148 PHE E O   1 
ATOM   8975  C CB  . PHE E 1 145 ? 21.576  -42.262 -14.545 1.00 90.34  ? 148 PHE E CB  1 
ATOM   8976  C CG  . PHE E 1 145 ? 20.751  -42.603 -13.339 1.00 83.60  ? 148 PHE E CG  1 
ATOM   8977  C CD1 . PHE E 1 145 ? 19.556  -41.945 -13.090 1.00 92.38  ? 148 PHE E CD1 1 
ATOM   8978  C CD2 . PHE E 1 145 ? 21.167  -43.579 -12.455 1.00 71.51  ? 148 PHE E CD2 1 
ATOM   8979  C CE1 . PHE E 1 145 ? 18.790  -42.261 -11.979 1.00 93.62  ? 148 PHE E CE1 1 
ATOM   8980  C CE2 . PHE E 1 145 ? 20.408  -43.896 -11.344 1.00 74.14  ? 148 PHE E CE2 1 
ATOM   8981  C CZ  . PHE E 1 145 ? 19.218  -43.238 -11.106 1.00 82.35  ? 148 PHE E CZ  1 
ATOM   8982  N N   . ARG E 1 146 ? 21.492  -41.694 -18.006 1.00 96.62  ? 149 ARG E N   1 
ATOM   8983  C CA  . ARG E 1 146 ? 22.240  -41.579 -19.255 1.00 110.87 ? 149 ARG E CA  1 
ATOM   8984  C C   . ARG E 1 146 ? 23.742  -41.316 -19.081 1.00 114.40 ? 149 ARG E C   1 
ATOM   8985  O O   . ARG E 1 146 ? 24.545  -41.707 -19.933 1.00 124.94 ? 149 ARG E O   1 
ATOM   8986  C CB  . ARG E 1 146 ? 21.603  -40.529 -20.169 1.00 118.62 ? 149 ARG E CB  1 
ATOM   8987  C CG  . ARG E 1 146 ? 20.113  -40.744 -20.394 1.00 130.92 ? 149 ARG E CG  1 
ATOM   8988  C CD  . ARG E 1 146 ? 19.811  -42.187 -20.768 1.00 141.78 ? 149 ARG E CD  1 
ATOM   8989  N NE  . ARG E 1 146 ? 20.454  -42.577 -22.020 1.00 145.65 ? 149 ARG E NE  1 
ATOM   8990  C CZ  . ARG E 1 146 ? 19.823  -42.668 -23.185 1.00 155.34 ? 149 ARG E CZ  1 
ATOM   8991  N NH1 . ARG E 1 146 ? 18.525  -42.402 -23.259 1.00 162.07 ? 149 ARG E NH1 1 
ATOM   8992  N NH2 . ARG E 1 146 ? 20.487  -43.030 -24.274 1.00 160.60 ? 149 ARG E NH2 1 
ATOM   8993  N N   . ASN E 1 147 ? 24.121  -40.662 -17.986 1.00 106.34 ? 150 ASN E N   1 
ATOM   8994  C CA  . ASN E 1 147 ? 25.536  -40.432 -17.697 1.00 110.08 ? 150 ASN E CA  1 
ATOM   8995  C C   . ASN E 1 147 ? 26.082  -41.402 -16.653 1.00 114.77 ? 150 ASN E C   1 
ATOM   8996  O O   . ASN E 1 147 ? 27.283  -41.430 -16.388 1.00 123.40 ? 150 ASN E O   1 
ATOM   8997  C CB  . ASN E 1 147 ? 25.787  -38.990 -17.247 1.00 107.21 ? 150 ASN E CB  1 
ATOM   8998  C CG  . ASN E 1 147 ? 25.337  -37.972 -18.272 1.00 107.75 ? 150 ASN E CG  1 
ATOM   8999  O OD1 . ASN E 1 147 ? 25.082  -36.816 -17.941 1.00 109.29 ? 150 ASN E OD1 1 
ATOM   9000  N ND2 . ASN E 1 147 ? 25.225  -38.398 -19.522 1.00 108.88 ? 150 ASN E ND2 1 
ATOM   9001  N N   . MET E 1 148 ? 25.195  -42.195 -16.060 1.00 103.87 ? 151 MET E N   1 
ATOM   9002  C CA  . MET E 1 148 ? 25.596  -43.154 -15.037 1.00 108.12 ? 151 MET E CA  1 
ATOM   9003  C C   . MET E 1 148 ? 25.658  -44.592 -15.554 1.00 122.89 ? 151 MET E C   1 
ATOM   9004  O O   . MET E 1 148 ? 24.633  -45.245 -15.769 1.00 124.30 ? 151 MET E O   1 
ATOM   9005  C CB  . MET E 1 148 ? 24.686  -43.056 -13.808 1.00 93.63  ? 151 MET E CB  1 
ATOM   9006  C CG  . MET E 1 148 ? 24.809  -41.733 -13.086 1.00 90.55  ? 151 MET E CG  1 
ATOM   9007  S SD  . MET E 1 148 ? 26.536  -41.299 -12.786 1.00 98.03  ? 151 MET E SD  1 
ATOM   9008  C CE  . MET E 1 148 ? 26.885  -42.291 -11.339 1.00 268.13 ? 151 MET E CE  1 
ATOM   9009  N N   . VAL E 1 149 ? 26.880  -45.074 -15.746 1.00 154.19 ? 152 VAL E N   1 
ATOM   9010  C CA  . VAL E 1 149 ? 27.121  -46.437 -16.186 1.00 159.93 ? 152 VAL E CA  1 
ATOM   9011  C C   . VAL E 1 149 ? 26.868  -47.403 -15.035 1.00 154.31 ? 152 VAL E C   1 
ATOM   9012  O O   . VAL E 1 149 ? 27.560  -47.344 -14.018 1.00 161.07 ? 152 VAL E O   1 
ATOM   9013  C CB  . VAL E 1 149 ? 28.587  -46.604 -16.631 1.00 123.54 ? 152 VAL E CB  1 
ATOM   9014  C CG1 . VAL E 1 149 ? 28.759  -47.872 -17.446 1.00 125.73 ? 152 VAL E CG1 1 
ATOM   9015  C CG2 . VAL E 1 149 ? 29.042  -45.390 -17.424 1.00 125.22 ? 152 VAL E CG2 1 
ATOM   9016  N N   . TRP E 1 150 ? 25.879  -48.285 -15.179 1.00 102.68 ? 153 TRP E N   1 
ATOM   9017  C CA  . TRP E 1 150 ? 25.673  -49.332 -14.176 1.00 96.59  ? 153 TRP E CA  1 
ATOM   9018  C C   . TRP E 1 150 ? 26.595  -50.512 -14.444 1.00 109.43 ? 153 TRP E C   1 
ATOM   9019  O O   . TRP E 1 150 ? 26.318  -51.337 -15.313 1.00 120.19 ? 153 TRP E O   1 
ATOM   9020  C CB  . TRP E 1 150 ? 24.216  -49.814 -14.115 1.00 83.07  ? 153 TRP E CB  1 
ATOM   9021  C CG  . TRP E 1 150 ? 23.951  -50.649 -12.886 1.00 75.11  ? 153 TRP E CG  1 
ATOM   9022  C CD1 . TRP E 1 150 ? 24.890  -51.242 -12.088 1.00 77.47  ? 153 TRP E CD1 1 
ATOM   9023  C CD2 . TRP E 1 150 ? 22.677  -50.960 -12.298 1.00 70.61  ? 153 TRP E CD2 1 
ATOM   9024  N NE1 . TRP E 1 150 ? 24.283  -51.910 -11.051 1.00 72.53  ? 153 TRP E NE1 1 
ATOM   9025  C CE2 . TRP E 1 150 ? 22.927  -51.748 -11.151 1.00 67.25  ? 153 TRP E CE2 1 
ATOM   9026  C CE3 . TRP E 1 150 ? 21.353  -50.650 -12.626 1.00 69.29  ? 153 TRP E CE3 1 
ATOM   9027  C CZ2 . TRP E 1 150 ? 21.902  -52.233 -10.335 1.00 59.26  ? 153 TRP E CZ2 1 
ATOM   9028  C CZ3 . TRP E 1 150 ? 20.334  -51.135 -11.814 1.00 70.41  ? 153 TRP E CZ3 1 
ATOM   9029  C CH2 . TRP E 1 150 ? 20.616  -51.919 -10.683 1.00 64.32  ? 153 TRP E CH2 1 
ATOM   9030  N N   . LEU E 1 151 ? 27.694  -50.589 -13.702 1.00 71.60  ? 154 LEU E N   1 
ATOM   9031  C CA  . LEU E 1 151 ? 28.591  -51.731 -13.816 1.00 81.65  ? 154 LEU E CA  1 
ATOM   9032  C C   . LEU E 1 151 ? 28.023  -52.946 -13.088 1.00 82.36  ? 154 LEU E C   1 
ATOM   9033  O O   . LEU E 1 151 ? 27.697  -52.876 -11.899 1.00 78.21  ? 154 LEU E O   1 
ATOM   9034  C CB  . LEU E 1 151 ? 29.989  -51.396 -13.293 1.00 91.73  ? 154 LEU E CB  1 
ATOM   9035  C CG  . LEU E 1 151 ? 30.994  -50.964 -14.363 1.00 108.97 ? 154 LEU E CG  1 
ATOM   9036  C CD1 . LEU E 1 151 ? 30.532  -49.692 -15.055 1.00 104.10 ? 154 LEU E CD1 1 
ATOM   9037  C CD2 . LEU E 1 151 ? 32.385  -50.784 -13.773 1.00 119.73 ? 154 LEU E CD2 1 
ATOM   9038  N N   . THR E 1 152 ? 27.892  -54.051 -13.821 1.00 131.06 ? 155 THR E N   1 
ATOM   9039  C CA  . THR E 1 152 ? 27.459  -55.326 -13.255 1.00 128.21 ? 155 THR E CA  1 
ATOM   9040  C C   . THR E 1 152 ? 28.385  -56.443 -13.722 1.00 140.70 ? 155 THR E C   1 
ATOM   9041  O O   . THR E 1 152 ? 29.336  -56.203 -14.465 1.00 144.39 ? 155 THR E O   1 
ATOM   9042  C CB  . THR E 1 152 ? 26.016  -55.680 -13.657 1.00 119.74 ? 155 THR E CB  1 
ATOM   9043  O OG1 . THR E 1 152 ? 25.944  -55.859 -15.077 1.00 126.22 ? 155 THR E OG1 1 
ATOM   9044  C CG2 . THR E 1 152 ? 25.054  -54.581 -13.235 1.00 110.10 ? 155 THR E CG2 1 
ATOM   9045  N N   . GLU E 1 153 ? 28.092  -57.666 -13.292 1.00 164.35 ? 156 GLU E N   1 
ATOM   9046  C CA  . GLU E 1 153 ? 28.946  -58.813 -13.586 1.00 178.97 ? 156 GLU E CA  1 
ATOM   9047  C C   . GLU E 1 153 ? 28.862  -59.285 -15.033 1.00 177.17 ? 156 GLU E C   1 
ATOM   9048  O O   . GLU E 1 153 ? 27.794  -59.263 -15.648 1.00 163.43 ? 156 GLU E O   1 
ATOM   9049  C CB  . GLU E 1 153 ? 28.627  -59.973 -12.637 1.00 182.37 ? 156 GLU E CB  1 
ATOM   9050  C CG  . GLU E 1 153 ? 28.930  -61.354 -13.202 1.00 197.32 ? 156 GLU E CG  1 
ATOM   9051  C CD  . GLU E 1 153 ? 27.843  -61.852 -14.137 1.00 196.93 ? 156 GLU E CD  1 
ATOM   9052  O OE1 . GLU E 1 153 ? 26.764  -61.223 -14.180 1.00 190.68 ? 156 GLU E OE1 1 
ATOM   9053  O OE2 . GLU E 1 153 ? 28.065  -62.866 -14.831 1.00 204.72 ? 156 GLU E OE2 1 
ATOM   9054  N N   . LYS E 1 154 ? 30.004  -59.710 -15.564 1.00 158.39 ? 157 LYS E N   1 
ATOM   9055  C CA  . LYS E 1 154 ? 30.065  -60.361 -16.867 1.00 163.78 ? 157 LYS E CA  1 
ATOM   9056  C C   . LYS E 1 154 ? 31.090  -61.487 -16.824 1.00 177.46 ? 157 LYS E C   1 
ATOM   9057  O O   . LYS E 1 154 ? 32.166  -61.335 -16.246 1.00 184.65 ? 157 LYS E O   1 
ATOM   9058  C CB  . LYS E 1 154 ? 30.418  -59.364 -17.971 1.00 168.76 ? 157 LYS E CB  1 
ATOM   9059  C CG  . LYS E 1 154 ? 30.325  -59.954 -19.371 1.00 168.33 ? 157 LYS E CG  1 
ATOM   9060  C CD  . LYS E 1 154 ? 30.550  -58.906 -20.449 1.00 171.64 ? 157 LYS E CD  1 
ATOM   9061  C CE  . LYS E 1 154 ? 31.978  -58.397 -20.442 1.00 189.18 ? 157 LYS E CE  1 
ATOM   9062  N NZ  . LYS E 1 154 ? 32.195  -57.390 -21.516 1.00 195.92 ? 157 LYS E NZ  1 
ATOM   9063  N N   . GLY E 1 155 ? 30.752  -62.616 -17.438 1.00 111.97 ? 158 GLY E N   1 
ATOM   9064  C CA  . GLY E 1 155 ? 31.598  -63.793 -17.380 1.00 122.93 ? 158 GLY E CA  1 
ATOM   9065  C C   . GLY E 1 155 ? 31.586  -64.388 -15.986 1.00 117.00 ? 158 GLY E C   1 
ATOM   9066  O O   . GLY E 1 155 ? 32.569  -64.984 -15.545 1.00 124.73 ? 158 GLY E O   1 
ATOM   9067  N N   . SER E 1 156 ? 30.465  -64.215 -15.291 1.00 131.79 ? 159 SER E N   1 
ATOM   9068  C CA  . SER E 1 156 ? 30.326  -64.668 -13.911 1.00 125.16 ? 159 SER E CA  1 
ATOM   9069  C C   . SER E 1 156 ? 31.577  -64.349 -13.101 1.00 131.25 ? 159 SER E C   1 
ATOM   9070  O O   . SER E 1 156 ? 31.854  -64.973 -12.076 1.00 129.25 ? 159 SER E O   1 
ATOM   9071  C CB  . SER E 1 156 ? 29.989  -66.156 -13.860 1.00 123.56 ? 159 SER E CB  1 
ATOM   9072  O OG  . SER E 1 156 ? 28.698  -66.387 -14.399 1.00 118.72 ? 159 SER E OG  1 
ATOM   9073  N N   . ASN E 1 157 ? 32.325  -63.366 -13.587 1.00 154.67 ? 160 ASN E N   1 
ATOM   9074  C CA  . ASN E 1 157 ? 33.472  -62.823 -12.881 1.00 156.14 ? 160 ASN E CA  1 
ATOM   9075  C C   . ASN E 1 157 ? 33.352  -61.308 -12.802 1.00 150.33 ? 160 ASN E C   1 
ATOM   9076  O O   . ASN E 1 157 ? 33.064  -60.644 -13.799 1.00 150.20 ? 160 ASN E O   1 
ATOM   9077  C CB  . ASN E 1 157 ? 34.778  -63.206 -13.583 1.00 161.85 ? 160 ASN E CB  1 
ATOM   9078  C CG  . ASN E 1 157 ? 35.353  -64.513 -13.078 1.00 163.93 ? 160 ASN E CG  1 
ATOM   9079  O OD1 . ASN E 1 157 ? 34.639  -65.341 -12.515 1.00 161.54 ? 160 ASN E OD1 1 
ATOM   9080  N ND2 . ASN E 1 157 ? 36.652  -64.703 -13.276 1.00 169.64 ? 160 ASN E ND2 1 
ATOM   9081  N N   . TYR E 1 158 ? 33.551  -60.765 -11.608 1.00 138.61 ? 161 TYR E N   1 
ATOM   9082  C CA  . TYR E 1 158 ? 33.607  -59.325 -11.437 1.00 132.98 ? 161 TYR E CA  1 
ATOM   9083  C C   . TYR E 1 158 ? 34.984  -58.958 -10.912 1.00 126.30 ? 161 TYR E C   1 
ATOM   9084  O O   . TYR E 1 158 ? 35.230  -59.001 -9.705  1.00 119.04 ? 161 TYR E O   1 
ATOM   9085  C CB  . TYR E 1 158 ? 32.521  -58.844 -10.476 1.00 128.97 ? 161 TYR E CB  1 
ATOM   9086  C CG  . TYR E 1 158 ? 32.307  -57.343 -10.490 1.00 131.79 ? 161 TYR E CG  1 
ATOM   9087  C CD1 . TYR E 1 158 ? 31.190  -56.784 -11.101 1.00 126.03 ? 161 TYR E CD1 1 
ATOM   9088  C CD2 . TYR E 1 158 ? 33.223  -56.483 -9.894  1.00 135.59 ? 161 TYR E CD2 1 
ATOM   9089  C CE1 . TYR E 1 158 ? 30.990  -55.409 -11.113 1.00 119.99 ? 161 TYR E CE1 1 
ATOM   9090  C CE2 . TYR E 1 158 ? 33.033  -55.108 -9.904  1.00 130.16 ? 161 TYR E CE2 1 
ATOM   9091  C CZ  . TYR E 1 158 ? 31.915  -54.577 -10.512 1.00 122.45 ? 161 TYR E CZ  1 
ATOM   9092  O OH  . TYR E 1 158 ? 31.726  -53.212 -10.519 1.00 118.13 ? 161 TYR E OH  1 
ATOM   9093  N N   . PRO E 1 159 ? 35.898  -58.613 -11.827 1.00 67.93  ? 162 PRO E N   1 
ATOM   9094  C CA  . PRO E 1 159 ? 37.263  -58.233 -11.461 1.00 72.82  ? 162 PRO E CA  1 
ATOM   9095  C C   . PRO E 1 159 ? 37.361  -56.742 -11.119 1.00 70.87  ? 162 PRO E C   1 
ATOM   9096  O O   . PRO E 1 159 ? 36.638  -55.913 -11.690 1.00 68.24  ? 162 PRO E O   1 
ATOM   9097  C CB  . PRO E 1 159 ? 38.064  -58.554 -12.731 1.00 83.54  ? 162 PRO E CB  1 
ATOM   9098  C CG  . PRO E 1 159 ? 37.049  -58.536 -13.866 1.00 87.45  ? 162 PRO E CG  1 
ATOM   9099  C CD  . PRO E 1 159 ? 35.660  -58.473 -13.274 1.00 78.82  ? 162 PRO E CD  1 
ATOM   9100  N N   . VAL E 1 160 ? 38.255  -56.414 -10.191 1.00 102.71 ? 163 VAL E N   1 
ATOM   9101  C CA  . VAL E 1 160 ? 38.417  -55.040 -9.744  1.00 96.31  ? 163 VAL E CA  1 
ATOM   9102  C C   . VAL E 1 160 ? 38.290  -54.072 -10.916 1.00 96.15  ? 163 VAL E C   1 
ATOM   9103  O O   . VAL E 1 160 ? 38.942  -54.236 -11.944 1.00 99.29  ? 163 VAL E O   1 
ATOM   9104  C CB  . VAL E 1 160 ? 39.764  -54.832 -9.020  1.00 98.17  ? 163 VAL E CB  1 
ATOM   9105  C CG1 . VAL E 1 160 ? 40.927  -55.027 -9.979  1.00 110.09 ? 163 VAL E CG1 1 
ATOM   9106  C CG2 . VAL E 1 160 ? 39.813  -53.453 -8.385  1.00 97.13  ? 163 VAL E CG2 1 
ATOM   9107  N N   . ALA E 1 161 ? 37.420  -53.082 -10.764 1.00 87.06  ? 164 ALA E N   1 
ATOM   9108  C CA  . ALA E 1 161 ? 37.229  -52.074 -11.795 1.00 94.95  ? 164 ALA E CA  1 
ATOM   9109  C C   . ALA E 1 161 ? 38.006  -50.817 -11.430 1.00 97.93  ? 164 ALA E C   1 
ATOM   9110  O O   . ALA E 1 161 ? 37.907  -50.328 -10.304 1.00 94.40  ? 164 ALA E O   1 
ATOM   9111  C CB  . ALA E 1 161 ? 35.749  -51.761 -11.959 1.00 89.30  ? 164 ALA E CB  1 
ATOM   9112  N N   . LYS E 1 162 ? 38.789  -50.304 -12.376 1.00 84.95  ? 165 LYS E N   1 
ATOM   9113  C CA  . LYS E 1 162 ? 39.549  -49.075 -12.148 1.00 89.30  ? 165 LYS E CA  1 
ATOM   9114  C C   . LYS E 1 162 ? 39.081  -47.940 -13.060 1.00 97.31  ? 165 LYS E C   1 
ATOM   9115  O O   . LYS E 1 162 ? 38.582  -48.176 -14.160 1.00 105.59 ? 165 LYS E O   1 
ATOM   9116  C CB  . LYS E 1 162 ? 41.059  -49.316 -12.298 1.00 92.04  ? 165 LYS E CB  1 
ATOM   9117  C CG  . LYS E 1 162 ? 41.704  -50.014 -11.099 1.00 83.41  ? 165 LYS E CG  1 
ATOM   9118  C CD  . LYS E 1 162 ? 43.186  -50.308 -11.330 1.00 94.16  ? 165 LYS E CD  1 
ATOM   9119  C CE  . LYS E 1 162 ? 43.754  -51.197 -10.227 1.00 98.47  ? 165 LYS E CE  1 
ATOM   9120  N NZ  . LYS E 1 162 ? 45.132  -51.682 -10.528 1.00 110.76 ? 165 LYS E NZ  1 
ATOM   9121  N N   . GLY E 1 163 ? 39.237  -46.708 -12.581 1.00 104.56 ? 166 GLY E N   1 
ATOM   9122  C CA  . GLY E 1 163 ? 38.846  -45.529 -13.333 1.00 108.79 ? 166 GLY E CA  1 
ATOM   9123  C C   . GLY E 1 163 ? 39.633  -44.308 -12.897 1.00 107.13 ? 166 GLY E C   1 
ATOM   9124  O O   . GLY E 1 163 ? 39.567  -43.901 -11.739 1.00 109.03 ? 166 GLY E O   1 
ATOM   9125  N N   . SER E 1 164 ? 40.382  -43.721 -13.825 1.00 64.94  ? 167 SER E N   1 
ATOM   9126  C CA  . SER E 1 164 ? 41.253  -42.594 -13.503 1.00 73.12  ? 167 SER E CA  1 
ATOM   9127  C C   . SER E 1 164 ? 41.181  -41.492 -14.563 1.00 84.66  ? 167 SER E C   1 
ATOM   9128  O O   . SER E 1 164 ? 41.066  -41.774 -15.754 1.00 95.74  ? 167 SER E O   1 
ATOM   9129  C CB  . SER E 1 164 ? 42.696  -43.074 -13.329 1.00 83.29  ? 167 SER E CB  1 
ATOM   9130  O OG  . SER E 1 164 ? 43.582  -41.982 -13.183 1.00 91.99  ? 167 SER E OG  1 
ATOM   9131  N N   . TYR E 1 165 ? 41.245  -40.238 -14.124 1.00 90.19  ? 168 TYR E N   1 
ATOM   9132  C CA  . TYR E 1 165 ? 41.178  -39.100 -15.041 1.00 90.41  ? 168 TYR E CA  1 
ATOM   9133  C C   . TYR E 1 165 ? 41.939  -37.876 -14.526 1.00 93.26  ? 168 TYR E C   1 
ATOM   9134  O O   . TYR E 1 165 ? 41.814  -37.498 -13.361 1.00 83.41  ? 168 TYR E O   1 
ATOM   9135  C CB  . TYR E 1 165 ? 39.723  -38.720 -15.339 1.00 76.14  ? 168 TYR E CB  1 
ATOM   9136  C CG  . TYR E 1 165 ? 39.598  -37.323 -15.880 1.00 71.78  ? 168 TYR E CG  1 
ATOM   9137  C CD1 . TYR E 1 165 ? 39.780  -37.059 -17.230 1.00 75.00  ? 168 TYR E CD1 1 
ATOM   9138  C CD2 . TYR E 1 165 ? 39.327  -36.251 -15.036 1.00 62.80  ? 168 TYR E CD2 1 
ATOM   9139  C CE1 . TYR E 1 165 ? 39.680  -35.767 -17.729 1.00 68.85  ? 168 TYR E CE1 1 
ATOM   9140  C CE2 . TYR E 1 165 ? 39.230  -34.956 -15.526 1.00 67.45  ? 168 TYR E CE2 1 
ATOM   9141  C CZ  . TYR E 1 165 ? 39.405  -34.722 -16.871 1.00 67.36  ? 168 TYR E CZ  1 
ATOM   9142  O OH  . TYR E 1 165 ? 39.303  -33.441 -17.351 1.00 70.07  ? 168 TYR E OH  1 
ATOM   9143  N N   . ASN E 1 166 ? 42.717  -37.258 -15.414 1.00 72.71  ? 169 ASN E N   1 
ATOM   9144  C CA  . ASN E 1 166 ? 43.478  -36.041 -15.108 1.00 70.14  ? 169 ASN E CA  1 
ATOM   9145  C C   . ASN E 1 166 ? 42.675  -34.805 -15.527 1.00 66.79  ? 169 ASN E C   1 
ATOM   9146  O O   . ASN E 1 166 ? 42.334  -34.661 -16.698 1.00 68.99  ? 169 ASN E O   1 
ATOM   9147  C CB  . ASN E 1 166 ? 44.827  -36.096 -15.841 1.00 81.11  ? 169 ASN E CB  1 
ATOM   9148  C CG  . ASN E 1 166 ? 45.772  -34.966 -15.458 1.00 88.98  ? 169 ASN E CG  1 
ATOM   9149  O OD1 . ASN E 1 166 ? 45.938  -34.003 -16.207 1.00 89.26  ? 169 ASN E OD1 1 
ATOM   9150  N ND2 . ASN E 1 166 ? 46.429  -35.102 -14.311 1.00 97.60  ? 169 ASN E ND2 1 
ATOM   9151  N N   . ASN E 1 167 ? 42.349  -33.931 -14.576 1.00 95.39  ? 170 ASN E N   1 
ATOM   9152  C CA  . ASN E 1 167 ? 41.566  -32.734 -14.898 1.00 96.55  ? 170 ASN E CA  1 
ATOM   9153  C C   . ASN E 1 167 ? 42.346  -31.742 -15.749 1.00 107.49 ? 170 ASN E C   1 
ATOM   9154  O O   . ASN E 1 167 ? 43.254  -31.069 -15.263 1.00 106.33 ? 170 ASN E O   1 
ATOM   9155  C CB  . ASN E 1 167 ? 41.042  -32.029 -13.641 1.00 85.71  ? 170 ASN E CB  1 
ATOM   9156  C CG  . ASN E 1 167 ? 40.016  -30.938 -13.966 1.00 80.76  ? 170 ASN E CG  1 
ATOM   9157  O OD1 . ASN E 1 167 ? 39.185  -31.097 -14.865 1.00 84.45  ? 170 ASN E OD1 1 
ATOM   9158  N ND2 . ASN E 1 167 ? 40.078  -29.825 -13.237 1.00 70.45  ? 170 ASN E ND2 1 
ATOM   9159  N N   . THR E 1 168 ? 41.977  -31.657 -17.021 1.00 126.16 ? 171 THR E N   1 
ATOM   9160  C CA  . THR E 1 168 ? 42.653  -30.777 -17.962 1.00 130.91 ? 171 THR E CA  1 
ATOM   9161  C C   . THR E 1 168 ? 41.641  -29.959 -18.758 1.00 131.96 ? 171 THR E C   1 
ATOM   9162  O O   . THR E 1 168 ? 41.938  -29.503 -19.861 1.00 141.76 ? 171 THR E O   1 
ATOM   9163  C CB  . THR E 1 168 ? 43.531  -31.584 -18.939 1.00 135.87 ? 171 THR E CB  1 
ATOM   9164  O OG1 . THR E 1 168 ? 42.762  -32.659 -19.495 1.00 130.01 ? 171 THR E OG1 1 
ATOM   9165  C CG2 . THR E 1 168 ? 44.741  -32.162 -18.221 1.00 137.45 ? 171 THR E CG2 1 
ATOM   9166  N N   . SER E 1 169 ? 40.448  -29.774 -18.198 1.00 107.00 ? 172 SER E N   1 
ATOM   9167  C CA  . SER E 1 169 ? 39.382  -29.054 -18.895 1.00 110.84 ? 172 SER E CA  1 
ATOM   9168  C C   . SER E 1 169 ? 39.464  -27.545 -18.670 1.00 112.59 ? 172 SER E C   1 
ATOM   9169  O O   . SER E 1 169 ? 38.499  -26.817 -18.922 1.00 113.91 ? 172 SER E O   1 
ATOM   9170  C CB  . SER E 1 169 ? 38.006  -29.569 -18.473 1.00 103.44 ? 172 SER E CB  1 
ATOM   9171  O OG  . SER E 1 169 ? 37.535  -28.885 -17.325 1.00 99.92  ? 172 SER E OG  1 
ATOM   9172  N N   . GLY E 1 170 ? 40.619  -27.087 -18.195 1.00 142.66 ? 173 GLY E N   1 
ATOM   9173  C CA  . GLY E 1 170 ? 40.859  -25.672 -17.970 1.00 142.55 ? 173 GLY E CA  1 
ATOM   9174  C C   . GLY E 1 170 ? 40.296  -25.167 -16.655 1.00 132.09 ? 173 GLY E C   1 
ATOM   9175  O O   . GLY E 1 170 ? 40.864  -24.279 -16.021 1.00 131.80 ? 173 GLY E O   1 
ATOM   9176  N N   . GLU E 1 171 ? 39.170  -25.741 -16.249 1.00 106.55 ? 174 GLU E N   1 
ATOM   9177  C CA  . GLU E 1 171 ? 38.493  -25.340 -15.027 1.00 88.53  ? 174 GLU E CA  1 
ATOM   9178  C C   . GLU E 1 171 ? 38.235  -26.556 -14.146 1.00 75.52  ? 174 GLU E C   1 
ATOM   9179  O O   . GLU E 1 171 ? 38.736  -27.643 -14.425 1.00 73.38  ? 174 GLU E O   1 
ATOM   9180  C CB  . GLU E 1 171 ? 37.183  -24.640 -15.373 1.00 88.27  ? 174 GLU E CB  1 
ATOM   9181  C CG  . GLU E 1 171 ? 36.391  -25.335 -16.468 1.00 93.97  ? 174 GLU E CG  1 
ATOM   9182  C CD  . GLU E 1 171 ? 35.416  -24.402 -17.153 1.00 96.25  ? 174 GLU E CD  1 
ATOM   9183  O OE1 . GLU E 1 171 ? 35.722  -23.195 -17.260 1.00 93.44  ? 174 GLU E OE1 1 
ATOM   9184  O OE2 . GLU E 1 171 ? 34.342  -24.870 -17.581 1.00 97.41  ? 174 GLU E OE2 1 
ATOM   9185  N N   . GLN E 1 172 ? 37.460  -26.372 -13.082 1.00 118.29 ? 175 GLN E N   1 
ATOM   9186  C CA  . GLN E 1 172 ? 37.167  -27.465 -12.161 1.00 106.21 ? 175 GLN E CA  1 
ATOM   9187  C C   . GLN E 1 172 ? 36.073  -28.369 -12.703 1.00 101.88 ? 175 GLN E C   1 
ATOM   9188  O O   . GLN E 1 172 ? 35.320  -27.980 -13.596 1.00 103.09 ? 175 GLN E O   1 
ATOM   9189  C CB  . GLN E 1 172 ? 36.749  -26.921 -10.803 1.00 99.39  ? 175 GLN E CB  1 
ATOM   9190  C CG  . GLN E 1 172 ? 37.746  -25.967 -10.196 1.00 103.95 ? 175 GLN E CG  1 
ATOM   9191  C CD  . GLN E 1 172 ? 37.406  -25.632 -8.760  1.00 91.79  ? 175 GLN E CD  1 
ATOM   9192  O OE1 . GLN E 1 172 ? 36.847  -26.462 -8.036  1.00 79.53  ? 175 GLN E OE1 1 
ATOM   9193  N NE2 . GLN E 1 172 ? 37.736  -24.409 -8.339  1.00 88.82  ? 175 GLN E NE2 1 
ATOM   9194  N N   . MET E 1 173 ? 35.978  -29.575 -12.155 1.00 68.26  ? 176 MET E N   1 
ATOM   9195  C CA  . MET E 1 173 ? 34.991  -30.525 -12.650 1.00 70.85  ? 176 MET E CA  1 
ATOM   9196  C C   . MET E 1 173 ? 34.150  -31.195 -11.561 1.00 55.98  ? 176 MET E C   1 
ATOM   9197  O O   . MET E 1 173 ? 34.670  -31.726 -10.579 1.00 49.65  ? 176 MET E O   1 
ATOM   9198  C CB  . MET E 1 173 ? 35.655  -31.573 -13.544 1.00 81.15  ? 176 MET E CB  1 
ATOM   9199  C CG  . MET E 1 173 ? 34.684  -32.280 -14.478 1.00 82.13  ? 176 MET E CG  1 
ATOM   9200  S SD  . MET E 1 173 ? 35.542  -33.186 -15.773 1.00 119.70 ? 176 MET E SD  1 
ATOM   9201  C CE  . MET E 1 173 ? 36.755  -31.961 -16.262 1.00 77.51  ? 176 MET E CE  1 
ATOM   9202  N N   . LEU E 1 174 ? 32.839  -31.150 -11.760 1.00 129.70 ? 177 LEU E N   1 
ATOM   9203  C CA  . LEU E 1 174 ? 31.895  -31.794 -10.869 1.00 116.10 ? 177 LEU E CA  1 
ATOM   9204  C C   . LEU E 1 174 ? 31.641  -33.210 -11.348 1.00 120.41 ? 177 LEU E C   1 
ATOM   9205  O O   . LEU E 1 174 ? 30.906  -33.425 -12.310 1.00 119.62 ? 177 LEU E O   1 
ATOM   9206  C CB  . LEU E 1 174 ? 30.584  -31.013 -10.844 1.00 84.21  ? 177 LEU E CB  1 
ATOM   9207  C CG  . LEU E 1 174 ? 29.333  -31.794 -10.440 1.00 57.23  ? 177 LEU E CG  1 
ATOM   9208  C CD1 . LEU E 1 174 ? 29.455  -32.351 -9.017  1.00 52.19  ? 177 LEU E CD1 1 
ATOM   9209  C CD2 . LEU E 1 174 ? 28.090  -30.932 -10.596 1.00 35.81  ? 177 LEU E CD2 1 
ATOM   9210  N N   . ILE E 1 175 ? 32.259  -34.177 -10.678 1.00 109.39 ? 178 ILE E N   1 
ATOM   9211  C CA  . ILE E 1 175 ? 32.082  -35.587 -11.019 1.00 101.81 ? 178 ILE E CA  1 
ATOM   9212  C C   . ILE E 1 175 ? 31.195  -36.259 -9.974  1.00 82.68  ? 178 ILE E C   1 
ATOM   9213  O O   . ILE E 1 175 ? 31.246  -35.912 -8.796  1.00 82.34  ? 178 ILE E O   1 
ATOM   9214  C CB  . ILE E 1 175 ? 33.437  -36.307 -11.112 1.00 103.85 ? 178 ILE E CB  1 
ATOM   9215  C CG1 . ILE E 1 175 ? 34.369  -35.542 -12.057 1.00 111.78 ? 178 ILE E CG1 1 
ATOM   9216  C CG2 . ILE E 1 175 ? 33.244  -37.755 -11.555 1.00 101.10 ? 178 ILE E CG2 1 
ATOM   9217  C CD1 . ILE E 1 175 ? 35.780  -35.384 -11.543 1.00 116.62 ? 178 ILE E CD1 1 
ATOM   9218  N N   . ILE E 1 176 ? 30.380  -37.215 -10.403 1.00 124.30 ? 179 ILE E N   1 
ATOM   9219  C CA  . ILE E 1 176 ? 29.375  -37.785 -9.517  1.00 109.69 ? 179 ILE E CA  1 
ATOM   9220  C C   . ILE E 1 176 ? 29.321  -39.303 -9.562  1.00 113.68 ? 179 ILE E C   1 
ATOM   9221  O O   . ILE E 1 176 ? 29.157  -39.891 -10.627 1.00 134.68 ? 179 ILE E O   1 
ATOM   9222  C CB  . ILE E 1 176 ? 27.986  -37.254 -9.875  1.00 72.13  ? 179 ILE E CB  1 
ATOM   9223  C CG1 . ILE E 1 176 ? 27.945  -35.741 -9.684  1.00 63.41  ? 179 ILE E CG1 1 
ATOM   9224  C CG2 . ILE E 1 176 ? 26.917  -37.935 -9.040  1.00 61.65  ? 179 ILE E CG2 1 
ATOM   9225  C CD1 . ILE E 1 176 ? 26.589  -35.132 -9.944  1.00 55.35  ? 179 ILE E CD1 1 
ATOM   9226  N N   . TRP E 1 177 ? 29.437  -39.940 -8.403  1.00 66.34  ? 180 TRP E N   1 
ATOM   9227  C CA  . TRP E 1 177 ? 29.340  -41.396 -8.354  1.00 67.79  ? 180 TRP E CA  1 
ATOM   9228  C C   . TRP E 1 177 ? 28.268  -41.900 -7.388  1.00 54.30  ? 180 TRP E C   1 
ATOM   9229  O O   . TRP E 1 177 ? 27.447  -41.129 -6.888  1.00 46.36  ? 180 TRP E O   1 
ATOM   9230  C CB  . TRP E 1 177 ? 30.700  -42.029 -8.049  1.00 89.71  ? 180 TRP E CB  1 
ATOM   9231  C CG  . TRP E 1 177 ? 31.202  -41.797 -6.667  1.00 97.15  ? 180 TRP E CG  1 
ATOM   9232  C CD1 . TRP E 1 177 ? 31.179  -42.676 -5.633  1.00 91.64  ? 180 TRP E CD1 1 
ATOM   9233  C CD2 . TRP E 1 177 ? 31.818  -40.607 -6.167  1.00 103.43 ? 180 TRP E CD2 1 
ATOM   9234  N NE1 . TRP E 1 177 ? 31.742  -42.114 -4.518  1.00 90.61  ? 180 TRP E NE1 1 
ATOM   9235  C CE2 . TRP E 1 177 ? 32.140  -40.840 -4.819  1.00 96.78  ? 180 TRP E CE2 1 
ATOM   9236  C CE3 . TRP E 1 177 ? 32.123  -39.365 -6.726  1.00 113.73 ? 180 TRP E CE3 1 
ATOM   9237  C CZ2 . TRP E 1 177 ? 32.754  -39.877 -4.021  1.00 97.57  ? 180 TRP E CZ2 1 
ATOM   9238  C CZ3 . TRP E 1 177 ? 32.734  -38.410 -5.932  1.00 113.88 ? 180 TRP E CZ3 1 
ATOM   9239  C CH2 . TRP E 1 177 ? 33.040  -38.671 -4.596  1.00 106.69 ? 180 TRP E CH2 1 
ATOM   9240  N N   . GLY E 1 178 ? 28.272  -43.204 -7.151  1.00 59.02  ? 181 GLY E N   1 
ATOM   9241  C CA  . GLY E 1 178 ? 27.304  -43.827 -6.271  1.00 53.10  ? 181 GLY E CA  1 
ATOM   9242  C C   . GLY E 1 178 ? 27.623  -45.295 -6.027  1.00 55.63  ? 181 GLY E C   1 
ATOM   9243  O O   . GLY E 1 178 ? 28.299  -45.935 -6.830  1.00 59.14  ? 181 GLY E O   1 
ATOM   9244  N N   . VAL E 1 179 ? 27.150  -45.827 -4.906  1.00 53.98  ? 182 VAL E N   1 
ATOM   9245  C CA  . VAL E 1 179 ? 27.278  -47.244 -4.625  1.00 64.29  ? 182 VAL E CA  1 
ATOM   9246  C C   . VAL E 1 179 ? 25.874  -47.799 -4.478  1.00 67.99  ? 182 VAL E C   1 
ATOM   9247  O O   . VAL E 1 179 ? 24.928  -47.042 -4.252  1.00 63.75  ? 182 VAL E O   1 
ATOM   9248  C CB  . VAL E 1 179 ? 28.083  -47.497 -3.344  1.00 69.36  ? 182 VAL E CB  1 
ATOM   9249  C CG1 . VAL E 1 179 ? 29.452  -46.865 -3.455  1.00 89.75  ? 182 VAL E CG1 1 
ATOM   9250  C CG2 . VAL E 1 179 ? 27.346  -46.940 -2.147  1.00 55.21  ? 182 VAL E CG2 1 
ATOM   9251  N N   . HIS E 1 180 ? 25.732  -49.113 -4.617  1.00 85.51  ? 183 HIS E N   1 
ATOM   9252  C CA  . HIS E 1 180 ? 24.421  -49.747 -4.558  1.00 80.88  ? 183 HIS E CA  1 
ATOM   9253  C C   . HIS E 1 180 ? 24.217  -50.484 -3.238  1.00 82.94  ? 183 HIS E C   1 
ATOM   9254  O O   . HIS E 1 180 ? 25.158  -51.047 -2.683  1.00 90.41  ? 183 HIS E O   1 
ATOM   9255  C CB  . HIS E 1 180 ? 24.248  -50.705 -5.732  1.00 82.90  ? 183 HIS E CB  1 
ATOM   9256  C CG  . HIS E 1 180 ? 22.930  -51.411 -5.742  1.00 97.32  ? 183 HIS E CG  1 
ATOM   9257  N ND1 . HIS E 1 180 ? 22.732  -52.608 -6.398  1.00 106.30 ? 183 HIS E ND1 1 
ATOM   9258  C CD2 . HIS E 1 180 ? 21.743  -51.089 -5.178  1.00 106.29 ? 183 HIS E CD2 1 
ATOM   9259  C CE1 . HIS E 1 180 ? 21.480  -52.994 -6.235  1.00 115.27 ? 183 HIS E CE1 1 
ATOM   9260  N NE2 . HIS E 1 180 ? 20.859  -52.092 -5.497  1.00 117.19 ? 183 HIS E NE2 1 
ATOM   9261  N N   . HIS E 1 181 ? 22.985  -50.475 -2.738  1.00 88.41  ? 184 HIS E N   1 
ATOM   9262  C CA  . HIS E 1 181 ? 22.665  -51.135 -1.477  1.00 88.67  ? 184 HIS E CA  1 
ATOM   9263  C C   . HIS E 1 181 ? 21.515  -52.124 -1.646  1.00 104.13 ? 184 HIS E C   1 
ATOM   9264  O O   . HIS E 1 181 ? 20.359  -51.786 -1.387  1.00 111.32 ? 184 HIS E O   1 
ATOM   9265  C CB  . HIS E 1 181 ? 22.319  -50.102 -0.401  1.00 81.38  ? 184 HIS E CB  1 
ATOM   9266  C CG  . HIS E 1 181 ? 23.439  -49.162 -0.084  1.00 77.17  ? 184 HIS E CG  1 
ATOM   9267  N ND1 . HIS E 1 181 ? 24.542  -49.541 0.650   1.00 80.97  ? 184 HIS E ND1 1 
ATOM   9268  C CD2 . HIS E 1 181 ? 23.632  -47.862 -0.406  1.00 77.43  ? 184 HIS E CD2 1 
ATOM   9269  C CE1 . HIS E 1 181 ? 25.365  -48.515 0.768   1.00 81.00  ? 184 HIS E CE1 1 
ATOM   9270  N NE2 . HIS E 1 181 ? 24.836  -47.483 0.136   1.00 77.76  ? 184 HIS E NE2 1 
ATOM   9271  N N   . PRO E 1 182 ? 21.836  -53.354 -2.085  1.00 91.79  ? 185 PRO E N   1 
ATOM   9272  C CA  . PRO E 1 182 ? 20.897  -54.449 -2.377  1.00 102.58 ? 185 PRO E CA  1 
ATOM   9273  C C   . PRO E 1 182 ? 20.118  -54.960 -1.161  1.00 111.42 ? 185 PRO E C   1 
ATOM   9274  O O   . PRO E 1 182 ? 20.615  -54.904 -0.035  1.00 102.49 ? 185 PRO E O   1 
ATOM   9275  C CB  . PRO E 1 182 ? 21.810  -55.551 -2.916  1.00 99.70  ? 185 PRO E CB  1 
ATOM   9276  C CG  . PRO E 1 182 ? 23.013  -54.825 -3.438  1.00 93.72  ? 185 PRO E CG  1 
ATOM   9277  C CD  . PRO E 1 182 ? 23.213  -53.695 -2.485  1.00 89.33  ? 185 PRO E CD  1 
ATOM   9278  N N   . ASN E 1 183 ? 18.912  -55.469 -1.407  1.00 121.49 ? 186 ASN E N   1 
ATOM   9279  C CA  . ASN E 1 183 ? 17.992  -55.875 -0.340  1.00 127.90 ? 186 ASN E CA  1 
ATOM   9280  C C   . ASN E 1 183 ? 18.399  -57.175 0.357   1.00 129.08 ? 186 ASN E C   1 
ATOM   9281  O O   . ASN E 1 183 ? 18.415  -57.247 1.586   1.00 122.97 ? 186 ASN E O   1 
ATOM   9282  C CB  . ASN E 1 183 ? 16.560  -55.992 -0.883  1.00 127.77 ? 186 ASN E CB  1 
ATOM   9283  C CG  . ASN E 1 183 ? 15.507  -55.971 0.217   1.00 122.42 ? 186 ASN E CG  1 
ATOM   9284  O OD1 . ASN E 1 183 ? 15.669  -55.303 1.240   1.00 115.48 ? 186 ASN E OD1 1 
ATOM   9285  N ND2 . ASN E 1 183 ? 14.419  -56.703 0.007   1.00 122.67 ? 186 ASN E ND2 1 
ATOM   9286  N N   . ASP E 1 184 ? 18.719  -58.197 -0.435  1.00 123.80 ? 187 ASP E N   1 
ATOM   9287  C CA  . ASP E 1 184 ? 19.123  -59.500 0.096   1.00 121.52 ? 187 ASP E CA  1 
ATOM   9288  C C   . ASP E 1 184 ? 20.469  -59.925 -0.483  1.00 119.24 ? 187 ASP E C   1 
ATOM   9289  O O   . ASP E 1 184 ? 21.006  -59.260 -1.371  1.00 115.27 ? 187 ASP E O   1 
ATOM   9290  C CB  . ASP E 1 184 ? 18.061  -60.562 -0.209  1.00 126.01 ? 187 ASP E CB  1 
ATOM   9291  C CG  . ASP E 1 184 ? 17.785  -60.705 -1.700  1.00 130.17 ? 187 ASP E CG  1 
ATOM   9292  O OD1 . ASP E 1 184 ? 16.675  -61.151 -2.059  1.00 126.95 ? 187 ASP E OD1 1 
ATOM   9293  O OD2 . ASP E 1 184 ? 18.673  -60.372 -2.515  1.00 135.14 ? 187 ASP E OD2 1 
ATOM   9294  N N   . GLU E 1 185 ? 21.010  -61.035 0.012   1.00 130.44 ? 188 GLU E N   1 
ATOM   9295  C CA  . GLU E 1 185 ? 22.294  -61.530 -0.475  1.00 127.72 ? 188 GLU E CA  1 
ATOM   9296  C C   . GLU E 1 185 ? 22.188  -62.056 -1.905  1.00 125.07 ? 188 GLU E C   1 
ATOM   9297  O O   . GLU E 1 185 ? 23.069  -61.817 -2.734  1.00 118.29 ? 188 GLU E O   1 
ATOM   9298  C CB  . GLU E 1 185 ? 22.841  -62.628 0.437   1.00 125.38 ? 188 GLU E CB  1 
ATOM   9299  C CG  . GLU E 1 185 ? 24.268  -63.034 0.091   1.00 126.85 ? 188 GLU E CG  1 
ATOM   9300  C CD  . GLU E 1 185 ? 24.565  -64.491 0.398   1.00 124.58 ? 188 GLU E CD  1 
ATOM   9301  O OE1 . GLU E 1 185 ? 25.751  -64.884 0.326   1.00 118.66 ? 188 GLU E OE1 1 
ATOM   9302  O OE2 . GLU E 1 185 ? 23.614  -65.244 0.705   1.00 126.14 ? 188 GLU E OE2 1 
ATOM   9303  N N   . THR E 1 186 ? 21.103  -62.774 -2.185  1.00 96.97  ? 189 THR E N   1 
ATOM   9304  C CA  . THR E 1 186 ? 20.903  -63.389 -3.497  1.00 104.34 ? 189 THR E CA  1 
ATOM   9305  C C   . THR E 1 186 ? 20.838  -62.359 -4.636  1.00 103.68 ? 189 THR E C   1 
ATOM   9306  O O   . THR E 1 186 ? 21.012  -62.709 -5.803  1.00 100.42 ? 189 THR E O   1 
ATOM   9307  C CB  . THR E 1 186 ? 19.660  -64.321 -3.509  1.00 93.13  ? 189 THR E CB  1 
ATOM   9308  O OG1 . THR E 1 186 ? 18.715  -63.869 -4.486  1.00 95.22  ? 189 THR E OG1 1 
ATOM   9309  C CG2 . THR E 1 186 ? 18.998  -64.356 -2.138  1.00 88.59  ? 189 THR E CG2 1 
ATOM   9310  N N   . GLU E 1 187 ? 20.598  -61.096 -4.289  1.00 106.81 ? 190 GLU E N   1 
ATOM   9311  C CA  . GLU E 1 187 ? 20.605  -60.009 -5.267  1.00 110.02 ? 190 GLU E CA  1 
ATOM   9312  C C   . GLU E 1 187 ? 22.039  -59.557 -5.553  1.00 100.48 ? 190 GLU E C   1 
ATOM   9313  O O   . GLU E 1 187 ? 22.439  -59.393 -6.710  1.00 94.70  ? 190 GLU E O   1 
ATOM   9314  C CB  . GLU E 1 187 ? 19.767  -58.828 -4.763  1.00 109.04 ? 190 GLU E CB  1 
ATOM   9315  C CG  . GLU E 1 187 ? 19.823  -57.585 -5.651  1.00 109.79 ? 190 GLU E CG  1 
ATOM   9316  C CD  . GLU E 1 187 ? 19.102  -56.387 -5.042  1.00 108.99 ? 190 GLU E CD  1 
ATOM   9317  O OE1 . GLU E 1 187 ? 18.324  -56.578 -4.080  1.00 105.29 ? 190 GLU E OE1 1 
ATOM   9318  O OE2 . GLU E 1 187 ? 19.318  -55.252 -5.524  1.00 110.59 ? 190 GLU E OE2 1 
ATOM   9319  N N   . GLN E 1 188 ? 22.803  -59.361 -4.481  1.00 101.78 ? 191 GLN E N   1 
ATOM   9320  C CA  . GLN E 1 188 ? 24.216  -59.002 -4.573  1.00 96.40  ? 191 GLN E CA  1 
ATOM   9321  C C   . GLN E 1 188 ? 24.988  -59.959 -5.482  1.00 107.15 ? 191 GLN E C   1 
ATOM   9322  O O   . GLN E 1 188 ? 25.669  -59.532 -6.415  1.00 108.50 ? 191 GLN E O   1 
ATOM   9323  C CB  . GLN E 1 188 ? 24.835  -58.985 -3.170  1.00 87.87  ? 191 GLN E CB  1 
ATOM   9324  C CG  . GLN E 1 188 ? 26.352  -59.098 -3.132  1.00 95.54  ? 191 GLN E CG  1 
ATOM   9325  C CD  . GLN E 1 188 ? 27.047  -57.753 -3.041  1.00 100.12 ? 191 GLN E CD  1 
ATOM   9326  O OE1 . GLN E 1 188 ? 26.681  -56.801 -3.735  1.00 95.71  ? 191 GLN E OE1 1 
ATOM   9327  N NE2 . GLN E 1 188 ? 28.056  -57.666 -2.177  1.00 111.40 ? 191 GLN E NE2 1 
ATOM   9328  N N   . ARG E 1 189 ? 24.868  -61.255 -5.195  1.00 102.77 ? 192 ARG E N   1 
ATOM   9329  C CA  . ARG E 1 189 ? 25.554  -62.303 -5.948  1.00 100.12 ? 192 ARG E CA  1 
ATOM   9330  C C   . ARG E 1 189 ? 25.152  -62.271 -7.424  1.00 86.78  ? 192 ARG E C   1 
ATOM   9331  O O   . ARG E 1 189 ? 26.007  -62.210 -8.313  1.00 77.07  ? 192 ARG E O   1 
ATOM   9332  C CB  . ARG E 1 189 ? 25.231  -63.672 -5.335  1.00 106.08 ? 192 ARG E CB  1 
ATOM   9333  C CG  . ARG E 1 189 ? 26.107  -64.828 -5.813  1.00 115.29 ? 192 ARG E CG  1 
ATOM   9334  C CD  . ARG E 1 189 ? 27.422  -64.913 -5.043  1.00 115.92 ? 192 ARG E CD  1 
ATOM   9335  N NE  . ARG E 1 189 ? 27.216  -65.117 -3.609  1.00 108.15 ? 192 ARG E NE  1 
ATOM   9336  C CZ  . ARG E 1 189 ? 28.187  -65.413 -2.747  1.00 103.82 ? 192 ARG E CZ  1 
ATOM   9337  N NH1 . ARG E 1 189 ? 29.438  -65.550 -3.171  1.00 105.33 ? 192 ARG E NH1 1 
ATOM   9338  N NH2 . ARG E 1 189 ? 27.905  -65.575 -1.459  1.00 96.28  ? 192 ARG E NH2 1 
ATOM   9339  N N   . THR E 1 190 ? 23.843  -62.308 -7.669  1.00 84.46  ? 193 THR E N   1 
ATOM   9340  C CA  . THR E 1 190 ? 23.285  -62.268 -9.021  1.00 94.11  ? 193 THR E CA  1 
ATOM   9341  C C   . THR E 1 190 ? 23.892  -61.158 -9.873  1.00 94.97  ? 193 THR E C   1 
ATOM   9342  O O   . THR E 1 190 ? 23.977  -61.276 -11.096 1.00 96.00  ? 193 THR E O   1 
ATOM   9343  C CB  . THR E 1 190 ? 21.748  -62.066 -8.987  1.00 101.21 ? 193 THR E CB  1 
ATOM   9344  O OG1 . THR E 1 190 ? 21.124  -63.179 -8.333  1.00 107.04 ? 193 THR E OG1 1 
ATOM   9345  C CG2 . THR E 1 190 ? 21.185  -61.930 -10.398 1.00 104.74 ? 193 THR E CG2 1 
ATOM   9346  N N   . LEU E 1 191 ? 24.322  -60.084 -9.217  1.00 129.45 ? 194 LEU E N   1 
ATOM   9347  C CA  . LEU E 1 191 ? 24.743  -58.877 -9.921  1.00 124.72 ? 194 LEU E CA  1 
ATOM   9348  C C   . LEU E 1 191 ? 26.243  -58.606 -9.890  1.00 130.95 ? 194 LEU E C   1 
ATOM   9349  O O   . LEU E 1 191 ? 26.816  -58.172 -10.889 1.00 131.40 ? 194 LEU E O   1 
ATOM   9350  C CB  . LEU E 1 191 ? 23.988  -57.667 -9.372  1.00 108.37 ? 194 LEU E CB  1 
ATOM   9351  C CG  . LEU E 1 191 ? 22.566  -57.516 -9.907  1.00 102.22 ? 194 LEU E CG  1 
ATOM   9352  C CD1 . LEU E 1 191 ? 21.646  -56.863 -8.886  1.00 93.48  ? 194 LEU E CD1 1 
ATOM   9353  C CD2 . LEU E 1 191 ? 22.589  -56.735 -11.214 1.00 102.45 ? 194 LEU E CD2 1 
ATOM   9354  N N   . TYR E 1 192 ? 26.876  -58.853 -8.749  1.00 134.15 ? 195 TYR E N   1 
ATOM   9355  C CA  . TYR E 1 192 ? 28.281  -58.496 -8.577  1.00 143.35 ? 195 TYR E CA  1 
ATOM   9356  C C   . TYR E 1 192 ? 29.179  -59.701 -8.297  1.00 153.86 ? 195 TYR E C   1 
ATOM   9357  O O   . TYR E 1 192 ? 30.403  -59.575 -8.282  1.00 164.86 ? 195 TYR E O   1 
ATOM   9358  C CB  . TYR E 1 192 ? 28.426  -57.418 -7.492  1.00 135.81 ? 195 TYR E CB  1 
ATOM   9359  C CG  . TYR E 1 192 ? 27.591  -56.182 -7.779  1.00 119.30 ? 195 TYR E CG  1 
ATOM   9360  C CD1 . TYR E 1 192 ? 28.072  -55.168 -8.600  1.00 120.92 ? 195 TYR E CD1 1 
ATOM   9361  C CD2 . TYR E 1 192 ? 26.314  -56.041 -7.248  1.00 104.99 ? 195 TYR E CD2 1 
ATOM   9362  C CE1 . TYR E 1 192 ? 27.307  -54.048 -8.877  1.00 109.16 ? 195 TYR E CE1 1 
ATOM   9363  C CE2 . TYR E 1 192 ? 25.545  -54.924 -7.520  1.00 98.97  ? 195 TYR E CE2 1 
ATOM   9364  C CZ  . TYR E 1 192 ? 26.046  -53.932 -8.333  1.00 99.37  ? 195 TYR E CZ  1 
ATOM   9365  O OH  . TYR E 1 192 ? 25.279  -52.825 -8.605  1.00 94.75  ? 195 TYR E OH  1 
ATOM   9366  N N   . GLN E 1 193 ? 28.564  -60.866 -8.101  1.00 120.14 ? 196 GLN E N   1 
ATOM   9367  C CA  . GLN E 1 193 ? 29.293  -62.112 -7.853  1.00 118.29 ? 196 GLN E CA  1 
ATOM   9368  C C   . GLN E 1 193 ? 30.127  -62.056 -6.576  1.00 107.43 ? 196 GLN E C   1 
ATOM   9369  O O   . GLN E 1 193 ? 29.840  -62.761 -5.605  1.00 105.71 ? 196 GLN E O   1 
ATOM   9370  C CB  . GLN E 1 193 ? 30.180  -62.476 -9.048  1.00 126.50 ? 196 GLN E CB  1 
ATOM   9371  C CG  . GLN E 1 193 ? 29.425  -63.035 -10.246 1.00 128.88 ? 196 GLN E CG  1 
ATOM   9372  C CD  . GLN E 1 193 ? 29.245  -64.543 -10.185 1.00 130.86 ? 196 GLN E CD  1 
ATOM   9373  O OE1 . GLN E 1 193 ? 28.824  -65.164 -11.160 1.00 135.20 ? 196 GLN E OE1 1 
ATOM   9374  N NE2 . GLN E 1 193 ? 29.567  -65.139 -9.039  1.00 125.32 ? 196 GLN E NE2 1 
ATOM   9375  N N   . ASN E 1 194 ? 31.165  -61.225 -6.587  1.00 77.91  ? 197 ASN E N   1 
ATOM   9376  C CA  . ASN E 1 194 ? 31.981  -61.011 -5.401  1.00 75.83  ? 197 ASN E CA  1 
ATOM   9377  C C   . ASN E 1 194 ? 31.100  -60.610 -4.224  1.00 64.11  ? 197 ASN E C   1 
ATOM   9378  O O   . ASN E 1 194 ? 29.926  -60.287 -4.397  1.00 59.41  ? 197 ASN E O   1 
ATOM   9379  C CB  . ASN E 1 194 ? 33.048  -59.938 -5.652  1.00 87.84  ? 197 ASN E CB  1 
ATOM   9380  C CG  . ASN E 1 194 ? 34.102  -60.376 -6.653  1.00 103.29 ? 197 ASN E CG  1 
ATOM   9381  O OD1 . ASN E 1 194 ? 33.868  -61.262 -7.474  1.00 110.53 ? 197 ASN E OD1 1 
ATOM   9382  N ND2 . ASN E 1 194 ? 35.273  -59.752 -6.587  1.00 103.46 ? 197 ASN E ND2 1 
ATOM   9383  N N   . VAL E 1 195 ? 31.668  -60.636 -3.025  1.00 84.64  ? 198 VAL E N   1 
ATOM   9384  C CA  . VAL E 1 195 ? 30.921  -60.294 -1.824  1.00 74.91  ? 198 VAL E CA  1 
ATOM   9385  C C   . VAL E 1 195 ? 31.869  -59.704 -0.795  1.00 81.35  ? 198 VAL E C   1 
ATOM   9386  O O   . VAL E 1 195 ? 33.050  -60.056 -0.757  1.00 87.48  ? 198 VAL E O   1 
ATOM   9387  C CB  . VAL E 1 195 ? 30.199  -61.522 -1.240  1.00 73.31  ? 198 VAL E CB  1 
ATOM   9388  C CG1 . VAL E 1 195 ? 29.797  -61.269 0.205   1.00 74.56  ? 198 VAL E CG1 1 
ATOM   9389  C CG2 . VAL E 1 195 ? 28.983  -61.875 -2.090  1.00 67.94  ? 198 VAL E CG2 1 
ATOM   9390  N N   . GLY E 1 196 ? 31.353  -58.807 0.038   1.00 110.02 ? 199 GLY E N   1 
ATOM   9391  C CA  . GLY E 1 196 ? 32.211  -58.007 0.886   1.00 114.32 ? 199 GLY E CA  1 
ATOM   9392  C C   . GLY E 1 196 ? 32.959  -57.069 -0.037  1.00 122.53 ? 199 GLY E C   1 
ATOM   9393  O O   . GLY E 1 196 ? 34.175  -56.902 0.062   1.00 128.76 ? 199 GLY E O   1 
ATOM   9394  N N   . THR E 1 197 ? 32.207  -56.472 -0.956  1.00 78.64  ? 200 THR E N   1 
ATOM   9395  C CA  . THR E 1 197 ? 32.757  -55.602 -1.985  1.00 83.18  ? 200 THR E CA  1 
ATOM   9396  C C   . THR E 1 197 ? 33.051  -54.213 -1.433  1.00 79.60  ? 200 THR E C   1 
ATOM   9397  O O   . THR E 1 197 ? 32.821  -53.939 -0.255  1.00 67.61  ? 200 THR E O   1 
ATOM   9398  C CB  . THR E 1 197 ? 31.775  -55.465 -3.158  1.00 80.35  ? 200 THR E CB  1 
ATOM   9399  O OG1 . THR E 1 197 ? 30.496  -55.054 -2.660  1.00 72.11  ? 200 THR E OG1 1 
ATOM   9400  C CG2 . THR E 1 197 ? 31.619  -56.790 -3.880  1.00 76.23  ? 200 THR E CG2 1 
ATOM   9401  N N   . TYR E 1 198 ? 33.556  -53.332 -2.288  1.00 81.93  ? 201 TYR E N   1 
ATOM   9402  C CA  . TYR E 1 198 ? 33.857  -51.975 -1.865  1.00 76.66  ? 201 TYR E CA  1 
ATOM   9403  C C   . TYR E 1 198 ? 33.912  -51.018 -3.044  1.00 75.68  ? 201 TYR E C   1 
ATOM   9404  O O   . TYR E 1 198 ? 34.037  -51.440 -4.194  1.00 83.36  ? 201 TYR E O   1 
ATOM   9405  C CB  . TYR E 1 198 ? 35.183  -51.931 -1.105  1.00 82.48  ? 201 TYR E CB  1 
ATOM   9406  C CG  . TYR E 1 198 ? 36.384  -52.236 -1.966  1.00 89.30  ? 201 TYR E CG  1 
ATOM   9407  C CD1 . TYR E 1 198 ? 36.879  -51.295 -2.859  1.00 94.90  ? 201 TYR E CD1 1 
ATOM   9408  C CD2 . TYR E 1 198 ? 37.027  -53.465 -1.884  1.00 90.55  ? 201 TYR E CD2 1 
ATOM   9409  C CE1 . TYR E 1 198 ? 37.973  -51.569 -3.650  1.00 108.24 ? 201 TYR E CE1 1 
ATOM   9410  C CE2 . TYR E 1 198 ? 38.126  -53.746 -2.668  1.00 103.23 ? 201 TYR E CE2 1 
ATOM   9411  C CZ  . TYR E 1 198 ? 38.594  -52.794 -3.551  1.00 112.47 ? 201 TYR E CZ  1 
ATOM   9412  O OH  . TYR E 1 198 ? 39.689  -53.065 -4.338  1.00 116.50 ? 201 TYR E OH  1 
ATOM   9413  N N   . VAL E 1 199 ? 33.821  -49.725 -2.740  1.00 61.42  ? 202 VAL E N   1 
ATOM   9414  C CA  . VAL E 1 199 ? 33.923  -48.680 -3.748  1.00 60.41  ? 202 VAL E CA  1 
ATOM   9415  C C   . VAL E 1 199 ? 34.789  -47.537 -3.227  1.00 67.81  ? 202 VAL E C   1 
ATOM   9416  O O   . VAL E 1 199 ? 34.392  -46.816 -2.307  1.00 68.01  ? 202 VAL E O   1 
ATOM   9417  C CB  . VAL E 1 199 ? 32.547  -48.125 -4.119  1.00 47.32  ? 202 VAL E CB  1 
ATOM   9418  C CG1 . VAL E 1 199 ? 32.675  -47.126 -5.252  1.00 58.51  ? 202 VAL E CG1 1 
ATOM   9419  C CG2 . VAL E 1 199 ? 31.599  -49.250 -4.503  1.00 36.84  ? 202 VAL E CG2 1 
ATOM   9420  N N   . SER E 1 200 ? 35.970  -47.369 -3.819  1.00 61.49  ? 203 SER E N   1 
ATOM   9421  C CA  A SER E 1 200 ? 36.890  -46.320 -3.388  0.23 60.69  ? 203 SER E CA  1 
ATOM   9422  C CA  B SER E 1 200 ? 36.899  -46.328 -3.387  0.77 61.00  ? 203 SER E CA  1 
ATOM   9423  C C   . SER E 1 200 ? 37.043  -45.210 -4.419  1.00 65.59  ? 203 SER E C   1 
ATOM   9424  O O   . SER E 1 200 ? 37.163  -45.465 -5.614  1.00 76.34  ? 203 SER E O   1 
ATOM   9425  C CB  A SER E 1 200 ? 38.262  -46.905 -3.045  0.23 63.24  ? 203 SER E CB  1 
ATOM   9426  C CB  B SER E 1 200 ? 38.269  -46.928 -3.048  0.77 63.31  ? 203 SER E CB  1 
ATOM   9427  O OG  A SER E 1 200 ? 38.290  -47.388 -1.714  0.23 59.80  ? 203 SER E OG  1 
ATOM   9428  O OG  B SER E 1 200 ? 39.293  -46.360 -3.845  0.77 69.42  ? 203 SER E OG  1 
ATOM   9429  N N   . VAL E 1 201 ? 37.031  -43.973 -3.939  1.00 60.23  ? 204 VAL E N   1 
ATOM   9430  C CA  . VAL E 1 201 ? 37.250  -42.816 -4.793  1.00 64.79  ? 204 VAL E CA  1 
ATOM   9431  C C   . VAL E 1 201 ? 38.377  -41.993 -4.187  1.00 66.36  ? 204 VAL E C   1 
ATOM   9432  O O   . VAL E 1 201 ? 38.547  -41.962 -2.967  1.00 62.82  ? 204 VAL E O   1 
ATOM   9433  C CB  . VAL E 1 201 ? 35.992  -41.957 -4.928  1.00 53.93  ? 204 VAL E CB  1 
ATOM   9434  C CG1 . VAL E 1 201 ? 36.182  -40.942 -6.032  1.00 64.58  ? 204 VAL E CG1 1 
ATOM   9435  C CG2 . VAL E 1 201 ? 34.788  -42.834 -5.221  1.00 47.18  ? 204 VAL E CG2 1 
ATOM   9436  N N   . GLY E 1 202 ? 39.164  -41.343 -5.034  1.00 84.25  ? 205 GLY E N   1 
ATOM   9437  C CA  . GLY E 1 202 ? 40.331  -40.640 -4.544  1.00 90.93  ? 205 GLY E CA  1 
ATOM   9438  C C   . GLY E 1 202 ? 40.780  -39.444 -5.357  1.00 100.15 ? 205 GLY E C   1 
ATOM   9439  O O   . GLY E 1 202 ? 40.767  -39.468 -6.586  1.00 111.34 ? 205 GLY E O   1 
ATOM   9440  N N   . THR E 1 203 ? 41.158  -38.383 -4.650  1.00 49.56  ? 206 THR E N   1 
ATOM   9441  C CA  . THR E 1 203 ? 41.880  -37.265 -5.238  1.00 51.64  ? 206 THR E CA  1 
ATOM   9442  C C   . THR E 1 203 ? 42.825  -36.738 -4.176  1.00 53.53  ? 206 THR E C   1 
ATOM   9443  O O   . THR E 1 203 ? 43.216  -37.468 -3.269  1.00 63.26  ? 206 THR E O   1 
ATOM   9444  C CB  . THR E 1 203 ? 40.952  -36.124 -5.680  1.00 46.31  ? 206 THR E CB  1 
ATOM   9445  O OG1 . THR E 1 203 ? 40.735  -35.233 -4.580  1.00 45.80  ? 206 THR E OG1 1 
ATOM   9446  C CG2 . THR E 1 203 ? 39.620  -36.677 -6.181  1.00 40.51  ? 206 THR E CG2 1 
ATOM   9447  N N   . SER E 1 204 ? 43.182  -35.468 -4.281  1.00 57.04  ? 207 SER E N   1 
ATOM   9448  C CA  . SER E 1 204 ? 44.095  -34.877 -3.325  1.00 59.71  ? 207 SER E CA  1 
ATOM   9449  C C   . SER E 1 204 ? 43.319  -34.394 -2.106  1.00 60.43  ? 207 SER E C   1 
ATOM   9450  O O   . SER E 1 204 ? 43.891  -34.170 -1.034  1.00 64.47  ? 207 SER E O   1 
ATOM   9451  C CB  . SER E 1 204 ? 44.838  -33.708 -3.971  1.00 65.24  ? 207 SER E CB  1 
ATOM   9452  O OG  . SER E 1 204 ? 45.349  -34.054 -5.252  1.00 81.15  ? 207 SER E OG  1 
ATOM   9453  N N   . THR E 1 205 ? 42.011  -34.220 -2.284  1.00 91.43  ? 208 THR E N   1 
ATOM   9454  C CA  . THR E 1 205 ? 41.146  -33.688 -1.234  1.00 88.01  ? 208 THR E CA  1 
ATOM   9455  C C   . THR E 1 205 ? 40.008  -34.646 -0.928  1.00 91.19  ? 208 THR E C   1 
ATOM   9456  O O   . THR E 1 205 ? 39.222  -34.414 -0.010  1.00 83.22  ? 208 THR E O   1 
ATOM   9457  C CB  . THR E 1 205 ? 40.526  -32.336 -1.633  1.00 81.77  ? 208 THR E CB  1 
ATOM   9458  O OG1 . THR E 1 205 ? 39.529  -32.542 -2.644  1.00 86.77  ? 208 THR E OG1 1 
ATOM   9459  C CG2 . THR E 1 205 ? 41.595  -31.394 -2.152  1.00 77.85  ? 208 THR E CG2 1 
ATOM   9460  N N   . LEU E 1 206 ? 39.910  -35.713 -1.713  1.00 77.09  ? 209 LEU E N   1 
ATOM   9461  C CA  . LEU E 1 206 ? 38.871  -36.707 -1.502  1.00 64.36  ? 209 LEU E CA  1 
ATOM   9462  C C   . LEU E 1 206 ? 39.485  -38.022 -1.053  1.00 66.60  ? 209 LEU E C   1 
ATOM   9463  O O   . LEU E 1 206 ? 40.685  -38.246 -1.237  1.00 66.52  ? 209 LEU E O   1 
ATOM   9464  C CB  . LEU E 1 206 ? 38.041  -36.913 -2.770  1.00 56.34  ? 209 LEU E CB  1 
ATOM   9465  C CG  . LEU E 1 206 ? 36.855  -37.868 -2.590  1.00 46.51  ? 209 LEU E CG  1 
ATOM   9466  C CD1 . LEU E 1 206 ? 36.058  -37.521 -1.331  1.00 36.78  ? 209 LEU E CD1 1 
ATOM   9467  C CD2 . LEU E 1 206 ? 35.947  -37.886 -3.813  1.00 44.76  ? 209 LEU E CD2 1 
ATOM   9468  N N   . ASN E 1 207 ? 38.652  -38.871 -0.447  1.00 73.36  ? 210 ASN E N   1 
ATOM   9469  C CA  . ASN E 1 207 ? 39.049  -40.212 -0.021  1.00 66.37  ? 210 ASN E CA  1 
ATOM   9470  C C   . ASN E 1 207 ? 37.915  -41.012 0.625   1.00 60.65  ? 210 ASN E C   1 
ATOM   9471  O O   . ASN E 1 207 ? 37.858  -41.130 1.845   1.00 62.02  ? 210 ASN E O   1 
ATOM   9472  C CB  . ASN E 1 207 ? 40.220  -40.141 0.956   1.00 56.78  ? 210 ASN E CB  1 
ATOM   9473  C CG  . ASN E 1 207 ? 40.813  -41.501 1.228   1.00 60.50  ? 210 ASN E CG  1 
ATOM   9474  O OD1 . ASN E 1 207 ? 41.030  -42.287 0.300   1.00 71.80  ? 210 ASN E OD1 1 
ATOM   9475  N ND2 . ASN E 1 207 ? 41.058  -41.802 2.501   1.00 49.92  ? 210 ASN E ND2 1 
ATOM   9476  N N   . LYS E 1 208 ? 37.016  -41.564 -0.178  1.00 71.76  ? 211 LYS E N   1 
ATOM   9477  C CA  . LYS E 1 208 ? 35.954  -42.391 0.379   1.00 73.08  ? 211 LYS E CA  1 
ATOM   9478  C C   . LYS E 1 208 ? 36.093  -43.854 -0.019  1.00 83.45  ? 211 LYS E C   1 
ATOM   9479  O O   . LYS E 1 208 ? 36.559  -44.170 -1.113  1.00 96.30  ? 211 LYS E O   1 
ATOM   9480  C CB  . LYS E 1 208 ? 34.569  -41.870 -0.016  1.00 72.34  ? 211 LYS E CB  1 
ATOM   9481  C CG  . LYS E 1 208 ? 33.420  -42.816 0.361   1.00 74.86  ? 211 LYS E CG  1 
ATOM   9482  C CD  . LYS E 1 208 ? 32.189  -42.066 0.864   1.00 77.38  ? 211 LYS E CD  1 
ATOM   9483  C CE  . LYS E 1 208 ? 31.679  -41.068 -0.179  1.00 81.59  ? 211 LYS E CE  1 
ATOM   9484  N NZ  . LYS E 1 208 ? 30.933  -39.914 0.417   1.00 67.91  ? 211 LYS E NZ  1 
ATOM   9485  N N   . ARG E 1 209 ? 35.700  -44.741 0.891   1.00 68.05  ? 212 ARG E N   1 
ATOM   9486  C CA  . ARG E 1 209 ? 35.541  -46.151 0.581   1.00 68.47  ? 212 ARG E CA  1 
ATOM   9487  C C   . ARG E 1 209 ? 34.226  -46.635 1.179   1.00 62.49  ? 212 ARG E C   1 
ATOM   9488  O O   . ARG E 1 209 ? 34.132  -46.913 2.374   1.00 59.68  ? 212 ARG E O   1 
ATOM   9489  C CB  . ARG E 1 209 ? 36.712  -46.970 1.117   1.00 69.64  ? 212 ARG E CB  1 
ATOM   9490  C CG  . ARG E 1 209 ? 36.666  -48.443 0.728   1.00 71.21  ? 212 ARG E CG  1 
ATOM   9491  C CD  . ARG E 1 209 ? 37.855  -49.197 1.301   1.00 71.56  ? 212 ARG E CD  1 
ATOM   9492  N NE  . ARG E 1 209 ? 38.703  -49.745 0.248   1.00 87.45  ? 212 ARG E NE  1 
ATOM   9493  C CZ  . ARG E 1 209 ? 38.749  -51.031 -0.082  1.00 95.86  ? 212 ARG E CZ  1 
ATOM   9494  N NH1 . ARG E 1 209 ? 38.004  -51.913 0.571   1.00 95.06  ? 212 ARG E NH1 1 
ATOM   9495  N NH2 . ARG E 1 209 ? 39.551  -51.435 -1.057  1.00 94.67  ? 212 ARG E NH2 1 
ATOM   9496  N N   . SER E 1 210 ? 33.203  -46.714 0.340   1.00 79.42  ? 213 SER E N   1 
ATOM   9497  C CA  . SER E 1 210 ? 31.893  -47.144 0.788   1.00 77.31  ? 213 SER E CA  1 
ATOM   9498  C C   . SER E 1 210 ? 31.820  -48.662 0.799   1.00 78.71  ? 213 SER E C   1 
ATOM   9499  O O   . SER E 1 210 ? 32.181  -49.308 -0.184  1.00 86.38  ? 213 SER E O   1 
ATOM   9500  C CB  . SER E 1 210 ? 30.814  -46.577 -0.133  1.00 80.53  ? 213 SER E CB  1 
ATOM   9501  O OG  . SER E 1 210 ? 30.945  -45.168 -0.253  1.00 90.09  ? 213 SER E OG  1 
ATOM   9502  N N   . THR E 1 211 ? 31.375  -49.230 1.916   1.00 94.63  ? 214 THR E N   1 
ATOM   9503  C CA  . THR E 1 211 ? 31.121  -50.665 1.986   1.00 91.62  ? 214 THR E CA  1 
ATOM   9504  C C   . THR E 1 211 ? 29.619  -50.874 1.955   1.00 85.47  ? 214 THR E C   1 
ATOM   9505  O O   . THR E 1 211 ? 28.917  -50.490 2.893   1.00 81.48  ? 214 THR E O   1 
ATOM   9506  C CB  . THR E 1 211 ? 31.686  -51.300 3.267   1.00 90.88  ? 214 THR E CB  1 
ATOM   9507  O OG1 . THR E 1 211 ? 32.756  -50.499 3.783   1.00 100.33 ? 214 THR E OG1 1 
ATOM   9508  C CG2 . THR E 1 211 ? 32.189  -52.706 2.977   1.00 89.46  ? 214 THR E CG2 1 
ATOM   9509  N N   . PRO E 1 212 ? 29.115  -51.472 0.867   1.00 62.05  ? 215 PRO E N   1 
ATOM   9510  C CA  . PRO E 1 212 ? 27.668  -51.617 0.681   1.00 47.45  ? 215 PRO E CA  1 
ATOM   9511  C C   . PRO E 1 212 ? 26.984  -52.209 1.909   1.00 52.60  ? 215 PRO E C   1 
ATOM   9512  O O   . PRO E 1 212 ? 27.254  -53.352 2.269   1.00 60.89  ? 215 PRO E O   1 
ATOM   9513  C CB  . PRO E 1 212 ? 27.570  -52.565 -0.511  1.00 46.70  ? 215 PRO E CB  1 
ATOM   9514  C CG  . PRO E 1 212 ? 28.813  -52.293 -1.297  1.00 60.70  ? 215 PRO E CG  1 
ATOM   9515  C CD  . PRO E 1 212 ? 29.879  -52.023 -0.267  1.00 71.81  ? 215 PRO E CD  1 
ATOM   9516  N N   . GLU E 1 213 ? 26.120  -51.424 2.547   1.00 94.15  ? 216 GLU E N   1 
ATOM   9517  C CA  . GLU E 1 213 ? 25.351  -51.887 3.696   1.00 94.51  ? 216 GLU E CA  1 
ATOM   9518  C C   . GLU E 1 213 ? 24.096  -52.599 3.212   1.00 101.75 ? 216 GLU E C   1 
ATOM   9519  O O   . GLU E 1 213 ? 23.375  -52.079 2.362   1.00 105.58 ? 216 GLU E O   1 
ATOM   9520  C CB  . GLU E 1 213 ? 24.962  -50.706 4.596   1.00 89.77  ? 216 GLU E CB  1 
ATOM   9521  C CG  . GLU E 1 213 ? 26.145  -49.979 5.245   1.00 94.75  ? 216 GLU E CG  1 
ATOM   9522  C CD  . GLU E 1 213 ? 25.734  -48.722 6.014   1.00 90.30  ? 216 GLU E CD  1 
ATOM   9523  O OE1 . GLU E 1 213 ? 24.799  -48.022 5.568   1.00 93.34  ? 216 GLU E OE1 1 
ATOM   9524  O OE2 . GLU E 1 213 ? 26.350  -48.432 7.065   1.00 86.07  ? 216 GLU E OE2 1 
ATOM   9525  N N   . ILE E 1 214 ? 23.836  -53.790 3.746   1.00 90.67  ? 217 ILE E N   1 
ATOM   9526  C CA  . ILE E 1 214 ? 22.646  -54.558 3.359   1.00 92.05  ? 217 ILE E CA  1 
ATOM   9527  C C   . ILE E 1 214 ? 21.594  -54.628 4.470   1.00 101.38 ? 217 ILE E C   1 
ATOM   9528  O O   . ILE E 1 214 ? 21.929  -54.662 5.657   1.00 96.67  ? 217 ILE E O   1 
ATOM   9529  C CB  . ILE E 1 214 ? 23.000  -55.993 2.897   1.00 86.78  ? 217 ILE E CB  1 
ATOM   9530  C CG1 . ILE E 1 214 ? 23.840  -55.961 1.618   1.00 77.23  ? 217 ILE E CG1 1 
ATOM   9531  C CG2 . ILE E 1 214 ? 21.739  -56.801 2.654   1.00 93.34  ? 217 ILE E CG2 1 
ATOM   9532  C CD1 . ILE E 1 214 ? 24.061  -57.330 1.001   1.00 72.95  ? 217 ILE E CD1 1 
ATOM   9533  N N   . ALA E 1 215 ? 20.322  -54.644 4.073   1.00 114.67 ? 218 ALA E N   1 
ATOM   9534  C CA  . ALA E 1 215 ? 19.217  -54.749 5.025   1.00 119.56 ? 218 ALA E CA  1 
ATOM   9535  C C   . ALA E 1 215 ? 17.871  -54.999 4.340   1.00 128.75 ? 218 ALA E C   1 
ATOM   9536  O O   . ALA E 1 215 ? 17.787  -55.067 3.112   1.00 129.97 ? 218 ALA E O   1 
ATOM   9537  C CB  . ALA E 1 215 ? 19.145  -53.506 5.898   1.00 114.74 ? 218 ALA E CB  1 
ATOM   9538  N N   . THR E 1 216 ? 16.824  -55.130 5.151   1.00 102.48 ? 219 THR E N   1 
ATOM   9539  C CA  . THR E 1 216 ? 15.479  -55.402 4.654   1.00 101.75 ? 219 THR E CA  1 
ATOM   9540  C C   . THR E 1 216 ? 14.622  -54.145 4.725   1.00 93.42  ? 219 THR E C   1 
ATOM   9541  O O   . THR E 1 216 ? 14.377  -53.613 5.812   1.00 79.99  ? 219 THR E O   1 
ATOM   9542  C CB  . THR E 1 216 ? 14.794  -56.513 5.474   1.00 105.11 ? 219 THR E CB  1 
ATOM   9543  O OG1 . THR E 1 216 ? 15.775  -57.225 6.241   1.00 104.38 ? 219 THR E OG1 1 
ATOM   9544  C CG2 . THR E 1 216 ? 14.061  -57.482 4.553   1.00 109.43 ? 219 THR E CG2 1 
ATOM   9545  N N   . ARG E 1 217 ? 14.162  -53.679 3.565   1.00 120.76 ? 220 ARG E N   1 
ATOM   9546  C CA  . ARG E 1 217 ? 13.458  -52.401 3.473   1.00 119.02 ? 220 ARG E CA  1 
ATOM   9547  C C   . ARG E 1 217 ? 12.194  -52.486 2.629   1.00 117.59 ? 220 ARG E C   1 
ATOM   9548  O O   . ARG E 1 217 ? 12.128  -53.270 1.680   1.00 121.67 ? 220 ARG E O   1 
ATOM   9549  C CB  . ARG E 1 217 ? 14.383  -51.339 2.874   1.00 121.47 ? 220 ARG E CB  1 
ATOM   9550  C CG  . ARG E 1 217 ? 15.796  -51.402 3.410   1.00 119.26 ? 220 ARG E CG  1 
ATOM   9551  C CD  . ARG E 1 217 ? 16.744  -50.521 2.627   1.00 117.77 ? 220 ARG E CD  1 
ATOM   9552  N NE  . ARG E 1 217 ? 18.121  -50.967 2.804   1.00 109.65 ? 220 ARG E NE  1 
ATOM   9553  C CZ  . ARG E 1 217 ? 18.839  -51.563 1.859   1.00 104.06 ? 220 ARG E CZ  1 
ATOM   9554  N NH1 . ARG E 1 217 ? 18.319  -51.766 0.656   1.00 109.60 ? 220 ARG E NH1 1 
ATOM   9555  N NH2 . ARG E 1 217 ? 20.084  -51.943 2.112   1.00 92.96  ? 220 ARG E NH2 1 
ATOM   9556  N N   . PRO E 1 218 ? 11.184  -51.675 2.979   1.00 88.18  ? 221 PRO E N   1 
ATOM   9557  C CA  . PRO E 1 218 ? 9.983   -51.499 2.158   1.00 87.62  ? 221 PRO E CA  1 
ATOM   9558  C C   . PRO E 1 218 ? 10.352  -51.210 0.710   1.00 87.44  ? 221 PRO E C   1 
ATOM   9559  O O   . PRO E 1 218 ? 11.185  -50.345 0.450   1.00 75.73  ? 221 PRO E O   1 
ATOM   9560  C CB  . PRO E 1 218 ? 9.321   -50.272 2.782   1.00 85.83  ? 221 PRO E CB  1 
ATOM   9561  C CG  . PRO E 1 218 ? 9.697   -50.359 4.227   1.00 82.94  ? 221 PRO E CG  1 
ATOM   9562  C CD  . PRO E 1 218 ? 11.090  -50.950 4.260   1.00 82.51  ? 221 PRO E CD  1 
ATOM   9563  N N   . LYS E 1 219 ? 9.751   -51.948 -0.217  1.00 116.57 ? 222 LYS E N   1 
ATOM   9564  C CA  . LYS E 1 219 ? 10.004  -51.739 -1.634  1.00 122.36 ? 222 LYS E CA  1 
ATOM   9565  C C   . LYS E 1 219 ? 9.434   -50.399 -2.059  1.00 120.76 ? 222 LYS E C   1 
ATOM   9566  O O   . LYS E 1 219 ? 8.233   -50.159 -1.943  1.00 117.49 ? 222 LYS E O   1 
ATOM   9567  C CB  . LYS E 1 219 ? 9.387   -52.862 -2.479  1.00 132.05 ? 222 LYS E CB  1 
ATOM   9568  C CG  . LYS E 1 219 ? 10.296  -54.073 -2.731  1.00 138.24 ? 222 LYS E CG  1 
ATOM   9569  C CD  . LYS E 1 219 ? 9.937   -55.268 -1.843  1.00 136.56 ? 222 LYS E CD  1 
ATOM   9570  C CE  . LYS E 1 219 ? 10.754  -55.281 -0.557  1.00 131.91 ? 222 LYS E CE  1 
ATOM   9571  N NZ  . LYS E 1 219 ? 10.257  -56.293 0.413   1.00 128.57 ? 222 LYS E NZ  1 
ATOM   9572  N N   . VAL E 1 220 ? 10.309  -49.521 -2.534  1.00 110.21 ? 223 VAL E N   1 
ATOM   9573  C CA  . VAL E 1 220 ? 9.891   -48.230 -3.070  1.00 115.53 ? 223 VAL E CA  1 
ATOM   9574  C C   . VAL E 1 220 ? 10.132  -48.199 -4.577  1.00 120.48 ? 223 VAL E C   1 
ATOM   9575  O O   . VAL E 1 220 ? 11.258  -48.392 -5.038  1.00 123.53 ? 223 VAL E O   1 
ATOM   9576  C CB  . VAL E 1 220 ? 10.625  -47.057 -2.379  1.00 93.44  ? 223 VAL E CB  1 
ATOM   9577  C CG1 . VAL E 1 220 ? 10.884  -45.932 -3.364  1.00 97.24  ? 223 VAL E CG1 1 
ATOM   9578  C CG2 . VAL E 1 220 ? 9.825   -46.559 -1.182  1.00 85.77  ? 223 VAL E CG2 1 
ATOM   9579  N N   . ASN E 1 221 ? 9.070   -47.966 -5.340  1.00 113.12 ? 224 ASN E N   1 
ATOM   9580  C CA  . ASN E 1 221 ? 9.145   -48.062 -6.792  1.00 119.99 ? 224 ASN E CA  1 
ATOM   9581  C C   . ASN E 1 221 ? 9.550   -49.466 -7.228  1.00 124.25 ? 224 ASN E C   1 
ATOM   9582  O O   . ASN E 1 221 ? 10.319  -49.638 -8.177  1.00 128.72 ? 224 ASN E O   1 
ATOM   9583  C CB  . ASN E 1 221 ? 10.112  -47.023 -7.361  1.00 125.48 ? 224 ASN E CB  1 
ATOM   9584  C CG  . ASN E 1 221 ? 9.581   -45.605 -7.246  1.00 130.05 ? 224 ASN E CG  1 
ATOM   9585  O OD1 . ASN E 1 221 ? 8.627   -45.344 -6.511  1.00 129.44 ? 224 ASN E OD1 1 
ATOM   9586  N ND2 . ASN E 1 221 ? 10.199  -44.681 -7.976  1.00 132.37 ? 224 ASN E ND2 1 
ATOM   9587  N N   . GLY E 1 222 ? 9.033   -50.467 -6.519  1.00 130.73 ? 225 GLY E N   1 
ATOM   9588  C CA  . GLY E 1 222 ? 9.264   -51.859 -6.864  1.00 130.11 ? 225 GLY E CA  1 
ATOM   9589  C C   . GLY E 1 222 ? 10.705  -52.303 -6.712  1.00 124.55 ? 225 GLY E C   1 
ATOM   9590  O O   . GLY E 1 222 ? 11.185  -53.155 -7.461  1.00 125.05 ? 225 GLY E O   1 
ATOM   9591  N N   . GLN E 1 223 ? 11.400  -51.722 -5.742  1.00 114.11 ? 226 GLN E N   1 
ATOM   9592  C CA  . GLN E 1 223 ? 12.786  -52.082 -5.472  1.00 110.10 ? 226 GLN E CA  1 
ATOM   9593  C C   . GLN E 1 223 ? 13.063  -52.003 -3.978  1.00 102.09 ? 226 GLN E C   1 
ATOM   9594  O O   . GLN E 1 223 ? 12.619  -51.074 -3.303  1.00 98.98  ? 226 GLN E O   1 
ATOM   9595  C CB  . GLN E 1 223 ? 13.743  -51.163 -6.233  1.00 111.97 ? 226 GLN E CB  1 
ATOM   9596  C CG  . GLN E 1 223 ? 13.580  -51.189 -7.747  1.00 125.38 ? 226 GLN E CG  1 
ATOM   9597  C CD  . GLN E 1 223 ? 13.995  -52.510 -8.360  1.00 130.02 ? 226 GLN E CD  1 
ATOM   9598  O OE1 . GLN E 1 223 ? 14.025  -53.539 -7.688  1.00 127.13 ? 226 GLN E OE1 1 
ATOM   9599  N NE2 . GLN E 1 223 ? 14.323  -52.487 -9.646  1.00 135.98 ? 226 GLN E NE2 1 
ATOM   9600  N N   . GLY E 1 224 ? 13.783  -52.990 -3.460  1.00 111.40 ? 227 GLY E N   1 
ATOM   9601  C CA  . GLY E 1 224 ? 14.161  -52.987 -2.061  1.00 105.92 ? 227 GLY E CA  1 
ATOM   9602  C C   . GLY E 1 224 ? 15.500  -52.303 -1.903  1.00 98.29  ? 227 GLY E C   1 
ATOM   9603  O O   . GLY E 1 224 ? 15.877  -51.890 -0.808  1.00 87.18  ? 227 GLY E O   1 
ATOM   9604  N N   . GLY E 1 225 ? 16.216  -52.177 -3.013  1.00 92.49  ? 228 GLY E N   1 
ATOM   9605  C CA  . GLY E 1 225 ? 17.546  -51.603 -2.993  1.00 90.06  ? 228 GLY E CA  1 
ATOM   9606  C C   . GLY E 1 225 ? 17.545  -50.090 -2.931  1.00 89.54  ? 228 GLY E C   1 
ATOM   9607  O O   . GLY E 1 225 ? 16.487  -49.458 -2.904  1.00 95.36  ? 228 GLY E O   1 
ATOM   9608  N N   . ARG E 1 226 ? 18.745  -49.514 -2.907  1.00 97.60  ? 229 ARG E N   1 
ATOM   9609  C CA  . ARG E 1 226 ? 18.923  -48.067 -2.873  1.00 88.29  ? 229 ARG E CA  1 
ATOM   9610  C C   . ARG E 1 226 ? 20.319  -47.690 -3.366  1.00 72.36  ? 229 ARG E C   1 
ATOM   9611  O O   . ARG E 1 226 ? 21.284  -48.411 -3.117  1.00 63.97  ? 229 ARG E O   1 
ATOM   9612  C CB  . ARG E 1 226 ? 18.683  -47.525 -1.460  1.00 88.63  ? 229 ARG E CB  1 
ATOM   9613  C CG  . ARG E 1 226 ? 17.213  -47.451 -1.088  1.00 110.46 ? 229 ARG E CG  1 
ATOM   9614  C CD  . ARG E 1 226 ? 16.977  -47.018 0.351   1.00 113.12 ? 229 ARG E CD  1 
ATOM   9615  N NE  . ARG E 1 226 ? 15.825  -47.704 0.937   1.00 114.45 ? 229 ARG E NE  1 
ATOM   9616  C CZ  . ARG E 1 226 ? 14.656  -47.886 0.325   1.00 110.66 ? 229 ARG E CZ  1 
ATOM   9617  N NH1 . ARG E 1 226 ? 14.455  -47.425 -0.903  1.00 108.19 ? 229 ARG E NH1 1 
ATOM   9618  N NH2 . ARG E 1 226 ? 13.678  -48.530 0.945   1.00 107.08 ? 229 ARG E NH2 1 
ATOM   9619  N N   . MET E 1 227 ? 20.425  -46.571 -4.078  1.00 93.17  ? 230 MET E N   1 
ATOM   9620  C CA  . MET E 1 227 ? 21.726  -46.112 -4.555  1.00 89.35  ? 230 MET E CA  1 
ATOM   9621  C C   . MET E 1 227 ? 22.138  -44.813 -3.866  1.00 83.85  ? 230 MET E C   1 
ATOM   9622  O O   . MET E 1 227 ? 21.438  -43.806 -3.945  1.00 84.56  ? 230 MET E O   1 
ATOM   9623  C CB  . MET E 1 227 ? 21.727  -45.947 -6.078  1.00 93.99  ? 230 MET E CB  1 
ATOM   9624  C CG  . MET E 1 227 ? 21.233  -47.178 -6.829  1.00 102.63 ? 230 MET E CG  1 
ATOM   9625  S SD  . MET E 1 227 ? 21.828  -47.313 -8.531  1.00 112.98 ? 230 MET E SD  1 
ATOM   9626  C CE  . MET E 1 227 ? 20.753  -48.605 -9.147  1.00 159.45 ? 230 MET E CE  1 
ATOM   9627  N N   . GLU E 1 228 ? 23.275  -44.846 -3.179  1.00 74.94  ? 231 GLU E N   1 
ATOM   9628  C CA  . GLU E 1 228 ? 23.733  -43.695 -2.413  1.00 66.24  ? 231 GLU E CA  1 
ATOM   9629  C C   . GLU E 1 228 ? 24.763  -42.896 -3.193  1.00 62.38  ? 231 GLU E C   1 
ATOM   9630  O O   . GLU E 1 228 ? 25.918  -43.307 -3.308  1.00 69.70  ? 231 GLU E O   1 
ATOM   9631  C CB  . GLU E 1 228 ? 24.331  -44.148 -1.082  1.00 62.07  ? 231 GLU E CB  1 
ATOM   9632  C CG  . GLU E 1 228 ? 25.004  -43.041 -0.293  1.00 58.15  ? 231 GLU E CG  1 
ATOM   9633  C CD  . GLU E 1 228 ? 25.831  -43.578 0.854   1.00 65.27  ? 231 GLU E CD  1 
ATOM   9634  O OE1 . GLU E 1 228 ? 25.867  -44.815 1.035   1.00 70.86  ? 231 GLU E OE1 1 
ATOM   9635  O OE2 . GLU E 1 228 ? 26.449  -42.770 1.576   1.00 67.26  ? 231 GLU E OE2 1 
ATOM   9636  N N   . PHE E 1 229 ? 24.344  -41.744 -3.711  1.00 58.47  ? 232 PHE E N   1 
ATOM   9637  C CA  . PHE E 1 229 ? 25.225  -40.906 -4.523  1.00 61.74  ? 232 PHE E CA  1 
ATOM   9638  C C   . PHE E 1 229 ? 25.997  -39.870 -3.722  1.00 66.94  ? 232 PHE E C   1 
ATOM   9639  O O   . PHE E 1 229 ? 25.435  -39.166 -2.889  1.00 69.64  ? 232 PHE E O   1 
ATOM   9640  C CB  . PHE E 1 229 ? 24.439  -40.216 -5.639  1.00 63.90  ? 232 PHE E CB  1 
ATOM   9641  C CG  . PHE E 1 229 ? 23.874  -41.169 -6.660  1.00 70.73  ? 232 PHE E CG  1 
ATOM   9642  C CD1 . PHE E 1 229 ? 24.685  -41.705 -7.653  1.00 75.95  ? 232 PHE E CD1 1 
ATOM   9643  C CD2 . PHE E 1 229 ? 22.534  -41.537 -6.623  1.00 75.89  ? 232 PHE E CD2 1 
ATOM   9644  C CE1 . PHE E 1 229 ? 24.171  -42.583 -8.587  1.00 81.05  ? 232 PHE E CE1 1 
ATOM   9645  C CE2 . PHE E 1 229 ? 22.014  -42.415 -7.558  1.00 80.08  ? 232 PHE E CE2 1 
ATOM   9646  C CZ  . PHE E 1 229 ? 22.832  -42.935 -8.542  1.00 81.23  ? 232 PHE E CZ  1 
ATOM   9647  N N   . SER E 1 230 ? 27.296  -39.793 -3.981  1.00 53.60  ? 233 SER E N   1 
ATOM   9648  C CA  . SER E 1 230 ? 28.121  -38.717 -3.464  1.00 62.29  ? 233 SER E CA  1 
ATOM   9649  C C   . SER E 1 230 ? 28.531  -37.863 -4.641  1.00 76.03  ? 233 SER E C   1 
ATOM   9650  O O   . SER E 1 230 ? 28.160  -38.149 -5.778  1.00 86.56  ? 233 SER E O   1 
ATOM   9651  C CB  . SER E 1 230 ? 29.367  -39.259 -2.764  1.00 74.98  ? 233 SER E CB  1 
ATOM   9652  O OG  . SER E 1 230 ? 29.053  -39.787 -1.488  1.00 65.86  ? 233 SER E OG  1 
ATOM   9653  N N   . TRP E 1 231 ? 29.288  -36.809 -4.365  1.00 71.66  ? 234 TRP E N   1 
ATOM   9654  C CA  . TRP E 1 231 ? 29.852  -35.986 -5.418  1.00 77.67  ? 234 TRP E CA  1 
ATOM   9655  C C   . TRP E 1 231 ? 31.104  -35.281 -4.941  1.00 104.50 ? 234 TRP E C   1 
ATOM   9656  O O   . TRP E 1 231 ? 31.407  -35.254 -3.751  1.00 111.42 ? 234 TRP E O   1 
ATOM   9657  C CB  . TRP E 1 231 ? 28.829  -34.981 -5.955  1.00 59.33  ? 234 TRP E CB  1 
ATOM   9658  C CG  . TRP E 1 231 ? 28.259  -34.015 -4.935  1.00 51.13  ? 234 TRP E CG  1 
ATOM   9659  C CD1 . TRP E 1 231 ? 27.185  -34.226 -4.115  1.00 41.97  ? 234 TRP E CD1 1 
ATOM   9660  C CD2 . TRP E 1 231 ? 28.706  -32.678 -4.666  1.00 54.99  ? 234 TRP E CD2 1 
ATOM   9661  N NE1 . TRP E 1 231 ? 26.956  -33.123 -3.342  1.00 41.55  ? 234 TRP E NE1 1 
ATOM   9662  C CE2 . TRP E 1 231 ? 27.872  -32.156 -3.663  1.00 47.50  ? 234 TRP E CE2 1 
ATOM   9663  C CE3 . TRP E 1 231 ? 29.736  -31.882 -5.166  1.00 71.57  ? 234 TRP E CE3 1 
ATOM   9664  C CZ2 . TRP E 1 231 ? 28.038  -30.866 -3.152  1.00 51.84  ? 234 TRP E CZ2 1 
ATOM   9665  C CZ3 . TRP E 1 231 ? 29.899  -30.612 -4.655  1.00 71.02  ? 234 TRP E CZ3 1 
ATOM   9666  C CH2 . TRP E 1 231 ? 29.058  -30.117 -3.659  1.00 59.73  ? 234 TRP E CH2 1 
ATOM   9667  N N   . THR E 1 232 ? 31.839  -34.725 -5.890  1.00 55.19  ? 235 THR E N   1 
ATOM   9668  C CA  . THR E 1 232 ? 33.045  -33.984 -5.578  1.00 60.75  ? 235 THR E CA  1 
ATOM   9669  C C   . THR E 1 232 ? 33.296  -32.944 -6.661  1.00 70.06  ? 235 THR E C   1 
ATOM   9670  O O   . THR E 1 232 ? 32.578  -32.883 -7.662  1.00 65.70  ? 235 THR E O   1 
ATOM   9671  C CB  . THR E 1 232 ? 34.267  -34.914 -5.469  1.00 61.56  ? 235 THR E CB  1 
ATOM   9672  O OG1 . THR E 1 232 ? 35.344  -34.223 -4.825  1.00 65.65  ? 235 THR E OG1 1 
ATOM   9673  C CG2 . THR E 1 232 ? 34.704  -35.384 -6.848  1.00 60.85  ? 235 THR E CG2 1 
ATOM   9674  N N   . LEU E 1 233 ? 34.316  -32.124 -6.442  1.00 86.92  ? 236 LEU E N   1 
ATOM   9675  C CA  . LEU E 1 233 ? 34.726  -31.118 -7.404  1.00 88.55  ? 236 LEU E CA  1 
ATOM   9676  C C   . LEU E 1 233 ? 36.221  -31.242 -7.614  1.00 89.81  ? 236 LEU E C   1 
ATOM   9677  O O   . LEU E 1 233 ? 37.010  -30.847 -6.752  1.00 85.50  ? 236 LEU E O   1 
ATOM   9678  C CB  . LEU E 1 233 ? 34.384  -29.720 -6.895  1.00 84.89  ? 236 LEU E CB  1 
ATOM   9679  C CG  . LEU E 1 233 ? 33.255  -29.001 -7.629  1.00 84.27  ? 236 LEU E CG  1 
ATOM   9680  C CD1 . LEU E 1 233 ? 32.036  -29.894 -7.742  1.00 77.99  ? 236 LEU E CD1 1 
ATOM   9681  C CD2 . LEU E 1 233 ? 32.910  -27.706 -6.922  1.00 83.58  ? 236 LEU E CD2 1 
ATOM   9682  N N   . LEU E 1 234 ? 36.611  -31.801 -8.756  1.00 61.31  ? 237 LEU E N   1 
ATOM   9683  C CA  . LEU E 1 234 ? 38.023  -32.042 -9.029  1.00 71.09  ? 237 LEU E CA  1 
ATOM   9684  C C   . LEU E 1 234 ? 38.733  -30.763 -9.449  1.00 84.59  ? 237 LEU E C   1 
ATOM   9685  O O   . LEU E 1 234 ? 38.412  -30.164 -10.480 1.00 88.76  ? 237 LEU E O   1 
ATOM   9686  C CB  . LEU E 1 234 ? 38.210  -33.135 -10.091 1.00 69.77  ? 237 LEU E CB  1 
ATOM   9687  C CG  . LEU E 1 234 ? 39.648  -33.630 -10.281 1.00 73.29  ? 237 LEU E CG  1 
ATOM   9688  C CD1 . LEU E 1 234 ? 40.110  -34.395 -9.052  1.00 68.72  ? 237 LEU E CD1 1 
ATOM   9689  C CD2 . LEU E 1 234 ? 39.756  -34.491 -11.524 1.00 79.17  ? 237 LEU E CD2 1 
ATOM   9690  N N   . ASP E 1 235 ? 39.700  -30.352 -8.636  1.00 84.62  ? 238 ASP E N   1 
ATOM   9691  C CA  . ASP E 1 235 ? 40.463  -29.148 -8.917  1.00 85.99  ? 238 ASP E CA  1 
ATOM   9692  C C   . ASP E 1 235 ? 41.215  -29.299 -10.226 1.00 99.07  ? 238 ASP E C   1 
ATOM   9693  O O   . ASP E 1 235 ? 41.554  -30.408 -10.629 1.00 103.73 ? 238 ASP E O   1 
ATOM   9694  C CB  . ASP E 1 235 ? 41.438  -28.830 -7.778  1.00 88.27  ? 238 ASP E CB  1 
ATOM   9695  C CG  . ASP E 1 235 ? 40.777  -28.071 -6.637  1.00 87.59  ? 238 ASP E CG  1 
ATOM   9696  O OD1 . ASP E 1 235 ? 39.731  -27.422 -6.875  1.00 84.10  ? 238 ASP E OD1 1 
ATOM   9697  O OD2 . ASP E 1 235 ? 41.308  -28.123 -5.505  1.00 90.83  ? 238 ASP E OD2 1 
ATOM   9698  N N   . MET E 1 236 ? 41.456  -28.174 -10.891 1.00 98.91  ? 239 MET E N   1 
ATOM   9699  C CA  . MET E 1 236 ? 42.233  -28.162 -12.118 1.00 98.79  ? 239 MET E CA  1 
ATOM   9700  C C   . MET E 1 236 ? 43.502  -28.994 -11.955 1.00 98.61  ? 239 MET E C   1 
ATOM   9701  O O   . MET E 1 236 ? 44.180  -28.915 -10.927 1.00 89.83  ? 239 MET E O   1 
ATOM   9702  C CB  . MET E 1 236 ? 42.584  -26.723 -12.510 1.00 101.93 ? 239 MET E CB  1 
ATOM   9703  C CG  . MET E 1 236 ? 41.408  -25.909 -13.032 1.00 100.82 ? 239 MET E CG  1 
ATOM   9704  S SD  . MET E 1 236 ? 41.838  -24.186 -13.353 1.00 117.35 ? 239 MET E SD  1 
ATOM   9705  C CE  . MET E 1 236 ? 42.054  -23.568 -11.685 1.00 157.48 ? 239 MET E CE  1 
ATOM   9706  N N   . TRP E 1 237 ? 43.799  -29.808 -12.965 1.00 111.89 ? 240 TRP E N   1 
ATOM   9707  C CA  . TRP E 1 237 ? 45.056  -30.551 -13.024 1.00 117.62 ? 240 TRP E CA  1 
ATOM   9708  C C   . TRP E 1 237 ? 45.180  -31.589 -11.914 1.00 119.88 ? 240 TRP E C   1 
ATOM   9709  O O   . TRP E 1 237 ? 46.277  -31.865 -11.426 1.00 129.16 ? 240 TRP E O   1 
ATOM   9710  C CB  . TRP E 1 237 ? 46.247  -29.584 -13.002 1.00 117.96 ? 240 TRP E CB  1 
ATOM   9711  C CG  . TRP E 1 237 ? 46.210  -28.570 -14.117 1.00 123.37 ? 240 TRP E CG  1 
ATOM   9712  C CD1 . TRP E 1 237 ? 45.835  -27.262 -14.025 1.00 118.35 ? 240 TRP E CD1 1 
ATOM   9713  C CD2 . TRP E 1 237 ? 46.548  -28.794 -15.495 1.00 134.29 ? 240 TRP E CD2 1 
ATOM   9714  N NE1 . TRP E 1 237 ? 45.922  -26.658 -15.255 1.00 126.41 ? 240 TRP E NE1 1 
ATOM   9715  C CE2 . TRP E 1 237 ? 46.357  -27.576 -16.173 1.00 136.28 ? 240 TRP E CE2 1 
ATOM   9716  C CE3 . TRP E 1 237 ? 46.997  -29.906 -16.217 1.00 149.25 ? 240 TRP E CE3 1 
ATOM   9717  C CZ2 . TRP E 1 237 ? 46.601  -27.438 -17.538 1.00 152.80 ? 240 TRP E CZ2 1 
ATOM   9718  C CZ3 . TRP E 1 237 ? 47.238  -29.766 -17.570 1.00 164.95 ? 240 TRP E CZ3 1 
ATOM   9719  C CH2 . TRP E 1 237 ? 47.040  -28.541 -18.217 1.00 166.89 ? 240 TRP E CH2 1 
ATOM   9720  N N   . ASP E 1 238 ? 44.048  -32.163 -11.521 1.00 110.60 ? 241 ASP E N   1 
ATOM   9721  C CA  . ASP E 1 238 ? 44.034  -33.208 -10.505 1.00 107.84 ? 241 ASP E CA  1 
ATOM   9722  C C   . ASP E 1 238 ? 43.651  -34.530 -11.157 1.00 109.37 ? 241 ASP E C   1 
ATOM   9723  O O   . ASP E 1 238 ? 43.469  -34.599 -12.371 1.00 118.92 ? 241 ASP E O   1 
ATOM   9724  C CB  . ASP E 1 238 ? 43.053  -32.860 -9.382  1.00 100.47 ? 241 ASP E CB  1 
ATOM   9725  C CG  . ASP E 1 238 ? 43.439  -33.486 -8.054  1.00 98.24  ? 241 ASP E CG  1 
ATOM   9726  O OD1 . ASP E 1 238 ? 44.633  -33.802 -7.871  1.00 103.85 ? 241 ASP E OD1 1 
ATOM   9727  O OD2 . ASP E 1 238 ? 42.554  -33.653 -7.189  1.00 88.04  ? 241 ASP E OD2 1 
ATOM   9728  N N   . THR E 1 239 ? 43.529  -35.579 -10.354 1.00 108.16 ? 242 THR E N   1 
ATOM   9729  C CA  . THR E 1 239 ? 43.183  -36.889 -10.887 1.00 105.30 ? 242 THR E CA  1 
ATOM   9730  C C   . THR E 1 239 ? 42.267  -37.644 -9.928  1.00 94.06  ? 242 THR E C   1 
ATOM   9731  O O   . THR E 1 239 ? 42.588  -37.798 -8.748  1.00 90.72  ? 242 THR E O   1 
ATOM   9732  C CB  . THR E 1 239 ? 44.445  -37.725 -11.170 1.00 111.61 ? 242 THR E CB  1 
ATOM   9733  O OG1 . THR E 1 239 ? 45.414  -36.915 -11.847 1.00 124.57 ? 242 THR E OG1 1 
ATOM   9734  C CG2 . THR E 1 239 ? 44.108  -38.934 -12.029 1.00 108.34 ? 242 THR E CG2 1 
ATOM   9735  N N   . ILE E 1 240 ? 41.128  -38.107 -10.441 1.00 90.11  ? 243 ILE E N   1 
ATOM   9736  C CA  . ILE E 1 240 ? 40.158  -38.848 -9.635  1.00 79.65  ? 243 ILE E CA  1 
ATOM   9737  C C   . ILE E 1 240 ? 40.219  -40.350 -9.934  1.00 84.32  ? 243 ILE E C   1 
ATOM   9738  O O   . ILE E 1 240 ? 39.926  -40.782 -11.048 1.00 104.70 ? 243 ILE E O   1 
ATOM   9739  C CB  . ILE E 1 240 ? 38.721  -38.311 -9.843  1.00 67.76  ? 243 ILE E CB  1 
ATOM   9740  C CG1 . ILE E 1 240 ? 37.793  -38.783 -8.717  1.00 58.69  ? 243 ILE E CG1 1 
ATOM   9741  C CG2 . ILE E 1 240 ? 38.182  -38.693 -11.215 1.00 72.84  ? 243 ILE E CG2 1 
ATOM   9742  C CD1 . ILE E 1 240 ? 36.333  -38.391 -8.925  1.00 51.40  ? 243 ILE E CD1 1 
ATOM   9743  N N   . ASN E 1 241 ? 40.603  -41.144 -8.937  1.00 62.58  ? 244 ASN E N   1 
ATOM   9744  C CA  . ASN E 1 241 ? 40.811  -42.577 -9.139  1.00 72.06  ? 244 ASN E CA  1 
ATOM   9745  C C   . ASN E 1 241 ? 39.797  -43.482 -8.430  1.00 74.61  ? 244 ASN E C   1 
ATOM   9746  O O   . ASN E 1 241 ? 39.882  -43.698 -7.220  1.00 69.74  ? 244 ASN E O   1 
ATOM   9747  C CB  . ASN E 1 241 ? 42.228  -42.964 -8.711  1.00 79.32  ? 244 ASN E CB  1 
ATOM   9748  C CG  . ASN E 1 241 ? 43.280  -42.028 -9.269  1.00 98.02  ? 244 ASN E CG  1 
ATOM   9749  O OD1 . ASN E 1 241 ? 43.656  -42.123 -10.437 1.00 106.35 ? 244 ASN E OD1 1 
ATOM   9750  N ND2 . ASN E 1 241 ? 43.766  -41.118 -8.430  1.00 102.77 ? 244 ASN E ND2 1 
ATOM   9751  N N   . PHE E 1 242 ? 38.849  -44.020 -9.191  1.00 96.98  ? 245 PHE E N   1 
ATOM   9752  C CA  . PHE E 1 242 ? 37.925  -45.021 -8.667  1.00 91.00  ? 245 PHE E CA  1 
ATOM   9753  C C   . PHE E 1 242 ? 38.606  -46.387 -8.538  1.00 99.93  ? 245 PHE E C   1 
ATOM   9754  O O   . PHE E 1 242 ? 39.700  -46.594 -9.066  1.00 109.37 ? 245 PHE E O   1 
ATOM   9755  C CB  . PHE E 1 242 ? 36.703  -45.146 -9.574  1.00 86.27  ? 245 PHE E CB  1 
ATOM   9756  C CG  . PHE E 1 242 ? 35.861  -43.905 -9.640  1.00 89.34  ? 245 PHE E CG  1 
ATOM   9757  C CD1 . PHE E 1 242 ? 34.933  -43.622 -8.647  1.00 81.46  ? 245 PHE E CD1 1 
ATOM   9758  C CD2 . PHE E 1 242 ? 35.985  -43.027 -10.700 1.00 101.21 ? 245 PHE E CD2 1 
ATOM   9759  C CE1 . PHE E 1 242 ? 34.149  -42.482 -8.711  1.00 78.56  ? 245 PHE E CE1 1 
ATOM   9760  C CE2 . PHE E 1 242 ? 35.204  -41.884 -10.771 1.00 101.11 ? 245 PHE E CE2 1 
ATOM   9761  C CZ  . PHE E 1 242 ? 34.285  -41.613 -9.775  1.00 89.02  ? 245 PHE E CZ  1 
ATOM   9762  N N   . GLU E 1 243 ? 37.948  -47.312 -7.837  1.00 93.82  ? 246 GLU E N   1 
ATOM   9763  C CA  . GLU E 1 243 ? 38.412  -48.699 -7.680  1.00 99.50  ? 246 GLU E CA  1 
ATOM   9764  C C   . GLU E 1 243 ? 37.312  -49.499 -6.998  1.00 97.28  ? 246 GLU E C   1 
ATOM   9765  O O   . GLU E 1 243 ? 37.030  -49.280 -5.823  1.00 95.82  ? 246 GLU E O   1 
ATOM   9766  C CB  . GLU E 1 243 ? 39.693  -48.774 -6.835  1.00 101.23 ? 246 GLU E CB  1 
ATOM   9767  C CG  . GLU E 1 243 ? 40.288  -50.188 -6.686  1.00 103.36 ? 246 GLU E CG  1 
ATOM   9768  C CD  . GLU E 1 243 ? 41.420  -50.255 -5.658  1.00 98.66  ? 246 GLU E CD  1 
ATOM   9769  O OE1 . GLU E 1 243 ? 41.468  -49.378 -4.769  1.00 103.44 ? 246 GLU E OE1 1 
ATOM   9770  O OE2 . GLU E 1 243 ? 42.260  -51.179 -5.735  1.00 82.73  ? 246 GLU E OE2 1 
ATOM   9771  N N   . SER E 1 244 ? 36.684  -50.421 -7.718  1.00 105.99 ? 247 SER E N   1 
ATOM   9772  C CA  . SER E 1 244 ? 35.539  -51.130 -7.153  1.00 102.90 ? 247 SER E CA  1 
ATOM   9773  C C   . SER E 1 244 ? 35.468  -52.621 -7.491  1.00 105.33 ? 247 SER E C   1 
ATOM   9774  O O   . SER E 1 244 ? 35.549  -53.017 -8.657  1.00 111.82 ? 247 SER E O   1 
ATOM   9775  C CB  . SER E 1 244 ? 34.235  -50.442 -7.563  1.00 102.71 ? 247 SER E CB  1 
ATOM   9776  O OG  . SER E 1 244 ? 33.110  -51.136 -7.054  1.00 96.30  ? 247 SER E OG  1 
ATOM   9777  N N   . THR E 1 245 ? 35.300  -53.442 -6.458  1.00 89.19  ? 248 THR E N   1 
ATOM   9778  C CA  . THR E 1 245 ? 35.078  -54.868 -6.641  1.00 81.85  ? 248 THR E CA  1 
ATOM   9779  C C   . THR E 1 245 ? 33.586  -55.140 -6.793  1.00 74.64  ? 248 THR E C   1 
ATOM   9780  O O   . THR E 1 245 ? 33.144  -56.286 -6.715  1.00 69.26  ? 248 THR E O   1 
ATOM   9781  C CB  . THR E 1 245 ? 35.643  -55.700 -5.464  1.00 76.07  ? 248 THR E CB  1 
ATOM   9782  O OG1 . THR E 1 245 ? 34.930  -55.392 -4.259  1.00 70.96  ? 248 THR E OG1 1 
ATOM   9783  C CG2 . THR E 1 245 ? 37.124  -55.412 -5.262  1.00 74.08  ? 248 THR E CG2 1 
ATOM   9784  N N   . GLY E 1 246 ? 32.813  -54.078 -7.008  1.00 93.33  ? 249 GLY E N   1 
ATOM   9785  C CA  . GLY E 1 246 ? 31.379  -54.206 -7.197  1.00 87.17  ? 249 GLY E CA  1 
ATOM   9786  C C   . GLY E 1 246 ? 30.552  -53.173 -6.452  1.00 78.12  ? 249 GLY E C   1 
ATOM   9787  O O   . GLY E 1 246 ? 31.010  -52.590 -5.467  1.00 76.19  ? 249 GLY E O   1 
ATOM   9788  N N   . ASN E 1 247 ? 29.329  -52.955 -6.931  1.00 104.41 ? 250 ASN E N   1 
ATOM   9789  C CA  . ASN E 1 247 ? 28.375  -52.023 -6.322  1.00 88.99  ? 250 ASN E CA  1 
ATOM   9790  C C   . ASN E 1 247 ? 28.506  -50.577 -6.803  1.00 87.51  ? 250 ASN E C   1 
ATOM   9791  O O   . ASN E 1 247 ? 27.525  -49.830 -6.829  1.00 78.56  ? 250 ASN E O   1 
ATOM   9792  C CB  . ASN E 1 247 ? 28.422  -52.097 -4.797  1.00 87.88  ? 250 ASN E CB  1 
ATOM   9793  C CG  . ASN E 1 247 ? 27.905  -53.411 -4.272  1.00 89.19  ? 250 ASN E CG  1 
ATOM   9794  O OD1 . ASN E 1 247 ? 26.853  -53.469 -3.639  1.00 100.47 ? 250 ASN E OD1 1 
ATOM   9795  N ND2 . ASN E 1 247 ? 28.634  -54.482 -4.550  1.00 77.64  ? 250 ASN E ND2 1 
ATOM   9796  N N   . LEU E 1 248 ? 29.718  -50.189 -7.185  1.00 76.69  ? 251 LEU E N   1 
ATOM   9797  C CA  . LEU E 1 248 ? 29.948  -48.879 -7.785  1.00 73.23  ? 251 LEU E CA  1 
ATOM   9798  C C   . LEU E 1 248 ? 29.016  -48.614 -8.968  1.00 66.66  ? 251 LEU E C   1 
ATOM   9799  O O   . LEU E 1 248 ? 28.881  -49.444 -9.866  1.00 72.62  ? 251 LEU E O   1 
ATOM   9800  C CB  . LEU E 1 248 ? 31.402  -48.758 -8.243  1.00 87.03  ? 251 LEU E CB  1 
ATOM   9801  C CG  . LEU E 1 248 ? 31.708  -47.753 -9.355  1.00 89.25  ? 251 LEU E CG  1 
ATOM   9802  C CD1 . LEU E 1 248 ? 31.388  -46.337 -8.911  1.00 85.06  ? 251 LEU E CD1 1 
ATOM   9803  C CD2 . LEU E 1 248 ? 33.163  -47.856 -9.786  1.00 97.18  ? 251 LEU E CD2 1 
ATOM   9804  N N   . ILE E 1 249 ? 28.362  -47.459 -8.956  1.00 92.65  ? 252 ILE E N   1 
ATOM   9805  C CA  . ILE E 1 249 ? 27.643  -46.991 -10.130 1.00 84.30  ? 252 ILE E CA  1 
ATOM   9806  C C   . ILE E 1 249 ? 28.454  -45.853 -10.715 1.00 89.10  ? 252 ILE E C   1 
ATOM   9807  O O   . ILE E 1 249 ? 28.243  -44.695 -10.380 1.00 90.74  ? 252 ILE E O   1 
ATOM   9808  C CB  . ILE E 1 249 ? 26.221  -46.502 -9.806  1.00 68.02  ? 252 ILE E CB  1 
ATOM   9809  C CG1 . ILE E 1 249 ? 25.417  -47.601 -9.104  1.00 63.78  ? 252 ILE E CG1 1 
ATOM   9810  C CG2 . ILE E 1 249 ? 25.520  -46.068 -11.077 1.00 64.79  ? 252 ILE E CG2 1 
ATOM   9811  C CD1 . ILE E 1 249 ? 25.627  -48.995 -9.676  1.00 60.76  ? 252 ILE E CD1 1 
ATOM   9812  N N   . ALA E 1 250 ? 29.398  -46.199 -11.579 1.00 77.88  ? 253 ALA E N   1 
ATOM   9813  C CA  . ALA E 1 250 ? 30.373  -45.239 -12.079 1.00 94.92  ? 253 ALA E CA  1 
ATOM   9814  C C   . ALA E 1 250 ? 29.746  -44.065 -12.819 1.00 96.78  ? 253 ALA E C   1 
ATOM   9815  O O   . ALA E 1 250 ? 28.627  -44.165 -13.323 1.00 92.58  ? 253 ALA E O   1 
ATOM   9816  C CB  . ALA E 1 250 ? 31.383  -45.940 -12.973 1.00 114.46 ? 253 ALA E CB  1 
ATOM   9817  N N   . PRO E 1 251 ? 30.481  -42.943 -12.880 1.00 75.29  ? 254 PRO E N   1 
ATOM   9818  C CA  . PRO E 1 251 ? 30.123  -41.771 -13.677 1.00 68.86  ? 254 PRO E CA  1 
ATOM   9819  C C   . PRO E 1 251 ? 30.703  -41.874 -15.091 1.00 94.04  ? 254 PRO E C   1 
ATOM   9820  O O   . PRO E 1 251 ? 31.855  -42.286 -15.253 1.00 119.06 ? 254 PRO E O   1 
ATOM   9821  C CB  . PRO E 1 251 ? 30.795  -40.618 -12.917 1.00 67.31  ? 254 PRO E CB  1 
ATOM   9822  C CG  . PRO E 1 251 ? 31.622  -41.255 -11.799 1.00 74.34  ? 254 PRO E CG  1 
ATOM   9823  C CD  . PRO E 1 251 ? 31.710  -42.707 -12.106 1.00 87.12  ? 254 PRO E CD  1 
ATOM   9824  N N   . GLU E 1 252 ? 29.914  -41.512 -16.098 1.00 101.71 ? 255 GLU E N   1 
ATOM   9825  C CA  . GLU E 1 252 ? 30.390  -41.543 -17.476 1.00 113.74 ? 255 GLU E CA  1 
ATOM   9826  C C   . GLU E 1 252 ? 30.809  -40.144 -17.921 1.00 118.78 ? 255 GLU E C   1 
ATOM   9827  O O   . GLU E 1 252 ? 31.840  -39.972 -18.569 1.00 137.91 ? 255 GLU E O   1 
ATOM   9828  C CB  . GLU E 1 252 ? 29.318  -42.111 -18.412 1.00 106.01 ? 255 GLU E CB  1 
ATOM   9829  C CG  . GLU E 1 252 ? 29.854  -42.610 -19.751 1.00 121.76 ? 255 GLU E CG  1 
ATOM   9830  C CD  . GLU E 1 252 ? 28.752  -43.051 -20.704 1.00 111.92 ? 255 GLU E CD  1 
ATOM   9831  O OE1 . GLU E 1 252 ? 27.583  -43.164 -20.266 1.00 93.24  ? 255 GLU E OE1 1 
ATOM   9832  O OE2 . GLU E 1 252 ? 29.060  -43.277 -21.896 1.00 122.84 ? 255 GLU E OE2 1 
ATOM   9833  N N   . TYR E 1 253 ? 30.011  -39.147 -17.556 1.00 128.25 ? 256 TYR E N   1 
ATOM   9834  C CA  . TYR E 1 253 ? 30.312  -37.765 -17.904 1.00 137.67 ? 256 TYR E CA  1 
ATOM   9835  C C   . TYR E 1 253 ? 30.782  -36.971 -16.689 1.00 134.61 ? 256 TYR E C   1 
ATOM   9836  O O   . TYR E 1 253 ? 30.650  -37.416 -15.549 1.00 129.74 ? 256 TYR E O   1 
ATOM   9837  C CB  . TYR E 1 253 ? 29.088  -37.084 -18.519 1.00 133.24 ? 256 TYR E CB  1 
ATOM   9838  C CG  . TYR E 1 253 ? 28.624  -37.684 -19.825 1.00 140.80 ? 256 TYR E CG  1 
ATOM   9839  C CD1 . TYR E 1 253 ? 28.811  -37.014 -21.026 1.00 147.76 ? 256 TYR E CD1 1 
ATOM   9840  C CD2 . TYR E 1 253 ? 27.995  -38.919 -19.855 1.00 140.70 ? 256 TYR E CD2 1 
ATOM   9841  C CE1 . TYR E 1 253 ? 28.382  -37.561 -22.222 1.00 150.96 ? 256 TYR E CE1 1 
ATOM   9842  C CE2 . TYR E 1 253 ? 27.563  -39.474 -21.043 1.00 143.18 ? 256 TYR E CE2 1 
ATOM   9843  C CZ  . TYR E 1 253 ? 27.758  -38.793 -22.223 1.00 147.68 ? 256 TYR E CZ  1 
ATOM   9844  O OH  . TYR E 1 253 ? 27.325  -39.355 -23.403 1.00 149.71 ? 256 TYR E OH  1 
ATOM   9845  N N   . GLY E 1 254 ? 31.330  -35.789 -16.952 1.00 139.63 ? 257 GLY E N   1 
ATOM   9846  C CA  . GLY E 1 254 ? 31.741  -34.863 -15.912 1.00 131.54 ? 257 GLY E CA  1 
ATOM   9847  C C   . GLY E 1 254 ? 31.286  -33.457 -16.258 1.00 121.36 ? 257 GLY E C   1 
ATOM   9848  O O   . GLY E 1 254 ? 30.856  -33.200 -17.381 1.00 134.37 ? 257 GLY E O   1 
ATOM   9849  N N   . PHE E 1 255 ? 31.374  -32.542 -15.302 1.00 94.91  ? 258 PHE E N   1 
ATOM   9850  C CA  . PHE E 1 255 ? 30.897  -31.183 -15.527 1.00 95.35  ? 258 PHE E CA  1 
ATOM   9851  C C   . PHE E 1 255 ? 31.968  -30.148 -15.237 1.00 121.28 ? 258 PHE E C   1 
ATOM   9852  O O   . PHE E 1 255 ? 32.345  -29.939 -14.085 1.00 116.83 ? 258 PHE E O   1 
ATOM   9853  C CB  . PHE E 1 255 ? 29.661  -30.888 -14.676 1.00 72.82  ? 258 PHE E CB  1 
ATOM   9854  C CG  . PHE E 1 255 ? 28.486  -31.761 -14.991 1.00 62.58  ? 258 PHE E CG  1 
ATOM   9855  C CD1 . PHE E 1 255 ? 27.591  -31.406 -15.984 1.00 55.79  ? 258 PHE E CD1 1 
ATOM   9856  C CD2 . PHE E 1 255 ? 28.272  -32.939 -14.292 1.00 61.51  ? 258 PHE E CD2 1 
ATOM   9857  C CE1 . PHE E 1 255 ? 26.502  -32.212 -16.283 1.00 47.52  ? 258 PHE E CE1 1 
ATOM   9858  C CE2 . PHE E 1 255 ? 27.187  -33.749 -14.581 1.00 53.49  ? 258 PHE E CE2 1 
ATOM   9859  C CZ  . PHE E 1 255 ? 26.298  -33.382 -15.580 1.00 49.46  ? 258 PHE E CZ  1 
ATOM   9860  N N   . LYS E 1 256 ? 32.460  -29.502 -16.287 1.00 92.36  ? 259 LYS E N   1 
ATOM   9861  C CA  . LYS E 1 256 ? 33.343  -28.367 -16.106 1.00 106.34 ? 259 LYS E CA  1 
ATOM   9862  C C   . LYS E 1 256 ? 32.548  -27.321 -15.340 1.00 101.17 ? 259 LYS E C   1 
ATOM   9863  O O   . LYS E 1 256 ? 31.324  -27.249 -15.470 1.00 85.14  ? 259 LYS E O   1 
ATOM   9864  C CB  . LYS E 1 256 ? 33.795  -27.816 -17.458 1.00 109.95 ? 259 LYS E CB  1 
ATOM   9865  C CG  . LYS E 1 256 ? 34.720  -28.736 -18.231 1.00 126.59 ? 259 LYS E CG  1 
ATOM   9866  C CD  . LYS E 1 256 ? 35.250  -28.072 -19.493 1.00 144.91 ? 259 LYS E CD  1 
ATOM   9867  C CE  . LYS E 1 256 ? 34.147  -27.860 -20.514 1.00 151.92 ? 259 LYS E CE  1 
ATOM   9868  N NZ  . LYS E 1 256 ? 34.680  -27.320 -21.792 1.00 164.54 ? 259 LYS E NZ  1 
ATOM   9869  N N   . ILE E 1 257 ? 33.224  -26.514 -14.532 1.00 121.25 ? 260 ILE E N   1 
ATOM   9870  C CA  . ILE E 1 257 ? 32.508  -25.498 -13.776 1.00 109.44 ? 260 ILE E CA  1 
ATOM   9871  C C   . ILE E 1 257 ? 33.345  -24.275 -13.438 1.00 116.68 ? 260 ILE E C   1 
ATOM   9872  O O   . ILE E 1 257 ? 34.532  -24.375 -13.122 1.00 124.20 ? 260 ILE E O   1 
ATOM   9873  C CB  . ILE E 1 257 ? 31.899  -26.078 -12.485 1.00 86.84  ? 260 ILE E CB  1 
ATOM   9874  C CG1 . ILE E 1 257 ? 30.482  -25.545 -12.288 1.00 57.19  ? 260 ILE E CG1 1 
ATOM   9875  C CG2 . ILE E 1 257 ? 32.778  -25.773 -11.277 1.00 95.57  ? 260 ILE E CG2 1 
ATOM   9876  C CD1 . ILE E 1 257 ? 29.853  -25.974 -10.994 1.00 39.19  ? 260 ILE E CD1 1 
ATOM   9877  N N   . SER E 1 258 ? 32.703  -23.116 -13.523 1.00 117.42 ? 261 SER E N   1 
ATOM   9878  C CA  . SER E 1 258 ? 33.291  -21.859 -13.089 1.00 124.35 ? 261 SER E CA  1 
ATOM   9879  C C   . SER E 1 258 ? 32.183  -21.022 -12.477 1.00 111.19 ? 261 SER E C   1 
ATOM   9880  O O   . SER E 1 258 ? 31.142  -20.828 -13.097 1.00 107.30 ? 261 SER E O   1 
ATOM   9881  C CB  . SER E 1 258 ? 33.917  -21.112 -14.268 1.00 140.42 ? 261 SER E CB  1 
ATOM   9882  O OG  . SER E 1 258 ? 35.008  -21.831 -14.815 1.00 155.00 ? 261 SER E OG  1 
ATOM   9883  N N   . LYS E 1 259 ? 32.394  -20.542 -11.256 1.00 134.02 ? 262 LYS E N   1 
ATOM   9884  C CA  . LYS E 1 259 ? 31.402  -19.696 -10.600 1.00 129.56 ? 262 LYS E CA  1 
ATOM   9885  C C   . LYS E 1 259 ? 31.867  -18.249 -10.468 1.00 145.34 ? 262 LYS E C   1 
ATOM   9886  O O   . LYS E 1 259 ? 33.002  -17.984 -10.072 1.00 154.76 ? 262 LYS E O   1 
ATOM   9887  C CB  . LYS E 1 259 ? 31.042  -20.244 -9.216  1.00 118.14 ? 262 LYS E CB  1 
ATOM   9888  C CG  . LYS E 1 259 ? 29.962  -21.316 -9.212  1.00 93.77  ? 262 LYS E CG  1 
ATOM   9889  C CD  . LYS E 1 259 ? 28.962  -21.085 -8.084  1.00 76.63  ? 262 LYS E CD  1 
ATOM   9890  C CE  . LYS E 1 259 ? 29.665  -20.702 -6.793  1.00 90.55  ? 262 LYS E CE  1 
ATOM   9891  N NZ  . LYS E 1 259 ? 30.763  -21.647 -6.455  1.00 116.84 ? 262 LYS E NZ  1 
ATOM   9892  N N   . ARG E 1 260 ? 30.979  -17.318 -10.804 1.00 157.63 ? 263 ARG E N   1 
ATOM   9893  C CA  . ARG E 1 260 ? 31.232  -15.902 -10.572 1.00 178.76 ? 263 ARG E CA  1 
ATOM   9894  C C   . ARG E 1 260 ? 30.712  -15.551 -9.187  1.00 161.61 ? 263 ARG E C   1 
ATOM   9895  O O   . ARG E 1 260 ? 31.174  -14.601 -8.553  1.00 168.00 ? 263 ARG E O   1 
ATOM   9896  C CB  . ARG E 1 260 ? 30.518  -15.044 -11.618 1.00 188.50 ? 263 ARG E CB  1 
ATOM   9897  C CG  . ARG E 1 260 ? 29.020  -14.901 -11.377 1.00 173.60 ? 263 ARG E CG  1 
ATOM   9898  C CD  . ARG E 1 260 ? 28.407  -13.820 -12.254 1.00 178.04 ? 263 ARG E CD  1 
ATOM   9899  N NE  . ARG E 1 260 ? 28.355  -14.210 -13.660 1.00 182.50 ? 263 ARG E NE  1 
ATOM   9900  C CZ  . ARG E 1 260 ? 27.277  -14.704 -14.260 1.00 172.21 ? 263 ARG E CZ  1 
ATOM   9901  N NH1 . ARG E 1 260 ? 26.151  -14.869 -13.578 1.00 159.34 ? 263 ARG E NH1 1 
ATOM   9902  N NH2 . ARG E 1 260 ? 27.323  -15.031 -15.544 1.00 175.26 ? 263 ARG E NH2 1 
ATOM   9903  N N   . GLY E 1 261 A 29.742  -16.337 -8.730  1.00 138.62 ? 263 GLY E N   1 
ATOM   9904  C CA  . GLY E 1 261 A 29.094  -16.126 -7.451  1.00 120.22 ? 263 GLY E CA  1 
ATOM   9905  C C   . GLY E 1 261 A 27.964  -17.120 -7.292  1.00 107.05 ? 263 GLY E C   1 
ATOM   9906  O O   . GLY E 1 261 A 27.923  -18.126 -8.000  1.00 112.37 ? 263 GLY E O   1 
ATOM   9907  N N   . SER E 1 262 ? 27.040  -16.844 -6.376  1.00 136.25 ? 264 SER E N   1 
ATOM   9908  C CA  . SER E 1 262 ? 25.946  -17.774 -6.104  1.00 121.89 ? 264 SER E CA  1 
ATOM   9909  C C   . SER E 1 262 ? 24.558  -17.138 -6.185  1.00 104.06 ? 264 SER E C   1 
ATOM   9910  O O   . SER E 1 262 ? 24.392  -15.939 -5.963  1.00 102.77 ? 264 SER E O   1 
ATOM   9911  C CB  . SER E 1 262 ? 26.136  -18.447 -4.741  1.00 123.56 ? 264 SER E CB  1 
ATOM   9912  O OG  . SER E 1 262 ? 27.233  -19.346 -4.764  1.00 133.51 ? 264 SER E OG  1 
ATOM   9913  N N   . SER E 1 263 ? 23.565  -17.964 -6.503  1.00 71.27  ? 265 SER E N   1 
ATOM   9914  C CA  . SER E 1 263 ? 22.173  -17.534 -6.580  1.00 65.07  ? 265 SER E CA  1 
ATOM   9915  C C   . SER E 1 263 ? 21.274  -18.445 -5.738  1.00 64.48  ? 265 SER E C   1 
ATOM   9916  O O   . SER E 1 263 ? 21.557  -18.685 -4.562  1.00 62.90  ? 265 SER E O   1 
ATOM   9917  C CB  . SER E 1 263 ? 21.700  -17.507 -8.035  1.00 65.39  ? 265 SER E CB  1 
ATOM   9918  O OG  . SER E 1 263 ? 20.315  -17.211 -8.124  1.00 64.74  ? 265 SER E OG  1 
ATOM   9919  N N   . GLY E 1 264 ? 20.197  -18.952 -6.338  1.00 72.19  ? 266 GLY E N   1 
ATOM   9920  C CA  . GLY E 1 264 ? 19.250  -19.796 -5.627  1.00 70.82  ? 266 GLY E CA  1 
ATOM   9921  C C   . GLY E 1 264 ? 18.082  -20.301 -6.462  1.00 77.02  ? 266 GLY E C   1 
ATOM   9922  O O   . GLY E 1 264 ? 17.765  -19.744 -7.512  1.00 83.33  ? 266 GLY E O   1 
ATOM   9923  N N   . ILE E 1 265 ? 17.432  -21.352 -5.972  1.00 53.66  ? 267 ILE E N   1 
ATOM   9924  C CA  . ILE E 1 265 ? 16.360  -22.043 -6.684  1.00 61.41  ? 267 ILE E CA  1 
ATOM   9925  C C   . ILE E 1 265 ? 14.991  -21.427 -6.405  1.00 81.87  ? 267 ILE E C   1 
ATOM   9926  O O   . ILE E 1 265 ? 14.703  -21.042 -5.274  1.00 83.11  ? 267 ILE E O   1 
ATOM   9927  C CB  . ILE E 1 265 ? 16.308  -23.537 -6.272  1.00 56.87  ? 267 ILE E CB  1 
ATOM   9928  C CG1 . ILE E 1 265 ? 17.502  -24.300 -6.837  1.00 44.48  ? 267 ILE E CG1 1 
ATOM   9929  C CG2 . ILE E 1 265 ? 15.015  -24.186 -6.736  1.00 76.58  ? 267 ILE E CG2 1 
ATOM   9930  C CD1 . ILE E 1 265 ? 18.819  -23.945 -6.201  1.00 32.48  ? 267 ILE E CD1 1 
ATOM   9931  N N   . MET E 1 266 ? 14.143  -21.358 -7.429  1.00 50.10  ? 268 MET E N   1 
ATOM   9932  C CA  . MET E 1 266 ? 12.812  -20.772 -7.278  1.00 63.93  ? 268 MET E CA  1 
ATOM   9933  C C   . MET E 1 266 ? 11.693  -21.805 -7.362  1.00 77.10  ? 268 MET E C   1 
ATOM   9934  O O   . MET E 1 266 ? 11.621  -22.567 -8.322  1.00 87.30  ? 268 MET E O   1 
ATOM   9935  C CB  . MET E 1 266 ? 12.583  -19.667 -8.317  1.00 67.62  ? 268 MET E CB  1 
ATOM   9936  C CG  . MET E 1 266 ? 11.216  -19.013 -8.222  1.00 76.87  ? 268 MET E CG  1 
ATOM   9937  S SD  . MET E 1 266 ? 11.244  -17.292 -8.738  1.00 107.56 ? 268 MET E SD  1 
ATOM   9938  C CE  . MET E 1 266 ? 12.508  -16.636 -7.641  1.00 47.81  ? 268 MET E CE  1 
ATOM   9939  N N   . LYS E 1 267 ? 10.813  -21.807 -6.364  1.00 96.81  ? 269 LYS E N   1 
ATOM   9940  C CA  . LYS E 1 267 ? 9.725   -22.778 -6.291  1.00 100.12 ? 269 LYS E CA  1 
ATOM   9941  C C   . LYS E 1 267 ? 8.486   -22.359 -7.076  1.00 119.19 ? 269 LYS E C   1 
ATOM   9942  O O   . LYS E 1 267 ? 7.445   -22.052 -6.493  1.00 124.48 ? 269 LYS E O   1 
ATOM   9943  C CB  . LYS E 1 267 ? 9.344   -23.059 -4.834  1.00 92.08  ? 269 LYS E CB  1 
ATOM   9944  C CG  . LYS E 1 267 ? 10.376  -23.874 -4.062  1.00 92.11  ? 269 LYS E CG  1 
ATOM   9945  C CD  . LYS E 1 267 ? 10.692  -25.183 -4.777  1.00 94.34  ? 269 LYS E CD  1 
ATOM   9946  C CE  . LYS E 1 267 ? 11.490  -26.137 -3.898  1.00 87.26  ? 269 LYS E CE  1 
ATOM   9947  N NZ  . LYS E 1 267 ? 11.567  -27.506 -4.498  1.00 89.40  ? 269 LYS E NZ  1 
ATOM   9948  N N   . THR E 1 268 ? 8.599   -22.371 -8.402  1.00 110.88 ? 270 THR E N   1 
ATOM   9949  C CA  . THR E 1 268 ? 7.486   -22.007 -9.272  1.00 120.58 ? 270 THR E CA  1 
ATOM   9950  C C   . THR E 1 268 ? 7.025   -23.165 -10.157 1.00 133.02 ? 270 THR E C   1 
ATOM   9951  O O   . THR E 1 268 ? 7.751   -24.138 -10.363 1.00 134.18 ? 270 THR E O   1 
ATOM   9952  C CB  . THR E 1 268 ? 7.855   -20.835 -10.187 1.00 124.43 ? 270 THR E CB  1 
ATOM   9953  O OG1 . THR E 1 268 ? 6.677   -20.356 -10.846 1.00 133.58 ? 270 THR E OG1 1 
ATOM   9954  C CG2 . THR E 1 268 ? 8.870   -21.282 -11.229 1.00 126.69 ? 270 THR E CG2 1 
ATOM   9955  N N   . GLU E 1 269 ? 5.811   -23.040 -10.685 1.00 142.43 ? 271 GLU E N   1 
ATOM   9956  C CA  . GLU E 1 269 ? 5.261   -24.032 -11.599 1.00 147.23 ? 271 GLU E CA  1 
ATOM   9957  C C   . GLU E 1 269 ? 5.212   -23.463 -13.014 1.00 151.31 ? 271 GLU E C   1 
ATOM   9958  O O   . GLU E 1 269 ? 5.162   -24.206 -13.994 1.00 159.90 ? 271 GLU E O   1 
ATOM   9959  C CB  . GLU E 1 269 ? 3.857   -24.446 -11.156 1.00 148.93 ? 271 GLU E CB  1 
ATOM   9960  C CG  . GLU E 1 269 ? 3.737   -24.741 -9.671  1.00 144.03 ? 271 GLU E CG  1 
ATOM   9961  C CD  . GLU E 1 269 ? 4.639   -25.875 -9.225  1.00 143.04 ? 271 GLU E CD  1 
ATOM   9962  O OE1 . GLU E 1 269 ? 4.570   -26.967 -9.830  1.00 153.34 ? 271 GLU E OE1 1 
ATOM   9963  O OE2 . GLU E 1 269 ? 5.421   -25.672 -8.270  1.00 129.04 ? 271 GLU E OE2 1 
ATOM   9964  N N   . GLY E 1 270 ? 5.228   -22.138 -13.109 1.00 113.93 ? 272 GLY E N   1 
ATOM   9965  C CA  . GLY E 1 270 ? 5.163   -21.460 -14.390 1.00 123.15 ? 272 GLY E CA  1 
ATOM   9966  C C   . GLY E 1 270 ? 6.373   -21.731 -15.261 1.00 126.32 ? 272 GLY E C   1 
ATOM   9967  O O   . GLY E 1 270 ? 7.247   -22.519 -14.902 1.00 127.49 ? 272 GLY E O   1 
ATOM   9968  N N   . THR E 1 271 ? 6.426   -21.068 -16.411 1.00 110.41 ? 273 THR E N   1 
ATOM   9969  C CA  . THR E 1 271 ? 7.498   -21.298 -17.372 1.00 113.28 ? 273 THR E CA  1 
ATOM   9970  C C   . THR E 1 271 ? 8.062   -19.988 -17.929 1.00 109.76 ? 273 THR E C   1 
ATOM   9971  O O   . THR E 1 271 ? 7.342   -18.999 -18.074 1.00 105.78 ? 273 THR E O   1 
ATOM   9972  C CB  . THR E 1 271 ? 7.024   -22.204 -18.528 1.00 127.40 ? 273 THR E CB  1 
ATOM   9973  O OG1 . THR E 1 271 ? 5.970   -21.555 -19.249 1.00 136.31 ? 273 THR E OG1 1 
ATOM   9974  C CG2 . THR E 1 271 ? 6.511   -23.534 -17.987 1.00 125.89 ? 273 THR E CG2 1 
ATOM   9975  N N   . LEU E 1 272 ? 9.355   -20.000 -18.239 1.00 110.05 ? 274 LEU E N   1 
ATOM   9976  C CA  . LEU E 1 272 ? 10.074  -18.814 -18.702 1.00 109.46 ? 274 LEU E CA  1 
ATOM   9977  C C   . LEU E 1 272 ? 9.480   -18.182 -19.960 1.00 122.91 ? 274 LEU E C   1 
ATOM   9978  O O   . LEU E 1 272 ? 9.004   -18.879 -20.855 1.00 126.13 ? 274 LEU E O   1 
ATOM   9979  C CB  . LEU E 1 272 ? 11.555  -19.147 -18.931 1.00 98.23  ? 274 LEU E CB  1 
ATOM   9980  C CG  . LEU E 1 272 ? 12.427  -18.103 -19.640 1.00 72.67  ? 274 LEU E CG  1 
ATOM   9981  C CD1 . LEU E 1 272 ? 13.901  -18.283 -19.306 1.00 49.42  ? 274 LEU E CD1 1 
ATOM   9982  C CD2 . LEU E 1 272 ? 12.223  -18.133 -21.149 1.00 80.73  ? 274 LEU E CD2 1 
ATOM   9983  N N   . GLU E 1 273 ? 9.530   -16.853 -20.020 1.00 98.01  ? 275 GLU E N   1 
ATOM   9984  C CA  . GLU E 1 273 ? 9.069   -16.114 -21.191 1.00 111.35 ? 275 GLU E CA  1 
ATOM   9985  C C   . GLU E 1 273 ? 10.151  -15.171 -21.717 1.00 112.52 ? 275 GLU E C   1 
ATOM   9986  O O   . GLU E 1 273 ? 11.205  -15.005 -21.098 1.00 100.28 ? 275 GLU E O   1 
ATOM   9987  C CB  . GLU E 1 273 ? 7.795   -15.332 -20.869 1.00 111.07 ? 275 GLU E CB  1 
ATOM   9988  C CG  . GLU E 1 273 ? 6.739   -16.148 -20.153 1.00 107.09 ? 275 GLU E CG  1 
ATOM   9989  C CD  . GLU E 1 273 ? 5.392   -15.464 -20.150 1.00 107.61 ? 275 GLU E CD  1 
ATOM   9990  O OE1 . GLU E 1 273 ? 5.119   -14.697 -21.099 1.00 113.87 ? 275 GLU E OE1 1 
ATOM   9991  O OE2 . GLU E 1 273 ? 4.610   -15.690 -19.200 1.00 100.42 ? 275 GLU E OE2 1 
ATOM   9992  N N   . ASN E 1 274 ? 9.881   -14.561 -22.867 1.00 148.76 ? 276 ASN E N   1 
ATOM   9993  C CA  . ASN E 1 274 ? 10.823  -13.644 -23.499 1.00 147.87 ? 276 ASN E CA  1 
ATOM   9994  C C   . ASN E 1 274 ? 10.729  -12.236 -22.921 1.00 142.25 ? 276 ASN E C   1 
ATOM   9995  O O   . ASN E 1 274 ? 10.131  -11.345 -23.524 1.00 151.41 ? 276 ASN E O   1 
ATOM   9996  C CB  . ASN E 1 274 ? 10.593  -13.608 -25.014 1.00 166.10 ? 276 ASN E CB  1 
ATOM   9997  C CG  . ASN E 1 274 ? 11.555  -12.678 -25.731 1.00 150.87 ? 276 ASN E CG  1 
ATOM   9998  O OD1 . ASN E 1 274 ? 12.659  -12.415 -25.252 1.00 133.07 ? 276 ASN E OD1 1 
ATOM   9999  N ND2 . ASN E 1 274 ? 11.138  -12.173 -26.888 1.00 158.80 ? 276 ASN E ND2 1 
ATOM   10000 N N   . CYS E 1 275 ? 11.320  -12.042 -21.746 1.00 140.19 ? 277 CYS E N   1 
ATOM   10001 C CA  . CYS E 1 275 ? 11.324  -10.734 -21.097 1.00 139.18 ? 277 CYS E CA  1 
ATOM   10002 C C   . CYS E 1 275 ? 12.633  -10.477 -20.355 1.00 110.89 ? 277 CYS E C   1 
ATOM   10003 O O   . CYS E 1 275 ? 13.636  -11.146 -20.598 1.00 98.53  ? 277 CYS E O   1 
ATOM   10004 C CB  . CYS E 1 275 ? 10.125  -10.589 -20.153 1.00 148.92 ? 277 CYS E CB  1 
ATOM   10005 S SG  . CYS E 1 275 ? 9.731   -12.058 -19.172 1.00 153.95 ? 277 CYS E SG  1 
ATOM   10006 N N   . GLU E 1 276 ? 12.624  -9.503  -19.454 1.00 174.79 ? 278 GLU E N   1 
ATOM   10007 C CA  . GLU E 1 276 ? 13.834  -9.163  -18.720 1.00 145.94 ? 278 GLU E CA  1 
ATOM   10008 C C   . GLU E 1 276 ? 13.511  -8.480  -17.399 1.00 141.53 ? 278 GLU E C   1 
ATOM   10009 O O   . GLU E 1 276 ? 12.446  -7.882  -17.239 1.00 155.94 ? 278 GLU E O   1 
ATOM   10010 C CB  . GLU E 1 276 ? 14.739  -8.270  -19.569 1.00 135.82 ? 278 GLU E CB  1 
ATOM   10011 C CG  . GLU E 1 276 ? 16.151  -8.164  -19.042 1.00 119.36 ? 278 GLU E CG  1 
ATOM   10012 C CD  . GLU E 1 276 ? 16.817  -9.518  -18.922 1.00 117.28 ? 278 GLU E CD  1 
ATOM   10013 O OE1 . GLU E 1 276 ? 16.659  -10.346 -19.845 1.00 119.05 ? 278 GLU E OE1 1 
ATOM   10014 O OE2 . GLU E 1 276 ? 17.493  -9.760  -17.901 1.00 115.42 ? 278 GLU E OE2 1 
ATOM   10015 N N   . THR E 1 277 ? 14.440  -8.573  -16.453 1.00 110.72 ? 279 THR E N   1 
ATOM   10016 C CA  . THR E 1 277 ? 14.256  -7.969  -15.139 1.00 107.38 ? 279 THR E CA  1 
ATOM   10017 C C   . THR E 1 277 ? 15.537  -8.030  -14.313 1.00 91.16  ? 279 THR E C   1 
ATOM   10018 O O   . THR E 1 277 ? 16.429  -8.838  -14.580 1.00 81.59  ? 279 THR E O   1 
ATOM   10019 C CB  . THR E 1 277 ? 13.111  -8.648  -14.362 1.00 118.89 ? 279 THR E CB  1 
ATOM   10020 O OG1 . THR E 1 277 ? 13.011  -8.078  -13.052 1.00 111.94 ? 279 THR E OG1 1 
ATOM   10021 C CG2 . THR E 1 277 ? 13.362  -10.141 -14.241 1.00 114.42 ? 279 THR E CG2 1 
ATOM   10022 N N   . LYS E 1 278 ? 15.625  -7.159  -13.314 1.00 119.14 ? 280 LYS E N   1 
ATOM   10023 C CA  . LYS E 1 278 ? 16.764  -7.139  -12.411 1.00 117.07 ? 280 LYS E CA  1 
ATOM   10024 C C   . LYS E 1 278 ? 16.325  -7.734  -11.080 1.00 117.34 ? 280 LYS E C   1 
ATOM   10025 O O   . LYS E 1 278 ? 17.127  -7.888  -10.159 1.00 105.94 ? 280 LYS E O   1 
ATOM   10026 C CB  . LYS E 1 278 ? 17.265  -5.705  -12.215 1.00 123.22 ? 280 LYS E CB  1 
ATOM   10027 C CG  . LYS E 1 278 ? 18.745  -5.591  -11.863 1.00 119.10 ? 280 LYS E CG  1 
ATOM   10028 C CD  . LYS E 1 278 ? 19.134  -4.163  -11.456 1.00 117.45 ? 280 LYS E CD  1 
ATOM   10029 C CE  . LYS E 1 278 ? 19.120  -3.188  -12.632 1.00 122.36 ? 280 LYS E CE  1 
ATOM   10030 N NZ  . LYS E 1 278 ? 20.253  -3.399  -13.576 1.00 120.99 ? 280 LYS E NZ  1 
ATOM   10031 N N   . CYS E 1 279 ? 15.040  -8.073  -10.993 1.00 101.61 ? 281 CYS E N   1 
ATOM   10032 C CA  . CYS E 1 279 ? 14.450  -8.594  -9.762  1.00 101.31 ? 281 CYS E CA  1 
ATOM   10033 C C   . CYS E 1 279 ? 13.301  -9.552  -10.081 1.00 112.02 ? 281 CYS E C   1 
ATOM   10034 O O   . CYS E 1 279 ? 12.246  -9.136  -10.568 1.00 125.79 ? 281 CYS E O   1 
ATOM   10035 C CB  . CYS E 1 279 ? 13.955  -7.443  -8.878  1.00 103.39 ? 281 CYS E CB  1 
ATOM   10036 S SG  . CYS E 1 279 ? 13.562  -7.874  -7.156  1.00 82.02  ? 281 CYS E SG  1 
ATOM   10037 N N   . GLN E 1 280 ? 13.514  -10.838 -9.805  1.00 62.08  ? 282 GLN E N   1 
ATOM   10038 C CA  . GLN E 1 280 ? 12.511  -11.852 -10.096 1.00 68.74  ? 282 GLN E CA  1 
ATOM   10039 C C   . GLN E 1 280 ? 11.882  -12.433 -8.831  1.00 67.95  ? 282 GLN E C   1 
ATOM   10040 O O   . GLN E 1 280 ? 12.539  -12.558 -7.795  1.00 61.14  ? 282 GLN E O   1 
ATOM   10041 C CB  . GLN E 1 280 ? 13.109  -12.967 -10.953 1.00 63.84  ? 282 GLN E CB  1 
ATOM   10042 C CG  . GLN E 1 280 ? 12.085  -13.987 -11.425 1.00 83.84  ? 282 GLN E CG  1 
ATOM   10043 C CD  . GLN E 1 280 ? 10.988  -13.365 -12.265 1.00 100.34 ? 282 GLN E CD  1 
ATOM   10044 O OE1 . GLN E 1 280 ? 11.241  -12.850 -13.353 1.00 107.45 ? 282 GLN E OE1 1 
ATOM   10045 N NE2 . GLN E 1 280 ? 9.761   -13.403 -11.761 1.00 103.25 ? 282 GLN E NE2 1 
ATOM   10046 N N   . THR E 1 281 ? 10.603  -12.776 -8.928  1.00 70.40  ? 283 THR E N   1 
ATOM   10047 C CA  . THR E 1 281 ? 9.882   -13.376 -7.820  1.00 63.93  ? 283 THR E CA  1 
ATOM   10048 C C   . THR E 1 281 ? 9.000   -14.496 -8.347  1.00 72.24  ? 283 THR E C   1 
ATOM   10049 O O   . THR E 1 281 ? 8.760   -14.579 -9.548  1.00 87.79  ? 283 THR E O   1 
ATOM   10050 C CB  . THR E 1 281 ? 8.983   -12.347 -7.101  1.00 54.19  ? 283 THR E CB  1 
ATOM   10051 O OG1 . THR E 1 281 ? 7.633   -12.456 -7.582  1.00 57.87  ? 283 THR E OG1 1 
ATOM   10052 C CG2 . THR E 1 281 ? 9.494   -10.930 -7.320  1.00 56.80  ? 283 THR E CG2 1 
ATOM   10053 N N   . PRO E 1 282 ? 8.511   -15.362 -7.450  1.00 93.84  ? 284 PRO E N   1 
ATOM   10054 C CA  . PRO E 1 282 ? 7.572   -16.410 -7.848  1.00 100.25 ? 284 PRO E CA  1 
ATOM   10055 C C   . PRO E 1 282 ? 6.382   -15.825 -8.598  1.00 117.97 ? 284 PRO E C   1 
ATOM   10056 O O   . PRO E 1 282 ? 5.915   -16.416 -9.570  1.00 130.61 ? 284 PRO E O   1 
ATOM   10057 C CB  . PRO E 1 282 ? 7.094   -16.969 -6.507  1.00 87.96  ? 284 PRO E CB  1 
ATOM   10058 C CG  . PRO E 1 282 ? 8.196   -16.698 -5.572  1.00 85.95  ? 284 PRO E CG  1 
ATOM   10059 C CD  . PRO E 1 282 ? 8.800   -15.401 -6.007  1.00 87.05  ? 284 PRO E CD  1 
ATOM   10060 N N   . LEU E 1 283 ? 5.905   -14.668 -8.148  1.00 91.71  ? 285 LEU E N   1 
ATOM   10061 C CA  . LEU E 1 283 ? 4.675   -14.092 -8.679  1.00 91.32  ? 285 LEU E CA  1 
ATOM   10062 C C   . LEU E 1 283 ? 4.899   -13.158 -9.865  1.00 97.42  ? 285 LEU E C   1 
ATOM   10063 O O   . LEU E 1 283 ? 3.943   -12.708 -10.491 1.00 108.74 ? 285 LEU E O   1 
ATOM   10064 C CB  . LEU E 1 283 ? 3.899   -13.381 -7.567  1.00 82.80  ? 285 LEU E CB  1 
ATOM   10065 C CG  . LEU E 1 283 ? 3.582   -14.266 -6.358  1.00 67.28  ? 285 LEU E CG  1 
ATOM   10066 C CD1 . LEU E 1 283 ? 2.547   -13.608 -5.456  1.00 51.38  ? 285 LEU E CD1 1 
ATOM   10067 C CD2 . LEU E 1 283 ? 3.102   -15.631 -6.809  1.00 67.44  ? 285 LEU E CD2 1 
ATOM   10068 N N   . GLY E 1 284 ? 6.158   -12.878 -10.179 1.00 94.81  ? 286 GLY E N   1 
ATOM   10069 C CA  . GLY E 1 284 ? 6.479   -12.028 -11.310 1.00 101.17 ? 286 GLY E CA  1 
ATOM   10070 C C   . GLY E 1 284 ? 7.752   -11.237 -11.090 1.00 98.84  ? 286 GLY E C   1 
ATOM   10071 O O   . GLY E 1 284 ? 8.404   -11.377 -10.058 1.00 96.50  ? 286 GLY E O   1 
ATOM   10072 N N   . ALA E 1 285 ? 8.114   -10.410 -12.065 1.00 69.24  ? 287 ALA E N   1 
ATOM   10073 C CA  . ALA E 1 285 ? 9.305   -9.580  -11.953 1.00 70.20  ? 287 ALA E CA  1 
ATOM   10074 C C   . ALA E 1 285 ? 8.926   -8.180  -11.481 1.00 80.10  ? 287 ALA E C   1 
ATOM   10075 O O   . ALA E 1 285 ? 7.742   -7.877  -11.298 1.00 86.52  ? 287 ALA E O   1 
ATOM   10076 C CB  . ALA E 1 285 ? 10.030  -9.515  -13.277 1.00 73.75  ? 287 ALA E CB  1 
ATOM   10077 N N   . ILE E 1 286 ? 9.928   -7.328  -11.283 1.00 109.26 ? 288 ILE E N   1 
ATOM   10078 C CA  . ILE E 1 286 ? 9.682   -5.973  -10.802 1.00 111.09 ? 288 ILE E CA  1 
ATOM   10079 C C   . ILE E 1 286 ? 10.551  -4.932  -11.502 1.00 121.95 ? 288 ILE E C   1 
ATOM   10080 O O   . ILE E 1 286 ? 11.776  -4.933  -11.364 1.00 117.70 ? 288 ILE E O   1 
ATOM   10081 C CB  . ILE E 1 286 ? 9.908   -5.865  -9.285  1.00 96.07  ? 288 ILE E CB  1 
ATOM   10082 C CG1 . ILE E 1 286 ? 9.003   -6.841  -8.534  1.00 84.40  ? 288 ILE E CG1 1 
ATOM   10083 C CG2 . ILE E 1 286 ? 9.631   -4.458  -8.817  1.00 97.87  ? 288 ILE E CG2 1 
ATOM   10084 C CD1 . ILE E 1 286 ? 9.191   -6.810  -7.037  1.00 73.75  ? 288 ILE E CD1 1 
ATOM   10085 N N   . ASN E 1 287 ? 9.907   -4.046  -12.256 1.00 139.72 ? 289 ASN E N   1 
ATOM   10086 C CA  . ASN E 1 287 ? 10.594  -2.931  -12.896 1.00 139.15 ? 289 ASN E CA  1 
ATOM   10087 C C   . ASN E 1 287 ? 10.266  -1.647  -12.146 1.00 131.67 ? 289 ASN E C   1 
ATOM   10088 O O   . ASN E 1 287 ? 9.467   -0.833  -12.610 1.00 138.29 ? 289 ASN E O   1 
ATOM   10089 C CB  . ASN E 1 287 ? 10.176  -2.813  -14.367 1.00 153.57 ? 289 ASN E CB  1 
ATOM   10090 C CG  . ASN E 1 287 ? 11.132  -1.955  -15.185 1.00 155.54 ? 289 ASN E CG  1 
ATOM   10091 O OD1 . ASN E 1 287 ? 12.285  -1.751  -14.803 1.00 145.98 ? 289 ASN E OD1 1 
ATOM   10092 N ND2 . ASN E 1 287 ? 10.655  -1.457  -16.322 1.00 157.81 ? 289 ASN E ND2 1 
ATOM   10093 N N   . THR E 1 288 ? 10.878  -1.479  -10.978 1.00 110.78 ? 290 THR E N   1 
ATOM   10094 C CA  . THR E 1 288 ? 10.572  -0.347  -10.109 1.00 109.39 ? 290 THR E CA  1 
ATOM   10095 C C   . THR E 1 288 ? 11.828  0.332   -9.576  1.00 104.77 ? 290 THR E C   1 
ATOM   10096 O O   . THR E 1 288 ? 12.903  -0.267  -9.531  1.00 94.46  ? 290 THR E O   1 
ATOM   10097 C CB  . THR E 1 288 ? 9.732   -0.782  -8.902  1.00 104.22 ? 290 THR E CB  1 
ATOM   10098 O OG1 . THR E 1 288 ? 9.091   0.361   -8.326  1.00 99.14  ? 290 THR E OG1 1 
ATOM   10099 C CG2 . THR E 1 288 ? 10.614  -1.440  -7.853  1.00 96.05  ? 290 THR E CG2 1 
ATOM   10100 N N   . THR E 1 289 ? 11.676  1.585   -9.157  1.00 119.99 ? 291 THR E N   1 
ATOM   10101 C CA  . THR E 1 289 ? 12.786  2.346   -8.603  1.00 103.48 ? 291 THR E CA  1 
ATOM   10102 C C   . THR E 1 289 ? 12.563  2.592   -7.121  1.00 102.10 ? 291 THR E C   1 
ATOM   10103 O O   . THR E 1 289 ? 13.498  2.910   -6.388  1.00 92.51  ? 291 THR E O   1 
ATOM   10104 C CB  . THR E 1 289 ? 12.930  3.701   -9.299  1.00 100.55 ? 291 THR E CB  1 
ATOM   10105 O OG1 . THR E 1 289 ? 12.301  3.647   -10.585 1.00 114.42 ? 291 THR E OG1 1 
ATOM   10106 C CG2 . THR E 1 289 ? 14.401  4.061   -9.456  1.00 75.99  ? 291 THR E CG2 1 
ATOM   10107 N N   . LEU E 1 290 ? 11.314  2.443   -6.693  1.00 101.76 ? 292 LEU E N   1 
ATOM   10108 C CA  . LEU E 1 290 ? 10.941  2.635   -5.298  1.00 86.13  ? 292 LEU E CA  1 
ATOM   10109 C C   . LEU E 1 290 ? 11.871  1.863   -4.366  1.00 73.07  ? 292 LEU E C   1 
ATOM   10110 O O   . LEU E 1 290 ? 12.459  0.859   -4.761  1.00 75.32  ? 292 LEU E O   1 
ATOM   10111 C CB  . LEU E 1 290 ? 9.499   2.190   -5.075  1.00 88.32  ? 292 LEU E CB  1 
ATOM   10112 C CG  . LEU E 1 290 ? 8.515   2.587   -6.173  1.00 95.34  ? 292 LEU E CG  1 
ATOM   10113 C CD1 . LEU E 1 290 ? 7.086   2.343   -5.718  1.00 97.27  ? 292 LEU E CD1 1 
ATOM   10114 C CD2 . LEU E 1 290 ? 8.709   4.037   -6.571  1.00 93.35  ? 292 LEU E CD2 1 
ATOM   10115 N N   . PRO E 1 291 ? 12.013  2.339   -3.124  1.00 85.13  ? 293 PRO E N   1 
ATOM   10116 C CA  . PRO E 1 291 ? 12.890  1.710   -2.132  1.00 76.60  ? 293 PRO E CA  1 
ATOM   10117 C C   . PRO E 1 291 ? 12.247  0.545   -1.382  1.00 86.44  ? 293 PRO E C   1 
ATOM   10118 O O   . PRO E 1 291 ? 12.922  -0.052  -0.545  1.00 88.69  ? 293 PRO E O   1 
ATOM   10119 C CB  . PRO E 1 291 ? 13.174  2.847   -1.142  1.00 72.50  ? 293 PRO E CB  1 
ATOM   10120 C CG  . PRO E 1 291 ? 12.652  4.102   -1.796  1.00 80.73  ? 293 PRO E CG  1 
ATOM   10121 C CD  . PRO E 1 291 ? 11.537  3.653   -2.671  1.00 87.39  ? 293 PRO E CD  1 
ATOM   10122 N N   . PHE E 1 292 ? 10.983  0.229   -1.653  1.00 79.22  ? 294 PHE E N   1 
ATOM   10123 C CA  . PHE E 1 292 ? 10.326  -0.874  -0.949  1.00 76.64  ? 294 PHE E CA  1 
ATOM   10124 C C   . PHE E 1 292 ? 9.325   -1.661  -1.794  1.00 88.33  ? 294 PHE E C   1 
ATOM   10125 O O   . PHE E 1 292 ? 8.897   -1.214  -2.857  1.00 92.76  ? 294 PHE E O   1 
ATOM   10126 C CB  . PHE E 1 292 ? 9.639   -0.375  0.321   1.00 67.89  ? 294 PHE E CB  1 
ATOM   10127 C CG  . PHE E 1 292 ? 10.529  0.449   1.202   1.00 70.14  ? 294 PHE E CG  1 
ATOM   10128 C CD1 . PHE E 1 292 ? 11.433  -0.154  2.063   1.00 60.05  ? 294 PHE E CD1 1 
ATOM   10129 C CD2 . PHE E 1 292 ? 10.462  1.837   1.170   1.00 77.62  ? 294 PHE E CD2 1 
ATOM   10130 C CE1 . PHE E 1 292 ? 12.259  0.617   2.876   1.00 47.18  ? 294 PHE E CE1 1 
ATOM   10131 C CE2 . PHE E 1 292 ? 11.278  2.610   1.976   1.00 65.06  ? 294 PHE E CE2 1 
ATOM   10132 C CZ  . PHE E 1 292 ? 12.177  2.005   2.829   1.00 49.41  ? 294 PHE E CZ  1 
ATOM   10133 N N   . HIS E 1 293 ? 8.958   -2.843  -1.308  1.00 77.54  ? 295 HIS E N   1 
ATOM   10134 C CA  . HIS E 1 293 ? 7.928   -3.647  -1.954  1.00 79.81  ? 295 HIS E CA  1 
ATOM   10135 C C   . HIS E 1 293 ? 7.228   -4.566  -0.955  1.00 76.77  ? 295 HIS E C   1 
ATOM   10136 O O   . HIS E 1 293 ? 7.710   -4.780  0.158   1.00 67.35  ? 295 HIS E O   1 
ATOM   10137 C CB  . HIS E 1 293 ? 8.512   -4.453  -3.115  1.00 83.15  ? 295 HIS E CB  1 
ATOM   10138 C CG  . HIS E 1 293 ? 9.114   -5.763  -2.707  1.00 82.54  ? 295 HIS E CG  1 
ATOM   10139 N ND1 . HIS E 1 293 ? 8.387   -6.933  -2.661  1.00 80.19  ? 295 HIS E ND1 1 
ATOM   10140 C CD2 . HIS E 1 293 ? 10.376  -6.089  -2.338  1.00 78.29  ? 295 HIS E CD2 1 
ATOM   10141 C CE1 . HIS E 1 293 ? 9.173   -7.922  -2.275  1.00 72.76  ? 295 HIS E CE1 1 
ATOM   10142 N NE2 . HIS E 1 293 ? 10.384  -7.436  -2.070  1.00 70.44  ? 295 HIS E NE2 1 
ATOM   10143 N N   . ASN E 1 294 ? 6.081   -5.095  -1.358  1.00 76.26  ? 296 ASN E N   1 
ATOM   10144 C CA  . ASN E 1 294 ? 5.336   -6.031  -0.525  1.00 74.93  ? 296 ASN E CA  1 
ATOM   10145 C C   . ASN E 1 294 ? 4.858   -7.237  -1.334  1.00 80.55  ? 296 ASN E C   1 
ATOM   10146 O O   . ASN E 1 294 ? 3.940   -7.947  -0.921  1.00 80.08  ? 296 ASN E O   1 
ATOM   10147 C CB  . ASN E 1 294 ? 4.149   -5.329  0.133   1.00 66.08  ? 296 ASN E CB  1 
ATOM   10148 C CG  . ASN E 1 294 ? 3.153   -4.801  -0.880  1.00 78.62  ? 296 ASN E CG  1 
ATOM   10149 O OD1 . ASN E 1 294 ? 3.491   -4.588  -2.043  1.00 84.17  ? 296 ASN E OD1 1 
ATOM   10150 N ND2 . ASN E 1 294 ? 1.917   -4.584  -0.443  1.00 85.92  ? 296 ASN E ND2 1 
ATOM   10151 N N   . VAL E 1 295 ? 5.493   -7.454  -2.486  1.00 80.68  ? 297 VAL E N   1 
ATOM   10152 C CA  . VAL E 1 295 ? 5.110   -8.513  -3.424  1.00 82.42  ? 297 VAL E CA  1 
ATOM   10153 C C   . VAL E 1 295 ? 5.199   -9.904  -2.804  1.00 85.30  ? 297 VAL E C   1 
ATOM   10154 O O   . VAL E 1 295 ? 4.225   -10.421 -2.248  1.00 90.70  ? 297 VAL E O   1 
ATOM   10155 C CB  . VAL E 1 295 ? 6.016   -8.510  -4.670  1.00 75.28  ? 297 VAL E CB  1 
ATOM   10156 C CG1 . VAL E 1 295 ? 5.494   -9.492  -5.698  1.00 80.76  ? 297 VAL E CG1 1 
ATOM   10157 C CG2 . VAL E 1 295 ? 6.118   -7.118  -5.260  1.00 67.86  ? 297 VAL E CG2 1 
ATOM   10158 N N   . HIS E 1 296 ? 6.380   -10.505 -2.921  1.00 84.33  ? 298 HIS E N   1 
ATOM   10159 C CA  . HIS E 1 296 ? 6.655   -11.797 -2.314  1.00 77.21  ? 298 HIS E CA  1 
ATOM   10160 C C   . HIS E 1 296 ? 8.040   -11.784 -1.671  1.00 76.57  ? 298 HIS E C   1 
ATOM   10161 O O   . HIS E 1 296 ? 8.992   -11.265 -2.251  1.00 79.21  ? 298 HIS E O   1 
ATOM   10162 C CB  . HIS E 1 296 ? 6.559   -12.913 -3.359  1.00 72.93  ? 298 HIS E CB  1 
ATOM   10163 C CG  . HIS E 1 296 ? 6.427   -14.282 -2.769  1.00 74.01  ? 298 HIS E CG  1 
ATOM   10164 N ND1 . HIS E 1 296 ? 7.489   -15.153 -2.665  1.00 71.50  ? 298 HIS E ND1 1 
ATOM   10165 C CD2 . HIS E 1 296 ? 5.358   -14.923 -2.238  1.00 83.09  ? 298 HIS E CD2 1 
ATOM   10166 C CE1 . HIS E 1 296 ? 7.079   -16.274 -2.098  1.00 74.08  ? 298 HIS E CE1 1 
ATOM   10167 N NE2 . HIS E 1 296 ? 5.791   -16.160 -1.830  1.00 84.27  ? 298 HIS E NE2 1 
ATOM   10168 N N   . PRO E 1 297 ? 8.148   -12.353 -0.462  1.00 66.33  ? 299 PRO E N   1 
ATOM   10169 C CA  . PRO E 1 297 ? 9.400   -12.407 0.299   1.00 62.81  ? 299 PRO E CA  1 
ATOM   10170 C C   . PRO E 1 297 ? 10.521  -13.084 -0.478  1.00 73.18  ? 299 PRO E C   1 
ATOM   10171 O O   . PRO E 1 297 ? 11.662  -12.630 -0.430  1.00 76.71  ? 299 PRO E O   1 
ATOM   10172 C CB  . PRO E 1 297 ? 9.039   -13.280 1.505   1.00 54.04  ? 299 PRO E CB  1 
ATOM   10173 C CG  . PRO E 1 297 ? 7.565   -13.170 1.637   1.00 56.38  ? 299 PRO E CG  1 
ATOM   10174 C CD  . PRO E 1 297 ? 7.041   -13.019 0.246   1.00 66.75  ? 299 PRO E CD  1 
ATOM   10175 N N   . LEU E 1 298 ? 10.188  -14.162 -1.181  1.00 83.92  ? 300 LEU E N   1 
ATOM   10176 C CA  . LEU E 1 298 ? 11.180  -15.021 -1.813  1.00 79.26  ? 300 LEU E CA  1 
ATOM   10177 C C   . LEU E 1 298 ? 11.684  -14.469 -3.142  1.00 88.57  ? 300 LEU E C   1 
ATOM   10178 O O   . LEU E 1 298 ? 11.453  -15.053 -4.196  1.00 98.84  ? 300 LEU E O   1 
ATOM   10179 C CB  . LEU E 1 298 ? 10.591  -16.416 -1.993  1.00 71.17  ? 300 LEU E CB  1 
ATOM   10180 C CG  . LEU E 1 298 ? 10.196  -17.057 -0.656  1.00 56.08  ? 300 LEU E CG  1 
ATOM   10181 C CD1 . LEU E 1 298 ? 9.249   -18.244 -0.822  1.00 49.51  ? 300 LEU E CD1 1 
ATOM   10182 C CD2 . LEU E 1 298 ? 11.440  -17.470 0.112   1.00 51.07  ? 300 LEU E CD2 1 
ATOM   10183 N N   . THR E 1 299 ? 12.397  -13.351 -3.069  1.00 99.61  ? 301 THR E N   1 
ATOM   10184 C CA  . THR E 1 299 ? 12.858  -12.623 -4.243  1.00 93.87  ? 301 THR E CA  1 
ATOM   10185 C C   . THR E 1 299 ? 14.261  -13.057 -4.678  1.00 69.30  ? 301 THR E C   1 
ATOM   10186 O O   . THR E 1 299 ? 15.031  -13.580 -3.874  1.00 56.03  ? 301 THR E O   1 
ATOM   10187 C CB  . THR E 1 299 ? 12.891  -11.117 -3.941  1.00 95.60  ? 301 THR E CB  1 
ATOM   10188 O OG1 . THR E 1 299 ? 12.604  -10.377 -5.131  1.00 113.64 ? 301 THR E OG1 1 
ATOM   10189 C CG2 . THR E 1 299 ? 14.257  -10.706 -3.396  1.00 71.16  ? 301 THR E CG2 1 
ATOM   10190 N N   . ILE E 1 300 ? 14.594  -12.841 -5.948  1.00 71.20  ? 302 ILE E N   1 
ATOM   10191 C CA  . ILE E 1 300 ? 15.962  -13.056 -6.419  1.00 57.54  ? 302 ILE E CA  1 
ATOM   10192 C C   . ILE E 1 300 ? 16.427  -11.904 -7.293  1.00 62.17  ? 302 ILE E C   1 
ATOM   10193 O O   . ILE E 1 300 ? 15.769  -11.564 -8.275  1.00 65.51  ? 302 ILE E O   1 
ATOM   10194 C CB  . ILE E 1 300 ? 16.112  -14.342 -7.255  1.00 59.60  ? 302 ILE E CB  1 
ATOM   10195 C CG1 . ILE E 1 300 ? 15.905  -15.590 -6.405  1.00 54.17  ? 302 ILE E CG1 1 
ATOM   10196 C CG2 . ILE E 1 300 ? 17.492  -14.404 -7.889  1.00 51.80  ? 302 ILE E CG2 1 
ATOM   10197 C CD1 . ILE E 1 300 ? 16.207  -16.866 -7.161  1.00 44.23  ? 302 ILE E CD1 1 
ATOM   10198 N N   . GLY E 1 301 ? 17.568  -11.318 -6.936  1.00 83.23  ? 303 GLY E N   1 
ATOM   10199 C CA  . GLY E 1 301 ? 18.171  -10.256 -7.724  1.00 84.26  ? 303 GLY E CA  1 
ATOM   10200 C C   . GLY E 1 301 ? 18.594  -9.036  -6.923  1.00 83.46  ? 303 GLY E C   1 
ATOM   10201 O O   . GLY E 1 301 ? 18.936  -9.139  -5.742  1.00 83.78  ? 303 GLY E O   1 
ATOM   10202 N N   . GLU E 1 302 ? 18.598  -7.881  -7.588  1.00 102.08 ? 304 GLU E N   1 
ATOM   10203 C CA  . GLU E 1 302 ? 18.759  -6.586  -6.926  1.00 106.29 ? 304 GLU E CA  1 
ATOM   10204 C C   . GLU E 1 302 ? 17.366  -6.021  -6.656  1.00 113.93 ? 304 GLU E C   1 
ATOM   10205 O O   . GLU E 1 302 ? 16.662  -5.625  -7.587  1.00 123.18 ? 304 GLU E O   1 
ATOM   10206 C CB  . GLU E 1 302 ? 19.554  -5.615  -7.806  1.00 109.36 ? 304 GLU E CB  1 
ATOM   10207 C CG  . GLU E 1 302 ? 21.046  -5.910  -7.912  1.00 110.41 ? 304 GLU E CG  1 
ATOM   10208 C CD  . GLU E 1 302 ? 21.455  -6.445  -9.274  1.00 118.88 ? 304 GLU E CD  1 
ATOM   10209 O OE1 . GLU E 1 302 ? 22.672  -6.471  -9.563  1.00 120.35 ? 304 GLU E OE1 1 
ATOM   10210 O OE2 . GLU E 1 302 ? 20.564  -6.845  -10.052 1.00 125.01 ? 304 GLU E OE2 1 
ATOM   10211 N N   . CYS E 1 303 ? 16.967  -5.980  -5.388  1.00 81.73  ? 305 CYS E N   1 
ATOM   10212 C CA  . CYS E 1 303 ? 15.561  -5.767  -5.052  1.00 88.22  ? 305 CYS E CA  1 
ATOM   10213 C C   . CYS E 1 303 ? 15.275  -4.705  -3.993  1.00 80.96  ? 305 CYS E C   1 
ATOM   10214 O O   . CYS E 1 303 ? 16.124  -4.399  -3.153  1.00 77.07  ? 305 CYS E O   1 
ATOM   10215 C CB  . CYS E 1 303 ? 14.945  -7.094  -4.606  1.00 97.47  ? 305 CYS E CB  1 
ATOM   10216 S SG  . CYS E 1 303 ? 15.045  -8.377  -5.850  1.00 87.69  ? 305 CYS E SG  1 
ATOM   10217 N N   . PRO E 1 304 ? 14.053  -4.153  -4.021  1.00 65.25  ? 306 PRO E N   1 
ATOM   10218 C CA  . PRO E 1 304 ? 13.589  -3.247  -2.969  1.00 72.76  ? 306 PRO E CA  1 
ATOM   10219 C C   . PRO E 1 304 ? 13.674  -3.959  -1.632  1.00 77.03  ? 306 PRO E C   1 
ATOM   10220 O O   . PRO E 1 304 ? 13.984  -5.149  -1.600  1.00 79.50  ? 306 PRO E O   1 
ATOM   10221 C CB  . PRO E 1 304 ? 12.118  -3.020  -3.330  1.00 85.95  ? 306 PRO E CB  1 
ATOM   10222 C CG  . PRO E 1 304 ? 12.030  -3.304  -4.781  1.00 89.78  ? 306 PRO E CG  1 
ATOM   10223 C CD  . PRO E 1 304 ? 13.023  -4.387  -5.047  1.00 78.65  ? 306 PRO E CD  1 
ATOM   10224 N N   . LYS E 1 305 ? 13.404  -3.254  -0.543  1.00 87.43  ? 307 LYS E N   1 
ATOM   10225 C CA  . LYS E 1 305 ? 13.343  -3.905  0.756   1.00 91.67  ? 307 LYS E CA  1 
ATOM   10226 C C   . LYS E 1 305 ? 11.947  -4.458  0.992   1.00 106.16 ? 307 LYS E C   1 
ATOM   10227 O O   . LYS E 1 305 ? 10.965  -3.719  0.964   1.00 114.87 ? 307 LYS E O   1 
ATOM   10228 C CB  . LYS E 1 305 ? 13.733  -2.934  1.864   1.00 77.88  ? 307 LYS E CB  1 
ATOM   10229 C CG  . LYS E 1 305 ? 15.195  -3.013  2.265   1.00 63.14  ? 307 LYS E CG  1 
ATOM   10230 C CD  . LYS E 1 305 ? 16.080  -3.348  1.076   1.00 60.01  ? 307 LYS E CD  1 
ATOM   10231 C CE  . LYS E 1 305 ? 17.545  -3.441  1.488   1.00 48.74  ? 307 LYS E CE  1 
ATOM   10232 N NZ  . LYS E 1 305 ? 17.728  -4.336  2.677   1.00 47.97  ? 307 LYS E NZ  1 
ATOM   10233 N N   . TYR E 1 306 ? 11.855  -5.766  1.206   1.00 67.74  ? 308 TYR E N   1 
ATOM   10234 C CA  . TYR E 1 306 ? 10.560  -6.374  1.474   1.00 66.42  ? 308 TYR E CA  1 
ATOM   10235 C C   . TYR E 1 306 ? 10.052  -5.944  2.846   1.00 58.97  ? 308 TYR E C   1 
ATOM   10236 O O   . TYR E 1 306 ? 10.694  -6.206  3.865   1.00 49.81  ? 308 TYR E O   1 
ATOM   10237 C CB  . TYR E 1 306 ? 10.624  -7.900  1.389   1.00 61.45  ? 308 TYR E CB  1 
ATOM   10238 C CG  . TYR E 1 306 ? 9.281   -8.547  1.627   1.00 65.17  ? 308 TYR E CG  1 
ATOM   10239 C CD1 . TYR E 1 306 ? 8.299   -8.531  0.642   1.00 74.24  ? 308 TYR E CD1 1 
ATOM   10240 C CD2 . TYR E 1 306 ? 8.980   -9.150  2.839   1.00 55.25  ? 308 TYR E CD2 1 
ATOM   10241 C CE1 . TYR E 1 306 ? 7.062   -9.110  0.852   1.00 73.38  ? 308 TYR E CE1 1 
ATOM   10242 C CE2 . TYR E 1 306 ? 7.743   -9.730  3.060   1.00 63.68  ? 308 TYR E CE2 1 
ATOM   10243 C CZ  . TYR E 1 306 ? 6.789   -9.709  2.061   1.00 70.98  ? 308 TYR E CZ  1 
ATOM   10244 O OH  . TYR E 1 306 ? 5.557   -10.285 2.274   1.00 70.55  ? 308 TYR E OH  1 
ATOM   10245 N N   . VAL E 1 307 ? 8.903   -5.279  2.868   1.00 65.81  ? 309 VAL E N   1 
ATOM   10246 C CA  . VAL E 1 307 ? 8.325   -4.836  4.128   1.00 65.71  ? 309 VAL E CA  1 
ATOM   10247 C C   . VAL E 1 307 ? 6.913   -5.362  4.324   1.00 72.94  ? 309 VAL E C   1 
ATOM   10248 O O   . VAL E 1 307 ? 6.149   -5.501  3.367   1.00 75.13  ? 309 VAL E O   1 
ATOM   10249 C CB  . VAL E 1 307 ? 8.297   -3.306  4.235   1.00 66.56  ? 309 VAL E CB  1 
ATOM   10250 C CG1 . VAL E 1 307 ? 9.710   -2.755  4.269   1.00 64.47  ? 309 VAL E CG1 1 
ATOM   10251 C CG2 . VAL E 1 307 ? 7.511   -2.709  3.079   1.00 73.97  ? 309 VAL E CG2 1 
ATOM   10252 N N   . LYS E 1 308 ? 6.581   -5.657  5.577   1.00 99.70  ? 310 LYS E N   1 
ATOM   10253 C CA  . LYS E 1 308 ? 5.239   -6.077  5.953   1.00 109.81 ? 310 LYS E CA  1 
ATOM   10254 C C   . LYS E 1 308 ? 4.367   -4.834  6.053   1.00 110.70 ? 310 LYS E C   1 
ATOM   10255 O O   . LYS E 1 308 ? 3.864   -4.492  7.125   1.00 112.74 ? 310 LYS E O   1 
ATOM   10256 C CB  . LYS E 1 308 ? 5.272   -6.815  7.294   1.00 113.10 ? 310 LYS E CB  1 
ATOM   10257 C CG  . LYS E 1 308 ? 4.392   -8.059  7.364   1.00 124.27 ? 310 LYS E CG  1 
ATOM   10258 C CD  . LYS E 1 308 ? 2.932   -7.715  7.601   1.00 131.71 ? 310 LYS E CD  1 
ATOM   10259 C CE  . LYS E 1 308 ? 2.101   -8.972  7.796   1.00 136.87 ? 310 LYS E CE  1 
ATOM   10260 N NZ  . LYS E 1 308 ? 0.690   -8.657  8.144   1.00 140.75 ? 310 LYS E NZ  1 
ATOM   10261 N N   . SER E 1 309 ? 4.201   -4.154  4.923   1.00 74.59  ? 311 SER E N   1 
ATOM   10262 C CA  . SER E 1 309 ? 3.487   -2.886  4.889   1.00 74.13  ? 311 SER E CA  1 
ATOM   10263 C C   . SER E 1 309 ? 2.522   -2.834  3.714   1.00 77.70  ? 311 SER E C   1 
ATOM   10264 O O   . SER E 1 309 ? 2.828   -3.327  2.631   1.00 84.15  ? 311 SER E O   1 
ATOM   10265 C CB  . SER E 1 309 ? 4.487   -1.731  4.803   1.00 72.74  ? 311 SER E CB  1 
ATOM   10266 O OG  . SER E 1 309 ? 3.951   -0.638  4.082   1.00 79.40  ? 311 SER E OG  1 
ATOM   10267 N N   . GLU E 1 310 ? 1.354   -2.238  3.929   1.00 65.74  ? 312 GLU E N   1 
ATOM   10268 C CA  . GLU E 1 310 ? 0.370   -2.111  2.861   1.00 68.99  ? 312 GLU E CA  1 
ATOM   10269 C C   . GLU E 1 310 ? 0.633   -0.867  2.010   1.00 74.39  ? 312 GLU E C   1 
ATOM   10270 O O   . GLU E 1 310 ? 0.806   -0.955  0.793   1.00 80.86  ? 312 GLU E O   1 
ATOM   10271 C CB  . GLU E 1 310 ? -1.045  -2.083  3.436   1.00 74.53  ? 312 GLU E CB  1 
ATOM   10272 C CG  . GLU E 1 310 ? -2.108  -2.617  2.483   1.00 89.01  ? 312 GLU E CG  1 
ATOM   10273 C CD  . GLU E 1 310 ? -1.807  -4.031  1.991   1.00 97.43  ? 312 GLU E CD  1 
ATOM   10274 O OE1 . GLU E 1 310 ? -2.062  -5.001  2.744   1.00 97.80  ? 312 GLU E OE1 1 
ATOM   10275 O OE2 . GLU E 1 310 ? -1.312  -4.169  0.848   1.00 100.48 ? 312 GLU E OE2 1 
ATOM   10276 N N   . LYS E 1 311 ? 0.675   0.291   2.663   1.00 76.21  ? 313 LYS E N   1 
ATOM   10277 C CA  . LYS E 1 311 ? 0.868   1.558   1.968   1.00 74.81  ? 313 LYS E CA  1 
ATOM   10278 C C   . LYS E 1 311 ? 2.022   2.366   2.549   1.00 76.71  ? 313 LYS E C   1 
ATOM   10279 O O   . LYS E 1 311 ? 2.231   2.385   3.765   1.00 70.01  ? 313 LYS E O   1 
ATOM   10280 C CB  . LYS E 1 311 ? -0.419  2.382   2.014   1.00 70.73  ? 313 LYS E CB  1 
ATOM   10281 C CG  . LYS E 1 311 ? -0.968  2.593   3.417   1.00 74.44  ? 313 LYS E CG  1 
ATOM   10282 C CD  . LYS E 1 311 ? -2.307  3.323   3.389   1.00 88.74  ? 313 LYS E CD  1 
ATOM   10283 C CE  . LYS E 1 311 ? -2.202  4.661   2.664   1.00 101.65 ? 313 LYS E CE  1 
ATOM   10284 N NZ  . LYS E 1 311 ? -1.233  5.597   3.304   1.00 97.95  ? 313 LYS E NZ  1 
ATOM   10285 N N   . LEU E 1 312 ? 2.770   3.022   1.663   1.00 94.02  ? 314 LEU E N   1 
ATOM   10286 C CA  . LEU E 1 312 ? 3.823   3.956   2.052   1.00 84.67  ? 314 LEU E CA  1 
ATOM   10287 C C   . LEU E 1 312 ? 3.715   5.226   1.220   1.00 94.57  ? 314 LEU E C   1 
ATOM   10288 O O   . LEU E 1 312 ? 4.444   5.402   0.242   1.00 102.68 ? 314 LEU E O   1 
ATOM   10289 C CB  . LEU E 1 312 ? 5.208   3.333   1.875   1.00 71.21  ? 314 LEU E CB  1 
ATOM   10290 C CG  . LEU E 1 312 ? 5.588   2.239   2.877   1.00 63.53  ? 314 LEU E CG  1 
ATOM   10291 C CD1 . LEU E 1 312 ? 7.020   1.755   2.645   1.00 50.16  ? 314 LEU E CD1 1 
ATOM   10292 C CD2 . LEU E 1 312 ? 5.407   2.741   4.303   1.00 63.06  ? 314 LEU E CD2 1 
ATOM   10293 N N   . VAL E 1 313 ? 2.798   6.105   1.625   1.00 103.69 ? 315 VAL E N   1 
ATOM   10294 C CA  . VAL E 1 313 ? 2.480   7.320   0.877   1.00 102.94 ? 315 VAL E CA  1 
ATOM   10295 C C   . VAL E 1 313 ? 3.213   8.549   1.403   1.00 98.88  ? 315 VAL E C   1 
ATOM   10296 O O   . VAL E 1 313 ? 2.985   8.977   2.536   1.00 96.64  ? 315 VAL E O   1 
ATOM   10297 C CB  . VAL E 1 313 ? 0.968   7.625   0.932   1.00 101.33 ? 315 VAL E CB  1 
ATOM   10298 C CG1 . VAL E 1 313 ? 0.628   8.770   -0.006  1.00 107.51 ? 315 VAL E CG1 1 
ATOM   10299 C CG2 . VAL E 1 313 ? 0.155   6.390   0.585   1.00 100.70 ? 315 VAL E CG2 1 
ATOM   10300 N N   . LEU E 1 314 ? 4.082   9.118   0.574   1.00 76.28  ? 316 LEU E N   1 
ATOM   10301 C CA  . LEU E 1 314 ? 4.737   10.383  0.904   1.00 72.65  ? 316 LEU E CA  1 
ATOM   10302 C C   . LEU E 1 314 ? 3.940   11.586  0.395   1.00 85.55  ? 316 LEU E C   1 
ATOM   10303 O O   . LEU E 1 314 ? 3.614   11.669  -0.791  1.00 94.85  ? 316 LEU E O   1 
ATOM   10304 C CB  . LEU E 1 314 ? 6.151   10.447  0.319   1.00 65.34  ? 316 LEU E CB  1 
ATOM   10305 C CG  . LEU E 1 314 ? 7.317   9.820   1.077   1.00 61.67  ? 316 LEU E CG  1 
ATOM   10306 C CD1 . LEU E 1 314 ? 8.622   10.247  0.428   1.00 62.72  ? 316 LEU E CD1 1 
ATOM   10307 C CD2 . LEU E 1 314 ? 7.297   10.212  2.542   1.00 54.80  ? 316 LEU E CD2 1 
ATOM   10308 N N   . ALA E 1 315 ? 3.634   12.519  1.292   1.00 80.56  ? 317 ALA E N   1 
ATOM   10309 C CA  . ALA E 1 315 ? 3.037   13.791  0.896   1.00 86.93  ? 317 ALA E CA  1 
ATOM   10310 C C   . ALA E 1 315 ? 4.082   14.670  0.217   1.00 84.50  ? 317 ALA E C   1 
ATOM   10311 O O   . ALA E 1 315 ? 5.166   14.873  0.756   1.00 84.77  ? 317 ALA E O   1 
ATOM   10312 C CB  . ALA E 1 315 ? 2.462   14.505  2.107   1.00 85.80  ? 317 ALA E CB  1 
ATOM   10313 N N   . THR E 1 316 ? 3.760   15.190  -0.962  1.00 77.60  ? 318 THR E N   1 
ATOM   10314 C CA  . THR E 1 316 ? 4.670   16.095  -1.660  1.00 76.81  ? 318 THR E CA  1 
ATOM   10315 C C   . THR E 1 316 ? 4.051   17.490  -1.804  1.00 85.56  ? 318 THR E C   1 
ATOM   10316 O O   . THR E 1 316 ? 4.752   18.507  -1.775  1.00 84.17  ? 318 THR E O   1 
ATOM   10317 C CB  . THR E 1 316 ? 5.069   15.549  -3.045  1.00 70.33  ? 318 THR E CB  1 
ATOM   10318 O OG1 . THR E 1 316 ? 4.030   15.812  -3.997  1.00 75.34  ? 318 THR E OG1 1 
ATOM   10319 C CG2 . THR E 1 316 ? 5.314   14.058  -2.959  1.00 59.96  ? 318 THR E CG2 1 
ATOM   10320 N N   . GLY E 1 317 ? 2.731   17.524  -1.954  1.00 131.25 ? 319 GLY E N   1 
ATOM   10321 C CA  . GLY E 1 317 ? 2.003   18.775  -2.027  1.00 131.67 ? 319 GLY E CA  1 
ATOM   10322 C C   . GLY E 1 317 ? 1.725   19.309  -0.638  1.00 125.54 ? 319 GLY E C   1 
ATOM   10323 O O   . GLY E 1 317 ? 2.406   18.944  0.319   1.00 118.17 ? 319 GLY E O   1 
ATOM   10324 N N   . LEU E 1 318 ? 0.718   20.169  -0.529  1.00 83.24  ? 320 LEU E N   1 
ATOM   10325 C CA  . LEU E 1 318 ? 0.378   20.802  0.740   1.00 79.65  ? 320 LEU E CA  1 
ATOM   10326 C C   . LEU E 1 318 ? -1.050  20.481  1.148   1.00 84.23  ? 320 LEU E C   1 
ATOM   10327 O O   . LEU E 1 318 ? -1.897  20.197  0.304   1.00 92.53  ? 320 LEU E O   1 
ATOM   10328 C CB  . LEU E 1 318 ? 0.568   22.314  0.642   1.00 79.11  ? 320 LEU E CB  1 
ATOM   10329 C CG  . LEU E 1 318 ? -0.162  23.005  -0.517  1.00 83.93  ? 320 LEU E CG  1 
ATOM   10330 C CD1 . LEU E 1 318 ? -1.562  23.449  -0.099  1.00 93.26  ? 320 LEU E CD1 1 
ATOM   10331 C CD2 . LEU E 1 318 ? 0.642   24.185  -1.030  1.00 76.57  ? 320 LEU E CD2 1 
ATOM   10332 N N   . ARG E 1 319 ? -1.309  20.525  2.450   1.00 82.22  ? 321 ARG E N   1 
ATOM   10333 C CA  . ARG E 1 319 ? -2.628  20.205  2.972   1.00 86.28  ? 321 ARG E CA  1 
ATOM   10334 C C   . ARG E 1 319 ? -3.686  20.884  2.113   1.00 102.00 ? 321 ARG E C   1 
ATOM   10335 O O   . ARG E 1 319 ? -3.679  22.105  1.956   1.00 114.28 ? 321 ARG E O   1 
ATOM   10336 C CB  . ARG E 1 319 ? -2.739  20.641  4.436   1.00 79.92  ? 321 ARG E CB  1 
ATOM   10337 C CG  . ARG E 1 319 ? -4.062  20.301  5.111   1.00 86.68  ? 321 ARG E CG  1 
ATOM   10338 C CD  . ARG E 1 319 ? -3.950  20.416  6.631   1.00 91.06  ? 321 ARG E CD  1 
ATOM   10339 N NE  . ARG E 1 319 ? -2.962  19.484  7.177   1.00 96.27  ? 321 ARG E NE  1 
ATOM   10340 C CZ  . ARG E 1 319 ? -2.626  19.411  8.461   1.00 97.57  ? 321 ARG E CZ  1 
ATOM   10341 N NH1 . ARG E 1 319 ? -3.194  20.223  9.344   1.00 105.58 ? 321 ARG E NH1 1 
ATOM   10342 N NH2 . ARG E 1 319 ? -1.717  18.530  8.862   1.00 87.89  ? 321 ARG E NH2 1 
ATOM   10343 N N   . ASN E 1 320 ? -4.575  20.087  1.532   1.00 105.91 ? 322 ASN E N   1 
ATOM   10344 C CA  . ASN E 1 320 ? -5.636  20.627  0.690   1.00 110.96 ? 322 ASN E CA  1 
ATOM   10345 C C   . ASN E 1 320 ? -6.905  20.921  1.482   1.00 117.42 ? 322 ASN E C   1 
ATOM   10346 O O   . ASN E 1 320 ? -7.429  20.055  2.184   1.00 112.67 ? 322 ASN E O   1 
ATOM   10347 C CB  . ASN E 1 320 ? -5.944  19.681  -0.469  1.00 112.57 ? 322 ASN E CB  1 
ATOM   10348 C CG  . ASN E 1 320 ? -7.107  20.158  -1.313  1.00 116.72 ? 322 ASN E CG  1 
ATOM   10349 O OD1 . ASN E 1 320 ? -7.306  21.359  -1.493  1.00 120.19 ? 322 ASN E OD1 1 
ATOM   10350 N ND2 . ASN E 1 320 ? -7.889  19.218  -1.827  1.00 122.36 ? 322 ASN E ND2 1 
ATOM   10351 N N   . VAL E 1 321 ? -7.396  22.150  1.358   1.00 143.38 ? 323 VAL E N   1 
ATOM   10352 C CA  . VAL E 1 321 ? -8.541  22.600  2.135   1.00 148.65 ? 323 VAL E CA  1 
ATOM   10353 C C   . VAL E 1 321 ? -9.586  23.285  1.265   1.00 160.22 ? 323 VAL E C   1 
ATOM   10354 O O   . VAL E 1 321 ? -9.249  23.905  0.256   1.00 162.91 ? 323 VAL E O   1 
ATOM   10355 C CB  . VAL E 1 321 ? -8.104  23.579  3.238   1.00 141.25 ? 323 VAL E CB  1 
ATOM   10356 C CG1 . VAL E 1 321 ? -7.429  22.831  4.379   1.00 134.55 ? 323 VAL E CG1 1 
ATOM   10357 C CG2 . VAL E 1 321 ? -7.176  24.637  2.662   1.00 138.11 ? 323 VAL E CG2 1 
ATOM   10358 N N   . PRO E 1 322 ? -10.864 23.164  1.655   1.00 127.93 ? 324 PRO E N   1 
ATOM   10359 C CA  . PRO E 1 322 ? -11.972 23.877  1.010   1.00 135.40 ? 324 PRO E CA  1 
ATOM   10360 C C   . PRO E 1 322 ? -11.830 25.389  1.184   1.00 131.56 ? 324 PRO E C   1 
ATOM   10361 O O   . PRO E 1 322 ? -12.640 26.147  0.651   1.00 134.72 ? 324 PRO E O   1 
ATOM   10362 C CB  . PRO E 1 322 ? -13.203 23.378  1.774   1.00 139.68 ? 324 PRO E CB  1 
ATOM   10363 C CG  . PRO E 1 322 ? -12.786 22.074  2.368   1.00 131.97 ? 324 PRO E CG  1 
ATOM   10364 C CD  . PRO E 1 322 ? -11.337 22.238  2.699   1.00 123.22 ? 324 PRO E CD  1 
ATOM   10365 N N   . GLY F 2 1   ? -1.214  24.918  10.056  1.00 106.99 ? 1   GLY F N   1 
ATOM   10366 C CA  . GLY F 2 1   ? -0.428  23.764  10.450  1.00 96.44  ? 1   GLY F CA  1 
ATOM   10367 C C   . GLY F 2 1   ? 0.417   24.069  11.668  1.00 89.01  ? 1   GLY F C   1 
ATOM   10368 O O   . GLY F 2 1   ? -0.107  24.404  12.731  1.00 89.76  ? 1   GLY F O   1 
ATOM   10369 N N   . LEU F 2 2   ? 1.731   23.960  11.509  1.00 81.36  ? 2   LEU F N   1 
ATOM   10370 C CA  . LEU F 2 2   ? 2.649   24.227  12.607  1.00 74.91  ? 2   LEU F CA  1 
ATOM   10371 C C   . LEU F 2 2   ? 3.136   25.673  12.582  1.00 80.31  ? 2   LEU F C   1 
ATOM   10372 O O   . LEU F 2 2   ? 3.623   26.193  13.582  1.00 85.48  ? 2   LEU F O   1 
ATOM   10373 C CB  . LEU F 2 2   ? 3.841   23.270  12.558  1.00 65.69  ? 2   LEU F CB  1 
ATOM   10374 C CG  . LEU F 2 2   ? 4.816   23.383  13.734  1.00 50.75  ? 2   LEU F CG  1 
ATOM   10375 C CD1 . LEU F 2 2   ? 4.252   22.702  14.965  1.00 42.71  ? 2   LEU F CD1 1 
ATOM   10376 C CD2 . LEU F 2 2   ? 6.180   22.815  13.381  1.00 41.79  ? 2   LEU F CD2 1 
ATOM   10377 N N   . PHE F 2 3   ? 3.010   26.321  11.432  1.00 91.94  ? 3   PHE F N   1 
ATOM   10378 C CA  . PHE F 2 3   ? 3.406   27.717  11.308  1.00 82.85  ? 3   PHE F CA  1 
ATOM   10379 C C   . PHE F 2 3   ? 2.197   28.657  11.251  1.00 92.29  ? 3   PHE F C   1 
ATOM   10380 O O   . PHE F 2 3   ? 2.322   29.830  10.901  1.00 91.40  ? 3   PHE F O   1 
ATOM   10381 C CB  . PHE F 2 3   ? 4.336   27.906  10.112  1.00 73.20  ? 3   PHE F CB  1 
ATOM   10382 C CG  . PHE F 2 3   ? 5.763   27.526  10.396  1.00 69.71  ? 3   PHE F CG  1 
ATOM   10383 C CD1 . PHE F 2 3   ? 6.719   28.500  10.633  1.00 68.34  ? 3   PHE F CD1 1 
ATOM   10384 C CD2 . PHE F 2 3   ? 6.149   26.198  10.443  1.00 72.67  ? 3   PHE F CD2 1 
ATOM   10385 C CE1 . PHE F 2 3   ? 8.038   28.161  10.903  1.00 65.69  ? 3   PHE F CE1 1 
ATOM   10386 C CE2 . PHE F 2 3   ? 7.470   25.847  10.710  1.00 75.69  ? 3   PHE F CE2 1 
ATOM   10387 C CZ  . PHE F 2 3   ? 8.414   26.832  10.942  1.00 70.68  ? 3   PHE F CZ  1 
ATOM   10388 N N   . GLY F 2 4   ? 1.027   28.126  11.604  1.00 83.16  ? 4   GLY F N   1 
ATOM   10389 C CA  . GLY F 2 4   ? -0.167  28.927  11.810  1.00 76.52  ? 4   GLY F CA  1 
ATOM   10390 C C   . GLY F 2 4   ? -0.809  29.481  10.558  1.00 77.79  ? 4   GLY F C   1 
ATOM   10391 O O   . GLY F 2 4   ? -1.923  29.998  10.609  1.00 84.35  ? 4   GLY F O   1 
ATOM   10392 N N   . ALA F 2 5   ? -0.107  29.386  9.434   1.00 67.30  ? 5   ALA F N   1 
ATOM   10393 C CA  . ALA F 2 5   ? -0.614  29.917  8.174   1.00 66.43  ? 5   ALA F CA  1 
ATOM   10394 C C   . ALA F 2 5   ? -1.623  28.967  7.520   1.00 77.04  ? 5   ALA F C   1 
ATOM   10395 O O   . ALA F 2 5   ? -2.813  29.005  7.831   1.00 84.26  ? 5   ALA F O   1 
ATOM   10396 C CB  . ALA F 2 5   ? 0.539   30.223  7.222   1.00 48.25  ? 5   ALA F CB  1 
ATOM   10397 N N   . ILE F 2 6   ? -1.143  28.128  6.605   1.00 66.19  ? 6   ILE F N   1 
ATOM   10398 C CA  . ILE F 2 6   ? -1.980  27.127  5.947   1.00 69.70  ? 6   ILE F CA  1 
ATOM   10399 C C   . ILE F 2 6   ? -2.943  26.468  6.922   1.00 73.10  ? 6   ILE F C   1 
ATOM   10400 O O   . ILE F 2 6   ? -2.520  25.805  7.865   1.00 66.05  ? 6   ILE F O   1 
ATOM   10401 C CB  . ILE F 2 6   ? -1.124  26.030  5.290   1.00 66.37  ? 6   ILE F CB  1 
ATOM   10402 C CG1 . ILE F 2 6   ? -0.164  26.647  4.273   1.00 66.88  ? 6   ILE F CG1 1 
ATOM   10403 C CG2 . ILE F 2 6   ? -2.007  24.975  4.637   1.00 69.01  ? 6   ILE F CG2 1 
ATOM   10404 C CD1 . ILE F 2 6   ? 0.734   25.639  3.595   1.00 61.62  ? 6   ILE F CD1 1 
ATOM   10405 N N   . ALA F 2 7   ? -4.238  26.651  6.680   1.00 65.90  ? 7   ALA F N   1 
ATOM   10406 C CA  . ALA F 2 7   ? -5.288  26.105  7.540   1.00 70.63  ? 7   ALA F CA  1 
ATOM   10407 C C   . ALA F 2 7   ? -5.321  26.769  8.915   1.00 73.84  ? 7   ALA F C   1 
ATOM   10408 O O   . ALA F 2 7   ? -5.941  26.255  9.846   1.00 75.32  ? 7   ALA F O   1 
ATOM   10409 C CB  . ALA F 2 7   ? -5.144  24.597  7.678   1.00 65.96  ? 7   ALA F CB  1 
ATOM   10410 N N   . GLY F 2 8   ? -4.655  27.914  9.030   1.00 165.66 ? 8   GLY F N   1 
ATOM   10411 C CA  . GLY F 2 8   ? -4.608  28.663  10.274  1.00 165.98 ? 8   GLY F CA  1 
ATOM   10412 C C   . GLY F 2 8   ? -5.362  29.975  10.166  1.00 171.71 ? 8   GLY F C   1 
ATOM   10413 O O   . GLY F 2 8   ? -6.590  29.995  10.257  1.00 176.81 ? 8   GLY F O   1 
ATOM   10414 N N   . PHE F 2 9   ? -4.634  31.072  9.971   1.00 94.51  ? 9   PHE F N   1 
ATOM   10415 C CA  . PHE F 2 9   ? -5.273  32.378  9.794   1.00 91.38  ? 9   PHE F CA  1 
ATOM   10416 C C   . PHE F 2 9   ? -5.641  32.635  8.333   1.00 97.11  ? 9   PHE F C   1 
ATOM   10417 O O   . PHE F 2 9   ? -6.440  33.521  8.035   1.00 105.57 ? 9   PHE F O   1 
ATOM   10418 C CB  . PHE F 2 9   ? -4.427  33.523  10.372  1.00 83.07  ? 9   PHE F CB  1 
ATOM   10419 C CG  . PHE F 2 9   ? -3.140  33.782  9.633   1.00 78.39  ? 9   PHE F CG  1 
ATOM   10420 C CD1 . PHE F 2 9   ? -3.148  34.253  8.332   1.00 79.57  ? 9   PHE F CD1 1 
ATOM   10421 C CD2 . PHE F 2 9   ? -1.922  33.591  10.258  1.00 71.58  ? 9   PHE F CD2 1 
ATOM   10422 C CE1 . PHE F 2 9   ? -1.962  34.504  7.660   1.00 73.70  ? 9   PHE F CE1 1 
ATOM   10423 C CE2 . PHE F 2 9   ? -0.734  33.841  9.589   1.00 65.96  ? 9   PHE F CE2 1 
ATOM   10424 C CZ  . PHE F 2 9   ? -0.756  34.301  8.289   1.00 66.68  ? 9   PHE F CZ  1 
ATOM   10425 N N   . ILE F 2 10  ? -5.051  31.859  7.427   1.00 82.46  ? 10  ILE F N   1 
ATOM   10426 C CA  . ILE F 2 10  ? -5.496  31.833  6.038   1.00 86.37  ? 10  ILE F CA  1 
ATOM   10427 C C   . ILE F 2 10  ? -6.371  30.598  5.843   1.00 92.49  ? 10  ILE F C   1 
ATOM   10428 O O   . ILE F 2 10  ? -6.011  29.676  5.109   1.00 89.86  ? 10  ILE F O   1 
ATOM   10429 C CB  . ILE F 2 10  ? -4.316  31.780  5.059   1.00 77.42  ? 10  ILE F CB  1 
ATOM   10430 C CG1 . ILE F 2 10  ? -3.273  32.821  5.432   1.00 66.03  ? 10  ILE F CG1 1 
ATOM   10431 C CG2 . ILE F 2 10  ? -4.788  32.002  3.629   1.00 85.02  ? 10  ILE F CG2 1 
ATOM   10432 C CD1 . ILE F 2 10  ? -2.082  32.833  4.510   1.00 60.20  ? 10  ILE F CD1 1 
ATOM   10433 N N   . GLU F 2 11  ? -7.519  30.596  6.517   1.00 117.64 ? 11  GLU F N   1 
ATOM   10434 C CA  . GLU F 2 11  ? -8.437  29.459  6.545   1.00 119.08 ? 11  GLU F CA  1 
ATOM   10435 C C   . GLU F 2 11  ? -8.239  28.431  5.429   1.00 115.56 ? 11  GLU F C   1 
ATOM   10436 O O   . GLU F 2 11  ? -7.854  27.291  5.690   1.00 109.55 ? 11  GLU F O   1 
ATOM   10437 C CB  . GLU F 2 11  ? -9.882  29.952  6.541   1.00 129.66 ? 11  GLU F CB  1 
ATOM   10438 C CG  . GLU F 2 11  ? -10.190 30.937  7.647   1.00 138.14 ? 11  GLU F CG  1 
ATOM   10439 C CD  . GLU F 2 11  ? -11.676 31.099  7.873   1.00 152.45 ? 11  GLU F CD  1 
ATOM   10440 O OE1 . GLU F 2 11  ? -12.072 32.046  8.586   1.00 153.87 ? 11  GLU F OE1 1 
ATOM   10441 O OE2 . GLU F 2 11  ? -12.448 30.272  7.341   1.00 156.19 ? 11  GLU F OE2 1 
ATOM   10442 N N   . GLY F 2 12  ? -8.506  28.837  4.192   1.00 86.20  ? 12  GLY F N   1 
ATOM   10443 C CA  . GLY F 2 12  ? -8.460  27.920  3.067   1.00 88.35  ? 12  GLY F CA  1 
ATOM   10444 C C   . GLY F 2 12  ? -7.474  28.304  1.982   1.00 87.63  ? 12  GLY F C   1 
ATOM   10445 O O   . GLY F 2 12  ? -6.755  29.298  2.095   1.00 83.78  ? 12  GLY F O   1 
ATOM   10446 N N   . GLY F 2 13  ? -7.443  27.501  0.924   1.00 72.92  ? 13  GLY F N   1 
ATOM   10447 C CA  . GLY F 2 13  ? -6.539  27.723  -0.190  1.00 74.43  ? 13  GLY F CA  1 
ATOM   10448 C C   . GLY F 2 13  ? -7.314  28.110  -1.430  1.00 87.43  ? 13  GLY F C   1 
ATOM   10449 O O   . GLY F 2 13  ? -8.546  28.171  -1.406  1.00 94.73  ? 13  GLY F O   1 
ATOM   10450 N N   . TRP F 2 14  ? -6.598  28.354  -2.522  1.00 112.77 ? 14  TRP F N   1 
ATOM   10451 C CA  . TRP F 2 14  ? -7.208  28.931  -3.717  1.00 123.36 ? 14  TRP F CA  1 
ATOM   10452 C C   . TRP F 2 14  ? -7.329  27.978  -4.898  1.00 130.78 ? 14  TRP F C   1 
ATOM   10453 O O   . TRP F 2 14  ? -6.335  27.667  -5.560  1.00 129.07 ? 14  TRP F O   1 
ATOM   10454 C CB  . TRP F 2 14  ? -6.417  30.160  -4.157  1.00 118.11 ? 14  TRP F CB  1 
ATOM   10455 C CG  . TRP F 2 14  ? -6.417  31.253  -3.154  1.00 111.56 ? 14  TRP F CG  1 
ATOM   10456 C CD1 . TRP F 2 14  ? -7.299  31.429  -2.129  1.00 109.33 ? 14  TRP F CD1 1 
ATOM   10457 C CD2 . TRP F 2 14  ? -5.481  32.326  -3.071  1.00 107.99 ? 14  TRP F CD2 1 
ATOM   10458 N NE1 . TRP F 2 14  ? -6.972  32.553  -1.415  1.00 106.31 ? 14  TRP F NE1 1 
ATOM   10459 C CE2 . TRP F 2 14  ? -5.858  33.123  -1.974  1.00 106.47 ? 14  TRP F CE2 1 
ATOM   10460 C CE3 . TRP F 2 14  ? -4.360  32.693  -3.821  1.00 107.44 ? 14  TRP F CE3 1 
ATOM   10461 C CZ2 . TRP F 2 14  ? -5.155  34.265  -1.607  1.00 106.36 ? 14  TRP F CZ2 1 
ATOM   10462 C CZ3 . TRP F 2 14  ? -3.662  33.824  -3.455  1.00 107.32 ? 14  TRP F CZ3 1 
ATOM   10463 C CH2 . TRP F 2 14  ? -4.063  34.600  -2.360  1.00 107.10 ? 14  TRP F CH2 1 
ATOM   10464 N N   . GLN F 2 15  ? -8.552  27.537  -5.175  1.00 116.67 ? 15  GLN F N   1 
ATOM   10465 C CA  . GLN F 2 15  ? -8.815  26.766  -6.380  1.00 121.54 ? 15  GLN F CA  1 
ATOM   10466 C C   . GLN F 2 15  ? -8.409  27.603  -7.593  1.00 125.57 ? 15  GLN F C   1 
ATOM   10467 O O   . GLN F 2 15  ? -7.826  27.090  -8.551  1.00 125.15 ? 15  GLN F O   1 
ATOM   10468 C CB  . GLN F 2 15  ? -10.296 26.380  -6.464  1.00 125.77 ? 15  GLN F CB  1 
ATOM   10469 C CG  . GLN F 2 15  ? -10.795 25.502  -5.313  1.00 116.84 ? 15  GLN F CG  1 
ATOM   10470 C CD  . GLN F 2 15  ? -10.513 24.014  -5.517  1.00 109.04 ? 15  GLN F CD  1 
ATOM   10471 O OE1 . GLN F 2 15  ? -10.181 23.576  -6.620  1.00 110.65 ? 15  GLN F OE1 1 
ATOM   10472 N NE2 . GLN F 2 15  ? -10.650 23.233  -4.448  1.00 102.71 ? 15  GLN F NE2 1 
ATOM   10473 N N   . GLY F 2 16  ? -8.700  28.901  -7.528  1.00 111.46 ? 16  GLY F N   1 
ATOM   10474 C CA  . GLY F 2 16  ? -8.448  29.809  -8.633  1.00 118.68 ? 16  GLY F CA  1 
ATOM   10475 C C   . GLY F 2 16  ? -6.995  29.934  -9.051  1.00 114.53 ? 16  GLY F C   1 
ATOM   10476 O O   . GLY F 2 16  ? -6.694  30.518  -10.091 1.00 121.62 ? 16  GLY F O   1 
ATOM   10477 N N   . MET F 2 17  ? -6.089  29.391  -8.246  1.00 139.27 ? 17  MET F N   1 
ATOM   10478 C CA  . MET F 2 17  ? -4.667  29.467  -8.552  1.00 134.26 ? 17  MET F CA  1 
ATOM   10479 C C   . MET F 2 17  ? -4.205  28.175  -9.209  1.00 140.72 ? 17  MET F C   1 
ATOM   10480 O O   . MET F 2 17  ? -4.567  27.090  -8.760  1.00 139.52 ? 17  MET F O   1 
ATOM   10481 C CB  . MET F 2 17  ? -3.871  29.732  -7.279  1.00 121.51 ? 17  MET F CB  1 
ATOM   10482 C CG  . MET F 2 17  ? -2.410  30.049  -7.516  1.00 114.54 ? 17  MET F CG  1 
ATOM   10483 S SD  . MET F 2 17  ? -1.756  31.039  -6.165  1.00 113.40 ? 17  MET F SD  1 
ATOM   10484 C CE  . MET F 2 17  ? -2.290  30.071  -4.755  1.00 174.05 ? 17  MET F CE  1 
ATOM   10485 N N   . VAL F 2 18  ? -3.409  28.284  -10.270 1.00 129.06 ? 18  VAL F N   1 
ATOM   10486 C CA  . VAL F 2 18  ? -3.075  27.106  -11.067 1.00 124.58 ? 18  VAL F CA  1 
ATOM   10487 C C   . VAL F 2 18  ? -1.696  27.126  -11.728 1.00 123.52 ? 18  VAL F C   1 
ATOM   10488 O O   . VAL F 2 18  ? -1.434  26.325  -12.625 1.00 127.40 ? 18  VAL F O   1 
ATOM   10489 C CB  . VAL F 2 18  ? -4.116  26.883  -12.186 1.00 123.54 ? 18  VAL F CB  1 
ATOM   10490 C CG1 . VAL F 2 18  ? -5.504  26.667  -11.602 1.00 119.78 ? 18  VAL F CG1 1 
ATOM   10491 C CG2 . VAL F 2 18  ? -4.113  28.060  -13.150 1.00 125.92 ? 18  VAL F CG2 1 
ATOM   10492 N N   . ASP F 2 19  ? -0.814  28.021  -11.298 1.00 107.95 ? 19  ASP F N   1 
ATOM   10493 C CA  . ASP F 2 19  ? 0.492   28.146  -11.949 1.00 107.22 ? 19  ASP F CA  1 
ATOM   10494 C C   . ASP F 2 19  ? 1.669   27.920  -10.999 1.00 97.13  ? 19  ASP F C   1 
ATOM   10495 O O   . ASP F 2 19  ? 2.828   27.885  -11.422 1.00 99.67  ? 19  ASP F O   1 
ATOM   10496 C CB  . ASP F 2 19  ? 0.618   29.499  -12.656 1.00 116.93 ? 19  ASP F CB  1 
ATOM   10497 C CG  . ASP F 2 19  ? 0.174   30.662  -11.781 1.00 116.53 ? 19  ASP F CG  1 
ATOM   10498 O OD1 . ASP F 2 19  ? -0.906  30.569  -11.153 1.00 117.66 ? 19  ASP F OD1 1 
ATOM   10499 O OD2 . ASP F 2 19  ? 0.907   31.672  -11.719 1.00 111.81 ? 19  ASP F OD2 1 
ATOM   10500 N N   . GLY F 2 20  ? 1.359   27.762  -9.717  1.00 91.82  ? 20  GLY F N   1 
ATOM   10501 C CA  . GLY F 2 20  ? 2.362   27.515  -8.696  1.00 77.18  ? 20  GLY F CA  1 
ATOM   10502 C C   . GLY F 2 20  ? 1.671   27.133  -7.403  1.00 76.17  ? 20  GLY F C   1 
ATOM   10503 O O   . GLY F 2 20  ? 0.447   27.007  -7.373  1.00 82.92  ? 20  GLY F O   1 
ATOM   10504 N N   . TRP F 2 21  ? 2.441   26.949  -6.336  1.00 106.05 ? 21  TRP F N   1 
ATOM   10505 C CA  . TRP F 2 21  ? 1.865   26.545  -5.056  1.00 106.84 ? 21  TRP F CA  1 
ATOM   10506 C C   . TRP F 2 21  ? 1.233   27.713  -4.304  1.00 105.73 ? 21  TRP F C   1 
ATOM   10507 O O   . TRP F 2 21  ? 0.017   27.790  -4.168  1.00 107.48 ? 21  TRP F O   1 
ATOM   10508 C CB  . TRP F 2 21  ? 2.917   25.868  -4.177  1.00 104.98 ? 21  TRP F CB  1 
ATOM   10509 C CG  . TRP F 2 21  ? 2.987   24.375  -4.332  1.00 107.33 ? 21  TRP F CG  1 
ATOM   10510 C CD1 . TRP F 2 21  ? 1.960   23.484  -4.191  1.00 112.98 ? 21  TRP F CD1 1 
ATOM   10511 C CD2 . TRP F 2 21  ? 4.154   23.599  -4.624  1.00 103.22 ? 21  TRP F CD2 1 
ATOM   10512 N NE1 . TRP F 2 21  ? 2.416   22.205  -4.393  1.00 113.81 ? 21  TRP F NE1 1 
ATOM   10513 C CE2 . TRP F 2 21  ? 3.760   22.249  -4.658  1.00 109.90 ? 21  TRP F CE2 1 
ATOM   10514 C CE3 . TRP F 2 21  ? 5.494   23.916  -4.865  1.00 99.54  ? 21  TRP F CE3 1 
ATOM   10515 C CZ2 . TRP F 2 21  ? 4.660   21.219  -4.927  1.00 111.12 ? 21  TRP F CZ2 1 
ATOM   10516 C CZ3 . TRP F 2 21  ? 6.382   22.893  -5.128  1.00 100.26 ? 21  TRP F CZ3 1 
ATOM   10517 C CH2 . TRP F 2 21  ? 5.964   21.564  -5.159  1.00 106.00 ? 21  TRP F CH2 1 
ATOM   10518 N N   . TYR F 2 22  ? 2.066   28.620  -3.809  1.00 104.57 ? 22  TYR F N   1 
ATOM   10519 C CA  . TYR F 2 22  ? 1.582   29.778  -3.070  1.00 100.29 ? 22  TYR F CA  1 
ATOM   10520 C C   . TYR F 2 22  ? 1.641   31.012  -3.955  1.00 106.93 ? 22  TYR F C   1 
ATOM   10521 O O   . TYR F 2 22  ? 2.520   31.124  -4.809  1.00 111.51 ? 22  TYR F O   1 
ATOM   10522 C CB  . TYR F 2 22  ? 2.439   29.993  -1.830  1.00 92.31  ? 22  TYR F CB  1 
ATOM   10523 C CG  . TYR F 2 22  ? 3.394   28.854  -1.560  1.00 90.22  ? 22  TYR F CG  1 
ATOM   10524 C CD1 . TYR F 2 22  ? 3.033   27.806  -0.728  1.00 84.95  ? 22  TYR F CD1 1 
ATOM   10525 C CD2 . TYR F 2 22  ? 4.656   28.825  -2.144  1.00 85.62  ? 22  TYR F CD2 1 
ATOM   10526 C CE1 . TYR F 2 22  ? 3.902   26.767  -0.480  1.00 75.27  ? 22  TYR F CE1 1 
ATOM   10527 C CE2 . TYR F 2 22  ? 5.531   27.789  -1.903  1.00 74.02  ? 22  TYR F CE2 1 
ATOM   10528 C CZ  . TYR F 2 22  ? 5.149   26.762  -1.071  1.00 68.40  ? 22  TYR F CZ  1 
ATOM   10529 O OH  . TYR F 2 22  ? 6.016   25.722  -0.821  1.00 61.90  ? 22  TYR F OH  1 
ATOM   10530 N N   . GLY F 2 23  ? 0.709   31.939  -3.753  1.00 115.05 ? 23  GLY F N   1 
ATOM   10531 C CA  . GLY F 2 23  ? 0.660   33.135  -4.576  1.00 115.68 ? 23  GLY F CA  1 
ATOM   10532 C C   . GLY F 2 23  ? -0.187  34.261  -4.020  1.00 114.91 ? 23  GLY F C   1 
ATOM   10533 O O   . GLY F 2 23  ? -0.578  34.241  -2.852  1.00 111.69 ? 23  GLY F O   1 
ATOM   10534 N N   . TYR F 2 24  ? -0.474  35.246  -4.869  1.00 98.28  ? 24  TYR F N   1 
ATOM   10535 C CA  . TYR F 2 24  ? -1.203  36.441  -4.449  1.00 94.82  ? 24  TYR F CA  1 
ATOM   10536 C C   . TYR F 2 24  ? -2.617  36.507  -5.030  1.00 102.67 ? 24  TYR F C   1 
ATOM   10537 O O   . TYR F 2 24  ? -3.057  35.603  -5.742  1.00 112.42 ? 24  TYR F O   1 
ATOM   10538 C CB  . TYR F 2 24  ? -0.457  37.708  -4.874  1.00 95.90  ? 24  TYR F CB  1 
ATOM   10539 C CG  . TYR F 2 24  ? 1.050   37.675  -4.739  1.00 94.28  ? 24  TYR F CG  1 
ATOM   10540 C CD1 . TYR F 2 24  ? 1.667   37.899  -3.513  1.00 86.00  ? 24  TYR F CD1 1 
ATOM   10541 C CD2 . TYR F 2 24  ? 1.857   37.461  -5.850  1.00 97.34  ? 24  TYR F CD2 1 
ATOM   10542 C CE1 . TYR F 2 24  ? 3.049   37.889  -3.395  1.00 81.88  ? 24  TYR F CE1 1 
ATOM   10543 C CE2 . TYR F 2 24  ? 3.236   37.451  -5.744  1.00 95.24  ? 24  TYR F CE2 1 
ATOM   10544 C CZ  . TYR F 2 24  ? 3.827   37.667  -4.516  1.00 89.71  ? 24  TYR F CZ  1 
ATOM   10545 O OH  . TYR F 2 24  ? 5.201   37.657  -4.412  1.00 90.46  ? 24  TYR F OH  1 
ATOM   10546 N N   . HIS F 2 25  ? -3.309  37.603  -4.727  1.00 121.28 ? 25  HIS F N   1 
ATOM   10547 C CA  . HIS F 2 25  ? -4.628  37.891  -5.288  1.00 132.61 ? 25  HIS F CA  1 
ATOM   10548 C C   . HIS F 2 25  ? -4.968  39.370  -5.121  1.00 139.46 ? 25  HIS F C   1 
ATOM   10549 O O   . HIS F 2 25  ? -5.487  39.772  -4.078  1.00 140.25 ? 25  HIS F O   1 
ATOM   10550 C CB  . HIS F 2 25  ? -5.700  37.036  -4.611  1.00 137.10 ? 25  HIS F CB  1 
ATOM   10551 C CG  . HIS F 2 25  ? -7.102  37.437  -4.955  1.00 153.07 ? 25  HIS F CG  1 
ATOM   10552 N ND1 . HIS F 2 25  ? -7.607  37.361  -6.236  1.00 162.68 ? 25  HIS F ND1 1 
ATOM   10553 C CD2 . HIS F 2 25  ? -8.107  37.918  -4.185  1.00 158.09 ? 25  HIS F CD2 1 
ATOM   10554 C CE1 . HIS F 2 25  ? -8.861  37.776  -6.239  1.00 168.67 ? 25  HIS F CE1 1 
ATOM   10555 N NE2 . HIS F 2 25  ? -9.188  38.120  -5.007  1.00 164.78 ? 25  HIS F NE2 1 
ATOM   10556 N N   . HIS F 2 26  ? -4.680  40.179  -6.141  1.00 120.60 ? 26  HIS F N   1 
ATOM   10557 C CA  . HIS F 2 26  ? -4.923  41.623  -6.049  1.00 125.01 ? 26  HIS F CA  1 
ATOM   10558 C C   . HIS F 2 26  ? -6.357  42.032  -6.394  1.00 130.34 ? 26  HIS F C   1 
ATOM   10559 O O   . HIS F 2 26  ? -6.998  41.434  -7.255  1.00 137.08 ? 26  HIS F O   1 
ATOM   10560 C CB  . HIS F 2 26  ? -3.892  42.437  -6.850  1.00 129.95 ? 26  HIS F CB  1 
ATOM   10561 C CG  . HIS F 2 26  ? -3.859  42.132  -8.317  1.00 140.77 ? 26  HIS F CG  1 
ATOM   10562 N ND1 . HIS F 2 26  ? -4.990  42.118  -9.104  1.00 153.49 ? 26  HIS F ND1 1 
ATOM   10563 C CD2 . HIS F 2 26  ? -2.821  41.863  -9.146  1.00 142.87 ? 26  HIS F CD2 1 
ATOM   10564 C CE1 . HIS F 2 26  ? -4.653  41.837  -10.351 1.00 159.87 ? 26  HIS F CE1 1 
ATOM   10565 N NE2 . HIS F 2 26  ? -3.343  41.679  -10.403 1.00 154.54 ? 26  HIS F NE2 1 
ATOM   10566 N N   . SER F 2 27  ? -6.847  43.060  -5.707  1.00 135.04 ? 27  SER F N   1 
ATOM   10567 C CA  . SER F 2 27  ? -8.245  43.461  -5.812  1.00 140.94 ? 27  SER F CA  1 
ATOM   10568 C C   . SER F 2 27  ? -8.406  44.984  -5.822  1.00 148.16 ? 27  SER F C   1 
ATOM   10569 O O   . SER F 2 27  ? -8.971  45.562  -4.890  1.00 149.27 ? 27  SER F O   1 
ATOM   10570 C CB  . SER F 2 27  ? -9.044  42.848  -4.656  1.00 132.93 ? 27  SER F CB  1 
ATOM   10571 O OG  . SER F 2 27  ? -10.370 43.344  -4.614  1.00 134.66 ? 27  SER F OG  1 
ATOM   10572 N N   . ASN F 2 28  ? -7.912  45.628  -6.878  1.00 112.17 ? 28  ASN F N   1 
ATOM   10573 C CA  . ASN F 2 28  ? -7.998  47.086  -7.001  1.00 110.57 ? 28  ASN F CA  1 
ATOM   10574 C C   . ASN F 2 28  ? -9.143  47.561  -7.899  1.00 115.85 ? 28  ASN F C   1 
ATOM   10575 O O   . ASN F 2 28  ? -10.173 46.894  -8.011  1.00 116.62 ? 28  ASN F O   1 
ATOM   10576 C CB  . ASN F 2 28  ? -6.658  47.685  -7.461  1.00 106.12 ? 28  ASN F CB  1 
ATOM   10577 C CG  . ASN F 2 28  ? -6.080  46.984  -8.682  1.00 106.26 ? 28  ASN F CG  1 
ATOM   10578 O OD1 . ASN F 2 28  ? -6.781  46.268  -9.399  1.00 112.46 ? 28  ASN F OD1 1 
ATOM   10579 N ND2 . ASN F 2 28  ? -4.791  47.193  -8.922  1.00 99.70  ? 28  ASN F ND2 1 
ATOM   10580 N N   . ASP F 2 29  ? -8.963  48.720  -8.527  1.00 122.65 ? 29  ASP F N   1 
ATOM   10581 C CA  . ASP F 2 29  ? -9.977  49.267  -9.424  1.00 133.97 ? 29  ASP F CA  1 
ATOM   10582 C C   . ASP F 2 29  ? -9.985  48.529  -10.757 1.00 139.52 ? 29  ASP F C   1 
ATOM   10583 O O   . ASP F 2 29  ? -11.047 48.192  -11.282 1.00 142.38 ? 29  ASP F O   1 
ATOM   10584 C CB  . ASP F 2 29  ? -9.752  50.764  -9.650  1.00 134.36 ? 29  ASP F CB  1 
ATOM   10585 C CG  . ASP F 2 29  ? -10.029 51.593  -8.407  1.00 128.15 ? 29  ASP F CG  1 
ATOM   10586 O OD1 . ASP F 2 29  ? -10.918 51.207  -7.615  1.00 128.61 ? 29  ASP F OD1 1 
ATOM   10587 O OD2 . ASP F 2 29  ? -9.359  52.634  -8.225  1.00 122.53 ? 29  ASP F OD2 1 
ATOM   10588 N N   . GLN F 2 30  ? -8.795  48.280  -11.298 1.00 138.46 ? 30  GLN F N   1 
ATOM   10589 C CA  . GLN F 2 30  ? -8.657  47.557  -12.558 1.00 142.41 ? 30  GLN F CA  1 
ATOM   10590 C C   . GLN F 2 30  ? -8.611  46.044  -12.343 1.00 143.21 ? 30  GLN F C   1 
ATOM   10591 O O   . GLN F 2 30  ? -7.537  45.436  -12.334 1.00 141.55 ? 30  GLN F O   1 
ATOM   10592 C CB  . GLN F 2 30  ? -7.405  48.007  -13.313 1.00 138.08 ? 30  GLN F CB  1 
ATOM   10593 C CG  . GLN F 2 30  ? -7.089  49.483  -13.176 1.00 132.44 ? 30  GLN F CG  1 
ATOM   10594 C CD  . GLN F 2 30  ? -6.014  49.748  -12.142 1.00 119.05 ? 30  GLN F CD  1 
ATOM   10595 O OE1 . GLN F 2 30  ? -4.823  49.567  -12.410 1.00 111.39 ? 30  GLN F OE1 1 
ATOM   10596 N NE2 . GLN F 2 30  ? -6.426  50.175  -10.951 1.00 114.11 ? 30  GLN F NE2 1 
ATOM   10597 N N   . GLY F 2 31  ? -9.786  45.448  -12.160 1.00 221.16 ? 31  GLY F N   1 
ATOM   10598 C CA  . GLY F 2 31  ? -9.920  44.005  -12.089 1.00 217.67 ? 31  GLY F CA  1 
ATOM   10599 C C   . GLY F 2 31  ? -9.417  43.358  -10.813 1.00 206.19 ? 31  GLY F C   1 
ATOM   10600 O O   . GLY F 2 31  ? -9.087  44.034  -9.838  1.00 195.89 ? 31  GLY F O   1 
ATOM   10601 N N   . SER F 2 32  ? -9.367  42.030  -10.833 1.00 175.69 ? 32  SER F N   1 
ATOM   10602 C CA  . SER F 2 32  ? -8.906  41.240  -9.700  1.00 167.04 ? 32  SER F CA  1 
ATOM   10603 C C   . SER F 2 32  ? -8.551  39.833  -10.174 1.00 166.70 ? 32  SER F C   1 
ATOM   10604 O O   . SER F 2 32  ? -9.106  39.348  -11.160 1.00 173.39 ? 32  SER F O   1 
ATOM   10605 C CB  . SER F 2 32  ? -9.985  41.180  -8.616  1.00 167.93 ? 32  SER F CB  1 
ATOM   10606 O OG  . SER F 2 32  ? -11.194 40.643  -9.126  1.00 178.39 ? 32  SER F OG  1 
ATOM   10607 N N   . GLY F 2 33  ? -7.623  39.180  -9.478  1.00 167.07 ? 33  GLY F N   1 
ATOM   10608 C CA  . GLY F 2 33  ? -7.204  37.844  -9.864  1.00 162.07 ? 33  GLY F CA  1 
ATOM   10609 C C   . GLY F 2 33  ? -6.108  37.220  -9.017  1.00 146.92 ? 33  GLY F C   1 
ATOM   10610 O O   . GLY F 2 33  ? -5.688  37.778  -8.003  1.00 132.01 ? 33  GLY F O   1 
ATOM   10611 N N   . TYR F 2 34  ? -5.643  36.051  -9.450  1.00 87.32  ? 34  TYR F N   1 
ATOM   10612 C CA  . TYR F 2 34  ? -4.636  35.281  -8.726  1.00 77.91  ? 34  TYR F CA  1 
ATOM   10613 C C   . TYR F 2 34  ? -3.298  35.255  -9.467  1.00 76.79  ? 34  TYR F C   1 
ATOM   10614 O O   . TYR F 2 34  ? -3.249  35.198  -10.700 1.00 85.91  ? 34  TYR F O   1 
ATOM   10615 C CB  . TYR F 2 34  ? -5.117  33.844  -8.515  1.00 74.02  ? 34  TYR F CB  1 
ATOM   10616 C CG  . TYR F 2 34  ? -6.426  33.715  -7.775  1.00 74.90  ? 34  TYR F CG  1 
ATOM   10617 C CD1 . TYR F 2 34  ? -6.464  33.713  -6.388  1.00 69.55  ? 34  TYR F CD1 1 
ATOM   10618 C CD2 . TYR F 2 34  ? -7.624  33.575  -8.464  1.00 85.87  ? 34  TYR F CD2 1 
ATOM   10619 C CE1 . TYR F 2 34  ? -7.664  33.589  -5.702  1.00 73.87  ? 34  TYR F CE1 1 
ATOM   10620 C CE2 . TYR F 2 34  ? -8.829  33.449  -7.787  1.00 90.65  ? 34  TYR F CE2 1 
ATOM   10621 C CZ  . TYR F 2 34  ? -8.844  33.457  -6.405  1.00 83.79  ? 34  TYR F CZ  1 
ATOM   10622 O OH  . TYR F 2 34  ? -10.037 33.335  -5.722  1.00 87.14  ? 34  TYR F OH  1 
ATOM   10623 N N   . ALA F 2 35  ? -2.211  35.286  -8.707  1.00 127.18 ? 35  ALA F N   1 
ATOM   10624 C CA  . ALA F 2 35  ? -0.884  35.187  -9.290  1.00 123.90 ? 35  ALA F CA  1 
ATOM   10625 C C   . ALA F 2 35  ? 0.055   34.475  -8.330  1.00 121.35 ? 35  ALA F C   1 
ATOM   10626 O O   . ALA F 2 35  ? 0.584   35.079  -7.398  1.00 124.93 ? 35  ALA F O   1 
ATOM   10627 C CB  . ALA F 2 35  ? -0.350  36.564  -9.639  1.00 119.94 ? 35  ALA F CB  1 
ATOM   10628 N N   . ALA F 2 36  ? 0.249   33.182  -8.559  1.00 91.28  ? 36  ALA F N   1 
ATOM   10629 C CA  . ALA F 2 36  ? 1.150   32.392  -7.735  1.00 81.57  ? 36  ALA F CA  1 
ATOM   10630 C C   . ALA F 2 36  ? 2.579   32.910  -7.858  1.00 84.22  ? 36  ALA F C   1 
ATOM   10631 O O   . ALA F 2 36  ? 2.970   33.461  -8.891  1.00 89.89  ? 36  ALA F O   1 
ATOM   10632 C CB  . ALA F 2 36  ? 1.076   30.927  -8.117  1.00 76.37  ? 36  ALA F CB  1 
ATOM   10633 N N   . ASP F 2 37  ? 3.351   32.725  -6.794  1.00 109.91 ? 37  ASP F N   1 
ATOM   10634 C CA  . ASP F 2 37  ? 4.713   33.233  -6.730  1.00 106.87 ? 37  ASP F CA  1 
ATOM   10635 C C   . ASP F 2 37  ? 5.694   32.221  -7.308  1.00 109.19 ? 37  ASP F C   1 
ATOM   10636 O O   . ASP F 2 37  ? 6.083   31.269  -6.639  1.00 102.91 ? 37  ASP F O   1 
ATOM   10637 C CB  . ASP F 2 37  ? 5.080   33.565  -5.281  1.00 100.37 ? 37  ASP F CB  1 
ATOM   10638 C CG  . ASP F 2 37  ? 6.363   34.363  -5.169  1.00 100.97 ? 37  ASP F CG  1 
ATOM   10639 O OD1 . ASP F 2 37  ? 7.122   34.424  -6.160  1.00 106.31 ? 37  ASP F OD1 1 
ATOM   10640 O OD2 . ASP F 2 37  ? 6.615   34.929  -4.085  1.00 95.74  ? 37  ASP F OD2 1 
ATOM   10641 N N   . LYS F 2 38  ? 6.087   32.439  -8.557  1.00 118.26 ? 38  LYS F N   1 
ATOM   10642 C CA  . LYS F 2 38  ? 7.032   31.563  -9.237  1.00 122.32 ? 38  LYS F CA  1 
ATOM   10643 C C   . LYS F 2 38  ? 8.311   31.350  -8.426  1.00 117.43 ? 38  LYS F C   1 
ATOM   10644 O O   . LYS F 2 38  ? 8.872   30.254  -8.419  1.00 119.18 ? 38  LYS F O   1 
ATOM   10645 C CB  . LYS F 2 38  ? 7.370   32.128  -10.621 1.00 136.00 ? 38  LYS F CB  1 
ATOM   10646 C CG  . LYS F 2 38  ? 8.344   31.281  -11.429 1.00 146.84 ? 38  LYS F CG  1 
ATOM   10647 C CD  . LYS F 2 38  ? 8.651   31.922  -12.777 1.00 160.85 ? 38  LYS F CD  1 
ATOM   10648 C CE  . LYS F 2 38  ? 9.627   31.076  -13.581 1.00 167.69 ? 38  LYS F CE  1 
ATOM   10649 N NZ  . LYS F 2 38  ? 9.961   31.687  -14.898 1.00 175.13 ? 38  LYS F NZ  1 
ATOM   10650 N N   . GLU F 2 39  ? 8.765   32.398  -7.743  1.00 111.98 ? 39  GLU F N   1 
ATOM   10651 C CA  . GLU F 2 39  ? 9.994   32.333  -6.952  1.00 110.31 ? 39  GLU F CA  1 
ATOM   10652 C C   . GLU F 2 39  ? 9.905   31.327  -5.808  1.00 100.36 ? 39  GLU F C   1 
ATOM   10653 O O   . GLU F 2 39  ? 10.639  30.339  -5.779  1.00 101.36 ? 39  GLU F O   1 
ATOM   10654 C CB  . GLU F 2 39  ? 10.360  33.712  -6.390  1.00 117.73 ? 39  GLU F CB  1 
ATOM   10655 C CG  . GLU F 2 39  ? 11.166  34.595  -7.334  1.00 133.04 ? 39  GLU F CG  1 
ATOM   10656 C CD  . GLU F 2 39  ? 10.300  35.324  -8.343  1.00 147.97 ? 39  GLU F CD  1 
ATOM   10657 O OE1 . GLU F 2 39  ? 9.059   35.209  -8.258  1.00 152.67 ? 39  GLU F OE1 1 
ATOM   10658 O OE2 . GLU F 2 39  ? 10.861  36.015  -9.221  1.00 153.80 ? 39  GLU F OE2 1 
ATOM   10659 N N   . SER F 2 40  ? 9.008   31.585  -4.862  1.00 106.62 ? 40  SER F N   1 
ATOM   10660 C CA  . SER F 2 40  ? 8.880   30.736  -3.680  1.00 97.64  ? 40  SER F CA  1 
ATOM   10661 C C   . SER F 2 40  ? 8.177   29.408  -3.978  1.00 98.78  ? 40  SER F C   1 
ATOM   10662 O O   . SER F 2 40  ? 7.964   28.594  -3.080  1.00 99.26  ? 40  SER F O   1 
ATOM   10663 C CB  . SER F 2 40  ? 8.160   31.485  -2.554  1.00 93.47  ? 40  SER F CB  1 
ATOM   10664 O OG  . SER F 2 40  ? 6.934   32.033  -3.004  1.00 95.73  ? 40  SER F OG  1 
ATOM   10665 N N   . THR F 2 41  ? 7.818   29.200  -5.241  1.00 78.24  ? 41  THR F N   1 
ATOM   10666 C CA  . THR F 2 41  ? 7.186   27.959  -5.670  1.00 73.58  ? 41  THR F CA  1 
ATOM   10667 C C   . THR F 2 41  ? 8.230   27.015  -6.269  1.00 67.56  ? 41  THR F C   1 
ATOM   10668 O O   . THR F 2 41  ? 8.171   25.806  -6.072  1.00 57.83  ? 41  THR F O   1 
ATOM   10669 C CB  . THR F 2 41  ? 6.042   28.228  -6.681  1.00 79.90  ? 41  THR F CB  1 
ATOM   10670 O OG1 . THR F 2 41  ? 4.794   28.334  -5.979  1.00 75.19  ? 41  THR F OG1 1 
ATOM   10671 C CG2 . THR F 2 41  ? 5.945   27.111  -7.709  1.00 84.53  ? 41  THR F CG2 1 
ATOM   10672 N N   . GLN F 2 42  ? 9.197   27.588  -6.979  1.00 98.14  ? 42  GLN F N   1 
ATOM   10673 C CA  . GLN F 2 42  ? 10.256  26.816  -7.619  1.00 104.63 ? 42  GLN F CA  1 
ATOM   10674 C C   . GLN F 2 42  ? 11.376  26.470  -6.630  1.00 98.26  ? 42  GLN F C   1 
ATOM   10675 O O   . GLN F 2 42  ? 12.291  25.713  -6.950  1.00 91.61  ? 42  GLN F O   1 
ATOM   10676 C CB  . GLN F 2 42  ? 10.816  27.591  -8.821  1.00 116.08 ? 42  GLN F CB  1 
ATOM   10677 C CG  . GLN F 2 42  ? 11.760  26.799  -9.722  1.00 124.19 ? 42  GLN F CG  1 
ATOM   10678 C CD  . GLN F 2 42  ? 11.064  25.674  -10.477 1.00 132.94 ? 42  GLN F CD  1 
ATOM   10679 O OE1 . GLN F 2 42  ? 9.845   25.686  -10.652 1.00 145.17 ? 42  GLN F OE1 1 
ATOM   10680 N NE2 . GLN F 2 42  ? 11.842  24.695  -10.927 1.00 121.94 ? 42  GLN F NE2 1 
ATOM   10681 N N   . LYS F 2 43  ? 11.299  27.026  -5.426  1.00 98.46  ? 43  LYS F N   1 
ATOM   10682 C CA  . LYS F 2 43  ? 12.301  26.761  -4.399  1.00 93.98  ? 43  LYS F CA  1 
ATOM   10683 C C   . LYS F 2 43  ? 11.824  25.619  -3.514  1.00 89.74  ? 43  LYS F C   1 
ATOM   10684 O O   . LYS F 2 43  ? 12.617  24.808  -3.038  1.00 84.92  ? 43  LYS F O   1 
ATOM   10685 C CB  . LYS F 2 43  ? 12.553  28.020  -3.559  1.00 93.85  ? 43  LYS F CB  1 
ATOM   10686 C CG  . LYS F 2 43  ? 13.777  27.944  -2.652  1.00 91.75  ? 43  LYS F CG  1 
ATOM   10687 C CD  . LYS F 2 43  ? 13.953  29.224  -1.844  1.00 91.94  ? 43  LYS F CD  1 
ATOM   10688 C CE  . LYS F 2 43  ? 15.206  29.166  -0.985  1.00 88.36  ? 43  LYS F CE  1 
ATOM   10689 N NZ  . LYS F 2 43  ? 16.439  28.985  -1.805  1.00 84.39  ? 43  LYS F NZ  1 
ATOM   10690 N N   . ALA F 2 44  ? 10.514  25.564  -3.305  1.00 95.23  ? 44  ALA F N   1 
ATOM   10691 C CA  . ALA F 2 44  ? 9.902   24.506  -2.516  1.00 86.37  ? 44  ALA F CA  1 
ATOM   10692 C C   . ALA F 2 44  ? 9.782   23.234  -3.343  1.00 91.57  ? 44  ALA F C   1 
ATOM   10693 O O   . ALA F 2 44  ? 9.983   22.133  -2.835  1.00 87.25  ? 44  ALA F O   1 
ATOM   10694 C CB  . ALA F 2 44  ? 8.543   24.941  -2.021  1.00 80.71  ? 44  ALA F CB  1 
ATOM   10695 N N   . PHE F 2 45  ? 9.438   23.397  -4.617  1.00 90.95  ? 45  PHE F N   1 
ATOM   10696 C CA  . PHE F 2 45  ? 9.426   22.288  -5.556  1.00 90.72  ? 45  PHE F CA  1 
ATOM   10697 C C   . PHE F 2 45  ? 10.782  21.615  -5.490  1.00 92.04  ? 45  PHE F C   1 
ATOM   10698 O O   . PHE F 2 45  ? 10.883  20.432  -5.168  1.00 96.12  ? 45  PHE F O   1 
ATOM   10699 C CB  . PHE F 2 45  ? 9.155   22.796  -6.970  1.00 96.43  ? 45  PHE F CB  1 
ATOM   10700 C CG  . PHE F 2 45  ? 9.074   21.712  -8.006  1.00 113.28 ? 45  PHE F CG  1 
ATOM   10701 C CD1 . PHE F 2 45  ? 7.897   21.008  -8.199  1.00 122.42 ? 45  PHE F CD1 1 
ATOM   10702 C CD2 . PHE F 2 45  ? 10.169  21.411  -8.799  1.00 120.61 ? 45  PHE F CD2 1 
ATOM   10703 C CE1 . PHE F 2 45  ? 7.819   20.015  -9.157  1.00 130.81 ? 45  PHE F CE1 1 
ATOM   10704 C CE2 . PHE F 2 45  ? 10.096  20.419  -9.759  1.00 127.01 ? 45  PHE F CE2 1 
ATOM   10705 C CZ  . PHE F 2 45  ? 8.919   19.720  -9.938  1.00 133.35 ? 45  PHE F CZ  1 
ATOM   10706 N N   . ASP F 2 46  ? 11.828  22.380  -5.778  1.00 88.70  ? 46  ASP F N   1 
ATOM   10707 C CA  . ASP F 2 46  ? 13.184  21.867  -5.654  1.00 83.56  ? 46  ASP F CA  1 
ATOM   10708 C C   . ASP F 2 46  ? 13.378  21.190  -4.296  1.00 79.04  ? 46  ASP F C   1 
ATOM   10709 O O   . ASP F 2 46  ? 14.035  20.154  -4.199  1.00 80.78  ? 46  ASP F O   1 
ATOM   10710 C CB  . ASP F 2 46  ? 14.209  22.983  -5.866  1.00 86.39  ? 46  ASP F CB  1 
ATOM   10711 C CG  . ASP F 2 46  ? 14.281  23.437  -7.311  1.00 99.85  ? 46  ASP F CG  1 
ATOM   10712 O OD1 . ASP F 2 46  ? 13.272  23.281  -8.031  1.00 109.39 ? 46  ASP F OD1 1 
ATOM   10713 O OD2 . ASP F 2 46  ? 15.344  23.945  -7.729  1.00 98.85  ? 46  ASP F OD2 1 
ATOM   10714 N N   . GLY F 2 47  ? 12.792  21.772  -3.254  1.00 79.10  ? 47  GLY F N   1 
ATOM   10715 C CA  . GLY F 2 47  ? 12.839  21.178  -1.931  1.00 69.67  ? 47  GLY F CA  1 
ATOM   10716 C C   . GLY F 2 47  ? 12.260  19.776  -1.917  1.00 69.49  ? 47  GLY F C   1 
ATOM   10717 O O   . GLY F 2 47  ? 13.001  18.797  -1.866  1.00 68.46  ? 47  GLY F O   1 
ATOM   10718 N N   . ILE F 2 48  ? 10.933  19.686  -1.965  1.00 64.09  ? 48  ILE F N   1 
ATOM   10719 C CA  . ILE F 2 48  ? 10.229  18.407  -1.974  1.00 64.08  ? 48  ILE F CA  1 
ATOM   10720 C C   . ILE F 2 48  ? 10.812  17.405  -2.971  1.00 61.88  ? 48  ILE F C   1 
ATOM   10721 O O   . ILE F 2 48  ? 11.137  16.276  -2.608  1.00 60.39  ? 48  ILE F O   1 
ATOM   10722 C CB  . ILE F 2 48  ? 8.731   18.590  -2.269  1.00 66.02  ? 48  ILE F CB  1 
ATOM   10723 C CG1 . ILE F 2 48  ? 8.030   19.213  -1.062  1.00 70.29  ? 48  ILE F CG1 1 
ATOM   10724 C CG2 . ILE F 2 48  ? 8.096   17.254  -2.636  1.00 65.68  ? 48  ILE F CG2 1 
ATOM   10725 C CD1 . ILE F 2 48  ? 8.318   18.504  0.244   1.00 71.19  ? 48  ILE F CD1 1 
ATOM   10726 N N   . THR F 2 49  ? 10.932  17.813  -4.227  1.00 71.67  ? 49  THR F N   1 
ATOM   10727 C CA  . THR F 2 49  ? 11.555  16.960  -5.228  1.00 69.48  ? 49  THR F CA  1 
ATOM   10728 C C   . THR F 2 49  ? 12.897  16.429  -4.736  1.00 68.92  ? 49  THR F C   1 
ATOM   10729 O O   . THR F 2 49  ? 13.204  15.256  -4.915  1.00 69.57  ? 49  THR F O   1 
ATOM   10730 C CB  . THR F 2 49  ? 11.734  17.681  -6.580  1.00 75.59  ? 49  THR F CB  1 
ATOM   10731 O OG1 . THR F 2 49  ? 10.688  17.279  -7.473  1.00 95.10  ? 49  THR F OG1 1 
ATOM   10732 C CG2 . THR F 2 49  ? 13.078  17.332  -7.203  1.00 67.70  ? 49  THR F CG2 1 
ATOM   10733 N N   . ASN F 2 50  ? 13.698  17.274  -4.103  1.00 83.10  ? 50  ASN F N   1 
ATOM   10734 C CA  . ASN F 2 50  ? 14.981  16.803  -3.610  1.00 74.91  ? 50  ASN F CA  1 
ATOM   10735 C C   . ASN F 2 50  ? 14.830  15.954  -2.358  1.00 77.03  ? 50  ASN F C   1 
ATOM   10736 O O   . ASN F 2 50  ? 15.718  15.172  -2.019  1.00 77.34  ? 50  ASN F O   1 
ATOM   10737 C CB  . ASN F 2 50  ? 15.952  17.950  -3.362  1.00 77.92  ? 50  ASN F CB  1 
ATOM   10738 C CG  . ASN F 2 50  ? 17.322  17.457  -2.951  1.00 76.47  ? 50  ASN F CG  1 
ATOM   10739 O OD1 . ASN F 2 50  ? 17.682  17.493  -1.775  1.00 71.40  ? 50  ASN F OD1 1 
ATOM   10740 N ND2 . ASN F 2 50  ? 18.082  16.959  -3.917  1.00 81.70  ? 50  ASN F ND2 1 
ATOM   10741 N N   . LYS F 2 51  ? 13.698  16.104  -1.677  1.00 58.02  ? 51  LYS F N   1 
ATOM   10742 C CA  . LYS F 2 51  ? 13.393  15.270  -0.516  1.00 55.70  ? 51  LYS F CA  1 
ATOM   10743 C C   . LYS F 2 51  ? 13.101  13.835  -0.951  1.00 67.29  ? 51  LYS F C   1 
ATOM   10744 O O   . LYS F 2 51  ? 13.767  12.904  -0.506  1.00 68.32  ? 51  LYS F O   1 
ATOM   10745 C CB  . LYS F 2 51  ? 12.215  15.840  0.283   1.00 54.38  ? 51  LYS F CB  1 
ATOM   10746 C CG  . LYS F 2 51  ? 11.676  14.895  1.340   1.00 48.39  ? 51  LYS F CG  1 
ATOM   10747 C CD  . LYS F 2 51  ? 10.441  15.449  2.033   1.00 54.58  ? 51  LYS F CD  1 
ATOM   10748 C CE  . LYS F 2 51  ? 10.815  16.395  3.145   1.00 56.57  ? 51  LYS F CE  1 
ATOM   10749 N NZ  . LYS F 2 51  ? 9.846   16.321  4.269   1.00 58.76  ? 51  LYS F NZ  1 
ATOM   10750 N N   . VAL F 2 52  ? 12.121  13.665  -1.836  1.00 71.40  ? 52  VAL F N   1 
ATOM   10751 C CA  . VAL F 2 52  ? 11.711  12.333  -2.278  1.00 68.89  ? 52  VAL F CA  1 
ATOM   10752 C C   . VAL F 2 52  ? 12.843  11.602  -2.983  1.00 68.86  ? 52  VAL F C   1 
ATOM   10753 O O   . VAL F 2 52  ? 12.867  10.372  -3.027  1.00 75.85  ? 52  VAL F O   1 
ATOM   10754 C CB  . VAL F 2 52  ? 10.481  12.373  -3.211  1.00 75.10  ? 52  VAL F CB  1 
ATOM   10755 C CG1 . VAL F 2 52  ? 9.763   13.704  -3.087  1.00 73.72  ? 52  VAL F CG1 1 
ATOM   10756 C CG2 . VAL F 2 52  ? 10.889  12.111  -4.658  1.00 79.08  ? 52  VAL F CG2 1 
ATOM   10757 N N   . ASN F 2 53  ? 13.781  12.354  -3.540  1.00 106.29 ? 53  ASN F N   1 
ATOM   10758 C CA  . ASN F 2 53  ? 14.926  11.732  -4.183  1.00 99.84  ? 53  ASN F CA  1 
ATOM   10759 C C   . ASN F 2 53  ? 15.941  11.213  -3.167  1.00 85.56  ? 53  ASN F C   1 
ATOM   10760 O O   . ASN F 2 53  ? 16.689  10.287  -3.457  1.00 75.89  ? 53  ASN F O   1 
ATOM   10761 C CB  . ASN F 2 53  ? 15.574  12.680  -5.195  1.00 103.57 ? 53  ASN F CB  1 
ATOM   10762 C CG  . ASN F 2 53  ? 14.733  12.853  -6.447  1.00 116.53 ? 53  ASN F CG  1 
ATOM   10763 O OD1 . ASN F 2 53  ? 13.551  12.509  -6.468  1.00 132.03 ? 53  ASN F OD1 1 
ATOM   10764 N ND2 . ASN F 2 53  ? 15.341  13.387  -7.499  1.00 111.50 ? 53  ASN F ND2 1 
ATOM   10765 N N   . SER F 2 54  ? 15.952  11.796  -1.971  1.00 96.95  ? 54  SER F N   1 
ATOM   10766 C CA  . SER F 2 54  ? 16.831  11.317  -0.907  1.00 93.49  ? 54  SER F CA  1 
ATOM   10767 C C   . SER F 2 54  ? 16.359  9.984   -0.325  1.00 89.77  ? 54  SER F C   1 
ATOM   10768 O O   . SER F 2 54  ? 17.161  9.070   -0.122  1.00 80.68  ? 54  SER F O   1 
ATOM   10769 C CB  . SER F 2 54  ? 16.969  12.359  0.204   1.00 100.44 ? 54  SER F CB  1 
ATOM   10770 O OG  . SER F 2 54  ? 17.857  13.391  -0.180  1.00 105.87 ? 54  SER F OG  1 
ATOM   10771 N N   . VAL F 2 55  ? 15.061  9.872   -0.057  1.00 64.70  ? 55  VAL F N   1 
ATOM   10772 C CA  . VAL F 2 55  ? 14.518  8.642   0.508   1.00 60.01  ? 55  VAL F CA  1 
ATOM   10773 C C   . VAL F 2 55  ? 14.516  7.511   -0.519  1.00 62.86  ? 55  VAL F C   1 
ATOM   10774 O O   . VAL F 2 55  ? 14.408  6.339   -0.160  1.00 65.17  ? 55  VAL F O   1 
ATOM   10775 C CB  . VAL F 2 55  ? 13.091  8.828   1.083   1.00 64.31  ? 55  VAL F CB  1 
ATOM   10776 C CG1 . VAL F 2 55  ? 12.939  10.215  1.660   1.00 55.92  ? 55  VAL F CG1 1 
ATOM   10777 C CG2 . VAL F 2 55  ? 12.040  8.563   0.019   1.00 72.04  ? 55  VAL F CG2 1 
ATOM   10778 N N   . ILE F 2 56  ? 14.637  7.859   -1.795  1.00 68.44  ? 56  ILE F N   1 
ATOM   10779 C CA  . ILE F 2 56  ? 14.694  6.848   -2.846  1.00 68.61  ? 56  ILE F CA  1 
ATOM   10780 C C   . ILE F 2 56  ? 16.135  6.470   -3.183  1.00 62.06  ? 56  ILE F C   1 
ATOM   10781 O O   . ILE F 2 56  ? 16.483  5.293   -3.184  1.00 58.50  ? 56  ILE F O   1 
ATOM   10782 C CB  . ILE F 2 56  ? 13.960  7.302   -4.123  1.00 78.18  ? 56  ILE F CB  1 
ATOM   10783 C CG1 . ILE F 2 56  ? 12.451  7.333   -3.889  1.00 87.38  ? 56  ILE F CG1 1 
ATOM   10784 C CG2 . ILE F 2 56  ? 14.274  6.377   -5.272  1.00 70.72  ? 56  ILE F CG2 1 
ATOM   10785 C CD1 . ILE F 2 56  ? 11.658  7.592   -5.143  1.00 88.02  ? 56  ILE F CD1 1 
ATOM   10786 N N   . GLU F 2 57  ? 16.973  7.470   -3.445  1.00 94.24  ? 57  GLU F N   1 
ATOM   10787 C CA  . GLU F 2 57  ? 18.344  7.235   -3.899  1.00 96.71  ? 57  GLU F CA  1 
ATOM   10788 C C   . GLU F 2 57  ? 19.258  6.569   -2.872  1.00 95.03  ? 57  GLU F C   1 
ATOM   10789 O O   . GLU F 2 57  ? 20.155  5.808   -3.240  1.00 95.79  ? 57  GLU F O   1 
ATOM   10790 C CB  . GLU F 2 57  ? 18.988  8.544   -4.363  1.00 103.30 ? 57  GLU F CB  1 
ATOM   10791 C CG  . GLU F 2 57  ? 18.357  9.155   -5.603  1.00 117.04 ? 57  GLU F CG  1 
ATOM   10792 C CD  . GLU F 2 57  ? 18.765  10.605  -5.813  1.00 120.17 ? 57  GLU F CD  1 
ATOM   10793 O OE1 . GLU F 2 57  ? 19.599  11.116  -5.032  1.00 118.88 ? 57  GLU F OE1 1 
ATOM   10794 O OE2 . GLU F 2 57  ? 18.244  11.233  -6.760  1.00 120.28 ? 57  GLU F OE2 1 
ATOM   10795 N N   . LYS F 2 58  ? 19.042  6.856   -1.592  1.00 90.04  ? 58  LYS F N   1 
ATOM   10796 C CA  . LYS F 2 58  ? 19.958  6.392   -0.548  1.00 84.85  ? 58  LYS F CA  1 
ATOM   10797 C C   . LYS F 2 58  ? 19.786  4.914   -0.185  1.00 90.49  ? 58  LYS F C   1 
ATOM   10798 O O   . LYS F 2 58  ? 20.565  4.372   0.600   1.00 93.68  ? 58  LYS F O   1 
ATOM   10799 C CB  . LYS F 2 58  ? 19.843  7.268   0.707   1.00 81.05  ? 58  LYS F CB  1 
ATOM   10800 C CG  . LYS F 2 58  ? 21.096  8.087   1.022   1.00 85.06  ? 58  LYS F CG  1 
ATOM   10801 C CD  . LYS F 2 58  ? 21.333  9.173   -0.019  1.00 88.55  ? 58  LYS F CD  1 
ATOM   10802 C CE  . LYS F 2 58  ? 22.613  9.943   0.260   1.00 88.07  ? 58  LYS F CE  1 
ATOM   10803 N NZ  . LYS F 2 58  ? 22.591  10.611  1.592   1.00 87.47  ? 58  LYS F NZ  1 
ATOM   10804 N N   . MET F 2 59  ? 18.777  4.268   -0.762  1.00 98.38  ? 59  MET F N   1 
ATOM   10805 C CA  . MET F 2 59  ? 18.522  2.853   -0.500  1.00 101.80 ? 59  MET F CA  1 
ATOM   10806 C C   . MET F 2 59  ? 19.474  1.933   -1.261  1.00 108.64 ? 59  MET F C   1 
ATOM   10807 O O   . MET F 2 59  ? 19.243  1.614   -2.430  1.00 109.52 ? 59  MET F O   1 
ATOM   10808 C CB  . MET F 2 59  ? 17.076  2.486   -0.842  1.00 109.25 ? 59  MET F CB  1 
ATOM   10809 C CG  . MET F 2 59  ? 16.206  2.171   0.369   1.00 115.35 ? 59  MET F CG  1 
ATOM   10810 S SD  . MET F 2 59  ? 16.908  0.906   1.447   1.00 98.15  ? 59  MET F SD  1 
ATOM   10811 C CE  . MET F 2 59  ? 17.402  -0.317  0.243   1.00 58.34  ? 59  MET F CE  1 
ATOM   10812 N N   . ASN F 2 60  ? 20.539  1.508   -0.588  1.00 124.54 ? 60  ASN F N   1 
ATOM   10813 C CA  . ASN F 2 60  ? 21.486  0.559   -1.163  1.00 129.38 ? 60  ASN F CA  1 
ATOM   10814 C C   . ASN F 2 60  ? 20.873  -0.835  -1.210  1.00 124.99 ? 60  ASN F C   1 
ATOM   10815 O O   . ASN F 2 60  ? 20.526  -1.408  -0.179  1.00 128.75 ? 60  ASN F O   1 
ATOM   10816 C CB  . ASN F 2 60  ? 22.789  0.548   -0.361  1.00 133.13 ? 60  ASN F CB  1 
ATOM   10817 C CG  . ASN F 2 60  ? 23.854  -0.326  -0.989  1.00 139.12 ? 60  ASN F CG  1 
ATOM   10818 O OD1 . ASN F 2 60  ? 23.746  -0.718  -2.152  1.00 143.80 ? 60  ASN F OD1 1 
ATOM   10819 N ND2 . ASN F 2 60  ? 24.895  -0.631  -0.223  1.00 140.16 ? 60  ASN F ND2 1 
ATOM   10820 N N   . THR F 2 61  ? 20.740  -1.379  -2.412  1.00 104.96 ? 61  THR F N   1 
ATOM   10821 C CA  . THR F 2 61  ? 19.983  -2.608  -2.595  1.00 100.25 ? 61  THR F CA  1 
ATOM   10822 C C   . THR F 2 61  ? 20.833  -3.881  -2.561  1.00 101.21 ? 61  THR F C   1 
ATOM   10823 O O   . THR F 2 61  ? 20.406  -4.896  -2.010  1.00 103.43 ? 61  THR F O   1 
ATOM   10824 C CB  . THR F 2 61  ? 19.149  -2.557  -3.890  1.00 100.43 ? 61  THR F CB  1 
ATOM   10825 O OG1 . THR F 2 61  ? 19.985  -2.152  -4.981  1.00 103.35 ? 61  THR F OG1 1 
ATOM   10826 C CG2 . THR F 2 61  ? 18.005  -1.567  -3.743  1.00 98.42  ? 61  THR F CG2 1 
ATOM   10827 N N   . GLN F 2 62  ? 22.027  -3.830  -3.148  1.00 114.39 ? 62  GLN F N   1 
ATOM   10828 C CA  . GLN F 2 62  ? 22.909  -4.996  -3.188  1.00 115.94 ? 62  GLN F CA  1 
ATOM   10829 C C   . GLN F 2 62  ? 22.358  -6.054  -4.147  1.00 108.93 ? 62  GLN F C   1 
ATOM   10830 O O   . GLN F 2 62  ? 21.882  -5.721  -5.231  1.00 114.46 ? 62  GLN F O   1 
ATOM   10831 C CB  . GLN F 2 62  ? 23.086  -5.583  -1.783  1.00 115.08 ? 62  GLN F CB  1 
ATOM   10832 C CG  . GLN F 2 62  ? 24.429  -6.251  -1.544  1.00 123.33 ? 62  GLN F CG  1 
ATOM   10833 C CD  . GLN F 2 62  ? 25.175  -5.648  -0.365  1.00 129.43 ? 62  GLN F CD  1 
ATOM   10834 O OE1 . GLN F 2 62  ? 24.591  -4.943  0.460   1.00 123.52 ? 62  GLN F OE1 1 
ATOM   10835 N NE2 . GLN F 2 62  ? 26.473  -5.919  -0.283  1.00 142.62 ? 62  GLN F NE2 1 
ATOM   10836 N N   . PHE F 2 63  ? 22.426  -7.323  -3.746  1.00 105.07 ? 63  PHE F N   1 
ATOM   10837 C CA  . PHE F 2 63  ? 21.872  -8.427  -4.532  1.00 102.22 ? 63  PHE F CA  1 
ATOM   10838 C C   . PHE F 2 63  ? 21.853  -9.716  -3.732  1.00 96.73  ? 63  PHE F C   1 
ATOM   10839 O O   . PHE F 2 63  ? 22.897  -10.171 -3.268  1.00 102.32 ? 63  PHE F O   1 
ATOM   10840 C CB  . PHE F 2 63  ? 22.689  -8.666  -5.799  1.00 106.58 ? 63  PHE F CB  1 
ATOM   10841 C CG  . PHE F 2 63  ? 22.508  -10.046 -6.380  1.00 106.34 ? 63  PHE F CG  1 
ATOM   10842 C CD1 . PHE F 2 63  ? 21.519  -10.297 -7.318  1.00 109.42 ? 63  PHE F CD1 1 
ATOM   10843 C CD2 . PHE F 2 63  ? 23.326  -11.093 -5.985  1.00 106.32 ? 63  PHE F CD2 1 
ATOM   10844 C CE1 . PHE F 2 63  ? 21.350  -11.566 -7.851  1.00 104.52 ? 63  PHE F CE1 1 
ATOM   10845 C CE2 . PHE F 2 63  ? 23.161  -12.360 -6.514  1.00 105.42 ? 63  PHE F CE2 1 
ATOM   10846 C CZ  . PHE F 2 63  ? 22.171  -12.596 -7.447  1.00 102.37 ? 63  PHE F CZ  1 
ATOM   10847 N N   . GLU F 2 64  ? 20.680  -10.322 -3.592  1.00 82.37  ? 64  GLU F N   1 
ATOM   10848 C CA  . GLU F 2 64  ? 20.557  -11.540 -2.798  1.00 78.75  ? 64  GLU F CA  1 
ATOM   10849 C C   . GLU F 2 64  ? 19.495  -12.474 -3.369  1.00 82.54  ? 64  GLU F C   1 
ATOM   10850 O O   . GLU F 2 64  ? 18.609  -12.045 -4.113  1.00 92.70  ? 64  GLU F O   1 
ATOM   10851 C CB  . GLU F 2 64  ? 20.193  -11.204 -1.342  1.00 80.94  ? 64  GLU F CB  1 
ATOM   10852 C CG  . GLU F 2 64  ? 21.052  -10.133 -0.669  1.00 85.15  ? 64  GLU F CG  1 
ATOM   10853 C CD  . GLU F 2 64  ? 22.411  -10.643 -0.214  1.00 93.02  ? 64  GLU F CD  1 
ATOM   10854 O OE1 . GLU F 2 64  ? 22.721  -11.832 -0.453  1.00 101.94 ? 64  GLU F OE1 1 
ATOM   10855 O OE2 . GLU F 2 64  ? 23.169  -9.850  0.389   1.00 88.76  ? 64  GLU F OE2 1 
ATOM   10856 N N   . ALA F 2 65  ? 19.592  -13.752 -3.007  1.00 55.32  ? 65  ALA F N   1 
ATOM   10857 C CA  . ALA F 2 65  ? 18.526  -14.721 -3.265  1.00 59.56  ? 65  ALA F CA  1 
ATOM   10858 C C   . ALA F 2 65  ? 18.091  -15.372 -1.951  1.00 65.00  ? 65  ALA F C   1 
ATOM   10859 O O   . ALA F 2 65  ? 18.928  -15.707 -1.115  1.00 67.98  ? 65  ALA F O   1 
ATOM   10860 C CB  . ALA F 2 65  ? 18.986  -15.767 -4.254  1.00 56.48  ? 65  ALA F CB  1 
ATOM   10861 N N   . VAL F 2 66  ? 16.783  -15.531 -1.764  1.00 51.12  ? 66  VAL F N   1 
ATOM   10862 C CA  . VAL F 2 66  ? 16.249  -16.186 -0.573  1.00 54.66  ? 66  VAL F CA  1 
ATOM   10863 C C   . VAL F 2 66  ? 15.750  -17.580 -0.946  1.00 66.94  ? 66  VAL F C   1 
ATOM   10864 O O   . VAL F 2 66  ? 15.632  -17.899 -2.129  1.00 80.35  ? 66  VAL F O   1 
ATOM   10865 C CB  . VAL F 2 66  ? 15.083  -15.383 0.035   1.00 68.73  ? 66  VAL F CB  1 
ATOM   10866 C CG1 . VAL F 2 66  ? 14.779  -15.873 1.442   1.00 78.87  ? 66  VAL F CG1 1 
ATOM   10867 C CG2 . VAL F 2 66  ? 15.408  -13.888 0.050   1.00 49.75  ? 66  VAL F CG2 1 
ATOM   10868 N N   . GLY F 2 67  ? 15.462  -18.418 0.046   1.00 89.14  ? 67  GLY F N   1 
ATOM   10869 C CA  . GLY F 2 67  ? 14.864  -19.710 -0.234  1.00 101.00 ? 67  GLY F CA  1 
ATOM   10870 C C   . GLY F 2 67  ? 15.129  -20.786 0.798   1.00 103.24 ? 67  GLY F C   1 
ATOM   10871 O O   . GLY F 2 67  ? 15.859  -20.567 1.764   1.00 87.09  ? 67  GLY F O   1 
ATOM   10872 N N   . LYS F 2 68  ? 14.531  -21.956 0.571   1.00 126.94 ? 68  LYS F N   1 
ATOM   10873 C CA  . LYS F 2 68  ? 14.677  -23.127 1.439   1.00 127.57 ? 68  LYS F CA  1 
ATOM   10874 C C   . LYS F 2 68  ? 16.128  -23.393 1.826   1.00 102.85 ? 68  LYS F C   1 
ATOM   10875 O O   . LYS F 2 68  ? 16.606  -22.887 2.837   1.00 100.56 ? 68  LYS F O   1 
ATOM   10876 C CB  . LYS F 2 68  ? 14.083  -24.362 0.755   1.00 145.85 ? 68  LYS F CB  1 
ATOM   10877 C CG  . LYS F 2 68  ? 14.217  -25.661 1.538   1.00 154.31 ? 68  LYS F CG  1 
ATOM   10878 C CD  . LYS F 2 68  ? 13.670  -26.829 0.734   1.00 163.54 ? 68  LYS F CD  1 
ATOM   10879 C CE  . LYS F 2 68  ? 13.707  -28.118 1.533   1.00 163.68 ? 68  LYS F CE  1 
ATOM   10880 N NZ  . LYS F 2 68  ? 13.044  -29.237 0.807   1.00 168.89 ? 68  LYS F NZ  1 
ATOM   10881 N N   . GLU F 2 69  ? 16.817  -24.200 1.025   1.00 104.17 ? 69  GLU F N   1 
ATOM   10882 C CA  . GLU F 2 69  ? 18.230  -24.496 1.251   1.00 92.22  ? 69  GLU F CA  1 
ATOM   10883 C C   . GLU F 2 69  ? 18.488  -25.538 2.339   1.00 82.52  ? 69  GLU F C   1 
ATOM   10884 O O   . GLU F 2 69  ? 19.600  -26.047 2.443   1.00 72.73  ? 69  GLU F O   1 
ATOM   10885 C CB  . GLU F 2 69  ? 19.016  -23.218 1.589   1.00 93.02  ? 69  GLU F CB  1 
ATOM   10886 C CG  . GLU F 2 69  ? 19.649  -22.502 0.402   1.00 110.18 ? 69  GLU F CG  1 
ATOM   10887 C CD  . GLU F 2 69  ? 20.656  -21.433 0.826   1.00 121.72 ? 69  GLU F CD  1 
ATOM   10888 O OE1 . GLU F 2 69  ? 20.808  -21.192 2.045   1.00 122.16 ? 69  GLU F OE1 1 
ATOM   10889 O OE2 . GLU F 2 69  ? 21.301  -20.833 -0.063  1.00 130.14 ? 69  GLU F OE2 1 
ATOM   10890 N N   . PHE F 2 70  ? 17.479  -25.848 3.151   1.00 68.21  ? 70  PHE F N   1 
ATOM   10891 C CA  . PHE F 2 70  ? 17.695  -26.698 4.329   1.00 54.64  ? 70  PHE F CA  1 
ATOM   10892 C C   . PHE F 2 70  ? 16.838  -27.960 4.399   1.00 59.37  ? 70  PHE F C   1 
ATOM   10893 O O   . PHE F 2 70  ? 15.639  -27.939 4.130   1.00 90.64  ? 70  PHE F O   1 
ATOM   10894 C CB  . PHE F 2 70  ? 17.542  -25.885 5.611   1.00 58.30  ? 70  PHE F CB  1 
ATOM   10895 C CG  . PHE F 2 70  ? 18.425  -24.676 5.655   1.00 52.05  ? 70  PHE F CG  1 
ATOM   10896 C CD1 . PHE F 2 70  ? 19.738  -24.771 6.094   1.00 47.39  ? 70  PHE F CD1 1 
ATOM   10897 C CD2 . PHE F 2 70  ? 17.952  -23.444 5.236   1.00 60.28  ? 70  PHE F CD2 1 
ATOM   10898 C CE1 . PHE F 2 70  ? 20.563  -23.656 6.118   1.00 45.00  ? 70  PHE F CE1 1 
ATOM   10899 C CE2 . PHE F 2 70  ? 18.770  -22.329 5.253   1.00 56.41  ? 70  PHE F CE2 1 
ATOM   10900 C CZ  . PHE F 2 70  ? 20.078  -22.437 5.694   1.00 50.43  ? 70  PHE F CZ  1 
ATOM   10901 N N   . SER F 2 71  ? 17.481  -29.057 4.780   1.00 42.68  ? 71  SER F N   1 
ATOM   10902 C CA  . SER F 2 71  ? 16.830  -30.359 4.879   1.00 63.58  ? 71  SER F CA  1 
ATOM   10903 C C   . SER F 2 71  ? 15.899  -30.457 6.078   1.00 87.07  ? 71  SER F C   1 
ATOM   10904 O O   . SER F 2 71  ? 15.462  -29.449 6.637   1.00 104.35 ? 71  SER F O   1 
ATOM   10905 C CB  . SER F 2 71  ? 17.881  -31.457 5.003   1.00 58.55  ? 71  SER F CB  1 
ATOM   10906 O OG  . SER F 2 71  ? 18.471  -31.429 6.289   1.00 54.93  ? 71  SER F OG  1 
ATOM   10907 N N   . ASN F 2 72  ? 15.612  -31.693 6.470   1.00 64.59  ? 72  ASN F N   1 
ATOM   10908 C CA  . ASN F 2 72  ? 14.725  -31.976 7.591   1.00 61.91  ? 72  ASN F CA  1 
ATOM   10909 C C   . ASN F 2 72  ? 15.499  -32.361 8.846   1.00 52.05  ? 72  ASN F C   1 
ATOM   10910 O O   . ASN F 2 72  ? 14.919  -32.589 9.907   1.00 56.94  ? 72  ASN F O   1 
ATOM   10911 C CB  . ASN F 2 72  ? 13.708  -33.061 7.224   1.00 67.37  ? 72  ASN F CB  1 
ATOM   10912 C CG  . ASN F 2 72  ? 14.216  -34.003 6.142   1.00 87.60  ? 72  ASN F CG  1 
ATOM   10913 O OD1 . ASN F 2 72  ? 14.657  -33.569 5.073   1.00 87.73  ? 72  ASN F OD1 1 
ATOM   10914 N ND2 . ASN F 2 72  ? 14.152  -35.304 6.413   1.00 95.35  ? 72  ASN F ND2 1 
ATOM   10915 N N   . LEU F 2 73  ? 16.816  -32.426 8.715   1.00 63.76  ? 73  LEU F N   1 
ATOM   10916 C CA  . LEU F 2 73  ? 17.681  -32.616 9.863   1.00 55.02  ? 73  LEU F CA  1 
ATOM   10917 C C   . LEU F 2 73  ? 18.443  -31.318 10.077  1.00 46.11  ? 73  LEU F C   1 
ATOM   10918 O O   . LEU F 2 73  ? 19.474  -31.291 10.747  1.00 37.86  ? 73  LEU F O   1 
ATOM   10919 C CB  . LEU F 2 73  ? 18.644  -33.778 9.620   1.00 53.06  ? 73  LEU F CB  1 
ATOM   10920 C CG  . LEU F 2 73  ? 18.860  -34.767 10.772  1.00 48.57  ? 73  LEU F CG  1 
ATOM   10921 C CD1 . LEU F 2 73  ? 17.659  -34.790 11.718  1.00 55.75  ? 73  LEU F CD1 1 
ATOM   10922 C CD2 . LEU F 2 73  ? 19.150  -36.159 10.218  1.00 39.08  ? 73  LEU F CD2 1 
ATOM   10923 N N   . GLU F 2 74  ? 17.919  -30.240 9.491   1.00 69.30  ? 74  GLU F N   1 
ATOM   10924 C CA  . GLU F 2 74  ? 18.521  -28.913 9.591   1.00 57.27  ? 74  GLU F CA  1 
ATOM   10925 C C   . GLU F 2 74  ? 17.499  -27.887 10.041  1.00 70.24  ? 74  GLU F C   1 
ATOM   10926 O O   . GLU F 2 74  ? 17.699  -26.685 9.873   1.00 69.75  ? 74  GLU F O   1 
ATOM   10927 C CB  . GLU F 2 74  ? 19.109  -28.495 8.246   1.00 54.02  ? 74  GLU F CB  1 
ATOM   10928 C CG  . GLU F 2 74  ? 20.417  -29.195 7.903   1.00 53.27  ? 74  GLU F CG  1 
ATOM   10929 C CD  . GLU F 2 74  ? 20.849  -28.975 6.466   1.00 48.05  ? 74  GLU F CD  1 
ATOM   10930 O OE1 . GLU F 2 74  ? 19.969  -28.823 5.592   1.00 64.16  ? 74  GLU F OE1 1 
ATOM   10931 O OE2 . GLU F 2 74  ? 22.071  -28.953 6.214   1.00 34.71  ? 74  GLU F OE2 1 
ATOM   10932 N N   . ARG F 2 75  ? 16.401  -28.379 10.609  1.00 60.20  ? 75  ARG F N   1 
ATOM   10933 C CA  . ARG F 2 75  ? 15.324  -27.531 11.117  1.00 69.96  ? 75  ARG F CA  1 
ATOM   10934 C C   . ARG F 2 75  ? 15.856  -26.271 11.795  1.00 57.61  ? 75  ARG F C   1 
ATOM   10935 O O   . ARG F 2 75  ? 15.329  -25.181 11.596  1.00 64.63  ? 75  ARG F O   1 
ATOM   10936 C CB  . ARG F 2 75  ? 14.438  -28.317 12.094  1.00 77.37  ? 75  ARG F CB  1 
ATOM   10937 C CG  . ARG F 2 75  ? 13.650  -29.442 11.456  1.00 95.90  ? 75  ARG F CG  1 
ATOM   10938 C CD  . ARG F 2 75  ? 12.892  -28.936 10.240  1.00 120.43 ? 75  ARG F CD  1 
ATOM   10939 N NE  . ARG F 2 75  ? 12.230  -30.014 9.515   1.00 139.52 ? 75  ARG F NE  1 
ATOM   10940 C CZ  . ARG F 2 75  ? 11.708  -29.881 8.300   1.00 153.55 ? 75  ARG F CZ  1 
ATOM   10941 N NH1 . ARG F 2 75  ? 11.778  -28.714 7.674   1.00 158.11 ? 75  ARG F NH1 1 
ATOM   10942 N NH2 . ARG F 2 75  ? 11.123  -30.915 7.710   1.00 155.13 ? 75  ARG F NH2 1 
ATOM   10943 N N   . ARG F 2 76  ? 16.901  -26.431 12.596  1.00 56.52  ? 76  ARG F N   1 
ATOM   10944 C CA  . ARG F 2 76  ? 17.482  -25.307 13.309  1.00 47.70  ? 76  ARG F CA  1 
ATOM   10945 C C   . ARG F 2 76  ? 17.966  -24.194 12.369  1.00 56.43  ? 76  ARG F C   1 
ATOM   10946 O O   . ARG F 2 76  ? 17.496  -23.063 12.469  1.00 67.35  ? 76  ARG F O   1 
ATOM   10947 C CB  . ARG F 2 76  ? 18.598  -25.770 14.246  1.00 42.59  ? 76  ARG F CB  1 
ATOM   10948 C CG  . ARG F 2 76  ? 18.095  -26.450 15.516  1.00 41.81  ? 76  ARG F CG  1 
ATOM   10949 C CD  . ARG F 2 76  ? 19.249  -26.937 16.386  1.00 34.39  ? 76  ARG F CD  1 
ATOM   10950 N NE  . ARG F 2 76  ? 20.073  -27.907 15.672  1.00 40.39  ? 76  ARG F NE  1 
ATOM   10951 C CZ  . ARG F 2 76  ? 21.383  -28.057 15.841  1.00 38.17  ? 76  ARG F CZ  1 
ATOM   10952 N NH1 . ARG F 2 76  ? 22.038  -27.304 16.710  1.00 36.71  ? 76  ARG F NH1 1 
ATOM   10953 N NH2 . ARG F 2 76  ? 22.040  -28.968 15.134  1.00 36.80  ? 76  ARG F NH2 1 
ATOM   10954 N N   . LEU F 2 77  ? 18.897  -24.498 11.464  1.00 51.36  ? 77  LEU F N   1 
ATOM   10955 C CA  . LEU F 2 77  ? 19.352  -23.488 10.507  1.00 41.43  ? 77  LEU F CA  1 
ATOM   10956 C C   . LEU F 2 77  ? 18.172  -22.839 9.820   1.00 45.75  ? 77  LEU F C   1 
ATOM   10957 O O   . LEU F 2 77  ? 18.052  -21.617 9.797   1.00 42.61  ? 77  LEU F O   1 
ATOM   10958 C CB  . LEU F 2 77  ? 20.264  -24.078 9.442   1.00 40.18  ? 77  LEU F CB  1 
ATOM   10959 C CG  . LEU F 2 77  ? 21.727  -24.253 9.831   1.00 50.11  ? 77  LEU F CG  1 
ATOM   10960 C CD1 . LEU F 2 77  ? 21.906  -25.519 10.666  1.00 62.15  ? 77  LEU F CD1 1 
ATOM   10961 C CD2 . LEU F 2 77  ? 22.591  -24.303 8.576   1.00 44.84  ? 77  LEU F CD2 1 
ATOM   10962 N N   . GLU F 2 78  ? 17.303  -23.670 9.255   1.00 39.06  ? 78  GLU F N   1 
ATOM   10963 C CA  . GLU F 2 78  ? 16.116  -23.182 8.573   1.00 54.18  ? 78  GLU F CA  1 
ATOM   10964 C C   . GLU F 2 78  ? 15.454  -22.119 9.445   1.00 58.65  ? 78  GLU F C   1 
ATOM   10965 O O   . GLU F 2 78  ? 14.920  -21.128 8.943   1.00 77.34  ? 78  GLU F O   1 
ATOM   10966 C CB  . GLU F 2 78  ? 15.149  -24.337 8.299   1.00 73.92  ? 78  GLU F CB  1 
ATOM   10967 C CG  . GLU F 2 78  ? 14.148  -24.073 7.184   1.00 93.47  ? 78  GLU F CG  1 
ATOM   10968 C CD  . GLU F 2 78  ? 13.174  -25.224 6.985   1.00 113.59 ? 78  GLU F CD  1 
ATOM   10969 O OE1 . GLU F 2 78  ? 13.076  -26.089 7.882   1.00 114.35 ? 78  GLU F OE1 1 
ATOM   10970 O OE2 . GLU F 2 78  ? 12.505  -25.263 5.931   1.00 127.54 ? 78  GLU F OE2 1 
ATOM   10971 N N   . ASN F 2 79  ? 15.517  -22.324 10.756  1.00 53.91  ? 79  ASN F N   1 
ATOM   10972 C CA  . ASN F 2 79  ? 14.878  -21.420 11.702  1.00 73.07  ? 79  ASN F CA  1 
ATOM   10973 C C   . ASN F 2 79  ? 15.676  -20.144 11.921  1.00 66.45  ? 79  ASN F C   1 
ATOM   10974 O O   . ASN F 2 79  ? 15.132  -19.045 11.839  1.00 79.81  ? 79  ASN F O   1 
ATOM   10975 C CB  . ASN F 2 79  ? 14.633  -22.119 13.039  1.00 70.45  ? 79  ASN F CB  1 
ATOM   10976 C CG  . ASN F 2 79  ? 13.870  -21.249 14.013  1.00 65.93  ? 79  ASN F CG  1 
ATOM   10977 O OD1 . ASN F 2 79  ? 12.681  -20.989 13.827  1.00 71.15  ? 79  ASN F OD1 1 
ATOM   10978 N ND2 . ASN F 2 79  ? 14.547  -20.797 15.063  1.00 57.91  ? 79  ASN F ND2 1 
ATOM   10979 N N   . LEU F 2 80  ? 16.959  -20.298 12.223  1.00 67.15  ? 80  LEU F N   1 
ATOM   10980 C CA  . LEU F 2 80  ? 17.862  -19.165 12.341  1.00 55.59  ? 80  LEU F CA  1 
ATOM   10981 C C   . LEU F 2 80  ? 17.611  -18.228 11.174  1.00 61.91  ? 80  LEU F C   1 
ATOM   10982 O O   . LEU F 2 80  ? 17.256  -17.066 11.354  1.00 71.54  ? 80  LEU F O   1 
ATOM   10983 C CB  . LEU F 2 80  ? 19.299  -19.658 12.298  1.00 49.21  ? 80  LEU F CB  1 
ATOM   10984 C CG  . LEU F 2 80  ? 20.400  -18.788 12.898  1.00 39.78  ? 80  LEU F CG  1 
ATOM   10985 C CD1 . LEU F 2 80  ? 21.712  -19.580 12.853  1.00 31.41  ? 80  LEU F CD1 1 
ATOM   10986 C CD2 . LEU F 2 80  ? 20.534  -17.460 12.171  1.00 37.13  ? 80  LEU F CD2 1 
ATOM   10987 N N   . ASN F 2 81  ? 17.790  -18.757 9.971   1.00 57.15  ? 81  ASN F N   1 
ATOM   10988 C CA  . ASN F 2 81  ? 17.416  -18.057 8.753   1.00 58.26  ? 81  ASN F CA  1 
ATOM   10989 C C   . ASN F 2 81  ? 16.159  -17.222 8.975   1.00 67.39  ? 81  ASN F C   1 
ATOM   10990 O O   . ASN F 2 81  ? 16.187  -16.003 8.867   1.00 70.19  ? 81  ASN F O   1 
ATOM   10991 C CB  . ASN F 2 81  ? 17.170  -19.072 7.639   1.00 66.01  ? 81  ASN F CB  1 
ATOM   10992 C CG  . ASN F 2 81  ? 17.359  -18.483 6.267   1.00 74.41  ? 81  ASN F CG  1 
ATOM   10993 O OD1 . ASN F 2 81  ? 18.351  -17.807 6.004   1.00 73.58  ? 81  ASN F OD1 1 
ATOM   10994 N ND2 . ASN F 2 81  ? 16.403  -18.725 5.382   1.00 86.98  ? 81  ASN F ND2 1 
ATOM   10995 N N   . LYS F 2 82  ? 15.061  -17.895 9.304   1.00 53.48  ? 82  LYS F N   1 
ATOM   10996 C CA  . LYS F 2 82  ? 13.775  -17.251 9.546   1.00 65.76  ? 82  LYS F CA  1 
ATOM   10997 C C   . LYS F 2 82  ? 13.873  -16.157 10.603  1.00 57.35  ? 82  LYS F C   1 
ATOM   10998 O O   . LYS F 2 82  ? 13.374  -15.052 10.402  1.00 64.56  ? 82  LYS F O   1 
ATOM   10999 C CB  . LYS F 2 82  ? 12.741  -18.299 9.960   1.00 79.24  ? 82  LYS F CB  1 
ATOM   11000 C CG  . LYS F 2 82  ? 11.323  -17.781 10.126  1.00 89.97  ? 82  LYS F CG  1 
ATOM   11001 C CD  . LYS F 2 82  ? 10.383  -18.925 10.497  1.00 92.85  ? 82  LYS F CD  1 
ATOM   11002 C CE  . LYS F 2 82  ? 8.954   -18.451 10.667  1.00 93.43  ? 82  LYS F CE  1 
ATOM   11003 N NZ  . LYS F 2 82  ? 8.870   -17.378 11.689  1.00 87.39  ? 82  LYS F NZ  1 
ATOM   11004 N N   . LYS F 2 83  ? 14.516  -16.461 11.726  1.00 67.15  ? 83  LYS F N   1 
ATOM   11005 C CA  . LYS F 2 83  ? 14.708  -15.470 12.781  1.00 65.75  ? 83  LYS F CA  1 
ATOM   11006 C C   . LYS F 2 83  ? 15.403  -14.220 12.244  1.00 63.37  ? 83  LYS F C   1 
ATOM   11007 O O   . LYS F 2 83  ? 15.327  -13.143 12.839  1.00 70.60  ? 83  LYS F O   1 
ATOM   11008 C CB  . LYS F 2 83  ? 15.525  -16.050 13.936  1.00 64.81  ? 83  LYS F CB  1 
ATOM   11009 C CG  . LYS F 2 83  ? 14.700  -16.649 15.057  1.00 74.23  ? 83  LYS F CG  1 
ATOM   11010 C CD  . LYS F 2 83  ? 15.452  -16.566 16.382  1.00 77.28  ? 83  LYS F CD  1 
ATOM   11011 C CE  . LYS F 2 83  ? 16.675  -17.475 16.412  1.00 77.06  ? 83  LYS F CE  1 
ATOM   11012 N NZ  . LYS F 2 83  ? 16.487  -18.622 17.358  1.00 75.87  ? 83  LYS F NZ  1 
ATOM   11013 N N   . MET F 2 84  ? 16.077  -14.375 11.111  1.00 62.40  ? 84  MET F N   1 
ATOM   11014 C CA  . MET F 2 84  ? 16.821  -13.288 10.493  1.00 50.36  ? 84  MET F CA  1 
ATOM   11015 C C   . MET F 2 84  ? 15.967  -12.543 9.475   1.00 63.62  ? 84  MET F C   1 
ATOM   11016 O O   . MET F 2 84  ? 15.655  -11.370 9.659   1.00 72.09  ? 84  MET F O   1 
ATOM   11017 C CB  . MET F 2 84  ? 18.078  -13.834 9.819   1.00 40.95  ? 84  MET F CB  1 
ATOM   11018 C CG  . MET F 2 84  ? 18.922  -12.788 9.136   1.00 37.06  ? 84  MET F CG  1 
ATOM   11019 S SD  . MET F 2 84  ? 20.368  -13.508 8.338   1.00 71.06  ? 84  MET F SD  1 
ATOM   11020 C CE  . MET F 2 84  ? 19.648  -14.047 6.788   1.00 23.36  ? 84  MET F CE  1 
ATOM   11021 N N   . GLU F 2 85  ? 15.602  -13.227 8.395   1.00 45.63  ? 85  GLU F N   1 
ATOM   11022 C CA  . GLU F 2 85  ? 14.761  -12.633 7.363   1.00 58.38  ? 85  GLU F CA  1 
ATOM   11023 C C   . GLU F 2 85  ? 13.634  -11.862 8.023   1.00 64.72  ? 85  GLU F C   1 
ATOM   11024 O O   . GLU F 2 85  ? 13.302  -10.755 7.607   1.00 74.24  ? 85  GLU F O   1 
ATOM   11025 C CB  . GLU F 2 85  ? 14.187  -13.707 6.433   1.00 80.57  ? 85  GLU F CB  1 
ATOM   11026 C CG  . GLU F 2 85  ? 15.231  -14.517 5.676   1.00 89.66  ? 85  GLU F CG  1 
ATOM   11027 C CD  . GLU F 2 85  ? 16.091  -13.658 4.769   1.00 96.83  ? 85  GLU F CD  1 
ATOM   11028 O OE1 . GLU F 2 85  ? 17.236  -14.061 4.468   1.00 93.87  ? 85  GLU F OE1 1 
ATOM   11029 O OE2 . GLU F 2 85  ? 15.621  -12.577 4.356   1.00 103.13 ? 85  GLU F OE2 1 
ATOM   11030 N N   . ASP F 2 86  ? 13.059  -12.458 9.062   1.00 39.93  ? 86  ASP F N   1 
ATOM   11031 C CA  . ASP F 2 86  ? 12.008  -11.820 9.843   1.00 50.47  ? 86  ASP F CA  1 
ATOM   11032 C C   . ASP F 2 86  ? 12.565  -10.630 10.617  1.00 61.18  ? 86  ASP F C   1 
ATOM   11033 O O   . ASP F 2 86  ? 11.993  -9.539  10.597  1.00 67.09  ? 86  ASP F O   1 
ATOM   11034 C CB  . ASP F 2 86  ? 11.385  -12.815 10.827  1.00 51.82  ? 86  ASP F CB  1 
ATOM   11035 C CG  . ASP F 2 86  ? 10.506  -13.838 10.148  1.00 64.57  ? 86  ASP F CG  1 
ATOM   11036 O OD1 . ASP F 2 86  ? 10.147  -13.646 8.967   1.00 71.72  ? 86  ASP F OD1 1 
ATOM   11037 O OD2 . ASP F 2 86  ? 10.161  -14.833 10.806  1.00 68.31  ? 86  ASP F OD2 1 
ATOM   11038 N N   . GLY F 2 87  ? 13.679  -10.854 11.310  1.00 78.00  ? 87  GLY F N   1 
ATOM   11039 C CA  . GLY F 2 87  ? 14.327  -9.807  12.079  1.00 68.59  ? 87  GLY F CA  1 
ATOM   11040 C C   . GLY F 2 87  ? 14.484  -8.521  11.292  1.00 66.54  ? 87  GLY F C   1 
ATOM   11041 O O   . GLY F 2 87  ? 14.177  -7.439  11.789  1.00 76.95  ? 87  GLY F O   1 
ATOM   11042 N N   . PHE F 2 88  ? 14.960  -8.642  10.058  1.00 60.73  ? 88  PHE F N   1 
ATOM   11043 C CA  . PHE F 2 88  ? 15.165  -7.488  9.199   1.00 63.98  ? 88  PHE F CA  1 
ATOM   11044 C C   . PHE F 2 88  ? 13.852  -6.924  8.689   1.00 90.28  ? 88  PHE F C   1 
ATOM   11045 O O   . PHE F 2 88  ? 13.722  -5.719  8.492   1.00 100.66 ? 88  PHE F O   1 
ATOM   11046 C CB  . PHE F 2 88  ? 16.062  -7.856  8.024   1.00 57.55  ? 88  PHE F CB  1 
ATOM   11047 C CG  . PHE F 2 88  ? 17.513  -7.897  8.369   1.00 46.82  ? 88  PHE F CG  1 
ATOM   11048 C CD1 . PHE F 2 88  ? 18.102  -6.846  9.048   1.00 44.36  ? 88  PHE F CD1 1 
ATOM   11049 C CD2 . PHE F 2 88  ? 18.290  -8.986  8.026   1.00 40.34  ? 88  PHE F CD2 1 
ATOM   11050 C CE1 . PHE F 2 88  ? 19.446  -6.873  9.373   1.00 37.19  ? 88  PHE F CE1 1 
ATOM   11051 C CE2 . PHE F 2 88  ? 19.636  -9.025  8.348   1.00 30.08  ? 88  PHE F CE2 1 
ATOM   11052 C CZ  . PHE F 2 88  ? 20.215  -7.966  9.026   1.00 32.75  ? 88  PHE F CZ  1 
ATOM   11053 N N   . LEU F 2 89  ? 12.879  -7.797  8.469   1.00 53.79  ? 89  LEU F N   1 
ATOM   11054 C CA  . LEU F 2 89  ? 11.564  -7.358  8.020   1.00 54.45  ? 89  LEU F CA  1 
ATOM   11055 C C   . LEU F 2 89  ? 10.986  -6.401  9.037   1.00 54.67  ? 89  LEU F C   1 
ATOM   11056 O O   . LEU F 2 89  ? 10.537  -5.309  8.696   1.00 64.88  ? 89  LEU F O   1 
ATOM   11057 C CB  . LEU F 2 89  ? 10.617  -8.541  7.862   1.00 57.76  ? 89  LEU F CB  1 
ATOM   11058 C CG  . LEU F 2 89  ? 9.248   -8.164  7.304   1.00 60.89  ? 89  LEU F CG  1 
ATOM   11059 C CD1 . LEU F 2 89  ? 9.359   -7.907  5.817   1.00 71.44  ? 89  LEU F CD1 1 
ATOM   11060 C CD2 . LEU F 2 89  ? 8.226   -9.251  7.574   1.00 58.31  ? 89  LEU F CD2 1 
ATOM   11061 N N   . ASP F 2 90  ? 11.005  -6.826  10.293  1.00 66.04  ? 90  ASP F N   1 
ATOM   11062 C CA  . ASP F 2 90  ? 10.532  -5.997  11.384  1.00 70.17  ? 90  ASP F CA  1 
ATOM   11063 C C   . ASP F 2 90  ? 11.208  -4.626  11.413  1.00 73.88  ? 90  ASP F C   1 
ATOM   11064 O O   . ASP F 2 90  ? 10.553  -3.614  11.676  1.00 78.19  ? 90  ASP F O   1 
ATOM   11065 C CB  . ASP F 2 90  ? 10.733  -6.716  12.709  1.00 66.74  ? 90  ASP F CB  1 
ATOM   11066 C CG  . ASP F 2 90  ? 9.729   -7.815  12.920  1.00 72.88  ? 90  ASP F CG  1 
ATOM   11067 O OD1 . ASP F 2 90  ? 9.108   -8.258  11.929  1.00 81.96  ? 90  ASP F OD1 1 
ATOM   11068 O OD2 . ASP F 2 90  ? 9.563   -8.239  14.077  1.00 66.34  ? 90  ASP F OD2 1 
ATOM   11069 N N   . VAL F 2 91  ? 12.511  -4.591  11.144  1.00 62.53  ? 91  VAL F N   1 
ATOM   11070 C CA  . VAL F 2 91  ? 13.239  -3.329  11.133  1.00 50.43  ? 91  VAL F CA  1 
ATOM   11071 C C   . VAL F 2 91  ? 12.806  -2.471  9.952   1.00 54.68  ? 91  VAL F C   1 
ATOM   11072 O O   . VAL F 2 91  ? 12.237  -1.403  10.136  1.00 62.37  ? 91  VAL F O   1 
ATOM   11073 C CB  . VAL F 2 91  ? 14.768  -3.532  11.111  1.00 33.19  ? 91  VAL F CB  1 
ATOM   11074 C CG1 . VAL F 2 91  ? 15.462  -2.245  10.733  1.00 18.61  ? 91  VAL F CG1 1 
ATOM   11075 C CG2 . VAL F 2 91  ? 15.261  -4.007  12.467  1.00 29.66  ? 91  VAL F CG2 1 
ATOM   11076 N N   . TRP F 2 92  ? 13.057  -2.953  8.741   1.00 66.33  ? 92  TRP F N   1 
ATOM   11077 C CA  . TRP F 2 92  ? 12.730  -2.200  7.535   1.00 68.62  ? 92  TRP F CA  1 
ATOM   11078 C C   . TRP F 2 92  ? 11.287  -1.726  7.493   1.00 73.11  ? 92  TRP F C   1 
ATOM   11079 O O   . TRP F 2 92  ? 10.983  -0.694  6.909   1.00 77.73  ? 92  TRP F O   1 
ATOM   11080 C CB  . TRP F 2 92  ? 13.025  -3.027  6.292   1.00 71.75  ? 92  TRP F CB  1 
ATOM   11081 C CG  . TRP F 2 92  ? 14.464  -3.064  5.941   1.00 61.93  ? 92  TRP F CG  1 
ATOM   11082 C CD1 . TRP F 2 92  ? 15.228  -4.172  5.731   1.00 52.38  ? 92  TRP F CD1 1 
ATOM   11083 C CD2 . TRP F 2 92  ? 15.327  -1.937  5.762   1.00 52.05  ? 92  TRP F CD2 1 
ATOM   11084 N NE1 . TRP F 2 92  ? 16.519  -3.806  5.425   1.00 41.45  ? 92  TRP F NE1 1 
ATOM   11085 C CE2 . TRP F 2 92  ? 16.607  -2.440  5.440   1.00 35.54  ? 92  TRP F CE2 1 
ATOM   11086 C CE3 . TRP F 2 92  ? 15.142  -0.548  5.844   1.00 55.31  ? 92  TRP F CE3 1 
ATOM   11087 C CZ2 . TRP F 2 92  ? 17.700  -1.611  5.196   1.00 26.94  ? 92  TRP F CZ2 1 
ATOM   11088 C CZ3 . TRP F 2 92  ? 16.222  0.280   5.606   1.00 42.69  ? 92  TRP F CZ3 1 
ATOM   11089 C CH2 . TRP F 2 92  ? 17.495  -0.258  5.283   1.00 33.75  ? 92  TRP F CH2 1 
ATOM   11090 N N   . THR F 2 93  ? 10.395  -2.495  8.098   1.00 45.29  ? 93  THR F N   1 
ATOM   11091 C CA  . THR F 2 93  ? 8.988   -2.131  8.139   1.00 57.94  ? 93  THR F CA  1 
ATOM   11092 C C   . THR F 2 93  ? 8.817   -0.929  9.046   1.00 69.33  ? 93  THR F C   1 
ATOM   11093 O O   . THR F 2 93  ? 8.293   0.101   8.637   1.00 89.51  ? 93  THR F O   1 
ATOM   11094 C CB  . THR F 2 93  ? 8.107   -3.300  8.646   1.00 62.60  ? 93  THR F CB  1 
ATOM   11095 O OG1 . THR F 2 93  ? 8.088   -4.349  7.668   1.00 74.88  ? 93  THR F OG1 1 
ATOM   11096 C CG2 . THR F 2 93  ? 6.684   -2.830  8.898   1.00 65.18  ? 93  THR F CG2 1 
ATOM   11097 N N   . TYR F 2 94  ? 9.286   -1.062  10.279  1.00 70.45  ? 94  TYR F N   1 
ATOM   11098 C CA  . TYR F 2 94  ? 9.145   -0.009  11.271  1.00 68.56  ? 94  TYR F CA  1 
ATOM   11099 C C   . TYR F 2 94  ? 9.759   1.292   10.781  1.00 68.11  ? 94  TYR F C   1 
ATOM   11100 O O   . TYR F 2 94  ? 9.090   2.321   10.730  1.00 78.53  ? 94  TYR F O   1 
ATOM   11101 C CB  . TYR F 2 94  ? 9.813   -0.429  12.572  1.00 61.80  ? 94  TYR F CB  1 
ATOM   11102 C CG  . TYR F 2 94  ? 9.361   0.365   13.764  1.00 63.16  ? 94  TYR F CG  1 
ATOM   11103 C CD1 . TYR F 2 94  ? 8.204   0.014   14.446  1.00 67.70  ? 94  TYR F CD1 1 
ATOM   11104 C CD2 . TYR F 2 94  ? 10.085  1.461   14.212  1.00 58.78  ? 94  TYR F CD2 1 
ATOM   11105 C CE1 . TYR F 2 94  ? 7.777   0.732   15.540  1.00 68.36  ? 94  TYR F CE1 1 
ATOM   11106 C CE2 . TYR F 2 94  ? 9.666   2.190   15.308  1.00 58.47  ? 94  TYR F CE2 1 
ATOM   11107 C CZ  . TYR F 2 94  ? 8.507   1.820   15.970  1.00 63.49  ? 94  TYR F CZ  1 
ATOM   11108 O OH  . TYR F 2 94  ? 8.069   2.528   17.068  1.00 53.53  ? 94  TYR F OH  1 
ATOM   11109 N N   . ASN F 2 95  ? 11.038  1.240   10.432  1.00 69.04  ? 95  ASN F N   1 
ATOM   11110 C CA  . ASN F 2 95  ? 11.749  2.402   9.919   1.00 69.58  ? 95  ASN F CA  1 
ATOM   11111 C C   . ASN F 2 95  ? 10.983  3.140   8.824   1.00 65.16  ? 95  ASN F C   1 
ATOM   11112 O O   . ASN F 2 95  ? 10.771  4.345   8.913   1.00 67.08  ? 95  ASN F O   1 
ATOM   11113 C CB  . ASN F 2 95  ? 13.129  1.997   9.404   1.00 78.24  ? 95  ASN F CB  1 
ATOM   11114 C CG  . ASN F 2 95  ? 14.078  1.603   10.520  1.00 79.82  ? 95  ASN F CG  1 
ATOM   11115 O OD1 . ASN F 2 95  ? 13.714  1.623   11.701  1.00 75.12  ? 95  ASN F OD1 1 
ATOM   11116 N ND2 . ASN F 2 95  ? 15.306  1.231   10.150  1.00 72.06  ? 95  ASN F ND2 1 
ATOM   11117 N N   . ALA F 2 96  ? 10.568  2.420   7.789   1.00 39.34  ? 96  ALA F N   1 
ATOM   11118 C CA  . ALA F 2 96  ? 9.834   3.045   6.693   1.00 46.68  ? 96  ALA F CA  1 
ATOM   11119 C C   . ALA F 2 96  ? 8.479   3.580   7.149   1.00 54.83  ? 96  ALA F C   1 
ATOM   11120 O O   . ALA F 2 96  ? 8.079   4.669   6.756   1.00 58.97  ? 96  ALA F O   1 
ATOM   11121 C CB  . ALA F 2 96  ? 9.669   2.073   5.524   1.00 43.22  ? 96  ALA F CB  1 
ATOM   11122 N N   . GLU F 2 97  ? 7.772   2.816   7.976   1.00 65.71  ? 97  GLU F N   1 
ATOM   11123 C CA  . GLU F 2 97  ? 6.475   3.253   8.479   1.00 66.78  ? 97  GLU F CA  1 
ATOM   11124 C C   . GLU F 2 97  ? 6.600   4.621   9.137   1.00 67.23  ? 97  GLU F C   1 
ATOM   11125 O O   . GLU F 2 97  ? 5.811   5.527   8.859   1.00 72.68  ? 97  GLU F O   1 
ATOM   11126 C CB  . GLU F 2 97  ? 5.894   2.244   9.471   1.00 66.97  ? 97  GLU F CB  1 
ATOM   11127 C CG  . GLU F 2 97  ? 5.345   0.975   8.838   1.00 75.61  ? 97  GLU F CG  1 
ATOM   11128 C CD  . GLU F 2 97  ? 4.158   1.229   7.928   1.00 81.21  ? 97  GLU F CD  1 
ATOM   11129 O OE1 . GLU F 2 97  ? 3.639   2.365   7.925   1.00 83.83  ? 97  GLU F OE1 1 
ATOM   11130 O OE2 . GLU F 2 97  ? 3.744   0.289   7.213   1.00 82.71  ? 97  GLU F OE2 1 
ATOM   11131 N N   . LEU F 2 98  ? 7.595   4.776   10.004  1.00 61.27  ? 98  LEU F N   1 
ATOM   11132 C CA  . LEU F 2 98  ? 7.800   6.053   10.675  1.00 59.01  ? 98  LEU F CA  1 
ATOM   11133 C C   . LEU F 2 98  ? 8.407   7.074   9.731   1.00 60.47  ? 98  LEU F C   1 
ATOM   11134 O O   . LEU F 2 98  ? 7.853   8.149   9.545   1.00 67.13  ? 98  LEU F O   1 
ATOM   11135 C CB  . LEU F 2 98  ? 8.647   5.897   11.936  1.00 52.07  ? 98  LEU F CB  1 
ATOM   11136 C CG  . LEU F 2 98  ? 7.790   5.668   13.183  1.00 53.42  ? 98  LEU F CG  1 
ATOM   11137 C CD1 . LEU F 2 98  ? 6.838   4.509   12.968  1.00 40.93  ? 98  LEU F CD1 1 
ATOM   11138 C CD2 . LEU F 2 98  ? 8.648   5.439   14.417  1.00 60.23  ? 98  LEU F CD2 1 
ATOM   11139 N N   . LEU F 2 99  ? 9.540   6.730   9.132   1.00 68.23  ? 99  LEU F N   1 
ATOM   11140 C CA  . LEU F 2 99  ? 10.195  7.601   8.162   1.00 57.86  ? 99  LEU F CA  1 
ATOM   11141 C C   . LEU F 2 99  ? 9.174   8.394   7.368   1.00 65.99  ? 99  LEU F C   1 
ATOM   11142 O O   . LEU F 2 99  ? 9.362   9.580   7.113   1.00 74.19  ? 99  LEU F O   1 
ATOM   11143 C CB  . LEU F 2 99  ? 11.061  6.780   7.208   1.00 56.68  ? 99  LEU F CB  1 
ATOM   11144 C CG  . LEU F 2 99  ? 11.667  7.569   6.056   1.00 49.44  ? 99  LEU F CG  1 
ATOM   11145 C CD1 . LEU F 2 99  ? 12.424  8.756   6.613   1.00 39.55  ? 99  LEU F CD1 1 
ATOM   11146 C CD2 . LEU F 2 99  ? 12.574  6.686   5.218   1.00 41.61  ? 99  LEU F CD2 1 
ATOM   11147 N N   . VAL F 2 100 ? 8.088   7.736   6.979   1.00 59.11  ? 100 VAL F N   1 
ATOM   11148 C CA  . VAL F 2 100 ? 7.006   8.424   6.293   1.00 62.97  ? 100 VAL F CA  1 
ATOM   11149 C C   . VAL F 2 100 ? 6.323   9.405   7.246   1.00 64.39  ? 100 VAL F C   1 
ATOM   11150 O O   . VAL F 2 100 ? 6.420   10.616  7.060   1.00 70.59  ? 100 VAL F O   1 
ATOM   11151 C CB  . VAL F 2 100 ? 5.985   7.437   5.699   1.00 68.96  ? 100 VAL F CB  1 
ATOM   11152 C CG1 . VAL F 2 100 ? 4.700   8.157   5.319   1.00 79.24  ? 100 VAL F CG1 1 
ATOM   11153 C CG2 . VAL F 2 100 ? 6.579   6.738   4.493   1.00 64.44  ? 100 VAL F CG2 1 
ATOM   11154 N N   . LEU F 2 101 ? 5.655   8.877   8.270   1.00 53.89  ? 101 LEU F N   1 
ATOM   11155 C CA  . LEU F 2 101 ? 5.017   9.705   9.295   1.00 60.37  ? 101 LEU F CA  1 
ATOM   11156 C C   . LEU F 2 101 ? 5.794   10.986  9.643   1.00 64.65  ? 101 LEU F C   1 
ATOM   11157 O O   . LEU F 2 101 ? 5.200   12.058  9.791   1.00 62.70  ? 101 LEU F O   1 
ATOM   11158 C CB  . LEU F 2 101 ? 4.759   8.887   10.563  1.00 55.61  ? 101 LEU F CB  1 
ATOM   11159 C CG  . LEU F 2 101 ? 3.710   7.794   10.390  1.00 57.06  ? 101 LEU F CG  1 
ATOM   11160 C CD1 . LEU F 2 101 ? 3.047   7.466   11.722  1.00 54.53  ? 101 LEU F CD1 1 
ATOM   11161 C CD2 . LEU F 2 101 ? 2.673   8.228   9.371   1.00 61.77  ? 101 LEU F CD2 1 
ATOM   11162 N N   . MET F 2 102 ? 7.113   10.863  9.786   1.00 89.12  ? 102 MET F N   1 
ATOM   11163 C CA  . MET F 2 102 ? 7.972   12.017  10.033  1.00 88.57  ? 102 MET F CA  1 
ATOM   11164 C C   . MET F 2 102 ? 8.035   12.900  8.799   1.00 87.92  ? 102 MET F C   1 
ATOM   11165 O O   . MET F 2 102 ? 7.527   14.020  8.796   1.00 97.03  ? 102 MET F O   1 
ATOM   11166 C CB  . MET F 2 102 ? 9.392   11.580  10.393  1.00 85.15  ? 102 MET F CB  1 
ATOM   11167 C CG  . MET F 2 102 ? 9.567   11.039  11.798  1.00 85.28  ? 102 MET F CG  1 
ATOM   11168 S SD  . MET F 2 102 ? 11.314  10.764  12.171  1.00 129.54 ? 102 MET F SD  1 
ATOM   11169 C CE  . MET F 2 102 ? 11.202  9.914   13.742  1.00 163.72 ? 102 MET F CE  1 
ATOM   11170 N N   . GLU F 2 103 ? 8.671   12.384  7.752   1.00 52.19  ? 103 GLU F N   1 
ATOM   11171 C CA  . GLU F 2 103 ? 8.833   13.128  6.512   1.00 53.05  ? 103 GLU F CA  1 
ATOM   11172 C C   . GLU F 2 103 ? 7.536   13.793  6.059   1.00 66.86  ? 103 GLU F C   1 
ATOM   11173 O O   . GLU F 2 103 ? 7.550   14.922  5.580   1.00 73.82  ? 103 GLU F O   1 
ATOM   11174 C CB  . GLU F 2 103 ? 9.382   12.225  5.411   1.00 56.84  ? 103 GLU F CB  1 
ATOM   11175 C CG  . GLU F 2 103 ? 10.833  11.860  5.609   1.00 60.10  ? 103 GLU F CG  1 
ATOM   11176 C CD  . GLU F 2 103 ? 11.672  13.057  6.018   1.00 77.38  ? 103 GLU F CD  1 
ATOM   11177 O OE1 . GLU F 2 103 ? 12.063  13.844  5.127   1.00 84.99  ? 103 GLU F OE1 1 
ATOM   11178 O OE2 . GLU F 2 103 ? 11.936  13.215  7.233   1.00 81.32  ? 103 GLU F OE2 1 
ATOM   11179 N N   . ASN F 2 104 ? 6.418   13.092  6.204   1.00 76.15  ? 104 ASN F N   1 
ATOM   11180 C CA  . ASN F 2 104 ? 5.115   13.664  5.881   1.00 77.70  ? 104 ASN F CA  1 
ATOM   11181 C C   . ASN F 2 104 ? 4.828   14.917  6.700   1.00 73.91  ? 104 ASN F C   1 
ATOM   11182 O O   . ASN F 2 104 ? 4.388   15.930  6.164   1.00 76.20  ? 104 ASN F O   1 
ATOM   11183 C CB  . ASN F 2 104 ? 4.004   12.633  6.099   1.00 83.27  ? 104 ASN F CB  1 
ATOM   11184 C CG  . ASN F 2 104 ? 3.814   11.719  4.906   1.00 94.39  ? 104 ASN F CG  1 
ATOM   11185 O OD1 . ASN F 2 104 ? 4.540   11.815  3.918   1.00 96.19  ? 104 ASN F OD1 1 
ATOM   11186 N ND2 . ASN F 2 104 ? 2.835   10.823  4.993   1.00 98.21  ? 104 ASN F ND2 1 
ATOM   11187 N N   . GLU F 2 105 ? 5.083   14.839  8.002   1.00 63.17  ? 105 GLU F N   1 
ATOM   11188 C CA  . GLU F 2 105 ? 4.872   15.963  8.909   1.00 55.05  ? 105 GLU F CA  1 
ATOM   11189 C C   . GLU F 2 105 ? 5.774   17.143  8.534   1.00 57.57  ? 105 GLU F C   1 
ATOM   11190 O O   . GLU F 2 105 ? 5.298   18.236  8.251   1.00 65.71  ? 105 GLU F O   1 
ATOM   11191 C CB  . GLU F 2 105 ? 5.153   15.525  10.346  1.00 53.73  ? 105 GLU F CB  1 
ATOM   11192 C CG  . GLU F 2 105 ? 4.859   16.569  11.400  1.00 70.19  ? 105 GLU F CG  1 
ATOM   11193 C CD  . GLU F 2 105 ? 3.504   16.376  12.052  1.00 93.40  ? 105 GLU F CD  1 
ATOM   11194 O OE1 . GLU F 2 105 ? 3.023   17.319  12.719  1.00 100.11 ? 105 GLU F OE1 1 
ATOM   11195 O OE2 . GLU F 2 105 ? 2.923   15.279  11.907  1.00 102.22 ? 105 GLU F OE2 1 
ATOM   11196 N N   . HIS F 2 106 ? 7.079   16.905  8.528   1.00 61.15  ? 106 HIS F N   1 
ATOM   11197 C CA  A HIS F 2 106 ? 8.053   17.931  8.177   0.58 67.68  ? 106 HIS F CA  1 
ATOM   11198 C CA  B HIS F 2 106 ? 8.041   17.942  8.191   0.42 66.62  ? 106 HIS F CA  1 
ATOM   11199 C C   . HIS F 2 106 ? 7.793   18.535  6.802   1.00 74.67  ? 106 HIS F C   1 
ATOM   11200 O O   . HIS F 2 106 ? 8.223   19.648  6.516   1.00 79.12  ? 106 HIS F O   1 
ATOM   11201 C CB  A HIS F 2 106 ? 9.474   17.360  8.222   0.58 70.18  ? 106 HIS F CB  1 
ATOM   11202 C CB  B HIS F 2 106 ? 9.468   17.395  8.298   0.42 64.76  ? 106 HIS F CB  1 
ATOM   11203 C CG  A HIS F 2 106 ? 10.477  18.174  7.463   0.58 74.38  ? 106 HIS F CG  1 
ATOM   11204 C CG  B HIS F 2 106 ? 9.807   16.853  9.653   0.42 52.27  ? 106 HIS F CG  1 
ATOM   11205 N ND1 A HIS F 2 106 ? 10.791  17.926  6.144   0.58 71.42  ? 106 HIS F ND1 1 
ATOM   11206 N ND1 B HIS F 2 106 ? 9.627   15.529  9.993   0.42 41.78  ? 106 HIS F ND1 1 
ATOM   11207 C CD2 A HIS F 2 106 ? 11.229  19.237  7.835   0.58 75.83  ? 106 HIS F CD2 1 
ATOM   11208 C CD2 B HIS F 2 106 ? 10.307  17.460  10.756  0.42 47.85  ? 106 HIS F CD2 1 
ATOM   11209 C CE1 A HIS F 2 106 ? 11.698  18.797  5.738   0.58 72.30  ? 106 HIS F CE1 1 
ATOM   11210 C CE1 B HIS F 2 106 ? 10.006  15.342  11.244  0.42 37.67  ? 106 HIS F CE1 1 
ATOM   11211 N NE2 A HIS F 2 106 ? 11.981  19.604  6.745   0.58 74.84  ? 106 HIS F NE2 1 
ATOM   11212 N NE2 B HIS F 2 106 ? 10.423  16.498  11.730  0.42 42.15  ? 106 HIS F NE2 1 
ATOM   11213 N N   . THR F 2 107 ? 7.097   17.793  5.945   1.00 74.91  ? 107 THR F N   1 
ATOM   11214 C CA  . THR F 2 107 ? 6.796   18.280  4.599   1.00 72.14  ? 107 THR F CA  1 
ATOM   11215 C C   . THR F 2 107 ? 5.585   19.209  4.586   1.00 74.26  ? 107 THR F C   1 
ATOM   11216 O O   . THR F 2 107 ? 5.617   20.265  3.960   1.00 79.32  ? 107 THR F O   1 
ATOM   11217 C CB  . THR F 2 107 ? 6.575   17.138  3.595   1.00 73.53  ? 107 THR F CB  1 
ATOM   11218 O OG1 . THR F 2 107 ? 7.829   16.767  3.012   1.00 80.51  ? 107 THR F OG1 1 
ATOM   11219 C CG2 . THR F 2 107 ? 5.648   17.591  2.487   1.00 68.26  ? 107 THR F CG2 1 
ATOM   11220 N N   . LEU F 2 108 ? 4.519   18.818  5.276   1.00 68.46  ? 108 LEU F N   1 
ATOM   11221 C CA  . LEU F 2 108 ? 3.350   19.678  5.398   1.00 70.91  ? 108 LEU F CA  1 
ATOM   11222 C C   . LEU F 2 108 ? 3.671   20.979  6.146   1.00 75.55  ? 108 LEU F C   1 
ATOM   11223 O O   . LEU F 2 108 ? 3.057   22.016  5.895   1.00 77.78  ? 108 LEU F O   1 
ATOM   11224 C CB  . LEU F 2 108 ? 2.200   18.945  6.091   1.00 70.75  ? 108 LEU F CB  1 
ATOM   11225 C CG  . LEU F 2 108 ? 1.576   17.799  5.302   1.00 75.99  ? 108 LEU F CG  1 
ATOM   11226 C CD1 . LEU F 2 108 ? 0.225   17.445  5.890   1.00 79.64  ? 108 LEU F CD1 1 
ATOM   11227 C CD2 . LEU F 2 108 ? 1.446   18.172  3.836   1.00 80.99  ? 108 LEU F CD2 1 
ATOM   11228 N N   . ASP F 2 109 ? 4.627   20.915  7.068   1.00 70.91  ? 109 ASP F N   1 
ATOM   11229 C CA  . ASP F 2 109 ? 5.029   22.086  7.833   1.00 66.19  ? 109 ASP F CA  1 
ATOM   11230 C C   . ASP F 2 109 ? 5.930   22.971  6.990   1.00 68.96  ? 109 ASP F C   1 
ATOM   11231 O O   . ASP F 2 109 ? 5.885   24.196  7.083   1.00 69.59  ? 109 ASP F O   1 
ATOM   11232 C CB  . ASP F 2 109 ? 5.739   21.665  9.120   1.00 61.86  ? 109 ASP F CB  1 
ATOM   11233 C CG  . ASP F 2 109 ? 4.774   21.147  10.174  1.00 66.80  ? 109 ASP F CG  1 
ATOM   11234 O OD1 . ASP F 2 109 ? 3.566   21.054  9.868   1.00 68.24  ? 109 ASP F OD1 1 
ATOM   11235 O OD2 . ASP F 2 109 ? 5.214   20.827  11.302  1.00 68.10  ? 109 ASP F OD2 1 
ATOM   11236 N N   . PHE F 2 110 ? 6.750   22.341  6.162   1.00 70.48  ? 110 PHE F N   1 
ATOM   11237 C CA  . PHE F 2 110 ? 7.599   23.081  5.242   1.00 67.12  ? 110 PHE F CA  1 
ATOM   11238 C C   . PHE F 2 110 ? 6.736   24.023  4.413   1.00 74.90  ? 110 PHE F C   1 
ATOM   11239 O O   . PHE F 2 110 ? 7.067   25.194  4.236   1.00 80.71  ? 110 PHE F O   1 
ATOM   11240 C CB  . PHE F 2 110 ? 8.362   22.120  4.334   1.00 64.42  ? 110 PHE F CB  1 
ATOM   11241 C CG  . PHE F 2 110 ? 9.312   22.797  3.398   1.00 65.38  ? 110 PHE F CG  1 
ATOM   11242 C CD1 . PHE F 2 110 ? 10.438  23.437  3.879   1.00 62.60  ? 110 PHE F CD1 1 
ATOM   11243 C CD2 . PHE F 2 110 ? 9.089   22.777  2.035   1.00 74.53  ? 110 PHE F CD2 1 
ATOM   11244 C CE1 . PHE F 2 110 ? 11.323  24.062  3.015   1.00 69.59  ? 110 PHE F CE1 1 
ATOM   11245 C CE2 . PHE F 2 110 ? 9.966   23.394  1.167   1.00 81.70  ? 110 PHE F CE2 1 
ATOM   11246 C CZ  . PHE F 2 110 ? 11.085  24.040  1.657   1.00 76.64  ? 110 PHE F CZ  1 
ATOM   11247 N N   . HIS F 2 111 ? 5.622   23.502  3.913   1.00 82.22  ? 111 HIS F N   1 
ATOM   11248 C CA  . HIS F 2 111 ? 4.675   24.306  3.159   1.00 80.94  ? 111 HIS F CA  1 
ATOM   11249 C C   . HIS F 2 111 ? 4.171   25.466  4.005   1.00 79.52  ? 111 HIS F C   1 
ATOM   11250 O O   . HIS F 2 111 ? 4.226   26.623  3.586   1.00 85.24  ? 111 HIS F O   1 
ATOM   11251 C CB  . HIS F 2 111 ? 3.494   23.451  2.696   1.00 79.19  ? 111 HIS F CB  1 
ATOM   11252 C CG  . HIS F 2 111 ? 3.776   22.652  1.466   1.00 83.73  ? 111 HIS F CG  1 
ATOM   11253 N ND1 . HIS F 2 111 ? 4.304   23.212  0.322   1.00 90.98  ? 111 HIS F ND1 1 
ATOM   11254 C CD2 . HIS F 2 111 ? 3.603   21.338  1.195   1.00 85.54  ? 111 HIS F CD2 1 
ATOM   11255 C CE1 . HIS F 2 111 ? 4.445   22.276  -0.599  1.00 95.27  ? 111 HIS F CE1 1 
ATOM   11256 N NE2 . HIS F 2 111 ? 4.027   21.129  -0.095  1.00 89.64  ? 111 HIS F NE2 1 
ATOM   11257 N N   . ASP F 2 112 ? 3.684   25.142  5.201   1.00 76.96  ? 112 ASP F N   1 
ATOM   11258 C CA  . ASP F 2 112 ? 3.133   26.143  6.105   1.00 79.75  ? 112 ASP F CA  1 
ATOM   11259 C C   . ASP F 2 112 ? 4.139   27.261  6.348   1.00 81.42  ? 112 ASP F C   1 
ATOM   11260 O O   . ASP F 2 112 ? 3.772   28.430  6.385   1.00 82.52  ? 112 ASP F O   1 
ATOM   11261 C CB  . ASP F 2 112 ? 2.709   25.510  7.429   1.00 77.99  ? 112 ASP F CB  1 
ATOM   11262 C CG  . ASP F 2 112 ? 1.643   26.312  8.134   1.00 78.28  ? 112 ASP F CG  1 
ATOM   11263 O OD1 . ASP F 2 112 ? 0.923   27.052  7.445   1.00 77.44  ? 112 ASP F OD1 1 
ATOM   11264 O OD2 . ASP F 2 112 ? 1.512   26.200  9.368   1.00 78.29  ? 112 ASP F OD2 1 
ATOM   11265 N N   . SER F 2 113 ? 5.408   26.897  6.502   1.00 72.51  ? 113 SER F N   1 
ATOM   11266 C CA  . SER F 2 113 ? 6.467   27.885  6.655   1.00 68.19  ? 113 SER F CA  1 
ATOM   11267 C C   . SER F 2 113 ? 6.602   28.733  5.398   1.00 65.87  ? 113 SER F C   1 
ATOM   11268 O O   . SER F 2 113 ? 6.701   29.956  5.471   1.00 69.13  ? 113 SER F O   1 
ATOM   11269 C CB  . SER F 2 113 ? 7.802   27.207  6.965   1.00 70.18  ? 113 SER F CB  1 
ATOM   11270 O OG  . SER F 2 113 ? 8.892   28.063  6.656   1.00 72.10  ? 113 SER F OG  1 
ATOM   11271 N N   . ASN F 2 114 ? 6.608   28.079  4.244   1.00 67.71  ? 114 ASN F N   1 
ATOM   11272 C CA  . ASN F 2 114 ? 6.794   28.788  2.980   1.00 73.89  ? 114 ASN F CA  1 
ATOM   11273 C C   . ASN F 2 114 ? 5.689   29.807  2.687   1.00 77.17  ? 114 ASN F C   1 
ATOM   11274 O O   . ASN F 2 114 ? 5.928   30.812  2.027   1.00 74.32  ? 114 ASN F O   1 
ATOM   11275 C CB  . ASN F 2 114 ? 6.965   27.794  1.826   1.00 75.41  ? 114 ASN F CB  1 
ATOM   11276 C CG  . ASN F 2 114 ? 8.355   27.178  1.793   1.00 75.87  ? 114 ASN F CG  1 
ATOM   11277 O OD1 . ASN F 2 114 ? 9.160   27.386  2.704   1.00 76.62  ? 114 ASN F OD1 1 
ATOM   11278 N ND2 . ASN F 2 114 ? 8.644   26.422  0.742   1.00 76.97  ? 114 ASN F ND2 1 
ATOM   11279 N N   . VAL F 2 115 ? 4.487   29.538  3.188   1.00 85.12  ? 115 VAL F N   1 
ATOM   11280 C CA  . VAL F 2 115 ? 3.376   30.473  3.075   1.00 88.51  ? 115 VAL F CA  1 
ATOM   11281 C C   . VAL F 2 115 ? 3.569   31.614  4.064   1.00 84.54  ? 115 VAL F C   1 
ATOM   11282 O O   . VAL F 2 115 ? 3.447   32.790  3.712   1.00 82.49  ? 115 VAL F O   1 
ATOM   11283 C CB  . VAL F 2 115 ? 2.025   29.786  3.366   1.00 89.40  ? 115 VAL F CB  1 
ATOM   11284 C CG1 . VAL F 2 115 ? 1.034   30.780  3.951   1.00 89.39  ? 115 VAL F CG1 1 
ATOM   11285 C CG2 . VAL F 2 115 ? 1.471   29.139  2.107   1.00 94.75  ? 115 VAL F CG2 1 
ATOM   11286 N N   . LYS F 2 116 ? 3.878   31.256  5.307   1.00 76.94  ? 116 LYS F N   1 
ATOM   11287 C CA  . LYS F 2 116 ? 4.108   32.240  6.355   1.00 73.29  ? 116 LYS F CA  1 
ATOM   11288 C C   . LYS F 2 116 ? 5.245   33.189  5.967   1.00 73.33  ? 116 LYS F C   1 
ATOM   11289 O O   . LYS F 2 116 ? 5.080   34.405  5.984   1.00 78.98  ? 116 LYS F O   1 
ATOM   11290 C CB  . LYS F 2 116 ? 4.426   31.542  7.678   1.00 68.46  ? 116 LYS F CB  1 
ATOM   11291 C CG  . LYS F 2 116 ? 4.210   32.411  8.898   1.00 71.12  ? 116 LYS F CG  1 
ATOM   11292 C CD  . LYS F 2 116 ? 4.658   31.707  10.166  1.00 74.49  ? 116 LYS F CD  1 
ATOM   11293 C CE  . LYS F 2 116 ? 4.474   32.597  11.384  1.00 77.42  ? 116 LYS F CE  1 
ATOM   11294 N NZ  . LYS F 2 116 ? 5.227   33.875  11.234  1.00 75.16  ? 116 LYS F NZ  1 
ATOM   11295 N N   . ASN F 2 117 ? 6.394   32.625  5.609   1.00 80.78  ? 117 ASN F N   1 
ATOM   11296 C CA  . ASN F 2 117 ? 7.572   33.415  5.260   1.00 82.72  ? 117 ASN F CA  1 
ATOM   11297 C C   . ASN F 2 117 ? 7.351   34.363  4.087   1.00 91.32  ? 117 ASN F C   1 
ATOM   11298 O O   . ASN F 2 117 ? 8.109   35.312  3.901   1.00 95.81  ? 117 ASN F O   1 
ATOM   11299 C CB  . ASN F 2 117 ? 8.758   32.499  4.951   1.00 77.65  ? 117 ASN F CB  1 
ATOM   11300 C CG  . ASN F 2 117 ? 9.256   31.756  6.172   1.00 73.13  ? 117 ASN F CG  1 
ATOM   11301 O OD1 . ASN F 2 117 ? 8.516   31.544  7.139   1.00 66.58  ? 117 ASN F OD1 1 
ATOM   11302 N ND2 . ASN F 2 117 ? 10.521  31.358  6.137   1.00 75.39  ? 117 ASN F ND2 1 
ATOM   11303 N N   . LEU F 2 118 ? 6.324   34.091  3.287   1.00 82.11  ? 118 LEU F N   1 
ATOM   11304 C CA  . LEU F 2 118 ? 5.998   34.947  2.152   1.00 81.95  ? 118 LEU F CA  1 
ATOM   11305 C C   . LEU F 2 118 ? 5.084   36.064  2.621   1.00 89.98  ? 118 LEU F C   1 
ATOM   11306 O O   . LEU F 2 118 ? 5.279   37.227  2.274   1.00 101.42 ? 118 LEU F O   1 
ATOM   11307 C CB  . LEU F 2 118 ? 5.314   34.150  1.039   1.00 81.23  ? 118 LEU F CB  1 
ATOM   11308 C CG  . LEU F 2 118 ? 5.009   34.917  -0.251  1.00 89.43  ? 118 LEU F CG  1 
ATOM   11309 C CD1 . LEU F 2 118 ? 6.292   35.344  -0.940  1.00 91.97  ? 118 LEU F CD1 1 
ATOM   11310 C CD2 . LEU F 2 118 ? 4.152   34.088  -1.193  1.00 95.08  ? 118 LEU F CD2 1 
ATOM   11311 N N   . TYR F 2 119 ? 4.086   35.703  3.419   1.00 82.02  ? 119 TYR F N   1 
ATOM   11312 C CA  . TYR F 2 119 ? 3.169   36.681  3.984   1.00 79.58  ? 119 TYR F CA  1 
ATOM   11313 C C   . TYR F 2 119 ? 3.898   37.725  4.831   1.00 77.99  ? 119 TYR F C   1 
ATOM   11314 O O   . TYR F 2 119 ? 3.432   38.855  4.966   1.00 78.59  ? 119 TYR F O   1 
ATOM   11315 C CB  . TYR F 2 119 ? 2.102   35.987  4.822   1.00 80.38  ? 119 TYR F CB  1 
ATOM   11316 C CG  . TYR F 2 119 ? 1.194   36.936  5.561   1.00 79.66  ? 119 TYR F CG  1 
ATOM   11317 C CD1 . TYR F 2 119 ? 0.053   37.446  4.958   1.00 91.03  ? 119 TYR F CD1 1 
ATOM   11318 C CD2 . TYR F 2 119 ? 1.473   37.320  6.863   1.00 71.52  ? 119 TYR F CD2 1 
ATOM   11319 C CE1 . TYR F 2 119 ? -0.785  38.312  5.629   1.00 96.26  ? 119 TYR F CE1 1 
ATOM   11320 C CE2 . TYR F 2 119 ? 0.643   38.186  7.542   1.00 79.69  ? 119 TYR F CE2 1 
ATOM   11321 C CZ  . TYR F 2 119 ? -0.486  38.681  6.922   1.00 92.56  ? 119 TYR F CZ  1 
ATOM   11322 O OH  . TYR F 2 119 ? -1.320  39.548  7.597   1.00 97.13  ? 119 TYR F OH  1 
ATOM   11323 N N   . ASP F 2 120 ? 5.036   37.346  5.406   1.00 83.84  ? 120 ASP F N   1 
ATOM   11324 C CA  . ASP F 2 120 ? 5.833   38.274  6.208   1.00 84.52  ? 120 ASP F CA  1 
ATOM   11325 C C   . ASP F 2 120 ? 6.838   39.051  5.358   1.00 84.88  ? 120 ASP F C   1 
ATOM   11326 O O   . ASP F 2 120 ? 7.204   40.173  5.693   1.00 84.08  ? 120 ASP F O   1 
ATOM   11327 C CB  . ASP F 2 120 ? 6.555   37.548  7.352   1.00 80.32  ? 120 ASP F CB  1 
ATOM   11328 C CG  . ASP F 2 120 ? 5.624   37.176  8.499   1.00 78.40  ? 120 ASP F CG  1 
ATOM   11329 O OD1 . ASP F 2 120 ? 4.432   37.546  8.457   1.00 79.17  ? 120 ASP F OD1 1 
ATOM   11330 O OD2 . ASP F 2 120 ? 6.089   36.519  9.453   1.00 77.33  ? 120 ASP F OD2 1 
ATOM   11331 N N   . LYS F 2 121 ? 7.291   38.448  4.264   1.00 76.64  ? 121 LYS F N   1 
ATOM   11332 C CA  . LYS F 2 121 ? 8.215   39.119  3.357   1.00 73.79  ? 121 LYS F CA  1 
ATOM   11333 C C   . LYS F 2 121 ? 7.506   40.327  2.778   1.00 78.95  ? 121 LYS F C   1 
ATOM   11334 O O   . LYS F 2 121 ? 8.138   41.317  2.409   1.00 85.90  ? 121 LYS F O   1 
ATOM   11335 C CB  . LYS F 2 121 ? 8.652   38.174  2.234   1.00 73.69  ? 121 LYS F CB  1 
ATOM   11336 C CG  . LYS F 2 121 ? 9.822   38.680  1.395   1.00 78.07  ? 121 LYS F CG  1 
ATOM   11337 C CD  . LYS F 2 121 ? 10.139  37.714  0.254   1.00 91.21  ? 121 LYS F CD  1 
ATOM   11338 C CE  . LYS F 2 121 ? 11.339  38.172  -0.575  1.00 102.28 ? 121 LYS F CE  1 
ATOM   11339 N NZ  . LYS F 2 121 ? 11.111  39.461  -1.291  1.00 106.26 ? 121 LYS F NZ  1 
ATOM   11340 N N   . VAL F 2 122 ? 6.180   40.231  2.720   1.00 76.00  ? 122 VAL F N   1 
ATOM   11341 C CA  . VAL F 2 122 ? 5.333   41.292  2.185   1.00 77.69  ? 122 VAL F CA  1 
ATOM   11342 C C   . VAL F 2 122 ? 4.932   42.299  3.259   1.00 79.64  ? 122 VAL F C   1 
ATOM   11343 O O   . VAL F 2 122 ? 5.195   43.493  3.132   1.00 86.30  ? 122 VAL F O   1 
ATOM   11344 C CB  . VAL F 2 122 ? 4.058   40.710  1.545   1.00 71.62  ? 122 VAL F CB  1 
ATOM   11345 C CG1 . VAL F 2 122 ? 2.937   41.747  1.538   1.00 68.04  ? 122 VAL F CG1 1 
ATOM   11346 C CG2 . VAL F 2 122 ? 4.356   40.208  0.143   1.00 65.17  ? 122 VAL F CG2 1 
ATOM   11347 N N   . ARG F 2 123 ? 4.289   41.807  4.312   1.00 84.44  ? 123 ARG F N   1 
ATOM   11348 C CA  . ARG F 2 123 ? 3.889   42.648  5.430   1.00 83.00  ? 123 ARG F CA  1 
ATOM   11349 C C   . ARG F 2 123 ? 5.004   43.621  5.837   1.00 78.44  ? 123 ARG F C   1 
ATOM   11350 O O   . ARG F 2 123 ? 4.783   44.828  5.928   1.00 77.02  ? 123 ARG F O   1 
ATOM   11351 C CB  . ARG F 2 123 ? 3.480   41.773  6.622   1.00 82.70  ? 123 ARG F CB  1 
ATOM   11352 C CG  . ARG F 2 123 ? 2.928   42.538  7.813   1.00 87.31  ? 123 ARG F CG  1 
ATOM   11353 C CD  . ARG F 2 123 ? 2.723   41.628  9.011   1.00 93.48  ? 123 ARG F CD  1 
ATOM   11354 N NE  . ARG F 2 123 ? 3.892   40.786  9.252   1.00 95.69  ? 123 ARG F NE  1 
ATOM   11355 C CZ  . ARG F 2 123 ? 5.061   41.233  9.700   1.00 93.57  ? 123 ARG F CZ  1 
ATOM   11356 N NH1 . ARG F 2 123 ? 5.228   42.525  9.954   1.00 85.15  ? 123 ARG F NH1 1 
ATOM   11357 N NH2 . ARG F 2 123 ? 6.069   40.388  9.888   1.00 95.74  ? 123 ARG F NH2 1 
ATOM   11358 N N   . MET F 2 124 ? 6.201   43.087  6.063   1.00 81.73  ? 124 MET F N   1 
ATOM   11359 C CA  . MET F 2 124 ? 7.317   43.859  6.609   1.00 85.64  ? 124 MET F CA  1 
ATOM   11360 C C   . MET F 2 124 ? 7.891   44.901  5.648   1.00 88.02  ? 124 MET F C   1 
ATOM   11361 O O   . MET F 2 124 ? 8.737   45.704  6.040   1.00 89.65  ? 124 MET F O   1 
ATOM   11362 C CB  . MET F 2 124 ? 8.423   42.921  7.115   1.00 88.50  ? 124 MET F CB  1 
ATOM   11363 C CG  . MET F 2 124 ? 8.181   42.374  8.526   1.00 90.02  ? 124 MET F CG  1 
ATOM   11364 S SD  . MET F 2 124 ? 9.183   40.928  8.959   1.00 84.56  ? 124 MET F SD  1 
ATOM   11365 C CE  . MET F 2 124 ? 10.816  41.441  8.418   1.00 100.22 ? 124 MET F CE  1 
ATOM   11366 N N   . GLN F 2 125 ? 7.438   44.882  4.397   1.00 82.48  ? 125 GLN F N   1 
ATOM   11367 C CA  . GLN F 2 125 ? 7.800   45.919  3.432   1.00 89.30  ? 125 GLN F CA  1 
ATOM   11368 C C   . GLN F 2 125 ? 6.724   46.994  3.421   1.00 88.97  ? 125 GLN F C   1 
ATOM   11369 O O   . GLN F 2 125 ? 7.014   48.182  3.278   1.00 88.50  ? 125 GLN F O   1 
ATOM   11370 C CB  . GLN F 2 125 ? 7.952   45.340  2.021   1.00 100.49 ? 125 GLN F CB  1 
ATOM   11371 C CG  . GLN F 2 125 ? 9.349   44.836  1.672   1.00 108.62 ? 125 GLN F CG  1 
ATOM   11372 C CD  . GLN F 2 125 ? 9.433   44.263  0.261   1.00 120.41 ? 125 GLN F CD  1 
ATOM   11373 O OE1 . GLN F 2 125 ? 8.993   44.885  -0.707  1.00 125.03 ? 125 GLN F OE1 1 
ATOM   11374 N NE2 . GLN F 2 125 ? 9.996   43.065  0.145   1.00 123.38 ? 125 GLN F NE2 1 
ATOM   11375 N N   . LEU F 2 126 ? 5.478   46.562  3.581   1.00 89.53  ? 126 LEU F N   1 
ATOM   11376 C CA  . LEU F 2 126 ? 4.333   47.461  3.513   1.00 91.22  ? 126 LEU F CA  1 
ATOM   11377 C C   . LEU F 2 126 ? 4.123   48.285  4.780   1.00 92.82  ? 126 LEU F C   1 
ATOM   11378 O O   . LEU F 2 126 ? 3.787   49.464  4.706   1.00 97.31  ? 126 LEU F O   1 
ATOM   11379 C CB  . LEU F 2 126 ? 3.063   46.683  3.175   1.00 87.88  ? 126 LEU F CB  1 
ATOM   11380 C CG  . LEU F 2 126 ? 3.041   46.094  1.766   1.00 88.52  ? 126 LEU F CG  1 
ATOM   11381 C CD1 . LEU F 2 126 ? 1.722   45.382  1.500   1.00 90.20  ? 126 LEU F CD1 1 
ATOM   11382 C CD2 . LEU F 2 126 ? 3.289   47.188  0.738   1.00 94.70  ? 126 LEU F CD2 1 
ATOM   11383 N N   . ARG F 2 127 ? 4.306   47.664  5.938   1.00 85.79  ? 127 ARG F N   1 
ATOM   11384 C CA  . ARG F 2 127 ? 4.177   48.369  7.210   1.00 84.86  ? 127 ARG F CA  1 
ATOM   11385 C C   . ARG F 2 127 ? 2.813   49.045  7.387   1.00 97.90  ? 127 ARG F C   1 
ATOM   11386 O O   . ARG F 2 127 ? 1.767   48.416  7.219   1.00 104.66 ? 127 ARG F O   1 
ATOM   11387 C CB  . ARG F 2 127 ? 5.286   49.415  7.358   1.00 76.04  ? 127 ARG F CB  1 
ATOM   11388 C CG  . ARG F 2 127 ? 6.695   48.876  7.237   1.00 71.53  ? 127 ARG F CG  1 
ATOM   11389 C CD  . ARG F 2 127 ? 7.675   49.836  7.888   1.00 72.11  ? 127 ARG F CD  1 
ATOM   11390 N NE  . ARG F 2 127 ? 8.699   50.315  6.964   1.00 76.57  ? 127 ARG F NE  1 
ATOM   11391 C CZ  . ARG F 2 127 ? 9.516   51.333  7.222   1.00 78.97  ? 127 ARG F CZ  1 
ATOM   11392 N NH1 . ARG F 2 127 ? 9.423   51.985  8.377   1.00 69.30  ? 127 ARG F NH1 1 
ATOM   11393 N NH2 . ARG F 2 127 ? 10.423  51.706  6.324   1.00 87.39  ? 127 ARG F NH2 1 
ATOM   11394 N N   . ASP F 2 128 ? 2.839   50.334  7.727   1.00 113.48 ? 128 ASP F N   1 
ATOM   11395 C CA  . ASP F 2 128 ? 1.614   51.098  7.979   1.00 115.74 ? 128 ASP F CA  1 
ATOM   11396 C C   . ASP F 2 128 ? 1.113   51.878  6.760   1.00 120.09 ? 128 ASP F C   1 
ATOM   11397 O O   . ASP F 2 128 ? 0.434   52.897  6.898   1.00 117.75 ? 128 ASP F O   1 
ATOM   11398 C CB  . ASP F 2 128 ? 1.774   52.031  9.191   1.00 110.61 ? 128 ASP F CB  1 
ATOM   11399 C CG  . ASP F 2 128 ? 3.016   52.906  9.107   1.00 104.01 ? 128 ASP F CG  1 
ATOM   11400 O OD1 . ASP F 2 128 ? 3.566   53.067  7.997   1.00 110.03 ? 128 ASP F OD1 1 
ATOM   11401 O OD2 . ASP F 2 128 ? 3.440   53.437  10.156  1.00 92.29  ? 128 ASP F OD2 1 
ATOM   11402 N N   . ASN F 2 129 ? 1.458   51.401  5.570   1.00 111.79 ? 129 ASN F N   1 
ATOM   11403 C CA  . ASN F 2 129 ? 0.855   51.906  4.345   1.00 116.55 ? 129 ASN F CA  1 
ATOM   11404 C C   . ASN F 2 129 ? -0.366  51.061  4.011   1.00 119.12 ? 129 ASN F C   1 
ATOM   11405 O O   . ASN F 2 129 ? -1.073  51.324  3.036   1.00 124.82 ? 129 ASN F O   1 
ATOM   11406 C CB  . ASN F 2 129 ? 1.854   51.859  3.188   1.00 116.37 ? 129 ASN F CB  1 
ATOM   11407 C CG  . ASN F 2 129 ? 3.021   52.799  3.388   1.00 115.19 ? 129 ASN F CG  1 
ATOM   11408 O OD1 . ASN F 2 129 ? 3.152   53.425  4.438   1.00 117.20 ? 129 ASN F OD1 1 
ATOM   11409 N ND2 . ASN F 2 129 ? 3.881   52.902  2.380   1.00 112.00 ? 129 ASN F ND2 1 
ATOM   11410 N N   . VAL F 2 130 ? -0.603  50.044  4.836   1.00 109.32 ? 130 VAL F N   1 
ATOM   11411 C CA  . VAL F 2 130 ? -1.676  49.083  4.612   1.00 105.56 ? 130 VAL F CA  1 
ATOM   11412 C C   . VAL F 2 130 ? -2.316  48.650  5.925   1.00 103.51 ? 130 VAL F C   1 
ATOM   11413 O O   . VAL F 2 130 ? -1.836  48.999  7.005   1.00 99.53  ? 130 VAL F O   1 
ATOM   11414 C CB  . VAL F 2 130 ? -1.160  47.836  3.886   1.00 100.51 ? 130 VAL F CB  1 
ATOM   11415 C CG1 . VAL F 2 130 ? -0.905  48.143  2.421   1.00 99.69  ? 130 VAL F CG1 1 
ATOM   11416 C CG2 . VAL F 2 130 ? 0.103   47.335  4.558   1.00 98.41  ? 130 VAL F CG2 1 
ATOM   11417 N N   . LYS F 2 131 ? -3.391  47.874  5.818   1.00 111.26 ? 131 LYS F N   1 
ATOM   11418 C CA  . LYS F 2 131 ? -4.197  47.487  6.971   1.00 115.33 ? 131 LYS F CA  1 
ATOM   11419 C C   . LYS F 2 131 ? -4.270  45.967  7.104   1.00 116.40 ? 131 LYS F C   1 
ATOM   11420 O O   . LYS F 2 131 ? -5.042  45.312  6.401   1.00 125.68 ? 131 LYS F O   1 
ATOM   11421 C CB  . LYS F 2 131 ? -5.606  48.074  6.831   1.00 125.27 ? 131 LYS F CB  1 
ATOM   11422 C CG  . LYS F 2 131 ? -6.479  47.989  8.076   1.00 131.10 ? 131 LYS F CG  1 
ATOM   11423 C CD  . LYS F 2 131 ? -7.746  48.816  7.884   1.00 143.22 ? 131 LYS F CD  1 
ATOM   11424 C CE  . LYS F 2 131 ? -8.641  48.781  9.109   1.00 147.94 ? 131 LYS F CE  1 
ATOM   11425 N NZ  . LYS F 2 131 ? -9.210  47.428  9.337   1.00 150.27 ? 131 LYS F NZ  1 
ATOM   11426 N N   . GLU F 2 132 ? -3.464  45.413  8.006   1.00 112.75 ? 132 GLU F N   1 
ATOM   11427 C CA  . GLU F 2 132 ? -3.416  43.970  8.216   1.00 105.54 ? 132 GLU F CA  1 
ATOM   11428 C C   . GLU F 2 132 ? -4.776  43.425  8.645   1.00 102.60 ? 132 GLU F C   1 
ATOM   11429 O O   . GLU F 2 132 ? -5.213  43.629  9.778   1.00 105.44 ? 132 GLU F O   1 
ATOM   11430 C CB  . GLU F 2 132 ? -2.343  43.617  9.248   1.00 102.64 ? 132 GLU F CB  1 
ATOM   11431 C CG  . GLU F 2 132 ? -2.188  42.125  9.499   1.00 108.01 ? 132 GLU F CG  1 
ATOM   11432 C CD  . GLU F 2 132 ? -0.993  41.796  10.377  1.00 107.33 ? 132 GLU F CD  1 
ATOM   11433 O OE1 . GLU F 2 132 ? -0.211  42.719  10.701  1.00 107.00 ? 132 GLU F OE1 1 
ATOM   11434 O OE2 . GLU F 2 132 ? -0.835  40.612  10.743  1.00 105.26 ? 132 GLU F OE2 1 
ATOM   11435 N N   . LEU F 2 133 ? -5.439  42.726  7.730   1.00 96.06  ? 133 LEU F N   1 
ATOM   11436 C CA  . LEU F 2 133 ? -6.797  42.243  7.959   1.00 110.31 ? 133 LEU F CA  1 
ATOM   11437 C C   . LEU F 2 133 ? -6.865  40.951  8.778   1.00 119.45 ? 133 LEU F C   1 
ATOM   11438 O O   . LEU F 2 133 ? -7.951  40.508  9.153   1.00 129.37 ? 133 LEU F O   1 
ATOM   11439 C CB  . LEU F 2 133 ? -7.527  42.061  6.625   1.00 118.76 ? 133 LEU F CB  1 
ATOM   11440 C CG  . LEU F 2 133 ? -7.819  43.343  5.840   1.00 125.95 ? 133 LEU F CG  1 
ATOM   11441 C CD1 . LEU F 2 133 ? -8.359  43.021  4.455   1.00 132.83 ? 133 LEU F CD1 1 
ATOM   11442 C CD2 . LEU F 2 133 ? -8.789  44.233  6.606   1.00 127.35 ? 133 LEU F CD2 1 
ATOM   11443 N N   . GLY F 2 134 ? -5.710  40.351  9.054   1.00 110.56 ? 134 GLY F N   1 
ATOM   11444 C CA  . GLY F 2 134 ? -5.659  39.132  9.846   1.00 103.95 ? 134 GLY F CA  1 
ATOM   11445 C C   . GLY F 2 134 ? -6.465  38.006  9.228   1.00 104.27 ? 134 GLY F C   1 
ATOM   11446 O O   . GLY F 2 134 ? -7.113  37.226  9.925   1.00 103.19 ? 134 GLY F O   1 
ATOM   11447 N N   . ASN F 2 135 ? -6.426  37.934  7.904   1.00 75.59  ? 135 ASN F N   1 
ATOM   11448 C CA  . ASN F 2 135 ? -7.145  36.915  7.161   1.00 80.26  ? 135 ASN F CA  1 
ATOM   11449 C C   . ASN F 2 135 ? -6.248  36.396  6.048   1.00 77.84  ? 135 ASN F C   1 
ATOM   11450 O O   . ASN F 2 135 ? -6.517  35.355  5.438   1.00 78.37  ? 135 ASN F O   1 
ATOM   11451 C CB  . ASN F 2 135 ? -8.430  37.492  6.565   1.00 90.63  ? 135 ASN F CB  1 
ATOM   11452 C CG  . ASN F 2 135 ? -8.163  38.428  5.396   1.00 98.45  ? 135 ASN F CG  1 
ATOM   11453 O OD1 . ASN F 2 135 ? -7.188  39.180  5.396   1.00 98.67  ? 135 ASN F OD1 1 
ATOM   11454 N ND2 . ASN F 2 135 ? -9.029  38.379  4.390   1.00 103.95 ? 135 ASN F ND2 1 
ATOM   11455 N N   . GLY F 2 136 ? -5.173  37.136  5.795   1.00 107.12 ? 136 GLY F N   1 
ATOM   11456 C CA  . GLY F 2 136 ? -4.241  36.810  4.733   1.00 104.35 ? 136 GLY F CA  1 
ATOM   11457 C C   . GLY F 2 136 ? -4.108  37.973  3.776   1.00 107.24 ? 136 GLY F C   1 
ATOM   11458 O O   . GLY F 2 136 ? -3.277  37.953  2.869   1.00 108.31 ? 136 GLY F O   1 
ATOM   11459 N N   . CYS F 2 137 ? -4.934  38.994  3.992   1.00 93.64  ? 137 CYS F N   1 
ATOM   11460 C CA  . CYS F 2 137 ? -4.974  40.159  3.116   1.00 92.62  ? 137 CYS F CA  1 
ATOM   11461 C C   . CYS F 2 137 ? -4.601  41.442  3.854   1.00 90.62  ? 137 CYS F C   1 
ATOM   11462 O O   . CYS F 2 137 ? -4.723  41.533  5.079   1.00 89.02  ? 137 CYS F O   1 
ATOM   11463 C CB  . CYS F 2 137 ? -6.371  40.324  2.511   1.00 99.55  ? 137 CYS F CB  1 
ATOM   11464 S SG  . CYS F 2 137 ? -7.029  38.872  1.674   1.00 87.74  ? 137 CYS F SG  1 
ATOM   11465 N N   . PHE F 2 138 ? -4.148  42.429  3.086   1.00 127.89 ? 138 PHE F N   1 
ATOM   11466 C CA  . PHE F 2 138 ? -3.935  43.778  3.592   1.00 128.72 ? 138 PHE F CA  1 
ATOM   11467 C C   . PHE F 2 138 ? -4.815  44.739  2.805   1.00 140.20 ? 138 PHE F C   1 
ATOM   11468 O O   . PHE F 2 138 ? -5.022  44.558  1.604   1.00 148.32 ? 138 PHE F O   1 
ATOM   11469 C CB  . PHE F 2 138 ? -2.473  44.202  3.435   1.00 123.31 ? 138 PHE F CB  1 
ATOM   11470 C CG  . PHE F 2 138 ? -1.489  43.232  4.017   1.00 119.37 ? 138 PHE F CG  1 
ATOM   11471 C CD1 . PHE F 2 138 ? -1.452  42.995  5.381   1.00 117.42 ? 138 PHE F CD1 1 
ATOM   11472 C CD2 . PHE F 2 138 ? -0.588  42.568  3.200   1.00 116.73 ? 138 PHE F CD2 1 
ATOM   11473 C CE1 . PHE F 2 138 ? -0.541  42.103  5.919   1.00 116.44 ? 138 PHE F CE1 1 
ATOM   11474 C CE2 . PHE F 2 138 ? 0.326   41.677  3.730   1.00 112.29 ? 138 PHE F CE2 1 
ATOM   11475 C CZ  . PHE F 2 138 ? 0.350   41.444  5.091   1.00 113.21 ? 138 PHE F CZ  1 
ATOM   11476 N N   . GLU F 2 139 ? -5.333  45.761  3.478   1.00 112.77 ? 139 GLU F N   1 
ATOM   11477 C CA  . GLU F 2 139 ? -6.070  46.815  2.793   1.00 114.61 ? 139 GLU F CA  1 
ATOM   11478 C C   . GLU F 2 139 ? -5.206  48.064  2.674   1.00 110.03 ? 139 GLU F C   1 
ATOM   11479 O O   . GLU F 2 139 ? -4.830  48.664  3.679   1.00 104.26 ? 139 GLU F O   1 
ATOM   11480 C CB  . GLU F 2 139 ? -7.370  47.140  3.529   1.00 120.93 ? 139 GLU F CB  1 
ATOM   11481 C CG  . GLU F 2 139 ? -8.259  48.127  2.790   1.00 132.24 ? 139 GLU F CG  1 
ATOM   11482 C CD  . GLU F 2 139 ? -9.577  48.366  3.497   1.00 140.61 ? 139 GLU F CD  1 
ATOM   11483 O OE1 . GLU F 2 139 ? -9.657  48.094  4.714   1.00 135.09 ? 139 GLU F OE1 1 
ATOM   11484 O OE2 . GLU F 2 139 ? -10.533 48.823  2.833   1.00 152.59 ? 139 GLU F OE2 1 
ATOM   11485 N N   . PHE F 2 140 ? -4.884  48.447  1.445   1.00 108.51 ? 140 PHE F N   1 
ATOM   11486 C CA  . PHE F 2 140 ? -4.081  49.642  1.212   1.00 109.58 ? 140 PHE F CA  1 
ATOM   11487 C C   . PHE F 2 140 ? -4.775  50.917  1.684   1.00 114.42 ? 140 PHE F C   1 
ATOM   11488 O O   . PHE F 2 140 ? -5.956  51.144  1.405   1.00 123.84 ? 140 PHE F O   1 
ATOM   11489 C CB  . PHE F 2 140 ? -3.730  49.775  -0.267  1.00 113.26 ? 140 PHE F CB  1 
ATOM   11490 C CG  . PHE F 2 140 ? -2.612  48.885  -0.703  1.00 108.37 ? 140 PHE F CG  1 
ATOM   11491 C CD1 . PHE F 2 140 ? -1.297  49.292  -0.564  1.00 103.08 ? 140 PHE F CD1 1 
ATOM   11492 C CD2 . PHE F 2 140 ? -2.872  47.649  -1.261  1.00 113.07 ? 140 PHE F CD2 1 
ATOM   11493 C CE1 . PHE F 2 140 ? -0.260  48.483  -0.968  1.00 104.63 ? 140 PHE F CE1 1 
ATOM   11494 C CE2 . PHE F 2 140 ? -1.840  46.833  -1.670  1.00 114.61 ? 140 PHE F CE2 1 
ATOM   11495 C CZ  . PHE F 2 140 ? -0.530  47.251  -1.523  1.00 110.52 ? 140 PHE F CZ  1 
ATOM   11496 N N   . TYR F 2 141 ? -4.023  51.749  2.396   1.00 113.63 ? 141 TYR F N   1 
ATOM   11497 C CA  . TYR F 2 141 ? -4.508  53.048  2.841   1.00 111.45 ? 141 TYR F CA  1 
ATOM   11498 C C   . TYR F 2 141 ? -4.488  54.045  1.689   1.00 121.76 ? 141 TYR F C   1 
ATOM   11499 O O   . TYR F 2 141 ? -4.978  55.168  1.807   1.00 129.87 ? 141 TYR F O   1 
ATOM   11500 C CB  . TYR F 2 141 ? -3.657  53.555  4.004   1.00 103.11 ? 141 TYR F CB  1 
ATOM   11501 C CG  . TYR F 2 141 ? -4.114  53.050  5.351   1.00 105.64 ? 141 TYR F CG  1 
ATOM   11502 C CD1 . TYR F 2 141 ? -5.467  52.950  5.652   1.00 112.82 ? 141 TYR F CD1 1 
ATOM   11503 C CD2 . TYR F 2 141 ? -3.197  52.671  6.322   1.00 103.95 ? 141 TYR F CD2 1 
ATOM   11504 C CE1 . TYR F 2 141 ? -5.892  52.493  6.883   1.00 117.14 ? 141 TYR F CE1 1 
ATOM   11505 C CE2 . TYR F 2 141 ? -3.613  52.211  7.558   1.00 107.88 ? 141 TYR F CE2 1 
ATOM   11506 C CZ  . TYR F 2 141 ? -4.961  52.124  7.831   1.00 116.28 ? 141 TYR F CZ  1 
ATOM   11507 O OH  . TYR F 2 141 ? -5.380  51.666  9.058   1.00 121.33 ? 141 TYR F OH  1 
ATOM   11508 N N   . HIS F 2 142 ? -3.918  53.621  0.569   1.00 116.61 ? 142 HIS F N   1 
ATOM   11509 C CA  . HIS F 2 142 ? -3.887  54.439  -0.631  1.00 120.62 ? 142 HIS F CA  1 
ATOM   11510 C C   . HIS F 2 142 ? -4.406  53.623  -1.803  1.00 125.27 ? 142 HIS F C   1 
ATOM   11511 O O   . HIS F 2 142 ? -4.726  52.441  -1.661  1.00 121.72 ? 142 HIS F O   1 
ATOM   11512 C CB  . HIS F 2 142 ? -2.458  54.880  -0.921  1.00 113.32 ? 142 HIS F CB  1 
ATOM   11513 C CG  . HIS F 2 142 ? -1.514  53.740  -1.134  1.00 105.50 ? 142 HIS F CG  1 
ATOM   11514 N ND1 . HIS F 2 142 ? -0.782  53.179  -0.109  1.00 100.94 ? 142 HIS F ND1 1 
ATOM   11515 C CD2 . HIS F 2 142 ? -1.195  53.042  -2.250  1.00 106.02 ? 142 HIS F CD2 1 
ATOM   11516 C CE1 . HIS F 2 142 ? -0.043  52.195  -0.587  1.00 100.51 ? 142 HIS F CE1 1 
ATOM   11517 N NE2 . HIS F 2 142 ? -0.274  52.092  -1.883  1.00 101.36 ? 142 HIS F NE2 1 
ATOM   11518 N N   . LYS F 2 143 ? -4.490  54.256  -2.965  1.00 123.94 ? 143 LYS F N   1 
ATOM   11519 C CA  . LYS F 2 143 ? -4.839  53.532  -4.173  1.00 131.51 ? 143 LYS F CA  1 
ATOM   11520 C C   . LYS F 2 143 ? -3.617  52.775  -4.684  1.00 127.88 ? 143 LYS F C   1 
ATOM   11521 O O   . LYS F 2 143 ? -2.589  53.376  -5.009  1.00 124.41 ? 143 LYS F O   1 
ATOM   11522 C CB  . LYS F 2 143 ? -5.379  54.484  -5.242  1.00 138.62 ? 143 LYS F CB  1 
ATOM   11523 C CG  . LYS F 2 143 ? -6.744  55.069  -4.912  1.00 142.88 ? 143 LYS F CG  1 
ATOM   11524 C CD  . LYS F 2 143 ? -7.780  53.973  -4.703  1.00 145.99 ? 143 LYS F CD  1 
ATOM   11525 C CE  . LYS F 2 143 ? -9.154  54.559  -4.417  1.00 152.24 ? 143 LYS F CE  1 
ATOM   11526 N NZ  . LYS F 2 143 ? -10.176 53.505  -4.176  1.00 155.19 ? 143 LYS F NZ  1 
ATOM   11527 N N   . CYS F 2 144 ? -3.729  51.450  -4.728  1.00 125.65 ? 144 CYS F N   1 
ATOM   11528 C CA  . CYS F 2 144 ? -2.673  50.617  -5.287  1.00 121.31 ? 144 CYS F CA  1 
ATOM   11529 C C   . CYS F 2 144 ? -3.164  49.920  -6.549  1.00 131.52 ? 144 CYS F C   1 
ATOM   11530 O O   . CYS F 2 144 ? -3.802  48.868  -6.486  1.00 135.67 ? 144 CYS F O   1 
ATOM   11531 C CB  . CYS F 2 144 ? -2.180  49.589  -4.267  1.00 113.49 ? 144 CYS F CB  1 
ATOM   11532 S SG  . CYS F 2 144 ? -0.582  48.848  -4.694  1.00 135.50 ? 144 CYS F SG  1 
ATOM   11533 N N   . ASP F 2 145 ? -2.866  50.525  -7.693  1.00 129.40 ? 145 ASP F N   1 
ATOM   11534 C CA  . ASP F 2 145 ? -3.246  49.969  -8.985  1.00 138.09 ? 145 ASP F CA  1 
ATOM   11535 C C   . ASP F 2 145 ? -2.326  48.818  -9.383  1.00 129.79 ? 145 ASP F C   1 
ATOM   11536 O O   . ASP F 2 145 ? -1.529  48.343  -8.574  1.00 119.15 ? 145 ASP F O   1 
ATOM   11537 C CB  . ASP F 2 145 ? -3.243  51.060  -10.060 1.00 148.51 ? 145 ASP F CB  1 
ATOM   11538 C CG  . ASP F 2 145 ? -1.945  51.850  -10.090 1.00 150.02 ? 145 ASP F CG  1 
ATOM   11539 O OD1 . ASP F 2 145 ? -1.422  52.090  -11.199 1.00 156.86 ? 145 ASP F OD1 1 
ATOM   11540 O OD2 . ASP F 2 145 ? -1.448  52.239  -9.009  1.00 143.32 ? 145 ASP F OD2 1 
ATOM   11541 N N   . ASP F 2 146 ? -2.441  48.375  -10.630 1.00 113.41 ? 146 ASP F N   1 
ATOM   11542 C CA  . ASP F 2 146 ? -1.670  47.234  -11.117 1.00 108.32 ? 146 ASP F CA  1 
ATOM   11543 C C   . ASP F 2 146 ? -0.154  47.416  -11.012 1.00 102.30 ? 146 ASP F C   1 
ATOM   11544 O O   . ASP F 2 146 ? 0.484   46.791  -10.172 1.00 98.57  ? 146 ASP F O   1 
ATOM   11545 C CB  . ASP F 2 146 ? -2.069  46.878  -12.551 1.00 116.23 ? 146 ASP F CB  1 
ATOM   11546 C CG  . ASP F 2 146 ? -3.357  46.073  -12.617 1.00 117.60 ? 146 ASP F CG  1 
ATOM   11547 O OD1 . ASP F 2 146 ? -4.230  46.248  -11.736 1.00 115.89 ? 146 ASP F OD1 1 
ATOM   11548 O OD2 . ASP F 2 146 ? -3.494  45.258  -13.553 1.00 119.20 ? 146 ASP F OD2 1 
ATOM   11549 N N   . GLU F 2 147 ? 0.421   48.264  -11.859 1.00 121.15 ? 147 GLU F N   1 
ATOM   11550 C CA  . GLU F 2 147 ? 1.875   48.423  -11.899 1.00 122.22 ? 147 GLU F CA  1 
ATOM   11551 C C   . GLU F 2 147 ? 2.492   48.635  -10.514 1.00 116.77 ? 147 GLU F C   1 
ATOM   11552 O O   . GLU F 2 147 ? 3.693   48.431  -10.327 1.00 113.42 ? 147 GLU F O   1 
ATOM   11553 C CB  . GLU F 2 147 ? 2.278   49.546  -12.861 1.00 133.36 ? 147 GLU F CB  1 
ATOM   11554 C CG  . GLU F 2 147 ? 1.834   50.933  -12.437 1.00 140.55 ? 147 GLU F CG  1 
ATOM   11555 C CD  . GLU F 2 147 ? 2.824   51.603  -11.506 1.00 138.51 ? 147 GLU F CD  1 
ATOM   11556 O OE1 . GLU F 2 147 ? 2.398   52.473  -10.716 1.00 142.68 ? 147 GLU F OE1 1 
ATOM   11557 O OE2 . GLU F 2 147 ? 4.026   51.265  -11.568 1.00 129.93 ? 147 GLU F OE2 1 
ATOM   11558 N N   . CYS F 2 148 ? 1.668   49.041  -9.550  1.00 141.18 ? 148 CYS F N   1 
ATOM   11559 C CA  . CYS F 2 148 ? 2.095   49.127  -8.156  1.00 136.45 ? 148 CYS F CA  1 
ATOM   11560 C C   . CYS F 2 148 ? 2.368   47.741  -7.588  1.00 131.69 ? 148 CYS F C   1 
ATOM   11561 O O   . CYS F 2 148 ? 3.494   47.432  -7.196  1.00 126.59 ? 148 CYS F O   1 
ATOM   11562 C CB  . CYS F 2 148 ? 1.030   49.817  -7.302  1.00 137.41 ? 148 CYS F CB  1 
ATOM   11563 S SG  . CYS F 2 148 ? 1.167   49.459  -5.527  1.00 127.66 ? 148 CYS F SG  1 
ATOM   11564 N N   . MET F 2 149 ? 1.324   46.917  -7.540  1.00 114.55 ? 149 MET F N   1 
ATOM   11565 C CA  . MET F 2 149 ? 1.426   45.542  -7.057  1.00 108.35 ? 149 MET F CA  1 
ATOM   11566 C C   . MET F 2 149 ? 2.700   44.859  -7.569  1.00 115.09 ? 149 MET F C   1 
ATOM   11567 O O   . MET F 2 149 ? 3.369   44.146  -6.826  1.00 112.43 ? 149 MET F O   1 
ATOM   11568 C CB  . MET F 2 149 ? 0.197   44.733  -7.489  1.00 105.11 ? 149 MET F CB  1 
ATOM   11569 C CG  . MET F 2 149 ? -1.152  45.409  -7.233  1.00 105.24 ? 149 MET F CG  1 
ATOM   11570 S SD  . MET F 2 149 ? -1.759  45.268  -5.536  1.00 95.11  ? 149 MET F SD  1 
ATOM   11571 C CE  . MET F 2 149 ? -3.410  45.948  -5.690  1.00 104.84 ? 149 MET F CE  1 
ATOM   11572 N N   . ASN F 2 150 ? 3.030   45.087  -8.839  1.00 129.22 ? 150 ASN F N   1 
ATOM   11573 C CA  . ASN F 2 150 ? 4.200   44.467  -9.464  1.00 131.74 ? 150 ASN F CA  1 
ATOM   11574 C C   . ASN F 2 150 ? 5.538   44.844  -8.827  1.00 129.73 ? 150 ASN F C   1 
ATOM   11575 O O   . ASN F 2 150 ? 6.460   44.030  -8.787  1.00 126.57 ? 150 ASN F O   1 
ATOM   11576 C CB  . ASN F 2 150 ? 4.235   44.757  -10.969 1.00 136.12 ? 150 ASN F CB  1 
ATOM   11577 C CG  . ASN F 2 150 ? 3.297   43.864  -11.759 1.00 136.84 ? 150 ASN F CG  1 
ATOM   11578 O OD1 . ASN F 2 150 ? 2.326   43.332  -11.220 1.00 134.79 ? 150 ASN F OD1 1 
ATOM   11579 N ND2 . ASN F 2 150 ? 3.587   43.690  -13.043 1.00 140.40 ? 150 ASN F ND2 1 
ATOM   11580 N N   . SER F 2 151 ? 5.648   46.077  -8.343  1.00 162.65 ? 151 SER F N   1 
ATOM   11581 C CA  . SER F 2 151 ? 6.861   46.507  -7.657  1.00 161.55 ? 151 SER F CA  1 
ATOM   11582 C C   . SER F 2 151 ? 6.916   45.877  -6.270  1.00 159.42 ? 151 SER F C   1 
ATOM   11583 O O   . SER F 2 151 ? 7.961   45.871  -5.619  1.00 155.31 ? 151 SER F O   1 
ATOM   11584 C CB  . SER F 2 151 ? 6.924   48.032  -7.557  1.00 161.70 ? 151 SER F CB  1 
ATOM   11585 O OG  . SER F 2 151 ? 5.906   48.534  -6.709  1.00 157.80 ? 151 SER F OG  1 
ATOM   11586 N N   . VAL F 2 152 ? 5.778   45.348  -5.827  1.00 191.06 ? 152 VAL F N   1 
ATOM   11587 C CA  . VAL F 2 152 ? 5.689   44.638  -4.556  1.00 185.79 ? 152 VAL F CA  1 
ATOM   11588 C C   . VAL F 2 152 ? 6.143   43.197  -4.726  1.00 186.33 ? 152 VAL F C   1 
ATOM   11589 O O   . VAL F 2 152 ? 6.961   42.697  -3.955  1.00 188.95 ? 152 VAL F O   1 
ATOM   11590 C CB  . VAL F 2 152 ? 4.242   44.605  -4.024  1.00 184.21 ? 152 VAL F CB  1 
ATOM   11591 C CG1 . VAL F 2 152 ? 4.189   43.909  -2.671  1.00 176.35 ? 152 VAL F CG1 1 
ATOM   11592 C CG2 . VAL F 2 152 ? 3.669   46.006  -3.939  1.00 184.95 ? 152 VAL F CG2 1 
ATOM   11593 N N   . LYS F 2 153 ? 5.594   42.535  -5.741  1.00 129.25 ? 153 LYS F N   1 
ATOM   11594 C CA  . LYS F 2 153 ? 5.872   41.128  -6.000  1.00 118.78 ? 153 LYS F CA  1 
ATOM   11595 C C   . LYS F 2 153 ? 7.371   40.856  -6.102  1.00 115.65 ? 153 LYS F C   1 
ATOM   11596 O O   . LYS F 2 153 ? 7.878   39.924  -5.477  1.00 114.54 ? 153 LYS F O   1 
ATOM   11597 C CB  . LYS F 2 153 ? 5.148   40.663  -7.268  1.00 119.58 ? 153 LYS F CB  1 
ATOM   11598 C CG  . LYS F 2 153 ? 3.629   40.746  -7.180  1.00 119.28 ? 153 LYS F CG  1 
ATOM   11599 C CD  . LYS F 2 153 ? 2.960   40.368  -8.501  1.00 123.25 ? 153 LYS F CD  1 
ATOM   11600 C CE  . LYS F 2 153 ? 1.438   40.441  -8.392  1.00 120.94 ? 153 LYS F CE  1 
ATOM   11601 N NZ  . LYS F 2 153 ? 0.738   40.070  -9.656  1.00 122.55 ? 153 LYS F NZ  1 
ATOM   11602 N N   . ASN F 2 154 ? 8.078   41.665  -6.887  1.00 131.32 ? 154 ASN F N   1 
ATOM   11603 C CA  . ASN F 2 154 ? 9.530   41.540  -6.970  1.00 128.62 ? 154 ASN F CA  1 
ATOM   11604 C C   . ASN F 2 154 ? 10.237  42.180  -5.772  1.00 120.16 ? 154 ASN F C   1 
ATOM   11605 O O   . ASN F 2 154 ? 11.458  42.357  -5.773  1.00 115.25 ? 154 ASN F O   1 
ATOM   11606 C CB  . ASN F 2 154 ? 10.073  42.070  -8.306  1.00 139.49 ? 154 ASN F CB  1 
ATOM   11607 C CG  . ASN F 2 154 ? 9.479   43.413  -8.697  1.00 148.08 ? 154 ASN F CG  1 
ATOM   11608 O OD1 . ASN F 2 154 ? 8.951   44.143  -7.858  1.00 150.33 ? 154 ASN F OD1 1 
ATOM   11609 N ND2 . ASN F 2 154 ? 9.567   43.745  -9.982  1.00 150.72 ? 154 ASN F ND2 1 
ATOM   11610 N N   . GLY F 2 155 ? 9.449   42.524  -4.754  1.00 123.73 ? 155 GLY F N   1 
ATOM   11611 C CA  . GLY F 2 155 ? 9.964   42.948  -3.462  1.00 121.11 ? 155 GLY F CA  1 
ATOM   11612 C C   . GLY F 2 155 ? 10.777  44.227  -3.449  1.00 120.26 ? 155 GLY F C   1 
ATOM   11613 O O   . GLY F 2 155 ? 11.753  44.339  -2.707  1.00 113.53 ? 155 GLY F O   1 
ATOM   11614 N N   . THR F 2 156 ? 10.372  45.196  -4.263  1.00 139.06 ? 156 THR F N   1 
ATOM   11615 C CA  . THR F 2 156 ? 11.066  46.476  -4.339  1.00 143.21 ? 156 THR F CA  1 
ATOM   11616 C C   . THR F 2 156 ? 10.112  47.623  -4.022  1.00 149.31 ? 156 THR F C   1 
ATOM   11617 O O   . THR F 2 156 ? 10.368  48.775  -4.374  1.00 153.87 ? 156 THR F O   1 
ATOM   11618 C CB  . THR F 2 156 ? 11.688  46.695  -5.731  1.00 145.11 ? 156 THR F CB  1 
ATOM   11619 O OG1 . THR F 2 156 ? 10.681  46.530  -6.737  1.00 145.18 ? 156 THR F OG1 1 
ATOM   11620 C CG2 . THR F 2 156 ? 12.808  45.695  -5.980  1.00 144.43 ? 156 THR F CG2 1 
ATOM   11621 N N   . TYR F 2 157 ? 9.012   47.293  -3.351  1.00 123.28 ? 157 TYR F N   1 
ATOM   11622 C CA  . TYR F 2 157 ? 7.984   48.267  -2.998  1.00 119.68 ? 157 TYR F CA  1 
ATOM   11623 C C   . TYR F 2 157 ? 8.572   49.467  -2.279  1.00 113.07 ? 157 TYR F C   1 
ATOM   11624 O O   . TYR F 2 157 ? 9.328   49.322  -1.318  1.00 102.00 ? 157 TYR F O   1 
ATOM   11625 C CB  . TYR F 2 157 ? 6.918   47.616  -2.120  1.00 117.78 ? 157 TYR F CB  1 
ATOM   11626 C CG  . TYR F 2 157 ? 5.808   48.544  -1.671  1.00 116.02 ? 157 TYR F CG  1 
ATOM   11627 C CD1 . TYR F 2 157 ? 4.587   48.567  -2.332  1.00 120.28 ? 157 TYR F CD1 1 
ATOM   11628 C CD2 . TYR F 2 157 ? 5.975   49.381  -0.578  1.00 110.48 ? 157 TYR F CD2 1 
ATOM   11629 C CE1 . TYR F 2 157 ? 3.565   49.399  -1.923  1.00 123.43 ? 157 TYR F CE1 1 
ATOM   11630 C CE2 . TYR F 2 157 ? 4.960   50.222  -0.162  1.00 114.56 ? 157 TYR F CE2 1 
ATOM   11631 C CZ  . TYR F 2 157 ? 3.756   50.227  -0.838  1.00 122.35 ? 157 TYR F CZ  1 
ATOM   11632 O OH  . TYR F 2 157 ? 2.741   51.065  -0.425  1.00 125.61 ? 157 TYR F OH  1 
ATOM   11633 N N   . ASP F 2 158 ? 8.202   50.654  -2.749  1.00 161.82 ? 158 ASP F N   1 
ATOM   11634 C CA  . ASP F 2 158 ? 8.680   51.901  -2.172  1.00 164.65 ? 158 ASP F CA  1 
ATOM   11635 C C   . ASP F 2 158 ? 7.757   52.366  -1.047  1.00 159.94 ? 158 ASP F C   1 
ATOM   11636 O O   . ASP F 2 158 ? 6.688   52.928  -1.297  1.00 161.45 ? 158 ASP F O   1 
ATOM   11637 C CB  . ASP F 2 158 ? 8.780   52.979  -3.254  1.00 170.35 ? 158 ASP F CB  1 
ATOM   11638 C CG  . ASP F 2 158 ? 9.565   54.193  -2.800  1.00 165.33 ? 158 ASP F CG  1 
ATOM   11639 O OD1 . ASP F 2 158 ? 10.494  54.028  -1.982  1.00 159.29 ? 158 ASP F OD1 1 
ATOM   11640 O OD2 . ASP F 2 158 ? 9.257   55.310  -3.264  1.00 165.09 ? 158 ASP F OD2 1 
ATOM   11641 N N   . TYR F 2 159 ? 8.173   52.119  0.192   1.00 135.22 ? 159 TYR F N   1 
ATOM   11642 C CA  . TYR F 2 159 ? 7.404   52.536  1.363   1.00 129.19 ? 159 TYR F CA  1 
ATOM   11643 C C   . TYR F 2 159 ? 7.247   54.055  1.463   1.00 130.77 ? 159 TYR F C   1 
ATOM   11644 O O   . TYR F 2 159 ? 6.150   54.545  1.738   1.00 134.84 ? 159 TYR F O   1 
ATOM   11645 C CB  . TYR F 2 159 ? 8.023   51.972  2.649   1.00 118.05 ? 159 TYR F CB  1 
ATOM   11646 C CG  . TYR F 2 159 ? 7.480   52.581  3.926   1.00 108.94 ? 159 TYR F CG  1 
ATOM   11647 C CD1 . TYR F 2 159 ? 6.168   52.357  4.327   1.00 103.91 ? 159 TYR F CD1 1 
ATOM   11648 C CD2 . TYR F 2 159 ? 8.285   53.365  4.738   1.00 104.93 ? 159 TYR F CD2 1 
ATOM   11649 C CE1 . TYR F 2 159 ? 5.673   52.907  5.497   1.00 98.74  ? 159 TYR F CE1 1 
ATOM   11650 C CE2 . TYR F 2 159 ? 7.798   53.922  5.907   1.00 102.82 ? 159 TYR F CE2 1 
ATOM   11651 C CZ  . TYR F 2 159 ? 6.492   53.691  6.284   1.00 100.57 ? 159 TYR F CZ  1 
ATOM   11652 O OH  . TYR F 2 159 ? 6.014   54.247  7.451   1.00 98.93  ? 159 TYR F OH  1 
ATOM   11653 N N   . PRO F 2 160 ? 8.345   54.806  1.247   1.00 114.70 ? 160 PRO F N   1 
ATOM   11654 C CA  . PRO F 2 160 ? 8.279   56.273  1.300   1.00 114.51 ? 160 PRO F CA  1 
ATOM   11655 C C   . PRO F 2 160 ? 7.291   56.859  0.291   1.00 122.51 ? 160 PRO F C   1 
ATOM   11656 O O   . PRO F 2 160 ? 6.751   57.943  0.514   1.00 121.84 ? 160 PRO F O   1 
ATOM   11657 C CB  . PRO F 2 160 ? 9.707   56.696  0.940   1.00 110.55 ? 160 PRO F CB  1 
ATOM   11658 C CG  . PRO F 2 160 ? 10.556  55.539  1.338   1.00 107.55 ? 160 PRO F CG  1 
ATOM   11659 C CD  . PRO F 2 160 ? 9.725   54.326  1.044   1.00 110.53 ? 160 PRO F CD  1 
ATOM   11660 N N   . LYS F 2 161 ? 7.059   56.138  -0.800  1.00 144.66 ? 161 LYS F N   1 
ATOM   11661 C CA  . LYS F 2 161 ? 6.199   56.609  -1.883  1.00 149.80 ? 161 LYS F CA  1 
ATOM   11662 C C   . LYS F 2 161 ? 4.761   56.908  -1.448  1.00 154.34 ? 161 LYS F C   1 
ATOM   11663 O O   . LYS F 2 161 ? 4.153   57.873  -1.915  1.00 159.44 ? 161 LYS F O   1 
ATOM   11664 C CB  . LYS F 2 161 ? 6.199   55.589  -3.025  1.00 152.14 ? 161 LYS F CB  1 
ATOM   11665 C CG  . LYS F 2 161 ? 5.359   55.986  -4.225  1.00 160.52 ? 161 LYS F CG  1 
ATOM   11666 C CD  . LYS F 2 161 ? 5.511   54.977  -5.352  1.00 167.20 ? 161 LYS F CD  1 
ATOM   11667 C CE  . LYS F 2 161 ? 6.969   54.823  -5.763  1.00 168.59 ? 161 LYS F CE  1 
ATOM   11668 N NZ  . LYS F 2 161 ? 7.558   56.107  -6.233  1.00 170.58 ? 161 LYS F NZ  1 
ATOM   11669 N N   . TYR F 2 162 ? 4.219   56.081  -0.559  1.00 117.66 ? 162 TYR F N   1 
ATOM   11670 C CA  . TYR F 2 162 ? 2.821   56.208  -0.152  1.00 118.87 ? 162 TYR F CA  1 
ATOM   11671 C C   . TYR F 2 162 ? 2.671   56.542  1.332   1.00 108.89 ? 162 TYR F C   1 
ATOM   11672 O O   . TYR F 2 162 ? 1.578   56.436  1.889   1.00 103.89 ? 162 TYR F O   1 
ATOM   11673 C CB  . TYR F 2 162 ? 2.060   54.916  -0.463  1.00 124.76 ? 162 TYR F CB  1 
ATOM   11674 C CG  . TYR F 2 162 ? 2.021   54.534  -1.930  1.00 132.66 ? 162 TYR F CG  1 
ATOM   11675 C CD1 . TYR F 2 162 ? 1.014   55.005  -2.762  1.00 140.48 ? 162 TYR F CD1 1 
ATOM   11676 C CD2 . TYR F 2 162 ? 2.982   53.693  -2.477  1.00 132.36 ? 162 TYR F CD2 1 
ATOM   11677 C CE1 . TYR F 2 162 ? 0.965   54.653  -4.098  1.00 146.42 ? 162 TYR F CE1 1 
ATOM   11678 C CE2 . TYR F 2 162 ? 2.942   53.339  -3.815  1.00 139.11 ? 162 TYR F CE2 1 
ATOM   11679 C CZ  . TYR F 2 162 ? 1.931   53.822  -4.620  1.00 145.18 ? 162 TYR F CZ  1 
ATOM   11680 O OH  . TYR F 2 162 ? 1.882   53.475  -5.951  1.00 148.66 ? 162 TYR F OH  1 
ATOM   11681 N N   . GLU F 2 163 ? 3.767   56.946  1.965   1.00 123.37 ? 163 GLU F N   1 
ATOM   11682 C CA  . GLU F 2 163 ? 3.776   57.203  3.404   1.00 122.11 ? 163 GLU F CA  1 
ATOM   11683 C C   . GLU F 2 163 ? 2.747   58.248  3.835   1.00 126.25 ? 163 GLU F C   1 
ATOM   11684 O O   . GLU F 2 163 ? 1.771   57.927  4.512   1.00 125.24 ? 163 GLU F O   1 
ATOM   11685 C CB  . GLU F 2 163 ? 5.178   57.612  3.871   1.00 116.80 ? 163 GLU F CB  1 
ATOM   11686 C CG  . GLU F 2 163 ? 5.285   57.888  5.366   1.00 112.41 ? 163 GLU F CG  1 
ATOM   11687 C CD  . GLU F 2 163 ? 6.722   57.895  5.861   1.00 109.78 ? 163 GLU F CD  1 
ATOM   11688 O OE1 . GLU F 2 163 ? 7.646   57.783  5.027   1.00 109.56 ? 163 GLU F OE1 1 
ATOM   11689 O OE2 . GLU F 2 163 ? 6.928   58.006  7.088   1.00 108.37 ? 163 GLU F OE2 1 
ATOM   11690 N N   . GLU F 2 164 ? 2.977   59.497  3.440   1.00 159.30 ? 164 GLU F N   1 
ATOM   11691 C CA  . GLU F 2 164 ? 2.113   60.604  3.835   1.00 158.56 ? 164 GLU F CA  1 
ATOM   11692 C C   . GLU F 2 164 ? 0.709   60.456  3.254   1.00 155.20 ? 164 GLU F C   1 
ATOM   11693 O O   . GLU F 2 164 ? -0.288  60.632  3.958   1.00 153.13 ? 164 GLU F O   1 
ATOM   11694 C CB  . GLU F 2 164 ? 2.728   61.939  3.405   1.00 163.38 ? 164 GLU F CB  1 
ATOM   11695 C CG  . GLU F 2 164 ? 4.150   62.165  3.912   1.00 162.48 ? 164 GLU F CG  1 
ATOM   11696 C CD  . GLU F 2 164 ? 4.222   62.305  5.422   1.00 161.34 ? 164 GLU F CD  1 
ATOM   11697 O OE1 . GLU F 2 164 ? 3.183   62.617  6.041   1.00 164.54 ? 164 GLU F OE1 1 
ATOM   11698 O OE2 . GLU F 2 164 ? 5.316   62.100  5.990   1.00 156.48 ? 164 GLU F OE2 1 
ATOM   11699 N N   . GLU F 2 165 ? 0.640   60.133  1.965   1.00 98.53  ? 165 GLU F N   1 
ATOM   11700 C CA  . GLU F 2 165 ? -0.638  59.944  1.284   1.00 99.56  ? 165 GLU F CA  1 
ATOM   11701 C C   . GLU F 2 165 ? -1.570  59.047  2.092   1.00 97.80  ? 165 GLU F C   1 
ATOM   11702 O O   . GLU F 2 165 ? -2.785  59.252  2.119   1.00 91.92  ? 165 GLU F O   1 
ATOM   11703 C CB  . GLU F 2 165 ? -0.412  59.345  -0.106  1.00 100.06 ? 165 GLU F CB  1 
ATOM   11704 C CG  . GLU F 2 165 ? -1.690  58.957  -0.837  1.00 105.23 ? 165 GLU F CG  1 
ATOM   11705 C CD  . GLU F 2 165 ? -1.416  58.372  -2.214  1.00 108.31 ? 165 GLU F CD  1 
ATOM   11706 O OE1 . GLU F 2 165 ? -0.233  58.339  -2.625  1.00 106.06 ? 165 GLU F OE1 1 
ATOM   11707 O OE2 . GLU F 2 165 ? -2.384  57.944  -2.883  1.00 112.00 ? 165 GLU F OE2 1 
ATOM   11708 N N   . SER F 2 166 ? -0.980  58.058  2.756   1.00 104.41 ? 166 SER F N   1 
ATOM   11709 C CA  . SER F 2 166 ? -1.742  57.081  3.520   1.00 104.53 ? 166 SER F CA  1 
ATOM   11710 C C   . SER F 2 166 ? -1.748  57.391  5.021   1.00 103.19 ? 166 SER F C   1 
ATOM   11711 O O   . SER F 2 166 ? -2.742  57.141  5.707   1.00 101.94 ? 166 SER F O   1 
ATOM   11712 C CB  . SER F 2 166 ? -1.212  55.669  3.250   1.00 102.09 ? 166 SER F CB  1 
ATOM   11713 O OG  . SER F 2 166 ? -1.421  55.293  1.896   1.00 105.23 ? 166 SER F OG  1 
ATOM   11714 N N   . LYS F 2 167 ? -0.649  57.942  5.531   1.00 140.46 ? 167 LYS F N   1 
ATOM   11715 C CA  . LYS F 2 167 ? -0.609  58.366  6.928   1.00 137.96 ? 167 LYS F CA  1 
ATOM   11716 C C   . LYS F 2 167 ? -1.704  59.402  7.146   1.00 134.41 ? 167 LYS F C   1 
ATOM   11717 O O   . LYS F 2 167 ? -2.026  59.764  8.279   1.00 131.17 ? 167 LYS F O   1 
ATOM   11718 C CB  . LYS F 2 167 ? 0.762   58.943  7.307   1.00 134.53 ? 167 LYS F CB  1 
ATOM   11719 C CG  . LYS F 2 167 ? 0.815   60.469  7.368   1.00 135.95 ? 167 LYS F CG  1 
ATOM   11720 C CD  . LYS F 2 167 ? 1.592   60.971  8.590   1.00 129.78 ? 167 LYS F CD  1 
ATOM   11721 C CE  . LYS F 2 167 ? 3.077   60.650  8.496   1.00 123.23 ? 167 LYS F CE  1 
ATOM   11722 N NZ  . LYS F 2 167 ? 3.847   61.197  9.649   1.00 118.96 ? 167 LYS F NZ  1 
ATOM   11723 N N   . LEU F 2 168 ? -2.269  59.872  6.038   1.00 85.31  ? 168 LEU F N   1 
ATOM   11724 C CA  . LEU F 2 168 ? -3.384  60.801  6.067   1.00 89.91  ? 168 LEU F CA  1 
ATOM   11725 C C   . LEU F 2 168 ? -4.696  60.031  6.203   1.00 92.02  ? 168 LEU F C   1 
ATOM   11726 O O   . LEU F 2 168 ? -5.555  60.387  7.014   1.00 88.53  ? 168 LEU F O   1 
ATOM   11727 C CB  . LEU F 2 168 ? -3.384  61.656  4.794   1.00 92.18  ? 168 LEU F CB  1 
ATOM   11728 C CG  . LEU F 2 168 ? -3.684  63.160  4.925   1.00 86.99  ? 168 LEU F CG  1 
ATOM   11729 C CD1 . LEU F 2 168 ? -2.848  63.962  3.932   1.00 83.21  ? 168 LEU F CD1 1 
ATOM   11730 C CD2 . LEU F 2 168 ? -5.175  63.452  4.752   1.00 93.01  ? 168 LEU F CD2 1 
ATOM   11731 N N   . ASN F 2 169 ? -4.839  58.970  5.412   1.00 116.30 ? 169 ASN F N   1 
ATOM   11732 C CA  . ASN F 2 169 ? -6.026  58.119  5.478   1.00 125.29 ? 169 ASN F CA  1 
ATOM   11733 C C   . ASN F 2 169 ? -6.122  57.348  6.790   1.00 127.43 ? 169 ASN F C   1 
ATOM   11734 O O   . ASN F 2 169 ? -7.188  56.848  7.150   1.00 133.27 ? 169 ASN F O   1 
ATOM   11735 C CB  . ASN F 2 169 ? -6.066  57.138  4.304   1.00 128.79 ? 169 ASN F CB  1 
ATOM   11736 C CG  . ASN F 2 169 ? -6.404  57.809  2.991   1.00 139.00 ? 169 ASN F CG  1 
ATOM   11737 O OD1 . ASN F 2 169 ? -5.776  58.795  2.604   1.00 143.12 ? 169 ASN F OD1 1 
ATOM   11738 N ND2 . ASN F 2 169 ? -7.409  57.280  2.298   1.00 143.98 ? 169 ASN F ND2 1 
ATOM   11739 N N   . ARG F 2 170 ? -5.001  57.250  7.497   1.00 133.96 ? 170 ARG F N   1 
ATOM   11740 C CA  . ARG F 2 170 ? -4.944  56.518  8.758   1.00 128.53 ? 170 ARG F CA  1 
ATOM   11741 C C   . ARG F 2 170 ? -5.387  57.397  9.924   1.00 128.18 ? 170 ARG F C   1 
ATOM   11742 O O   . ARG F 2 170 ? -6.213  56.994  10.744  1.00 130.61 ? 170 ARG F O   1 
ATOM   11743 C CB  . ARG F 2 170 ? -3.526  55.991  8.994   1.00 118.96 ? 170 ARG F CB  1 
ATOM   11744 C CG  . ARG F 2 170 ? -3.372  55.068  10.197  1.00 110.91 ? 170 ARG F CG  1 
ATOM   11745 C CD  . ARG F 2 170 ? -2.137  54.180  10.056  1.00 100.23 ? 170 ARG F CD  1 
ATOM   11746 N NE  . ARG F 2 170 ? -0.882  54.933  10.086  1.00 96.08  ? 170 ARG F NE  1 
ATOM   11747 C CZ  . ARG F 2 170 ? -0.288  55.457  9.015   1.00 96.21  ? 170 ARG F CZ  1 
ATOM   11748 N NH1 . ARG F 2 170 ? -0.833  55.321  7.815   1.00 103.70 ? 170 ARG F NH1 1 
ATOM   11749 N NH2 . ARG F 2 170 ? 0.854   56.120  9.144   1.00 89.28  ? 170 ARG F NH2 1 
ATOM   11750 N N   . ASN F 2 171 ? -4.833  58.603  9.985   1.00 118.41 ? 171 ASN F N   1 
ATOM   11751 C CA  . ASN F 2 171 ? -5.162  59.550  11.040  1.00 118.39 ? 171 ASN F CA  1 
ATOM   11752 C C   . ASN F 2 171 ? -6.378  60.396  10.669  1.00 122.43 ? 171 ASN F C   1 
ATOM   11753 O O   . ASN F 2 171 ? -6.264  61.379  9.936   1.00 123.33 ? 171 ASN F O   1 
ATOM   11754 C CB  . ASN F 2 171 ? -3.952  60.438  11.344  1.00 114.84 ? 171 ASN F CB  1 
ATOM   11755 C CG  . ASN F 2 171 ? -2.717  59.634  11.733  1.00 108.71 ? 171 ASN F CG  1 
ATOM   11756 O OD1 . ASN F 2 171 ? -2.777  58.762  12.602  1.00 105.27 ? 171 ASN F OD1 1 
ATOM   11757 N ND2 . ASN F 2 171 ? -1.593  59.922  11.082  1.00 105.84 ? 171 ASN F ND2 1 
ATOM   11758 N N   . GLU F 2 172 ? -7.544  59.997  11.169  1.00 118.78 ? 172 GLU F N   1 
ATOM   11759 C CA  . GLU F 2 172 ? -8.793  60.700  10.886  1.00 122.97 ? 172 GLU F CA  1 
ATOM   11760 C C   . GLU F 2 172 ? -9.470  61.176  12.169  1.00 118.57 ? 172 GLU F C   1 
ATOM   11761 O O   . GLU F 2 172 ? -10.183 62.180  12.172  1.00 114.19 ? 172 GLU F O   1 
ATOM   11762 C CB  . GLU F 2 172 ? -9.750  59.805  10.090  1.00 130.65 ? 172 GLU F CB  1 
ATOM   11763 C CG  . GLU F 2 172 ? -9.395  59.658  8.617   1.00 134.59 ? 172 GLU F CG  1 
ATOM   11764 C CD  . GLU F 2 172 ? -9.816  60.860  7.789   1.00 140.32 ? 172 GLU F CD  1 
ATOM   11765 O OE1 . GLU F 2 172 ? -9.044  61.270  6.896   1.00 144.26 ? 172 GLU F OE1 1 
ATOM   11766 O OE2 . GLU F 2 172 ? -10.923 61.388  8.027   1.00 139.43 ? 172 GLU F OE2 1 
HETATM 11767 C C1  . NAG G 3 .   ? 1.233   17.454  43.089  1.00 172.86 ? 330 NAG A C1  1 
HETATM 11768 C C2  . NAG G 3 .   ? 1.354   16.606  44.351  1.00 180.45 ? 330 NAG A C2  1 
HETATM 11769 C C3  . NAG G 3 .   ? 0.438   15.390  44.300  1.00 186.70 ? 330 NAG A C3  1 
HETATM 11770 C C4  . NAG G 3 .   ? -0.970  15.799  43.896  1.00 192.09 ? 330 NAG A C4  1 
HETATM 11771 C C5  . NAG G 3 .   ? -0.940  16.648  42.631  1.00 185.08 ? 330 NAG A C5  1 
HETATM 11772 C C6  . NAG G 3 .   ? -2.340  17.115  42.251  1.00 189.07 ? 330 NAG A C6  1 
HETATM 11773 C C7  . NAG G 3 .   ? 3.384   16.445  45.670  1.00 175.43 ? 330 NAG A C7  1 
HETATM 11774 C C8  . NAG G 3 .   ? 4.307   15.372  46.169  1.00 172.51 ? 330 NAG A C8  1 
HETATM 11775 N N2  . NAG G 3 .   ? 2.729   16.185  44.541  1.00 174.03 ? 330 NAG A N2  1 
HETATM 11776 O O3  . NAG G 3 .   ? 0.402   14.776  45.568  1.00 193.93 ? 330 NAG A O3  1 
HETATM 11777 O O4  . NAG G 3 .   ? -1.750  14.645  43.676  1.00 194.69 ? 330 NAG A O4  1 
HETATM 11778 O O5  . NAG G 3 .   ? -0.115  17.777  42.824  1.00 180.84 ? 330 NAG A O5  1 
HETATM 11779 O O6  . NAG G 3 .   ? -2.266  17.917  41.093  1.00 182.40 ? 330 NAG A O6  1 
HETATM 11780 O O7  . NAG G 3 .   ? 3.258   17.500  46.292  1.00 179.21 ? 330 NAG A O7  1 
HETATM 11781 C C1  . NAG H 3 .   ? 0.144   -51.279 7.002   1.00 94.13  ? 331 NAG A C1  1 
HETATM 11782 C C2  . NAG H 3 .   ? 0.363   -51.994 5.677   1.00 99.81  ? 331 NAG A C2  1 
HETATM 11783 C C3  . NAG H 3 .   ? -0.341  -51.252 4.553   1.00 103.89 ? 331 NAG A C3  1 
HETATM 11784 C C4  . NAG H 3 .   ? -1.824  -51.298 4.863   1.00 114.90 ? 331 NAG A C4  1 
HETATM 11785 C C5  . NAG H 3 .   ? -2.084  -50.654 6.221   1.00 112.53 ? 331 NAG A C5  1 
HETATM 11786 C C6  . NAG H 3 .   ? -3.539  -50.858 6.623   1.00 122.30 ? 331 NAG A C6  1 
HETATM 11787 C C7  . NAG H 3 .   ? 2.330   -53.352 5.314   1.00 90.34  ? 331 NAG A C7  1 
HETATM 11788 C C8  . NAG H 3 .   ? 3.828   -53.408 5.406   1.00 86.38  ? 331 NAG A C8  1 
HETATM 11789 N N2  . NAG H 3 .   ? 1.775   -52.148 5.402   1.00 95.79  ? 331 NAG A N2  1 
HETATM 11790 O O3  . NAG H 3 .   ? -0.066  -51.862 3.307   1.00 99.36  ? 331 NAG A O3  1 
HETATM 11791 O O4  . NAG H 3 .   ? -2.546  -50.626 3.866   1.00 127.36 ? 331 NAG A O4  1 
HETATM 11792 O O5  . NAG H 3 .   ? -1.257  -51.209 7.245   1.00 102.62 ? 331 NAG A O5  1 
HETATM 11793 O O6  . NAG H 3 .   ? -3.680  -52.129 7.218   1.00 125.70 ? 331 NAG A O6  1 
HETATM 11794 O O7  . NAG H 3 .   ? 1.654   -54.368 5.161   1.00 85.50  ? 331 NAG A O7  1 
HETATM 11795 C C1  . NAG I 3 .   ? 43.376  6.813   20.826  1.00 132.70 ? 331 NAG C C1  1 
HETATM 11796 C C2  . NAG I 3 .   ? 44.887  6.849   21.029  1.00 140.80 ? 331 NAG C C2  1 
HETATM 11797 C C3  . NAG I 3 .   ? 45.307  7.886   22.061  1.00 145.61 ? 331 NAG C C3  1 
HETATM 11798 C C4  . NAG I 3 .   ? 44.606  9.220   21.841  1.00 137.45 ? 331 NAG C C4  1 
HETATM 11799 C C5  . NAG I 3 .   ? 43.110  8.995   21.684  1.00 135.76 ? 331 NAG C C5  1 
HETATM 11800 C C6  . NAG I 3 .   ? 42.408  10.314  21.393  1.00 136.14 ? 331 NAG C C6  1 
HETATM 11801 C C7  . NAG I 3 .   ? 46.482  5.024   20.972  1.00 150.56 ? 331 NAG C C7  1 
HETATM 11802 C C8  . NAG I 3 .   ? 47.073  3.905   21.771  1.00 152.15 ? 331 NAG C C8  1 
HETATM 11803 N N2  . NAG I 3 .   ? 45.359  5.546   21.459  1.00 147.21 ? 331 NAG C N2  1 
HETATM 11804 O O3  . NAG I 3 .   ? 46.702  8.066   21.972  1.00 153.61 ? 331 NAG C O3  1 
HETATM 11805 O O4  . NAG I 3 .   ? 44.829  10.062  22.953  1.00 130.64 ? 331 NAG C O4  1 
HETATM 11806 O O5  . NAG I 3 .   ? 42.841  8.102   20.630  1.00 132.76 ? 331 NAG C O5  1 
HETATM 11807 O O6  . NAG I 3 .   ? 41.140  10.055  20.826  1.00 129.69 ? 331 NAG C O6  1 
HETATM 11808 O O7  . NAG I 3 .   ? 47.025  5.415   19.939  1.00 151.86 ? 331 NAG C O7  1 
HETATM 11809 O O   . HOH J 4 .   ? 18.830  -31.853 27.416  1.00 44.00  ? 1   HOH A O   1 
HETATM 11810 O O   . HOH J 4 .   ? 11.196  -45.066 21.644  1.00 45.92  ? 2   HOH A O   1 
HETATM 11811 O O   . HOH J 4 .   ? 20.183  -40.803 36.297  1.00 50.43  ? 3   HOH A O   1 
HETATM 11812 O O   . HOH J 4 .   ? 22.410  -29.302 28.994  1.00 48.28  ? 5   HOH A O   1 
HETATM 11813 O O   . HOH J 4 .   ? 16.089  -54.456 29.399  1.00 32.41  ? 6   HOH A O   1 
HETATM 11814 O O   . HOH J 4 .   ? 24.238  -67.263 19.437  1.00 51.70  ? 332 HOH A O   1 
HETATM 11815 O O   . HOH J 4 .   ? 13.335  10.221  27.487  1.00 69.42  ? 333 HOH A O   1 
HETATM 11816 O O   . HOH J 4 .   ? 27.439  -40.431 18.993  1.00 39.17  ? 334 HOH A O   1 
HETATM 11817 O O   . HOH J 4 .   ? 22.565  -46.433 16.345  1.00 45.02  ? 335 HOH A O   1 
HETATM 11818 O O   . HOH J 4 .   ? 24.260  -35.362 16.313  1.00 62.02  ? 336 HOH A O   1 
HETATM 11819 O O   . HOH J 4 .   ? 27.728  -42.873 14.773  1.00 49.38  ? 337 HOH A O   1 
HETATM 11820 O O   . HOH J 4 .   ? 11.560  -62.710 26.701  1.00 68.05  ? 338 HOH A O   1 
HETATM 11821 O O   . HOH J 4 .   ? 27.121  -39.904 29.307  1.00 44.62  ? 339 HOH A O   1 
HETATM 11822 O O   . HOH J 4 .   ? 22.259  -72.831 18.221  1.00 53.66  ? 340 HOH A O   1 
HETATM 11823 O O   . HOH J 4 .   ? 23.208  -39.928 34.961  1.00 46.10  ? 341 HOH A O   1 
HETATM 11824 O O   . HOH J 4 .   ? 25.698  -40.019 31.946  1.00 52.86  ? 342 HOH A O   1 
HETATM 11825 O O   . HOH J 4 .   ? 22.363  -33.279 9.656   1.00 63.29  ? 343 HOH A O   1 
HETATM 11826 O O   . HOH J 4 .   ? 23.071  -32.782 13.974  1.00 38.77  ? 344 HOH A O   1 
HETATM 11827 O O   . HOH J 4 .   ? 23.167  -35.987 10.359  1.00 65.86  ? 345 HOH A O   1 
HETATM 11828 O O   . HOH J 4 .   ? 17.970  5.183   27.604  1.00 60.72  ? 346 HOH A O   1 
HETATM 11829 O O   . HOH J 4 .   ? 10.901  -54.128 22.139  1.00 38.62  ? 347 HOH A O   1 
HETATM 11830 O O   . HOH J 4 .   ? 21.716  -36.947 29.746  1.00 48.75  ? 348 HOH A O   1 
HETATM 11831 O O   . HOH J 4 .   ? 7.575   -39.290 32.548  1.00 47.97  ? 349 HOH A O   1 
HETATM 11832 O O   . HOH J 4 .   ? 8.143   -44.594 32.685  1.00 42.71  ? 350 HOH A O   1 
HETATM 11833 O O   . HOH J 4 .   ? 8.633   31.486  39.023  1.00 72.12  ? 351 HOH A O   1 
HETATM 11834 O O   . HOH J 4 .   ? 27.719  -37.782 24.828  1.00 42.15  ? 352 HOH A O   1 
HETATM 11835 O O   . HOH J 4 .   ? 16.642  -20.058 28.980  1.00 50.26  ? 353 HOH A O   1 
HETATM 11836 O O   . HOH J 4 .   ? 18.917  -26.583 24.067  1.00 59.95  ? 354 HOH A O   1 
HETATM 11837 O O   . HOH K 4 .   ? 18.490  -27.359 21.387  1.00 57.87  ? 175 HOH B O   1 
HETATM 11838 O O   . HOH K 4 .   ? 29.619  -27.213 12.952  1.00 34.84  ? 176 HOH B O   1 
HETATM 11839 O O   . HOH K 4 .   ? 0.591   48.600  31.158  1.00 59.30  ? 177 HOH B O   1 
HETATM 11840 O O   . HOH L 4 .   ? 48.587  -32.893 20.140  1.00 55.47  ? 4   HOH C O   1 
HETATM 11841 O O   . HOH L 4 .   ? 44.540  -52.109 -2.931  1.00 42.68  ? 332 HOH C O   1 
HETATM 11842 O O   . HOH L 4 .   ? 27.292  10.142  2.321   1.00 55.66  ? 333 HOH C O   1 
HETATM 11843 O O   . HOH L 4 .   ? 41.162  5.278   13.760  1.00 56.02  ? 334 HOH C O   1 
HETATM 11844 O O   . HOH L 4 .   ? 37.359  -29.298 8.500   1.00 71.20  ? 335 HOH C O   1 
HETATM 11845 O O   . HOH L 4 .   ? 31.834  -45.298 11.443  1.00 58.09  ? 336 HOH C O   1 
HETATM 11846 O O   . HOH L 4 .   ? 34.273  -46.370 12.624  1.00 42.59  ? 337 HOH C O   1 
HETATM 11847 O O   . HOH L 4 .   ? 57.554  -45.929 14.589  1.00 43.87  ? 338 HOH C O   1 
HETATM 11848 O O   . HOH L 4 .   ? 26.424  40.256  2.346   1.00 75.35  ? 339 HOH C O   1 
HETATM 11849 O O   . HOH M 4 .   ? 28.082  -16.051 -0.335  1.00 37.65  ? 175 HOH D O   1 
HETATM 11850 O O   . HOH M 4 .   ? 27.701  -27.156 8.778   1.00 26.78  ? 176 HOH D O   1 
HETATM 11851 O O   . HOH M 4 .   ? 16.099  52.309  32.788  1.00 37.91  ? 177 HOH D O   1 
HETATM 11852 O O   . HOH M 4 .   ? 27.468  49.172  23.246  1.00 65.61  ? 178 HOH D O   1 
HETATM 11853 O O   . HOH M 4 .   ? 26.379  -27.283 5.611   1.00 59.19  ? 179 HOH D O   1 
HETATM 11854 O O   . HOH M 4 .   ? 23.476  57.720  33.816  1.00 56.61  ? 180 HOH D O   1 
HETATM 11855 O O   . HOH M 4 .   ? 16.878  51.421  29.716  1.00 52.28  ? 181 HOH D O   1 
HETATM 11856 O O   . HOH N 4 .   ? 22.806  -41.185 1.997   1.00 45.78  ? 7   HOH E O   1 
HETATM 11857 O O   . HOH N 4 .   ? 28.900  -35.474 -1.183  1.00 53.56  ? 330 HOH E O   1 
HETATM 11858 O O   . HOH N 4 .   ? 37.952  -34.201 -5.111  1.00 56.05  ? 331 HOH E O   1 
HETATM 11859 O O   . HOH N 4 .   ? 13.355  -6.888  3.633   1.00 45.65  ? 332 HOH E O   1 
HETATM 11860 O O   . HOH O 4 .   ? 7.025   -16.715 13.510  1.00 52.50  ? 175 HOH F O   1 
HETATM 11861 O O   . HOH O 4 .   ? 21.753  -30.560 12.274  1.00 40.48  ? 176 HOH F O   1 
HETATM 11862 O O   . HOH O 4 .   ? 24.111  -28.287 8.304   1.00 66.37  ? 177 HOH F O   1 
HETATM 11863 O O   . HOH O 4 .   ? 20.677  -32.856 6.663   1.00 51.63  ? 178 HOH F O   1 
HETATM 11864 O O   . HOH O 4 .   ? 7.524   31.811  11.286  1.00 50.09  ? 179 HOH F 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   PRO 1   9   9   PRO PRO A . n 
A 1 2   GLY 2   10  10  GLY GLY A . n 
A 1 3   ASP 3   11  11  ASP ASP A . n 
A 1 4   GLN 4   12  12  GLN GLN A . n 
A 1 5   ILE 5   13  13  ILE ILE A . n 
A 1 6   CYS 6   14  14  CYS CYS A . n 
A 1 7   ILE 7   15  15  ILE ILE A . n 
A 1 8   GLY 8   16  16  GLY GLY A . n 
A 1 9   TYR 9   17  17  TYR TYR A . n 
A 1 10  HIS 10  18  18  HIS HIS A . n 
A 1 11  ALA 11  19  19  ALA ALA A . n 
A 1 12  ASN 12  20  20  ASN ASN A . n 
A 1 13  ASN 13  21  21  ASN ASN A . n 
A 1 14  SER 14  22  22  SER SER A . n 
A 1 15  THR 15  23  23  THR THR A . n 
A 1 16  GLU 16  24  24  GLU GLU A . n 
A 1 17  LYS 17  25  25  LYS LYS A . n 
A 1 18  VAL 18  26  26  VAL VAL A . n 
A 1 19  ASP 19  27  27  ASP ASP A . n 
A 1 20  THR 20  28  28  THR THR A . n 
A 1 21  ILE 21  29  29  ILE ILE A . n 
A 1 22  LEU 22  30  30  LEU LEU A . n 
A 1 23  GLU 23  31  31  GLU GLU A . n 
A 1 24  ARG 24  32  32  ARG ARG A . n 
A 1 25  ASN 25  33  33  ASN ASN A . n 
A 1 26  VAL 26  34  34  VAL VAL A . n 
A 1 27  THR 27  35  35  THR THR A . n 
A 1 28  VAL 28  36  36  VAL VAL A . n 
A 1 29  THR 29  37  37  THR THR A . n 
A 1 30  HIS 30  38  38  HIS HIS A . n 
A 1 31  ALA 31  39  39  ALA ALA A . n 
A 1 32  LYS 32  40  40  LYS LYS A . n 
A 1 33  ASP 33  41  41  ASP ASP A . n 
A 1 34  ILE 34  42  42  ILE ILE A . n 
A 1 35  LEU 35  43  43  LEU LEU A . n 
A 1 36  GLU 36  44  44  GLU GLU A . n 
A 1 37  LYS 37  45  45  LYS LYS A . n 
A 1 38  THR 38  46  46  THR THR A . n 
A 1 39  HIS 39  47  47  HIS HIS A . n 
A 1 40  ASN 40  48  48  ASN ASN A . n 
A 1 41  GLY 41  49  49  GLY GLY A . n 
A 1 42  LYS 42  50  50  LYS LYS A . n 
A 1 43  LEU 43  51  51  LEU LEU A . n 
A 1 44  CYS 44  52  52  CYS CYS A . n 
A 1 45  LYS 45  53  53  LYS LYS A . n 
A 1 46  LEU 46  53  53  LEU LEU A A n 
A 1 47  ASN 47  54  54  ASN ASN A . n 
A 1 48  GLY 48  55  55  GLY GLY A . n 
A 1 49  ILE 49  56  56  ILE ILE A . n 
A 1 50  PRO 50  57  57  PRO PRO A . n 
A 1 51  PRO 51  58  58  PRO PRO A . n 
A 1 52  LEU 52  59  59  LEU LEU A . n 
A 1 53  GLU 53  60  60  GLU GLU A . n 
A 1 54  LEU 54  61  61  LEU LEU A . n 
A 1 55  GLY 55  62  62  GLY GLY A . n 
A 1 56  ASP 56  63  63  ASP ASP A . n 
A 1 57  CYS 57  64  64  CYS CYS A . n 
A 1 58  SER 58  65  65  SER SER A . n 
A 1 59  ILE 59  66  66  ILE ILE A . n 
A 1 60  ALA 60  67  67  ALA ALA A . n 
A 1 61  GLY 61  68  68  GLY GLY A . n 
A 1 62  TRP 62  69  69  TRP TRP A . n 
A 1 63  LEU 63  70  70  LEU LEU A . n 
A 1 64  LEU 64  71  71  LEU LEU A . n 
A 1 65  GLY 65  72  72  GLY GLY A . n 
A 1 66  ASN 66  73  73  ASN ASN A . n 
A 1 67  PRO 67  74  74  PRO PRO A . n 
A 1 68  GLU 68  75  75  GLU GLU A . n 
A 1 69  CYS 69  76  76  CYS CYS A . n 
A 1 70  ASP 70  77  77  ASP ASP A . n 
A 1 71  ARG 71  78  78  ARG ARG A . n 
A 1 72  LEU 72  79  79  LEU LEU A . n 
A 1 73  LEU 73  80  80  LEU LEU A . n 
A 1 74  SER 74  81  81  SER SER A . n 
A 1 75  VAL 75  81  81  VAL VAL A A n 
A 1 76  PRO 76  82  82  PRO PRO A . n 
A 1 77  GLU 77  83  83  GLU GLU A . n 
A 1 78  TRP 78  84  84  TRP TRP A . n 
A 1 79  SER 79  85  85  SER SER A . n 
A 1 80  TYR 80  86  86  TYR TYR A . n 
A 1 81  ILE 81  87  87  ILE ILE A . n 
A 1 82  MET 82  88  88  MET MET A . n 
A 1 83  GLU 83  89  89  GLU GLU A . n 
A 1 84  LYS 84  90  90  LYS LYS A . n 
A 1 85  GLU 85  91  91  GLU GLU A . n 
A 1 86  ASN 86  92  92  ASN ASN A . n 
A 1 87  PRO 87  93  93  PRO PRO A . n 
A 1 88  ARG 88  94  94  ARG ARG A . n 
A 1 89  ASP 89  95  95  ASP ASP A . n 
A 1 90  GLY 90  95  95  GLY GLY A A n 
A 1 91  LEU 91  96  96  LEU LEU A . n 
A 1 92  CYS 92  97  97  CYS CYS A . n 
A 1 93  TYR 93  98  98  TYR TYR A . n 
A 1 94  PRO 94  99  99  PRO PRO A . n 
A 1 95  GLY 95  100 100 GLY GLY A . n 
A 1 96  SER 96  101 101 SER SER A . n 
A 1 97  PHE 97  102 102 PHE PHE A . n 
A 1 98  ASN 98  103 103 ASN ASN A . n 
A 1 99  ASP 99  104 104 ASP ASP A . n 
A 1 100 TYR 100 105 105 TYR TYR A . n 
A 1 101 GLU 101 106 106 GLU GLU A . n 
A 1 102 GLU 102 107 107 GLU GLU A . n 
A 1 103 LEU 103 108 108 LEU LEU A . n 
A 1 104 LYS 104 109 109 LYS LYS A . n 
A 1 105 HIS 105 110 110 HIS HIS A . n 
A 1 106 LEU 106 111 111 LEU LEU A . n 
A 1 107 LEU 107 112 112 LEU LEU A . n 
A 1 108 SER 108 113 113 SER SER A . n 
A 1 109 SER 109 114 114 SER SER A . n 
A 1 110 VAL 110 115 115 VAL VAL A . n 
A 1 111 LYS 111 116 116 LYS LYS A . n 
A 1 112 HIS 112 116 116 HIS HIS A A n 
A 1 113 PHE 113 116 116 PHE PHE A B n 
A 1 114 GLU 114 116 116 GLU GLU A C n 
A 1 115 LYS 115 117 117 LYS LYS A . n 
A 1 116 VAL 116 118 118 VAL VAL A . n 
A 1 117 LYS 117 119 119 LYS LYS A . n 
A 1 118 ILE 118 120 120 ILE ILE A . n 
A 1 119 LEU 119 121 121 LEU LEU A . n 
A 1 120 PRO 120 122 122 PRO PRO A . n 
A 1 121 LYS 121 123 123 LYS LYS A . n 
A 1 122 ASP 122 125 125 ASP ASP A . n 
A 1 123 ARG 123 126 126 ARG ARG A . n 
A 1 124 TRP 124 127 127 TRP TRP A . n 
A 1 125 THR 125 128 128 THR THR A . n 
A 1 126 GLN 126 129 129 GLN GLN A . n 
A 1 127 HIS 127 130 130 HIS HIS A . n 
A 1 128 THR 128 131 131 THR THR A . n 
A 1 129 THR 129 132 132 THR THR A . n 
A 1 130 THR 130 133 133 THR THR A . n 
A 1 131 GLY 131 134 134 GLY GLY A . n 
A 1 132 GLY 132 135 135 GLY GLY A . n 
A 1 133 SER 133 136 136 SER SER A . n 
A 1 134 ARG 134 137 137 ARG ARG A . n 
A 1 135 ALA 135 138 138 ALA ALA A . n 
A 1 136 CYS 136 139 139 CYS CYS A . n 
A 1 137 ALA 137 140 140 ALA ALA A . n 
A 1 138 VAL 138 141 141 VAL VAL A . n 
A 1 139 SER 139 142 142 SER SER A . n 
A 1 140 GLY 140 143 143 GLY GLY A . n 
A 1 141 ASN 141 144 144 ASN ASN A . n 
A 1 142 PRO 142 145 145 PRO PRO A . n 
A 1 143 SER 143 146 146 SER SER A . n 
A 1 144 PHE 144 147 147 PHE PHE A . n 
A 1 145 PHE 145 148 148 PHE PHE A . n 
A 1 146 ARG 146 149 149 ARG ARG A . n 
A 1 147 ASN 147 150 150 ASN ASN A . n 
A 1 148 MET 148 151 151 MET MET A . n 
A 1 149 VAL 149 152 152 VAL VAL A . n 
A 1 150 TRP 150 153 153 TRP TRP A . n 
A 1 151 LEU 151 154 154 LEU LEU A . n 
A 1 152 THR 152 155 155 THR THR A . n 
A 1 153 GLU 153 156 156 GLU GLU A . n 
A 1 154 LYS 154 157 157 LYS LYS A . n 
A 1 155 GLY 155 158 158 GLY GLY A . n 
A 1 156 SER 156 159 159 SER SER A . n 
A 1 157 ASN 157 160 160 ASN ASN A . n 
A 1 158 TYR 158 161 161 TYR TYR A . n 
A 1 159 PRO 159 162 162 PRO PRO A . n 
A 1 160 VAL 160 163 163 VAL VAL A . n 
A 1 161 ALA 161 164 164 ALA ALA A . n 
A 1 162 LYS 162 165 165 LYS LYS A . n 
A 1 163 GLY 163 166 166 GLY GLY A . n 
A 1 164 SER 164 167 167 SER SER A . n 
A 1 165 TYR 165 168 168 TYR TYR A . n 
A 1 166 ASN 166 169 169 ASN ASN A . n 
A 1 167 ASN 167 170 170 ASN ASN A . n 
A 1 168 THR 168 171 171 THR THR A . n 
A 1 169 SER 169 172 172 SER SER A . n 
A 1 170 GLY 170 173 173 GLY GLY A . n 
A 1 171 GLU 171 174 174 GLU GLU A . n 
A 1 172 GLN 172 175 175 GLN GLN A . n 
A 1 173 MET 173 176 176 MET MET A . n 
A 1 174 LEU 174 177 177 LEU LEU A . n 
A 1 175 ILE 175 178 178 ILE ILE A . n 
A 1 176 ILE 176 179 179 ILE ILE A . n 
A 1 177 TRP 177 180 180 TRP TRP A . n 
A 1 178 GLY 178 181 181 GLY GLY A . n 
A 1 179 VAL 179 182 182 VAL VAL A . n 
A 1 180 HIS 180 183 183 HIS HIS A . n 
A 1 181 HIS 181 184 184 HIS HIS A . n 
A 1 182 PRO 182 185 185 PRO PRO A . n 
A 1 183 ASN 183 186 186 ASN ASN A . n 
A 1 184 ASP 184 187 187 ASP ASP A . n 
A 1 185 GLU 185 188 188 GLU GLU A . n 
A 1 186 THR 186 189 189 THR THR A . n 
A 1 187 GLU 187 190 190 GLU GLU A . n 
A 1 188 GLN 188 191 191 GLN GLN A . n 
A 1 189 ARG 189 192 192 ARG ARG A . n 
A 1 190 THR 190 193 193 THR THR A . n 
A 1 191 LEU 191 194 194 LEU LEU A . n 
A 1 192 TYR 192 195 195 TYR TYR A . n 
A 1 193 GLN 193 196 196 GLN GLN A . n 
A 1 194 ASN 194 197 197 ASN ASN A . n 
A 1 195 VAL 195 198 198 VAL VAL A . n 
A 1 196 GLY 196 199 199 GLY GLY A . n 
A 1 197 THR 197 200 200 THR THR A . n 
A 1 198 TYR 198 201 201 TYR TYR A . n 
A 1 199 VAL 199 202 202 VAL VAL A . n 
A 1 200 SER 200 203 203 SER SER A . n 
A 1 201 VAL 201 204 204 VAL VAL A . n 
A 1 202 GLY 202 205 205 GLY GLY A . n 
A 1 203 THR 203 206 206 THR THR A . n 
A 1 204 SER 204 207 207 SER SER A . n 
A 1 205 THR 205 208 208 THR THR A . n 
A 1 206 LEU 206 209 209 LEU LEU A . n 
A 1 207 ASN 207 210 210 ASN ASN A . n 
A 1 208 LYS 208 211 211 LYS LYS A . n 
A 1 209 ARG 209 212 212 ARG ARG A . n 
A 1 210 SER 210 213 213 SER SER A . n 
A 1 211 THR 211 214 214 THR THR A . n 
A 1 212 PRO 212 215 215 PRO PRO A . n 
A 1 213 GLU 213 216 216 GLU GLU A . n 
A 1 214 ILE 214 217 217 ILE ILE A . n 
A 1 215 ALA 215 218 218 ALA ALA A . n 
A 1 216 THR 216 219 219 THR THR A . n 
A 1 217 ARG 217 220 220 ARG ARG A . n 
A 1 218 PRO 218 221 221 PRO PRO A . n 
A 1 219 LYS 219 222 222 LYS LYS A . n 
A 1 220 VAL 220 223 223 VAL VAL A . n 
A 1 221 ASN 221 224 224 ASN ASN A . n 
A 1 222 GLY 222 225 225 GLY GLY A . n 
A 1 223 GLN 223 226 226 GLN GLN A . n 
A 1 224 GLY 224 227 227 GLY GLY A . n 
A 1 225 GLY 225 228 228 GLY GLY A . n 
A 1 226 ARG 226 229 229 ARG ARG A . n 
A 1 227 MET 227 230 230 MET MET A . n 
A 1 228 GLU 228 231 231 GLU GLU A . n 
A 1 229 PHE 229 232 232 PHE PHE A . n 
A 1 230 SER 230 233 233 SER SER A . n 
A 1 231 TRP 231 234 234 TRP TRP A . n 
A 1 232 THR 232 235 235 THR THR A . n 
A 1 233 LEU 233 236 236 LEU LEU A . n 
A 1 234 LEU 234 237 237 LEU LEU A . n 
A 1 235 ASP 235 238 238 ASP ASP A . n 
A 1 236 MET 236 239 239 MET MET A . n 
A 1 237 TRP 237 240 240 TRP TRP A . n 
A 1 238 ASP 238 241 241 ASP ASP A . n 
A 1 239 THR 239 242 242 THR THR A . n 
A 1 240 ILE 240 243 243 ILE ILE A . n 
A 1 241 ASN 241 244 244 ASN ASN A . n 
A 1 242 PHE 242 245 245 PHE PHE A . n 
A 1 243 GLU 243 246 246 GLU GLU A . n 
A 1 244 SER 244 247 247 SER SER A . n 
A 1 245 THR 245 248 248 THR THR A . n 
A 1 246 GLY 246 249 249 GLY GLY A . n 
A 1 247 ASN 247 250 250 ASN ASN A . n 
A 1 248 LEU 248 251 251 LEU LEU A . n 
A 1 249 ILE 249 252 252 ILE ILE A . n 
A 1 250 ALA 250 253 253 ALA ALA A . n 
A 1 251 PRO 251 254 254 PRO PRO A . n 
A 1 252 GLU 252 255 255 GLU GLU A . n 
A 1 253 TYR 253 256 256 TYR TYR A . n 
A 1 254 GLY 254 257 257 GLY GLY A . n 
A 1 255 PHE 255 258 258 PHE PHE A . n 
A 1 256 LYS 256 259 259 LYS LYS A . n 
A 1 257 ILE 257 260 260 ILE ILE A . n 
A 1 258 SER 258 261 261 SER SER A . n 
A 1 259 LYS 259 262 262 LYS LYS A . n 
A 1 260 ARG 260 263 263 ARG ARG A . n 
A 1 261 GLY 261 263 263 GLY GLY A A n 
A 1 262 SER 262 264 264 SER SER A . n 
A 1 263 SER 263 265 265 SER SER A . n 
A 1 264 GLY 264 266 266 GLY GLY A . n 
A 1 265 ILE 265 267 267 ILE ILE A . n 
A 1 266 MET 266 268 268 MET MET A . n 
A 1 267 LYS 267 269 269 LYS LYS A . n 
A 1 268 THR 268 270 270 THR THR A . n 
A 1 269 GLU 269 271 271 GLU GLU A . n 
A 1 270 GLY 270 272 272 GLY GLY A . n 
A 1 271 THR 271 273 273 THR THR A . n 
A 1 272 LEU 272 274 274 LEU LEU A . n 
A 1 273 GLU 273 275 275 GLU GLU A . n 
A 1 274 ASN 274 276 276 ASN ASN A . n 
A 1 275 CYS 275 277 277 CYS CYS A . n 
A 1 276 GLU 276 278 278 GLU GLU A . n 
A 1 277 THR 277 279 279 THR THR A . n 
A 1 278 LYS 278 280 280 LYS LYS A . n 
A 1 279 CYS 279 281 281 CYS CYS A . n 
A 1 280 GLN 280 282 282 GLN GLN A . n 
A 1 281 THR 281 283 283 THR THR A . n 
A 1 282 PRO 282 284 284 PRO PRO A . n 
A 1 283 LEU 283 285 285 LEU LEU A . n 
A 1 284 GLY 284 286 286 GLY GLY A . n 
A 1 285 ALA 285 287 287 ALA ALA A . n 
A 1 286 ILE 286 288 288 ILE ILE A . n 
A 1 287 ASN 287 289 289 ASN ASN A . n 
A 1 288 THR 288 290 290 THR THR A . n 
A 1 289 THR 289 291 291 THR THR A . n 
A 1 290 LEU 290 292 292 LEU LEU A . n 
A 1 291 PRO 291 293 293 PRO PRO A . n 
A 1 292 PHE 292 294 294 PHE PHE A . n 
A 1 293 HIS 293 295 295 HIS HIS A . n 
A 1 294 ASN 294 296 296 ASN ASN A . n 
A 1 295 VAL 295 297 297 VAL VAL A . n 
A 1 296 HIS 296 298 298 HIS HIS A . n 
A 1 297 PRO 297 299 299 PRO PRO A . n 
A 1 298 LEU 298 300 300 LEU LEU A . n 
A 1 299 THR 299 301 301 THR THR A . n 
A 1 300 ILE 300 302 302 ILE ILE A . n 
A 1 301 GLY 301 303 303 GLY GLY A . n 
A 1 302 GLU 302 304 304 GLU GLU A . n 
A 1 303 CYS 303 305 305 CYS CYS A . n 
A 1 304 PRO 304 306 306 PRO PRO A . n 
A 1 305 LYS 305 307 307 LYS LYS A . n 
A 1 306 TYR 306 308 308 TYR TYR A . n 
A 1 307 VAL 307 309 309 VAL VAL A . n 
A 1 308 LYS 308 310 310 LYS LYS A . n 
A 1 309 SER 309 311 311 SER SER A . n 
A 1 310 GLU 310 312 312 GLU GLU A . n 
A 1 311 LYS 311 313 313 LYS LYS A . n 
A 1 312 LEU 312 314 314 LEU LEU A . n 
A 1 313 VAL 313 315 315 VAL VAL A . n 
A 1 314 LEU 314 316 316 LEU LEU A . n 
A 1 315 ALA 315 317 317 ALA ALA A . n 
A 1 316 THR 316 318 318 THR THR A . n 
A 1 317 GLY 317 319 319 GLY GLY A . n 
A 1 318 LEU 318 320 320 LEU LEU A . n 
A 1 319 ARG 319 321 321 ARG ARG A . n 
A 1 320 ASN 320 322 322 ASN ASN A . n 
A 1 321 VAL 321 323 323 VAL VAL A . n 
A 1 322 PRO 322 324 324 PRO PRO A . n 
A 1 323 GLN 323 325 ?   ?   ?   A . n 
A 1 324 ILE 324 326 ?   ?   ?   A . n 
A 1 325 GLU 325 327 ?   ?   ?   A . n 
A 1 326 SER 326 328 ?   ?   ?   A . n 
A 1 327 ARG 327 329 ?   ?   ?   A . n 
B 2 1   GLY 1   1   1   GLY GLY B . n 
B 2 2   LEU 2   2   2   LEU LEU B . n 
B 2 3   PHE 3   3   3   PHE PHE B . n 
B 2 4   GLY 4   4   4   GLY GLY B . n 
B 2 5   ALA 5   5   5   ALA ALA B . n 
B 2 6   ILE 6   6   6   ILE ILE B . n 
B 2 7   ALA 7   7   7   ALA ALA B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   PHE 9   9   9   PHE PHE B . n 
B 2 10  ILE 10  10  10  ILE ILE B . n 
B 2 11  GLU 11  11  11  GLU GLU B . n 
B 2 12  GLY 12  12  12  GLY GLY B . n 
B 2 13  GLY 13  13  13  GLY GLY B . n 
B 2 14  TRP 14  14  14  TRP TRP B . n 
B 2 15  GLN 15  15  15  GLN GLN 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  SER 27  27  27  SER SER B . n 
B 2 28  ASN 28  28  28  ASN ASN B . n 
B 2 29  ASP 29  29  29  ASP ASP 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  LYS 38  38  38  LYS LYS B . n 
B 2 39  GLU 39  39  39  GLU GLU 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  LYS 43  43  43  LYS LYS B . n 
B 2 44  ALA 44  44  44  ALA ALA B . n 
B 2 45  PHE 45  45  45  PHE PHE B . n 
B 2 46  ASP 46  46  46  ASP ASP B . n 
B 2 47  GLY 47  47  47  GLY GLY 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  GLU 64  64  64  GLU GLU B . n 
B 2 65  ALA 65  65  65  ALA ALA B . n 
B 2 66  VAL 66  66  66  VAL VAL B . n 
B 2 67  GLY 67  67  67  GLY GLY B . n 
B 2 68  LYS 68  68  68  LYS LYS B . n 
B 2 69  GLU 69  69  69  GLU GLU B . n 
B 2 70  PHE 70  70  70  PHE PHE B . n 
B 2 71  SER 71  71  71  SER SER B . n 
B 2 72  ASN 72  72  72  ASN ASN B . n 
B 2 73  LEU 73  73  73  LEU LEU B . n 
B 2 74  GLU 74  74  74  GLU GLU B . n 
B 2 75  ARG 75  75  75  ARG ARG B . n 
B 2 76  ARG 76  76  76  ARG ARG B . n 
B 2 77  LEU 77  77  77  LEU LEU B . n 
B 2 78  GLU 78  78  78  GLU GLU B . n 
B 2 79  ASN 79  79  79  ASN ASN B . n 
B 2 80  LEU 80  80  80  LEU LEU B . n 
B 2 81  ASN 81  81  81  ASN ASN B . n 
B 2 82  LYS 82  82  82  LYS LYS B . n 
B 2 83  LYS 83  83  83  LYS LYS B . n 
B 2 84  MET 84  84  84  MET MET B . n 
B 2 85  GLU 85  85  85  GLU GLU 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  VAL 91  91  91  VAL VAL 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 MET 102 102 102 MET MET 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 HIS 106 106 106 HIS HIS 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 PHE 110 110 110 PHE PHE 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 ASP 120 120 120 ASP ASP 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 MET 124 124 124 MET MET 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 ARG 127 127 127 ARG ARG B . n 
B 2 128 ASP 128 128 128 ASP ASP B . n 
B 2 129 ASN 129 129 129 ASN ASN B . n 
B 2 130 VAL 130 130 130 VAL VAL 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 LEU 133 133 133 LEU LEU 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 ASP 146 146 146 ASP ASP B . n 
B 2 147 GLU 147 147 147 GLU GLU 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 ASN 150 150 150 ASN ASN 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 GLU 163 163 163 GLU GLU 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 SER 166 166 166 SER SER 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 ASN 171 171 171 ASN ASN B . n 
B 2 172 GLU 172 172 172 GLU GLU B . n 
B 2 173 ILE 173 173 ?   ?   ?   B . n 
B 2 174 LYS 174 174 ?   ?   ?   B . n 
C 1 1   PRO 1   9   9   PRO PRO C . n 
C 1 2   GLY 2   10  10  GLY GLY C . n 
C 1 3   ASP 3   11  11  ASP ASP C . n 
C 1 4   GLN 4   12  12  GLN GLN C . n 
C 1 5   ILE 5   13  13  ILE ILE C . n 
C 1 6   CYS 6   14  14  CYS CYS C . n 
C 1 7   ILE 7   15  15  ILE ILE C . n 
C 1 8   GLY 8   16  16  GLY GLY C . n 
C 1 9   TYR 9   17  17  TYR TYR C . n 
C 1 10  HIS 10  18  18  HIS HIS C . n 
C 1 11  ALA 11  19  19  ALA ALA C . n 
C 1 12  ASN 12  20  20  ASN ASN C . n 
C 1 13  ASN 13  21  21  ASN ASN C . n 
C 1 14  SER 14  22  22  SER SER C . n 
C 1 15  THR 15  23  23  THR THR C . n 
C 1 16  GLU 16  24  24  GLU GLU C . n 
C 1 17  LYS 17  25  25  LYS LYS C . n 
C 1 18  VAL 18  26  26  VAL VAL C . n 
C 1 19  ASP 19  27  27  ASP ASP C . n 
C 1 20  THR 20  28  28  THR THR C . n 
C 1 21  ILE 21  29  29  ILE ILE C . n 
C 1 22  LEU 22  30  30  LEU LEU C . n 
C 1 23  GLU 23  31  31  GLU GLU C . n 
C 1 24  ARG 24  32  32  ARG ARG C . n 
C 1 25  ASN 25  33  33  ASN ASN C . n 
C 1 26  VAL 26  34  34  VAL VAL C . n 
C 1 27  THR 27  35  35  THR THR C . n 
C 1 28  VAL 28  36  36  VAL VAL C . n 
C 1 29  THR 29  37  37  THR THR C . n 
C 1 30  HIS 30  38  38  HIS HIS C . n 
C 1 31  ALA 31  39  39  ALA ALA C . n 
C 1 32  LYS 32  40  40  LYS LYS C . n 
C 1 33  ASP 33  41  41  ASP ASP C . n 
C 1 34  ILE 34  42  42  ILE ILE C . n 
C 1 35  LEU 35  43  43  LEU LEU C . n 
C 1 36  GLU 36  44  44  GLU GLU C . n 
C 1 37  LYS 37  45  45  LYS LYS C . n 
C 1 38  THR 38  46  46  THR THR C . n 
C 1 39  HIS 39  47  47  HIS HIS C . n 
C 1 40  ASN 40  48  48  ASN ASN C . n 
C 1 41  GLY 41  49  49  GLY GLY C . n 
C 1 42  LYS 42  50  50  LYS LYS C . n 
C 1 43  LEU 43  51  51  LEU LEU C . n 
C 1 44  CYS 44  52  52  CYS CYS C . n 
C 1 45  LYS 45  53  53  LYS LYS C . n 
C 1 46  LEU 46  53  53  LEU LEU C A n 
C 1 47  ASN 47  54  54  ASN ASN C . n 
C 1 48  GLY 48  55  55  GLY GLY C . n 
C 1 49  ILE 49  56  56  ILE ILE C . n 
C 1 50  PRO 50  57  57  PRO PRO C . n 
C 1 51  PRO 51  58  58  PRO PRO C . n 
C 1 52  LEU 52  59  59  LEU LEU C . n 
C 1 53  GLU 53  60  60  GLU GLU C . n 
C 1 54  LEU 54  61  61  LEU LEU C . n 
C 1 55  GLY 55  62  62  GLY GLY C . n 
C 1 56  ASP 56  63  63  ASP ASP C . n 
C 1 57  CYS 57  64  64  CYS CYS C . n 
C 1 58  SER 58  65  65  SER SER C . n 
C 1 59  ILE 59  66  66  ILE ILE C . n 
C 1 60  ALA 60  67  67  ALA ALA C . n 
C 1 61  GLY 61  68  68  GLY GLY C . n 
C 1 62  TRP 62  69  69  TRP TRP C . n 
C 1 63  LEU 63  70  70  LEU LEU C . n 
C 1 64  LEU 64  71  71  LEU LEU C . n 
C 1 65  GLY 65  72  72  GLY GLY C . n 
C 1 66  ASN 66  73  73  ASN ASN C . n 
C 1 67  PRO 67  74  74  PRO PRO C . n 
C 1 68  GLU 68  75  75  GLU GLU C . n 
C 1 69  CYS 69  76  76  CYS CYS C . n 
C 1 70  ASP 70  77  77  ASP ASP C . n 
C 1 71  ARG 71  78  78  ARG ARG C . n 
C 1 72  LEU 72  79  79  LEU LEU C . n 
C 1 73  LEU 73  80  80  LEU LEU C . n 
C 1 74  SER 74  81  81  SER SER C . n 
C 1 75  VAL 75  81  81  VAL VAL C A n 
C 1 76  PRO 76  82  82  PRO PRO C . n 
C 1 77  GLU 77  83  83  GLU GLU C . n 
C 1 78  TRP 78  84  84  TRP TRP C . n 
C 1 79  SER 79  85  85  SER SER C . n 
C 1 80  TYR 80  86  86  TYR TYR C . n 
C 1 81  ILE 81  87  87  ILE ILE C . n 
C 1 82  MET 82  88  88  MET MET C . n 
C 1 83  GLU 83  89  89  GLU GLU C . n 
C 1 84  LYS 84  90  90  LYS LYS C . n 
C 1 85  GLU 85  91  91  GLU GLU C . n 
C 1 86  ASN 86  92  92  ASN ASN C . n 
C 1 87  PRO 87  93  93  PRO PRO C . n 
C 1 88  ARG 88  94  94  ARG ARG C . n 
C 1 89  ASP 89  95  95  ASP ASP C . n 
C 1 90  GLY 90  95  95  GLY GLY C A n 
C 1 91  LEU 91  96  96  LEU LEU C . n 
C 1 92  CYS 92  97  97  CYS CYS C . n 
C 1 93  TYR 93  98  98  TYR TYR C . n 
C 1 94  PRO 94  99  99  PRO PRO C . n 
C 1 95  GLY 95  100 100 GLY GLY C . n 
C 1 96  SER 96  101 101 SER SER C . n 
C 1 97  PHE 97  102 102 PHE PHE C . n 
C 1 98  ASN 98  103 103 ASN ASN C . n 
C 1 99  ASP 99  104 104 ASP ASP C . n 
C 1 100 TYR 100 105 105 TYR TYR C . n 
C 1 101 GLU 101 106 106 GLU GLU C . n 
C 1 102 GLU 102 107 107 GLU GLU C . n 
C 1 103 LEU 103 108 108 LEU LEU C . n 
C 1 104 LYS 104 109 109 LYS LYS C . n 
C 1 105 HIS 105 110 110 HIS HIS C . n 
C 1 106 LEU 106 111 111 LEU LEU C . n 
C 1 107 LEU 107 112 112 LEU LEU C . n 
C 1 108 SER 108 113 113 SER SER C . n 
C 1 109 SER 109 114 114 SER SER C . n 
C 1 110 VAL 110 115 115 VAL VAL C . n 
C 1 111 LYS 111 116 116 LYS LYS C . n 
C 1 112 HIS 112 116 116 HIS HIS C A n 
C 1 113 PHE 113 116 116 PHE PHE C B n 
C 1 114 GLU 114 116 116 GLU GLU C C n 
C 1 115 LYS 115 117 117 LYS LYS C . n 
C 1 116 VAL 116 118 118 VAL VAL C . n 
C 1 117 LYS 117 119 119 LYS LYS C . n 
C 1 118 ILE 118 120 120 ILE ILE C . n 
C 1 119 LEU 119 121 121 LEU LEU C . n 
C 1 120 PRO 120 122 122 PRO PRO C . n 
C 1 121 LYS 121 123 123 LYS LYS C . n 
C 1 122 ASP 122 125 125 ASP ASP C . n 
C 1 123 ARG 123 126 126 ARG ARG C . n 
C 1 124 TRP 124 127 127 TRP TRP C . n 
C 1 125 THR 125 128 128 THR THR C . n 
C 1 126 GLN 126 129 129 GLN GLN C . n 
C 1 127 HIS 127 130 130 HIS HIS C . n 
C 1 128 THR 128 131 131 THR THR C . n 
C 1 129 THR 129 132 132 THR THR C . n 
C 1 130 THR 130 133 133 THR THR C . n 
C 1 131 GLY 131 134 134 GLY GLY C . n 
C 1 132 GLY 132 135 135 GLY GLY C . n 
C 1 133 SER 133 136 136 SER SER C . n 
C 1 134 ARG 134 137 137 ARG ARG C . n 
C 1 135 ALA 135 138 138 ALA ALA C . n 
C 1 136 CYS 136 139 139 CYS CYS C . n 
C 1 137 ALA 137 140 140 ALA ALA C . n 
C 1 138 VAL 138 141 141 VAL VAL C . n 
C 1 139 SER 139 142 142 SER SER C . n 
C 1 140 GLY 140 143 143 GLY GLY C . n 
C 1 141 ASN 141 144 144 ASN ASN C . n 
C 1 142 PRO 142 145 145 PRO PRO C . n 
C 1 143 SER 143 146 146 SER SER C . n 
C 1 144 PHE 144 147 147 PHE PHE C . n 
C 1 145 PHE 145 148 148 PHE PHE C . n 
C 1 146 ARG 146 149 149 ARG ARG C . n 
C 1 147 ASN 147 150 150 ASN ASN C . n 
C 1 148 MET 148 151 151 MET MET C . n 
C 1 149 VAL 149 152 152 VAL VAL C . n 
C 1 150 TRP 150 153 153 TRP TRP C . n 
C 1 151 LEU 151 154 154 LEU LEU C . n 
C 1 152 THR 152 155 155 THR THR C . n 
C 1 153 GLU 153 156 156 GLU GLU C . n 
C 1 154 LYS 154 157 157 LYS LYS C . n 
C 1 155 GLY 155 158 158 GLY GLY C . n 
C 1 156 SER 156 159 159 SER SER C . n 
C 1 157 ASN 157 160 160 ASN ASN C . n 
C 1 158 TYR 158 161 161 TYR TYR C . n 
C 1 159 PRO 159 162 162 PRO PRO C . n 
C 1 160 VAL 160 163 163 VAL VAL C . n 
C 1 161 ALA 161 164 164 ALA ALA C . n 
C 1 162 LYS 162 165 165 LYS LYS C . n 
C 1 163 GLY 163 166 166 GLY GLY C . n 
C 1 164 SER 164 167 167 SER SER C . n 
C 1 165 TYR 165 168 168 TYR TYR C . n 
C 1 166 ASN 166 169 169 ASN ASN C . n 
C 1 167 ASN 167 170 170 ASN ASN C . n 
C 1 168 THR 168 171 171 THR THR C . n 
C 1 169 SER 169 172 172 SER SER C . n 
C 1 170 GLY 170 173 173 GLY GLY C . n 
C 1 171 GLU 171 174 174 GLU GLU C . n 
C 1 172 GLN 172 175 175 GLN GLN C . n 
C 1 173 MET 173 176 176 MET MET C . n 
C 1 174 LEU 174 177 177 LEU LEU C . n 
C 1 175 ILE 175 178 178 ILE ILE C . n 
C 1 176 ILE 176 179 179 ILE ILE C . n 
C 1 177 TRP 177 180 180 TRP TRP C . n 
C 1 178 GLY 178 181 181 GLY GLY C . n 
C 1 179 VAL 179 182 182 VAL VAL C . n 
C 1 180 HIS 180 183 183 HIS HIS C . n 
C 1 181 HIS 181 184 184 HIS HIS C . n 
C 1 182 PRO 182 185 185 PRO PRO C . n 
C 1 183 ASN 183 186 186 ASN ASN C . n 
C 1 184 ASP 184 187 187 ASP ASP C . n 
C 1 185 GLU 185 188 188 GLU GLU C . n 
C 1 186 THR 186 189 189 THR THR C . n 
C 1 187 GLU 187 190 190 GLU GLU C . n 
C 1 188 GLN 188 191 191 GLN GLN C . n 
C 1 189 ARG 189 192 192 ARG ARG C . n 
C 1 190 THR 190 193 193 THR THR C . n 
C 1 191 LEU 191 194 194 LEU LEU C . n 
C 1 192 TYR 192 195 195 TYR TYR C . n 
C 1 193 GLN 193 196 196 GLN GLN C . n 
C 1 194 ASN 194 197 197 ASN ASN C . n 
C 1 195 VAL 195 198 198 VAL VAL C . n 
C 1 196 GLY 196 199 199 GLY GLY C . n 
C 1 197 THR 197 200 200 THR THR C . n 
C 1 198 TYR 198 201 201 TYR TYR C . n 
C 1 199 VAL 199 202 202 VAL VAL C . n 
C 1 200 SER 200 203 203 SER SER C . n 
C 1 201 VAL 201 204 204 VAL VAL C . n 
C 1 202 GLY 202 205 205 GLY GLY C . n 
C 1 203 THR 203 206 206 THR THR C . n 
C 1 204 SER 204 207 207 SER SER C . n 
C 1 205 THR 205 208 208 THR THR C . n 
C 1 206 LEU 206 209 209 LEU LEU C . n 
C 1 207 ASN 207 210 210 ASN ASN C . n 
C 1 208 LYS 208 211 211 LYS LYS C . n 
C 1 209 ARG 209 212 212 ARG ARG C . n 
C 1 210 SER 210 213 213 SER SER C . n 
C 1 211 THR 211 214 214 THR THR C . n 
C 1 212 PRO 212 215 215 PRO PRO C . n 
C 1 213 GLU 213 216 216 GLU GLU C . n 
C 1 214 ILE 214 217 217 ILE ILE C . n 
C 1 215 ALA 215 218 218 ALA ALA C . n 
C 1 216 THR 216 219 219 THR THR C . n 
C 1 217 ARG 217 220 220 ARG ARG C . n 
C 1 218 PRO 218 221 221 PRO PRO C . n 
C 1 219 LYS 219 222 222 LYS LYS C . n 
C 1 220 VAL 220 223 223 VAL VAL C . n 
C 1 221 ASN 221 224 224 ASN ASN C . n 
C 1 222 GLY 222 225 225 GLY GLY C . n 
C 1 223 GLN 223 226 226 GLN GLN C . n 
C 1 224 GLY 224 227 227 GLY GLY C . n 
C 1 225 GLY 225 228 228 GLY GLY C . n 
C 1 226 ARG 226 229 229 ARG ARG C . n 
C 1 227 MET 227 230 230 MET MET C . n 
C 1 228 GLU 228 231 231 GLU GLU C . n 
C 1 229 PHE 229 232 232 PHE PHE C . n 
C 1 230 SER 230 233 233 SER SER C . n 
C 1 231 TRP 231 234 234 TRP TRP C . n 
C 1 232 THR 232 235 235 THR THR C . n 
C 1 233 LEU 233 236 236 LEU LEU C . n 
C 1 234 LEU 234 237 237 LEU LEU C . n 
C 1 235 ASP 235 238 238 ASP ASP C . n 
C 1 236 MET 236 239 239 MET MET C . n 
C 1 237 TRP 237 240 240 TRP TRP C . n 
C 1 238 ASP 238 241 241 ASP ASP C . n 
C 1 239 THR 239 242 242 THR THR C . n 
C 1 240 ILE 240 243 243 ILE ILE C . n 
C 1 241 ASN 241 244 244 ASN ASN C . n 
C 1 242 PHE 242 245 245 PHE PHE C . n 
C 1 243 GLU 243 246 246 GLU GLU C . n 
C 1 244 SER 244 247 247 SER SER C . n 
C 1 245 THR 245 248 248 THR THR C . n 
C 1 246 GLY 246 249 249 GLY GLY C . n 
C 1 247 ASN 247 250 250 ASN ASN C . n 
C 1 248 LEU 248 251 251 LEU LEU C . n 
C 1 249 ILE 249 252 252 ILE ILE C . n 
C 1 250 ALA 250 253 253 ALA ALA C . n 
C 1 251 PRO 251 254 254 PRO PRO C . n 
C 1 252 GLU 252 255 255 GLU GLU C . n 
C 1 253 TYR 253 256 256 TYR TYR C . n 
C 1 254 GLY 254 257 257 GLY GLY C . n 
C 1 255 PHE 255 258 258 PHE PHE C . n 
C 1 256 LYS 256 259 259 LYS LYS C . n 
C 1 257 ILE 257 260 260 ILE ILE C . n 
C 1 258 SER 258 261 261 SER SER C . n 
C 1 259 LYS 259 262 262 LYS LYS C . n 
C 1 260 ARG 260 263 263 ARG ARG C . n 
C 1 261 GLY 261 263 263 GLY GLY C A n 
C 1 262 SER 262 265 265 SER SER C . n 
C 1 263 SER 263 266 266 SER SER C . n 
C 1 264 GLY 264 267 267 GLY GLY C . n 
C 1 265 ILE 265 268 268 ILE ILE C . n 
C 1 266 MET 266 269 269 MET MET C . n 
C 1 267 LYS 267 270 270 LYS LYS C . n 
C 1 268 THR 268 271 271 THR THR C . n 
C 1 269 GLU 269 272 272 GLU GLU C . n 
C 1 270 GLY 270 273 273 GLY GLY C . n 
C 1 271 THR 271 274 274 THR THR C . n 
C 1 272 LEU 272 275 275 LEU LEU C . n 
C 1 273 GLU 273 276 276 GLU GLU C . n 
C 1 274 ASN 274 277 277 ASN ASN C . n 
C 1 275 CYS 275 278 278 CYS CYS C . n 
C 1 276 GLU 276 279 279 GLU GLU C . n 
C 1 277 THR 277 280 280 THR THR C . n 
C 1 278 LYS 278 281 281 LYS LYS C . n 
C 1 279 CYS 279 282 282 CYS CYS C . n 
C 1 280 GLN 280 283 283 GLN GLN C . n 
C 1 281 THR 281 284 284 THR THR C . n 
C 1 282 PRO 282 285 285 PRO PRO C . n 
C 1 283 LEU 283 286 286 LEU LEU C . n 
C 1 284 GLY 284 287 287 GLY GLY C . n 
C 1 285 ALA 285 288 288 ALA ALA C . n 
C 1 286 ILE 286 289 289 ILE ILE C . n 
C 1 287 ASN 287 290 290 ASN ASN C . n 
C 1 288 THR 288 291 291 THR THR C . n 
C 1 289 THR 289 292 292 THR THR C . n 
C 1 290 LEU 290 293 293 LEU LEU C . n 
C 1 291 PRO 291 294 294 PRO PRO C . n 
C 1 292 PHE 292 295 295 PHE PHE C . n 
C 1 293 HIS 293 296 296 HIS HIS C . n 
C 1 294 ASN 294 297 297 ASN ASN C . n 
C 1 295 VAL 295 298 298 VAL VAL C . n 
C 1 296 HIS 296 299 299 HIS HIS C . n 
C 1 297 PRO 297 300 300 PRO PRO C . n 
C 1 298 LEU 298 301 301 LEU LEU C . n 
C 1 299 THR 299 302 302 THR THR C . n 
C 1 300 ILE 300 303 303 ILE ILE C . n 
C 1 301 GLY 301 304 304 GLY GLY C . n 
C 1 302 GLU 302 305 305 GLU GLU C . n 
C 1 303 CYS 303 306 306 CYS CYS C . n 
C 1 304 PRO 304 307 307 PRO PRO C . n 
C 1 305 LYS 305 308 308 LYS LYS C . n 
C 1 306 TYR 306 309 309 TYR TYR C . n 
C 1 307 VAL 307 310 310 VAL VAL C . n 
C 1 308 LYS 308 311 311 LYS LYS C . n 
C 1 309 SER 309 312 312 SER SER C . n 
C 1 310 GLU 310 313 313 GLU GLU C . n 
C 1 311 LYS 311 314 314 LYS LYS C . n 
C 1 312 LEU 312 315 315 LEU LEU C . n 
C 1 313 VAL 313 316 316 VAL VAL C . n 
C 1 314 LEU 314 317 317 LEU LEU C . n 
C 1 315 ALA 315 318 318 ALA ALA C . n 
C 1 316 THR 316 319 319 THR THR C . n 
C 1 317 GLY 317 320 320 GLY GLY C . n 
C 1 318 LEU 318 321 321 LEU LEU C . n 
C 1 319 ARG 319 322 322 ARG ARG C . n 
C 1 320 ASN 320 323 323 ASN ASN C . n 
C 1 321 VAL 321 324 324 VAL VAL C . n 
C 1 322 PRO 322 325 325 PRO PRO C . n 
C 1 323 GLN 323 326 ?   ?   ?   C . n 
C 1 324 ILE 324 327 ?   ?   ?   C . n 
C 1 325 GLU 325 328 ?   ?   ?   C . n 
C 1 326 SER 326 329 ?   ?   ?   C . n 
C 1 327 ARG 327 330 ?   ?   ?   C . n 
D 2 1   GLY 1   1   1   GLY GLY D . n 
D 2 2   LEU 2   2   2   LEU LEU D . n 
D 2 3   PHE 3   3   3   PHE PHE D . n 
D 2 4   GLY 4   4   4   GLY GLY D . n 
D 2 5   ALA 5   5   5   ALA ALA D . n 
D 2 6   ILE 6   6   6   ILE ILE D . n 
D 2 7   ALA 7   7   7   ALA ALA D . n 
D 2 8   GLY 8   8   8   GLY GLY D . n 
D 2 9   PHE 9   9   9   PHE PHE D . n 
D 2 10  ILE 10  10  10  ILE ILE D . n 
D 2 11  GLU 11  11  11  GLU GLU D . n 
D 2 12  GLY 12  12  12  GLY GLY D . n 
D 2 13  GLY 13  13  13  GLY GLY D . n 
D 2 14  TRP 14  14  14  TRP TRP D . n 
D 2 15  GLN 15  15  15  GLN GLN D . n 
D 2 16  GLY 16  16  16  GLY GLY D . n 
D 2 17  MET 17  17  17  MET MET D . n 
D 2 18  VAL 18  18  18  VAL VAL D . n 
D 2 19  ASP 19  19  19  ASP ASP D . n 
D 2 20  GLY 20  20  20  GLY GLY D . n 
D 2 21  TRP 21  21  21  TRP TRP D . n 
D 2 22  TYR 22  22  22  TYR TYR D . n 
D 2 23  GLY 23  23  23  GLY GLY D . n 
D 2 24  TYR 24  24  24  TYR TYR D . n 
D 2 25  HIS 25  25  25  HIS HIS D . n 
D 2 26  HIS 26  26  26  HIS HIS D . n 
D 2 27  SER 27  27  27  SER SER D . n 
D 2 28  ASN 28  28  28  ASN ASN D . n 
D 2 29  ASP 29  29  29  ASP ASP D . n 
D 2 30  GLN 30  30  30  GLN GLN D . n 
D 2 31  GLY 31  31  31  GLY GLY D . n 
D 2 32  SER 32  32  32  SER SER D . n 
D 2 33  GLY 33  33  33  GLY GLY D . n 
D 2 34  TYR 34  34  34  TYR TYR D . n 
D 2 35  ALA 35  35  35  ALA ALA D . n 
D 2 36  ALA 36  36  36  ALA ALA D . n 
D 2 37  ASP 37  37  37  ASP ASP D . n 
D 2 38  LYS 38  38  38  LYS LYS D . n 
D 2 39  GLU 39  39  39  GLU GLU 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  LYS 43  43  43  LYS LYS D . n 
D 2 44  ALA 44  44  44  ALA ALA D . n 
D 2 45  PHE 45  45  45  PHE PHE D . n 
D 2 46  ASP 46  46  46  ASP ASP D . n 
D 2 47  GLY 47  47  47  GLY GLY D . n 
D 2 48  ILE 48  48  48  ILE ILE D . n 
D 2 49  THR 49  49  49  THR THR D . n 
D 2 50  ASN 50  50  50  ASN ASN D . n 
D 2 51  LYS 51  51  51  LYS LYS D . n 
D 2 52  VAL 52  52  52  VAL VAL D . n 
D 2 53  ASN 53  53  53  ASN ASN D . n 
D 2 54  SER 54  54  54  SER SER D . n 
D 2 55  VAL 55  55  55  VAL VAL D . n 
D 2 56  ILE 56  56  56  ILE ILE D . n 
D 2 57  GLU 57  57  57  GLU GLU D . n 
D 2 58  LYS 58  58  58  LYS LYS D . n 
D 2 59  MET 59  59  59  MET MET D . n 
D 2 60  ASN 60  60  60  ASN ASN D . n 
D 2 61  THR 61  61  61  THR THR D . n 
D 2 62  GLN 62  62  62  GLN GLN D . n 
D 2 63  PHE 63  63  63  PHE PHE D . n 
D 2 64  GLU 64  64  64  GLU GLU D . n 
D 2 65  ALA 65  65  65  ALA ALA D . n 
D 2 66  VAL 66  66  66  VAL VAL D . n 
D 2 67  GLY 67  67  67  GLY GLY D . n 
D 2 68  LYS 68  68  68  LYS LYS D . n 
D 2 69  GLU 69  69  69  GLU GLU D . n 
D 2 70  PHE 70  70  70  PHE PHE D . n 
D 2 71  SER 71  71  71  SER SER D . n 
D 2 72  ASN 72  72  72  ASN ASN D . n 
D 2 73  LEU 73  73  73  LEU LEU D . n 
D 2 74  GLU 74  74  74  GLU GLU D . n 
D 2 75  ARG 75  75  75  ARG ARG D . n 
D 2 76  ARG 76  76  76  ARG ARG D . n 
D 2 77  LEU 77  77  77  LEU LEU D . n 
D 2 78  GLU 78  78  78  GLU GLU D . n 
D 2 79  ASN 79  79  79  ASN ASN D . n 
D 2 80  LEU 80  80  80  LEU LEU D . n 
D 2 81  ASN 81  81  81  ASN ASN D . n 
D 2 82  LYS 82  82  82  LYS LYS D . n 
D 2 83  LYS 83  83  83  LYS LYS D . n 
D 2 84  MET 84  84  84  MET MET D . n 
D 2 85  GLU 85  85  85  GLU GLU 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  VAL 91  91  91  VAL VAL 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 MET 102 102 102 MET MET 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 HIS 106 106 106 HIS HIS 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 PHE 110 110 110 PHE PHE 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 ASP 120 120 120 ASP ASP 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 MET 124 124 124 MET MET 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 ARG 127 127 127 ARG ARG D . n 
D 2 128 ASP 128 128 128 ASP ASP D . n 
D 2 129 ASN 129 129 129 ASN ASN D . n 
D 2 130 VAL 130 130 130 VAL VAL 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 LEU 133 133 133 LEU LEU D . n 
D 2 134 GLY 134 134 134 GLY GLY D . n 
D 2 135 ASN 135 135 135 ASN ASN D . n 
D 2 136 GLY 136 136 136 GLY GLY D . n 
D 2 137 CYS 137 137 137 CYS CYS D . n 
D 2 138 PHE 138 138 138 PHE PHE D . n 
D 2 139 GLU 139 139 139 GLU GLU D . n 
D 2 140 PHE 140 140 140 PHE PHE D . n 
D 2 141 TYR 141 141 141 TYR TYR D . n 
D 2 142 HIS 142 142 142 HIS HIS D . n 
D 2 143 LYS 143 143 143 LYS LYS D . n 
D 2 144 CYS 144 144 144 CYS CYS D . n 
D 2 145 ASP 145 145 145 ASP ASP D . n 
D 2 146 ASP 146 146 146 ASP ASP D . n 
D 2 147 GLU 147 147 147 GLU GLU 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 ASN 150 150 150 ASN ASN D . n 
D 2 151 SER 151 151 151 SER SER D . n 
D 2 152 VAL 152 152 152 VAL VAL D . n 
D 2 153 LYS 153 153 153 LYS LYS D . n 
D 2 154 ASN 154 154 154 ASN ASN D . n 
D 2 155 GLY 155 155 155 GLY GLY D . n 
D 2 156 THR 156 156 156 THR THR D . n 
D 2 157 TYR 157 157 157 TYR TYR D . n 
D 2 158 ASP 158 158 158 ASP ASP D . n 
D 2 159 TYR 159 159 159 TYR TYR D . n 
D 2 160 PRO 160 160 160 PRO PRO D . n 
D 2 161 LYS 161 161 161 LYS LYS D . n 
D 2 162 TYR 162 162 162 TYR TYR D . n 
D 2 163 GLU 163 163 163 GLU GLU 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 SER 166 166 166 SER SER 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 ASN 171 171 171 ASN ASN D . n 
D 2 172 GLU 172 172 172 GLU GLU D . n 
D 2 173 ILE 173 173 ?   ?   ?   D . n 
D 2 174 LYS 174 174 ?   ?   ?   D . n 
E 1 1   PRO 1   9   9   PRO PRO E . n 
E 1 2   GLY 2   10  10  GLY GLY E . n 
E 1 3   ASP 3   11  11  ASP ASP E . n 
E 1 4   GLN 4   12  12  GLN GLN E . n 
E 1 5   ILE 5   13  13  ILE ILE E . n 
E 1 6   CYS 6   14  14  CYS CYS E . n 
E 1 7   ILE 7   15  15  ILE ILE E . n 
E 1 8   GLY 8   16  16  GLY GLY E . n 
E 1 9   TYR 9   17  17  TYR TYR E . n 
E 1 10  HIS 10  18  18  HIS HIS E . n 
E 1 11  ALA 11  19  19  ALA ALA E . n 
E 1 12  ASN 12  20  20  ASN ASN E . n 
E 1 13  ASN 13  21  21  ASN ASN E . n 
E 1 14  SER 14  22  22  SER SER E . n 
E 1 15  THR 15  23  23  THR THR E . n 
E 1 16  GLU 16  24  24  GLU GLU E . n 
E 1 17  LYS 17  25  25  LYS LYS E . n 
E 1 18  VAL 18  26  26  VAL VAL E . n 
E 1 19  ASP 19  27  27  ASP ASP E . n 
E 1 20  THR 20  28  28  THR THR E . n 
E 1 21  ILE 21  29  29  ILE ILE E . n 
E 1 22  LEU 22  30  30  LEU LEU E . n 
E 1 23  GLU 23  31  31  GLU GLU E . n 
E 1 24  ARG 24  32  32  ARG ARG E . n 
E 1 25  ASN 25  33  33  ASN ASN E . n 
E 1 26  VAL 26  34  34  VAL VAL E . n 
E 1 27  THR 27  35  35  THR THR E . n 
E 1 28  VAL 28  36  36  VAL VAL E . n 
E 1 29  THR 29  37  37  THR THR E . n 
E 1 30  HIS 30  38  38  HIS HIS E . n 
E 1 31  ALA 31  39  39  ALA ALA E . n 
E 1 32  LYS 32  40  40  LYS LYS E . n 
E 1 33  ASP 33  41  41  ASP ASP E . n 
E 1 34  ILE 34  42  42  ILE ILE E . n 
E 1 35  LEU 35  43  43  LEU LEU E . n 
E 1 36  GLU 36  44  44  GLU GLU E . n 
E 1 37  LYS 37  45  45  LYS LYS E . n 
E 1 38  THR 38  46  46  THR THR E . n 
E 1 39  HIS 39  47  47  HIS HIS E . n 
E 1 40  ASN 40  48  48  ASN ASN E . n 
E 1 41  GLY 41  49  49  GLY GLY E . n 
E 1 42  LYS 42  50  50  LYS LYS E . n 
E 1 43  LEU 43  51  51  LEU LEU E . n 
E 1 44  CYS 44  52  52  CYS CYS E . n 
E 1 45  LYS 45  53  53  LYS LYS E . n 
E 1 46  LEU 46  53  53  LEU LEU E A n 
E 1 47  ASN 47  54  54  ASN ASN E . n 
E 1 48  GLY 48  55  55  GLY GLY E . n 
E 1 49  ILE 49  56  56  ILE ILE E . n 
E 1 50  PRO 50  57  57  PRO PRO E . n 
E 1 51  PRO 51  58  58  PRO PRO E . n 
E 1 52  LEU 52  59  59  LEU LEU E . n 
E 1 53  GLU 53  60  60  GLU GLU E . n 
E 1 54  LEU 54  61  61  LEU LEU E . n 
E 1 55  GLY 55  62  62  GLY GLY E . n 
E 1 56  ASP 56  63  63  ASP ASP E . n 
E 1 57  CYS 57  64  64  CYS CYS E . n 
E 1 58  SER 58  65  65  SER SER E . n 
E 1 59  ILE 59  66  66  ILE ILE E . n 
E 1 60  ALA 60  67  67  ALA ALA E . n 
E 1 61  GLY 61  68  68  GLY GLY E . n 
E 1 62  TRP 62  69  69  TRP TRP E . n 
E 1 63  LEU 63  70  70  LEU LEU E . n 
E 1 64  LEU 64  71  71  LEU LEU E . n 
E 1 65  GLY 65  72  72  GLY GLY E . n 
E 1 66  ASN 66  73  73  ASN ASN E . n 
E 1 67  PRO 67  74  74  PRO PRO E . n 
E 1 68  GLU 68  75  75  GLU GLU E . n 
E 1 69  CYS 69  76  76  CYS CYS E . n 
E 1 70  ASP 70  77  77  ASP ASP E . n 
E 1 71  ARG 71  78  78  ARG ARG E . n 
E 1 72  LEU 72  79  79  LEU LEU E . n 
E 1 73  LEU 73  80  80  LEU LEU E . n 
E 1 74  SER 74  81  81  SER SER E . n 
E 1 75  VAL 75  81  81  VAL VAL E A n 
E 1 76  PRO 76  82  82  PRO PRO E . n 
E 1 77  GLU 77  83  83  GLU GLU E . n 
E 1 78  TRP 78  84  84  TRP TRP E . n 
E 1 79  SER 79  85  85  SER SER E . n 
E 1 80  TYR 80  86  86  TYR TYR E . n 
E 1 81  ILE 81  87  87  ILE ILE E . n 
E 1 82  MET 82  88  88  MET MET E . n 
E 1 83  GLU 83  89  89  GLU GLU E . n 
E 1 84  LYS 84  90  90  LYS LYS E . n 
E 1 85  GLU 85  91  91  GLU GLU E . n 
E 1 86  ASN 86  92  92  ASN ASN E . n 
E 1 87  PRO 87  93  93  PRO PRO E . n 
E 1 88  ARG 88  94  94  ARG ARG E . n 
E 1 89  ASP 89  95  95  ASP ASP E . n 
E 1 90  GLY 90  95  95  GLY GLY E A n 
E 1 91  LEU 91  96  96  LEU LEU E . n 
E 1 92  CYS 92  97  97  CYS CYS E . n 
E 1 93  TYR 93  98  98  TYR TYR E . n 
E 1 94  PRO 94  99  99  PRO PRO E . n 
E 1 95  GLY 95  100 100 GLY GLY E . n 
E 1 96  SER 96  101 101 SER SER E . n 
E 1 97  PHE 97  102 102 PHE PHE E . n 
E 1 98  ASN 98  103 103 ASN ASN E . n 
E 1 99  ASP 99  104 104 ASP ASP E . n 
E 1 100 TYR 100 105 105 TYR TYR E . n 
E 1 101 GLU 101 106 106 GLU GLU E . n 
E 1 102 GLU 102 107 107 GLU GLU E . n 
E 1 103 LEU 103 108 108 LEU LEU E . n 
E 1 104 LYS 104 109 109 LYS LYS E . n 
E 1 105 HIS 105 110 110 HIS HIS E . n 
E 1 106 LEU 106 111 111 LEU LEU E . n 
E 1 107 LEU 107 112 112 LEU LEU E . n 
E 1 108 SER 108 113 113 SER SER E . n 
E 1 109 SER 109 114 114 SER SER E . n 
E 1 110 VAL 110 115 115 VAL VAL E . n 
E 1 111 LYS 111 116 116 LYS LYS E . n 
E 1 112 HIS 112 116 116 HIS HIS E A n 
E 1 113 PHE 113 116 116 PHE PHE E B n 
E 1 114 GLU 114 116 116 GLU GLU E C n 
E 1 115 LYS 115 117 117 LYS LYS E . n 
E 1 116 VAL 116 118 118 VAL VAL E . n 
E 1 117 LYS 117 119 119 LYS LYS E . n 
E 1 118 ILE 118 120 120 ILE ILE E . n 
E 1 119 LEU 119 121 121 LEU LEU E . n 
E 1 120 PRO 120 122 122 PRO PRO E . n 
E 1 121 LYS 121 123 123 LYS LYS E . n 
E 1 122 ASP 122 125 125 ASP ASP E . n 
E 1 123 ARG 123 126 126 ARG ARG E . n 
E 1 124 TRP 124 127 127 TRP TRP E . n 
E 1 125 THR 125 128 128 THR THR E . n 
E 1 126 GLN 126 129 129 GLN GLN E . n 
E 1 127 HIS 127 130 130 HIS HIS E . n 
E 1 128 THR 128 131 131 THR THR E . n 
E 1 129 THR 129 132 132 THR THR E . n 
E 1 130 THR 130 133 133 THR THR E . n 
E 1 131 GLY 131 134 134 GLY GLY E . n 
E 1 132 GLY 132 135 135 GLY GLY E . n 
E 1 133 SER 133 136 136 SER SER E . n 
E 1 134 ARG 134 137 137 ARG ARG E . n 
E 1 135 ALA 135 138 138 ALA ALA E . n 
E 1 136 CYS 136 139 139 CYS CYS E . n 
E 1 137 ALA 137 140 140 ALA ALA E . n 
E 1 138 VAL 138 141 141 VAL VAL E . n 
E 1 139 SER 139 142 142 SER SER E . n 
E 1 140 GLY 140 143 143 GLY GLY E . n 
E 1 141 ASN 141 144 144 ASN ASN E . n 
E 1 142 PRO 142 145 145 PRO PRO E . n 
E 1 143 SER 143 146 146 SER SER E . n 
E 1 144 PHE 144 147 147 PHE PHE E . n 
E 1 145 PHE 145 148 148 PHE PHE E . n 
E 1 146 ARG 146 149 149 ARG ARG E . n 
E 1 147 ASN 147 150 150 ASN ASN E . n 
E 1 148 MET 148 151 151 MET MET E . n 
E 1 149 VAL 149 152 152 VAL VAL E . n 
E 1 150 TRP 150 153 153 TRP TRP E . n 
E 1 151 LEU 151 154 154 LEU LEU E . n 
E 1 152 THR 152 155 155 THR THR E . n 
E 1 153 GLU 153 156 156 GLU GLU E . n 
E 1 154 LYS 154 157 157 LYS LYS E . n 
E 1 155 GLY 155 158 158 GLY GLY E . n 
E 1 156 SER 156 159 159 SER SER E . n 
E 1 157 ASN 157 160 160 ASN ASN E . n 
E 1 158 TYR 158 161 161 TYR TYR E . n 
E 1 159 PRO 159 162 162 PRO PRO E . n 
E 1 160 VAL 160 163 163 VAL VAL E . n 
E 1 161 ALA 161 164 164 ALA ALA E . n 
E 1 162 LYS 162 165 165 LYS LYS E . n 
E 1 163 GLY 163 166 166 GLY GLY E . n 
E 1 164 SER 164 167 167 SER SER E . n 
E 1 165 TYR 165 168 168 TYR TYR E . n 
E 1 166 ASN 166 169 169 ASN ASN E . n 
E 1 167 ASN 167 170 170 ASN ASN E . n 
E 1 168 THR 168 171 171 THR THR E . n 
E 1 169 SER 169 172 172 SER SER E . n 
E 1 170 GLY 170 173 173 GLY GLY E . n 
E 1 171 GLU 171 174 174 GLU GLU E . n 
E 1 172 GLN 172 175 175 GLN GLN E . n 
E 1 173 MET 173 176 176 MET MET E . n 
E 1 174 LEU 174 177 177 LEU LEU E . n 
E 1 175 ILE 175 178 178 ILE ILE E . n 
E 1 176 ILE 176 179 179 ILE ILE E . n 
E 1 177 TRP 177 180 180 TRP TRP E . n 
E 1 178 GLY 178 181 181 GLY GLY E . n 
E 1 179 VAL 179 182 182 VAL VAL E . n 
E 1 180 HIS 180 183 183 HIS HIS E . n 
E 1 181 HIS 181 184 184 HIS HIS E . n 
E 1 182 PRO 182 185 185 PRO PRO E . n 
E 1 183 ASN 183 186 186 ASN ASN E . n 
E 1 184 ASP 184 187 187 ASP ASP E . n 
E 1 185 GLU 185 188 188 GLU GLU E . n 
E 1 186 THR 186 189 189 THR THR E . n 
E 1 187 GLU 187 190 190 GLU GLU E . n 
E 1 188 GLN 188 191 191 GLN GLN E . n 
E 1 189 ARG 189 192 192 ARG ARG E . n 
E 1 190 THR 190 193 193 THR THR E . n 
E 1 191 LEU 191 194 194 LEU LEU E . n 
E 1 192 TYR 192 195 195 TYR TYR E . n 
E 1 193 GLN 193 196 196 GLN GLN E . n 
E 1 194 ASN 194 197 197 ASN ASN E . n 
E 1 195 VAL 195 198 198 VAL VAL E . n 
E 1 196 GLY 196 199 199 GLY GLY E . n 
E 1 197 THR 197 200 200 THR THR E . n 
E 1 198 TYR 198 201 201 TYR TYR E . n 
E 1 199 VAL 199 202 202 VAL VAL E . n 
E 1 200 SER 200 203 203 SER SER E . n 
E 1 201 VAL 201 204 204 VAL VAL E . n 
E 1 202 GLY 202 205 205 GLY GLY E . n 
E 1 203 THR 203 206 206 THR THR E . n 
E 1 204 SER 204 207 207 SER SER E . n 
E 1 205 THR 205 208 208 THR THR E . n 
E 1 206 LEU 206 209 209 LEU LEU E . n 
E 1 207 ASN 207 210 210 ASN ASN E . n 
E 1 208 LYS 208 211 211 LYS LYS E . n 
E 1 209 ARG 209 212 212 ARG ARG E . n 
E 1 210 SER 210 213 213 SER SER E . n 
E 1 211 THR 211 214 214 THR THR E . n 
E 1 212 PRO 212 215 215 PRO PRO E . n 
E 1 213 GLU 213 216 216 GLU GLU E . n 
E 1 214 ILE 214 217 217 ILE ILE E . n 
E 1 215 ALA 215 218 218 ALA ALA E . n 
E 1 216 THR 216 219 219 THR THR E . n 
E 1 217 ARG 217 220 220 ARG ARG E . n 
E 1 218 PRO 218 221 221 PRO PRO E . n 
E 1 219 LYS 219 222 222 LYS LYS E . n 
E 1 220 VAL 220 223 223 VAL VAL E . n 
E 1 221 ASN 221 224 224 ASN ASN E . n 
E 1 222 GLY 222 225 225 GLY GLY E . n 
E 1 223 GLN 223 226 226 GLN GLN E . n 
E 1 224 GLY 224 227 227 GLY GLY E . n 
E 1 225 GLY 225 228 228 GLY GLY E . n 
E 1 226 ARG 226 229 229 ARG ARG E . n 
E 1 227 MET 227 230 230 MET MET E . n 
E 1 228 GLU 228 231 231 GLU GLU E . n 
E 1 229 PHE 229 232 232 PHE PHE E . n 
E 1 230 SER 230 233 233 SER SER E . n 
E 1 231 TRP 231 234 234 TRP TRP E . n 
E 1 232 THR 232 235 235 THR THR E . n 
E 1 233 LEU 233 236 236 LEU LEU E . n 
E 1 234 LEU 234 237 237 LEU LEU E . n 
E 1 235 ASP 235 238 238 ASP ASP E . n 
E 1 236 MET 236 239 239 MET MET E . n 
E 1 237 TRP 237 240 240 TRP TRP E . n 
E 1 238 ASP 238 241 241 ASP ASP E . n 
E 1 239 THR 239 242 242 THR THR E . n 
E 1 240 ILE 240 243 243 ILE ILE E . n 
E 1 241 ASN 241 244 244 ASN ASN E . n 
E 1 242 PHE 242 245 245 PHE PHE E . n 
E 1 243 GLU 243 246 246 GLU GLU E . n 
E 1 244 SER 244 247 247 SER SER E . n 
E 1 245 THR 245 248 248 THR THR E . n 
E 1 246 GLY 246 249 249 GLY GLY E . n 
E 1 247 ASN 247 250 250 ASN ASN E . n 
E 1 248 LEU 248 251 251 LEU LEU E . n 
E 1 249 ILE 249 252 252 ILE ILE E . n 
E 1 250 ALA 250 253 253 ALA ALA E . n 
E 1 251 PRO 251 254 254 PRO PRO E . n 
E 1 252 GLU 252 255 255 GLU GLU E . n 
E 1 253 TYR 253 256 256 TYR TYR E . n 
E 1 254 GLY 254 257 257 GLY GLY E . n 
E 1 255 PHE 255 258 258 PHE PHE E . n 
E 1 256 LYS 256 259 259 LYS LYS E . n 
E 1 257 ILE 257 260 260 ILE ILE E . n 
E 1 258 SER 258 261 261 SER SER E . n 
E 1 259 LYS 259 262 262 LYS LYS E . n 
E 1 260 ARG 260 263 263 ARG ARG E . n 
E 1 261 GLY 261 263 263 GLY GLY E A n 
E 1 262 SER 262 264 264 SER SER E . n 
E 1 263 SER 263 265 265 SER SER E . n 
E 1 264 GLY 264 266 266 GLY GLY E . n 
E 1 265 ILE 265 267 267 ILE ILE E . n 
E 1 266 MET 266 268 268 MET MET E . n 
E 1 267 LYS 267 269 269 LYS LYS E . n 
E 1 268 THR 268 270 270 THR THR E . n 
E 1 269 GLU 269 271 271 GLU GLU E . n 
E 1 270 GLY 270 272 272 GLY GLY E . n 
E 1 271 THR 271 273 273 THR THR E . n 
E 1 272 LEU 272 274 274 LEU LEU E . n 
E 1 273 GLU 273 275 275 GLU GLU E . n 
E 1 274 ASN 274 276 276 ASN ASN E . n 
E 1 275 CYS 275 277 277 CYS CYS E . n 
E 1 276 GLU 276 278 278 GLU GLU E . n 
E 1 277 THR 277 279 279 THR THR E . n 
E 1 278 LYS 278 280 280 LYS LYS E . n 
E 1 279 CYS 279 281 281 CYS CYS E . n 
E 1 280 GLN 280 282 282 GLN GLN E . n 
E 1 281 THR 281 283 283 THR THR E . n 
E 1 282 PRO 282 284 284 PRO PRO E . n 
E 1 283 LEU 283 285 285 LEU LEU E . n 
E 1 284 GLY 284 286 286 GLY GLY E . n 
E 1 285 ALA 285 287 287 ALA ALA E . n 
E 1 286 ILE 286 288 288 ILE ILE E . n 
E 1 287 ASN 287 289 289 ASN ASN E . n 
E 1 288 THR 288 290 290 THR THR E . n 
E 1 289 THR 289 291 291 THR THR E . n 
E 1 290 LEU 290 292 292 LEU LEU E . n 
E 1 291 PRO 291 293 293 PRO PRO E . n 
E 1 292 PHE 292 294 294 PHE PHE E . n 
E 1 293 HIS 293 295 295 HIS HIS E . n 
E 1 294 ASN 294 296 296 ASN ASN E . n 
E 1 295 VAL 295 297 297 VAL VAL E . n 
E 1 296 HIS 296 298 298 HIS HIS E . n 
E 1 297 PRO 297 299 299 PRO PRO E . n 
E 1 298 LEU 298 300 300 LEU LEU E . n 
E 1 299 THR 299 301 301 THR THR E . n 
E 1 300 ILE 300 302 302 ILE ILE E . n 
E 1 301 GLY 301 303 303 GLY GLY E . n 
E 1 302 GLU 302 304 304 GLU GLU E . n 
E 1 303 CYS 303 305 305 CYS CYS E . n 
E 1 304 PRO 304 306 306 PRO PRO E . n 
E 1 305 LYS 305 307 307 LYS LYS E . n 
E 1 306 TYR 306 308 308 TYR TYR E . n 
E 1 307 VAL 307 309 309 VAL VAL E . n 
E 1 308 LYS 308 310 310 LYS LYS E . n 
E 1 309 SER 309 311 311 SER SER E . n 
E 1 310 GLU 310 312 312 GLU GLU E . n 
E 1 311 LYS 311 313 313 LYS LYS E . n 
E 1 312 LEU 312 314 314 LEU LEU E . n 
E 1 313 VAL 313 315 315 VAL VAL E . n 
E 1 314 LEU 314 316 316 LEU LEU E . n 
E 1 315 ALA 315 317 317 ALA ALA E . n 
E 1 316 THR 316 318 318 THR THR E . n 
E 1 317 GLY 317 319 319 GLY GLY E . n 
E 1 318 LEU 318 320 320 LEU LEU E . n 
E 1 319 ARG 319 321 321 ARG ARG E . n 
E 1 320 ASN 320 322 322 ASN ASN E . n 
E 1 321 VAL 321 323 323 VAL VAL E . n 
E 1 322 PRO 322 324 324 PRO PRO E . n 
E 1 323 GLN 323 325 ?   ?   ?   E . n 
E 1 324 ILE 324 326 ?   ?   ?   E . n 
E 1 325 GLU 325 327 ?   ?   ?   E . n 
E 1 326 SER 326 328 ?   ?   ?   E . n 
E 1 327 ARG 327 329 ?   ?   ?   E . n 
F 2 1   GLY 1   1   1   GLY GLY F . n 
F 2 2   LEU 2   2   2   LEU LEU F . n 
F 2 3   PHE 3   3   3   PHE PHE F . n 
F 2 4   GLY 4   4   4   GLY GLY F . n 
F 2 5   ALA 5   5   5   ALA ALA F . n 
F 2 6   ILE 6   6   6   ILE ILE F . n 
F 2 7   ALA 7   7   7   ALA ALA F . n 
F 2 8   GLY 8   8   8   GLY GLY F . n 
F 2 9   PHE 9   9   9   PHE PHE F . n 
F 2 10  ILE 10  10  10  ILE ILE F . n 
F 2 11  GLU 11  11  11  GLU GLU F . n 
F 2 12  GLY 12  12  12  GLY GLY F . n 
F 2 13  GLY 13  13  13  GLY GLY F . n 
F 2 14  TRP 14  14  14  TRP TRP F . n 
F 2 15  GLN 15  15  15  GLN GLN F . n 
F 2 16  GLY 16  16  16  GLY GLY F . n 
F 2 17  MET 17  17  17  MET MET F . n 
F 2 18  VAL 18  18  18  VAL VAL F . n 
F 2 19  ASP 19  19  19  ASP ASP F . n 
F 2 20  GLY 20  20  20  GLY GLY F . n 
F 2 21  TRP 21  21  21  TRP TRP F . n 
F 2 22  TYR 22  22  22  TYR TYR F . n 
F 2 23  GLY 23  23  23  GLY GLY F . n 
F 2 24  TYR 24  24  24  TYR TYR F . n 
F 2 25  HIS 25  25  25  HIS HIS F . n 
F 2 26  HIS 26  26  26  HIS HIS F . n 
F 2 27  SER 27  27  27  SER SER F . n 
F 2 28  ASN 28  28  28  ASN ASN F . n 
F 2 29  ASP 29  29  29  ASP ASP F . n 
F 2 30  GLN 30  30  30  GLN GLN F . n 
F 2 31  GLY 31  31  31  GLY GLY F . n 
F 2 32  SER 32  32  32  SER SER F . n 
F 2 33  GLY 33  33  33  GLY GLY F . n 
F 2 34  TYR 34  34  34  TYR TYR F . n 
F 2 35  ALA 35  35  35  ALA ALA F . n 
F 2 36  ALA 36  36  36  ALA ALA F . n 
F 2 37  ASP 37  37  37  ASP ASP F . n 
F 2 38  LYS 38  38  38  LYS LYS F . n 
F 2 39  GLU 39  39  39  GLU GLU F . n 
F 2 40  SER 40  40  40  SER SER F . n 
F 2 41  THR 41  41  41  THR THR F . n 
F 2 42  GLN 42  42  42  GLN GLN F . n 
F 2 43  LYS 43  43  43  LYS LYS F . n 
F 2 44  ALA 44  44  44  ALA ALA F . n 
F 2 45  PHE 45  45  45  PHE PHE F . n 
F 2 46  ASP 46  46  46  ASP ASP F . n 
F 2 47  GLY 47  47  47  GLY GLY F . n 
F 2 48  ILE 48  48  48  ILE ILE F . n 
F 2 49  THR 49  49  49  THR THR F . n 
F 2 50  ASN 50  50  50  ASN ASN F . n 
F 2 51  LYS 51  51  51  LYS LYS F . n 
F 2 52  VAL 52  52  52  VAL VAL F . n 
F 2 53  ASN 53  53  53  ASN ASN F . n 
F 2 54  SER 54  54  54  SER SER F . n 
F 2 55  VAL 55  55  55  VAL VAL F . n 
F 2 56  ILE 56  56  56  ILE ILE F . n 
F 2 57  GLU 57  57  57  GLU GLU F . n 
F 2 58  LYS 58  58  58  LYS LYS F . n 
F 2 59  MET 59  59  59  MET MET F . n 
F 2 60  ASN 60  60  60  ASN ASN F . n 
F 2 61  THR 61  61  61  THR THR F . n 
F 2 62  GLN 62  62  62  GLN GLN F . n 
F 2 63  PHE 63  63  63  PHE PHE F . n 
F 2 64  GLU 64  64  64  GLU GLU F . n 
F 2 65  ALA 65  65  65  ALA ALA F . n 
F 2 66  VAL 66  66  66  VAL VAL F . n 
F 2 67  GLY 67  67  67  GLY GLY F . n 
F 2 68  LYS 68  68  68  LYS LYS F . n 
F 2 69  GLU 69  69  69  GLU GLU F . n 
F 2 70  PHE 70  70  70  PHE PHE F . n 
F 2 71  SER 71  71  71  SER SER F . n 
F 2 72  ASN 72  72  72  ASN ASN F . n 
F 2 73  LEU 73  73  73  LEU LEU F . n 
F 2 74  GLU 74  74  74  GLU GLU F . n 
F 2 75  ARG 75  75  75  ARG ARG F . n 
F 2 76  ARG 76  76  76  ARG ARG F . n 
F 2 77  LEU 77  77  77  LEU LEU F . n 
F 2 78  GLU 78  78  78  GLU GLU F . n 
F 2 79  ASN 79  79  79  ASN ASN F . n 
F 2 80  LEU 80  80  80  LEU LEU F . n 
F 2 81  ASN 81  81  81  ASN ASN F . n 
F 2 82  LYS 82  82  82  LYS LYS F . n 
F 2 83  LYS 83  83  83  LYS LYS F . n 
F 2 84  MET 84  84  84  MET MET F . n 
F 2 85  GLU 85  85  85  GLU GLU F . n 
F 2 86  ASP 86  86  86  ASP ASP F . n 
F 2 87  GLY 87  87  87  GLY GLY F . n 
F 2 88  PHE 88  88  88  PHE PHE F . n 
F 2 89  LEU 89  89  89  LEU LEU F . n 
F 2 90  ASP 90  90  90  ASP ASP F . n 
F 2 91  VAL 91  91  91  VAL VAL F . n 
F 2 92  TRP 92  92  92  TRP TRP F . n 
F 2 93  THR 93  93  93  THR THR F . n 
F 2 94  TYR 94  94  94  TYR TYR F . n 
F 2 95  ASN 95  95  95  ASN ASN F . n 
F 2 96  ALA 96  96  96  ALA ALA F . n 
F 2 97  GLU 97  97  97  GLU GLU F . n 
F 2 98  LEU 98  98  98  LEU LEU F . n 
F 2 99  LEU 99  99  99  LEU LEU F . n 
F 2 100 VAL 100 100 100 VAL VAL F . n 
F 2 101 LEU 101 101 101 LEU LEU F . n 
F 2 102 MET 102 102 102 MET MET F . n 
F 2 103 GLU 103 103 103 GLU GLU F . n 
F 2 104 ASN 104 104 104 ASN ASN F . n 
F 2 105 GLU 105 105 105 GLU GLU F . n 
F 2 106 HIS 106 106 106 HIS HIS F . n 
F 2 107 THR 107 107 107 THR THR F . n 
F 2 108 LEU 108 108 108 LEU LEU F . n 
F 2 109 ASP 109 109 109 ASP ASP F . n 
F 2 110 PHE 110 110 110 PHE PHE F . n 
F 2 111 HIS 111 111 111 HIS HIS F . n 
F 2 112 ASP 112 112 112 ASP ASP F . n 
F 2 113 SER 113 113 113 SER SER F . n 
F 2 114 ASN 114 114 114 ASN ASN F . n 
F 2 115 VAL 115 115 115 VAL VAL F . n 
F 2 116 LYS 116 116 116 LYS LYS F . n 
F 2 117 ASN 117 117 117 ASN ASN F . n 
F 2 118 LEU 118 118 118 LEU LEU F . n 
F 2 119 TYR 119 119 119 TYR TYR F . n 
F 2 120 ASP 120 120 120 ASP ASP F . n 
F 2 121 LYS 121 121 121 LYS LYS F . n 
F 2 122 VAL 122 122 122 VAL VAL F . n 
F 2 123 ARG 123 123 123 ARG ARG F . n 
F 2 124 MET 124 124 124 MET MET F . n 
F 2 125 GLN 125 125 125 GLN GLN F . n 
F 2 126 LEU 126 126 126 LEU LEU F . n 
F 2 127 ARG 127 127 127 ARG ARG F . n 
F 2 128 ASP 128 128 128 ASP ASP F . n 
F 2 129 ASN 129 129 129 ASN ASN F . n 
F 2 130 VAL 130 130 130 VAL VAL F . n 
F 2 131 LYS 131 131 131 LYS LYS F . n 
F 2 132 GLU 132 132 132 GLU GLU F . n 
F 2 133 LEU 133 133 133 LEU LEU F . n 
F 2 134 GLY 134 134 134 GLY GLY F . n 
F 2 135 ASN 135 135 135 ASN ASN F . n 
F 2 136 GLY 136 136 136 GLY GLY F . n 
F 2 137 CYS 137 137 137 CYS CYS F . n 
F 2 138 PHE 138 138 138 PHE PHE F . n 
F 2 139 GLU 139 139 139 GLU GLU F . n 
F 2 140 PHE 140 140 140 PHE PHE F . n 
F 2 141 TYR 141 141 141 TYR TYR F . n 
F 2 142 HIS 142 142 142 HIS HIS F . n 
F 2 143 LYS 143 143 143 LYS LYS F . n 
F 2 144 CYS 144 144 144 CYS CYS F . n 
F 2 145 ASP 145 145 145 ASP ASP F . n 
F 2 146 ASP 146 146 146 ASP ASP F . n 
F 2 147 GLU 147 147 147 GLU GLU F . n 
F 2 148 CYS 148 148 148 CYS CYS F . n 
F 2 149 MET 149 149 149 MET MET F . n 
F 2 150 ASN 150 150 150 ASN ASN F . n 
F 2 151 SER 151 151 151 SER SER F . n 
F 2 152 VAL 152 152 152 VAL VAL F . n 
F 2 153 LYS 153 153 153 LYS LYS F . n 
F 2 154 ASN 154 154 154 ASN ASN F . n 
F 2 155 GLY 155 155 155 GLY GLY F . n 
F 2 156 THR 156 156 156 THR THR F . n 
F 2 157 TYR 157 157 157 TYR TYR F . n 
F 2 158 ASP 158 158 158 ASP ASP F . n 
F 2 159 TYR 159 159 159 TYR TYR F . n 
F 2 160 PRO 160 160 160 PRO PRO F . n 
F 2 161 LYS 161 161 161 LYS LYS F . n 
F 2 162 TYR 162 162 162 TYR TYR F . n 
F 2 163 GLU 163 163 163 GLU GLU F . n 
F 2 164 GLU 164 164 164 GLU GLU F . n 
F 2 165 GLU 165 165 165 GLU GLU F . n 
F 2 166 SER 166 166 166 SER SER F . n 
F 2 167 LYS 167 167 167 LYS LYS F . n 
F 2 168 LEU 168 168 168 LEU LEU F . n 
F 2 169 ASN 169 169 169 ASN ASN F . n 
F 2 170 ARG 170 170 170 ARG ARG F . n 
F 2 171 ASN 171 171 171 ASN ASN F . n 
F 2 172 GLU 172 172 172 GLU GLU F . n 
F 2 173 ILE 173 173 ?   ?   ?   F . n 
F 2 174 LYS 174 174 ?   ?   ?   F . 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 
G 3 NAG 1  330 101 NAG NAG A . 
H 3 NAG 1  331 111 NAG NAG A . 
I 3 NAG 1  331 321 NAG NAG C . 
J 4 HOH 1  1   1   HOH HOH A . 
J 4 HOH 2  2   2   HOH HOH A . 
J 4 HOH 3  3   3   HOH HOH A . 
J 4 HOH 4  5   5   HOH HOH A . 
J 4 HOH 5  6   6   HOH HOH A . 
J 4 HOH 6  332 9   HOH HOH A . 
J 4 HOH 7  333 11  HOH HOH A . 
J 4 HOH 8  334 12  HOH HOH A . 
J 4 HOH 9  335 13  HOH HOH A . 
J 4 HOH 10 336 14  HOH HOH A . 
J 4 HOH 11 337 17  HOH HOH A . 
J 4 HOH 12 338 18  HOH HOH A . 
J 4 HOH 13 339 20  HOH HOH A . 
J 4 HOH 14 340 22  HOH HOH A . 
J 4 HOH 15 341 25  HOH HOH A . 
J 4 HOH 16 342 26  HOH HOH A . 
J 4 HOH 17 343 30  HOH HOH A . 
J 4 HOH 18 344 31  HOH HOH A . 
J 4 HOH 19 345 33  HOH HOH A . 
J 4 HOH 20 346 34  HOH HOH A . 
J 4 HOH 21 347 38  HOH HOH A . 
J 4 HOH 22 348 43  HOH HOH A . 
J 4 HOH 23 349 45  HOH HOH A . 
J 4 HOH 24 350 48  HOH HOH A . 
J 4 HOH 25 351 49  HOH HOH A . 
J 4 HOH 26 352 51  HOH HOH A . 
J 4 HOH 27 353 52  HOH HOH A . 
J 4 HOH 28 354 56  HOH HOH A . 
K 4 HOH 1  175 55  HOH HOH B . 
K 4 HOH 2  176 19  HOH HOH B . 
K 4 HOH 3  177 44  HOH HOH B . 
L 4 HOH 1  4   4   HOH HOH C . 
L 4 HOH 2  332 27  HOH HOH C . 
L 4 HOH 3  333 28  HOH HOH C . 
L 4 HOH 4  334 29  HOH HOH C . 
L 4 HOH 5  335 40  HOH HOH C . 
L 4 HOH 6  336 41  HOH HOH C . 
L 4 HOH 7  337 42  HOH HOH C . 
L 4 HOH 8  338 46  HOH HOH C . 
L 4 HOH 9  339 50  HOH HOH C . 
M 4 HOH 1  175 16  HOH HOH D . 
M 4 HOH 2  176 35  HOH HOH D . 
M 4 HOH 3  177 37  HOH HOH D . 
M 4 HOH 4  178 39  HOH HOH D . 
M 4 HOH 5  179 53  HOH HOH D . 
M 4 HOH 6  180 8   HOH HOH D . 
M 4 HOH 7  181 15  HOH HOH D . 
N 4 HOH 1  7   7   HOH HOH E . 
N 4 HOH 2  330 10  HOH HOH E . 
N 4 HOH 3  331 21  HOH HOH E . 
N 4 HOH 4  332 47  HOH HOH E . 
O 4 HOH 1  175 32  HOH HOH F . 
O 4 HOH 2  176 36  HOH HOH F . 
O 4 HOH 3  177 54  HOH HOH F . 
O 4 HOH 4  178 23  HOH HOH F . 
O 4 HOH 5  179 24  HOH HOH F . 
# 
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 13  A ASN 21  ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 166 A ASN 169 ? ASN 'GLYCOSYLATION SITE' 
3 C ASN 287 C ASN 290 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O 
# 
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)' 32120 ? 
1 MORE         -166  ? 
1 'SSA (A^2)'  59290 ? 
# 
_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 2011-03-09 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-11-08 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' '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 
# 
_diffrn_reflns.diffrn_id                   1 
_diffrn_reflns.pdbx_d_res_high             2.900 
_diffrn_reflns.pdbx_d_res_low              45.000 
_diffrn_reflns.pdbx_number_obs             39294 
_diffrn_reflns.pdbx_Rmerge_I_obs           0.078 
_diffrn_reflns.pdbx_Rsym_value             ? 
_diffrn_reflns.pdbx_chi_squared            1.04 
_diffrn_reflns.av_sigmaI_over_netI         14.44 
_diffrn_reflns.pdbx_redundancy             3.40 
_diffrn_reflns.pdbx_percent_possible_obs   88.40 
_diffrn_reflns.number                      133153 
_diffrn_reflns.pdbx_observed_criterion     ? 
_diffrn_reflns.limit_h_max                 ? 
_diffrn_reflns.limit_h_min                 ? 
_diffrn_reflns.limit_k_max                 ? 
_diffrn_reflns.limit_k_min                 ? 
_diffrn_reflns.limit_l_max                 ? 
_diffrn_reflns.limit_l_min                 ? 
# 
loop_
_pdbx_diffrn_reflns_shell.diffrn_id 
_pdbx_diffrn_reflns_shell.d_res_high 
_pdbx_diffrn_reflns_shell.d_res_low 
_pdbx_diffrn_reflns_shell.number_obs 
_pdbx_diffrn_reflns_shell.rejects 
_pdbx_diffrn_reflns_shell.Rmerge_I_obs 
_pdbx_diffrn_reflns_shell.Rsym_value 
_pdbx_diffrn_reflns_shell.chi_squared 
_pdbx_diffrn_reflns_shell.redundancy 
_pdbx_diffrn_reflns_shell.percent_possible_obs 
1 6.24 45.00 ? ? 0.048 ? 0.974 3.60 99.60  
1 4.96 6.24  ? ? 0.065 ? 1.042 3.70 100.00 
1 4.33 4.96  ? ? 0.070 ? 1.003 3.60 100.00 
1 3.94 4.33  ? ? 0.080 ? 1.035 3.60 100.00 
1 3.65 3.94  ? ? 0.104 ? 1.084 3.50 99.60  
1 3.44 3.65  ? ? 0.134 ? 1.060 3.30 98.40  
1 3.27 3.44  ? ? 0.181 ? 1.069 3.30 92.50  
1 3.12 3.27  ? ? 0.217 ? 1.079 3.10 81.90  
1 3.00 3.12  ? ? 0.262 ? 1.023 2.90 64.40  
1 2.90 3.00  ? ? 0.322 ? 0.998 2.70 46.90  
# 
_pdbx_phasing_MR.entry_id                     3QQO 
_pdbx_phasing_MR.method_rotation              ? 
_pdbx_phasing_MR.method_translation           ? 
_pdbx_phasing_MR.model_details                'Phaser MODE: MR_AUTO' 
_pdbx_phasing_MR.R_factor                     ? 
_pdbx_phasing_MR.R_rigid_body                 ? 
_pdbx_phasing_MR.correlation_coeff_Fo_to_Fc   ? 
_pdbx_phasing_MR.correlation_coeff_Io_to_Ic   ? 
_pdbx_phasing_MR.d_res_high_rotation          2.750 
_pdbx_phasing_MR.d_res_low_rotation           49.440 
_pdbx_phasing_MR.d_res_high_translation       2.750 
_pdbx_phasing_MR.d_res_low_translation        49.440 
_pdbx_phasing_MR.packing                      ? 
_pdbx_phasing_MR.reflns_percent_rotation      ? 
_pdbx_phasing_MR.reflns_percent_translation   ? 
_pdbx_phasing_MR.sigma_F_rotation             ? 
_pdbx_phasing_MR.sigma_F_translation          ? 
_pdbx_phasing_MR.sigma_I_rotation             ? 
_pdbx_phasing_MR.sigma_I_translation          ? 
# 
_phasing.method   mr 
# 
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 PHASER      1.3.3     'Fri Oct 20 12:51:01 2006' program 'Randy J. Read'      cimr-phaser@lists.cam.ac.uk phasing           
http://www-structmed.cimr.cam.ac.uk/phaser/ ?   ? 
4 PHENIX      1.6.2_432 ?                          package 'Paul D. Adams'      PDAdams@lbl.gov             refinement        
http://www.phenix-online.org/               C++ ? 
5 PDB_EXTRACT 3.10      'June 10, 2010'            package PDB                  deposit@deposit.rcsb.org    'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/   C++ ? 
6 HKL-2000    .         ?                          ?       ?                    ?                           'data collection' ? ? 
? 
7 HKL-2000    .         ?                          ?       ?                    ?                           'data reduction'  ? ? 
? 
8 HKL-2000    .         ?                          ?       ?                    ?                           'data scaling'    ? ? 
? 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   ND2 
_pdbx_validate_close_contact.auth_asym_id_1   C 
_pdbx_validate_close_contact.auth_comp_id_1   ASN 
_pdbx_validate_close_contact.auth_seq_id_1    290 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   C2 
_pdbx_validate_close_contact.auth_asym_id_2   C 
_pdbx_validate_close_contact.auth_comp_id_2   NAG 
_pdbx_validate_close_contact.auth_seq_id_2    331 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.02 
# 
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 ASN A 20  ? ? -162.49 -169.76 
2   1 ASN A 21  ? ? -97.38  41.35   
3   1 GLU A 24  ? ? -54.19  109.06  
4   1 LYS A 45  ? ? -142.81 25.20   
5   1 GLU A 75  ? ? -56.83  -6.24   
6   1 SER A 81  ? ? -101.44 59.78   
7   1 GLU A 89  ? ? -174.15 136.68  
8   1 LEU A 96  ? ? -65.66  87.11   
9   1 PHE A 148 ? ? -38.35  116.93  
10  1 GLU A 174 ? ? 179.58  153.88  
11  1 GLN A 175 ? ? -46.18  150.91  
12  1 GLN A 196 ? ? 78.47   -69.10  
13  1 TRP A 240 ? ? 73.88   -16.12  
14  1 SER A 265 ? ? -135.12 -121.64 
15  1 LEU A 292 ? ? -48.12  150.11  
16  1 HIS A 298 ? ? -172.50 139.62  
17  1 LYS A 310 ? ? -93.18  58.40   
18  1 SER B 27  ? ? -143.09 54.03   
19  1 ASN B 28  ? ? -81.85  -155.65 
20  1 GLN B 30  ? ? -115.15 52.36   
21  1 ALA B 44  ? ? -63.02  -73.67  
22  1 GLN B 62  ? ? 64.25   120.09  
23  1 LYS B 68  ? ? -60.90  -102.01 
24  1 GLU B 69  ? ? 82.25   30.74   
25  1 ARG B 127 ? ? 66.77   -123.41 
26  1 ASN B 129 ? ? -65.07  3.81    
27  1 ASN B 135 ? ? -145.08 19.36   
28  1 HIS B 142 ? ? -172.57 144.28  
29  1 ASP B 145 ? ? -79.91  -168.75 
30  1 ASN B 150 ? ? -67.76  7.39    
31  1 LEU B 168 ? ? -70.42  -86.87  
32  1 ASN B 171 ? ? -60.94  -79.18  
33  1 GLU C 24  ? ? -36.54  122.47  
34  1 HIS C 38  ? ? 177.21  158.90  
35  1 HIS C 47  ? ? -90.83  -141.21 
36  1 ASN C 48  ? ? -150.33 18.78   
37  1 ASN C 54  ? ? 48.35   24.45   
38  1 PRO C 57  ? ? -50.94  171.12  
39  1 PHE C 116 B ? -173.18 143.93  
40  1 GLU C 116 C ? -179.01 108.68  
41  1 THR C 132 ? ? -140.79 33.19   
42  1 THR C 133 ? ? -140.74 23.42   
43  1 SER C 146 ? ? -159.59 -159.14 
44  1 ARG C 149 ? ? -52.55  -8.69   
45  1 LEU C 154 ? ? -34.20  118.24  
46  1 PRO C 162 ? ? -58.44  -165.67 
47  1 ALA C 164 ? ? -68.59  99.19   
48  1 GLU C 174 ? ? 179.57  161.56  
49  1 GLN C 175 ? ? -45.02  155.19  
50  1 GLN C 196 ? ? 71.44   -77.70  
51  1 THR C 206 ? ? -128.59 -164.42 
52  1 TRP C 240 ? ? 85.90   -16.66  
53  1 GLU C 246 ? ? -167.81 107.44  
54  1 ASN C 250 ? ? 72.19   -2.42   
55  1 ILE C 260 ? ? -174.33 127.31  
56  1 SER C 266 ? ? -144.84 -126.56 
57  1 THR C 280 ? ? 177.35  148.45  
58  1 THR C 292 ? ? -144.37 -15.97  
59  1 ASN C 297 ? ? -156.56 26.73   
60  1 VAL C 298 ? ? -65.26  -77.46  
61  1 LEU C 301 ? ? -55.84  97.09   
62  1 ALA D 5   ? ? -73.40  -74.14  
63  1 ALA D 35  ? ? 171.47  108.14  
64  1 GLU D 39  ? ? -66.80  -70.88  
65  1 GLN D 62  ? ? 83.49   -109.67 
66  1 PHE D 63  ? ? 160.25  104.94  
67  1 LYS D 68  ? ? -64.72  -110.72 
68  1 ARG D 127 ? ? 66.65   -146.68 
69  1 ASP D 128 ? ? -64.66  5.04    
70  1 ASP D 145 ? ? -64.08  -161.18 
71  1 ASP D 158 ? ? -101.74 65.43   
72  1 LEU D 168 ? ? -61.88  -73.54  
73  1 ASN D 171 ? ? -90.43  -84.75  
74  1 GLU E 24  ? ? -36.09  133.75  
75  1 ASN E 33  ? ? 55.93   80.31   
76  1 HIS E 47  ? ? -92.27  -137.61 
77  1 ASN E 48  ? ? -153.68 -2.69   
78  1 LYS E 53  ? ? -61.53  -171.26 
79  1 ASN E 54  ? ? 57.19   16.27   
80  1 PRO E 58  ? ? -69.77  -135.91 
81  1 LEU E 59  ? ? -164.90 62.23   
82  1 TRP E 69  ? ? -58.30  -77.22  
83  1 PRO E 74  ? ? -47.93  -19.93  
84  1 LYS E 90  ? ? -49.54  159.98  
85  1 PRO E 99  ? ? -48.73  153.58  
86  1 LEU E 112 ? ? -96.49  37.28   
87  1 LYS E 116 ? ? -72.79  -76.99  
88  1 PHE E 116 B ? -176.74 134.83  
89  1 THR E 132 ? ? -117.90 50.55   
90  1 THR E 133 ? ? -152.22 -2.48   
91  1 SER E 159 ? ? 42.81   22.37   
92  1 VAL E 163 ? ? -38.87  127.52  
93  1 GLN E 196 ? ? 61.82   -67.75  
94  1 THR E 206 ? ? -146.16 -154.53 
95  1 ASN E 210 ? ? -178.79 78.27   
96  1 GLU E 246 ? ? -171.77 111.00  
97  1 ASN E 250 ? ? 87.00   -29.18  
98  1 SER E 265 ? ? -127.96 -128.74 
99  1 ASN E 289 ? ? -105.44 75.24   
100 1 LEU E 292 ? ? -49.39  153.67  
101 1 VAL E 297 ? ? -60.20  -89.08  
102 1 PRO E 306 ? ? -57.24  174.25  
103 1 ALA F 5   ? ? -80.09  -95.04  
104 1 ILE F 10  ? ? -100.09 65.69   
105 1 GLU F 11  ? ? -18.18  -66.64  
106 1 VAL F 18  ? ? -148.95 15.09   
107 1 TRP F 21  ? ? -79.30  -70.11  
108 1 HIS F 25  ? ? -162.09 94.04   
109 1 ASN F 28  ? ? -99.35  -151.32 
110 1 GLN F 62  ? ? 71.26   -138.24 
111 1 LYS F 68  ? ? -46.25  -90.58  
112 1 GLU F 69  ? ? 79.10   -14.17  
113 1 SER F 71  ? ? -73.18  -159.67 
114 1 MET F 84  ? ? -92.53  -65.88  
115 1 ARG F 127 ? ? 56.47   -128.55 
116 1 ASP F 145 ? ? -77.12  -169.63 
117 1 ASP F 146 ? ? -58.56  -72.41  
118 1 GLU F 147 ? ? -49.14  -19.35  
# 
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 GLN 325 ? A GLN 323 
2  1 Y 1 A ILE 326 ? A ILE 324 
3  1 Y 1 A GLU 327 ? A GLU 325 
4  1 Y 1 A SER 328 ? A SER 326 
5  1 Y 1 A ARG 329 ? A ARG 327 
6  1 Y 1 B ILE 173 ? B ILE 173 
7  1 Y 1 B LYS 174 ? B LYS 174 
8  1 Y 1 C GLN 326 ? C GLN 323 
9  1 Y 1 C ILE 327 ? C ILE 324 
10 1 Y 1 C GLU 328 ? C GLU 325 
11 1 Y 1 C SER 329 ? C SER 326 
12 1 Y 1 C ARG 330 ? C ARG 327 
13 1 Y 1 D ILE 173 ? D ILE 173 
14 1 Y 1 D LYS 174 ? D LYS 174 
15 1 Y 1 E GLN 325 ? E GLN 323 
16 1 Y 1 E ILE 326 ? E ILE 324 
17 1 Y 1 E GLU 327 ? E GLU 325 
18 1 Y 1 E SER 328 ? E SER 326 
19 1 Y 1 E ARG 329 ? E ARG 327 
20 1 Y 1 F ILE 173 ? F ILE 173 
21 1 Y 1 F LYS 174 ? F LYS 174 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 N-ACETYL-D-GLUCOSAMINE NAG 
4 water                  HOH 
# 
