data_8UVW
# 
_entry.id   8UVW 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8UVW         pdb_00008uvw 10.2210/pdb8uvw/pdb 
WWPDB D_1000278863 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_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         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8UVW 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jatainer@gmail.com 
_pdbx_contact_author.name_first         John 
_pdbx_contact_author.name_last          Tainer 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-1659-2429 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Longo, M.A.'  1 ?                   
'Perera, R.'   2 ?                   
'Tsai, C.-L.'  3 0000-0002-0365-2405 
'Tainer, J.A.' 4 0000-0003-1659-2429 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Molecular Recognition of RAD51 by the BRCA2 Carboxy Terminal Domain' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Longo, M.A.' 1 ? 
primary 'Syed, M.A.'  2 ? 
# 
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 'Breast cancer type 2 susceptibility protein, DNA repair protein RAD51 homolog 1 fusion' 32212.562 1  ? C319S ? 
? 
2 polymer     man 'DNA repair protein RAD51 homolog 1,Breast cancer type 2 susceptibility protein'         31215.408 1  ? 
S208E,A209D,C3287A,C3304A,C391S ? ? 
3 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"                                                               427.201   2  ? ? ? ? 
4 non-polymer syn 'BERYLLIUM TRIFLUORIDE ION'                                                              66.007    2  ? ? ? ? 
5 non-polymer syn 1,2-ETHANEDIOL                                                                           62.068    2  ? ? ? ? 
6 water       nat water                                                                                    18.015    33 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Fanconi anemia group D1 protein,HsRAD51,hRAD51,RAD51 homolog A' 
2 'Fanconi anemia group D1 protein'                                
# 
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 
;GSKEPTLLGFHTASGKKVKIAKESLDKVKNLFDTGSTGSTGSGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSI
TEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQ
LLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAAD
PKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPSLPEAEAMFAINADGVGDAKD
;
;GSKEPTLLGFHTASGKKVKIAKESLDKVKNLFDTGSTGSTGSGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSI
TEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQ
LLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAAD
PKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPSLPEAEAMFAINADGVGDAKD
;
B ? 
2 'polypeptide(L)' no no 
;SEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAE
RYGLSGSDVLDNVAYARAFNTDHQTQLLYQAEDMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLA
DEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPSLPEAEAMFAINADGVGD
AKDSSDSSLSSPSALDFLSRLPLPPPVSPIATFVSPAAQKAFQPPRSAG
;
;SEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAE
RYGLSGSDVLDNVAYARAFNTDHQTQLLYQAEDMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLA
DEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPSLPEAEAMFAINADGVGD
AKDSSDSSLSSPSALDFLSRLPLPPPVSPIATFVSPAAQKAFQPPRSAG
;
D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 "ADENOSINE-5'-DIPHOSPHATE"  ADP 
4 'BERYLLIUM TRIFLUORIDE ION' BEF 
5 1,2-ETHANEDIOL              EDO 
6 water                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   LYS n 
1 4   GLU n 
1 5   PRO n 
1 6   THR n 
1 7   LEU n 
1 8   LEU n 
1 9   GLY n 
1 10  PHE n 
1 11  HIS n 
1 12  THR n 
1 13  ALA n 
1 14  SER n 
1 15  GLY n 
1 16  LYS n 
1 17  LYS n 
1 18  VAL n 
1 19  LYS n 
1 20  ILE n 
1 21  ALA n 
1 22  LYS n 
1 23  GLU n 
1 24  SER n 
1 25  LEU n 
1 26  ASP n 
1 27  LYS n 
1 28  VAL n 
1 29  LYS n 
1 30  ASN n 
1 31  LEU n 
1 32  PHE n 
1 33  ASP n 
1 34  THR n 
1 35  GLY n 
1 36  SER n 
1 37  THR n 
1 38  GLY n 
1 39  SER n 
1 40  THR n 
1 41  GLY n 
1 42  SER n 
1 43  GLY n 
1 44  PHE n 
1 45  THR n 
1 46  THR n 
1 47  ALA n 
1 48  THR n 
1 49  GLU n 
1 50  PHE n 
1 51  HIS n 
1 52  GLN n 
1 53  ARG n 
1 54  ARG n 
1 55  SER n 
1 56  GLU n 
1 57  ILE n 
1 58  ILE n 
1 59  GLN n 
1 60  ILE n 
1 61  THR n 
1 62  THR n 
1 63  GLY n 
1 64  SER n 
1 65  LYS n 
1 66  GLU n 
1 67  LEU n 
1 68  ASP n 
1 69  LYS n 
1 70  LEU n 
1 71  LEU n 
1 72  GLN n 
1 73  GLY n 
1 74  GLY n 
1 75  ILE n 
1 76  GLU n 
1 77  THR n 
1 78  GLY n 
1 79  SER n 
1 80  ILE n 
1 81  THR n 
1 82  GLU n 
1 83  MET n 
1 84  PHE n 
1 85  GLY n 
1 86  GLU n 
1 87  PHE n 
1 88  ARG n 
1 89  THR n 
1 90  GLY n 
1 91  LYS n 
1 92  THR n 
1 93  GLN n 
1 94  ILE n 
1 95  CYS n 
1 96  HIS n 
1 97  THR n 
1 98  LEU n 
1 99  ALA n 
1 100 VAL n 
1 101 THR n 
1 102 CYS n 
1 103 GLN n 
1 104 LEU n 
1 105 PRO n 
1 106 ILE n 
1 107 ASP n 
1 108 ARG n 
1 109 GLY n 
1 110 GLY n 
1 111 GLY n 
1 112 GLU n 
1 113 GLY n 
1 114 LYS n 
1 115 ALA n 
1 116 MET n 
1 117 TYR n 
1 118 ILE n 
1 119 ASP n 
1 120 THR n 
1 121 GLU n 
1 122 GLY n 
1 123 THR n 
1 124 PHE n 
1 125 ARG n 
1 126 PRO n 
1 127 GLU n 
1 128 ARG n 
1 129 LEU n 
1 130 LEU n 
1 131 ALA n 
1 132 VAL n 
1 133 ALA n 
1 134 GLU n 
1 135 ARG n 
1 136 TYR n 
1 137 GLY n 
1 138 LEU n 
1 139 SER n 
1 140 GLY n 
1 141 SER n 
1 142 ASP n 
1 143 VAL n 
1 144 LEU n 
1 145 ASP n 
1 146 ASN n 
1 147 VAL n 
1 148 ALA n 
1 149 TYR n 
1 150 ALA n 
1 151 ARG n 
1 152 ALA n 
1 153 PHE n 
1 154 ASN n 
1 155 THR n 
1 156 ASP n 
1 157 HIS n 
1 158 GLN n 
1 159 THR n 
1 160 GLN n 
1 161 LEU n 
1 162 LEU n 
1 163 TYR n 
1 164 GLN n 
1 165 ALA n 
1 166 SER n 
1 167 ALA n 
1 168 MET n 
1 169 MET n 
1 170 VAL n 
1 171 GLU n 
1 172 SER n 
1 173 ARG n 
1 174 TYR n 
1 175 ALA n 
1 176 LEU n 
1 177 LEU n 
1 178 ILE n 
1 179 VAL n 
1 180 ASP n 
1 181 SER n 
1 182 ALA n 
1 183 THR n 
1 184 ALA n 
1 185 LEU n 
1 186 TYR n 
1 187 ARG n 
1 188 THR n 
1 189 ASP n 
1 190 TYR n 
1 191 SER n 
1 192 GLY n 
1 193 ARG n 
1 194 GLY n 
1 195 GLU n 
1 196 LEU n 
1 197 SER n 
1 198 ALA n 
1 199 ARG n 
1 200 GLN n 
1 201 MET n 
1 202 HIS n 
1 203 LEU n 
1 204 ALA n 
1 205 ARG n 
1 206 PHE n 
1 207 LEU n 
1 208 ARG n 
1 209 MET n 
1 210 LEU n 
1 211 LEU n 
1 212 ARG n 
1 213 LEU n 
1 214 ALA n 
1 215 ASP n 
1 216 GLU n 
1 217 PHE n 
1 218 GLY n 
1 219 VAL n 
1 220 ALA n 
1 221 VAL n 
1 222 VAL n 
1 223 ILE n 
1 224 THR n 
1 225 ASN n 
1 226 GLN n 
1 227 VAL n 
1 228 VAL n 
1 229 ALA n 
1 230 GLN n 
1 231 VAL n 
1 232 ASP n 
1 233 GLY n 
1 234 ALA n 
1 235 ALA n 
1 236 MET n 
1 237 PHE n 
1 238 ALA n 
1 239 ALA n 
1 240 ASP n 
1 241 PRO n 
1 242 LYS n 
1 243 LYS n 
1 244 PRO n 
1 245 ILE n 
1 246 GLY n 
1 247 GLY n 
1 248 ASN n 
1 249 ILE n 
1 250 ILE n 
1 251 ALA n 
1 252 HIS n 
1 253 ALA n 
1 254 SER n 
1 255 THR n 
1 256 THR n 
1 257 ARG n 
1 258 LEU n 
1 259 TYR n 
1 260 LEU n 
1 261 ARG n 
1 262 LYS n 
1 263 GLY n 
1 264 ARG n 
1 265 GLY n 
1 266 GLU n 
1 267 THR n 
1 268 ARG n 
1 269 ILE n 
1 270 CYS n 
1 271 LYS n 
1 272 ILE n 
1 273 TYR n 
1 274 ASP n 
1 275 SER n 
1 276 PRO n 
1 277 SER n 
1 278 LEU n 
1 279 PRO n 
1 280 GLU n 
1 281 ALA n 
1 282 GLU n 
1 283 ALA n 
1 284 MET n 
1 285 PHE n 
1 286 ALA n 
1 287 ILE n 
1 288 ASN n 
1 289 ALA n 
1 290 ASP n 
1 291 GLY n 
1 292 VAL n 
1 293 GLY n 
1 294 ASP n 
1 295 ALA n 
1 296 LYS n 
1 297 ASP n 
2 1   SER n 
2 2   GLU n 
2 3   ILE n 
2 4   ILE n 
2 5   GLN n 
2 6   ILE n 
2 7   THR n 
2 8   THR n 
2 9   GLY n 
2 10  SER n 
2 11  LYS n 
2 12  GLU n 
2 13  LEU n 
2 14  ASP n 
2 15  LYS n 
2 16  LEU n 
2 17  LEU n 
2 18  GLN n 
2 19  GLY n 
2 20  GLY n 
2 21  ILE n 
2 22  GLU n 
2 23  THR n 
2 24  GLY n 
2 25  SER n 
2 26  ILE n 
2 27  THR n 
2 28  GLU n 
2 29  MET n 
2 30  PHE n 
2 31  GLY n 
2 32  GLU n 
2 33  PHE n 
2 34  ARG n 
2 35  THR n 
2 36  GLY n 
2 37  LYS n 
2 38  THR n 
2 39  GLN n 
2 40  ILE n 
2 41  CYS n 
2 42  HIS n 
2 43  THR n 
2 44  LEU n 
2 45  ALA n 
2 46  VAL n 
2 47  THR n 
2 48  CYS n 
2 49  GLN n 
2 50  LEU n 
2 51  PRO n 
2 52  ILE n 
2 53  ASP n 
2 54  ARG n 
2 55  GLY n 
2 56  GLY n 
2 57  GLY n 
2 58  GLU n 
2 59  GLY n 
2 60  LYS n 
2 61  ALA n 
2 62  MET n 
2 63  TYR n 
2 64  ILE n 
2 65  ASP n 
2 66  THR n 
2 67  GLU n 
2 68  GLY n 
2 69  THR n 
2 70  PHE n 
2 71  ARG n 
2 72  PRO n 
2 73  GLU n 
2 74  ARG n 
2 75  LEU n 
2 76  LEU n 
2 77  ALA n 
2 78  VAL n 
2 79  ALA n 
2 80  GLU n 
2 81  ARG n 
2 82  TYR n 
2 83  GLY n 
2 84  LEU n 
2 85  SER n 
2 86  GLY n 
2 87  SER n 
2 88  ASP n 
2 89  VAL n 
2 90  LEU n 
2 91  ASP n 
2 92  ASN n 
2 93  VAL n 
2 94  ALA n 
2 95  TYR n 
2 96  ALA n 
2 97  ARG n 
2 98  ALA n 
2 99  PHE n 
2 100 ASN n 
2 101 THR n 
2 102 ASP n 
2 103 HIS n 
2 104 GLN n 
2 105 THR n 
2 106 GLN n 
2 107 LEU n 
2 108 LEU n 
2 109 TYR n 
2 110 GLN n 
2 111 ALA n 
2 112 GLU n 
2 113 ASP n 
2 114 MET n 
2 115 MET n 
2 116 VAL n 
2 117 GLU n 
2 118 SER n 
2 119 ARG n 
2 120 TYR n 
2 121 ALA n 
2 122 LEU n 
2 123 LEU n 
2 124 ILE n 
2 125 VAL n 
2 126 ASP n 
2 127 SER n 
2 128 ALA n 
2 129 THR n 
2 130 ALA n 
2 131 LEU n 
2 132 TYR n 
2 133 ARG n 
2 134 THR n 
2 135 ASP n 
2 136 TYR n 
2 137 SER n 
2 138 GLY n 
2 139 ARG n 
2 140 GLY n 
2 141 GLU n 
2 142 LEU n 
2 143 SER n 
2 144 ALA n 
2 145 ARG n 
2 146 GLN n 
2 147 MET n 
2 148 HIS n 
2 149 LEU n 
2 150 ALA n 
2 151 ARG n 
2 152 PHE n 
2 153 LEU n 
2 154 ARG n 
2 155 MET n 
2 156 LEU n 
2 157 LEU n 
2 158 ARG n 
2 159 LEU n 
2 160 ALA n 
2 161 ASP n 
2 162 GLU n 
2 163 PHE n 
2 164 GLY n 
2 165 VAL n 
2 166 ALA n 
2 167 VAL n 
2 168 VAL n 
2 169 ILE n 
2 170 THR n 
2 171 ASN n 
2 172 GLN n 
2 173 VAL n 
2 174 VAL n 
2 175 ALA n 
2 176 GLN n 
2 177 VAL n 
2 178 ASP n 
2 179 GLY n 
2 180 ALA n 
2 181 ALA n 
2 182 MET n 
2 183 PHE n 
2 184 ALA n 
2 185 ALA n 
2 186 ASP n 
2 187 PRO n 
2 188 LYS n 
2 189 LYS n 
2 190 PRO n 
2 191 ILE n 
2 192 GLY n 
2 193 GLY n 
2 194 ASN n 
2 195 ILE n 
2 196 ILE n 
2 197 ALA n 
2 198 HIS n 
2 199 ALA n 
2 200 SER n 
2 201 THR n 
2 202 THR n 
2 203 ARG n 
2 204 LEU n 
2 205 TYR n 
2 206 LEU n 
2 207 ARG n 
2 208 LYS n 
2 209 GLY n 
2 210 ARG n 
2 211 GLY n 
2 212 GLU n 
2 213 THR n 
2 214 ARG n 
2 215 ILE n 
2 216 CYS n 
2 217 LYS n 
2 218 ILE n 
2 219 TYR n 
2 220 ASP n 
2 221 SER n 
2 222 PRO n 
2 223 SER n 
2 224 LEU n 
2 225 PRO n 
2 226 GLU n 
2 227 ALA n 
2 228 GLU n 
2 229 ALA n 
2 230 MET n 
2 231 PHE n 
2 232 ALA n 
2 233 ILE n 
2 234 ASN n 
2 235 ALA n 
2 236 ASP n 
2 237 GLY n 
2 238 VAL n 
2 239 GLY n 
2 240 ASP n 
2 241 ALA n 
2 242 LYS n 
2 243 ASP n 
2 244 SER n 
2 245 SER n 
2 246 ASP n 
2 247 SER n 
2 248 SER n 
2 249 LEU n 
2 250 SER n 
2 251 SER n 
2 252 PRO n 
2 253 SER n 
2 254 ALA n 
2 255 LEU n 
2 256 ASP n 
2 257 PHE n 
2 258 LEU n 
2 259 SER n 
2 260 ARG n 
2 261 LEU n 
2 262 PRO n 
2 263 LEU n 
2 264 PRO n 
2 265 PRO n 
2 266 PRO n 
2 267 VAL n 
2 268 SER n 
2 269 PRO n 
2 270 ILE n 
2 271 ALA n 
2 272 THR n 
2 273 PHE n 
2 274 VAL n 
2 275 SER n 
2 276 PRO n 
2 277 ALA n 
2 278 ALA n 
2 279 GLN n 
2 280 LYS n 
2 281 ALA n 
2 282 PHE n 
2 283 GLN n 
2 284 PRO n 
2 285 PRO n 
2 286 ARG n 
2 287 SER n 
2 288 ALA n 
2 289 GLY 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 'Biological sequence' 1   42  Human ? 'BRCA2, FACD, FANCD1' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 43  297 Human ? 'RAD51, RAD51A, RECA' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1   243 human ? RAD51                 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 2 sample 'Biological sequence' 244 289 human ? 'BRCA2, FACD, FANCD1' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE"  ?                 'C10 H15 N5 O10 P2' 427.201 
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 
BEF non-polymer         . 'BERYLLIUM TRIFLUORIDE ION' ?                 'Be F3 -1'          66.007  
CYS 'L-peptide linking' y CYSTEINE                    ?                 'C3 H7 N O2 S'      121.158 
EDO non-polymer         . 1,2-ETHANEDIOL              'ETHYLENE GLYCOL' 'C2 H6 O2'          62.068  
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 
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 
TYR 'L-peptide linking' y TYROSINE                    ?                 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                      ?                 'C5 H11 N O2'       117.146 
# 
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   GLY 1   1515 ?    ?   ?   B . n 
A 1 2   SER 2   1516 ?    ?   ?   B . n 
A 1 3   LYS 3   1517 ?    ?   ?   B . n 
A 1 4   GLU 4   1518 ?    ?   ?   B . n 
A 1 5   PRO 5   1519 ?    ?   ?   B . n 
A 1 6   THR 6   1520 1520 THR THR B . n 
A 1 7   LEU 7   1521 1521 LEU LEU B . n 
A 1 8   LEU 8   1522 1522 LEU LEU B . n 
A 1 9   GLY 9   1523 1523 GLY GLY B . n 
A 1 10  PHE 10  1524 1524 PHE PHE B . n 
A 1 11  HIS 11  1525 1525 HIS HIS B . n 
A 1 12  THR 12  1526 1526 THR THR B . n 
A 1 13  ALA 13  1527 1527 ALA ALA B . n 
A 1 14  SER 14  1528 1528 SER SER B . n 
A 1 15  GLY 15  1529 1529 GLY GLY B . n 
A 1 16  LYS 16  1530 1530 LYS LYS B . n 
A 1 17  LYS 17  1531 1531 LYS LYS B . n 
A 1 18  VAL 18  1532 1532 VAL VAL B . n 
A 1 19  LYS 19  1533 1533 LYS LYS B . n 
A 1 20  ILE 20  1534 1534 ILE ILE B . n 
A 1 21  ALA 21  1535 1535 ALA ALA B . n 
A 1 22  LYS 22  1536 1536 LYS LYS B . n 
A 1 23  GLU 23  1537 1537 GLU GLU B . n 
A 1 24  SER 24  1538 1538 SER SER B . n 
A 1 25  LEU 25  1539 1539 LEU LEU B . n 
A 1 26  ASP 26  1540 1540 ASP ASP B . n 
A 1 27  LYS 27  1541 1541 LYS LYS B . n 
A 1 28  VAL 28  1542 1542 VAL VAL B . n 
A 1 29  LYS 29  1543 1543 LYS LYS B . n 
A 1 30  ASN 30  1544 1544 ASN ASN B . n 
A 1 31  LEU 31  1545 1545 LEU LEU B . n 
A 1 32  PHE 32  1546 1546 PHE PHE B . n 
A 1 33  ASP 33  1547 1547 ASP ASP B . n 
A 1 34  THR 34  76   ?    ?   ?   B . n 
A 1 35  GLY 35  77   ?    ?   ?   B . n 
A 1 36  SER 36  78   ?    ?   ?   B . n 
A 1 37  THR 37  79   ?    ?   ?   B . n 
A 1 38  GLY 38  80   ?    ?   ?   B . n 
A 1 39  SER 39  81   ?    ?   ?   B . n 
A 1 40  THR 40  82   ?    ?   ?   B . n 
A 1 41  GLY 41  83   83   GLY GLY B . n 
A 1 42  SER 42  84   84   SER SER B . n 
A 1 43  GLY 43  85   85   GLY GLY B . n 
A 1 44  PHE 44  86   86   PHE PHE B . n 
A 1 45  THR 45  87   87   THR THR B . n 
A 1 46  THR 46  88   88   THR THR B . n 
A 1 47  ALA 47  89   89   ALA ALA B . n 
A 1 48  THR 48  90   90   THR THR B . n 
A 1 49  GLU 49  91   91   GLU GLU B . n 
A 1 50  PHE 50  92   92   PHE PHE B . n 
A 1 51  HIS 51  93   93   HIS HIS B . n 
A 1 52  GLN 52  94   94   GLN GLN B . n 
A 1 53  ARG 53  95   95   ARG ARG B . n 
A 1 54  ARG 54  96   96   ARG ARG B . n 
A 1 55  SER 55  97   97   SER SER B . n 
A 1 56  GLU 56  98   98   GLU GLU B . n 
A 1 57  ILE 57  99   99   ILE ILE B . n 
A 1 58  ILE 58  100  100  ILE ILE B . n 
A 1 59  GLN 59  101  101  GLN GLN B . n 
A 1 60  ILE 60  102  102  ILE ILE B . n 
A 1 61  THR 61  103  103  THR THR B . n 
A 1 62  THR 62  104  104  THR THR B . n 
A 1 63  GLY 63  105  105  GLY GLY B . n 
A 1 64  SER 64  106  106  SER SER B . n 
A 1 65  LYS 65  107  107  LYS LYS B . n 
A 1 66  GLU 66  108  108  GLU GLU B . n 
A 1 67  LEU 67  109  109  LEU LEU B . n 
A 1 68  ASP 68  110  110  ASP ASP B . n 
A 1 69  LYS 69  111  111  LYS LYS B . n 
A 1 70  LEU 70  112  112  LEU LEU B . n 
A 1 71  LEU 71  113  113  LEU LEU B . n 
A 1 72  GLN 72  114  114  GLN GLN B . n 
A 1 73  GLY 73  115  115  GLY GLY B . n 
A 1 74  GLY 74  116  116  GLY GLY B . n 
A 1 75  ILE 75  117  117  ILE ILE B . n 
A 1 76  GLU 76  118  118  GLU GLU B . n 
A 1 77  THR 77  119  119  THR THR B . n 
A 1 78  GLY 78  120  120  GLY GLY B . n 
A 1 79  SER 79  121  121  SER SER B . n 
A 1 80  ILE 80  122  122  ILE ILE B . n 
A 1 81  THR 81  123  123  THR THR B . n 
A 1 82  GLU 82  124  124  GLU GLU B . n 
A 1 83  MET 83  125  125  MET MET B . n 
A 1 84  PHE 84  126  126  PHE PHE B . n 
A 1 85  GLY 85  127  127  GLY GLY B . n 
A 1 86  GLU 86  128  128  GLU GLU B . n 
A 1 87  PHE 87  129  129  PHE PHE B . n 
A 1 88  ARG 88  130  130  ARG ARG B . n 
A 1 89  THR 89  131  131  THR THR B . n 
A 1 90  GLY 90  132  132  GLY GLY B . n 
A 1 91  LYS 91  133  133  LYS LYS B . n 
A 1 92  THR 92  134  134  THR THR B . n 
A 1 93  GLN 93  135  135  GLN GLN B . n 
A 1 94  ILE 94  136  136  ILE ILE B . n 
A 1 95  CYS 95  137  137  CYS CYS B . n 
A 1 96  HIS 96  138  138  HIS HIS B . n 
A 1 97  THR 97  139  139  THR THR B . n 
A 1 98  LEU 98  140  140  LEU LEU B . n 
A 1 99  ALA 99  141  141  ALA ALA B . n 
A 1 100 VAL 100 142  142  VAL VAL B . n 
A 1 101 THR 101 143  143  THR THR B . n 
A 1 102 CYS 102 144  144  CYS CYS B . n 
A 1 103 GLN 103 145  145  GLN GLN B . n 
A 1 104 LEU 104 146  146  LEU LEU B . n 
A 1 105 PRO 105 147  147  PRO PRO B . n 
A 1 106 ILE 106 148  148  ILE ILE B . n 
A 1 107 ASP 107 149  149  ASP ASP B . n 
A 1 108 ARG 108 150  150  ARG ARG B . n 
A 1 109 GLY 109 151  151  GLY GLY B . n 
A 1 110 GLY 110 152  152  GLY GLY B . n 
A 1 111 GLY 111 153  153  GLY GLY B . n 
A 1 112 GLU 112 154  154  GLU GLU B . n 
A 1 113 GLY 113 155  155  GLY GLY B . n 
A 1 114 LYS 114 156  156  LYS LYS B . n 
A 1 115 ALA 115 157  157  ALA ALA B . n 
A 1 116 MET 116 158  158  MET MET B . n 
A 1 117 TYR 117 159  159  TYR TYR B . n 
A 1 118 ILE 118 160  160  ILE ILE B . n 
A 1 119 ASP 119 161  161  ASP ASP B . n 
A 1 120 THR 120 162  162  THR THR B . n 
A 1 121 GLU 121 163  163  GLU GLU B . n 
A 1 122 GLY 122 164  164  GLY GLY B . n 
A 1 123 THR 123 165  165  THR THR B . n 
A 1 124 PHE 124 166  166  PHE PHE B . n 
A 1 125 ARG 125 167  167  ARG ARG B . n 
A 1 126 PRO 126 168  168  PRO PRO B . n 
A 1 127 GLU 127 169  169  GLU GLU B . n 
A 1 128 ARG 128 170  170  ARG ARG B . n 
A 1 129 LEU 129 171  171  LEU LEU B . n 
A 1 130 LEU 130 172  172  LEU LEU B . n 
A 1 131 ALA 131 173  173  ALA ALA B . n 
A 1 132 VAL 132 174  174  VAL VAL B . n 
A 1 133 ALA 133 175  175  ALA ALA B . n 
A 1 134 GLU 134 176  176  GLU GLU B . n 
A 1 135 ARG 135 177  177  ARG ARG B . n 
A 1 136 TYR 136 178  178  TYR TYR B . n 
A 1 137 GLY 137 179  179  GLY GLY B . n 
A 1 138 LEU 138 180  180  LEU LEU B . n 
A 1 139 SER 139 181  181  SER SER B . n 
A 1 140 GLY 140 182  182  GLY GLY B . n 
A 1 141 SER 141 183  183  SER SER B . n 
A 1 142 ASP 142 184  184  ASP ASP B . n 
A 1 143 VAL 143 185  185  VAL VAL B . n 
A 1 144 LEU 144 186  186  LEU LEU B . n 
A 1 145 ASP 145 187  187  ASP ASP B . n 
A 1 146 ASN 146 188  188  ASN ASN B . n 
A 1 147 VAL 147 189  189  VAL VAL B . n 
A 1 148 ALA 148 190  190  ALA ALA B . n 
A 1 149 TYR 149 191  191  TYR TYR B . n 
A 1 150 ALA 150 192  192  ALA ALA B . n 
A 1 151 ARG 151 193  193  ARG ARG B . n 
A 1 152 ALA 152 194  194  ALA ALA B . n 
A 1 153 PHE 153 195  195  PHE PHE B . n 
A 1 154 ASN 154 196  196  ASN ASN B . n 
A 1 155 THR 155 197  197  THR THR B . n 
A 1 156 ASP 156 198  198  ASP ASP B . n 
A 1 157 HIS 157 199  199  HIS HIS B . n 
A 1 158 GLN 158 200  200  GLN GLN B . n 
A 1 159 THR 159 201  201  THR THR B . n 
A 1 160 GLN 160 202  202  GLN GLN B . n 
A 1 161 LEU 161 203  203  LEU LEU B . n 
A 1 162 LEU 162 204  204  LEU LEU B . n 
A 1 163 TYR 163 205  205  TYR TYR B . n 
A 1 164 GLN 164 206  206  GLN GLN B . n 
A 1 165 ALA 165 207  207  ALA ALA B . n 
A 1 166 SER 166 208  208  SER SER B . n 
A 1 167 ALA 167 209  209  ALA ALA B . n 
A 1 168 MET 168 210  210  MET MET B . n 
A 1 169 MET 169 211  211  MET MET B . n 
A 1 170 VAL 170 212  212  VAL VAL B . n 
A 1 171 GLU 171 213  213  GLU GLU B . n 
A 1 172 SER 172 214  214  SER SER B . n 
A 1 173 ARG 173 215  215  ARG ARG B . n 
A 1 174 TYR 174 216  216  TYR TYR B . n 
A 1 175 ALA 175 217  217  ALA ALA B . n 
A 1 176 LEU 176 218  218  LEU LEU B . n 
A 1 177 LEU 177 219  219  LEU LEU B . n 
A 1 178 ILE 178 220  220  ILE ILE B . n 
A 1 179 VAL 179 221  221  VAL VAL B . n 
A 1 180 ASP 180 222  222  ASP ASP B . n 
A 1 181 SER 181 223  223  SER SER B . n 
A 1 182 ALA 182 224  224  ALA ALA B . n 
A 1 183 THR 183 225  225  THR THR B . n 
A 1 184 ALA 184 226  226  ALA ALA B . n 
A 1 185 LEU 185 227  227  LEU LEU B . n 
A 1 186 TYR 186 228  228  TYR TYR B . n 
A 1 187 ARG 187 229  229  ARG ARG B . n 
A 1 188 THR 188 230  230  THR THR B . n 
A 1 189 ASP 189 231  231  ASP ASP B . n 
A 1 190 TYR 190 232  232  TYR TYR B . n 
A 1 191 SER 191 233  233  SER SER B . n 
A 1 192 GLY 192 234  234  GLY GLY B . n 
A 1 193 ARG 193 235  235  ARG ARG B . n 
A 1 194 GLY 194 236  236  GLY GLY B . n 
A 1 195 GLU 195 237  237  GLU GLU B . n 
A 1 196 LEU 196 238  238  LEU LEU B . n 
A 1 197 SER 197 239  239  SER SER B . n 
A 1 198 ALA 198 240  240  ALA ALA B . n 
A 1 199 ARG 199 241  241  ARG ARG B . n 
A 1 200 GLN 200 242  242  GLN GLN B . n 
A 1 201 MET 201 243  243  MET MET B . n 
A 1 202 HIS 202 244  244  HIS HIS B . n 
A 1 203 LEU 203 245  245  LEU LEU B . n 
A 1 204 ALA 204 246  246  ALA ALA B . n 
A 1 205 ARG 205 247  247  ARG ARG B . n 
A 1 206 PHE 206 248  248  PHE PHE B . n 
A 1 207 LEU 207 249  249  LEU LEU B . n 
A 1 208 ARG 208 250  250  ARG ARG B . n 
A 1 209 MET 209 251  251  MET MET B . n 
A 1 210 LEU 210 252  252  LEU LEU B . n 
A 1 211 LEU 211 253  253  LEU LEU B . n 
A 1 212 ARG 212 254  254  ARG ARG B . n 
A 1 213 LEU 213 255  255  LEU LEU B . n 
A 1 214 ALA 214 256  256  ALA ALA B . n 
A 1 215 ASP 215 257  257  ASP ASP B . n 
A 1 216 GLU 216 258  258  GLU GLU B . n 
A 1 217 PHE 217 259  259  PHE PHE B . n 
A 1 218 GLY 218 260  260  GLY GLY B . n 
A 1 219 VAL 219 261  261  VAL VAL B . n 
A 1 220 ALA 220 262  262  ALA ALA B . n 
A 1 221 VAL 221 263  263  VAL VAL B . n 
A 1 222 VAL 222 264  264  VAL VAL B . n 
A 1 223 ILE 223 265  265  ILE ILE B . n 
A 1 224 THR 224 266  266  THR THR B . n 
A 1 225 ASN 225 267  267  ASN ASN B . n 
A 1 226 GLN 226 268  268  GLN GLN B . n 
A 1 227 VAL 227 269  269  VAL VAL B . n 
A 1 228 VAL 228 270  270  VAL VAL B . n 
A 1 229 ALA 229 271  271  ALA ALA B . n 
A 1 230 GLN 230 272  ?    ?   ?   B . n 
A 1 231 VAL 231 273  ?    ?   ?   B . n 
A 1 232 ASP 232 274  ?    ?   ?   B . n 
A 1 233 GLY 233 275  ?    ?   ?   B . n 
A 1 234 ALA 234 276  ?    ?   ?   B . n 
A 1 235 ALA 235 277  ?    ?   ?   B . n 
A 1 236 MET 236 278  ?    ?   ?   B . n 
A 1 237 PHE 237 279  ?    ?   ?   B . n 
A 1 238 ALA 238 280  ?    ?   ?   B . n 
A 1 239 ALA 239 281  ?    ?   ?   B . n 
A 1 240 ASP 240 282  ?    ?   ?   B . n 
A 1 241 PRO 241 283  ?    ?   ?   B . n 
A 1 242 LYS 242 284  ?    ?   ?   B . n 
A 1 243 LYS 243 285  ?    ?   ?   B . n 
A 1 244 PRO 244 286  ?    ?   ?   B . n 
A 1 245 ILE 245 287  ?    ?   ?   B . n 
A 1 246 GLY 246 288  ?    ?   ?   B . n 
A 1 247 GLY 247 289  ?    ?   ?   B . n 
A 1 248 ASN 248 290  ?    ?   ?   B . n 
A 1 249 ILE 249 291  291  ILE ILE B . n 
A 1 250 ILE 250 292  292  ILE ILE B . n 
A 1 251 ALA 251 293  293  ALA ALA B . n 
A 1 252 HIS 252 294  294  HIS HIS B . n 
A 1 253 ALA 253 295  295  ALA ALA B . n 
A 1 254 SER 254 296  296  SER SER B . n 
A 1 255 THR 255 297  297  THR THR B . n 
A 1 256 THR 256 298  298  THR THR B . n 
A 1 257 ARG 257 299  299  ARG ARG B . n 
A 1 258 LEU 258 300  300  LEU LEU B . n 
A 1 259 TYR 259 301  301  TYR TYR B . n 
A 1 260 LEU 260 302  302  LEU LEU B . n 
A 1 261 ARG 261 303  303  ARG ARG B . n 
A 1 262 LYS 262 304  304  LYS LYS B . n 
A 1 263 GLY 263 305  305  GLY GLY B . n 
A 1 264 ARG 264 306  306  ARG ARG B . n 
A 1 265 GLY 265 307  307  GLY GLY B . n 
A 1 266 GLU 266 308  308  GLU GLU B . n 
A 1 267 THR 267 309  309  THR THR B . n 
A 1 268 ARG 268 310  310  ARG ARG B . n 
A 1 269 ILE 269 311  311  ILE ILE B . n 
A 1 270 CYS 270 312  312  CYS CYS B . n 
A 1 271 LYS 271 313  313  LYS LYS B . n 
A 1 272 ILE 272 314  314  ILE ILE B . n 
A 1 273 TYR 273 315  315  TYR TYR B . n 
A 1 274 ASP 274 316  316  ASP ASP B . n 
A 1 275 SER 275 317  317  SER SER B . n 
A 1 276 PRO 276 318  318  PRO PRO B . n 
A 1 277 SER 277 319  319  SER SER B . n 
A 1 278 LEU 278 320  320  LEU LEU B . n 
A 1 279 PRO 279 321  321  PRO PRO B . n 
A 1 280 GLU 280 322  322  GLU GLU B . n 
A 1 281 ALA 281 323  323  ALA ALA B . n 
A 1 282 GLU 282 324  324  GLU GLU B . n 
A 1 283 ALA 283 325  325  ALA ALA B . n 
A 1 284 MET 284 326  326  MET MET B . n 
A 1 285 PHE 285 327  327  PHE PHE B . n 
A 1 286 ALA 286 328  328  ALA ALA B . n 
A 1 287 ILE 287 329  329  ILE ILE B . n 
A 1 288 ASN 288 330  330  ASN ASN B . n 
A 1 289 ALA 289 331  331  ALA ALA B . n 
A 1 290 ASP 290 332  332  ASP ASP B . n 
A 1 291 GLY 291 333  333  GLY GLY B . n 
A 1 292 VAL 292 334  334  VAL VAL B . n 
A 1 293 GLY 293 335  335  GLY GLY B . n 
A 1 294 ASP 294 336  336  ASP ASP B . n 
A 1 295 ALA 295 337  337  ALA ALA B . n 
A 1 296 LYS 296 338  338  LYS LYS B . n 
A 1 297 ASP 297 339  339  ASP ASP B . n 
B 2 1   SER 1   97   97   SER SER D . n 
B 2 2   GLU 2   98   98   GLU GLU D . n 
B 2 3   ILE 3   99   99   ILE ILE D . n 
B 2 4   ILE 4   100  100  ILE ILE D . n 
B 2 5   GLN 5   101  101  GLN GLN D . n 
B 2 6   ILE 6   102  102  ILE ILE D . n 
B 2 7   THR 7   103  103  THR THR D . n 
B 2 8   THR 8   104  104  THR THR D . n 
B 2 9   GLY 9   105  105  GLY GLY D . n 
B 2 10  SER 10  106  106  SER SER D . n 
B 2 11  LYS 11  107  107  LYS LYS D . n 
B 2 12  GLU 12  108  108  GLU GLU D . n 
B 2 13  LEU 13  109  109  LEU LEU D . n 
B 2 14  ASP 14  110  110  ASP ASP D . n 
B 2 15  LYS 15  111  111  LYS LYS D . n 
B 2 16  LEU 16  112  112  LEU LEU D . n 
B 2 17  LEU 17  113  113  LEU LEU D . n 
B 2 18  GLN 18  114  114  GLN GLN D . n 
B 2 19  GLY 19  115  115  GLY GLY D . n 
B 2 20  GLY 20  116  116  GLY GLY D . n 
B 2 21  ILE 21  117  117  ILE ILE D . n 
B 2 22  GLU 22  118  118  GLU GLU D . n 
B 2 23  THR 23  119  119  THR THR D . n 
B 2 24  GLY 24  120  120  GLY GLY D . n 
B 2 25  SER 25  121  121  SER SER D . n 
B 2 26  ILE 26  122  122  ILE ILE D . n 
B 2 27  THR 27  123  123  THR THR D . n 
B 2 28  GLU 28  124  124  GLU GLU D . n 
B 2 29  MET 29  125  125  MET MET D . n 
B 2 30  PHE 30  126  126  PHE PHE D . n 
B 2 31  GLY 31  127  127  GLY GLY D . n 
B 2 32  GLU 32  128  128  GLU GLU D . n 
B 2 33  PHE 33  129  129  PHE PHE D . n 
B 2 34  ARG 34  130  130  ARG ARG D . n 
B 2 35  THR 35  131  131  THR THR D . n 
B 2 36  GLY 36  132  132  GLY GLY D . n 
B 2 37  LYS 37  133  133  LYS LYS D . n 
B 2 38  THR 38  134  134  THR THR D . n 
B 2 39  GLN 39  135  135  GLN GLN D . n 
B 2 40  ILE 40  136  136  ILE ILE D . n 
B 2 41  CYS 41  137  137  CYS CYS D . n 
B 2 42  HIS 42  138  138  HIS HIS D . n 
B 2 43  THR 43  139  139  THR THR D . n 
B 2 44  LEU 44  140  140  LEU LEU D . n 
B 2 45  ALA 45  141  141  ALA ALA D . n 
B 2 46  VAL 46  142  142  VAL VAL D . n 
B 2 47  THR 47  143  143  THR THR D . n 
B 2 48  CYS 48  144  144  CYS CYS D . n 
B 2 49  GLN 49  145  145  GLN GLN D . n 
B 2 50  LEU 50  146  146  LEU LEU D . n 
B 2 51  PRO 51  147  147  PRO PRO D . n 
B 2 52  ILE 52  148  148  ILE ILE D . n 
B 2 53  ASP 53  149  149  ASP ASP D . n 
B 2 54  ARG 54  150  150  ARG ARG D . n 
B 2 55  GLY 55  151  151  GLY GLY D . n 
B 2 56  GLY 56  152  152  GLY GLY D . n 
B 2 57  GLY 57  153  153  GLY GLY D . n 
B 2 58  GLU 58  154  154  GLU GLU D . n 
B 2 59  GLY 59  155  155  GLY GLY D . n 
B 2 60  LYS 60  156  156  LYS LYS D . n 
B 2 61  ALA 61  157  157  ALA ALA D . n 
B 2 62  MET 62  158  158  MET MET D . n 
B 2 63  TYR 63  159  159  TYR TYR D . n 
B 2 64  ILE 64  160  160  ILE ILE D . n 
B 2 65  ASP 65  161  161  ASP ASP D . n 
B 2 66  THR 66  162  162  THR THR D . n 
B 2 67  GLU 67  163  163  GLU GLU D . n 
B 2 68  GLY 68  164  164  GLY GLY D . n 
B 2 69  THR 69  165  165  THR THR D . n 
B 2 70  PHE 70  166  166  PHE PHE D . n 
B 2 71  ARG 71  167  167  ARG ARG D . n 
B 2 72  PRO 72  168  168  PRO PRO D . n 
B 2 73  GLU 73  169  169  GLU GLU D . n 
B 2 74  ARG 74  170  170  ARG ARG D . n 
B 2 75  LEU 75  171  171  LEU LEU D . n 
B 2 76  LEU 76  172  172  LEU LEU D . n 
B 2 77  ALA 77  173  173  ALA ALA D . n 
B 2 78  VAL 78  174  174  VAL VAL D . n 
B 2 79  ALA 79  175  175  ALA ALA D . n 
B 2 80  GLU 80  176  176  GLU GLU D . n 
B 2 81  ARG 81  177  177  ARG ARG D . n 
B 2 82  TYR 82  178  178  TYR TYR D . n 
B 2 83  GLY 83  179  179  GLY GLY D . n 
B 2 84  LEU 84  180  180  LEU LEU D . n 
B 2 85  SER 85  181  181  SER SER D . n 
B 2 86  GLY 86  182  182  GLY GLY D . n 
B 2 87  SER 87  183  183  SER SER D . n 
B 2 88  ASP 88  184  184  ASP ASP D . n 
B 2 89  VAL 89  185  185  VAL VAL D . n 
B 2 90  LEU 90  186  186  LEU LEU D . n 
B 2 91  ASP 91  187  187  ASP ASP D . n 
B 2 92  ASN 92  188  188  ASN ASN D . n 
B 2 93  VAL 93  189  189  VAL VAL D . n 
B 2 94  ALA 94  190  190  ALA ALA D . n 
B 2 95  TYR 95  191  191  TYR TYR D . n 
B 2 96  ALA 96  192  192  ALA ALA D . n 
B 2 97  ARG 97  193  193  ARG ARG D . n 
B 2 98  ALA 98  194  194  ALA ALA D . n 
B 2 99  PHE 99  195  195  PHE PHE D . n 
B 2 100 ASN 100 196  196  ASN ASN D . n 
B 2 101 THR 101 197  197  THR THR D . n 
B 2 102 ASP 102 198  198  ASP ASP D . n 
B 2 103 HIS 103 199  199  HIS HIS D . n 
B 2 104 GLN 104 200  200  GLN GLN D . n 
B 2 105 THR 105 201  201  THR THR D . n 
B 2 106 GLN 106 202  202  GLN GLN D . n 
B 2 107 LEU 107 203  203  LEU LEU D . n 
B 2 108 LEU 108 204  204  LEU LEU D . n 
B 2 109 TYR 109 205  205  TYR TYR D . n 
B 2 110 GLN 110 206  206  GLN GLN D . n 
B 2 111 ALA 111 207  207  ALA ALA D . n 
B 2 112 GLU 112 208  208  GLU GLU D . n 
B 2 113 ASP 113 209  209  ASP ASP D . n 
B 2 114 MET 114 210  210  MET MET D . n 
B 2 115 MET 115 211  211  MET MET D . n 
B 2 116 VAL 116 212  212  VAL VAL D . n 
B 2 117 GLU 117 213  213  GLU GLU D . n 
B 2 118 SER 118 214  214  SER SER D . n 
B 2 119 ARG 119 215  215  ARG ARG D . n 
B 2 120 TYR 120 216  216  TYR TYR D . n 
B 2 121 ALA 121 217  217  ALA ALA D . n 
B 2 122 LEU 122 218  218  LEU LEU D . n 
B 2 123 LEU 123 219  219  LEU LEU D . n 
B 2 124 ILE 124 220  220  ILE ILE D . n 
B 2 125 VAL 125 221  221  VAL VAL D . n 
B 2 126 ASP 126 222  222  ASP ASP D . n 
B 2 127 SER 127 223  223  SER SER D . n 
B 2 128 ALA 128 224  224  ALA ALA D . n 
B 2 129 THR 129 225  225  THR THR D . n 
B 2 130 ALA 130 226  226  ALA ALA D . n 
B 2 131 LEU 131 227  227  LEU LEU D . n 
B 2 132 TYR 132 228  228  TYR TYR D . n 
B 2 133 ARG 133 229  229  ARG ARG D . n 
B 2 134 THR 134 230  230  THR THR D . n 
B 2 135 ASP 135 231  231  ASP ASP D . n 
B 2 136 TYR 136 232  232  TYR TYR D . n 
B 2 137 SER 137 233  233  SER SER D . n 
B 2 138 GLY 138 234  234  GLY GLY D . n 
B 2 139 ARG 139 235  235  ARG ARG D . n 
B 2 140 GLY 140 236  236  GLY GLY D . n 
B 2 141 GLU 141 237  237  GLU GLU D . n 
B 2 142 LEU 142 238  238  LEU LEU D . n 
B 2 143 SER 143 239  239  SER SER D . n 
B 2 144 ALA 144 240  240  ALA ALA D . n 
B 2 145 ARG 145 241  241  ARG ARG D . n 
B 2 146 GLN 146 242  242  GLN GLN D . n 
B 2 147 MET 147 243  243  MET MET D . n 
B 2 148 HIS 148 244  244  HIS HIS D . n 
B 2 149 LEU 149 245  245  LEU LEU D . n 
B 2 150 ALA 150 246  246  ALA ALA D . n 
B 2 151 ARG 151 247  247  ARG ARG D . n 
B 2 152 PHE 152 248  248  PHE PHE D . n 
B 2 153 LEU 153 249  249  LEU LEU D . n 
B 2 154 ARG 154 250  250  ARG ARG D . n 
B 2 155 MET 155 251  251  MET MET D . n 
B 2 156 LEU 156 252  252  LEU LEU D . n 
B 2 157 LEU 157 253  253  LEU LEU D . n 
B 2 158 ARG 158 254  254  ARG ARG D . n 
B 2 159 LEU 159 255  255  LEU LEU D . n 
B 2 160 ALA 160 256  256  ALA ALA D . n 
B 2 161 ASP 161 257  257  ASP ASP D . n 
B 2 162 GLU 162 258  258  GLU GLU D . n 
B 2 163 PHE 163 259  259  PHE PHE D . n 
B 2 164 GLY 164 260  260  GLY GLY D . n 
B 2 165 VAL 165 261  261  VAL VAL D . n 
B 2 166 ALA 166 262  262  ALA ALA D . n 
B 2 167 VAL 167 263  263  VAL VAL D . n 
B 2 168 VAL 168 264  264  VAL VAL D . n 
B 2 169 ILE 169 265  265  ILE ILE D . n 
B 2 170 THR 170 266  266  THR THR D . n 
B 2 171 ASN 171 267  267  ASN ASN D . n 
B 2 172 GLN 172 268  268  GLN GLN D . n 
B 2 173 VAL 173 269  269  VAL VAL D . n 
B 2 174 VAL 174 270  270  VAL VAL D . n 
B 2 175 ALA 175 271  ?    ?   ?   D . n 
B 2 176 GLN 176 272  ?    ?   ?   D . n 
B 2 177 VAL 177 273  ?    ?   ?   D . n 
B 2 178 ASP 178 274  ?    ?   ?   D . n 
B 2 179 GLY 179 275  ?    ?   ?   D . n 
B 2 180 ALA 180 276  ?    ?   ?   D . n 
B 2 181 ALA 181 277  ?    ?   ?   D . n 
B 2 182 MET 182 278  ?    ?   ?   D . n 
B 2 183 PHE 183 279  ?    ?   ?   D . n 
B 2 184 ALA 184 280  ?    ?   ?   D . n 
B 2 185 ALA 185 281  ?    ?   ?   D . n 
B 2 186 ASP 186 282  ?    ?   ?   D . n 
B 2 187 PRO 187 283  ?    ?   ?   D . n 
B 2 188 LYS 188 284  ?    ?   ?   D . n 
B 2 189 LYS 189 285  ?    ?   ?   D . n 
B 2 190 PRO 190 286  ?    ?   ?   D . n 
B 2 191 ILE 191 287  ?    ?   ?   D . n 
B 2 192 GLY 192 288  288  GLY GLY D . n 
B 2 193 GLY 193 289  289  GLY GLY D . n 
B 2 194 ASN 194 290  290  ASN ASN D . n 
B 2 195 ILE 195 291  291  ILE ILE D . n 
B 2 196 ILE 196 292  292  ILE ILE D . n 
B 2 197 ALA 197 293  293  ALA ALA D . n 
B 2 198 HIS 198 294  294  HIS HIS D . n 
B 2 199 ALA 199 295  295  ALA ALA D . n 
B 2 200 SER 200 296  296  SER SER D . n 
B 2 201 THR 201 297  297  THR THR D . n 
B 2 202 THR 202 298  298  THR THR D . n 
B 2 203 ARG 203 299  299  ARG ARG D . n 
B 2 204 LEU 204 300  300  LEU LEU D . n 
B 2 205 TYR 205 301  301  TYR TYR D . n 
B 2 206 LEU 206 302  302  LEU LEU D . n 
B 2 207 ARG 207 303  303  ARG ARG D . n 
B 2 208 LYS 208 304  304  LYS LYS D . n 
B 2 209 GLY 209 305  305  GLY GLY D . n 
B 2 210 ARG 210 306  306  ARG ARG D . n 
B 2 211 GLY 211 307  307  GLY GLY D . n 
B 2 212 GLU 212 308  308  GLU GLU D . n 
B 2 213 THR 213 309  309  THR THR D . n 
B 2 214 ARG 214 310  310  ARG ARG D . n 
B 2 215 ILE 215 311  311  ILE ILE D . n 
B 2 216 CYS 216 312  312  CYS CYS D . n 
B 2 217 LYS 217 313  313  LYS LYS D . n 
B 2 218 ILE 218 314  314  ILE ILE D . n 
B 2 219 TYR 219 315  315  TYR TYR D . n 
B 2 220 ASP 220 316  316  ASP ASP D . n 
B 2 221 SER 221 317  317  SER SER D . n 
B 2 222 PRO 222 318  318  PRO PRO D . n 
B 2 223 SER 223 319  319  SER SER D . n 
B 2 224 LEU 224 320  320  LEU LEU D . n 
B 2 225 PRO 225 321  321  PRO PRO D . n 
B 2 226 GLU 226 322  322  GLU GLU D . n 
B 2 227 ALA 227 323  323  ALA ALA D . n 
B 2 228 GLU 228 324  324  GLU GLU D . n 
B 2 229 ALA 229 325  325  ALA ALA D . n 
B 2 230 MET 230 326  326  MET MET D . n 
B 2 231 PHE 231 327  327  PHE PHE D . n 
B 2 232 ALA 232 328  328  ALA ALA D . n 
B 2 233 ILE 233 329  329  ILE ILE D . n 
B 2 234 ASN 234 330  330  ASN ASN D . n 
B 2 235 ALA 235 331  331  ALA ALA D . n 
B 2 236 ASP 236 332  332  ASP ASP D . n 
B 2 237 GLY 237 333  333  GLY GLY D . n 
B 2 238 VAL 238 334  334  VAL VAL D . n 
B 2 239 GLY 239 335  335  GLY GLY D . n 
B 2 240 ASP 240 336  336  ASP ASP D . n 
B 2 241 ALA 241 337  337  ALA ALA D . n 
B 2 242 LYS 242 338  338  LYS LYS D . n 
B 2 243 ASP 243 339  339  ASP ASP D . n 
B 2 244 SER 244 3260 ?    ?   ?   D . n 
B 2 245 SER 245 3261 ?    ?   ?   D . n 
B 2 246 ASP 246 3262 ?    ?   ?   D . n 
B 2 247 SER 247 3263 ?    ?   ?   D . n 
B 2 248 SER 248 3264 ?    ?   ?   D . n 
B 2 249 LEU 249 3265 ?    ?   ?   D . n 
B 2 250 SER 250 3266 ?    ?   ?   D . n 
B 2 251 SER 251 3267 ?    ?   ?   D . n 
B 2 252 PRO 252 3268 ?    ?   ?   D . n 
B 2 253 SER 253 3269 ?    ?   ?   D . n 
B 2 254 ALA 254 3270 ?    ?   ?   D . n 
B 2 255 LEU 255 3271 ?    ?   ?   D . n 
B 2 256 ASP 256 3272 ?    ?   ?   D . n 
B 2 257 PHE 257 3273 ?    ?   ?   D . n 
B 2 258 LEU 258 3274 ?    ?   ?   D . n 
B 2 259 SER 259 3275 ?    ?   ?   D . n 
B 2 260 ARG 260 3276 ?    ?   ?   D . n 
B 2 261 LEU 261 3277 ?    ?   ?   D . n 
B 2 262 PRO 262 3278 ?    ?   ?   D . n 
B 2 263 LEU 263 3279 ?    ?   ?   D . n 
B 2 264 PRO 264 3280 ?    ?   ?   D . n 
B 2 265 PRO 265 3281 ?    ?   ?   D . n 
B 2 266 PRO 266 3282 ?    ?   ?   D . n 
B 2 267 VAL 267 3283 ?    ?   ?   D . n 
B 2 268 SER 268 3284 ?    ?   ?   D . n 
B 2 269 PRO 269 3285 ?    ?   ?   D . n 
B 2 270 ILE 270 3286 ?    ?   ?   D . n 
B 2 271 ALA 271 3287 ?    ?   ?   D . n 
B 2 272 THR 272 3288 3288 THR THR D . n 
B 2 273 PHE 273 3289 3289 PHE PHE D . n 
B 2 274 VAL 274 3290 3290 VAL VAL D . n 
B 2 275 SER 275 3291 3291 SER SER D . n 
B 2 276 PRO 276 3292 3292 PRO PRO D . n 
B 2 277 ALA 277 3293 3293 ALA ALA D . n 
B 2 278 ALA 278 3294 3294 ALA ALA D . n 
B 2 279 GLN 279 3295 3295 GLN GLN D . n 
B 2 280 LYS 280 3296 3296 LYS LYS D . n 
B 2 281 ALA 281 3297 3297 ALA ALA D . n 
B 2 282 PHE 282 3298 3298 PHE PHE D . n 
B 2 283 GLN 283 3299 3299 GLN GLN D . n 
B 2 284 PRO 284 3300 3300 PRO PRO D . n 
B 2 285 PRO 285 3301 3301 PRO PRO D . n 
B 2 286 ARG 286 3302 3302 ARG ARG D . n 
B 2 287 SER 287 3303 3303 SER SER D . n 
B 2 288 ALA 288 3304 3304 ALA ALA D . n 
B 2 289 GLY 289 3305 3305 GLY GLY D . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 BEF ? ? BEF ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
C 3 ADP 1  2000 2000 ADP ADP B . 
D 4 BEF 1  2001 2001 BEF BEF B . 
E 5 EDO 1  2002 2002 EDO EDO B . 
F 5 EDO 1  2003 2003 EDO EDO B . 
G 3 ADP 1  5000 5000 ADP ADP D . 
H 4 BEF 1  5001 5001 BEF BEF D . 
I 6 HOH 1  2101 13   HOH HOH B . 
I 6 HOH 2  2102 41   HOH HOH B . 
I 6 HOH 3  2103 8    HOH HOH B . 
I 6 HOH 4  2104 19   HOH HOH B . 
I 6 HOH 5  2105 22   HOH HOH B . 
I 6 HOH 6  2106 37   HOH HOH B . 
I 6 HOH 7  2107 6    HOH HOH B . 
I 6 HOH 8  2108 42   HOH HOH B . 
I 6 HOH 9  2109 27   HOH HOH B . 
I 6 HOH 10 2110 25   HOH HOH B . 
I 6 HOH 11 2111 28   HOH HOH B . 
I 6 HOH 12 2112 32   HOH HOH B . 
I 6 HOH 13 2113 34   HOH HOH B . 
I 6 HOH 14 2114 18   HOH HOH B . 
I 6 HOH 15 2115 1    HOH HOH B . 
J 6 HOH 1  5101 35   HOH HOH D . 
J 6 HOH 2  5102 26   HOH HOH D . 
J 6 HOH 3  5103 24   HOH HOH D . 
J 6 HOH 4  5104 29   HOH HOH D . 
J 6 HOH 5  5105 38   HOH HOH D . 
J 6 HOH 6  5106 36   HOH HOH D . 
J 6 HOH 7  5107 30   HOH HOH D . 
J 6 HOH 8  5108 39   HOH HOH D . 
J 6 HOH 9  5109 10   HOH HOH D . 
J 6 HOH 10 5110 33   HOH HOH D . 
J 6 HOH 11 5111 16   HOH HOH D . 
J 6 HOH 12 5112 5    HOH HOH D . 
J 6 HOH 13 5113 3    HOH HOH D . 
J 6 HOH 14 5114 12   HOH HOH D . 
J 6 HOH 15 5115 40   HOH HOH D . 
J 6 HOH 16 5116 11   HOH HOH D . 
J 6 HOH 17 5117 7    HOH HOH D . 
J 6 HOH 18 5118 31   HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.21rc1_4924:000)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8UVW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.463 
_cell.length_a_esd                 ? 
_cell.length_b                     98.551 
_cell.length_b_esd                 ? 
_cell.length_c                     128.324 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8UVW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8UVW 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.59 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          52.43 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;25% v/v 1,4-Dioxane
0.05 M MOPS pH 7.0
0.005 M Magnesium chloride hexahydrate
0.001 M Spermine
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-07-12 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9795 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8UVW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.73 
_reflns.d_resolution_low                               39.24 
_reflns.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.number_all                                     ? 
_reflns.number_obs                                     17974 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.73 
_reflns_shell.d_res_low                                     2.86 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2352 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               13.6 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.340 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8UVW 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.73 
_refine.ls_d_res_low                             31.82 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     17681 
_refine.ls_number_reflns_R_free                  881 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.38 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2496 
_refine.ls_R_factor_R_free                       0.2821 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2479 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 36.59 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.40 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.73 
_refine_hist.d_res_low                        31.82 
_refine_hist.number_atoms_solvent             34 
_refine_hist.number_atoms_total               4023 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3919 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         70 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002  ? 4073 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.467  ? 5495 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 10.173 ? 1517 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.038  ? 625  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.003  ? 702  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.73 2.90  . . 136 2670 96.00  . . . . 0.3929 . . . . . . . . . . . 0.3962 
'X-RAY DIFFRACTION' 2.90 3.12  . . 137 2775 100.00 . . . . 0.3423 . . . . . . . . . . . 0.3488 
'X-RAY DIFFRACTION' 3.13 3.44  . . 136 2795 98.00  . . . . 0.3191 . . . . . . . . . . . 0.3346 
'X-RAY DIFFRACTION' 3.44 3.93  . . 166 2716 97.00  . . . . 0.3178 . . . . . . . . . . . 0.3435 
'X-RAY DIFFRACTION' 3.94 4.96  . . 143 2852 100.00 . . . . 0.2151 . . . . . . . . . . . 0.2966 
'X-RAY DIFFRACTION' 4.96 31.82 . . 163 2992 100.00 . . . . 0.2073 . . . . . . . . . . . 0.2262 
# 
_struct.entry_id                     8UVW 
_struct.title                        'Crystal structure of RAD51-BRCA2 Cter complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8UVW 
_struct_keywords.text            'Homologous recombination, DNA repair, DSB repair, RECOMBINATION' 
_struct_keywords.pdbx_keywords   RECOMBINATION 
# 
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 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 3 ? 
H N N 4 ? 
I N N 6 ? 
J N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP BRCA2_HUMAN P51587 ? 1 KEPTLLGFHTASGKKVKIAKESLDKVKNLFD 1517 
2 UNP RAD51_HUMAN Q06609 ? 1 
;GFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEG
TFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMH
LARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAE
AMFAINADGVGDAKD
;
85   
3 UNP RAD51_HUMAN Q06609 ? 2 
;SEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAE
RYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLA
DEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGD
AKD
;
97   
4 UNP BRCA2_HUMAN P51587 ? 2 ALDFLSRLPLPPPVSPICTFVSPAAQKAFQPPRSCG 3270 
# 
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 8UVW B 3   ? 33  ? P51587 1517 ? 1547 ? 1517 1547 
2 2 8UVW B 43  ? 297 ? Q06609 85   ? 339  ? 85   339  
3 3 8UVW D 1   ? 243 ? Q06609 97   ? 339  ? 97   339  
4 4 8UVW D 254 ? 289 ? P51587 3270 ? 3305 ? 3270 3305 
# 
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 8UVW GLY B 1   ? UNP P51587 ?   ?    'expression tag'      1515 1  
1 8UVW SER B 2   ? UNP P51587 ?   ?    'expression tag'      1516 2  
1 8UVW THR B 34  ? UNP P51587 ?   ?    linker                76   3  
1 8UVW GLY B 35  ? UNP P51587 ?   ?    linker                77   4  
1 8UVW SER B 36  ? UNP P51587 ?   ?    linker                78   5  
1 8UVW THR B 37  ? UNP P51587 ?   ?    linker                79   6  
1 8UVW GLY B 38  ? UNP P51587 ?   ?    linker                80   7  
1 8UVW SER B 39  ? UNP P51587 ?   ?    linker                81   8  
1 8UVW THR B 40  ? UNP P51587 ?   ?    linker                82   9  
1 8UVW GLY B 41  ? UNP P51587 ?   ?    linker                83   10 
1 8UVW SER B 42  ? UNP P51587 ?   ?    linker                84   11 
2 8UVW SER B 277 ? UNP Q06609 CYS 319  'engineered mutation' 319  12 
3 8UVW GLU D 112 ? UNP Q06609 SER 208  'engineered mutation' 208  13 
3 8UVW ASP D 113 ? UNP Q06609 ALA 209  'engineered mutation' 209  14 
3 8UVW SER D 223 ? UNP Q06609 CYS 319  'engineered mutation' 319  15 
3 8UVW SER D 244 ? UNP Q06609 ?   ?    linker                3260 16 
3 8UVW SER D 245 ? UNP Q06609 ?   ?    linker                3261 17 
3 8UVW ASP D 246 ? UNP Q06609 ?   ?    linker                3262 18 
3 8UVW SER D 247 ? UNP Q06609 ?   ?    linker                3263 19 
3 8UVW SER D 248 ? UNP Q06609 ?   ?    linker                3264 20 
3 8UVW LEU D 249 ? UNP Q06609 ?   ?    linker                3265 21 
3 8UVW SER D 250 ? UNP Q06609 ?   ?    linker                3266 22 
3 8UVW SER D 251 ? UNP Q06609 ?   ?    linker                3267 23 
3 8UVW PRO D 252 ? UNP Q06609 ?   ?    linker                3268 24 
3 8UVW SER D 253 ? UNP Q06609 ?   ?    linker                3269 25 
4 8UVW ALA D 271 ? UNP P51587 CYS 3287 'engineered mutation' 3287 26 
4 8UVW ALA D 288 ? UNP P51587 CYS 3304 'engineered mutation' 3304 27 
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 4910  ? 
1 MORE         -16   ? 
1 'SSA (A^2)'  22710 ? 
# 
_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 
# 
_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_
_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  AA1 ALA A 21  ? VAL A 28  ? ALA B 1535 VAL B 1542 1 ? 8  
HELX_P HELX_P2  AA2 ALA A 47  ? GLU A 56  ? ALA B 89   GLU B 98   1 ? 10 
HELX_P HELX_P3  AA3 SER A 64  ? LEU A 71  ? SER B 106  LEU B 113  1 ? 8  
HELX_P HELX_P4  AA4 GLY A 90  ? CYS A 102 ? GLY B 132  CYS B 144  1 ? 13 
HELX_P HELX_P5  AA5 GLN A 103 ? LEU A 104 ? GLN B 145  LEU B 146  5 ? 2  
HELX_P HELX_P6  AA6 PRO A 105 ? GLY A 109 ? PRO B 147  GLY B 151  5 ? 5  
HELX_P HELX_P7  AA7 ARG A 125 ? GLY A 137 ? ARG B 167  GLY B 179  1 ? 13 
HELX_P HELX_P8  AA8 SER A 139 ? ASN A 146 ? SER B 181  ASN B 188  1 ? 8  
HELX_P HELX_P9  AA9 ASN A 154 ? MET A 169 ? ASN B 196  MET B 211  1 ? 16 
HELX_P HELX_P10 AB1 GLY A 194 ? GLY A 218 ? GLY B 236  GLY B 260  1 ? 25 
HELX_P HELX_P11 AB2 SER B 10  ? LEU B 17  ? SER D 106  LEU D 113  1 ? 8  
HELX_P HELX_P12 AB3 GLY B 36  ? CYS B 48  ? GLY D 132  CYS D 144  1 ? 13 
HELX_P HELX_P13 AB4 GLN B 49  ? LEU B 50  ? GLN D 145  LEU D 146  5 ? 2  
HELX_P HELX_P14 AB5 PRO B 51  ? GLY B 55  ? PRO D 147  GLY D 151  5 ? 5  
HELX_P HELX_P15 AB6 ARG B 71  ? TYR B 82  ? ARG D 167  TYR D 178  1 ? 12 
HELX_P HELX_P16 AB7 SER B 85  ? ASN B 92  ? SER D 181  ASN D 188  1 ? 8  
HELX_P HELX_P17 AB8 ASN B 100 ? SER B 118 ? ASN D 196  SER D 214  1 ? 19 
HELX_P HELX_P18 AB9 LEU B 142 ? GLY B 164 ? LEU D 238  GLY D 260  1 ? 23 
HELX_P HELX_P19 AC1 ASN B 194 ? SER B 200 ? ASN D 290  SER D 296  1 ? 7  
HELX_P HELX_P20 AC2 PRO B 276 ? LYS B 280 ? PRO D 3292 LYS D 3296 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 10 ? 
AA2 ? 10 ? 
AA3 ? 2  ? 
AA4 ? 2  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? anti-parallel 
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA1 5 6  ? parallel      
AA1 6 7  ? parallel      
AA1 7 8  ? anti-parallel 
AA1 8 9  ? anti-parallel 
AA1 9 10 ? anti-parallel 
AA2 1 2  ? anti-parallel 
AA2 2 3  ? parallel      
AA2 3 4  ? parallel      
AA2 4 5  ? parallel      
AA2 5 6  ? parallel      
AA2 6 7  ? parallel      
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA4 1 2  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  HIS A 11  ? THR A 12  ? HIS B 1525 THR B 1526 
AA1 2  VAL A 147 ? ARG A 151 ? VAL B 189  ARG B 193  
AA1 3  LYS A 114 ? ASP A 119 ? LYS B 156  ASP B 161  
AA1 4  TYR A 174 ? ASP A 180 ? TYR B 216  ASP B 222  
AA1 5  ALA A 220 ? GLN A 226 ? ALA B 262  GLN B 268  
AA1 6  ILE A 80  ? GLY A 85  ? ILE B 122  GLY B 127  
AA1 7  THR A 256 ? LYS A 262 ? THR B 298  LYS B 304  
AA1 8  ARG A 268 ? ASP A 274 ? ARG B 310  ASP B 316  
AA1 9  GLU A 282 ? ASN A 288 ? GLU B 324  ASN B 330  
AA1 10 GLY A 291 ? GLY A 293 ? GLY B 333  GLY B 335  
AA2 1  THR A 45  ? THR A 46  ? THR B 87   THR B 88   
AA2 2  VAL B 93  ? ARG B 97  ? VAL D 189  ARG D 193  
AA2 3  LYS B 60  ? ASP B 65  ? LYS D 156  ASP D 161  
AA2 4  TYR B 120 ? ASP B 126 ? TYR D 216  ASP D 222  
AA2 5  ALA B 166 ? GLN B 172 ? ALA D 262  GLN D 268  
AA2 6  ILE B 26  ? GLY B 31  ? ILE D 122  GLY D 127  
AA2 7  THR B 202 ? LYS B 208 ? THR D 298  LYS D 304  
AA2 8  ARG B 214 ? ASP B 220 ? ARG D 310  ASP D 316  
AA2 9  GLU B 228 ? ASN B 234 ? GLU D 324  ASN D 330  
AA2 10 GLY B 237 ? GLY B 239 ? GLY D 333  GLY D 335  
AA3 1  GLN A 59  ? ILE A 60  ? GLN B 101  ILE B 102  
AA3 2  ILE A 75  ? GLU A 76  ? ILE B 117  GLU B 118  
AA4 1  GLN B 5   ? ILE B 6   ? GLN D 101  ILE D 102  
AA4 2  ILE B 21  ? GLU B 22  ? ILE D 117  GLU D 118  
# 
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 
AA1 1 2  N HIS A 11  ? N HIS B 1525 O TYR A 149 ? O TYR B 191 
AA1 2 3  O ALA A 148 ? O ALA B 190  N ALA A 115 ? N ALA B 157 
AA1 3 4  N MET A 116 ? N MET B 158  O ILE A 178 ? O ILE B 220 
AA1 4 5  N LEU A 177 ? N LEU B 219  O ALA A 220 ? O ALA B 262 
AA1 5 6  O VAL A 221 ? O VAL B 263  N THR A 81  ? N THR B 123 
AA1 6 7  N PHE A 84  ? N PHE B 126  O LEU A 258 ? O LEU B 300 
AA1 7 8  N ARG A 257 ? N ARG B 299  O ASP A 274 ? O ASP B 316 
AA1 8 9  N ARG A 268 ? N ARG B 310  O PHE A 285 ? O PHE B 327 
AA1 9 10 N ALA A 286 ? N ALA B 328  O GLY A 293 ? O GLY B 335 
AA2 1 2  N THR A 45  ? N THR B 87   O TYR B 95  ? O TYR D 191 
AA2 2 3  O ALA B 94  ? O ALA D 190  N ALA B 61  ? N ALA D 157 
AA2 3 4  N MET B 62  ? N MET D 158  O ILE B 124 ? O ILE D 220 
AA2 4 5  N VAL B 125 ? N VAL D 221  O VAL B 168 ? O VAL D 264 
AA2 5 6  O VAL B 167 ? O VAL D 263  N THR B 27  ? N THR D 123 
AA2 6 7  N GLU B 28  ? N GLU D 124  O THR B 202 ? O THR D 298 
AA2 7 8  N ARG B 207 ? N ARG D 303  O ILE B 215 ? O ILE D 311 
AA2 8 9  N CYS B 216 ? N CYS D 312  O ALA B 229 ? O ALA D 325 
AA2 9 10 N ALA B 232 ? N ALA D 328  O GLY B 239 ? O GLY D 335 
AA3 1 2  N ILE A 60  ? N ILE B 102  O ILE A 75  ? O ILE B 117 
AA4 1 2  N ILE B 6   ? N ILE D 102  O ILE B 21  ? O ILE D 117 
# 
_pdbx_entry_details.entry_id                   8UVW 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER B 223  ? ? 60.00  73.92   
2 1 TYR D 232  ? ? 51.73  -97.42  
3 1 LEU D 238  ? ? 55.83  -103.52 
4 1 PRO D 3292 ? ? -90.49 -96.37  
# 
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 B GLY 1515 ? A GLY 1   
2  1 Y 1 B SER 1516 ? A SER 2   
3  1 Y 1 B LYS 1517 ? A LYS 3   
4  1 Y 1 B GLU 1518 ? A GLU 4   
5  1 Y 1 B PRO 1519 ? A PRO 5   
6  1 Y 1 B THR 76   ? A THR 34  
7  1 Y 1 B GLY 77   ? A GLY 35  
8  1 Y 1 B SER 78   ? A SER 36  
9  1 Y 1 B THR 79   ? A THR 37  
10 1 Y 1 B GLY 80   ? A GLY 38  
11 1 Y 1 B SER 81   ? A SER 39  
12 1 Y 1 B THR 82   ? A THR 40  
13 1 Y 1 B GLN 272  ? A GLN 230 
14 1 Y 1 B VAL 273  ? A VAL 231 
15 1 Y 1 B ASP 274  ? A ASP 232 
16 1 Y 1 B GLY 275  ? A GLY 233 
17 1 Y 1 B ALA 276  ? A ALA 234 
18 1 Y 1 B ALA 277  ? A ALA 235 
19 1 Y 1 B MET 278  ? A MET 236 
20 1 Y 1 B PHE 279  ? A PHE 237 
21 1 Y 1 B ALA 280  ? A ALA 238 
22 1 Y 1 B ALA 281  ? A ALA 239 
23 1 Y 1 B ASP 282  ? A ASP 240 
24 1 Y 1 B PRO 283  ? A PRO 241 
25 1 Y 1 B LYS 284  ? A LYS 242 
26 1 Y 1 B LYS 285  ? A LYS 243 
27 1 Y 1 B PRO 286  ? A PRO 244 
28 1 Y 1 B ILE 287  ? A ILE 245 
29 1 Y 1 B GLY 288  ? A GLY 246 
30 1 Y 1 B GLY 289  ? A GLY 247 
31 1 Y 1 B ASN 290  ? A ASN 248 
32 1 Y 1 D ALA 271  ? B ALA 175 
33 1 Y 1 D GLN 272  ? B GLN 176 
34 1 Y 1 D VAL 273  ? B VAL 177 
35 1 Y 1 D ASP 274  ? B ASP 178 
36 1 Y 1 D GLY 275  ? B GLY 179 
37 1 Y 1 D ALA 276  ? B ALA 180 
38 1 Y 1 D ALA 277  ? B ALA 181 
39 1 Y 1 D MET 278  ? B MET 182 
40 1 Y 1 D PHE 279  ? B PHE 183 
41 1 Y 1 D ALA 280  ? B ALA 184 
42 1 Y 1 D ALA 281  ? B ALA 185 
43 1 Y 1 D ASP 282  ? B ASP 186 
44 1 Y 1 D PRO 283  ? B PRO 187 
45 1 Y 1 D LYS 284  ? B LYS 188 
46 1 Y 1 D LYS 285  ? B LYS 189 
47 1 Y 1 D PRO 286  ? B PRO 190 
48 1 Y 1 D ILE 287  ? B ILE 191 
49 1 Y 1 D SER 3260 ? B SER 244 
50 1 Y 1 D SER 3261 ? B SER 245 
51 1 Y 1 D ASP 3262 ? B ASP 246 
52 1 Y 1 D SER 3263 ? B SER 247 
53 1 Y 1 D SER 3264 ? B SER 248 
54 1 Y 1 D LEU 3265 ? B LEU 249 
55 1 Y 1 D SER 3266 ? B SER 250 
56 1 Y 1 D SER 3267 ? B SER 251 
57 1 Y 1 D PRO 3268 ? B PRO 252 
58 1 Y 1 D SER 3269 ? B SER 253 
59 1 Y 1 D ALA 3270 ? B ALA 254 
60 1 Y 1 D LEU 3271 ? B LEU 255 
61 1 Y 1 D ASP 3272 ? B ASP 256 
62 1 Y 1 D PHE 3273 ? B PHE 257 
63 1 Y 1 D LEU 3274 ? B LEU 258 
64 1 Y 1 D SER 3275 ? B SER 259 
65 1 Y 1 D ARG 3276 ? B ARG 260 
66 1 Y 1 D LEU 3277 ? B LEU 261 
67 1 Y 1 D PRO 3278 ? B PRO 262 
68 1 Y 1 D LEU 3279 ? B LEU 263 
69 1 Y 1 D PRO 3280 ? B PRO 264 
70 1 Y 1 D PRO 3281 ? B PRO 265 
71 1 Y 1 D PRO 3282 ? B PRO 266 
72 1 Y 1 D VAL 3283 ? B VAL 267 
73 1 Y 1 D SER 3284 ? B SER 268 
74 1 Y 1 D PRO 3285 ? B PRO 269 
75 1 Y 1 D ILE 3286 ? B ILE 270 
76 1 Y 1 D ALA 3287 ? B ALA 271 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ADP PB     P  N N 1   
ADP O1B    O  N N 2   
ADP O2B    O  N N 3   
ADP O3B    O  N N 4   
ADP PA     P  N S 5   
ADP O1A    O  N N 6   
ADP O2A    O  N N 7   
ADP O3A    O  N N 8   
ADP "O5'"  O  N N 9   
ADP "C5'"  C  N N 10  
ADP "C4'"  C  N R 11  
ADP "O4'"  O  N N 12  
ADP "C3'"  C  N S 13  
ADP "O3'"  O  N N 14  
ADP "C2'"  C  N R 15  
ADP "O2'"  O  N N 16  
ADP "C1'"  C  N R 17  
ADP N9     N  Y N 18  
ADP C8     C  Y N 19  
ADP N7     N  Y N 20  
ADP C5     C  Y N 21  
ADP C6     C  Y N 22  
ADP N6     N  N N 23  
ADP N1     N  Y N 24  
ADP C2     C  Y N 25  
ADP N3     N  Y N 26  
ADP C4     C  Y N 27  
ADP HOB2   H  N N 28  
ADP HOB3   H  N N 29  
ADP HOA2   H  N N 30  
ADP "H5'1" H  N N 31  
ADP "H5'2" H  N N 32  
ADP "H4'"  H  N N 33  
ADP "H3'"  H  N N 34  
ADP "HO3'" H  N N 35  
ADP "H2'"  H  N N 36  
ADP "HO2'" H  N N 37  
ADP "H1'"  H  N N 38  
ADP H8     H  N N 39  
ADP HN61   H  N N 40  
ADP HN62   H  N N 41  
ADP H2     H  N N 42  
ALA N      N  N N 43  
ALA CA     C  N S 44  
ALA C      C  N N 45  
ALA O      O  N N 46  
ALA CB     C  N N 47  
ALA OXT    O  N N 48  
ALA H      H  N N 49  
ALA H2     H  N N 50  
ALA HA     H  N N 51  
ALA HB1    H  N N 52  
ALA HB2    H  N N 53  
ALA HB3    H  N N 54  
ALA HXT    H  N N 55  
ARG N      N  N N 56  
ARG CA     C  N S 57  
ARG C      C  N N 58  
ARG O      O  N N 59  
ARG CB     C  N N 60  
ARG CG     C  N N 61  
ARG CD     C  N N 62  
ARG NE     N  N N 63  
ARG CZ     C  N N 64  
ARG NH1    N  N N 65  
ARG NH2    N  N N 66  
ARG OXT    O  N N 67  
ARG H      H  N N 68  
ARG H2     H  N N 69  
ARG HA     H  N N 70  
ARG HB2    H  N N 71  
ARG HB3    H  N N 72  
ARG HG2    H  N N 73  
ARG HG3    H  N N 74  
ARG HD2    H  N N 75  
ARG HD3    H  N N 76  
ARG HE     H  N N 77  
ARG HH11   H  N N 78  
ARG HH12   H  N N 79  
ARG HH21   H  N N 80  
ARG HH22   H  N N 81  
ARG HXT    H  N N 82  
ASN N      N  N N 83  
ASN CA     C  N S 84  
ASN C      C  N N 85  
ASN O      O  N N 86  
ASN CB     C  N N 87  
ASN CG     C  N N 88  
ASN OD1    O  N N 89  
ASN ND2    N  N N 90  
ASN OXT    O  N N 91  
ASN H      H  N N 92  
ASN H2     H  N N 93  
ASN HA     H  N N 94  
ASN HB2    H  N N 95  
ASN HB3    H  N N 96  
ASN HD21   H  N N 97  
ASN HD22   H  N N 98  
ASN HXT    H  N N 99  
ASP N      N  N N 100 
ASP CA     C  N S 101 
ASP C      C  N N 102 
ASP O      O  N N 103 
ASP CB     C  N N 104 
ASP CG     C  N N 105 
ASP OD1    O  N N 106 
ASP OD2    O  N N 107 
ASP OXT    O  N N 108 
ASP H      H  N N 109 
ASP H2     H  N N 110 
ASP HA     H  N N 111 
ASP HB2    H  N N 112 
ASP HB3    H  N N 113 
ASP HD2    H  N N 114 
ASP HXT    H  N N 115 
BEF BE     BE N N 116 
BEF F1     F  N N 117 
BEF F2     F  N N 118 
BEF F3     F  N N 119 
CYS N      N  N N 120 
CYS CA     C  N R 121 
CYS C      C  N N 122 
CYS O      O  N N 123 
CYS CB     C  N N 124 
CYS SG     S  N N 125 
CYS OXT    O  N N 126 
CYS H      H  N N 127 
CYS H2     H  N N 128 
CYS HA     H  N N 129 
CYS HB2    H  N N 130 
CYS HB3    H  N N 131 
CYS HG     H  N N 132 
CYS HXT    H  N N 133 
EDO C1     C  N N 134 
EDO O1     O  N N 135 
EDO C2     C  N N 136 
EDO O2     O  N N 137 
EDO H11    H  N N 138 
EDO H12    H  N N 139 
EDO HO1    H  N N 140 
EDO H21    H  N N 141 
EDO H22    H  N N 142 
EDO HO2    H  N N 143 
GLN N      N  N N 144 
GLN CA     C  N S 145 
GLN C      C  N N 146 
GLN O      O  N N 147 
GLN CB     C  N N 148 
GLN CG     C  N N 149 
GLN CD     C  N N 150 
GLN OE1    O  N N 151 
GLN NE2    N  N N 152 
GLN OXT    O  N N 153 
GLN H      H  N N 154 
GLN H2     H  N N 155 
GLN HA     H  N N 156 
GLN HB2    H  N N 157 
GLN HB3    H  N N 158 
GLN HG2    H  N N 159 
GLN HG3    H  N N 160 
GLN HE21   H  N N 161 
GLN HE22   H  N N 162 
GLN HXT    H  N N 163 
GLU N      N  N N 164 
GLU CA     C  N S 165 
GLU C      C  N N 166 
GLU O      O  N N 167 
GLU CB     C  N N 168 
GLU CG     C  N N 169 
GLU CD     C  N N 170 
GLU OE1    O  N N 171 
GLU OE2    O  N N 172 
GLU OXT    O  N N 173 
GLU H      H  N N 174 
GLU H2     H  N N 175 
GLU HA     H  N N 176 
GLU HB2    H  N N 177 
GLU HB3    H  N N 178 
GLU HG2    H  N N 179 
GLU HG3    H  N N 180 
GLU HE2    H  N N 181 
GLU HXT    H  N N 182 
GLY N      N  N N 183 
GLY CA     C  N N 184 
GLY C      C  N N 185 
GLY O      O  N N 186 
GLY OXT    O  N N 187 
GLY H      H  N N 188 
GLY H2     H  N N 189 
GLY HA2    H  N N 190 
GLY HA3    H  N N 191 
GLY HXT    H  N N 192 
HIS N      N  N N 193 
HIS CA     C  N S 194 
HIS C      C  N N 195 
HIS O      O  N N 196 
HIS CB     C  N N 197 
HIS CG     C  Y N 198 
HIS ND1    N  Y N 199 
HIS CD2    C  Y N 200 
HIS CE1    C  Y N 201 
HIS NE2    N  Y N 202 
HIS OXT    O  N N 203 
HIS H      H  N N 204 
HIS H2     H  N N 205 
HIS HA     H  N N 206 
HIS HB2    H  N N 207 
HIS HB3    H  N N 208 
HIS HD1    H  N N 209 
HIS HD2    H  N N 210 
HIS HE1    H  N N 211 
HIS HE2    H  N N 212 
HIS HXT    H  N N 213 
HOH O      O  N N 214 
HOH H1     H  N N 215 
HOH H2     H  N N 216 
ILE N      N  N N 217 
ILE CA     C  N S 218 
ILE C      C  N N 219 
ILE O      O  N N 220 
ILE CB     C  N S 221 
ILE CG1    C  N N 222 
ILE CG2    C  N N 223 
ILE CD1    C  N N 224 
ILE OXT    O  N N 225 
ILE H      H  N N 226 
ILE H2     H  N N 227 
ILE HA     H  N N 228 
ILE HB     H  N N 229 
ILE HG12   H  N N 230 
ILE HG13   H  N N 231 
ILE HG21   H  N N 232 
ILE HG22   H  N N 233 
ILE HG23   H  N N 234 
ILE HD11   H  N N 235 
ILE HD12   H  N N 236 
ILE HD13   H  N N 237 
ILE HXT    H  N N 238 
LEU N      N  N N 239 
LEU CA     C  N S 240 
LEU C      C  N N 241 
LEU O      O  N N 242 
LEU CB     C  N N 243 
LEU CG     C  N N 244 
LEU CD1    C  N N 245 
LEU CD2    C  N N 246 
LEU OXT    O  N N 247 
LEU H      H  N N 248 
LEU H2     H  N N 249 
LEU HA     H  N N 250 
LEU HB2    H  N N 251 
LEU HB3    H  N N 252 
LEU HG     H  N N 253 
LEU HD11   H  N N 254 
LEU HD12   H  N N 255 
LEU HD13   H  N N 256 
LEU HD21   H  N N 257 
LEU HD22   H  N N 258 
LEU HD23   H  N N 259 
LEU HXT    H  N N 260 
LYS N      N  N N 261 
LYS CA     C  N S 262 
LYS C      C  N N 263 
LYS O      O  N N 264 
LYS CB     C  N N 265 
LYS CG     C  N N 266 
LYS CD     C  N N 267 
LYS CE     C  N N 268 
LYS NZ     N  N N 269 
LYS OXT    O  N N 270 
LYS H      H  N N 271 
LYS H2     H  N N 272 
LYS HA     H  N N 273 
LYS HB2    H  N N 274 
LYS HB3    H  N N 275 
LYS HG2    H  N N 276 
LYS HG3    H  N N 277 
LYS HD2    H  N N 278 
LYS HD3    H  N N 279 
LYS HE2    H  N N 280 
LYS HE3    H  N N 281 
LYS HZ1    H  N N 282 
LYS HZ2    H  N N 283 
LYS HZ3    H  N N 284 
LYS HXT    H  N N 285 
MET N      N  N N 286 
MET CA     C  N S 287 
MET C      C  N N 288 
MET O      O  N N 289 
MET CB     C  N N 290 
MET CG     C  N N 291 
MET SD     S  N N 292 
MET CE     C  N N 293 
MET OXT    O  N N 294 
MET H      H  N N 295 
MET H2     H  N N 296 
MET HA     H  N N 297 
MET HB2    H  N N 298 
MET HB3    H  N N 299 
MET HG2    H  N N 300 
MET HG3    H  N N 301 
MET HE1    H  N N 302 
MET HE2    H  N N 303 
MET HE3    H  N N 304 
MET HXT    H  N N 305 
PHE N      N  N N 306 
PHE CA     C  N S 307 
PHE C      C  N N 308 
PHE O      O  N N 309 
PHE CB     C  N N 310 
PHE CG     C  Y N 311 
PHE CD1    C  Y N 312 
PHE CD2    C  Y N 313 
PHE CE1    C  Y N 314 
PHE CE2    C  Y N 315 
PHE CZ     C  Y N 316 
PHE OXT    O  N N 317 
PHE H      H  N N 318 
PHE H2     H  N N 319 
PHE HA     H  N N 320 
PHE HB2    H  N N 321 
PHE HB3    H  N N 322 
PHE HD1    H  N N 323 
PHE HD2    H  N N 324 
PHE HE1    H  N N 325 
PHE HE2    H  N N 326 
PHE HZ     H  N N 327 
PHE HXT    H  N N 328 
PRO N      N  N N 329 
PRO CA     C  N S 330 
PRO C      C  N N 331 
PRO O      O  N N 332 
PRO CB     C  N N 333 
PRO CG     C  N N 334 
PRO CD     C  N N 335 
PRO OXT    O  N N 336 
PRO H      H  N N 337 
PRO HA     H  N N 338 
PRO HB2    H  N N 339 
PRO HB3    H  N N 340 
PRO HG2    H  N N 341 
PRO HG3    H  N N 342 
PRO HD2    H  N N 343 
PRO HD3    H  N N 344 
PRO HXT    H  N N 345 
SER N      N  N N 346 
SER CA     C  N S 347 
SER C      C  N N 348 
SER O      O  N N 349 
SER CB     C  N N 350 
SER OG     O  N N 351 
SER OXT    O  N N 352 
SER H      H  N N 353 
SER H2     H  N N 354 
SER HA     H  N N 355 
SER HB2    H  N N 356 
SER HB3    H  N N 357 
SER HG     H  N N 358 
SER HXT    H  N N 359 
THR N      N  N N 360 
THR CA     C  N S 361 
THR C      C  N N 362 
THR O      O  N N 363 
THR CB     C  N R 364 
THR OG1    O  N N 365 
THR CG2    C  N N 366 
THR OXT    O  N N 367 
THR H      H  N N 368 
THR H2     H  N N 369 
THR HA     H  N N 370 
THR HB     H  N N 371 
THR HG1    H  N N 372 
THR HG21   H  N N 373 
THR HG22   H  N N 374 
THR HG23   H  N N 375 
THR HXT    H  N N 376 
TYR N      N  N N 377 
TYR CA     C  N S 378 
TYR C      C  N N 379 
TYR O      O  N N 380 
TYR CB     C  N N 381 
TYR CG     C  Y N 382 
TYR CD1    C  Y N 383 
TYR CD2    C  Y N 384 
TYR CE1    C  Y N 385 
TYR CE2    C  Y N 386 
TYR CZ     C  Y N 387 
TYR OH     O  N N 388 
TYR OXT    O  N N 389 
TYR H      H  N N 390 
TYR H2     H  N N 391 
TYR HA     H  N N 392 
TYR HB2    H  N N 393 
TYR HB3    H  N N 394 
TYR HD1    H  N N 395 
TYR HD2    H  N N 396 
TYR HE1    H  N N 397 
TYR HE2    H  N N 398 
TYR HH     H  N N 399 
TYR HXT    H  N N 400 
VAL N      N  N N 401 
VAL CA     C  N S 402 
VAL C      C  N N 403 
VAL O      O  N N 404 
VAL CB     C  N N 405 
VAL CG1    C  N N 406 
VAL CG2    C  N N 407 
VAL OXT    O  N N 408 
VAL H      H  N N 409 
VAL H2     H  N N 410 
VAL HA     H  N N 411 
VAL HB     H  N N 412 
VAL HG11   H  N N 413 
VAL HG12   H  N N 414 
VAL HG13   H  N N 415 
VAL HG21   H  N N 416 
VAL HG22   H  N N 417 
VAL HG23   H  N N 418 
VAL HXT    H  N N 419 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
BEF BE    F1     sing N N 114 
BEF BE    F2     sing N N 115 
BEF BE    F3     sing N N 116 
CYS N     CA     sing N N 117 
CYS N     H      sing N N 118 
CYS N     H2     sing N N 119 
CYS CA    C      sing N N 120 
CYS CA    CB     sing N N 121 
CYS CA    HA     sing N N 122 
CYS C     O      doub N N 123 
CYS C     OXT    sing N N 124 
CYS CB    SG     sing N N 125 
CYS CB    HB2    sing N N 126 
CYS CB    HB3    sing N N 127 
CYS SG    HG     sing N N 128 
CYS OXT   HXT    sing N N 129 
EDO C1    O1     sing N N 130 
EDO C1    C2     sing N N 131 
EDO C1    H11    sing N N 132 
EDO C1    H12    sing N N 133 
EDO O1    HO1    sing N N 134 
EDO C2    O2     sing N N 135 
EDO C2    H21    sing N N 136 
EDO C2    H22    sing N N 137 
EDO O2    HO2    sing N N 138 
GLN N     CA     sing N N 139 
GLN N     H      sing N N 140 
GLN N     H2     sing N N 141 
GLN CA    C      sing N N 142 
GLN CA    CB     sing N N 143 
GLN CA    HA     sing N N 144 
GLN C     O      doub N N 145 
GLN C     OXT    sing N N 146 
GLN CB    CG     sing N N 147 
GLN CB    HB2    sing N N 148 
GLN CB    HB3    sing N N 149 
GLN CG    CD     sing N N 150 
GLN CG    HG2    sing N N 151 
GLN CG    HG3    sing N N 152 
GLN CD    OE1    doub N N 153 
GLN CD    NE2    sing N N 154 
GLN NE2   HE21   sing N N 155 
GLN NE2   HE22   sing N N 156 
GLN OXT   HXT    sing N N 157 
GLU N     CA     sing N N 158 
GLU N     H      sing N N 159 
GLU N     H2     sing N N 160 
GLU CA    C      sing N N 161 
GLU CA    CB     sing N N 162 
GLU CA    HA     sing N N 163 
GLU C     O      doub N N 164 
GLU C     OXT    sing N N 165 
GLU CB    CG     sing N N 166 
GLU CB    HB2    sing N N 167 
GLU CB    HB3    sing N N 168 
GLU CG    CD     sing N N 169 
GLU CG    HG2    sing N N 170 
GLU CG    HG3    sing N N 171 
GLU CD    OE1    doub N N 172 
GLU CD    OE2    sing N N 173 
GLU OE2   HE2    sing N N 174 
GLU OXT   HXT    sing N N 175 
GLY N     CA     sing N N 176 
GLY N     H      sing N N 177 
GLY N     H2     sing N N 178 
GLY CA    C      sing N N 179 
GLY CA    HA2    sing N N 180 
GLY CA    HA3    sing N N 181 
GLY C     O      doub N N 182 
GLY C     OXT    sing N N 183 
GLY OXT   HXT    sing N N 184 
HIS N     CA     sing N N 185 
HIS N     H      sing N N 186 
HIS N     H2     sing N N 187 
HIS CA    C      sing N N 188 
HIS CA    CB     sing N N 189 
HIS CA    HA     sing N N 190 
HIS C     O      doub N N 191 
HIS C     OXT    sing N N 192 
HIS CB    CG     sing N N 193 
HIS CB    HB2    sing N N 194 
HIS CB    HB3    sing N N 195 
HIS CG    ND1    sing Y N 196 
HIS CG    CD2    doub Y N 197 
HIS ND1   CE1    doub Y N 198 
HIS ND1   HD1    sing N N 199 
HIS CD2   NE2    sing Y N 200 
HIS CD2   HD2    sing N N 201 
HIS CE1   NE2    sing Y N 202 
HIS CE1   HE1    sing N N 203 
HIS NE2   HE2    sing N N 204 
HIS OXT   HXT    sing N N 205 
HOH O     H1     sing N N 206 
HOH O     H2     sing N N 207 
ILE N     CA     sing N N 208 
ILE N     H      sing N N 209 
ILE N     H2     sing N N 210 
ILE CA    C      sing N N 211 
ILE CA    CB     sing N N 212 
ILE CA    HA     sing N N 213 
ILE C     O      doub N N 214 
ILE C     OXT    sing N N 215 
ILE CB    CG1    sing N N 216 
ILE CB    CG2    sing N N 217 
ILE CB    HB     sing N N 218 
ILE CG1   CD1    sing N N 219 
ILE CG1   HG12   sing N N 220 
ILE CG1   HG13   sing N N 221 
ILE CG2   HG21   sing N N 222 
ILE CG2   HG22   sing N N 223 
ILE CG2   HG23   sing N N 224 
ILE CD1   HD11   sing N N 225 
ILE CD1   HD12   sing N N 226 
ILE CD1   HD13   sing N N 227 
ILE OXT   HXT    sing N N 228 
LEU N     CA     sing N N 229 
LEU N     H      sing N N 230 
LEU N     H2     sing N N 231 
LEU CA    C      sing N N 232 
LEU CA    CB     sing N N 233 
LEU CA    HA     sing N N 234 
LEU C     O      doub N N 235 
LEU C     OXT    sing N N 236 
LEU CB    CG     sing N N 237 
LEU CB    HB2    sing N N 238 
LEU CB    HB3    sing N N 239 
LEU CG    CD1    sing N N 240 
LEU CG    CD2    sing N N 241 
LEU CG    HG     sing N N 242 
LEU CD1   HD11   sing N N 243 
LEU CD1   HD12   sing N N 244 
LEU CD1   HD13   sing N N 245 
LEU CD2   HD21   sing N N 246 
LEU CD2   HD22   sing N N 247 
LEU CD2   HD23   sing N N 248 
LEU OXT   HXT    sing N N 249 
LYS N     CA     sing N N 250 
LYS N     H      sing N N 251 
LYS N     H2     sing N N 252 
LYS CA    C      sing N N 253 
LYS CA    CB     sing N N 254 
LYS CA    HA     sing N N 255 
LYS C     O      doub N N 256 
LYS C     OXT    sing N N 257 
LYS CB    CG     sing N N 258 
LYS CB    HB2    sing N N 259 
LYS CB    HB3    sing N N 260 
LYS CG    CD     sing N N 261 
LYS CG    HG2    sing N N 262 
LYS CG    HG3    sing N N 263 
LYS CD    CE     sing N N 264 
LYS CD    HD2    sing N N 265 
LYS CD    HD3    sing N N 266 
LYS CE    NZ     sing N N 267 
LYS CE    HE2    sing N N 268 
LYS CE    HE3    sing N N 269 
LYS NZ    HZ1    sing N N 270 
LYS NZ    HZ2    sing N N 271 
LYS NZ    HZ3    sing N N 272 
LYS OXT   HXT    sing N N 273 
MET N     CA     sing N N 274 
MET N     H      sing N N 275 
MET N     H2     sing N N 276 
MET CA    C      sing N N 277 
MET CA    CB     sing N N 278 
MET CA    HA     sing N N 279 
MET C     O      doub N N 280 
MET C     OXT    sing N N 281 
MET CB    CG     sing N N 282 
MET CB    HB2    sing N N 283 
MET CB    HB3    sing N N 284 
MET CG    SD     sing N N 285 
MET CG    HG2    sing N N 286 
MET CG    HG3    sing N N 287 
MET SD    CE     sing N N 288 
MET CE    HE1    sing N N 289 
MET CE    HE2    sing N N 290 
MET CE    HE3    sing N N 291 
MET OXT   HXT    sing N N 292 
PHE N     CA     sing N N 293 
PHE N     H      sing N N 294 
PHE N     H2     sing N N 295 
PHE CA    C      sing N N 296 
PHE CA    CB     sing N N 297 
PHE CA    HA     sing N N 298 
PHE C     O      doub N N 299 
PHE C     OXT    sing N N 300 
PHE CB    CG     sing N N 301 
PHE CB    HB2    sing N N 302 
PHE CB    HB3    sing N N 303 
PHE CG    CD1    doub Y N 304 
PHE CG    CD2    sing Y N 305 
PHE CD1   CE1    sing Y N 306 
PHE CD1   HD1    sing N N 307 
PHE CD2   CE2    doub Y N 308 
PHE CD2   HD2    sing N N 309 
PHE CE1   CZ     doub Y N 310 
PHE CE1   HE1    sing N N 311 
PHE CE2   CZ     sing Y N 312 
PHE CE2   HE2    sing N N 313 
PHE CZ    HZ     sing N N 314 
PHE OXT   HXT    sing N N 315 
PRO N     CA     sing N N 316 
PRO N     CD     sing N N 317 
PRO N     H      sing N N 318 
PRO CA    C      sing N N 319 
PRO CA    CB     sing N N 320 
PRO CA    HA     sing N N 321 
PRO C     O      doub N N 322 
PRO C     OXT    sing N N 323 
PRO CB    CG     sing N N 324 
PRO CB    HB2    sing N N 325 
PRO CB    HB3    sing N N 326 
PRO CG    CD     sing N N 327 
PRO CG    HG2    sing N N 328 
PRO CG    HG3    sing N N 329 
PRO CD    HD2    sing N N 330 
PRO CD    HD3    sing N N 331 
PRO OXT   HXT    sing N N 332 
SER N     CA     sing N N 333 
SER N     H      sing N N 334 
SER N     H2     sing N N 335 
SER CA    C      sing N N 336 
SER CA    CB     sing N N 337 
SER CA    HA     sing N N 338 
SER C     O      doub N N 339 
SER C     OXT    sing N N 340 
SER CB    OG     sing N N 341 
SER CB    HB2    sing N N 342 
SER CB    HB3    sing N N 343 
SER OG    HG     sing N N 344 
SER OXT   HXT    sing N N 345 
THR N     CA     sing N N 346 
THR N     H      sing N N 347 
THR N     H2     sing N N 348 
THR CA    C      sing N N 349 
THR CA    CB     sing N N 350 
THR CA    HA     sing N N 351 
THR C     O      doub N N 352 
THR C     OXT    sing N N 353 
THR CB    OG1    sing N N 354 
THR CB    CG2    sing N N 355 
THR CB    HB     sing N N 356 
THR OG1   HG1    sing N N 357 
THR CG2   HG21   sing N N 358 
THR CG2   HG22   sing N N 359 
THR CG2   HG23   sing N N 360 
THR OXT   HXT    sing N N 361 
TYR N     CA     sing N N 362 
TYR N     H      sing N N 363 
TYR N     H2     sing N N 364 
TYR CA    C      sing N N 365 
TYR CA    CB     sing N N 366 
TYR CA    HA     sing N N 367 
TYR C     O      doub N N 368 
TYR C     OXT    sing N N 369 
TYR CB    CG     sing N N 370 
TYR CB    HB2    sing N N 371 
TYR CB    HB3    sing N N 372 
TYR CG    CD1    doub Y N 373 
TYR CG    CD2    sing Y N 374 
TYR CD1   CE1    sing Y N 375 
TYR CD1   HD1    sing N N 376 
TYR CD2   CE2    doub Y N 377 
TYR CD2   HD2    sing N N 378 
TYR CE1   CZ     doub Y N 379 
TYR CE1   HE1    sing N N 380 
TYR CE2   CZ     sing Y N 381 
TYR CE2   HE2    sing N N 382 
TYR CZ    OH     sing N N 383 
TYR OH    HH     sing N N 384 
TYR OXT   HXT    sing N N 385 
VAL N     CA     sing N N 386 
VAL N     H      sing N N 387 
VAL N     H2     sing N N 388 
VAL CA    C      sing N N 389 
VAL CA    CB     sing N N 390 
VAL CA    HA     sing N N 391 
VAL C     O      doub N N 392 
VAL C     OXT    sing N N 393 
VAL CB    CG1    sing N N 394 
VAL CB    CG2    sing N N 395 
VAL CB    HB     sing N N 396 
VAL CG1   HG11   sing N N 397 
VAL CG1   HG12   sing N N 398 
VAL CG1   HG13   sing N N 399 
VAL CG2   HG21   sing N N 400 
VAL CG2   HG22   sing N N 401 
VAL CG2   HG23   sing N N 402 
VAL OXT   HXT    sing N N 403 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Cancer Institute (NIH/NCI)' 'United States' R35CA220430 1 
'Cancer Prevention and Research Institute of Texas (CPRIT)'         'United States' RP180813    2 
'National Institutes of Health/National Cancer Institute (NIH/NCI)' 'United States' F31CA142313 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1N0W 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8UVW 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.019431 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010147 
_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]   0.007793 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
BE 
C  
F  
N  
O  
P  
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     . THR A 1 6   ? 44.903  -11.271 -14.274 1.00 149.13 ? 1520 THR B N     1 
ATOM   2    C  CA    . THR A 1 6   ? 43.738  -12.146 -14.324 1.00 146.06 ? 1520 THR B CA    1 
ATOM   3    C  C     . THR A 1 6   ? 43.230  -12.457 -12.919 1.00 152.81 ? 1520 THR B C     1 
ATOM   4    O  O     . THR A 1 6   ? 43.739  -13.357 -12.250 1.00 146.49 ? 1520 THR B O     1 
ATOM   5    C  CB    . THR A 1 6   ? 44.053  -13.467 -15.054 1.00 142.10 ? 1520 THR B CB    1 
ATOM   6    O  OG1   . THR A 1 6   ? 44.585  -13.182 -16.354 1.00 131.19 ? 1520 THR B OG1   1 
ATOM   7    C  CG2   . THR A 1 6   ? 42.793  -14.309 -15.203 1.00 131.54 ? 1520 THR B CG2   1 
ATOM   8    N  N     . LEU A 1 7   ? 42.226  -11.705 -12.476 1.00 152.52 ? 1521 LEU B N     1 
ATOM   9    C  CA    . LEU A 1 7   ? 41.627  -11.922 -11.169 1.00 147.53 ? 1521 LEU B CA    1 
ATOM   10   C  C     . LEU A 1 7   ? 40.717  -13.148 -11.200 1.00 145.37 ? 1521 LEU B C     1 
ATOM   11   O  O     . LEU A 1 7   ? 40.593  -13.843 -12.213 1.00 142.95 ? 1521 LEU B O     1 
ATOM   12   C  CB    . LEU A 1 7   ? 40.856  -10.681 -10.723 1.00 135.21 ? 1521 LEU B CB    1 
ATOM   13   C  CG    . LEU A 1 7   ? 41.667  -9.548  -10.093 1.00 129.73 ? 1521 LEU B CG    1 
ATOM   14   C  CD1   . LEU A 1 7   ? 40.788  -8.332  -9.853  1.00 120.51 ? 1521 LEU B CD1   1 
ATOM   15   C  CD2   . LEU A 1 7   ? 42.303  -10.015 -8.792  1.00 131.71 ? 1521 LEU B CD2   1 
ATOM   16   N  N     . LEU A 1 8   ? 40.073  -13.419 -10.068 1.00 142.83 ? 1522 LEU B N     1 
ATOM   17   C  CA    . LEU A 1 8   ? 39.128  -14.526 -9.983  1.00 140.27 ? 1522 LEU B CA    1 
ATOM   18   C  C     . LEU A 1 8   ? 37.931  -14.246 -10.883 1.00 127.88 ? 1522 LEU B C     1 
ATOM   19   O  O     . LEU A 1 8   ? 37.286  -13.199 -10.761 1.00 120.36 ? 1522 LEU B O     1 
ATOM   20   C  CB    . LEU A 1 8   ? 38.682  -14.732 -8.538  1.00 131.79 ? 1522 LEU B CB    1 
ATOM   21   C  CG    . LEU A 1 8   ? 39.779  -15.082 -7.531  1.00 122.15 ? 1522 LEU B CG    1 
ATOM   22   C  CD1   . LEU A 1 8   ? 39.193  -15.261 -6.139  1.00 121.59 ? 1522 LEU B CD1   1 
ATOM   23   C  CD2   . LEU A 1 8   ? 40.528  -16.332 -7.967  1.00 130.34 ? 1522 LEU B CD2   1 
ATOM   24   N  N     . GLY A 1 9   ? 37.641  -15.175 -11.789 1.00 121.44 ? 1523 GLY B N     1 
ATOM   25   C  CA    . GLY A 1 9   ? 36.549  -15.002 -12.725 1.00 122.44 ? 1523 GLY B CA    1 
ATOM   26   C  C     . GLY A 1 9   ? 35.182  -15.175 -12.098 1.00 122.31 ? 1523 GLY B C     1 
ATOM   27   O  O     . GLY A 1 9   ? 34.875  -14.557 -11.074 1.00 123.11 ? 1523 GLY B O     1 
ATOM   28   N  N     . PHE A 1 10  ? 34.350  -16.016 -12.705 1.00 112.95 ? 1524 PHE B N     1 
ATOM   29   C  CA    . PHE A 1 10  ? 32.994  -16.262 -12.229 1.00 111.31 ? 1524 PHE B CA    1 
ATOM   30   C  C     . PHE A 1 10  ? 32.961  -17.593 -11.489 1.00 116.61 ? 1524 PHE B C     1 
ATOM   31   O  O     . PHE A 1 10  ? 33.029  -18.659 -12.110 1.00 119.77 ? 1524 PHE B O     1 
ATOM   32   C  CB    . PHE A 1 10  ? 32.000  -16.257 -13.387 1.00 119.23 ? 1524 PHE B CB    1 
ATOM   33   C  CG    . PHE A 1 10  ? 31.173  -15.008 -13.471 1.00 118.57 ? 1524 PHE B CG    1 
ATOM   34   C  CD1   . PHE A 1 10  ? 30.052  -14.852 -12.673 1.00 109.95 ? 1524 PHE B CD1   1 
ATOM   35   C  CD2   . PHE A 1 10  ? 31.512  -13.993 -14.349 1.00 119.29 ? 1524 PHE B CD2   1 
ATOM   36   C  CE1   . PHE A 1 10  ? 29.288  -13.705 -12.746 1.00 103.71 ? 1524 PHE B CE1   1 
ATOM   37   C  CE2   . PHE A 1 10  ? 30.749  -12.843 -14.427 1.00 105.07 ? 1524 PHE B CE2   1 
ATOM   38   C  CZ    . PHE A 1 10  ? 29.636  -12.700 -13.625 1.00 104.63 ? 1524 PHE B CZ    1 
ATOM   39   N  N     . HIS A 1 11  ? 32.858  -17.529 -10.167 1.00 106.70 ? 1525 HIS B N     1 
ATOM   40   C  CA    . HIS A 1 11  ? 32.667  -18.706 -9.337  1.00 104.98 ? 1525 HIS B CA    1 
ATOM   41   C  C     . HIS A 1 11  ? 31.198  -18.833 -8.953  1.00 93.26  ? 1525 HIS B C     1 
ATOM   42   O  O     . HIS A 1 11  ? 30.370  -17.973 -9.260  1.00 87.08  ? 1525 HIS B O     1 
ATOM   43   C  CB    . HIS A 1 11  ? 33.547  -18.634 -8.085  1.00 109.90 ? 1525 HIS B CB    1 
ATOM   44   C  CG    . HIS A 1 11  ? 35.009  -18.506 -8.380  1.00 108.01 ? 1525 HIS B CG    1 
ATOM   45   N  ND1   . HIS A 1 11  ? 35.850  -19.594 -8.466  1.00 114.65 ? 1525 HIS B ND1   1 
ATOM   46   C  CD2   . HIS A 1 11  ? 35.780  -17.416 -8.608  1.00 111.93 ? 1525 HIS B CD2   1 
ATOM   47   C  CE1   . HIS A 1 11  ? 37.076  -19.181 -8.735  1.00 124.14 ? 1525 HIS B CE1   1 
ATOM   48   N  NE2   . HIS A 1 11  ? 37.061  -17.864 -8.826  1.00 125.72 ? 1525 HIS B NE2   1 
ATOM   49   N  N     . THR A 1 12  ? 30.876  -19.927 -8.275  1.00 100.25 ? 1526 THR B N     1 
ATOM   50   C  CA    . THR A 1 12  ? 29.526  -20.159 -7.788  1.00 106.93 ? 1526 THR B CA    1 
ATOM   51   C  C     . THR A 1 12  ? 29.426  -19.769 -6.318  1.00 112.78 ? 1526 THR B C     1 
ATOM   52   O  O     . THR A 1 12  ? 30.422  -19.474 -5.653  1.00 112.58 ? 1526 THR B O     1 
ATOM   53   C  CB    . THR A 1 12  ? 29.121  -21.623 -7.980  1.00 113.48 ? 1526 THR B CB    1 
ATOM   54   O  OG1   . THR A 1 12  ? 27.729  -21.779 -7.679  1.00 123.22 ? 1526 THR B OG1   1 
ATOM   55   C  CG2   . THR A 1 12  ? 29.928  -22.515 -7.057  1.00 111.37 ? 1526 THR B CG2   1 
ATOM   56   N  N     . ALA A 1 13  ? 28.191  -19.766 -5.811  1.00 114.66 ? 1527 ALA B N     1 
ATOM   57   C  CA    . ALA A 1 13  ? 27.976  -19.479 -4.398  1.00 115.90 ? 1527 ALA B CA    1 
ATOM   58   C  C     . ALA A 1 13  ? 28.530  -20.575 -3.499  1.00 121.61 ? 1527 ALA B C     1 
ATOM   59   O  O     . ALA A 1 13  ? 28.801  -20.317 -2.322  1.00 121.48 ? 1527 ALA B O     1 
ATOM   60   C  CB    . ALA A 1 13  ? 26.486  -19.274 -4.123  1.00 101.79 ? 1527 ALA B CB    1 
ATOM   61   N  N     . SER A 1 14  ? 28.706  -21.789 -4.027  1.00 118.27 ? 1528 SER B N     1 
ATOM   62   C  CA    . SER A 1 14  ? 29.306  -22.872 -3.260  1.00 112.95 ? 1528 SER B CA    1 
ATOM   63   C  C     . SER A 1 14  ? 30.823  -22.761 -3.178  1.00 113.14 ? 1528 SER B C     1 
ATOM   64   O  O     . SER A 1 14  ? 31.425  -23.352 -2.275  1.00 130.59 ? 1528 SER B O     1 
ATOM   65   C  CB    . SER A 1 14  ? 28.925  -24.225 -3.866  1.00 113.39 ? 1528 SER B CB    1 
ATOM   66   O  OG    . SER A 1 14  ? 27.520  -24.391 -3.901  1.00 108.17 ? 1528 SER B OG    1 
ATOM   67   N  N     . GLY A 1 15  ? 31.449  -22.029 -4.097  1.00 116.92 ? 1529 GLY B N     1 
ATOM   68   C  CA    . GLY A 1 15  ? 32.882  -21.801 -4.083  1.00 112.18 ? 1529 GLY B CA    1 
ATOM   69   C  C     . GLY A 1 15  ? 33.634  -22.403 -5.252  1.00 116.95 ? 1529 GLY B C     1 
ATOM   70   O  O     . GLY A 1 15  ? 34.726  -21.917 -5.583  1.00 111.81 ? 1529 GLY B O     1 
ATOM   71   N  N     . LYS A 1 16  ? 33.097  -23.440 -5.888  1.00 112.66 ? 1530 LYS B N     1 
ATOM   72   C  CA    . LYS A 1 16  ? 33.816  -24.092 -6.972  1.00 115.34 ? 1530 LYS B CA    1 
ATOM   73   C  C     . LYS A 1 16  ? 33.856  -23.200 -8.209  1.00 123.55 ? 1530 LYS B C     1 
ATOM   74   O  O     . LYS A 1 16  ? 32.973  -22.369 -8.437  1.00 124.55 ? 1530 LYS B O     1 
ATOM   75   C  CB    . LYS A 1 16  ? 33.175  -25.439 -7.308  1.00 114.49 ? 1530 LYS B CB    1 
ATOM   76   C  CG    . LYS A 1 16  ? 31.823  -25.343 -7.992  1.00 119.66 ? 1530 LYS B CG    1 
ATOM   77   C  CD    . LYS A 1 16  ? 31.083  -26.668 -7.947  1.00 133.05 ? 1530 LYS B CD    1 
ATOM   78   C  CE    . LYS A 1 16  ? 30.749  -27.062 -6.516  1.00 129.06 ? 1530 LYS B CE    1 
ATOM   79   N  NZ    . LYS A 1 16  ? 29.970  -28.329 -6.458  1.00 124.40 ? 1530 LYS B NZ    1 
ATOM   80   N  N     . LYS A 1 17  ? 34.905  -23.376 -9.009  1.00 124.64 ? 1531 LYS B N     1 
ATOM   81   C  CA    . LYS A 1 17  ? 35.120  -22.541 -10.182 1.00 116.57 ? 1531 LYS B CA    1 
ATOM   82   C  C     . LYS A 1 17  ? 34.296  -23.044 -11.360 1.00 122.28 ? 1531 LYS B C     1 
ATOM   83   O  O     . LYS A 1 17  ? 34.168  -24.252 -11.578 1.00 125.07 ? 1531 LYS B O     1 
ATOM   84   C  CB    . LYS A 1 17  ? 36.605  -22.521 -10.549 1.00 103.50 ? 1531 LYS B CB    1 
ATOM   85   C  CG    . LYS A 1 17  ? 36.953  -21.614 -11.718 1.00 110.23 ? 1531 LYS B CG    1 
ATOM   86   C  CD    . LYS A 1 17  ? 38.440  -21.672 -12.034 1.00 129.21 ? 1531 LYS B CD    1 
ATOM   87   C  CE    . LYS A 1 17  ? 38.791  -20.791 -13.222 1.00 116.09 ? 1531 LYS B CE    1 
ATOM   88   N  NZ    . LYS A 1 17  ? 40.242  -20.860 -13.551 1.00 108.48 ? 1531 LYS B NZ    1 
ATOM   89   N  N     . VAL A 1 18  ? 33.736  -22.106 -12.119 1.00 116.98 ? 1532 VAL B N     1 
ATOM   90   C  CA    . VAL A 1 18  ? 32.974  -22.424 -13.320 1.00 121.10 ? 1532 VAL B CA    1 
ATOM   91   C  C     . VAL A 1 18  ? 33.927  -22.462 -14.506 1.00 125.25 ? 1532 VAL B C     1 
ATOM   92   O  O     . VAL A 1 18  ? 34.694  -21.517 -14.730 1.00 123.35 ? 1532 VAL B O     1 
ATOM   93   C  CB    . VAL A 1 18  ? 31.850  -21.399 -13.547 1.00 121.30 ? 1532 VAL B CB    1 
ATOM   94   C  CG1   . VAL A 1 18  ? 31.045  -21.759 -14.787 1.00 111.86 ? 1532 VAL B CG1   1 
ATOM   95   C  CG2   . VAL A 1 18  ? 30.951  -21.315 -12.323 1.00 123.34 ? 1532 VAL B CG2   1 
ATOM   96   N  N     . LYS A 1 19  ? 33.882  -23.551 -15.266 1.00 122.07 ? 1533 LYS B N     1 
ATOM   97   C  CA    . LYS A 1 19  ? 34.767  -23.746 -16.406 1.00 125.75 ? 1533 LYS B CA    1 
ATOM   98   C  C     . LYS A 1 19  ? 34.009  -23.506 -17.705 1.00 119.66 ? 1533 LYS B C     1 
ATOM   99   O  O     . LYS A 1 19  ? 32.861  -23.933 -17.856 1.00 110.51 ? 1533 LYS B O     1 
ATOM   100  C  CB    . LYS A 1 19  ? 35.365  -25.155 -16.395 1.00 126.98 ? 1533 LYS B CB    1 
ATOM   101  C  CG    . LYS A 1 19  ? 36.644  -25.290 -17.203 1.00 115.55 ? 1533 LYS B CG    1 
ATOM   102  C  CD    . LYS A 1 19  ? 37.329  -26.619 -16.929 1.00 112.76 ? 1533 LYS B CD    1 
ATOM   103  C  CE    . LYS A 1 19  ? 38.709  -26.668 -17.565 1.00 127.23 ? 1533 LYS B CE    1 
ATOM   104  N  NZ    . LYS A 1 19  ? 39.409  -27.949 -17.273 1.00 118.52 ? 1533 LYS B NZ    1 
ATOM   105  N  N     . ILE A 1 20  ? 34.660  -22.818 -18.640 1.00 120.97 ? 1534 ILE B N     1 
ATOM   106  C  CA    . ILE A 1 20  ? 34.054  -22.426 -19.906 1.00 123.56 ? 1534 ILE B CA    1 
ATOM   107  C  C     . ILE A 1 20  ? 34.816  -23.094 -21.041 1.00 117.36 ? 1534 ILE B C     1 
ATOM   108  O  O     . ILE A 1 20  ? 36.042  -23.235 -20.981 1.00 120.45 ? 1534 ILE B O     1 
ATOM   109  C  CB    . ILE A 1 20  ? 34.052  -20.893 -20.082 1.00 120.48 ? 1534 ILE B CB    1 
ATOM   110  C  CG1   . ILE A 1 20  ? 33.609  -20.207 -18.790 1.00 127.36 ? 1534 ILE B CG1   1 
ATOM   111  C  CG2   . ILE A 1 20  ? 33.141  -20.485 -21.233 1.00 111.36 ? 1534 ILE B CG2   1 
ATOM   112  C  CD1   . ILE A 1 20  ? 33.759  -18.706 -18.823 1.00 124.85 ? 1534 ILE B CD1   1 
ATOM   113  N  N     . ALA A 1 21  ? 34.087  -23.503 -22.074 1.00 107.01 ? 1535 ALA B N     1 
ATOM   114  C  CA    . ALA A 1 21  ? 34.709  -24.074 -23.257 1.00 117.45 ? 1535 ALA B CA    1 
ATOM   115  C  C     . ALA A 1 21  ? 35.175  -22.969 -24.199 1.00 111.13 ? 1535 ALA B C     1 
ATOM   116  O  O     . ALA A 1 21  ? 34.623  -21.866 -24.217 1.00 111.41 ? 1535 ALA B O     1 
ATOM   117  C  CB    . ALA A 1 21  ? 33.735  -25.005 -23.979 1.00 123.83 ? 1535 ALA B CB    1 
ATOM   118  N  N     . LYS A 1 22  ? 36.202  -23.278 -24.993 1.00 115.50 ? 1536 LYS B N     1 
ATOM   119  C  CA    . LYS A 1 22  ? 36.751  -22.278 -25.905 1.00 115.34 ? 1536 LYS B CA    1 
ATOM   120  C  C     . LYS A 1 22  ? 35.797  -21.978 -27.055 1.00 107.84 ? 1536 LYS B C     1 
ATOM   121  O  O     . LYS A 1 22  ? 35.846  -20.882 -27.627 1.00 99.37  ? 1536 LYS B O     1 
ATOM   122  C  CB    . LYS A 1 22  ? 38.109  -22.740 -26.436 1.00 108.64 ? 1536 LYS B CB    1 
ATOM   123  C  CG    . LYS A 1 22  ? 38.839  -21.701 -27.270 1.00 99.13  ? 1536 LYS B CG    1 
ATOM   124  C  CD    . LYS A 1 22  ? 38.961  -20.378 -26.530 1.00 129.08 ? 1536 LYS B CD    1 
ATOM   125  C  CE    . LYS A 1 22  ? 39.611  -19.316 -27.400 1.00 131.19 ? 1536 LYS B CE    1 
ATOM   126  N  NZ    . LYS A 1 22  ? 39.654  -17.991 -26.724 1.00 141.55 ? 1536 LYS B NZ    1 
ATOM   127  N  N     . GLU A 1 23  ? 34.918  -22.923 -27.399 1.00 110.11 ? 1537 GLU B N     1 
ATOM   128  C  CA    . GLU A 1 23  ? 33.937  -22.668 -28.450 1.00 114.97 ? 1537 GLU B CA    1 
ATOM   129  C  C     . GLU A 1 23  ? 32.978  -21.550 -28.063 1.00 109.07 ? 1537 GLU B C     1 
ATOM   130  O  O     . GLU A 1 23  ? 32.527  -20.789 -28.928 1.00 98.32  ? 1537 GLU B O     1 
ATOM   131  C  CB    . GLU A 1 23  ? 33.154  -23.942 -28.769 1.00 117.05 ? 1537 GLU B CB    1 
ATOM   132  C  CG    . GLU A 1 23  ? 34.019  -25.129 -29.166 1.00 116.26 ? 1537 GLU B CG    1 
ATOM   133  C  CD    . GLU A 1 23  ? 34.506  -25.926 -27.972 1.00 123.55 ? 1537 GLU B CD    1 
ATOM   134  O  OE1   . GLU A 1 23  ? 33.698  -26.182 -27.055 1.00 127.29 ? 1537 GLU B OE1   1 
ATOM   135  O  OE2   . GLU A 1 23  ? 35.700  -26.288 -27.946 1.00 123.11 ? 1537 GLU B OE2   1 
ATOM   136  N  N     . SER A 1 24  ? 32.657  -21.433 -26.773 1.00 114.65 ? 1538 SER B N     1 
ATOM   137  C  CA    . SER A 1 24  ? 31.766  -20.367 -26.328 1.00 103.58 ? 1538 SER B CA    1 
ATOM   138  C  C     . SER A 1 24  ? 32.462  -19.012 -26.368 1.00 109.65 ? 1538 SER B C     1 
ATOM   139  O  O     . SER A 1 24  ? 31.832  -17.994 -26.678 1.00 112.50 ? 1538 SER B O     1 
ATOM   140  C  CB    . SER A 1 24  ? 31.254  -20.670 -24.921 1.00 95.40  ? 1538 SER B CB    1 
ATOM   141  O  OG    . SER A 1 24  ? 30.509  -21.875 -24.905 1.00 86.25  ? 1538 SER B OG    1 
ATOM   142  N  N     . LEU A 1 25  ? 33.759  -18.978 -26.052 1.00 103.62 ? 1539 LEU B N     1 
ATOM   143  C  CA    . LEU A 1 25  ? 34.504  -17.725 -26.118 1.00 106.69 ? 1539 LEU B CA    1 
ATOM   144  C  C     . LEU A 1 25  ? 34.595  -17.212 -27.550 1.00 115.19 ? 1539 LEU B C     1 
ATOM   145  O  O     . LEU A 1 25  ? 34.443  -16.010 -27.794 1.00 120.18 ? 1539 LEU B O     1 
ATOM   146  C  CB    . LEU A 1 25  ? 35.900  -17.913 -25.523 1.00 116.83 ? 1539 LEU B CB    1 
ATOM   147  C  CG    . LEU A 1 25  ? 35.977  -18.075 -24.005 1.00 113.01 ? 1539 LEU B CG    1 
ATOM   148  C  CD1   . LEU A 1 25  ? 37.369  -18.510 -23.576 1.00 113.47 ? 1539 LEU B CD1   1 
ATOM   149  C  CD2   . LEU A 1 25  ? 35.589  -16.778 -23.317 1.00 106.98 ? 1539 LEU B CD2   1 
ATOM   150  N  N     . ASP A 1 26  ? 34.840  -18.108 -28.508 1.00 114.46 ? 1540 ASP B N     1 
ATOM   151  C  CA    . ASP A 1 26  ? 34.877  -17.734 -29.915 1.00 123.28 ? 1540 ASP B CA    1 
ATOM   152  C  C     . ASP A 1 26  ? 33.492  -17.493 -30.500 1.00 112.49 ? 1540 ASP B C     1 
ATOM   153  O  O     . ASP A 1 26  ? 33.391  -16.947 -31.604 1.00 111.86 ? 1540 ASP B O     1 
ATOM   154  C  CB    . ASP A 1 26  ? 35.593  -18.816 -30.726 1.00 131.44 ? 1540 ASP B CB    1 
ATOM   155  C  CG    . ASP A 1 26  ? 37.058  -18.947 -30.359 1.00 125.35 ? 1540 ASP B CG    1 
ATOM   156  O  OD1   . ASP A 1 26  ? 37.557  -18.102 -29.588 1.00 115.18 ? 1540 ASP B OD1   1 
ATOM   157  O  OD2   . ASP A 1 26  ? 37.709  -19.898 -30.841 1.00 117.21 ? 1540 ASP B OD2   1 
ATOM   158  N  N     . LYS A 1 27  ? 32.432  -17.884 -29.794 1.00 110.04 ? 1541 LYS B N     1 
ATOM   159  C  CA    . LYS A 1 27  ? 31.071  -17.693 -30.276 1.00 117.32 ? 1541 LYS B CA    1 
ATOM   160  C  C     . LYS A 1 27  ? 30.492  -16.339 -29.893 1.00 115.87 ? 1541 LYS B C     1 
ATOM   161  O  O     . LYS A 1 27  ? 29.492  -15.918 -30.486 1.00 103.95 ? 1541 LYS B O     1 
ATOM   162  C  CB    . LYS A 1 27  ? 30.167  -18.809 -29.740 1.00 110.82 ? 1541 LYS B CB    1 
ATOM   163  C  CG    . LYS A 1 27  ? 28.884  -19.028 -30.529 1.00 117.09 ? 1541 LYS B CG    1 
ATOM   164  C  CD    . LYS A 1 27  ? 28.129  -20.243 -30.010 1.00 109.61 ? 1541 LYS B CD    1 
ATOM   165  C  CE    . LYS A 1 27  ? 26.897  -20.536 -30.851 1.00 121.83 ? 1541 LYS B CE    1 
ATOM   166  N  NZ    . LYS A 1 27  ? 25.922  -19.412 -30.823 1.00 127.01 ? 1541 LYS B NZ    1 
ATOM   167  N  N     . VAL A 1 28  ? 31.097  -15.646 -28.928 1.00 106.65 ? 1542 VAL B N     1 
ATOM   168  C  CA    . VAL A 1 28  ? 30.596  -14.365 -28.448 1.00 114.02 ? 1542 VAL B CA    1 
ATOM   169  C  C     . VAL A 1 28  ? 31.556  -13.218 -28.717 1.00 116.97 ? 1542 VAL B C     1 
ATOM   170  O  O     . VAL A 1 28  ? 31.267  -12.083 -28.326 1.00 117.37 ? 1542 VAL B O     1 
ATOM   171  C  CB    . VAL A 1 28  ? 30.251  -14.425 -26.945 1.00 114.88 ? 1542 VAL B CB    1 
ATOM   172  C  CG1   . VAL A 1 28  ? 29.186  -15.479 -26.687 1.00 101.61 ? 1542 VAL B CG1   1 
ATOM   173  C  CG2   . VAL A 1 28  ? 31.501  -14.702 -26.124 1.00 112.73 ? 1542 VAL B CG2   1 
ATOM   174  N  N     . LYS A 1 29  ? 32.694  -13.473 -29.369 1.00 115.67 ? 1543 LYS B N     1 
ATOM   175  C  CA    . LYS A 1 29  ? 33.605  -12.381 -29.697 1.00 112.82 ? 1543 LYS B CA    1 
ATOM   176  C  C     . LYS A 1 29  ? 33.013  -11.451 -30.747 1.00 114.66 ? 1543 LYS B C     1 
ATOM   177  O  O     . LYS A 1 29  ? 33.337  -10.258 -30.771 1.00 109.04 ? 1543 LYS B O     1 
ATOM   178  C  CB    . LYS A 1 29  ? 34.950  -12.932 -30.172 1.00 110.94 ? 1543 LYS B CB    1 
ATOM   179  C  CG    . LYS A 1 29  ? 35.883  -13.347 -29.047 1.00 123.17 ? 1543 LYS B CG    1 
ATOM   180  C  CD    . LYS A 1 29  ? 37.249  -13.746 -29.580 1.00 128.14 ? 1543 LYS B CD    1 
ATOM   181  C  CE    . LYS A 1 29  ? 38.224  -14.032 -28.448 1.00 121.32 ? 1543 LYS B CE    1 
ATOM   182  N  NZ    . LYS A 1 29  ? 38.456  -12.833 -27.596 1.00 100.86 ? 1543 LYS B NZ    1 
ATOM   183  N  N     . ASN A 1 30  ? 32.146  -11.972 -31.618 1.00 120.14 ? 1544 ASN B N     1 
ATOM   184  C  CA    . ASN A 1 30  ? 31.483  -11.137 -32.612 1.00 124.10 ? 1544 ASN B CA    1 
ATOM   185  C  C     . ASN A 1 30  ? 30.379  -10.277 -32.013 1.00 130.41 ? 1544 ASN B C     1 
ATOM   186  O  O     . ASN A 1 30  ? 29.817  -9.438  -32.726 1.00 135.00 ? 1544 ASN B O     1 
ATOM   187  C  CB    . ASN A 1 30  ? 30.912  -12.007 -33.733 1.00 128.20 ? 1544 ASN B CB    1 
ATOM   188  C  CG    . ASN A 1 30  ? 31.984  -12.786 -34.471 1.00 142.98 ? 1544 ASN B CG    1 
ATOM   189  O  OD1   . ASN A 1 30  ? 33.138  -12.364 -34.538 1.00 132.74 ? 1544 ASN B OD1   1 
ATOM   190  N  ND2   . ASN A 1 30  ? 31.606  -13.929 -35.031 1.00 133.88 ? 1544 ASN B ND2   1 
ATOM   191  N  N     . LEU A 1 31  ? 30.055  -10.464 -30.737 1.00 117.56 ? 1545 LEU B N     1 
ATOM   192  C  CA    . LEU A 1 31  ? 29.047  -9.654  -30.075 1.00 105.63 ? 1545 LEU B CA    1 
ATOM   193  C  C     . LEU A 1 31  ? 29.629  -8.289  -29.705 1.00 113.09 ? 1545 LEU B C     1 
ATOM   194  O  O     . LEU A 1 31  ? 30.838  -8.054  -29.792 1.00 121.37 ? 1545 LEU B O     1 
ATOM   195  C  CB    . LEU A 1 31  ? 28.517  -10.377 -28.835 1.00 99.51  ? 1545 LEU B CB    1 
ATOM   196  C  CG    . LEU A 1 31  ? 27.154  -9.958  -28.277 1.00 102.08 ? 1545 LEU B CG    1 
ATOM   197  C  CD1   . LEU A 1 31  ? 26.070  -10.116 -29.332 1.00 107.05 ? 1545 LEU B CD1   1 
ATOM   198  C  CD2   . LEU A 1 31  ? 26.815  -10.760 -27.031 1.00 99.00  ? 1545 LEU B CD2   1 
ATOM   199  N  N     . PHE A 1 32  ? 28.742  -7.381  -29.294 1.00 111.01 ? 1546 PHE B N     1 
ATOM   200  C  CA    . PHE A 1 32  ? 29.104  -6.015  -28.914 1.00 109.23 ? 1546 PHE B CA    1 
ATOM   201  C  C     . PHE A 1 32  ? 29.782  -5.290  -30.078 1.00 121.36 ? 1546 PHE B C     1 
ATOM   202  O  O     . PHE A 1 32  ? 30.931  -4.851  -29.995 1.00 125.84 ? 1546 PHE B O     1 
ATOM   203  C  CB    . PHE A 1 32  ? 29.989  -6.005  -27.662 1.00 102.34 ? 1546 PHE B CB    1 
ATOM   204  C  CG    . PHE A 1 32  ? 29.501  -6.907  -26.565 1.00 114.66 ? 1546 PHE B CG    1 
ATOM   205  C  CD1   . PHE A 1 32  ? 28.343  -6.608  -25.867 1.00 108.51 ? 1546 PHE B CD1   1 
ATOM   206  C  CD2   . PHE A 1 32  ? 30.206  -8.050  -26.226 1.00 117.22 ? 1546 PHE B CD2   1 
ATOM   207  C  CE1   . PHE A 1 32  ? 27.893  -7.436  -24.855 1.00 95.35  ? 1546 PHE B CE1   1 
ATOM   208  C  CE2   . PHE A 1 32  ? 29.761  -8.882  -25.215 1.00 109.26 ? 1546 PHE B CE2   1 
ATOM   209  C  CZ    . PHE A 1 32  ? 28.604  -8.574  -24.529 1.00 92.87  ? 1546 PHE B CZ    1 
ATOM   210  N  N     . ASP A 1 33  ? 29.042  -5.174  -31.176 1.00 129.85 ? 1547 ASP B N     1 
ATOM   211  C  CA    . ASP A 1 33  ? 29.547  -4.518  -32.376 1.00 117.46 ? 1547 ASP B CA    1 
ATOM   212  C  C     . ASP A 1 33  ? 28.475  -3.639  -33.012 1.00 114.80 ? 1547 ASP B C     1 
ATOM   213  O  O     . ASP A 1 33  ? 28.517  -3.361  -34.211 1.00 105.75 ? 1547 ASP B O     1 
ATOM   214  C  CB    . ASP A 1 33  ? 30.043  -5.557  -33.384 1.00 124.95 ? 1547 ASP B CB    1 
ATOM   215  C  CG    . ASP A 1 33  ? 28.972  -6.562  -33.761 1.00 133.37 ? 1547 ASP B CG    1 
ATOM   216  O  OD1   . ASP A 1 33  ? 28.101  -6.852  -32.913 1.00 116.41 ? 1547 ASP B OD1   1 
ATOM   217  O  OD2   . ASP A 1 33  ? 29.002  -7.064  -34.905 1.00 132.30 ? 1547 ASP B OD2   1 
ATOM   218  N  N     . GLY A 1 41  ? 17.351  -9.854  -39.535 1.00 129.20 ? 83   GLY B N     1 
ATOM   219  C  CA    . GLY A 1 41  ? 16.394  -10.373 -40.494 1.00 136.93 ? 83   GLY B CA    1 
ATOM   220  C  C     . GLY A 1 41  ? 14.954  -10.250 -40.037 1.00 147.07 ? 83   GLY B C     1 
ATOM   221  O  O     . GLY A 1 41  ? 14.060  -10.883 -40.599 1.00 148.57 ? 83   GLY B O     1 
ATOM   222  N  N     . SER A 1 42  ? 14.730  -9.433  -39.011 1.00 133.79 ? 84   SER B N     1 
ATOM   223  C  CA    . SER A 1 42  ? 13.385  -9.227  -38.494 1.00 122.65 ? 84   SER B CA    1 
ATOM   224  C  C     . SER A 1 42  ? 12.530  -8.474  -39.508 1.00 117.81 ? 84   SER B C     1 
ATOM   225  O  O     . SER A 1 42  ? 13.010  -7.601  -40.237 1.00 130.64 ? 84   SER B O     1 
ATOM   226  C  CB    . SER A 1 42  ? 13.431  -8.459  -37.173 1.00 120.45 ? 84   SER B CB    1 
ATOM   227  O  OG    . SER A 1 42  ? 12.126  -8.212  -36.681 1.00 125.32 ? 84   SER B OG    1 
ATOM   228  N  N     . GLY A 1 43  ? 11.242  -8.821  -39.547 1.00 92.80  ? 85   GLY B N     1 
ATOM   229  C  CA    . GLY A 1 43  ? 10.318  -8.241  -40.496 1.00 98.56  ? 85   GLY B CA    1 
ATOM   230  C  C     . GLY A 1 43  ? 9.082   -7.679  -39.809 1.00 90.79  ? 85   GLY B C     1 
ATOM   231  O  O     . GLY A 1 43  ? 8.962   -7.704  -38.583 1.00 99.26  ? 85   GLY B O     1 
ATOM   232  N  N     . PHE A 1 44  ? 8.174   -7.176  -40.639 1.00 98.54  ? 86   PHE B N     1 
ATOM   233  C  CA    . PHE A 1 44  ? 6.937   -6.586  -40.148 1.00 90.05  ? 86   PHE B CA    1 
ATOM   234  C  C     . PHE A 1 44  ? 5.949   -7.667  -39.731 1.00 90.08  ? 86   PHE B C     1 
ATOM   235  O  O     . PHE A 1 44  ? 5.769   -8.668  -40.429 1.00 98.31  ? 86   PHE B O     1 
ATOM   236  C  CB    . PHE A 1 44  ? 6.304   -5.698  -41.220 1.00 92.87  ? 86   PHE B CB    1 
ATOM   237  C  CG    . PHE A 1 44  ? 6.973   -4.365  -41.380 1.00 86.76  ? 86   PHE B CG    1 
ATOM   238  C  CD1   . PHE A 1 44  ? 8.080   -4.222  -42.200 1.00 83.07  ? 86   PHE B CD1   1 
ATOM   239  C  CD2   . PHE A 1 44  ? 6.489   -3.251  -40.715 1.00 68.16  ? 86   PHE B CD2   1 
ATOM   240  C  CE1   . PHE A 1 44  ? 8.695   -2.994  -42.349 1.00 87.06  ? 86   PHE B CE1   1 
ATOM   241  C  CE2   . PHE A 1 44  ? 7.100   -2.021  -40.859 1.00 82.41  ? 86   PHE B CE2   1 
ATOM   242  C  CZ    . PHE A 1 44  ? 8.204   -1.892  -41.678 1.00 78.94  ? 86   PHE B CZ    1 
ATOM   243  N  N     . THR A 1 45  ? 5.314   -7.458  -38.581 1.00 74.92  ? 87   THR B N     1 
ATOM   244  C  CA    . THR A 1 45  ? 4.231   -8.306  -38.109 1.00 74.85  ? 87   THR B CA    1 
ATOM   245  C  C     . THR A 1 45  ? 3.099   -7.421  -37.609 1.00 75.03  ? 87   THR B C     1 
ATOM   246  O  O     . THR A 1 45  ? 3.284   -6.229  -37.351 1.00 82.92  ? 87   THR B O     1 
ATOM   247  C  CB    . THR A 1 45  ? 4.686   -9.255  -36.988 1.00 88.78  ? 87   THR B CB    1 
ATOM   248  O  OG1   . THR A 1 45  ? 5.230   -8.494  -35.902 1.00 86.43  ? 87   THR B OG1   1 
ATOM   249  C  CG2   . THR A 1 45  ? 5.735   -10.234 -37.498 1.00 86.01  ? 87   THR B CG2   1 
ATOM   250  N  N     . THR A 1 46  ? 1.917   -8.014  -37.476 1.00 80.71  ? 88   THR B N     1 
ATOM   251  C  CA    . THR A 1 46  ? 0.791   -7.267  -36.942 1.00 85.22  ? 88   THR B CA    1 
ATOM   252  C  C     . THR A 1 46  ? 0.949   -7.070  -35.437 1.00 83.35  ? 88   THR B C     1 
ATOM   253  O  O     . THR A 1 46  ? 1.635   -7.832  -34.748 1.00 83.48  ? 88   THR B O     1 
ATOM   254  C  CB    . THR A 1 46  ? -0.529  -7.977  -37.248 1.00 92.55  ? 88   THR B CB    1 
ATOM   255  O  OG1   . THR A 1 46  ? -1.606  -7.281  -36.609 1.00 103.87 ? 88   THR B OG1   1 
ATOM   256  C  CG2   . THR A 1 46  ? -0.496  -9.408  -36.753 1.00 80.80  ? 88   THR B CG2   1 
ATOM   257  N  N     . ALA A 1 47  ? 0.302   -6.018  -34.928 1.00 81.34  ? 89   ALA B N     1 
ATOM   258  C  CA    . ALA A 1 47  ? 0.387   -5.713  -33.505 1.00 80.93  ? 89   ALA B CA    1 
ATOM   259  C  C     . ALA A 1 47  ? -0.207  -6.816  -32.642 1.00 82.94  ? 89   ALA B C     1 
ATOM   260  O  O     . ALA A 1 47  ? 0.178   -6.948  -31.476 1.00 90.26  ? 89   ALA B O     1 
ATOM   261  C  CB    . ALA A 1 47  ? -0.308  -4.385  -33.205 1.00 72.39  ? 89   ALA B CB    1 
ATOM   262  N  N     . THR A 1 48  ? -1.129  -7.614  -33.185 1.00 97.22  ? 90   THR B N     1 
ATOM   263  C  CA    . THR A 1 48  ? -1.681  -8.730  -32.424 1.00 88.08  ? 90   THR B CA    1 
ATOM   264  C  C     . THR A 1 48  ? -0.628  -9.806  -32.182 1.00 77.34  ? 90   THR B C     1 
ATOM   265  O  O     . THR A 1 48  ? -0.530  -10.349 -31.075 1.00 105.15 ? 90   THR B O     1 
ATOM   266  C  CB    . THR A 1 48  ? -2.892  -9.314  -33.152 1.00 90.76  ? 90   THR B CB    1 
ATOM   267  O  OG1   . THR A 1 48  ? -3.874  -8.289  -33.349 1.00 81.45  ? 90   THR B OG1   1 
ATOM   268  C  CG2   . THR A 1 48  ? -3.507  -10.446 -32.343 1.00 86.20  ? 90   THR B CG2   1 
ATOM   269  N  N     . GLU A 1 49  ? 0.171   -10.123 -33.205 1.00 68.64  ? 91   GLU B N     1 
ATOM   270  C  CA    . GLU A 1 49  ? 1.235   -11.107 -33.032 1.00 86.56  ? 91   GLU B CA    1 
ATOM   271  C  C     . GLU A 1 49  ? 2.261   -10.635 -32.010 1.00 95.49  ? 91   GLU B C     1 
ATOM   272  O  O     . GLU A 1 49  ? 2.724   -11.422 -31.177 1.00 98.53  ? 91   GLU B O     1 
ATOM   273  C  CB    . GLU A 1 49  ? 1.908   -11.397 -34.374 1.00 87.73  ? 91   GLU B CB    1 
ATOM   274  C  CG    . GLU A 1 49  ? 1.068   -12.238 -35.321 1.00 98.81  ? 91   GLU B CG    1 
ATOM   275  C  CD    . GLU A 1 49  ? 1.674   -12.334 -36.708 1.00 117.69 ? 91   GLU B CD    1 
ATOM   276  O  OE1   . GLU A 1 49  ? 2.886   -12.067 -36.850 1.00 128.99 ? 91   GLU B OE1   1 
ATOM   277  O  OE2   . GLU A 1 49  ? 0.936   -12.672 -37.658 1.00 115.38 ? 91   GLU B OE2   1 
ATOM   278  N  N     . PHE A 1 50  ? 2.619   -9.349  -32.045 1.00 86.55  ? 92   PHE B N     1 
ATOM   279  C  CA    . PHE A 1 50  ? 3.579   -8.836  -31.074 1.00 81.04  ? 92   PHE B CA    1 
ATOM   280  C  C     . PHE A 1 50  ? 2.987   -8.783  -29.671 1.00 88.22  ? 92   PHE B C     1 
ATOM   281  O  O     . PHE A 1 50  ? 3.702   -9.017  -28.690 1.00 88.19  ? 92   PHE B O     1 
ATOM   282  C  CB    . PHE A 1 50  ? 4.075   -7.454  -31.497 1.00 65.54  ? 92   PHE B CB    1 
ATOM   283  C  CG    . PHE A 1 50  ? 5.114   -6.879  -30.579 1.00 76.56  ? 92   PHE B CG    1 
ATOM   284  C  CD1   . PHE A 1 50  ? 6.375   -7.446  -30.497 1.00 75.25  ? 92   PHE B CD1   1 
ATOM   285  C  CD2   . PHE A 1 50  ? 4.832   -5.771  -29.797 1.00 77.57  ? 92   PHE B CD2   1 
ATOM   286  C  CE1   . PHE A 1 50  ? 7.335   -6.920  -29.652 1.00 77.59  ? 92   PHE B CE1   1 
ATOM   287  C  CE2   . PHE A 1 50  ? 5.788   -5.239  -28.951 1.00 76.38  ? 92   PHE B CE2   1 
ATOM   288  C  CZ    . PHE A 1 50  ? 7.041   -5.814  -28.879 1.00 79.72  ? 92   PHE B CZ    1 
ATOM   289  N  N     . HIS A 1 51  ? 1.691   -8.482  -29.553 1.00 85.59  ? 93   HIS B N     1 
ATOM   290  C  CA    . HIS A 1 51  ? 1.046   -8.501  -28.245 1.00 77.65  ? 93   HIS B CA    1 
ATOM   291  C  C     . HIS A 1 51  ? 0.999   -9.915  -27.681 1.00 88.92  ? 93   HIS B C     1 
ATOM   292  O  O     . HIS A 1 51  ? 1.142   -10.113 -26.468 1.00 90.35  ? 93   HIS B O     1 
ATOM   293  C  CB    . HIS A 1 51  ? -0.360  -7.913  -28.345 1.00 68.02  ? 93   HIS B CB    1 
ATOM   294  C  CG    . HIS A 1 51  ? -1.037  -7.735  -27.021 1.00 91.53  ? 93   HIS B CG    1 
ATOM   295  N  ND1   . HIS A 1 51  ? -2.407  -7.675  -26.888 1.00 93.03  ? 93   HIS B ND1   1 
ATOM   296  C  CD2   . HIS A 1 51  ? -0.532  -7.598  -25.772 1.00 86.51  ? 93   HIS B CD2   1 
ATOM   297  C  CE1   . HIS A 1 51  ? -2.717  -7.512  -25.614 1.00 87.27  ? 93   HIS B CE1   1 
ATOM   298  N  NE2   . HIS A 1 51  ? -1.597  -7.462  -24.916 1.00 80.15  ? 93   HIS B NE2   1 
ATOM   299  N  N     . GLN A 1 52  ? 0.796   -10.912 -28.546 1.00 84.38  ? 94   GLN B N     1 
ATOM   300  C  CA    . GLN A 1 52  ? 0.862   -12.299 -28.099 1.00 89.24  ? 94   GLN B CA    1 
ATOM   301  C  C     . GLN A 1 52  ? 2.283   -12.677 -27.697 1.00 89.47  ? 94   GLN B C     1 
ATOM   302  O  O     . GLN A 1 52  ? 2.485   -13.396 -26.711 1.00 97.47  ? 94   GLN B O     1 
ATOM   303  C  CB    . GLN A 1 52  ? 0.346   -13.231 -29.195 1.00 101.38 ? 94   GLN B CB    1 
ATOM   304  C  CG    . GLN A 1 52  ? 0.482   -14.709 -28.866 1.00 109.30 ? 94   GLN B CG    1 
ATOM   305  C  CD    . GLN A 1 52  ? -0.013  -15.604 -29.985 1.00 121.83 ? 94   GLN B CD    1 
ATOM   306  O  OE1   . GLN A 1 52  ? -0.779  -15.174 -30.847 1.00 121.57 ? 94   GLN B OE1   1 
ATOM   307  N  NE2   . GLN A 1 52  ? 0.428   -16.857 -29.979 1.00 126.31 ? 94   GLN B NE2   1 
ATOM   308  N  N     . ARG A 1 53  ? 3.279   -12.199 -28.448 1.00 84.46  ? 95   ARG B N     1 
ATOM   309  C  CA    . ARG A 1 53  ? 4.671   -12.466 -28.099 1.00 94.76  ? 95   ARG B CA    1 
ATOM   310  C  C     . ARG A 1 53  ? 5.049   -11.835 -26.765 1.00 91.23  ? 95   ARG B C     1 
ATOM   311  O  O     . ARG A 1 53  ? 5.871   -12.389 -26.028 1.00 75.74  ? 95   ARG B O     1 
ATOM   312  C  CB    . ARG A 1 53  ? 5.599   -11.960 -29.203 1.00 81.84  ? 95   ARG B CB    1 
ATOM   313  C  CG    . ARG A 1 53  ? 5.561   -12.784 -30.480 1.00 105.88 ? 95   ARG B CG    1 
ATOM   314  C  CD    . ARG A 1 53  ? 6.098   -14.185 -30.245 1.00 115.65 ? 95   ARG B CD    1 
ATOM   315  N  NE    . ARG A 1 53  ? 6.109   -14.976 -31.469 1.00 118.95 ? 95   ARG B NE    1 
ATOM   316  C  CZ    . ARG A 1 53  ? 6.592   -16.208 -31.560 1.00 129.72 ? 95   ARG B CZ    1 
ATOM   317  N  NH1   . ARG A 1 53  ? 7.118   -16.823 -30.513 1.00 112.43 ? 95   ARG B NH1   1 
ATOM   318  N  NH2   . ARG A 1 53  ? 6.548   -16.837 -32.731 1.00 124.06 ? 95   ARG B NH2   1 
ATOM   319  N  N     . ARG A 1 54  ? 4.469   -10.677 -26.438 1.00 90.22  ? 96   ARG B N     1 
ATOM   320  C  CA    . ARG A 1 54  ? 4.751   -10.057 -25.147 1.00 88.40  ? 96   ARG B CA    1 
ATOM   321  C  C     . ARG A 1 54  ? 4.047   -10.782 -24.009 1.00 97.19  ? 96   ARG B C     1 
ATOM   322  O  O     . ARG A 1 54  ? 4.533   -10.765 -22.872 1.00 101.91 ? 96   ARG B O     1 
ATOM   323  C  CB    . ARG A 1 54  ? 4.355   -8.581  -25.164 1.00 83.12  ? 96   ARG B CB    1 
ATOM   324  C  CG    . ARG A 1 54  ? 5.337   -7.692  -25.907 1.00 77.69  ? 96   ARG B CG    1 
ATOM   325  C  CD    . ARG A 1 54  ? 5.095   -6.224  -25.594 1.00 81.69  ? 96   ARG B CD    1 
ATOM   326  N  NE    . ARG A 1 54  ? 5.197   -5.949  -24.166 1.00 83.49  ? 96   ARG B NE    1 
ATOM   327  C  CZ    . ARG A 1 54  ? 6.334   -5.698  -23.530 1.00 87.78  ? 96   ARG B CZ    1 
ATOM   328  N  NH1   . ARG A 1 54  ? 7.494   -5.688  -24.166 1.00 87.39  ? 96   ARG B NH1   1 
ATOM   329  N  NH2   . ARG A 1 54  ? 6.305   -5.452  -22.224 1.00 98.92  ? 96   ARG B NH2   1 
ATOM   330  N  N     . SER A 1 55  ? 2.908   -11.421 -24.287 1.00 85.39  ? 97   SER B N     1 
ATOM   331  C  CA    . SER A 1 55  ? 2.246   -12.229 -23.270 1.00 91.34  ? 97   SER B CA    1 
ATOM   332  C  C     . SER A 1 55  ? 3.029   -13.495 -22.948 1.00 74.97  ? 97   SER B C     1 
ATOM   333  O  O     . SER A 1 55  ? 2.816   -14.088 -21.886 1.00 94.40  ? 97   SER B O     1 
ATOM   334  C  CB    . SER A 1 55  ? 0.831   -12.592 -23.720 1.00 85.06  ? 97   SER B CB    1 
ATOM   335  O  OG    . SER A 1 55  ? 0.852   -13.359 -24.912 1.00 109.56 ? 97   SER B OG    1 
ATOM   336  N  N     . GLU A 1 56  ? 3.923   -13.918 -23.838 1.00 89.19  ? 98   GLU B N     1 
ATOM   337  C  CA    . GLU A 1 56  ? 4.780   -15.074 -23.613 1.00 92.90  ? 98   GLU B CA    1 
ATOM   338  C  C     . GLU A 1 56  ? 6.058   -14.724 -22.863 1.00 89.35  ? 98   GLU B C     1 
ATOM   339  O  O     . GLU A 1 56  ? 6.859   -15.621 -22.581 1.00 100.71 ? 98   GLU B O     1 
ATOM   340  C  CB    . GLU A 1 56  ? 5.139   -15.731 -24.951 1.00 106.37 ? 98   GLU B CB    1 
ATOM   341  C  CG    . GLU A 1 56  ? 3.939   -16.135 -25.789 1.00 105.89 ? 98   GLU B CG    1 
ATOM   342  C  CD    . GLU A 1 56  ? 4.323   -16.533 -27.201 1.00 121.68 ? 98   GLU B CD    1 
ATOM   343  O  OE1   . GLU A 1 56  ? 5.530   -16.498 -27.523 1.00 127.06 ? 98   GLU B OE1   1 
ATOM   344  O  OE2   . GLU A 1 56  ? 3.418   -16.877 -27.990 1.00 126.67 ? 98   GLU B OE2   1 
ATOM   345  N  N     . ILE A 1 57  ? 6.270   -13.449 -22.541 1.00 81.89  ? 99   ILE B N     1 
ATOM   346  C  CA    . ILE A 1 57  ? 7.486   -13.034 -21.851 1.00 93.35  ? 99   ILE B CA    1 
ATOM   347  C  C     . ILE A 1 57  ? 7.465   -13.587 -20.433 1.00 87.49  ? 99   ILE B C     1 
ATOM   348  O  O     . ILE A 1 57  ? 6.539   -13.320 -19.659 1.00 76.43  ? 99   ILE B O     1 
ATOM   349  C  CB    . ILE A 1 57  ? 7.624   -11.506 -21.850 1.00 92.36  ? 99   ILE B CB    1 
ATOM   350  C  CG1   . ILE A 1 57  ? 7.804   -10.985 -23.277 1.00 83.89  ? 99   ILE B CG1   1 
ATOM   351  C  CG2   . ILE A 1 57  ? 8.792   -11.078 -20.972 1.00 86.50  ? 99   ILE B CG2   1 
ATOM   352  C  CD1   . ILE A 1 57  ? 7.971   -9.483  -23.363 1.00 73.31  ? 99   ILE B CD1   1 
ATOM   353  N  N     . ILE A 1 58  ? 8.489   -14.366 -20.089 1.00 88.57  ? 100  ILE B N     1 
ATOM   354  C  CA    . ILE A 1 58  ? 8.593   -14.930 -18.749 1.00 90.91  ? 100  ILE B CA    1 
ATOM   355  C  C     . ILE A 1 58  ? 8.929   -13.812 -17.770 1.00 89.81  ? 100  ILE B C     1 
ATOM   356  O  O     . ILE A 1 58  ? 9.908   -13.080 -17.953 1.00 84.16  ? 100  ILE B O     1 
ATOM   357  C  CB    . ILE A 1 58  ? 9.646   -16.045 -18.705 1.00 87.91  ? 100  ILE B CB    1 
ATOM   358  C  CG1   . ILE A 1 58  ? 9.278   -17.161 -19.685 1.00 94.69  ? 100  ILE B CG1   1 
ATOM   359  C  CG2   . ILE A 1 58  ? 9.784   -16.594 -17.293 1.00 88.07  ? 100  ILE B CG2   1 
ATOM   360  C  CD1   . ILE A 1 58  ? 10.298  -18.276 -19.754 1.00 92.88  ? 100  ILE B CD1   1 
ATOM   361  N  N     . GLN A 1 59  ? 8.111   -13.670 -16.731 1.00 89.93  ? 101  GLN B N     1 
ATOM   362  C  CA    . GLN A 1 59  ? 8.319   -12.668 -15.694 1.00 88.06  ? 101  GLN B CA    1 
ATOM   363  C  C     . GLN A 1 59  ? 8.595   -13.372 -14.374 1.00 80.79  ? 101  GLN B C     1 
ATOM   364  O  O     . GLN A 1 59  ? 7.843   -14.267 -13.973 1.00 83.57  ? 101  GLN B O     1 
ATOM   365  C  CB    . GLN A 1 59  ? 7.109   -11.738 -15.573 1.00 87.98  ? 101  GLN B CB    1 
ATOM   366  C  CG    . GLN A 1 59  ? 6.961   -10.783 -16.748 1.00 90.11  ? 101  GLN B CG    1 
ATOM   367  C  CD    . GLN A 1 59  ? 5.740   -9.895  -16.632 1.00 100.67 ? 101  GLN B CD    1 
ATOM   368  O  OE1   . GLN A 1 59  ? 4.727   -10.287 -16.056 1.00 92.08  ? 101  GLN B OE1   1 
ATOM   369  N  NE2   . GLN A 1 59  ? 5.831   -8.688  -17.180 1.00 99.00  ? 101  GLN B NE2   1 
ATOM   370  N  N     . ILE A 1 60  ? 9.671   -12.967 -13.708 1.00 85.84  ? 102  ILE B N     1 
ATOM   371  C  CA    . ILE A 1 60  ? 10.141  -13.628 -12.497 1.00 90.79  ? 102  ILE B CA    1 
ATOM   372  C  C     . ILE A 1 60  ? 9.480   -12.984 -11.286 1.00 93.30  ? 102  ILE B C     1 
ATOM   373  O  O     . ILE A 1 60  ? 9.465   -11.754 -11.153 1.00 72.48  ? 102  ILE B O     1 
ATOM   374  C  CB    . ILE A 1 60  ? 11.673  -13.553 -12.394 1.00 93.02  ? 102  ILE B CB    1 
ATOM   375  C  CG1   . ILE A 1 60  ? 12.317  -14.164 -13.642 1.00 94.12  ? 102  ILE B CG1   1 
ATOM   376  C  CG2   . ILE A 1 60  ? 12.160  -14.255 -11.137 1.00 81.07  ? 102  ILE B CG2   1 
ATOM   377  C  CD1   . ILE A 1 60  ? 13.823  -14.039 -13.678 1.00 94.46  ? 102  ILE B CD1   1 
ATOM   378  N  N     . THR A 1 61  ? 8.936   -13.815 -10.399 1.00 92.95  ? 103  THR B N     1 
ATOM   379  C  CA    . THR A 1 61  ? 8.295   -13.311 -9.196  1.00 89.95  ? 103  THR B CA    1 
ATOM   380  C  C     . THR A 1 61  ? 9.333   -12.738 -8.234  1.00 93.69  ? 103  THR B C     1 
ATOM   381  O  O     . THR A 1 61  ? 10.522  -13.063 -8.288  1.00 85.85  ? 103  THR B O     1 
ATOM   382  C  CB    . THR A 1 61  ? 7.496   -14.417 -8.502  1.00 90.07  ? 103  THR B CB    1 
ATOM   383  O  OG1   . THR A 1 61  ? 6.792   -13.868 -7.381  1.00 100.48 ? 103  THR B OG1   1 
ATOM   384  C  CG2   . THR A 1 61  ? 8.423   -15.522 -8.015  1.00 85.99  ? 103  THR B CG2   1 
ATOM   385  N  N     . THR A 1 62  ? 8.862   -11.868 -7.342  1.00 93.04  ? 104  THR B N     1 
ATOM   386  C  CA    . THR A 1 62  ? 9.717   -11.215 -6.361  1.00 96.80  ? 104  THR B CA    1 
ATOM   387  C  C     . THR A 1 62  ? 9.466   -11.696 -4.939  1.00 101.13 ? 104  THR B C     1 
ATOM   388  O  O     . THR A 1 62  ? 10.164  -11.256 -4.019  1.00 89.62  ? 104  THR B O     1 
ATOM   389  C  CB    . THR A 1 62  ? 9.528   -9.694  -6.423  1.00 92.71  ? 104  THR B CB    1 
ATOM   390  O  OG1   . THR A 1 62  ? 8.202   -9.359  -5.995  1.00 94.21  ? 104  THR B OG1   1 
ATOM   391  C  CG2   . THR A 1 62  ? 9.736   -9.190  -7.843  1.00 77.75  ? 104  THR B CG2   1 
ATOM   392  N  N     . GLY A 1 63  ? 8.496   -12.586 -4.734  1.00 97.44  ? 105  GLY B N     1 
ATOM   393  C  CA    . GLY A 1 63  ? 8.126   -13.035 -3.414  1.00 105.61 ? 105  GLY B CA    1 
ATOM   394  C  C     . GLY A 1 63  ? 7.047   -12.212 -2.743  1.00 100.22 ? 105  GLY B C     1 
ATOM   395  O  O     . GLY A 1 63  ? 6.426   -12.691 -1.788  1.00 96.59  ? 105  GLY B O     1 
ATOM   396  N  N     . SER A 1 64  ? 6.807   -10.993 -3.215  1.00 95.90  ? 106  SER B N     1 
ATOM   397  C  CA    . SER A 1 64  ? 5.777   -10.122 -2.667  1.00 93.90  ? 106  SER B CA    1 
ATOM   398  C  C     . SER A 1 64  ? 4.582   -10.092 -3.608  1.00 97.57  ? 106  SER B C     1 
ATOM   399  O  O     . SER A 1 64  ? 4.739   -9.864  -4.812  1.00 107.44 ? 106  SER B O     1 
ATOM   400  C  CB    . SER A 1 64  ? 6.316   -8.706  -2.454  1.00 91.60  ? 106  SER B CB    1 
ATOM   401  O  OG    . SER A 1 64  ? 5.285   -7.827  -2.037  1.00 113.35 ? 106  SER B OG    1 
ATOM   402  N  N     . LYS A 1 65  ? 3.390   -10.327 -3.057  1.00 99.98  ? 107  LYS B N     1 
ATOM   403  C  CA    . LYS A 1 65  ? 2.178   -10.291 -3.869  1.00 108.02 ? 107  LYS B CA    1 
ATOM   404  C  C     . LYS A 1 65  ? 1.919   -8.889  -4.406  1.00 109.56 ? 107  LYS B C     1 
ATOM   405  O  O     . LYS A 1 65  ? 1.619   -8.712  -5.593  1.00 111.94 ? 107  LYS B O     1 
ATOM   406  C  CB    . LYS A 1 65  ? 0.984   -10.783 -3.051  1.00 101.76 ? 107  LYS B CB    1 
ATOM   407  C  CG    . LYS A 1 65  ? -0.358  -10.598 -3.741  1.00 101.63 ? 107  LYS B CG    1 
ATOM   408  C  CD    . LYS A 1 65  ? -1.511  -10.915 -2.804  1.00 115.17 ? 107  LYS B CD    1 
ATOM   409  C  CE    . LYS A 1 65  ? -2.850  -10.616 -3.458  1.00 127.17 ? 107  LYS B CE    1 
ATOM   410  N  NZ    . LYS A 1 65  ? -3.988  -10.846 -2.526  1.00 116.14 ? 107  LYS B NZ    1 
ATOM   411  N  N     . GLU A 1 66  ? 2.036   -7.876  -3.544  1.00 110.21 ? 108  GLU B N     1 
ATOM   412  C  CA    . GLU A 1 66  ? 1.745   -6.509  -3.963  1.00 113.51 ? 108  GLU B CA    1 
ATOM   413  C  C     . GLU A 1 66  ? 2.763   -6.011  -4.982  1.00 112.56 ? 108  GLU B C     1 
ATOM   414  O  O     . GLU A 1 66  ? 2.412   -5.260  -5.899  1.00 121.50 ? 108  GLU B O     1 
ATOM   415  C  CB    . GLU A 1 66  ? 1.699   -5.588  -2.745  1.00 115.64 ? 108  GLU B CB    1 
ATOM   416  C  CG    . GLU A 1 66  ? 0.653   -5.987  -1.715  1.00 124.31 ? 108  GLU B CG    1 
ATOM   417  C  CD    . GLU A 1 66  ? 0.617   -5.051  -0.524  1.00 145.68 ? 108  GLU B CD    1 
ATOM   418  O  OE1   . GLU A 1 66  ? 1.298   -4.005  -0.566  1.00 145.45 ? 108  GLU B OE1   1 
ATOM   419  O  OE2   . GLU A 1 66  ? -0.092  -5.363  0.456   1.00 151.18 ? 108  GLU B OE2   1 
ATOM   420  N  N     . LEU A 1 67  ? 4.027   -6.420  -4.845  1.00 110.96 ? 109  LEU B N     1 
ATOM   421  C  CA    . LEU A 1 67  ? 5.032   -6.025  -5.827  1.00 108.69 ? 109  LEU B CA    1 
ATOM   422  C  C     . LEU A 1 67  ? 4.772   -6.677  -7.179  1.00 100.29 ? 109  LEU B C     1 
ATOM   423  O  O     . LEU A 1 67  ? 4.934   -6.036  -8.225  1.00 97.10  ? 109  LEU B O     1 
ATOM   424  C  CB    . LEU A 1 67  ? 6.433   -6.374  -5.324  1.00 95.26  ? 109  LEU B CB    1 
ATOM   425  C  CG    . LEU A 1 67  ? 7.022   -5.443  -4.264  1.00 105.72 ? 109  LEU B CG    1 
ATOM   426  C  CD1   . LEU A 1 67  ? 8.446   -5.854  -3.920  1.00 101.34 ? 109  LEU B CD1   1 
ATOM   427  C  CD2   . LEU A 1 67  ? 6.978   -4.000  -4.742  1.00 95.08  ? 109  LEU B CD2   1 
ATOM   428  N  N     . ASP A 1 68  ? 4.367   -7.949  -7.181  1.00 105.77 ? 110  ASP B N     1 
ATOM   429  C  CA    . ASP A 1 68  ? 4.050   -8.616  -8.439  1.00 94.03  ? 110  ASP B CA    1 
ATOM   430  C  C     . ASP A 1 68  ? 2.798   -8.036  -9.082  1.00 94.33  ? 110  ASP B C     1 
ATOM   431  O  O     . ASP A 1 68  ? 2.703   -7.987  -10.314 1.00 110.01 ? 110  ASP B O     1 
ATOM   432  C  CB    . ASP A 1 68  ? 3.886   -10.120 -8.214  1.00 98.01  ? 110  ASP B CB    1 
ATOM   433  C  CG    . ASP A 1 68  ? 5.178   -10.789 -7.787  1.00 100.84 ? 110  ASP B CG    1 
ATOM   434  O  OD1   . ASP A 1 68  ? 6.260   -10.277 -8.144  1.00 100.61 ? 110  ASP B OD1   1 
ATOM   435  O  OD2   . ASP A 1 68  ? 5.112   -11.828 -7.097  1.00 111.66 ? 110  ASP B OD2   1 
ATOM   436  N  N     . LYS A 1 69  ? 1.829   -7.595  -8.275  1.00 95.57  ? 111  LYS B N     1 
ATOM   437  C  CA    . LYS A 1 69  ? 0.649   -6.949  -8.839  1.00 110.53 ? 111  LYS B CA    1 
ATOM   438  C  C     . LYS A 1 69  ? 0.967   -5.549  -9.349  1.00 104.55 ? 111  LYS B C     1 
ATOM   439  O  O     . LYS A 1 69  ? 0.336   -5.081  -10.304 1.00 115.11 ? 111  LYS B O     1 
ATOM   440  C  CB    . LYS A 1 69  ? -0.475  -6.896  -7.804  1.00 118.98 ? 111  LYS B CB    1 
ATOM   441  C  CG    . LYS A 1 69  ? -0.951  -8.260  -7.334  1.00 123.20 ? 111  LYS B CG    1 
ATOM   442  C  CD    . LYS A 1 69  ? -1.330  -9.152  -8.504  1.00 130.93 ? 111  LYS B CD    1 
ATOM   443  C  CE    . LYS A 1 69  ? -1.696  -10.550 -8.032  1.00 133.87 ? 111  LYS B CE    1 
ATOM   444  N  NZ    . LYS A 1 69  ? -0.572  -11.202 -7.304  1.00 125.23 ? 111  LYS B NZ    1 
ATOM   445  N  N     . LEU A 1 70  ? 1.934   -4.868  -8.729  1.00 95.58  ? 112  LEU B N     1 
ATOM   446  C  CA    . LEU A 1 70  ? 2.348   -3.559  -9.223  1.00 97.55  ? 112  LEU B CA    1 
ATOM   447  C  C     . LEU A 1 70  ? 3.038   -3.677  -10.575 1.00 98.70  ? 112  LEU B C     1 
ATOM   448  O  O     . LEU A 1 70  ? 2.816   -2.850  -11.468 1.00 105.98 ? 112  LEU B O     1 
ATOM   449  C  CB    . LEU A 1 70  ? 3.272   -2.882  -8.210  1.00 88.83  ? 112  LEU B CB    1 
ATOM   450  C  CG    . LEU A 1 70  ? 3.821   -1.513  -8.618  1.00 88.35  ? 112  LEU B CG    1 
ATOM   451  C  CD1   . LEU A 1 70  ? 2.719   -0.465  -8.593  1.00 95.72  ? 112  LEU B CD1   1 
ATOM   452  C  CD2   . LEU A 1 70  ? 4.986   -1.099  -7.731  1.00 78.55  ? 112  LEU B CD2   1 
ATOM   453  N  N     . LEU A 1 71  ? 3.876   -4.696  -10.744 1.00 93.61  ? 113  LEU B N     1 
ATOM   454  C  CA    . LEU A 1 71  ? 4.582   -4.933  -11.995 1.00 86.28  ? 113  LEU B CA    1 
ATOM   455  C  C     . LEU A 1 71  ? 3.821   -5.858  -12.936 1.00 101.52 ? 113  LEU B C     1 
ATOM   456  O  O     . LEU A 1 71  ? 4.339   -6.187  -14.009 1.00 112.79 ? 113  LEU B O     1 
ATOM   457  C  CB    . LEU A 1 71  ? 5.975   -5.512  -11.715 1.00 82.27  ? 113  LEU B CB    1 
ATOM   458  C  CG    . LEU A 1 71  ? 7.125   -4.536  -11.435 1.00 86.73  ? 113  LEU B CG    1 
ATOM   459  C  CD1   . LEU A 1 71  ? 6.852   -3.654  -10.224 1.00 94.02  ? 113  LEU B CD1   1 
ATOM   460  C  CD2   . LEU A 1 71  ? 8.432   -5.295  -11.257 1.00 93.49  ? 113  LEU B CD2   1 
ATOM   461  N  N     . GLN A 1 72  ? 2.612   -6.282  -12.557 1.00 99.74  ? 114  GLN B N     1 
ATOM   462  C  CA    . GLN A 1 72  ? 1.760   -7.134  -13.390 1.00 107.27 ? 114  GLN B CA    1 
ATOM   463  C  C     . GLN A 1 72  ? 2.474   -8.430  -13.773 1.00 94.31  ? 114  GLN B C     1 
ATOM   464  O  O     . GLN A 1 72  ? 2.472   -8.851  -14.932 1.00 111.38 ? 114  GLN B O     1 
ATOM   465  C  CB    . GLN A 1 72  ? 1.277   -6.381  -14.632 1.00 102.89 ? 114  GLN B CB    1 
ATOM   466  C  CG    . GLN A 1 72  ? 0.444   -5.148  -14.320 1.00 110.62 ? 114  GLN B CG    1 
ATOM   467  C  CD    . GLN A 1 72  ? -0.076  -4.462  -15.568 1.00 118.23 ? 114  GLN B CD    1 
ATOM   468  O  OE1   . GLN A 1 72  ? 0.132   -4.937  -16.684 1.00 147.89 ? 114  GLN B OE1   1 
ATOM   469  N  NE2   . GLN A 1 72  ? -0.756  -3.336  -15.384 1.00 89.31  ? 114  GLN B NE2   1 
ATOM   470  N  N     . GLY A 1 73  ? 3.091   -9.066  -12.780 1.00 80.20  ? 115  GLY B N     1 
ATOM   471  C  CA    . GLY A 1 73  ? 3.775   -10.324 -13.005 1.00 91.89  ? 115  GLY B CA    1 
ATOM   472  C  C     . GLY A 1 73  ? 5.119   -10.419 -12.313 1.00 103.46 ? 115  GLY B C     1 
ATOM   473  O  O     . GLY A 1 73  ? 5.436   -11.441 -11.697 1.00 96.32  ? 115  GLY B O     1 
ATOM   474  N  N     . GLY A 1 74  ? 5.921   -9.362  -12.410 1.00 107.11 ? 116  GLY B N     1 
ATOM   475  C  CA    . GLY A 1 74  ? 7.228   -9.352  -11.783 1.00 87.51  ? 116  GLY B CA    1 
ATOM   476  C  C     . GLY A 1 74  ? 8.319   -8.790  -12.670 1.00 92.53  ? 116  GLY B C     1 
ATOM   477  O  O     . GLY A 1 74  ? 8.049   -7.980  -13.561 1.00 89.07  ? 116  GLY B O     1 
ATOM   478  N  N     . ILE A 1 75  ? 9.559   -9.215  -12.434 1.00 92.29  ? 117  ILE B N     1 
ATOM   479  C  CA    . ILE A 1 75  ? 10.690  -8.720  -13.211 1.00 84.21  ? 117  ILE B CA    1 
ATOM   480  C  C     . ILE A 1 75  ? 10.593  -9.264  -14.630 1.00 79.26  ? 117  ILE B C     1 
ATOM   481  O  O     . ILE A 1 75  ? 10.613  -10.481 -14.849 1.00 69.95  ? 117  ILE B O     1 
ATOM   482  C  CB    . ILE A 1 75  ? 12.020  -9.110  -12.555 1.00 80.17  ? 117  ILE B CB    1 
ATOM   483  C  CG1   . ILE A 1 75  ? 12.099  -8.541  -11.136 1.00 78.14  ? 117  ILE B CG1   1 
ATOM   484  C  CG2   . ILE A 1 75  ? 13.189  -8.623  -13.396 1.00 78.06  ? 117  ILE B CG2   1 
ATOM   485  C  CD1   . ILE A 1 75  ? 11.964  -7.034  -11.073 1.00 79.06  ? 117  ILE B CD1   1 
ATOM   486  N  N     . GLU A 1 76  ? 10.489  -8.361  -15.601 1.00 91.89  ? 118  GLU B N     1 
ATOM   487  C  CA    . GLU A 1 76  ? 10.344  -8.752  -16.996 1.00 87.24  ? 118  GLU B CA    1 
ATOM   488  C  C     . GLU A 1 76  ? 11.693  -9.159  -17.577 1.00 85.27  ? 118  GLU B C     1 
ATOM   489  O  O     . GLU A 1 76  ? 12.696  -8.462  -17.392 1.00 79.36  ? 118  GLU B O     1 
ATOM   490  C  CB    . GLU A 1 76  ? 9.742   -7.603  -17.806 1.00 84.99  ? 118  GLU B CB    1 
ATOM   491  C  CG    . GLU A 1 76  ? 9.693   -7.853  -19.304 1.00 100.50 ? 118  GLU B CG    1 
ATOM   492  C  CD    . GLU A 1 76  ? 9.060   -6.704  -20.066 1.00 98.36  ? 118  GLU B CD    1 
ATOM   493  O  OE1   . GLU A 1 76  ? 8.249   -5.966  -19.467 1.00 99.41  ? 118  GLU B OE1   1 
ATOM   494  O  OE2   . GLU A 1 76  ? 9.376   -6.537  -21.263 1.00 107.54 ? 118  GLU B OE2   1 
ATOM   495  N  N     . THR A 1 77  ? 11.715  -10.291 -18.275 1.00 82.38  ? 119  THR B N     1 
ATOM   496  C  CA    . THR A 1 77  ? 12.924  -10.750 -18.942 1.00 87.62  ? 119  THR B CA    1 
ATOM   497  C  C     . THR A 1 77  ? 13.082  -10.065 -20.295 1.00 94.27  ? 119  THR B C     1 
ATOM   498  O  O     . THR A 1 77  ? 12.102  -9.709  -20.955 1.00 83.25  ? 119  THR B O     1 
ATOM   499  C  CB    . THR A 1 77  ? 12.899  -12.267 -19.133 1.00 81.35  ? 119  THR B CB    1 
ATOM   500  O  OG1   . THR A 1 77  ? 11.642  -12.661 -19.697 1.00 87.11  ? 119  THR B OG1   1 
ATOM   501  C  CG2   . THR A 1 77  ? 13.105  -12.982 -17.806 1.00 70.71  ? 119  THR B CG2   1 
ATOM   502  N  N     . GLY A 1 78  ? 14.337  -9.886  -20.704 1.00 88.84  ? 120  GLY B N     1 
ATOM   503  C  CA    . GLY A 1 78  ? 14.657  -9.251  -21.961 1.00 82.36  ? 120  GLY B CA    1 
ATOM   504  C  C     . GLY A 1 78  ? 14.943  -7.767  -21.875 1.00 96.68  ? 120  GLY B C     1 
ATOM   505  O  O     . GLY A 1 78  ? 15.524  -7.209  -22.813 1.00 110.27 ? 120  GLY B O     1 
ATOM   506  N  N     . SER A 1 79  ? 14.555  -7.114  -20.787 1.00 96.87  ? 121  SER B N     1 
ATOM   507  C  CA    . SER A 1 79  ? 14.785  -5.691  -20.585 1.00 93.34  ? 121  SER B CA    1 
ATOM   508  C  C     . SER A 1 79  ? 15.613  -5.483  -19.320 1.00 84.50  ? 121  SER B C     1 
ATOM   509  O  O     . SER A 1 79  ? 15.932  -6.428  -18.594 1.00 88.82  ? 121  SER B O     1 
ATOM   510  C  CB    . SER A 1 79  ? 13.459  -4.930  -20.504 1.00 91.67  ? 121  SER B CB    1 
ATOM   511  O  OG    . SER A 1 79  ? 12.686  -5.370  -19.402 1.00 108.17 ? 121  SER B OG    1 
ATOM   512  N  N     . ILE A 1 80  ? 15.960  -4.226  -19.060 1.00 86.16  ? 122  ILE B N     1 
ATOM   513  C  CA    . ILE A 1 80  ? 16.752  -3.851  -17.896 1.00 68.95  ? 122  ILE B CA    1 
ATOM   514  C  C     . ILE A 1 80  ? 15.827  -3.268  -16.838 1.00 86.56  ? 122  ILE B C     1 
ATOM   515  O  O     . ILE A 1 80  ? 15.013  -2.382  -17.131 1.00 95.58  ? 122  ILE B O     1 
ATOM   516  C  CB    . ILE A 1 80  ? 17.861  -2.852  -18.270 1.00 77.16  ? 122  ILE B CB    1 
ATOM   517  C  CG1   . ILE A 1 80  ? 18.954  -3.549  -19.083 1.00 82.61  ? 122  ILE B CG1   1 
ATOM   518  C  CG2   . ILE A 1 80  ? 18.450  -2.212  -17.023 1.00 77.89  ? 122  ILE B CG2   1 
ATOM   519  C  CD1   . ILE A 1 80  ? 20.174  -2.687  -19.321 1.00 74.04  ? 122  ILE B CD1   1 
ATOM   520  N  N     . THR A 1 81  ? 15.947  -3.769  -15.613 1.00 84.65  ? 123  THR B N     1 
ATOM   521  C  CA    . THR A 1 81  ? 15.229  -3.239  -14.462 1.00 74.19  ? 123  THR B CA    1 
ATOM   522  C  C     . THR A 1 81  ? 16.238  -2.560  -13.545 1.00 70.85  ? 123  THR B C     1 
ATOM   523  O  O     . THR A 1 81  ? 17.153  -3.213  -13.032 1.00 78.67  ? 123  THR B O     1 
ATOM   524  C  CB    . THR A 1 81  ? 14.479  -4.345  -13.719 1.00 81.20  ? 123  THR B CB    1 
ATOM   525  O  OG1   . THR A 1 81  ? 13.627  -5.044  -14.634 1.00 86.44  ? 123  THR B OG1   1 
ATOM   526  C  CG2   . THR A 1 81  ? 13.632  -3.754  -12.603 1.00 81.40  ? 123  THR B CG2   1 
ATOM   527  N  N     . GLU A 1 82  ? 16.074  -1.255  -13.349 1.00 70.34  ? 124  GLU B N     1 
ATOM   528  C  CA    . GLU A 1 82  ? 16.985  -0.451  -12.541 1.00 91.75  ? 124  GLU B CA    1 
ATOM   529  C  C     . GLU A 1 82  ? 16.291  -0.086  -11.235 1.00 87.33  ? 124  GLU B C     1 
ATOM   530  O  O     . GLU A 1 82  ? 15.378  0.745   -11.224 1.00 93.36  ? 124  GLU B O     1 
ATOM   531  C  CB    . GLU A 1 82  ? 17.419  0.805   -13.294 1.00 113.98 ? 124  GLU B CB    1 
ATOM   532  C  CG    . GLU A 1 82  ? 18.252  1.766   -12.459 1.00 110.26 ? 124  GLU B CG    1 
ATOM   533  C  CD    . GLU A 1 82  ? 18.485  3.095   -13.152 1.00 129.63 ? 124  GLU B CD    1 
ATOM   534  O  OE1   . GLU A 1 82  ? 17.971  3.281   -14.275 1.00 129.32 ? 124  GLU B OE1   1 
ATOM   535  O  OE2   . GLU A 1 82  ? 19.182  3.954   -12.572 1.00 124.07 ? 124  GLU B OE2   1 
ATOM   536  N  N     . MET A 1 83  ? 16.725  -0.703  -10.139 1.00 79.46  ? 125  MET B N     1 
ATOM   537  C  CA    . MET A 1 83  ? 16.212  -0.396  -8.810  1.00 91.06  ? 125  MET B CA    1 
ATOM   538  C  C     . MET A 1 83  ? 17.171  0.570   -8.128  1.00 77.71  ? 125  MET B C     1 
ATOM   539  O  O     . MET A 1 83  ? 18.350  0.249   -7.939  1.00 82.41  ? 125  MET B O     1 
ATOM   540  C  CB    . MET A 1 83  ? 16.049  -1.666  -7.976  1.00 68.11  ? 125  MET B CB    1 
ATOM   541  C  CG    . MET A 1 83  ? 15.206  -2.739  -8.635  1.00 87.12  ? 125  MET B CG    1 
ATOM   542  S  SD    . MET A 1 83  ? 15.015  -4.183  -7.577  1.00 95.74  ? 125  MET B SD    1 
ATOM   543  C  CE    . MET A 1 83  ? 16.728  -4.561  -7.213  1.00 90.85  ? 125  MET B CE    1 
ATOM   544  N  N     . PHE A 1 84  ? 16.670  1.747   -7.761  1.00 69.73  ? 126  PHE B N     1 
ATOM   545  C  CA    . PHE A 1 84  ? 17.497  2.772   -7.143  1.00 92.76  ? 126  PHE B CA    1 
ATOM   546  C  C     . PHE A 1 84  ? 16.820  3.314   -5.892  1.00 100.38 ? 126  PHE B C     1 
ATOM   547  O  O     . PHE A 1 84  ? 15.593  3.285   -5.763  1.00 90.25  ? 126  PHE B O     1 
ATOM   548  C  CB    . PHE A 1 84  ? 17.800  3.922   -8.120  1.00 93.60  ? 126  PHE B CB    1 
ATOM   549  C  CG    . PHE A 1 84  ? 16.577  4.535   -8.741  1.00 102.11 ? 126  PHE B CG    1 
ATOM   550  C  CD1   . PHE A 1 84  ? 16.055  4.029   -9.921  1.00 112.70 ? 126  PHE B CD1   1 
ATOM   551  C  CD2   . PHE A 1 84  ? 15.956  5.625   -8.153  1.00 103.26 ? 126  PHE B CD2   1 
ATOM   552  C  CE1   . PHE A 1 84  ? 14.932  4.593   -10.497 1.00 113.03 ? 126  PHE B CE1   1 
ATOM   553  C  CE2   . PHE A 1 84  ? 14.834  6.193   -8.725  1.00 104.08 ? 126  PHE B CE2   1 
ATOM   554  C  CZ    . PHE A 1 84  ? 14.322  5.676   -9.898  1.00 109.25 ? 126  PHE B CZ    1 
ATOM   555  N  N     . GLY A 1 85  ? 17.641  3.808   -4.974  1.00 100.83 ? 127  GLY B N     1 
ATOM   556  C  CA    . GLY A 1 85  ? 17.133  4.354   -3.732  1.00 87.83  ? 127  GLY B CA    1 
ATOM   557  C  C     . GLY A 1 85  ? 18.276  4.729   -2.816  1.00 94.40  ? 127  GLY B C     1 
ATOM   558  O  O     . GLY A 1 85  ? 19.446  4.691   -3.203  1.00 80.20  ? 127  GLY B O     1 
ATOM   559  N  N     . GLU A 1 86  ? 17.921  5.095   -1.587  1.00 114.57 ? 128  GLU B N     1 
ATOM   560  C  CA    . GLU A 1 86  ? 18.919  5.452   -0.592  1.00 97.01  ? 128  GLU B CA    1 
ATOM   561  C  C     . GLU A 1 86  ? 19.547  4.192   0.002   1.00 96.72  ? 128  GLU B C     1 
ATOM   562  O  O     . GLU A 1 86  ? 19.260  3.064   -0.409  1.00 105.29 ? 128  GLU B O     1 
ATOM   563  C  CB    . GLU A 1 86  ? 18.300  6.324   0.497   1.00 108.22 ? 128  GLU B CB    1 
ATOM   564  C  CG    . GLU A 1 86  ? 17.927  7.723   0.036   1.00 120.67 ? 128  GLU B CG    1 
ATOM   565  C  CD    . GLU A 1 86  ? 17.438  8.598   1.174   1.00 136.89 ? 128  GLU B CD    1 
ATOM   566  O  OE1   . GLU A 1 86  ? 17.258  8.074   2.293   1.00 144.40 ? 128  GLU B OE1   1 
ATOM   567  O  OE2   . GLU A 1 86  ? 17.237  9.810   0.949   1.00 135.33 ? 128  GLU B OE2   1 
ATOM   568  N  N     . PHE A 1 87  ? 20.421  4.388   0.984   1.00 98.16  ? 129  PHE B N     1 
ATOM   569  C  CA    . PHE A 1 87  ? 21.070  3.263   1.639   1.00 100.65 ? 129  PHE B CA    1 
ATOM   570  C  C     . PHE A 1 87  ? 20.081  2.538   2.543   1.00 102.83 ? 129  PHE B C     1 
ATOM   571  O  O     . PHE A 1 87  ? 19.230  3.161   3.185   1.00 96.19  ? 129  PHE B O     1 
ATOM   572  C  CB    . PHE A 1 87  ? 22.279  3.745   2.443   1.00 99.84  ? 129  PHE B CB    1 
ATOM   573  C  CG    . PHE A 1 87  ? 23.176  2.637   2.919   1.00 100.93 ? 129  PHE B CG    1 
ATOM   574  C  CD1   . PHE A 1 87  ? 23.742  1.751   2.017   1.00 98.65  ? 129  PHE B CD1   1 
ATOM   575  C  CD2   . PHE A 1 87  ? 23.469  2.495   4.265   1.00 100.15 ? 129  PHE B CD2   1 
ATOM   576  C  CE1   . PHE A 1 87  ? 24.572  0.733   2.451   1.00 102.15 ? 129  PHE B CE1   1 
ATOM   577  C  CE2   . PHE A 1 87  ? 24.298  1.479   4.705   1.00 88.97  ? 129  PHE B CE2   1 
ATOM   578  C  CZ    . PHE A 1 87  ? 24.850  0.598   3.797   1.00 100.78 ? 129  PHE B CZ    1 
ATOM   579  N  N     . ARG A 1 88  ? 20.191  1.208   2.575   1.00 100.04 ? 130  ARG B N     1 
ATOM   580  C  CA    . ARG A 1 88  ? 19.322  0.351   3.386   1.00 104.80 ? 130  ARG B CA    1 
ATOM   581  C  C     . ARG A 1 88  ? 17.857  0.498   2.977   1.00 96.86  ? 130  ARG B C     1 
ATOM   582  O  O     . ARG A 1 88  ? 16.974  0.735   3.805   1.00 98.61  ? 130  ARG B O     1 
ATOM   583  C  CB    . ARG A 1 88  ? 19.508  0.632   4.879   1.00 103.00 ? 130  ARG B CB    1 
ATOM   584  C  CG    . ARG A 1 88  ? 20.920  0.398   5.376   1.00 90.74  ? 130  ARG B CG    1 
ATOM   585  C  CD    . ARG A 1 88  ? 21.038  0.698   6.857   1.00 101.95 ? 130  ARG B CD    1 
ATOM   586  N  NE    . ARG A 1 88  ? 20.119  -0.113  7.646   1.00 98.75  ? 130  ARG B NE    1 
ATOM   587  C  CZ    . ARG A 1 88  ? 20.358  -1.362  8.019   1.00 93.12  ? 130  ARG B CZ    1 
ATOM   588  N  NH1   . ARG A 1 88  ? 21.476  -1.983  7.682   1.00 86.53  ? 130  ARG B NH1   1 
ATOM   589  N  NH2   . ARG A 1 88  ? 19.451  -2.006  8.748   1.00 99.52  ? 130  ARG B NH2   1 
ATOM   590  N  N     . THR A 1 89  ? 17.600  0.348   1.677   1.00 100.06 ? 131  THR B N     1 
ATOM   591  C  CA    . THR A 1 89  ? 16.245  0.383   1.147   1.00 90.29  ? 131  THR B CA    1 
ATOM   592  C  C     . THR A 1 89  ? 15.785  -0.951  0.577   1.00 84.50  ? 131  THR B C     1 
ATOM   593  O  O     . THR A 1 89  ? 14.610  -1.077  0.217   1.00 72.18  ? 131  THR B O     1 
ATOM   594  C  CB    . THR A 1 89  ? 16.119  1.465   0.064   1.00 87.19  ? 131  THR B CB    1 
ATOM   595  O  OG1   . THR A 1 89  ? 17.166  1.306   -0.901  1.00 89.64  ? 131  THR B OG1   1 
ATOM   596  C  CG2   . THR A 1 89  ? 16.205  2.851   0.685   1.00 90.82  ? 131  THR B CG2   1 
ATOM   597  N  N     . GLY A 1 90  ? 16.669  -1.941  0.481   1.00 83.89  ? 132  GLY B N     1 
ATOM   598  C  CA    . GLY A 1 90  ? 16.289  -3.274  0.068   1.00 77.68  ? 132  GLY B CA    1 
ATOM   599  C  C     . GLY A 1 90  ? 16.782  -3.722  -1.291  1.00 85.16  ? 132  GLY B C     1 
ATOM   600  O  O     . GLY A 1 90  ? 16.346  -4.777  -1.764  1.00 78.01  ? 132  GLY B O     1 
ATOM   601  N  N     . LYS A 1 91  ? 17.678  -2.969  -1.933  1.00 76.50  ? 133  LYS B N     1 
ATOM   602  C  CA    . LYS A 1 91  ? 18.149  -3.353  -3.261  1.00 82.27  ? 133  LYS B CA    1 
ATOM   603  C  C     . LYS A 1 91  ? 18.892  -4.684  -3.215  1.00 90.26  ? 133  LYS B C     1 
ATOM   604  O  O     . LYS A 1 91  ? 18.586  -5.607  -3.980  1.00 93.27  ? 133  LYS B O     1 
ATOM   605  C  CB    . LYS A 1 91  ? 19.043  -2.253  -3.836  1.00 76.38  ? 133  LYS B CB    1 
ATOM   606  C  CG    . LYS A 1 91  ? 18.494  -0.846  -3.645  1.00 77.22  ? 133  LYS B CG    1 
ATOM   607  C  CD    . LYS A 1 91  ? 19.446  0.200   -4.201  1.00 71.85  ? 133  LYS B CD    1 
ATOM   608  C  CE    . LYS A 1 91  ? 19.504  1.429   -3.312  1.00 95.09  ? 133  LYS B CE    1 
ATOM   609  N  NZ    . LYS A 1 91  ? 20.087  1.117   -1.978  1.00 87.70  ? 133  LYS B NZ    1 
ATOM   610  N  N     . THR A 1 92  ? 19.867  -4.803  -2.311  1.00 75.26  ? 134  THR B N     1 
ATOM   611  C  CA    . THR A 1 92  ? 20.638  -6.037  -2.209  1.00 77.69  ? 134  THR B CA    1 
ATOM   612  C  C     . THR A 1 92  ? 19.765  -7.201  -1.753  1.00 86.75  ? 134  THR B C     1 
ATOM   613  O  O     . THR A 1 92  ? 19.937  -8.334  -2.220  1.00 77.88  ? 134  THR B O     1 
ATOM   614  C  CB    . THR A 1 92  ? 21.815  -5.838  -1.253  1.00 82.48  ? 134  THR B CB    1 
ATOM   615  O  OG1   . THR A 1 92  ? 22.550  -4.669  -1.638  1.00 69.99  ? 134  THR B OG1   1 
ATOM   616  C  CG2   . THR A 1 92  ? 22.744  -7.041  -1.289  1.00 68.35  ? 134  THR B CG2   1 
ATOM   617  N  N     . GLN A 1 93  ? 18.812  -6.942  -0.854  1.00 84.13  ? 135  GLN B N     1 
ATOM   618  C  CA    . GLN A 1 93  ? 17.926  -8.008  -0.394  1.00 87.87  ? 135  GLN B CA    1 
ATOM   619  C  C     . GLN A 1 93  ? 16.997  -8.475  -1.509  1.00 84.22  ? 135  GLN B C     1 
ATOM   620  O  O     . GLN A 1 93  ? 16.761  -9.680  -1.665  1.00 79.53  ? 135  GLN B O     1 
ATOM   621  C  CB    . GLN A 1 93  ? 17.123  -7.536  0.818   1.00 100.13 ? 135  GLN B CB    1 
ATOM   622  C  CG    . GLN A 1 93  ? 17.979  -7.154  2.017   1.00 98.97  ? 135  GLN B CG    1 
ATOM   623  C  CD    . GLN A 1 93  ? 18.771  -8.326  2.568   1.00 100.28 ? 135  GLN B CD    1 
ATOM   624  O  OE1   . GLN A 1 93  ? 18.273  -9.450  2.638   1.00 92.52  ? 135  GLN B OE1   1 
ATOM   625  N  NE2   . GLN A 1 93  ? 20.014  -8.068  2.959   1.00 98.17  ? 135  GLN B NE2   1 
ATOM   626  N  N     . ILE A 1 94  ? 16.462  -7.538  -2.297  1.00 86.64  ? 136  ILE B N     1 
ATOM   627  C  CA    . ILE A 1 94  ? 15.631  -7.916  -3.438  1.00 82.82  ? 136  ILE B CA    1 
ATOM   628  C  C     . ILE A 1 94  ? 16.451  -8.706  -4.450  1.00 70.84  ? 136  ILE B C     1 
ATOM   629  O  O     . ILE A 1 94  ? 15.964  -9.678  -5.041  1.00 66.15  ? 136  ILE B O     1 
ATOM   630  C  CB    . ILE A 1 94  ? 14.987  -6.670  -4.074  1.00 59.23  ? 136  ILE B CB    1 
ATOM   631  C  CG1   . ILE A 1 94  ? 13.906  -6.097  -3.155  1.00 79.48  ? 136  ILE B CG1   1 
ATOM   632  C  CG2   . ILE A 1 94  ? 14.392  -7.004  -5.433  1.00 72.93  ? 136  ILE B CG2   1 
ATOM   633  C  CD1   . ILE A 1 94  ? 13.233  -4.855  -3.702  1.00 84.08  ? 136  ILE B CD1   1 
ATOM   634  N  N     . CYS A 1 95  ? 17.710  -8.310  -4.660  1.00 65.87  ? 137  CYS B N     1 
ATOM   635  C  CA    . CYS A 1 95  ? 18.569  -9.054  -5.576  1.00 73.55  ? 137  CYS B CA    1 
ATOM   636  C  C     . CYS A 1 95  ? 18.817  -10.472 -5.073  1.00 76.15  ? 137  CYS B C     1 
ATOM   637  O  O     . CYS A 1 95  ? 18.774  -11.432 -5.852  1.00 76.88  ? 137  CYS B O     1 
ATOM   638  C  CB    . CYS A 1 95  ? 19.892  -8.315  -5.775  1.00 79.99  ? 137  CYS B CB    1 
ATOM   639  S  SG    . CYS A 1 95  ? 19.748  -6.761  -6.692  1.00 88.37  ? 137  CYS B SG    1 
ATOM   640  N  N     . HIS A 1 96  ? 19.077  -10.623 -3.771  1.00 89.58  ? 138  HIS B N     1 
ATOM   641  C  CA    . HIS A 1 96  ? 19.284  -11.954 -3.208  1.00 77.84  ? 138  HIS B CA    1 
ATOM   642  C  C     . HIS A 1 96  ? 18.027  -12.807 -3.326  1.00 70.35  ? 138  HIS B C     1 
ATOM   643  O  O     . HIS A 1 96  ? 18.108  -14.014 -3.580  1.00 63.75  ? 138  HIS B O     1 
ATOM   644  C  CB    . HIS A 1 96  ? 19.723  -11.848 -1.747  1.00 71.65  ? 138  HIS B CB    1 
ATOM   645  C  CG    . HIS A 1 96  ? 21.190  -11.610 -1.575  1.00 70.55  ? 138  HIS B CG    1 
ATOM   646  N  ND1   . HIS A 1 96  ? 21.764  -10.364 -1.706  1.00 75.45  ? 138  HIS B ND1   1 
ATOM   647  C  CD2   . HIS A 1 96  ? 22.202  -12.462 -1.286  1.00 62.77  ? 138  HIS B CD2   1 
ATOM   648  C  CE1   . HIS A 1 96  ? 23.066  -10.458 -1.504  1.00 75.61  ? 138  HIS B CE1   1 
ATOM   649  N  NE2   . HIS A 1 96  ? 23.358  -11.720 -1.247  1.00 80.19  ? 138  HIS B NE2   1 
ATOM   650  N  N     . THR A 1 97  ? 16.854  -12.197 -3.140  1.00 62.70  ? 139  THR B N     1 
ATOM   651  C  CA    . THR A 1 97  ? 15.609  -12.943 -3.294  1.00 57.08  ? 139  THR B CA    1 
ATOM   652  C  C     . THR A 1 97  ? 15.405  -13.382 -4.740  1.00 84.58  ? 139  THR B C     1 
ATOM   653  O  O     . THR A 1 97  ? 15.035  -14.535 -4.998  1.00 88.16  ? 139  THR B O     1 
ATOM   654  C  CB    . THR A 1 97  ? 14.427  -12.099 -2.818  1.00 64.14  ? 139  THR B CB    1 
ATOM   655  O  OG1   . THR A 1 97  ? 14.589  -11.789 -1.428  1.00 90.64  ? 139  THR B OG1   1 
ATOM   656  C  CG2   . THR A 1 97  ? 13.118  -12.852 -3.015  1.00 79.07  ? 139  THR B CG2   1 
ATOM   657  N  N     . LEU A 1 98  ? 15.651  -12.479 -5.693  1.00 83.24  ? 140  LEU B N     1 
ATOM   658  C  CA    . LEU A 1 98  ? 15.457  -12.807 -7.102  1.00 75.26  ? 140  LEU B CA    1 
ATOM   659  C  C     . LEU A 1 98  ? 16.437  -13.878 -7.564  1.00 76.70  ? 140  LEU B C     1 
ATOM   660  O  O     . LEU A 1 98  ? 16.075  -14.753 -8.360  1.00 76.24  ? 140  LEU B O     1 
ATOM   661  C  CB    . LEU A 1 98  ? 15.594  -11.548 -7.958  1.00 59.56  ? 140  LEU B CB    1 
ATOM   662  C  CG    . LEU A 1 98  ? 14.484  -10.502 -7.824  1.00 53.07  ? 140  LEU B CG    1 
ATOM   663  C  CD1   . LEU A 1 98  ? 14.797  -9.272  -8.661  1.00 51.64  ? 140  LEU B CD1   1 
ATOM   664  C  CD2   . LEU A 1 98  ? 13.143  -11.096 -8.221  1.00 63.78  ? 140  LEU B CD2   1 
ATOM   665  N  N     . ALA A 1 99  ? 17.677  -13.835 -7.065  1.00 73.45  ? 141  ALA B N     1 
ATOM   666  C  CA    . ALA A 1 99  ? 18.690  -14.811 -7.452  1.00 74.47  ? 141  ALA B CA    1 
ATOM   667  C  C     . ALA A 1 99  ? 18.297  -16.242 -7.112  1.00 84.31  ? 141  ALA B C     1 
ATOM   668  O  O     . ALA A 1 99  ? 18.947  -17.176 -7.595  1.00 85.24  ? 141  ALA B O     1 
ATOM   669  C  CB    . ALA A 1 99  ? 20.024  -14.471 -6.785  1.00 55.40  ? 141  ALA B CB    1 
ATOM   670  N  N     . VAL A 1 100 ? 17.264  -16.438 -6.298  1.00 84.71  ? 142  VAL B N     1 
ATOM   671  C  CA    . VAL A 1 100 ? 16.754  -17.761 -5.983  1.00 85.43  ? 142  VAL B CA    1 
ATOM   672  C  C     . VAL A 1 100 ? 15.365  -17.981 -6.571  1.00 79.04  ? 142  VAL B C     1 
ATOM   673  O  O     . VAL A 1 100 ? 15.056  -19.079 -7.041  1.00 85.51  ? 142  VAL B O     1 
ATOM   674  C  CB    . VAL A 1 100 ? 16.755  -17.996 -4.457  1.00 92.81  ? 142  VAL B CB    1 
ATOM   675  C  CG1   . VAL A 1 100 ? 16.089  -19.319 -4.109  1.00 82.66  ? 142  VAL B CG1   1 
ATOM   676  C  CG2   . VAL A 1 100 ? 18.180  -17.963 -3.928  1.00 88.94  ? 142  VAL B CG2   1 
ATOM   677  N  N     . THR A 1 101 ? 14.521  -16.945 -6.578  1.00 72.88  ? 143  THR B N     1 
ATOM   678  C  CA    . THR A 1 101 ? 13.192  -17.092 -7.161  1.00 81.68  ? 143  THR B CA    1 
ATOM   679  C  C     . THR A 1 101 ? 13.237  -17.277 -8.673  1.00 100.35 ? 143  THR B C     1 
ATOM   680  O  O     . THR A 1 101 ? 12.270  -17.788 -9.247  1.00 105.14 ? 143  THR B O     1 
ATOM   681  C  CB    . THR A 1 101 ? 12.311  -15.888 -6.820  1.00 88.38  ? 143  THR B CB    1 
ATOM   682  O  OG1   . THR A 1 101 ? 12.910  -14.691 -7.331  1.00 88.77  ? 143  THR B OG1   1 
ATOM   683  C  CG2   . THR A 1 101 ? 12.128  -15.766 -5.313  1.00 91.88  ? 143  THR B CG2   1 
ATOM   684  N  N     . CYS A 1 102 ? 14.331  -16.881 -9.330  1.00 96.30  ? 144  CYS B N     1 
ATOM   685  C  CA    . CYS A 1 102 ? 14.441  -17.102 -10.767 1.00 76.82  ? 144  CYS B CA    1 
ATOM   686  C  C     . CYS A 1 102 ? 14.616  -18.575 -11.112 1.00 95.18  ? 144  CYS B C     1 
ATOM   687  O  O     . CYS A 1 102 ? 14.371  -18.963 -12.259 1.00 99.09  ? 144  CYS B O     1 
ATOM   688  C  CB    . CYS A 1 102 ? 15.605  -16.294 -11.340 1.00 77.56  ? 144  CYS B CB    1 
ATOM   689  S  SG    . CYS A 1 102 ? 17.235  -16.851 -10.803 1.00 93.72  ? 144  CYS B SG    1 
ATOM   690  N  N     . GLN A 1 103 ? 15.033  -19.399 -10.149 1.00 92.89  ? 145  GLN B N     1 
ATOM   691  C  CA    . GLN A 1 103 ? 15.187  -20.830 -10.375 1.00 104.90 ? 145  GLN B CA    1 
ATOM   692  C  C     . GLN A 1 103 ? 13.883  -21.599 -10.209 1.00 104.17 ? 145  GLN B C     1 
ATOM   693  O  O     . GLN A 1 103 ? 13.860  -22.807 -10.466 1.00 106.89 ? 145  GLN B O     1 
ATOM   694  C  CB    . GLN A 1 103 ? 16.242  -21.400 -9.425  1.00 86.53  ? 145  GLN B CB    1 
ATOM   695  C  CG    . GLN A 1 103 ? 17.564  -20.653 -9.450  1.00 90.02  ? 145  GLN B CG    1 
ATOM   696  C  CD    . GLN A 1 103 ? 18.588  -21.253 -8.509  1.00 96.60  ? 145  GLN B CD    1 
ATOM   697  O  OE1   . GLN A 1 103 ? 18.576  -22.455 -8.244  1.00 108.37 ? 145  GLN B OE1   1 
ATOM   698  N  NE2   . GLN A 1 103 ? 19.479  -20.415 -7.993  1.00 89.22  ? 145  GLN B NE2   1 
ATOM   699  N  N     . LEU A 1 104 ? 12.810  -20.935 -9.786  1.00 95.25  ? 146  LEU B N     1 
ATOM   700  C  CA    . LEU A 1 104 ? 11.526  -21.593 -9.627  1.00 103.20 ? 146  LEU B CA    1 
ATOM   701  C  C     . LEU A 1 104 ? 10.958  -21.995 -10.986 1.00 110.27 ? 146  LEU B C     1 
ATOM   702  O  O     . LEU A 1 104 ? 11.318  -21.420 -12.016 1.00 101.16 ? 146  LEU B O     1 
ATOM   703  C  CB    . LEU A 1 104 ? 10.545  -20.672 -8.905  1.00 105.19 ? 146  LEU B CB    1 
ATOM   704  C  CG    . LEU A 1 104 ? 10.854  -20.322 -7.450  1.00 104.77 ? 146  LEU B CG    1 
ATOM   705  C  CD1   . LEU A 1 104 ? 9.853   -19.306 -6.923  1.00 93.73  ? 146  LEU B CD1   1 
ATOM   706  C  CD2   . LEU A 1 104 ? 10.846  -21.575 -6.592  1.00 109.51 ? 146  LEU B CD2   1 
ATOM   707  N  N     . PRO A 1 105 ? 10.075  -22.993 -11.014 1.00 113.46 ? 147  PRO B N     1 
ATOM   708  C  CA    . PRO A 1 105 ? 9.386   -23.327 -12.265 1.00 109.17 ? 147  PRO B CA    1 
ATOM   709  C  C     . PRO A 1 105 ? 8.521   -22.171 -12.745 1.00 114.03 ? 147  PRO B C     1 
ATOM   710  O  O     . PRO A 1 105 ? 8.176   -21.259 -11.990 1.00 113.66 ? 147  PRO B O     1 
ATOM   711  C  CB    . PRO A 1 105 ? 8.534   -24.545 -11.889 1.00 114.24 ? 147  PRO B CB    1 
ATOM   712  C  CG    . PRO A 1 105 ? 9.221   -25.134 -10.702 1.00 116.05 ? 147  PRO B CG    1 
ATOM   713  C  CD    . PRO A 1 105 ? 9.785   -23.967 -9.948  1.00 112.27 ? 147  PRO B CD    1 
ATOM   714  N  N     . ILE A 1 106 ? 8.174   -22.219 -14.033 1.00 104.51 ? 148  ILE B N     1 
ATOM   715  C  CA    . ILE A 1 106 ? 7.355   -21.162 -14.623 1.00 107.37 ? 148  ILE B CA    1 
ATOM   716  C  C     . ILE A 1 106 ? 5.986   -21.114 -13.956 1.00 121.41 ? 148  ILE B C     1 
ATOM   717  O  O     . ILE A 1 106 ? 5.424   -20.034 -13.732 1.00 126.33 ? 148  ILE B O     1 
ATOM   718  C  CB    . ILE A 1 106 ? 7.244   -21.361 -16.146 1.00 101.55 ? 148  ILE B CB    1 
ATOM   719  C  CG1   . ILE A 1 106 ? 8.617   -21.200 -16.804 1.00 102.15 ? 148  ILE B CG1   1 
ATOM   720  C  CG2   . ILE A 1 106 ? 6.249   -20.380 -16.750 1.00 82.80  ? 148  ILE B CG2   1 
ATOM   721  C  CD1   . ILE A 1 106 ? 8.598   -21.359 -18.308 1.00 103.39 ? 148  ILE B CD1   1 
ATOM   722  N  N     . ASP A 1 107 ? 5.432   -22.280 -13.614 1.00 120.11 ? 149  ASP B N     1 
ATOM   723  C  CA    . ASP A 1 107 ? 4.143   -22.321 -12.933 1.00 119.35 ? 149  ASP B CA    1 
ATOM   724  C  C     . ASP A 1 107 ? 4.210   -21.739 -11.527 1.00 121.89 ? 149  ASP B C     1 
ATOM   725  O  O     . ASP A 1 107 ? 3.175   -21.331 -10.989 1.00 122.21 ? 149  ASP B O     1 
ATOM   726  C  CB    . ASP A 1 107 ? 3.620   -23.758 -12.875 1.00 127.77 ? 149  ASP B CB    1 
ATOM   727  C  CG    . ASP A 1 107 ? 3.199   -24.278 -14.235 1.00 144.06 ? 149  ASP B CG    1 
ATOM   728  O  OD1   . ASP A 1 107 ? 2.773   -23.462 -15.080 1.00 135.67 ? 149  ASP B OD1   1 
ATOM   729  O  OD2   . ASP A 1 107 ? 3.291   -25.504 -14.459 1.00 156.26 ? 149  ASP B OD2   1 
ATOM   730  N  N     . ARG A 1 108 ? 5.396   -21.690 -10.922 1.00 110.26 ? 150  ARG B N     1 
ATOM   731  C  CA    . ARG A 1 108 ? 5.576   -21.102 -9.602  1.00 104.44 ? 150  ARG B CA    1 
ATOM   732  C  C     . ARG A 1 108 ? 6.038   -19.652 -9.667  1.00 103.60 ? 150  ARG B C     1 
ATOM   733  O  O     . ARG A 1 108 ? 6.339   -19.061 -8.625  1.00 95.33  ? 150  ARG B O     1 
ATOM   734  C  CB    . ARG A 1 108 ? 6.568   -21.932 -8.784  1.00 112.81 ? 150  ARG B CB    1 
ATOM   735  C  CG    . ARG A 1 108 ? 6.133   -23.372 -8.557  1.00 115.26 ? 150  ARG B CG    1 
ATOM   736  C  CD    . ARG A 1 108 ? 7.007   -24.055 -7.518  1.00 106.61 ? 150  ARG B CD    1 
ATOM   737  N  NE    . ARG A 1 108 ? 6.914   -23.401 -6.218  1.00 100.46 ? 150  ARG B NE    1 
ATOM   738  C  CZ    . ARG A 1 108 ? 7.572   -23.789 -5.134  1.00 102.89 ? 150  ARG B CZ    1 
ATOM   739  N  NH1   . ARG A 1 108 ? 8.385   -24.832 -5.156  1.00 106.93 ? 150  ARG B NH1   1 
ATOM   740  N  NH2   . ARG A 1 108 ? 7.409   -23.114 -4.000  1.00 101.64 ? 150  ARG B NH2   1 
ATOM   741  N  N     . GLY A 1 109 ? 6.100   -19.068 -10.861 1.00 111.52 ? 151  GLY B N     1 
ATOM   742  C  CA    . GLY A 1 109 ? 6.495   -17.685 -11.017 1.00 95.70  ? 151  GLY B CA    1 
ATOM   743  C  C     . GLY A 1 109 ? 7.968   -17.450 -11.264 1.00 91.99  ? 151  GLY B C     1 
ATOM   744  O  O     . GLY A 1 109 ? 8.414   -16.299 -11.181 1.00 81.70  ? 151  GLY B O     1 
ATOM   745  N  N     . GLY A 1 110 ? 8.738   -18.495 -11.566 1.00 100.31 ? 152  GLY B N     1 
ATOM   746  C  CA    . GLY A 1 110 ? 10.158  -18.369 -11.798 1.00 96.37  ? 152  GLY B CA    1 
ATOM   747  C  C     . GLY A 1 110 ? 10.506  -18.295 -13.274 1.00 97.10  ? 152  GLY B C     1 
ATOM   748  O  O     . GLY A 1 110 ? 9.658   -18.077 -14.142 1.00 102.25 ? 152  GLY B O     1 
ATOM   749  N  N     . GLY A 1 111 ? 11.794  -18.483 -13.554 1.00 84.66  ? 153  GLY B N     1 
ATOM   750  C  CA    . GLY A 1 111 ? 12.284  -18.444 -14.917 1.00 96.83  ? 153  GLY B CA    1 
ATOM   751  C  C     . GLY A 1 111 ? 12.960  -19.731 -15.343 1.00 99.65  ? 153  GLY B C     1 
ATOM   752  O  O     . GLY A 1 111 ? 13.372  -19.868 -16.499 1.00 97.63  ? 153  GLY B O     1 
ATOM   753  N  N     . GLU A 1 112 ? 13.080  -20.678 -14.410 1.00 100.49 ? 154  GLU B N     1 
ATOM   754  C  CA    . GLU A 1 112 ? 13.700  -21.980 -14.664 1.00 101.39 ? 154  GLU B CA    1 
ATOM   755  C  C     . GLU A 1 112 ? 15.128  -21.839 -15.182 1.00 89.10  ? 154  GLU B C     1 
ATOM   756  O  O     . GLU A 1 112 ? 15.590  -22.647 -15.992 1.00 104.23 ? 154  GLU B O     1 
ATOM   757  C  CB    . GLU A 1 112 ? 12.862  -22.817 -15.635 1.00 87.11  ? 154  GLU B CB    1 
ATOM   758  C  CG    . GLU A 1 112 ? 11.433  -23.044 -15.181 1.00 106.65 ? 154  GLU B CG    1 
ATOM   759  C  CD    . GLU A 1 112 ? 10.658  -23.949 -16.118 1.00 113.93 ? 154  GLU B CD    1 
ATOM   760  O  OE1   . GLU A 1 112 ? 11.230  -24.375 -17.144 1.00 116.97 ? 154  GLU B OE1   1 
ATOM   761  O  OE2   . GLU A 1 112 ? 9.477   -24.234 -15.829 1.00 110.78 ? 154  GLU B OE2   1 
ATOM   762  N  N     . GLY A 1 113 ? 15.840  -20.812 -14.721 1.00 92.05  ? 155  GLY B N     1 
ATOM   763  C  CA    . GLY A 1 113 ? 17.202  -20.588 -15.151 1.00 96.01  ? 155  GLY B CA    1 
ATOM   764  C  C     . GLY A 1 113 ? 18.086  -20.223 -13.976 1.00 86.83  ? 155  GLY B C     1 
ATOM   765  O  O     . GLY A 1 113 ? 17.613  -19.821 -12.911 1.00 103.00 ? 155  GLY B O     1 
ATOM   766  N  N     . LYS A 1 114 ? 19.389  -20.375 -14.190 1.00 79.84  ? 156  LYS B N     1 
ATOM   767  C  CA    . LYS A 1 114 ? 20.361  -20.056 -13.159 1.00 94.53  ? 156  LYS B CA    1 
ATOM   768  C  C     . LYS A 1 114 ? 20.531  -18.544 -13.032 1.00 93.22  ? 156  LYS B C     1 
ATOM   769  O  O     . LYS A 1 114 ? 20.206  -17.775 -13.941 1.00 85.91  ? 156  LYS B O     1 
ATOM   770  C  CB    . LYS A 1 114 ? 21.705  -20.719 -13.463 1.00 82.99  ? 156  LYS B CB    1 
ATOM   771  C  CG    . LYS A 1 114 ? 21.630  -22.232 -13.595 1.00 94.90  ? 156  LYS B CG    1 
ATOM   772  C  CD    . LYS A 1 114 ? 23.014  -22.859 -13.588 1.00 101.38 ? 156  LYS B CD    1 
ATOM   773  C  CE    . LYS A 1 114 ? 23.889  -22.276 -14.682 1.00 103.69 ? 156  LYS B CE    1 
ATOM   774  N  NZ    . LYS A 1 114 ? 25.247  -22.888 -14.696 1.00 123.91 ? 156  LYS B NZ    1 
ATOM   775  N  N     . ALA A 1 115 ? 21.045  -18.123 -11.882 1.00 82.85  ? 157  ALA B N     1 
ATOM   776  C  CA    . ALA A 1 115 ? 21.223  -16.714 -11.572 1.00 65.12  ? 157  ALA B CA    1 
ATOM   777  C  C     . ALA A 1 115 ? 22.688  -16.310 -11.686 1.00 80.16  ? 157  ALA B C     1 
ATOM   778  O  O     . ALA A 1 115 ? 23.599  -17.135 -11.586 1.00 88.02  ? 157  ALA B O     1 
ATOM   779  C  CB    . ALA A 1 115 ? 20.707  -16.398 -10.167 1.00 88.71  ? 157  ALA B CB    1 
ATOM   780  N  N     . MET A 1 116 ? 22.903  -15.012 -11.881 1.00 79.23  ? 158  MET B N     1 
ATOM   781  C  CA    . MET A 1 116 ? 24.243  -14.459 -12.034 1.00 80.78  ? 158  MET B CA    1 
ATOM   782  C  C     . MET A 1 116 ? 24.325  -13.164 -11.242 1.00 84.17  ? 158  MET B C     1 
ATOM   783  O  O     . MET A 1 116 ? 23.554  -12.233 -11.492 1.00 78.68  ? 158  MET B O     1 
ATOM   784  C  CB    . MET A 1 116 ? 24.567  -14.219 -13.509 1.00 89.18  ? 158  MET B CB    1 
ATOM   785  C  CG    . MET A 1 116 ? 26.039  -14.056 -13.794 1.00 95.85  ? 158  MET B CG    1 
ATOM   786  S  SD    . MET A 1 116 ? 26.367  -14.035 -15.560 1.00 130.78 ? 158  MET B SD    1 
ATOM   787  C  CE    . MET A 1 116 ? 25.754  -15.644 -16.048 1.00 107.40 ? 158  MET B CE    1 
ATOM   788  N  N     . TYR A 1 117 ? 25.260  -13.104 -10.295 1.00 84.24  ? 159  TYR B N     1 
ATOM   789  C  CA    . TYR A 1 117 ? 25.359  -12.002 -9.343  1.00 91.44  ? 159  TYR B CA    1 
ATOM   790  C  C     . TYR A 1 117 ? 26.738  -11.364 -9.456  1.00 88.55  ? 159  TYR B C     1 
ATOM   791  O  O     . TYR A 1 117 ? 27.741  -11.962 -9.047  1.00 96.99  ? 159  TYR B O     1 
ATOM   792  C  CB    . TYR A 1 117 ? 25.102  -12.495 -7.919  1.00 79.29  ? 159  TYR B CB    1 
ATOM   793  C  CG    . TYR A 1 117 ? 24.641  -11.418 -6.964  1.00 75.32  ? 159  TYR B CG    1 
ATOM   794  C  CD1   . TYR A 1 117 ? 25.540  -10.504 -6.429  1.00 87.24  ? 159  TYR B CD1   1 
ATOM   795  C  CD2   . TYR A 1 117 ? 23.307  -11.321 -6.591  1.00 92.91  ? 159  TYR B CD2   1 
ATOM   796  C  CE1   . TYR A 1 117 ? 25.121  -9.520  -5.554  1.00 91.32  ? 159  TYR B CE1   1 
ATOM   797  C  CE2   . TYR A 1 117 ? 22.879  -10.341 -5.716  1.00 83.03  ? 159  TYR B CE2   1 
ATOM   798  C  CZ    . TYR A 1 117 ? 23.790  -9.443  -5.201  1.00 83.82  ? 159  TYR B CZ    1 
ATOM   799  O  OH    . TYR A 1 117 ? 23.367  -8.465  -4.331  1.00 93.65  ? 159  TYR B OH    1 
ATOM   800  N  N     . ILE A 1 118 ? 26.783  -10.150 -9.995  1.00 84.03  ? 160  ILE B N     1 
ATOM   801  C  CA    . ILE A 1 118 ? 27.999  -9.348  -10.053 1.00 92.82  ? 160  ILE B CA    1 
ATOM   802  C  C     . ILE A 1 118 ? 27.951  -8.366  -8.890  1.00 93.90  ? 160  ILE B C     1 
ATOM   803  O  O     . ILE A 1 118 ? 27.145  -7.428  -8.888  1.00 96.68  ? 160  ILE B O     1 
ATOM   804  C  CB    . ILE A 1 118 ? 28.138  -8.621  -11.396 1.00 94.95  ? 160  ILE B CB    1 
ATOM   805  C  CG1   . ILE A 1 118 ? 28.196  -9.630  -12.544 1.00 74.69  ? 160  ILE B CG1   1 
ATOM   806  C  CG2   . ILE A 1 118 ? 29.375  -7.734  -11.398 1.00 90.25  ? 160  ILE B CG2   1 
ATOM   807  C  CD1   . ILE A 1 118 ? 28.359  -8.996  -13.908 1.00 92.35  ? 160  ILE B CD1   1 
ATOM   808  N  N     . ASP A 1 119 ? 28.809  -8.579  -7.897  1.00 95.90  ? 161  ASP B N     1 
ATOM   809  C  CA    . ASP A 1 119 ? 28.834  -7.768  -6.687  1.00 95.28  ? 161  ASP B CA    1 
ATOM   810  C  C     . ASP A 1 119 ? 29.978  -6.765  -6.763  1.00 99.53  ? 161  ASP B C     1 
ATOM   811  O  O     . ASP A 1 119 ? 31.104  -7.125  -7.123  1.00 101.85 ? 161  ASP B O     1 
ATOM   812  C  CB    . ASP A 1 119 ? 28.985  -8.652  -5.447  1.00 106.61 ? 161  ASP B CB    1 
ATOM   813  C  CG    . ASP A 1 119 ? 28.831  -7.877  -4.152  1.00 110.76 ? 161  ASP B CG    1 
ATOM   814  O  OD1   . ASP A 1 119 ? 28.436  -6.692  -4.201  1.00 107.74 ? 161  ASP B OD1   1 
ATOM   815  O  OD2   . ASP A 1 119 ? 29.105  -8.457  -3.081  1.00 108.50 ? 161  ASP B OD2   1 
ATOM   816  N  N     . THR A 1 120 ? 29.686  -5.511  -6.419  1.00 93.47  ? 162  THR B N     1 
ATOM   817  C  CA    . THR A 1 120 ? 30.680  -4.448  -6.423  1.00 90.44  ? 162  THR B CA    1 
ATOM   818  C  C     . THR A 1 120 ? 30.884  -3.812  -5.056  1.00 102.83 ? 162  THR B C     1 
ATOM   819  O  O     . THR A 1 120 ? 31.765  -2.956  -4.914  1.00 101.20 ? 162  THR B O     1 
ATOM   820  C  CB    . THR A 1 120 ? 30.295  -3.355  -7.431  1.00 105.61 ? 162  THR B CB    1 
ATOM   821  O  OG1   . THR A 1 120 ? 29.034  -2.783  -7.060  1.00 95.41  ? 162  THR B OG1   1 
ATOM   822  C  CG2   . THR A 1 120 ? 30.192  -3.933  -8.835  1.00 106.68 ? 162  THR B CG2   1 
ATOM   823  N  N     . GLU A 1 121 ? 30.101  -4.199  -4.048  1.00 100.26 ? 163  GLU B N     1 
ATOM   824  C  CA    . GLU A 1 121 ? 30.199  -3.617  -2.716  1.00 109.59 ? 163  GLU B CA    1 
ATOM   825  C  C     . GLU A 1 121 ? 30.514  -4.651  -1.642  1.00 110.00 ? 163  GLU B C     1 
ATOM   826  O  O     . GLU A 1 121 ? 30.531  -4.308  -0.454  1.00 102.10 ? 163  GLU B O     1 
ATOM   827  C  CB    . GLU A 1 121 ? 28.904  -2.878  -2.364  1.00 96.60  ? 163  GLU B CB    1 
ATOM   828  C  CG    . GLU A 1 121 ? 28.643  -1.646  -3.212  1.00 91.75  ? 163  GLU B CG    1 
ATOM   829  C  CD    . GLU A 1 121 ? 27.296  -1.015  -2.921  1.00 110.66 ? 163  GLU B CD    1 
ATOM   830  O  OE1   . GLU A 1 121 ? 26.380  -1.743  -2.483  1.00 116.00 ? 163  GLU B OE1   1 
ATOM   831  O  OE2   . GLU A 1 121 ? 27.153  0.208   -3.129  1.00 103.01 ? 163  GLU B OE2   1 
ATOM   832  N  N     . GLY A 1 122 ? 30.763  -5.901  -2.023  1.00 106.85 ? 164  GLY B N     1 
ATOM   833  C  CA    . GLY A 1 122 ? 31.065  -6.931  -1.048  1.00 98.24  ? 164  GLY B CA    1 
ATOM   834  C  C     . GLY A 1 122 ? 29.913  -7.279  -0.133  1.00 109.11 ? 164  GLY B C     1 
ATOM   835  O  O     . GLY A 1 122 ? 30.141  -7.687  1.011   1.00 121.90 ? 164  GLY B O     1 
ATOM   836  N  N     . THR A 1 123 ? 28.676  -7.129  -0.605  1.00 98.52  ? 165  THR B N     1 
ATOM   837  C  CA    . THR A 1 123 ? 27.487  -7.405  0.190   1.00 83.84  ? 165  THR B CA    1 
ATOM   838  C  C     . THR A 1 123 ? 26.751  -8.652  -0.294  1.00 84.17  ? 165  THR B C     1 
ATOM   839  O  O     . THR A 1 123 ? 25.521  -8.720  -0.225  1.00 99.93  ? 165  THR B O     1 
ATOM   840  C  CB    . THR A 1 123 ? 26.548  -6.199  0.185   1.00 87.40  ? 165  THR B CB    1 
ATOM   841  O  OG1   . THR A 1 123 ? 26.133  -5.920  -1.158  1.00 104.95 ? 165  THR B OG1   1 
ATOM   842  C  CG2   . THR A 1 123 ? 27.252  -4.976  0.755   1.00 81.45  ? 165  THR B CG2   1 
ATOM   843  N  N     . PHE A 1 124 ? 27.490  -9.645  -0.785  1.00 84.60  ? 166  PHE B N     1 
ATOM   844  C  CA    . PHE A 1 124 ? 26.913  -10.901 -1.246  1.00 93.42  ? 166  PHE B CA    1 
ATOM   845  C  C     . PHE A 1 124 ? 26.965  -11.916 -0.111  1.00 102.58 ? 166  PHE B C     1 
ATOM   846  O  O     . PHE A 1 124 ? 28.047  -12.217 0.405   1.00 99.91  ? 166  PHE B O     1 
ATOM   847  C  CB    . PHE A 1 124 ? 27.654  -11.427 -2.474  1.00 93.31  ? 166  PHE B CB    1 
ATOM   848  C  CG    . PHE A 1 124 ? 27.154  -12.758 -2.958  1.00 94.55  ? 166  PHE B CG    1 
ATOM   849  C  CD1   . PHE A 1 124 ? 25.976  -12.849 -3.682  1.00 90.25  ? 166  PHE B CD1   1 
ATOM   850  C  CD2   . PHE A 1 124 ? 27.862  -13.918 -2.691  1.00 96.14  ? 166  PHE B CD2   1 
ATOM   851  C  CE1   . PHE A 1 124 ? 25.514  -14.073 -4.130  1.00 90.58  ? 166  PHE B CE1   1 
ATOM   852  C  CE2   . PHE A 1 124 ? 27.406  -15.143 -3.136  1.00 94.08  ? 166  PHE B CE2   1 
ATOM   853  C  CZ    . PHE A 1 124 ? 26.231  -15.221 -3.856  1.00 96.21  ? 166  PHE B CZ    1 
ATOM   854  N  N     . ARG A 1 125 ? 25.806  -12.437 0.267   1.00 98.30  ? 167  ARG B N     1 
ATOM   855  C  CA    . ARG A 1 125 ? 25.690  -13.392 1.369   1.00 101.36 ? 167  ARG B CA    1 
ATOM   856  C  C     . ARG A 1 125 ? 24.922  -14.616 0.900   1.00 96.07  ? 167  ARG B C     1 
ATOM   857  O  O     . ARG A 1 125 ? 23.695  -14.518 0.662   1.00 102.06 ? 167  ARG B O     1 
ATOM   858  C  CB    . ARG A 1 125 ? 25.000  -12.753 2.571   1.00 93.56  ? 167  ARG B CB    1 
ATOM   859  C  CG    . ARG A 1 125 ? 25.641  -11.460 3.056   1.00 109.64 ? 167  ARG B CG    1 
ATOM   860  C  CD    . ARG A 1 125 ? 27.034  -11.702 3.614   1.00 121.99 ? 167  ARG B CD    1 
ATOM   861  N  NE    . ARG A 1 125 ? 27.628  -10.479 4.142   1.00 108.69 ? 167  ARG B NE    1 
ATOM   862  C  CZ    . ARG A 1 125 ? 28.409  -9.664  3.446   1.00 99.09  ? 167  ARG B CZ    1 
ATOM   863  N  NH1   . ARG A 1 125 ? 28.717  -9.913  2.184   1.00 110.27 ? 167  ARG B NH1   1 
ATOM   864  N  NH2   . ARG A 1 125 ? 28.892  -8.572  4.031   1.00 99.65  ? 167  ARG B NH2   1 
ATOM   865  N  N     . PRO A 1 126 ? 25.568  -15.773 0.745   1.00 86.35  ? 168  PRO B N     1 
ATOM   866  C  CA    . PRO A 1 126 ? 24.821  -16.991 0.394   1.00 90.06  ? 168  PRO B CA    1 
ATOM   867  C  C     . PRO A 1 126 ? 23.849  -17.437 1.474   1.00 96.92  ? 168  PRO B C     1 
ATOM   868  O  O     . PRO A 1 126 ? 22.976  -18.270 1.194   1.00 99.67  ? 168  PRO B O     1 
ATOM   869  C  CB    . PRO A 1 126 ? 25.925  -18.036 0.173   1.00 96.53  ? 168  PRO B CB    1 
ATOM   870  C  CG    . PRO A 1 126 ? 27.171  -17.240 -0.074  1.00 85.85  ? 168  PRO B CG    1 
ATOM   871  C  CD    . PRO A 1 126 ? 27.024  -15.999 0.752   1.00 90.02  ? 168  PRO B CD    1 
ATOM   872  N  N     . GLU A 1 127 ? 23.975  -16.914 2.697   1.00 101.71 ? 169  GLU B N     1 
ATOM   873  C  CA    . GLU A 1 127 ? 23.057  -17.292 3.766   1.00 91.54  ? 169  GLU B CA    1 
ATOM   874  C  C     . GLU A 1 127 ? 21.638  -16.826 3.462   1.00 99.89  ? 169  GLU B C     1 
ATOM   875  O  O     . GLU A 1 127 ? 20.668  -17.541 3.740   1.00 100.92 ? 169  GLU B O     1 
ATOM   876  C  CB    . GLU A 1 127 ? 23.544  -16.717 5.095   1.00 99.91  ? 169  GLU B CB    1 
ATOM   877  C  CG    . GLU A 1 127 ? 25.021  -16.959 5.363   1.00 105.14 ? 169  GLU B CG    1 
ATOM   878  C  CD    . GLU A 1 127 ? 25.506  -16.277 6.627   1.00 137.91 ? 169  GLU B CD    1 
ATOM   879  O  OE1   . GLU A 1 127 ? 24.667  -15.983 7.505   1.00 148.28 ? 169  GLU B OE1   1 
ATOM   880  O  OE2   . GLU A 1 127 ? 26.725  -16.030 6.739   1.00 120.03 ? 169  GLU B OE2   1 
ATOM   881  N  N     . ARG A 1 128 ? 21.497  -15.630 2.885   1.00 99.29  ? 170  ARG B N     1 
ATOM   882  C  CA    . ARG A 1 128 ? 20.177  -15.161 2.476   1.00 93.28  ? 170  ARG B CA    1 
ATOM   883  C  C     . ARG A 1 128 ? 19.601  -16.040 1.374   1.00 96.67  ? 170  ARG B C     1 
ATOM   884  O  O     . ARG A 1 128 ? 18.392  -16.303 1.343   1.00 98.67  ? 170  ARG B O     1 
ATOM   885  C  CB    . ARG A 1 128 ? 20.258  -13.705 2.018   1.00 82.56  ? 170  ARG B CB    1 
ATOM   886  C  CG    . ARG A 1 128 ? 20.766  -12.750 3.086   1.00 102.95 ? 170  ARG B CG    1 
ATOM   887  C  CD    . ARG A 1 128 ? 19.834  -12.727 4.285   1.00 108.68 ? 170  ARG B CD    1 
ATOM   888  N  NE    . ARG A 1 128 ? 18.524  -12.184 3.945   1.00 101.04 ? 170  ARG B NE    1 
ATOM   889  C  CZ    . ARG A 1 128 ? 17.479  -12.180 4.761   1.00 90.66  ? 170  ARG B CZ    1 
ATOM   890  N  NH1   . ARG A 1 128 ? 17.548  -12.701 5.975   1.00 108.25 ? 170  ARG B NH1   1 
ATOM   891  N  NH2   . ARG A 1 128 ? 16.335  -11.642 4.348   1.00 90.13  ? 170  ARG B NH2   1 
ATOM   892  N  N     . LEU A 1 129 ? 20.456  -16.504 0.458   1.00 87.90  ? 171  LEU B N     1 
ATOM   893  C  CA    . LEU A 1 129 ? 20.009  -17.429 -0.577  1.00 92.61  ? 171  LEU B CA    1 
ATOM   894  C  C     . LEU A 1 129 ? 19.495  -18.723 0.040   1.00 94.77  ? 171  LEU B C     1 
ATOM   895  O  O     . LEU A 1 129 ? 18.435  -19.230 -0.342  1.00 88.37  ? 171  LEU B O     1 
ATOM   896  C  CB    . LEU A 1 129 ? 21.151  -17.715 -1.554  1.00 91.26  ? 171  LEU B CB    1 
ATOM   897  C  CG    . LEU A 1 129 ? 21.856  -16.506 -2.173  1.00 84.15  ? 171  LEU B CG    1 
ATOM   898  C  CD1   . LEU A 1 129 ? 22.979  -16.956 -3.093  1.00 78.60  ? 171  LEU B CD1   1 
ATOM   899  C  CD2   . LEU A 1 129 ? 20.867  -15.626 -2.920  1.00 69.68  ? 171  LEU B CD2   1 
ATOM   900  N  N     . LEU A 1 130 ? 20.239  -19.270 1.005   1.00 103.51 ? 172  LEU B N     1 
ATOM   901  C  CA    . LEU A 1 130 ? 19.790  -20.476 1.696   1.00 88.25  ? 172  LEU B CA    1 
ATOM   902  C  C     . LEU A 1 130 ? 18.464  -20.241 2.409   1.00 81.85  ? 172  LEU B C     1 
ATOM   903  O  O     . LEU A 1 130 ? 17.575  -21.102 2.384   1.00 77.29  ? 172  LEU B O     1 
ATOM   904  C  CB    . LEU A 1 130 ? 20.857  -20.939 2.688   1.00 86.01  ? 172  LEU B CB    1 
ATOM   905  C  CG    . LEU A 1 130 ? 22.181  -21.434 2.104   1.00 105.46 ? 172  LEU B CG    1 
ATOM   906  C  CD1   . LEU A 1 130 ? 23.231  -21.567 3.196   1.00 93.99  ? 172  LEU B CD1   1 
ATOM   907  C  CD2   . LEU A 1 130 ? 21.982  -22.761 1.392   1.00 107.50 ? 172  LEU B CD2   1 
ATOM   908  N  N     . ALA A 1 131 ? 18.310  -19.076 3.041   1.00 80.66  ? 173  ALA B N     1 
ATOM   909  C  CA    . ALA A 1 131 ? 17.083  -18.781 3.775   1.00 84.35  ? 173  ALA B CA    1 
ATOM   910  C  C     . ALA A 1 131 ? 15.882  -18.706 2.839   1.00 93.56  ? 173  ALA B C     1 
ATOM   911  O  O     . ALA A 1 131 ? 14.831  -19.301 3.108   1.00 98.66  ? 173  ALA B O     1 
ATOM   912  C  CB    . ALA A 1 131 ? 17.242  -17.476 4.556   1.00 84.50  ? 173  ALA B CB    1 
ATOM   913  N  N     . VAL A 1 132 ? 16.018  -17.984 1.725   1.00 107.73 ? 174  VAL B N     1 
ATOM   914  C  CA    . VAL A 1 132 ? 14.886  -17.856 0.811   1.00 90.35  ? 174  VAL B CA    1 
ATOM   915  C  C     . VAL A 1 132 ? 14.613  -19.178 0.096   1.00 81.01  ? 174  VAL B C     1 
ATOM   916  O  O     . VAL A 1 132 ? 13.461  -19.482 -0.245  1.00 86.27  ? 174  VAL B O     1 
ATOM   917  C  CB    . VAL A 1 132 ? 15.117  -16.695 -0.176  1.00 87.09  ? 174  VAL B CB    1 
ATOM   918  C  CG1   . VAL A 1 132 ? 16.343  -16.942 -1.025  1.00 102.55 ? 174  VAL B CG1   1 
ATOM   919  C  CG2   . VAL A 1 132 ? 13.886  -16.471 -1.048  1.00 97.04  ? 174  VAL B CG2   1 
ATOM   920  N  N     . ALA A 1 133 ? 15.646  -20.000 -0.117  1.00 76.50  ? 175  ALA B N     1 
ATOM   921  C  CA    . ALA A 1 133 ? 15.422  -21.319 -0.700  1.00 88.72  ? 175  ALA B CA    1 
ATOM   922  C  C     . ALA A 1 133 ? 14.662  -22.222 0.262   1.00 101.33 ? 175  ALA B C     1 
ATOM   923  O  O     . ALA A 1 133 ? 13.773  -22.973 -0.154  1.00 99.75  ? 175  ALA B O     1 
ATOM   924  C  CB    . ALA A 1 133 ? 16.755  -21.953 -1.094  1.00 92.97  ? 175  ALA B CB    1 
ATOM   925  N  N     . GLU A 1 134 ? 15.004  -22.168 1.552   1.00 103.30 ? 176  GLU B N     1 
ATOM   926  C  CA    . GLU A 1 134 ? 14.224  -22.889 2.553   1.00 110.31 ? 176  GLU B CA    1 
ATOM   927  C  C     . GLU A 1 134 ? 12.795  -22.366 2.606   1.00 101.33 ? 176  GLU B C     1 
ATOM   928  O  O     . GLU A 1 134 ? 11.850  -23.134 2.828   1.00 104.83 ? 176  GLU B O     1 
ATOM   929  C  CB    . GLU A 1 134 ? 14.892  -22.772 3.923   1.00 118.07 ? 176  GLU B CB    1 
ATOM   930  C  CG    . GLU A 1 134 ? 14.136  -23.460 5.049   1.00 129.12 ? 176  GLU B CG    1 
ATOM   931  C  CD    . GLU A 1 134 ? 14.765  -23.220 6.407   1.00 151.22 ? 176  GLU B CD    1 
ATOM   932  O  OE1   . GLU A 1 134 ? 15.804  -22.529 6.468   1.00 133.65 ? 176  GLU B OE1   1 
ATOM   933  O  OE2   . GLU A 1 134 ? 14.219  -23.720 7.413   1.00 165.89 ? 176  GLU B OE2   1 
ATOM   934  N  N     . ARG A 1 135 ? 12.619  -21.058 2.406   1.00 93.77  ? 177  ARG B N     1 
ATOM   935  C  CA    . ARG A 1 135 ? 11.277  -20.487 2.335   1.00 98.94  ? 177  ARG B CA    1 
ATOM   936  C  C     . ARG A 1 135 ? 10.474  -21.113 1.202   1.00 107.88 ? 177  ARG B C     1 
ATOM   937  O  O     . ARG A 1 135 ? 9.361   -21.609 1.412   1.00 115.24 ? 177  ARG B O     1 
ATOM   938  C  CB    . ARG A 1 135 ? 11.356  -18.971 2.155   1.00 97.81  ? 177  ARG B CB    1 
ATOM   939  C  CG    . ARG A 1 135 ? 10.026  -18.335 1.782   1.00 104.38 ? 177  ARG B CG    1 
ATOM   940  C  CD    . ARG A 1 135 ? 10.209  -16.930 1.234   1.00 100.40 ? 177  ARG B CD    1 
ATOM   941  N  NE    . ARG A 1 135 ? 8.951   -16.369 0.754   1.00 98.54  ? 177  ARG B NE    1 
ATOM   942  C  CZ    . ARG A 1 135 ? 8.832   -15.186 0.167   1.00 105.09 ? 177  ARG B CZ    1 
ATOM   943  N  NH1   . ARG A 1 135 ? 9.881   -14.404 -0.031  1.00 92.37  ? 177  ARG B NH1   1 
ATOM   944  N  NH2   . ARG A 1 135 ? 7.631   -14.777 -0.231  1.00 109.92 ? 177  ARG B NH2   1 
ATOM   945  N  N     . TYR A 1 136 ? 11.022  -21.096 -0.012  1.00 107.42 ? 178  TYR B N     1 
ATOM   946  C  CA    . TYR A 1 136 ? 10.323  -21.665 -1.158  1.00 112.05 ? 178  TYR B CA    1 
ATOM   947  C  C     . TYR A 1 136 ? 10.450  -23.181 -1.248  1.00 112.22 ? 178  TYR B C     1 
ATOM   948  O  O     . TYR A 1 136 ? 9.914   -23.774 -2.191  1.00 96.94  ? 178  TYR B O     1 
ATOM   949  C  CB    . TYR A 1 136 ? 10.820  -21.022 -2.456  1.00 103.79 ? 178  TYR B CB    1 
ATOM   950  C  CG    . TYR A 1 136 ? 10.088  -19.747 -2.809  1.00 96.39  ? 178  TYR B CG    1 
ATOM   951  C  CD1   . TYR A 1 136 ? 8.844   -19.790 -3.427  1.00 97.65  ? 178  TYR B CD1   1 
ATOM   952  C  CD2   . TYR A 1 136 ? 10.634  -18.503 -2.521  1.00 86.33  ? 178  TYR B CD2   1 
ATOM   953  C  CE1   . TYR A 1 136 ? 8.166   -18.631 -3.751  1.00 86.21  ? 178  TYR B CE1   1 
ATOM   954  C  CE2   . TYR A 1 136 ? 9.962   -17.337 -2.841  1.00 76.92  ? 178  TYR B CE2   1 
ATOM   955  C  CZ    . TYR A 1 136 ? 8.729   -17.408 -3.456  1.00 84.64  ? 178  TYR B CZ    1 
ATOM   956  O  OH    . TYR A 1 136 ? 8.055   -16.253 -3.778  1.00 100.29 ? 178  TYR B OH    1 
ATOM   957  N  N     . GLY A 1 137 ? 11.131  -23.819 -0.300  1.00 107.81 ? 179  GLY B N     1 
ATOM   958  C  CA    . GLY A 1 137 ? 11.227  -25.265 -0.278  1.00 109.62 ? 179  GLY B CA    1 
ATOM   959  C  C     . GLY A 1 137 ? 12.107  -25.840 -1.369  1.00 100.11 ? 179  GLY B C     1 
ATOM   960  O  O     . GLY A 1 137 ? 11.697  -26.755 -2.089  1.00 93.75  ? 179  GLY B O     1 
ATOM   961  N  N     . LEU A 1 138 ? 13.320  -25.312 -1.499  1.00 98.30  ? 180  LEU B N     1 
ATOM   962  C  CA    . LEU A 1 138 ? 14.284  -25.786 -2.479  1.00 92.73  ? 180  LEU B CA    1 
ATOM   963  C  C     . LEU A 1 138 ? 15.517  -26.329 -1.770  1.00 89.46  ? 180  LEU B C     1 
ATOM   964  O  O     . LEU A 1 138 ? 15.774  -26.026 -0.602  1.00 101.25 ? 180  LEU B O     1 
ATOM   965  C  CB    . LEU A 1 138 ? 14.693  -24.671 -3.454  1.00 97.51  ? 180  LEU B CB    1 
ATOM   966  C  CG    . LEU A 1 138 ? 13.796  -24.406 -4.668  1.00 108.22 ? 180  LEU B CG    1 
ATOM   967  C  CD1   . LEU A 1 138 ? 12.439  -23.863 -4.253  1.00 106.18 ? 180  LEU B CD1   1 
ATOM   968  C  CD2   . LEU A 1 138 ? 14.482  -23.455 -5.638  1.00 94.04  ? 180  LEU B CD2   1 
ATOM   969  N  N     . SER A 1 139 ? 16.281  -27.141 -2.496  1.00 94.39  ? 181  SER B N     1 
ATOM   970  C  CA    . SER A 1 139 ? 17.519  -27.691 -1.960  1.00 105.30 ? 181  SER B CA    1 
ATOM   971  C  C     . SER A 1 139 ? 18.552  -26.582 -1.811  1.00 110.78 ? 181  SER B C     1 
ATOM   972  O  O     . SER A 1 139 ? 18.881  -25.895 -2.784  1.00 123.35 ? 181  SER B O     1 
ATOM   973  C  CB    . SER A 1 139 ? 18.044  -28.798 -2.872  1.00 119.94 ? 181  SER B CB    1 
ATOM   974  O  OG    . SER A 1 139 ? 19.268  -29.320 -2.386  1.00 136.77 ? 181  SER B OG    1 
ATOM   975  N  N     . GLY A 1 140 ? 19.061  -26.405 -0.590  1.00 113.10 ? 182  GLY B N     1 
ATOM   976  C  CA    . GLY A 1 140 ? 20.039  -25.358 -0.349  1.00 116.96 ? 182  GLY B CA    1 
ATOM   977  C  C     . GLY A 1 140 ? 21.337  -25.565 -1.102  1.00 123.43 ? 182  GLY B C     1 
ATOM   978  O  O     . GLY A 1 140 ? 22.020  -24.597 -1.448  1.00 122.05 ? 182  GLY B O     1 
ATOM   979  N  N     . SER A 1 141 ? 21.698  -26.822 -1.365  1.00 126.00 ? 183  SER B N     1 
ATOM   980  C  CA    . SER A 1 141 ? 22.911  -27.100 -2.124  1.00 130.19 ? 183  SER B CA    1 
ATOM   981  C  C     . SER A 1 141 ? 22.720  -26.854 -3.615  1.00 130.66 ? 183  SER B C     1 
ATOM   982  O  O     . SER A 1 141 ? 23.683  -26.510 -4.309  1.00 129.58 ? 183  SER B O     1 
ATOM   983  C  CB    . SER A 1 141 ? 23.363  -28.541 -1.884  1.00 133.31 ? 183  SER B CB    1 
ATOM   984  O  OG    . SER A 1 141 ? 24.542  -28.835 -2.613  1.00 137.61 ? 183  SER B OG    1 
ATOM   985  N  N     . ASP A 1 142 ? 21.496  -27.017 -4.121  1.00 124.52 ? 184  ASP B N     1 
ATOM   986  C  CA    . ASP A 1 142 ? 21.248  -26.817 -5.544  1.00 133.72 ? 184  ASP B CA    1 
ATOM   987  C  C     . ASP A 1 142 ? 21.141  -25.338 -5.896  1.00 129.06 ? 184  ASP B C     1 
ATOM   988  O  O     . ASP A 1 142 ? 21.581  -24.921 -6.973  1.00 121.60 ? 184  ASP B O     1 
ATOM   989  C  CB    . ASP A 1 142 ? 19.976  -27.555 -5.966  1.00 145.32 ? 184  ASP B CB    1 
ATOM   990  C  CG    . ASP A 1 142 ? 20.069  -29.051 -5.741  1.00 149.93 ? 184  ASP B CG    1 
ATOM   991  O  OD1   . ASP A 1 142 ? 21.077  -29.506 -5.160  1.00 148.04 ? 184  ASP B OD1   1 
ATOM   992  O  OD2   . ASP A 1 142 ? 19.133  -29.773 -6.147  1.00 148.97 ? 184  ASP B OD2   1 
ATOM   993  N  N     . VAL A 1 143 ? 20.561  -24.531 -5.004  1.00 122.42 ? 185  VAL B N     1 
ATOM   994  C  CA    . VAL A 1 143 ? 20.403  -23.110 -5.295  1.00 105.01 ? 185  VAL B CA    1 
ATOM   995  C  C     . VAL A 1 143 ? 21.746  -22.394 -5.250  1.00 101.76 ? 185  VAL B C     1 
ATOM   996  O  O     . VAL A 1 143 ? 21.935  -21.375 -5.925  1.00 113.35 ? 185  VAL B O     1 
ATOM   997  C  CB    . VAL A 1 143 ? 19.388  -22.472 -4.328  1.00 86.58  ? 185  VAL B CB    1 
ATOM   998  C  CG1   . VAL A 1 143 ? 18.022  -23.118 -4.493  1.00 85.39  ? 185  VAL B CG1   1 
ATOM   999  C  CG2   . VAL A 1 143 ? 19.870  -22.592 -2.892  1.00 115.97 ? 185  VAL B CG2   1 
ATOM   1000 N  N     . LEU A 1 144 ? 22.699  -22.905 -4.468  1.00 107.55 ? 186  LEU B N     1 
ATOM   1001 C  CA    . LEU A 1 144 ? 24.023  -22.301 -4.413  1.00 110.07 ? 186  LEU B CA    1 
ATOM   1002 C  C     . LEU A 1 144 ? 24.898  -22.703 -5.592  1.00 109.79 ? 186  LEU B C     1 
ATOM   1003 O  O     . LEU A 1 144 ? 25.866  -21.998 -5.897  1.00 111.28 ? 186  LEU B O     1 
ATOM   1004 C  CB    . LEU A 1 144 ? 24.720  -22.668 -3.100  1.00 114.75 ? 186  LEU B CB    1 
ATOM   1005 C  CG    . LEU A 1 144 ? 24.644  -21.629 -1.978  1.00 101.81 ? 186  LEU B CG    1 
ATOM   1006 C  CD1   . LEU A 1 144 ? 23.204  -21.236 -1.683  1.00 102.00 ? 186  LEU B CD1   1 
ATOM   1007 C  CD2   . LEU A 1 144 ? 25.331  -22.143 -0.721  1.00 122.27 ? 186  LEU B CD2   1 
ATOM   1008 N  N     . ASP A 1 145 ? 24.582  -23.813 -6.258  1.00 107.56 ? 187  ASP B N     1 
ATOM   1009 C  CA    . ASP A 1 145 ? 25.306  -24.216 -7.455  1.00 123.88 ? 187  ASP B CA    1 
ATOM   1010 C  C     . ASP A 1 145 ? 24.762  -23.568 -8.720  1.00 119.58 ? 187  ASP B C     1 
ATOM   1011 O  O     . ASP A 1 145 ? 25.473  -23.520 -9.731  1.00 119.66 ? 187  ASP B O     1 
ATOM   1012 C  CB    . ASP A 1 145 ? 25.270  -25.740 -7.611  1.00 134.48 ? 187  ASP B CB    1 
ATOM   1013 C  CG    . ASP A 1 145 ? 25.933  -26.461 -6.453  1.00 136.90 ? 187  ASP B CG    1 
ATOM   1014 O  OD1   . ASP A 1 145 ? 26.825  -25.866 -5.812  1.00 131.46 ? 187  ASP B OD1   1 
ATOM   1015 O  OD2   . ASP A 1 145 ? 25.564  -27.624 -6.184  1.00 134.66 ? 187  ASP B OD2   1 
ATOM   1016 N  N     . ASN A 1 146 ? 23.525  -23.070 -8.688  1.00 111.27 ? 188  ASN B N     1 
ATOM   1017 C  CA    . ASN A 1 146 ? 22.910  -22.404 -9.827  1.00 99.74  ? 188  ASN B CA    1 
ATOM   1018 C  C     . ASN A 1 146 ? 22.983  -20.884 -9.722  1.00 96.95  ? 188  ASN B C     1 
ATOM   1019 O  O     . ASN A 1 146 ? 22.159  -20.187 -10.323 1.00 96.36  ? 188  ASN B O     1 
ATOM   1020 C  CB    . ASN A 1 146 ? 21.456  -22.853 -9.980  1.00 97.74  ? 188  ASN B CB    1 
ATOM   1021 C  CG    . ASN A 1 146 ? 21.334  -24.315 -10.363 1.00 113.57 ? 188  ASN B CG    1 
ATOM   1022 O  OD1   . ASN A 1 146 ? 22.211  -24.871 -11.025 1.00 117.19 ? 188  ASN B OD1   1 
ATOM   1023 N  ND2   . ASN A 1 146 ? 20.241  -24.946 -9.950  1.00 106.64 ? 188  ASN B ND2   1 
ATOM   1024 N  N     . VAL A 1 147 ? 23.945  -20.358 -8.967  1.00 83.14  ? 189  VAL B N     1 
ATOM   1025 C  CA    . VAL A 1 147 ? 24.148  -18.920 -8.825  1.00 95.12  ? 189  VAL B CA    1 
ATOM   1026 C  C     . VAL A 1 147 ? 25.631  -18.646 -9.034  1.00 105.84 ? 189  VAL B C     1 
ATOM   1027 O  O     . VAL A 1 147 ? 26.459  -19.003 -8.187  1.00 101.89 ? 189  VAL B O     1 
ATOM   1028 C  CB    . VAL A 1 147 ? 23.681  -18.394 -7.460  1.00 87.50  ? 189  VAL B CB    1 
ATOM   1029 C  CG1   . VAL A 1 147 ? 24.134  -16.955 -7.263  1.00 83.24  ? 189  VAL B CG1   1 
ATOM   1030 C  CG2   . VAL A 1 147 ? 22.168  -18.490 -7.347  1.00 78.14  ? 189  VAL B CG2   1 
ATOM   1031 N  N     . ALA A 1 148 ? 25.967  -18.018 -10.158 1.00 92.31  ? 190  ALA B N     1 
ATOM   1032 C  CA    . ALA A 1 148 ? 27.348  -17.672 -10.479 1.00 96.92  ? 190  ALA B CA    1 
ATOM   1033 C  C     . ALA A 1 148 ? 27.655  -16.297 -9.896  1.00 96.68  ? 190  ALA B C     1 
ATOM   1034 O  O     . ALA A 1 148 ? 27.145  -15.283 -10.380 1.00 109.53 ? 190  ALA B O     1 
ATOM   1035 C  CB    . ALA A 1 148 ? 27.574  -17.695 -11.989 1.00 98.59  ? 190  ALA B CB    1 
ATOM   1036 N  N     . TYR A 1 149 ? 28.488  -16.263 -8.861  1.00 87.45  ? 191  TYR B N     1 
ATOM   1037 C  CA    . TYR A 1 149 ? 28.827  -15.032 -8.161  1.00 93.61  ? 191  TYR B CA    1 
ATOM   1038 C  C     . TYR A 1 149 ? 30.217  -14.555 -8.561  1.00 96.30  ? 191  TYR B C     1 
ATOM   1039 O  O     . TYR A 1 149 ? 31.146  -15.357 -8.696  1.00 102.54 ? 191  TYR B O     1 
ATOM   1040 C  CB    . TYR A 1 149 ? 28.760  -15.237 -6.646  1.00 100.25 ? 191  TYR B CB    1 
ATOM   1041 C  CG    . TYR A 1 149 ? 29.628  -14.290 -5.847  1.00 93.36  ? 191  TYR B CG    1 
ATOM   1042 C  CD1   . TYR A 1 149 ? 29.278  -12.954 -5.694  1.00 92.42  ? 191  TYR B CD1   1 
ATOM   1043 C  CD2   . TYR A 1 149 ? 30.793  -14.735 -5.234  1.00 93.72  ? 191  TYR B CD2   1 
ATOM   1044 C  CE1   . TYR A 1 149 ? 30.068  -12.087 -4.962  1.00 112.95 ? 191  TYR B CE1   1 
ATOM   1045 C  CE2   . TYR A 1 149 ? 31.589  -13.876 -4.500  1.00 98.73  ? 191  TYR B CE2   1 
ATOM   1046 C  CZ    . TYR A 1 149 ? 31.222  -12.554 -4.366  1.00 116.13 ? 191  TYR B CZ    1 
ATOM   1047 O  OH    . TYR A 1 149 ? 32.010  -11.695 -3.635  1.00 105.98 ? 191  TYR B OH    1 
ATOM   1048 N  N     . ALA A 1 150 ? 30.356  -13.244 -8.746  1.00 79.59  ? 192  ALA B N     1 
ATOM   1049 C  CA    . ALA A 1 150 ? 31.648  -12.663 -9.089  1.00 95.05  ? 192  ALA B CA    1 
ATOM   1050 C  C     . ALA A 1 150 ? 31.779  -11.292 -8.446  1.00 104.27 ? 192  ALA B C     1 
ATOM   1051 O  O     . ALA A 1 150 ? 30.906  -10.437 -8.619  1.00 100.57 ? 192  ALA B O     1 
ATOM   1052 C  CB    . ALA A 1 150 ? 31.822  -12.555 -10.606 1.00 107.89 ? 192  ALA B CB    1 
ATOM   1053 N  N     . ARG A 1 151 ? 32.872  -11.089 -7.714  1.00 109.81 ? 193  ARG B N     1 
ATOM   1054 C  CA    . ARG A 1 151 ? 33.159  -9.809  -7.079  1.00 105.88 ? 193  ARG B CA    1 
ATOM   1055 C  C     . ARG A 1 151 ? 34.018  -8.958  -8.005  1.00 105.56 ? 193  ARG B C     1 
ATOM   1056 O  O     . ARG A 1 151 ? 35.015  -9.438  -8.554  1.00 109.80 ? 193  ARG B O     1 
ATOM   1057 C  CB    . ARG A 1 151 ? 33.870  -10.017 -5.741  1.00 100.25 ? 193  ARG B CB    1 
ATOM   1058 C  CG    . ARG A 1 151 ? 34.320  -8.728  -5.070  1.00 104.17 ? 193  ARG B CG    1 
ATOM   1059 C  CD    . ARG A 1 151 ? 33.134  -7.890  -4.621  1.00 111.84 ? 193  ARG B CD    1 
ATOM   1060 N  NE    . ARG A 1 151 ? 33.527  -6.528  -4.278  1.00 113.27 ? 193  ARG B NE    1 
ATOM   1061 C  CZ    . ARG A 1 151 ? 34.020  -6.162  -3.102  1.00 110.99 ? 193  ARG B CZ    1 
ATOM   1062 N  NH1   . ARG A 1 151 ? 34.204  -7.037  -2.126  1.00 108.68 ? 193  ARG B NH1   1 
ATOM   1063 N  NH2   . ARG A 1 151 ? 34.338  -4.886  -2.901  1.00 106.89 ? 193  ARG B NH2   1 
ATOM   1064 N  N     . ALA A 1 152 ? 33.630  -7.697  -8.174  1.00 97.95  ? 194  ALA B N     1 
ATOM   1065 C  CA    . ALA A 1 152 ? 34.344  -6.756  -9.024  1.00 102.32 ? 194  ALA B CA    1 
ATOM   1066 C  C     . ALA A 1 152 ? 35.003  -5.682  -8.171  1.00 105.86 ? 194  ALA B C     1 
ATOM   1067 O  O     . ALA A 1 152 ? 34.410  -5.194  -7.203  1.00 114.82 ? 194  ALA B O     1 
ATOM   1068 C  CB    . ALA A 1 152 ? 33.402  -6.110  -10.044 1.00 99.05  ? 194  ALA B CB    1 
ATOM   1069 N  N     . PHE A 1 153 ? 36.233  -5.313  -8.536  1.00 116.49 ? 195  PHE B N     1 
ATOM   1070 C  CA    . PHE A 1 153 ? 36.986  -4.305  -7.804  1.00 108.18 ? 195  PHE B CA    1 
ATOM   1071 C  C     . PHE A 1 153 ? 37.218  -3.020  -8.586  1.00 113.19 ? 195  PHE B C     1 
ATOM   1072 O  O     . PHE A 1 153 ? 37.525  -1.994  -7.972  1.00 120.89 ? 195  PHE B O     1 
ATOM   1073 C  CB    . PHE A 1 153 ? 38.343  -4.872  -7.358  1.00 113.31 ? 195  PHE B CB    1 
ATOM   1074 C  CG    . PHE A 1 153 ? 38.230  -6.042  -6.420  1.00 117.66 ? 195  PHE B CG    1 
ATOM   1075 C  CD1   . PHE A 1 153 ? 38.060  -5.843  -5.060  1.00 109.68 ? 195  PHE B CD1   1 
ATOM   1076 C  CD2   . PHE A 1 153 ? 38.293  -7.341  -6.899  1.00 113.28 ? 195  PHE B CD2   1 
ATOM   1077 C  CE1   . PHE A 1 153 ? 37.955  -6.916  -4.194  1.00 111.10 ? 195  PHE B CE1   1 
ATOM   1078 C  CE2   . PHE A 1 153 ? 38.189  -8.419  -6.038  1.00 112.86 ? 195  PHE B CE2   1 
ATOM   1079 C  CZ    . PHE A 1 153 ? 38.019  -8.206  -4.684  1.00 103.86 ? 195  PHE B CZ    1 
ATOM   1080 N  N     . ASN A 1 154 ? 37.083  -3.048  -9.911  1.00 118.01 ? 196  ASN B N     1 
ATOM   1081 C  CA    . ASN A 1 154 ? 37.173  -1.839  -10.717 1.00 116.73 ? 196  ASN B CA    1 
ATOM   1082 C  C     . ASN A 1 154 ? 36.316  -2.018  -11.965 1.00 111.63 ? 196  ASN B C     1 
ATOM   1083 O  O     . ASN A 1 154 ? 35.784  -3.099  -12.229 1.00 110.22 ? 196  ASN B O     1 
ATOM   1084 C  CB    . ASN A 1 154 ? 38.628  -1.500  -11.071 1.00 108.56 ? 196  ASN B CB    1 
ATOM   1085 C  CG    . ASN A 1 154 ? 39.393  -2.686  -11.626 1.00 120.14 ? 196  ASN B CG    1 
ATOM   1086 O  OD1   . ASN A 1 154 ? 38.864  -3.474  -12.408 1.00 118.80 ? 196  ASN B OD1   1 
ATOM   1087 N  ND2   . ASN A 1 154 ? 40.650  -2.819  -11.219 1.00 112.21 ? 196  ASN B ND2   1 
ATOM   1088 N  N     . THR A 1 155 ? 36.187  -0.933  -12.732 1.00 103.67 ? 197  THR B N     1 
ATOM   1089 C  CA    . THR A 1 155 ? 35.289  -0.936  -13.884 1.00 110.24 ? 197  THR B CA    1 
ATOM   1090 C  C     . THR A 1 155 ? 35.773  -1.887  -14.973 1.00 113.61 ? 197  THR B C     1 
ATOM   1091 O  O     . THR A 1 155 ? 34.960  -2.534  -15.648 1.00 109.52 ? 197  THR B O     1 
ATOM   1092 C  CB    . THR A 1 155 ? 35.146  0.481   -14.437 1.00 113.23 ? 197  THR B CB    1 
ATOM   1093 O  OG1   . THR A 1 155 ? 36.430  0.964   -14.852 1.00 116.17 ? 197  THR B OG1   1 
ATOM   1094 C  CG2   . THR A 1 155 ? 34.585  1.411   -13.371 1.00 100.18 ? 197  THR B CG2   1 
ATOM   1095 N  N     . ASP A 1 156 ? 37.091  -1.979  -15.166 1.00 119.08 ? 198  ASP B N     1 
ATOM   1096 C  CA    . ASP A 1 156 ? 37.626  -2.908  -16.156 1.00 118.80 ? 198  ASP B CA    1 
ATOM   1097 C  C     . ASP A 1 156 ? 37.282  -4.347  -15.796 1.00 112.25 ? 198  ASP B C     1 
ATOM   1098 O  O     . ASP A 1 156 ? 36.876  -5.133  -16.662 1.00 109.33 ? 198  ASP B O     1 
ATOM   1099 C  CB    . ASP A 1 156 ? 39.138  -2.729  -16.281 1.00 120.77 ? 198  ASP B CB    1 
ATOM   1100 C  CG    . ASP A 1 156 ? 39.525  -1.332  -16.723 1.00 131.64 ? 198  ASP B CG    1 
ATOM   1101 O  OD1   . ASP A 1 156 ? 38.618  -0.489  -16.892 1.00 112.77 ? 198  ASP B OD1   1 
ATOM   1102 O  OD2   . ASP A 1 156 ? 40.734  -1.076  -16.903 1.00 143.32 ? 198  ASP B OD2   1 
ATOM   1103 N  N     . HIS A 1 157 ? 37.430  -4.709  -14.518 1.00 108.62 ? 199  HIS B N     1 
ATOM   1104 C  CA    . HIS A 1 157 ? 37.017  -6.036  -14.077 1.00 108.86 ? 199  HIS B CA    1 
ATOM   1105 C  C     . HIS A 1 157 ? 35.518  -6.233  -14.247 1.00 106.44 ? 199  HIS B C     1 
ATOM   1106 O  O     . HIS A 1 157 ? 35.072  -7.342  -14.545 1.00 94.69  ? 199  HIS B O     1 
ATOM   1107 C  CB    . HIS A 1 157 ? 37.421  -6.259  -12.619 1.00 118.43 ? 199  HIS B CB    1 
ATOM   1108 C  CG    . HIS A 1 157 ? 37.306  -7.683  -12.170 1.00 121.31 ? 199  HIS B CG    1 
ATOM   1109 N  ND1   . HIS A 1 157 ? 37.319  -8.047  -10.841 1.00 117.77 ? 199  HIS B ND1   1 
ATOM   1110 C  CD2   . HIS A 1 157 ? 37.182  -8.833  -12.874 1.00 118.22 ? 199  HIS B CD2   1 
ATOM   1111 C  CE1   . HIS A 1 157 ? 37.205  -9.360  -10.745 1.00 118.23 ? 199  HIS B CE1   1 
ATOM   1112 N  NE2   . HIS A 1 157 ? 37.120  -9.861  -11.964 1.00 125.69 ? 199  HIS B NE2   1 
ATOM   1113 N  N     . GLN A 1 158 ? 34.730  -5.168  -14.084 1.00 101.53 ? 200  GLN B N     1 
ATOM   1114 C  CA    . GLN A 1 158 ? 33.286  -5.265  -14.278 1.00 96.19  ? 200  GLN B CA    1 
ATOM   1115 C  C     . GLN A 1 158 ? 32.950  -5.608  -15.727 1.00 106.53 ? 200  GLN B C     1 
ATOM   1116 O  O     . GLN A 1 158 ? 32.132  -6.497  -16.002 1.00 109.33 ? 200  GLN B O     1 
ATOM   1117 C  CB    . GLN A 1 158 ? 32.632  -3.948  -13.858 1.00 93.52  ? 200  GLN B CB    1 
ATOM   1118 C  CG    . GLN A 1 158 ? 31.139  -4.011  -13.606 1.00 94.01  ? 200  GLN B CG    1 
ATOM   1119 C  CD    . GLN A 1 158 ? 30.602  -2.706  -13.044 1.00 92.78  ? 200  GLN B CD    1 
ATOM   1120 O  OE1   . GLN A 1 158 ? 31.367  -1.838  -12.625 1.00 83.08  ? 200  GLN B OE1   1 
ATOM   1121 N  NE2   . GLN A 1 158 ? 29.282  -2.563  -13.034 1.00 83.97  ? 200  GLN B NE2   1 
ATOM   1122 N  N     . THR A 1 159 ? 33.594  -4.922  -16.674 1.00 101.28 ? 201  THR B N     1 
ATOM   1123 C  CA    . THR A 1 159 ? 33.341  -5.211  -18.083 1.00 83.35  ? 201  THR B CA    1 
ATOM   1124 C  C     . THR A 1 159 ? 33.874  -6.588  -18.475 1.00 96.08  ? 201  THR B C     1 
ATOM   1125 O  O     . THR A 1 159 ? 33.262  -7.289  -19.291 1.00 105.84 ? 201  THR B O     1 
ATOM   1126 C  CB    . THR A 1 159 ? 33.951  -4.116  -18.958 1.00 105.44 ? 201  THR B CB    1 
ATOM   1127 O  OG1   . THR A 1 159 ? 33.461  -2.840  -18.529 1.00 92.96  ? 201  THR B OG1   1 
ATOM   1128 C  CG2   . THR A 1 159 ? 33.566  -4.323  -20.416 1.00 113.93 ? 201  THR B CG2   1 
ATOM   1129 N  N     . GLN A 1 160 ? 35.006  -7.001  -17.898 1.00 92.32  ? 202  GLN B N     1 
ATOM   1130 C  CA    . GLN A 1 160 ? 35.506  -8.349  -18.159 1.00 101.36 ? 202  GLN B CA    1 
ATOM   1131 C  C     . GLN A 1 160 ? 34.553  -9.400  -17.599 1.00 107.62 ? 202  GLN B C     1 
ATOM   1132 O  O     . GLN A 1 160 ? 34.379  -10.473 -18.191 1.00 93.39  ? 202  GLN B O     1 
ATOM   1133 C  CB    . GLN A 1 160 ? 36.908  -8.516  -17.571 1.00 109.28 ? 202  GLN B CB    1 
ATOM   1134 C  CG    . GLN A 1 160 ? 37.967  -7.652  -18.237 1.00 128.81 ? 202  GLN B CG    1 
ATOM   1135 C  CD    . GLN A 1 160 ? 38.163  -7.980  -19.705 1.00 132.32 ? 202  GLN B CD    1 
ATOM   1136 O  OE1   . GLN A 1 160 ? 37.901  -9.098  -20.147 1.00 123.13 ? 202  GLN B OE1   1 
ATOM   1137 N  NE2   . GLN A 1 160 ? 38.624  -6.998  -20.471 1.00 120.57 ? 202  GLN B NE2   1 
ATOM   1138 N  N     . LEU A 1 161 ? 33.921  -9.107  -16.461 1.00 120.69 ? 203  LEU B N     1 
ATOM   1139 C  CA    . LEU A 1 161 ? 32.894  -9.997  -15.935 1.00 114.90 ? 203  LEU B CA    1 
ATOM   1140 C  C     . LEU A 1 161 ? 31.696  -10.057 -16.870 1.00 109.63 ? 203  LEU B C     1 
ATOM   1141 O  O     . LEU A 1 161 ? 31.083  -11.114 -17.034 1.00 112.13 ? 203  LEU B O     1 
ATOM   1142 C  CB    . LEU A 1 161 ? 32.459  -9.546  -14.542 1.00 107.76 ? 203  LEU B CB    1 
ATOM   1143 C  CG    . LEU A 1 161 ? 33.450  -9.772  -13.401 1.00 103.41 ? 203  LEU B CG    1 
ATOM   1144 C  CD1   . LEU A 1 161 ? 32.856  -9.321  -12.073 1.00 112.52 ? 203  LEU B CD1   1 
ATOM   1145 C  CD2   . LEU A 1 161 ? 33.877  -11.228 -13.339 1.00 109.17 ? 203  LEU B CD2   1 
ATOM   1146 N  N     . LEU A 1 162 ? 31.344  -8.929  -17.492 1.00 110.12 ? 204  LEU B N     1 
ATOM   1147 C  CA    . LEU A 1 162 ? 30.271  -8.954  -18.485 1.00 98.30  ? 204  LEU B CA    1 
ATOM   1148 C  C     . LEU A 1 162 ? 30.645  -9.820  -19.686 1.00 110.87 ? 204  LEU B C     1 
ATOM   1149 O  O     . LEU A 1 162 ? 29.802  -10.550 -20.223 1.00 98.14  ? 204  LEU B O     1 
ATOM   1150 C  CB    . LEU A 1 162 ? 29.923  -7.537  -18.938 1.00 81.56  ? 204  LEU B CB    1 
ATOM   1151 C  CG    . LEU A 1 162 ? 28.689  -6.910  -18.286 1.00 86.23  ? 204  LEU B CG    1 
ATOM   1152 C  CD1   . LEU A 1 162 ? 28.131  -5.803  -19.165 1.00 97.89  ? 204  LEU B CD1   1 
ATOM   1153 C  CD2   . LEU A 1 162 ? 27.627  -7.961  -17.998 1.00 88.27  ? 204  LEU B CD2   1 
ATOM   1154 N  N     . TYR A 1 163 ? 31.902  -9.743  -20.127 1.00 116.15 ? 205  TYR B N     1 
ATOM   1155 C  CA    . TYR A 1 163 ? 32.352  -10.592 -21.230 1.00 101.12 ? 205  TYR B CA    1 
ATOM   1156 C  C     . TYR A 1 163 ? 32.280  -12.069 -20.850 1.00 107.38 ? 205  TYR B C     1 
ATOM   1157 O  O     . TYR A 1 163 ? 31.797  -12.905 -21.627 1.00 103.72 ? 205  TYR B O     1 
ATOM   1158 C  CB    . TYR A 1 163 ? 33.775  -10.216 -21.646 1.00 103.51 ? 205  TYR B CB    1 
ATOM   1159 C  CG    . TYR A 1 163 ? 33.870  -8.975  -22.505 1.00 104.26 ? 205  TYR B CG    1 
ATOM   1160 C  CD1   . TYR A 1 163 ? 33.329  -8.949  -23.784 1.00 102.10 ? 205  TYR B CD1   1 
ATOM   1161 C  CD2   . TYR A 1 163 ? 34.517  -7.836  -22.045 1.00 104.16 ? 205  TYR B CD2   1 
ATOM   1162 C  CE1   . TYR A 1 163 ? 33.417  -7.818  -24.575 1.00 111.32 ? 205  TYR B CE1   1 
ATOM   1163 C  CE2   . TYR A 1 163 ? 34.611  -6.701  -22.829 1.00 114.90 ? 205  TYR B CE2   1 
ATOM   1164 C  CZ    . TYR A 1 163 ? 34.060  -6.697  -24.092 1.00 120.34 ? 205  TYR B CZ    1 
ATOM   1165 O  OH    . TYR A 1 163 ? 34.153  -5.569  -24.874 1.00 119.43 ? 205  TYR B OH    1 
ATOM   1166 N  N     . GLN A 1 164 ? 32.764  -12.409 -19.653 1.00 114.05 ? 206  GLN B N     1 
ATOM   1167 C  CA    . GLN A 1 164 ? 32.679  -13.789 -19.186 1.00 98.72  ? 206  GLN B CA    1 
ATOM   1168 C  C     . GLN A 1 164 ? 31.229  -14.234 -19.031 1.00 97.55  ? 206  GLN B C     1 
ATOM   1169 O  O     . GLN A 1 164 ? 30.910  -15.405 -19.259 1.00 97.29  ? 206  GLN B O     1 
ATOM   1170 C  CB    . GLN A 1 164 ? 33.435  -13.941 -17.865 1.00 113.96 ? 206  GLN B CB    1 
ATOM   1171 C  CG    . GLN A 1 164 ? 33.571  -15.375 -17.381 1.00 115.28 ? 206  GLN B CG    1 
ATOM   1172 C  CD    . GLN A 1 164 ? 34.486  -15.498 -16.177 1.00 125.20 ? 206  GLN B CD    1 
ATOM   1173 O  OE1   . GLN A 1 164 ? 34.670  -16.586 -15.631 1.00 136.86 ? 206  GLN B OE1   1 
ATOM   1174 N  NE2   . GLN A 1 164 ? 35.067  -14.380 -15.758 1.00 114.56 ? 206  GLN B NE2   1 
ATOM   1175 N  N     . ALA A 1 165 ? 30.338  -13.312 -18.666 1.00 94.39  ? 207  ALA B N     1 
ATOM   1176 C  CA    . ALA A 1 165 ? 28.916  -13.625 -18.582 1.00 96.65  ? 207  ALA B CA    1 
ATOM   1177 C  C     . ALA A 1 165 ? 28.342  -13.949 -19.953 1.00 107.12 ? 207  ALA B C     1 
ATOM   1178 O  O     . ALA A 1 165 ? 27.561  -14.897 -20.101 1.00 103.56 ? 207  ALA B O     1 
ATOM   1179 C  CB    . ALA A 1 165 ? 28.167  -12.450 -17.957 1.00 104.54 ? 207  ALA B CB    1 
ATOM   1180 N  N     . SER A 1 166 ? 28.694  -13.147 -20.960 1.00 96.39  ? 208  SER B N     1 
ATOM   1181 C  CA    . SER A 1 166 ? 28.272  -13.443 -22.325 1.00 108.65 ? 208  SER B CA    1 
ATOM   1182 C  C     . SER A 1 166 ? 28.801  -14.798 -22.774 1.00 109.01 ? 208  SER B C     1 
ATOM   1183 O  O     . SER A 1 166 ? 28.114  -15.539 -23.488 1.00 115.57 ? 208  SER B O     1 
ATOM   1184 C  CB    . SER A 1 166 ? 28.744  -12.342 -23.273 1.00 120.05 ? 208  SER B CB    1 
ATOM   1185 O  OG    . SER A 1 166 ? 30.159  -12.267 -23.306 1.00 122.81 ? 208  SER B OG    1 
ATOM   1186 N  N     . ALA A 1 167 ? 30.022  -15.140 -22.359 1.00 103.60 ? 209  ALA B N     1 
ATOM   1187 C  CA    . ALA A 1 167 ? 30.585  -16.438 -22.721 1.00 108.84 ? 209  ALA B CA    1 
ATOM   1188 C  C     . ALA A 1 167 ? 29.861  -17.579 -22.014 1.00 111.63 ? 209  ALA B C     1 
ATOM   1189 O  O     . ALA A 1 167 ? 29.695  -18.664 -22.583 1.00 110.37 ? 209  ALA B O     1 
ATOM   1190 C  CB    . ALA A 1 167 ? 32.078  -16.469 -22.397 1.00 114.64 ? 209  ALA B CB    1 
ATOM   1191 N  N     . MET A 1 168 ? 29.425  -17.354 -20.773 1.00 105.20 ? 210  MET B N     1 
ATOM   1192 C  CA    . MET A 1 168 ? 28.795  -18.414 -19.991 1.00 102.86 ? 210  MET B CA    1 
ATOM   1193 C  C     . MET A 1 168 ? 27.334  -18.633 -20.362 1.00 108.52 ? 210  MET B C     1 
ATOM   1194 O  O     . MET A 1 168 ? 26.841  -19.762 -20.268 1.00 105.35 ? 210  MET B O     1 
ATOM   1195 C  CB    . MET A 1 168 ? 28.896  -18.098 -18.499 1.00 106.47 ? 210  MET B CB    1 
ATOM   1196 C  CG    . MET A 1 168 ? 30.291  -18.227 -17.922 1.00 116.78 ? 210  MET B CG    1 
ATOM   1197 S  SD    . MET A 1 168 ? 30.429  -17.453 -16.302 1.00 126.94 ? 210  MET B SD    1 
ATOM   1198 C  CE    . MET A 1 168 ? 29.120  -18.288 -15.410 1.00 103.51 ? 210  MET B CE    1 
ATOM   1199 N  N     . MET A 1 169 ? 26.627  -17.579 -20.777 1.00 112.81 ? 211  MET B N     1 
ATOM   1200 C  CA    . MET A 1 169 ? 25.185  -17.678 -20.978 1.00 107.97 ? 211  MET B CA    1 
ATOM   1201 C  C     . MET A 1 169 ? 24.788  -18.563 -22.154 1.00 102.64 ? 211  MET B C     1 
ATOM   1202 O  O     . MET A 1 169 ? 23.590  -18.801 -22.342 1.00 88.18  ? 211  MET B O     1 
ATOM   1203 C  CB    . MET A 1 169 ? 24.583  -16.284 -21.165 1.00 100.73 ? 211  MET B CB    1 
ATOM   1204 C  CG    . MET A 1 169 ? 24.468  -15.479 -19.881 1.00 94.66  ? 211  MET B CG    1 
ATOM   1205 S  SD    . MET A 1 169 ? 23.785  -13.832 -20.149 1.00 105.85 ? 211  MET B SD    1 
ATOM   1206 C  CE    . MET A 1 169 ? 23.828  -13.172 -18.485 1.00 107.49 ? 211  MET B CE    1 
ATOM   1207 N  N     . VAL A 1 170 ? 25.741  -19.058 -22.940 1.00 102.64 ? 212  VAL B N     1 
ATOM   1208 C  CA    . VAL A 1 170 ? 25.390  -19.890 -24.086 1.00 108.97 ? 212  VAL B CA    1 
ATOM   1209 C  C     . VAL A 1 170 ? 25.389  -21.379 -23.737 1.00 107.14 ? 212  VAL B C     1 
ATOM   1210 O  O     . VAL A 1 170 ? 24.573  -22.137 -24.273 1.00 118.09 ? 212  VAL B O     1 
ATOM   1211 C  CB    . VAL A 1 170 ? 26.330  -19.591 -25.269 1.00 104.01 ? 212  VAL B CB    1 
ATOM   1212 C  CG1   . VAL A 1 170 ? 27.775  -19.859 -24.890 1.00 112.94 ? 212  VAL B CG1   1 
ATOM   1213 C  CG2   . VAL A 1 170 ? 25.931  -20.399 -26.498 1.00 91.55  ? 212  VAL B CG2   1 
ATOM   1214 N  N     . GLU A 1 171 ? 26.272  -21.817 -22.838 1.00 98.43  ? 213  GLU B N     1 
ATOM   1215 C  CA    . GLU A 1 171 ? 26.306  -23.227 -22.460 1.00 91.71  ? 213  GLU B CA    1 
ATOM   1216 C  C     . GLU A 1 171 ? 25.106  -23.588 -21.593 1.00 95.61  ? 213  GLU B C     1 
ATOM   1217 O  O     . GLU A 1 171 ? 24.284  -24.433 -21.966 1.00 107.26 ? 213  GLU B O     1 
ATOM   1218 C  CB    . GLU A 1 171 ? 27.614  -23.546 -21.734 1.00 89.99  ? 213  GLU B CB    1 
ATOM   1219 C  CG    . GLU A 1 171 ? 28.859  -23.357 -22.581 1.00 101.39 ? 213  GLU B CG    1 
ATOM   1220 C  CD    . GLU A 1 171 ? 30.124  -23.786 -21.863 1.00 113.23 ? 213  GLU B CD    1 
ATOM   1221 O  OE1   . GLU A 1 171 ? 30.016  -24.382 -20.771 1.00 115.27 ? 213  GLU B OE1   1 
ATOM   1222 O  OE2   . GLU A 1 171 ? 31.226  -23.526 -22.391 1.00 112.48 ? 213  GLU B OE2   1 
ATOM   1223 N  N     . SER A 1 172 ? 24.990  -22.956 -20.430 1.00 108.04 ? 214  SER B N     1 
ATOM   1224 C  CA    . SER A 1 172 ? 23.886  -23.195 -19.514 1.00 105.32 ? 214  SER B CA    1 
ATOM   1225 C  C     . SER A 1 172 ? 22.850  -22.085 -19.637 1.00 103.82 ? 214  SER B C     1 
ATOM   1226 O  O     . SER A 1 172 ? 23.165  -20.954 -20.018 1.00 106.02 ? 214  SER B O     1 
ATOM   1227 C  CB    . SER A 1 172 ? 24.387  -23.289 -18.072 1.00 115.84 ? 214  SER B CB    1 
ATOM   1228 O  OG    . SER A 1 172 ? 25.320  -24.346 -17.925 1.00 122.27 ? 214  SER B OG    1 
ATOM   1229 N  N     . ARG A 1 173 ? 21.606  -22.419 -19.306 1.00 89.47  ? 215  ARG B N     1 
ATOM   1230 C  CA    . ARG A 1 173 ? 20.485  -21.496 -19.452 1.00 84.63  ? 215  ARG B CA    1 
ATOM   1231 C  C     . ARG A 1 173 ? 20.388  -20.620 -18.209 1.00 100.95 ? 215  ARG B C     1 
ATOM   1232 O  O     . ARG A 1 173 ? 20.075  -21.108 -17.117 1.00 94.35  ? 215  ARG B O     1 
ATOM   1233 C  CB    . ARG A 1 173 ? 19.185  -22.261 -19.689 1.00 90.46  ? 215  ARG B CB    1 
ATOM   1234 C  CG    . ARG A 1 173 ? 17.948  -21.378 -19.729 1.00 93.17  ? 215  ARG B CG    1 
ATOM   1235 C  CD    . ARG A 1 173 ? 16.754  -22.123 -20.302 1.00 118.18 ? 215  ARG B CD    1 
ATOM   1236 N  NE    . ARG A 1 173 ? 15.538  -21.319 -20.264 1.00 130.77 ? 215  ARG B NE    1 
ATOM   1237 C  CZ    . ARG A 1 173 ? 14.619  -21.400 -19.312 1.00 113.37 ? 215  ARG B CZ    1 
ATOM   1238 N  NH1   . ARG A 1 173 ? 14.739  -22.250 -18.306 1.00 103.21 ? 215  ARG B NH1   1 
ATOM   1239 N  NH2   . ARG A 1 173 ? 13.550  -20.611 -19.373 1.00 117.12 ? 215  ARG B NH2   1 
ATOM   1240 N  N     . TYR A 1 174 ? 20.656  -19.330 -18.374 1.00 95.34  ? 216  TYR B N     1 
ATOM   1241 C  CA    . TYR A 1 174 ? 20.476  -18.345 -17.320 1.00 65.68  ? 216  TYR B CA    1 
ATOM   1242 C  C     . TYR A 1 174 ? 19.213  -17.533 -17.578 1.00 78.56  ? 216  TYR B C     1 
ATOM   1243 O  O     . TYR A 1 174 ? 18.810  -17.323 -18.725 1.00 100.98 ? 216  TYR B O     1 
ATOM   1244 C  CB    . TYR A 1 174 ? 21.682  -17.408 -17.224 1.00 79.89  ? 216  TYR B CB    1 
ATOM   1245 C  CG    . TYR A 1 174 ? 22.906  -18.032 -16.594 1.00 97.15  ? 216  TYR B CG    1 
ATOM   1246 C  CD1   . TYR A 1 174 ? 23.845  -18.703 -17.367 1.00 95.14  ? 216  TYR B CD1   1 
ATOM   1247 C  CD2   . TYR A 1 174 ? 23.126  -17.945 -15.226 1.00 95.51  ? 216  TYR B CD2   1 
ATOM   1248 C  CE1   . TYR A 1 174 ? 24.966  -19.273 -16.794 1.00 104.40 ? 216  TYR B CE1   1 
ATOM   1249 C  CE2   . TYR A 1 174 ? 24.244  -18.512 -14.644 1.00 94.10  ? 216  TYR B CE2   1 
ATOM   1250 C  CZ    . TYR A 1 174 ? 25.160  -19.173 -15.432 1.00 102.38 ? 216  TYR B CZ    1 
ATOM   1251 O  OH    . TYR A 1 174 ? 26.274  -19.740 -14.856 1.00 101.73 ? 216  TYR B OH    1 
ATOM   1252 N  N     . ALA A 1 175 ? 18.588  -17.077 -16.493 1.00 82.80  ? 217  ALA B N     1 
ATOM   1253 C  CA    . ALA A 1 175 ? 17.394  -16.253 -16.579 1.00 74.80  ? 217  ALA B CA    1 
ATOM   1254 C  C     . ALA A 1 175 ? 17.535  -14.893 -15.916 1.00 74.16  ? 217  ALA B C     1 
ATOM   1255 O  O     . ALA A 1 175 ? 16.730  -14.000 -16.206 1.00 84.26  ? 217  ALA B O     1 
ATOM   1256 C  CB    . ALA A 1 175 ? 16.190  -16.980 -15.957 1.00 83.70  ? 217  ALA B CB    1 
ATOM   1257 N  N     . LEU A 1 176 ? 18.533  -14.701 -15.055 1.00 63.08  ? 218  LEU B N     1 
ATOM   1258 C  CA    . LEU A 1 176 ? 18.683  -13.463 -14.303 1.00 71.50  ? 218  LEU B CA    1 
ATOM   1259 C  C     . LEU A 1 176 ? 20.151  -13.071 -14.254 1.00 68.69  ? 218  LEU B C     1 
ATOM   1260 O  O     . LEU A 1 176 ? 21.014  -13.915 -13.997 1.00 72.78  ? 218  LEU B O     1 
ATOM   1261 C  CB    . LEU A 1 176 ? 18.127  -13.617 -12.884 1.00 78.36  ? 218  LEU B CB    1 
ATOM   1262 C  CG    . LEU A 1 176 ? 18.196  -12.396 -11.968 1.00 76.28  ? 218  LEU B CG    1 
ATOM   1263 C  CD1   . LEU A 1 176 ? 17.332  -11.269 -12.506 1.00 70.17  ? 218  LEU B CD1   1 
ATOM   1264 C  CD2   . LEU A 1 176 ? 17.767  -12.780 -10.567 1.00 83.04  ? 218  LEU B CD2   1 
ATOM   1265 N  N     . LEU A 1 177 ? 20.426  -11.792 -14.505 1.00 68.71  ? 219  LEU B N     1 
ATOM   1266 C  CA    . LEU A 1 177 ? 21.765  -11.222 -14.388 1.00 67.02  ? 219  LEU B CA    1 
ATOM   1267 C  C     . LEU A 1 177 ? 21.679  -10.018 -13.460 1.00 79.74  ? 219  LEU B C     1 
ATOM   1268 O  O     . LEU A 1 177 ? 21.045  -9.013  -13.798 1.00 78.53  ? 219  LEU B O     1 
ATOM   1269 C  CB    . LEU A 1 177 ? 22.325  -10.822 -15.754 1.00 72.23  ? 219  LEU B CB    1 
ATOM   1270 C  CG    . LEU A 1 177 ? 23.632  -10.025 -15.735 1.00 70.99  ? 219  LEU B CG    1 
ATOM   1271 C  CD1   . LEU A 1 177 ? 24.729  -10.794 -15.016 1.00 73.72  ? 219  LEU B CD1   1 
ATOM   1272 C  CD2   . LEU A 1 177 ? 24.065  -9.664  -17.149 1.00 72.68  ? 219  LEU B CD2   1 
ATOM   1273 N  N     . ILE A 1 178 ? 22.316  -10.119 -12.297 1.00 70.14  ? 220  ILE B N     1 
ATOM   1274 C  CA    . ILE A 1 178 ? 22.254  -9.094  -11.262 1.00 66.68  ? 220  ILE B CA    1 
ATOM   1275 C  C     . ILE A 1 178 ? 23.567  -8.327  -11.251 1.00 71.10  ? 220  ILE B C     1 
ATOM   1276 O  O     . ILE A 1 178 ? 24.647  -8.930  -11.214 1.00 82.76  ? 220  ILE B O     1 
ATOM   1277 C  CB    . ILE A 1 178 ? 21.968  -9.707  -9.881  1.00 82.07  ? 220  ILE B CB    1 
ATOM   1278 C  CG1   . ILE A 1 178 ? 20.629  -10.442 -9.892  1.00 71.35  ? 220  ILE B CG1   1 
ATOM   1279 C  CG2   . ILE A 1 178 ? 21.981  -8.633  -8.808  1.00 66.12  ? 220  ILE B CG2   1 
ATOM   1280 C  CD1   . ILE A 1 178 ? 20.328  -11.155 -8.601  1.00 70.79  ? 220  ILE B CD1   1 
ATOM   1281 N  N     . VAL A 1 179 ? 23.473  -7.004  -11.284 1.00 69.82  ? 221  VAL B N     1 
ATOM   1282 C  CA    . VAL A 1 179 ? 24.629  -6.121  -11.145 1.00 79.83  ? 221  VAL B CA    1 
ATOM   1283 C  C     . VAL A 1 179 ? 24.369  -5.274  -9.905  1.00 93.06  ? 221  VAL B C     1 
ATOM   1284 O  O     . VAL A 1 179 ? 23.751  -4.206  -9.970  1.00 91.27  ? 221  VAL B O     1 
ATOM   1285 C  CB    . VAL A 1 179 ? 24.861  -5.254  -12.384 1.00 78.07  ? 221  VAL B CB    1 
ATOM   1286 C  CG1   . VAL A 1 179 ? 26.223  -4.586  -12.308 1.00 63.17  ? 221  VAL B CG1   1 
ATOM   1287 C  CG2   . VAL A 1 179 ? 24.744  -6.092  -13.648 1.00 78.57  ? 221  VAL B CG2   1 
ATOM   1288 N  N     . ASP A 1 180 ? 24.838  -5.758  -8.755  1.00 100.54 ? 222  ASP B N     1 
ATOM   1289 C  CA    . ASP A 1 180 ? 24.612  -5.079  -7.484  1.00 95.08  ? 222  ASP B CA    1 
ATOM   1290 C  C     . ASP A 1 180 ? 25.495  -3.840  -7.408  1.00 97.51  ? 222  ASP B C     1 
ATOM   1291 O  O     . ASP A 1 180 ? 26.716  -3.946  -7.250  1.00 85.39  ? 222  ASP B O     1 
ATOM   1292 C  CB    . ASP A 1 180 ? 24.893  -6.025  -6.321  1.00 102.52 ? 222  ASP B CB    1 
ATOM   1293 C  CG    . ASP A 1 180 ? 24.353  -5.503  -5.003  1.00 98.73  ? 222  ASP B CG    1 
ATOM   1294 O  OD1   . ASP A 1 180 ? 23.645  -4.474  -5.013  1.00 76.53  ? 222  ASP B OD1   1 
ATOM   1295 O  OD2   . ASP A 1 180 ? 24.638  -6.122  -3.956  1.00 96.10  ? 222  ASP B OD2   1 
ATOM   1296 N  N     . SER A 1 181 ? 24.871  -2.667  -7.519  1.00 105.47 ? 223  SER B N     1 
ATOM   1297 C  CA    . SER A 1 181 ? 25.549  -1.372  -7.514  1.00 100.68 ? 223  SER B CA    1 
ATOM   1298 C  C     . SER A 1 181 ? 26.546  -1.282  -8.674  1.00 105.20 ? 223  SER B C     1 
ATOM   1299 O  O     . SER A 1 181 ? 27.765  -1.360  -8.508  1.00 110.50 ? 223  SER B O     1 
ATOM   1300 C  CB    . SER A 1 181 ? 26.227  -1.107  -6.165  1.00 110.82 ? 223  SER B CB    1 
ATOM   1301 O  OG    . SER A 1 181 ? 26.480  0.276   -5.993  1.00 119.19 ? 223  SER B OG    1 
ATOM   1302 N  N     . ALA A 1 182 ? 25.975  -1.120  -9.870  1.00 97.87  ? 224  ALA B N     1 
ATOM   1303 C  CA    . ALA A 1 182 ? 26.784  -0.936  -11.067 1.00 95.66  ? 224  ALA B CA    1 
ATOM   1304 C  C     . ALA A 1 182 ? 27.551  0.378   -11.046 1.00 103.61 ? 224  ALA B C     1 
ATOM   1305 O  O     . ALA A 1 182 ? 28.548  0.510   -11.764 1.00 108.37 ? 224  ALA B O     1 
ATOM   1306 C  CB    . ALA A 1 182 ? 25.902  -0.999  -12.314 1.00 84.91  ? 224  ALA B CB    1 
ATOM   1307 N  N     . THR A 1 183 ? 27.112  1.345   -10.243 1.00 99.86  ? 225  THR B N     1 
ATOM   1308 C  CA    . THR A 1 183 ? 27.760  2.644   -10.146 1.00 103.38 ? 225  THR B CA    1 
ATOM   1309 C  C     . THR A 1 183 ? 28.698  2.755   -8.952  1.00 109.92 ? 225  THR B C     1 
ATOM   1310 O  O     . THR A 1 183 ? 29.288  3.820   -8.746  1.00 120.89 ? 225  THR B O     1 
ATOM   1311 C  CB    . THR A 1 183 ? 26.707  3.755   -10.074 1.00 82.22  ? 225  THR B CB    1 
ATOM   1312 O  OG1   . THR A 1 183 ? 25.871  3.549   -8.928  1.00 107.31 ? 225  THR B OG1   1 
ATOM   1313 C  CG2   . THR A 1 183 ? 25.846  3.755   -11.328 1.00 110.14 ? 225  THR B CG2   1 
ATOM   1314 N  N     . ALA A 1 184 ? 28.849  1.690   -8.161  1.00 118.18 ? 226  ALA B N     1 
ATOM   1315 C  CA    . ALA A 1 184 ? 29.726  1.749   -6.995  1.00 110.10 ? 226  ALA B CA    1 
ATOM   1316 C  C     . ALA A 1 184 ? 31.168  2.017   -7.406  1.00 110.47 ? 226  ALA B C     1 
ATOM   1317 O  O     . ALA A 1 184 ? 31.837  2.892   -6.844  1.00 111.24 ? 226  ALA B O     1 
ATOM   1318 C  CB    . ALA A 1 184 ? 29.628  0.450   -6.195  1.00 110.96 ? 226  ALA B CB    1 
ATOM   1319 N  N     . LEU A 1 185 ? 31.664  1.269   -8.390  1.00 104.73 ? 227  LEU B N     1 
ATOM   1320 C  CA    . LEU A 1 185 ? 33.023  1.456   -8.876  1.00 103.15 ? 227  LEU B CA    1 
ATOM   1321 C  C     . LEU A 1 185 ? 33.168  2.687   -9.760  1.00 114.58 ? 227  LEU B C     1 
ATOM   1322 O  O     . LEU A 1 185 ? 34.299  3.083   -10.061 1.00 115.77 ? 227  LEU B O     1 
ATOM   1323 C  CB    . LEU A 1 185 ? 33.475  0.205   -9.633  1.00 103.47 ? 227  LEU B CB    1 
ATOM   1324 C  CG    . LEU A 1 185 ? 33.351  -1.097  -8.837  1.00 105.71 ? 227  LEU B CG    1 
ATOM   1325 C  CD1   . LEU A 1 185 ? 33.660  -2.305  -9.708  1.00 116.67 ? 227  LEU B CD1   1 
ATOM   1326 C  CD2   . LEU A 1 185 ? 34.256  -1.070  -7.614  1.00 97.14  ? 227  LEU B CD2   1 
ATOM   1327 N  N     . TYR A 1 186 ? 32.060  3.298   -10.176 1.00 107.90 ? 228  TYR B N     1 
ATOM   1328 C  CA    . TYR A 1 186 ? 32.090  4.514   -10.978 1.00 117.50 ? 228  TYR B CA    1 
ATOM   1329 C  C     . TYR A 1 186 ? 31.960  5.784   -10.151 1.00 120.16 ? 228  TYR B C     1 
ATOM   1330 O  O     . TYR A 1 186 ? 32.499  6.824   -10.546 1.00 125.70 ? 228  TYR B O     1 
ATOM   1331 C  CB    . TYR A 1 186 ? 30.968  4.491   -12.022 1.00 121.35 ? 228  TYR B CB    1 
ATOM   1332 C  CG    . TYR A 1 186 ? 31.203  3.529   -13.164 1.00 104.02 ? 228  TYR B CG    1 
ATOM   1333 C  CD1   . TYR A 1 186 ? 30.804  2.202   -13.074 1.00 100.55 ? 228  TYR B CD1   1 
ATOM   1334 C  CD2   . TYR A 1 186 ? 31.821  3.949   -14.333 1.00 102.99 ? 228  TYR B CD2   1 
ATOM   1335 C  CE1   . TYR A 1 186 ? 31.015  1.320   -14.115 1.00 110.16 ? 228  TYR B CE1   1 
ATOM   1336 C  CE2   . TYR A 1 186 ? 32.036  3.075   -15.380 1.00 112.72 ? 228  TYR B CE2   1 
ATOM   1337 C  CZ    . TYR A 1 186 ? 31.631  1.761   -15.266 1.00 109.59 ? 228  TYR B CZ    1 
ATOM   1338 O  OH    . TYR A 1 186 ? 31.844  0.886   -16.307 1.00 104.14 ? 228  TYR B OH    1 
ATOM   1339 N  N     . ARG A 1 187 ? 31.263  5.730   -9.015  1.00 140.74 ? 229  ARG B N     1 
ATOM   1340 C  CA    . ARG A 1 187 ? 31.065  6.900   -8.170  1.00 139.45 ? 229  ARG B CA    1 
ATOM   1341 C  C     . ARG A 1 187 ? 32.273  7.221   -7.299  1.00 143.41 ? 229  ARG B C     1 
ATOM   1342 O  O     . ARG A 1 187 ? 32.126  7.935   -6.300  1.00 142.60 ? 229  ARG B O     1 
ATOM   1343 C  CB    . ARG A 1 187 ? 29.823  6.719   -7.294  1.00 119.06 ? 229  ARG B CB    1 
ATOM   1344 C  CG    . ARG A 1 187 ? 28.511  6.805   -8.057  1.00 131.58 ? 229  ARG B CG    1 
ATOM   1345 C  CD    . ARG A 1 187 ? 27.316  6.781   -7.120  1.00 114.61 ? 229  ARG B CD    1 
ATOM   1346 N  NE    . ARG A 1 187 ? 26.055  6.809   -7.852  1.00 123.26 ? 229  ARG B NE    1 
ATOM   1347 C  CZ    . ARG A 1 187 ? 25.481  7.913   -8.312  1.00 129.42 ? 229  ARG B CZ    1 
ATOM   1348 N  NH1   . ARG A 1 187 ? 26.027  9.104   -8.130  1.00 139.21 ? 229  ARG B NH1   1 
ATOM   1349 N  NH2   . ARG A 1 187 ? 24.331  7.818   -8.973  1.00 129.75 ? 229  ARG B NH2   1 
ATOM   1350 N  N     . THR A 1 188 ? 33.455  6.712   -7.644  1.00 149.61 ? 230  THR B N     1 
ATOM   1351 C  CA    . THR A 1 188 ? 34.693  7.089   -6.963  1.00 158.85 ? 230  THR B CA    1 
ATOM   1352 C  C     . THR A 1 188 ? 35.249  8.376   -7.578  1.00 167.12 ? 230  THR B C     1 
ATOM   1353 O  O     . THR A 1 188 ? 36.388  8.452   -8.037  1.00 169.31 ? 230  THR B O     1 
ATOM   1354 C  CB    . THR A 1 188 ? 35.706  5.953   -7.033  1.00 149.80 ? 230  THR B CB    1 
ATOM   1355 O  OG1   . THR A 1 188 ? 36.000  5.656   -8.404  1.00 156.24 ? 230  THR B OG1   1 
ATOM   1356 C  CG2   . THR A 1 188 ? 35.155  4.706   -6.356  1.00 124.42 ? 230  THR B CG2   1 
ATOM   1357 N  N     . ASP A 1 189 ? 34.402  9.406   -7.578  1.00 164.33 ? 231  ASP B N     1 
ATOM   1358 C  CA    . ASP A 1 189 ? 34.722  10.671  -8.228  1.00 169.81 ? 231  ASP B CA    1 
ATOM   1359 C  C     . ASP A 1 189 ? 35.561  11.568  -7.327  1.00 173.87 ? 231  ASP B C     1 
ATOM   1360 O  O     . ASP A 1 189 ? 35.185  12.714  -7.059  1.00 174.34 ? 231  ASP B O     1 
ATOM   1361 C  CB    . ASP A 1 189 ? 33.439  11.393  -8.646  1.00 170.34 ? 231  ASP B CB    1 
ATOM   1362 C  CG    . ASP A 1 189 ? 32.648  10.623  -9.687  1.00 164.59 ? 231  ASP B CG    1 
ATOM   1363 O  OD1   . ASP A 1 189 ? 33.272  9.912   -10.503 1.00 162.52 ? 231  ASP B OD1   1 
ATOM   1364 O  OD2   . ASP A 1 189 ? 31.404  10.729  -9.690  1.00 154.08 ? 231  ASP B OD2   1 
ATOM   1365 N  N     . TYR A 1 190 ? 36.700  11.057  -6.856  1.00 175.39 ? 232  TYR B N     1 
ATOM   1366 C  CA    . TYR A 1 190 ? 37.615  11.882  -6.077  1.00 175.32 ? 232  TYR B CA    1 
ATOM   1367 C  C     . TYR A 1 190 ? 38.394  12.857  -6.949  1.00 176.11 ? 232  TYR B C     1 
ATOM   1368 O  O     . TYR A 1 190 ? 38.965  13.818  -6.424  1.00 175.04 ? 232  TYR B O     1 
ATOM   1369 C  CB    . TYR A 1 190 ? 38.581  10.997  -5.286  1.00 175.38 ? 232  TYR B CB    1 
ATOM   1370 C  CG    . TYR A 1 190 ? 38.993  9.734   -6.009  1.00 179.92 ? 232  TYR B CG    1 
ATOM   1371 C  CD1   . TYR A 1 190 ? 39.858  9.780   -7.095  1.00 181.40 ? 232  TYR B CD1   1 
ATOM   1372 C  CD2   . TYR A 1 190 ? 38.522  8.493   -5.600  1.00 176.47 ? 232  TYR B CD2   1 
ATOM   1373 C  CE1   . TYR A 1 190 ? 40.237  8.627   -7.756  1.00 185.69 ? 232  TYR B CE1   1 
ATOM   1374 C  CE2   . TYR A 1 190 ? 38.897  7.335   -6.253  1.00 179.04 ? 232  TYR B CE2   1 
ATOM   1375 C  CZ    . TYR A 1 190 ? 39.753  7.407   -7.331  1.00 188.87 ? 232  TYR B CZ    1 
ATOM   1376 O  OH    . TYR A 1 190 ? 40.128  6.255   -7.984  1.00 190.61 ? 232  TYR B OH    1 
ATOM   1377 N  N     . SER A 1 191 ? 38.429  12.634  -8.260  1.00 170.47 ? 233  SER B N     1 
ATOM   1378 C  CA    . SER A 1 191 ? 39.119  13.536  -9.166  1.00 164.29 ? 233  SER B CA    1 
ATOM   1379 C  C     . SER A 1 191 ? 38.266  14.771  -9.445  1.00 164.59 ? 233  SER B C     1 
ATOM   1380 O  O     . SER A 1 191 ? 37.040  14.759  -9.306  1.00 162.57 ? 233  SER B O     1 
ATOM   1381 C  CB    . SER A 1 191 ? 39.458  12.826  -10.478 1.00 142.87 ? 233  SER B CB    1 
ATOM   1382 O  OG    . SER A 1 191 ? 40.269  11.687  -10.248 1.00 135.52 ? 233  SER B OG    1 
ATOM   1383 N  N     . GLY A 1 192 ? 38.938  15.849  -9.842  1.00 160.95 ? 234  GLY B N     1 
ATOM   1384 C  CA    . GLY A 1 192 ? 38.256  17.088  -10.158 1.00 158.66 ? 234  GLY B CA    1 
ATOM   1385 C  C     . GLY A 1 192 ? 37.443  17.005  -11.433 1.00 166.39 ? 234  GLY B C     1 
ATOM   1386 O  O     . GLY A 1 192 ? 36.244  16.713  -11.396 1.00 166.23 ? 234  GLY B O     1 
ATOM   1387 N  N     . ARG A 1 193 ? 38.085  17.260  -12.567 1.00 164.55 ? 235  ARG B N     1 
ATOM   1388 C  CA    . ARG A 1 193 ? 37.455  17.181  -13.877 1.00 162.87 ? 235  ARG B CA    1 
ATOM   1389 C  C     . ARG A 1 193 ? 38.147  16.107  -14.713 1.00 155.14 ? 235  ARG B C     1 
ATOM   1390 O  O     . ARG A 1 193 ? 39.078  15.436  -14.261 1.00 154.13 ? 235  ARG B O     1 
ATOM   1391 C  CB    . ARG A 1 193 ? 37.496  18.535  -14.592 1.00 167.74 ? 235  ARG B CB    1 
ATOM   1392 C  CG    . ARG A 1 193 ? 36.672  19.631  -13.933 1.00 164.20 ? 235  ARG B CG    1 
ATOM   1393 C  CD    . ARG A 1 193 ? 37.527  20.512  -13.035 1.00 162.63 ? 235  ARG B CD    1 
ATOM   1394 N  NE    . ARG A 1 193 ? 36.785  21.668  -12.545 1.00 174.66 ? 235  ARG B NE    1 
ATOM   1395 C  CZ    . ARG A 1 193 ? 36.669  22.816  -13.199 1.00 166.87 ? 235  ARG B CZ    1 
ATOM   1396 N  NH1   . ARG A 1 193 ? 37.236  22.998  -14.381 1.00 161.39 ? 235  ARG B NH1   1 
ATOM   1397 N  NH2   . ARG A 1 193 ? 35.967  23.805  -12.654 1.00 149.94 ? 235  ARG B NH2   1 
ATOM   1398 N  N     . GLY A 1 194 ? 37.681  15.951  -15.939 1.00 147.98 ? 236  GLY B N     1 
ATOM   1399 C  CA    . GLY A 1 194 ? 38.263  14.990  -16.872 1.00 148.06 ? 236  GLY B CA    1 
ATOM   1400 C  C     . GLY A 1 194 ? 37.669  13.599  -16.847 1.00 152.62 ? 236  GLY B C     1 
ATOM   1401 O  O     . GLY A 1 194 ? 37.285  13.068  -17.889 1.00 145.38 ? 236  GLY B O     1 
ATOM   1402 N  N     . GLU A 1 195 ? 37.585  12.994  -15.660 1.00 157.80 ? 237  GLU B N     1 
ATOM   1403 C  CA    . GLU A 1 195 ? 37.053  11.642  -15.550 1.00 150.70 ? 237  GLU B CA    1 
ATOM   1404 C  C     . GLU A 1 195 ? 35.545  11.590  -15.750 1.00 150.38 ? 237  GLU B C     1 
ATOM   1405 O  O     . GLU A 1 195 ? 35.007  10.510  -16.017 1.00 143.79 ? 237  GLU B O     1 
ATOM   1406 C  CB    . GLU A 1 195 ? 37.419  11.041  -14.192 1.00 145.33 ? 237  GLU B CB    1 
ATOM   1407 C  CG    . GLU A 1 195 ? 38.912  10.846  -13.984 1.00 150.26 ? 237  GLU B CG    1 
ATOM   1408 C  CD    . GLU A 1 195 ? 39.513  9.849   -14.957 1.00 155.13 ? 237  GLU B CD    1 
ATOM   1409 O  OE1   . GLU A 1 195 ? 38.790  8.929   -15.396 1.00 147.75 ? 237  GLU B OE1   1 
ATOM   1410 O  OE2   . GLU A 1 195 ? 40.710  9.988   -15.287 1.00 162.22 ? 237  GLU B OE2   1 
ATOM   1411 N  N     . LEU A 1 196 ? 34.853  12.727  -15.634 1.00 151.33 ? 238  LEU B N     1 
ATOM   1412 C  CA    . LEU A 1 196 ? 33.409  12.753  -15.840 1.00 147.12 ? 238  LEU B CA    1 
ATOM   1413 C  C     . LEU A 1 196 ? 33.011  12.388  -17.263 1.00 144.22 ? 238  LEU B C     1 
ATOM   1414 O  O     . LEU A 1 196 ? 31.827  12.139  -17.513 1.00 138.30 ? 238  LEU B O     1 
ATOM   1415 C  CB    . LEU A 1 196 ? 32.844  14.133  -15.484 1.00 150.70 ? 238  LEU B CB    1 
ATOM   1416 C  CG    . LEU A 1 196 ? 32.684  14.481  -14.000 1.00 144.24 ? 238  LEU B CG    1 
ATOM   1417 C  CD1   . LEU A 1 196 ? 34.015  14.855  -13.359 1.00 155.66 ? 238  LEU B CD1   1 
ATOM   1418 C  CD2   . LEU A 1 196 ? 31.663  15.595  -13.816 1.00 113.09 ? 238  LEU B CD2   1 
ATOM   1419 N  N     . SER A 1 197 ? 33.962  12.352  -18.196 1.00 144.76 ? 239  SER B N     1 
ATOM   1420 C  CA    . SER A 1 197 ? 33.714  11.913  -19.563 1.00 139.70 ? 239  SER B CA    1 
ATOM   1421 C  C     . SER A 1 197 ? 34.089  10.451  -19.779 1.00 136.99 ? 239  SER B C     1 
ATOM   1422 O  O     . SER A 1 197 ? 33.301  9.685   -20.340 1.00 136.31 ? 239  SER B O     1 
ATOM   1423 C  CB    . SER A 1 197 ? 34.483  12.803  -20.548 1.00 143.79 ? 239  SER B CB    1 
ATOM   1424 O  OG    . SER A 1 197 ? 35.873  12.782  -20.273 1.00 149.13 ? 239  SER B OG    1 
ATOM   1425 N  N     . ALA A 1 198 ? 35.280  10.045  -19.331 1.00 124.17 ? 240  ALA B N     1 
ATOM   1426 C  CA    . ALA A 1 198 ? 35.716  8.667   -19.533 1.00 118.37 ? 240  ALA B CA    1 
ATOM   1427 C  C     . ALA A 1 198 ? 34.869  7.691   -18.725 1.00 138.16 ? 240  ALA B C     1 
ATOM   1428 O  O     . ALA A 1 198 ? 34.494  6.623   -19.225 1.00 140.37 ? 240  ALA B O     1 
ATOM   1429 C  CB    . ALA A 1 198 ? 37.193  8.525   -19.171 1.00 111.13 ? 240  ALA B CB    1 
ATOM   1430 N  N     . ARG A 1 199 ? 34.557  8.038   -17.474 1.00 139.31 ? 241  ARG B N     1 
ATOM   1431 C  CA    . ARG A 1 199 ? 33.706  7.173   -16.666 1.00 126.97 ? 241  ARG B CA    1 
ATOM   1432 C  C     . ARG A 1 199 ? 32.291  7.117   -17.226 1.00 131.43 ? 241  ARG B C     1 
ATOM   1433 O  O     . ARG A 1 199 ? 31.645  6.063   -17.189 1.00 130.18 ? 241  ARG B O     1 
ATOM   1434 C  CB    . ARG A 1 199 ? 33.702  7.654   -15.216 1.00 140.38 ? 241  ARG B CB    1 
ATOM   1435 C  CG    . ARG A 1 199 ? 35.032  7.446   -14.508 1.00 135.45 ? 241  ARG B CG    1 
ATOM   1436 C  CD    . ARG A 1 199 ? 35.116  8.245   -13.220 1.00 131.18 ? 241  ARG B CD    1 
ATOM   1437 N  NE    . ARG A 1 199 ? 36.339  7.956   -12.481 1.00 143.31 ? 241  ARG B NE    1 
ATOM   1438 C  CZ    . ARG A 1 199 ? 36.788  8.681   -11.466 1.00 146.80 ? 241  ARG B CZ    1 
ATOM   1439 N  NH1   . ARG A 1 199 ? 36.150  9.764   -11.055 1.00 147.30 ? 241  ARG B NH1   1 
ATOM   1440 N  NH2   . ARG A 1 199 ? 37.908  8.312   -10.851 1.00 152.84 ? 241  ARG B NH2   1 
ATOM   1441 N  N     . GLN A 1 200 ? 31.796  8.238   -17.757 1.00 132.32 ? 242  GLN B N     1 
ATOM   1442 C  CA    . GLN A 1 200 ? 30.487  8.227   -18.402 1.00 129.22 ? 242  GLN B CA    1 
ATOM   1443 C  C     . GLN A 1 200 ? 30.487  7.318   -19.622 1.00 130.38 ? 242  GLN B C     1 
ATOM   1444 O  O     . GLN A 1 200 ? 29.532  6.567   -19.845 1.00 133.89 ? 242  GLN B O     1 
ATOM   1445 C  CB    . GLN A 1 200 ? 30.076  9.644   -18.799 1.00 142.43 ? 242  GLN B CB    1 
ATOM   1446 C  CG    . GLN A 1 200 ? 29.008  9.694   -19.883 1.00 153.43 ? 242  GLN B CG    1 
ATOM   1447 C  CD    . GLN A 1 200 ? 27.839  10.591  -19.520 1.00 158.09 ? 242  GLN B CD    1 
ATOM   1448 O  OE1   . GLN A 1 200 ? 27.761  11.112  -18.407 1.00 143.72 ? 242  GLN B OE1   1 
ATOM   1449 N  NE2   . GLN A 1 200 ? 26.920  10.773  -20.462 1.00 152.08 ? 242  GLN B NE2   1 
ATOM   1450 N  N     . MET A 1 201 ? 31.548  7.377   -20.427 1.00 122.56 ? 243  MET B N     1 
ATOM   1451 C  CA    . MET A 1 201 ? 31.649  6.476   -21.570 1.00 133.01 ? 243  MET B CA    1 
ATOM   1452 C  C     . MET A 1 201 ? 31.674  5.020   -21.126 1.00 122.49 ? 243  MET B C     1 
ATOM   1453 O  O     . MET A 1 201 ? 30.973  4.180   -21.701 1.00 109.82 ? 243  MET B O     1 
ATOM   1454 C  CB    . MET A 1 201 ? 32.893  6.802   -22.396 1.00 145.18 ? 243  MET B CB    1 
ATOM   1455 C  CG    . MET A 1 201 ? 32.852  8.155   -23.091 1.00 148.75 ? 243  MET B CG    1 
ATOM   1456 S  SD    . MET A 1 201 ? 31.454  8.330   -24.217 1.00 156.31 ? 243  MET B SD    1 
ATOM   1457 C  CE    . MET A 1 201 ? 31.543  10.078  -24.604 1.00 146.60 ? 243  MET B CE    1 
ATOM   1458 N  N     . HIS A 1 202 ? 32.479  4.702   -20.107 1.00 115.05 ? 244  HIS B N     1 
ATOM   1459 C  CA    . HIS A 1 202 ? 32.553  3.327   -19.619 1.00 110.59 ? 244  HIS B CA    1 
ATOM   1460 C  C     . HIS A 1 202 ? 31.193  2.845   -19.124 1.00 106.02 ? 244  HIS B C     1 
ATOM   1461 O  O     . HIS A 1 202 ? 30.779  1.717   -19.419 1.00 103.07 ? 244  HIS B O     1 
ATOM   1462 C  CB    . HIS A 1 202 ? 33.601  3.228   -18.507 1.00 113.84 ? 244  HIS B CB    1 
ATOM   1463 C  CG    . HIS A 1 202 ? 34.413  1.969   -18.538 1.00 114.49 ? 244  HIS B CG    1 
ATOM   1464 N  ND1   . HIS A 1 202 ? 33.849  0.713   -18.479 1.00 115.52 ? 244  HIS B ND1   1 
ATOM   1465 C  CD2   . HIS A 1 202 ? 35.752  1.776   -18.607 1.00 118.10 ? 244  HIS B CD2   1 
ATOM   1466 C  CE1   . HIS A 1 202 ? 34.804  -0.199  -18.517 1.00 114.00 ? 244  HIS B CE1   1 
ATOM   1467 N  NE2   . HIS A 1 202 ? 35.968  0.420   -18.595 1.00 124.28 ? 244  HIS B NE2   1 
ATOM   1468 N  N     . LEU A 1 203 ? 30.472  3.696   -18.387 1.00 97.88  ? 245  LEU B N     1 
ATOM   1469 C  CA    . LEU A 1 203 ? 29.165  3.301   -17.871 1.00 112.26 ? 245  LEU B CA    1 
ATOM   1470 C  C     . LEU A 1 203 ? 28.148  3.145   -18.997 1.00 104.92 ? 245  LEU B C     1 
ATOM   1471 O  O     . LEU A 1 203 ? 27.305  2.241   -18.958 1.00 97.94  ? 245  LEU B O     1 
ATOM   1472 C  CB    . LEU A 1 203 ? 28.679  4.318   -16.839 1.00 106.14 ? 245  LEU B CB    1 
ATOM   1473 C  CG    . LEU A 1 203 ? 27.367  3.981   -16.129 1.00 100.19 ? 245  LEU B CG    1 
ATOM   1474 C  CD1   . LEU A 1 203 ? 27.476  2.647   -15.405 1.00 88.01  ? 245  LEU B CD1   1 
ATOM   1475 C  CD2   . LEU A 1 203 ? 26.977  5.086   -15.162 1.00 100.62 ? 245  LEU B CD2   1 
ATOM   1476 N  N     . ALA A 1 204 ? 28.214  4.012   -20.011 1.00 108.94 ? 246  ALA B N     1 
ATOM   1477 C  CA    . ALA A 1 204 ? 27.305  3.891   -21.145 1.00 90.86  ? 246  ALA B CA    1 
ATOM   1478 C  C     . ALA A 1 204 ? 27.565  2.605   -21.917 1.00 92.84  ? 246  ALA B C     1 
ATOM   1479 O  O     . ALA A 1 204 ? 26.623  1.911   -22.321 1.00 95.83  ? 246  ALA B O     1 
ATOM   1480 C  CB    . ALA A 1 204 ? 27.443  5.108   -22.059 1.00 81.78  ? 246  ALA B CB    1 
ATOM   1481 N  N     . ARG A 1 205 ? 28.841  2.264   -22.121 1.00 83.76  ? 247  ARG B N     1 
ATOM   1482 C  CA    . ARG A 1 205 ? 29.170  1.011   -22.792 1.00 88.81  ? 247  ARG B CA    1 
ATOM   1483 C  C     . ARG A 1 205 ? 28.728  -0.184  -21.959 1.00 98.64  ? 247  ARG B C     1 
ATOM   1484 O  O     . ARG A 1 205 ? 28.258  -1.189  -22.502 1.00 94.33  ? 247  ARG B O     1 
ATOM   1485 C  CB    . ARG A 1 205 ? 30.670  0.942   -23.088 1.00 86.29  ? 247  ARG B CB    1 
ATOM   1486 C  CG    . ARG A 1 205 ? 31.090  -0.342  -23.795 1.00 94.14  ? 247  ARG B CG    1 
ATOM   1487 C  CD    . ARG A 1 205 ? 32.475  -0.248  -24.424 1.00 105.57 ? 247  ARG B CD    1 
ATOM   1488 N  NE    . ARG A 1 205 ? 33.535  -0.068  -23.439 1.00 118.80 ? 247  ARG B NE    1 
ATOM   1489 C  CZ    . ARG A 1 205 ? 34.165  1.078   -23.218 1.00 132.63 ? 247  ARG B CZ    1 
ATOM   1490 N  NH1   . ARG A 1 205 ? 33.873  2.171   -23.905 1.00 129.76 ? 247  ARG B NH1   1 
ATOM   1491 N  NH2   . ARG A 1 205 ? 35.114  1.128   -22.288 1.00 130.31 ? 247  ARG B NH2   1 
ATOM   1492 N  N     . PHE A 1 206 ? 28.852  -0.083  -20.634 1.00 97.41  ? 248  PHE B N     1 
ATOM   1493 C  CA    . PHE A 1 206 ? 28.397  -1.154  -19.755 1.00 78.70  ? 248  PHE B CA    1 
ATOM   1494 C  C     . PHE A 1 206 ? 26.889  -1.358  -19.872 1.00 88.29  ? 248  PHE B C     1 
ATOM   1495 O  O     . PHE A 1 206 ? 26.407  -2.493  -19.990 1.00 93.51  ? 248  PHE B O     1 
ATOM   1496 C  CB    . PHE A 1 206 ? 28.797  -0.833  -18.316 1.00 85.23  ? 248  PHE B CB    1 
ATOM   1497 C  CG    . PHE A 1 206 ? 28.450  -1.906  -17.333 1.00 83.65  ? 248  PHE B CG    1 
ATOM   1498 C  CD1   . PHE A 1 206 ? 29.251  -3.027  -17.203 1.00 80.11  ? 248  PHE B CD1   1 
ATOM   1499 C  CD2   . PHE A 1 206 ? 27.333  -1.788  -16.526 1.00 85.50  ? 248  PHE B CD2   1 
ATOM   1500 C  CE1   . PHE A 1 206 ? 28.938  -4.014  -16.293 1.00 72.67  ? 248  PHE B CE1   1 
ATOM   1501 C  CE2   . PHE A 1 206 ? 27.016  -2.773  -15.613 1.00 92.62  ? 248  PHE B CE2   1 
ATOM   1502 C  CZ    . PHE A 1 206 ? 27.817  -3.889  -15.500 1.00 97.59  ? 248  PHE B CZ    1 
ATOM   1503 N  N     . LEU A 1 207 ? 26.127  -0.262  -19.849 1.00 83.27  ? 249  LEU B N     1 
ATOM   1504 C  CA    . LEU A 1 207 ? 24.676  -0.366  -19.980 1.00 86.30  ? 249  LEU B CA    1 
ATOM   1505 C  C     . LEU A 1 207 ? 24.281  -0.910  -21.348 1.00 88.16  ? 249  LEU B C     1 
ATOM   1506 O  O     . LEU A 1 207 ? 23.331  -1.695  -21.463 1.00 88.41  ? 249  LEU B O     1 
ATOM   1507 C  CB    . LEU A 1 207 ? 24.026  0.997   -19.739 1.00 69.48  ? 249  LEU B CB    1 
ATOM   1508 C  CG    . LEU A 1 207 ? 24.202  1.602   -18.346 1.00 77.59  ? 249  LEU B CG    1 
ATOM   1509 C  CD1   . LEU A 1 207 ? 23.536  2.967   -18.274 1.00 83.30  ? 249  LEU B CD1   1 
ATOM   1510 C  CD2   . LEU A 1 207 ? 23.645  0.671   -17.280 1.00 82.16  ? 249  LEU B CD2   1 
ATOM   1511 N  N     . ARG A 1 208 ? 24.999  -0.508  -22.398 1.00 94.44  ? 250  ARG B N     1 
ATOM   1512 C  CA    . ARG A 1 208 ? 24.681  -1.010  -23.730 1.00 93.25  ? 250  ARG B CA    1 
ATOM   1513 C  C     . ARG A 1 208 ? 25.009  -2.493  -23.857 1.00 87.57  ? 250  ARG B C     1 
ATOM   1514 O  O     . ARG A 1 208 ? 24.279  -3.239  -24.517 1.00 73.52  ? 250  ARG B O     1 
ATOM   1515 C  CB    . ARG A 1 208 ? 25.417  -0.188  -24.787 1.00 97.70  ? 250  ARG B CB    1 
ATOM   1516 C  CG    . ARG A 1 208 ? 24.844  1.210   -24.950 1.00 104.13 ? 250  ARG B CG    1 
ATOM   1517 C  CD    . ARG A 1 208 ? 25.483  1.956   -26.101 1.00 88.56  ? 250  ARG B CD    1 
ATOM   1518 N  NE    . ARG A 1 208 ? 26.658  2.718   -25.694 1.00 98.13  ? 250  ARG B NE    1 
ATOM   1519 C  CZ    . ARG A 1 208 ? 27.908  2.296   -25.824 1.00 98.05  ? 250  ARG B CZ    1 
ATOM   1520 N  NH1   . ARG A 1 208 ? 28.187  1.110   -26.339 1.00 95.62  ? 250  ARG B NH1   1 
ATOM   1521 N  NH2   . ARG A 1 208 ? 28.903  3.084   -25.428 1.00 91.88  ? 250  ARG B NH2   1 
ATOM   1522 N  N     . MET A 1 209 ? 26.089  -2.944  -23.215 1.00 84.94  ? 251  MET B N     1 
ATOM   1523 C  CA    . MET A 1 209 ? 26.386  -4.373  -23.191 1.00 89.74  ? 251  MET B CA    1 
ATOM   1524 C  C     . MET A 1 209 ? 25.322  -5.142  -22.416 1.00 90.35  ? 251  MET B C     1 
ATOM   1525 O  O     . MET A 1 209 ? 24.952  -6.259  -22.799 1.00 94.88  ? 251  MET B O     1 
ATOM   1526 C  CB    . MET A 1 209 ? 27.770  -4.612  -22.588 1.00 80.59  ? 251  MET B CB    1 
ATOM   1527 C  CG    . MET A 1 209 ? 28.920  -4.100  -23.441 1.00 85.21  ? 251  MET B CG    1 
ATOM   1528 S  SD    . MET A 1 209 ? 30.518  -4.261  -22.621 1.00 110.16 ? 251  MET B SD    1 
ATOM   1529 C  CE    . MET A 1 209 ? 30.569  -6.026  -22.325 1.00 108.18 ? 251  MET B CE    1 
ATOM   1530 N  N     . LEU A 1 210 ? 24.819  -4.559  -21.325 1.00 73.08  ? 252  LEU B N     1 
ATOM   1531 C  CA    . LEU A 1 210 ? 23.725  -5.191  -20.591 1.00 78.56  ? 252  LEU B CA    1 
ATOM   1532 C  C     . LEU A 1 210 ? 22.480  -5.321  -21.460 1.00 80.87  ? 252  LEU B C     1 
ATOM   1533 O  O     . LEU A 1 210 ? 21.820  -6.368  -21.463 1.00 73.29  ? 252  LEU B O     1 
ATOM   1534 C  CB    . LEU A 1 210 ? 23.408  -4.394  -19.327 1.00 79.34  ? 252  LEU B CB    1 
ATOM   1535 C  CG    . LEU A 1 210 ? 24.434  -4.426  -18.196 1.00 69.66  ? 252  LEU B CG    1 
ATOM   1536 C  CD1   . LEU A 1 210 ? 23.986  -3.505  -17.081 1.00 71.49  ? 252  LEU B CD1   1 
ATOM   1537 C  CD2   . LEU A 1 210 ? 24.619  -5.843  -17.681 1.00 70.72  ? 252  LEU B CD2   1 
ATOM   1538 N  N     . LEU A 1 211 ? 22.137  -4.260  -22.195 1.00 74.63  ? 253  LEU B N     1 
ATOM   1539 C  CA    . LEU A 1 211 ? 20.995  -4.327  -23.104 1.00 82.26  ? 253  LEU B CA    1 
ATOM   1540 C  C     . LEU A 1 211 ? 21.215  -5.372  -24.190 1.00 86.35  ? 253  LEU B C     1 
ATOM   1541 O  O     . LEU A 1 211 ? 20.285  -6.099  -24.563 1.00 77.81  ? 253  LEU B O     1 
ATOM   1542 C  CB    . LEU A 1 211 ? 20.734  -2.957  -23.729 1.00 78.57  ? 253  LEU B CB    1 
ATOM   1543 C  CG    . LEU A 1 211 ? 19.909  -1.964  -22.912 1.00 89.56  ? 253  LEU B CG    1 
ATOM   1544 C  CD1   . LEU A 1 211 ? 19.833  -0.626  -23.627 1.00 108.18 ? 253  LEU B CD1   1 
ATOM   1545 C  CD2   . LEU A 1 211 ? 18.515  -2.516  -22.656 1.00 85.52  ? 253  LEU B CD2   1 
ATOM   1546 N  N     . ARG A 1 212 ? 22.440  -5.460  -24.713 1.00 86.07  ? 254  ARG B N     1 
ATOM   1547 C  CA    . ARG A 1 212 ? 22.747  -6.460  -25.729 1.00 80.44  ? 254  ARG B CA    1 
ATOM   1548 C  C     . ARG A 1 212 ? 22.556  -7.870  -25.185 1.00 82.91  ? 254  ARG B C     1 
ATOM   1549 O  O     . ARG A 1 212 ? 21.975  -8.729  -25.858 1.00 82.04  ? 254  ARG B O     1 
ATOM   1550 C  CB    . ARG A 1 212 ? 24.176  -6.267  -26.234 1.00 84.19  ? 254  ARG B CB    1 
ATOM   1551 C  CG    . ARG A 1 212 ? 24.528  -7.088  -27.464 1.00 97.05  ? 254  ARG B CG    1 
ATOM   1552 C  CD    . ARG A 1 212 ? 23.716  -6.650  -28.671 1.00 92.33  ? 254  ARG B CD    1 
ATOM   1553 N  NE    . ARG A 1 212 ? 24.265  -7.176  -29.915 1.00 97.63  ? 254  ARG B NE    1 
ATOM   1554 C  CZ    . ARG A 1 212 ? 25.184  -6.560  -30.645 1.00 117.23 ? 254  ARG B CZ    1 
ATOM   1555 N  NH1   . ARG A 1 212 ? 25.681  -5.387  -30.286 1.00 113.01 ? 254  ARG B NH1   1 
ATOM   1556 N  NH2   . ARG A 1 212 ? 25.616  -7.134  -31.765 1.00 120.10 ? 254  ARG B NH2   1 
ATOM   1557 N  N     . LEU A 1 213 ? 23.034  -8.123  -23.964 1.00 84.87  ? 255  LEU B N     1 
ATOM   1558 C  CA    . LEU A 1 213 ? 22.846  -9.437  -23.353 1.00 91.93  ? 255  LEU B CA    1 
ATOM   1559 C  C     . LEU A 1 213 ? 21.369  -9.734  -23.127 1.00 80.00  ? 255  LEU B C     1 
ATOM   1560 O  O     . LEU A 1 213 ? 20.905  -10.852 -23.389 1.00 70.16  ? 255  LEU B O     1 
ATOM   1561 C  CB    . LEU A 1 213 ? 23.614  -9.521  -22.034 1.00 86.16  ? 255  LEU B CB    1 
ATOM   1562 C  CG    . LEU A 1 213 ? 25.138  -9.420  -22.113 1.00 87.81  ? 255  LEU B CG    1 
ATOM   1563 C  CD1   . LEU A 1 213 ? 25.758  -9.619  -20.741 1.00 75.16  ? 255  LEU B CD1   1 
ATOM   1564 C  CD2   . LEU A 1 213 ? 25.687  -10.429 -23.107 1.00 99.43  ? 255  LEU B CD2   1 
ATOM   1565 N  N     . ALA A 1 214 ? 20.615  -8.745  -22.639 1.00 71.89  ? 256  ALA B N     1 
ATOM   1566 C  CA    . ALA A 1 214 ? 19.194  -8.955  -22.381 1.00 69.57  ? 256  ALA B CA    1 
ATOM   1567 C  C     . ALA A 1 214 ? 18.436  -9.256  -23.668 1.00 79.64  ? 256  ALA B C     1 
ATOM   1568 O  O     . ALA A 1 214 ? 17.506  -10.071 -23.673 1.00 77.00  ? 256  ALA B O     1 
ATOM   1569 C  CB    . ALA A 1 214 ? 18.601  -7.731  -21.683 1.00 73.99  ? 256  ALA B CB    1 
ATOM   1570 N  N     . ASP A 1 215 ? 18.817  -8.607  -24.770 1.00 87.24  ? 257  ASP B N     1 
ATOM   1571 C  CA    . ASP A 1 215 ? 18.143  -8.865  -26.039 1.00 92.75  ? 257  ASP B CA    1 
ATOM   1572 C  C     . ASP A 1 215 ? 18.562  -10.205 -26.630 1.00 84.90  ? 257  ASP B C     1 
ATOM   1573 O  O     . ASP A 1 215 ? 17.740  -10.912 -27.224 1.00 84.25  ? 257  ASP B O     1 
ATOM   1574 C  CB    . ASP A 1 215 ? 18.427  -7.734  -27.028 1.00 104.72 ? 257  ASP B CB    1 
ATOM   1575 C  CG    . ASP A 1 215 ? 17.794  -6.421  -26.612 1.00 116.81 ? 257  ASP B CG    1 
ATOM   1576 O  OD1   . ASP A 1 215 ? 17.160  -6.378  -25.537 1.00 114.90 ? 257  ASP B OD1   1 
ATOM   1577 O  OD2   . ASP A 1 215 ? 17.929  -5.432  -27.364 1.00 109.57 ? 257  ASP B OD2   1 
ATOM   1578 N  N     . GLU A 1 216 ? 19.835  -10.576 -26.471 1.00 77.63  ? 258  GLU B N     1 
ATOM   1579 C  CA    . GLU A 1 216 ? 20.335  -11.795 -27.095 1.00 78.00  ? 258  GLU B CA    1 
ATOM   1580 C  C     . GLU A 1 216 ? 19.837  -13.037 -26.366 1.00 86.43  ? 258  GLU B C     1 
ATOM   1581 O  O     . GLU A 1 216 ? 19.275  -13.948 -26.986 1.00 90.09  ? 258  GLU B O     1 
ATOM   1582 C  CB    . GLU A 1 216 ? 21.864  -11.768 -27.133 1.00 85.97  ? 258  GLU B CB    1 
ATOM   1583 C  CG    . GLU A 1 216 ? 22.508  -12.978 -27.797 1.00 109.02 ? 258  GLU B CG    1 
ATOM   1584 C  CD    . GLU A 1 216 ? 22.528  -12.884 -29.314 1.00 129.55 ? 258  GLU B CD    1 
ATOM   1585 O  OE1   . GLU A 1 216 ? 21.475  -12.586 -29.917 1.00 116.74 ? 258  GLU B OE1   1 
ATOM   1586 O  OE2   . GLU A 1 216 ? 23.607  -13.102 -29.906 1.00 130.75 ? 258  GLU B OE2   1 
ATOM   1587 N  N     . PHE A 1 217 ? 20.033  -13.094 -25.050 1.00 93.18  ? 259  PHE B N     1 
ATOM   1588 C  CA    . PHE A 1 217 ? 19.729  -14.291 -24.278 1.00 82.63  ? 259  PHE B CA    1 
ATOM   1589 C  C     . PHE A 1 217 ? 18.367  -14.243 -23.599 1.00 83.03  ? 259  PHE B C     1 
ATOM   1590 O  O     . PHE A 1 217 ? 17.973  -15.229 -22.968 1.00 88.65  ? 259  PHE B O     1 
ATOM   1591 C  CB    . PHE A 1 217 ? 20.818  -14.526 -23.227 1.00 84.55  ? 259  PHE B CB    1 
ATOM   1592 C  CG    . PHE A 1 217 ? 22.203  -14.601 -23.799 1.00 80.36  ? 259  PHE B CG    1 
ATOM   1593 C  CD1   . PHE A 1 217 ? 22.671  -15.775 -24.364 1.00 87.70  ? 259  PHE B CD1   1 
ATOM   1594 C  CD2   . PHE A 1 217 ? 23.039  -13.497 -23.770 1.00 81.07  ? 259  PHE B CD2   1 
ATOM   1595 C  CE1   . PHE A 1 217 ? 23.946  -15.847 -24.892 1.00 91.06  ? 259  PHE B CE1   1 
ATOM   1596 C  CE2   . PHE A 1 217 ? 24.316  -13.562 -24.295 1.00 87.08  ? 259  PHE B CE2   1 
ATOM   1597 C  CZ    . PHE A 1 217 ? 24.770  -14.739 -24.857 1.00 88.08  ? 259  PHE B CZ    1 
ATOM   1598 N  N     . GLY A 1 218 ? 17.640  -13.134 -23.711 1.00 80.93  ? 260  GLY B N     1 
ATOM   1599 C  CA    . GLY A 1 218 ? 16.366  -13.019 -23.025 1.00 83.78  ? 260  GLY B CA    1 
ATOM   1600 C  C     . GLY A 1 218 ? 16.472  -13.035 -21.519 1.00 91.83  ? 260  GLY B C     1 
ATOM   1601 O  O     . GLY A 1 218 ? 15.495  -13.356 -20.838 1.00 75.66  ? 260  GLY B O     1 
ATOM   1602 N  N     . VAL A 1 219 ? 17.637  -12.699 -20.979 1.00 84.99  ? 261  VAL B N     1 
ATOM   1603 C  CA    . VAL A 1 219 ? 17.866  -12.737 -19.540 1.00 71.26  ? 261  VAL B CA    1 
ATOM   1604 C  C     . VAL A 1 219 ? 17.388  -11.434 -18.916 1.00 90.26  ? 261  VAL B C     1 
ATOM   1605 O  O     . VAL A 1 219 ? 17.603  -10.346 -19.464 1.00 93.32  ? 261  VAL B O     1 
ATOM   1606 C  CB    . VAL A 1 219 ? 19.356  -12.995 -19.246 1.00 80.38  ? 261  VAL B CB    1 
ATOM   1607 C  CG1   . VAL A 1 219 ? 20.232  -12.042 -20.048 1.00 87.10  ? 261  VAL B CG1   1 
ATOM   1608 C  CG2   . VAL A 1 219 ? 19.646  -12.863 -17.761 1.00 84.76  ? 261  VAL B CG2   1 
ATOM   1609 N  N     . ALA A 1 220 ? 16.719  -11.540 -17.769 1.00 91.77  ? 262  ALA B N     1 
ATOM   1610 C  CA    . ALA A 1 220 ? 16.302  -10.354 -17.032 1.00 65.88  ? 262  ALA B CA    1 
ATOM   1611 C  C     . ALA A 1 220 ? 17.513  -9.720  -16.362 1.00 70.71  ? 262  ALA B C     1 
ATOM   1612 O  O     . ALA A 1 220 ? 18.139  -10.332 -15.492 1.00 90.90  ? 262  ALA B O     1 
ATOM   1613 C  CB    . ALA A 1 220 ? 15.243  -10.716 -15.995 1.00 87.82  ? 262  ALA B CB    1 
ATOM   1614 N  N     . VAL A 1 221 ? 17.849  -8.500  -16.767 1.00 70.15  ? 263  VAL B N     1 
ATOM   1615 C  CA    . VAL A 1 221 ? 18.995  -7.779  -16.226 1.00 73.70  ? 263  VAL B CA    1 
ATOM   1616 C  C     . VAL A 1 221 ? 18.494  -6.818  -15.158 1.00 75.51  ? 263  VAL B C     1 
ATOM   1617 O  O     . VAL A 1 221 ? 17.748  -5.877  -15.458 1.00 76.04  ? 263  VAL B O     1 
ATOM   1618 C  CB    . VAL A 1 221 ? 19.764  -7.034  -17.328 1.00 81.54  ? 263  VAL B CB    1 
ATOM   1619 C  CG1   . VAL A 1 221 ? 20.930  -6.263  -16.730 1.00 72.59  ? 263  VAL B CG1   1 
ATOM   1620 C  CG2   . VAL A 1 221 ? 20.252  -8.013  -18.383 1.00 66.07  ? 263  VAL B CG2   1 
ATOM   1621 N  N     . VAL A 1 222 ? 18.899  -7.053  -13.913 1.00 82.09  ? 264  VAL B N     1 
ATOM   1622 C  CA    . VAL A 1 222 ? 18.529  -6.209  -12.783 1.00 70.91  ? 264  VAL B CA    1 
ATOM   1623 C  C     . VAL A 1 222 ? 19.792  -5.538  -12.264 1.00 76.45  ? 264  VAL B C     1 
ATOM   1624 O  O     . VAL A 1 222 ? 20.749  -6.219  -11.874 1.00 82.30  ? 264  VAL B O     1 
ATOM   1625 C  CB    . VAL A 1 222 ? 17.837  -7.014  -11.673 1.00 67.19  ? 264  VAL B CB    1 
ATOM   1626 C  CG1   . VAL A 1 222 ? 17.546  -6.123  -10.477 1.00 59.72  ? 264  VAL B CG1   1 
ATOM   1627 C  CG2   . VAL A 1 222 ? 16.557  -7.644  -12.196 1.00 71.09  ? 264  VAL B CG2   1 
ATOM   1628 N  N     . ILE A 1 223 ? 19.795  -4.208  -12.257 1.00 61.51  ? 265  ILE B N     1 
ATOM   1629 C  CA    . ILE A 1 223 ? 20.940  -3.433  -11.800 1.00 81.32  ? 265  ILE B CA    1 
ATOM   1630 C  C     . ILE A 1 223 ? 20.525  -2.599  -10.597 1.00 78.25  ? 265  ILE B C     1 
ATOM   1631 O  O     . ILE A 1 223 ? 19.371  -2.175  -10.474 1.00 69.91  ? 265  ILE B O     1 
ATOM   1632 C  CB    . ILE A 1 223 ? 21.511  -2.534  -12.918 1.00 81.37  ? 265  ILE B CB    1 
ATOM   1633 C  CG1   . ILE A 1 223 ? 20.429  -1.598  -13.461 1.00 82.56  ? 265  ILE B CG1   1 
ATOM   1634 C  CG2   . ILE A 1 223 ? 22.089  -3.384  -14.033 1.00 80.26  ? 265  ILE B CG2   1 
ATOM   1635 C  CD1   . ILE A 1 223 ? 20.914  -0.681  -14.563 1.00 91.60  ? 265  ILE B CD1   1 
ATOM   1636 N  N     . THR A 1 224 ? 21.482  -2.368  -9.704  1.00 99.75  ? 266  THR B N     1 
ATOM   1637 C  CA    . THR A 1 224 ? 21.268  -1.585  -8.496  1.00 93.44  ? 266  THR B CA    1 
ATOM   1638 C  C     . THR A 1 224 ? 22.022  -0.265  -8.604  1.00 91.18  ? 266  THR B C     1 
ATOM   1639 O  O     . THR A 1 224 ? 23.141  -0.222  -9.123  1.00 96.27  ? 266  THR B O     1 
ATOM   1640 C  CB    . THR A 1 224 ? 21.721  -2.373  -7.259  1.00 84.00  ? 266  THR B CB    1 
ATOM   1641 O  OG1   . THR A 1 224 ? 20.733  -3.356  -6.925  1.00 100.28 ? 266  THR B OG1   1 
ATOM   1642 C  CG2   . THR A 1 224 ? 21.958  -1.460  -6.065  1.00 105.52 ? 266  THR B CG2   1 
ATOM   1643 N  N     . ASN A 1 225 ? 21.396  0.816   -8.139  1.00 75.90  ? 267  ASN B N     1 
ATOM   1644 C  CA    . ASN A 1 225 ? 22.001  2.141   -8.171  1.00 90.85  ? 267  ASN B CA    1 
ATOM   1645 C  C     . ASN A 1 225 ? 21.821  2.817   -6.821  1.00 102.89 ? 267  ASN B C     1 
ATOM   1646 O  O     . ASN A 1 225 ? 20.695  2.929   -6.324  1.00 86.18  ? 267  ASN B O     1 
ATOM   1647 C  CB    . ASN A 1 225 ? 21.391  3.004   -9.280  1.00 99.76  ? 267  ASN B CB    1 
ATOM   1648 C  CG    . ASN A 1 225 ? 22.081  4.348   -9.419  1.00 98.87  ? 267  ASN B CG    1 
ATOM   1649 O  OD1   . ASN A 1 225 ? 23.257  4.492   -9.082  1.00 93.53  ? 267  ASN B OD1   1 
ATOM   1650 N  ND2   . ASN A 1 225 ? 21.351  5.340   -9.914  1.00 96.21  ? 267  ASN B ND2   1 
ATOM   1651 N  N     . GLN A 1 226 ? 22.928  3.266   -6.234  1.00 104.64 ? 268  GLN B N     1 
ATOM   1652 C  CA    . GLN A 1 226 ? 22.887  3.982   -4.966  1.00 104.33 ? 268  GLN B CA    1 
ATOM   1653 C  C     . GLN A 1 226 ? 22.568  5.452   -5.211  1.00 103.09 ? 268  GLN B C     1 
ATOM   1654 O  O     . GLN A 1 226 ? 23.189  6.097   -6.061  1.00 102.82 ? 268  GLN B O     1 
ATOM   1655 C  CB    . GLN A 1 226 ? 24.223  3.845   -4.234  1.00 106.39 ? 268  GLN B CB    1 
ATOM   1656 C  CG    . GLN A 1 226 ? 24.266  4.523   -2.872  1.00 114.78 ? 268  GLN B CG    1 
ATOM   1657 C  CD    . GLN A 1 226 ? 23.570  3.715   -1.794  1.00 111.14 ? 268  GLN B CD    1 
ATOM   1658 O  OE1   . GLN A 1 226 ? 22.729  4.234   -1.060  1.00 120.06 ? 268  GLN B OE1   1 
ATOM   1659 N  NE2   . GLN A 1 226 ? 23.925  2.440   -1.686  1.00 94.17  ? 268  GLN B NE2   1 
ATOM   1660 N  N     . VAL A 1 227 ? 21.599  5.979   -4.466  1.00 96.30  ? 269  VAL B N     1 
ATOM   1661 C  CA    . VAL A 1 227 ? 21.160  7.363   -4.599  1.00 100.64 ? 269  VAL B CA    1 
ATOM   1662 C  C     . VAL A 1 227 ? 21.363  8.064   -3.264  1.00 121.50 ? 269  VAL B C     1 
ATOM   1663 O  O     . VAL A 1 227 ? 20.869  7.598   -2.231  1.00 124.41 ? 269  VAL B O     1 
ATOM   1664 C  CB    . VAL A 1 227 ? 19.689  7.454   -5.045  1.00 106.84 ? 269  VAL B CB    1 
ATOM   1665 C  CG1   . VAL A 1 227 ? 19.217  8.900   -5.025  1.00 113.22 ? 269  VAL B CG1   1 
ATOM   1666 C  CG2   . VAL A 1 227 ? 19.519  6.853   -6.432  1.00 109.69 ? 269  VAL B CG2   1 
ATOM   1667 N  N     . VAL A 1 228 ? 22.088  9.178   -3.288  1.00 129.04 ? 270  VAL B N     1 
ATOM   1668 C  CA    . VAL A 1 228 ? 22.327  9.982   -2.094  1.00 132.68 ? 270  VAL B CA    1 
ATOM   1669 C  C     . VAL A 1 228 ? 21.228  11.035  -2.015  1.00 132.47 ? 270  VAL B C     1 
ATOM   1670 O  O     . VAL A 1 228 ? 21.180  11.956  -2.836  1.00 130.80 ? 270  VAL B O     1 
ATOM   1671 C  CB    . VAL A 1 228 ? 23.717  10.627  -2.117  1.00 127.97 ? 270  VAL B CB    1 
ATOM   1672 C  CG1   . VAL A 1 228 ? 23.954  11.421  -0.840  1.00 130.70 ? 270  VAL B CG1   1 
ATOM   1673 C  CG2   . VAL A 1 228 ? 24.793  9.567   -2.302  1.00 104.36 ? 270  VAL B CG2   1 
ATOM   1674 N  N     . ALA A 1 229 ? 20.347  10.896  -1.027  1.00 135.86 ? 271  ALA B N     1 
ATOM   1675 C  CA    . ALA A 1 229 ? 19.223  11.809  -0.822  1.00 133.14 ? 271  ALA B CA    1 
ATOM   1676 C  C     . ALA A 1 229 ? 18.364  11.941  -2.077  1.00 120.87 ? 271  ALA B C     1 
ATOM   1677 O  O     . ALA A 1 229 ? 17.172  12.237  -1.998  1.00 122.16 ? 271  ALA B O     1 
ATOM   1678 C  CB    . ALA A 1 229 ? 19.722  13.179  -0.373  1.00 126.10 ? 271  ALA B CB    1 
ATOM   1679 N  N     . ILE A 1 249 ? 21.869  5.534   -14.960 1.00 92.96  ? 291  ILE B N     1 
ATOM   1680 C  CA    . ILE A 1 249 ? 22.009  6.969   -15.173 1.00 120.84 ? 291  ILE B CA    1 
ATOM   1681 C  C     . ILE A 1 249 ? 21.371  7.355   -16.502 1.00 119.22 ? 291  ILE B C     1 
ATOM   1682 O  O     . ILE A 1 249 ? 20.261  7.886   -16.536 1.00 117.82 ? 291  ILE B O     1 
ATOM   1683 C  CB    . ILE A 1 249 ? 23.484  7.397   -15.120 1.00 125.96 ? 291  ILE B CB    1 
ATOM   1684 C  CG1   . ILE A 1 249 ? 24.130  6.913   -13.820 1.00 127.56 ? 291  ILE B CG1   1 
ATOM   1685 C  CG2   . ILE A 1 249 ? 23.606  8.908   -15.242 1.00 120.19 ? 291  ILE B CG2   1 
ATOM   1686 C  CD1   . ILE A 1 249 ? 23.451  7.428   -12.570 1.00 111.03 ? 291  ILE B CD1   1 
ATOM   1687 N  N     . ILE A 1 250 ? 22.078  7.085   -17.598 1.00 118.60 ? 292  ILE B N     1 
ATOM   1688 C  CA    . ILE A 1 250 ? 21.535  7.300   -18.934 1.00 126.99 ? 292  ILE B CA    1 
ATOM   1689 C  C     . ILE A 1 250 ? 20.571  6.164   -19.249 1.00 133.73 ? 292  ILE B C     1 
ATOM   1690 O  O     . ILE A 1 250 ? 20.865  5.291   -20.074 1.00 136.02 ? 292  ILE B O     1 
ATOM   1691 C  CB    . ILE A 1 250 ? 22.648  7.408   -19.995 1.00 130.89 ? 292  ILE B CB    1 
ATOM   1692 C  CG1   . ILE A 1 250 ? 23.769  6.392   -19.729 1.00 121.52 ? 292  ILE B CG1   1 
ATOM   1693 C  CG2   . ILE A 1 250 ? 23.188  8.833   -20.061 1.00 127.53 ? 292  ILE B CG2   1 
ATOM   1694 C  CD1   . ILE A 1 250 ? 24.966  6.949   -18.971 1.00 124.08 ? 292  ILE B CD1   1 
ATOM   1695 N  N     . ALA A 1 251 ? 19.412  6.173   -18.593 1.00 121.38 ? 293  ALA B N     1 
ATOM   1696 C  CA    . ALA A 1 251 ? 18.466  5.072   -18.712 1.00 112.65 ? 293  ALA B CA    1 
ATOM   1697 C  C     . ALA A 1 251 ? 17.904  4.991   -20.125 1.00 104.41 ? 293  ALA B C     1 
ATOM   1698 O  O     . ALA A 1 251 ? 17.428  5.988   -20.677 1.00 114.59 ? 293  ALA B O     1 
ATOM   1699 C  CB    . ALA A 1 251 ? 17.332  5.239   -17.702 1.00 111.59 ? 293  ALA B CB    1 
ATOM   1700 N  N     . HIS A 1 252 ? 17.965  3.798   -20.710 1.00 85.09  ? 294  HIS B N     1 
ATOM   1701 C  CA    . HIS A 1 252 ? 17.378  3.571   -22.019 1.00 97.53  ? 294  HIS B CA    1 
ATOM   1702 C  C     . HIS A 1 252 ? 15.858  3.694   -21.942 1.00 102.49 ? 294  HIS B C     1 
ATOM   1703 O  O     . HIS A 1 252 ? 15.252  3.605   -20.870 1.00 111.94 ? 294  HIS B O     1 
ATOM   1704 C  CB    . HIS A 1 252 ? 17.781  2.194   -22.551 1.00 100.08 ? 294  HIS B CB    1 
ATOM   1705 C  CG    . HIS A 1 252 ? 17.398  1.957   -23.979 1.00 96.32  ? 294  HIS B CG    1 
ATOM   1706 N  ND1   . HIS A 1 252 ? 16.560  0.932   -24.364 1.00 103.21 ? 294  HIS B ND1   1 
ATOM   1707 C  CD2   . HIS A 1 252 ? 17.736  2.613   -25.114 1.00 102.86 ? 294  HIS B CD2   1 
ATOM   1708 C  CE1   . HIS A 1 252 ? 16.401  0.965   -25.675 1.00 89.96  ? 294  HIS B CE1   1 
ATOM   1709 N  NE2   . HIS A 1 252 ? 17.103  1.976   -26.154 1.00 99.09  ? 294  HIS B NE2   1 
ATOM   1710 N  N     . ALA A 1 253 ? 15.240  3.907   -23.107 1.00 103.04 ? 295  ALA B N     1 
ATOM   1711 C  CA    . ALA A 1 253 ? 13.798  4.125   -23.148 1.00 95.81  ? 295  ALA B CA    1 
ATOM   1712 C  C     . ALA A 1 253 ? 13.022  2.893   -22.698 1.00 92.70  ? 295  ALA B C     1 
ATOM   1713 O  O     . ALA A 1 253 ? 11.936  3.023   -22.121 1.00 90.93  ? 295  ALA B O     1 
ATOM   1714 C  CB    . ALA A 1 253 ? 13.373  4.542   -24.556 1.00 93.57  ? 295  ALA B CB    1 
ATOM   1715 N  N     . SER A 1 254 ? 13.555  1.698   -22.945 1.00 97.57  ? 296  SER B N     1 
ATOM   1716 C  CA    . SER A 1 254 ? 12.887  0.458   -22.572 1.00 96.61  ? 296  SER B CA    1 
ATOM   1717 C  C     . SER A 1 254 ? 13.197  0.018   -21.146 1.00 95.92  ? 296  SER B C     1 
ATOM   1718 O  O     . SER A 1 254 ? 12.647  -0.992  -20.692 1.00 80.97  ? 296  SER B O     1 
ATOM   1719 C  CB    . SER A 1 254 ? 13.269  -0.662  -23.547 1.00 84.31  ? 296  SER B CB    1 
ATOM   1720 O  OG    . SER A 1 254 ? 14.660  -0.929  -23.500 1.00 87.68  ? 296  SER B OG    1 
ATOM   1721 N  N     . THR A 1 255 ? 14.052  0.746   -20.433 1.00 93.92  ? 297  THR B N     1 
ATOM   1722 C  CA    . THR A 1 255 ? 14.424  0.358   -19.079 1.00 83.30  ? 297  THR B CA    1 
ATOM   1723 C  C     . THR A 1 255 ? 13.288  0.657   -18.108 1.00 87.24  ? 297  THR B C     1 
ATOM   1724 O  O     . THR A 1 255 ? 12.724  1.755   -18.114 1.00 95.32  ? 297  THR B O     1 
ATOM   1725 C  CB    . THR A 1 255 ? 15.694  1.093   -18.649 1.00 82.31  ? 297  THR B CB    1 
ATOM   1726 O  OG1   . THR A 1 255 ? 16.772  0.741   -19.526 1.00 87.01  ? 297  THR B OG1   1 
ATOM   1727 C  CG2   . THR A 1 255 ? 16.071  0.729   -17.220 1.00 86.34  ? 297  THR B CG2   1 
ATOM   1728 N  N     . THR A 1 256 ? 12.950  -0.324  -17.274 1.00 83.61  ? 298  THR B N     1 
ATOM   1729 C  CA    . THR A 1 256 ? 11.943  -0.146  -16.235 1.00 88.98  ? 298  THR B CA    1 
ATOM   1730 C  C     . THR A 1 256 ? 12.638  0.274   -14.945 1.00 94.08  ? 298  THR B C     1 
ATOM   1731 O  O     . THR A 1 256 ? 13.519  -0.438  -14.450 1.00 96.76  ? 298  THR B O     1 
ATOM   1732 C  CB    . THR A 1 256 ? 11.141  -1.429  -16.025 1.00 87.97  ? 298  THR B CB    1 
ATOM   1733 O  OG1   . THR A 1 256 ? 10.499  -1.800  -17.252 1.00 117.71 ? 298  THR B OG1   1 
ATOM   1734 C  CG2   . THR A 1 256 ? 10.085  -1.223  -14.951 1.00 92.44  ? 298  THR B CG2   1 
ATOM   1735 N  N     . ARG A 1 257 ? 12.239  1.419   -14.401 1.00 89.19  ? 299  ARG B N     1 
ATOM   1736 C  CA    . ARG A 1 257 ? 12.929  2.041   -13.277 1.00 106.25 ? 299  ARG B CA    1 
ATOM   1737 C  C     . ARG A 1 257 ? 12.049  1.978   -12.035 1.00 103.20 ? 299  ARG B C     1 
ATOM   1738 O  O     . ARG A 1 257 ? 10.905  2.448   -12.050 1.00 100.24 ? 299  ARG B O     1 
ATOM   1739 C  CB    . ARG A 1 257 ? 13.302  3.486   -13.609 1.00 107.13 ? 299  ARG B CB    1 
ATOM   1740 C  CG    . ARG A 1 257 ? 13.985  3.635   -14.959 1.00 111.35 ? 299  ARG B CG    1 
ATOM   1741 C  CD    . ARG A 1 257 ? 14.473  5.056   -15.202 1.00 126.74 ? 299  ARG B CD    1 
ATOM   1742 N  NE    . ARG A 1 257 ? 15.589  5.407   -14.333 1.00 127.07 ? 299  ARG B NE    1 
ATOM   1743 C  CZ    . ARG A 1 257 ? 16.273  6.540   -14.413 1.00 136.20 ? 299  ARG B CZ    1 
ATOM   1744 N  NH1   . ARG A 1 257 ? 15.985  7.460   -15.319 1.00 139.66 ? 299  ARG B NH1   1 
ATOM   1745 N  NH2   . ARG A 1 257 ? 17.274  6.755   -13.564 1.00 131.17 ? 299  ARG B NH2   1 
ATOM   1746 N  N     . LEU A 1 258 ? 12.591  1.408   -10.962 1.00 96.68  ? 300  LEU B N     1 
ATOM   1747 C  CA    . LEU A 1 258 ? 11.908  1.292   -9.683  1.00 96.42  ? 300  LEU B CA    1 
ATOM   1748 C  C     . LEU A 1 258 ? 12.662  2.093   -8.631  1.00 96.13  ? 300  LEU B C     1 
ATOM   1749 O  O     . LEU A 1 258 ? 13.898  2.090   -8.598  1.00 90.44  ? 300  LEU B O     1 
ATOM   1750 C  CB    . LEU A 1 258 ? 11.793  -0.174  -9.252  1.00 90.98  ? 300  LEU B CB    1 
ATOM   1751 C  CG    . LEU A 1 258 ? 11.145  -1.113  -10.273 1.00 72.90  ? 300  LEU B CG    1 
ATOM   1752 C  CD1   . LEU A 1 258 ? 11.128  -2.545  -9.759  1.00 66.96  ? 300  LEU B CD1   1 
ATOM   1753 C  CD2   . LEU A 1 258 ? 9.739   -0.646  -10.618 1.00 73.69  ? 300  LEU B CD2   1 
ATOM   1754 N  N     . TYR A 1 259 ? 11.908  2.786   -7.782  1.00 87.35  ? 301  TYR B N     1 
ATOM   1755 C  CA    . TYR A 1 259 ? 12.451  3.632   -6.727  1.00 105.38 ? 301  TYR B CA    1 
ATOM   1756 C  C     . TYR A 1 259 ? 12.030  3.058   -5.384  1.00 97.94  ? 301  TYR B C     1 
ATOM   1757 O  O     . TYR A 1 259 ? 10.832  2.936   -5.105  1.00 91.16  ? 301  TYR B O     1 
ATOM   1758 C  CB    . TYR A 1 259 ? 11.964  5.075   -6.883  1.00 96.76  ? 301  TYR B CB    1 
ATOM   1759 C  CG    . TYR A 1 259 ? 12.204  5.951   -5.674  1.00 114.97 ? 301  TYR B CG    1 
ATOM   1760 C  CD1   . TYR A 1 259 ? 13.460  6.484   -5.415  1.00 106.96 ? 301  TYR B CD1   1 
ATOM   1761 C  CD2   . TYR A 1 259 ? 11.169  6.257   -4.799  1.00 113.65 ? 301  TYR B CD2   1 
ATOM   1762 C  CE1   . TYR A 1 259 ? 13.681  7.289   -4.313  1.00 102.88 ? 301  TYR B CE1   1 
ATOM   1763 C  CE2   . TYR A 1 259 ? 11.380  7.061   -3.696  1.00 109.34 ? 301  TYR B CE2   1 
ATOM   1764 C  CZ    . TYR A 1 259 ? 12.637  7.574   -3.457  1.00 116.64 ? 301  TYR B CZ    1 
ATOM   1765 O  OH    . TYR A 1 259 ? 12.851  8.376   -2.359  1.00 129.83 ? 301  TYR B OH    1 
ATOM   1766 N  N     . LEU A 1 260 ? 13.012  2.699   -4.563  1.00 92.34  ? 302  LEU B N     1 
ATOM   1767 C  CA    . LEU A 1 260 ? 12.769  2.108   -3.254  1.00 104.75 ? 302  LEU B CA    1 
ATOM   1768 C  C     . LEU A 1 260 ? 12.949  3.167   -2.175  1.00 97.72  ? 302  LEU B C     1 
ATOM   1769 O  O     . LEU A 1 260 ? 13.947  3.895   -2.174  1.00 87.56  ? 302  LEU B O     1 
ATOM   1770 C  CB    . LEU A 1 260 ? 13.714  0.931   -3.005  1.00 92.74  ? 302  LEU B CB    1 
ATOM   1771 C  CG    . LEU A 1 260 ? 13.705  -0.176  -4.063  1.00 80.57  ? 302  LEU B CG    1 
ATOM   1772 C  CD1   . LEU A 1 260 ? 14.653  -1.301  -3.675  1.00 64.85  ? 302  LEU B CD1   1 
ATOM   1773 C  CD2   . LEU A 1 260 ? 12.296  -0.706  -4.276  1.00 93.08  ? 302  LEU B CD2   1 
ATOM   1774 N  N     . ARG A 1 261 ? 11.987  3.248   -1.257  1.00 101.31 ? 303  ARG B N     1 
ATOM   1775 C  CA    . ARG A 1 261 ? 12.031  4.221   -0.178  1.00 98.30  ? 303  ARG B CA    1 
ATOM   1776 C  C     . ARG A 1 261 ? 11.559  3.557   1.106   1.00 96.85  ? 303  ARG B C     1 
ATOM   1777 O  O     . ARG A 1 261 ? 10.780  2.602   1.078   1.00 85.14  ? 303  ARG B O     1 
ATOM   1778 C  CB    . ARG A 1 261 ? 11.163  5.448   -0.501  1.00 91.01  ? 303  ARG B CB    1 
ATOM   1779 C  CG    . ARG A 1 261 ? 11.344  6.627   0.443   1.00 119.44 ? 303  ARG B CG    1 
ATOM   1780 C  CD    . ARG A 1 261 ? 10.428  7.788   0.075   1.00 115.20 ? 303  ARG B CD    1 
ATOM   1781 N  NE    . ARG A 1 261 ? 9.018   7.464   0.256   1.00 115.95 ? 303  ARG B NE    1 
ATOM   1782 C  CZ    . ARG A 1 261 ? 8.197   7.105   -0.723  1.00 108.00 ? 303  ARG B CZ    1 
ATOM   1783 N  NH1   . ARG A 1 261 ? 8.612   7.017   -1.976  1.00 114.30 ? 303  ARG B NH1   1 
ATOM   1784 N  NH2   . ARG A 1 261 ? 6.928   6.830   -0.437  1.00 105.95 ? 303  ARG B NH2   1 
ATOM   1785 N  N     . LYS A 1 262 ? 12.050  4.061   2.235   1.00 103.38 ? 304  LYS B N     1 
ATOM   1786 C  CA    . LYS A 1 262 ? 11.620  3.578   3.539   1.00 107.09 ? 304  LYS B CA    1 
ATOM   1787 C  C     . LYS A 1 262 ? 10.457  4.427   4.035   1.00 97.02  ? 304  LYS B C     1 
ATOM   1788 O  O     . LYS A 1 262 ? 10.545  5.659   4.058   1.00 98.80  ? 304  LYS B O     1 
ATOM   1789 C  CB    . LYS A 1 262 ? 12.771  3.613   4.544   1.00 95.71  ? 304  LYS B CB    1 
ATOM   1790 C  CG    . LYS A 1 262 ? 12.397  3.084   5.920   1.00 117.48 ? 304  LYS B CG    1 
ATOM   1791 C  CD    . LYS A 1 262 ? 13.568  3.152   6.885   1.00 136.33 ? 304  LYS B CD    1 
ATOM   1792 C  CE    . LYS A 1 262 ? 13.184  2.613   8.254   1.00 117.62 ? 304  LYS B CE    1 
ATOM   1793 N  NZ    . LYS A 1 262 ? 14.317  2.680   9.218   1.00 116.06 ? 304  LYS B NZ    1 
ATOM   1794 N  N     . GLY A 1 263 ? 9.370   3.766   4.421   1.00 93.66  ? 305  GLY B N     1 
ATOM   1795 C  CA    . GLY A 1 263 ? 8.215   4.464   4.948   1.00 118.03 ? 305  GLY B CA    1 
ATOM   1796 C  C     . GLY A 1 263 ? 8.288   4.648   6.449   1.00 134.65 ? 305  GLY B C     1 
ATOM   1797 O  O     . GLY A 1 263 ? 9.319   5.070   6.980   1.00 122.60 ? 305  GLY B O     1 
ATOM   1798 N  N     . ARG A 1 264 ? 7.199   4.334   7.144   1.00 133.23 ? 306  ARG B N     1 
ATOM   1799 C  CA    . ARG A 1 264 ? 7.136   4.423   8.596   1.00 138.36 ? 306  ARG B CA    1 
ATOM   1800 C  C     . ARG A 1 264 ? 7.136   3.014   9.173   1.00 134.36 ? 306  ARG B C     1 
ATOM   1801 O  O     . ARG A 1 264 ? 6.207   2.237   8.925   1.00 130.44 ? 306  ARG B O     1 
ATOM   1802 C  CB    . ARG A 1 264 ? 5.896   5.198   9.045   1.00 133.42 ? 306  ARG B CB    1 
ATOM   1803 C  CG    . ARG A 1 264 ? 5.926   6.668   8.657   1.00 131.32 ? 306  ARG B CG    1 
ATOM   1804 C  CD    . ARG A 1 264 ? 4.728   7.421   9.212   1.00 137.23 ? 306  ARG B CD    1 
ATOM   1805 N  NE    . ARG A 1 264 ? 3.476   6.996   8.598   1.00 150.48 ? 306  ARG B NE    1 
ATOM   1806 C  CZ    . ARG A 1 264 ? 2.294   7.534   8.862   1.00 151.14 ? 306  ARG B CZ    1 
ATOM   1807 N  NH1   . ARG A 1 264 ? 2.163   8.524   9.730   1.00 125.42 ? 306  ARG B NH1   1 
ATOM   1808 N  NH2   . ARG A 1 264 ? 1.215   7.069   8.238   1.00 155.65 ? 306  ARG B NH2   1 
ATOM   1809 N  N     . GLY A 1 265 ? 8.175   2.689   9.931   1.00 132.90 ? 307  GLY B N     1 
ATOM   1810 C  CA    . GLY A 1 265 ? 8.304   1.362   10.509  1.00 127.72 ? 307  GLY B CA    1 
ATOM   1811 C  C     . GLY A 1 265 ? 9.003   0.416   9.553   1.00 127.25 ? 307  GLY B C     1 
ATOM   1812 O  O     . GLY A 1 265 ? 10.023  0.767   8.959   1.00 120.00 ? 307  GLY B O     1 
ATOM   1813 N  N     . GLU A 1 266 ? 8.451   -0.787  9.406   1.00 126.82 ? 308  GLU B N     1 
ATOM   1814 C  CA    . GLU A 1 266 ? 9.002   -1.785  8.500   1.00 142.99 ? 308  GLU B CA    1 
ATOM   1815 C  C     . GLU A 1 266 ? 8.459   -1.668  7.083   1.00 136.44 ? 308  GLU B C     1 
ATOM   1816 O  O     . GLU A 1 266 ? 8.961   -2.355  6.186   1.00 126.86 ? 308  GLU B O     1 
ATOM   1817 C  CB    . GLU A 1 266 ? 8.717   -3.194  9.031   1.00 141.84 ? 308  GLU B CB    1 
ATOM   1818 C  CG    . GLU A 1 266 ? 9.263   -3.465  10.420  1.00 129.88 ? 308  GLU B CG    1 
ATOM   1819 C  CD    . GLU A 1 266 ? 8.837   -4.819  10.948  1.00 135.08 ? 308  GLU B CD    1 
ATOM   1820 O  OE1   . GLU A 1 266 ? 7.855   -5.380  10.419  1.00 137.62 ? 308  GLU B OE1   1 
ATOM   1821 O  OE2   . GLU A 1 266 ? 9.488   -5.327  11.884  1.00 134.95 ? 308  GLU B OE2   1 
ATOM   1822 N  N     . THR A 1 267 ? 7.458   -0.821  6.861   1.00 133.37 ? 309  THR B N     1 
ATOM   1823 C  CA    . THR A 1 267 ? 6.829   -0.713  5.550   1.00 126.00 ? 309  THR B CA    1 
ATOM   1824 C  C     . THR A 1 267 ? 7.756   0.006   4.578   1.00 125.28 ? 309  THR B C     1 
ATOM   1825 O  O     . THR A 1 267 ? 8.102   1.174   4.787   1.00 120.61 ? 309  THR B O     1 
ATOM   1826 C  CB    . THR A 1 267 ? 5.499   0.028   5.665   1.00 124.65 ? 309  THR B CB    1 
ATOM   1827 O  OG1   . THR A 1 267 ? 4.624   -0.686  6.547   1.00 136.85 ? 309  THR B OG1   1 
ATOM   1828 C  CG2   . THR A 1 267 ? 4.842   0.156   4.300   1.00 106.52 ? 309  THR B CG2   1 
ATOM   1829 N  N     . ARG A 1 268 ? 8.157   -0.689  3.517   1.00 120.11 ? 310  ARG B N     1 
ATOM   1830 C  CA    . ARG A 1 268 ? 8.949   -0.098  2.449   1.00 98.71  ? 310  ARG B CA    1 
ATOM   1831 C  C     . ARG A 1 268 ? 8.064   0.125   1.230   1.00 94.11  ? 310  ARG B C     1 
ATOM   1832 O  O     . ARG A 1 268 ? 7.173   -0.680  0.944   1.00 104.90 ? 310  ARG B O     1 
ATOM   1833 C  CB    . ARG A 1 268 ? 10.136  -0.993  2.089   1.00 97.79  ? 310  ARG B CB    1 
ATOM   1834 C  CG    . ARG A 1 268 ? 11.004  -1.364  3.281   1.00 101.51 ? 310  ARG B CG    1 
ATOM   1835 C  CD    . ARG A 1 268 ? 12.192  -2.216  2.868   1.00 102.13 ? 310  ARG B CD    1 
ATOM   1836 N  NE    . ARG A 1 268 ? 12.935  -2.702  4.025   1.00 118.89 ? 310  ARG B NE    1 
ATOM   1837 C  CZ    . ARG A 1 268 ? 13.917  -2.038  4.619   1.00 120.50 ? 310  ARG B CZ    1 
ATOM   1838 N  NH1   . ARG A 1 268 ? 14.308  -0.850  4.187   1.00 113.02 ? 310  ARG B NH1   1 
ATOM   1839 N  NH2   . ARG A 1 268 ? 14.521  -2.579  5.673   1.00 114.91 ? 310  ARG B NH2   1 
ATOM   1840 N  N     . ILE A 1 269 ? 8.304   1.224   0.519   1.00 94.92  ? 311  ILE B N     1 
ATOM   1841 C  CA    . ILE A 1 269 ? 7.465   1.640   -0.598  1.00 108.32 ? 311  ILE B CA    1 
ATOM   1842 C  C     . ILE A 1 269 ? 8.284   1.587   -1.880  1.00 94.38  ? 311  ILE B C     1 
ATOM   1843 O  O     . ILE A 1 269 ? 9.361   2.190   -1.964  1.00 100.36 ? 311  ILE B O     1 
ATOM   1844 C  CB    . ILE A 1 269 ? 6.882   3.048   -0.373  1.00 111.84 ? 311  ILE B CB    1 
ATOM   1845 C  CG1   . ILE A 1 269 ? 5.930   3.038   0.826   1.00 93.49  ? 311  ILE B CG1   1 
ATOM   1846 C  CG2   . ILE A 1 269 ? 6.173   3.540   -1.626  1.00 97.58  ? 311  ILE B CG2   1 
ATOM   1847 C  CD1   . ILE A 1 269 ? 5.265   4.369   1.097   1.00 92.44  ? 311  ILE B CD1   1 
ATOM   1848 N  N     . CYS A 1 270 ? 7.769   0.868   -2.872  1.00 97.00  ? 312  CYS B N     1 
ATOM   1849 C  CA    . CYS A 1 270 ? 8.373   0.783   -4.195  1.00 102.55 ? 312  CYS B CA    1 
ATOM   1850 C  C     . CYS A 1 270 ? 7.491   1.519   -5.193  1.00 88.98  ? 312  CYS B C     1 
ATOM   1851 O  O     . CYS A 1 270 ? 6.293   1.232   -5.298  1.00 94.14  ? 312  CYS B O     1 
ATOM   1852 C  CB    . CYS A 1 270 ? 8.558   -0.675  -4.623  1.00 111.57 ? 312  CYS B CB    1 
ATOM   1853 S  SG    . CYS A 1 270 ? 9.203   -0.885  -6.300  1.00 103.53 ? 312  CYS B SG    1 
ATOM   1854 N  N     . LYS A 1 271 ? 8.083   2.463   -5.919  1.00 95.31  ? 313  LYS B N     1 
ATOM   1855 C  CA    . LYS A 1 271 ? 7.370   3.283   -6.885  1.00 101.85 ? 313  LYS B CA    1 
ATOM   1856 C  C     . LYS A 1 271 ? 7.919   3.035   -8.283  1.00 99.20  ? 313  LYS B C     1 
ATOM   1857 O  O     . LYS A 1 271 ? 9.116   2.796   -8.463  1.00 100.28 ? 313  LYS B O     1 
ATOM   1858 C  CB    . LYS A 1 271 ? 7.485   4.774   -6.531  1.00 108.61 ? 313  LYS B CB    1 
ATOM   1859 C  CG    . LYS A 1 271 ? 6.733   5.710   -7.465  1.00 105.11 ? 313  LYS B CG    1 
ATOM   1860 C  CD    . LYS A 1 271 ? 6.907   7.163   -7.051  1.00 101.93 ? 313  LYS B CD    1 
ATOM   1861 C  CE    . LYS A 1 271 ? 6.186   8.100   -8.007  1.00 125.06 ? 313  LYS B CE    1 
ATOM   1862 N  NZ    . LYS A 1 271 ? 4.722   7.831   -8.054  1.00 128.48 ? 313  LYS B NZ    1 
ATOM   1863 N  N     . ILE A 1 272 ? 7.034   3.084   -9.276  1.00 100.37 ? 314  ILE B N     1 
ATOM   1864 C  CA    . ILE A 1 272 ? 7.424   2.948   -10.675 1.00 86.92  ? 314  ILE B CA    1 
ATOM   1865 C  C     . ILE A 1 272 ? 7.818   4.338   -11.164 1.00 93.33  ? 314  ILE B C     1 
ATOM   1866 O  O     . ILE A 1 272 ? 6.962   5.167   -11.476 1.00 111.64 ? 314  ILE B O     1 
ATOM   1867 C  CB    . ILE A 1 272 ? 6.304   2.342   -11.522 1.00 97.74  ? 314  ILE B CB    1 
ATOM   1868 C  CG1   . ILE A 1 272 ? 5.924   0.958   -10.992 1.00 92.26  ? 314  ILE B CG1   1 
ATOM   1869 C  CG2   . ILE A 1 272 ? 6.726   2.256   -12.981 1.00 106.82 ? 314  ILE B CG2   1 
ATOM   1870 C  CD1   . ILE A 1 272 ? 4.822   0.284   -11.780 1.00 87.79  ? 314  ILE B CD1   1 
ATOM   1871 N  N     . TYR A 1 273 ? 9.127   4.599   -11.224 1.00 94.38  ? 315  TYR B N     1 
ATOM   1872 C  CA    . TYR A 1 273 ? 9.594   5.922   -11.625 1.00 111.13 ? 315  TYR B CA    1 
ATOM   1873 C  C     . TYR A 1 273 ? 9.403   6.145   -13.120 1.00 119.51 ? 315  TYR B C     1 
ATOM   1874 O  O     . TYR A 1 273 ? 8.998   7.234   -13.545 1.00 123.56 ? 315  TYR B O     1 
ATOM   1875 C  CB    . TYR A 1 273 ? 11.062  6.093   -11.233 1.00 112.28 ? 315  TYR B CB    1 
ATOM   1876 C  CG    . TYR A 1 273 ? 11.673  7.414   -11.646 1.00 127.74 ? 315  TYR B CG    1 
ATOM   1877 C  CD1   . TYR A 1 273 ? 11.494  8.556   -10.876 1.00 123.22 ? 315  TYR B CD1   1 
ATOM   1878 C  CD2   . TYR A 1 273 ? 12.441  7.515   -12.800 1.00 133.91 ? 315  TYR B CD2   1 
ATOM   1879 C  CE1   . TYR A 1 273 ? 12.055  9.764   -11.248 1.00 139.47 ? 315  TYR B CE1   1 
ATOM   1880 C  CE2   . TYR A 1 273 ? 13.006  8.718   -13.180 1.00 141.13 ? 315  TYR B CE2   1 
ATOM   1881 C  CZ    . TYR A 1 273 ? 12.810  9.839   -12.401 1.00 147.85 ? 315  TYR B CZ    1 
ATOM   1882 O  OH    . TYR A 1 273 ? 13.371  11.038  -12.776 1.00 143.98 ? 315  TYR B OH    1 
ATOM   1883 N  N     . ASP A 1 274 ? 9.686   5.128   -13.932 1.00 117.69 ? 316  ASP B N     1 
ATOM   1884 C  CA    . ASP A 1 274 ? 9.523   5.231   -15.376 1.00 109.11 ? 316  ASP B CA    1 
ATOM   1885 C  C     . ASP A 1 274 ? 9.403   3.830   -15.953 1.00 114.47 ? 316  ASP B C     1 
ATOM   1886 O  O     . ASP A 1 274 ? 10.186  2.944   -15.598 1.00 113.78 ? 316  ASP B O     1 
ATOM   1887 C  CB    . ASP A 1 274 ? 10.700  5.977   -16.015 1.00 108.52 ? 316  ASP B CB    1 
ATOM   1888 C  CG    . ASP A 1 274 ? 10.560  6.104   -17.519 1.00 135.79 ? 316  ASP B CG    1 
ATOM   1889 O  OD1   . ASP A 1 274 ? 9.634   6.809   -17.973 1.00 133.47 ? 316  ASP B OD1   1 
ATOM   1890 O  OD2   . ASP A 1 274 ? 11.376  5.500   -18.247 1.00 136.37 ? 316  ASP B OD2   1 
ATOM   1891 N  N     . SER A 1 275 ? 8.424   3.634   -16.838 1.00 110.19 ? 317  SER B N     1 
ATOM   1892 C  CA    . SER A 1 275 ? 8.194   2.341   -17.458 1.00 108.70 ? 317  SER B CA    1 
ATOM   1893 C  C     . SER A 1 275 ? 7.529   2.554   -18.808 1.00 112.25 ? 317  SER B C     1 
ATOM   1894 O  O     . SER A 1 275 ? 6.626   3.396   -18.919 1.00 116.28 ? 317  SER B O     1 
ATOM   1895 C  CB    . SER A 1 275 ? 7.322   1.436   -16.584 1.00 106.82 ? 317  SER B CB    1 
ATOM   1896 O  OG    . SER A 1 275 ? 7.091   0.188   -17.215 1.00 109.59 ? 317  SER B OG    1 
ATOM   1897 N  N     . PRO A 1 276 ? 7.947   1.821   -19.843 1.00 97.28  ? 318  PRO B N     1 
ATOM   1898 C  CA    . PRO A 1 276 ? 7.312   1.995   -21.158 1.00 87.23  ? 318  PRO B CA    1 
ATOM   1899 C  C     . PRO A 1 276 ? 5.871   1.520   -21.197 1.00 100.00 ? 318  PRO B C     1 
ATOM   1900 O  O     . PRO A 1 276 ? 5.082   2.040   -21.995 1.00 104.13 ? 318  PRO B O     1 
ATOM   1901 C  CB    . PRO A 1 276 ? 8.202   1.162   -22.094 1.00 89.76  ? 318  PRO B CB    1 
ATOM   1902 C  CG    . PRO A 1 276 ? 9.480   0.944   -21.336 1.00 94.64  ? 318  PRO B CG    1 
ATOM   1903 C  CD    . PRO A 1 276 ? 9.089   0.894   -19.896 1.00 96.37  ? 318  PRO B CD    1 
ATOM   1904 N  N     . SER A 1 277 ? 5.501   0.551   -20.359 1.00 109.73 ? 319  SER B N     1 
ATOM   1905 C  CA    . SER A 1 277 ? 4.159   -0.011  -20.367 1.00 114.88 ? 319  SER B CA    1 
ATOM   1906 C  C     . SER A 1 277 ? 3.384   0.211   -19.078 1.00 121.01 ? 319  SER B C     1 
ATOM   1907 O  O     . SER A 1 277 ? 2.167   -0.007  -19.068 1.00 123.46 ? 319  SER B O     1 
ATOM   1908 C  CB    . SER A 1 277 ? 4.215   -1.521  -20.655 1.00 112.85 ? 319  SER B CB    1 
ATOM   1909 O  OG    . SER A 1 277 ? 5.049   -2.187  -19.723 1.00 107.79 ? 319  SER B OG    1 
ATOM   1910 N  N     . LEU A 1 278 ? 4.040   0.636   -17.996 1.00 117.95 ? 320  LEU B N     1 
ATOM   1911 C  CA    . LEU A 1 278 ? 3.355   0.806   -16.726 1.00 115.43 ? 320  LEU B CA    1 
ATOM   1912 C  C     . LEU A 1 278 ? 3.331   2.272   -16.309 1.00 120.11 ? 320  LEU B C     1 
ATOM   1913 O  O     . LEU A 1 278 ? 4.340   2.972   -16.448 1.00 118.55 ? 320  LEU B O     1 
ATOM   1914 C  CB    . LEU A 1 278 ? 4.029   -0.019  -15.623 1.00 118.20 ? 320  LEU B CB    1 
ATOM   1915 C  CG    . LEU A 1 278 ? 3.963   -1.541  -15.761 1.00 117.31 ? 320  LEU B CG    1 
ATOM   1916 C  CD1   . LEU A 1 278 ? 4.778   -2.212  -14.668 1.00 88.55  ? 320  LEU B CD1   1 
ATOM   1917 C  CD2   . LEU A 1 278 ? 2.519   -2.017  -15.723 1.00 114.35 ? 320  LEU B CD2   1 
ATOM   1918 N  N     . PRO A 1 279 ? 2.203   2.761   -15.805 1.00 121.07 ? 321  PRO B N     1 
ATOM   1919 C  CA    . PRO A 1 279 ? 2.148   4.130   -15.287 1.00 116.62 ? 321  PRO B CA    1 
ATOM   1920 C  C     . PRO A 1 279 ? 2.778   4.215   -13.902 1.00 120.48 ? 321  PRO B C     1 
ATOM   1921 O  O     . PRO A 1 279 ? 3.074   3.209   -13.256 1.00 119.43 ? 321  PRO B O     1 
ATOM   1922 C  CB    . PRO A 1 279 ? 0.647   4.424   -15.235 1.00 98.73  ? 321  PRO B CB    1 
ATOM   1923 C  CG    . PRO A 1 279 ? 0.028   3.087   -15.002 1.00 104.47 ? 321  PRO B CG    1 
ATOM   1924 C  CD    . PRO A 1 279 ? 0.892   2.091   -15.740 1.00 119.73 ? 321  PRO B CD    1 
ATOM   1925 N  N     . GLU A 1 280 ? 2.977   5.451   -13.451 1.00 119.67 ? 322  GLU B N     1 
ATOM   1926 C  CA    . GLU A 1 280 ? 3.593   5.684   -12.150 1.00 128.03 ? 322  GLU B CA    1 
ATOM   1927 C  C     . GLU A 1 280 ? 2.627   5.299   -11.036 1.00 126.61 ? 322  GLU B C     1 
ATOM   1928 O  O     . GLU A 1 280 ? 1.565   5.912   -10.884 1.00 121.29 ? 322  GLU B O     1 
ATOM   1929 C  CB    . GLU A 1 280 ? 4.015   7.145   -12.015 1.00 133.57 ? 322  GLU B CB    1 
ATOM   1930 C  CG    . GLU A 1 280 ? 5.090   7.577   -12.998 1.00 133.47 ? 322  GLU B CG    1 
ATOM   1931 C  CD    . GLU A 1 280 ? 5.752   8.881   -12.598 1.00 137.06 ? 322  GLU B CD    1 
ATOM   1932 O  OE1   . GLU A 1 280 ? 5.624   9.277   -11.420 1.00 131.27 ? 322  GLU B OE1   1 
ATOM   1933 O  OE2   . GLU A 1 280 ? 6.400   9.511   -13.460 1.00 135.56 ? 322  GLU B OE2   1 
ATOM   1934 N  N     . ALA A 1 281 ? 2.997   4.284   -10.259 1.00 123.46 ? 323  ALA B N     1 
ATOM   1935 C  CA    . ALA A 1 281 ? 2.197   3.838   -9.128  1.00 104.10 ? 323  ALA B CA    1 
ATOM   1936 C  C     . ALA A 1 281 ? 3.136   3.366   -8.028  1.00 103.53 ? 323  ALA B C     1 
ATOM   1937 O  O     . ALA A 1 281 ? 4.352   3.280   -8.216  1.00 103.52 ? 323  ALA B O     1 
ATOM   1938 C  CB    . ALA A 1 281 ? 1.217   2.732   -9.534  1.00 101.27 ? 323  ALA B CB    1 
ATOM   1939 N  N     . GLU A 1 282 ? 2.558   3.057   -6.869  1.00 124.07 ? 324  GLU B N     1 
ATOM   1940 C  CA    . GLU A 1 282 ? 3.329   2.652   -5.704  1.00 100.86 ? 324  GLU B CA    1 
ATOM   1941 C  C     . GLU A 1 282 ? 2.761   1.370   -5.113  1.00 98.95  ? 324  GLU B C     1 
ATOM   1942 O  O     . GLU A 1 282 ? 1.603   1.010   -5.340  1.00 101.75 ? 324  GLU B O     1 
ATOM   1943 C  CB    . GLU A 1 282 ? 3.351   3.749   -4.630  1.00 92.08  ? 324  GLU B CB    1 
ATOM   1944 C  CG    . GLU A 1 282 ? 4.057   5.024   -5.055  1.00 109.68 ? 324  GLU B CG    1 
ATOM   1945 C  CD    . GLU A 1 282 ? 4.157   6.035   -3.930  1.00 106.99 ? 324  GLU B CD    1 
ATOM   1946 O  OE1   . GLU A 1 282 ? 3.624   5.760   -2.834  1.00 103.90 ? 324  GLU B OE1   1 
ATOM   1947 O  OE2   . GLU A 1 282 ? 4.769   7.103   -4.141  1.00 113.06 ? 324  GLU B OE2   1 
ATOM   1948 N  N     . ALA A 1 283 ? 3.605   0.682   -4.347  1.00 93.92  ? 325  ALA B N     1 
ATOM   1949 C  CA    . ALA A 1 283 ? 3.205   -0.525  -3.639  1.00 100.12 ? 325  ALA B CA    1 
ATOM   1950 C  C     . ALA A 1 283 ? 4.037   -0.650  -2.372  1.00 100.24 ? 325  ALA B C     1 
ATOM   1951 O  O     . ALA A 1 283 ? 5.085   -0.015  -2.229  1.00 105.72 ? 325  ALA B O     1 
ATOM   1952 C  CB    . ALA A 1 283 ? 3.360   -1.775  -4.513  1.00 102.01 ? 325  ALA B CB    1 
ATOM   1953 N  N     . MET A 1 284 ? 3.558   -1.479  -1.450  1.00 99.16  ? 326  MET B N     1 
ATOM   1954 C  CA    . MET A 1 284 ? 4.213   -1.693  -0.170  1.00 113.43 ? 326  MET B CA    1 
ATOM   1955 C  C     . MET A 1 284 ? 4.761   -3.112  -0.082  1.00 111.52 ? 326  MET B C     1 
ATOM   1956 O  O     . MET A 1 284 ? 4.177   -4.058  -0.619  1.00 119.71 ? 326  MET B O     1 
ATOM   1957 C  CB    . MET A 1 284 ? 3.249   -1.435  0.993   1.00 113.03 ? 326  MET B CB    1 
ATOM   1958 C  CG    . MET A 1 284 ? 2.796   0.011   1.115   1.00 125.15 ? 326  MET B CG    1 
ATOM   1959 S  SD    . MET A 1 284 ? 1.674   0.278   2.501   1.00 140.30 ? 326  MET B SD    1 
ATOM   1960 C  CE    . MET A 1 284 ? 1.441   2.051   2.413   1.00 108.12 ? 326  MET B CE    1 
ATOM   1961 N  N     . PHE A 1 285 ? 5.893   -3.248  0.603   1.00 97.68  ? 327  PHE B N     1 
ATOM   1962 C  CA    . PHE A 1 285 ? 6.532   -4.544  0.786   1.00 105.83 ? 327  PHE B CA    1 
ATOM   1963 C  C     . PHE A 1 285 ? 7.425   -4.476  2.017   1.00 97.78  ? 327  PHE B C     1 
ATOM   1964 O  O     . PHE A 1 285 ? 7.628   -3.411  2.607   1.00 106.23 ? 327  PHE B O     1 
ATOM   1965 C  CB    . PHE A 1 285 ? 7.332   -4.957  -0.456  1.00 91.11  ? 327  PHE B CB    1 
ATOM   1966 C  CG    . PHE A 1 285 ? 8.601   -4.174  -0.651  1.00 84.89  ? 327  PHE B CG    1 
ATOM   1967 C  CD1   . PHE A 1 285 ? 8.570   -2.895  -1.182  1.00 95.10  ? 327  PHE B CD1   1 
ATOM   1968 C  CD2   . PHE A 1 285 ? 9.828   -4.723  -0.313  1.00 84.43  ? 327  PHE B CD2   1 
ATOM   1969 C  CE1   . PHE A 1 285 ? 9.736   -2.175  -1.364  1.00 87.91  ? 327  PHE B CE1   1 
ATOM   1970 C  CE2   . PHE A 1 285 ? 10.998  -4.009  -0.493  1.00 93.40  ? 327  PHE B CE2   1 
ATOM   1971 C  CZ    . PHE A 1 285 ? 10.952  -2.733  -1.019  1.00 89.40  ? 327  PHE B CZ    1 
ATOM   1972 N  N     . ALA A 1 286 ? 7.960   -5.635  2.396   1.00 96.25  ? 328  ALA B N     1 
ATOM   1973 C  CA    . ALA A 1 286 ? 8.818   -5.741  3.567   1.00 101.54 ? 328  ALA B CA    1 
ATOM   1974 C  C     . ALA A 1 286 ? 9.887   -6.794  3.308   1.00 90.56  ? 328  ALA B C     1 
ATOM   1975 O  O     . ALA A 1 286 ? 9.809   -7.573  2.354   1.00 97.16  ? 328  ALA B O     1 
ATOM   1976 C  CB    . ALA A 1 286 ? 8.010   -6.081  4.824   1.00 98.83  ? 328  ALA B CB    1 
ATOM   1977 N  N     . ILE A 1 287 ? 10.892  -6.808  4.180   1.00 92.10  ? 329  ILE B N     1 
ATOM   1978 C  CA    . ILE A 1 287 ? 12.013  -7.736  4.090   1.00 89.10  ? 329  ILE B CA    1 
ATOM   1979 C  C     . ILE A 1 287 ? 12.005  -8.572  5.362   1.00 103.88 ? 329  ILE B C     1 
ATOM   1980 O  O     . ILE A 1 287 ? 12.461  -8.119  6.419   1.00 101.20 ? 329  ILE B O     1 
ATOM   1981 C  CB    . ILE A 1 287 ? 13.353  -7.015  3.910   1.00 83.06  ? 329  ILE B CB    1 
ATOM   1982 C  CG1   . ILE A 1 287 ? 13.317  -6.122  2.671   1.00 89.84  ? 329  ILE B CG1   1 
ATOM   1983 C  CG2   . ILE A 1 287 ? 14.490  -8.022  3.810   1.00 94.22  ? 329  ILE B CG2   1 
ATOM   1984 C  CD1   . ILE A 1 287 ? 14.585  -5.331  2.464   1.00 95.80  ? 329  ILE B CD1   1 
ATOM   1985 N  N     . ASN A 1 288 ? 11.485  -9.793  5.270   1.00 94.93  ? 330  ASN B N     1 
ATOM   1986 C  CA    . ASN A 1 288 ? 11.507  -10.719 6.387   1.00 96.11  ? 330  ASN B CA    1 
ATOM   1987 C  C     . ASN A 1 288 ? 12.804  -11.526 6.356   1.00 98.44  ? 330  ASN B C     1 
ATOM   1988 O  O     . ASN A 1 288 ? 13.625  -11.398 5.443   1.00 83.35  ? 330  ASN B O     1 
ATOM   1989 C  CB    . ASN A 1 288 ? 10.282  -11.632 6.345   1.00 90.92  ? 330  ASN B CB    1 
ATOM   1990 C  CG    . ASN A 1 288 ? 8.986   -10.861 6.186   1.00 112.77 ? 330  ASN B CG    1 
ATOM   1991 O  OD1   . ASN A 1 288 ? 8.891   -9.696  6.574   1.00 104.91 ? 330  ASN B OD1   1 
ATOM   1992 N  ND2   . ASN A 1 288 ? 7.978   -11.510 5.613   1.00 104.69 ? 330  ASN B ND2   1 
ATOM   1993 N  N     . ALA A 1 289 ? 12.986  -12.381 7.366   1.00 107.18 ? 331  ALA B N     1 
ATOM   1994 C  CA    . ALA A 1 289 ? 14.206  -13.176 7.462   1.00 109.24 ? 331  ALA B CA    1 
ATOM   1995 C  C     . ALA A 1 289 ? 14.398  -14.095 6.263   1.00 100.65 ? 331  ALA B C     1 
ATOM   1996 O  O     . ALA A 1 289 ? 15.530  -14.510 5.991   1.00 95.90  ? 331  ALA B O     1 
ATOM   1997 C  CB    . ALA A 1 289 ? 14.198  -13.998 8.752   1.00 82.50  ? 331  ALA B CB    1 
ATOM   1998 N  N     . ASP A 1 290 ? 13.328  -14.416 5.539   1.00 92.68  ? 332  ASP B N     1 
ATOM   1999 C  CA    . ASP A 1 290 ? 13.406  -15.270 4.364   1.00 102.69 ? 332  ASP B CA    1 
ATOM   2000 C  C     . ASP A 1 290 ? 13.376  -14.484 3.058   1.00 101.98 ? 332  ASP B C     1 
ATOM   2001 O  O     . ASP A 1 290 ? 13.213  -15.084 1.991   1.00 95.41  ? 332  ASP B O     1 
ATOM   2002 C  CB    . ASP A 1 290 ? 12.274  -16.300 4.385   1.00 89.91  ? 332  ASP B CB    1 
ATOM   2003 C  CG    . ASP A 1 290 ? 10.909  -15.664 4.561   1.00 102.68 ? 332  ASP B CG    1 
ATOM   2004 O  OD1   . ASP A 1 290 ? 10.841  -14.430 4.737   1.00 109.29 ? 332  ASP B OD1   1 
ATOM   2005 O  OD2   . ASP A 1 290 ? 9.901   -16.401 4.525   1.00 103.35 ? 332  ASP B OD2   1 
ATOM   2006 N  N     . GLY A 1 291 ? 13.522  -13.161 3.115   1.00 99.01  ? 333  GLY B N     1 
ATOM   2007 C  CA    . GLY A 1 291 ? 13.594  -12.373 1.899   1.00 89.06  ? 333  GLY B CA    1 
ATOM   2008 C  C     . GLY A 1 291 ? 12.443  -11.409 1.698   1.00 94.30  ? 333  GLY B C     1 
ATOM   2009 O  O     . GLY A 1 291 ? 11.805  -10.979 2.662   1.00 101.24 ? 333  GLY B O     1 
ATOM   2010 N  N     . VAL A 1 292 ? 12.167  -11.063 0.440   1.00 86.99  ? 334  VAL B N     1 
ATOM   2011 C  CA    . VAL A 1 292 ? 11.124  -10.091 0.139   1.00 89.30  ? 334  VAL B CA    1 
ATOM   2012 C  C     . VAL A 1 292 ? 9.754   -10.717 0.360   1.00 97.90  ? 334  VAL B C     1 
ATOM   2013 O  O     . VAL A 1 292 ? 9.509   -11.873 -0.011  1.00 91.89  ? 334  VAL B O     1 
ATOM   2014 C  CB    . VAL A 1 292 ? 11.274  -9.578  -1.304  1.00 77.08  ? 334  VAL B CB    1 
ATOM   2015 C  CG1   . VAL A 1 292 ? 10.257  -8.482  -1.592  1.00 80.82  ? 334  VAL B CG1   1 
ATOM   2016 C  CG2   . VAL A 1 292 ? 12.686  -9.076  -1.538  1.00 74.01  ? 334  VAL B CG2   1 
ATOM   2017 N  N     . GLY A 1 293 ? 8.853   -9.955  0.970   1.00 94.00  ? 335  GLY B N     1 
ATOM   2018 C  CA    . GLY A 1 293 ? 7.502   -10.417 1.182   1.00 94.09  ? 335  GLY B CA    1 
ATOM   2019 C  C     . GLY A 1 293 ? 6.566   -9.251  1.405   1.00 102.83 ? 335  GLY B C     1 
ATOM   2020 O  O     . GLY A 1 293 ? 6.939   -8.088  1.240   1.00 99.65  ? 335  GLY B O     1 
ATOM   2021 N  N     . ASP A 1 294 ? 5.335   -9.580  1.782   1.00 106.30 ? 336  ASP B N     1 
ATOM   2022 C  CA    . ASP A 1 294 ? 4.353   -8.553  2.084   1.00 113.82 ? 336  ASP B CA    1 
ATOM   2023 C  C     . ASP A 1 294 ? 4.523   -8.055  3.516   1.00 116.60 ? 336  ASP B C     1 
ATOM   2024 O  O     . ASP A 1 294 ? 5.095   -8.732  4.376   1.00 112.90 ? 336  ASP B O     1 
ATOM   2025 C  CB    . ASP A 1 294 ? 2.934   -9.083  1.872   1.00 123.57 ? 336  ASP B CB    1 
ATOM   2026 C  CG    . ASP A 1 294 ? 2.626   -9.356  0.413   1.00 121.62 ? 336  ASP B CG    1 
ATOM   2027 O  OD1   . ASP A 1 294 ? 3.152   -8.626  -0.455  1.00 108.00 ? 336  ASP B OD1   1 
ATOM   2028 O  OD2   . ASP A 1 294 ? 1.857   -10.300 0.132   1.00 112.03 ? 336  ASP B OD2   1 
ATOM   2029 N  N     . ALA A 1 295 ? 4.019   -6.848  3.763   1.00 118.91 ? 337  ALA B N     1 
ATOM   2030 C  CA    . ALA A 1 295 ? 4.108   -6.235  5.084   1.00 131.14 ? 337  ALA B CA    1 
ATOM   2031 C  C     . ALA A 1 295 ? 3.245   -7.018  6.066   1.00 139.18 ? 337  ALA B C     1 
ATOM   2032 O  O     . ALA A 1 295 ? 2.014   -7.016  5.963   1.00 134.61 ? 337  ALA B O     1 
ATOM   2033 C  CB    . ALA A 1 295 ? 3.677   -4.774  5.018   1.00 126.26 ? 337  ALA B CB    1 
ATOM   2034 N  N     . LYS A 1 296 ? 3.887   -7.690  7.019   1.00 132.42 ? 338  LYS B N     1 
ATOM   2035 C  CA    . LYS A 1 296 ? 3.184   -8.490  8.020   1.00 134.92 ? 338  LYS B CA    1 
ATOM   2036 C  C     . LYS A 1 296 ? 2.660   -7.553  9.101   1.00 145.81 ? 338  LYS B C     1 
ATOM   2037 O  O     . LYS A 1 296 ? 3.354   -7.223  10.064  1.00 150.10 ? 338  LYS B O     1 
ATOM   2038 C  CB    . LYS A 1 296 ? 4.103   -9.559  8.599   1.00 127.94 ? 338  LYS B CB    1 
ATOM   2039 C  CG    . LYS A 1 296 ? 3.425   -10.485 9.595   1.00 127.66 ? 338  LYS B CG    1 
ATOM   2040 C  CD    . LYS A 1 296 ? 4.372   -11.575 10.069  1.00 126.44 ? 338  LYS B CD    1 
ATOM   2041 C  CE    . LYS A 1 296 ? 3.686   -12.509 11.053  1.00 122.24 ? 338  LYS B CE    1 
ATOM   2042 N  NZ    . LYS A 1 296 ? 4.590   -13.602 11.506  1.00 102.73 ? 338  LYS B NZ    1 
ATOM   2043 N  N     . ASP A 1 297 ? 1.414   -7.119  8.937   1.00 150.54 ? 339  ASP B N     1 
ATOM   2044 C  CA    . ASP A 1 297 ? 0.788   -6.207  9.887   1.00 156.63 ? 339  ASP B CA    1 
ATOM   2045 C  C     . ASP A 1 297 ? 0.113   -6.973  11.020  1.00 142.86 ? 339  ASP B C     1 
ATOM   2046 O  O     . ASP A 1 297 ? 0.596   -8.021  11.449  1.00 128.63 ? 339  ASP B O     1 
ATOM   2047 C  CB    . ASP A 1 297 ? -0.230  -5.311  9.177   1.00 136.50 ? 339  ASP B CB    1 
ATOM   2048 C  CG    . ASP A 1 297 ? 0.389   -4.504  8.051   1.00 142.38 ? 339  ASP B CG    1 
ATOM   2049 O  OD1   . ASP A 1 297 ? 1.593   -4.183  8.140   1.00 143.87 ? 339  ASP B OD1   1 
ATOM   2050 O  OD2   . ASP A 1 297 ? -0.328  -4.191  7.078   1.00 147.06 ? 339  ASP B OD2   1 
ATOM   2051 N  N     . SER B 2 1   ? -3.701  12.733  -54.845 1.00 147.24 ? 97   SER D N     1 
ATOM   2052 C  CA    . SER B 2 1   ? -4.784  12.625  -53.874 1.00 149.77 ? 97   SER D CA    1 
ATOM   2053 C  C     . SER B 2 1   ? -4.850  13.864  -52.988 1.00 138.24 ? 97   SER D C     1 
ATOM   2054 O  O     . SER B 2 1   ? -3.854  14.565  -52.808 1.00 123.98 ? 97   SER D O     1 
ATOM   2055 C  CB    . SER B 2 1   ? -4.609  11.372  -53.013 1.00 148.88 ? 97   SER D CB    1 
ATOM   2056 O  OG    . SER B 2 1   ? -3.395  11.419  -52.284 1.00 147.35 ? 97   SER D OG    1 
ATOM   2057 N  N     . GLU B 2 2   ? -6.031  14.130  -52.437 1.00 132.34 ? 98   GLU D N     1 
ATOM   2058 C  CA    . GLU B 2 2   ? -6.205  15.279  -51.564 1.00 146.95 ? 98   GLU D CA    1 
ATOM   2059 C  C     . GLU B 2 2   ? -5.553  15.026  -50.207 1.00 137.98 ? 98   GLU D C     1 
ATOM   2060 O  O     . GLU B 2 2   ? -5.367  13.884  -49.775 1.00 133.38 ? 98   GLU D O     1 
ATOM   2061 C  CB    . GLU B 2 2   ? -7.689  15.600  -51.388 1.00 151.04 ? 98   GLU D CB    1 
ATOM   2062 C  CG    . GLU B 2 2   ? -8.392  15.982  -52.681 1.00 155.32 ? 98   GLU D CG    1 
ATOM   2063 C  CD    . GLU B 2 2   ? -9.852  16.331  -52.471 1.00 172.90 ? 98   GLU D CD    1 
ATOM   2064 O  OE1   . GLU B 2 2   ? -10.327 16.241  -51.319 1.00 174.74 ? 98   GLU D OE1   1 
ATOM   2065 O  OE2   . GLU B 2 2   ? -10.525 16.696  -53.458 1.00 172.14 ? 98   GLU D OE2   1 
ATOM   2066 N  N     . ILE B 2 3   ? -5.207  16.117  -49.531 1.00 121.38 ? 99   ILE D N     1 
ATOM   2067 C  CA    . ILE B 2 3   ? -4.490  16.041  -48.262 1.00 122.47 ? 99   ILE D CA    1 
ATOM   2068 C  C     . ILE B 2 3   ? -5.480  15.747  -47.142 1.00 129.20 ? 99   ILE D C     1 
ATOM   2069 O  O     . ILE B 2 3   ? -6.432  16.504  -46.924 1.00 124.51 ? 99   ILE D O     1 
ATOM   2070 C  CB    . ILE B 2 3   ? -3.715  17.337  -47.987 1.00 107.99 ? 99   ILE D CB    1 
ATOM   2071 C  CG1   . ILE B 2 3   ? -2.575  17.501  -48.995 1.00 100.09 ? 99   ILE D CG1   1 
ATOM   2072 C  CG2   . ILE B 2 3   ? -3.184  17.346  -46.563 1.00 108.90 ? 99   ILE D CG2   1 
ATOM   2073 C  CD1   . ILE B 2 3   ? -1.741  18.745  -48.777 1.00 89.73  ? 99   ILE D CD1   1 
ATOM   2074 N  N     . ILE B 2 4   ? -5.255  14.648  -46.430 1.00 122.31 ? 100  ILE D N     1 
ATOM   2075 C  CA    . ILE B 2 4   ? -6.039  14.288  -45.256 1.00 111.57 ? 100  ILE D CA    1 
ATOM   2076 C  C     . ILE B 2 4   ? -5.247  14.678  -44.018 1.00 112.80 ? 100  ILE D C     1 
ATOM   2077 O  O     . ILE B 2 4   ? -4.011  14.632  -44.005 1.00 112.78 ? 100  ILE D O     1 
ATOM   2078 C  CB    . ILE B 2 4   ? -6.385  12.783  -45.249 1.00 105.92 ? 100  ILE D CB    1 
ATOM   2079 C  CG1   . ILE B 2 4   ? -6.907  12.346  -46.619 1.00 133.40 ? 100  ILE D CG1   1 
ATOM   2080 C  CG2   . ILE B 2 4   ? -7.415  12.470  -44.173 1.00 96.54  ? 100  ILE D CG2   1 
ATOM   2081 C  CD1   . ILE B 2 4   ? -7.235  10.869  -46.705 1.00 113.33 ? 100  ILE D CD1   1 
ATOM   2082 N  N     . GLN B 2 5   ? -5.958  15.081  -42.968 1.00 107.89 ? 101  GLN D N     1 
ATOM   2083 C  CA    . GLN B 2 5   ? -5.344  15.440  -41.698 1.00 102.70 ? 101  GLN D CA    1 
ATOM   2084 C  C     . GLN B 2 5   ? -5.893  14.536  -40.604 1.00 103.19 ? 101  GLN D C     1 
ATOM   2085 O  O     . GLN B 2 5   ? -7.109  14.341  -40.505 1.00 99.85  ? 101  GLN D O     1 
ATOM   2086 C  CB    . GLN B 2 5   ? -5.585  16.914  -41.365 1.00 94.57  ? 101  GLN D CB    1 
ATOM   2087 C  CG    . GLN B 2 5   ? -4.792  17.864  -42.250 1.00 102.53 ? 101  GLN D CG    1 
ATOM   2088 C  CD    . GLN B 2 5   ? -4.972  19.316  -41.864 1.00 112.56 ? 101  GLN D CD    1 
ATOM   2089 O  OE1   . GLN B 2 5   ? -6.014  19.706  -41.341 1.00 130.59 ? 101  GLN D OE1   1 
ATOM   2090 N  NE2   . GLN B 2 5   ? -3.951  20.127  -42.119 1.00 114.22 ? 101  GLN D NE2   1 
ATOM   2091 N  N     . ILE B 2 6   ? -4.994  13.989  -39.790 1.00 105.45 ? 102  ILE D N     1 
ATOM   2092 C  CA    . ILE B 2 6   ? -5.330  12.970  -38.802 1.00 99.15  ? 102  ILE D CA    1 
ATOM   2093 C  C     . ILE B 2 6   ? -5.510  13.631  -37.443 1.00 99.83  ? 102  ILE D C     1 
ATOM   2094 O  O     . ILE B 2 6   ? -4.671  14.433  -37.016 1.00 100.07 ? 102  ILE D O     1 
ATOM   2095 C  CB    . ILE B 2 6   ? -4.246  11.880  -38.742 1.00 74.73  ? 102  ILE D CB    1 
ATOM   2096 C  CG1   . ILE B 2 6   ? -4.029  11.269  -40.128 1.00 95.75  ? 102  ILE D CG1   1 
ATOM   2097 C  CG2   . ILE B 2 6   ? -4.625  10.803  -37.737 1.00 89.26  ? 102  ILE D CG2   1 
ATOM   2098 C  CD1   . ILE B 2 6   ? -2.942  10.218  -40.169 1.00 96.38  ? 102  ILE D CD1   1 
ATOM   2099 N  N     . THR B 2 7   ? -6.603  13.290  -36.763 1.00 99.20  ? 103  THR D N     1 
ATOM   2100 C  CA    . THR B 2 7   ? -6.848  13.794  -35.419 1.00 100.75 ? 103  THR D CA    1 
ATOM   2101 C  C     . THR B 2 7   ? -5.814  13.230  -34.450 1.00 103.04 ? 103  THR D C     1 
ATOM   2102 O  O     . THR B 2 7   ? -5.540  12.026  -34.450 1.00 98.66  ? 103  THR D O     1 
ATOM   2103 C  CB    . THR B 2 7   ? -8.262  13.425  -34.967 1.00 105.32 ? 103  THR D CB    1 
ATOM   2104 O  OG1   . THR B 2 7   ? -9.218  14.192  -35.709 1.00 120.04 ? 103  THR D OG1   1 
ATOM   2105 C  CG2   . THR B 2 7   ? -8.447  13.693  -33.481 1.00 99.35  ? 103  THR D CG2   1 
ATOM   2106 N  N     . THR B 2 8   ? -5.237  14.104  -33.627 1.00 105.00 ? 104  THR D N     1 
ATOM   2107 C  CA    . THR B 2 8   ? -4.208  13.706  -32.676 1.00 101.33 ? 104  THR D CA    1 
ATOM   2108 C  C     . THR B 2 8   ? -4.770  13.261  -31.332 1.00 102.15 ? 104  THR D C     1 
ATOM   2109 O  O     . THR B 2 8   ? -4.005  12.781  -30.488 1.00 106.04 ? 104  THR D O     1 
ATOM   2110 C  CB    . THR B 2 8   ? -3.222  14.857  -32.450 1.00 111.81 ? 104  THR D CB    1 
ATOM   2111 O  OG1   . THR B 2 8   ? -3.890  15.937  -31.784 1.00 113.51 ? 104  THR D OG1   1 
ATOM   2112 C  CG2   . THR B 2 8   ? -2.674  15.353  -33.780 1.00 109.78 ? 104  THR D CG2   1 
ATOM   2113 N  N     . GLY B 2 9   ? -6.075  13.405  -31.110 1.00 106.44 ? 105  GLY D N     1 
ATOM   2114 C  CA    . GLY B 2 9   ? -6.700  13.050  -29.858 1.00 105.63 ? 105  GLY D CA    1 
ATOM   2115 C  C     . GLY B 2 9   ? -6.887  14.206  -28.898 1.00 113.10 ? 105  GLY D C     1 
ATOM   2116 O  O     . GLY B 2 9   ? -7.710  14.106  -27.981 1.00 102.63 ? 105  GLY D O     1 
ATOM   2117 N  N     . SER B 2 10  ? -6.146  15.295  -29.083 1.00 116.57 ? 106  SER D N     1 
ATOM   2118 C  CA    . SER B 2 10  ? -6.251  16.482  -28.248 1.00 108.97 ? 106  SER D CA    1 
ATOM   2119 C  C     . SER B 2 10  ? -6.888  17.606  -29.051 1.00 122.51 ? 106  SER D C     1 
ATOM   2120 O  O     . SER B 2 10  ? -6.428  17.924  -30.153 1.00 122.65 ? 106  SER D O     1 
ATOM   2121 C  CB    . SER B 2 10  ? -4.876  16.911  -27.732 1.00 102.80 ? 106  SER D CB    1 
ATOM   2122 O  OG    . SER B 2 10  ? -4.935  18.183  -27.113 1.00 100.88 ? 106  SER D OG    1 
ATOM   2123 N  N     . LYS B 2 11  ? -7.947  18.204  -28.498 1.00 124.11 ? 107  LYS D N     1 
ATOM   2124 C  CA    . LYS B 2 11  ? -8.641  19.280  -29.200 1.00 126.54 ? 107  LYS D CA    1 
ATOM   2125 C  C     . LYS B 2 11  ? -7.724  20.475  -29.428 1.00 128.05 ? 107  LYS D C     1 
ATOM   2126 O  O     . LYS B 2 11  ? -7.704  21.052  -30.522 1.00 118.56 ? 107  LYS D O     1 
ATOM   2127 C  CB    . LYS B 2 11  ? -9.885  19.701  -28.418 1.00 133.25 ? 107  LYS D CB    1 
ATOM   2128 C  CG    . LYS B 2 11  ? -10.609 20.902  -29.005 1.00 147.84 ? 107  LYS D CG    1 
ATOM   2129 C  CD    . LYS B 2 11  ? -11.740 21.363  -28.100 1.00 140.44 ? 107  LYS D CD    1 
ATOM   2130 C  CE    . LYS B 2 11  ? -12.413 22.609  -28.652 1.00 142.33 ? 107  LYS D CE    1 
ATOM   2131 N  NZ    . LYS B 2 11  ? -13.491 23.103  -27.752 1.00 140.66 ? 107  LYS D NZ    1 
ATOM   2132 N  N     . GLU B 2 12  ? -6.955  20.860  -28.406 1.00 129.09 ? 108  GLU D N     1 
ATOM   2133 C  CA    . GLU B 2 12  ? -6.054  21.999  -28.550 1.00 126.27 ? 108  GLU D CA    1 
ATOM   2134 C  C     . GLU B 2 12  ? -4.964  21.715  -29.576 1.00 126.16 ? 108  GLU D C     1 
ATOM   2135 O  O     . GLU B 2 12  ? -4.593  22.598  -30.357 1.00 116.54 ? 108  GLU D O     1 
ATOM   2136 C  CB    . GLU B 2 12  ? -5.441  22.357  -27.196 1.00 124.10 ? 108  GLU D CB    1 
ATOM   2137 C  CG    . GLU B 2 12  ? -6.461  22.754  -26.143 1.00 137.59 ? 108  GLU D CG    1 
ATOM   2138 C  CD    . GLU B 2 12  ? -5.817  23.194  -24.844 1.00 143.14 ? 108  GLU D CD    1 
ATOM   2139 O  OE1   . GLU B 2 12  ? -4.573  23.292  -24.798 1.00 143.73 ? 108  GLU D OE1   1 
ATOM   2140 O  OE2   . GLU B 2 12  ? -6.556  23.443  -23.867 1.00 145.18 ? 108  GLU D OE2   1 
ATOM   2141 N  N     . LEU B 2 13  ? -4.447  20.485  -29.598 1.00 131.73 ? 109  LEU D N     1 
ATOM   2142 C  CA    . LEU B 2 13  ? -3.427  20.136  -30.582 1.00 116.62 ? 109  LEU D CA    1 
ATOM   2143 C  C     . LEU B 2 13  ? -4.017  20.046  -31.983 1.00 112.34 ? 109  LEU D C     1 
ATOM   2144 O  O     . LEU B 2 13  ? -3.352  20.397  -32.965 1.00 129.64 ? 109  LEU D O     1 
ATOM   2145 C  CB    . LEU B 2 13  ? -2.750  18.821  -30.196 1.00 102.05 ? 109  LEU D CB    1 
ATOM   2146 C  CG    . LEU B 2 13  ? -1.962  18.835  -28.884 1.00 118.32 ? 109  LEU D CG    1 
ATOM   2147 C  CD1   . LEU B 2 13  ? -1.264  17.503  -28.660 1.00 106.95 ? 109  LEU D CD1   1 
ATOM   2148 C  CD2   . LEU B 2 13  ? -0.961  19.980  -28.872 1.00 110.06 ? 109  LEU D CD2   1 
ATOM   2149 N  N     . ASP B 2 14  ? -5.262  19.577  -32.099 1.00 120.14 ? 110  ASP D N     1 
ATOM   2150 C  CA    . ASP B 2 14  ? -5.907  19.515  -33.407 1.00 119.79 ? 110  ASP D CA    1 
ATOM   2151 C  C     . ASP B 2 14  ? -6.173  20.910  -33.957 1.00 124.41 ? 110  ASP D C     1 
ATOM   2152 O  O     . ASP B 2 14  ? -6.001  21.153  -35.157 1.00 121.70 ? 110  ASP D O     1 
ATOM   2153 C  CB    . ASP B 2 14  ? -7.208  18.718  -33.318 1.00 126.31 ? 110  ASP D CB    1 
ATOM   2154 C  CG    . ASP B 2 14  ? -6.972  17.241  -33.071 1.00 121.47 ? 110  ASP D CG    1 
ATOM   2155 O  OD1   . ASP B 2 14  ? -5.996  16.692  -33.625 1.00 120.43 ? 110  ASP D OD1   1 
ATOM   2156 O  OD2   . ASP B 2 14  ? -7.762  16.630  -32.320 1.00 112.63 ? 110  ASP D OD2   1 
ATOM   2157 N  N     . LYS B 2 15  ? -6.594  21.841  -33.096 1.00 128.85 ? 111  LYS D N     1 
ATOM   2158 C  CA    . LYS B 2 15  ? -6.813  23.210  -33.549 1.00 132.51 ? 111  LYS D CA    1 
ATOM   2159 C  C     . LYS B 2 15  ? -5.497  23.941  -33.781 1.00 125.56 ? 111  LYS D C     1 
ATOM   2160 O  O     . LYS B 2 15  ? -5.443  24.875  -34.589 1.00 127.48 ? 111  LYS D O     1 
ATOM   2161 C  CB    . LYS B 2 15  ? -7.676  23.968  -32.541 1.00 139.04 ? 111  LYS D CB    1 
ATOM   2162 C  CG    . LYS B 2 15  ? -9.043  23.345  -32.308 1.00 146.94 ? 111  LYS D CG    1 
ATOM   2163 C  CD    . LYS B 2 15  ? -9.803  23.173  -33.614 1.00 152.40 ? 111  LYS D CD    1 
ATOM   2164 C  CE    . LYS B 2 15  ? -11.120 22.447  -33.393 1.00 155.88 ? 111  LYS D CE    1 
ATOM   2165 N  NZ    . LYS B 2 15  ? -10.914 21.086  -32.822 1.00 155.23 ? 111  LYS D NZ    1 
ATOM   2166 N  N     . LEU B 2 16  ? -4.433  23.536  -33.084 1.00 119.31 ? 112  LEU D N     1 
ATOM   2167 C  CA    . LEU B 2 16  ? -3.123  24.136  -33.313 1.00 117.45 ? 112  LEU D CA    1 
ATOM   2168 C  C     . LEU B 2 16  ? -2.602  23.801  -34.704 1.00 114.56 ? 112  LEU D C     1 
ATOM   2169 O  O     . LEU B 2 16  ? -1.966  24.638  -35.355 1.00 108.82 ? 112  LEU D O     1 
ATOM   2170 C  CB    . LEU B 2 16  ? -2.139  23.664  -32.243 1.00 111.63 ? 112  LEU D CB    1 
ATOM   2171 C  CG    . LEU B 2 16  ? -0.715  24.214  -32.334 1.00 106.65 ? 112  LEU D CG    1 
ATOM   2172 C  CD1   . LEU B 2 16  ? -0.711  25.716  -32.112 1.00 110.98 ? 112  LEU D CD1   1 
ATOM   2173 C  CD2   . LEU B 2 16  ? 0.201   23.516  -31.340 1.00 109.59 ? 112  LEU D CD2   1 
ATOM   2174 N  N     . LEU B 2 17  ? -2.862  22.584  -35.174 1.00 109.20 ? 113  LEU D N     1 
ATOM   2175 C  CA    . LEU B 2 17  ? -2.465  22.153  -36.507 1.00 107.94 ? 113  LEU D CA    1 
ATOM   2176 C  C     . LEU B 2 17  ? -3.576  22.334  -37.534 1.00 120.71 ? 113  LEU D C     1 
ATOM   2177 O  O     . LEU B 2 17  ? -3.426  21.883  -38.675 1.00 124.81 ? 113  LEU D O     1 
ATOM   2178 C  CB    . LEU B 2 17  ? -2.012  20.688  -36.477 1.00 109.04 ? 113  LEU D CB    1 
ATOM   2179 C  CG    . LEU B 2 17  ? -0.568  20.380  -36.058 1.00 105.25 ? 113  LEU D CG    1 
ATOM   2180 C  CD1   . LEU B 2 17  ? -0.275  20.805  -34.624 1.00 103.89 ? 113  LEU D CD1   1 
ATOM   2181 C  CD2   . LEU B 2 17  ? -0.262  18.902  -36.246 1.00 96.34  ? 113  LEU D CD2   1 
ATOM   2182 N  N     . GLN B 2 18  ? -4.678  22.988  -37.149 1.00 126.70 ? 114  GLN D N     1 
ATOM   2183 C  CA    . GLN B 2 18  ? -5.800  23.270  -38.045 1.00 125.78 ? 114  GLN D CA    1 
ATOM   2184 C  C     . GLN B 2 18  ? -6.387  21.982  -38.616 1.00 127.61 ? 114  GLN D C     1 
ATOM   2185 O  O     . GLN B 2 18  ? -6.779  21.919  -39.783 1.00 119.81 ? 114  GLN D O     1 
ATOM   2186 C  CB    . GLN B 2 18  ? -5.385  24.233  -39.161 1.00 112.83 ? 114  GLN D CB    1 
ATOM   2187 C  CG    . GLN B 2 18  ? -4.922  25.580  -38.642 1.00 108.14 ? 114  GLN D CG    1 
ATOM   2188 C  CD    . GLN B 2 18  ? -4.534  26.527  -39.749 1.00 132.76 ? 114  GLN D CD    1 
ATOM   2189 O  OE1   . GLN B 2 18  ? -4.724  26.233  -40.927 1.00 127.40 ? 114  GLN D OE1   1 
ATOM   2190 N  NE2   . GLN B 2 18  ? -3.981  27.675  -39.377 1.00 128.95 ? 114  GLN D NE2   1 
ATOM   2191 N  N     . GLY B 2 19  ? -6.439  20.942  -37.785 1.00 127.12 ? 115  GLY D N     1 
ATOM   2192 C  CA    . GLY B 2 19  ? -6.925  19.647  -38.223 1.00 127.10 ? 115  GLY D CA    1 
ATOM   2193 C  C     . GLY B 2 19  ? -6.147  18.472  -37.662 1.00 123.43 ? 115  GLY D C     1 
ATOM   2194 O  O     . GLY B 2 19  ? -6.732  17.444  -37.305 1.00 119.46 ? 115  GLY D O     1 
ATOM   2195 N  N     . GLY B 2 20  ? -4.824  18.610  -37.588 1.00 120.86 ? 116  GLY D N     1 
ATOM   2196 C  CA    . GLY B 2 20  ? -3.986  17.549  -37.061 1.00 105.56 ? 116  GLY D CA    1 
ATOM   2197 C  C     . GLY B 2 20  ? -2.789  17.209  -37.928 1.00 113.86 ? 116  GLY D C     1 
ATOM   2198 O  O     . GLY B 2 20  ? -2.309  18.056  -38.687 1.00 112.03 ? 116  GLY D O     1 
ATOM   2199 N  N     . ILE B 2 21  ? -2.284  15.978  -37.819 1.00 114.43 ? 117  ILE D N     1 
ATOM   2200 C  CA    . ILE B 2 21  ? -1.111  15.581  -38.590 1.00 105.50 ? 117  ILE D CA    1 
ATOM   2201 C  C     . ILE B 2 21  ? -1.467  15.523  -40.068 1.00 99.27  ? 117  ILE D C     1 
ATOM   2202 O  O     . ILE B 2 21  ? -2.427  14.853  -40.470 1.00 95.11  ? 117  ILE D O     1 
ATOM   2203 C  CB    . ILE B 2 21  ? -0.563  14.234  -38.096 1.00 99.96  ? 117  ILE D CB    1 
ATOM   2204 C  CG1   . ILE B 2 21  ? -0.194  14.316  -36.613 1.00 91.93  ? 117  ILE D CG1   1 
ATOM   2205 C  CG2   . ILE B 2 21  ? 0.653   13.834  -38.913 1.00 87.63  ? 117  ILE D CG2   1 
ATOM   2206 C  CD1   . ILE B 2 21  ? 0.852   15.353  -36.292 1.00 78.75  ? 117  ILE D CD1   1 
ATOM   2207 N  N     . GLU B 2 22  ? -0.685  16.222  -40.886 1.00 108.07 ? 118  GLU D N     1 
ATOM   2208 C  CA    . GLU B 2 22  ? -0.931  16.315  -42.317 1.00 103.46 ? 118  GLU D CA    1 
ATOM   2209 C  C     . GLU B 2 22  ? -0.271  15.145  -43.035 1.00 89.07  ? 118  GLU D C     1 
ATOM   2210 O  O     . GLU B 2 22  ? 0.899   14.836  -42.785 1.00 100.94 ? 118  GLU D O     1 
ATOM   2211 C  CB    . GLU B 2 22  ? -0.399  17.641  -42.861 1.00 106.79 ? 118  GLU D CB    1 
ATOM   2212 C  CG    . GLU B 2 22  ? -0.332  17.714  -44.376 1.00 123.90 ? 118  GLU D CG    1 
ATOM   2213 C  CD    . GLU B 2 22  ? 0.180   19.054  -44.876 1.00 133.82 ? 118  GLU D CD    1 
ATOM   2214 O  OE1   . GLU B 2 22  ? 0.159   20.031  -44.098 1.00 135.08 ? 118  GLU D OE1   1 
ATOM   2215 O  OE2   . GLU B 2 22  ? 0.605   19.131  -46.048 1.00 137.36 ? 118  GLU D OE2   1 
ATOM   2216 N  N     . THR B 2 23  ? -1.023  14.499  -43.924 1.00 87.58  ? 119  THR D N     1 
ATOM   2217 C  CA    . THR B 2 23  ? -0.493  13.395  -44.706 1.00 98.31  ? 119  THR D CA    1 
ATOM   2218 C  C     . THR B 2 23  ? 0.310   13.918  -45.896 1.00 101.43 ? 119  THR D C     1 
ATOM   2219 O  O     . THR B 2 23  ? 0.236   15.092  -46.269 1.00 100.54 ? 119  THR D O     1 
ATOM   2220 C  CB    . THR B 2 23  ? -1.620  12.484  -45.193 1.00 102.49 ? 119  THR D CB    1 
ATOM   2221 O  OG1   . THR B 2 23  ? -2.530  13.236  -46.005 1.00 108.98 ? 119  THR D OG1   1 
ATOM   2222 C  CG2   . THR B 2 23  ? -2.374  11.883  -44.014 1.00 107.77 ? 119  THR D CG2   1 
ATOM   2223 N  N     . GLY B 2 24  ? 1.090   13.019  -46.499 1.00 93.79  ? 120  GLY D N     1 
ATOM   2224 C  CA    . GLY B 2 24  ? 1.899   13.347  -47.650 1.00 100.44 ? 120  GLY D CA    1 
ATOM   2225 C  C     . GLY B 2 24  ? 3.234   13.989  -47.347 1.00 93.52  ? 120  GLY D C     1 
ATOM   2226 O  O     . GLY B 2 24  ? 4.133   13.940  -48.194 1.00 96.53  ? 120  GLY D O     1 
ATOM   2227 N  N     . SER B 2 25  ? 3.397   14.590  -46.174 1.00 86.92  ? 121  SER D N     1 
ATOM   2228 C  CA    . SER B 2 25  ? 4.633   15.249  -45.775 1.00 99.12  ? 121  SER D CA    1 
ATOM   2229 C  C     . SER B 2 25  ? 5.209   14.554  -44.544 1.00 102.60 ? 121  SER D C     1 
ATOM   2230 O  O     . SER B 2 25  ? 4.682   13.546  -44.067 1.00 93.08  ? 121  SER D O     1 
ATOM   2231 C  CB    . SER B 2 25  ? 4.392   16.737  -45.506 1.00 106.86 ? 121  SER D CB    1 
ATOM   2232 O  OG    . SER B 2 25  ? 3.495   16.921  -44.424 1.00 119.53 ? 121  SER D OG    1 
ATOM   2233 N  N     . ILE B 2 26  ? 6.302   15.108  -44.027 1.00 101.37 ? 122  ILE D N     1 
ATOM   2234 C  CA    . ILE B 2 26  ? 7.000   14.558  -42.870 1.00 88.29  ? 122  ILE D CA    1 
ATOM   2235 C  C     . ILE B 2 26  ? 6.729   15.451  -41.667 1.00 91.05  ? 122  ILE D C     1 
ATOM   2236 O  O     . ILE B 2 26  ? 6.825   16.682  -41.760 1.00 104.13 ? 122  ILE D O     1 
ATOM   2237 C  CB    . ILE B 2 26  ? 8.510   14.421  -43.131 1.00 94.89  ? 122  ILE D CB    1 
ATOM   2238 C  CG1   . ILE B 2 26  ? 8.772   13.339  -44.181 1.00 78.14  ? 122  ILE D CG1   1 
ATOM   2239 C  CG2   . ILE B 2 26  ? 9.254   14.101  -41.841 1.00 67.40  ? 122  ILE D CG2   1 
ATOM   2240 C  CD1   . ILE B 2 26  ? 10.232  12.958  -44.316 1.00 73.31  ? 122  ILE D CD1   1 
ATOM   2241 N  N     . THR B 2 27  ? 6.384   14.827  -40.542 1.00 86.81  ? 123  THR D N     1 
ATOM   2242 C  CA    . THR B 2 27  ? 6.152   15.517  -39.277 1.00 83.48  ? 123  THR D CA    1 
ATOM   2243 C  C     . THR B 2 27  ? 7.192   15.030  -38.276 1.00 79.48  ? 123  THR D C     1 
ATOM   2244 O  O     . THR B 2 27  ? 7.137   13.881  -37.825 1.00 82.31  ? 123  THR D O     1 
ATOM   2245 C  CB    . THR B 2 27  ? 4.736   15.264  -38.763 1.00 86.40  ? 123  THR D CB    1 
ATOM   2246 O  OG1   . THR B 2 27  ? 3.784   15.784  -39.700 1.00 101.19 ? 123  THR D OG1   1 
ATOM   2247 C  CG2   . THR B 2 27  ? 4.533   15.935  -37.414 1.00 76.20  ? 123  THR D CG2   1 
ATOM   2248 N  N     . GLU B 2 28  ? 8.138   15.900  -37.934 1.00 82.04  ? 124  GLU D N     1 
ATOM   2249 C  CA    . GLU B 2 28  ? 9.204   15.578  -36.991 1.00 76.12  ? 124  GLU D CA    1 
ATOM   2250 C  C     . GLU B 2 28  ? 8.813   16.086  -35.610 1.00 81.09  ? 124  GLU D C     1 
ATOM   2251 O  O     . GLU B 2 28  ? 8.703   17.297  -35.395 1.00 84.07  ? 124  GLU D O     1 
ATOM   2252 C  CB    . GLU B 2 28  ? 10.533  16.190  -37.428 1.00 86.51  ? 124  GLU D CB    1 
ATOM   2253 C  CG    . GLU B 2 28  ? 11.639  16.014  -36.399 1.00 85.03  ? 124  GLU D CG    1 
ATOM   2254 C  CD    . GLU B 2 28  ? 12.717  17.075  -36.504 1.00 103.11 ? 124  GLU D CD    1 
ATOM   2255 O  OE1   . GLU B 2 28  ? 12.633  17.922  -37.419 1.00 121.74 ? 124  GLU D OE1   1 
ATOM   2256 O  OE2   . GLU B 2 28  ? 13.645  17.065  -35.668 1.00 82.59  ? 124  GLU D OE2   1 
ATOM   2257 N  N     . MET B 2 29  ? 8.611   15.163  -34.676 1.00 82.44  ? 125  MET D N     1 
ATOM   2258 C  CA    . MET B 2 29  ? 8.360   15.493  -33.280 1.00 92.25  ? 125  MET D CA    1 
ATOM   2259 C  C     . MET B 2 29  ? 9.653   15.297  -32.500 1.00 76.52  ? 125  MET D C     1 
ATOM   2260 O  O     . MET B 2 29  ? 10.213  14.195  -32.495 1.00 82.19  ? 125  MET D O     1 
ATOM   2261 C  CB    . MET B 2 29  ? 7.252   14.617  -32.702 1.00 94.62  ? 125  MET D CB    1 
ATOM   2262 C  CG    . MET B 2 29  ? 5.914   14.746  -33.403 1.00 100.04 ? 125  MET D CG    1 
ATOM   2263 S  SD    . MET B 2 29  ? 4.788   13.449  -32.866 1.00 105.64 ? 125  MET D SD    1 
ATOM   2264 C  CE    . MET B 2 29  ? 5.193   13.378  -31.123 1.00 88.74  ? 125  MET D CE    1 
ATOM   2265 N  N     . PHE B 2 30  ? 10.127  16.354  -31.846 1.00 77.48  ? 126  PHE D N     1 
ATOM   2266 C  CA    . PHE B 2 30  ? 11.373  16.271  -31.098 1.00 89.13  ? 126  PHE D CA    1 
ATOM   2267 C  C     . PHE B 2 30  ? 11.215  16.903  -29.722 1.00 89.35  ? 126  PHE D C     1 
ATOM   2268 O  O     . PHE B 2 30  ? 10.450  17.853  -29.534 1.00 86.44  ? 126  PHE D O     1 
ATOM   2269 C  CB    . PHE B 2 30  ? 12.542  16.927  -31.857 1.00 79.62  ? 126  PHE D CB    1 
ATOM   2270 C  CG    . PHE B 2 30  ? 12.369  18.398  -32.105 1.00 100.41 ? 126  PHE D CG    1 
ATOM   2271 C  CD1   . PHE B 2 30  ? 11.630  18.851  -33.186 1.00 101.26 ? 126  PHE D CD1   1 
ATOM   2272 C  CD2   . PHE B 2 30  ? 12.967  19.330  -31.272 1.00 90.75  ? 126  PHE D CD2   1 
ATOM   2273 C  CE1   . PHE B 2 30  ? 11.476  20.204  -33.420 1.00 101.51 ? 126  PHE D CE1   1 
ATOM   2274 C  CE2   . PHE B 2 30  ? 12.819  20.683  -31.504 1.00 86.16  ? 126  PHE D CE2   1 
ATOM   2275 C  CZ    . PHE B 2 30  ? 12.071  21.121  -32.578 1.00 93.15  ? 126  PHE D CZ    1 
ATOM   2276 N  N     . GLY B 2 31  ? 11.951  16.353  -28.765 1.00 86.61  ? 127  GLY D N     1 
ATOM   2277 C  CA    . GLY B 2 31  ? 11.894  16.834  -27.399 1.00 93.17  ? 127  GLY D CA    1 
ATOM   2278 C  C     . GLY B 2 31  ? 12.791  15.999  -26.513 1.00 95.79  ? 127  GLY D C     1 
ATOM   2279 O  O     . GLY B 2 31  ? 13.527  15.130  -26.986 1.00 99.62  ? 127  GLY D O     1 
ATOM   2280 N  N     . GLU B 2 32  ? 12.721  16.273  -25.214 1.00 94.87  ? 128  GLU D N     1 
ATOM   2281 C  CA    . GLU B 2 32  ? 13.526  15.548  -24.241 1.00 99.60  ? 128  GLU D CA    1 
ATOM   2282 C  C     . GLU B 2 32  ? 12.825  14.243  -23.864 1.00 92.67  ? 128  GLU D C     1 
ATOM   2283 O  O     . GLU B 2 32  ? 11.828  13.843  -24.472 1.00 94.07  ? 128  GLU D O     1 
ATOM   2284 C  CB    . GLU B 2 32  ? 13.804  16.425  -23.023 1.00 104.36 ? 128  GLU D CB    1 
ATOM   2285 C  CG    . GLU B 2 32  ? 14.739  17.590  -23.301 1.00 99.32  ? 128  GLU D CG    1 
ATOM   2286 C  CD    . GLU B 2 32  ? 15.156  18.316  -22.037 1.00 118.24 ? 128  GLU D CD    1 
ATOM   2287 O  OE1   . GLU B 2 32  ? 14.566  18.043  -20.971 1.00 115.49 ? 128  GLU D OE1   1 
ATOM   2288 O  OE2   . GLU B 2 32  ? 16.077  19.157  -22.110 1.00 121.84 ? 128  GLU D OE2   1 
ATOM   2289 N  N     . PHE B 2 33  ? 13.348  13.560  -22.850 1.00 100.14 ? 129  PHE D N     1 
ATOM   2290 C  CA    . PHE B 2 33  ? 12.769  12.304  -22.404 1.00 97.21  ? 129  PHE D CA    1 
ATOM   2291 C  C     . PHE B 2 33  ? 11.511  12.560  -21.582 1.00 91.00  ? 129  PHE D C     1 
ATOM   2292 O  O     . PHE B 2 33  ? 11.386  13.584  -20.903 1.00 92.79  ? 129  PHE D O     1 
ATOM   2293 C  CB    . PHE B 2 33  ? 13.787  11.507  -21.587 1.00 86.56  ? 129  PHE D CB    1 
ATOM   2294 C  CG    . PHE B 2 33  ? 13.365  10.095  -21.298 1.00 92.60  ? 129  PHE D CG    1 
ATOM   2295 C  CD1   . PHE B 2 33  ? 13.152  9.197   -22.331 1.00 98.66  ? 129  PHE D CD1   1 
ATOM   2296 C  CD2   . PHE B 2 33  ? 13.198  9.661   -19.994 1.00 106.90 ? 129  PHE D CD2   1 
ATOM   2297 C  CE1   . PHE B 2 33  ? 12.767  7.895   -22.068 1.00 107.47 ? 129  PHE D CE1   1 
ATOM   2298 C  CE2   . PHE B 2 33  ? 12.814  8.360   -19.725 1.00 114.26 ? 129  PHE D CE2   1 
ATOM   2299 C  CZ    . PHE B 2 33  ? 12.598  7.476   -20.763 1.00 124.13 ? 129  PHE D CZ    1 
ATOM   2300 N  N     . ARG B 2 34  ? 10.573  11.611  -21.659 1.00 84.08  ? 130  ARG D N     1 
ATOM   2301 C  CA    A ARG B 2 34  ? 9.286   11.708  -20.968 0.47 94.28  ? 130  ARG D CA    1 
ATOM   2302 C  CA    B ARG B 2 34  ? 9.284   11.707  -20.971 0.53 89.42  ? 130  ARG D CA    1 
ATOM   2303 C  C     . ARG B 2 34  ? 8.553   12.997  -21.344 1.00 86.77  ? 130  ARG D C     1 
ATOM   2304 O  O     . ARG B 2 34  ? 8.041   13.722  -20.488 1.00 92.95  ? 130  ARG D O     1 
ATOM   2305 C  CB    A ARG B 2 34  ? 9.462   11.599  -19.451 0.47 98.63  ? 130  ARG D CB    1 
ATOM   2306 C  CB    B ARG B 2 34  ? 9.453   11.588  -19.453 0.53 98.91  ? 130  ARG D CB    1 
ATOM   2307 C  CG    A ARG B 2 34  ? 9.876   10.219  -18.967 0.47 101.20 ? 130  ARG D CG    1 
ATOM   2308 C  CG    B ARG B 2 34  ? 9.766   10.181  -18.970 0.53 101.16 ? 130  ARG D CG    1 
ATOM   2309 C  CD    A ARG B 2 34  ? 10.089  10.204  -17.462 0.47 103.53 ? 130  ARG D CD    1 
ATOM   2310 C  CD    B ARG B 2 34  ? 9.629   10.071  -17.458 0.53 103.43 ? 130  ARG D CD    1 
ATOM   2311 N  NE    A ARG B 2 34  ? 8.877   10.563  -16.736 0.47 102.86 ? 130  ARG D NE    1 
ATOM   2312 N  NE    B ARG B 2 34  ? 10.634  10.856  -16.753 0.53 102.74 ? 130  ARG D NE    1 
ATOM   2313 C  CZ    A ARG B 2 34  ? 7.992   9.689   -16.277 0.47 108.15 ? 130  ARG D CZ    1 
ATOM   2314 C  CZ    B ARG B 2 34  ? 11.779  10.368  -16.295 0.53 101.85 ? 130  ARG D CZ    1 
ATOM   2315 N  NH1   A ARG B 2 34  ? 8.156   8.386   -16.443 0.47 109.82 ? 130  ARG D NH1   1 
ATOM   2316 N  NH1   B ARG B 2 34  ? 12.097  9.093   -16.448 0.53 105.91 ? 130  ARG D NH1   1 
ATOM   2317 N  NH2   A ARG B 2 34  ? 6.915   10.132  -15.635 0.47 102.04 ? 130  ARG D NH2   1 
ATOM   2318 N  NH2   B ARG B 2 34  ? 12.625  11.179  -15.665 0.53 87.71  ? 130  ARG D NH2   1 
ATOM   2319 N  N     . THR B 2 35  ? 8.508   13.280  -22.647 1.00 86.57  ? 131  THR D N     1 
ATOM   2320 C  CA    . THR B 2 35  ? 7.797   14.442  -23.160 1.00 78.59  ? 131  THR D CA    1 
ATOM   2321 C  C     . THR B 2 35  ? 6.511   14.093  -23.893 1.00 84.50  ? 131  THR D C     1 
ATOM   2322 O  O     . THR B 2 35  ? 5.673   14.979  -24.088 1.00 93.37  ? 131  THR D O     1 
ATOM   2323 C  CB    . THR B 2 35  ? 8.698   15.255  -24.102 1.00 79.89  ? 131  THR D CB    1 
ATOM   2324 O  OG1   . THR B 2 35  ? 9.361   14.373  -25.017 1.00 98.78  ? 131  THR D OG1   1 
ATOM   2325 C  CG2   . THR B 2 35  ? 9.733   16.039  -23.308 1.00 92.27  ? 131  THR D CG2   1 
ATOM   2326 N  N     . GLY B 2 36  ? 6.334   12.839  -24.301 1.00 78.47  ? 132  GLY D N     1 
ATOM   2327 C  CA    . GLY B 2 36  ? 5.117   12.401  -24.948 1.00 86.09  ? 132  GLY D CA    1 
ATOM   2328 C  C     . GLY B 2 36  ? 5.247   11.990  -26.399 1.00 82.22  ? 132  GLY D C     1 
ATOM   2329 O  O     . GLY B 2 36  ? 4.221   11.842  -27.072 1.00 83.48  ? 132  GLY D O     1 
ATOM   2330 N  N     . LYS B 2 37  ? 6.466   11.792  -26.905 1.00 71.65  ? 133  LYS D N     1 
ATOM   2331 C  CA    . LYS B 2 37  ? 6.634   11.443  -28.313 1.00 70.52  ? 133  LYS D CA    1 
ATOM   2332 C  C     . LYS B 2 37  ? 6.071   10.058  -28.609 1.00 77.51  ? 133  LYS D C     1 
ATOM   2333 O  O     . LYS B 2 37  ? 5.253   9.889   -29.524 1.00 78.14  ? 133  LYS D O     1 
ATOM   2334 C  CB    . LYS B 2 37  ? 8.113   11.525  -28.695 1.00 66.94  ? 133  LYS D CB    1 
ATOM   2335 C  CG    . LYS B 2 37  ? 8.755   12.867  -28.365 1.00 83.32  ? 133  LYS D CG    1 
ATOM   2336 C  CD    . LYS B 2 37  ? 10.234  12.894  -28.720 1.00 73.04  ? 133  LYS D CD    1 
ATOM   2337 C  CE    . LYS B 2 37  ? 11.028  11.903  -27.884 1.00 87.55  ? 133  LYS D CE    1 
ATOM   2338 N  NZ    . LYS B 2 37  ? 10.991  12.241  -26.435 1.00 92.26  ? 133  LYS D NZ    1 
ATOM   2339 N  N     . THR B 2 38  ? 6.490   9.053   -27.836 1.00 58.93  ? 134  THR D N     1 
ATOM   2340 C  CA    . THR B 2 38  ? 6.013   7.693   -28.063 1.00 66.03  ? 134  THR D CA    1 
ATOM   2341 C  C     . THR B 2 38  ? 4.517   7.577   -27.790 1.00 78.23  ? 134  THR D C     1 
ATOM   2342 O  O     . THR B 2 38  ? 3.810   6.833   -28.480 1.00 74.08  ? 134  THR D O     1 
ATOM   2343 C  CB    . THR B 2 38  ? 6.799   6.713   -27.191 1.00 74.75  ? 134  THR D CB    1 
ATOM   2344 O  OG1   . THR B 2 38  ? 8.203   6.911   -27.398 1.00 78.19  ? 134  THR D OG1   1 
ATOM   2345 C  CG2   . THR B 2 38  ? 6.445   5.278   -27.545 1.00 73.54  ? 134  THR D CG2   1 
ATOM   2346 N  N     . GLN B 2 39  ? 4.012   8.316   -26.800 1.00 77.22  ? 135  GLN D N     1 
ATOM   2347 C  CA    . GLN B 2 39  ? 2.582   8.274   -26.508 1.00 77.15  ? 135  GLN D CA    1 
ATOM   2348 C  C     . GLN B 2 39  ? 1.768   8.895   -27.637 1.00 82.91  ? 135  GLN D C     1 
ATOM   2349 O  O     . GLN B 2 39  ? 0.713   8.367   -28.014 1.00 85.22  ? 135  GLN D O     1 
ATOM   2350 C  CB    . GLN B 2 39  ? 2.296   8.978   -25.182 1.00 81.41  ? 135  GLN D CB    1 
ATOM   2351 C  CG    . GLN B 2 39  ? 3.009   8.360   -23.987 1.00 92.65  ? 135  GLN D CG    1 
ATOM   2352 C  CD    . GLN B 2 39  ? 2.584   6.927   -23.727 1.00 90.41  ? 135  GLN D CD    1 
ATOM   2353 O  OE1   . GLN B 2 39  ? 1.444   6.545   -23.995 1.00 88.16  ? 135  GLN D OE1   1 
ATOM   2354 N  NE2   . GLN B 2 39  ? 3.503   6.124   -23.205 1.00 97.96  ? 135  GLN D NE2   1 
ATOM   2355 N  N     . ILE B 2 40  ? 2.241   10.013  -28.194 1.00 74.62  ? 136  ILE D N     1 
ATOM   2356 C  CA    . ILE B 2 40  ? 1.558   10.614  -29.336 1.00 78.79  ? 136  ILE D CA    1 
ATOM   2357 C  C     . ILE B 2 40  ? 1.608   9.676   -30.535 1.00 71.83  ? 136  ILE D C     1 
ATOM   2358 O  O     . ILE B 2 40  ? 0.636   9.561   -31.292 1.00 79.67  ? 136  ILE D O     1 
ATOM   2359 C  CB    . ILE B 2 40  ? 2.162   11.993  -29.664 1.00 73.31  ? 136  ILE D CB    1 
ATOM   2360 C  CG1   . ILE B 2 40  ? 1.791   13.011  -28.585 1.00 76.14  ? 136  ILE D CG1   1 
ATOM   2361 C  CG2   . ILE B 2 40  ? 1.686   12.480  -31.025 1.00 73.24  ? 136  ILE D CG2   1 
ATOM   2362 C  CD1   . ILE B 2 40  ? 2.383   14.384  -28.812 1.00 74.45  ? 136  ILE D CD1   1 
ATOM   2363 N  N     . CYS B 2 41  ? 2.735   8.984   -30.725 1.00 71.56  ? 137  CYS D N     1 
ATOM   2364 C  CA    . CYS B 2 41  ? 2.819   8.013   -31.812 1.00 75.00  ? 137  CYS D CA    1 
ATOM   2365 C  C     . CYS B 2 41  ? 1.813   6.883   -31.622 1.00 74.76  ? 137  CYS D C     1 
ATOM   2366 O  O     . CYS B 2 41  ? 1.143   6.470   -32.577 1.00 78.04  ? 137  CYS D O     1 
ATOM   2367 C  CB    . CYS B 2 41  ? 4.239   7.457   -31.915 1.00 74.05  ? 137  CYS D CB    1 
ATOM   2368 S  SG    . CYS B 2 41  ? 5.464   8.648   -32.504 1.00 74.93  ? 137  CYS D SG    1 
ATOM   2369 N  N     . HIS B 2 42  ? 1.693   6.371   -30.394 1.00 73.59  ? 138  HIS D N     1 
ATOM   2370 C  CA    . HIS B 2 42  ? 0.723   5.313   -30.123 1.00 78.89  ? 138  HIS D CA    1 
ATOM   2371 C  C     . HIS B 2 42  ? -0.703  5.796   -30.359 1.00 76.33  ? 138  HIS D C     1 
ATOM   2372 O  O     . HIS B 2 42  ? -1.538  5.054   -30.889 1.00 64.45  ? 138  HIS D O     1 
ATOM   2373 C  CB    . HIS B 2 42  ? 0.885   4.802   -28.692 1.00 76.99  ? 138  HIS D CB    1 
ATOM   2374 C  CG    . HIS B 2 42  ? 1.971   3.785   -28.532 1.00 76.26  ? 138  HIS D CG    1 
ATOM   2375 N  ND1   . HIS B 2 42  ? 3.308   4.094   -28.669 1.00 67.01  ? 138  HIS D ND1   1 
ATOM   2376 C  CD2   . HIS B 2 42  ? 1.918   2.462   -28.250 1.00 79.94  ? 138  HIS D CD2   1 
ATOM   2377 C  CE1   . HIS B 2 42  ? 4.030   3.005   -28.477 1.00 73.72  ? 138  HIS D CE1   1 
ATOM   2378 N  NE2   . HIS B 2 42  ? 3.212   2.001   -28.221 1.00 70.90  ? 138  HIS D NE2   1 
ATOM   2379 N  N     . THR B 2 43  ? -1.001  7.038   -29.971 1.00 66.53  ? 139  THR D N     1 
ATOM   2380 C  CA    . THR B 2 43  ? -2.338  7.576   -30.200 1.00 70.66  ? 139  THR D CA    1 
ATOM   2381 C  C     . THR B 2 43  ? -2.625  7.732   -31.690 1.00 86.51  ? 139  THR D C     1 
ATOM   2382 O  O     . THR B 2 43  ? -3.724  7.403   -32.154 1.00 90.50  ? 139  THR D O     1 
ATOM   2383 C  CB    . THR B 2 43  ? -2.497  8.914   -29.477 1.00 75.28  ? 139  THR D CB    1 
ATOM   2384 O  OG1   . THR B 2 43  ? -2.304  8.724   -28.070 1.00 93.74  ? 139  THR D OG1   1 
ATOM   2385 C  CG2   . THR B 2 43  ? -3.886  9.491   -29.716 1.00 67.95  ? 139  THR D CG2   1 
ATOM   2386 N  N     . LEU B 2 44  ? -1.645  8.223   -32.453 1.00 75.40  ? 140  LEU D N     1 
ATOM   2387 C  CA    . LEU B 2 44  ? -1.841  8.413   -33.887 1.00 82.49  ? 140  LEU D CA    1 
ATOM   2388 C  C     . LEU B 2 44  ? -2.002  7.081   -34.608 1.00 85.35  ? 140  LEU D C     1 
ATOM   2389 O  O     . LEU B 2 44  ? -2.810  6.967   -35.539 1.00 75.54  ? 140  LEU D O     1 
ATOM   2390 C  CB    . LEU B 2 44  ? -0.673  9.204   -34.476 1.00 80.70  ? 140  LEU D CB    1 
ATOM   2391 C  CG    . LEU B 2 44  ? -0.569  10.680  -34.087 1.00 79.49  ? 140  LEU D CG    1 
ATOM   2392 C  CD1   . LEU B 2 44  ? 0.701   11.293  -34.655 1.00 87.68  ? 140  LEU D CD1   1 
ATOM   2393 C  CD2   . LEU B 2 44  ? -1.795  11.445  -34.561 1.00 88.68  ? 140  LEU D CD2   1 
ATOM   2394 N  N     . ALA B 2 45  ? -1.249  6.059   -34.187 1.00 78.03  ? 141  ALA D N     1 
ATOM   2395 C  CA    . ALA B 2 45  ? -1.329  4.744   -34.814 1.00 74.14  ? 141  ALA D CA    1 
ATOM   2396 C  C     . ALA B 2 45  ? -2.715  4.123   -34.711 1.00 66.30  ? 141  ALA D C     1 
ATOM   2397 O  O     . ALA B 2 45  ? -2.980  3.123   -35.388 1.00 86.91  ? 141  ALA D O     1 
ATOM   2398 C  CB    . ALA B 2 45  ? -0.298  3.802   -34.191 1.00 67.44  ? 141  ALA D CB    1 
ATOM   2399 N  N     . VAL B 2 46  ? -3.597  4.681   -33.887 1.00 73.46  ? 142  VAL D N     1 
ATOM   2400 C  CA    . VAL B 2 46  ? -4.970  4.223   -33.778 1.00 78.35  ? 142  VAL D CA    1 
ATOM   2401 C  C     . VAL B 2 46  ? -5.949  5.246   -34.343 1.00 91.66  ? 142  VAL D C     1 
ATOM   2402 O  O     . VAL B 2 46  ? -6.947  4.875   -34.965 1.00 95.29  ? 142  VAL D O     1 
ATOM   2403 C  CB    . VAL B 2 46  ? -5.311  3.880   -32.312 1.00 91.88  ? 142  VAL D CB    1 
ATOM   2404 C  CG1   . VAL B 2 46  ? -6.769  3.468   -32.174 1.00 87.33  ? 142  VAL D CG1   1 
ATOM   2405 C  CG2   . VAL B 2 46  ? -4.391  2.778   -31.813 1.00 100.17 ? 142  VAL D CG2   1 
ATOM   2406 N  N     . THR B 2 47  ? -5.670  6.539   -34.158 1.00 84.43  ? 143  THR D N     1 
ATOM   2407 C  CA    . THR B 2 47  ? -6.563  7.562   -34.690 1.00 72.89  ? 143  THR D CA    1 
ATOM   2408 C  C     . THR B 2 47  ? -6.488  7.670   -36.208 1.00 89.22  ? 143  THR D C     1 
ATOM   2409 O  O     . THR B 2 47  ? -7.405  8.230   -36.819 1.00 99.91  ? 143  THR D O     1 
ATOM   2410 C  CB    . THR B 2 47  ? -6.261  8.924   -34.062 1.00 88.44  ? 143  THR D CB    1 
ATOM   2411 O  OG1   . THR B 2 47  ? -4.895  9.278   -34.310 1.00 89.48  ? 143  THR D OG1   1 
ATOM   2412 C  CG2   . THR B 2 47  ? -6.513  8.890   -32.562 1.00 98.72  ? 143  THR D CG2   1 
ATOM   2413 N  N     . CYS B 2 48  ? -5.426  7.151   -36.832 1.00 88.58  ? 144  CYS D N     1 
ATOM   2414 C  CA    . CYS B 2 48  ? -5.346  7.157   -38.288 1.00 84.79  ? 144  CYS D CA    1 
ATOM   2415 C  C     . CYS B 2 48  ? -6.254  6.120   -38.936 1.00 91.27  ? 144  CYS D C     1 
ATOM   2416 O  O     . CYS B 2 48  ? -6.381  6.114   -40.165 1.00 91.83  ? 144  CYS D O     1 
ATOM   2417 C  CB    . CYS B 2 48  ? -3.903  6.923   -38.741 1.00 76.18  ? 144  CYS D CB    1 
ATOM   2418 S  SG    . CYS B 2 48  ? -3.339  5.213   -38.593 1.00 108.59 ? 144  CYS D SG    1 
ATOM   2419 N  N     . GLN B 2 49  ? -6.878  5.246   -38.148 1.00 94.03  ? 145  GLN D N     1 
ATOM   2420 C  CA    . GLN B 2 49  ? -7.799  4.245   -38.668 1.00 94.55  ? 145  GLN D CA    1 
ATOM   2421 C  C     . GLN B 2 49  ? -9.253  4.696   -38.624 1.00 99.30  ? 145  GLN D C     1 
ATOM   2422 O  O     . GLN B 2 49  ? -10.117 4.003   -39.172 1.00 99.24  ? 145  GLN D O     1 
ATOM   2423 C  CB    . GLN B 2 49  ? -7.650  2.935   -37.887 1.00 82.04  ? 145  GLN D CB    1 
ATOM   2424 C  CG    . GLN B 2 49  ? -6.219  2.436   -37.780 1.00 92.47  ? 145  GLN D CG    1 
ATOM   2425 C  CD    . GLN B 2 49  ? -6.117  1.116   -37.041 1.00 92.51  ? 145  GLN D CD    1 
ATOM   2426 O  OE1   . GLN B 2 49  ? -7.030  0.292   -37.091 1.00 105.34 ? 145  GLN D OE1   1 
ATOM   2427 N  NE2   . GLN B 2 49  ? -5.005  0.912   -36.346 1.00 91.88  ? 145  GLN D NE2   1 
ATOM   2428 N  N     . LEU B 2 50  ? -9.540  5.827   -37.984 1.00 92.00  ? 146  LEU D N     1 
ATOM   2429 C  CA    . LEU B 2 50  ? -10.894 6.348   -37.930 1.00 97.92  ? 146  LEU D CA    1 
ATOM   2430 C  C     . LEU B 2 50  ? -11.367 6.752   -39.324 1.00 100.41 ? 146  LEU D C     1 
ATOM   2431 O  O     . LEU B 2 50  ? -10.555 6.980   -40.224 1.00 110.39 ? 146  LEU D O     1 
ATOM   2432 C  CB    . LEU B 2 50  ? -10.961 7.549   -36.989 1.00 105.41 ? 146  LEU D CB    1 
ATOM   2433 C  CG    . LEU B 2 50  ? -10.765 7.280   -35.497 1.00 93.29  ? 146  LEU D CG    1 
ATOM   2434 C  CD1   . LEU B 2 50  ? -10.829 8.578   -34.710 1.00 91.06  ? 146  LEU D CD1   1 
ATOM   2435 C  CD2   . LEU B 2 50  ? -11.810 6.299   -35.001 1.00 87.62  ? 146  LEU D CD2   1 
ATOM   2436 N  N     . PRO B 2 51  ? -12.681 6.835   -39.532 1.00 105.15 ? 147  PRO D N     1 
ATOM   2437 C  CA    . PRO B 2 51  ? -13.187 7.370   -40.800 1.00 116.69 ? 147  PRO D CA    1 
ATOM   2438 C  C     . PRO B 2 51  ? -12.775 8.823   -40.986 1.00 116.56 ? 147  PRO D C     1 
ATOM   2439 O  O     . PRO B 2 51  ? -12.414 9.524   -40.038 1.00 114.61 ? 147  PRO D O     1 
ATOM   2440 C  CB    . PRO B 2 51  ? -14.710 7.228   -40.671 1.00 114.30 ? 147  PRO D CB    1 
ATOM   2441 C  CG    . PRO B 2 51  ? -14.964 7.074   -39.206 1.00 120.36 ? 147  PRO D CG    1 
ATOM   2442 C  CD    . PRO B 2 51  ? -13.770 6.354   -38.666 1.00 108.90 ? 147  PRO D CD    1 
ATOM   2443 N  N     . ILE B 2 52  ? -12.830 9.271   -42.244 1.00 111.42 ? 148  ILE D N     1 
ATOM   2444 C  CA    . ILE B 2 52  ? -12.387 10.622  -42.579 1.00 114.41 ? 148  ILE D CA    1 
ATOM   2445 C  C     . ILE B 2 52  ? -13.222 11.667  -41.853 1.00 118.12 ? 148  ILE D C     1 
ATOM   2446 O  O     . ILE B 2 52  ? -12.704 12.714  -41.444 1.00 122.82 ? 148  ILE D O     1 
ATOM   2447 C  CB    . ILE B 2 52  ? -12.424 10.827  -44.107 1.00 112.02 ? 148  ILE D CB    1 
ATOM   2448 C  CG1   . ILE B 2 52  ? -11.507 9.818   -44.800 1.00 111.08 ? 148  ILE D CG1   1 
ATOM   2449 C  CG2   . ILE B 2 52  ? -12.019 12.248  -44.473 1.00 100.88 ? 148  ILE D CG2   1 
ATOM   2450 C  CD1   . ILE B 2 52  ? -11.458 9.971   -46.305 1.00 127.65 ? 148  ILE D CD1   1 
ATOM   2451 N  N     . ASP B 2 53  ? -14.516 11.401  -41.663 1.00 129.19 ? 149  ASP D N     1 
ATOM   2452 C  CA    . ASP B 2 53  ? -15.371 12.368  -40.983 1.00 134.57 ? 149  ASP D CA    1 
ATOM   2453 C  C     . ASP B 2 53  ? -15.034 12.483  -39.502 1.00 122.88 ? 149  ASP D C     1 
ATOM   2454 O  O     . ASP B 2 53  ? -15.234 13.546  -38.905 1.00 138.08 ? 149  ASP D O     1 
ATOM   2455 C  CB    . ASP B 2 53  ? -16.839 11.989  -41.169 1.00 141.46 ? 149  ASP D CB    1 
ATOM   2456 C  CG    . ASP B 2 53  ? -17.279 12.057  -42.620 1.00 154.21 ? 149  ASP D CG    1 
ATOM   2457 O  OD1   . ASP B 2 53  ? -16.739 12.901  -43.366 1.00 152.57 ? 149  ASP D OD1   1 
ATOM   2458 O  OD2   . ASP B 2 53  ? -18.164 11.269  -43.013 1.00 160.99 ? 149  ASP D OD2   1 
ATOM   2459 N  N     . ARG B 2 54  ? -14.526 11.413  -38.893 1.00 116.56 ? 150  ARG D N     1 
ATOM   2460 C  CA    . ARG B 2 54  ? -14.127 11.443  -37.492 1.00 130.69 ? 150  ARG D CA    1 
ATOM   2461 C  C     . ARG B 2 54  ? -12.696 11.925  -37.292 1.00 118.95 ? 150  ARG D C     1 
ATOM   2462 O  O     . ARG B 2 54  ? -12.215 11.936  -36.155 1.00 98.01  ? 150  ARG D O     1 
ATOM   2463 C  CB    . ARG B 2 54  ? -14.293 10.056  -36.862 1.00 125.65 ? 150  ARG D CB    1 
ATOM   2464 C  CG    . ARG B 2 54  ? -15.740 9.619   -36.693 1.00 132.40 ? 150  ARG D CG    1 
ATOM   2465 C  CD    . ARG B 2 54  ? -15.842 8.370   -35.832 1.00 116.29 ? 150  ARG D CD    1 
ATOM   2466 N  NE    . ARG B 2 54  ? -15.314 8.593   -34.492 1.00 119.77 ? 150  ARG D NE    1 
ATOM   2467 C  CZ    . ARG B 2 54  ? -15.284 7.676   -33.535 1.00 123.61 ? 150  ARG D CZ    1 
ATOM   2468 N  NH1   . ARG B 2 54  ? -15.745 6.452   -33.736 1.00 123.21 ? 150  ARG D NH1   1 
ATOM   2469 N  NH2   . ARG B 2 54  ? -14.779 7.994   -32.346 1.00 120.28 ? 150  ARG D NH2   1 
ATOM   2470 N  N     . GLY B 2 55  ? -12.011 12.322  -38.359 1.00 117.19 ? 151  GLY D N     1 
ATOM   2471 C  CA    . GLY B 2 55  ? -10.653 12.816  -38.252 1.00 106.13 ? 151  GLY D CA    1 
ATOM   2472 C  C     . GLY B 2 55  ? -9.569  11.794  -38.486 1.00 100.03 ? 151  GLY D C     1 
ATOM   2473 O  O     . GLY B 2 55  ? -8.412  12.049  -38.133 1.00 99.97  ? 151  GLY D O     1 
ATOM   2474 N  N     . GLY B 2 56  ? -9.895  10.640  -39.071 1.00 102.75 ? 152  GLY D N     1 
ATOM   2475 C  CA    . GLY B 2 56  ? -8.925  9.611   -39.346 1.00 96.33  ? 152  GLY D CA    1 
ATOM   2476 C  C     . GLY B 2 56  ? -8.427  9.645   -40.782 1.00 99.72  ? 152  GLY D C     1 
ATOM   2477 O  O     . GLY B 2 56  ? -8.611  10.617  -41.518 1.00 100.35 ? 152  GLY D O     1 
ATOM   2478 N  N     . GLY B 2 57  ? -7.784  8.551   -41.177 1.00 91.18  ? 153  GLY D N     1 
ATOM   2479 C  CA    . GLY B 2 57  ? -7.241  8.438   -42.516 1.00 85.10  ? 153  GLY D CA    1 
ATOM   2480 C  C     . GLY B 2 57  ? -7.746  7.226   -43.268 1.00 95.48  ? 153  GLY D C     1 
ATOM   2481 O  O     . GLY B 2 57  ? -7.452  7.061   -44.457 1.00 109.23 ? 153  GLY D O     1 
ATOM   2482 N  N     . GLU B 2 58  ? -8.507  6.373   -42.580 1.00 93.04  ? 154  GLU D N     1 
ATOM   2483 C  CA    . GLU B 2 58  ? -9.066  5.154   -43.167 1.00 99.93  ? 154  GLU D CA    1 
ATOM   2484 C  C     . GLU B 2 58  ? -7.973  4.274   -43.768 1.00 99.42  ? 154  GLU D C     1 
ATOM   2485 O  O     . GLU B 2 58  ? -8.110  3.749   -44.874 1.00 113.91 ? 154  GLU D O     1 
ATOM   2486 C  CB    . GLU B 2 58  ? -10.136 5.481   -44.212 1.00 111.17 ? 154  GLU D CB    1 
ATOM   2487 C  CG    . GLU B 2 58  ? -11.332 6.236   -43.660 1.00 109.09 ? 154  GLU D CG    1 
ATOM   2488 C  CD    . GLU B 2 58  ? -12.412 6.462   -44.700 1.00 132.97 ? 154  GLU D CD    1 
ATOM   2489 O  OE1   . GLU B 2 58  ? -12.234 6.017   -45.853 1.00 148.36 ? 154  GLU D OE1   1 
ATOM   2490 O  OE2   . GLU B 2 58  ? -13.441 7.086   -44.363 1.00 125.57 ? 154  GLU D OE2   1 
ATOM   2491 N  N     . GLY B 2 59  ? -6.876  4.114   -43.033 1.00 97.10  ? 155  GLY D N     1 
ATOM   2492 C  CA    . GLY B 2 59  ? -5.767  3.308   -43.506 1.00 101.48 ? 155  GLY D CA    1 
ATOM   2493 C  C     . GLY B 2 59  ? -5.026  2.671   -42.352 1.00 98.81  ? 155  GLY D C     1 
ATOM   2494 O  O     . GLY B 2 59  ? -5.117  3.114   -41.202 1.00 79.37  ? 155  GLY D O     1 
ATOM   2495 N  N     . LYS B 2 60  ? -4.288  1.613   -42.677 1.00 93.51  ? 156  LYS D N     1 
ATOM   2496 C  CA    . LYS B 2 60  ? -3.504  0.911   -41.675 1.00 75.67  ? 156  LYS D CA    1 
ATOM   2497 C  C     . LYS B 2 60  ? -2.359  1.789   -41.179 1.00 81.49  ? 156  LYS D C     1 
ATOM   2498 O  O     . LYS B 2 60  ? -1.919  2.728   -41.848 1.00 83.77  ? 156  LYS D O     1 
ATOM   2499 C  CB    . LYS B 2 60  ? -2.950  -0.396  -42.243 1.00 72.40  ? 156  LYS D CB    1 
ATOM   2500 C  CG    . LYS B 2 60  ? -4.009  -1.358  -42.751 1.00 90.20  ? 156  LYS D CG    1 
ATOM   2501 C  CD    . LYS B 2 60  ? -3.382  -2.630  -43.300 1.00 79.54  ? 156  LYS D CD    1 
ATOM   2502 C  CE    . LYS B 2 60  ? -2.578  -3.352  -42.232 1.00 88.35  ? 156  LYS D CE    1 
ATOM   2503 N  NZ    . LYS B 2 60  ? -1.965  -4.607  -42.749 1.00 93.87  ? 156  LYS D NZ    1 
ATOM   2504 N  N     . ALA B 2 61  ? -1.878  1.470   -39.983 1.00 87.70  ? 157  ALA D N     1 
ATOM   2505 C  CA    . ALA B 2 61  ? -0.748  2.163   -39.385 1.00 71.64  ? 157  ALA D CA    1 
ATOM   2506 C  C     . ALA B 2 61  ? 0.504   1.301   -39.479 1.00 68.38  ? 157  ALA D C     1 
ATOM   2507 O  O     . ALA B 2 61  ? 0.433   0.070   -39.526 1.00 65.95  ? 157  ALA D O     1 
ATOM   2508 C  CB    . ALA B 2 61  ? -1.030  2.514   -37.923 1.00 82.08  ? 157  ALA D CB    1 
ATOM   2509 N  N     . MET B 2 62  ? 1.657   1.962   -39.508 1.00 64.32  ? 158  MET D N     1 
ATOM   2510 C  CA    . MET B 2 62  ? 2.945   1.283   -39.566 1.00 70.73  ? 158  MET D CA    1 
ATOM   2511 C  C     . MET B 2 62  ? 3.849   1.868   -38.494 1.00 80.35  ? 158  MET D C     1 
ATOM   2512 O  O     . MET B 2 62  ? 4.081   3.082   -38.469 1.00 78.43  ? 158  MET D O     1 
ATOM   2513 C  CB    . MET B 2 62  ? 3.582   1.423   -40.949 1.00 73.99  ? 158  MET D CB    1 
ATOM   2514 C  CG    . MET B 2 62  ? 4.847   0.610   -41.118 1.00 79.95  ? 158  MET D CG    1 
ATOM   2515 S  SD    . MET B 2 62  ? 5.444   0.619   -42.814 1.00 83.56  ? 158  MET D SD    1 
ATOM   2516 C  CE    . MET B 2 62  ? 4.030   -0.064  -43.676 1.00 85.38  ? 158  MET D CE    1 
ATOM   2517 N  N     . TYR B 2 63  ? 4.358   1.008   -37.614 1.00 71.47  ? 159  TYR D N     1 
ATOM   2518 C  CA    . TYR B 2 63  ? 5.166   1.425   -36.472 1.00 70.01  ? 159  TYR D CA    1 
ATOM   2519 C  C     . TYR B 2 63  ? 6.539   0.774   -36.580 1.00 66.48  ? 159  TYR D C     1 
ATOM   2520 O  O     . TYR B 2 63  ? 6.680   -0.434  -36.355 1.00 67.60  ? 159  TYR D O     1 
ATOM   2521 C  CB    . TYR B 2 63  ? 4.483   1.050   -35.157 1.00 66.20  ? 159  TYR D CB    1 
ATOM   2522 C  CG    . TYR B 2 63  ? 4.934   1.871   -33.969 1.00 75.21  ? 159  TYR D CG    1 
ATOM   2523 C  CD1   . TYR B 2 63  ? 6.159   1.634   -33.359 1.00 79.89  ? 159  TYR D CD1   1 
ATOM   2524 C  CD2   . TYR B 2 63  ? 4.129   2.879   -33.453 1.00 73.31  ? 159  TYR D CD2   1 
ATOM   2525 C  CE1   . TYR B 2 63  ? 6.573   2.382   -32.272 1.00 76.59  ? 159  TYR D CE1   1 
ATOM   2526 C  CE2   . TYR B 2 63  ? 4.534   3.632   -32.366 1.00 75.67  ? 159  TYR D CE2   1 
ATOM   2527 C  CZ    . TYR B 2 63  ? 5.757   3.379   -31.780 1.00 77.61  ? 159  TYR D CZ    1 
ATOM   2528 O  OH    . TYR B 2 63  ? 6.166   4.124   -30.698 1.00 74.50  ? 159  TYR D OH    1 
ATOM   2529 N  N     . ILE B 2 64  ? 7.545   1.574   -36.917 1.00 67.34  ? 160  ILE D N     1 
ATOM   2530 C  CA    . ILE B 2 64  ? 8.933   1.131   -36.947 1.00 80.56  ? 160  ILE D CA    1 
ATOM   2531 C  C     . ILE B 2 64  ? 9.578   1.630   -35.660 1.00 78.04  ? 160  ILE D C     1 
ATOM   2532 O  O     . ILE B 2 64  ? 9.911   2.812   -35.531 1.00 78.96  ? 160  ILE D O     1 
ATOM   2533 C  CB    . ILE B 2 64  ? 9.669   1.638   -38.190 1.00 83.80  ? 160  ILE D CB    1 
ATOM   2534 C  CG1   . ILE B 2 64  ? 8.989   1.119   -39.458 1.00 68.52  ? 160  ILE D CG1   1 
ATOM   2535 C  CG2   . ILE B 2 64  ? 11.128  1.210   -38.154 1.00 69.07  ? 160  ILE D CG2   1 
ATOM   2536 C  CD1   . ILE B 2 64  ? 9.677   1.541   -40.736 1.00 71.56  ? 160  ILE D CD1   1 
ATOM   2537 N  N     . ASP B 2 65  ? 9.751   0.727   -34.701 1.00 76.89  ? 161  ASP D N     1 
ATOM   2538 C  CA    . ASP B 2 65  ? 10.313  1.058   -33.401 1.00 71.45  ? 161  ASP D CA    1 
ATOM   2539 C  C     . ASP B 2 65  ? 11.797  0.719   -33.370 1.00 70.21  ? 161  ASP D C     1 
ATOM   2540 O  O     . ASP B 2 65  ? 12.231  -0.270  -33.968 1.00 80.72  ? 161  ASP D O     1 
ATOM   2541 C  CB    . ASP B 2 65  ? 9.579   0.309   -32.287 1.00 85.77  ? 161  ASP D CB    1 
ATOM   2542 C  CG    . ASP B 2 65  ? 10.198  0.539   -30.924 1.00 87.48  ? 161  ASP D CG    1 
ATOM   2543 O  OD1   . ASP B 2 65  ? 9.896   1.575   -30.294 1.00 79.58  ? 161  ASP D OD1   1 
ATOM   2544 O  OD2   . ASP B 2 65  ? 10.993  -0.317  -30.488 1.00 83.54  ? 161  ASP D OD2   1 
ATOM   2545 N  N     . THR B 2 66  ? 12.575  1.551   -32.674 1.00 70.62  ? 162  THR D N     1 
ATOM   2546 C  CA    . THR B 2 66  ? 14.006  1.331   -32.530 1.00 79.75  ? 162  THR D CA    1 
ATOM   2547 C  C     . THR B 2 66  ? 14.476  1.326   -31.082 1.00 76.81  ? 162  THR D C     1 
ATOM   2548 O  O     . THR B 2 66  ? 15.676  1.150   -30.842 1.00 85.81  ? 162  THR D O     1 
ATOM   2549 C  CB    . THR B 2 66  ? 14.800  2.396   -33.305 1.00 62.09  ? 162  THR D CB    1 
ATOM   2550 O  OG1   . THR B 2 66  ? 14.507  3.694   -32.775 1.00 73.66  ? 162  THR D OG1   1 
ATOM   2551 C  CG2   . THR B 2 66  ? 14.443  2.363   -34.784 1.00 87.44  ? 162  THR D CG2   1 
ATOM   2552 N  N     . GLU B 2 67  ? 13.578  1.512   -30.115 1.00 70.46  ? 163  GLU D N     1 
ATOM   2553 C  CA    . GLU B 2 67  ? 13.953  1.581   -28.710 1.00 86.03  ? 163  GLU D CA    1 
ATOM   2554 C  C     . GLU B 2 67  ? 13.243  0.555   -27.838 1.00 79.57  ? 163  GLU D C     1 
ATOM   2555 O  O     . GLU B 2 67  ? 13.422  0.579   -26.615 1.00 82.43  ? 163  GLU D O     1 
ATOM   2556 C  CB    . GLU B 2 67  ? 13.685  2.987   -28.158 1.00 83.54  ? 163  GLU D CB    1 
ATOM   2557 C  CG    . GLU B 2 67  ? 14.553  4.072   -28.771 1.00 92.66  ? 163  GLU D CG    1 
ATOM   2558 C  CD    . GLU B 2 67  ? 14.206  5.455   -28.255 1.00 106.05 ? 163  GLU D CD    1 
ATOM   2559 O  OE1   . GLU B 2 67  ? 13.062  5.647   -27.792 1.00 105.65 ? 163  GLU D OE1   1 
ATOM   2560 O  OE2   . GLU B 2 67  ? 15.076  6.349   -28.313 1.00 101.08 ? 163  GLU D OE2   1 
ATOM   2561 N  N     . GLY B 2 68  ? 12.448  -0.339  -28.419 1.00 83.11  ? 164  GLY D N     1 
ATOM   2562 C  CA    . GLY B 2 68  ? 11.757  -1.341  -27.630 1.00 69.78  ? 164  GLY D CA    1 
ATOM   2563 C  C     . GLY B 2 68  ? 10.658  -0.795  -26.748 1.00 72.75  ? 164  GLY D C     1 
ATOM   2564 O  O     . GLY B 2 68  ? 10.370  -1.376  -25.697 1.00 84.24  ? 164  GLY D O     1 
ATOM   2565 N  N     . THR B 2 69  ? 10.030  0.311   -27.149 1.00 70.93  ? 165  THR D N     1 
ATOM   2566 C  CA    . THR B 2 69  ? 8.983   0.950   -26.361 1.00 74.02  ? 165  THR D CA    1 
ATOM   2567 C  C     . THR B 2 69  ? 7.640   0.936   -27.086 1.00 85.65  ? 165  THR D C     1 
ATOM   2568 O  O     . THR B 2 69  ? 6.845   1.868   -26.951 1.00 92.66  ? 165  THR D O     1 
ATOM   2569 C  CB    . THR B 2 69  ? 9.374   2.382   -25.998 1.00 66.58  ? 165  THR D CB    1 
ATOM   2570 O  OG1   . THR B 2 69  ? 9.761   3.090   -27.183 1.00 63.28  ? 165  THR D OG1   1 
ATOM   2571 C  CG2   . THR B 2 69  ? 10.528  2.378   -25.016 1.00 84.14  ? 165  THR D CG2   1 
ATOM   2572 N  N     . PHE B 2 70  ? 7.376   -0.112  -27.859 1.00 77.89  ? 166  PHE D N     1 
ATOM   2573 C  CA    . PHE B 2 70  ? 6.090   -0.289  -28.520 1.00 71.31  ? 166  PHE D CA    1 
ATOM   2574 C  C     . PHE B 2 70  ? 5.239   -1.239  -27.688 1.00 74.79  ? 166  PHE D C     1 
ATOM   2575 O  O     . PHE B 2 70  ? 5.588   -2.413  -27.525 1.00 70.86  ? 166  PHE D O     1 
ATOM   2576 C  CB    . PHE B 2 70  ? 6.265   -0.828  -29.940 1.00 68.35  ? 166  PHE D CB    1 
ATOM   2577 C  CG    . PHE B 2 70  ? 4.967   -1.130  -30.634 1.00 61.60  ? 166  PHE D CG    1 
ATOM   2578 C  CD1   . PHE B 2 70  ? 4.167   -0.105  -31.113 1.00 71.23  ? 166  PHE D CD1   1 
ATOM   2579 C  CD2   . PHE B 2 70  ? 4.546   -2.438  -30.808 1.00 70.65  ? 166  PHE D CD2   1 
ATOM   2580 C  CE1   . PHE B 2 70  ? 2.971   -0.379  -31.751 1.00 68.18  ? 166  PHE D CE1   1 
ATOM   2581 C  CE2   . PHE B 2 70  ? 3.352   -2.719  -31.447 1.00 62.33  ? 166  PHE D CE2   1 
ATOM   2582 C  CZ    . PHE B 2 70  ? 2.564   -1.688  -31.919 1.00 61.37  ? 166  PHE D CZ    1 
ATOM   2583 N  N     . ARG B 2 71  ? 4.131   -0.730  -27.163 1.00 63.55  ? 167  ARG D N     1 
ATOM   2584 C  CA    . ARG B 2 71  ? 3.225   -1.520  -26.332 1.00 81.90  ? 167  ARG D CA    1 
ATOM   2585 C  C     . ARG B 2 71  ? 1.825   -1.486  -26.925 1.00 82.87  ? 167  ARG D C     1 
ATOM   2586 O  O     . ARG B 2 71  ? 1.165   -0.430  -26.884 1.00 81.57  ? 167  ARG D O     1 
ATOM   2587 C  CB    . ARG B 2 71  ? 3.209   -0.990  -24.898 1.00 77.45  ? 167  ARG D CB    1 
ATOM   2588 C  CG    . ARG B 2 71  ? 4.567   -1.002  -24.217 1.00 80.40  ? 167  ARG D CG    1 
ATOM   2589 C  CD    . ARG B 2 71  ? 5.117   -2.415  -24.107 1.00 79.40  ? 167  ARG D CD    1 
ATOM   2590 N  NE    . ARG B 2 71  ? 6.394   -2.453  -23.404 1.00 73.91  ? 167  ARG D NE    1 
ATOM   2591 C  CZ    . ARG B 2 71  ? 7.578   -2.362  -23.994 1.00 85.38  ? 167  ARG D CZ    1 
ATOM   2592 N  NH1   . ARG B 2 71  ? 7.687   -2.223  -25.305 1.00 90.04  ? 167  ARG D NH1   1 
ATOM   2593 N  NH2   . ARG B 2 71  ? 8.679   -2.412  -23.251 1.00 81.45  ? 167  ARG D NH2   1 
ATOM   2594 N  N     . PRO B 2 72  ? 1.329   -2.593  -27.487 1.00 78.08  ? 168  PRO D N     1 
ATOM   2595 C  CA    . PRO B 2 72  ? -0.052  -2.604  -28.000 1.00 61.22  ? 168  PRO D CA    1 
ATOM   2596 C  C     . PRO B 2 72  ? -1.104  -2.371  -26.926 1.00 77.48  ? 168  PRO D C     1 
ATOM   2597 O  O     . PRO B 2 72  ? -2.273  -2.146  -27.270 1.00 78.15  ? 168  PRO D O     1 
ATOM   2598 C  CB    . PRO B 2 72  ? -0.189  -4.004  -28.616 1.00 76.75  ? 168  PRO D CB    1 
ATOM   2599 C  CG    . PRO B 2 72  ? 1.218   -4.440  -28.889 1.00 61.82  ? 168  PRO D CG    1 
ATOM   2600 C  CD    . PRO B 2 72  ? 2.045   -3.842  -27.792 1.00 67.40  ? 168  PRO D CD    1 
ATOM   2601 N  N     . GLU B 2 73  ? -0.731  -2.425  -25.646 1.00 92.64  ? 169  GLU D N     1 
ATOM   2602 C  CA    . GLU B 2 73  ? -1.683  -2.137  -24.579 1.00 79.41  ? 169  GLU D CA    1 
ATOM   2603 C  C     . GLU B 2 73  ? -2.165  -0.693  -24.651 1.00 87.31  ? 169  GLU D C     1 
ATOM   2604 O  O     . GLU B 2 73  ? -3.348  -0.410  -24.423 1.00 81.26  ? 169  GLU D O     1 
ATOM   2605 C  CB    . GLU B 2 73  ? -1.041  -2.429  -23.224 1.00 82.47  ? 169  GLU D CB    1 
ATOM   2606 C  CG    . GLU B 2 73  ? -0.235  -3.719  -23.202 1.00 90.66  ? 169  GLU D CG    1 
ATOM   2607 C  CD    . GLU B 2 73  ? 0.581   -3.881  -21.936 1.00 130.71 ? 169  GLU D CD    1 
ATOM   2608 O  OE1   . GLU B 2 73  ? 0.215   -3.274  -20.908 1.00 155.07 ? 169  GLU D OE1   1 
ATOM   2609 O  OE2   . GLU B 2 73  ? 1.594   -4.612  -21.972 1.00 111.54 ? 169  GLU D OE2   1 
ATOM   2610 N  N     . ARG B 2 74  ? -1.261  0.236   -24.973 1.00 80.52  ? 170  ARG D N     1 
ATOM   2611 C  CA    . ARG B 2 74  ? -1.665  1.625   -25.167 1.00 76.75  ? 170  ARG D CA    1 
ATOM   2612 C  C     . ARG B 2 74  ? -2.619  1.754   -26.348 1.00 93.30  ? 170  ARG D C     1 
ATOM   2613 O  O     . ARG B 2 74  ? -3.561  2.557   -26.315 1.00 101.16 ? 170  ARG D O     1 
ATOM   2614 C  CB    . ARG B 2 74  ? -0.432  2.504   -25.373 1.00 82.15  ? 170  ARG D CB    1 
ATOM   2615 C  CG    . ARG B 2 74  ? -0.494  3.842   -24.661 1.00 82.64  ? 170  ARG D CG    1 
ATOM   2616 C  CD    . ARG B 2 74  ? -0.293  3.674   -23.165 1.00 88.59  ? 170  ARG D CD    1 
ATOM   2617 N  NE    . ARG B 2 74  ? -0.518  4.921   -22.446 1.00 102.56 ? 170  ARG D NE    1 
ATOM   2618 C  CZ    . ARG B 2 74  ? -1.678  5.275   -21.910 1.00 106.53 ? 170  ARG D CZ    1 
ATOM   2619 N  NH1   . ARG B 2 74  ? -2.741  4.490   -21.984 1.00 90.69  ? 170  ARG D NH1   1 
ATOM   2620 N  NH2   . ARG B 2 74  ? -1.774  6.445   -21.285 1.00 113.41 ? 170  ARG D NH2   1 
ATOM   2621 N  N     . LEU B 2 75  ? -2.389  0.965   -27.401 1.00 81.74  ? 171  LEU D N     1 
ATOM   2622 C  CA    . LEU B 2 75  ? -3.294  0.973   -28.546 1.00 88.09  ? 171  LEU D CA    1 
ATOM   2623 C  C     . LEU B 2 75  ? -4.677  0.473   -28.152 1.00 86.60  ? 171  LEU D C     1 
ATOM   2624 O  O     . LEU B 2 75  ? -5.692  1.053   -28.552 1.00 96.66  ? 171  LEU D O     1 
ATOM   2625 C  CB    . LEU B 2 75  ? -2.715  0.125   -29.678 1.00 93.51  ? 171  LEU D CB    1 
ATOM   2626 C  CG    . LEU B 2 75  ? -1.269  0.417   -30.084 1.00 74.65  ? 171  LEU D CG    1 
ATOM   2627 C  CD1   . LEU B 2 75  ? -0.854  -0.449  -31.265 1.00 75.40  ? 171  LEU D CD1   1 
ATOM   2628 C  CD2   . LEU B 2 75  ? -1.080  1.891   -30.403 1.00 76.72  ? 171  LEU D CD2   1 
ATOM   2629 N  N     . LEU B 2 76  ? -4.737  -0.605  -27.365 1.00 89.78  ? 172  LEU D N     1 
ATOM   2630 C  CA    . LEU B 2 76  ? -6.022  -1.091  -26.871 1.00 87.23  ? 172  LEU D CA    1 
ATOM   2631 C  C     . LEU B 2 76  ? -6.715  -0.040  -26.011 1.00 95.60  ? 172  LEU D C     1 
ATOM   2632 O  O     . LEU B 2 76  ? -7.934  0.150   -26.107 1.00 109.42 ? 172  LEU D O     1 
ATOM   2633 C  CB    . LEU B 2 76  ? -5.827  -2.383  -26.077 1.00 80.13  ? 172  LEU D CB    1 
ATOM   2634 C  CG    . LEU B 2 76  ? -5.375  -3.622  -26.851 1.00 86.75  ? 172  LEU D CG    1 
ATOM   2635 C  CD1   . LEU B 2 76  ? -5.037  -4.754  -25.895 1.00 80.12  ? 172  LEU D CD1   1 
ATOM   2636 C  CD2   . LEU B 2 76  ? -6.451  -4.056  -27.831 1.00 82.69  ? 172  LEU D CD2   1 
ATOM   2637 N  N     . ALA B 2 77  ? -5.948  0.658   -25.169 1.00 91.39  ? 173  ALA D N     1 
ATOM   2638 C  CA    . ALA B 2 77  ? -6.529  1.681   -24.305 1.00 83.41  ? 173  ALA D CA    1 
ATOM   2639 C  C     . ALA B 2 77  ? -7.132  2.817   -25.123 1.00 102.47 ? 173  ALA D C     1 
ATOM   2640 O  O     . ALA B 2 77  ? -8.271  3.234   -24.884 1.00 104.16 ? 173  ALA D O     1 
ATOM   2641 C  CB    . ALA B 2 77  ? -5.470  2.213   -23.339 1.00 87.77  ? 173  ALA D CB    1 
ATOM   2642 N  N     . VAL B 2 78  ? -6.384  3.325   -26.105 1.00 100.47 ? 174  VAL D N     1 
ATOM   2643 C  CA    . VAL B 2 78  ? -6.900  4.441   -26.894 1.00 98.17  ? 174  VAL D CA    1 
ATOM   2644 C  C     . VAL B 2 78  ? -8.026  3.984   -27.818 1.00 98.77  ? 174  VAL D C     1 
ATOM   2645 O  O     . VAL B 2 78  ? -8.912  4.777   -28.165 1.00 95.57  ? 174  VAL D O     1 
ATOM   2646 C  CB    . VAL B 2 78  ? -5.762  5.128   -27.672 1.00 82.96  ? 174  VAL D CB    1 
ATOM   2647 C  CG1   . VAL B 2 78  ? -4.706  5.650   -26.713 1.00 90.77  ? 174  VAL D CG1   1 
ATOM   2648 C  CG2   . VAL B 2 78  ? -5.145  4.176   -28.665 1.00 103.35 ? 174  VAL D CG2   1 
ATOM   2649 N  N     . ALA B 2 79  ? -8.033  2.708   -28.216 1.00 93.80  ? 175  ALA D N     1 
ATOM   2650 C  CA    . ALA B 2 79  ? -9.136  2.196   -29.022 1.00 91.12  ? 175  ALA D CA    1 
ATOM   2651 C  C     . ALA B 2 79  ? -10.412 2.088   -28.199 1.00 100.89 ? 175  ALA D C     1 
ATOM   2652 O  O     . ALA B 2 79  ? -11.503 2.396   -28.692 1.00 107.38 ? 175  ALA D O     1 
ATOM   2653 C  CB    . ALA B 2 79  ? -8.764  0.840   -29.621 1.00 91.81  ? 175  ALA D CB    1 
ATOM   2654 N  N     . GLU B 2 80  ? -10.296 1.644   -26.945 1.00 116.65 ? 176  GLU D N     1 
ATOM   2655 C  CA    . GLU B 2 80  ? -11.442 1.681   -26.044 1.00 103.71 ? 176  GLU D CA    1 
ATOM   2656 C  C     . GLU B 2 80  ? -11.886 3.116   -25.790 1.00 100.86 ? 176  GLU D C     1 
ATOM   2657 O  O     . GLU B 2 80  ? -13.085 3.391   -25.652 1.00 101.94 ? 176  GLU D O     1 
ATOM   2658 C  CB    . GLU B 2 80  ? -11.098 0.982   -24.728 1.00 117.90 ? 176  GLU D CB    1 
ATOM   2659 C  CG    . GLU B 2 80  ? -12.207 1.022   -23.689 1.00 110.92 ? 176  GLU D CG    1 
ATOM   2660 C  CD    . GLU B 2 80  ? -11.780 0.436   -22.358 1.00 132.14 ? 176  GLU D CD    1 
ATOM   2661 O  OE1   . GLU B 2 80  ? -10.646 -0.080  -22.272 1.00 139.86 ? 176  GLU D OE1   1 
ATOM   2662 O  OE2   . GLU B 2 80  ? -12.577 0.494   -21.398 1.00 134.70 ? 176  GLU D OE2   1 
ATOM   2663 N  N     . ARG B 2 81  ? -10.929 4.045   -25.729 1.00 108.04 ? 177  ARG D N     1 
ATOM   2664 C  CA    . ARG B 2 81  ? -11.261 5.456   -25.562 1.00 107.33 ? 177  ARG D CA    1 
ATOM   2665 C  C     . ARG B 2 81  ? -12.098 5.965   -26.729 1.00 100.06 ? 177  ARG D C     1 
ATOM   2666 O  O     . ARG B 2 81  ? -13.106 6.654   -26.533 1.00 97.83  ? 177  ARG D O     1 
ATOM   2667 C  CB    . ARG B 2 81  ? -9.977  6.275   -25.412 1.00 109.33 ? 177  ARG D CB    1 
ATOM   2668 C  CG    . ARG B 2 81  ? -10.177 7.778   -25.256 1.00 101.99 ? 177  ARG D CG    1 
ATOM   2669 C  CD    . ARG B 2 81  ? -9.943  8.510   -26.569 1.00 98.90  ? 177  ARG D CD    1 
ATOM   2670 N  NE    . ARG B 2 81  ? -9.780  9.947   -26.384 1.00 96.35  ? 177  ARG D NE    1 
ATOM   2671 C  CZ    . ARG B 2 81  ? -8.609  10.559  -26.278 1.00 107.90 ? 177  ARG D CZ    1 
ATOM   2672 N  NH1   . ARG B 2 81  ? -7.470  9.886   -26.333 1.00 103.58 ? 177  ARG D NH1   1 
ATOM   2673 N  NH2   . ARG B 2 81  ? -8.578  11.878  -26.115 1.00 111.56 ? 177  ARG D NH2   1 
ATOM   2674 N  N     . TYR B 2 82  ? -11.695 5.637   -27.954 1.00 103.31 ? 178  TYR D N     1 
ATOM   2675 C  CA    . TYR B 2 82  ? -12.437 6.042   -29.141 1.00 107.44 ? 178  TYR D CA    1 
ATOM   2676 C  C     . TYR B 2 82  ? -13.575 5.091   -29.489 1.00 113.52 ? 178  TYR D C     1 
ATOM   2677 O  O     . TYR B 2 82  ? -14.265 5.318   -30.488 1.00 112.67 ? 178  TYR D O     1 
ATOM   2678 C  CB    . TYR B 2 82  ? -11.492 6.175   -30.340 1.00 110.76 ? 178  TYR D CB    1 
ATOM   2679 C  CG    . TYR B 2 82  ? -10.891 7.554   -30.483 1.00 92.59  ? 178  TYR D CG    1 
ATOM   2680 C  CD1   . TYR B 2 82  ? -11.586 8.570   -31.125 1.00 94.83  ? 178  TYR D CD1   1 
ATOM   2681 C  CD2   . TYR B 2 82  ? -9.631  7.841   -29.976 1.00 90.42  ? 178  TYR D CD2   1 
ATOM   2682 C  CE1   . TYR B 2 82  ? -11.045 9.833   -31.259 1.00 103.63 ? 178  TYR D CE1   1 
ATOM   2683 C  CE2   . TYR B 2 82  ? -9.081  9.102   -30.103 1.00 91.98  ? 178  TYR D CE2   1 
ATOM   2684 C  CZ    . TYR B 2 82  ? -9.792  10.094  -30.746 1.00 102.29 ? 178  TYR D CZ    1 
ATOM   2685 O  OH    . TYR B 2 82  ? -9.250  11.351  -30.878 1.00 110.41 ? 178  TYR D OH    1 
ATOM   2686 N  N     . GLY B 2 83  ? -13.789 4.043   -28.697 1.00 114.55 ? 179  GLY D N     1 
ATOM   2687 C  CA    . GLY B 2 83  ? -14.877 3.117   -28.945 1.00 110.10 ? 179  GLY D CA    1 
ATOM   2688 C  C     . GLY B 2 83  ? -14.672 2.258   -30.175 1.00 104.43 ? 179  GLY D C     1 
ATOM   2689 O  O     . GLY B 2 83  ? -15.575 2.120   -31.004 1.00 112.53 ? 179  GLY D O     1 
ATOM   2690 N  N     . LEU B 2 84  ? -13.483 1.677   -30.302 1.00 107.48 ? 180  LEU D N     1 
ATOM   2691 C  CA    . LEU B 2 84  ? -13.141 0.812   -31.419 1.00 109.82 ? 180  LEU D CA    1 
ATOM   2692 C  C     . LEU B 2 84  ? -12.827 -0.587  -30.908 1.00 109.41 ? 180  LEU D C     1 
ATOM   2693 O  O     . LEU B 2 84  ? -12.359 -0.763  -29.779 1.00 101.40 ? 180  LEU D O     1 
ATOM   2694 C  CB    . LEU B 2 84  ? -11.940 1.357   -32.208 1.00 99.17  ? 180  LEU D CB    1 
ATOM   2695 C  CG    . LEU B 2 84  ? -12.191 2.368   -33.331 1.00 103.61 ? 180  LEU D CG    1 
ATOM   2696 C  CD1   . LEU B 2 84  ? -12.885 3.617   -32.819 1.00 105.90 ? 180  LEU D CD1   1 
ATOM   2697 C  CD2   . LEU B 2 84  ? -10.882 2.733   -34.017 1.00 109.92 ? 180  LEU D CD2   1 
ATOM   2698 N  N     . SER B 2 85  ? -13.095 -1.583  -31.750 1.00 108.25 ? 181  SER D N     1 
ATOM   2699 C  CA    . SER B 2 85  ? -12.779 -2.963  -31.405 1.00 104.78 ? 181  SER D CA    1 
ATOM   2700 C  C     . SER B 2 85  ? -11.267 -3.147  -31.382 1.00 106.59 ? 181  SER D C     1 
ATOM   2701 O  O     . SER B 2 85  ? -10.587 -2.883  -32.380 1.00 103.90 ? 181  SER D O     1 
ATOM   2702 C  CB    . SER B 2 85  ? -13.424 -3.920  -32.403 1.00 111.20 ? 181  SER D CB    1 
ATOM   2703 O  OG    . SER B 2 85  ? -13.162 -5.269  -32.057 1.00 111.18 ? 181  SER D OG    1 
ATOM   2704 N  N     . GLY B 2 86  ? -10.740 -3.595  -30.239 1.00 115.95 ? 182  GLY D N     1 
ATOM   2705 C  CA    . GLY B 2 86  ? -9.301  -3.738  -30.101 1.00 91.86  ? 182  GLY D CA    1 
ATOM   2706 C  C     . GLY B 2 86  ? -8.694  -4.714  -31.088 1.00 96.61  ? 182  GLY D C     1 
ATOM   2707 O  O     . GLY B 2 86  ? -7.550  -4.537  -31.517 1.00 101.50 ? 182  GLY D O     1 
ATOM   2708 N  N     . SER B 2 87  ? -9.445  -5.750  -31.467 1.00 86.76  ? 183  SER D N     1 
ATOM   2709 C  CA    . SER B 2 87  ? -8.936  -6.724  -32.427 1.00 106.35 ? 183  SER D CA    1 
ATOM   2710 C  C     . SER B 2 87  ? -8.672  -6.075  -33.780 1.00 106.74 ? 183  SER D C     1 
ATOM   2711 O  O     . SER B 2 87  ? -7.584  -6.218  -34.349 1.00 107.80 ? 183  SER D O     1 
ATOM   2712 C  CB    . SER B 2 87  ? -9.923  -7.884  -32.567 1.00 109.76 ? 183  SER D CB    1 
ATOM   2713 O  OG    . SER B 2 87  ? -9.469  -8.826  -33.524 1.00 119.06 ? 183  SER D OG    1 
ATOM   2714 N  N     . ASP B 2 88  ? -9.660  -5.347  -34.308 1.00 106.33 ? 184  ASP D N     1 
ATOM   2715 C  CA    . ASP B 2 88  ? -9.489  -4.700  -35.604 1.00 107.20 ? 184  ASP D CA    1 
ATOM   2716 C  C     . ASP B 2 88  ? -8.420  -3.617  -35.558 1.00 98.76  ? 184  ASP D C     1 
ATOM   2717 O  O     . ASP B 2 88  ? -7.740  -3.377  -36.562 1.00 105.78 ? 184  ASP D O     1 
ATOM   2718 C  CB    . ASP B 2 88  ? -10.818 -4.110  -36.077 1.00 110.37 ? 184  ASP D CB    1 
ATOM   2719 C  CG    . ASP B 2 88  ? -11.924 -5.143  -36.141 1.00 119.56 ? 184  ASP D CG    1 
ATOM   2720 O  OD1   . ASP B 2 88  ? -11.697 -6.288  -35.697 1.00 118.50 ? 184  ASP D OD1   1 
ATOM   2721 O  OD2   . ASP B 2 88  ? -13.020 -4.810  -36.638 1.00 125.81 ? 184  ASP D OD2   1 
ATOM   2722 N  N     . VAL B 2 89  ? -8.254  -2.956  -34.411 1.00 97.36  ? 185  VAL D N     1 
ATOM   2723 C  CA    . VAL B 2 89  ? -7.242  -1.912  -34.295 1.00 93.39  ? 185  VAL D CA    1 
ATOM   2724 C  C     . VAL B 2 89  ? -5.845  -2.522  -34.285 1.00 94.98  ? 185  VAL D C     1 
ATOM   2725 O  O     . VAL B 2 89  ? -4.937  -2.046  -34.976 1.00 90.11  ? 185  VAL D O     1 
ATOM   2726 C  CB    . VAL B 2 89  ? -7.496  -1.056  -33.042 1.00 93.02  ? 185  VAL D CB    1 
ATOM   2727 C  CG1   . VAL B 2 89  ? -6.328  -0.121  -32.796 1.00 92.79  ? 185  VAL D CG1   1 
ATOM   2728 C  CG2   . VAL B 2 89  ? -8.785  -0.267  -33.196 1.00 95.31  ? 185  VAL D CG2   1 
ATOM   2729 N  N     . LEU B 2 90  ? -5.653  -3.587  -33.504 1.00 96.22  ? 186  LEU D N     1 
ATOM   2730 C  CA    . LEU B 2 90  ? -4.345  -4.228  -33.441 1.00 90.82  ? 186  LEU D CA    1 
ATOM   2731 C  C     . LEU B 2 90  ? -4.018  -5.012  -34.705 1.00 94.74  ? 186  LEU D C     1 
ATOM   2732 O  O     . LEU B 2 90  ? -2.837  -5.246  -34.983 1.00 84.55  ? 186  LEU D O     1 
ATOM   2733 C  CB    . LEU B 2 90  ? -4.264  -5.147  -32.221 1.00 89.33  ? 186  LEU D CB    1 
ATOM   2734 C  CG    . LEU B 2 90  ? -3.548  -4.574  -30.995 1.00 91.85  ? 186  LEU D CG    1 
ATOM   2735 C  CD1   . LEU B 2 90  ? -4.148  -3.239  -30.583 1.00 80.09  ? 186  LEU D CD1   1 
ATOM   2736 C  CD2   . LEU B 2 90  ? -3.586  -5.563  -29.839 1.00 89.48  ? 186  LEU D CD2   1 
ATOM   2737 N  N     . ASP B 2 91  ? -5.027  -5.420  -35.477 1.00 98.33  ? 187  ASP D N     1 
ATOM   2738 C  CA    . ASP B 2 91  ? -4.766  -6.132  -36.721 1.00 89.64  ? 187  ASP D CA    1 
ATOM   2739 C  C     . ASP B 2 91  ? -4.400  -5.199  -37.868 1.00 93.70  ? 187  ASP D C     1 
ATOM   2740 O  O     . ASP B 2 91  ? -3.820  -5.656  -38.858 1.00 93.92  ? 187  ASP D O     1 
ATOM   2741 C  CB    . ASP B 2 91  ? -5.980  -6.978  -37.112 1.00 101.82 ? 187  ASP D CB    1 
ATOM   2742 C  CG    . ASP B 2 91  ? -6.186  -8.163  -36.188 1.00 112.28 ? 187  ASP D CG    1 
ATOM   2743 O  OD1   . ASP B 2 91  ? -5.185  -8.675  -35.644 1.00 112.56 ? 187  ASP D OD1   1 
ATOM   2744 O  OD2   . ASP B 2 91  ? -7.349  -8.581  -36.005 1.00 113.71 ? 187  ASP D OD2   1 
ATOM   2745 N  N     . ASN B 2 92  ? -4.720  -3.909  -37.758 1.00 94.94  ? 188  ASN D N     1 
ATOM   2746 C  CA    . ASN B 2 92  ? -4.423  -2.935  -38.799 1.00 96.48  ? 188  ASN D CA    1 
ATOM   2747 C  C     . ASN B 2 92  ? -3.168  -2.122  -38.499 1.00 90.78  ? 188  ASN D C     1 
ATOM   2748 O  O     . ASN B 2 92  ? -3.027  -1.002  -39.001 1.00 90.05  ? 188  ASN D O     1 
ATOM   2749 C  CB    . ASN B 2 92  ? -5.618  -2.002  -39.006 1.00 90.41  ? 188  ASN D CB    1 
ATOM   2750 C  CG    . ASN B 2 92  ? -6.856  -2.738  -39.477 1.00 92.79  ? 188  ASN D CG    1 
ATOM   2751 O  OD1   . ASN B 2 92  ? -6.765  -3.788  -40.113 1.00 88.95  ? 188  ASN D OD1   1 
ATOM   2752 N  ND2   . ASN B 2 92  ? -8.024  -2.189  -39.166 1.00 97.90  ? 188  ASN D ND2   1 
ATOM   2753 N  N     . VAL B 2 93  ? -2.257  -2.661  -37.691 1.00 79.64  ? 189  VAL D N     1 
ATOM   2754 C  CA    . VAL B 2 93  ? -1.001  -1.998  -37.362 1.00 76.87  ? 189  VAL D CA    1 
ATOM   2755 C  C     . VAL B 2 93  ? 0.134   -2.971  -37.645 1.00 78.90  ? 189  VAL D C     1 
ATOM   2756 O  O     . VAL B 2 93  ? 0.199   -4.047  -37.039 1.00 78.10  ? 189  VAL D O     1 
ATOM   2757 C  CB    . VAL B 2 93  ? -0.956  -1.529  -35.898 1.00 86.21  ? 189  VAL D CB    1 
ATOM   2758 C  CG1   . VAL B 2 93  ? 0.432   -1.013  -35.552 1.00 71.84  ? 189  VAL D CG1   1 
ATOM   2759 C  CG2   . VAL B 2 93  ? -2.002  -0.454  -35.652 1.00 88.45  ? 189  VAL D CG2   1 
ATOM   2760 N  N     . ALA B 2 94  ? 1.023   -2.595  -38.560 1.00 82.60  ? 190  ALA D N     1 
ATOM   2761 C  CA    . ALA B 2 94  ? 2.190   -3.398  -38.907 1.00 85.00  ? 190  ALA D CA    1 
ATOM   2762 C  C     . ALA B 2 94  ? 3.386   -2.869  -38.123 1.00 85.11  ? 190  ALA D C     1 
ATOM   2763 O  O     . ALA B 2 94  ? 3.831   -1.739  -38.345 1.00 94.22  ? 190  ALA D O     1 
ATOM   2764 C  CB    . ALA B 2 94  ? 2.451   -3.357  -40.410 1.00 82.43  ? 190  ALA D CB    1 
ATOM   2765 N  N     . TYR B 2 95  ? 3.903   -3.685  -37.209 1.00 71.98  ? 191  TYR D N     1 
ATOM   2766 C  CA    . TYR B 2 95  ? 4.993   -3.296  -36.327 1.00 73.50  ? 191  TYR D CA    1 
ATOM   2767 C  C     . TYR B 2 95  ? 6.286   -3.981  -36.746 1.00 68.48  ? 191  TYR D C     1 
ATOM   2768 O  O     . TYR B 2 95  ? 6.278   -5.142  -37.168 1.00 72.45  ? 191  TYR D O     1 
ATOM   2769 C  CB    . TYR B 2 95  ? 4.666   -3.644  -34.871 1.00 74.08  ? 191  TYR D CB    1 
ATOM   2770 C  CG    . TYR B 2 95  ? 5.876   -3.727  -33.967 1.00 73.09  ? 191  TYR D CG    1 
ATOM   2771 C  CD1   . TYR B 2 95  ? 6.541   -2.579  -33.554 1.00 67.83  ? 191  TYR D CD1   1 
ATOM   2772 C  CD2   . TYR B 2 95  ? 6.350   -4.954  -33.521 1.00 83.38  ? 191  TYR D CD2   1 
ATOM   2773 C  CE1   . TYR B 2 95  ? 7.646   -2.653  -32.726 1.00 74.69  ? 191  TYR D CE1   1 
ATOM   2774 C  CE2   . TYR B 2 95  ? 7.454   -5.037  -32.693 1.00 74.14  ? 191  TYR D CE2   1 
ATOM   2775 C  CZ    . TYR B 2 95  ? 8.098   -3.884  -32.299 1.00 79.58  ? 191  TYR D CZ    1 
ATOM   2776 O  OH    . TYR B 2 95  ? 9.197   -3.964  -31.474 1.00 96.08  ? 191  TYR D OH    1 
ATOM   2777 N  N     . ALA B 2 96  ? 7.396   -3.254  -36.628 1.00 59.14  ? 192  ALA D N     1 
ATOM   2778 C  CA    . ALA B 2 96  ? 8.710   -3.813  -36.917 1.00 77.13  ? 192  ALA D CA    1 
ATOM   2779 C  C     . ALA B 2 96  ? 9.748   -3.148  -36.027 1.00 82.07  ? 192  ALA D C     1 
ATOM   2780 O  O     . ALA B 2 96  ? 9.759   -1.920  -35.894 1.00 85.74  ? 192  ALA D O     1 
ATOM   2781 C  CB    . ALA B 2 96  ? 9.082   -3.631  -38.391 1.00 75.12  ? 192  ALA D CB    1 
ATOM   2782 N  N     . ARG B 2 97  ? 10.618  -3.959  -35.432 1.00 73.34  ? 193  ARG D N     1 
ATOM   2783 C  CA    . ARG B 2 97  ? 11.697  -3.474  -34.583 1.00 87.75  ? 193  ARG D CA    1 
ATOM   2784 C  C     . ARG B 2 97  ? 12.994  -3.434  -35.381 1.00 71.80  ? 193  ARG D C     1 
ATOM   2785 O  O     . ARG B 2 97  ? 13.369  -4.427  -36.013 1.00 62.79  ? 193  ARG D O     1 
ATOM   2786 C  CB    . ARG B 2 97  ? 11.865  -4.362  -33.350 1.00 66.61  ? 193  ARG D CB    1 
ATOM   2787 C  CG    . ARG B 2 97  ? 13.103  -4.048  -32.525 1.00 72.12  ? 193  ARG D CG    1 
ATOM   2788 C  CD    . ARG B 2 97  ? 13.015  -2.668  -31.895 1.00 80.19  ? 193  ARG D CD    1 
ATOM   2789 N  NE    . ARG B 2 97  ? 14.297  -2.234  -31.352 1.00 94.16  ? 193  ARG D NE    1 
ATOM   2790 C  CZ    . ARG B 2 97  ? 14.742  -2.543  -30.142 1.00 95.37  ? 193  ARG D CZ    1 
ATOM   2791 N  NH1   . ARG B 2 97  ? 14.035  -3.296  -29.316 1.00 80.04  ? 193  ARG D NH1   1 
ATOM   2792 N  NH2   . ARG B 2 97  ? 15.928  -2.084  -29.750 1.00 101.21 ? 193  ARG D NH2   1 
ATOM   2793 N  N     . ALA B 2 98  ? 13.670  -2.290  -35.350 1.00 75.01  ? 194  ALA D N     1 
ATOM   2794 C  CA    . ALA B 2 98  ? 14.945  -2.111  -36.033 1.00 82.62  ? 194  ALA D CA    1 
ATOM   2795 C  C     . ALA B 2 98  ? 16.073  -2.133  -35.011 1.00 96.43  ? 194  ALA D C     1 
ATOM   2796 O  O     . ALA B 2 98  ? 15.986  -1.478  -33.968 1.00 102.38 ? 194  ALA D O     1 
ATOM   2797 C  CB    . ALA B 2 98  ? 14.965  -0.799  -36.819 1.00 78.04  ? 194  ALA D CB    1 
ATOM   2798 N  N     . PHE B 2 99  ? 17.130  -2.888  -35.314 1.00 93.41  ? 195  PHE D N     1 
ATOM   2799 C  CA    . PHE B 2 99  ? 18.259  -3.024  -34.404 1.00 80.28  ? 195  PHE D CA    1 
ATOM   2800 C  C     . PHE B 2 99  ? 19.476  -2.210  -34.820 1.00 83.55  ? 195  PHE D C     1 
ATOM   2801 O  O     . PHE B 2 99  ? 20.292  -1.865  -33.958 1.00 89.72  ? 195  PHE D O     1 
ATOM   2802 C  CB    . PHE B 2 99  ? 18.659  -4.499  -34.271 1.00 104.91 ? 195  PHE D CB    1 
ATOM   2803 C  CG    . PHE B 2 99  ? 17.602  -5.356  -33.634 1.00 107.69 ? 195  PHE D CG    1 
ATOM   2804 C  CD1   . PHE B 2 99  ? 17.503  -5.444  -32.255 1.00 92.14  ? 195  PHE D CD1   1 
ATOM   2805 C  CD2   . PHE B 2 99  ? 16.708  -6.072  -34.413 1.00 109.75 ? 195  PHE D CD2   1 
ATOM   2806 C  CE1   . PHE B 2 99  ? 16.532  -6.231  -31.664 1.00 86.66  ? 195  PHE D CE1   1 
ATOM   2807 C  CE2   . PHE B 2 99  ? 15.735  -6.861  -33.828 1.00 110.80 ? 195  PHE D CE2   1 
ATOM   2808 C  CZ    . PHE B 2 99  ? 15.647  -6.940  -32.452 1.00 85.47  ? 195  PHE D CZ    1 
ATOM   2809 N  N     . ASN B 2 100 ? 19.622  -1.899  -36.105 1.00 90.65  ? 196  ASN D N     1 
ATOM   2810 C  CA    . ASN B 2 100 ? 20.725  -1.070  -36.569 1.00 89.24  ? 196  ASN D CA    1 
ATOM   2811 C  C     . ASN B 2 100 ? 20.247  -0.230  -37.746 1.00 90.16  ? 196  ASN D C     1 
ATOM   2812 O  O     . ASN B 2 100 ? 19.124  -0.388  -38.234 1.00 87.27  ? 196  ASN D O     1 
ATOM   2813 C  CB    . ASN B 2 100 ? 21.949  -1.918  -36.941 1.00 89.46  ? 196  ASN D CB    1 
ATOM   2814 C  CG    . ASN B 2 100 ? 21.597  -3.109  -37.813 1.00 101.82 ? 196  ASN D CG    1 
ATOM   2815 O  OD1   . ASN B 2 100 ? 20.704  -3.037  -38.656 1.00 107.52 ? 196  ASN D OD1   1 
ATOM   2816 N  ND2   . ASN B 2 100 ? 22.301  -4.217  -37.610 1.00 122.09 ? 196  ASN D ND2   1 
ATOM   2817 N  N     . THR B 2 101 ? 21.120  0.674   -38.197 1.00 87.87  ? 197  THR D N     1 
ATOM   2818 C  CA    . THR B 2 101 ? 20.744  1.604   -39.257 1.00 84.69  ? 197  THR D CA    1 
ATOM   2819 C  C     . THR B 2 101 ? 20.432  0.872   -40.557 1.00 93.96  ? 197  THR D C     1 
ATOM   2820 O  O     . THR B 2 101 ? 19.526  1.270   -41.300 1.00 91.57  ? 197  THR D O     1 
ATOM   2821 C  CB    . THR B 2 101 ? 21.858  2.629   -39.476 1.00 92.60  ? 197  THR D CB    1 
ATOM   2822 O  OG1   . THR B 2 101 ? 23.077  1.952   -39.804 1.00 94.81  ? 197  THR D OG1   1 
ATOM   2823 C  CG2   . THR B 2 101 ? 22.069  3.460   -38.219 1.00 86.13  ? 197  THR D CG2   1 
ATOM   2824 N  N     . ASP B 2 102 ? 21.167  -0.205  -40.846 1.00 103.13 ? 198  ASP D N     1 
ATOM   2825 C  CA    . ASP B 2 102 ? 20.923  -0.957  -42.072 1.00 104.25 ? 198  ASP D CA    1 
ATOM   2826 C  C     . ASP B 2 102 ? 19.539  -1.595  -42.063 1.00 101.39 ? 198  ASP D C     1 
ATOM   2827 O  O     . ASP B 2 102 ? 18.822  -1.551  -43.068 1.00 102.48 ? 198  ASP D O     1 
ATOM   2828 C  CB    . ASP B 2 102 ? 22.006  -2.019  -42.263 1.00 118.65 ? 198  ASP D CB    1 
ATOM   2829 C  CG    . ASP B 2 102 ? 23.366  -1.418  -42.558 1.00 130.92 ? 198  ASP D CG    1 
ATOM   2830 O  OD1   . ASP B 2 102 ? 23.453  -0.179  -42.699 1.00 114.88 ? 198  ASP D OD1   1 
ATOM   2831 O  OD2   . ASP B 2 102 ? 24.349  -2.183  -42.649 1.00 155.01 ? 198  ASP D OD2   1 
ATOM   2832 N  N     . HIS B 2 103 ? 19.144  -2.188  -40.934 1.00 96.87  ? 199  HIS D N     1 
ATOM   2833 C  CA    . HIS B 2 103 ? 17.812  -2.777  -40.835 1.00 96.55  ? 199  HIS D CA    1 
ATOM   2834 C  C     . HIS B 2 103 ? 16.731  -1.706  -40.914 1.00 88.49  ? 199  HIS D C     1 
ATOM   2835 O  O     . HIS B 2 103 ? 15.694  -1.904  -41.561 1.00 69.57  ? 199  HIS D O     1 
ATOM   2836 C  CB    . HIS B 2 103 ? 17.693  -3.570  -39.533 1.00 96.17  ? 199  HIS D CB    1 
ATOM   2837 C  CG    . HIS B 2 103 ? 16.458  -4.410  -39.444 1.00 98.76  ? 199  HIS D CG    1 
ATOM   2838 N  ND1   . HIS B 2 103 ? 15.961  -4.875  -38.246 1.00 103.46 ? 199  HIS D ND1   1 
ATOM   2839 C  CD2   . HIS B 2 103 ? 15.625  -4.877  -40.404 1.00 117.26 ? 199  HIS D CD2   1 
ATOM   2840 C  CE1   . HIS B 2 103 ? 14.871  -5.587  -38.471 1.00 115.98 ? 199  HIS D CE1   1 
ATOM   2841 N  NE2   . HIS B 2 103 ? 14.646  -5.605  -39.772 1.00 124.03 ? 199  HIS D NE2   1 
ATOM   2842 N  N     . GLN B 2 104 ? 16.959  -0.565  -40.258 1.00 87.63  ? 200  GLN D N     1 
ATOM   2843 C  CA    . GLN B 2 104 ? 16.007  0.539   -40.314 1.00 82.47  ? 200  GLN D CA    1 
ATOM   2844 C  C     . GLN B 2 104 ? 15.820  1.034   -41.743 1.00 80.45  ? 200  GLN D C     1 
ATOM   2845 O  O     . GLN B 2 104 ? 14.709  1.406   -42.140 1.00 79.84  ? 200  GLN D O     1 
ATOM   2846 C  CB    . GLN B 2 104 ? 16.482  1.672   -39.402 1.00 81.82  ? 200  GLN D CB    1 
ATOM   2847 C  CG    . GLN B 2 104 ? 15.615  2.918   -39.412 1.00 65.84  ? 200  GLN D CG    1 
ATOM   2848 C  CD    . GLN B 2 104 ? 16.140  3.990   -38.475 1.00 84.05  ? 200  GLN D CD    1 
ATOM   2849 O  OE1   . GLN B 2 104 ? 16.936  3.711   -37.578 1.00 82.23  ? 200  GLN D OE1   1 
ATOM   2850 N  NE2   . GLN B 2 104 ? 15.700  5.226   -38.681 1.00 88.77  ? 200  GLN D NE2   1 
ATOM   2851 N  N     . THR B 2 105 ? 16.895  1.040   -42.534 1.00 97.32  ? 201  THR D N     1 
ATOM   2852 C  CA    . THR B 2 105 ? 16.778  1.441   -43.933 1.00 96.05  ? 201  THR D CA    1 
ATOM   2853 C  C     . THR B 2 105 ? 16.073  0.372   -44.759 1.00 91.51  ? 201  THR D C     1 
ATOM   2854 O  O     . THR B 2 105 ? 15.202  0.686   -45.580 1.00 98.88  ? 201  THR D O     1 
ATOM   2855 C  CB    . THR B 2 105 ? 18.163  1.739   -44.510 1.00 94.63  ? 201  THR D CB    1 
ATOM   2856 O  OG1   . THR B 2 105 ? 18.699  2.914   -43.889 1.00 104.57 ? 201  THR D OG1   1 
ATOM   2857 C  CG2   . THR B 2 105 ? 18.086  1.956   -46.015 1.00 105.53 ? 201  THR D CG2   1 
ATOM   2858 N  N     . GLN B 2 106 ? 16.427  -0.899  -44.551 1.00 81.85  ? 202  GLN D N     1 
ATOM   2859 C  CA    . GLN B 2 106 ? 15.852  -1.982  -45.340 1.00 80.35  ? 202  GLN D CA    1 
ATOM   2860 C  C     . GLN B 2 106 ? 14.371  -2.196  -45.055 1.00 90.62  ? 202  GLN D C     1 
ATOM   2861 O  O     . GLN B 2 106 ? 13.665  -2.737  -45.913 1.00 105.24 ? 202  GLN D O     1 
ATOM   2862 C  CB    . GLN B 2 106 ? 16.618  -3.282  -45.087 1.00 84.72  ? 202  GLN D CB    1 
ATOM   2863 C  CG    . GLN B 2 106 ? 18.062  -3.267  -45.565 1.00 114.39 ? 202  GLN D CG    1 
ATOM   2864 C  CD    . GLN B 2 106 ? 18.185  -3.324  -47.073 1.00 126.53 ? 202  GLN D CD    1 
ATOM   2865 O  OE1   . GLN B 2 106 ? 17.342  -3.908  -47.754 1.00 134.76 ? 202  GLN D OE1   1 
ATOM   2866 N  NE2   . GLN B 2 106 ? 19.240  -2.718  -47.605 1.00 121.91 ? 202  GLN D NE2   1 
ATOM   2867 N  N     . LEU B 2 107 ? 13.886  -1.797  -43.876 1.00 92.18  ? 203  LEU D N     1 
ATOM   2868 C  CA    . LEU B 2 107 ? 12.467  -1.976  -43.576 1.00 81.09  ? 203  LEU D CA    1 
ATOM   2869 C  C     . LEU B 2 107 ? 11.579  -1.145  -44.496 1.00 82.81  ? 203  LEU D C     1 
ATOM   2870 O  O     . LEU B 2 107 ? 10.455  -1.556  -44.810 1.00 88.00  ? 203  LEU D O     1 
ATOM   2871 C  CB    . LEU B 2 107 ? 12.187  -1.627  -42.113 1.00 96.17  ? 203  LEU D CB    1 
ATOM   2872 C  CG    . LEU B 2 107 ? 12.631  -2.649  -41.064 1.00 89.32  ? 203  LEU D CG    1 
ATOM   2873 C  CD1   . LEU B 2 107 ? 12.295  -2.162  -39.663 1.00 87.50  ? 203  LEU D CD1   1 
ATOM   2874 C  CD2   . LEU B 2 107 ? 12.000  -4.008  -41.329 1.00 82.72  ? 203  LEU D CD2   1 
ATOM   2875 N  N     . LEU B 2 108 ? 12.060  0.018   -44.945 1.00 89.72  ? 204  LEU D N     1 
ATOM   2876 C  CA    . LEU B 2 108 ? 11.244  0.864   -45.811 1.00 97.82  ? 204  LEU D CA    1 
ATOM   2877 C  C     . LEU B 2 108 ? 11.051  0.246   -47.191 1.00 88.53  ? 204  LEU D C     1 
ATOM   2878 O  O     . LEU B 2 108 ? 10.020  0.479   -47.835 1.00 85.91  ? 204  LEU D O     1 
ATOM   2879 C  CB    . LEU B 2 108 ? 11.870  2.253   -45.928 1.00 94.07  ? 204  LEU D CB    1 
ATOM   2880 C  CG    . LEU B 2 108 ? 11.938  3.063   -44.633 1.00 81.91  ? 204  LEU D CG    1 
ATOM   2881 C  CD1   . LEU B 2 108 ? 12.513  4.444   -44.897 1.00 96.54  ? 204  LEU D CD1   1 
ATOM   2882 C  CD2   . LEU B 2 108 ? 10.563  3.166   -43.990 1.00 78.38  ? 204  LEU D CD2   1 
ATOM   2883 N  N     . TYR B 2 109 ? 12.022  -0.541  -47.661 1.00 70.18  ? 205  TYR D N     1 
ATOM   2884 C  CA    . TYR B 2 109 ? 11.835  -1.284  -48.904 1.00 91.93  ? 205  TYR D CA    1 
ATOM   2885 C  C     . TYR B 2 109 ? 10.613  -2.189  -48.813 1.00 94.21  ? 205  TYR D C     1 
ATOM   2886 O  O     . TYR B 2 109 ? 9.757   -2.192  -49.705 1.00 99.09  ? 205  TYR D O     1 
ATOM   2887 C  CB    . TYR B 2 109 ? 13.081  -2.109  -49.220 1.00 102.27 ? 205  TYR D CB    1 
ATOM   2888 C  CG    . TYR B 2 109 ? 14.336  -1.305  -49.459 1.00 101.39 ? 205  TYR D CG    1 
ATOM   2889 C  CD1   . TYR B 2 109 ? 14.313  -0.151  -50.228 1.00 104.64 ? 205  TYR D CD1   1 
ATOM   2890 C  CD2   . TYR B 2 109 ? 15.550  -1.709  -48.921 1.00 106.35 ? 205  TYR D CD2   1 
ATOM   2891 C  CE1   . TYR B 2 109 ? 15.466  0.578   -50.451 1.00 113.54 ? 205  TYR D CE1   1 
ATOM   2892 C  CE2   . TYR B 2 109 ? 16.706  -0.988  -49.136 1.00 117.53 ? 205  TYR D CE2   1 
ATOM   2893 C  CZ    . TYR B 2 109 ? 16.660  0.153   -49.900 1.00 118.09 ? 205  TYR D CZ    1 
ATOM   2894 O  OH    . TYR B 2 109 ? 17.818  0.865   -50.110 1.00 106.48 ? 205  TYR D OH    1 
ATOM   2895 N  N     . GLN B 2 110 ? 10.523  -2.973  -47.735 1.00 99.24  ? 206  GLN D N     1 
ATOM   2896 C  CA    A GLN B 2 110 ? 9.356   -3.826  -47.537 0.44 96.48  ? 206  GLN D CA    1 
ATOM   2897 C  CA    B GLN B 2 110 ? 9.357   -3.827  -47.533 0.56 96.63  ? 206  GLN D CA    1 
ATOM   2898 C  C     . GLN B 2 110 ? 8.097   -2.992  -47.338 1.00 95.25  ? 206  GLN D C     1 
ATOM   2899 O  O     . GLN B 2 110 ? 7.012   -3.373  -47.798 1.00 97.25  ? 206  GLN D O     1 
ATOM   2900 C  CB    A GLN B 2 110 ? 9.585   -4.750  -46.341 0.44 91.86  ? 206  GLN D CB    1 
ATOM   2901 C  CB    B GLN B 2 110 ? 9.582   -4.741  -46.329 0.56 88.57  ? 206  GLN D CB    1 
ATOM   2902 C  CG    A GLN B 2 110 ? 8.423   -5.678  -46.038 0.44 96.16  ? 206  GLN D CG    1 
ATOM   2903 C  CG    B GLN B 2 110 ? 11.047  -5.004  -46.013 0.56 98.54  ? 206  GLN D CG    1 
ATOM   2904 C  CD    A GLN B 2 110 ? 8.148   -6.653  -47.164 0.44 97.89  ? 206  GLN D CD    1 
ATOM   2905 C  CD    B GLN B 2 110 ? 11.746  -5.814  -47.088 0.56 100.73 ? 206  GLN D CD    1 
ATOM   2906 O  OE1   A GLN B 2 110 ? 7.118   -6.571  -47.833 0.44 93.84  ? 206  GLN D OE1   1 
ATOM   2907 O  OE1   B GLN B 2 110 ? 12.802  -5.425  -47.587 0.56 101.06 ? 206  GLN D OE1   1 
ATOM   2908 N  NE2   A GLN B 2 110 ? 9.068   -7.587  -47.375 0.44 100.69 ? 206  GLN D NE2   1 
ATOM   2909 N  NE2   B GLN B 2 110 ? 11.161  -6.951  -47.445 0.56 92.91  ? 206  GLN D NE2   1 
ATOM   2910 N  N     . ALA B 2 111 ? 8.226   -1.850  -46.656 1.00 90.38  ? 207  ALA D N     1 
ATOM   2911 C  CA    . ALA B 2 111 ? 7.086   -0.965  -46.443 1.00 88.10  ? 207  ALA D CA    1 
ATOM   2912 C  C     . ALA B 2 111 ? 6.503   -0.468  -47.758 1.00 102.37 ? 207  ALA D C     1 
ATOM   2913 O  O     . ALA B 2 111 ? 5.288   -0.270  -47.861 1.00 102.11 ? 207  ALA D O     1 
ATOM   2914 C  CB    . ALA B 2 111 ? 7.504   0.218   -45.572 1.00 83.04  ? 207  ALA D CB    1 
ATOM   2915 N  N     . GLU B 2 112 ? 7.352   -0.248  -48.764 1.00 107.71 ? 208  GLU D N     1 
ATOM   2916 C  CA    . GLU B 2 112 ? 6.856   0.183   -50.069 1.00 100.13 ? 208  GLU D CA    1 
ATOM   2917 C  C     . GLU B 2 112 ? 5.883   -0.837  -50.651 1.00 95.64  ? 208  GLU D C     1 
ATOM   2918 O  O     . GLU B 2 112 ? 4.766   -0.490  -51.053 1.00 105.76 ? 208  GLU D O     1 
ATOM   2919 C  CB    . GLU B 2 112 ? 8.023   0.418   -51.029 1.00 99.42  ? 208  GLU D CB    1 
ATOM   2920 C  CG    . GLU B 2 112 ? 7.584   0.826   -52.427 1.00 98.10  ? 208  GLU D CG    1 
ATOM   2921 C  CD    . GLU B 2 112 ? 8.728   0.850   -53.422 1.00 117.65 ? 208  GLU D CD    1 
ATOM   2922 O  OE1   . GLU B 2 112 ? 9.892   0.693   -52.998 1.00 112.72 ? 208  GLU D OE1   1 
ATOM   2923 O  OE2   . GLU B 2 112 ? 8.460   1.023   -54.630 1.00 119.88 ? 208  GLU D OE2   1 
ATOM   2924 N  N     . ASP B 2 113 ? 6.289   -2.109  -50.695 1.00 88.60  ? 209  ASP D N     1 
ATOM   2925 C  CA    . ASP B 2 113 ? 5.408   -3.147  -51.222 1.00 95.48  ? 209  ASP D CA    1 
ATOM   2926 C  C     . ASP B 2 113 ? 4.181   -3.332  -50.337 1.00 88.61  ? 209  ASP D C     1 
ATOM   2927 O  O     . ASP B 2 113 ? 3.082   -3.607  -50.837 1.00 97.40  ? 209  ASP D O     1 
ATOM   2928 C  CB    . ASP B 2 113 ? 6.174   -4.463  -51.361 1.00 109.06 ? 209  ASP D CB    1 
ATOM   2929 C  CG    . ASP B 2 113 ? 7.413   -4.328  -52.226 1.00 119.46 ? 209  ASP D CG    1 
ATOM   2930 O  OD1   . ASP B 2 113 ? 8.396   -3.709  -51.767 1.00 105.95 ? 209  ASP D OD1   1 
ATOM   2931 O  OD2   . ASP B 2 113 ? 7.405   -4.841  -53.365 1.00 110.14 ? 209  ASP D OD2   1 
ATOM   2932 N  N     . MET B 2 114 ? 4.347   -3.182  -49.021 1.00 103.13 ? 210  MET D N     1 
ATOM   2933 C  CA    . MET B 2 114 ? 3.207   -3.315  -48.119 1.00 92.00  ? 210  MET D CA    1 
ATOM   2934 C  C     . MET B 2 114 ? 2.167   -2.231  -48.380 1.00 94.91  ? 210  MET D C     1 
ATOM   2935 O  O     . MET B 2 114 ? 0.959   -2.495  -48.338 1.00 91.21  ? 210  MET D O     1 
ATOM   2936 C  CB    . MET B 2 114 ? 3.683   -3.276  -46.667 1.00 86.14  ? 210  MET D CB    1 
ATOM   2937 C  CG    . MET B 2 114 ? 4.470   -4.507  -46.245 1.00 100.57 ? 210  MET D CG    1 
ATOM   2938 S  SD    . MET B 2 114 ? 5.345   -4.278  -44.686 1.00 84.54  ? 210  MET D SD    1 
ATOM   2939 C  CE    . MET B 2 114 ? 3.995   -3.807  -43.614 1.00 73.23  ? 210  MET D CE    1 
ATOM   2940 N  N     . MET B 2 115 ? 2.619   -1.005  -48.658 1.00 82.26  ? 211  MET D N     1 
ATOM   2941 C  CA    . MET B 2 115 ? 1.701   0.076   -48.998 1.00 84.02  ? 211  MET D CA    1 
ATOM   2942 C  C     . MET B 2 115 ? 1.140   -0.075  -50.406 1.00 104.04 ? 211  MET D C     1 
ATOM   2943 O  O     . MET B 2 115 ? 0.049   0.432   -50.691 1.00 106.53 ? 211  MET D O     1 
ATOM   2944 C  CB    . MET B 2 115 ? 2.400   1.429   -48.856 1.00 76.36  ? 211  MET D CB    1 
ATOM   2945 C  CG    . MET B 2 115 ? 2.823   1.764   -47.436 1.00 97.33  ? 211  MET D CG    1 
ATOM   2946 S  SD    . MET B 2 115 ? 3.606   3.380   -47.289 1.00 105.97 ? 211  MET D SD    1 
ATOM   2947 C  CE    . MET B 2 115 ? 4.061   3.375   -45.557 1.00 87.84  ? 211  MET D CE    1 
ATOM   2948 N  N     . VAL B 2 116 ? 1.873   -0.744  -51.298 1.00 101.80 ? 212  VAL D N     1 
ATOM   2949 C  CA    . VAL B 2 116 ? 1.322   -1.058  -52.613 1.00 94.88  ? 212  VAL D CA    1 
ATOM   2950 C  C     . VAL B 2 116 ? 0.155   -2.028  -52.480 1.00 95.55  ? 212  VAL D C     1 
ATOM   2951 O  O     . VAL B 2 116 ? -0.894  -1.850  -53.111 1.00 101.81 ? 212  VAL D O     1 
ATOM   2952 C  CB    . VAL B 2 116 ? 2.416   -1.619  -53.539 1.00 99.50  ? 212  VAL D CB    1 
ATOM   2953 C  CG1   . VAL B 2 116 ? 1.793   -2.211  -54.794 1.00 103.94 ? 212  VAL D CG1   1 
ATOM   2954 C  CG2   . VAL B 2 116 ? 3.404   -0.531  -53.908 1.00 90.52  ? 212  VAL D CG2   1 
ATOM   2955 N  N     . GLU B 2 117 ? 0.313   -3.061  -51.650 1.00 107.91 ? 213  GLU D N     1 
ATOM   2956 C  CA    . GLU B 2 117 ? -0.745  -4.056  -51.495 1.00 103.83 ? 213  GLU D CA    1 
ATOM   2957 C  C     . GLU B 2 117 ? -1.948  -3.478  -50.756 1.00 99.15  ? 213  GLU D C     1 
ATOM   2958 O  O     . GLU B 2 117 ? -3.056  -3.412  -51.301 1.00 101.72 ? 213  GLU D O     1 
ATOM   2959 C  CB    . GLU B 2 117 ? -0.206  -5.289  -50.769 1.00 109.93 ? 213  GLU D CB    1 
ATOM   2960 C  CG    . GLU B 2 117 ? 0.748   -6.132  -51.597 1.00 102.14 ? 213  GLU D CG    1 
ATOM   2961 C  CD    . GLU B 2 117 ? 1.091   -7.448  -50.927 1.00 137.41 ? 213  GLU D CD    1 
ATOM   2962 O  OE1   . GLU B 2 117 ? 0.594   -7.694  -49.808 1.00 129.08 ? 213  GLU D OE1   1 
ATOM   2963 O  OE2   . GLU B 2 117 ? 1.855   -8.238  -51.521 1.00 134.20 ? 213  GLU D OE2   1 
ATOM   2964 N  N     . SER B 2 118 ? -1.750  -3.057  -49.511 1.00 99.14  ? 214  SER D N     1 
ATOM   2965 C  CA    . SER B 2 118 ? -2.833  -2.581  -48.664 1.00 100.45 ? 214  SER D CA    1 
ATOM   2966 C  C     . SER B 2 118 ? -2.745  -1.072  -48.471 1.00 102.92 ? 214  SER D C     1 
ATOM   2967 O  O     . SER B 2 118 ? -1.696  -0.454  -48.670 1.00 98.69  ? 214  SER D O     1 
ATOM   2968 C  CB    . SER B 2 118 ? -2.810  -3.284  -47.302 1.00 98.09  ? 214  SER D CB    1 
ATOM   2969 O  OG    . SER B 2 118 ? -2.951  -4.686  -47.450 1.00 100.62 ? 214  SER D OG    1 
ATOM   2970 N  N     . ARG B 2 119 ? -3.872  -0.485  -48.073 1.00 96.28  ? 215  ARG D N     1 
ATOM   2971 C  CA    . ARG B 2 119 ? -3.955  0.952   -47.846 1.00 97.72  ? 215  ARG D CA    1 
ATOM   2972 C  C     . ARG B 2 119 ? -3.356  1.297   -46.488 1.00 101.98 ? 215  ARG D C     1 
ATOM   2973 O  O     . ARG B 2 119 ? -3.835  0.823   -45.452 1.00 100.83 ? 215  ARG D O     1 
ATOM   2974 C  CB    . ARG B 2 119 ? -5.408  1.420   -47.922 1.00 103.61 ? 215  ARG D CB    1 
ATOM   2975 C  CG    . ARG B 2 119 ? -5.649  2.807   -47.340 1.00 98.52  ? 215  ARG D CG    1 
ATOM   2976 C  CD    . ARG B 2 119 ? -5.222  3.910   -48.296 1.00 106.66 ? 215  ARG D CD    1 
ATOM   2977 N  NE    . ARG B 2 119 ? -5.139  5.206   -47.631 1.00 110.77 ? 215  ARG D NE    1 
ATOM   2978 C  CZ    . ARG B 2 119 ? -6.180  5.982   -47.361 1.00 112.88 ? 215  ARG D CZ    1 
ATOM   2979 N  NH1   . ARG B 2 119 ? -7.414  5.619   -47.672 1.00 103.26 ? 215  ARG D NH1   1 
ATOM   2980 N  NH2   . ARG B 2 119 ? -5.979  7.152   -46.760 1.00 102.51 ? 215  ARG D NH2   1 
ATOM   2981 N  N     . TYR B 2 120 ? -2.310  2.117   -46.493 1.00 99.79  ? 216  TYR D N     1 
ATOM   2982 C  CA    . TYR B 2 120 ? -1.718  2.647   -45.275 1.00 74.70  ? 216  TYR D CA    1 
ATOM   2983 C  C     . TYR B 2 120 ? -1.908  4.157   -45.228 1.00 80.27  ? 216  TYR D C     1 
ATOM   2984 O  O     . TYR B 2 120 ? -1.936  4.830   -46.262 1.00 102.17 ? 216  TYR D O     1 
ATOM   2985 C  CB    . TYR B 2 120 ? -0.227  2.304   -45.182 1.00 69.33  ? 216  TYR D CB    1 
ATOM   2986 C  CG    . TYR B 2 120 ? 0.052   0.896   -44.703 1.00 90.46  ? 216  TYR D CG    1 
ATOM   2987 C  CD1   . TYR B 2 120 ? 0.082   -0.170  -45.592 1.00 81.87  ? 216  TYR D CD1   1 
ATOM   2988 C  CD2   . TYR B 2 120 ? 0.290   0.635   -43.359 1.00 77.89  ? 216  TYR D CD2   1 
ATOM   2989 C  CE1   . TYR B 2 120 ? 0.337   -1.458  -45.157 1.00 93.31  ? 216  TYR D CE1   1 
ATOM   2990 C  CE2   . TYR B 2 120 ? 0.546   -0.650  -42.914 1.00 69.58  ? 216  TYR D CE2   1 
ATOM   2991 C  CZ    . TYR B 2 120 ? 0.568   -1.691  -43.817 1.00 82.10  ? 216  TYR D CZ    1 
ATOM   2992 O  OH    . TYR B 2 120 ? 0.822   -2.971  -43.380 1.00 73.91  ? 216  TYR D OH    1 
ATOM   2993 N  N     . ALA B 2 121 ? -2.049  4.683   -44.011 1.00 85.66  ? 217  ALA D N     1 
ATOM   2994 C  CA    . ALA B 2 121 ? -2.245  6.110   -43.805 1.00 83.26  ? 217  ALA D CA    1 
ATOM   2995 C  C     . ALA B 2 121 ? -1.203  6.753   -42.906 1.00 71.23  ? 217  ALA D C     1 
ATOM   2996 O  O     . ALA B 2 121 ? -1.096  7.985   -42.904 1.00 70.93  ? 217  ALA D O     1 
ATOM   2997 C  CB    . ALA B 2 121 ? -3.636  6.383   -43.211 1.00 76.66  ? 217  ALA D CB    1 
ATOM   2998 N  N     . LEU B 2 122 ? -0.433  5.969   -42.155 1.00 73.68  ? 218  LEU D N     1 
ATOM   2999 C  CA    . LEU B 2 122 ? 0.507   6.526   -41.193 1.00 75.05  ? 218  LEU D CA    1 
ATOM   3000 C  C     . LEU B 2 122 ? 1.727   5.624   -41.092 1.00 75.47  ? 218  LEU D C     1 
ATOM   3001 O  O     . LEU B 2 122 ? 1.593   4.414   -40.885 1.00 77.28  ? 218  LEU D O     1 
ATOM   3002 C  CB    . LEU B 2 122 ? -0.153  6.686   -39.820 1.00 71.76  ? 218  LEU D CB    1 
ATOM   3003 C  CG    . LEU B 2 122 ? 0.657   7.377   -38.723 1.00 83.11  ? 218  LEU D CG    1 
ATOM   3004 C  CD1   . LEU B 2 122 ? 0.826   8.857   -39.018 1.00 72.52  ? 218  LEU D CD1   1 
ATOM   3005 C  CD2   . LEU B 2 122 ? -0.019  7.174   -37.385 1.00 67.04  ? 218  LEU D CD2   1 
ATOM   3006 N  N     . LEU B 2 123 ? 2.909   6.219   -41.242 1.00 81.14  ? 219  LEU D N     1 
ATOM   3007 C  CA    . LEU B 2 123 ? 4.188   5.539   -41.064 1.00 82.62  ? 219  LEU D CA    1 
ATOM   3008 C  C     . LEU B 2 123 ? 4.915   6.213   -39.908 1.00 78.13  ? 219  LEU D C     1 
ATOM   3009 O  O     . LEU B 2 123 ? 5.300   7.384   -40.008 1.00 75.14  ? 219  LEU D O     1 
ATOM   3010 C  CB    . LEU B 2 123 ? 5.022   5.583   -42.343 1.00 72.79  ? 219  LEU D CB    1 
ATOM   3011 C  CG    . LEU B 2 123 ? 6.499   5.207   -42.203 1.00 67.96  ? 219  LEU D CG    1 
ATOM   3012 C  CD1   . LEU B 2 123 ? 6.656   3.800   -41.647 1.00 75.63  ? 219  LEU D CD1   1 
ATOM   3013 C  CD2   . LEU B 2 123 ? 7.214   5.339   -43.538 1.00 96.86  ? 219  LEU D CD2   1 
ATOM   3014 N  N     . ILE B 2 124 ? 5.108   5.473   -38.821 1.00 74.03  ? 220  ILE D N     1 
ATOM   3015 C  CA    . ILE B 2 124 ? 5.718   5.992   -37.603 1.00 72.79  ? 220  ILE D CA    1 
ATOM   3016 C  C     . ILE B 2 124 ? 7.132   5.440   -37.501 1.00 72.79  ? 220  ILE D C     1 
ATOM   3017 O  O     . ILE B 2 124 ? 7.334   4.219   -37.509 1.00 69.02  ? 220  ILE D O     1 
ATOM   3018 C  CB    . ILE B 2 124 ? 4.897   5.622   -36.360 1.00 62.94  ? 220  ILE D CB    1 
ATOM   3019 C  CG1   . ILE B 2 124 ? 3.488   6.205   -36.458 1.00 63.68  ? 220  ILE D CG1   1 
ATOM   3020 C  CG2   . ILE B 2 124 ? 5.595   6.103   -35.100 1.00 73.75  ? 220  ILE D CG2   1 
ATOM   3021 C  CD1   . ILE B 2 124 ? 2.597   5.809   -35.309 1.00 81.89  ? 220  ILE D CD1   1 
ATOM   3022 N  N     . VAL B 2 125 ? 8.109   6.339   -37.402 1.00 71.49  ? 221  VAL D N     1 
ATOM   3023 C  CA    . VAL B 2 125 ? 9.488   5.948   -37.142 1.00 76.02  ? 221  VAL D CA    1 
ATOM   3024 C  C     . VAL B 2 125 ? 9.876   6.466   -35.764 1.00 69.25  ? 221  VAL D C     1 
ATOM   3025 O  O     . VAL B 2 125 ? 10.351  7.600   -35.622 1.00 86.62  ? 221  VAL D O     1 
ATOM   3026 C  CB    . VAL B 2 125 ? 10.443  6.472   -38.228 1.00 68.05  ? 221  VAL D CB    1 
ATOM   3027 C  CG1   . VAL B 2 125 ? 11.790  5.781   -38.115 1.00 66.04  ? 221  VAL D CG1   1 
ATOM   3028 C  CG2   . VAL B 2 125 ? 9.845   6.257   -39.609 1.00 69.33  ? 221  VAL D CG2   1 
ATOM   3029 N  N     . ASP B 2 126 ? 9.660   5.642   -34.741 1.00 79.33  ? 222  ASP D N     1 
ATOM   3030 C  CA    . ASP B 2 126 ? 9.942   6.034   -33.365 1.00 84.63  ? 222  ASP D CA    1 
ATOM   3031 C  C     . ASP B 2 126 ? 11.449  6.064   -33.148 1.00 97.01  ? 222  ASP D C     1 
ATOM   3032 O  O     . ASP B 2 126 ? 12.111  5.021   -33.185 1.00 83.61  ? 222  ASP D O     1 
ATOM   3033 C  CB    . ASP B 2 126 ? 9.266   5.074   -32.392 1.00 76.88  ? 222  ASP D CB    1 
ATOM   3034 C  CG    . ASP B 2 126 ? 9.205   5.624   -30.980 1.00 97.63  ? 222  ASP D CG    1 
ATOM   3035 O  OD1   . ASP B 2 126 ? 9.600   6.793   -30.778 1.00 74.61  ? 222  ASP D OD1   1 
ATOM   3036 O  OD2   . ASP B 2 126 ? 8.760   4.890   -30.072 1.00 95.94  ? 222  ASP D OD2   1 
ATOM   3037 N  N     . SER B 2 127 ? 11.987  7.264   -32.923 1.00 108.24 ? 223  SER D N     1 
ATOM   3038 C  CA    . SER B 2 127 ? 13.419  7.498   -32.747 1.00 89.91  ? 223  SER D CA    1 
ATOM   3039 C  C     . SER B 2 127 ? 14.199  7.031   -33.980 1.00 90.41  ? 223  SER D C     1 
ATOM   3040 O  O     . SER B 2 127 ? 14.956  6.058   -33.957 1.00 105.05 ? 223  SER D O     1 
ATOM   3041 C  CB    . SER B 2 127 ? 13.932  6.828   -31.467 1.00 91.33  ? 223  SER D CB    1 
ATOM   3042 O  OG    . SER B 2 127 ? 13.394  7.459   -30.318 1.00 112.97 ? 223  SER D OG    1 
ATOM   3043 N  N     . ALA B 2 128 ? 13.979  7.766   -35.073 1.00 77.77  ? 224  ALA D N     1 
ATOM   3044 C  CA    . ALA B 2 128 ? 14.736  7.529   -36.296 1.00 79.47  ? 224  ALA D CA    1 
ATOM   3045 C  C     . ALA B 2 128 ? 16.213  7.844   -36.118 1.00 84.64  ? 224  ALA D C     1 
ATOM   3046 O  O     . ALA B 2 128 ? 17.040  7.357   -36.897 1.00 110.99 ? 224  ALA D O     1 
ATOM   3047 C  CB    . ALA B 2 128 ? 14.165  8.364   -37.442 1.00 85.88  ? 224  ALA D CB    1 
ATOM   3048 N  N     . THR B 2 129 ? 16.560  8.644   -35.112 1.00 77.86  ? 225  THR D N     1 
ATOM   3049 C  CA    . THR B 2 129 ? 17.937  9.037   -34.861 1.00 87.27  ? 225  THR D CA    1 
ATOM   3050 C  C     . THR B 2 129 ? 18.620  8.193   -33.794 1.00 96.57  ? 225  THR D C     1 
ATOM   3051 O  O     . THR B 2 129 ? 19.847  8.260   -33.674 1.00 103.59 ? 225  THR D O     1 
ATOM   3052 C  CB    . THR B 2 129 ? 17.995  10.512  -34.446 1.00 91.93  ? 225  THR D CB    1 
ATOM   3053 O  OG1   . THR B 2 129 ? 17.352  10.678  -33.177 1.00 102.89 ? 225  THR D OG1   1 
ATOM   3054 C  CG2   . THR B 2 129 ? 17.286  11.374  -35.473 1.00 88.29  ? 225  THR D CG2   1 
ATOM   3055 N  N     . ALA B 2 130 ? 17.864  7.404   -33.026 1.00 85.30  ? 226  ALA D N     1 
ATOM   3056 C  CA    . ALA B 2 130 ? 18.458  6.630   -31.938 1.00 64.54  ? 226  ALA D CA    1 
ATOM   3057 C  C     . ALA B 2 130 ? 19.541  5.692   -32.455 1.00 83.49  ? 226  ALA D C     1 
ATOM   3058 O  O     . ALA B 2 130 ? 20.625  5.591   -31.868 1.00 99.24  ? 226  ALA D O     1 
ATOM   3059 C  CB    . ALA B 2 130 ? 17.375  5.848   -31.196 1.00 83.04  ? 226  ALA D CB    1 
ATOM   3060 N  N     . LEU B 2 131 ? 19.270  4.999   -33.562 1.00 97.73  ? 227  LEU D N     1 
ATOM   3061 C  CA    . LEU B 2 131 ? 20.285  4.139   -34.155 1.00 82.68  ? 227  LEU D CA    1 
ATOM   3062 C  C     . LEU B 2 131 ? 21.366  4.942   -34.868 1.00 93.03  ? 227  LEU D C     1 
ATOM   3063 O  O     . LEU B 2 131 ? 22.470  4.426   -35.076 1.00 93.26  ? 227  LEU D O     1 
ATOM   3064 C  CB    . LEU B 2 131 ? 19.632  3.148   -35.119 1.00 83.85  ? 227  LEU D CB    1 
ATOM   3065 C  CG    . LEU B 2 131 ? 18.533  2.273   -34.504 1.00 71.89  ? 227  LEU D CG    1 
ATOM   3066 C  CD1   . LEU B 2 131 ? 17.971  1.282   -35.516 1.00 80.63  ? 227  LEU D CD1   1 
ATOM   3067 C  CD2   . LEU B 2 131 ? 19.045  1.547   -33.267 1.00 80.19  ? 227  LEU D CD2   1 
ATOM   3068 N  N     . TYR B 2 132 ? 21.075  6.188   -35.241 1.00 97.84  ? 228  TYR D N     1 
ATOM   3069 C  CA    . TYR B 2 132 ? 22.075  7.051   -35.858 1.00 103.31 ? 228  TYR D CA    1 
ATOM   3070 C  C     . TYR B 2 132 ? 22.829  7.893   -34.836 1.00 110.23 ? 228  TYR D C     1 
ATOM   3071 O  O     . TYR B 2 132 ? 23.993  8.241   -35.069 1.00 111.95 ? 228  TYR D O     1 
ATOM   3072 C  CB    . TYR B 2 132 ? 21.422  7.968   -36.896 1.00 101.59 ? 228  TYR D CB    1 
ATOM   3073 C  CG    . TYR B 2 132 ? 21.068  7.272   -38.195 1.00 103.74 ? 228  TYR D CG    1 
ATOM   3074 C  CD1   . TYR B 2 132 ? 22.027  7.074   -39.180 1.00 103.87 ? 228  TYR D CD1   1 
ATOM   3075 C  CD2   . TYR B 2 132 ? 19.776  6.819   -38.440 1.00 100.91 ? 228  TYR D CD2   1 
ATOM   3076 C  CE1   . TYR B 2 132 ? 21.715  6.440   -40.369 1.00 104.53 ? 228  TYR D CE1   1 
ATOM   3077 C  CE2   . TYR B 2 132 ? 19.453  6.182   -39.630 1.00 108.91 ? 228  TYR D CE2   1 
ATOM   3078 C  CZ    . TYR B 2 132 ? 20.427  5.997   -40.589 1.00 106.20 ? 228  TYR D CZ    1 
ATOM   3079 O  OH    . TYR B 2 132 ? 20.112  5.366   -41.770 1.00 89.42  ? 228  TYR D OH    1 
ATOM   3080 N  N     . ARG B 2 133 ? 22.203  8.226   -33.706 1.00 120.39 ? 229  ARG D N     1 
ATOM   3081 C  CA    . ARG B 2 133 ? 22.890  8.901   -32.613 1.00 123.91 ? 229  ARG D CA    1 
ATOM   3082 C  C     . ARG B 2 133 ? 23.809  7.976   -31.846 1.00 122.28 ? 229  ARG D C     1 
ATOM   3083 O  O     . ARG B 2 133 ? 24.263  8.338   -30.757 1.00 131.44 ? 229  ARG D O     1 
ATOM   3084 C  CB    . ARG B 2 133 ? 21.877  9.529   -31.655 1.00 121.76 ? 229  ARG D CB    1 
ATOM   3085 C  CG    . ARG B 2 133 ? 21.171  10.741  -32.237 1.00 124.79 ? 229  ARG D CG    1 
ATOM   3086 C  CD    . ARG B 2 133 ? 20.210  11.389  -31.246 1.00 117.96 ? 229  ARG D CD    1 
ATOM   3087 N  NE    . ARG B 2 133 ? 19.369  12.366  -31.926 1.00 136.05 ? 229  ARG D NE    1 
ATOM   3088 C  CZ    . ARG B 2 133 ? 19.712  13.626  -32.156 1.00 136.22 ? 229  ARG D CZ    1 
ATOM   3089 N  NH1   . ARG B 2 133 ? 20.857  14.125  -31.718 1.00 132.76 ? 229  ARG D NH1   1 
ATOM   3090 N  NH2   . ARG B 2 133 ? 18.885  14.405  -32.848 1.00 137.32 ? 229  ARG D NH2   1 
ATOM   3091 N  N     . THR B 2 134 ? 24.089  6.793   -32.384 1.00 121.30 ? 230  THR D N     1 
ATOM   3092 C  CA    . THR B 2 134 ? 25.053  5.887   -31.780 1.00 138.61 ? 230  THR D CA    1 
ATOM   3093 C  C     . THR B 2 134 ? 26.464  6.432   -31.959 1.00 147.65 ? 230  THR D C     1 
ATOM   3094 O  O     . THR B 2 134 ? 27.351  5.713   -32.429 1.00 152.44 ? 230  THR D O     1 
ATOM   3095 C  CB    . THR B 2 134 ? 24.948  4.486   -32.393 1.00 138.48 ? 230  THR D CB    1 
ATOM   3096 O  OG1   . THR B 2 134 ? 25.112  4.555   -33.818 1.00 146.47 ? 230  THR D OG1   1 
ATOM   3097 C  CG2   . THR B 2 134 ? 23.603  3.861   -32.064 1.00 125.65 ? 230  THR D CG2   1 
ATOM   3098 N  N     . ASP B 2 135 ? 26.676  7.703   -31.605 1.00 150.72 ? 231  ASP D N     1 
ATOM   3099 C  CA    . ASP B 2 135 ? 28.007  8.294   -31.700 1.00 154.24 ? 231  ASP D CA    1 
ATOM   3100 C  C     . ASP B 2 135 ? 29.012  7.506   -30.870 1.00 163.57 ? 231  ASP D C     1 
ATOM   3101 O  O     . ASP B 2 135 ? 30.106  7.176   -31.346 1.00 175.51 ? 231  ASP D O     1 
ATOM   3102 C  CB    . ASP B 2 135 ? 27.964  9.755   -31.250 1.00 153.42 ? 231  ASP D CB    1 
ATOM   3103 C  CG    . ASP B 2 135 ? 26.876  10.548  -31.946 1.00 152.91 ? 231  ASP D CG    1 
ATOM   3104 O  OD1   . ASP B 2 135 ? 26.441  10.130  -33.039 1.00 151.94 ? 231  ASP D OD1   1 
ATOM   3105 O  OD2   . ASP B 2 135 ? 26.454  11.590  -31.401 1.00 151.89 ? 231  ASP D OD2   1 
ATOM   3106 N  N     . TYR B 2 136 ? 28.649  7.190   -29.624 1.00 164.71 ? 232  TYR D N     1 
ATOM   3107 C  CA    . TYR B 2 136 ? 29.481  6.391   -28.731 1.00 156.95 ? 232  TYR D CA    1 
ATOM   3108 C  C     . TYR B 2 136 ? 30.890  6.965   -28.655 1.00 166.69 ? 232  TYR D C     1 
ATOM   3109 O  O     . TYR B 2 136 ? 31.146  7.912   -27.901 1.00 169.11 ? 232  TYR D O     1 
ATOM   3110 C  CB    . TYR B 2 136 ? 29.523  4.929   -29.193 1.00 144.70 ? 232  TYR D CB    1 
ATOM   3111 C  CG    . TYR B 2 136 ? 28.174  4.231   -29.253 1.00 139.06 ? 232  TYR D CG    1 
ATOM   3112 C  CD1   . TYR B 2 136 ? 27.049  4.780   -28.646 1.00 138.70 ? 232  TYR D CD1   1 
ATOM   3113 C  CD2   . TYR B 2 136 ? 28.030  3.015   -29.913 1.00 129.10 ? 232  TYR D CD2   1 
ATOM   3114 C  CE1   . TYR B 2 136 ? 25.820  4.144   -28.703 1.00 137.73 ? 232  TYR D CE1   1 
ATOM   3115 C  CE2   . TYR B 2 136 ? 26.807  2.370   -29.970 1.00 132.49 ? 232  TYR D CE2   1 
ATOM   3116 C  CZ    . TYR B 2 136 ? 25.706  2.938   -29.364 1.00 134.10 ? 232  TYR D CZ    1 
ATOM   3117 O  OH    . TYR B 2 136 ? 24.490  2.298   -29.419 1.00 116.31 ? 232  TYR D OH    1 
ATOM   3118 N  N     . SER B 2 137 ? 31.802  6.394   -29.441 1.00 173.96 ? 233  SER D N     1 
ATOM   3119 C  CA    . SER B 2 137 ? 33.143  6.934   -29.609 1.00 163.79 ? 233  SER D CA    1 
ATOM   3120 C  C     . SER B 2 137 ? 33.305  7.712   -30.910 1.00 164.25 ? 233  SER D C     1 
ATOM   3121 O  O     . SER B 2 137 ? 34.048  8.701   -30.939 1.00 165.28 ? 233  SER D O     1 
ATOM   3122 C  CB    . SER B 2 137 ? 34.180  5.805   -29.554 1.00 142.06 ? 233  SER D CB    1 
ATOM   3123 O  OG    . SER B 2 137 ? 34.110  5.099   -28.325 1.00 136.08 ? 233  SER D OG    1 
ATOM   3124 N  N     . GLY B 2 138 ? 32.618  7.298   -31.977 1.00 165.76 ? 234  GLY D N     1 
ATOM   3125 C  CA    . GLY B 2 138 ? 32.639  8.013   -33.239 1.00 160.23 ? 234  GLY D CA    1 
ATOM   3126 C  C     . GLY B 2 138 ? 31.749  9.235   -33.224 1.00 164.70 ? 234  GLY D C     1 
ATOM   3127 O  O     . GLY B 2 138 ? 30.715  9.272   -33.897 1.00 160.23 ? 234  GLY D O     1 
ATOM   3128 N  N     . ARG B 2 139 ? 32.144  10.244  -32.446 1.00 174.36 ? 235  ARG D N     1 
ATOM   3129 C  CA    . ARG B 2 139 ? 31.384  11.482  -32.308 1.00 171.12 ? 235  ARG D CA    1 
ATOM   3130 C  C     . ARG B 2 139 ? 31.719  12.500  -33.392 1.00 165.26 ? 235  ARG D C     1 
ATOM   3131 O  O     . ARG B 2 139 ? 31.541  13.709  -33.186 1.00 159.95 ? 235  ARG D O     1 
ATOM   3132 C  CB    . ARG B 2 139 ? 31.612  12.082  -30.921 1.00 165.11 ? 235  ARG D CB    1 
ATOM   3133 C  CG    . ARG B 2 139 ? 31.872  11.034  -29.856 1.00 161.96 ? 235  ARG D CG    1 
ATOM   3134 C  CD    . ARG B 2 139 ? 31.605  11.569  -28.460 1.00 160.53 ? 235  ARG D CD    1 
ATOM   3135 N  NE    . ARG B 2 139 ? 30.779  10.649  -27.687 1.00 161.08 ? 235  ARG D NE    1 
ATOM   3136 C  CZ    . ARG B 2 139 ? 29.453  10.652  -27.687 1.00 160.64 ? 235  ARG D CZ    1 
ATOM   3137 N  NH1   . ARG B 2 139 ? 28.764  11.538  -28.388 1.00 151.16 ? 235  ARG D NH1   1 
ATOM   3138 N  NH2   . ARG B 2 139 ? 28.801  9.742   -26.968 1.00 156.19 ? 235  ARG D NH2   1 
ATOM   3139 N  N     . GLY B 2 140 ? 32.196  12.046  -34.543 1.00 162.05 ? 236  GLY D N     1 
ATOM   3140 C  CA    . GLY B 2 140 ? 32.549  12.947  -35.616 1.00 157.97 ? 236  GLY D CA    1 
ATOM   3141 C  C     . GLY B 2 140 ? 32.589  12.234  -36.950 1.00 153.52 ? 236  GLY D C     1 
ATOM   3142 O  O     . GLY B 2 140 ? 33.222  12.721  -37.889 1.00 161.34 ? 236  GLY D O     1 
ATOM   3143 N  N     . GLU B 2 141 ? 31.929  11.072  -37.043 1.00 152.69 ? 237  GLU D N     1 
ATOM   3144 C  CA    . GLU B 2 141 ? 31.864  10.347  -38.311 1.00 162.36 ? 237  GLU D CA    1 
ATOM   3145 C  C     . GLU B 2 141 ? 31.210  11.193  -39.398 1.00 158.77 ? 237  GLU D C     1 
ATOM   3146 O  O     . GLU B 2 141 ? 31.615  11.142  -40.565 1.00 146.65 ? 237  GLU D O     1 
ATOM   3147 C  CB    . GLU B 2 141 ? 31.112  9.028   -38.123 1.00 155.64 ? 237  GLU D CB    1 
ATOM   3148 C  CG    . GLU B 2 141 ? 31.736  8.109   -37.081 1.00 157.82 ? 237  GLU D CG    1 
ATOM   3149 C  CD    . GLU B 2 141 ? 30.968  6.816   -36.904 1.00 161.19 ? 237  GLU D CD    1 
ATOM   3150 O  OE1   . GLU B 2 141 ? 30.062  6.551   -37.718 1.00 160.70 ? 237  GLU D OE1   1 
ATOM   3151 O  OE2   . GLU B 2 141 ? 31.267  6.065   -35.950 1.00 152.71 ? 237  GLU D OE2   1 
ATOM   3152 N  N     . LEU B 2 142 ? 30.189  11.969  -39.029 1.00 150.30 ? 238  LEU D N     1 
ATOM   3153 C  CA    . LEU B 2 142 ? 29.622  13.011  -39.880 1.00 147.45 ? 238  LEU D CA    1 
ATOM   3154 C  C     . LEU B 2 142 ? 29.166  12.486  -41.236 1.00 147.34 ? 238  LEU D C     1 
ATOM   3155 O  O     . LEU B 2 142 ? 28.117  11.842  -41.338 1.00 143.38 ? 238  LEU D O     1 
ATOM   3156 C  CB    . LEU B 2 142 ? 30.637  14.143  -40.067 1.00 151.11 ? 238  LEU D CB    1 
ATOM   3157 C  CG    . LEU B 2 142 ? 30.548  15.349  -39.126 1.00 146.21 ? 238  LEU D CG    1 
ATOM   3158 C  CD1   . LEU B 2 142 ? 30.311  14.925  -37.684 1.00 138.20 ? 238  LEU D CD1   1 
ATOM   3159 C  CD2   . LEU B 2 142 ? 31.811  16.193  -39.231 1.00 121.91 ? 238  LEU D CD2   1 
ATOM   3160 N  N     . SER B 2 143 ? 29.959  12.753  -42.278 1.00 145.20 ? 239  SER D N     1 
ATOM   3161 C  CA    . SER B 2 143 ? 29.534  12.456  -43.643 1.00 139.44 ? 239  SER D CA    1 
ATOM   3162 C  C     . SER B 2 143 ? 29.327  10.964  -43.870 1.00 131.09 ? 239  SER D C     1 
ATOM   3163 O  O     . SER B 2 143 ? 28.567  10.576  -44.764 1.00 125.59 ? 239  SER D O     1 
ATOM   3164 C  CB    . SER B 2 143 ? 30.556  13.005  -44.639 1.00 130.77 ? 239  SER D CB    1 
ATOM   3165 O  OG    . SER B 2 143 ? 30.688  14.411  -44.512 1.00 127.92 ? 239  SER D OG    1 
ATOM   3166 N  N     . ALA B 2 144 ? 29.991  10.115  -43.083 1.00 128.11 ? 240  ALA D N     1 
ATOM   3167 C  CA    . ALA B 2 144 ? 29.790  8.676   -43.217 1.00 125.40 ? 240  ALA D CA    1 
ATOM   3168 C  C     . ALA B 2 144 ? 28.357  8.292   -42.870 1.00 124.24 ? 240  ALA D C     1 
ATOM   3169 O  O     . ALA B 2 144 ? 27.717  7.515   -43.588 1.00 115.67 ? 240  ALA D O     1 
ATOM   3170 C  CB    . ALA B 2 144 ? 30.784  7.922   -42.333 1.00 130.98 ? 240  ALA D CB    1 
ATOM   3171 N  N     . ARG B 2 145 ? 27.835  8.834   -41.771 1.00 129.77 ? 241  ARG D N     1 
ATOM   3172 C  CA    . ARG B 2 145 ? 26.454  8.589   -41.381 1.00 114.21 ? 241  ARG D CA    1 
ATOM   3173 C  C     . ARG B 2 145 ? 25.486  9.624   -41.934 1.00 107.53 ? 241  ARG D C     1 
ATOM   3174 O  O     . ARG B 2 145 ? 24.277  9.366   -41.962 1.00 107.36 ? 241  ARG D O     1 
ATOM   3175 C  CB    . ARG B 2 145 ? 26.334  8.549   -39.855 1.00 113.84 ? 241  ARG D CB    1 
ATOM   3176 C  CG    . ARG B 2 145 ? 27.038  7.369   -39.214 1.00 119.34 ? 241  ARG D CG    1 
ATOM   3177 C  CD    . ARG B 2 145 ? 26.788  7.334   -37.720 1.00 122.43 ? 241  ARG D CD    1 
ATOM   3178 N  NE    . ARG B 2 145 ? 27.296  6.113   -37.109 1.00 135.34 ? 241  ARG D NE    1 
ATOM   3179 C  CZ    . ARG B 2 145 ? 27.152  5.806   -35.828 1.00 134.41 ? 241  ARG D CZ    1 
ATOM   3180 N  NH1   . ARG B 2 145 ? 26.522  6.615   -34.992 1.00 136.74 ? 241  ARG D NH1   1 
ATOM   3181 N  NH2   . ARG B 2 145 ? 27.652  4.660   -35.374 1.00 136.12 ? 241  ARG D NH2   1 
ATOM   3182 N  N     . GLN B 2 146 ? 25.985  10.784  -42.369 1.00 113.99 ? 242  GLN D N     1 
ATOM   3183 C  CA    . GLN B 2 146 ? 25.105  11.792  -42.950 1.00 116.95 ? 242  GLN D CA    1 
ATOM   3184 C  C     . GLN B 2 146 ? 24.523  11.325  -44.278 1.00 118.72 ? 242  GLN D C     1 
ATOM   3185 O  O     . GLN B 2 146 ? 23.406  11.715  -44.635 1.00 113.77 ? 242  GLN D O     1 
ATOM   3186 C  CB    . GLN B 2 146 ? 25.862  13.107  -43.139 1.00 122.40 ? 242  GLN D CB    1 
ATOM   3187 C  CG    . GLN B 2 146 ? 25.011  14.356  -42.963 1.00 115.38 ? 242  GLN D CG    1 
ATOM   3188 C  CD    . GLN B 2 146 ? 24.765  14.694  -41.504 1.00 130.21 ? 242  GLN D CD    1 
ATOM   3189 O  OE1   . GLN B 2 146 ? 25.352  14.088  -40.607 1.00 128.26 ? 242  GLN D OE1   1 
ATOM   3190 N  NE2   . GLN B 2 146 ? 23.896  15.668  -41.261 1.00 130.90 ? 242  GLN D NE2   1 
ATOM   3191 N  N     . MET B 2 147 ? 25.260  10.492  -45.018 1.00 109.42 ? 243  MET D N     1 
ATOM   3192 C  CA    . MET B 2 147 ? 24.759  9.994   -46.294 1.00 119.98 ? 243  MET D CA    1 
ATOM   3193 C  C     . MET B 2 147 ? 23.692  8.924   -46.103 1.00 119.74 ? 243  MET D C     1 
ATOM   3194 O  O     . MET B 2 147 ? 22.769  8.821   -46.918 1.00 122.00 ? 243  MET D O     1 
ATOM   3195 C  CB    . MET B 2 147 ? 25.913  9.447   -47.133 1.00 138.15 ? 243  MET D CB    1 
ATOM   3196 C  CG    . MET B 2 147 ? 26.886  10.508  -47.618 1.00 140.00 ? 243  MET D CG    1 
ATOM   3197 S  SD    . MET B 2 147 ? 26.124  11.661  -48.775 1.00 133.33 ? 243  MET D SD    1 
ATOM   3198 C  CE    . MET B 2 147 ? 25.635  10.545  -50.088 1.00 133.09 ? 243  MET D CE    1 
ATOM   3199 N  N     . HIS B 2 148 ? 23.800  8.121   -45.042 1.00 104.80 ? 244  HIS D N     1 
ATOM   3200 C  CA    . HIS B 2 148 ? 22.811  7.076   -44.802 1.00 104.51 ? 244  HIS D CA    1 
ATOM   3201 C  C     . HIS B 2 148 ? 21.491  7.673   -44.327 1.00 99.29  ? 244  HIS D C     1 
ATOM   3202 O  O     . HIS B 2 148 ? 20.415  7.302   -44.815 1.00 102.91 ? 244  HIS D O     1 
ATOM   3203 C  CB    . HIS B 2 148 ? 23.353  6.071   -43.785 1.00 97.22  ? 244  HIS D CB    1 
ATOM   3204 C  CG    . HIS B 2 148 ? 22.641  4.754   -43.796 1.00 98.54  ? 244  HIS D CG    1 
ATOM   3205 N  ND1   . HIS B 2 148 ? 23.039  3.687   -43.019 1.00 87.72  ? 244  HIS D ND1   1 
ATOM   3206 C  CD2   . HIS B 2 148 ? 21.560  4.329   -44.492 1.00 118.31 ? 244  HIS D CD2   1 
ATOM   3207 C  CE1   . HIS B 2 148 ? 22.233  2.664   -43.233 1.00 98.38  ? 244  HIS D CE1   1 
ATOM   3208 N  NE2   . HIS B 2 148 ? 21.327  3.027   -44.123 1.00 119.12 ? 244  HIS D NE2   1 
ATOM   3209 N  N     . LEU B 2 149 ? 21.557  8.604   -43.371 1.00 93.47  ? 245  LEU D N     1 
ATOM   3210 C  CA    . LEU B 2 149 ? 20.353  9.295   -42.924 1.00 94.15  ? 245  LEU D CA    1 
ATOM   3211 C  C     . LEU B 2 149 ? 19.714  10.085  -44.058 1.00 92.10  ? 245  LEU D C     1 
ATOM   3212 O  O     . LEU B 2 149 ? 18.485  10.201  -44.119 1.00 85.10  ? 245  LEU D O     1 
ATOM   3213 C  CB    . LEU B 2 149 ? 20.686  10.217  -41.751 1.00 89.07  ? 245  LEU D CB    1 
ATOM   3214 C  CG    . LEU B 2 149 ? 19.522  10.972  -41.105 1.00 92.33  ? 245  LEU D CG    1 
ATOM   3215 C  CD1   . LEU B 2 149 ? 18.513  10.000  -40.512 1.00 97.36  ? 245  LEU D CD1   1 
ATOM   3216 C  CD2   . LEU B 2 149 ? 20.029  11.939  -40.046 1.00 86.47  ? 245  LEU D CD2   1 
ATOM   3217 N  N     . ALA B 2 150 ? 20.530  10.627  -44.966 1.00 96.52  ? 246  ALA D N     1 
ATOM   3218 C  CA    . ALA B 2 150 ? 19.983  11.329  -46.121 1.00 78.23  ? 246  ALA D CA    1 
ATOM   3219 C  C     . ALA B 2 150 ? 19.152  10.395  -46.989 1.00 81.57  ? 246  ALA D C     1 
ATOM   3220 O  O     . ALA B 2 150 ? 18.049  10.750  -47.416 1.00 78.17  ? 246  ALA D O     1 
ATOM   3221 C  CB    . ALA B 2 150 ? 21.110  11.961  -46.937 1.00 87.38  ? 246  ALA D CB    1 
ATOM   3222 N  N     . ARG B 2 151 ? 19.659  9.187   -47.251 1.00 71.95  ? 247  ARG D N     1 
ATOM   3223 C  CA    . ARG B 2 151 ? 18.906  8.233   -48.057 1.00 86.37  ? 247  ARG D CA    1 
ATOM   3224 C  C     . ARG B 2 151 ? 17.659  7.754   -47.320 1.00 103.96 ? 247  ARG D C     1 
ATOM   3225 O  O     . ARG B 2 151 ? 16.610  7.532   -47.938 1.00 109.99 ? 247  ARG D O     1 
ATOM   3226 C  CB    . ARG B 2 151 ? 19.802  7.055   -48.443 1.00 88.06  ? 247  ARG D CB    1 
ATOM   3227 C  CG    . ARG B 2 151 ? 19.220  6.181   -49.537 1.00 126.01 ? 247  ARG D CG    1 
ATOM   3228 C  CD    . ARG B 2 151 ? 20.209  5.138   -50.044 1.00 139.78 ? 247  ARG D CD    1 
ATOM   3229 N  NE    . ARG B 2 151 ? 20.645  4.210   -49.007 1.00 131.80 ? 247  ARG D NE    1 
ATOM   3230 C  CZ    . ARG B 2 151 ? 21.855  4.209   -48.465 1.00 137.11 ? 247  ARG D CZ    1 
ATOM   3231 N  NH1   . ARG B 2 151 ? 22.780  5.078   -48.837 1.00 134.70 ? 247  ARG D NH1   1 
ATOM   3232 N  NH2   . ARG B 2 151 ? 22.147  3.309   -47.530 1.00 113.94 ? 247  ARG D NH2   1 
ATOM   3233 N  N     . PHE B 2 152 ? 17.752  7.605   -45.996 1.00 97.28  ? 248  PHE D N     1 
ATOM   3234 C  CA    . PHE B 2 152 ? 16.584  7.235   -45.200 1.00 82.97  ? 248  PHE D CA    1 
ATOM   3235 C  C     . PHE B 2 152 ? 15.482  8.285   -45.323 1.00 87.76  ? 248  PHE D C     1 
ATOM   3236 O  O     . PHE B 2 152 ? 14.315  7.958   -45.581 1.00 83.87  ? 248  PHE D O     1 
ATOM   3237 C  CB    . PHE B 2 152 ? 17.004  7.043   -43.741 1.00 98.00  ? 248  PHE D CB    1 
ATOM   3238 C  CG    . PHE B 2 152 ? 15.874  6.693   -42.818 1.00 83.82  ? 248  PHE D CG    1 
ATOM   3239 C  CD1   . PHE B 2 152 ? 15.325  5.421   -42.821 1.00 83.56  ? 248  PHE D CD1   1 
ATOM   3240 C  CD2   . PHE B 2 152 ? 15.376  7.629   -41.928 1.00 68.24  ? 248  PHE D CD2   1 
ATOM   3241 C  CE1   . PHE B 2 152 ? 14.291  5.096   -41.965 1.00 76.62  ? 248  PHE D CE1   1 
ATOM   3242 C  CE2   . PHE B 2 152 ? 14.343  7.309   -41.068 1.00 79.54  ? 248  PHE D CE2   1 
ATOM   3243 C  CZ    . PHE B 2 152 ? 13.798  6.042   -41.089 1.00 82.28  ? 248  PHE D CZ    1 
ATOM   3244 N  N     . LEU B 2 153 ? 15.842  9.559   -45.152 1.00 78.96  ? 249  LEU D N     1 
ATOM   3245 C  CA    . LEU B 2 153 ? 14.862  10.632  -45.295 1.00 83.47  ? 249  LEU D CA    1 
ATOM   3246 C  C     . LEU B 2 153 ? 14.349  10.740  -46.725 1.00 87.36  ? 249  LEU D C     1 
ATOM   3247 O  O     . LEU B 2 153 ? 13.179  11.082  -46.938 1.00 96.71  ? 249  LEU D O     1 
ATOM   3248 C  CB    . LEU B 2 153 ? 15.468  11.960  -44.843 1.00 83.41  ? 249  LEU D CB    1 
ATOM   3249 C  CG    . LEU B 2 153 ? 15.909  12.025  -43.379 1.00 93.00  ? 249  LEU D CG    1 
ATOM   3250 C  CD1   . LEU B 2 153 ? 16.472  13.396  -43.047 1.00 95.03  ? 249  LEU D CD1   1 
ATOM   3251 C  CD2   . LEU B 2 153 ? 14.754  11.673  -42.454 1.00 86.07  ? 249  LEU D CD2   1 
ATOM   3252 N  N     . ARG B 2 154 ? 15.199  10.451  -47.714 1.00 83.17  ? 250  ARG D N     1 
ATOM   3253 C  CA    . ARG B 2 154 ? 14.747  10.451  -49.101 1.00 97.84  ? 250  ARG D CA    1 
ATOM   3254 C  C     . ARG B 2 154 ? 13.684  9.386   -49.332 1.00 90.04  ? 250  ARG D C     1 
ATOM   3255 O  O     . ARG B 2 154 ? 12.682  9.637   -50.009 1.00 98.91  ? 250  ARG D O     1 
ATOM   3256 C  CB    . ARG B 2 154 ? 15.936  10.241  -50.039 1.00 105.59 ? 250  ARG D CB    1 
ATOM   3257 C  CG    . ARG B 2 154 ? 16.705  11.513  -50.356 1.00 108.26 ? 250  ARG D CG    1 
ATOM   3258 C  CD    . ARG B 2 154 ? 18.165  11.211  -50.648 1.00 104.48 ? 250  ARG D CD    1 
ATOM   3259 N  NE    . ARG B 2 154 ? 18.321  10.070  -51.542 1.00 102.24 ? 250  ARG D NE    1 
ATOM   3260 C  CZ    . ARG B 2 154 ? 19.477  9.472   -51.794 1.00 116.91 ? 250  ARG D CZ    1 
ATOM   3261 N  NH1   . ARG B 2 154 ? 20.603  9.880   -51.232 1.00 93.38  ? 250  ARG D NH1   1 
ATOM   3262 N  NH2   . ARG B 2 154 ? 19.503  8.435   -52.627 1.00 113.18 ? 250  ARG D NH2   1 
ATOM   3263 N  N     . MET B 2 155 ? 13.882  8.190   -48.773 1.00 91.71  ? 251  MET D N     1 
ATOM   3264 C  CA    A MET B 2 155 ? 12.868  7.148   -48.904 0.46 94.77  ? 251  MET D CA    1 
ATOM   3265 C  CA    B MET B 2 155 ? 12.871  7.145   -48.902 0.54 94.70  ? 251  MET D CA    1 
ATOM   3266 C  C     . MET B 2 155 ? 11.593  7.521   -48.161 1.00 91.28  ? 251  MET D C     1 
ATOM   3267 O  O     . MET B 2 155 ? 10.486  7.240   -48.638 1.00 89.14  ? 251  MET D O     1 
ATOM   3268 C  CB    A MET B 2 155 ? 13.413  5.817   -48.396 0.46 95.64  ? 251  MET D CB    1 
ATOM   3269 C  CB    B MET B 2 155 ? 13.421  5.815   -48.389 0.54 95.11  ? 251  MET D CB    1 
ATOM   3270 C  CG    A MET B 2 155 ? 14.583  5.304   -49.196 0.46 99.16  ? 251  MET D CG    1 
ATOM   3271 C  CG    B MET B 2 155 ? 12.455  4.647   -48.521 0.54 96.11  ? 251  MET D CG    1 
ATOM   3272 S  SD    A MET B 2 155 ? 15.246  3.773   -48.533 0.46 118.82 ? 251  MET D SD    1 
ATOM   3273 S  SD    B MET B 2 155 ? 12.026  4.259   -50.228 0.54 118.82 ? 251  MET D SD    1 
ATOM   3274 C  CE    A MET B 2 155 ? 16.775  3.693   -49.448 0.46 109.82 ? 251  MET D CE    1 
ATOM   3275 C  CE    B MET B 2 155 ? 13.623  3.775   -50.877 0.54 108.31 ? 251  MET D CE    1 
ATOM   3276 N  N     . LEU B 2 156 ? 11.725  8.148   -46.990 1.00 90.09  ? 252  LEU D N     1 
ATOM   3277 C  CA    . LEU B 2 156 ? 10.541  8.604   -46.266 1.00 91.96  ? 252  LEU D CA    1 
ATOM   3278 C  C     . LEU B 2 156 ? 9.738   9.588   -47.109 1.00 92.15  ? 252  LEU D C     1 
ATOM   3279 O  O     . LEU B 2 156 ? 8.512   9.466   -47.233 1.00 99.08  ? 252  LEU D O     1 
ATOM   3280 C  CB    . LEU B 2 156 ? 10.945  9.240   -44.936 1.00 93.12  ? 252  LEU D CB    1 
ATOM   3281 C  CG    . LEU B 2 156 ? 11.479  8.311   -43.847 1.00 75.39  ? 252  LEU D CG    1 
ATOM   3282 C  CD1   . LEU B 2 156 ? 11.814  9.117   -42.610 1.00 74.62  ? 252  LEU D CD1   1 
ATOM   3283 C  CD2   . LEU B 2 156 ? 10.469  7.223   -43.522 1.00 64.59  ? 252  LEU D CD2   1 
ATOM   3284 N  N     . LEU B 2 157 ? 10.421  10.572  -47.701 1.00 90.15  ? 253  LEU D N     1 
ATOM   3285 C  CA    . LEU B 2 157 ? 9.747   11.538  -48.563 1.00 87.00  ? 253  LEU D CA    1 
ATOM   3286 C  C     . LEU B 2 157 ? 9.129   10.860  -49.779 1.00 81.89  ? 253  LEU D C     1 
ATOM   3287 O  O     . LEU B 2 157 ? 8.016   11.206  -50.190 1.00 83.86  ? 253  LEU D O     1 
ATOM   3288 C  CB    . LEU B 2 157 ? 10.728  12.627  -48.998 1.00 87.94  ? 253  LEU D CB    1 
ATOM   3289 C  CG    . LEU B 2 157 ? 11.132  13.657  -47.942 1.00 83.28  ? 253  LEU D CG    1 
ATOM   3290 C  CD1   . LEU B 2 157 ? 12.297  14.497  -48.436 1.00 87.42  ? 253  LEU D CD1   1 
ATOM   3291 C  CD2   . LEU B 2 157 ? 9.948   14.541  -47.589 1.00 95.42  ? 253  LEU D CD2   1 
ATOM   3292 N  N     . ARG B 2 158 ? 9.834   9.888   -50.365 1.00 91.69  ? 254  ARG D N     1 
ATOM   3293 C  CA    A ARG B 2 158 ? 9.302   9.186   -51.528 0.40 89.73  ? 254  ARG D CA    1 
ATOM   3294 C  CA    B ARG B 2 158 ? 9.306   9.180   -51.526 0.60 87.85  ? 254  ARG D CA    1 
ATOM   3295 C  C     . ARG B 2 158 ? 8.008   8.459   -51.185 1.00 94.98  ? 254  ARG D C     1 
ATOM   3296 O  O     . ARG B 2 158 ? 7.021   8.547   -51.923 1.00 85.00  ? 254  ARG D O     1 
ATOM   3297 C  CB    A ARG B 2 158 ? 10.337  8.204   -52.077 0.40 92.10  ? 254  ARG D CB    1 
ATOM   3298 C  CB    B ARG B 2 158 ? 10.345  8.189   -52.049 0.60 86.97  ? 254  ARG D CB    1 
ATOM   3299 C  CG    A ARG B 2 158 ? 9.827   7.392   -53.259 0.40 95.50  ? 254  ARG D CG    1 
ATOM   3300 C  CG    B ARG B 2 158 ? 9.841   7.288   -53.162 0.60 95.58  ? 254  ARG D CG    1 
ATOM   3301 C  CD    A ARG B 2 158 ? 10.917  6.537   -53.885 0.40 95.00  ? 254  ARG D CD    1 
ATOM   3302 C  CD    B ARG B 2 158 ? 10.483  5.916   -53.074 0.60 94.98  ? 254  ARG D CD    1 
ATOM   3303 N  NE    A ARG B 2 158 ? 11.254  5.376   -53.070 0.40 93.51  ? 254  ARG D NE    1 
ATOM   3304 N  NE    B ARG B 2 158 ? 11.913  6.009   -52.808 0.60 92.96  ? 254  ARG D NE    1 
ATOM   3305 C  CZ    A ARG B 2 158 ? 10.606  4.219   -53.111 0.40 94.69  ? 254  ARG D CZ    1 
ATOM   3306 C  CZ    B ARG B 2 158 ? 12.851  6.028   -53.745 0.60 99.23  ? 254  ARG D CZ    1 
ATOM   3307 N  NH1   A ARG B 2 158 ? 9.555   4.043   -53.895 0.40 92.82  ? 254  ARG D NH1   1 
ATOM   3308 N  NH1   B ARG B 2 158 ? 12.546  5.942   -55.029 0.60 109.42 ? 254  ARG D NH1   1 
ATOM   3309 N  NH2   A ARG B 2 158 ? 11.021  3.215   -52.344 0.40 106.81 ? 254  ARG D NH2   1 
ATOM   3310 N  NH2   B ARG B 2 158 ? 14.126  6.138   -53.384 0.60 92.36  ? 254  ARG D NH2   1 
ATOM   3311 N  N     . LEU B 2 159 ? 7.997   7.732   -50.065 1.00 101.33 ? 255  LEU D N     1 
ATOM   3312 C  CA    . LEU B 2 159 ? 6.794   7.009   -49.670 1.00 92.91  ? 255  LEU D CA    1 
ATOM   3313 C  C     . LEU B 2 159 ? 5.658   7.968   -49.338 1.00 84.51  ? 255  LEU D C     1 
ATOM   3314 O  O     . LEU B 2 159 ? 4.511   7.747   -49.749 1.00 83.66  ? 255  LEU D O     1 
ATOM   3315 C  CB    . LEU B 2 159 ? 7.094   6.095   -48.482 1.00 73.63  ? 255  LEU D CB    1 
ATOM   3316 C  CG    . LEU B 2 159 ? 8.127   4.991   -48.724 1.00 88.47  ? 255  LEU D CG    1 
ATOM   3317 C  CD1   . LEU B 2 159 ? 8.254   4.091   -47.504 1.00 103.76 ? 255  LEU D CD1   1 
ATOM   3318 C  CD2   . LEU B 2 159 ? 7.774   4.179   -49.961 1.00 91.68  ? 255  LEU D CD2   1 
ATOM   3319 N  N     . ALA B 2 160 ? 5.959   9.050   -48.611 1.00 85.99  ? 256  ALA D N     1 
ATOM   3320 C  CA    . ALA B 2 160 ? 4.922   10.014  -48.258 1.00 92.83  ? 256  ALA D CA    1 
ATOM   3321 C  C     . ALA B 2 160 ? 4.338   10.692  -49.489 1.00 90.28  ? 256  ALA D C     1 
ATOM   3322 O  O     . ALA B 2 160 ? 3.141   11.002  -49.517 1.00 87.76  ? 256  ALA D O     1 
ATOM   3323 C  CB    . ALA B 2 160 ? 5.484   11.060  -47.295 1.00 75.84  ? 256  ALA D CB    1 
ATOM   3324 N  N     . ASP B 2 161 ? 5.157   10.927  -50.516 1.00 95.07  ? 257  ASP D N     1 
ATOM   3325 C  CA    . ASP B 2 161 ? 4.669   11.588  -51.720 1.00 86.28  ? 257  ASP D CA    1 
ATOM   3326 C  C     . ASP B 2 161 ? 3.911   10.622  -52.622 1.00 68.58  ? 257  ASP D C     1 
ATOM   3327 O  O     . ASP B 2 161 ? 2.909   11.001  -53.239 1.00 78.16  ? 257  ASP D O     1 
ATOM   3328 C  CB    . ASP B 2 161 ? 5.838   12.220  -52.476 1.00 83.37  ? 257  ASP D CB    1 
ATOM   3329 C  CG    . ASP B 2 161 ? 5.385   13.118  -53.612 1.00 111.26 ? 257  ASP D CG    1 
ATOM   3330 O  OD1   . ASP B 2 161 ? 4.193   13.488  -53.646 1.00 118.30 ? 257  ASP D OD1   1 
ATOM   3331 O  OD2   . ASP B 2 161 ? 6.225   13.453  -54.474 1.00 117.22 ? 257  ASP D OD2   1 
ATOM   3332 N  N     . GLU B 2 162 ? 4.367   9.371   -52.707 1.00 67.87  ? 258  GLU D N     1 
ATOM   3333 C  CA    . GLU B 2 162 ? 3.747   8.412   -53.613 1.00 70.27  ? 258  GLU D CA    1 
ATOM   3334 C  C     . GLU B 2 162 ? 2.436   7.873   -53.051 1.00 79.18  ? 258  GLU D C     1 
ATOM   3335 O  O     . GLU B 2 162 ? 1.410   7.881   -53.739 1.00 74.80  ? 258  GLU D O     1 
ATOM   3336 C  CB    . GLU B 2 162 ? 4.717   7.266   -53.905 1.00 71.71  ? 258  GLU D CB    1 
ATOM   3337 C  CG    . GLU B 2 162 ? 4.168   6.221   -54.859 1.00 67.62  ? 258  GLU D CG    1 
ATOM   3338 C  CD    . GLU B 2 162 ? 5.164   5.117   -55.149 1.00 91.95  ? 258  GLU D CD    1 
ATOM   3339 O  OE1   . GLU B 2 162 ? 6.173   5.016   -54.419 1.00 91.05  ? 258  GLU D OE1   1 
ATOM   3340 O  OE2   . GLU B 2 162 ? 4.939   4.352   -56.110 1.00 104.26 ? 258  GLU D OE2   1 
ATOM   3341 N  N     . PHE B 2 163 ? 2.449   7.401   -51.805 1.00 91.69  ? 259  PHE D N     1 
ATOM   3342 C  CA    . PHE B 2 163 ? 1.281   6.763   -51.214 1.00 69.33  ? 259  PHE D CA    1 
ATOM   3343 C  C     . PHE B 2 163 ? 0.429   7.718   -50.390 1.00 75.11  ? 259  PHE D C     1 
ATOM   3344 O  O     . PHE B 2 163 ? -0.623  7.310   -49.889 1.00 77.21  ? 259  PHE D O     1 
ATOM   3345 C  CB    . PHE B 2 163 ? 1.716   5.576   -50.350 1.00 84.60  ? 259  PHE D CB    1 
ATOM   3346 C  CG    . PHE B 2 163 ? 2.513   4.548   -51.099 1.00 76.97  ? 259  PHE D CG    1 
ATOM   3347 C  CD1   . PHE B 2 163 ? 1.880   3.607   -51.892 1.00 70.82  ? 259  PHE D CD1   1 
ATOM   3348 C  CD2   . PHE B 2 163 ? 3.895   4.527   -51.013 1.00 81.83  ? 259  PHE D CD2   1 
ATOM   3349 C  CE1   . PHE B 2 163 ? 2.610   2.661   -52.585 1.00 85.25  ? 259  PHE D CE1   1 
ATOM   3350 C  CE2   . PHE B 2 163 ? 4.631   3.583   -51.703 1.00 82.25  ? 259  PHE D CE2   1 
ATOM   3351 C  CZ    . PHE B 2 163 ? 3.988   2.649   -52.490 1.00 83.13  ? 259  PHE D CZ    1 
ATOM   3352 N  N     . GLY B 2 164 ? 0.849   8.972   -50.242 1.00 78.18  ? 260  GLY D N     1 
ATOM   3353 C  CA    . GLY B 2 164 ? 0.066   9.936   -49.492 1.00 86.38  ? 260  GLY D CA    1 
ATOM   3354 C  C     . GLY B 2 164 ? -0.087  9.614   -48.023 1.00 94.87  ? 260  GLY D C     1 
ATOM   3355 O  O     . GLY B 2 164 ? -1.071  10.030  -47.404 1.00 94.01  ? 260  GLY D O     1 
ATOM   3356 N  N     . VAL B 2 165 ? 0.860   8.885   -47.448 1.00 99.57  ? 261  VAL D N     1 
ATOM   3357 C  CA    . VAL B 2 165 ? 0.808   8.514   -46.040 1.00 81.41  ? 261  VAL D CA    1 
ATOM   3358 C  C     . VAL B 2 165 ? 1.409   9.638   -45.211 1.00 81.31  ? 261  VAL D C     1 
ATOM   3359 O  O     . VAL B 2 165 ? 2.229   10.428  -45.692 1.00 84.85  ? 261  VAL D O     1 
ATOM   3360 C  CB    . VAL B 2 165 ? 1.539   7.177   -45.790 1.00 74.35  ? 261  VAL D CB    1 
ATOM   3361 C  CG1   . VAL B 2 165 ? 0.996   6.094   -46.707 1.00 76.77  ? 261  VAL D CG1   1 
ATOM   3362 C  CG2   . VAL B 2 165 ? 3.041   7.342   -45.982 1.00 76.55  ? 261  VAL D CG2   1 
ATOM   3363 N  N     . ALA B 2 166 ? 0.993   9.718   -43.950 1.00 84.29  ? 262  ALA D N     1 
ATOM   3364 C  CA    . ALA B 2 166 ? 1.551   10.682  -43.007 1.00 84.40  ? 262  ALA D CA    1 
ATOM   3365 C  C     . ALA B 2 166 ? 2.765   10.048  -42.339 1.00 80.54  ? 262  ALA D C     1 
ATOM   3366 O  O     . ALA B 2 166 ? 2.635   9.058   -41.615 1.00 99.61  ? 262  ALA D O     1 
ATOM   3367 C  CB    . ALA B 2 166 ? 0.510   11.098  -41.973 1.00 85.82  ? 262  ALA D CB    1 
ATOM   3368 N  N     . VAL B 2 167 ? 3.944   10.609  -42.587 1.00 63.56  ? 263  VAL D N     1 
ATOM   3369 C  CA    . VAL B 2 167 ? 5.189   10.096  -42.029 1.00 84.75  ? 263  VAL D CA    1 
ATOM   3370 C  C     . VAL B 2 167 ? 5.533   10.913  -40.793 1.00 70.85  ? 263  VAL D C     1 
ATOM   3371 O  O     . VAL B 2 167 ? 5.799   12.117  -40.887 1.00 88.34  ? 263  VAL D O     1 
ATOM   3372 C  CB    . VAL B 2 167 ? 6.328   10.141  -43.059 1.00 75.15  ? 263  VAL D CB    1 
ATOM   3373 C  CG1   . VAL B 2 167 ? 7.649   9.780   -42.401 1.00 74.45  ? 263  VAL D CG1   1 
ATOM   3374 C  CG2   . VAL B 2 167 ? 6.031   9.196   -44.212 1.00 84.47  ? 263  VAL D CG2   1 
ATOM   3375 N  N     . VAL B 2 168 ? 5.526   10.262  -39.633 1.00 69.15  ? 264  VAL D N     1 
ATOM   3376 C  CA    . VAL B 2 168 ? 5.849   10.902  -38.363 1.00 85.27  ? 264  VAL D CA    1 
ATOM   3377 C  C     . VAL B 2 168 ? 7.103   10.242  -37.810 1.00 74.06  ? 264  VAL D C     1 
ATOM   3378 O  O     . VAL B 2 168 ? 7.097   9.042   -37.510 1.00 76.59  ? 264  VAL D O     1 
ATOM   3379 C  CB    . VAL B 2 168 ? 4.691   10.804  -37.358 1.00 66.42  ? 264  VAL D CB    1 
ATOM   3380 C  CG1   . VAL B 2 168 ? 5.064   11.493  -36.054 1.00 70.12  ? 264  VAL D CG1   1 
ATOM   3381 C  CG2   . VAL B 2 168 ? 3.425   11.409  -37.944 1.00 72.63  ? 264  VAL D CG2   1 
ATOM   3382 N  N     . ILE B 2 169 ? 8.171   11.021  -37.672 1.00 60.43  ? 265  ILE D N     1 
ATOM   3383 C  CA    . ILE B 2 169 ? 9.437   10.527  -37.147 1.00 73.49  ? 265  ILE D CA    1 
ATOM   3384 C  C     . ILE B 2 169 ? 9.703   11.187  -35.803 1.00 70.73  ? 265  ILE D C     1 
ATOM   3385 O  O     . ILE B 2 169 ? 9.324   12.339  -35.563 1.00 79.09  ? 265  ILE D O     1 
ATOM   3386 C  CB    . ILE B 2 169 ? 10.603  10.779  -38.126 1.00 73.15  ? 265  ILE D CB    1 
ATOM   3387 C  CG1   . ILE B 2 169 ? 10.760  12.274  -38.404 1.00 81.34  ? 265  ILE D CG1   1 
ATOM   3388 C  CG2   . ILE B 2 169 ? 10.378  10.019  -39.419 1.00 68.76  ? 265  ILE D CG2   1 
ATOM   3389 C  CD1   . ILE B 2 169 ? 11.888  12.601  -39.358 1.00 80.40  ? 265  ILE D CD1   1 
ATOM   3390 N  N     . THR B 2 170 ? 10.357  10.442  -34.917 1.00 72.57  ? 266  THR D N     1 
ATOM   3391 C  CA    . THR B 2 170 ? 10.675  10.911  -33.577 1.00 81.19  ? 266  THR D CA    1 
ATOM   3392 C  C     . THR B 2 170 ? 12.170  11.181  -33.467 1.00 77.75  ? 266  THR D C     1 
ATOM   3393 O  O     . THR B 2 170 ? 12.989  10.420  -33.992 1.00 84.59  ? 266  THR D O     1 
ATOM   3394 C  CB    . THR B 2 170 ? 10.235  9.884   -32.525 1.00 73.29  ? 266  THR D CB    1 
ATOM   3395 O  OG1   . THR B 2 170 ? 8.806   9.769   -32.534 1.00 79.31  ? 266  THR D OG1   1 
ATOM   3396 C  CG2   . THR B 2 170 ? 10.697  10.286  -31.135 1.00 86.52  ? 266  THR D CG2   1 
ATOM   3397 N  N     . ASN B 2 171 ? 12.522  12.277  -32.796 1.00 78.71  ? 267  ASN D N     1 
ATOM   3398 C  CA    . ASN B 2 171 ? 13.911  12.668  -32.596 1.00 86.42  ? 267  ASN D CA    1 
ATOM   3399 C  C     . ASN B 2 171 ? 14.126  13.022  -31.132 1.00 89.78  ? 267  ASN D C     1 
ATOM   3400 O  O     . ASN B 2 171 ? 13.337  13.772  -30.551 1.00 90.97  ? 267  ASN D O     1 
ATOM   3401 C  CB    . ASN B 2 171 ? 14.284  13.854  -33.493 1.00 89.75  ? 267  ASN D CB    1 
ATOM   3402 C  CG    . ASN B 2 171 ? 15.749  14.228  -33.387 1.00 99.04  ? 267  ASN D CG    1 
ATOM   3403 O  OD1   . ASN B 2 171 ? 16.577  13.427  -32.954 1.00 105.99 ? 267  ASN D OD1   1 
ATOM   3404 N  ND2   . ASN B 2 171 ? 16.076  15.452  -33.786 1.00 109.81 ? 267  ASN D ND2   1 
ATOM   3405 N  N     . GLN B 2 172 ? 15.189  12.481  -30.542 1.00 93.51  ? 268  GLN D N     1 
ATOM   3406 C  CA    . GLN B 2 172 ? 15.518  12.743  -29.147 1.00 96.51  ? 268  GLN D CA    1 
ATOM   3407 C  C     . GLN B 2 172 ? 16.465  13.933  -29.058 1.00 99.40  ? 268  GLN D C     1 
ATOM   3408 O  O     . GLN B 2 172 ? 17.478  13.983  -29.764 1.00 106.24 ? 268  GLN D O     1 
ATOM   3409 C  CB    . GLN B 2 172 ? 16.152  11.510  -28.500 1.00 103.68 ? 268  GLN D CB    1 
ATOM   3410 C  CG    . GLN B 2 172 ? 16.476  11.666  -27.020 1.00 88.75  ? 268  GLN D CG    1 
ATOM   3411 C  CD    . GLN B 2 172 ? 15.254  11.531  -26.130 1.00 105.22 ? 268  GLN D CD    1 
ATOM   3412 O  OE1   . GLN B 2 172 ? 14.143  11.298  -26.608 1.00 92.01  ? 268  GLN D OE1   1 
ATOM   3413 N  NE2   . GLN B 2 172 ? 15.456  11.671  -24.825 1.00 117.35 ? 268  GLN D NE2   1 
ATOM   3414 N  N     . VAL B 2 173 ? 16.133  14.887  -28.191 1.00 94.52  ? 269  VAL D N     1 
ATOM   3415 C  CA    . VAL B 2 173 ? 16.915  16.103  -28.008 1.00 88.13  ? 269  VAL D CA    1 
ATOM   3416 C  C     . VAL B 2 173 ? 17.281  16.228  -26.536 1.00 93.58  ? 269  VAL D C     1 
ATOM   3417 O  O     . VAL B 2 173 ? 16.447  15.985  -25.657 1.00 94.89  ? 269  VAL D O     1 
ATOM   3418 C  CB    . VAL B 2 173 ? 16.145  17.352  -28.488 1.00 86.80  ? 269  VAL D CB    1 
ATOM   3419 C  CG1   . VAL B 2 173 ? 16.997  18.603  -28.328 1.00 84.64  ? 269  VAL D CG1   1 
ATOM   3420 C  CG2   . VAL B 2 173 ? 15.704  17.183  -29.934 1.00 97.09  ? 269  VAL D CG2   1 
ATOM   3421 N  N     . VAL B 2 174 ? 18.529  16.602  -26.271 1.00 95.88  ? 270  VAL D N     1 
ATOM   3422 C  CA    . VAL B 2 174 ? 18.995  16.800  -24.904 1.00 112.79 ? 270  VAL D CA    1 
ATOM   3423 C  C     . VAL B 2 174 ? 19.128  18.289  -24.607 1.00 113.99 ? 270  VAL D C     1 
ATOM   3424 O  O     . VAL B 2 174 ? 18.650  18.773  -23.580 1.00 124.37 ? 270  VAL D O     1 
ATOM   3425 C  CB    . VAL B 2 174 ? 20.329  16.074  -24.658 1.00 111.91 ? 270  VAL D CB    1 
ATOM   3426 C  CG1   . VAL B 2 174 ? 21.408  16.626  -25.576 1.00 102.77 ? 270  VAL D CG1   1 
ATOM   3427 C  CG2   . VAL B 2 174 ? 20.741  16.203  -23.198 1.00 85.20  ? 270  VAL D CG2   1 
ATOM   3428 N  N     . GLY B 2 192 ? 27.202  21.046  -40.336 1.00 107.55 ? 288  GLY D N     1 
ATOM   3429 C  CA    . GLY B 2 192 ? 26.975  20.079  -41.394 1.00 112.57 ? 288  GLY D CA    1 
ATOM   3430 C  C     . GLY B 2 192 ? 25.576  20.142  -41.974 1.00 123.48 ? 288  GLY D C     1 
ATOM   3431 O  O     . GLY B 2 192 ? 25.270  19.468  -42.958 1.00 128.53 ? 288  GLY D O     1 
ATOM   3432 N  N     . GLY B 2 193 ? 24.722  20.957  -41.360 1.00 135.55 ? 289  GLY D N     1 
ATOM   3433 C  CA    . GLY B 2 193 ? 23.354  21.104  -41.817 1.00 132.95 ? 289  GLY D CA    1 
ATOM   3434 C  C     . GLY B 2 193 ? 22.465  19.946  -41.416 1.00 133.13 ? 289  GLY D C     1 
ATOM   3435 O  O     . GLY B 2 193 ? 22.670  18.813  -41.863 1.00 138.21 ? 289  GLY D O     1 
ATOM   3436 N  N     . ASN B 2 194 ? 21.472  20.217  -40.574 1.00 114.12 ? 290  ASN D N     1 
ATOM   3437 C  CA    . ASN B 2 194 ? 20.542  19.187  -40.117 1.00 109.57 ? 290  ASN D CA    1 
ATOM   3438 C  C     . ASN B 2 194 ? 19.617  18.814  -41.268 1.00 108.86 ? 290  ASN D C     1 
ATOM   3439 O  O     . ASN B 2 194 ? 18.698  19.560  -41.612 1.00 106.28 ? 290  ASN D O     1 
ATOM   3440 C  CB    . ASN B 2 194 ? 19.754  19.679  -38.909 1.00 116.89 ? 290  ASN D CB    1 
ATOM   3441 C  CG    . ASN B 2 194 ? 18.802  18.631  -38.368 1.00 117.50 ? 290  ASN D CG    1 
ATOM   3442 O  OD1   . ASN B 2 194 ? 17.631  18.587  -38.744 1.00 113.91 ? 290  ASN D OD1   1 
ATOM   3443 N  ND2   . ASN B 2 194 ? 19.301  17.779  -37.480 1.00 121.77 ? 290  ASN D ND2   1 
ATOM   3444 N  N     . ILE B 2 195 ? 19.861  17.648  -41.873 1.00 108.93 ? 291  ILE D N     1 
ATOM   3445 C  CA    . ILE B 2 195 ? 19.038  17.198  -42.989 1.00 101.59 ? 291  ILE D CA    1 
ATOM   3446 C  C     . ILE B 2 195 ? 17.625  16.846  -42.546 1.00 105.97 ? 291  ILE D C     1 
ATOM   3447 O  O     . ILE B 2 195 ? 16.704  16.842  -43.371 1.00 109.41 ? 291  ILE D O     1 
ATOM   3448 C  CB    . ILE B 2 195 ? 19.702  16.001  -43.693 1.00 108.53 ? 291  ILE D CB    1 
ATOM   3449 C  CG1   . ILE B 2 195 ? 20.232  15.002  -42.662 1.00 111.11 ? 291  ILE D CG1   1 
ATOM   3450 C  CG2   . ILE B 2 195 ? 20.818  16.476  -44.614 1.00 107.78 ? 291  ILE D CG2   1 
ATOM   3451 C  CD1   . ILE B 2 195 ? 21.000  13.848  -43.268 1.00 111.57 ? 291  ILE D CD1   1 
ATOM   3452 N  N     . ILE B 2 196 ? 17.426  16.550  -41.259 1.00 100.29 ? 292  ILE D N     1 
ATOM   3453 C  CA    . ILE B 2 196 ? 16.083  16.276  -40.760 1.00 93.50  ? 292  ILE D CA    1 
ATOM   3454 C  C     . ILE B 2 196 ? 15.218  17.526  -40.846 1.00 94.66  ? 292  ILE D C     1 
ATOM   3455 O  O     . ILE B 2 196 ? 14.036  17.457  -41.202 1.00 93.53  ? 292  ILE D O     1 
ATOM   3456 C  CB    . ILE B 2 196 ? 16.150  15.733  -39.322 1.00 92.57  ? 292  ILE D CB    1 
ATOM   3457 C  CG1   . ILE B 2 196 ? 17.109  14.545  -39.247 1.00 93.09  ? 292  ILE D CG1   1 
ATOM   3458 C  CG2   . ILE B 2 196 ? 14.766  15.334  -38.834 1.00 82.24  ? 292  ILE D CG2   1 
ATOM   3459 C  CD1   . ILE B 2 196 ? 17.361  14.065  -37.842 1.00 72.93  ? 292  ILE D CD1   1 
ATOM   3460 N  N     . ALA B 2 197 ? 15.792  18.688  -40.526 1.00 92.15  ? 293  ALA D N     1 
ATOM   3461 C  CA    . ALA B 2 197 ? 15.042  19.936  -40.615 1.00 103.66 ? 293  ALA D CA    1 
ATOM   3462 C  C     . ALA B 2 197 ? 14.674  20.270  -42.054 1.00 104.39 ? 293  ALA D C     1 
ATOM   3463 O  O     . ALA B 2 197 ? 13.630  20.885  -42.299 1.00 107.49 ? 293  ALA D O     1 
ATOM   3464 C  CB    . ALA B 2 197 ? 15.847  21.077  -39.995 1.00 106.75 ? 293  ALA D CB    1 
ATOM   3465 N  N     . HIS B 2 198 ? 15.510  19.874  -43.015 1.00 107.36 ? 294  HIS D N     1 
ATOM   3466 C  CA    . HIS B 2 198 ? 15.210  20.141  -44.417 1.00 109.22 ? 294  HIS D CA    1 
ATOM   3467 C  C     . HIS B 2 198 ? 14.176  19.164  -44.964 1.00 99.04  ? 294  HIS D C     1 
ATOM   3468 O  O     . HIS B 2 198 ? 13.280  19.562  -45.716 1.00 111.76 ? 294  HIS D O     1 
ATOM   3469 C  CB    . HIS B 2 198 ? 16.490  20.078  -45.252 1.00 106.86 ? 294  HIS D CB    1 
ATOM   3470 C  CG    . HIS B 2 198 ? 17.550  21.040  -44.811 1.00 111.23 ? 294  HIS D CG    1 
ATOM   3471 N  ND1   . HIS B 2 198 ? 17.300  22.078  -43.939 1.00 115.63 ? 294  HIS D ND1   1 
ATOM   3472 C  CD2   . HIS B 2 198 ? 18.866  21.118  -45.119 1.00 109.85 ? 294  HIS D CD2   1 
ATOM   3473 C  CE1   . HIS B 2 198 ? 18.415  22.754  -43.731 1.00 118.90 ? 294  HIS D CE1   1 
ATOM   3474 N  NE2   . HIS B 2 198 ? 19.381  22.192  -44.436 1.00 111.86 ? 294  HIS D NE2   1 
ATOM   3475 N  N     . ALA B 2 199 ? 14.281  17.886  -44.596 1.00 89.44  ? 295  ALA D N     1 
ATOM   3476 C  CA    . ALA B 2 199 ? 13.371  16.877  -45.120 1.00 87.98  ? 295  ALA D CA    1 
ATOM   3477 C  C     . ALA B 2 199 ? 11.993  16.923  -44.473 1.00 92.28  ? 295  ALA D C     1 
ATOM   3478 O  O     . ALA B 2 199 ? 11.025  16.453  -45.080 1.00 97.54  ? 295  ALA D O     1 
ATOM   3479 C  CB    . ALA B 2 199 ? 13.973  15.481  -44.942 1.00 99.56  ? 295  ALA D CB    1 
ATOM   3480 N  N     . SER B 2 200 ? 11.879  17.473  -43.267 1.00 86.73  ? 296  SER D N     1 
ATOM   3481 C  CA    . SER B 2 200 ? 10.610  17.512  -42.554 1.00 100.24 ? 296  SER D CA    1 
ATOM   3482 C  C     . SER B 2 200 ? 9.848   18.782  -42.907 1.00 95.28  ? 296  SER D C     1 
ATOM   3483 O  O     . SER B 2 200 ? 10.418  19.878  -42.909 1.00 98.53  ? 296  SER D O     1 
ATOM   3484 C  CB    . SER B 2 200 ? 10.834  17.433  -41.043 1.00 89.57  ? 296  SER D CB    1 
ATOM   3485 O  OG    . SER B 2 200 ? 11.583  18.543  -40.580 1.00 110.46 ? 296  SER D OG    1 
ATOM   3486 N  N     . THR B 2 201 ? 8.557   18.628  -43.204 1.00 97.45  ? 297  THR D N     1 
ATOM   3487 C  CA    . THR B 2 201 ? 7.708   19.781  -43.485 1.00 86.16  ? 297  THR D CA    1 
ATOM   3488 C  C     . THR B 2 201 ? 7.161   20.382  -42.195 1.00 97.64  ? 297  THR D C     1 
ATOM   3489 O  O     . THR B 2 201 ? 7.343   21.574  -41.925 1.00 99.08  ? 297  THR D O     1 
ATOM   3490 C  CB    . THR B 2 201 ? 6.562   19.380  -44.417 1.00 93.29  ? 297  THR D CB    1 
ATOM   3491 O  OG1   . THR B 2 201 ? 7.095   18.885  -45.651 1.00 90.02  ? 297  THR D OG1   1 
ATOM   3492 C  CG2   . THR B 2 201 ? 5.661   20.573  -44.699 1.00 93.80  ? 297  THR D CG2   1 
ATOM   3493 N  N     . THR B 2 202 ? 6.488   19.568  -41.386 1.00 101.05 ? 298  THR D N     1 
ATOM   3494 C  CA    . THR B 2 202 ? 5.951   20.007  -40.107 1.00 98.82  ? 298  THR D CA    1 
ATOM   3495 C  C     . THR B 2 202 ? 6.905   19.602  -38.991 1.00 86.90  ? 298  THR D C     1 
ATOM   3496 O  O     . THR B 2 202 ? 7.457   18.499  -39.003 1.00 92.31  ? 298  THR D O     1 
ATOM   3497 C  CB    . THR B 2 202 ? 4.564   19.409  -39.857 1.00 103.64 ? 298  THR D CB    1 
ATOM   3498 O  OG1   . THR B 2 202 ? 3.752   19.579  -41.025 1.00 96.95  ? 298  THR D OG1   1 
ATOM   3499 C  CG2   . THR B 2 202 ? 3.890   20.100  -38.682 1.00 90.82  ? 298  THR D CG2   1 
ATOM   3500 N  N     . ARG B 2 203 ? 7.106   20.503  -38.031 1.00 73.85  ? 299  ARG D N     1 
ATOM   3501 C  CA    . ARG B 2 203 ? 8.044   20.279  -36.938 1.00 95.72  ? 299  ARG D CA    1 
ATOM   3502 C  C     . ARG B 2 203 ? 7.388   20.669  -35.623 1.00 96.25  ? 299  ARG D C     1 
ATOM   3503 O  O     . ARG B 2 203 ? 6.997   21.827  -35.441 1.00 101.99 ? 299  ARG D O     1 
ATOM   3504 C  CB    . ARG B 2 203 ? 9.337   21.072  -37.149 1.00 88.95  ? 299  ARG D CB    1 
ATOM   3505 C  CG    . ARG B 2 203 ? 10.038  20.777  -38.465 1.00 88.03  ? 299  ARG D CG    1 
ATOM   3506 C  CD    . ARG B 2 203 ? 11.407  21.423  -38.503 1.00 95.44  ? 299  ARG D CD    1 
ATOM   3507 N  NE    . ARG B 2 203 ? 12.290  20.861  -37.490 1.00 96.84  ? 299  ARG D NE    1 
ATOM   3508 C  CZ    . ARG B 2 203 ? 13.464  21.375  -37.151 1.00 99.17  ? 299  ARG D CZ    1 
ATOM   3509 N  NH1   . ARG B 2 203 ? 13.922  22.481  -37.716 1.00 107.90 ? 299  ARG D NH1   1 
ATOM   3510 N  NH2   . ARG B 2 203 ? 14.193  20.769  -36.219 1.00 104.16 ? 299  ARG D NH2   1 
ATOM   3511 N  N     . LEU B 2 204 ? 7.284   19.711  -34.706 1.00 84.57  ? 300  LEU D N     1 
ATOM   3512 C  CA    . LEU B 2 204 ? 6.712   19.934  -33.386 1.00 89.98  ? 300  LEU D CA    1 
ATOM   3513 C  C     . LEU B 2 204 ? 7.788   19.751  -32.325 1.00 85.97  ? 300  LEU D C     1 
ATOM   3514 O  O     . LEU B 2 204 ? 8.566   18.789  -32.376 1.00 82.86  ? 300  LEU D O     1 
ATOM   3515 C  CB    . LEU B 2 204 ? 5.541   18.983  -33.122 1.00 83.77  ? 300  LEU D CB    1 
ATOM   3516 C  CG    . LEU B 2 204 ? 4.208   19.298  -33.809 1.00 93.07  ? 300  LEU D CG    1 
ATOM   3517 C  CD1   . LEU B 2 204 ? 3.876   20.780  -33.695 1.00 106.52 ? 300  LEU D CD1   1 
ATOM   3518 C  CD2   . LEU B 2 204 ? 4.205   18.850  -35.262 1.00 78.27  ? 300  LEU D CD2   1 
ATOM   3519 N  N     . TYR B 2 205 ? 7.832   20.681  -31.376 1.00 85.57  ? 301  TYR D N     1 
ATOM   3520 C  CA    . TYR B 2 205 ? 8.752   20.643  -30.248 1.00 91.40  ? 301  TYR D CA    1 
ATOM   3521 C  C     . TYR B 2 205 ? 7.944   20.391  -28.983 1.00 101.88 ? 301  TYR D C     1 
ATOM   3522 O  O     . TYR B 2 205 ? 7.042   21.170  -28.653 1.00 107.26 ? 301  TYR D O     1 
ATOM   3523 C  CB    . TYR B 2 205 ? 9.541   21.949  -30.145 1.00 84.29  ? 301  TYR D CB    1 
ATOM   3524 C  CG    . TYR B 2 205 ? 10.305  22.121  -28.852 1.00 94.08  ? 301  TYR D CG    1 
ATOM   3525 C  CD1   . TYR B 2 205 ? 11.383  21.303  -28.543 1.00 95.07  ? 301  TYR D CD1   1 
ATOM   3526 C  CD2   . TYR B 2 205 ? 9.957   23.114  -27.945 1.00 106.33 ? 301  TYR D CD2   1 
ATOM   3527 C  CE1   . TYR B 2 205 ? 12.088  21.461  -27.365 1.00 93.11  ? 301  TYR D CE1   1 
ATOM   3528 C  CE2   . TYR B 2 205 ? 10.656  23.281  -26.764 1.00 110.37 ? 301  TYR D CE2   1 
ATOM   3529 C  CZ    . TYR B 2 205 ? 11.721  22.451  -26.480 1.00 106.88 ? 301  TYR D CZ    1 
ATOM   3530 O  OH    . TYR B 2 205 ? 12.420  22.612  -25.305 1.00 120.11 ? 301  TYR D OH    1 
ATOM   3531 N  N     . LEU B 2 206 ? 8.256   19.298  -28.293 1.00 100.54 ? 302  LEU D N     1 
ATOM   3532 C  CA    . LEU B 2 206 ? 7.557   18.905  -27.077 1.00 94.49  ? 302  LEU D CA    1 
ATOM   3533 C  C     . LEU B 2 206 ? 8.437   19.219  -25.874 1.00 99.84  ? 302  LEU D C     1 
ATOM   3534 O  O     . LEU B 2 206 ? 9.571   18.734  -25.787 1.00 104.16 ? 302  LEU D O     1 
ATOM   3535 C  CB    . LEU B 2 206 ? 7.200   17.419  -27.109 1.00 74.73  ? 302  LEU D CB    1 
ATOM   3536 C  CG    . LEU B 2 206 ? 6.411   16.930  -28.326 1.00 91.12  ? 302  LEU D CG    1 
ATOM   3537 C  CD1   . LEU B 2 206 ? 6.090   15.450  -28.193 1.00 83.40  ? 302  LEU D CD1   1 
ATOM   3538 C  CD2   . LEU B 2 206 ? 5.141   17.743  -28.509 1.00 91.05  ? 302  LEU D CD2   1 
ATOM   3539 N  N     . ARG B 2 207 ? 7.915   20.025  -24.952 1.00 106.05 ? 303  ARG D N     1 
ATOM   3540 C  CA    . ARG B 2 207 ? 8.635   20.409  -23.749 1.00 111.92 ? 303  ARG D CA    1 
ATOM   3541 C  C     . ARG B 2 207 ? 7.772   20.114  -22.530 1.00 108.52 ? 303  ARG D C     1 
ATOM   3542 O  O     . ARG B 2 207 ? 6.542   20.050  -22.611 1.00 110.42 ? 303  ARG D O     1 
ATOM   3543 C  CB    . ARG B 2 207 ? 9.031   21.895  -23.780 1.00 111.96 ? 303  ARG D CB    1 
ATOM   3544 C  CG    . ARG B 2 207 ? 10.085  22.288  -22.754 1.00 128.82 ? 303  ARG D CG    1 
ATOM   3545 C  CD    . ARG B 2 207 ? 10.493  23.749  -22.887 1.00 122.99 ? 303  ARG D CD    1 
ATOM   3546 N  NE    . ARG B 2 207 ? 9.405   24.666  -22.567 1.00 119.85 ? 303  ARG D NE    1 
ATOM   3547 C  CZ    . ARG B 2 207 ? 8.663   25.295  -23.469 1.00 124.33 ? 303  ARG D CZ    1 
ATOM   3548 N  NH1   . ARG B 2 207 ? 8.862   25.128  -24.766 1.00 132.32 ? 303  ARG D NH1   1 
ATOM   3549 N  NH2   . ARG B 2 207 ? 7.698   26.113  -23.058 1.00 129.64 ? 303  ARG D NH2   1 
ATOM   3550 N  N     . LYS B 2 208 ? 8.435   19.921  -21.394 1.00 122.16 ? 304  LYS D N     1 
ATOM   3551 C  CA    . LYS B 2 208 ? 7.766   19.638  -20.132 1.00 120.30 ? 304  LYS D CA    1 
ATOM   3552 C  C     . LYS B 2 208 ? 7.686   20.927  -19.324 1.00 124.98 ? 304  LYS D C     1 
ATOM   3553 O  O     . LYS B 2 208 ? 8.717   21.489  -18.941 1.00 133.23 ? 304  LYS D O     1 
ATOM   3554 C  CB    . LYS B 2 208 ? 8.510   18.556  -19.350 1.00 112.77 ? 304  LYS D CB    1 
ATOM   3555 C  CG    . LYS B 2 208 ? 7.684   17.903  -18.254 1.00 119.13 ? 304  LYS D CG    1 
ATOM   3556 C  CD    . LYS B 2 208 ? 6.435   17.250  -18.825 1.00 124.88 ? 304  LYS D CD    1 
ATOM   3557 C  CE    . LYS B 2 208 ? 5.788   16.317  -17.814 1.00 128.19 ? 304  LYS D CE    1 
ATOM   3558 N  NZ    . LYS B 2 208 ? 6.695   15.196  -17.441 1.00 113.77 ? 304  LYS D NZ    1 
ATOM   3559 N  N     . GLY B 2 209 ? 6.467   21.393  -19.073 1.00 127.10 ? 305  GLY D N     1 
ATOM   3560 C  CA    . GLY B 2 209 ? 6.277   22.623  -18.332 1.00 130.76 ? 305  GLY D CA    1 
ATOM   3561 C  C     . GLY B 2 209 ? 6.354   22.423  -16.833 1.00 138.27 ? 305  GLY D C     1 
ATOM   3562 O  O     . GLY B 2 209 ? 7.409   22.066  -16.304 1.00 132.38 ? 305  GLY D O     1 
ATOM   3563 N  N     . ARG B 2 210 ? 5.246   22.646  -16.134 1.00 147.60 ? 306  ARG D N     1 
ATOM   3564 C  CA    . ARG B 2 210 ? 5.168   22.429  -14.695 1.00 141.34 ? 306  ARG D CA    1 
ATOM   3565 C  C     . ARG B 2 210 ? 4.151   21.331  -14.429 1.00 140.27 ? 306  ARG D C     1 
ATOM   3566 O  O     . ARG B 2 210 ? 2.961   21.502  -14.716 1.00 136.81 ? 306  ARG D O     1 
ATOM   3567 C  CB    . ARG B 2 210 ? 4.777   23.714  -13.966 1.00 129.05 ? 306  ARG D CB    1 
ATOM   3568 C  CG    . ARG B 2 210 ? 4.704   24.929  -14.871 1.00 131.46 ? 306  ARG D CG    1 
ATOM   3569 C  CD    . ARG B 2 210 ? 4.671   26.193  -14.060 1.00 135.88 ? 306  ARG D CD    1 
ATOM   3570 N  NE    . ARG B 2 210 ? 3.799   27.185  -14.667 1.00 143.45 ? 306  ARG D NE    1 
ATOM   3571 C  CZ    . ARG B 2 210 ? 2.504   27.288  -14.410 1.00 143.83 ? 306  ARG D CZ    1 
ATOM   3572 N  NH1   . ARG B 2 210 ? 1.889   26.431  -13.609 1.00 131.46 ? 306  ARG D NH1   1 
ATOM   3573 N  NH2   . ARG B 2 210 ? 1.815   28.287  -14.951 1.00 139.71 ? 306  ARG D NH2   1 
ATOM   3574 N  N     . GLY B 2 211 ? 4.618   20.212  -13.879 1.00 133.12 ? 307  GLY D N     1 
ATOM   3575 C  CA    . GLY B 2 211 ? 3.729   19.081  -13.673 1.00 129.60 ? 307  GLY D CA    1 
ATOM   3576 C  C     . GLY B 2 211 ? 3.395   18.406  -14.989 1.00 147.86 ? 307  GLY D C     1 
ATOM   3577 O  O     . GLY B 2 211 ? 4.238   18.272  -15.883 1.00 148.49 ? 307  GLY D O     1 
ATOM   3578 N  N     . GLU B 2 212 ? 2.138   17.991  -15.121 1.00 148.81 ? 308  GLU D N     1 
ATOM   3579 C  CA    . GLU B 2 212 ? 1.676   17.328  -16.332 1.00 152.15 ? 308  GLU D CA    1 
ATOM   3580 C  C     . GLU B 2 212 ? 1.503   18.299  -17.500 1.00 149.50 ? 308  GLU D C     1 
ATOM   3581 O  O     . GLU B 2 212 ? 1.072   17.880  -18.578 1.00 145.31 ? 308  GLU D O     1 
ATOM   3582 C  CB    . GLU B 2 212 ? 0.369   16.583  -16.023 1.00 151.66 ? 308  GLU D CB    1 
ATOM   3583 C  CG    . GLU B 2 212 ? -0.123  15.590  -17.089 1.00 159.80 ? 308  GLU D CG    1 
ATOM   3584 C  CD    . GLU B 2 212 ? 0.923   14.588  -17.532 1.00 153.51 ? 308  GLU D CD    1 
ATOM   3585 O  OE1   . GLU B 2 212 ? 1.798   14.209  -16.726 1.00 169.98 ? 308  GLU D OE1   1 
ATOM   3586 O  OE2   . GLU B 2 212 ? 0.860   14.174  -18.705 1.00 130.21 ? 308  GLU D OE2   1 
ATOM   3587 N  N     . THR B 2 213 ? 1.843   19.576  -17.324 1.00 151.77 ? 309  THR D N     1 
ATOM   3588 C  CA    . THR B 2 213 ? 1.766   20.568  -18.396 1.00 145.73 ? 309  THR D CA    1 
ATOM   3589 C  C     . THR B 2 213 ? 2.767   20.214  -19.491 1.00 133.90 ? 309  THR D C     1 
ATOM   3590 O  O     . THR B 2 213 ? 3.969   20.455  -19.353 1.00 132.59 ? 309  THR D O     1 
ATOM   3591 C  CB    . THR B 2 213 ? 2.032   21.964  -17.843 1.00 140.37 ? 309  THR D CB    1 
ATOM   3592 O  OG1   . THR B 2 213 ? 1.071   22.263  -16.822 1.00 138.84 ? 309  THR D OG1   1 
ATOM   3593 C  CG2   . THR B 2 213 ? 1.934   23.002  -18.952 1.00 133.50 ? 309  THR D CG2   1 
ATOM   3594 N  N     . ARG B 2 214 ? 2.279   19.640  -20.589 1.00 122.62 ? 310  ARG D N     1 
ATOM   3595 C  CA    . ARG B 2 214 ? 3.125   19.315  -21.730 1.00 126.73 ? 310  ARG D CA    1 
ATOM   3596 C  C     . ARG B 2 214 ? 2.863   20.333  -22.832 1.00 115.23 ? 310  ARG D C     1 
ATOM   3597 O  O     . ARG B 2 214 ? 1.731   20.460  -23.306 1.00 117.55 ? 310  ARG D O     1 
ATOM   3598 C  CB    . ARG B 2 214 ? 2.861   17.890  -22.215 1.00 129.72 ? 310  ARG D CB    1 
ATOM   3599 C  CG    . ARG B 2 214 ? 3.038   16.838  -21.130 1.00 124.41 ? 310  ARG D CG    1 
ATOM   3600 C  CD    . ARG B 2 214 ? 2.930   15.427  -21.682 1.00 121.49 ? 310  ARG D CD    1 
ATOM   3601 N  NE    . ARG B 2 214 ? 2.878   14.434  -20.616 1.00 121.78 ? 310  ARG D NE    1 
ATOM   3602 C  CZ    . ARG B 2 214 ? 3.943   13.900  -20.033 1.00 114.36 ? 310  ARG D CZ    1 
ATOM   3603 N  NH1   . ARG B 2 214 ? 5.170   14.236  -20.395 1.00 106.69 ? 310  ARG D NH1   1 
ATOM   3604 N  NH2   . ARG B 2 214 ? 3.772   13.008  -19.061 1.00 110.85 ? 310  ARG D NH2   1 
ATOM   3605 N  N     . ILE B 2 215 ? 3.900   21.064  -23.229 1.00 113.48 ? 311  ILE D N     1 
ATOM   3606 C  CA    . ILE B 2 215 ? 3.768   22.159  -24.182 1.00 113.48 ? 311  ILE D CA    1 
ATOM   3607 C  C     . ILE B 2 215 ? 4.248   21.681  -25.546 1.00 113.48 ? 311  ILE D C     1 
ATOM   3608 O  O     . ILE B 2 215 ? 5.402   21.263  -25.699 1.00 114.19 ? 311  ILE D O     1 
ATOM   3609 C  CB    . ILE B 2 215 ? 4.552   23.399  -23.724 1.00 115.25 ? 311  ILE D CB    1 
ATOM   3610 C  CG1   . ILE B 2 215 ? 4.036   23.877  -22.364 1.00 115.67 ? 311  ILE D CG1   1 
ATOM   3611 C  CG2   . ILE B 2 215 ? 4.447   24.508  -24.759 1.00 113.15 ? 311  ILE D CG2   1 
ATOM   3612 C  CD1   . ILE B 2 215 ? 4.745   25.103  -21.835 1.00 114.64 ? 311  ILE D CD1   1 
ATOM   3613 N  N     . CYS B 2 216 ? 3.362   21.744  -26.535 1.00 111.33 ? 312  CYS D N     1 
ATOM   3614 C  CA    . CYS B 2 216 ? 3.684   21.420  -27.919 1.00 111.61 ? 312  CYS D CA    1 
ATOM   3615 C  C     . CYS B 2 216 ? 3.723   22.714  -28.718 1.00 110.05 ? 312  CYS D C     1 
ATOM   3616 O  O     . CYS B 2 216 ? 2.725   23.440  -28.777 1.00 111.93 ? 312  CYS D O     1 
ATOM   3617 C  CB    . CYS B 2 216 ? 2.660   20.451  -28.510 1.00 117.50 ? 312  CYS D CB    1 
ATOM   3618 S  SG    . CYS B 2 216 ? 2.915   20.066  -30.257 1.00 110.01 ? 312  CYS D SG    1 
ATOM   3619 N  N     . LYS B 2 217 ? 4.872   23.003  -29.325 1.00 113.07 ? 313  LYS D N     1 
ATOM   3620 C  CA    . LYS B 2 217 ? 5.074   24.233  -30.079 1.00 104.61 ? 313  LYS D CA    1 
ATOM   3621 C  C     . LYS B 2 217 ? 5.378   23.899  -31.532 1.00 97.80  ? 313  LYS D C     1 
ATOM   3622 O  O     . LYS B 2 217 ? 6.216   23.037  -31.813 1.00 104.38 ? 313  LYS D O     1 
ATOM   3623 C  CB    . LYS B 2 217 ? 6.212   25.065  -29.481 1.00 108.04 ? 313  LYS D CB    1 
ATOM   3624 C  CG    . LYS B 2 217 ? 6.569   26.300  -30.293 1.00 117.20 ? 313  LYS D CG    1 
ATOM   3625 C  CD    . LYS B 2 217 ? 7.684   27.096  -29.636 1.00 112.39 ? 313  LYS D CD    1 
ATOM   3626 C  CE    . LYS B 2 217 ? 8.081   28.291  -30.488 1.00 119.39 ? 313  LYS D CE    1 
ATOM   3627 N  NZ    . LYS B 2 217 ? 6.926   29.192  -30.755 1.00 117.91 ? 313  LYS D NZ    1 
ATOM   3628 N  N     . ILE B 2 218 ? 4.695   24.580  -32.451 1.00 109.69 ? 314  ILE D N     1 
ATOM   3629 C  CA    . ILE B 2 218 ? 4.994   24.447  -33.871 1.00 103.91 ? 314  ILE D CA    1 
ATOM   3630 C  C     . ILE B 2 218 ? 6.320   25.143  -34.140 1.00 96.47  ? 314  ILE D C     1 
ATOM   3631 O  O     . ILE B 2 218 ? 6.365   26.360  -34.355 1.00 105.33 ? 314  ILE D O     1 
ATOM   3632 C  CB    . ILE B 2 218 ? 3.869   25.026  -34.746 1.00 88.20  ? 314  ILE D CB    1 
ATOM   3633 C  CG1   . ILE B 2 218 ? 2.537   24.348  -34.420 1.00 85.53  ? 314  ILE D CG1   1 
ATOM   3634 C  CG2   . ILE B 2 218 ? 4.200   24.856  -36.220 1.00 103.30 ? 314  ILE D CG2   1 
ATOM   3635 C  CD1   . ILE B 2 218 ? 1.388   24.819  -35.283 1.00 117.76 ? 314  ILE D CD1   1 
ATOM   3636 N  N     . TYR B 2 219 ? 7.412   24.375  -34.120 1.00 99.59  ? 315  TYR D N     1 
ATOM   3637 C  CA    . TYR B 2 219 ? 8.737   24.972  -34.245 1.00 103.75 ? 315  TYR D CA    1 
ATOM   3638 C  C     . TYR B 2 219 ? 8.972   25.509  -35.651 1.00 108.25 ? 315  TYR D C     1 
ATOM   3639 O  O     . TYR B 2 219 ? 9.620   26.547  -35.825 1.00 112.60 ? 315  TYR D O     1 
ATOM   3640 C  CB    . TYR B 2 219 ? 9.805   23.946  -33.868 1.00 94.82  ? 315  TYR D CB    1 
ATOM   3641 C  CG    . TYR B 2 219 ? 11.207  24.505  -33.792 1.00 86.80  ? 315  TYR D CG    1 
ATOM   3642 C  CD1   . TYR B 2 219 ? 11.593  25.323  -32.737 1.00 99.09  ? 315  TYR D CD1   1 
ATOM   3643 C  CD2   . TYR B 2 219 ? 12.149  24.204  -34.766 1.00 96.63  ? 315  TYR D CD2   1 
ATOM   3644 C  CE1   . TYR B 2 219 ? 12.875  25.832  -32.661 1.00 105.07 ? 315  TYR D CE1   1 
ATOM   3645 C  CE2   . TYR B 2 219 ? 13.434  24.708  -34.697 1.00 96.05  ? 315  TYR D CE2   1 
ATOM   3646 C  CZ    . TYR B 2 219 ? 13.791  25.521  -33.643 1.00 100.08 ? 315  TYR D CZ    1 
ATOM   3647 O  OH    . TYR B 2 219 ? 15.069  26.026  -33.572 1.00 97.15  ? 315  TYR D OH    1 
ATOM   3648 N  N     . ASP B 2 220 ? 8.451   24.821  -36.664 1.00 91.98  ? 316  ASP D N     1 
ATOM   3649 C  CA    . ASP B 2 220 ? 8.589   25.271  -38.041 1.00 104.51 ? 316  ASP D CA    1 
ATOM   3650 C  C     . ASP B 2 220 ? 7.479   24.651  -38.876 1.00 108.38 ? 316  ASP D C     1 
ATOM   3651 O  O     . ASP B 2 220 ? 7.189   23.459  -38.746 1.00 106.94 ? 316  ASP D O     1 
ATOM   3652 C  CB    . ASP B 2 220 ? 9.959   24.900  -38.620 1.00 110.26 ? 316  ASP D CB    1 
ATOM   3653 C  CG    . ASP B 2 220 ? 10.135  25.379  -40.048 1.00 116.06 ? 316  ASP D CG    1 
ATOM   3654 O  OD1   . ASP B 2 220 ? 10.310  26.600  -40.249 1.00 112.31 ? 316  ASP D OD1   1 
ATOM   3655 O  OD2   . ASP B 2 220 ? 10.095  24.537  -40.970 1.00 107.32 ? 316  ASP D OD2   1 
ATOM   3656 N  N     . SER B 2 221 ? 6.867   25.468  -39.729 1.00 111.35 ? 317  SER D N     1 
ATOM   3657 C  CA    . SER B 2 221 ? 5.816   25.011  -40.628 1.00 107.59 ? 317  SER D CA    1 
ATOM   3658 C  C     . SER B 2 221 ? 5.647   26.007  -41.768 1.00 114.14 ? 317  SER D C     1 
ATOM   3659 O  O     . SER B 2 221 ? 5.551   27.217  -41.527 1.00 121.37 ? 317  SER D O     1 
ATOM   3660 C  CB    . SER B 2 221 ? 4.496   24.830  -39.877 1.00 114.54 ? 317  SER D CB    1 
ATOM   3661 O  OG    . SER B 2 221 ? 3.482   24.347  -40.741 1.00 110.92 ? 317  SER D OG    1 
ATOM   3662 N  N     . PRO B 2 222 ? 5.614   25.541  -43.019 1.00 111.34 ? 318  PRO D N     1 
ATOM   3663 C  CA    . PRO B 2 222 ? 5.449   26.476  -44.144 1.00 115.64 ? 318  PRO D CA    1 
ATOM   3664 C  C     . PRO B 2 222 ? 4.106   27.184  -44.157 1.00 112.96 ? 318  PRO D C     1 
ATOM   3665 O  O     . PRO B 2 222 ? 3.986   28.240  -44.791 1.00 118.19 ? 318  PRO D O     1 
ATOM   3666 C  CB    . PRO B 2 222 ? 5.615   25.576  -45.378 1.00 106.34 ? 318  PRO D CB    1 
ATOM   3667 C  CG    . PRO B 2 222 ? 6.331   24.356  -44.877 1.00 109.77 ? 318  PRO D CG    1 
ATOM   3668 C  CD    . PRO B 2 222 ? 5.850   24.162  -43.473 1.00 106.80 ? 318  PRO D CD    1 
ATOM   3669 N  N     . SER B 2 223 ? 3.096   26.644  -43.483 1.00 112.82 ? 319  SER D N     1 
ATOM   3670 C  CA    . SER B 2 223 ? 1.760   27.226  -43.481 1.00 119.06 ? 319  SER D CA    1 
ATOM   3671 C  C     . SER B 2 223 ? 1.240   27.542  -42.088 1.00 115.14 ? 319  SER D C     1 
ATOM   3672 O  O     . SER B 2 223 ? 0.545   28.547  -41.909 1.00 122.45 ? 319  SER D O     1 
ATOM   3673 C  CB    . SER B 2 223 ? 0.776   26.282  -44.187 1.00 114.47 ? 319  SER D CB    1 
ATOM   3674 O  OG    . SER B 2 223 ? 0.735   25.017  -43.549 1.00 106.85 ? 319  SER D OG    1 
ATOM   3675 N  N     . LEU B 2 224 ? 1.558   26.713  -41.094 1.00 115.30 ? 320  LEU D N     1 
ATOM   3676 C  CA    . LEU B 2 224 ? 1.039   26.931  -39.751 1.00 113.34 ? 320  LEU D CA    1 
ATOM   3677 C  C     . LEU B 2 224 ? 1.902   27.949  -39.007 1.00 115.08 ? 320  LEU D C     1 
ATOM   3678 O  O     . LEU B 2 224 ? 3.131   27.915  -39.107 1.00 115.25 ? 320  LEU D O     1 
ATOM   3679 C  CB    . LEU B 2 224 ? 0.997   25.621  -38.968 1.00 105.39 ? 320  LEU D CB    1 
ATOM   3680 C  CG    . LEU B 2 224 ? 0.111   24.517  -39.545 1.00 114.23 ? 320  LEU D CG    1 
ATOM   3681 C  CD1   . LEU B 2 224 ? 0.274   23.236  -38.743 1.00 115.44 ? 320  LEU D CD1   1 
ATOM   3682 C  CD2   . LEU B 2 224 ? -1.346  24.957  -39.572 1.00 121.25 ? 320  LEU D CD2   1 
ATOM   3683 N  N     . PRO B 2 225 ? 1.286   28.862  -38.265 1.00 106.96 ? 321  PRO D N     1 
ATOM   3684 C  CA    . PRO B 2 225 ? 2.058   29.822  -37.473 1.00 105.99 ? 321  PRO D CA    1 
ATOM   3685 C  C     . PRO B 2 225 ? 2.690   29.169  -36.252 1.00 116.67 ? 321  PRO D C     1 
ATOM   3686 O  O     . PRO B 2 225 ? 2.218   28.157  -35.727 1.00 127.82 ? 321  PRO D O     1 
ATOM   3687 C  CB    . PRO B 2 225 ? 1.005   30.857  -37.062 1.00 117.69 ? 321  PRO D CB    1 
ATOM   3688 C  CG    . PRO B 2 225 ? -0.268  30.075  -37.017 1.00 113.06 ? 321  PRO D CG    1 
ATOM   3689 C  CD    . PRO B 2 225 ? -0.165  29.080  -38.143 1.00 111.04 ? 321  PRO D CD    1 
ATOM   3690 N  N     . GLU B 2 226 ? 3.785   29.778  -35.800 1.00 117.03 ? 322  GLU D N     1 
ATOM   3691 C  CA    . GLU B 2 226 ? 4.546   29.273  -34.659 1.00 121.76 ? 322  GLU D CA    1 
ATOM   3692 C  C     . GLU B 2 226 ? 3.803   29.612  -33.373 1.00 122.60 ? 322  GLU D C     1 
ATOM   3693 O  O     . GLU B 2 226 ? 4.037   30.645  -32.747 1.00 126.97 ? 322  GLU D O     1 
ATOM   3694 C  CB    . GLU B 2 226 ? 5.951   29.860  -34.654 1.00 126.05 ? 322  GLU D CB    1 
ATOM   3695 C  CG    . GLU B 2 226 ? 6.702   29.662  -35.964 1.00 127.53 ? 322  GLU D CG    1 
ATOM   3696 C  CD    . GLU B 2 226 ? 8.061   30.333  -35.971 1.00 143.38 ? 322  GLU D CD    1 
ATOM   3697 O  OE1   . GLU B 2 226 ? 8.534   30.736  -34.886 1.00 146.01 ? 322  GLU D OE1   1 
ATOM   3698 O  OE2   . GLU B 2 226 ? 8.655   30.460  -37.063 1.00 140.63 ? 322  GLU D OE2   1 
ATOM   3699 N  N     . ALA B 2 227 ? 2.899   28.726  -32.968 1.00 107.27 ? 323  ALA D N     1 
ATOM   3700 C  CA    . ALA B 2 227 ? 2.127   28.883  -31.746 1.00 107.16 ? 323  ALA D CA    1 
ATOM   3701 C  C     . ALA B 2 227 ? 2.337   27.674  -30.841 1.00 118.90 ? 323  ALA D C     1 
ATOM   3702 O  O     . ALA B 2 227 ? 2.925   26.663  -31.237 1.00 123.14 ? 323  ALA D O     1 
ATOM   3703 C  CB    . ALA B 2 227 ? 0.636   29.075  -32.056 1.00 106.98 ? 323  ALA D CB    1 
ATOM   3704 N  N     . GLU B 2 228 ? 1.851   27.791  -29.607 1.00 109.94 ? 324  GLU D N     1 
ATOM   3705 C  CA    . GLU B 2 228 ? 2.016   26.756  -28.599 1.00 99.76  ? 324  GLU D CA    1 
ATOM   3706 C  C     . GLU B 2 228 ? 0.657   26.289  -28.094 1.00 117.43 ? 324  GLU D C     1 
ATOM   3707 O  O     . GLU B 2 228 ? -0.335  27.021  -28.158 1.00 117.00 ? 324  GLU D O     1 
ATOM   3708 C  CB    . GLU B 2 228 ? 2.858   27.255  -27.418 1.00 103.76 ? 324  GLU D CB    1 
ATOM   3709 C  CG    . GLU B 2 228 ? 4.236   27.758  -27.802 1.00 109.20 ? 324  GLU D CG    1 
ATOM   3710 C  CD    . GLU B 2 228 ? 5.072   28.143  -26.597 1.00 121.77 ? 324  GLU D CD    1 
ATOM   3711 O  OE1   . GLU B 2 228 ? 4.642   27.870  -25.456 1.00 98.33  ? 324  GLU D OE1   1 
ATOM   3712 O  OE2   . GLU B 2 228 ? 6.162   28.720  -26.793 1.00 138.78 ? 324  GLU D OE2   1 
ATOM   3713 N  N     . ALA B 2 229 ? 0.627   25.058  -27.589 1.00 117.62 ? 325  ALA D N     1 
ATOM   3714 C  CA    . ALA B 2 229 ? -0.576  24.484  -27.006 1.00 119.74 ? 325  ALA D CA    1 
ATOM   3715 C  C     . ALA B 2 229 ? -0.189  23.590  -25.837 1.00 119.86 ? 325  ALA D C     1 
ATOM   3716 O  O     . ALA B 2 229 ? 0.953   23.138  -25.726 1.00 116.65 ? 325  ALA D O     1 
ATOM   3717 C  CB    . ALA B 2 229 ? -1.385  23.686  -28.038 1.00 119.02 ? 325  ALA D CB    1 
ATOM   3718 N  N     . MET B 2 230 ? -1.158  23.339  -24.963 1.00 125.86 ? 326  MET D N     1 
ATOM   3719 C  CA    . MET B 2 230 ? -0.965  22.503  -23.789 1.00 113.49 ? 326  MET D CA    1 
ATOM   3720 C  C     . MET B 2 230 ? -1.699  21.179  -23.957 1.00 122.66 ? 326  MET D C     1 
ATOM   3721 O  O     . MET B 2 230 ? -2.762  21.112  -24.582 1.00 125.87 ? 326  MET D O     1 
ATOM   3722 C  CB    . MET B 2 230 ? -1.456  23.208  -22.522 1.00 101.74 ? 326  MET D CB    1 
ATOM   3723 C  CG    . MET B 2 230 ? -0.598  24.386  -22.095 1.00 123.69 ? 326  MET D CG    1 
ATOM   3724 S  SD    . MET B 2 230 ? -1.287  25.259  -20.676 1.00 151.19 ? 326  MET D SD    1 
ATOM   3725 C  CE    . MET B 2 230 ? -1.543  23.901  -19.536 1.00 117.29 ? 326  MET D CE    1 
ATOM   3726 N  N     . PHE B 2 231 ? -1.118  20.124  -23.392 1.00 110.10 ? 327  PHE D N     1 
ATOM   3727 C  CA    . PHE B 2 231 ? -1.720  18.800  -23.454 1.00 106.32 ? 327  PHE D CA    1 
ATOM   3728 C  C     . PHE B 2 231 ? -1.118  17.928  -22.361 1.00 109.79 ? 327  PHE D C     1 
ATOM   3729 O  O     . PHE B 2 231 ? -0.167  18.315  -21.670 1.00 123.02 ? 327  PHE D O     1 
ATOM   3730 C  CB    . PHE B 2 231 ? -1.530  18.156  -24.834 1.00 109.97 ? 327  PHE D CB    1 
ATOM   3731 C  CG    . PHE B 2 231 ? -0.122  17.713  -25.110 1.00 107.50 ? 327  PHE D CG    1 
ATOM   3732 C  CD1   . PHE B 2 231 ? 0.818   18.609  -25.590 1.00 116.79 ? 327  PHE D CD1   1 
ATOM   3733 C  CD2   . PHE B 2 231 ? 0.261   16.398  -24.898 1.00 97.34  ? 327  PHE D CD2   1 
ATOM   3734 C  CE1   . PHE B 2 231 ? 2.114   18.205  -25.843 1.00 110.12 ? 327  PHE D CE1   1 
ATOM   3735 C  CE2   . PHE B 2 231 ? 1.555   15.988  -25.151 1.00 101.01 ? 327  PHE D CE2   1 
ATOM   3736 C  CZ    . PHE B 2 231 ? 2.483   16.893  -25.625 1.00 106.67 ? 327  PHE D CZ    1 
ATOM   3737 N  N     . ALA B 2 232 ? -1.687  16.730  -22.235 1.00 109.91 ? 328  ALA D N     1 
ATOM   3738 C  CA    . ALA B 2 232 ? -1.320  15.773  -21.203 1.00 120.78 ? 328  ALA D CA    1 
ATOM   3739 C  C     . ALA B 2 232 ? -1.485  14.365  -21.760 1.00 112.25 ? 328  ALA D C     1 
ATOM   3740 O  O     . ALA B 2 232 ? -2.072  14.159  -22.827 1.00 107.84 ? 328  ALA D O     1 
ATOM   3741 C  CB    . ALA B 2 232 ? -2.170  15.965  -19.944 1.00 127.05 ? 328  ALA D CB    1 
ATOM   3742 N  N     . ILE B 2 233 ? -0.965  13.392  -21.018 1.00 120.10 ? 329  ILE D N     1 
ATOM   3743 C  CA    . ILE B 2 233 ? -1.020  11.984  -21.401 1.00 109.07 ? 329  ILE D CA    1 
ATOM   3744 C  C     . ILE B 2 233 ? -1.814  11.257  -20.324 1.00 116.33 ? 329  ILE D C     1 
ATOM   3745 O  O     . ILE B 2 233 ? -1.276  10.918  -19.262 1.00 116.73 ? 329  ILE D O     1 
ATOM   3746 C  CB    . ILE B 2 233 ? 0.375   11.372  -21.571 1.00 96.49  ? 329  ILE D CB    1 
ATOM   3747 C  CG1   . ILE B 2 233 ? 1.178   12.152  -22.613 1.00 101.13 ? 329  ILE D CG1   1 
ATOM   3748 C  CG2   . ILE B 2 233 ? 0.267   9.907   -21.969 1.00 107.51 ? 329  ILE D CG2   1 
ATOM   3749 C  CD1   . ILE B 2 233 ? 0.549   12.158  -23.989 1.00 103.07 ? 329  ILE D CD1   1 
ATOM   3750 N  N     . ASN B 2 234 ? -3.095  11.017  -20.587 1.00 111.36 ? 330  ASN D N     1 
ATOM   3751 C  CA    . ASN B 2 234 ? -3.944  10.277  -19.670 1.00 106.57 ? 330  ASN D CA    1 
ATOM   3752 C  C     . ASN B 2 234 ? -3.856  8.782   -19.963 1.00 106.33 ? 330  ASN D C     1 
ATOM   3753 O  O     . ASN B 2 234 ? -3.249  8.346   -20.946 1.00 97.60  ? 330  ASN D O     1 
ATOM   3754 C  CB    . ASN B 2 234 ? -5.392  10.757  -19.776 1.00 118.57 ? 330  ASN D CB    1 
ATOM   3755 C  CG    . ASN B 2 234 ? -5.521  12.260  -19.630 1.00 121.07 ? 330  ASN D CG    1 
ATOM   3756 O  OD1   . ASN B 2 234 ? -4.809  12.883  -18.842 1.00 128.03 ? 330  ASN D OD1   1 
ATOM   3757 N  ND2   . ASN B 2 234 ? -6.430  12.852  -20.395 1.00 115.49 ? 330  ASN D ND2   1 
ATOM   3758 N  N     . ALA B 2 235 ? -4.499  7.990   -19.100 1.00 110.98 ? 331  ALA D N     1 
ATOM   3759 C  CA    . ALA B 2 235 ? -4.481  6.537   -19.235 1.00 106.56 ? 331  ALA D CA    1 
ATOM   3760 C  C     . ALA B 2 235 ? -5.086  6.052   -20.546 1.00 112.28 ? 331  ALA D C     1 
ATOM   3761 O  O     . ALA B 2 235 ? -5.001  4.854   -20.839 1.00 115.57 ? 331  ALA D O     1 
ATOM   3762 C  CB    . ALA B 2 235 ? -5.218  5.894   -18.059 1.00 93.15  ? 331  ALA D CB    1 
ATOM   3763 N  N     . ASP B 2 236 ? -5.687  6.940   -21.337 1.00 106.09 ? 332  ASP D N     1 
ATOM   3764 C  CA    . ASP B 2 236 ? -6.249  6.589   -22.635 1.00 109.82 ? 332  ASP D CA    1 
ATOM   3765 C  C     . ASP B 2 236 ? -5.618  7.407   -23.759 1.00 111.71 ? 332  ASP D C     1 
ATOM   3766 O  O     . ASP B 2 236 ? -6.266  7.691   -24.768 1.00 103.27 ? 332  ASP D O     1 
ATOM   3767 C  CB    . ASP B 2 236 ? -7.767  6.759   -22.629 1.00 111.06 ? 332  ASP D CB    1 
ATOM   3768 C  CG    . ASP B 2 236 ? -8.201  8.126   -22.137 1.00 122.89 ? 332  ASP D CG    1 
ATOM   3769 O  OD1   . ASP B 2 236 ? -7.325  8.935   -21.764 1.00 121.76 ? 332  ASP D OD1   1 
ATOM   3770 O  OD2   . ASP B 2 236 ? -9.422  8.392   -22.122 1.00 125.86 ? 332  ASP D OD2   1 
ATOM   3771 N  N     . GLY B 2 237 ? -4.360  7.798   -23.594 1.00 109.75 ? 333  GLY D N     1 
ATOM   3772 C  CA    . GLY B 2 237 ? -3.623  8.463   -24.649 1.00 97.49  ? 333  GLY D CA    1 
ATOM   3773 C  C     . GLY B 2 237 ? -3.524  9.964   -24.468 1.00 108.63 ? 333  GLY D C     1 
ATOM   3774 O  O     . GLY B 2 237 ? -3.647  10.509  -23.370 1.00 116.15 ? 333  GLY D O     1 
ATOM   3775 N  N     . VAL B 2 238 ? -3.292  10.644  -25.592 1.00 103.84 ? 334  VAL D N     1 
ATOM   3776 C  CA    . VAL B 2 238 ? -3.132  12.092  -25.575 1.00 105.79 ? 334  VAL D CA    1 
ATOM   3777 C  C     . VAL B 2 238 ? -4.474  12.754  -25.295 1.00 109.50 ? 334  VAL D C     1 
ATOM   3778 O  O     . VAL B 2 238 ? -5.517  12.335  -25.817 1.00 102.02 ? 334  VAL D O     1 
ATOM   3779 C  CB    . VAL B 2 238 ? -2.540  12.580  -26.908 1.00 96.58  ? 334  VAL D CB    1 
ATOM   3780 C  CG1   . VAL B 2 238 ? -2.190  14.060  -26.831 1.00 107.63 ? 334  VAL D CG1   1 
ATOM   3781 C  CG2   . VAL B 2 238 ? -1.321  11.754  -27.276 1.00 84.12  ? 334  VAL D CG2   1 
ATOM   3782 N  N     . GLY B 2 239 ? -4.456  13.795  -24.467 1.00 116.11 ? 335  GLY D N     1 
ATOM   3783 C  CA    . GLY B 2 239 ? -5.675  14.513  -24.154 1.00 121.81 ? 335  GLY D CA    1 
ATOM   3784 C  C     . GLY B 2 239 ? -5.364  15.916  -23.682 1.00 123.83 ? 335  GLY D C     1 
ATOM   3785 O  O     . GLY B 2 239 ? -4.206  16.333  -23.612 1.00 125.63 ? 335  GLY D O     1 
ATOM   3786 N  N     . ASP B 2 240 ? -6.426  16.643  -23.356 1.00 113.02 ? 336  ASP D N     1 
ATOM   3787 C  CA    . ASP B 2 240 ? -6.326  18.010  -22.869 1.00 120.53 ? 336  ASP D CA    1 
ATOM   3788 C  C     . ASP B 2 240 ? -6.527  18.051  -21.360 1.00 124.18 ? 336  ASP D C     1 
ATOM   3789 O  O     . ASP B 2 240 ? -7.313  17.284  -20.797 1.00 128.70 ? 336  ASP D O     1 
ATOM   3790 C  CB    . ASP B 2 240 ? -7.357  18.909  -23.553 1.00 130.87 ? 336  ASP D CB    1 
ATOM   3791 C  CG    . ASP B 2 240 ? -7.123  19.037  -25.043 1.00 131.99 ? 336  ASP D CG    1 
ATOM   3792 O  OD1   . ASP B 2 240 ? -5.957  19.230  -25.446 1.00 137.67 ? 336  ASP D OD1   1 
ATOM   3793 O  OD2   . ASP B 2 240 ? -8.102  18.938  -25.811 1.00 124.66 ? 336  ASP D OD2   1 
ATOM   3794 N  N     . ALA B 2 241 ? -5.804  18.959  -20.708 1.00 125.48 ? 337  ALA D N     1 
ATOM   3795 C  CA    . ALA B 2 241 ? -5.958  19.179  -19.274 1.00 142.80 ? 337  ALA D CA    1 
ATOM   3796 C  C     . ALA B 2 241 ? -7.216  20.006  -19.043 1.00 149.37 ? 337  ALA D C     1 
ATOM   3797 O  O     . ALA B 2 241 ? -7.234  21.211  -19.315 1.00 153.81 ? 337  ALA D O     1 
ATOM   3798 C  CB    . ALA B 2 241 ? -4.725  19.872  -18.702 1.00 138.25 ? 337  ALA D CB    1 
ATOM   3799 N  N     . LYS B 2 242 ? -8.270  19.362  -18.548 1.00 151.11 ? 338  LYS D N     1 
ATOM   3800 C  CA    . LYS B 2 242 ? -9.561  20.021  -18.357 1.00 157.33 ? 338  LYS D CA    1 
ATOM   3801 C  C     . LYS B 2 242 ? -9.448  21.017  -17.211 1.00 154.02 ? 338  LYS D C     1 
ATOM   3802 O  O     . LYS B 2 242 ? -9.434  20.639  -16.037 1.00 135.65 ? 338  LYS D O     1 
ATOM   3803 C  CB    . LYS B 2 242 ? -10.649 18.987  -18.090 1.00 146.30 ? 338  LYS D CB    1 
ATOM   3804 C  CG    . LYS B 2 242 ? -12.059 19.551  -18.126 1.00 154.00 ? 338  LYS D CG    1 
ATOM   3805 C  CD    . LYS B 2 242 ? -13.095 18.441  -18.101 1.00 156.01 ? 338  LYS D CD    1 
ATOM   3806 C  CE    . LYS B 2 242 ? -14.508 18.998  -18.173 1.00 151.76 ? 338  LYS D CE    1 
ATOM   3807 N  NZ    . LYS B 2 242 ? -15.532 17.918  -18.110 1.00 131.27 ? 338  LYS D NZ    1 
ATOM   3808 N  N     . ASP B 2 243 ? -9.369  22.300  -17.551 1.00 155.54 ? 339  ASP D N     1 
ATOM   3809 C  CA    . ASP B 2 243 ? -9.228  23.355  -16.555 1.00 153.58 ? 339  ASP D CA    1 
ATOM   3810 C  C     . ASP B 2 243 ? -10.591 23.864  -16.097 1.00 149.34 ? 339  ASP D C     1 
ATOM   3811 O  O     . ASP B 2 243 ? -11.048 24.920  -16.533 1.00 144.79 ? 339  ASP D O     1 
ATOM   3812 C  CB    . ASP B 2 243 ? -8.397  24.510  -17.118 1.00 151.39 ? 339  ASP D CB    1 
ATOM   3813 C  CG    . ASP B 2 243 ? -7.060  24.051  -17.668 1.00 160.61 ? 339  ASP D CG    1 
ATOM   3814 O  OD1   . ASP B 2 243 ? -6.500  23.072  -17.133 1.00 165.21 ? 339  ASP D OD1   1 
ATOM   3815 O  OD2   . ASP B 2 243 ? -6.572  24.669  -18.638 1.00 171.55 ? 339  ASP D OD2   1 
ATOM   3816 N  N     . THR B 2 272 ? 13.831  -12.400 -46.692 1.00 136.96 ? 3288 THR D N     1 
ATOM   3817 C  CA    . THR B 2 272 ? 14.433  -11.883 -45.468 1.00 155.11 ? 3288 THR D CA    1 
ATOM   3818 C  C     . THR B 2 272 ? 13.367  -11.257 -44.575 1.00 151.29 ? 3288 THR D C     1 
ATOM   3819 O  O     . THR B 2 272 ? 12.705  -11.951 -43.802 1.00 152.46 ? 3288 THR D O     1 
ATOM   3820 C  CB    . THR B 2 272 ? 15.524  -10.838 -45.769 1.00 155.64 ? 3288 THR D CB    1 
ATOM   3821 O  OG1   . THR B 2 272 ? 16.307  -11.270 -46.890 1.00 142.16 ? 3288 THR D OG1   1 
ATOM   3822 C  CG2   . THR B 2 272 ? 16.437  -10.662 -44.560 1.00 142.26 ? 3288 THR D CG2   1 
ATOM   3823 N  N     . PHE B 2 273 ? 13.209  -9.940  -44.687 1.00 142.23 ? 3289 PHE D N     1 
ATOM   3824 C  CA    . PHE B 2 273 ? 12.210  -9.211  -43.912 1.00 134.42 ? 3289 PHE D CA    1 
ATOM   3825 C  C     . PHE B 2 273 ? 10.822  -9.606  -44.401 1.00 126.85 ? 3289 PHE D C     1 
ATOM   3826 O  O     . PHE B 2 273 ? 10.407  -9.221  -45.499 1.00 130.98 ? 3289 PHE D O     1 
ATOM   3827 C  CB    . PHE B 2 273 ? 12.449  -7.710  -44.046 1.00 123.97 ? 3289 PHE D CB    1 
ATOM   3828 C  CG    . PHE B 2 273 ? 13.903  -7.342  -44.149 1.00 135.65 ? 3289 PHE D CG    1 
ATOM   3829 C  CD1   . PHE B 2 273 ? 14.694  -7.251  -43.015 1.00 138.95 ? 3289 PHE D CD1   1 
ATOM   3830 C  CD2   . PHE B 2 273 ? 14.482  -7.101  -45.384 1.00 139.54 ? 3289 PHE D CD2   1 
ATOM   3831 C  CE1   . PHE B 2 273 ? 16.036  -6.918  -43.112 1.00 142.71 ? 3289 PHE D CE1   1 
ATOM   3832 C  CE2   . PHE B 2 273 ? 15.820  -6.768  -45.487 1.00 141.24 ? 3289 PHE D CE2   1 
ATOM   3833 C  CZ    . PHE B 2 273 ? 16.598  -6.677  -44.350 1.00 139.41 ? 3289 PHE D CZ    1 
ATOM   3834 N  N     . VAL B 2 274 ? 10.104  -10.379 -43.590 1.00 116.51 ? 3290 VAL D N     1 
ATOM   3835 C  CA    . VAL B 2 274 ? 8.872   -11.027 -44.011 1.00 132.29 ? 3290 VAL D CA    1 
ATOM   3836 C  C     . VAL B 2 274 ? 7.676   -10.297 -43.402 1.00 117.54 ? 3290 VAL D C     1 
ATOM   3837 O  O     . VAL B 2 274 ? 7.808   -9.489  -42.482 1.00 121.24 ? 3290 VAL D O     1 
ATOM   3838 C  CB    . VAL B 2 274 ? 8.860   -12.525 -43.640 1.00 135.83 ? 3290 VAL D CB    1 
ATOM   3839 C  CG1   . VAL B 2 274 ? 8.422   -12.717 -42.193 1.00 111.08 ? 3290 VAL D CG1   1 
ATOM   3840 C  CG2   . VAL B 2 274 ? 7.982   -13.321 -44.600 1.00 128.80 ? 3290 VAL D CG2   1 
ATOM   3841 N  N     . SER B 2 275 ? 6.491   -10.593 -43.939 1.00 105.25 ? 3291 SER D N     1 
ATOM   3842 C  CA    . SER B 2 275 ? 5.226   -10.064 -43.447 1.00 107.49 ? 3291 SER D CA    1 
ATOM   3843 C  C     . SER B 2 275 ? 4.166   -11.158 -43.505 1.00 106.48 ? 3291 SER D C     1 
ATOM   3844 O  O     . SER B 2 275 ? 3.854   -11.660 -44.592 1.00 132.47 ? 3291 SER D O     1 
ATOM   3845 C  CB    . SER B 2 275 ? 4.790   -8.849  -44.268 1.00 108.53 ? 3291 SER D CB    1 
ATOM   3846 O  OG    . SER B 2 275 ? 5.802   -7.857  -44.297 1.00 104.93 ? 3291 SER D OG    1 
ATOM   3847 N  N     . PRO B 2 276 ? 3.596   -11.562 -42.367 1.00 100.77 ? 3292 PRO D N     1 
ATOM   3848 C  CA    . PRO B 2 276 ? 2.586   -12.627 -42.387 1.00 100.42 ? 3292 PRO D CA    1 
ATOM   3849 C  C     . PRO B 2 276 ? 1.176   -12.082 -42.548 1.00 97.20  ? 3292 PRO D C     1 
ATOM   3850 O  O     . PRO B 2 276 ? 0.726   -11.817 -43.666 1.00 92.32  ? 3292 PRO D O     1 
ATOM   3851 C  CB    . PRO B 2 276 ? 2.771   -13.311 -41.024 1.00 120.65 ? 3292 PRO D CB    1 
ATOM   3852 C  CG    . PRO B 2 276 ? 3.710   -12.396 -40.217 1.00 111.06 ? 3292 PRO D CG    1 
ATOM   3853 C  CD    . PRO B 2 276 ? 3.883   -11.127 -40.994 1.00 102.91 ? 3292 PRO D CD    1 
ATOM   3854 N  N     . ALA B 2 277 ? 0.472   -11.915 -41.429 1.00 116.90 ? 3293 ALA D N     1 
ATOM   3855 C  CA    . ALA B 2 277 ? -0.871  -11.350 -41.437 1.00 100.10 ? 3293 ALA D CA    1 
ATOM   3856 C  C     . ALA B 2 277 ? -0.875  -9.839  -41.624 1.00 103.26 ? 3293 ALA D C     1 
ATOM   3857 O  O     . ALA B 2 277 ? -1.956  -9.247  -41.720 1.00 106.92 ? 3293 ALA D O     1 
ATOM   3858 C  CB    . ALA B 2 277 ? -1.603  -11.711 -40.143 1.00 77.35  ? 3293 ALA D CB    1 
ATOM   3859 N  N     . ALA B 2 278 ? 0.298   -9.203  -41.673 1.00 102.72 ? 3294 ALA D N     1 
ATOM   3860 C  CA    . ALA B 2 278 ? 0.361   -7.770  -41.928 1.00 105.29 ? 3294 ALA D CA    1 
ATOM   3861 C  C     . ALA B 2 278 ? 0.024   -7.428  -43.373 1.00 103.58 ? 3294 ALA D C     1 
ATOM   3862 O  O     . ALA B 2 278 ? -0.239  -6.259  -43.676 1.00 94.28  ? 3294 ALA D O     1 
ATOM   3863 C  CB    . ALA B 2 278 ? 1.747   -7.230  -41.574 1.00 95.99  ? 3294 ALA D CB    1 
ATOM   3864 N  N     . GLN B 2 279 ? 0.026   -8.416  -44.267 1.00 102.95 ? 3295 GLN D N     1 
ATOM   3865 C  CA    . GLN B 2 279 ? -0.325  -8.192  -45.662 1.00 103.61 ? 3295 GLN D CA    1 
ATOM   3866 C  C     . GLN B 2 279 ? -1.822  -8.019  -45.876 1.00 107.04 ? 3295 GLN D C     1 
ATOM   3867 O  O     . GLN B 2 279 ? -2.236  -7.692  -46.994 1.00 112.33 ? 3295 GLN D O     1 
ATOM   3868 C  CB    . GLN B 2 279 ? 0.181   -9.353  -46.522 1.00 108.79 ? 3295 GLN D CB    1 
ATOM   3869 C  CG    . GLN B 2 279 ? 1.673   -9.612  -46.401 1.00 96.24  ? 3295 GLN D CG    1 
ATOM   3870 C  CD    . GLN B 2 279 ? 2.082   -10.938 -47.012 1.00 97.23  ? 3295 GLN D CD    1 
ATOM   3871 O  OE1   . GLN B 2 279 ? 1.245   -11.810 -47.246 1.00 102.38 ? 3295 GLN D OE1   1 
ATOM   3872 N  NE2   . GLN B 2 279 ? 3.374   -11.097 -47.273 1.00 92.71  ? 3295 GLN D NE2   1 
ATOM   3873 N  N     . LYS B 2 280 ? -2.636  -8.230  -44.844 1.00 100.61 ? 3296 LYS D N     1 
ATOM   3874 C  CA    . LYS B 2 280 ? -4.079  -8.108  -44.985 1.00 102.36 ? 3296 LYS D CA    1 
ATOM   3875 C  C     . LYS B 2 280 ? -4.476  -6.666  -45.282 1.00 102.33 ? 3296 LYS D C     1 
ATOM   3876 O  O     . LYS B 2 280 ? -3.774  -5.716  -44.925 1.00 97.28  ? 3296 LYS D O     1 
ATOM   3877 C  CB    . LYS B 2 280 ? -4.786  -8.593  -43.717 1.00 104.66 ? 3296 LYS D CB    1 
ATOM   3878 C  CG    . LYS B 2 280 ? -5.155  -10.073 -43.718 1.00 100.40 ? 3296 LYS D CG    1 
ATOM   3879 C  CD    . LYS B 2 280 ? -3.928  -10.969 -43.764 1.00 105.44 ? 3296 LYS D CD    1 
ATOM   3880 C  CE    . LYS B 2 280 ? -4.316  -12.439 -43.723 1.00 114.97 ? 3296 LYS D CE    1 
ATOM   3881 N  NZ    . LYS B 2 280 ? -5.051  -12.785 -42.475 1.00 107.35 ? 3296 LYS D NZ    1 
ATOM   3882 N  N     . ALA B 2 281 ? -5.618  -6.512  -45.947 1.00 97.84  ? 3297 ALA D N     1 
ATOM   3883 C  CA    . ALA B 2 281 ? -6.114  -5.192  -46.293 1.00 94.60  ? 3297 ALA D CA    1 
ATOM   3884 C  C     . ALA B 2 281 ? -6.598  -4.458  -45.043 1.00 93.56  ? 3297 ALA D C     1 
ATOM   3885 O  O     . ALA B 2 281 ? -6.762  -5.040  -43.967 1.00 92.82  ? 3297 ALA D O     1 
ATOM   3886 C  CB    . ALA B 2 281 ? -7.240  -5.295  -47.321 1.00 97.89  ? 3297 ALA D CB    1 
ATOM   3887 N  N     . PHE B 2 282 ? -6.825  -3.156  -45.199 1.00 94.56  ? 3298 PHE D N     1 
ATOM   3888 C  CA    . PHE B 2 282 ? -7.303  -2.328  -44.098 1.00 83.75  ? 3298 PHE D CA    1 
ATOM   3889 C  C     . PHE B 2 282 ? -8.731  -2.723  -43.746 1.00 96.74  ? 3298 PHE D C     1 
ATOM   3890 O  O     . PHE B 2 282 ? -9.659  -2.492  -44.528 1.00 113.66 ? 3298 PHE D O     1 
ATOM   3891 C  CB    . PHE B 2 282 ? -7.224  -0.851  -44.470 1.00 93.69  ? 3298 PHE D CB    1 
ATOM   3892 C  CG    . PHE B 2 282 ? -7.966  0.052   -43.525 1.00 100.22 ? 3298 PHE D CG    1 
ATOM   3893 C  CD1   . PHE B 2 282 ? -7.452  0.340   -42.271 1.00 100.31 ? 3298 PHE D CD1   1 
ATOM   3894 C  CD2   . PHE B 2 282 ? -9.179  0.614   -43.891 1.00 108.38 ? 3298 PHE D CD2   1 
ATOM   3895 C  CE1   . PHE B 2 282 ? -8.133  1.170   -41.400 1.00 100.66 ? 3298 PHE D CE1   1 
ATOM   3896 C  CE2   . PHE B 2 282 ? -9.865  1.444   -43.024 1.00 110.30 ? 3298 PHE D CE2   1 
ATOM   3897 C  CZ    . PHE B 2 282 ? -9.341  1.723   -41.777 1.00 88.65  ? 3298 PHE D CZ    1 
ATOM   3898 N  N     . GLN B 2 283 ? -8.910  -3.320  -42.572 1.00 110.89 ? 3299 GLN D N     1 
ATOM   3899 C  CA    . GLN B 2 283 ? -10.237 -3.673  -42.092 1.00 112.27 ? 3299 GLN D CA    1 
ATOM   3900 C  C     . GLN B 2 283 ? -10.779 -2.535  -41.239 1.00 109.91 ? 3299 GLN D C     1 
ATOM   3901 O  O     . GLN B 2 283 ? -10.186 -2.225  -40.196 1.00 111.80 ? 3299 GLN D O     1 
ATOM   3902 C  CB    . GLN B 2 283 ? -10.195 -4.958  -41.283 1.00 116.67 ? 3299 GLN D CB    1 
ATOM   3903 C  CG    . GLN B 2 283 ? -11.563 -5.542  -40.966 1.00 126.19 ? 3299 GLN D CG    1 
ATOM   3904 C  CD    . GLN B 2 283 ? -12.250 -6.122  -42.189 1.00 121.00 ? 3299 GLN D CD    1 
ATOM   3905 O  OE1   . GLN B 2 283 ? -11.611 -6.389  -43.207 1.00 107.52 ? 3299 GLN D OE1   1 
ATOM   3906 N  NE2   . GLN B 2 283 ? -13.559 -6.319  -42.093 1.00 115.63 ? 3299 GLN D NE2   1 
ATOM   3907 N  N     . PRO B 2 284 ? -11.867 -1.882  -41.638 1.00 114.48 ? 3300 PRO D N     1 
ATOM   3908 C  CA    . PRO B 2 284 ? -12.421 -0.786  -40.834 1.00 109.54 ? 3300 PRO D CA    1 
ATOM   3909 C  C     . PRO B 2 284 ? -12.798 -1.267  -39.446 1.00 112.48 ? 3300 PRO D C     1 
ATOM   3910 O  O     . PRO B 2 284 ? -13.515 -2.268  -39.299 1.00 115.67 ? 3300 PRO D O     1 
ATOM   3911 C  CB    . PRO B 2 284 ? -13.659 -0.353  -41.632 1.00 107.77 ? 3300 PRO D CB    1 
ATOM   3912 C  CG    . PRO B 2 284 ? -13.368 -0.780  -43.034 1.00 109.91 ? 3300 PRO D CG    1 
ATOM   3913 C  CD    . PRO B 2 284 ? -12.591 -2.059  -42.908 1.00 107.99 ? 3300 PRO D CD    1 
ATOM   3914 N  N     . PRO B 2 285 ? -12.323 -0.587  -38.402 1.00 117.31 ? 3301 PRO D N     1 
ATOM   3915 C  CA    . PRO B 2 285 ? -12.591 -1.053  -37.036 1.00 111.53 ? 3301 PRO D CA    1 
ATOM   3916 C  C     . PRO B 2 285 ? -14.076 -1.009  -36.708 1.00 112.80 ? 3301 PRO D C     1 
ATOM   3917 O  O     . PRO B 2 285 ? -14.788 -0.072  -37.075 1.00 113.19 ? 3301 PRO D O     1 
ATOM   3918 C  CB    . PRO B 2 285 ? -11.793 -0.074  -36.165 1.00 103.46 ? 3301 PRO D CB    1 
ATOM   3919 C  CG    . PRO B 2 285 ? -10.766 0.513   -37.084 1.00 98.42  ? 3301 PRO D CG    1 
ATOM   3920 C  CD    . PRO B 2 285 ? -11.426 0.579   -38.425 1.00 109.80 ? 3301 PRO D CD    1 
ATOM   3921 N  N     . ARG B 2 286 ? -14.537 -2.042  -36.008 1.00 117.89 ? 3302 ARG D N     1 
ATOM   3922 C  CA    . ARG B 2 286 ? -15.930 -2.137  -35.609 1.00 116.09 ? 3302 ARG D CA    1 
ATOM   3923 C  C     . ARG B 2 286 ? -16.177 -1.305  -34.352 1.00 117.41 ? 3302 ARG D C     1 
ATOM   3924 O  O     . ARG B 2 286 ? -15.276 -0.657  -33.811 1.00 121.34 ? 3302 ARG D O     1 
ATOM   3925 C  CB    . ARG B 2 286 ? -16.318 -3.599  -35.394 1.00 119.91 ? 3302 ARG D CB    1 
ATOM   3926 C  CG    . ARG B 2 286 ? -16.274 -4.439  -36.661 1.00 125.16 ? 3302 ARG D CG    1 
ATOM   3927 C  CD    . ARG B 2 286 ? -16.436 -5.923  -36.364 1.00 118.61 ? 3302 ARG D CD    1 
ATOM   3928 N  NE    . ARG B 2 286 ? -15.279 -6.476  -35.669 1.00 125.34 ? 3302 ARG D NE    1 
ATOM   3929 C  CZ    . ARG B 2 286 ? -15.217 -6.686  -34.361 1.00 132.96 ? 3302 ARG D CZ    1 
ATOM   3930 N  NH1   . ARG B 2 286 ? -16.238 -6.408  -33.567 1.00 133.44 ? 3302 ARG D NH1   1 
ATOM   3931 N  NH2   . ARG B 2 286 ? -14.103 -7.189  -33.838 1.00 135.33 ? 3302 ARG D NH2   1 
ATOM   3932 N  N     . SER B 2 287 ? -17.423 -1.323  -33.878 1.00 117.10 ? 3303 SER D N     1 
ATOM   3933 C  CA    . SER B 2 287 ? -17.794 -0.524  -32.714 1.00 127.07 ? 3303 SER D CA    1 
ATOM   3934 C  C     . SER B 2 287 ? -17.425 -1.230  -31.414 1.00 128.67 ? 3303 SER D C     1 
ATOM   3935 O  O     . SER B 2 287 ? -16.707 -0.674  -30.575 1.00 113.58 ? 3303 SER D O     1 
ATOM   3936 C  CB    . SER B 2 287 ? -19.292 -0.210  -32.751 1.00 127.02 ? 3303 SER D CB    1 
ATOM   3937 O  OG    . SER B 2 287 ? -19.686 0.529   -31.608 1.00 124.75 ? 3303 SER D OG    1 
ATOM   3938 N  N     . ALA B 2 288 ? -17.915 -2.460  -31.233 1.00 136.90 ? 3304 ALA D N     1 
ATOM   3939 C  CA    . ALA B 2 288 ? -17.698 -3.235  -30.009 1.00 132.49 ? 3304 ALA D CA    1 
ATOM   3940 C  C     . ALA B 2 288 ? -18.186 -2.473  -28.778 1.00 124.96 ? 3304 ALA D C     1 
ATOM   3941 O  O     . ALA B 2 288 ? -17.585 -2.537  -27.704 1.00 124.83 ? 3304 ALA D O     1 
ATOM   3942 C  CB    . ALA B 2 288 ? -16.230 -3.640  -29.855 1.00 126.70 ? 3304 ALA D CB    1 
ATOM   3943 N  N     . GLY B 2 289 ? -19.288 -1.746  -28.937 1.00 127.88 ? 3305 GLY D N     1 
ATOM   3944 C  CA    . GLY B 2 289 ? -19.854 -0.968  -27.852 1.00 119.90 ? 3305 GLY D CA    1 
ATOM   3945 C  C     . GLY B 2 289 ? -21.083 -0.178  -28.257 1.00 121.81 ? 3305 GLY D C     1 
ATOM   3946 O  O     . GLY B 2 289 ? -22.188 -0.445  -27.784 1.00 113.86 ? 3305 GLY D O     1 
HETATM 3947 P  PB    . ADP C 3 .   ? 20.999  -1.565  0.107   1.00 79.80  ? 2000 ADP B PB    1 
HETATM 3948 O  O1B   . ADP C 3 .   ? 19.841  -1.469  -0.854  1.00 88.86  ? 2000 ADP B O1B   1 
HETATM 3949 O  O2B   . ADP C 3 .   ? 21.643  -0.243  0.449   1.00 96.48  ? 2000 ADP B O2B   1 
HETATM 3950 O  O3B   . ADP C 3 .   ? 21.973  -2.678  -0.197  1.00 69.95  ? 2000 ADP B O3B   1 
HETATM 3951 P  PA    . ADP C 3 .   ? 19.928  -3.559  1.759   1.00 84.94  ? 2000 ADP B PA    1 
HETATM 3952 O  O1A   . ADP C 3 .   ? 19.338  -4.151  0.502   1.00 100.19 ? 2000 ADP B O1A   1 
HETATM 3953 O  O2A   . ADP C 3 .   ? 21.132  -4.199  2.408   1.00 91.01  ? 2000 ADP B O2A   1 
HETATM 3954 O  O3A   . ADP C 3 .   ? 20.295  -2.019  1.478   1.00 86.21  ? 2000 ADP B O3A   1 
HETATM 3955 O  "O5'" . ADP C 3 .   ? 18.764  -3.401  2.857   1.00 105.32 ? 2000 ADP B "O5'" 1 
HETATM 3956 C  "C5'" . ADP C 3 .   ? 18.983  -3.823  4.200   1.00 107.45 ? 2000 ADP B "C5'" 1 
HETATM 3957 C  "C4'" . ADP C 3 .   ? 17.643  -4.010  4.896   1.00 98.90  ? 2000 ADP B "C4'" 1 
HETATM 3958 O  "O4'" . ADP C 3 .   ? 17.322  -5.401  4.913   1.00 106.56 ? 2000 ADP B "O4'" 1 
HETATM 3959 C  "C3'" . ADP C 3 .   ? 17.691  -3.531  6.337   1.00 109.03 ? 2000 ADP B "C3'" 1 
HETATM 3960 O  "O3'" . ADP C 3 .   ? 16.826  -2.404  6.507   1.00 110.81 ? 2000 ADP B "O3'" 1 
HETATM 3961 C  "C2'" . ADP C 3 .   ? 17.205  -4.691  7.181   1.00 97.82  ? 2000 ADP B "C2'" 1 
HETATM 3962 O  "O2'" . ADP C 3 .   ? 16.017  -4.322  7.886   1.00 107.39 ? 2000 ADP B "O2'" 1 
HETATM 3963 C  "C1'" . ADP C 3 .   ? 16.904  -5.820  6.211   1.00 96.88  ? 2000 ADP B "C1'" 1 
HETATM 3964 N  N9    . ADP C 3 .   ? 17.674  -7.022  6.613   1.00 86.51  ? 2000 ADP B N9    1 
HETATM 3965 C  C8    . ADP C 3 .   ? 18.998  -7.195  6.442   1.00 81.92  ? 2000 ADP B C8    1 
HETATM 3966 N  N7    . ADP C 3 .   ? 19.399  -8.401  6.919   1.00 94.13  ? 2000 ADP B N7    1 
HETATM 3967 C  C5    . ADP C 3 .   ? 18.311  -9.021  7.412   1.00 86.08  ? 2000 ADP B C5    1 
HETATM 3968 C  C6    . ADP C 3 .   ? 18.027  -10.321 8.063   1.00 87.80  ? 2000 ADP B C6    1 
HETATM 3969 N  N6    . ADP C 3 .   ? 19.015  -11.221 8.288   1.00 95.07  ? 2000 ADP B N6    1 
HETATM 3970 N  N1    . ADP C 3 .   ? 16.750  -10.578 8.425   1.00 91.35  ? 2000 ADP B N1    1 
HETATM 3971 C  C2    . ADP C 3 .   ? 15.760  -9.692  8.206   1.00 95.96  ? 2000 ADP B C2    1 
HETATM 3972 N  N3    . ADP C 3 .   ? 15.946  -8.495  7.622   1.00 91.21  ? 2000 ADP B N3    1 
HETATM 3973 C  C4    . ADP C 3 .   ? 17.176  -8.107  7.210   1.00 89.07  ? 2000 ADP B C4    1 
HETATM 3974 BE BE    . BEF D 4 .   ? 23.958  -2.598  -1.393  1.00 92.74  ? 2001 BEF B BE    1 
HETATM 3975 F  F1    . BEF D 4 .   ? 24.106  -1.438  -0.492  1.00 99.22  ? 2001 BEF B F1    1 
HETATM 3976 F  F2    . BEF D 4 .   ? 23.373  -2.415  -2.736  1.00 89.99  ? 2001 BEF B F2    1 
HETATM 3977 F  F3    . BEF D 4 .   ? 24.567  -3.893  -1.030  1.00 78.79  ? 2001 BEF B F3    1 
HETATM 3978 C  C1    . EDO E 5 .   ? 7.881   -5.068  -15.785 1.00 107.29 ? 2002 EDO B C1    1 
HETATM 3979 O  O1    . EDO E 5 .   ? 7.182   -6.091  -15.111 1.00 100.03 ? 2002 EDO B O1    1 
HETATM 3980 C  C2    . EDO E 5 .   ? 6.963   -4.380  -16.764 1.00 111.85 ? 2002 EDO B C2    1 
HETATM 3981 O  O2    . EDO E 5 .   ? 6.337   -5.338  -17.587 1.00 91.13  ? 2002 EDO B O2    1 
HETATM 3982 C  C1    . EDO F 5 .   ? 8.016   -30.983 -4.685  1.00 109.40 ? 2003 EDO B C1    1 
HETATM 3983 O  O1    . EDO F 5 .   ? 8.842   -29.961 -5.195  1.00 106.95 ? 2003 EDO B O1    1 
HETATM 3984 C  C2    . EDO F 5 .   ? 7.209   -30.457 -3.525  1.00 112.24 ? 2003 EDO B C2    1 
HETATM 3985 O  O2    . EDO F 5 .   ? 6.320   -29.460 -3.976  1.00 117.76 ? 2003 EDO B O2    1 
HETATM 3986 P  PB    . ADP G 3 .   ? 9.375   9.776   -24.925 1.00 77.70  ? 5000 ADP D PB    1 
HETATM 3987 O  O1B   . ADP G 3 .   ? 8.807   10.977  -25.642 1.00 78.62  ? 5000 ADP D O1B   1 
HETATM 3988 O  O2B   . ADP G 3 .   ? 10.769  9.968   -24.381 1.00 91.77  ? 5000 ADP D O2B   1 
HETATM 3989 O  O3B   . ADP G 3 .   ? 9.156   8.461   -25.636 1.00 65.98  ? 5000 ADP D O3B   1 
HETATM 3990 P  PA    . ADP G 3 .   ? 7.011   8.974   -23.660 1.00 79.05  ? 5000 ADP D PA    1 
HETATM 3991 O  O1A   . ADP G 3 .   ? 6.309   9.418   -24.920 1.00 87.86  ? 5000 ADP D O1A   1 
HETATM 3992 O  O2A   . ADP G 3 .   ? 7.209   7.504   -23.378 1.00 94.01  ? 5000 ADP D O2A   1 
HETATM 3993 O  O3A   . ADP G 3 .   ? 8.459   9.671   -23.609 1.00 89.46  ? 5000 ADP D O3A   1 
HETATM 3994 O  "O5'" . ADP G 3 .   ? 6.299   9.661   -22.393 1.00 100.33 ? 5000 ADP D "O5'" 1 
HETATM 3995 C  "C5'" . ADP G 3 .   ? 6.001   8.895   -21.230 1.00 109.18 ? 5000 ADP D "C5'" 1 
HETATM 3996 C  "C4'" . ADP G 3 .   ? 5.080   9.698   -20.323 1.00 98.54  ? 5000 ADP D "C4'" 1 
HETATM 3997 O  "O4'" . ADP G 3 .   ? 3.733   9.280   -20.547 1.00 104.92 ? 5000 ADP D "O4'" 1 
HETATM 3998 C  "C3'" . ADP G 3 .   ? 5.398   9.469   -18.855 1.00 93.26  ? 5000 ADP D "C3'" 1 
HETATM 3999 O  "O3'" . ADP G 3 .   ? 5.845   10.691  -18.259 1.00 91.06  ? 5000 ADP D "O3'" 1 
HETATM 4000 C  "C2'" . ADP G 3 .   ? 4.103   9.025   -18.208 1.00 109.77 ? 5000 ADP D "C2'" 1 
HETATM 4001 O  "O2'" . ADP G 3 .   ? 3.719   9.956   -17.192 1.00 127.13 ? 5000 ADP D "O2'" 1 
HETATM 4002 C  "C1'" . ADP G 3 .   ? 3.064   9.003   -19.317 1.00 95.58  ? 5000 ADP D "C1'" 1 
HETATM 4003 N  N9    . ADP G 3 .   ? 2.462   7.650   -19.387 1.00 94.39  ? 5000 ADP D N9    1 
HETATM 4004 C  C8    . ADP G 3 .   ? 3.031   6.571   -19.957 1.00 97.46  ? 5000 ADP D C8    1 
HETATM 4005 N  N7    . ADP G 3 .   ? 2.228   5.483   -19.855 1.00 104.93 ? 5000 ADP D N7    1 
HETATM 4006 C  C5    . ADP G 3 .   ? 1.114   5.865   -19.204 1.00 104.99 ? 5000 ADP D C5    1 
HETATM 4007 C  C6    . ADP G 3 .   ? -0.140  5.211   -18.762 1.00 102.52 ? 5000 ADP D C6    1 
HETATM 4008 N  N6    . ADP G 3 .   ? -0.367  3.898   -19.005 1.00 91.29  ? 5000 ADP D N6    1 
HETATM 4009 N  N1    . ADP G 3 .   ? -1.049  5.971   -18.111 1.00 112.10 ? 5000 ADP D N1    1 
HETATM 4010 C  C2    . ADP G 3 .   ? -0.835  7.278   -17.864 1.00 103.16 ? 5000 ADP D C2    1 
HETATM 4011 N  N3    . ADP G 3 .   ? 0.279   7.934   -18.235 1.00 97.81  ? 5000 ADP D N3    1 
HETATM 4012 C  C4    . ADP G 3 .   ? 1.273   7.294   -18.896 1.00 103.25 ? 5000 ADP D C4    1 
HETATM 4013 BE BE    . BEF H 4 .   ? 10.901  7.450   -26.678 1.00 85.23  ? 5001 BEF D BE    1 
HETATM 4014 F  F1    . BEF H 4 .   ? 11.905  8.016   -25.756 1.00 83.11  ? 5001 BEF D F1    1 
HETATM 4015 F  F2    . BEF H 4 .   ? 10.728  8.029   -28.024 1.00 79.86  ? 5001 BEF D F2    1 
HETATM 4016 F  F3    . BEF H 4 .   ? 9.978   6.399   -26.207 1.00 83.64  ? 5001 BEF D F3    1 
HETATM 4017 O  O     . HOH I 6 .   ? 34.333  2.378   -26.314 1.00 95.06  ? 2101 HOH B O     1 
HETATM 4018 O  O     . HOH I 6 .   ? 10.918  -3.869  6.198   1.00 171.84 ? 2102 HOH B O     1 
HETATM 4019 O  O     . HOH I 6 .   ? 5.027   -11.942 2.856   1.00 98.25  ? 2103 HOH B O     1 
HETATM 4020 O  O     . HOH I 6 .   ? 10.765  -7.401  -23.332 1.00 88.74  ? 2104 HOH B O     1 
HETATM 4021 O  O     . HOH I 6 .   ? 27.531  9.752   -23.101 1.00 106.73 ? 2105 HOH B O     1 
HETATM 4022 O  O     . HOH I 6 .   ? 23.714  6.940   -0.627  1.00 97.26  ? 2106 HOH B O     1 
HETATM 4023 O  O     . HOH I 6 .   ? 33.399  -2.620  -1.233  1.00 102.75 ? 2107 HOH B O     1 
HETATM 4024 O  O     . HOH I 6 .   ? 31.401  4.521   -24.638 1.00 180.89 ? 2108 HOH B O     1 
HETATM 4025 O  O     . HOH I 6 .   ? 37.201  1.456   -10.128 1.00 89.86  ? 2109 HOH B O     1 
HETATM 4026 O  O     . HOH I 6 .   ? 27.405  9.064   -11.329 1.00 86.51  ? 2110 HOH B O     1 
HETATM 4027 O  O     . HOH I 6 .   ? 18.246  -24.051 -12.723 1.00 87.46  ? 2111 HOH B O     1 
HETATM 4028 O  O     . HOH I 6 .   ? 19.227  6.298   -24.141 1.00 84.73  ? 2112 HOH B O     1 
HETATM 4029 O  O     . HOH I 6 .   ? 4.432   -13.166 5.385   1.00 80.10  ? 2113 HOH B O     1 
HETATM 4030 O  O     . HOH I 6 .   ? 39.247  1.918   -11.645 1.00 83.31  ? 2114 HOH B O     1 
HETATM 4031 O  O     . HOH I 6 .   ? 24.782  11.595  -13.625 1.00 88.12  ? 2115 HOH B O     1 
HETATM 4032 O  O     . HOH J 6 .   ? -11.056 7.004   -47.684 1.00 87.68  ? 5101 HOH D O     1 
HETATM 4033 O  O     . HOH J 6 .   ? 3.326   3.376   -19.331 1.00 109.33 ? 5102 HOH D O     1 
HETATM 4034 O  O     . HOH J 6 .   ? 13.313  16.384  -19.441 1.00 90.75  ? 5103 HOH D O     1 
HETATM 4035 O  O     . HOH J 6 .   ? -5.369  -5.458  -41.535 1.00 93.78  ? 5104 HOH D O     1 
HETATM 4036 O  O     . HOH J 6 .   ? -2.702  -6.679  -41.178 1.00 91.78  ? 5105 HOH D O     1 
HETATM 4037 O  O     . HOH J 6 .   ? 10.080  22.914  -43.146 1.00 107.27 ? 5106 HOH D O     1 
HETATM 4038 O  O     . HOH J 6 .   ? 8.975   -3.347  -27.464 1.00 83.49  ? 5107 HOH D O     1 
HETATM 4039 O  O     . HOH J 6 .   ? -7.130  -8.812  -46.192 1.00 78.22  ? 5108 HOH D O     1 
HETATM 4040 O  O     . HOH J 6 .   ? 9.204   6.971   -21.533 1.00 92.83  ? 5109 HOH D O     1 
HETATM 4041 O  O     . HOH J 6 .   ? 17.241  5.530   -26.622 1.00 87.53  ? 5110 HOH D O     1 
HETATM 4042 O  O     . HOH J 6 .   ? 25.139  1.736   -37.470 1.00 81.73  ? 5111 HOH D O     1 
HETATM 4043 O  O     . HOH J 6 .   ? 17.307  9.213   -30.363 1.00 87.87  ? 5112 HOH D O     1 
HETATM 4044 O  O     . HOH J 6 .   ? 16.250  18.936  -34.350 1.00 94.62  ? 5113 HOH D O     1 
HETATM 4045 O  O     . HOH J 6 .   ? 18.084  7.769   -28.107 1.00 85.19  ? 5114 HOH D O     1 
HETATM 4046 O  O     . HOH J 6 .   ? -9.767  -6.649  -38.399 1.00 93.79  ? 5115 HOH D O     1 
HETATM 4047 O  O     . HOH J 6 .   ? 26.211  2.998   -40.326 1.00 75.90  ? 5116 HOH D O     1 
HETATM 4048 O  O     . HOH J 6 .   ? -5.593  -5.724  -51.290 1.00 86.63  ? 5117 HOH D O     1 
HETATM 4049 O  O     . HOH J 6 .   ? 22.720  12.901  -35.125 1.00 93.76  ? 5118 HOH D O     1 
# 
